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*** OXIDOREDUCTASE 20-AUG-09 3IQD ***elNémo ID: 240721195400599704Job options:ID = 240721195400599704 JOBID = OXIDOREDUCTASE 20-AUG-09 3IQD 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 OXIDOREDUCTASE 20-AUG-09 3IQD TITLE STRUCTURE OF OCTOPINE-DEHYDROGENASE IN COMPLEX WITH NADH AND AGMATINE COMPND MOL_ID: 1; COMPND 2 MOLECULE: OCTOPINE DEHYDROGENASE; COMPND 3 CHAIN: B; COMPND 4 EC: 1.5.1.11; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PECTEN MAXIMUS; SOURCE 3 ORGANISM_COMMON: KING SCALLOP; SOURCE 4 ORGANISM_TAXID: 6579; SOURCE 5 GENE: ODH1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET KEYWDS OCTOPINE, DEHYDROGENASE, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR S.H.J.SMITS,T.MEYER,A.MUELLER,D.WILLBOLD,M.K.GRIESHABER,L.SCHMITT REVDAT 4 01-NOV-23 3IQD 1 REMARK SEQADV REVDAT 3 06-NOV-13 3IQD 1 HET HETNAM HETATM VERSN REVDAT 2 08-DEC-10 3IQD 1 JRNL REVDAT 1 25-AUG-10 3IQD 0 JRNL AUTH S.H.J.SMITS,T.MEYER,A.MUELLER,N.VAN OS,M.STOLDT,D.WILLBOLD, JRNL AUTH 2 L.SCHMITT,M.K.GRIESHABER JRNL TITL INSIGHTS INTO THE MECHANISM OF LIGAND BINDING TO OCTOPINE JRNL TITL 2 DEHYDROGENASE FROM PECTEN MAXIMUS BY NMR AND CRYSTALLOGRAPHY JRNL REF PLOS ONE V. 5 12312 2010 JRNL REFN ESSN 1932-6203 JRNL PMID 20808820 JRNL DOI 10.1371/JOURNAL.PONE.0012312 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.45 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 11368 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) : 0.205 REMARK 3 R VALUE (WORKING SET) : 0.202 REMARK 3 FREE R VALUE : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 599 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87 REMARK 3 REFLECTION IN BIN (WORKING SET) : 859 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.3000 REMARK 3 BIN FREE R VALUE SET COUNT : 45 REMARK 3 BIN FREE R VALUE : 0.4230 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3086 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 53 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 45.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.06 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.34000 REMARK 3 B22 (A**2) : 0.34000 REMARK 3 B33 (A**2) : -0.67000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.385 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.262 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.476 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.842 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3213 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4368 ; 1.074 ; 1.970 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 402 ; 5.092 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;38.362 ;24.504 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 520 ;15.948 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;17.797 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 491 ; 0.071 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2403 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1516 ; 0.190 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2183 ; 0.301 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 94 ; 0.108 ; 0.200 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): 60 ; 0.154 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.164 ; 0.200 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): 2048 ; 0.233 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3213 ; 0.418 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1319 ; 0.509 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1155 ; 0.871 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 2 B 199 REMARK 3 ORIGIN FOR THE GROUP (A): 37.4420 18.0650 -8.5440 REMARK 3 T TENSOR REMARK 3 T11: 0.1602 T22: 0.1543 REMARK 3 T33: 0.1136 T12: 0.0126 REMARK 3 T13: 0.0214 T23: 0.0117 REMARK 3 L TENSOR REMARK 3 L11: 1.8424 L22: 1.9601 REMARK 3 L33: 1.5646 L12: 0.6839 REMARK 3 L13: -0.2507 L23: -0.1588 REMARK 3 S TENSOR REMARK 3 S11: 0.0543 S12: 0.0279 S13: 0.0792 REMARK 3 S21: 0.0325 S22: -0.0360 S23: 0.0189 REMARK 3 S31: -0.0813 S32: 0.1255 S33: -0.0184 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 200 B 404 REMARK 3 ORIGIN FOR THE GROUP (A): 22.9550 3.7930 -23.5200 REMARK 3 T TENSOR REMARK 3 T11: 0.1227 T22: 0.1481 REMARK 3 T33: 0.1655 T12: -0.0498 REMARK 3 T13: -0.0112 T23: 0.0083 REMARK 3 L TENSOR REMARK 3 L11: 1.2799 L22: 1.0172 REMARK 3 L33: 2.8185 L12: -0.3006 REMARK 3 L13: 0.1357 L23: -0.6984 REMARK 3 S TENSOR REMARK 3 S11: 0.0396 S12: 0.2378 S13: 0.0213 REMARK 3 S21: 0.0559 S22: 0.0352 S23: 0.0719 REMARK 3 S31: 0.1015 S32: -0.1360 S33: -0.0748 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : 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 RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3IQD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-AUG-09. REMARK 100 THE DEPOSITION ID IS D_1000054733. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-OCT-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5-6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.8 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11368 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 74.330 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.0 REMARK 200 DATA REDUNDANCY : 4.500 REMARK 200 R MERGE (I) : 0.10300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5 REMARK 200 DATA REDUNDANCY IN SHELL : 4.50 REMARK 200 R MERGE FOR SHELL (I) : 0.36300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 3C7C REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CITRATE, 30% PEG 400, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.70000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 48.10000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 48.10000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.35000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 48.10000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 48.10000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 88.05000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 48.10000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.10000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 29.35000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 48.10000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.10000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 88.05000 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 58.70000 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: B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 MET B 1 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA B 36 -118.05 46.33 REMARK 500 GLN B 118 176.36 62.29 REMARK 500 PHE B 234 -96.20 -86.98 REMARK 500 ASN B 323 -142.79 32.71 REMARK 500 HIS B 401 52.41 127.84 REMARK 500 HIS B 403 86.73 97.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AG2 B 406 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3C7A RELATED DB: PDB REMARK 900 THE SAME PROTEIN IN COMPLEX WITH ODH-NADH REMARK 900 RELATED ID: 3C7C RELATED DB: PDB REMARK 900 THE SAME PROTEIN IN COMPLEX WITH ODH-NADH-L-ARGININE REMARK 900 RELATED ID: 3C7D RELATED DB: PDB REMARK 900 THE SAME PROTEIN IN COMPLEX WITH ODH-NADH-PYRUVATE REMARK 999 REMARK 999 SEQUENCE REMARK 999 THERE ARE CONFLICTS BETWEEN THE REPORTED SEQUENCE AND DATABASE REMARK 999 REFERENCE SEQUENCE. THERE ARE SEVERAL ISOFORMS KNOWN THAT DOES NOT REMARK 999 AGREE WITH THE DATABASE. THE SEQUENCE IN THE PDB IS THE CORRECT ONE REMARK 999 AND MAYBE THE MISTAKE IS IN THE DATABASE. DBREF 3IQD B 1 399 UNP Q9BHM6 Q9BHM6_PECMA 1 399 SEQADV 3IQD ASP B 272 UNP Q9BHM6 VAL 272 SEE REMARK 999 SEQADV 3IQD ALA B 315 UNP Q9BHM6 GLY 315 SEE REMARK 999 SEQADV 3IQD HIS B 400 UNP Q9BHM6 EXPRESSION TAG SEQADV 3IQD HIS B 401 UNP Q9BHM6 EXPRESSION TAG SEQADV 3IQD HIS B 402 UNP Q9BHM6 EXPRESSION TAG SEQADV 3IQD HIS B 403 UNP Q9BHM6 EXPRESSION TAG SEQADV 3IQD HIS B 404 UNP Q9BHM6 EXPRESSION TAG SEQRES 1 B 404 MET THR VAL LYS VAL CYS VAL CYS GLY GLY GLY ASN GLY SEQRES 2 B 404 ALA HIS THR LEU SER GLY LEU ALA ALA SER ARG ASP GLY SEQRES 3 B 404 VAL GLU VAL ARG VAL LEU THR LEU PHE ALA ASP GLU ALA SEQRES 4 B 404 GLU ARG TRP THR LYS ALA LEU GLY ALA ASP GLU LEU THR SEQRES 5 B 404 VAL ILE VAL ASN GLU LYS ASP GLY THR GLN THR GLU VAL SEQRES 6 B 404 LYS SER ARG PRO LYS VAL ILE THR LYS ASP PRO GLU ILE SEQRES 7 B 404 ALA ILE SER GLY ALA ASP VAL VAL ILE LEU THR VAL PRO SEQRES 8 B 404 ALA PHE ALA HIS GLU GLY TYR PHE GLN ALA MET ALA PRO SEQRES 9 B 404 TYR VAL GLN ASP SER ALA LEU ILE VAL GLY LEU PRO SER SEQRES 10 B 404 GLN ALA GLY PHE GLU PHE GLN CYS ARG ASP ILE LEU GLY SEQRES 11 B 404 ASP LYS ALA ALA ALA VAL SER MET MET SER PHE GLU THR SEQRES 12 B 404 LEU PRO TRP ALA CYS ARG ILE LYS GLU PHE GLY ARG LYS SEQRES 13 B 404 VAL GLU VAL LEU GLY THR LYS SER VAL LEU ALA ALA SER SEQRES 14 B 404 LEU ILE LYS GLY THR ALA LYS THR VAL ASP PRO LEU SER SEQRES 15 B 404 THR LEU GLN MET LEU HIS GLY ALA GLU PRO VAL PHE ARG SEQRES 16 B 404 LEU ALA LYS HIS PHE LEU GLU MET LEU ILE MET SER TYR SEQRES 17 B 404 SER PHE VAL HIS PRO ALA ILE LEU PHE GLY ARG TRP GLY SEQRES 18 B 404 SER TRP ASP GLY LYS PRO VAL PRO GLU ALA PRO LEU PHE SEQRES 19 B 404 TYR GLN GLY ILE ASP GLN ALA THR ALA ASP MET LEU THR SEQRES 20 B 404 ALA CYS SER ASN GLU CYS LYS ASP VAL ALA ASN ALA ILE SEQRES 21 B 404 MET ALA ALA CYS PRO GLY ASN ASP LEU SER ASP ASP LYS SEQRES 22 B 404 ASP ILE TYR GLN TRP TYR LEU GLU TYR TYR HIS GLU ASP SEQRES 23 B 404 ILE GLN ASP ASP HIS ASP LEU TYR HIS ALA ILE THR THR SEQRES 24 B 404 ASN LYS SER TYR LYS GLY LEU VAL HIS PRO VAL LYS ALA SEQRES 25 B 404 VAL ASP ALA GLY VAL ALA PRO ASP PHE GLY ASN ARG TYR SEQRES 26 B 404 LEU THR GLU ASP ILE PRO MET GLY MET ILE VAL PHE LYS SEQRES 27 B 404 GLY VAL ALA ILE ALA ALA GLY VAL ALA ILE PRO SER ASN SEQRES 28 B 404 ASP LYS LEU ILE MET TRP ALA GLN GLU LYS ILE GLY LYS SEQRES 29 B 404 GLU TYR LEU VAL ASP GLY ALA LEU THR GLY LYS ASP VAL SEQRES 30 B 404 ALA THR THR ARG CYS PRO GLN ARG TYR GLY PHE ASN THR SEQRES 31 B 404 LEU ASP ALA ILE LEU THR GLY LYS LYS HIS HIS HIS HIS SEQRES 32 B 404 HIS HET NAI B 405 44 HET AG2 B 406 9 HETNAM NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE HETNAM AG2 AGMATINE HETSYN NAI NADH HETSYN AG2 (4-AMINOBUTYL)GUANIDINE FORMUL 2 NAI C21 H29 N7 O14 P2 FORMUL 3 AG2 C5 H14 N4 HELIX 1 1 GLY B 11 SER B 23 1 13 HELIX 2 2 ASP B 37 GLY B 47 1 11 HELIX 3 3 ASP B 75 SER B 81 1 7 HELIX 4 4 PRO B 91 PHE B 93 5 3 HELIX 5 5 ALA B 94 ALA B 103 1 10 HELIX 6 6 GLY B 120 GLY B 130 1 11 HELIX 7 7 ASP B 131 ALA B 133 5 3 HELIX 8 8 ASP B 179 GLY B 189 1 11 HELIX 9 9 HIS B 199 MET B 206 1 8 HELIX 10 10 PHE B 210 GLY B 221 1 12 HELIX 11 11 PHE B 234 ILE B 238 5 5 HELIX 12 12 ASP B 239 CYS B 264 1 26 HELIX 13 13 ASP B 274 HIS B 284 1 11 HELIX 14 14 ASP B 292 THR B 299 1 8 HELIX 15 15 ASN B 300 LYS B 304 5 5 HELIX 16 16 GLY B 333 GLY B 345 1 13 HELIX 17 17 ILE B 348 ILE B 362 1 15 HELIX 18 18 ASP B 376 THR B 380 5 5 HELIX 19 19 CYS B 382 GLY B 387 5 6 HELIX 20 20 THR B 390 GLY B 397 1 8 SHEET 1 A 8 VAL B 71 THR B 73 0 SHEET 2 A 8 VAL B 27 LEU B 32 1 N VAL B 31 O VAL B 71 SHEET 3 A 8 VAL B 3 CYS B 8 1 N VAL B 7 O LEU B 32 SHEET 4 A 8 VAL B 85 LEU B 88 1 O ILE B 87 N CYS B 8 SHEET 5 A 8 LEU B 111 GLY B 114 1 O VAL B 113 N VAL B 86 SHEET 6 A 8 SER B 137 PHE B 141 1 O SER B 137 N ILE B 112 SHEET 7 A 8 VAL B 165 ILE B 171 -1 O SER B 169 N SER B 140 SHEET 8 A 8 VAL B 193 LEU B 196 1 O ARG B 195 N LEU B 166 SHEET 1 B 4 GLN B 62 SER B 67 0 SHEET 2 B 4 LEU B 51 ASN B 56 -1 N VAL B 53 O VAL B 65 SHEET 3 B 4 LYS B 156 THR B 162 1 O VAL B 159 N ILE B 54 SHEET 4 B 4 TRP B 146 GLU B 152 -1 N ALA B 147 O GLY B 161 SHEET 1 C 2 VAL B 310 VAL B 313 0 SHEET 2 C 2 GLY B 316 PRO B 319 -1 O ALA B 318 N LYS B 311 CISPEP 1 LEU B 115 PRO B 116 0 -3.17 CISPEP 2 GLU B 191 PRO B 192 0 -2.39 CISPEP 3 HIS B 400 HIS B 401 0 -4.56 CISPEP 4 HIS B 402 HIS B 403 0 14.29 SITE 1 AC1 15 GLY B 10 GLY B 11 ASN B 12 GLY B 13 SITE 2 AC1 15 PHE B 35 GLU B 38 PRO B 91 PHE B 93 SITE 3 AC1 15 PRO B 116 LEU B 144 TRP B 146 ALA B 147 SITE 4 AC1 15 CYS B 148 ARG B 324 HIS B 403 SITE 1 AC2 8 GLU B 142 THR B 143 MET B 206 SER B 207 SITE 2 AC2 8 HIS B 212 TRP B 278 HIS B 403 HIS B 404 CRYST1 96.200 96.200 117.400 90.00 90.00 90.00 P 41 21 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010395 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010395 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008518 0.00000 ATOM 1 N THR B 2 39.082 24.597 7.826 1.00 32.70 N ANISOU 1 N THR B 2 5219 4352 2855 -1002 431 -624 N ATOM 2 CA THR B 2 39.426 24.597 6.382 1.00 31.52 C ANISOU 2 CA THR B 2 4945 4159 2873 -895 387 -545 C ATOM 3 C THR B 2 38.900 23.323 5.742 1.00 30.22 C ANISOU 3 C THR B 2 4698 4017 2769 -764 369 -433 C ATOM 4 O THR B 2 38.975 22.248 6.342 1.00 30.73 O ANISOU 4 O THR B 2 4768 4167 2739 -773 311 -369 O ATOM 5 CB THR B 2 40.956 24.641 6.156 1.00 31.70 C ANISOU 5 CB THR B 2 4905 4265 2875 -959 241 -490 C ATOM 6 OG1 THR B 2 41.584 25.387 7.206 1.00 33.65 O ANISOU 6 OG1 THR B 2 5243 4550 2994 -1122 212 -579 O ATOM 7 CG2 THR B 2 41.290 25.276 4.805 1.00 30.84 C ANISOU 7 CG2 THR B 2 4713 4081 2925 -899 248 -468 C ATOM 8 N VAL B 3 38.358 23.449 4.534 1.00 28.88 N ANISOU 8 N VAL B 3 4457 3764 2752 -650 415 -408 N ATOM 9 CA VAL B 3 38.033 22.287 3.719 1.00 27.39 C ANISOU 9 CA VAL B 3 4183 3595 2630 -536 382 -307 C ATOM 10 C VAL B 3 39.154 22.115 2.701 1.00 26.75 C ANISOU 10 C VAL B 3 4010 3550 2605 -505 282 -233 C ATOM 11 O VAL B 3 39.520 23.065 1.992 1.00 26.65 O ANISOU 11 O VAL B 3 3976 3488 2662 -511 293 -254 O ATOM 12 CB VAL B 3 36.667 22.431 3.009 1.00 26.89 C ANISOU 12 CB VAL B 3 4094 3436 2687 -437 487 -323 C ATOM 13 CG1 VAL B 3 36.345 21.175 2.192 1.00 25.59 C ANISOU 13 CG1 VAL B 3 3850 3297 2576 -339 444 -228 C ATOM 14 CG2 VAL B 3 35.561 22.707 4.024 1.00 27.45 C ANISOU 14 CG2 VAL B 3 4243 3469 2719 -468 608 -408 C ATOM 15 N LYS B 4 39.709 20.907 2.649 1.00 26.23 N ANISOU 15 N LYS B 4 3891 3564 2513 -473 192 -145 N ATOM 16 CA LYS B 4 40.831 20.607 1.762 1.00 25.55 C ANISOU 16 CA LYS B 4 3707 3521 2479 -439 108 -78 C ATOM 17 C LYS B 4 40.362 19.734 0.613 1.00 24.23 C ANISOU 17 C LYS B 4 3476 3328 2403 -319 121 -22 C ATOM 18 O LYS B 4 39.943 18.593 0.819 1.00 24.15 O ANISOU 18 O LYS B 4 3465 3331 2380 -273 107 21 O ATOM 19 CB LYS B 4 41.965 19.930 2.536 1.00 26.34 C ANISOU 19 CB LYS B 4 3783 3729 2497 -490 -9 -21 C ATOM 20 CG LYS B 4 42.602 20.824 3.586 1.00 27.91 C ANISOU 20 CG LYS B 4 4038 3972 2593 -629 -45 -77 C ATOM 21 CD LYS B 4 43.567 20.061 4.462 1.00 29.67 C ANISOU 21 CD LYS B 4 4238 4312 2724 -679 -177 -5 C ATOM 22 CE LYS B 4 44.166 20.973 5.522 1.00 31.92 C ANISOU 22 CE LYS B 4 4587 4653 2890 -837 -223 -68 C ATOM 23 NZ LYS B 4 45.273 20.303 6.260 1.00 33.72 N ANISOU 23 NZ LYS B 4 4766 5009 3035 -889 -381 19 N ATOM 24 N VAL B 5 40.418 20.286 -0.594 1.00 23.43 N ANISOU 24 N VAL B 5 3330 3185 2387 -278 148 -24 N ATOM 25 CA VAL B 5 39.942 19.586 -1.780 1.00 22.30 C ANISOU 25 CA VAL B 5 3137 3020 2317 -179 162 16 C ATOM 26 C VAL B 5 41.099 19.219 -2.705 1.00 22.07 C ANISOU 26 C VAL B 5 3024 3041 2320 -150 113 63 C ATOM 27 O VAL B 5 41.945 20.056 -3.027 1.00 22.32 O ANISOU 27 O VAL B 5 3029 3089 2364 -195 105 57 O ATOM 28 CB VAL B 5 38.887 20.414 -2.558 1.00 22.00 C ANISOU 28 CB VAL B 5 3115 2897 2345 -146 236 -12 C ATOM 29 CG1 VAL B 5 38.337 19.615 -3.735 1.00 21.26 C ANISOU 29 CG1 VAL B 5 2977 2795 2305 -59 235 27 C ATOM 30 CG2 VAL B 5 37.747 20.847 -1.639 1.00 22.40 C ANISOU 30 CG2 VAL B 5 3233 2894 2385 -167 303 -68 C ATOM 31 N CYS B 6 41.135 17.956 -3.115 1.00 21.53 N ANISOU 31 N CYS B 6 2916 2993 2272 -78 89 105 N ATOM 32 CA CYS B 6 42.061 17.516 -4.138 1.00 21.29 C ANISOU 32 CA CYS B 6 2806 2999 2285 -33 70 136 C ATOM 33 C CYS B 6 41.325 17.370 -5.462 1.00 20.69 C ANISOU 33 C CYS B 6 2729 2882 2250 26 119 129 C ATOM 34 O CYS B 6 40.440 16.521 -5.592 1.00 20.60 O ANISOU 34 O CYS B 6 2739 2839 2248 74 129 130 O ATOM 35 CB CYS B 6 42.711 16.194 -3.744 1.00 21.58 C ANISOU 35 CB CYS B 6 2798 3076 2325 10 14 182 C ATOM 36 SG CYS B 6 43.871 15.568 -4.973 1.00 21.93 S ANISOU 36 SG CYS B 6 2734 3159 2438 79 15 205 S ATOM 37 N VAL B 7 41.679 18.208 -6.434 1.00 20.59 N ANISOU 37 N VAL B 7 2696 2871 2255 13 146 127 N ATOM 38 CA VAL B 7 41.124 18.103 -7.786 1.00 20.04 C ANISOU 38 CA VAL B 7 2627 2781 2205 58 179 130 C ATOM 39 C VAL B 7 42.038 17.226 -8.641 1.00 20.33 C ANISOU 39 C VAL B 7 2604 2869 2252 99 182 140 C ATOM 40 O VAL B 7 43.220 17.537 -8.828 1.00 20.56 O ANISOU 40 O VAL B 7 2577 2948 2289 75 185 150 O ATOM 41 CB VAL B 7 40.929 19.483 -8.456 1.00 20.06 C ANISOU 41 CB VAL B 7 2654 2754 2216 20 210 135 C ATOM 42 CG1 VAL B 7 40.295 19.328 -9.826 1.00 19.40 C ANISOU 42 CG1 VAL B 7 2578 2661 2133 60 228 152 C ATOM 43 CG2 VAL B 7 40.074 20.392 -7.581 1.00 20.21 C ANISOU 43 CG2 VAL B 7 2728 2707 2245 -12 222 114 C ATOM 44 N CYS B 8 41.476 16.123 -9.139 1.00 20.15 N ANISOU 44 N CYS B 8 2590 2830 2235 158 188 131 N ATOM 45 CA CYS B 8 42.207 15.163 -9.963 1.00 20.49 C ANISOU 45 CA CYS B 8 2588 2903 2293 206 208 121 C ATOM 46 C CYS B 8 41.944 15.365 -11.454 1.00 20.49 C ANISOU 46 C CYS B 8 2606 2913 2265 208 251 106 C ATOM 47 O CYS B 8 40.803 15.269 -11.916 1.00 20.32 O ANISOU 47 O CYS B 8 2636 2861 2224 212 246 96 O ATOM 48 CB CYS B 8 41.869 13.729 -9.542 1.00 20.58 C ANISOU 48 CB CYS B 8 2608 2880 2331 262 190 114 C ATOM 49 SG CYS B 8 42.457 13.305 -7.884 1.00 20.78 S ANISOU 49 SG CYS B 8 2609 2911 2375 262 130 155 S ATOM 50 N GLY B 9 43.010 15.646 -12.200 1.00 20.90 N ANISOU 50 N GLY B 9 2612 3019 2311 197 291 106 N ATOM 51 CA GLY B 9 42.918 15.867 -13.642 1.00 20.79 C ANISOU 51 CA GLY B 9 2622 3030 2247 185 338 96 C ATOM 52 C GLY B 9 43.521 17.180 -14.091 1.00 20.96 C ANISOU 52 C GLY B 9 2632 3086 2245 121 365 132 C ATOM 53 O GLY B 9 43.856 18.033 -13.265 1.00 20.99 O ANISOU 53 O GLY B 9 2618 3082 2277 79 343 158 O ATOM 54 N GLY B 10 43.654 17.340 -15.406 1.00 21.21 N ANISOU 54 N GLY B 10 2684 3157 2219 102 414 133 N ATOM 55 CA GLY B 10 44.169 18.575 -16.004 1.00 21.36 C ANISOU 55 CA GLY B 10 2705 3205 2207 32 448 179 C ATOM 56 C GLY B 10 43.378 19.000 -17.233 1.00 21.48 C ANISOU 56 C GLY B 10 2800 3224 2138 6 453 211 C ATOM 57 O GLY B 10 43.870 19.757 -18.070 1.00 22.04 O ANISOU 57 O GLY B 10 2884 3332 2160 -51 497 251 O ATOM 58 N GLY B 11 42.148 18.506 -17.343 1.00 20.98 N ANISOU 58 N GLY B 11 2789 3126 2056 40 402 200 N ATOM 59 CA GLY B 11 41.287 18.839 -18.470 1.00 21.43 C ANISOU 59 CA GLY B 11 2916 3194 2032 16 380 238 C ATOM 60 C GLY B 11 40.494 20.115 -18.260 1.00 21.38 C ANISOU 60 C GLY B 11 2943 3129 2054 -6 326 320 C ATOM 61 O GLY B 11 40.770 20.886 -17.335 1.00 21.05 O ANISOU 61 O GLY B 11 2878 3037 2084 -17 326 339 O ATOM 62 N ASN B 12 39.507 20.336 -19.125 1.00 21.85 N ANISOU 62 N ASN B 12 3055 3190 2058 -13 278 368 N ATOM 63 CA ASN B 12 38.603 21.479 -18.997 1.00 22.08 C ANISOU 63 CA ASN B 12 3107 3150 2133 -14 221 454 C ATOM 64 C ASN B 12 37.967 21.542 -17.611 1.00 21.29 C ANISOU 64 C ASN B 12 2973 2967 2148 32 196 427 C ATOM 65 O ASN B 12 38.007 22.582 -16.949 1.00 21.50 O ANISOU 65 O ASN B 12 3000 2923 2246 23 204 458 O ATOM 66 CB ASN B 12 37.513 21.435 -20.075 1.00 22.76 C ANISOU 66 CB ASN B 12 3236 3262 2150 -15 151 509 C ATOM 67 CG ASN B 12 38.081 21.395 -21.487 1.00 23.88 C ANISOU 67 CG ASN B 12 3430 3495 2148 -74 177 537 C ATOM 68 OD1 ASN B 12 38.897 22.240 -21.874 1.00 24.87 O ANISOU 68 OD1 ASN B 12 3575 3630 2243 -123 225 594 O ATOM 69 ND2 ASN B 12 37.644 20.413 -22.267 1.00 22.99 N ANISOU 69 ND2 ASN B 12 3344 3450 1941 -81 151 493 N ATOM 70 N GLY B 13 37.405 20.418 -17.171 1.00 20.68 N ANISOU 70 N GLY B 13 2876 2897 2086 72 176 362 N ATOM 71 CA GLY B 13 36.748 20.335 -15.872 1.00 19.92 C ANISOU 71 CA GLY B 13 2752 2735 2081 107 162 333 C ATOM 72 C GLY B 13 37.672 20.626 -14.704 1.00 19.51 C ANISOU 72 C GLY B 13 2681 2657 2073 95 205 300 C ATOM 73 O GLY B 13 37.322 21.394 -13.806 1.00 19.48 O ANISOU 73 O GLY B 13 2680 2588 2135 95 208 306 O ATOM 74 N ALA B 14 38.851 20.009 -14.725 1.00 19.44 N ANISOU 74 N ALA B 14 2651 2705 2032 82 239 264 N ATOM 75 CA ALA B 14 39.859 20.183 -13.678 1.00 19.21 C ANISOU 75 CA ALA B 14 2590 2674 2036 61 263 240 C ATOM 76 C ALA B 14 40.284 21.643 -13.539 1.00 19.75 C ANISOU 76 C ALA B 14 2672 2705 2126 6 279 279 C ATOM 77 O ALA B 14 40.393 22.164 -12.422 1.00 19.38 O ANISOU 77 O ALA B 14 2625 2615 2122 -16 279 260 O ATOM 78 CB ALA B 14 41.057 19.316 -13.965 1.00 19.30 C ANISOU 78 CB ALA B 14 2557 2756 2019 65 293 209 C ATOM 79 N HIS B 15 40.520 22.295 -14.679 1.00 20.38 N ANISOU 79 N HIS B 15 2772 2800 2170 -25 296 333 N ATOM 80 CA HIS B 15 40.813 23.723 -14.706 1.00 20.85 C ANISOU 80 CA HIS B 15 2858 2806 2258 -82 313 383 C ATOM 81 C HIS B 15 39.683 24.514 -14.067 1.00 20.70 C ANISOU 81 C HIS B 15 2876 2679 2311 -59 289 397 C ATOM 82 O HIS B 15 39.927 25.363 -13.212 1.00 21.21 O ANISOU 82 O HIS B 15 2953 2677 2428 -96 307 381 O ATOM 83 CB HIS B 15 41.042 24.206 -16.134 1.00 21.54 C ANISOU 83 CB HIS B 15 2976 2925 2286 -117 331 457 C ATOM 84 CG HIS B 15 42.431 23.973 -16.637 1.00 22.03 C ANISOU 84 CG HIS B 15 2998 3074 2297 -168 388 447 C ATOM 85 ND1 HIS B 15 42.903 22.721 -16.967 1.00 21.84 N ANISOU 85 ND1 HIS B 15 2932 3139 2227 -138 412 392 N ATOM 86 CD2 HIS B 15 43.444 24.836 -16.887 1.00 23.12 C ANISOU 86 CD2 HIS B 15 3128 3222 2435 -247 435 483 C ATOM 87 CE1 HIS B 15 44.150 22.822 -17.394 1.00 22.82 C ANISOU 87 CE1 HIS B 15 3014 3329 2328 -188 476 393 C ATOM 88 NE2 HIS B 15 44.501 24.095 -17.357 1.00 23.53 N ANISOU 88 NE2 HIS B 15 3120 3378 2442 -261 489 450 N ATOM 89 N THR B 16 38.450 24.220 -14.466 1.00 20.38 N ANISOU 89 N THR B 16 2847 2620 2275 -2 252 420 N ATOM 90 CA THR B 16 37.300 24.980 -13.988 1.00 20.48 C ANISOU 90 CA THR B 16 2877 2530 2373 34 239 439 C ATOM 91 C THR B 16 37.054 24.757 -12.502 1.00 20.02 C ANISOU 91 C THR B 16 2807 2434 2366 47 259 357 C ATOM 92 O THR B 16 36.850 25.714 -11.752 1.00 20.58 O ANISOU 92 O THR B 16 2902 2414 2504 35 288 342 O ATOM 93 CB THR B 16 36.029 24.662 -14.788 1.00 20.51 C ANISOU 93 CB THR B 16 2875 2540 2379 90 184 489 C ATOM 94 OG1 THR B 16 36.314 24.764 -16.187 1.00 20.88 O ANISOU 94 OG1 THR B 16 2946 2642 2347 65 160 564 O ATOM 95 CG2 THR B 16 34.926 25.642 -14.434 1.00 20.79 C ANISOU 95 CG2 THR B 16 2912 2462 2526 134 177 527 C ATOM 96 N LEU B 17 37.092 23.495 -12.085 1.00 19.30 N ANISOU 96 N LEU B 17 2687 2409 2236 65 249 303 N ATOM 97 CA LEU B 17 36.847 23.136 -10.696 1.00 18.78 C ANISOU 97 CA LEU B 17 2617 2324 2195 70 265 236 C ATOM 98 C LEU B 17 37.951 23.681 -9.799 1.00 18.91 C ANISOU 98 C LEU B 17 2649 2335 2203 4 290 199 C ATOM 99 O LEU B 17 37.673 24.216 -8.734 1.00 19.49 O ANISOU 99 O LEU B 17 2749 2351 2307 -15 316 156 O ATOM 100 CB LEU B 17 36.758 21.623 -10.544 1.00 18.16 C ANISOU 100 CB LEU B 17 2511 2313 2076 97 244 205 C ATOM 101 CG LEU B 17 35.842 20.958 -9.510 1.00 17.96 C ANISOU 101 CG LEU B 17 2482 2268 2074 122 250 163 C ATOM 102 CD1 LEU B 17 36.631 19.836 -8.866 1.00 17.21 C ANISOU 102 CD1 LEU B 17 2378 2229 1932 111 240 133 C ATOM 103 CD2 LEU B 17 35.270 21.890 -8.439 1.00 17.50 C ANISOU 103 CD2 LEU B 17 2448 2135 2067 111 293 133 C ATOM 104 N SER B 18 39.202 23.547 -10.230 1.00 18.88 N ANISOU 104 N SER B 18 2623 2396 2156 -36 285 212 N ATOM 105 CA SER B 18 40.322 24.108 -9.484 1.00 19.09 C ANISOU 105 CA SER B 18 2647 2429 2177 -112 295 185 C ATOM 106 C SER B 18 40.146 25.609 -9.364 1.00 19.66 C ANISOU 106 C SER B 18 2771 2400 2300 -158 326 191 C ATOM 107 O SER B 18 40.347 26.173 -8.292 1.00 20.18 O ANISOU 107 O SER B 18 2866 2425 2378 -211 340 138 O ATOM 108 CB SER B 18 41.655 23.793 -10.162 1.00 19.29 C ANISOU 108 CB SER B 18 2620 2543 2167 -144 292 208 C ATOM 109 OG SER B 18 41.917 22.404 -10.131 1.00 18.93 O ANISOU 109 OG SER B 18 2526 2574 2091 -97 271 193 O ATOM 110 N GLY B 19 39.754 26.241 -10.470 1.00 19.72 N ANISOU 110 N GLY B 19 2796 2361 2334 -139 334 258 N ATOM 111 CA GLY B 19 39.530 27.674 -10.513 1.00 20.19 C ANISOU 111 CA GLY B 19 2909 2302 2460 -170 364 282 C ATOM 112 C GLY B 19 38.439 28.089 -9.553 1.00 20.17 C ANISOU 112 C GLY B 19 2942 2197 2526 -133 389 230 C ATOM 113 O GLY B 19 38.639 28.970 -8.716 1.00 20.62 O ANISOU 113 O GLY B 19 3043 2172 2620 -188 427 177 O ATOM 114 N LEU B 20 37.289 27.431 -9.660 1.00 19.67 N ANISOU 114 N LEU B 20 2856 2140 2480 -47 375 238 N ATOM 115 CA LEU B 20 36.125 27.792 -8.855 1.00 19.87 C ANISOU 115 CA LEU B 20 2897 2072 2582 -1 414 193 C ATOM 116 C LEU B 20 36.290 27.476 -7.370 1.00 19.68 C ANISOU 116 C LEU B 20 2892 2062 2523 -41 448 87 C ATOM 117 O LEU B 20 36.082 28.345 -6.519 1.00 20.50 O ANISOU 117 O LEU B 20 3045 2071 2672 -68 506 24 O ATOM 118 CB LEU B 20 34.848 27.168 -9.424 1.00 19.47 C ANISOU 118 CB LEU B 20 2798 2034 2564 93 386 237 C ATOM 119 CG LEU B 20 34.340 27.787 -10.733 1.00 19.99 C ANISOU 119 CG LEU B 20 2856 2056 2683 138 350 346 C ATOM 120 CD1 LEU B 20 33.022 27.146 -11.162 1.00 19.55 C ANISOU 120 CD1 LEU B 20 2741 2024 2663 221 309 381 C ATOM 121 CD2 LEU B 20 34.193 29.308 -10.628 1.00 20.45 C ANISOU 121 CD2 LEU B 20 2959 1962 2849 138 393 369 C ATOM 122 N ALA B 21 36.677 26.240 -7.069 1.00 18.78 N ANISOU 122 N ALA B 21 2747 2062 2325 -49 413 69 N ATOM 123 CA ALA B 21 36.845 25.796 -5.687 1.00 18.47 C ANISOU 123 CA ALA B 21 2731 2056 2232 -91 429 -10 C ATOM 124 C ALA B 21 37.848 26.655 -4.905 1.00 19.03 C ANISOU 124 C ALA B 21 2851 2106 2274 -194 444 -65 C ATOM 125 O ALA B 21 37.582 27.025 -3.762 1.00 19.66 O ANISOU 125 O ALA B 21 2984 2145 2341 -234 489 -145 O ATOM 126 CB ALA B 21 37.235 24.319 -5.646 1.00 17.52 C ANISOU 126 CB ALA B 21 2568 2054 2037 -79 376 5 C ATOM 127 N ALA B 22 38.979 26.990 -5.531 1.00 18.80 N ANISOU 127 N ALA B 22 2805 2106 2233 -246 411 -27 N ATOM 128 CA ALA B 22 40.042 27.764 -4.877 1.00 19.21 C ANISOU 128 CA ALA B 22 2890 2151 2258 -361 411 -74 C ATOM 129 C ALA B 22 39.657 29.210 -4.580 1.00 20.15 C ANISOU 129 C ALA B 22 3087 2122 2448 -400 478 -123 C ATOM 130 O ALA B 22 40.289 29.866 -3.750 1.00 21.13 O ANISOU 130 O ALA B 22 3260 2222 2546 -506 490 -194 O ATOM 131 CB ALA B 22 41.322 27.713 -5.695 1.00 19.15 C ANISOU 131 CB ALA B 22 2826 2218 2232 -407 368 -16 C ATOM 132 N SER B 23 38.619 29.700 -5.253 1.00 20.23 N ANISOU 132 N SER B 23 3108 2027 2552 -316 519 -85 N ATOM 133 CA SER B 23 38.126 31.064 -5.045 1.00 21.23 C ANISOU 133 CA SER B 23 3304 1985 2776 -327 592 -123 C ATOM 134 C SER B 23 37.277 31.224 -3.775 1.00 21.76 C ANISOU 134 C SER B 23 3424 1988 2854 -320 666 -238 C ATOM 135 O SER B 23 36.947 32.340 -3.384 1.00 22.68 O ANISOU 135 O SER B 23 3609 1960 3050 -338 743 -300 O ATOM 136 CB SER B 23 37.326 31.524 -6.263 1.00 21.33 C ANISOU 136 CB SER B 23 3299 1909 2897 -230 598 -21 C ATOM 137 OG SER B 23 36.030 30.953 -6.273 1.00 20.30 O ANISOU 137 OG SER B 23 3129 1778 2807 -117 609 -12 O ATOM 138 N ARG B 24 36.929 30.109 -3.141 1.00 21.31 N ANISOU 138 N ARG B 24 3340 2035 2720 -295 653 -267 N ATOM 139 CA ARG B 24 36.060 30.122 -1.964 1.00 22.20 C ANISOU 139 CA ARG B 24 3499 2109 2827 -289 735 -370 C ATOM 140 C ARG B 24 36.861 30.329 -0.672 1.00 23.34 C ANISOU 140 C ARG B 24 3724 2287 2859 -425 746 -480 C ATOM 141 O ARG B 24 37.992 29.847 -0.553 1.00 23.28 O ANISOU 141 O ARG B 24 3699 2394 2750 -504 660 -458 O ATOM 142 CB ARG B 24 35.247 28.819 -1.884 1.00 21.03 C ANISOU 142 CB ARG B 24 3290 2053 2646 -211 721 -341 C ATOM 143 CG ARG B 24 34.679 28.311 -3.218 1.00 19.76 C ANISOU 143 CG ARG B 24 3042 1909 2556 -102 673 -227 C ATOM 144 CD ARG B 24 33.720 29.304 -3.858 1.00 19.80 C ANISOU 144 CD ARG B 24 3036 1774 2715 -19 724 -198 C ATOM 145 NE ARG B 24 33.197 28.818 -5.132 1.00 19.14 N ANISOU 145 NE ARG B 24 2872 1723 2678 69 659 -83 N ATOM 146 CZ ARG B 24 32.428 29.532 -5.949 1.00 19.71 C ANISOU 146 CZ ARG B 24 2915 1698 2876 149 664 -16 C ATOM 147 NH1 ARG B 24 32.088 30.774 -5.636 1.00 20.89 N ANISOU 147 NH1 ARG B 24 3105 1694 3137 164 741 -52 N ATOM 148 NH2 ARG B 24 31.996 29.003 -7.085 1.00 19.42 N ANISOU 148 NH2 ARG B 24 2810 1714 2853 212 589 87 N ATOM 149 N ASP B 25 36.280 31.049 0.287 1.00 24.71 N ANISOU 149 N ASP B 25 3979 2363 3048 -454 851 -598 N ATOM 150 CA ASP B 25 36.926 31.235 1.582 1.00 26.17 C ANISOU 150 CA ASP B 25 4254 2586 3102 -595 862 -714 C ATOM 151 C ASP B 25 37.004 29.910 2.343 1.00 25.73 C ANISOU 151 C ASP B 25 4183 2697 2897 -617 809 -707 C ATOM 152 O ASP B 25 36.076 29.097 2.296 1.00 24.98 O ANISOU 152 O ASP B 25 4043 2631 2815 -524 835 -673 O ATOM 153 CB ASP B 25 36.201 32.296 2.427 1.00 27.88 C ANISOU 153 CB ASP B 25 4574 2653 3366 -620 1008 -860 C ATOM 154 CG ASP B 25 36.371 33.720 1.882 1.00 29.60 C ANISOU 154 CG ASP B 25 4835 2688 3723 -632 1055 -880 C ATOM 155 OD1 ASP B 25 37.016 33.915 0.820 1.00 29.16 O ANISOU 155 OD1 ASP B 25 4729 2627 3723 -625 977 -773 O ATOM 156 OD2 ASP B 25 35.845 34.655 2.531 1.00 31.25 O ANISOU 156 OD2 ASP B 25 5133 2752 3989 -650 1181 -1007 O ATOM 157 N GLY B 26 38.125 29.700 3.032 1.00 26.41 N ANISOU 157 N GLY B 26 4302 2889 2845 -745 729 -730 N ATOM 158 CA GLY B 26 38.340 28.499 3.835 1.00 26.37 C ANISOU 158 CA GLY B 26 4293 3038 2691 -778 663 -709 C ATOM 159 C GLY B 26 38.475 27.230 3.015 1.00 25.15 C ANISOU 159 C GLY B 26 4025 2980 2552 -682 572 -571 C ATOM 160 O GLY B 26 38.208 26.133 3.509 1.00 24.86 O ANISOU 160 O GLY B 26 3979 3031 2437 -662 546 -539 O ATOM 161 N VAL B 27 38.875 27.379 1.756 1.00 24.65 N ANISOU 161 N VAL B 27 3884 2894 2589 -626 530 -492 N ATOM 162 CA VAL B 27 39.091 26.234 0.883 1.00 23.84 C ANISOU 162 CA VAL B 27 3681 2876 2502 -541 451 -377 C ATOM 163 C VAL B 27 40.529 26.211 0.374 1.00 24.17 C ANISOU 163 C VAL B 27 3662 2991 2532 -591 355 -322 C ATOM 164 O VAL B 27 41.058 27.217 -0.103 1.00 24.73 O ANISOU 164 O VAL B 27 3736 3007 2654 -639 364 -333 O ATOM 165 CB VAL B 27 38.092 26.188 -0.295 1.00 22.92 C ANISOU 165 CB VAL B 27 3513 2685 2509 -412 496 -324 C ATOM 166 CG1 VAL B 27 38.354 24.968 -1.168 1.00 22.06 C ANISOU 166 CG1 VAL B 27 3316 2664 2400 -340 420 -225 C ATOM 167 CG2 VAL B 27 36.674 26.137 0.221 1.00 23.20 C ANISOU 167 CG2 VAL B 27 3581 2661 2572 -359 590 -373 C ATOM 168 N GLU B 28 41.152 25.049 0.502 1.00 24.15 N ANISOU 168 N GLU B 28 3599 3108 2467 -581 267 -260 N ATOM 169 CA GLU B 28 42.520 24.844 0.085 1.00 24.59 C ANISOU 169 CA GLU B 28 3574 3250 2520 -616 178 -204 C ATOM 170 C GLU B 28 42.486 23.778 -0.998 1.00 23.53 C ANISOU 170 C GLU B 28 3350 3152 2438 -497 156 -116 C ATOM 171 O GLU B 28 41.998 22.668 -0.765 1.00 23.32 O ANISOU 171 O GLU B 28 3316 3158 2387 -433 141 -87 O ATOM 172 CB GLU B 28 43.351 24.394 1.287 1.00 25.38 C ANISOU 172 CB GLU B 28 3678 3460 2506 -707 88 -210 C ATOM 173 CG GLU B 28 44.717 23.818 0.959 1.00 26.17 C ANISOU 173 CG GLU B 28 3660 3671 2612 -716 -17 -133 C ATOM 174 CD GLU B 28 45.440 23.285 2.187 1.00 27.22 C ANISOU 174 CD GLU B 28 3790 3917 2635 -794 -125 -118 C ATOM 175 OE1 GLU B 28 45.330 23.904 3.275 1.00 28.25 O ANISOU 175 OE1 GLU B 28 4018 4049 2669 -908 -127 -192 O ATOM 176 OE2 GLU B 28 46.125 22.246 2.055 1.00 28.10 O ANISOU 176 OE2 GLU B 28 3803 4116 2757 -741 -209 -31 O ATOM 177 N VAL B 29 42.980 24.119 -2.186 1.00 23.19 N ANISOU 177 N VAL B 29 3248 3099 2465 -476 162 -78 N ATOM 178 CA VAL B 29 42.927 23.196 -3.313 1.00 22.06 C ANISOU 178 CA VAL B 29 3034 2985 2364 -372 156 -11 C ATOM 179 C VAL B 29 44.307 22.658 -3.648 1.00 22.27 C ANISOU 179 C VAL B 29 2959 3112 2392 -383 97 35 C ATOM 180 O VAL B 29 45.253 23.423 -3.818 1.00 23.12 O ANISOU 180 O VAL B 29 3031 3240 2512 -460 87 34 O ATOM 181 CB VAL B 29 42.262 23.833 -4.566 1.00 21.69 C ANISOU 181 CB VAL B 29 2999 2857 2386 -324 218 6 C ATOM 182 CG1 VAL B 29 42.238 22.848 -5.733 1.00 20.60 C ANISOU 182 CG1 VAL B 29 2799 2760 2267 -234 211 62 C ATOM 183 CG2 VAL B 29 40.847 24.280 -4.243 1.00 21.48 C ANISOU 183 CG2 VAL B 29 3047 2731 2382 -293 275 -32 C ATOM 184 N ARG B 30 44.409 21.333 -3.716 1.00 21.81 N ANISOU 184 N ARG B 30 2849 3109 2329 -306 61 75 N ATOM 185 CA ARG B 30 45.595 20.659 -4.231 1.00 21.84 C ANISOU 185 CA ARG B 30 2741 3196 2363 -280 23 122 C ATOM 186 C ARG B 30 45.194 20.008 -5.543 1.00 21.08 C ANISOU 186 C ARG B 30 2622 3079 2309 -180 73 142 C ATOM 187 O ARG B 30 44.255 19.216 -5.579 1.00 20.91 O ANISOU 187 O ARG B 30 2638 3022 2283 -111 83 142 O ATOM 188 CB ARG B 30 46.099 19.578 -3.263 1.00 22.22 C ANISOU 188 CB ARG B 30 2747 3312 2384 -262 -59 155 C ATOM 189 CG ARG B 30 46.307 20.017 -1.808 1.00 22.94 C ANISOU 189 CG ARG B 30 2884 3435 2399 -365 -124 136 C ATOM 190 CD ARG B 30 45.092 19.679 -0.941 1.00 21.76 C ANISOU 190 CD ARG B 30 2846 3238 2185 -355 -110 114 C ATOM 191 NE ARG B 30 45.398 19.741 0.489 1.00 22.48 N ANISOU 191 NE ARG B 30 2978 3383 2179 -446 -182 110 N ATOM 192 CZ ARG B 30 45.747 18.697 1.241 1.00 22.25 C ANISOU 192 CZ ARG B 30 2927 3419 2108 -428 -267 174 C ATOM 193 NH1 ARG B 30 45.849 17.483 0.716 1.00 21.88 N ANISOU 193 NH1 ARG B 30 2814 3374 2124 -315 -284 242 N ATOM 194 NH2 ARG B 30 45.996 18.867 2.530 1.00 23.11 N ANISOU 194 NH2 ARG B 30 3088 3586 2108 -528 -338 172 N ATOM 195 N VAL B 31 45.880 20.356 -6.626 1.00 21.00 N ANISOU 195 N VAL B 31 2554 3093 2332 -185 109 156 N ATOM 196 CA VAL B 31 45.605 19.744 -7.920 1.00 20.10 C ANISOU 196 CA VAL B 31 2426 2974 2237 -106 158 168 C ATOM 197 C VAL B 31 46.500 18.522 -8.101 1.00 20.41 C ANISOU 197 C VAL B 31 2368 3080 2309 -42 144 185 C ATOM 198 O VAL B 31 47.728 18.624 -8.020 1.00 21.23 O ANISOU 198 O VAL B 31 2374 3250 2440 -71 130 200 O ATOM 199 CB VAL B 31 45.806 20.738 -9.089 1.00 20.28 C ANISOU 199 CB VAL B 31 2452 2989 2265 -146 217 179 C ATOM 200 CG1 VAL B 31 45.497 20.076 -10.422 1.00 19.93 C ANISOU 200 CG1 VAL B 31 2406 2952 2213 -77 265 186 C ATOM 201 CG2 VAL B 31 44.925 21.964 -8.911 1.00 20.07 C ANISOU 201 CG2 VAL B 31 2519 2876 2231 -197 231 171 C ATOM 202 N LEU B 32 45.879 17.366 -8.325 1.00 19.83 N ANISOU 202 N LEU B 32 2314 2980 2240 45 150 180 N ATOM 203 CA LEU B 32 46.616 16.156 -8.679 1.00 20.08 C ANISOU 203 CA LEU B 32 2264 3046 2319 124 156 188 C ATOM 204 C LEU B 32 46.386 15.783 -10.137 1.00 19.85 C ANISOU 204 C LEU B 32 2245 3007 2288 170 236 160 C ATOM 205 O LEU B 32 45.244 15.705 -10.602 1.00 19.31 O ANISOU 205 O LEU B 32 2262 2888 2185 182 252 141 O ATOM 206 CB LEU B 32 46.236 14.980 -7.772 1.00 19.98 C ANISOU 206 CB LEU B 32 2269 3002 2320 183 102 204 C ATOM 207 CG LEU B 32 46.975 13.651 -7.990 1.00 20.72 C ANISOU 207 CG LEU B 32 2282 3105 2485 278 104 218 C ATOM 208 CD1 LEU B 32 48.468 13.785 -7.709 1.00 21.83 C ANISOU 208 CD1 LEU B 32 2289 3326 2681 272 74 253 C ATOM 209 CD2 LEU B 32 46.377 12.535 -7.142 1.00 20.67 C ANISOU 209 CD2 LEU B 32 2321 3042 2489 330 54 244 C ATOM 210 N THR B 33 47.481 15.563 -10.855 1.00 20.25 N ANISOU 210 N THR B 33 2205 3113 2375 190 285 155 N ATOM 211 CA THR B 33 47.410 15.028 -12.208 1.00 20.16 C ANISOU 211 CA THR B 33 2204 3104 2353 234 370 116 C ATOM 212 C THR B 33 48.567 14.061 -12.442 1.00 21.14 C ANISOU 212 C THR B 33 2214 3265 2554 307 412 102 C ATOM 213 O THR B 33 49.733 14.419 -12.265 1.00 21.96 O ANISOU 213 O THR B 33 2204 3434 2706 287 419 124 O ATOM 214 CB THR B 33 47.327 16.143 -13.295 1.00 20.06 C ANISOU 214 CB THR B 33 2230 3118 2276 162 429 116 C ATOM 215 OG1 THR B 33 47.692 15.608 -14.573 1.00 20.34 O ANISOU 215 OG1 THR B 33 2250 3187 2292 192 521 78 O ATOM 216 CG2 THR B 33 48.232 17.305 -12.966 1.00 20.35 C ANISOU 216 CG2 THR B 33 2204 3201 2327 78 425 152 C ATOM 217 N LEU B 34 48.227 12.830 -12.817 1.00 21.17 N ANISOU 217 N LEU B 34 2242 3220 2580 391 442 62 N ATOM 218 CA LEU B 34 49.221 11.775 -13.009 1.00 22.21 C ANISOU 218 CA LEU B 34 2271 3359 2807 483 491 41 C ATOM 219 C LEU B 34 49.560 11.553 -14.479 1.00 23.08 C ANISOU 219 C LEU B 34 2376 3496 2896 498 624 -31 C ATOM 220 O LEU B 34 50.318 10.638 -14.803 1.00 24.44 O ANISOU 220 O LEU B 34 2470 3663 3152 582 692 -69 O ATOM 221 CB LEU B 34 48.738 10.457 -12.402 1.00 22.08 C ANISOU 221 CB LEU B 34 2288 3253 2848 570 448 40 C ATOM 222 CG LEU B 34 48.164 10.445 -10.985 1.00 21.08 C ANISOU 222 CG LEU B 34 2200 3090 2719 555 327 106 C ATOM 223 CD1 LEU B 34 47.254 9.238 -10.834 1.00 20.73 C ANISOU 223 CD1 LEU B 34 2240 2942 2693 614 316 88 C ATOM 224 CD2 LEU B 34 49.255 10.459 -9.920 1.00 20.44 C ANISOU 224 CD2 LEU B 34 2000 3057 2712 571 252 179 C ATOM 225 N PHE B 35 49.000 12.380 -15.363 1.00 22.57 N ANISOU 225 N PHE B 35 2397 3458 2720 419 662 -48 N ATOM 226 CA PHE B 35 49.299 12.292 -16.792 1.00 23.32 C ANISOU 226 CA PHE B 35 2505 3595 2760 410 788 -111 C ATOM 227 C PHE B 35 50.710 12.794 -17.089 1.00 24.30 C ANISOU 227 C PHE B 35 2494 3810 2928 390 869 -100 C ATOM 228 O PHE B 35 50.933 13.990 -17.281 1.00 24.16 O ANISOU 228 O PHE B 35 2472 3850 2859 294 874 -56 O ATOM 229 CB PHE B 35 48.255 13.038 -17.628 1.00 22.72 C ANISOU 229 CB PHE B 35 2565 3526 2543 326 786 -112 C ATOM 230 CG PHE B 35 48.406 12.838 -19.115 1.00 24.31 C ANISOU 230 CG PHE B 35 2809 3774 2653 306 906 -178 C ATOM 231 CD1 PHE B 35 48.824 11.612 -19.637 1.00 25.34 C ANISOU 231 CD1 PHE B 35 2920 3889 2820 381 1001 -272 C ATOM 232 CD2 PHE B 35 48.102 13.872 -20.001 1.00 25.13 C ANISOU 232 CD2 PHE B 35 2985 3931 2631 209 927 -147 C ATOM 233 CE1 PHE B 35 48.953 11.427 -21.020 1.00 26.73 C ANISOU 233 CE1 PHE B 35 3150 4113 2892 351 1124 -349 C ATOM 234 CE2 PHE B 35 48.228 13.696 -21.388 1.00 26.05 C ANISOU 234 CE2 PHE B 35 3157 4103 2636 176 1036 -205 C ATOM 235 CZ PHE B 35 48.654 12.472 -21.894 1.00 26.65 C ANISOU 235 CZ PHE B 35 3217 4175 2734 243 1139 -313 C ATOM 236 N ALA B 36 51.654 11.857 -17.121 1.00 25.42 N ANISOU 236 N ALA B 36 2522 3958 3180 481 937 -139 N ATOM 237 CA ALA B 36 53.067 12.162 -17.327 1.00 26.73 C ANISOU 237 CA ALA B 36 2525 4213 3420 478 1020 -131 C ATOM 238 C ALA B 36 53.496 13.332 -16.440 1.00 26.32 C ANISOU 238 C ALA B 36 2400 4214 3387 391 925 -39 C ATOM 239 O ALA B 36 53.411 13.231 -15.216 1.00 25.88 O ANISOU 239 O ALA B 36 2315 4128 3390 413 799 14 O ATOM 240 CB ALA B 36 53.354 12.428 -18.803 1.00 27.51 C ANISOU 240 CB ALA B 36 2649 4376 3427 428 1181 -193 C ATOM 241 N ASP B 37 53.929 14.435 -17.052 1.00 26.74 N ANISOU 241 N ASP B 37 2435 4344 3381 284 987 -21 N ATOM 242 CA ASP B 37 54.365 15.618 -16.310 1.00 26.65 C ANISOU 242 CA ASP B 37 2364 4376 3386 183 910 54 C ATOM 243 C ASP B 37 53.441 16.817 -16.520 1.00 25.79 C ANISOU 243 C ASP B 37 2409 4239 3152 69 875 88 C ATOM 244 O ASP B 37 53.890 17.965 -16.504 1.00 26.14 O ANISOU 244 O ASP B 37 2425 4323 3184 -41 877 132 O ATOM 245 CB ASP B 37 55.797 16.000 -16.687 1.00 28.20 C ANISOU 245 CB ASP B 37 2385 4678 3653 141 1006 62 C ATOM 246 CG ASP B 37 56.787 14.893 -16.421 1.00 29.47 C ANISOU 246 CG ASP B 37 2364 4865 3966 263 1037 40 C ATOM 247 OD1 ASP B 37 56.739 14.285 -15.328 1.00 28.64 O ANISOU 247 OD1 ASP B 37 2217 4719 3944 337 915 71 O ATOM 248 OD2 ASP B 37 57.624 14.643 -17.311 1.00 30.87 O ANISOU 248 OD2 ASP B 37 2439 5105 4184 284 1188 -4 O ATOM 249 N GLU B 38 52.152 16.546 -16.712 1.00 24.89 N ANISOU 249 N GLU B 38 2450 4052 2957 95 840 69 N ATOM 250 CA GLU B 38 51.150 17.600 -16.837 1.00 24.17 C ANISOU 250 CA GLU B 38 2497 3919 2769 12 793 109 C ATOM 251 C GLU B 38 51.229 18.576 -15.665 1.00 23.98 C ANISOU 251 C GLU B 38 2453 3874 2783 -58 694 163 C ATOM 252 O GLU B 38 51.047 19.778 -15.843 1.00 24.12 O ANISOU 252 O GLU B 38 2527 3879 2758 -154 692 203 O ATOM 253 CB GLU B 38 49.748 16.999 -16.930 1.00 22.96 C ANISOU 253 CB GLU B 38 2477 3689 2557 66 745 84 C ATOM 254 CG GLU B 38 48.667 17.977 -17.354 1.00 22.39 C ANISOU 254 CG GLU B 38 2538 3579 2390 -2 713 124 C ATOM 255 CD GLU B 38 47.378 17.281 -17.762 1.00 22.59 C ANISOU 255 CD GLU B 38 2673 3556 2354 46 683 93 C ATOM 256 OE1 GLU B 38 46.762 16.603 -16.910 1.00 22.41 O ANISOU 256 OE1 GLU B 38 2662 3477 2378 105 614 75 O ATOM 257 OE2 GLU B 38 46.972 17.420 -18.936 1.00 22.98 O ANISOU 257 OE2 GLU B 38 2798 3628 2304 16 726 91 O ATOM 258 N ALA B 39 51.515 18.051 -14.475 1.00 24.11 N ANISOU 258 N ALA B 39 2398 3885 2880 -12 613 164 N ATOM 259 CA ALA B 39 51.578 18.859 -13.256 1.00 24.12 C ANISOU 259 CA ALA B 39 2391 3871 2902 -82 513 200 C ATOM 260 C ALA B 39 52.656 19.943 -13.316 1.00 25.38 C ANISOU 260 C ALA B 39 2462 4093 3087 -197 539 228 C ATOM 261 O ALA B 39 52.391 21.101 -12.987 1.00 25.09 O ANISOU 261 O ALA B 39 2491 4020 3022 -298 507 250 O ATOM 262 CB ALA B 39 51.779 17.972 -12.052 1.00 24.04 C ANISOU 262 CB ALA B 39 2317 3861 2956 -15 422 203 C ATOM 263 N GLU B 40 53.862 19.563 -13.740 1.00 26.91 N ANISOU 263 N GLU B 40 2506 4375 3345 -184 606 224 N ATOM 264 CA GLU B 40 54.952 20.522 -13.935 1.00 28.38 C ANISOU 264 CA GLU B 40 2589 4632 3563 -301 648 250 C ATOM 265 C GLU B 40 54.619 21.540 -15.016 1.00 28.24 C ANISOU 265 C GLU B 40 2676 4592 3462 -393 737 268 C ATOM 266 O GLU B 40 54.923 22.721 -14.861 1.00 28.79 O ANISOU 266 O GLU B 40 2751 4657 3532 -520 728 301 O ATOM 267 CB GLU B 40 56.260 19.812 -14.291 1.00 30.16 C ANISOU 267 CB GLU B 40 2617 4960 3883 -254 722 240 C ATOM 268 CG GLU B 40 56.994 19.188 -13.104 1.00 31.99 C ANISOU 268 CG GLU B 40 2695 5234 4224 -205 614 257 C ATOM 269 CD GLU B 40 58.479 18.965 -13.381 1.00 35.14 C ANISOU 269 CD GLU B 40 2863 5748 4741 -202 680 265 C ATOM 270 OE1 GLU B 40 59.077 18.087 -12.723 1.00 36.61 O ANISOU 270 OE1 GLU B 40 2907 5970 5034 -110 617 280 O ATOM 271 OE2 GLU B 40 59.049 19.663 -14.254 1.00 35.76 O ANISOU 271 OE2 GLU B 40 2896 5881 4811 -291 796 264 O ATOM 272 N ARG B 41 53.999 21.076 -16.103 1.00 27.77 N ANISOU 272 N ARG B 41 2704 4518 3330 -334 816 249 N ATOM 273 CA ARG B 41 53.614 21.939 -17.223 1.00 27.86 C ANISOU 273 CA ARG B 41 2825 4514 3244 -413 892 280 C ATOM 274 C ARG B 41 52.646 23.032 -16.768 1.00 26.72 C ANISOU 274 C ARG B 41 2819 4267 3065 -478 807 324 C ATOM 275 O ARG B 41 52.900 24.213 -16.983 1.00 27.48 O ANISOU 275 O ARG B 41 2941 4347 3152 -594 830 374 O ATOM 276 CB ARG B 41 53.013 21.117 -18.377 1.00 27.94 C ANISOU 276 CB ARG B 41 2917 4532 3167 -338 968 246 C ATOM 277 CG ARG B 41 54.011 20.215 -19.125 1.00 30.00 C ANISOU 277 CG ARG B 41 3059 4888 3450 -290 1098 193 C ATOM 278 CD ARG B 41 54.827 20.981 -20.162 1.00 32.85 C ANISOU 278 CD ARG B 41 3389 5329 3765 -401 1231 222 C ATOM 279 NE ARG B 41 56.199 20.471 -20.262 1.00 35.84 N ANISOU 279 NE ARG B 41 3572 5805 4238 -381 1336 184 N ATOM 280 CZ ARG B 41 56.712 19.836 -21.317 1.00 37.68 C ANISOU 280 CZ ARG B 41 3765 6112 4441 -351 1493 129 C ATOM 281 NH1 ARG B 41 55.983 19.618 -22.406 1.00 37.70 N ANISOU 281 NH1 ARG B 41 3920 6108 4296 -349 1560 103 N ATOM 282 NH2 ARG B 41 57.974 19.419 -21.288 1.00 39.32 N ANISOU 282 NH2 ARG B 41 3772 6402 4764 -325 1587 97 N ATOM 283 N TRP B 42 51.552 22.627 -16.122 1.00 25.13 N ANISOU 283 N TRP B 42 2703 3991 2855 -403 718 306 N ATOM 284 CA TRP B 42 50.573 23.545 -15.535 1.00 23.93 C ANISOU 284 CA TRP B 42 2668 3734 2691 -441 642 333 C ATOM 285 C TRP B 42 51.274 24.570 -14.649 1.00 24.44 C ANISOU 285 C TRP B 42 2687 3784 2813 -552 608 346 C ATOM 286 O TRP B 42 50.991 25.766 -14.728 1.00 24.63 O ANISOU 286 O TRP B 42 2793 3736 2831 -638 610 383 O ATOM 287 CB TRP B 42 49.552 22.748 -14.716 1.00 22.53 C ANISOU 287 CB TRP B 42 2539 3502 2518 -343 560 296 C ATOM 288 CG TRP B 42 48.280 23.480 -14.321 1.00 21.60 C ANISOU 288 CG TRP B 42 2547 3274 2384 -350 505 314 C ATOM 289 CD1 TRP B 42 48.132 24.815 -14.083 1.00 21.69 C ANISOU 289 CD1 TRP B 42 2617 3213 2411 -437 496 346 C ATOM 290 CD2 TRP B 42 46.995 22.889 -14.070 1.00 20.51 C ANISOU 290 CD2 TRP B 42 2483 3081 2229 -265 458 295 C ATOM 291 NE1 TRP B 42 46.836 25.098 -13.729 1.00 20.64 N ANISOU 291 NE1 TRP B 42 2584 2982 2278 -399 454 347 N ATOM 292 CE2 TRP B 42 46.117 23.934 -13.709 1.00 19.80 C ANISOU 292 CE2 TRP B 42 2482 2891 2149 -298 428 318 C ATOM 293 CE3 TRP B 42 46.498 21.578 -14.128 1.00 19.91 C ANISOU 293 CE3 TRP B 42 2404 3022 2139 -169 444 259 C ATOM 294 CZ2 TRP B 42 44.771 23.712 -13.401 1.00 19.11 C ANISOU 294 CZ2 TRP B 42 2464 2736 2061 -233 388 308 C ATOM 295 CZ3 TRP B 42 45.160 21.358 -13.825 1.00 19.10 C ANISOU 295 CZ3 TRP B 42 2378 2852 2028 -119 398 252 C ATOM 296 CH2 TRP B 42 44.313 22.421 -13.460 1.00 18.63 C ANISOU 296 CH2 TRP B 42 2390 2708 1981 -150 371 277 C ATOM 297 N THR B 43 52.202 24.085 -13.823 1.00 24.80 N ANISOU 297 N THR B 43 2603 3898 2920 -552 573 318 N ATOM 298 CA THR B 43 52.973 24.914 -12.895 1.00 25.42 C ANISOU 298 CA THR B 43 2622 3986 3051 -667 524 320 C ATOM 299 C THR B 43 53.821 25.965 -13.615 1.00 26.74 C ANISOU 299 C THR B 43 2752 4177 3230 -799 602 359 C ATOM 300 O THR B 43 53.756 27.148 -13.273 1.00 27.08 O ANISOU 300 O THR B 43 2859 4147 3282 -913 584 373 O ATOM 301 CB THR B 43 53.860 24.045 -11.973 1.00 25.65 C ANISOU 301 CB THR B 43 2499 4106 3140 -633 459 297 C ATOM 302 OG1 THR B 43 53.040 23.094 -11.288 1.00 24.68 O ANISOU 302 OG1 THR B 43 2427 3951 3001 -521 388 273 O ATOM 303 CG2 THR B 43 54.590 24.896 -10.946 1.00 26.46 C ANISOU 303 CG2 THR B 43 2548 4227 3280 -767 386 295 C ATOM 304 N LYS B 44 54.604 25.534 -14.606 1.00 27.61 N ANISOU 304 N LYS B 44 2764 4382 3344 -788 699 372 N ATOM 305 CA LYS B 44 55.439 26.453 -15.391 1.00 29.24 C ANISOU 305 CA LYS B 44 2930 4625 3557 -919 793 415 C ATOM 306 C LYS B 44 54.573 27.479 -16.106 1.00 28.93 C ANISOU 306 C LYS B 44 3066 4477 3449 -975 826 468 C ATOM 307 O LYS B 44 54.942 28.651 -16.192 1.00 30.02 O ANISOU 307 O LYS B 44 3227 4574 3605 -1112 850 510 O ATOM 308 CB LYS B 44 56.322 25.712 -16.412 1.00 30.33 C ANISOU 308 CB LYS B 44 2940 4887 3698 -885 914 411 C ATOM 309 CG LYS B 44 57.472 24.906 -15.806 1.00 32.04 C ANISOU 309 CG LYS B 44 2941 5214 4017 -848 898 377 C ATOM 310 CD LYS B 44 58.738 24.925 -16.689 1.00 35.81 C ANISOU 310 CD LYS B 44 3259 5812 4536 -906 1038 388 C ATOM 311 CE LYS B 44 58.856 23.701 -17.612 1.00 37.25 C ANISOU 311 CE LYS B 44 3391 6058 4703 -772 1153 348 C ATOM 312 NZ LYS B 44 58.154 23.847 -18.936 1.00 37.42 N ANISOU 312 NZ LYS B 44 3575 6054 4590 -777 1263 357 N ATOM 313 N ALA B 45 53.418 27.030 -16.598 1.00 27.70 N ANISOU 313 N ALA B 45 3032 4271 3223 -870 821 472 N ATOM 314 CA ALA B 45 52.488 27.880 -17.335 1.00 27.52 C ANISOU 314 CA ALA B 45 3170 4151 3137 -899 836 538 C ATOM 315 C ALA B 45 51.843 28.933 -16.442 1.00 27.22 C ANISOU 315 C ALA B 45 3228 3970 3145 -947 759 549 C ATOM 316 O ALA B 45 51.848 30.120 -16.773 1.00 27.89 O ANISOU 316 O ALA B 45 3384 3974 3237 -1048 786 611 O ATOM 317 CB ALA B 45 51.422 27.035 -18.032 1.00 26.48 C ANISOU 317 CB ALA B 45 3122 4016 2922 -775 833 535 C ATOM 318 N LEU B 46 51.299 28.495 -15.308 1.00 26.35 N ANISOU 318 N LEU B 46 3123 3823 3067 -877 671 487 N ATOM 319 CA LEU B 46 50.607 29.400 -14.391 1.00 26.30 C ANISOU 319 CA LEU B 46 3213 3680 3100 -912 611 475 C ATOM 320 C LEU B 46 51.561 30.427 -13.780 1.00 27.70 C ANISOU 320 C LEU B 46 3354 3834 3336 -1066 612 465 C ATOM 321 O LEU B 46 51.175 31.579 -13.561 1.00 28.44 O ANISOU 321 O LEU B 46 3550 3795 3463 -1138 611 481 O ATOM 322 CB LEU B 46 49.863 28.622 -13.294 1.00 24.93 C ANISOU 322 CB LEU B 46 3050 3490 2931 -812 531 405 C ATOM 323 CG LEU B 46 49.016 29.418 -12.290 1.00 24.66 C ANISOU 323 CG LEU B 46 3120 3319 2931 -830 485 372 C ATOM 324 CD1 LEU B 46 47.901 30.186 -12.987 1.00 24.56 C ANISOU 324 CD1 LEU B 46 3233 3177 2923 -800 510 431 C ATOM 325 CD2 LEU B 46 48.445 28.522 -11.195 1.00 23.63 C ANISOU 325 CD2 LEU B 46 2985 3203 2790 -745 420 304 C ATOM 326 N GLY B 47 52.800 30.009 -13.521 1.00 28.28 N ANISOU 326 N GLY B 47 3278 4034 3433 -1119 615 440 N ATOM 327 CA GLY B 47 53.796 30.873 -12.900 1.00 29.70 C ANISOU 327 CA GLY B 47 3399 4216 3669 -1279 602 424 C ATOM 328 C GLY B 47 53.285 31.441 -11.594 1.00 29.75 C ANISOU 328 C GLY B 47 3491 4116 3696 -1319 521 361 C ATOM 329 O GLY B 47 52.661 30.727 -10.805 1.00 28.87 O ANISOU 329 O GLY B 47 3399 4008 3562 -1222 456 311 O ATOM 330 N ALA B 48 53.523 32.733 -11.382 1.00 31.07 N ANISOU 330 N ALA B 48 3718 4182 3903 -1466 536 361 N ATOM 331 CA ALA B 48 53.101 33.418 -10.158 1.00 31.43 C ANISOU 331 CA ALA B 48 3860 4115 3968 -1527 478 284 C ATOM 332 C ALA B 48 51.690 34.013 -10.259 1.00 31.11 C ANISOU 332 C ALA B 48 3997 3889 3934 -1455 503 289 C ATOM 333 O ALA B 48 51.194 34.634 -9.313 1.00 31.30 O ANISOU 333 O ALA B 48 4118 3796 3979 -1492 480 218 O ATOM 334 CB ALA B 48 54.108 34.488 -9.791 1.00 33.13 C ANISOU 334 CB ALA B 48 4050 4307 4232 -1733 479 262 C ATOM 335 N ASP B 49 51.044 33.805 -11.402 1.00 30.82 N ANISOU 335 N ASP B 49 3999 3832 3881 -1351 551 372 N ATOM 336 CA ASP B 49 49.724 34.370 -11.660 1.00 30.69 C ANISOU 336 CA ASP B 49 4127 3648 3886 -1274 570 403 C ATOM 337 C ASP B 49 48.615 33.517 -11.052 1.00 29.51 C ANISOU 337 C ASP B 49 4004 3498 3709 -1124 524 349 C ATOM 338 O ASP B 49 48.868 32.422 -10.537 1.00 28.80 O ANISOU 338 O ASP B 49 3830 3538 3575 -1076 479 301 O ATOM 339 CB ASP B 49 49.502 34.535 -13.167 1.00 30.85 C ANISOU 339 CB ASP B 49 4177 3657 3888 -1239 625 528 C ATOM 340 CG ASP B 49 50.656 35.251 -13.854 1.00 32.10 C ANISOU 340 CG ASP B 49 4299 3838 4059 -1392 684 592 C ATOM 341 OD1 ASP B 49 50.950 36.413 -13.506 1.00 33.21 O ANISOU 341 OD1 ASP B 49 4496 3855 4267 -1520 702 587 O ATOM 342 OD2 ASP B 49 51.268 34.646 -14.753 1.00 31.76 O ANISOU 342 OD2 ASP B 49 4171 3934 3961 -1388 723 642 O ATOM 343 N GLU B 50 47.390 34.036 -11.107 1.00 29.54 N ANISOU 343 N GLU B 50 4120 3352 3751 -1052 537 364 N ATOM 344 CA GLU B 50 46.210 33.304 -10.660 1.00 28.37 C ANISOU 344 CA GLU B 50 3997 3195 3589 -911 507 325 C ATOM 345 C GLU B 50 45.516 32.636 -11.840 1.00 27.69 C ANISOU 345 C GLU B 50 3900 3151 3468 -790 506 414 C ATOM 346 O GLU B 50 45.543 33.149 -12.963 1.00 28.47 O ANISOU 346 O GLU B 50 4027 3219 3570 -805 534 514 O ATOM 347 CB GLU B 50 45.234 34.236 -9.941 1.00 28.81 C ANISOU 347 CB GLU B 50 4164 3064 3720 -899 527 276 C ATOM 348 CG GLU B 50 45.610 34.536 -8.495 1.00 29.37 C ANISOU 348 CG GLU B 50 4257 3112 3791 -993 518 147 C ATOM 349 CD GLU B 50 44.674 35.537 -7.841 1.00 30.07 C ANISOU 349 CD GLU B 50 4465 3002 3959 -985 564 85 C ATOM 350 OE1 GLU B 50 44.438 36.613 -8.436 1.00 30.88 O ANISOU 350 OE1 GLU B 50 4636 2948 4150 -1002 610 142 O ATOM 351 OE2 GLU B 50 44.181 35.252 -6.727 1.00 29.45 O ANISOU 351 OE2 GLU B 50 4413 2919 3858 -963 561 -20 O ATOM 352 N LEU B 51 44.913 31.481 -11.575 1.00 26.39 N ANISOU 352 N LEU B 51 3702 3063 3264 -681 471 379 N ATOM 353 CA LEU B 51 44.131 30.756 -12.561 1.00 25.63 C ANISOU 353 CA LEU B 51 3601 3008 3130 -570 460 442 C ATOM 354 C LEU B 51 42.830 31.509 -12.820 1.00 25.86 C ANISOU 354 C LEU B 51 3714 2890 3222 -506 461 491 C ATOM 355 O LEU B 51 42.115 31.867 -11.882 1.00 25.96 O ANISOU 355 O LEU B 51 3765 2802 3296 -478 463 432 O ATOM 356 CB LEU B 51 43.853 29.331 -12.063 1.00 24.42 C ANISOU 356 CB LEU B 51 3391 2958 2931 -485 423 380 C ATOM 357 CG LEU B 51 43.062 28.363 -12.950 1.00 23.97 C ANISOU 357 CG LEU B 51 3323 2956 2828 -380 405 419 C ATOM 358 CD1 LEU B 51 43.781 28.105 -14.256 1.00 24.51 C ANISOU 358 CD1 LEU B 51 3363 3116 2833 -404 430 482 C ATOM 359 CD2 LEU B 51 42.793 27.051 -12.226 1.00 22.91 C ANISOU 359 CD2 LEU B 51 3144 2891 2668 -311 373 350 C ATOM 360 N THR B 52 42.529 31.745 -14.094 1.00 26.17 N ANISOU 360 N THR B 52 3778 2922 3244 -483 460 603 N ATOM 361 CA THR B 52 41.376 32.556 -14.476 1.00 26.73 C ANISOU 361 CA THR B 52 3917 2852 3388 -422 449 679 C ATOM 362 C THR B 52 40.243 31.738 -15.108 1.00 26.07 C ANISOU 362 C THR B 52 3815 2819 3270 -305 397 723 C ATOM 363 O THR B 52 40.462 30.966 -16.047 1.00 25.81 O ANISOU 363 O THR B 52 3757 2912 3137 -299 378 764 O ATOM 364 CB THR B 52 41.800 33.693 -15.432 1.00 28.19 C ANISOU 364 CB THR B 52 4160 2962 3589 -496 473 800 C ATOM 365 OG1 THR B 52 43.012 34.291 -14.953 1.00 28.70 O ANISOU 365 OG1 THR B 52 4225 3009 3670 -627 521 757 O ATOM 366 CG2 THR B 52 40.706 34.758 -15.542 1.00 28.90 C ANISOU 366 CG2 THR B 52 4322 2863 3795 -437 464 877 C ATOM 367 N VAL B 53 39.034 31.919 -14.579 1.00 25.91 N ANISOU 367 N VAL B 53 3806 2702 3337 -217 380 706 N ATOM 368 CA VAL B 53 37.832 31.293 -15.131 1.00 25.55 C ANISOU 368 CA VAL B 53 3735 2688 3284 -113 323 753 C ATOM 369 C VAL B 53 36.859 32.356 -15.653 1.00 26.65 C ANISOU 369 C VAL B 53 3912 2686 3526 -57 299 868 C ATOM 370 O VAL B 53 36.402 33.215 -14.893 1.00 27.16 O ANISOU 370 O VAL B 53 3999 2599 3720 -30 334 841 O ATOM 371 CB VAL B 53 37.102 30.414 -14.087 1.00 24.44 C ANISOU 371 CB VAL B 53 3547 2571 3167 -45 319 644 C ATOM 372 CG1 VAL B 53 35.932 29.688 -14.734 1.00 24.64 C ANISOU 372 CG1 VAL B 53 3533 2646 3181 45 256 692 C ATOM 373 CG2 VAL B 53 38.048 29.415 -13.464 1.00 23.51 C ANISOU 373 CG2 VAL B 53 3395 2572 2964 -93 335 544 C ATOM 374 N ILE B 54 36.553 32.291 -16.947 1.00 27.09 N ANISOU 374 N ILE B 54 3976 2793 3524 -40 239 996 N ATOM 375 CA ILE B 54 35.554 33.170 -17.550 1.00 28.48 C ANISOU 375 CA ILE B 54 4175 2853 3793 26 190 1132 C ATOM 376 C ILE B 54 34.207 32.461 -17.551 1.00 28.32 C ANISOU 376 C ILE B 54 4086 2870 3806 136 122 1131 C ATOM 377 O ILE B 54 34.058 31.393 -18.143 1.00 27.82 O ANISOU 377 O ILE B 54 3990 2956 3626 138 68 1130 O ATOM 378 CB ILE B 54 35.941 33.612 -18.990 1.00 29.52 C ANISOU 378 CB ILE B 54 4363 3018 3835 -28 149 1296 C ATOM 379 CG1 ILE B 54 37.095 34.613 -18.959 1.00 29.89 C ANISOU 379 CG1 ILE B 54 4478 2982 3896 -136 223 1320 C ATOM 380 CG2 ILE B 54 34.760 34.246 -19.711 1.00 30.80 C ANISOU 380 CG2 ILE B 54 4532 3094 4074 56 63 1455 C ATOM 381 CD1 ILE B 54 38.447 33.981 -19.152 1.00 29.47 C ANISOU 381 CD1 ILE B 54 4418 3079 3699 -246 273 1258 C ATOM 382 N VAL B 55 33.230 33.052 -16.874 1.00 29.15 N ANISOU 382 N VAL B 55 4164 2835 4075 223 133 1123 N ATOM 383 CA VAL B 55 31.906 32.453 -16.787 1.00 29.43 C ANISOU 383 CA VAL B 55 4115 2899 4168 326 78 1120 C ATOM 384 C VAL B 55 30.911 33.252 -17.628 1.00 31.49 C ANISOU 384 C VAL B 55 4360 3074 4533 407 -4 1291 C ATOM 385 O VAL B 55 30.677 34.436 -17.376 1.00 32.62 O ANISOU 385 O VAL B 55 4527 3037 4830 449 31 1341 O ATOM 386 CB VAL B 55 31.421 32.329 -15.311 1.00 28.81 C ANISOU 386 CB VAL B 55 3994 2752 4201 374 159 971 C ATOM 387 CG1 VAL B 55 30.061 31.639 -15.237 1.00 28.77 C ANISOU 387 CG1 VAL B 55 3887 2790 4255 469 111 969 C ATOM 388 CG2 VAL B 55 32.434 31.573 -14.472 1.00 27.19 C ANISOU 388 CG2 VAL B 55 3810 2634 3888 291 222 824 C ATOM 389 N ASN B 56 30.343 32.598 -18.638 1.00 32.27 N ANISOU 389 N ASN B 56 4418 3297 4546 424 -117 1381 N ATOM 390 CA ASN B 56 29.284 33.200 -19.441 1.00 34.71 C ANISOU 390 CA ASN B 56 4690 3552 4947 506 -223 1554 C ATOM 391 C ASN B 56 27.935 33.084 -18.732 1.00 35.46 C ANISOU 391 C ASN B 56 4664 3591 5219 627 -231 1515 C ATOM 392 O ASN B 56 27.361 31.999 -18.638 1.00 34.61 O ANISOU 392 O ASN B 56 4477 3608 5066 638 -270 1451 O ATOM 393 CB ASN B 56 29.231 32.569 -20.838 1.00 35.02 C ANISOU 393 CB ASN B 56 4740 3760 4804 459 -352 1667 C ATOM 394 CG ASN B 56 30.436 32.925 -21.687 1.00 35.20 C ANISOU 394 CG ASN B 56 4881 3820 4671 348 -339 1741 C ATOM 395 OD1 ASN B 56 30.557 34.048 -22.169 1.00 37.18 O ANISOU 395 OD1 ASN B 56 5192 3960 4974 347 -355 1887 O ATOM 396 ND2 ASN B 56 31.329 31.965 -21.883 1.00 33.50 N ANISOU 396 ND2 ASN B 56 4699 3756 4272 255 -303 1644 N ATOM 397 N GLU B 57 27.453 34.207 -18.213 1.00 37.52 N ANISOU 397 N GLU B 57 4910 3658 5689 713 -181 1547 N ATOM 398 CA GLU B 57 26.166 34.256 -17.527 1.00 39.20 C ANISOU 398 CA GLU B 57 4999 3799 6098 837 -166 1514 C ATOM 399 C GLU B 57 25.020 34.282 -18.546 1.00 41.46 C ANISOU 399 C GLU B 57 5184 4124 6444 920 -324 1694 C ATOM 400 O GLU B 57 25.246 34.428 -19.752 1.00 42.40 O ANISOU 400 O GLU B 57 5351 4303 6454 881 -443 1853 O ATOM 401 CB GLU B 57 26.076 35.485 -16.604 1.00 40.29 C ANISOU 401 CB GLU B 57 5160 3700 6448 904 -39 1471 C ATOM 402 CG GLU B 57 27.310 35.764 -15.740 1.00 39.61 C ANISOU 402 CG GLU B 57 5194 3552 6302 804 98 1325 C ATOM 403 CD GLU B 57 27.417 34.871 -14.510 1.00 38.51 C ANISOU 403 CD GLU B 57 5031 3490 6112 771 196 1115 C ATOM 404 OE1 GLU B 57 28.405 35.029 -13.758 1.00 37.46 O ANISOU 404 OE1 GLU B 57 4987 3326 5921 684 292 995 O ATOM 405 OE2 GLU B 57 26.522 34.022 -14.290 1.00 37.96 O ANISOU 405 OE2 GLU B 57 4853 3511 6058 823 173 1077 O ATOM 406 N LYS B 58 23.791 34.154 -18.049 1.00 42.85 N ANISOU 406 N LYS B 58 5217 4272 6793 1030 -325 1671 N ATOM 407 CA LYS B 58 22.592 34.172 -18.892 1.00 45.18 C ANISOU 407 CA LYS B 58 5384 4607 7176 1117 -482 1838 C ATOM 408 C LYS B 58 22.288 35.566 -19.459 1.00 47.76 C ANISOU 408 C LYS B 58 5718 4758 7672 1211 -537 2037 C ATOM 409 O LYS B 58 21.556 35.698 -20.445 1.00 49.23 O ANISOU 409 O LYS B 58 5831 4988 7886 1262 -704 2226 O ATOM 410 CB LYS B 58 21.387 33.624 -18.116 1.00 45.42 C ANISOU 410 CB LYS B 58 5240 4658 7358 1203 -451 1747 C ATOM 411 CG LYS B 58 21.612 32.235 -17.507 1.00 43.79 C ANISOU 411 CG LYS B 58 5027 4610 7001 1112 -396 1562 C ATOM 412 CD LYS B 58 21.668 31.134 -18.573 1.00 44.21 C ANISOU 412 CD LYS B 58 5082 4877 6840 1018 -551 1614 C ATOM 413 CE LYS B 58 20.282 30.571 -18.888 1.00 45.89 C ANISOU 413 CE LYS B 58 5114 5182 7140 1071 -670 1670 C ATOM 414 NZ LYS B 58 19.686 29.833 -17.723 1.00 44.89 N ANISOU 414 NZ LYS B 58 4883 5071 7101 1089 -558 1504 N ATOM 415 N ASP B 59 22.862 36.593 -18.830 1.00 48.45 N ANISOU 415 N ASP B 59 5897 4643 7868 1229 -402 1996 N ATOM 416 CA ASP B 59 22.763 37.982 -19.299 1.00 50.93 C ANISOU 416 CA ASP B 59 6251 4753 8346 1307 -430 2176 C ATOM 417 C ASP B 59 23.477 38.186 -20.637 1.00 51.44 C ANISOU 417 C ASP B 59 6435 4889 8223 1213 -562 2366 C ATOM 418 O ASP B 59 23.141 39.095 -21.401 1.00 53.61 O ANISOU 418 O ASP B 59 6716 5055 8598 1277 -658 2582 O ATOM 419 CB ASP B 59 23.386 38.936 -18.271 1.00 51.12 C ANISOU 419 CB ASP B 59 6375 4550 8499 1312 -238 2054 C ATOM 420 CG ASP B 59 22.722 38.858 -16.909 1.00 51.23 C ANISOU 420 CG ASP B 59 6294 4480 8691 1398 -86 1860 C ATOM 421 OD1 ASP B 59 23.310 38.235 -15.998 1.00 49.78 O ANISOU 421 OD1 ASP B 59 6158 4364 8393 1309 32 1652 O ATOM 422 OD2 ASP B 59 21.617 39.419 -16.750 1.00 53.33 O ANISOU 422 OD2 ASP B 59 6437 4616 9209 1553 -81 1919 O ATOM 423 N GLY B 60 24.466 37.336 -20.906 1.00 49.61 N ANISOU 423 N GLY B 60 6295 4834 7720 1061 -558 2285 N ATOM 424 CA GLY B 60 25.384 37.534 -22.024 1.00 49.86 C ANISOU 424 CA GLY B 60 6463 4931 7551 945 -629 2422 C ATOM 425 C GLY B 60 26.694 38.129 -21.532 1.00 49.06 C ANISOU 425 C GLY B 60 6506 4718 7418 852 -478 2335 C ATOM 426 O GLY B 60 27.677 38.192 -22.275 1.00 49.01 O ANISOU 426 O GLY B 60 6616 4776 7228 730 -492 2401 O ATOM 427 N THR B 61 26.695 38.568 -20.274 1.00 48.53 N ANISOU 427 N THR B 61 6428 4486 7525 900 -330 2182 N ATOM 428 CA THR B 61 27.886 39.104 -19.618 1.00 47.67 C ANISOU 428 CA THR B 61 6443 4270 7401 805 -183 2069 C ATOM 429 C THR B 61 28.839 37.983 -19.217 1.00 44.99 C ANISOU 429 C THR B 61 6130 4121 6844 677 -125 1886 C ATOM 430 O THR B 61 28.455 36.812 -19.181 1.00 43.64 O ANISOU 430 O THR B 61 5878 4126 6577 684 -169 1814 O ATOM 431 CB THR B 61 27.526 39.917 -18.354 1.00 48.37 C ANISOU 431 CB THR B 61 6517 4124 7738 892 -43 1947 C ATOM 432 OG1 THR B 61 26.698 39.122 -17.495 1.00 47.52 O ANISOU 432 OG1 THR B 61 6284 4083 7686 967 -6 1797 O ATOM 433 CG2 THR B 61 26.803 41.213 -18.721 1.00 50.91 C ANISOU 433 CG2 THR B 61 6834 4209 8302 1016 -74 2128 C ATOM 434 N GLN B 62 30.082 38.359 -18.923 1.00 44.32 N ANISOU 434 N GLN B 62 6153 3992 6694 561 -29 1818 N ATOM 435 CA GLN B 62 31.115 37.422 -18.491 1.00 42.06 C ANISOU 435 CA GLN B 62 5889 3865 6225 443 31 1654 C ATOM 436 C GLN B 62 31.719 37.875 -17.170 1.00 41.43 C ANISOU 436 C GLN B 62 5852 3662 6228 401 173 1479 C ATOM 437 O GLN B 62 32.262 38.975 -17.075 1.00 42.64 O ANISOU 437 O GLN B 62 6091 3649 6460 355 231 1510 O ATOM 438 CB GLN B 62 32.225 37.304 -19.544 1.00 41.97 C ANISOU 438 CB GLN B 62 5959 3972 6014 312 -1 1744 C ATOM 439 CG GLN B 62 31.760 36.851 -20.922 1.00 42.68 C ANISOU 439 CG GLN B 62 6035 4204 5979 323 -139 1911 C ATOM 440 CD GLN B 62 32.910 36.582 -21.876 1.00 42.61 C ANISOU 440 CD GLN B 62 6106 4335 5748 184 -142 1963 C ATOM 441 OE1 GLN B 62 33.871 37.351 -21.949 1.00 43.44 O ANISOU 441 OE1 GLN B 62 6296 4363 5847 94 -72 1995 O ATOM 442 NE2 GLN B 62 32.813 35.485 -22.620 1.00 41.88 N ANISOU 442 NE2 GLN B 62 5988 4450 5474 159 -214 1966 N ATOM 443 N THR B 63 31.616 37.027 -16.153 1.00 39.80 N ANISOU 443 N THR B 63 5591 3534 5997 408 225 1300 N ATOM 444 CA THR B 63 32.288 37.269 -14.880 1.00 39.09 C ANISOU 444 CA THR B 63 5547 3373 5934 344 347 1122 C ATOM 445 C THR B 63 33.629 36.534 -14.865 1.00 37.34 C ANISOU 445 C THR B 63 5355 3317 5515 205 357 1049 C ATOM 446 O THR B 63 33.709 35.374 -15.270 1.00 36.05 O ANISOU 446 O THR B 63 5142 3344 5213 196 300 1045 O ATOM 447 CB THR B 63 31.432 36.810 -13.676 1.00 38.66 C ANISOU 447 CB THR B 63 5423 3305 5959 422 407 968 C ATOM 448 OG1 THR B 63 30.048 37.096 -13.921 1.00 39.79 O ANISOU 448 OG1 THR B 63 5489 3363 6265 568 374 1052 O ATOM 449 CG2 THR B 63 31.876 37.521 -12.400 1.00 39.34 C ANISOU 449 CG2 THR B 63 5578 3248 6119 372 537 811 C ATOM 450 N GLU B 64 34.674 37.220 -14.407 1.00 37.34 N ANISOU 450 N GLU B 64 5432 3240 5517 97 428 991 N ATOM 451 CA GLU B 64 36.002 36.625 -14.265 1.00 36.00 C ANISOU 451 CA GLU B 64 5273 3216 5190 -34 444 917 C ATOM 452 C GLU B 64 36.299 36.197 -12.828 1.00 34.71 C ANISOU 452 C GLU B 64 5097 3079 5011 -70 506 724 C ATOM 453 O GLU B 64 36.389 37.040 -11.930 1.00 35.62 O ANISOU 453 O GLU B 64 5267 3047 5221 -103 579 637 O ATOM 454 CB GLU B 64 37.080 37.609 -14.719 1.00 37.27 C ANISOU 454 CB GLU B 64 5512 3300 5347 -154 474 984 C ATOM 455 CG GLU B 64 37.459 37.521 -16.191 1.00 38.42 C ANISOU 455 CG GLU B 64 5670 3539 5390 -190 415 1152 C ATOM 456 CD GLU B 64 38.840 38.101 -16.473 1.00 39.99 C ANISOU 456 CD GLU B 64 5923 3734 5536 -346 462 1177 C ATOM 457 OE1 GLU B 64 39.279 38.044 -17.645 1.00 40.75 O ANISOU 457 OE1 GLU B 64 6035 3915 5531 -395 435 1305 O ATOM 458 OE2 GLU B 64 39.490 38.607 -15.525 1.00 40.38 O ANISOU 458 OE2 GLU B 64 6000 3704 5640 -429 529 1065 O ATOM 459 N VAL B 65 36.455 34.891 -12.614 1.00 32.64 N ANISOU 459 N VAL B 65 4773 3001 4629 -69 477 658 N ATOM 460 CA VAL B 65 36.904 34.371 -11.320 1.00 31.27 C ANISOU 460 CA VAL B 65 4591 2881 4409 -120 519 497 C ATOM 461 C VAL B 65 38.408 34.109 -11.363 1.00 30.66 C ANISOU 461 C VAL B 65 4515 2917 4218 -249 514 474 C ATOM 462 O VAL B 65 38.900 33.425 -12.260 1.00 30.07 O ANISOU 462 O VAL B 65 4401 2976 4048 -262 471 541 O ATOM 463 CB VAL B 65 36.154 33.076 -10.906 1.00 30.06 C ANISOU 463 CB VAL B 65 4367 2847 4208 -41 493 440 C ATOM 464 CG1 VAL B 65 36.757 32.485 -9.641 1.00 28.65 C ANISOU 464 CG1 VAL B 65 4189 2741 3957 -107 523 298 C ATOM 465 CG2 VAL B 65 34.663 33.342 -10.705 1.00 30.13 C ANISOU 465 CG2 VAL B 65 4354 2749 4344 80 511 447 C ATOM 466 N LYS B 66 39.130 34.668 -10.395 1.00 30.84 N ANISOU 466 N LYS B 66 4579 2885 4253 -348 561 375 N ATOM 467 CA LYS B 66 40.568 34.449 -10.267 1.00 30.36 C ANISOU 467 CA LYS B 66 4499 2933 4101 -476 552 343 C ATOM 468 C LYS B 66 40.886 33.795 -8.929 1.00 29.47 C ANISOU 468 C LYS B 66 4366 2900 3929 -515 551 205 C ATOM 469 O LYS B 66 40.330 34.179 -7.896 1.00 29.75 O ANISOU 469 O LYS B 66 4452 2843 4010 -510 591 109 O ATOM 470 CB LYS B 66 41.336 35.766 -10.398 1.00 31.90 C ANISOU 470 CB LYS B 66 4760 3006 4356 -595 591 365 C ATOM 471 CG LYS B 66 41.200 36.446 -11.749 1.00 33.12 C ANISOU 471 CG LYS B 66 4943 3087 4553 -579 589 522 C ATOM 472 CD LYS B 66 42.414 37.308 -12.052 1.00 34.65 C ANISOU 472 CD LYS B 66 5171 3245 4752 -732 618 556 C ATOM 473 CE LYS B 66 42.386 37.783 -13.494 1.00 36.13 C ANISOU 473 CE LYS B 66 5384 3399 4944 -727 612 731 C ATOM 474 NZ LYS B 66 43.758 37.943 -14.049 1.00 37.02 N ANISOU 474 NZ LYS B 66 5478 3596 4993 -873 633 774 N ATOM 475 N SER B 67 41.783 32.811 -8.955 1.00 28.33 N ANISOU 475 N SER B 67 4150 2928 3684 -552 508 198 N ATOM 476 CA SER B 67 42.185 32.082 -7.752 1.00 27.45 C ANISOU 476 CA SER B 67 4012 2912 3505 -589 486 95 C ATOM 477 C SER B 67 43.470 31.292 -7.982 1.00 26.99 C ANISOU 477 C SER B 67 3866 3022 3368 -646 440 114 C ATOM 478 O SER B 67 43.876 31.083 -9.124 1.00 26.78 O ANISOU 478 O SER B 67 3794 3051 3330 -634 436 199 O ATOM 479 CB SER B 67 41.065 31.137 -7.295 1.00 26.51 C ANISOU 479 CB SER B 67 3882 2823 3369 -475 478 62 C ATOM 480 OG SER B 67 40.923 30.030 -8.169 1.00 24.89 O ANISOU 480 OG SER B 67 3609 2728 3121 -394 438 132 O ATOM 481 N ARG B 68 44.101 30.854 -6.894 1.00 26.92 N ANISOU 481 N ARG B 68 3831 3093 3304 -708 406 38 N ATOM 482 CA ARG B 68 45.260 29.963 -6.979 1.00 26.60 C ANISOU 482 CA ARG B 68 3686 3215 3206 -739 355 57 C ATOM 483 C ARG B 68 45.115 28.730 -6.092 1.00 25.83 C ANISOU 483 C ARG B 68 3553 3215 3046 -687 303 17 C ATOM 484 O ARG B 68 44.719 28.843 -4.932 1.00 25.95 O ANISOU 484 O ARG B 68 3625 3199 3034 -714 296 -56 O ATOM 485 CB ARG B 68 46.554 30.699 -6.633 1.00 27.63 C ANISOU 485 CB ARG B 68 3790 3368 3339 -893 341 33 C ATOM 486 CG ARG B 68 47.426 31.001 -7.834 1.00 28.52 C ANISOU 486 CG ARG B 68 3842 3517 3479 -937 366 114 C ATOM 487 CD ARG B 68 48.769 31.603 -7.429 1.00 29.33 C ANISOU 487 CD ARG B 68 3892 3664 3589 -1100 347 89 C ATOM 488 NE ARG B 68 49.650 30.643 -6.768 1.00 28.51 N ANISOU 488 NE ARG B 68 3673 3721 3440 -1117 274 66 N ATOM 489 CZ ARG B 68 50.820 30.227 -7.248 1.00 28.44 C ANISOU 489 CZ ARG B 68 3527 3840 3439 -1150 260 109 C ATOM 490 NH1 ARG B 68 51.277 30.679 -8.409 1.00 28.48 N ANISOU 490 NH1 ARG B 68 3499 3841 3480 -1183 326 173 N ATOM 491 NH2 ARG B 68 51.541 29.359 -6.553 1.00 28.69 N ANISOU 491 NH2 ARG B 68 3450 4005 3446 -1151 184 95 N ATOM 492 N PRO B 69 45.414 27.541 -6.646 1.00 25.15 N ANISOU 492 N PRO B 69 3380 3241 2935 -613 274 65 N ATOM 493 CA PRO B 69 45.563 26.333 -5.835 1.00 24.76 C ANISOU 493 CA PRO B 69 3285 3287 2835 -576 217 46 C ATOM 494 C PRO B 69 46.805 26.406 -4.956 1.00 25.65 C ANISOU 494 C PRO B 69 3343 3485 2919 -684 156 22 C ATOM 495 O PRO B 69 47.776 27.081 -5.314 1.00 26.51 O ANISOU 495 O PRO B 69 3403 3614 3054 -773 159 35 O ATOM 496 CB PRO B 69 45.729 25.220 -6.880 1.00 24.02 C ANISOU 496 CB PRO B 69 3112 3269 2745 -479 216 104 C ATOM 497 CG PRO B 69 45.233 25.802 -8.157 1.00 23.93 C ANISOU 497 CG PRO B 69 3133 3194 2764 -451 274 146 C ATOM 498 CD PRO B 69 45.579 27.253 -8.080 1.00 24.84 C ANISOU 498 CD PRO B 69 3293 3234 2911 -560 301 139 C ATOM 499 N LYS B 70 46.761 25.714 -3.818 1.00 25.72 N ANISOU 499 N LYS B 70 3355 3546 2871 -683 96 -6 N ATOM 500 CA LYS B 70 47.887 25.627 -2.884 1.00 26.87 C ANISOU 500 CA LYS B 70 3442 3792 2976 -782 11 -17 C ATOM 501 C LYS B 70 49.093 24.949 -3.539 1.00 26.91 C ANISOU 501 C LYS B 70 3293 3911 3021 -758 -27 50 C ATOM 502 O LYS B 70 50.219 25.437 -3.435 1.00 28.21 O ANISOU 502 O LYS B 70 3379 4136 3202 -861 -63 53 O ATOM 503 CB LYS B 70 47.461 24.873 -1.619 1.00 27.05 C ANISOU 503 CB LYS B 70 3509 3851 2916 -769 -47 -38 C ATOM 504 CG LYS B 70 48.545 24.690 -0.558 1.00 29.64 C ANISOU 504 CG LYS B 70 3783 4294 3183 -869 -160 -36 C ATOM 505 CD LYS B 70 48.428 25.727 0.551 1.00 33.25 C ANISOU 505 CD LYS B 70 4353 4717 3564 -1016 -168 -127 C ATOM 506 CE LYS B 70 48.971 25.190 1.876 1.00 35.22 C ANISOU 506 CE LYS B 70 4596 5084 3704 -1090 -290 -122 C ATOM 507 NZ LYS B 70 48.333 25.861 3.057 1.00 36.30 N ANISOU 507 NZ LYS B 70 4890 5175 3729 -1197 -271 -224 N ATOM 508 N VAL B 71 48.846 23.834 -4.222 1.00 25.75 N ANISOU 508 N VAL B 71 3097 3788 2897 -626 -12 96 N ATOM 509 CA VAL B 71 49.894 23.115 -4.942 1.00 25.76 C ANISOU 509 CA VAL B 71 2953 3884 2950 -580 -22 148 C ATOM 510 C VAL B 71 49.323 22.420 -6.177 1.00 24.71 C ANISOU 510 C VAL B 71 2821 3722 2846 -455 53 171 C ATOM 511 O VAL B 71 48.173 21.984 -6.176 1.00 23.78 O ANISOU 511 O VAL B 71 2788 3541 2704 -381 70 161 O ATOM 512 CB VAL B 71 50.639 22.098 -4.016 1.00 26.49 C ANISOU 512 CB VAL B 71 2951 4079 3035 -560 -127 180 C ATOM 513 CG1 VAL B 71 49.741 20.917 -3.631 1.00 25.32 C ANISOU 513 CG1 VAL B 71 2857 3905 2858 -446 -146 194 C ATOM 514 CG2 VAL B 71 51.950 21.622 -4.654 1.00 27.06 C ANISOU 514 CG2 VAL B 71 2846 4250 3186 -534 -134 227 C ATOM 515 N ILE B 72 50.128 22.355 -7.236 1.00 25.02 N ANISOU 515 N ILE B 72 2765 3811 2932 -444 101 198 N ATOM 516 CA ILE B 72 49.805 21.577 -8.434 1.00 24.26 C ANISOU 516 CA ILE B 72 2659 3711 2849 -336 170 212 C ATOM 517 C ILE B 72 50.908 20.530 -8.638 1.00 24.63 C ANISOU 517 C ILE B 72 2556 3852 2950 -275 164 233 C ATOM 518 O ILE B 72 52.051 20.873 -8.954 1.00 25.61 O ANISOU 518 O ILE B 72 2567 4048 3117 -328 185 247 O ATOM 519 CB ILE B 72 49.632 22.482 -9.679 1.00 24.43 C ANISOU 519 CB ILE B 72 2723 3696 2863 -375 258 222 C ATOM 520 CG1 ILE B 72 48.508 23.505 -9.433 1.00 23.96 C ANISOU 520 CG1 ILE B 72 2803 3525 2776 -416 259 210 C ATOM 521 CG2 ILE B 72 49.351 21.627 -10.927 1.00 24.09 C ANISOU 521 CG2 ILE B 72 2675 3666 2810 -277 325 229 C ATOM 522 CD1 ILE B 72 48.605 24.771 -10.255 1.00 24.12 C ANISOU 522 CD1 ILE B 72 2864 3500 2802 -497 318 235 C ATOM 523 N THR B 73 50.554 19.260 -8.445 1.00 23.70 N ANISOU 523 N THR B 73 2434 3728 2842 -163 141 235 N ATOM 524 CA THR B 73 51.541 18.193 -8.293 1.00 23.97 C ANISOU 524 CA THR B 73 2330 3832 2947 -91 115 259 C ATOM 525 C THR B 73 51.116 16.870 -8.939 1.00 23.23 C ANISOU 525 C THR B 73 2246 3703 2879 44 162 248 C ATOM 526 O THR B 73 49.941 16.661 -9.228 1.00 22.17 O ANISOU 526 O THR B 73 2232 3496 2697 76 186 224 O ATOM 527 CB THR B 73 51.861 17.965 -6.788 1.00 24.51 C ANISOU 527 CB THR B 73 2366 3933 3014 -116 -14 292 C ATOM 528 OG1 THR B 73 53.006 17.114 -6.646 1.00 25.34 O ANISOU 528 OG1 THR B 73 2307 4113 3207 -54 -52 334 O ATOM 529 CG2 THR B 73 50.664 17.347 -6.055 1.00 23.96 C ANISOU 529 CG2 THR B 73 2423 3791 2890 -67 -57 290 C ATOM 530 N LYS B 74 52.096 15.999 -9.179 1.00 24.02 N ANISOU 530 N LYS B 74 2210 3852 3064 120 179 261 N ATOM 531 CA LYS B 74 51.857 14.614 -9.596 1.00 23.75 C ANISOU 531 CA LYS B 74 2175 3774 3076 253 216 246 C ATOM 532 C LYS B 74 52.072 13.645 -8.429 1.00 24.15 C ANISOU 532 C LYS B 74 2178 3813 3182 321 110 298 C ATOM 533 O LYS B 74 51.947 12.425 -8.590 1.00 24.53 O ANISOU 533 O LYS B 74 2221 3809 3288 434 128 296 O ATOM 534 CB LYS B 74 52.740 14.230 -10.799 1.00 24.84 C ANISOU 534 CB LYS B 74 2203 3953 3280 308 335 214 C ATOM 535 CG LYS B 74 54.205 13.862 -10.504 1.00 26.10 C ANISOU 535 CG LYS B 74 2161 4192 3565 348 320 250 C ATOM 536 CD LYS B 74 54.794 13.091 -11.696 1.00 27.33 C ANISOU 536 CD LYS B 74 2233 4357 3796 444 462 199 C ATOM 537 CE LYS B 74 56.190 12.521 -11.428 1.00 28.66 C ANISOU 537 CE LYS B 74 2181 4589 4121 519 458 234 C ATOM 538 NZ LYS B 74 57.264 13.538 -11.608 1.00 29.01 N ANISOU 538 NZ LYS B 74 2082 4750 4191 419 485 252 N ATOM 539 N ASP B 75 52.389 14.202 -7.260 1.00 24.13 N ANISOU 539 N ASP B 75 2152 3857 3158 245 -1 346 N ATOM 540 CA ASP B 75 52.646 13.427 -6.050 1.00 24.64 C ANISOU 540 CA ASP B 75 2178 3930 3253 286 -123 416 C ATOM 541 C ASP B 75 51.362 13.250 -5.237 1.00 23.34 C ANISOU 541 C ASP B 75 2180 3693 2994 268 -173 421 C ATOM 542 O ASP B 75 50.863 14.212 -4.649 1.00 22.93 O ANISOU 542 O ASP B 75 2216 3648 2847 160 -205 405 O ATOM 543 CB ASP B 75 53.729 14.112 -5.208 1.00 25.88 C ANISOU 543 CB ASP B 75 2217 4195 3420 196 -226 466 C ATOM 544 CG ASP B 75 54.125 13.313 -3.975 1.00 27.51 C ANISOU 544 CG ASP B 75 2370 4429 3653 235 -371 558 C ATOM 545 OD1 ASP B 75 53.467 12.298 -3.646 1.00 28.09 O ANISOU 545 OD1 ASP B 75 2519 4427 3727 322 -391 587 O ATOM 546 OD2 ASP B 75 55.111 13.710 -3.323 1.00 29.57 O ANISOU 546 OD2 ASP B 75 2511 4790 3932 171 -471 607 O ATOM 547 N PRO B 76 50.826 12.015 -5.194 1.00 22.94 N ANISOU 547 N PRO B 76 2174 3566 2977 372 -170 438 N ATOM 548 CA PRO B 76 49.564 11.767 -4.487 1.00 21.86 C ANISOU 548 CA PRO B 76 2189 3360 2757 353 -201 443 C ATOM 549 C PRO B 76 49.641 11.996 -2.975 1.00 22.39 C ANISOU 549 C PRO B 76 2282 3471 2752 279 -326 508 C ATOM 550 O PRO B 76 48.639 12.363 -2.366 1.00 21.50 O ANISOU 550 O PRO B 76 2299 3330 2541 213 -332 489 O ATOM 551 CB PRO B 76 49.259 10.302 -4.807 1.00 22.03 C ANISOU 551 CB PRO B 76 2224 3293 2855 478 -173 456 C ATOM 552 CG PRO B 76 50.561 9.704 -5.208 1.00 23.24 C ANISOU 552 CG PRO B 76 2217 3477 3137 570 -168 485 C ATOM 553 CD PRO B 76 51.365 10.791 -5.819 1.00 23.59 C ANISOU 553 CD PRO B 76 2167 3613 3183 509 -127 448 C ATOM 554 N GLU B 77 50.820 11.790 -2.384 1.00 23.94 N ANISOU 554 N GLU B 77 2354 3745 2997 287 -423 582 N ATOM 555 CA GLU B 77 51.025 12.021 -0.953 1.00 24.72 C ANISOU 555 CA GLU B 77 2474 3908 3012 202 -558 649 C ATOM 556 C GLU B 77 50.769 13.477 -0.564 1.00 24.18 C ANISOU 556 C GLU B 77 2477 3885 2824 47 -559 585 C ATOM 557 O GLU B 77 50.129 13.745 0.449 1.00 24.21 O ANISOU 557 O GLU B 77 2598 3889 2710 -34 -605 586 O ATOM 558 CB GLU B 77 52.426 11.583 -0.513 1.00 26.59 C ANISOU 558 CB GLU B 77 2538 4231 3333 239 -675 746 C ATOM 559 CG GLU B 77 52.710 11.826 0.973 1.00 28.61 C ANISOU 559 CG GLU B 77 2815 4573 3483 136 -836 823 C ATOM 560 CD GLU B 77 53.719 10.854 1.564 1.00 32.15 C ANISOU 560 CD GLU B 77 3125 5071 4018 216 -974 962 C ATOM 561 OE1 GLU B 77 54.783 10.623 0.938 1.00 33.49 O ANISOU 561 OE1 GLU B 77 3109 5277 4338 296 -972 986 O ATOM 562 OE2 GLU B 77 53.445 10.325 2.669 1.00 33.46 O ANISOU 562 OE2 GLU B 77 3367 5241 4103 200 -1085 1053 O ATOM 563 N ILE B 78 51.268 14.411 -1.370 1.00 23.77 N ANISOU 563 N ILE B 78 2361 3866 2806 2 -499 527 N ATOM 564 CA ILE B 78 51.019 15.827 -1.131 1.00 23.17 C ANISOU 564 CA ILE B 78 2359 3806 2640 -140 -484 460 C ATOM 565 C ILE B 78 49.553 16.165 -1.422 1.00 21.69 C ANISOU 565 C ILE B 78 2332 3516 2392 -144 -385 391 C ATOM 566 O ILE B 78 48.918 16.901 -0.666 1.00 21.71 O ANISOU 566 O ILE B 78 2447 3504 2298 -238 -391 351 O ATOM 567 CB ILE B 78 51.990 16.732 -1.940 1.00 23.58 C ANISOU 567 CB ILE B 78 2295 3911 2753 -193 -445 431 C ATOM 568 CG1 ILE B 78 53.439 16.489 -1.487 1.00 25.56 C ANISOU 568 CG1 ILE B 78 2368 4279 3066 -207 -557 502 C ATOM 569 CG2 ILE B 78 51.629 18.211 -1.773 1.00 23.09 C ANISOU 569 CG2 ILE B 78 2329 3833 2611 -338 -415 358 C ATOM 570 CD1 ILE B 78 54.509 17.220 -2.297 1.00 25.97 C ANISOU 570 CD1 ILE B 78 2275 4395 3198 -256 -513 483 C ATOM 571 N ALA B 79 49.016 15.598 -2.496 1.00 20.61 N ANISOU 571 N ALA B 79 2203 3312 2314 -42 -294 373 N ATOM 572 CA ALA B 79 47.674 15.938 -2.966 1.00 19.26 C ANISOU 572 CA ALA B 79 2157 3054 2107 -40 -204 314 C ATOM 573 C ALA B 79 46.532 15.362 -2.115 1.00 18.81 C ANISOU 573 C ALA B 79 2214 2944 1989 -29 -218 321 C ATOM 574 O ALA B 79 45.558 16.063 -1.814 1.00 18.16 O ANISOU 574 O ALA B 79 2234 2820 1846 -84 -179 273 O ATOM 575 CB ALA B 79 47.516 15.522 -4.427 1.00 18.63 C ANISOU 575 CB ALA B 79 2047 2935 2097 49 -114 292 C ATOM 576 N ILE B 80 46.663 14.094 -1.729 1.00 19.15 N ANISOU 576 N ILE B 80 2235 2984 2056 43 -268 384 N ATOM 577 CA ILE B 80 45.573 13.344 -1.107 1.00 18.91 C ANISOU 577 CA ILE B 80 2306 2895 1982 62 -266 401 C ATOM 578 C ILE B 80 45.591 13.388 0.422 1.00 19.84 C ANISOU 578 C ILE B 80 2482 3059 1998 -18 -350 444 C ATOM 579 O ILE B 80 44.534 13.367 1.055 1.00 19.45 O ANISOU 579 O ILE B 80 2541 2973 1874 -55 -322 428 O ATOM 580 CB ILE B 80 45.558 11.861 -1.601 1.00 19.02 C ANISOU 580 CB ILE B 80 2288 2855 2083 182 -260 445 C ATOM 581 CG1 ILE B 80 45.349 11.783 -3.120 1.00 18.08 C ANISOU 581 CG1 ILE B 80 2142 2691 2037 247 -166 384 C ATOM 582 CG2 ILE B 80 44.517 11.020 -0.848 1.00 18.85 C ANISOU 582 CG2 ILE B 80 2368 2773 2020 188 -266 478 C ATOM 583 CD1 ILE B 80 43.983 12.291 -3.620 1.00 16.86 C ANISOU 583 CD1 ILE B 80 2080 2481 1843 218 -88 317 C ATOM 584 N SER B 81 46.787 13.439 1.007 1.00 21.30 N ANISOU 584 N SER B 81 2590 3330 2175 -49 -454 500 N ATOM 585 CA SER B 81 46.937 13.410 2.465 1.00 22.65 C ANISOU 585 CA SER B 81 2813 3562 2229 -134 -556 554 C ATOM 586 C SER B 81 46.247 14.598 3.115 1.00 22.75 C ANISOU 586 C SER B 81 2943 3582 2117 -263 -515 468 C ATOM 587 O SER B 81 46.548 15.753 2.801 1.00 22.87 O ANISOU 587 O SER B 81 2942 3615 2133 -329 -487 396 O ATOM 588 CB SER B 81 48.409 13.368 2.877 1.00 23.89 C ANISOU 588 CB SER B 81 2846 3824 2406 -153 -688 629 C ATOM 589 OG SER B 81 49.030 12.192 2.399 1.00 24.22 O ANISOU 589 OG SER B 81 2777 3850 2576 -20 -722 715 O ATOM 590 N GLY B 82 45.309 14.299 4.008 1.00 23.00 N ANISOU 590 N GLY B 82 3097 3592 2049 -300 -500 473 N ATOM 591 CA GLY B 82 44.577 15.324 4.733 1.00 23.29 C ANISOU 591 CA GLY B 82 3254 3629 1966 -417 -444 383 C ATOM 592 C GLY B 82 43.393 15.889 3.972 1.00 22.25 C ANISOU 592 C GLY B 82 3170 3400 1885 -388 -298 287 C ATOM 593 O GLY B 82 42.646 16.712 4.516 1.00 22.55 O ANISOU 593 O GLY B 82 3304 3417 1848 -465 -227 205 O ATOM 594 N ALA B 83 43.220 15.454 2.721 1.00 21.17 N ANISOU 594 N ALA B 83 2965 3204 1873 -278 -252 295 N ATOM 595 CA ALA B 83 42.130 15.938 1.876 1.00 20.13 C ANISOU 595 CA ALA B 83 2862 2989 1798 -244 -135 221 C ATOM 596 C ALA B 83 40.786 15.499 2.432 1.00 20.18 C ANISOU 596 C ALA B 83 2957 2948 1763 -245 -70 210 C ATOM 597 O ALA B 83 40.584 14.323 2.743 1.00 20.48 O ANISOU 597 O ALA B 83 3006 2982 1794 -209 -97 277 O ATOM 598 CB ALA B 83 42.294 15.457 0.446 1.00 19.19 C ANISOU 598 CB ALA B 83 2657 2835 1798 -139 -115 238 C ATOM 599 N ASP B 84 39.880 16.458 2.578 1.00 20.15 N ANISOU 599 N ASP B 84 3014 2903 1740 -287 21 126 N ATOM 600 CA ASP B 84 38.532 16.169 3.034 1.00 20.44 C ANISOU 600 CA ASP B 84 3117 2896 1753 -289 105 103 C ATOM 601 C ASP B 84 37.700 15.659 1.867 1.00 19.64 C ANISOU 601 C ASP B 84 2966 2729 1767 -194 153 109 C ATOM 602 O ASP B 84 36.824 14.814 2.045 1.00 19.96 O ANISOU 602 O ASP B 84 3027 2744 1814 -175 186 131 O ATOM 603 CB ASP B 84 37.885 17.419 3.642 1.00 20.91 C ANISOU 603 CB ASP B 84 3248 2931 1765 -363 195 3 C ATOM 604 CG ASP B 84 38.585 17.884 4.912 1.00 22.24 C ANISOU 604 CG ASP B 84 3490 3169 1793 -480 153 -20 C ATOM 605 OD1 ASP B 84 39.016 19.060 4.953 1.00 22.57 O ANISOU 605 OD1 ASP B 84 3546 3204 1824 -538 163 -91 O ATOM 606 OD2 ASP B 84 38.710 17.075 5.862 1.00 22.19 O ANISOU 606 OD2 ASP B 84 3528 3220 1682 -522 104 37 O ATOM 607 N VAL B 85 37.985 16.184 0.676 1.00 18.95 N ANISOU 607 N VAL B 85 2817 2619 1762 -147 155 91 N ATOM 608 CA VAL B 85 37.247 15.856 -0.536 1.00 18.08 C ANISOU 608 CA VAL B 85 2664 2459 1747 -70 189 91 C ATOM 609 C VAL B 85 38.245 15.571 -1.658 1.00 18.04 C ANISOU 609 C VAL B 85 2589 2473 1793 -18 137 122 C ATOM 610 O VAL B 85 39.217 16.308 -1.844 1.00 18.40 O ANISOU 610 O VAL B 85 2609 2550 1834 -42 112 116 O ATOM 611 CB VAL B 85 36.318 17.024 -0.963 1.00 17.65 C ANISOU 611 CB VAL B 85 2615 2351 1739 -70 267 30 C ATOM 612 CG1 VAL B 85 35.368 16.587 -2.058 1.00 17.19 C ANISOU 612 CG1 VAL B 85 2514 2253 1762 -3 289 39 C ATOM 613 CG2 VAL B 85 35.526 17.539 0.208 1.00 18.02 C ANISOU 613 CG2 VAL B 85 2726 2381 1739 -126 337 -21 C ATOM 614 N VAL B 86 38.011 14.487 -2.392 1.00 17.99 N ANISOU 614 N VAL B 86 2555 2447 1835 45 130 149 N ATOM 615 CA VAL B 86 38.836 14.132 -3.545 1.00 17.97 C ANISOU 615 CA VAL B 86 2492 2456 1880 99 105 163 C ATOM 616 C VAL B 86 37.901 14.035 -4.739 1.00 17.79 C ANISOU 616 C VAL B 86 2463 2394 1904 137 144 137 C ATOM 617 O VAL B 86 37.017 13.175 -4.784 1.00 17.87 O ANISOU 617 O VAL B 86 2489 2368 1933 155 155 138 O ATOM 618 CB VAL B 86 39.575 12.783 -3.347 1.00 18.37 C ANISOU 618 CB VAL B 86 2518 2516 1946 143 55 214 C ATOM 619 CG1 VAL B 86 40.453 12.472 -4.547 1.00 18.16 C ANISOU 619 CG1 VAL B 86 2425 2500 1974 201 53 212 C ATOM 620 CG2 VAL B 86 40.414 12.794 -2.068 1.00 18.95 C ANISOU 620 CG2 VAL B 86 2596 2638 1965 101 -6 259 C ATOM 621 N ILE B 87 38.087 14.942 -5.692 1.00 17.81 N ANISOU 621 N ILE B 87 2443 2404 1922 139 159 120 N ATOM 622 CA ILE B 87 37.203 15.050 -6.844 1.00 17.61 C ANISOU 622 CA ILE B 87 2413 2354 1925 163 181 105 C ATOM 623 C ILE B 87 37.939 14.637 -8.116 1.00 18.00 C ANISOU 623 C ILE B 87 2432 2429 1979 196 175 106 C ATOM 624 O ILE B 87 38.959 15.234 -8.479 1.00 18.37 O ANISOU 624 O ILE B 87 2452 2512 2016 186 177 113 O ATOM 625 CB ILE B 87 36.633 16.487 -6.995 1.00 17.51 C ANISOU 625 CB ILE B 87 2410 2319 1922 139 207 96 C ATOM 626 CG1 ILE B 87 35.994 16.960 -5.680 1.00 17.62 C ANISOU 626 CG1 ILE B 87 2459 2306 1932 105 236 76 C ATOM 627 CG2 ILE B 87 35.625 16.543 -8.136 1.00 17.50 C ANISOU 627 CG2 ILE B 87 2399 2299 1952 166 210 100 C ATOM 628 CD1 ILE B 87 35.387 18.365 -5.719 1.00 17.69 C ANISOU 628 CD1 ILE B 87 2479 2269 1974 93 276 59 C ATOM 629 N LEU B 88 37.422 13.606 -8.780 1.00 18.17 N ANISOU 629 N LEU B 88 2458 2434 2013 226 174 93 N ATOM 630 CA LEU B 88 37.995 13.132 -10.036 1.00 18.63 C ANISOU 630 CA LEU B 88 2501 2514 2065 253 184 75 C ATOM 631 C LEU B 88 37.255 13.749 -11.211 1.00 18.90 C ANISOU 631 C LEU B 88 2548 2558 2076 238 186 68 C ATOM 632 O LEU B 88 36.101 13.408 -11.470 1.00 19.26 O ANISOU 632 O LEU B 88 2610 2581 2128 233 171 58 O ATOM 633 CB LEU B 88 37.940 11.598 -10.129 1.00 18.87 C ANISOU 633 CB LEU B 88 2540 2510 2119 288 183 52 C ATOM 634 CG LEU B 88 38.954 10.749 -9.355 1.00 18.96 C ANISOU 634 CG LEU B 88 2530 2510 2164 325 176 71 C ATOM 635 CD1 LEU B 88 38.693 10.791 -7.857 1.00 18.89 C ANISOU 635 CD1 LEU B 88 2538 2487 2155 303 146 113 C ATOM 636 CD2 LEU B 88 38.926 9.310 -9.849 1.00 19.26 C ANISOU 636 CD2 LEU B 88 2583 2495 2239 368 190 40 C ATOM 637 N THR B 89 37.917 14.665 -11.912 1.00 19.24 N ANISOU 637 N THR B 89 2580 2638 2091 223 200 82 N ATOM 638 CA THR B 89 37.351 15.259 -13.124 1.00 19.63 C ANISOU 638 CA THR B 89 2649 2705 2105 206 194 95 C ATOM 639 C THR B 89 38.254 14.966 -14.319 1.00 20.11 C ANISOU 639 C THR B 89 2710 2817 2113 204 225 76 C ATOM 640 O THR B 89 39.080 15.791 -14.724 1.00 20.37 O ANISOU 640 O THR B 89 2733 2886 2122 182 251 101 O ATOM 641 CB THR B 89 37.060 16.760 -12.943 1.00 19.56 C ANISOU 641 CB THR B 89 2642 2679 2109 181 188 141 C ATOM 642 OG1 THR B 89 36.128 16.915 -11.869 1.00 20.70 O ANISOU 642 OG1 THR B 89 2787 2774 2303 187 178 141 O ATOM 643 CG2 THR B 89 36.435 17.340 -14.181 1.00 19.72 C ANISOU 643 CG2 THR B 89 2683 2715 2097 169 167 177 C ATOM 644 N VAL B 90 38.080 13.762 -14.858 1.00 20.40 N ANISOU 644 N VAL B 90 2764 2855 2134 222 231 27 N ATOM 645 CA VAL B 90 38.862 13.248 -15.978 1.00 21.07 C ANISOU 645 CA VAL B 90 2858 2983 2166 224 279 -16 C ATOM 646 C VAL B 90 38.012 12.246 -16.747 1.00 21.39 C ANISOU 646 C VAL B 90 2946 3013 2170 216 265 -71 C ATOM 647 O VAL B 90 37.084 11.672 -16.178 1.00 21.08 O ANISOU 647 O VAL B 90 2914 2924 2173 221 225 -80 O ATOM 648 CB VAL B 90 40.137 12.488 -15.505 1.00 21.47 C ANISOU 648 CB VAL B 90 2862 3029 2267 270 329 -48 C ATOM 649 CG1 VAL B 90 41.294 13.438 -15.271 1.00 21.40 C ANISOU 649 CG1 VAL B 90 2799 3064 2267 258 356 -9 C ATOM 650 CG2 VAL B 90 39.853 11.629 -14.263 1.00 20.98 C ANISOU 650 CG2 VAL B 90 2790 2901 2281 307 298 -49 C ATOM 651 N PRO B 91 38.318 12.037 -18.044 1.00 22.16 N ANISOU 651 N PRO B 91 3078 3159 2182 193 301 -113 N ATOM 652 CA PRO B 91 37.723 10.915 -18.767 1.00 22.67 C ANISOU 652 CA PRO B 91 3195 3211 2206 177 297 -190 C ATOM 653 C PRO B 91 37.860 9.619 -17.962 1.00 22.62 C ANISOU 653 C PRO B 91 3178 3122 2292 227 319 -245 C ATOM 654 O PRO B 91 38.920 9.343 -17.396 1.00 22.41 O ANISOU 654 O PRO B 91 3110 3075 2330 281 369 -248 O ATOM 655 CB PRO B 91 38.556 10.843 -20.047 1.00 23.74 C ANISOU 655 CB PRO B 91 3366 3413 2243 155 371 -242 C ATOM 656 CG PRO B 91 39.045 12.228 -20.260 1.00 23.56 C ANISOU 656 CG PRO B 91 3322 3451 2180 131 377 -159 C ATOM 657 CD PRO B 91 39.206 12.845 -18.903 1.00 22.68 C ANISOU 657 CD PRO B 91 3145 3296 2175 166 351 -93 C ATOM 658 N ALA B 92 36.784 8.840 -17.919 1.00 22.79 N ANISOU 658 N ALA B 92 3235 3097 2327 204 275 -277 N ATOM 659 CA ALA B 92 36.687 7.673 -17.042 1.00 22.71 C ANISOU 659 CA ALA B 92 3224 2992 2412 240 283 -306 C ATOM 660 C ALA B 92 37.856 6.685 -17.111 1.00 23.38 C ANISOU 660 C ALA B 92 3309 3030 2544 301 364 -370 C ATOM 661 O ALA B 92 38.116 5.977 -16.134 1.00 23.55 O ANISOU 661 O ALA B 92 3311 2974 2664 352 369 -354 O ATOM 662 CB ALA B 92 35.357 6.951 -17.261 1.00 23.07 C ANISOU 662 CB ALA B 92 3312 2999 2453 185 232 -344 C ATOM 663 N PHE B 93 38.556 6.633 -18.244 1.00 24.07 N ANISOU 663 N PHE B 93 3418 3162 2565 299 432 -436 N ATOM 664 CA PHE B 93 39.692 5.712 -18.390 1.00 24.81 C ANISOU 664 CA PHE B 93 3499 3208 2718 368 528 -505 C ATOM 665 C PHE B 93 40.872 6.080 -17.483 1.00 24.12 C ANISOU 665 C PHE B 93 3316 3128 2720 443 549 -435 C ATOM 666 O PHE B 93 41.709 5.232 -17.172 1.00 24.78 O ANISOU 666 O PHE B 93 3364 3150 2902 522 601 -461 O ATOM 667 CB PHE B 93 40.129 5.571 -19.856 1.00 26.27 C ANISOU 667 CB PHE B 93 3734 3447 2802 340 614 -607 C ATOM 668 CG PHE B 93 40.899 6.751 -20.392 1.00 27.05 C ANISOU 668 CG PHE B 93 3793 3661 2822 323 652 -566 C ATOM 669 CD1 PHE B 93 40.274 7.694 -21.207 1.00 27.43 C ANISOU 669 CD1 PHE B 93 3888 3801 2732 236 609 -535 C ATOM 670 CD2 PHE B 93 42.258 6.904 -20.112 1.00 28.28 C ANISOU 670 CD2 PHE B 93 3862 3834 3048 390 730 -551 C ATOM 671 CE1 PHE B 93 40.982 8.784 -21.723 1.00 27.84 C ANISOU 671 CE1 PHE B 93 3915 3950 2711 211 648 -488 C ATOM 672 CE2 PHE B 93 42.972 7.994 -20.614 1.00 29.23 C ANISOU 672 CE2 PHE B 93 3946 4060 3101 360 771 -512 C ATOM 673 CZ PHE B 93 42.329 8.937 -21.426 1.00 28.30 C ANISOU 673 CZ PHE B 93 3890 4023 2839 267 734 -480 C ATOM 674 N ALA B 94 40.920 7.342 -17.059 1.00 22.78 N ANISOU 674 N ALA B 94 3102 3030 2522 417 503 -347 N ATOM 675 CA ALA B 94 41.949 7.830 -16.146 1.00 22.00 C ANISOU 675 CA ALA B 94 2914 2952 2493 463 502 -277 C ATOM 676 C ALA B 94 41.647 7.531 -14.676 1.00 21.26 C ANISOU 676 C ALA B 94 2802 2795 2482 490 431 -210 C ATOM 677 O ALA B 94 42.533 7.668 -13.822 1.00 21.58 O ANISOU 677 O ALA B 94 2769 2844 2585 530 419 -156 O ATOM 678 CB ALA B 94 42.155 9.322 -16.341 1.00 21.49 C ANISOU 678 CB ALA B 94 2824 2981 2361 409 490 -220 C ATOM 679 N HIS B 95 40.411 7.121 -14.382 1.00 20.36 N ANISOU 679 N HIS B 95 2749 2624 2362 459 383 -212 N ATOM 680 CA HIS B 95 39.983 6.892 -13.001 1.00 19.56 C ANISOU 680 CA HIS B 95 2645 2471 2316 466 324 -146 C ATOM 681 C HIS B 95 40.807 5.831 -12.279 1.00 20.08 C ANISOU 681 C HIS B 95 2680 2467 2482 543 332 -126 C ATOM 682 O HIS B 95 41.216 6.035 -11.136 1.00 20.19 O ANISOU 682 O HIS B 95 2655 2488 2529 560 287 -48 O ATOM 683 CB HIS B 95 38.490 6.551 -12.921 1.00 19.31 C ANISOU 683 CB HIS B 95 2677 2393 2268 414 287 -158 C ATOM 684 CG HIS B 95 37.583 7.708 -13.207 1.00 18.48 C ANISOU 684 CG HIS B 95 2579 2352 2093 349 254 -140 C ATOM 685 ND1 HIS B 95 36.285 7.545 -13.635 1.00 18.92 N ANISOU 685 ND1 HIS B 95 2671 2394 2123 297 225 -164 N ATOM 686 CD2 HIS B 95 37.784 9.044 -13.131 1.00 18.20 C ANISOU 686 CD2 HIS B 95 2512 2384 2020 331 242 -96 C ATOM 687 CE1 HIS B 95 35.722 8.727 -13.801 1.00 18.31 C ANISOU 687 CE1 HIS B 95 2579 2376 2003 262 195 -129 C ATOM 688 NE2 HIS B 95 36.611 9.654 -13.500 1.00 17.90 N ANISOU 688 NE2 HIS B 95 2494 2365 1943 282 209 -88 N ATOM 689 N GLU B 96 41.053 4.706 -12.945 1.00 20.82 N ANISOU 689 N GLU B 96 2796 2491 2624 589 386 -196 N ATOM 690 CA GLU B 96 41.853 3.620 -12.379 1.00 21.48 C ANISOU 690 CA GLU B 96 2849 2488 2825 679 400 -175 C ATOM 691 C GLU B 96 43.149 4.136 -11.747 1.00 21.70 C ANISOU 691 C GLU B 96 2769 2579 2898 733 383 -101 C ATOM 692 O GLU B 96 43.473 3.789 -10.609 1.00 21.86 O ANISOU 692 O GLU B 96 2759 2565 2981 771 325 -13 O ATOM 693 CB GLU B 96 42.161 2.577 -13.454 1.00 22.72 C ANISOU 693 CB GLU B 96 3035 2571 3028 727 490 -285 C ATOM 694 CG GLU B 96 42.916 1.348 -12.960 1.00 23.88 C ANISOU 694 CG GLU B 96 3153 2597 3322 835 512 -267 C ATOM 695 CD GLU B 96 43.076 0.295 -14.040 1.00 24.98 C ANISOU 695 CD GLU B 96 3340 2641 3511 877 616 -397 C ATOM 696 OE1 GLU B 96 44.144 0.263 -14.683 1.00 26.12 O ANISOU 696 OE1 GLU B 96 3419 2810 3694 944 703 -450 O ATOM 697 OE2 GLU B 96 42.128 -0.484 -14.263 1.00 24.31 O ANISOU 697 OE2 GLU B 96 3355 2458 3423 834 619 -454 O ATOM 698 N GLY B 97 43.866 4.980 -12.487 1.00 21.60 N ANISOU 698 N GLY B 97 2699 2663 2844 725 429 -131 N ATOM 699 CA GLY B 97 45.147 5.519 -12.048 1.00 21.89 C ANISOU 699 CA GLY B 97 2619 2772 2926 761 419 -72 C ATOM 700 C GLY B 97 45.083 6.345 -10.778 1.00 21.14 C ANISOU 700 C GLY B 97 2502 2728 2803 714 319 28 C ATOM 701 O GLY B 97 45.976 6.254 -9.934 1.00 21.62 O ANISOU 701 O GLY B 97 2480 2807 2928 755 271 100 O ATOM 702 N TYR B 98 44.033 7.157 -10.649 1.00 20.09 N ANISOU 702 N TYR B 98 2440 2619 2574 627 288 31 N ATOM 703 CA TYR B 98 43.848 8.002 -9.467 1.00 19.39 C ANISOU 703 CA TYR B 98 2350 2571 2445 571 210 105 C ATOM 704 C TYR B 98 43.469 7.190 -8.244 1.00 19.64 C ANISOU 704 C TYR B 98 2416 2539 2508 588 147 168 C ATOM 705 O TYR B 98 44.006 7.427 -7.162 1.00 20.19 O ANISOU 705 O TYR B 98 2449 2644 2578 580 82 242 O ATOM 706 CB TYR B 98 42.836 9.123 -9.720 1.00 18.22 C ANISOU 706 CB TYR B 98 2263 2456 2205 486 210 85 C ATOM 707 CG TYR B 98 43.353 10.125 -10.717 1.00 18.53 C ANISOU 707 CG TYR B 98 2267 2566 2205 457 256 56 C ATOM 708 CD1 TYR B 98 44.308 11.070 -10.352 1.00 18.97 C ANISOU 708 CD1 TYR B 98 2255 2692 2260 429 241 92 C ATOM 709 CD2 TYR B 98 42.917 10.104 -12.039 1.00 18.75 C ANISOU 709 CD2 TYR B 98 2335 2596 2193 448 312 -5 C ATOM 710 CE1 TYR B 98 44.808 11.980 -11.281 1.00 19.47 C ANISOU 710 CE1 TYR B 98 2289 2816 2291 393 291 73 C ATOM 711 CE2 TYR B 98 43.407 11.006 -12.971 1.00 19.24 C ANISOU 711 CE2 TYR B 98 2376 2726 2209 415 357 -19 C ATOM 712 CZ TYR B 98 44.353 11.940 -12.588 1.00 19.07 C ANISOU 712 CZ TYR B 98 2286 2765 2196 388 351 22 C ATOM 713 OH TYR B 98 44.838 12.832 -13.515 1.00 19.02 O ANISOU 713 OH TYR B 98 2261 2820 2145 345 403 16 O ATOM 714 N PHE B 99 42.566 6.222 -8.418 1.00 19.46 N ANISOU 714 N PHE B 99 2466 2424 2503 601 165 142 N ATOM 715 CA PHE B 99 42.207 5.307 -7.334 1.00 19.51 C ANISOU 715 CA PHE B 99 2513 2355 2544 614 116 209 C ATOM 716 C PHE B 99 43.434 4.555 -6.803 1.00 20.75 C ANISOU 716 C PHE B 99 2600 2489 2795 702 82 278 C ATOM 717 O PHE B 99 43.599 4.412 -5.593 1.00 21.05 O ANISOU 717 O PHE B 99 2638 2530 2830 696 6 375 O ATOM 718 CB PHE B 99 41.125 4.320 -7.777 1.00 19.35 C ANISOU 718 CB PHE B 99 2575 2230 2545 609 151 161 C ATOM 719 CG PHE B 99 39.754 4.925 -7.906 1.00 18.08 C ANISOU 719 CG PHE B 99 2474 2089 2305 521 157 127 C ATOM 720 CD1 PHE B 99 39.204 5.683 -6.876 1.00 17.80 C ANISOU 720 CD1 PHE B 99 2455 2097 2210 458 119 179 C ATOM 721 CD2 PHE B 99 38.995 4.707 -9.045 1.00 17.82 C ANISOU 721 CD2 PHE B 99 2478 2030 2261 498 199 41 C ATOM 722 CE1 PHE B 99 37.928 6.235 -6.995 1.00 16.95 C ANISOU 722 CE1 PHE B 99 2384 2002 2053 390 133 148 C ATOM 723 CE2 PHE B 99 37.717 5.253 -9.171 1.00 17.30 C ANISOU 723 CE2 PHE B 99 2447 1986 2139 423 193 21 C ATOM 724 CZ PHE B 99 37.184 6.014 -8.145 1.00 16.38 C ANISOU 724 CZ PHE B 99 2332 1908 1986 376 164 76 C ATOM 725 N GLN B 100 44.289 4.089 -7.715 1.00 21.65 N ANISOU 725 N GLN B 100 2652 2584 2992 783 138 231 N ATOM 726 CA GLN B 100 45.540 3.406 -7.356 1.00 23.03 C ANISOU 726 CA GLN B 100 2729 2736 3284 885 114 294 C ATOM 727 C GLN B 100 46.528 4.325 -6.619 1.00 22.90 C ANISOU 727 C GLN B 100 2610 2843 3249 867 39 372 C ATOM 728 O GLN B 100 47.171 3.903 -5.654 1.00 23.80 O ANISOU 728 O GLN B 100 2671 2954 3418 910 -45 477 O ATOM 729 CB GLN B 100 46.193 2.773 -8.594 1.00 23.75 C ANISOU 729 CB GLN B 100 2772 2780 3472 975 218 204 C ATOM 730 CG GLN B 100 45.593 1.417 -8.989 1.00 25.04 C ANISOU 730 CG GLN B 100 3022 2785 3708 1024 269 154 C ATOM 731 CD GLN B 100 46.031 0.909 -10.379 1.00 25.96 C ANISOU 731 CD GLN B 100 3121 2857 3885 1088 397 24 C ATOM 732 OE1 GLN B 100 45.362 0.058 -10.972 1.00 26.17 O ANISOU 732 OE1 GLN B 100 3242 2772 3930 1090 455 -59 O ATOM 733 NE2 GLN B 100 47.149 1.428 -10.892 1.00 27.03 N ANISOU 733 NE2 GLN B 100 3140 3084 4048 1129 447 0 N ATOM 734 N ALA B 101 46.627 5.577 -7.065 1.00 21.86 N ANISOU 734 N ALA B 101 2452 2816 3037 796 63 324 N ATOM 735 CA ALA B 101 47.538 6.552 -6.461 1.00 21.97 C ANISOU 735 CA ALA B 101 2373 2947 3027 755 -1 380 C ATOM 736 C ALA B 101 47.074 7.027 -5.080 1.00 21.57 C ANISOU 736 C ALA B 101 2380 2929 2885 671 -104 455 C ATOM 737 O ALA B 101 47.893 7.231 -4.177 1.00 22.46 O ANISOU 737 O ALA B 101 2424 3108 3002 660 -195 536 O ATOM 738 CB ALA B 101 47.751 7.745 -7.393 1.00 21.04 C ANISOU 738 CB ALA B 101 2224 2913 2856 695 66 307 C ATOM 739 N MET B 102 45.766 7.198 -4.918 1.00 20.40 N ANISOU 739 N MET B 102 2357 2742 2653 608 -88 426 N ATOM 740 CA MET B 102 45.222 7.730 -3.676 1.00 20.08 C ANISOU 740 CA MET B 102 2384 2734 2513 519 -156 475 C ATOM 741 C MET B 102 45.143 6.683 -2.565 1.00 20.77 C ANISOU 741 C MET B 102 2507 2771 2612 545 -230 576 C ATOM 742 O MET B 102 45.265 7.019 -1.383 1.00 21.35 O ANISOU 742 O MET B 102 2601 2901 2610 482 -311 644 O ATOM 743 CB MET B 102 43.865 8.419 -3.912 1.00 18.78 C ANISOU 743 CB MET B 102 2319 2552 2264 443 -99 406 C ATOM 744 CG MET B 102 42.668 7.496 -4.137 1.00 18.48 C ANISOU 744 CG MET B 102 2367 2415 2241 461 -58 385 C ATOM 745 SD MET B 102 41.112 8.406 -4.364 1.00 17.86 S ANISOU 745 SD MET B 102 2370 2334 2082 376 -3 316 S ATOM 746 CE MET B 102 41.311 9.000 -6.047 1.00 15.54 C ANISOU 746 CE MET B 102 2033 2063 1810 397 60 231 C ATOM 747 N ALA B 103 44.975 5.421 -2.957 1.00 20.95 N ANISOU 747 N ALA B 103 2545 2687 2728 631 -201 586 N ATOM 748 CA ALA B 103 44.765 4.296 -2.028 1.00 21.61 C ANISOU 748 CA ALA B 103 2681 2693 2837 659 -259 688 C ATOM 749 C ALA B 103 45.537 4.337 -0.694 1.00 22.45 C ANISOU 749 C ALA B 103 2755 2868 2906 641 -386 820 C ATOM 750 O ALA B 103 44.918 4.266 0.369 1.00 22.59 O ANISOU 750 O ALA B 103 2866 2889 2829 570 -433 884 O ATOM 751 CB ALA B 103 44.979 2.950 -2.746 1.00 22.42 C ANISOU 751 CB ALA B 103 2767 2666 3087 777 -215 684 C ATOM 752 N PRO B 104 46.876 4.478 -0.733 1.00 23.15 N ANISOU 752 N PRO B 104 2710 3023 3063 696 -444 862 N ATOM 753 CA PRO B 104 47.548 4.427 0.565 1.00 24.35 C ANISOU 753 CA PRO B 104 2833 3243 3174 672 -586 999 C ATOM 754 C PRO B 104 47.629 5.773 1.296 1.00 23.97 C ANISOU 754 C PRO B 104 2799 3338 2972 535 -642 986 C ATOM 755 O PRO B 104 48.267 5.854 2.346 1.00 25.16 O ANISOU 755 O PRO B 104 2922 3569 3068 496 -770 1090 O ATOM 756 CB PRO B 104 48.955 3.917 0.209 1.00 25.77 C ANISOU 756 CB PRO B 104 2845 3431 3516 797 -630 1056 C ATOM 757 CG PRO B 104 49.166 4.289 -1.241 1.00 24.97 C ANISOU 757 CG PRO B 104 2673 3324 3490 840 -501 918 C ATOM 758 CD PRO B 104 47.834 4.682 -1.839 1.00 23.29 C ANISOU 758 CD PRO B 104 2594 3067 3188 770 -392 798 C ATOM 759 N TYR B 105 46.988 6.810 0.755 1.00 22.52 N ANISOU 759 N TYR B 105 2660 3179 2718 459 -552 861 N ATOM 760 CA TYR B 105 47.076 8.160 1.330 1.00 22.25 C ANISOU 760 CA TYR B 105 2641 3257 2554 331 -584 827 C ATOM 761 C TYR B 105 45.728 8.741 1.759 1.00 21.24 C ANISOU 761 C TYR B 105 2663 3112 2297 229 -523 764 C ATOM 762 O TYR B 105 45.675 9.673 2.568 1.00 21.37 O ANISOU 762 O TYR B 105 2726 3205 2191 117 -556 747 O ATOM 763 CB TYR B 105 47.799 9.119 0.370 1.00 21.82 C ANISOU 763 CB TYR B 105 2481 3261 2549 327 -540 745 C ATOM 764 CG TYR B 105 49.221 8.692 0.058 1.00 23.06 C ANISOU 764 CG TYR B 105 2469 3460 2834 413 -596 804 C ATOM 765 CD1 TYR B 105 50.198 8.685 1.054 1.00 24.56 C ANISOU 765 CD1 TYR B 105 2580 3741 3010 387 -739 908 C ATOM 766 CD2 TYR B 105 49.585 8.285 -1.226 1.00 22.93 C ANISOU 766 CD2 TYR B 105 2367 3396 2951 519 -504 754 C ATOM 767 CE1 TYR B 105 51.494 8.286 0.785 1.00 25.89 C ANISOU 767 CE1 TYR B 105 2571 3951 3314 474 -792 969 C ATOM 768 CE2 TYR B 105 50.885 7.884 -1.509 1.00 24.26 C ANISOU 768 CE2 TYR B 105 2366 3600 3250 606 -537 802 C ATOM 769 CZ TYR B 105 51.837 7.888 -0.498 1.00 25.73 C ANISOU 769 CZ TYR B 105 2459 3876 3442 588 -682 913 C ATOM 770 OH TYR B 105 53.133 7.496 -0.755 1.00 27.24 O ANISOU 770 OH TYR B 105 2459 4108 3782 680 -719 968 O ATOM 771 N VAL B 106 44.649 8.181 1.217 1.00 20.42 N ANISOU 771 N VAL B 106 2627 2907 2224 267 -432 724 N ATOM 772 CA VAL B 106 43.300 8.651 1.497 1.00 19.56 C ANISOU 772 CA VAL B 106 2635 2774 2022 187 -359 662 C ATOM 773 C VAL B 106 42.873 8.292 2.927 1.00 20.41 C ANISOU 773 C VAL B 106 2841 2897 2017 117 -410 741 C ATOM 774 O VAL B 106 43.089 7.165 3.397 1.00 21.37 O ANISOU 774 O VAL B 106 2973 2983 2164 160 -470 850 O ATOM 775 CB VAL B 106 42.288 8.156 0.412 1.00 18.58 C ANISOU 775 CB VAL B 106 2537 2550 1975 242 -255 596 C ATOM 776 CG1 VAL B 106 42.038 6.657 0.507 1.00 19.20 C ANISOU 776 CG1 VAL B 106 2644 2533 2119 306 -266 667 C ATOM 777 CG2 VAL B 106 40.994 8.922 0.492 1.00 17.71 C ANISOU 777 CG2 VAL B 106 2504 2431 1793 166 -177 520 C ATOM 778 N GLN B 107 42.295 9.267 3.622 1.00 20.22 N ANISOU 778 N GLN B 107 2893 2924 1867 6 -381 689 N ATOM 779 CA GLN B 107 41.877 9.064 5.003 1.00 21.16 C ANISOU 779 CA GLN B 107 3117 3074 1850 -81 -412 749 C ATOM 780 C GLN B 107 40.466 8.474 5.055 1.00 20.77 C ANISOU 780 C GLN B 107 3154 2941 1796 -88 -313 736 C ATOM 781 O GLN B 107 39.711 8.575 4.093 1.00 19.66 O ANISOU 781 O GLN B 107 2996 2737 1738 -50 -219 655 O ATOM 782 CB GLN B 107 41.983 10.369 5.802 1.00 21.48 C ANISOU 782 CB GLN B 107 3204 3208 1748 -205 -419 687 C ATOM 783 CG GLN B 107 41.010 11.460 5.389 1.00 20.39 C ANISOU 783 CG GLN B 107 3104 3043 1602 -245 -288 547 C ATOM 784 CD GLN B 107 41.153 12.728 6.207 1.00 20.94 C ANISOU 784 CD GLN B 107 3230 3186 1542 -368 -286 476 C ATOM 785 OE1 GLN B 107 41.188 13.825 5.655 1.00 20.34 O ANISOU 785 OE1 GLN B 107 3127 3102 1498 -382 -236 379 O ATOM 786 NE2 GLN B 107 41.234 12.587 7.526 1.00 22.25 N ANISOU 786 NE2 GLN B 107 3482 3417 1554 -462 -338 524 N ATOM 787 N ASP B 108 40.125 7.846 6.178 1.00 21.82 N ANISOU 787 N ASP B 108 3379 3081 1832 -145 -339 823 N ATOM 788 CA ASP B 108 38.821 7.220 6.357 1.00 21.74 C ANISOU 788 CA ASP B 108 3447 2998 1814 -169 -245 825 C ATOM 789 C ASP B 108 37.684 8.172 6.021 1.00 20.71 C ANISOU 789 C ASP B 108 3333 2861 1674 -212 -110 686 C ATOM 790 O ASP B 108 36.715 7.788 5.359 1.00 20.07 O ANISOU 790 O ASP B 108 3243 2703 1677 -182 -27 648 O ATOM 791 CB ASP B 108 38.662 6.729 7.795 1.00 23.23 C ANISOU 791 CB ASP B 108 3746 3226 1856 -259 -283 932 C ATOM 792 CG ASP B 108 39.411 5.445 8.063 1.00 24.41 C ANISOU 792 CG ASP B 108 3889 3337 2048 -199 -401 1097 C ATOM 793 OD1 ASP B 108 40.036 4.903 7.129 1.00 24.46 O ANISOU 793 OD1 ASP B 108 3802 3279 2212 -81 -440 1116 O ATOM 794 OD2 ASP B 108 39.367 4.967 9.213 1.00 25.88 O ANISOU 794 OD2 ASP B 108 4168 3555 2112 -270 -450 1211 O ATOM 795 N SER B 109 37.822 9.418 6.468 1.00 20.83 N ANISOU 795 N SER B 109 3368 2952 1593 -284 -94 612 N ATOM 796 CA SER B 109 36.752 10.411 6.370 1.00 20.34 C ANISOU 796 CA SER B 109 3329 2881 1517 -328 36 487 C ATOM 797 C SER B 109 36.601 11.049 4.988 1.00 18.90 C ANISOU 797 C SER B 109 3058 2654 1469 -253 79 398 C ATOM 798 O SER B 109 35.661 11.802 4.759 1.00 18.61 O ANISOU 798 O SER B 109 3024 2594 1453 -268 181 308 O ATOM 799 CB SER B 109 36.937 11.495 7.438 1.00 21.09 C ANISOU 799 CB SER B 109 3497 3059 1459 -439 47 433 C ATOM 800 OG SER B 109 38.065 12.298 7.146 1.00 21.37 O ANISOU 800 OG SER B 109 3480 3139 1499 -435 -31 405 O ATOM 801 N ALA B 110 37.512 10.751 4.068 1.00 18.40 N ANISOU 801 N ALA B 110 2915 2579 1498 -172 6 427 N ATOM 802 CA ALA B 110 37.480 11.384 2.748 1.00 17.35 C ANISOU 802 CA ALA B 110 2708 2417 1469 -113 41 353 C ATOM 803 C ALA B 110 36.166 11.154 2.005 1.00 16.88 C ANISOU 803 C ALA B 110 2640 2289 1487 -82 129 309 C ATOM 804 O ALA B 110 35.594 10.060 2.043 1.00 17.25 O ANISOU 804 O ALA B 110 2703 2290 1561 -69 140 351 O ATOM 805 CB ALA B 110 38.654 10.934 1.900 1.00 17.09 C ANISOU 805 CB ALA B 110 2593 2386 1514 -35 -37 393 C ATOM 806 N LEU B 111 35.692 12.204 1.346 1.00 16.39 N ANISOU 806 N LEU B 111 2549 2216 1463 -77 186 229 N ATOM 807 CA LEU B 111 34.576 12.103 0.428 1.00 16.04 C ANISOU 807 CA LEU B 111 2470 2119 1504 -40 245 193 C ATOM 808 C LEU B 111 35.151 11.986 -0.965 1.00 15.62 C ANISOU 808 C LEU B 111 2353 2053 1527 30 204 190 C ATOM 809 O LEU B 111 35.816 12.907 -1.443 1.00 15.74 O ANISOU 809 O LEU B 111 2342 2093 1547 39 190 165 O ATOM 810 CB LEU B 111 33.693 13.345 0.522 1.00 15.97 C ANISOU 810 CB LEU B 111 2463 2104 1502 -67 328 120 C ATOM 811 CG LEU B 111 32.527 13.462 -0.459 1.00 15.87 C ANISOU 811 CG LEU B 111 2396 2048 1587 -27 375 88 C ATOM 812 CD1 LEU B 111 31.415 12.479 -0.114 1.00 15.86 C ANISOU 812 CD1 LEU B 111 2398 2023 1605 -47 418 105 C ATOM 813 CD2 LEU B 111 32.006 14.887 -0.456 1.00 16.20 C ANISOU 813 CD2 LEU B 111 2427 2076 1654 -32 440 27 C ATOM 814 N ILE B 112 34.903 10.853 -1.612 1.00 15.63 N ANISOU 814 N ILE B 112 2340 2015 1585 70 192 211 N ATOM 815 CA ILE B 112 35.457 10.602 -2.941 1.00 15.27 C ANISOU 815 CA ILE B 112 2246 1959 1597 131 164 199 C ATOM 816 C ILE B 112 34.412 10.859 -4.031 1.00 14.95 C ANISOU 816 C ILE B 112 2179 1896 1605 141 198 152 C ATOM 817 O ILE B 112 33.409 10.151 -4.128 1.00 15.03 O ANISOU 817 O ILE B 112 2195 1869 1646 130 217 148 O ATOM 818 CB ILE B 112 36.136 9.215 -3.022 1.00 15.54 C ANISOU 818 CB ILE B 112 2283 1961 1662 174 123 245 C ATOM 819 CG1 ILE B 112 37.314 9.188 -2.038 1.00 15.73 C ANISOU 819 CG1 ILE B 112 2310 2024 1643 171 68 305 C ATOM 820 CG2 ILE B 112 36.604 8.926 -4.449 1.00 15.56 C ANISOU 820 CG2 ILE B 112 2242 1950 1721 232 119 211 C ATOM 821 CD1 ILE B 112 37.994 7.862 -1.864 1.00 16.18 C ANISOU 821 CD1 ILE B 112 2366 2041 1741 221 22 371 C ATOM 822 N VAL B 113 34.668 11.883 -4.841 1.00 14.93 N ANISOU 822 N VAL B 113 2146 1919 1608 155 198 125 N ATOM 823 CA VAL B 113 33.671 12.436 -5.759 1.00 15.15 C ANISOU 823 CA VAL B 113 2147 1937 1671 159 217 96 C ATOM 824 C VAL B 113 34.014 12.138 -7.216 1.00 15.31 C ANISOU 824 C VAL B 113 2146 1966 1704 191 190 84 C ATOM 825 O VAL B 113 35.167 12.290 -7.639 1.00 15.41 O ANISOU 825 O VAL B 113 2152 2005 1699 211 177 87 O ATOM 826 CB VAL B 113 33.507 13.973 -5.552 1.00 15.07 C ANISOU 826 CB VAL B 113 2131 1938 1658 144 244 83 C ATOM 827 CG1 VAL B 113 32.425 14.537 -6.449 1.00 15.43 C ANISOU 827 CG1 VAL B 113 2141 1968 1755 159 253 74 C ATOM 828 CG2 VAL B 113 33.175 14.291 -4.104 1.00 15.63 C ANISOU 828 CG2 VAL B 113 2235 2002 1702 103 286 75 C ATOM 829 N GLY B 114 33.007 11.701 -7.970 1.00 15.62 N ANISOU 829 N GLY B 114 2174 1990 1771 188 185 68 N ATOM 830 CA GLY B 114 33.134 11.489 -9.408 1.00 16.10 C ANISOU 830 CA GLY B 114 2227 2066 1823 202 161 47 C ATOM 831 C GLY B 114 32.402 12.592 -10.145 1.00 16.43 C ANISOU 831 C GLY B 114 2241 2131 1869 195 147 56 C ATOM 832 O GLY B 114 31.171 12.633 -10.144 1.00 16.91 O ANISOU 832 O GLY B 114 2275 2182 1967 180 140 59 O ATOM 833 N LEU B 115 33.153 13.488 -10.778 1.00 16.45 N ANISOU 833 N LEU B 115 2244 2165 1841 206 143 69 N ATOM 834 CA LEU B 115 32.563 14.666 -11.413 1.00 16.72 C ANISOU 834 CA LEU B 115 2259 2211 1885 204 127 98 C ATOM 835 C LEU B 115 33.040 14.821 -12.858 1.00 17.17 C ANISOU 835 C LEU B 115 2329 2311 1883 201 100 107 C ATOM 836 O LEU B 115 33.975 15.577 -13.122 1.00 17.00 O ANISOU 836 O LEU B 115 2318 2307 1833 201 117 126 O ATOM 837 CB LEU B 115 32.897 15.923 -10.593 1.00 16.56 C ANISOU 837 CB LEU B 115 2238 2169 1884 207 158 118 C ATOM 838 CG LEU B 115 32.121 17.218 -10.830 1.00 16.24 C ANISOU 838 CG LEU B 115 2177 2104 1891 216 156 153 C ATOM 839 CD1 LEU B 115 30.809 17.190 -10.097 1.00 16.67 C ANISOU 839 CD1 LEU B 115 2196 2123 2015 225 175 145 C ATOM 840 CD2 LEU B 115 32.936 18.419 -10.400 1.00 15.64 C ANISOU 840 CD2 LEU B 115 2123 2004 1816 208 187 163 C ATOM 841 N PRO B 116 32.410 14.092 -13.800 1.00 17.79 N ANISOU 841 N PRO B 116 2411 2411 1936 186 63 90 N ATOM 842 CA PRO B 116 31.354 13.111 -13.602 1.00 18.25 C ANISOU 842 CA PRO B 116 2455 2450 2030 170 41 63 C ATOM 843 C PRO B 116 31.924 11.730 -13.283 1.00 18.66 C ANISOU 843 C PRO B 116 2540 2475 2076 169 69 9 C ATOM 844 O PRO B 116 33.134 11.515 -13.390 1.00 18.79 O ANISOU 844 O PRO B 116 2580 2497 2061 189 100 -8 O ATOM 845 CB PRO B 116 30.665 13.085 -14.962 1.00 18.85 C ANISOU 845 CB PRO B 116 2529 2571 2062 140 -22 68 C ATOM 846 CG PRO B 116 31.753 13.327 -15.917 1.00 18.61 C ANISOU 846 CG PRO B 116 2543 2583 1944 138 -12 65 C ATOM 847 CD PRO B 116 32.741 14.234 -15.228 1.00 18.29 C ANISOU 847 CD PRO B 116 2501 2528 1922 168 38 95 C ATOM 848 N SER B 117 31.050 10.811 -12.887 1.00 19.18 N ANISOU 848 N SER B 117 2599 2507 2182 146 62 -13 N ATOM 849 CA SER B 117 31.447 9.453 -12.544 1.00 19.62 C ANISOU 849 CA SER B 117 2691 2514 2250 145 86 -53 C ATOM 850 C SER B 117 31.606 8.570 -13.762 1.00 20.12 C ANISOU 850 C SER B 117 2794 2580 2271 126 73 -115 C ATOM 851 O SER B 117 32.585 7.829 -13.882 1.00 20.24 O ANISOU 851 O SER B 117 2846 2567 2279 153 109 -153 O ATOM 852 CB SER B 117 30.394 8.822 -11.637 1.00 19.74 C ANISOU 852 CB SER B 117 2691 2482 2326 114 90 -48 C ATOM 853 OG SER B 117 30.739 9.018 -10.287 1.00 21.09 O ANISOU 853 OG SER B 117 2864 2630 2520 134 128 -12 O ATOM 854 N GLN B 118 30.627 8.666 -14.661 1.00 20.62 N ANISOU 854 N GLN B 118 2846 2679 2308 78 21 -127 N ATOM 855 CA GLN B 118 30.329 7.618 -15.637 1.00 21.39 C ANISOU 855 CA GLN B 118 2987 2771 2369 28 -1 -201 C ATOM 856 C GLN B 118 29.916 6.353 -14.872 1.00 21.36 C ANISOU 856 C GLN B 118 2998 2678 2439 6 19 -232 C ATOM 857 O GLN B 118 29.919 6.342 -13.641 1.00 20.67 O ANISOU 857 O GLN B 118 2891 2549 2415 31 49 -188 O ATOM 858 CB GLN B 118 31.501 7.390 -16.602 1.00 21.79 C ANISOU 858 CB GLN B 118 3097 2842 2341 45 35 -256 C ATOM 859 CG GLN B 118 31.796 8.595 -17.499 1.00 22.60 C ANISOU 859 CG GLN B 118 3194 3036 2356 44 14 -219 C ATOM 860 CD GLN B 118 30.671 8.871 -18.486 1.00 25.80 C ANISOU 860 CD GLN B 118 3597 3506 2702 -25 -74 -209 C ATOM 861 OE1 GLN B 118 30.359 8.035 -19.350 1.00 27.49 O ANISOU 861 OE1 GLN B 118 3858 3731 2855 -85 -97 -283 O ATOM 862 NE2 GLN B 118 30.052 10.048 -18.366 1.00 25.55 N ANISOU 862 NE2 GLN B 118 3507 3513 2689 -17 -127 -119 N ATOM 863 N ALA B 119 29.532 5.303 -15.585 1.00 22.05 N ANISOU 863 N ALA B 119 3130 2737 2513 -51 4 -307 N ATOM 864 CA ALA B 119 29.032 4.101 -14.928 1.00 22.27 C ANISOU 864 CA ALA B 119 3176 2669 2617 -87 21 -333 C ATOM 865 C ALA B 119 30.165 3.239 -14.363 1.00 22.15 C ANISOU 865 C ALA B 119 3217 2557 2643 -25 91 -350 C ATOM 866 O ALA B 119 31.254 3.187 -14.933 1.00 22.37 O ANISOU 866 O ALA B 119 3279 2588 2634 25 126 -389 O ATOM 867 CB ALA B 119 28.163 3.308 -15.882 1.00 23.37 C ANISOU 867 CB ALA B 119 3343 2803 2734 -184 -26 -411 C ATOM 868 N GLY B 120 29.907 2.587 -13.229 1.00 21.87 N ANISOU 868 N GLY B 120 3185 2438 2687 -28 112 -312 N ATOM 869 CA GLY B 120 30.863 1.650 -12.627 1.00 21.74 C ANISOU 869 CA GLY B 120 3219 2316 2726 30 162 -308 C ATOM 870 C GLY B 120 31.933 2.275 -11.753 1.00 20.74 C ANISOU 870 C GLY B 120 3066 2212 2604 117 183 -232 C ATOM 871 O GLY B 120 32.859 1.593 -11.313 1.00 20.97 O ANISOU 871 O GLY B 120 3121 2166 2679 179 212 -216 O ATOM 872 N PHE B 121 31.788 3.571 -11.498 1.00 19.68 N ANISOU 872 N PHE B 121 2876 2175 2425 121 163 -183 N ATOM 873 CA PHE B 121 32.711 4.359 -10.682 1.00 18.96 C ANISOU 873 CA PHE B 121 2758 2122 2324 181 173 -117 C ATOM 874 C PHE B 121 32.921 3.798 -9.258 1.00 19.14 C ANISOU 874 C PHE B 121 2798 2083 2393 196 182 -46 C ATOM 875 O PHE B 121 34.058 3.729 -8.770 1.00 19.21 O ANISOU 875 O PHE B 121 2805 2082 2411 257 186 -8 O ATOM 876 CB PHE B 121 32.201 5.806 -10.636 1.00 18.25 C ANISOU 876 CB PHE B 121 2617 2125 2191 162 153 -87 C ATOM 877 CG PHE B 121 33.039 6.739 -9.812 1.00 17.70 C ANISOU 877 CG PHE B 121 2525 2097 2104 202 162 -32 C ATOM 878 CD1 PHE B 121 32.690 7.025 -8.494 1.00 17.09 C ANISOU 878 CD1 PHE B 121 2443 2015 2036 185 169 21 C ATOM 879 CD2 PHE B 121 34.153 7.361 -10.361 1.00 18.02 C ANISOU 879 CD2 PHE B 121 2551 2185 2112 243 166 -38 C ATOM 880 CE1 PHE B 121 33.450 7.899 -7.727 1.00 16.69 C ANISOU 880 CE1 PHE B 121 2381 2005 1957 206 172 60 C ATOM 881 CE2 PHE B 121 34.923 8.242 -9.598 1.00 18.03 C ANISOU 881 CE2 PHE B 121 2529 2224 2098 264 168 8 C ATOM 882 CZ PHE B 121 34.567 8.507 -8.276 1.00 17.07 C ANISOU 882 CZ PHE B 121 2409 2095 1980 243 166 54 C ATOM 883 N GLU B 122 31.827 3.402 -8.603 1.00 19.07 N ANISOU 883 N GLU B 122 2800 2037 2408 135 184 -23 N ATOM 884 CA GLU B 122 31.883 2.879 -7.239 1.00 18.86 C ANISOU 884 CA GLU B 122 2802 1958 2405 130 194 55 C ATOM 885 C GLU B 122 32.452 1.461 -7.187 1.00 19.48 C ANISOU 885 C GLU B 122 2937 1917 2548 161 200 63 C ATOM 886 O GLU B 122 33.198 1.139 -6.265 1.00 19.96 O ANISOU 886 O GLU B 122 3017 1946 2623 202 192 140 O ATOM 887 CB GLU B 122 30.504 2.908 -6.569 1.00 19.07 C ANISOU 887 CB GLU B 122 2821 1987 2438 45 212 77 C ATOM 888 CG GLU B 122 29.796 4.256 -6.584 1.00 18.73 C ANISOU 888 CG GLU B 122 2714 2043 2360 23 216 68 C ATOM 889 CD GLU B 122 28.891 4.451 -7.795 1.00 19.19 C ANISOU 889 CD GLU B 122 2728 2130 2435 -11 194 4 C ATOM 890 OE1 GLU B 122 29.031 3.703 -8.792 1.00 20.10 O ANISOU 890 OE1 GLU B 122 2869 2208 2561 -16 173 -49 O ATOM 891 OE2 GLU B 122 28.038 5.366 -7.749 1.00 18.76 O ANISOU 891 OE2 GLU B 122 2612 2136 2382 -34 198 8 O ATOM 892 N PHE B 123 32.098 0.618 -8.160 1.00 19.62 N ANISOU 892 N PHE B 123 2983 1866 2606 139 210 -14 N ATOM 893 CA PHE B 123 32.617 -0.759 -8.216 1.00 20.31 C ANISOU 893 CA PHE B 123 3131 1814 2773 174 227 -21 C ATOM 894 C PHE B 123 34.139 -0.755 -8.295 1.00 20.29 C ANISOU 894 C PHE B 123 3113 1805 2790 289 230 -6 C ATOM 895 O PHE B 123 34.812 -1.494 -7.575 1.00 20.95 O ANISOU 895 O PHE B 123 3219 1804 2937 345 227 65 O ATOM 896 CB PHE B 123 32.062 -1.537 -9.418 1.00 20.83 C ANISOU 896 CB PHE B 123 3235 1812 2866 126 243 -136 C ATOM 897 CG PHE B 123 30.563 -1.574 -9.496 1.00 20.81 C ANISOU 897 CG PHE B 123 3227 1823 2855 6 230 -158 C ATOM 898 CD1 PHE B 123 29.924 -1.454 -10.730 1.00 20.87 C ANISOU 898 CD1 PHE B 123 3227 1874 2828 -55 212 -261 C ATOM 899 CD2 PHE B 123 29.783 -1.737 -8.348 1.00 20.52 C ANISOU 899 CD2 PHE B 123 3190 1766 2841 -54 234 -74 C ATOM 900 CE1 PHE B 123 28.529 -1.497 -10.825 1.00 21.16 C ANISOU 900 CE1 PHE B 123 3238 1933 2869 -169 188 -277 C ATOM 901 CE2 PHE B 123 28.389 -1.775 -8.429 1.00 20.54 C ANISOU 901 CE2 PHE B 123 3167 1788 2851 -167 229 -96 C ATOM 902 CZ PHE B 123 27.761 -1.655 -9.670 1.00 21.29 C ANISOU 902 CZ PHE B 123 3238 1926 2927 -222 201 -196 C ATOM 903 N GLN B 124 34.663 0.087 -9.183 1.00 19.59 N ANISOU 903 N GLN B 124 2980 1811 2651 321 236 -65 N ATOM 904 CA GLN B 124 36.094 0.269 -9.362 1.00 19.49 C ANISOU 904 CA GLN B 124 2929 1820 2655 420 247 -59 C ATOM 905 C GLN B 124 36.740 0.763 -8.066 1.00 19.18 C ANISOU 905 C GLN B 124 2852 1826 2610 456 208 61 C ATOM 906 O GLN B 124 37.750 0.214 -7.613 1.00 19.73 O ANISOU 906 O GLN B 124 2906 1846 2745 535 198 116 O ATOM 907 CB GLN B 124 36.331 1.269 -10.490 1.00 18.77 C ANISOU 907 CB GLN B 124 2800 1841 2489 417 262 -134 C ATOM 908 CG GLN B 124 37.782 1.518 -10.837 1.00 18.65 C ANISOU 908 CG GLN B 124 2733 1862 2490 507 290 -141 C ATOM 909 CD GLN B 124 37.925 2.413 -12.045 1.00 18.28 C ANISOU 909 CD GLN B 124 2665 1919 2361 487 316 -215 C ATOM 910 OE1 GLN B 124 37.323 3.487 -12.108 1.00 17.40 O ANISOU 910 OE1 GLN B 124 2540 1898 2173 429 285 -197 O ATOM 911 NE2 GLN B 124 38.727 1.977 -13.017 1.00 19.11 N ANISOU 911 NE2 GLN B 124 2771 2008 2485 535 380 -295 N ATOM 912 N CYS B 125 36.134 1.795 -7.480 1.00 18.30 N ANISOU 912 N CYS B 125 2724 1808 2422 394 183 98 N ATOM 913 CA CYS B 125 36.619 2.409 -6.250 1.00 17.94 C ANISOU 913 CA CYS B 125 2655 1821 2341 400 145 195 C ATOM 914 C CYS B 125 36.723 1.388 -5.124 1.00 18.75 C ANISOU 914 C CYS B 125 2802 1836 2488 411 120 292 C ATOM 915 O CYS B 125 37.740 1.333 -4.431 1.00 19.29 O ANISOU 915 O CYS B 125 2845 1916 2567 464 79 372 O ATOM 916 CB CYS B 125 35.700 3.555 -5.828 1.00 17.06 C ANISOU 916 CB CYS B 125 2538 1797 2149 322 143 197 C ATOM 917 SG CYS B 125 36.301 4.485 -4.400 1.00 17.38 S ANISOU 917 SG CYS B 125 2563 1920 2119 310 106 285 S ATOM 918 N ARG B 126 35.666 0.591 -4.958 1.00 18.86 N ANISOU 918 N ARG B 126 2875 1765 2525 354 140 293 N ATOM 919 CA ARG B 126 35.614 -0.472 -3.956 1.00 19.87 C ANISOU 919 CA ARG B 126 3062 1793 2696 349 123 393 C ATOM 920 C ARG B 126 36.707 -1.509 -4.170 1.00 21.00 C ANISOU 920 C ARG B 126 3207 1827 2947 455 111 422 C ATOM 921 O ARG B 126 37.402 -1.884 -3.228 1.00 21.80 O ANISOU 921 O ARG B 126 3312 1901 3068 498 63 540 O ATOM 922 CB ARG B 126 34.249 -1.153 -3.970 1.00 20.20 C ANISOU 922 CB ARG B 126 3162 1756 2757 258 160 371 C ATOM 923 CG ARG B 126 33.161 -0.392 -3.256 1.00 19.62 C ANISOU 923 CG ARG B 126 3088 1767 2599 158 175 390 C ATOM 924 CD ARG B 126 31.807 -0.917 -3.663 1.00 19.88 C ANISOU 924 CD ARG B 126 3142 1745 2668 69 216 336 C ATOM 925 NE ARG B 126 30.761 -0.507 -2.732 1.00 20.02 N ANISOU 925 NE ARG B 126 3161 1815 2631 -25 246 377 N ATOM 926 CZ ARG B 126 29.464 -0.748 -2.901 1.00 20.17 C ANISOU 926 CZ ARG B 126 3171 1817 2674 -116 284 341 C ATOM 927 NH1 ARG B 126 29.028 -1.398 -3.973 1.00 20.40 N ANISOU 927 NH1 ARG B 126 3199 1779 2773 -138 284 262 N ATOM 928 NH2 ARG B 126 28.598 -0.329 -1.994 1.00 20.65 N ANISOU 928 NH2 ARG B 126 3223 1933 2691 -194 327 379 N ATOM 929 N ASP B 127 36.857 -1.960 -5.411 1.00 21.24 N ANISOU 929 N ASP B 127 3232 1794 3043 496 154 314 N ATOM 930 CA ASP B 127 37.890 -2.928 -5.757 1.00 22.63 C ANISOU 930 CA ASP B 127 3402 1856 3340 608 166 316 C ATOM 931 C ASP B 127 39.304 -2.419 -5.464 1.00 22.86 C ANISOU 931 C ASP B 127 3341 1963 3382 707 127 377 C ATOM 932 O ASP B 127 40.116 -3.141 -4.892 1.00 24.29 O ANISOU 932 O ASP B 127 3509 2068 3654 792 93 473 O ATOM 933 CB ASP B 127 37.775 -3.343 -7.226 1.00 22.83 C ANISOU 933 CB ASP B 127 3443 1822 3410 621 237 160 C ATOM 934 CG ASP B 127 38.757 -4.446 -7.602 1.00 24.47 C ANISOU 934 CG ASP B 127 3652 1885 3761 740 274 143 C ATOM 935 OD1 ASP B 127 38.575 -5.595 -7.142 1.00 25.82 O ANISOU 935 OD1 ASP B 127 3888 1892 4029 754 274 196 O ATOM 936 OD2 ASP B 127 39.706 -4.161 -8.364 1.00 24.39 O ANISOU 936 OD2 ASP B 127 3577 1919 3773 820 311 77 O ATOM 937 N ILE B 128 39.593 -1.180 -5.846 1.00 21.98 N ANISOU 937 N ILE B 128 3163 2001 3186 693 127 330 N ATOM 938 CA ILE B 128 40.943 -0.646 -5.708 1.00 22.44 C ANISOU 938 CA ILE B 128 3123 2142 3261 773 95 372 C ATOM 939 C ILE B 128 41.298 -0.275 -4.260 1.00 22.94 C ANISOU 939 C ILE B 128 3168 2271 3276 756 2 517 C ATOM 940 O ILE B 128 42.385 -0.614 -3.787 1.00 24.13 O ANISOU 940 O ILE B 128 3258 2413 3496 839 -50 605 O ATOM 941 CB ILE B 128 41.211 0.515 -6.706 1.00 21.34 C ANISOU 941 CB ILE B 128 2924 2129 3057 757 135 271 C ATOM 942 CG1 ILE B 128 41.228 -0.029 -8.139 1.00 21.76 C ANISOU 942 CG1 ILE B 128 2989 2118 3161 793 223 138 C ATOM 943 CG2 ILE B 128 42.539 1.196 -6.409 1.00 21.84 C ANISOU 943 CG2 ILE B 128 2877 2293 3128 812 97 324 C ATOM 944 CD1 ILE B 128 41.332 1.016 -9.233 1.00 20.97 C ANISOU 944 CD1 ILE B 128 2853 2134 2980 763 268 42 C ATOM 945 N LEU B 129 40.384 0.389 -3.555 1.00 22.43 N ANISOU 945 N LEU B 129 3155 2272 3096 649 -18 540 N ATOM 946 CA LEU B 129 40.649 0.832 -2.184 1.00 23.00 C ANISOU 946 CA LEU B 129 3229 2421 3089 611 -98 660 C ATOM 947 C LEU B 129 40.536 -0.286 -1.156 1.00 24.71 C ANISOU 947 C LEU B 129 3511 2539 3338 617 -146 792 C ATOM 948 O LEU B 129 41.003 -0.143 -0.022 1.00 25.52 O ANISOU 948 O LEU B 129 3614 2699 3384 602 -229 911 O ATOM 949 CB LEU B 129 39.738 1.998 -1.782 1.00 21.80 C ANISOU 949 CB LEU B 129 3110 2372 2800 495 -85 625 C ATOM 950 CG LEU B 129 39.793 3.332 -2.542 1.00 20.89 C ANISOU 950 CG LEU B 129 2940 2362 2633 471 -52 524 C ATOM 951 CD1 LEU B 129 39.125 4.423 -1.715 1.00 19.52 C ANISOU 951 CD1 LEU B 129 2801 2276 2338 371 -56 527 C ATOM 952 CD2 LEU B 129 41.215 3.746 -2.914 1.00 20.78 C ANISOU 952 CD2 LEU B 129 2828 2412 2656 540 -83 526 C ATOM 953 N GLY B 130 39.908 -1.391 -1.550 1.00 25.65 N ANISOU 953 N GLY B 130 3693 2512 3542 629 -98 772 N ATOM 954 CA GLY B 130 39.760 -2.559 -0.683 1.00 27.52 C ANISOU 954 CA GLY B 130 4004 2627 3828 635 -134 902 C ATOM 955 C GLY B 130 38.999 -2.275 0.598 1.00 27.82 C ANISOU 955 C GLY B 130 4117 2722 3730 517 -164 995 C ATOM 956 O GLY B 130 37.886 -1.748 0.561 1.00 26.82 O ANISOU 956 O GLY B 130 4028 2640 3520 415 -106 924 O ATOM 957 N ASP B 131 39.617 -2.614 1.729 1.00 29.44 N ANISOU 957 N ASP B 131 4340 2933 3912 532 -254 1156 N ATOM 958 CA ASP B 131 39.004 -2.458 3.054 1.00 30.20 C ANISOU 958 CA ASP B 131 4524 3086 3863 416 -284 1261 C ATOM 959 C ASP B 131 38.740 -1.001 3.433 1.00 29.18 C ANISOU 959 C ASP B 131 4381 3136 3569 322 -275 1196 C ATOM 960 O ASP B 131 37.921 -0.720 4.312 1.00 29.56 O ANISOU 960 O ASP B 131 4507 3234 3490 208 -251 1224 O ATOM 961 CB ASP B 131 39.871 -3.133 4.122 1.00 32.07 C ANISOU 961 CB ASP B 131 4782 3299 4104 458 -402 1459 C ATOM 962 CG ASP B 131 39.867 -4.654 4.007 1.00 34.27 C ANISOU 962 CG ASP B 131 5110 3371 4539 529 -402 1549 C ATOM 963 OD1 ASP B 131 40.812 -5.297 4.521 1.00 36.65 O ANISOU 963 OD1 ASP B 131 5394 3624 4908 615 -502 1703 O ATOM 964 OD2 ASP B 131 38.918 -5.211 3.409 1.00 34.14 O ANISOU 964 OD2 ASP B 131 5150 3237 4586 497 -305 1468 O ATOM 965 N LYS B 132 39.434 -0.083 2.762 1.00 28.16 N ANISOU 965 N LYS B 132 4155 3096 3449 369 -283 1106 N ATOM 966 CA LYS B 132 39.278 1.350 2.983 1.00 26.84 C ANISOU 966 CA LYS B 132 3970 3078 3150 291 -270 1032 C ATOM 967 C LYS B 132 37.986 1.888 2.345 1.00 25.56 C ANISOU 967 C LYS B 132 3829 2914 2970 228 -157 897 C ATOM 968 O LYS B 132 37.506 2.961 2.716 1.00 25.10 O ANISOU 968 O LYS B 132 3783 2951 2804 148 -125 845 O ATOM 969 CB LYS B 132 40.516 2.087 2.446 1.00 26.41 C ANISOU 969 CB LYS B 132 3801 3105 3128 359 -319 995 C ATOM 970 CG LYS B 132 40.455 3.616 2.455 1.00 24.99 C ANISOU 970 CG LYS B 132 3597 3058 2841 287 -299 902 C ATOM 971 CD LYS B 132 40.646 4.202 3.844 1.00 25.28 C ANISOU 971 CD LYS B 132 3681 3200 2723 193 -366 973 C ATOM 972 CE LYS B 132 42.108 4.275 4.227 1.00 25.62 C ANISOU 972 CE LYS B 132 3648 3316 2772 233 -492 1060 C ATOM 973 NZ LYS B 132 42.282 4.966 5.524 1.00 25.41 N ANISOU 973 NZ LYS B 132 3675 3408 2572 120 -562 1109 N ATOM 974 N ALA B 133 37.428 1.138 1.395 1.00 25.20 N ANISOU 974 N ALA B 133 3784 2757 3033 262 -99 841 N ATOM 975 CA ALA B 133 36.243 1.571 0.644 1.00 23.85 C ANISOU 975 CA ALA B 133 3614 2587 2863 210 -10 719 C ATOM 976 C ALA B 133 35.003 1.763 1.517 1.00 23.80 C ANISOU 976 C ALA B 133 3671 2603 2768 96 43 733 C ATOM 977 O ALA B 133 34.224 2.688 1.297 1.00 22.95 O ANISOU 977 O ALA B 133 3543 2557 2622 47 100 647 O ATOM 978 CB ALA B 133 35.946 0.597 -0.486 1.00 23.89 C ANISOU 978 CB ALA B 133 3617 2469 2993 256 27 662 C ATOM 979 N ALA B 134 34.827 0.888 2.505 1.00 24.74 N ANISOU 979 N ALA B 134 3866 2669 2863 56 28 847 N ATOM 980 CA ALA B 134 33.659 0.938 3.381 1.00 24.85 C ANISOU 980 CA ALA B 134 3945 2703 2794 -60 94 867 C ATOM 981 C ALA B 134 33.710 2.110 4.370 1.00 24.59 C ANISOU 981 C ALA B 134 3930 2807 2608 -126 99 867 C ATOM 982 O ALA B 134 32.696 2.458 4.983 1.00 24.78 O ANISOU 982 O ALA B 134 3990 2868 2557 -220 181 845 O ATOM 983 CB ALA B 134 33.500 -0.381 4.120 1.00 26.29 C ANISOU 983 CB ALA B 134 4215 2784 2991 -92 80 999 C ATOM 984 N ALA B 135 34.891 2.706 4.517 1.00 24.13 N ANISOU 984 N ALA B 135 3842 2820 2507 -80 19 883 N ATOM 985 CA ALA B 135 35.102 3.817 5.437 1.00 23.94 C ANISOU 985 CA ALA B 135 3842 2921 2334 -147 12 874 C ATOM 986 C ALA B 135 34.730 5.147 4.785 1.00 22.61 C ANISOU 986 C ALA B 135 3613 2808 2168 -151 77 729 C ATOM 987 O ALA B 135 33.992 5.948 5.366 1.00 22.85 O ANISOU 987 O ALA B 135 3675 2893 2112 -229 153 675 O ATOM 988 CB ALA B 135 36.548 3.833 5.920 1.00 24.45 C ANISOU 988 CB ALA B 135 3896 3039 2355 -111 -117 964 C ATOM 989 N VAL B 136 35.237 5.365 3.573 1.00 21.48 N ANISOU 989 N VAL B 136 3387 2646 2129 -64 54 670 N ATOM 990 CA VAL B 136 34.976 6.582 2.796 1.00 20.11 C ANISOU 990 CA VAL B 136 3155 2513 1973 -56 102 551 C ATOM 991 C VAL B 136 33.549 6.650 2.240 1.00 19.70 C ANISOU 991 C VAL B 136 3089 2421 1975 -78 199 477 C ATOM 992 O VAL B 136 32.801 5.670 2.281 1.00 20.06 O ANISOU 992 O VAL B 136 3160 2403 2060 -99 229 508 O ATOM 993 CB VAL B 136 35.984 6.735 1.624 1.00 19.36 C ANISOU 993 CB VAL B 136 2980 2414 1963 36 51 521 C ATOM 994 CG1 VAL B 136 37.410 6.823 2.153 1.00 19.70 C ANISOU 994 CG1 VAL B 136 3007 2512 1966 56 -45 588 C ATOM 995 CG2 VAL B 136 35.841 5.588 0.621 1.00 18.52 C ANISOU 995 CG2 VAL B 136 2851 2211 1973 102 54 522 C ATOM 996 N SER B 137 33.183 7.819 1.723 1.00 19.10 N ANISOU 996 N SER B 137 2969 2381 1909 -77 243 387 N ATOM 997 CA SER B 137 31.918 7.985 1.013 1.00 18.76 C ANISOU 997 CA SER B 137 2884 2308 1937 -82 314 322 C ATOM 998 C SER B 137 32.185 8.222 -0.466 1.00 18.04 C ANISOU 998 C SER B 137 2724 2203 1927 -12 282 273 C ATOM 999 O SER B 137 33.152 8.892 -0.838 1.00 17.66 O ANISOU 999 O SER B 137 2655 2189 1867 25 243 259 O ATOM 1000 CB SER B 137 31.098 9.131 1.601 1.00 18.86 C ANISOU 1000 CB SER B 137 2895 2362 1907 -132 399 265 C ATOM 1001 OG SER B 137 30.661 8.824 2.915 1.00 19.99 O ANISOU 1001 OG SER B 137 3108 2521 1968 -210 451 300 O ATOM 1002 N MET B 138 31.328 7.656 -1.305 1.00 18.09 N ANISOU 1002 N MET B 138 2700 2164 2009 -7 300 248 N ATOM 1003 CA MET B 138 31.500 7.745 -2.746 1.00 17.62 C ANISOU 1003 CA MET B 138 2590 2095 2008 45 269 203 C ATOM 1004 C MET B 138 30.343 8.514 -3.375 1.00 17.52 C ANISOU 1004 C MET B 138 2521 2101 2034 31 303 150 C ATOM 1005 O MET B 138 29.190 8.091 -3.292 1.00 18.07 O ANISOU 1005 O MET B 138 2573 2150 2143 -10 337 144 O ATOM 1006 CB MET B 138 31.628 6.343 -3.339 1.00 17.91 C ANISOU 1006 CB MET B 138 2645 2063 2098 63 241 214 C ATOM 1007 CG MET B 138 32.804 5.561 -2.775 1.00 18.16 C ANISOU 1007 CG MET B 138 2719 2064 2117 97 202 277 C ATOM 1008 SD MET B 138 32.849 3.849 -3.314 1.00 19.18 S ANISOU 1008 SD MET B 138 2881 2077 2330 120 188 289 S ATOM 1009 CE MET B 138 31.614 3.097 -2.249 1.00 20.28 C ANISOU 1009 CE MET B 138 3072 2165 2468 29 230 341 C ATOM 1010 N MET B 139 30.659 9.651 -3.991 1.00 17.15 N ANISOU 1010 N MET B 139 2441 2092 1984 64 292 122 N ATOM 1011 CA MET B 139 29.648 10.540 -4.563 1.00 17.30 C ANISOU 1011 CA MET B 139 2401 2126 2048 64 314 89 C ATOM 1012 C MET B 139 29.716 10.525 -6.086 1.00 17.29 C ANISOU 1012 C MET B 139 2366 2131 2072 95 260 71 C ATOM 1013 O MET B 139 30.778 10.755 -6.664 1.00 17.15 O ANISOU 1013 O MET B 139 2362 2129 2024 128 229 70 O ATOM 1014 CB MET B 139 29.854 11.966 -4.045 1.00 17.22 C ANISOU 1014 CB MET B 139 2389 2140 2014 71 347 77 C ATOM 1015 CG MET B 139 28.610 12.832 -4.037 1.00 17.26 C ANISOU 1015 CG MET B 139 2338 2141 2081 70 400 54 C ATOM 1016 SD MET B 139 28.953 14.412 -3.251 1.00 17.42 S ANISOU 1016 SD MET B 139 2381 2162 2077 73 456 26 S ATOM 1017 CE MET B 139 27.336 15.176 -3.260 1.00 18.33 C ANISOU 1017 CE MET B 139 2413 2252 2299 90 531 0 C ATOM 1018 N SER B 140 28.585 10.267 -6.732 1.00 17.79 N ANISOU 1018 N SER B 140 2382 2190 2186 76 251 58 N ATOM 1019 CA SER B 140 28.553 10.154 -8.186 1.00 18.21 C ANISOU 1019 CA SER B 140 2415 2260 2243 88 192 40 C ATOM 1020 C SER B 140 27.659 11.205 -8.833 1.00 18.69 C ANISOU 1020 C SER B 140 2406 2353 2342 97 172 47 C ATOM 1021 O SER B 140 26.443 11.198 -8.625 1.00 19.48 O ANISOU 1021 O SER B 140 2445 2453 2504 73 184 50 O ATOM 1022 CB SER B 140 28.105 8.750 -8.600 1.00 18.79 C ANISOU 1022 CB SER B 140 2502 2302 2336 48 171 18 C ATOM 1023 OG SER B 140 29.114 7.792 -8.315 1.00 18.97 O ANISOU 1023 OG SER B 140 2592 2282 2335 60 177 16 O ATOM 1024 N PHE B 141 28.264 12.100 -9.613 1.00 18.53 N ANISOU 1024 N PHE B 141 2388 2359 2291 131 142 58 N ATOM 1025 CA PHE B 141 27.527 13.156 -10.314 1.00 19.02 C ANISOU 1025 CA PHE B 141 2390 2444 2391 148 110 85 C ATOM 1026 C PHE B 141 27.191 12.743 -11.736 1.00 19.52 C ANISOU 1026 C PHE B 141 2440 2546 2429 128 29 86 C ATOM 1027 O PHE B 141 28.033 12.171 -12.434 1.00 19.58 O ANISOU 1027 O PHE B 141 2506 2569 2365 119 9 61 O ATOM 1028 CB PHE B 141 28.328 14.459 -10.332 1.00 18.81 C ANISOU 1028 CB PHE B 141 2384 2417 2345 186 124 109 C ATOM 1029 CG PHE B 141 28.219 15.259 -9.064 1.00 19.06 C ANISOU 1029 CG PHE B 141 2412 2413 2418 199 197 105 C ATOM 1030 CD1 PHE B 141 29.046 14.986 -7.978 1.00 18.46 C ANISOU 1030 CD1 PHE B 141 2391 2325 2297 183 244 83 C ATOM 1031 CD2 PHE B 141 27.288 16.297 -8.960 1.00 19.83 C ANISOU 1031 CD2 PHE B 141 2449 2486 2598 227 218 124 C ATOM 1032 CE1 PHE B 141 28.945 15.733 -6.800 1.00 19.31 C ANISOU 1032 CE1 PHE B 141 2510 2407 2421 180 313 67 C ATOM 1033 CE2 PHE B 141 27.174 17.049 -7.784 1.00 20.03 C ANISOU 1033 CE2 PHE B 141 2481 2471 2659 235 303 101 C ATOM 1034 CZ PHE B 141 28.003 16.768 -6.703 1.00 19.66 C ANISOU 1034 CZ PHE B 141 2504 2420 2544 204 351 67 C ATOM 1035 N GLU B 142 25.964 13.051 -12.160 1.00 20.25 N ANISOU 1035 N GLU B 142 2454 2660 2580 120 -15 112 N ATOM 1036 CA GLU B 142 25.427 12.612 -13.464 1.00 20.84 C ANISOU 1036 CA GLU B 142 2509 2784 2626 82 -109 114 C ATOM 1037 C GLU B 142 26.263 13.032 -14.685 1.00 20.67 C ANISOU 1037 C GLU B 142 2545 2805 2505 88 -160 130 C ATOM 1038 O GLU B 142 26.566 12.210 -15.549 1.00 20.97 O ANISOU 1038 O GLU B 142 2634 2872 2461 45 -196 89 O ATOM 1039 CB GLU B 142 23.955 13.030 -13.624 1.00 21.69 C ANISOU 1039 CB GLU B 142 2498 2915 2828 78 -159 157 C ATOM 1040 CG GLU B 142 23.645 14.501 -13.298 1.00 22.25 C ANISOU 1040 CG GLU B 142 2507 2968 2980 149 -139 219 C ATOM 1041 CD GLU B 142 22.169 14.872 -13.484 1.00 23.38 C ANISOU 1041 CD GLU B 142 2511 3132 3241 159 -190 267 C ATOM 1042 OE1 GLU B 142 21.396 14.061 -14.042 1.00 24.37 O ANISOU 1042 OE1 GLU B 142 2584 3305 3371 99 -264 260 O ATOM 1043 OE2 GLU B 142 21.782 15.985 -13.069 1.00 23.66 O ANISOU 1043 OE2 GLU B 142 2483 3133 3374 226 -154 310 O ATOM 1044 N THR B 143 26.634 14.310 -14.735 1.00 20.33 N ANISOU 1044 N THR B 143 2499 2759 2466 136 -153 186 N ATOM 1045 CA THR B 143 27.447 14.869 -15.813 1.00 20.21 C ANISOU 1045 CA THR B 143 2539 2783 2357 137 -187 216 C ATOM 1046 C THR B 143 28.328 15.992 -15.251 1.00 19.48 C ANISOU 1046 C THR B 143 2470 2651 2281 182 -125 247 C ATOM 1047 O THR B 143 28.353 16.211 -14.043 1.00 18.96 O ANISOU 1047 O THR B 143 2389 2533 2282 207 -59 230 O ATOM 1048 CB THR B 143 26.562 15.351 -17.009 1.00 21.23 C ANISOU 1048 CB THR B 143 2627 2969 2471 121 -297 285 C ATOM 1049 OG1 THR B 143 27.389 15.718 -18.119 1.00 22.12 O ANISOU 1049 OG1 THR B 143 2812 3129 2464 104 -325 312 O ATOM 1050 CG2 THR B 143 25.687 16.530 -16.632 1.00 21.55 C ANISOU 1050 CG2 THR B 143 2580 2977 2633 176 -314 367 C ATOM 1051 N LEU B 144 29.056 16.692 -16.114 1.00 19.63 N ANISOU 1051 N LEU B 144 2532 2697 2230 181 -142 288 N ATOM 1052 CA LEU B 144 29.864 17.824 -15.672 1.00 19.26 C ANISOU 1052 CA LEU B 144 2507 2610 2203 209 -89 320 C ATOM 1053 C LEU B 144 28.984 19.066 -15.495 1.00 19.80 C ANISOU 1053 C LEU B 144 2523 2627 2373 250 -109 395 C ATOM 1054 O LEU B 144 28.194 19.396 -16.382 1.00 20.65 O ANISOU 1054 O LEU B 144 2599 2760 2488 255 -190 464 O ATOM 1055 CB LEU B 144 31.000 18.097 -16.662 1.00 19.39 C ANISOU 1055 CB LEU B 144 2587 2670 2111 183 -89 340 C ATOM 1056 CG LEU B 144 32.124 19.048 -16.239 1.00 19.35 C ANISOU 1056 CG LEU B 144 2610 2631 2111 189 -26 357 C ATOM 1057 CD1 LEU B 144 33.077 18.390 -15.244 1.00 18.14 C ANISOU 1057 CD1 LEU B 144 2465 2468 1958 187 42 281 C ATOM 1058 CD2 LEU B 144 32.882 19.527 -17.459 1.00 20.09 C ANISOU 1058 CD2 LEU B 144 2752 2774 2108 156 -36 406 C ATOM 1059 N PRO B 145 29.098 19.742 -14.334 1.00 19.53 N ANISOU 1059 N PRO B 145 2481 2520 2420 280 -36 379 N ATOM 1060 CA PRO B 145 28.339 20.965 -14.025 1.00 20.08 C ANISOU 1060 CA PRO B 145 2505 2516 2607 329 -27 432 C ATOM 1061 C PRO B 145 28.343 22.028 -15.130 1.00 20.89 C ANISOU 1061 C PRO B 145 2620 2609 2710 345 -89 538 C ATOM 1062 O PRO B 145 27.338 22.722 -15.324 1.00 21.84 O ANISOU 1062 O PRO B 145 2677 2688 2931 394 -127 608 O ATOM 1063 CB PRO B 145 29.026 21.508 -12.761 1.00 19.64 C ANISOU 1063 CB PRO B 145 2487 2393 2583 331 72 378 C ATOM 1064 CG PRO B 145 30.189 20.596 -12.478 1.00 18.56 C ANISOU 1064 CG PRO B 145 2404 2306 2341 285 97 316 C ATOM 1065 CD PRO B 145 29.944 19.327 -13.199 1.00 18.69 C ANISOU 1065 CD PRO B 145 2409 2396 2297 266 42 305 C ATOM 1066 N TRP B 146 29.454 22.145 -15.851 1.00 20.71 N ANISOU 1066 N TRP B 146 2669 2622 2577 304 -95 558 N ATOM 1067 CA TRP B 146 29.609 23.208 -16.844 1.00 21.61 C ANISOU 1067 CA TRP B 146 2814 2723 2676 305 -141 668 C ATOM 1068 C TRP B 146 29.854 22.659 -18.236 1.00 22.19 C ANISOU 1068 C TRP B 146 2925 2903 2604 255 -216 708 C ATOM 1069 O TRP B 146 30.270 21.511 -18.401 1.00 21.70 O ANISOU 1069 O TRP B 146 2883 2915 2447 215 -206 630 O ATOM 1070 CB TRP B 146 30.775 24.131 -16.473 1.00 21.12 C ANISOU 1070 CB TRP B 146 2813 2598 2612 286 -66 668 C ATOM 1071 CG TRP B 146 30.978 24.288 -15.005 1.00 20.37 C ANISOU 1071 CG TRP B 146 2712 2432 2597 298 24 580 C ATOM 1072 CD1 TRP B 146 30.359 25.184 -14.184 1.00 20.69 C ANISOU 1072 CD1 TRP B 146 2729 2363 2770 345 67 579 C ATOM 1073 CD2 TRP B 146 31.850 23.515 -14.173 1.00 18.83 C ANISOU 1073 CD2 TRP B 146 2537 2271 2347 262 82 480 C ATOM 1074 NE1 TRP B 146 30.797 25.022 -12.893 1.00 20.02 N ANISOU 1074 NE1 TRP B 146 2660 2250 2695 327 149 477 N ATOM 1075 CE2 TRP B 146 31.712 24.004 -12.857 1.00 18.74 C ANISOU 1075 CE2 TRP B 146 2522 2178 2420 276 150 425 C ATOM 1076 CE3 TRP B 146 32.734 22.456 -14.413 1.00 17.98 C ANISOU 1076 CE3 TRP B 146 2449 2252 2132 222 83 434 C ATOM 1077 CZ2 TRP B 146 32.429 23.476 -11.783 1.00 18.21 C ANISOU 1077 CZ2 TRP B 146 2474 2128 2316 243 202 338 C ATOM 1078 CZ3 TRP B 146 33.446 21.931 -13.351 1.00 17.53 C ANISOU 1078 CZ3 TRP B 146 2398 2200 2062 204 135 354 C ATOM 1079 CH2 TRP B 146 33.290 22.443 -12.049 1.00 18.00 C ANISOU 1079 CH2 TRP B 146 2457 2189 2191 210 186 313 C ATOM 1080 N ALA B 147 29.571 23.492 -19.231 1.00 23.49 N ANISOU 1080 N ALA B 147 3103 3069 2753 256 -288 830 N ATOM 1081 CA ALA B 147 30.118 23.319 -20.562 1.00 24.28 C ANISOU 1081 CA ALA B 147 3272 3264 2690 192 -335 879 C ATOM 1082 C ALA B 147 31.330 24.242 -20.592 1.00 24.50 C ANISOU 1082 C ALA B 147 3368 3249 2693 166 -260 913 C ATOM 1083 O ALA B 147 31.187 25.468 -20.542 1.00 25.44 O ANISOU 1083 O ALA B 147 3492 3276 2897 194 -265 1009 O ATOM 1084 CB ALA B 147 29.099 23.710 -21.621 1.00 25.36 C ANISOU 1084 CB ALA B 147 3389 3437 2812 199 -468 1011 C ATOM 1085 N CYS B 148 32.522 23.655 -20.633 1.00 24.03 N ANISOU 1085 N CYS B 148 3353 3245 2531 113 -186 832 N ATOM 1086 CA CYS B 148 33.755 24.436 -20.512 1.00 24.28 C ANISOU 1086 CA CYS B 148 3430 3242 2551 78 -104 846 C ATOM 1087 C CYS B 148 34.871 24.045 -21.485 1.00 24.82 C ANISOU 1087 C CYS B 148 3556 3415 2458 3 -63 836 C ATOM 1088 O CYS B 148 34.933 22.910 -21.962 1.00 24.83 O ANISOU 1088 O CYS B 148 3565 3509 2360 -17 -67 766 O ATOM 1089 CB CYS B 148 34.270 24.398 -19.069 1.00 23.10 C ANISOU 1089 CB CYS B 148 3250 3026 2500 98 -20 747 C ATOM 1090 SG CYS B 148 34.457 22.743 -18.382 1.00 21.74 S ANISOU 1090 SG CYS B 148 3041 2919 2299 107 10 601 S ATOM 1091 N ARG B 149 35.743 25.007 -21.776 1.00 25.55 N ANISOU 1091 N ARG B 149 3691 3484 2532 -43 -15 901 N ATOM 1092 CA ARG B 149 36.915 24.769 -22.606 1.00 26.25 C ANISOU 1092 CA ARG B 149 3824 3667 2481 -118 51 890 C ATOM 1093 C ARG B 149 38.110 25.599 -22.127 1.00 26.26 C ANISOU 1093 C ARG B 149 3826 3620 2532 -160 143 895 C ATOM 1094 O ARG B 149 37.966 26.775 -21.790 1.00 26.51 O ANISOU 1094 O ARG B 149 3872 3546 2657 -159 135 974 O ATOM 1095 CB ARG B 149 36.605 25.052 -24.083 1.00 27.72 C ANISOU 1095 CB ARG B 149 4082 3925 2526 -169 -8 1004 C ATOM 1096 CG ARG B 149 37.624 24.474 -25.045 1.00 28.80 C ANISOU 1096 CG ARG B 149 4267 4187 2489 -247 68 963 C ATOM 1097 CD ARG B 149 36.949 23.657 -26.137 1.00 31.36 C ANISOU 1097 CD ARG B 149 4638 4620 2658 -273 -2 958 C ATOM 1098 NE ARG B 149 36.544 24.471 -27.285 1.00 34.18 N ANISOU 1098 NE ARG B 149 5072 5012 2903 -327 -78 1118 N ATOM 1099 CZ ARG B 149 35.519 24.191 -28.089 1.00 35.05 C ANISOU 1099 CZ ARG B 149 5215 5185 2917 -339 -201 1172 C ATOM 1100 NH1 ARG B 149 34.764 23.118 -27.868 1.00 34.51 N ANISOU 1100 NH1 ARG B 149 5107 5146 2859 -306 -257 1070 N ATOM 1101 NH2 ARG B 149 35.241 24.993 -29.112 1.00 36.33 N ANISOU 1101 NH2 ARG B 149 5450 5381 2972 -392 -277 1336 N ATOM 1102 N ILE B 150 39.280 24.964 -22.082 1.00 26.04 N ANISOU 1102 N ILE B 150 3778 3665 2452 -197 231 808 N ATOM 1103 CA ILE B 150 40.539 25.646 -21.807 1.00 26.37 C ANISOU 1103 CA ILE B 150 3807 3691 2520 -257 317 812 C ATOM 1104 C ILE B 150 40.848 26.595 -22.961 1.00 28.18 C ANISOU 1104 C ILE B 150 4107 3937 2663 -336 334 940 C ATOM 1105 O ILE B 150 40.674 26.235 -24.130 1.00 29.07 O ANISOU 1105 O ILE B 150 4270 4140 2635 -363 322 977 O ATOM 1106 CB ILE B 150 41.695 24.635 -21.653 1.00 25.87 C ANISOU 1106 CB ILE B 150 3686 3720 2421 -270 403 698 C ATOM 1107 CG1 ILE B 150 41.479 23.754 -20.417 1.00 24.51 C ANISOU 1107 CG1 ILE B 150 3450 3521 2340 -197 383 591 C ATOM 1108 CG2 ILE B 150 43.038 25.350 -21.586 1.00 26.23 C ANISOU 1108 CG2 ILE B 150 3706 3776 2484 -348 490 715 C ATOM 1109 CD1 ILE B 150 42.252 22.447 -20.435 1.00 23.93 C ANISOU 1109 CD1 ILE B 150 3325 3535 2232 -178 441 486 C ATOM 1110 N LYS B 151 41.289 27.806 -22.633 1.00 28.90 N ANISOU 1110 N LYS B 151 4211 3938 2833 -381 361 1007 N ATOM 1111 CA LYS B 151 41.690 28.765 -23.653 1.00 30.76 C ANISOU 1111 CA LYS B 151 4516 4175 2994 -468 388 1139 C ATOM 1112 C LYS B 151 43.206 28.937 -23.671 1.00 31.19 C ANISOU 1112 C LYS B 151 4539 4282 3029 -563 507 1106 C ATOM 1113 O LYS B 151 43.816 29.135 -24.726 1.00 32.45 O ANISOU 1113 O LYS B 151 4740 4519 3070 -647 567 1170 O ATOM 1114 CB LYS B 151 40.973 30.105 -23.456 1.00 31.63 C ANISOU 1114 CB LYS B 151 4677 4127 3214 -456 328 1264 C ATOM 1115 CG LYS B 151 39.501 30.060 -23.883 1.00 32.95 C ANISOU 1115 CG LYS B 151 4874 4268 3377 -376 207 1344 C ATOM 1116 CD LYS B 151 39.101 31.260 -24.750 1.00 35.84 C ANISOU 1116 CD LYS B 151 5325 4561 3733 -406 156 1539 C ATOM 1117 CE LYS B 151 38.588 32.432 -23.913 1.00 36.62 C ANISOU 1117 CE LYS B 151 5424 4456 4032 -356 134 1594 C ATOM 1118 NZ LYS B 151 37.809 33.399 -24.741 1.00 38.29 N ANISOU 1118 NZ LYS B 151 5705 4585 4259 -341 48 1794 N ATOM 1119 N GLU B 152 43.801 28.845 -22.488 1.00 30.27 N ANISOU 1119 N GLU B 152 4345 4132 3026 -555 541 1008 N ATOM 1120 CA GLU B 152 45.236 28.957 -22.305 1.00 30.54 C ANISOU 1120 CA GLU B 152 4317 4218 3071 -639 640 967 C ATOM 1121 C GLU B 152 45.584 27.966 -21.198 1.00 28.96 C ANISOU 1121 C GLU B 152 4013 4052 2938 -579 642 824 C ATOM 1122 O GLU B 152 45.203 28.160 -20.040 1.00 27.92 O ANISOU 1122 O GLU B 152 3864 3831 2913 -541 591 784 O ATOM 1123 CB GLU B 152 45.587 30.394 -21.913 1.00 31.25 C ANISOU 1123 CB GLU B 152 4434 4185 3256 -721 654 1040 C ATOM 1124 CG GLU B 152 47.056 30.779 -21.997 1.00 32.63 C ANISOU 1124 CG GLU B 152 4553 4411 3431 -843 757 1036 C ATOM 1125 CD GLU B 152 47.251 32.294 -21.918 1.00 34.02 C ANISOU 1125 CD GLU B 152 4791 4453 3682 -943 769 1136 C ATOM 1126 OE1 GLU B 152 47.236 32.951 -22.983 1.00 35.90 O ANISOU 1126 OE1 GLU B 152 5111 4682 3849 -1008 795 1266 O ATOM 1127 OE2 GLU B 152 47.411 32.832 -20.796 1.00 34.03 O ANISOU 1127 OE2 GLU B 152 4769 4355 3808 -963 752 1085 O ATOM 1128 N PHE B 153 46.273 26.885 -21.569 1.00 28.73 N ANISOU 1128 N PHE B 153 3922 4150 2844 -569 702 750 N ATOM 1129 CA PHE B 153 46.596 25.809 -20.631 1.00 27.38 C ANISOU 1129 CA PHE B 153 3655 4015 2734 -500 698 631 C ATOM 1130 C PHE B 153 47.272 26.343 -19.383 1.00 26.89 C ANISOU 1130 C PHE B 153 3523 3904 2790 -536 690 604 C ATOM 1131 O PHE B 153 48.117 27.235 -19.455 1.00 27.78 O ANISOU 1131 O PHE B 153 3616 4013 2926 -636 738 645 O ATOM 1132 CB PHE B 153 47.471 24.731 -21.285 1.00 27.92 C ANISOU 1132 CB PHE B 153 3657 4214 2737 -492 787 564 C ATOM 1133 CG PHE B 153 47.958 23.666 -20.319 1.00 27.17 C ANISOU 1133 CG PHE B 153 3453 4146 2724 -420 784 460 C ATOM 1134 CD1 PHE B 153 49.281 23.659 -19.878 1.00 27.05 C ANISOU 1134 CD1 PHE B 153 3315 4184 2777 -456 841 431 C ATOM 1135 CD2 PHE B 153 47.091 22.681 -19.846 1.00 26.06 C ANISOU 1135 CD2 PHE B 153 3327 3978 2598 -320 718 402 C ATOM 1136 CE1 PHE B 153 49.734 22.687 -18.991 1.00 26.46 C ANISOU 1136 CE1 PHE B 153 3136 4134 2782 -384 823 355 C ATOM 1137 CE2 PHE B 153 47.537 21.701 -18.957 1.00 25.57 C ANISOU 1137 CE2 PHE B 153 3173 3932 2612 -254 710 324 C ATOM 1138 CZ PHE B 153 48.861 21.707 -18.526 1.00 25.87 C ANISOU 1138 CZ PHE B 153 3090 4022 2716 -281 757 306 C ATOM 1139 N GLY B 154 46.879 25.796 -18.239 1.00 25.52 N ANISOU 1139 N GLY B 154 3317 3695 2683 -466 627 535 N ATOM 1140 CA GLY B 154 47.461 26.182 -16.963 1.00 24.96 C ANISOU 1140 CA GLY B 154 3188 3591 2705 -504 605 498 C ATOM 1141 C GLY B 154 46.915 27.456 -16.337 1.00 24.78 C ANISOU 1141 C GLY B 154 3239 3437 2740 -550 566 532 C ATOM 1142 O GLY B 154 47.000 27.629 -15.116 1.00 24.58 O ANISOU 1142 O GLY B 154 3193 3369 2776 -563 529 480 O ATOM 1143 N ARG B 155 46.342 28.346 -17.147 1.00 24.80 N ANISOU 1143 N ARG B 155 3333 3369 2723 -576 575 619 N ATOM 1144 CA ARG B 155 46.037 29.685 -16.651 1.00 24.79 C ANISOU 1144 CA ARG B 155 3398 3226 2796 -630 561 655 C ATOM 1145 C ARG B 155 44.694 30.309 -17.029 1.00 24.81 C ANISOU 1145 C ARG B 155 3501 3108 2816 -575 523 729 C ATOM 1146 O ARG B 155 44.286 31.294 -16.404 1.00 25.24 O ANISOU 1146 O ARG B 155 3607 3024 2958 -592 512 736 O ATOM 1147 CB ARG B 155 47.197 30.647 -16.944 1.00 26.03 C ANISOU 1147 CB ARG B 155 3541 3381 2969 -767 621 699 C ATOM 1148 CG ARG B 155 47.678 30.674 -18.381 1.00 26.54 C ANISOU 1148 CG ARG B 155 3613 3526 2947 -814 685 784 C ATOM 1149 CD ARG B 155 49.163 31.039 -18.495 1.00 26.77 C ANISOU 1149 CD ARG B 155 3563 3623 2986 -944 762 786 C ATOM 1150 NE ARG B 155 49.613 32.003 -17.483 1.00 26.98 N ANISOU 1150 NE ARG B 155 3583 3556 3113 -1038 749 761 N ATOM 1151 CZ ARG B 155 49.327 33.304 -17.487 1.00 27.59 C ANISOU 1151 CZ ARG B 155 3758 3483 3243 -1110 751 825 C ATOM 1152 NH1 ARG B 155 48.567 33.832 -18.440 1.00 28.77 N ANISOU 1152 NH1 ARG B 155 4014 3557 3360 -1089 756 937 N ATOM 1153 NH2 ARG B 155 49.790 34.081 -16.526 1.00 27.34 N ANISOU 1153 NH2 ARG B 155 3720 3370 3298 -1204 743 778 N ATOM 1154 N LYS B 156 44.002 29.748 -18.019 1.00 24.51 N ANISOU 1154 N LYS B 156 3489 3121 2703 -511 501 779 N ATOM 1155 CA LYS B 156 42.705 30.302 -18.434 1.00 24.75 C ANISOU 1155 CA LYS B 156 3596 3050 2756 -454 449 864 C ATOM 1156 C LYS B 156 41.717 29.262 -18.991 1.00 23.80 C ANISOU 1156 C LYS B 156 3474 3000 2568 -360 393 865 C ATOM 1157 O LYS B 156 42.049 28.480 -19.888 1.00 23.87 O ANISOU 1157 O LYS B 156 3474 3133 2464 -370 408 867 O ATOM 1158 CB LYS B 156 42.906 31.466 -19.423 1.00 26.36 C ANISOU 1158 CB LYS B 156 3873 3197 2944 -529 470 1002 C ATOM 1159 CG LYS B 156 41.662 32.325 -19.667 1.00 27.32 C ANISOU 1159 CG LYS B 156 4069 3178 3134 -472 410 1108 C ATOM 1160 CD LYS B 156 41.896 33.365 -20.759 1.00 29.18 C ANISOU 1160 CD LYS B 156 4383 3366 3338 -546 424 1267 C ATOM 1161 CE LYS B 156 42.122 34.776 -20.192 1.00 31.75 C ANISOU 1161 CE LYS B 156 4758 3505 3801 -603 456 1303 C ATOM 1162 NZ LYS B 156 43.301 34.889 -19.279 1.00 31.62 N ANISOU 1162 NZ LYS B 156 4696 3495 3822 -698 527 1189 N ATOM 1163 N VAL B 157 40.500 29.277 -18.450 1.00 23.02 N ANISOU 1163 N VAL B 157 3383 2820 2542 -275 335 856 N ATOM 1164 CA VAL B 157 39.418 28.389 -18.893 1.00 22.30 C ANISOU 1164 CA VAL B 157 3284 2781 2407 -194 271 860 C ATOM 1165 C VAL B 157 38.094 29.167 -19.019 1.00 22.68 C ANISOU 1165 C VAL B 157 3364 2717 2538 -132 206 951 C ATOM 1166 O VAL B 157 37.848 30.113 -18.270 1.00 23.20 O ANISOU 1166 O VAL B 157 3442 2646 2726 -119 220 957 O ATOM 1167 CB VAL B 157 39.281 27.143 -17.957 1.00 21.00 C ANISOU 1167 CB VAL B 157 3058 2668 2254 -141 268 729 C ATOM 1168 CG1 VAL B 157 38.851 27.545 -16.545 1.00 20.65 C ANISOU 1168 CG1 VAL B 157 2999 2515 2331 -109 271 671 C ATOM 1169 CG2 VAL B 157 38.334 26.098 -18.541 1.00 20.49 C ANISOU 1169 CG2 VAL B 157 2984 2671 2130 -82 210 724 C ATOM 1170 N GLU B 158 37.262 28.781 -19.982 1.00 22.67 N ANISOU 1170 N GLU B 158 3373 2770 2472 -97 134 1020 N ATOM 1171 CA GLU B 158 35.976 29.436 -20.196 1.00 23.10 C ANISOU 1171 CA GLU B 158 3433 2733 2610 -29 57 1122 C ATOM 1172 C GLU B 158 34.810 28.489 -19.902 1.00 22.17 C ANISOU 1172 C GLU B 158 3254 2653 2519 52 -5 1068 C ATOM 1173 O GLU B 158 34.811 27.337 -20.338 1.00 21.71 O ANISOU 1173 O GLU B 158 3181 2719 2351 41 -28 1017 O ATOM 1174 CB GLU B 158 35.877 29.976 -21.628 1.00 24.53 C ANISOU 1174 CB GLU B 158 3676 2942 2701 -65 1 1284 C ATOM 1175 CG GLU B 158 34.650 30.853 -21.885 1.00 25.94 C ANISOU 1175 CG GLU B 158 3858 3011 2988 7 -88 1421 C ATOM 1176 CD GLU B 158 34.575 31.416 -23.302 1.00 27.73 C ANISOU 1176 CD GLU B 158 4154 3268 3114 -34 -157 1604 C ATOM 1177 OE1 GLU B 158 35.186 30.844 -24.228 1.00 28.44 O ANISOU 1177 OE1 GLU B 158 4286 3502 3017 -114 -153 1612 O ATOM 1178 OE2 GLU B 158 33.885 32.441 -23.491 1.00 29.81 O ANISOU 1178 OE2 GLU B 158 4431 3408 3485 14 -215 1745 O ATOM 1179 N VAL B 159 33.832 28.984 -19.147 1.00 21.82 N ANISOU 1179 N VAL B 159 3172 2493 2626 129 -22 1072 N ATOM 1180 CA VAL B 159 32.552 28.306 -18.969 1.00 21.59 C ANISOU 1180 CA VAL B 159 3073 2485 2645 205 -85 1051 C ATOM 1181 C VAL B 159 31.591 28.910 -19.996 1.00 23.07 C ANISOU 1181 C VAL B 159 3257 2653 2857 244 -191 1212 C ATOM 1182 O VAL B 159 31.221 30.085 -19.895 1.00 24.11 O ANISOU 1182 O VAL B 159 3394 2650 3116 288 -195 1302 O ATOM 1183 CB VAL B 159 32.004 28.482 -17.518 1.00 21.07 C ANISOU 1183 CB VAL B 159 2957 2313 2735 266 -28 959 C ATOM 1184 CG1 VAL B 159 30.608 27.896 -17.367 1.00 21.10 C ANISOU 1184 CG1 VAL B 159 2876 2334 2807 342 -86 952 C ATOM 1185 CG2 VAL B 159 32.940 27.853 -16.517 1.00 19.79 C ANISOU 1185 CG2 VAL B 159 2803 2185 2532 221 55 817 C ATOM 1186 N LEU B 160 31.223 28.113 -21.000 1.00 23.35 N ANISOU 1186 N LEU B 160 3286 2819 2766 223 -280 1249 N ATOM 1187 CA LEU B 160 30.285 28.549 -22.037 1.00 24.91 C ANISOU 1187 CA LEU B 160 3474 3028 2962 250 -408 1410 C ATOM 1188 C LEU B 160 28.861 28.573 -21.492 1.00 25.22 C ANISOU 1188 C LEU B 160 3402 3008 3171 352 -466 1420 C ATOM 1189 O LEU B 160 28.016 29.346 -21.955 1.00 26.71 O ANISOU 1189 O LEU B 160 3557 3140 3451 411 -555 1565 O ATOM 1190 CB LEU B 160 30.341 27.629 -23.265 1.00 25.26 C ANISOU 1190 CB LEU B 160 3553 3245 2798 178 -488 1429 C ATOM 1191 CG LEU B 160 31.575 27.481 -24.170 1.00 25.76 C ANISOU 1191 CG LEU B 160 3723 3405 2661 72 -444 1436 C ATOM 1192 CD1 LEU B 160 32.263 28.811 -24.474 1.00 27.14 C ANISOU 1192 CD1 LEU B 160 3969 3493 2851 43 -407 1562 C ATOM 1193 CD2 LEU B 160 32.565 26.459 -23.609 1.00 24.67 C ANISOU 1193 CD2 LEU B 160 3589 3326 2459 32 -330 1257 C ATOM 1194 N GLY B 161 28.610 27.710 -20.512 1.00 23.95 N ANISOU 1194 N GLY B 161 3180 2863 3057 373 -412 1273 N ATOM 1195 CA GLY B 161 27.309 27.589 -19.872 1.00 24.17 C ANISOU 1195 CA GLY B 161 3091 2848 3244 459 -439 1257 C ATOM 1196 C GLY B 161 27.424 26.689 -18.659 1.00 22.63 C ANISOU 1196 C GLY B 161 2866 2663 3070 455 -341 1083 C ATOM 1197 O GLY B 161 28.283 25.808 -18.613 1.00 21.52 O ANISOU 1197 O GLY B 161 2776 2603 2797 387 -302 990 O ATOM 1198 N THR B 162 26.564 26.910 -17.672 1.00 22.74 N ANISOU 1198 N THR B 162 2795 2592 3252 529 -297 1044 N ATOM 1199 CA THR B 162 26.585 26.110 -16.454 1.00 21.50 C ANISOU 1199 CA THR B 162 2614 2442 3114 521 -202 892 C ATOM 1200 C THR B 162 25.180 25.638 -16.071 1.00 21.94 C ANISOU 1200 C THR B 162 2541 2508 3286 576 -226 876 C ATOM 1201 O THR B 162 24.250 26.433 -16.012 1.00 23.16 O ANISOU 1201 O THR B 162 2614 2584 3600 658 -241 945 O ATOM 1202 CB THR B 162 27.329 26.833 -15.286 1.00 21.01 C ANISOU 1202 CB THR B 162 2608 2266 3110 524 -68 813 C ATOM 1203 OG1 THR B 162 26.776 26.428 -14.029 1.00 20.57 O ANISOU 1203 OG1 THR B 162 2499 2183 3134 550 14 703 O ATOM 1204 CG2 THR B 162 27.241 28.355 -15.413 1.00 22.28 C ANISOU 1204 CG2 THR B 162 2787 2284 3394 576 -54 904 C ATOM 1205 N LYS B 163 25.047 24.334 -15.820 1.00 21.07 N ANISOU 1205 N LYS B 163 2410 2491 3106 530 -226 788 N ATOM 1206 CA LYS B 163 23.736 23.686 -15.650 1.00 21.57 C ANISOU 1206 CA LYS B 163 2348 2593 3255 555 -264 777 C ATOM 1207 C LYS B 163 22.922 24.241 -14.485 1.00 22.04 C ANISOU 1207 C LYS B 163 2320 2553 3502 631 -164 741 C ATOM 1208 O LYS B 163 23.480 24.655 -13.475 1.00 21.49 O ANISOU 1208 O LYS B 163 2307 2403 3455 637 -41 665 O ATOM 1209 CB LYS B 163 23.887 22.163 -15.538 1.00 20.57 C ANISOU 1209 CB LYS B 163 2237 2566 3015 478 -266 682 C ATOM 1210 CG LYS B 163 24.270 21.497 -16.857 1.00 21.36 C ANISOU 1210 CG LYS B 163 2391 2773 2953 409 -378 715 C ATOM 1211 CD LYS B 163 23.891 20.026 -16.890 1.00 22.47 C ANISOU 1211 CD LYS B 163 2507 2995 3034 346 -405 637 C ATOM 1212 CE LYS B 163 23.938 19.471 -18.309 1.00 23.65 C ANISOU 1212 CE LYS B 163 2694 3250 3041 279 -529 672 C ATOM 1213 NZ LYS B 163 22.808 19.965 -19.161 1.00 25.64 N ANISOU 1213 NZ LYS B 163 2853 3543 3347 297 -667 790 N ATOM 1214 N SER B 164 21.603 24.267 -14.649 1.00 23.25 N ANISOU 1214 N SER B 164 2331 2714 3788 684 -217 793 N ATOM 1215 CA SER B 164 20.713 24.848 -13.651 1.00 24.07 C ANISOU 1215 CA SER B 164 2331 2724 4089 767 -114 764 C ATOM 1216 C SER B 164 20.603 23.932 -12.446 1.00 23.17 C ANISOU 1216 C SER B 164 2210 2634 3960 723 5 626 C ATOM 1217 O SER B 164 20.711 24.376 -11.299 1.00 23.17 O ANISOU 1217 O SER B 164 2233 2549 4020 747 150 544 O ATOM 1218 CB SER B 164 19.323 25.108 -14.241 1.00 25.84 C ANISOU 1218 CB SER B 164 2382 2963 4474 840 -213 871 C ATOM 1219 OG SER B 164 19.341 26.204 -15.137 1.00 27.02 O ANISOU 1219 OG SER B 164 2535 3055 4676 903 -304 1013 O ATOM 1220 N VAL B 165 20.376 22.653 -12.723 1.00 22.69 N ANISOU 1220 N VAL B 165 2124 2684 3812 650 -57 602 N ATOM 1221 CA VAL B 165 20.295 21.637 -11.685 1.00 21.96 C ANISOU 1221 CA VAL B 165 2035 2620 3689 594 41 489 C ATOM 1222 C VAL B 165 21.224 20.487 -12.035 1.00 20.64 C ANISOU 1222 C VAL B 165 1980 2531 3333 499 -7 450 C ATOM 1223 O VAL B 165 21.522 20.261 -13.210 1.00 20.86 O ANISOU 1223 O VAL B 165 2037 2617 3270 470 -128 505 O ATOM 1224 CB VAL B 165 18.841 21.115 -11.475 1.00 22.99 C ANISOU 1224 CB VAL B 165 1996 2791 3951 602 39 490 C ATOM 1225 CG1 VAL B 165 17.973 22.186 -10.835 1.00 24.33 C ANISOU 1225 CG1 VAL B 165 2049 2870 4324 705 135 499 C ATOM 1226 CG2 VAL B 165 18.229 20.626 -12.784 1.00 23.74 C ANISOU 1226 CG2 VAL B 165 2008 2981 4033 575 -139 576 C ATOM 1227 N LEU B 166 21.693 19.779 -11.016 1.00 19.68 N ANISOU 1227 N LEU B 166 1922 2406 3150 451 91 357 N ATOM 1228 CA LEU B 166 22.511 18.595 -11.226 1.00 18.69 C ANISOU 1228 CA LEU B 166 1889 2339 2874 373 59 316 C ATOM 1229 C LEU B 166 22.324 17.622 -10.074 1.00 18.44 C ANISOU 1229 C LEU B 166 1862 2308 2836 326 149 239 C ATOM 1230 O LEU B 166 22.266 18.032 -8.914 1.00 18.74 O ANISOU 1230 O LEU B 166 1907 2298 2917 342 265 198 O ATOM 1231 CB LEU B 166 23.987 18.969 -11.375 1.00 17.81 C ANISOU 1231 CB LEU B 166 1908 2211 2649 367 66 310 C ATOM 1232 CG LEU B 166 24.815 18.035 -12.262 1.00 17.34 C ANISOU 1232 CG LEU B 166 1923 2216 2450 311 -7 303 C ATOM 1233 CD1 LEU B 166 24.363 18.170 -13.705 1.00 18.20 C ANISOU 1233 CD1 LEU B 166 1995 2378 2542 309 -131 376 C ATOM 1234 CD2 LEU B 166 26.307 18.320 -12.131 1.00 16.29 C ANISOU 1234 CD2 LEU B 166 1898 2068 2222 303 30 284 C ATOM 1235 N ALA B 167 22.225 16.337 -10.400 1.00 18.18 N ANISOU 1235 N ALA B 167 1836 2327 2744 260 100 220 N ATOM 1236 CA ALA B 167 21.997 15.301 -9.403 1.00 18.04 C ANISOU 1236 CA ALA B 167 1827 2306 2721 206 175 165 C ATOM 1237 C ALA B 167 23.280 14.551 -9.085 1.00 17.10 C ANISOU 1237 C ALA B 167 1842 2181 2475 169 192 128 C ATOM 1238 O ALA B 167 24.170 14.438 -9.932 1.00 16.81 O ANISOU 1238 O ALA B 167 1870 2161 2356 169 126 136 O ATOM 1239 CB ALA B 167 20.927 14.337 -9.880 1.00 18.73 C ANISOU 1239 CB ALA B 167 1825 2438 2854 151 115 170 C ATOM 1240 N ALA B 168 23.369 14.048 -7.856 1.00 16.93 N ANISOU 1240 N ALA B 168 1857 2135 2439 139 282 93 N ATOM 1241 CA ALA B 168 24.472 13.188 -7.438 1.00 16.17 C ANISOU 1241 CA ALA B 168 1871 2031 2241 106 291 72 C ATOM 1242 C ALA B 168 23.969 12.127 -6.473 1.00 16.51 C ANISOU 1242 C ALA B 168 1921 2062 2292 47 351 56 C ATOM 1243 O ALA B 168 23.079 12.388 -5.669 1.00 17.29 O ANISOU 1243 O ALA B 168 1963 2155 2449 35 431 49 O ATOM 1244 CB ALA B 168 25.579 14.002 -6.796 1.00 15.45 C ANISOU 1244 CB ALA B 168 1856 1922 2094 135 334 65 C ATOM 1245 N SER B 169 24.530 10.927 -6.562 1.00 16.28 N ANISOU 1245 N SER B 169 1959 2021 2206 10 321 52 N ATOM 1246 CA SER B 169 24.213 9.873 -5.609 1.00 16.71 C ANISOU 1246 CA SER B 169 2042 2049 2258 -50 375 52 C ATOM 1247 C SER B 169 25.283 9.833 -4.534 1.00 16.29 C ANISOU 1247 C SER B 169 2088 1979 2122 -46 417 63 C ATOM 1248 O SER B 169 26.337 10.455 -4.674 1.00 15.72 O ANISOU 1248 O SER B 169 2058 1916 1999 -1 392 63 O ATOM 1249 CB SER B 169 24.123 8.518 -6.305 1.00 17.04 C ANISOU 1249 CB SER B 169 2103 2068 2304 -97 317 45 C ATOM 1250 OG SER B 169 25.414 8.001 -6.588 1.00 16.51 O ANISOU 1250 OG SER B 169 2129 1976 2169 -72 279 43 O ATOM 1251 N LEU B 170 25.015 9.092 -3.465 1.00 16.86 N ANISOU 1251 N LEU B 170 2196 2031 2177 -101 477 79 N ATOM 1252 CA LEU B 170 25.966 8.966 -2.368 1.00 16.78 C ANISOU 1252 CA LEU B 170 2283 2015 2078 -109 503 104 C ATOM 1253 C LEU B 170 25.893 7.598 -1.703 1.00 17.18 C ANISOU 1253 C LEU B 170 2394 2027 2109 -169 517 145 C ATOM 1254 O LEU B 170 24.818 7.148 -1.314 1.00 17.97 O ANISOU 1254 O LEU B 170 2463 2118 2249 -231 576 150 O ATOM 1255 CB LEU B 170 25.720 10.068 -1.334 1.00 17.23 C ANISOU 1255 CB LEU B 170 2340 2101 2105 -116 591 85 C ATOM 1256 CG LEU B 170 26.636 10.119 -0.110 1.00 17.90 C ANISOU 1256 CG LEU B 170 2527 2198 2075 -142 614 106 C ATOM 1257 CD1 LEU B 170 28.030 10.620 -0.485 1.00 17.60 C ANISOU 1257 CD1 LEU B 170 2526 2173 1990 -91 536 108 C ATOM 1258 CD2 LEU B 170 26.009 11.005 0.945 1.00 19.02 C ANISOU 1258 CD2 LEU B 170 2672 2365 2192 -175 728 68 C ATOM 1259 N ILE B 171 27.042 6.938 -1.595 1.00 17.01 N ANISOU 1259 N ILE B 171 2450 1977 2037 -150 464 182 N ATOM 1260 CA ILE B 171 27.178 5.752 -0.748 1.00 17.71 C ANISOU 1260 CA ILE B 171 2614 2018 2097 -198 474 244 C ATOM 1261 C ILE B 171 27.907 6.191 0.513 1.00 18.04 C ANISOU 1261 C ILE B 171 2724 2098 2032 -208 492 286 C ATOM 1262 O ILE B 171 29.100 6.514 0.467 1.00 17.73 O ANISOU 1262 O ILE B 171 2711 2076 1949 -157 432 298 O ATOM 1263 CB ILE B 171 27.960 4.621 -1.438 1.00 17.56 C ANISOU 1263 CB ILE B 171 2634 1930 2109 -164 400 266 C ATOM 1264 CG1 ILE B 171 27.210 4.137 -2.683 1.00 17.53 C ANISOU 1264 CG1 ILE B 171 2577 1891 2192 -176 382 212 C ATOM 1265 CG2 ILE B 171 28.206 3.474 -0.461 1.00 18.38 C ANISOU 1265 CG2 ILE B 171 2824 1972 2190 -203 405 351 C ATOM 1266 CD1 ILE B 171 27.968 3.123 -3.501 1.00 17.63 C ANISOU 1266 CD1 ILE B 171 2632 1830 2238 -139 325 204 C ATOM 1267 N LYS B 172 27.180 6.232 1.628 1.00 18.74 N ANISOU 1267 N LYS B 172 2839 2206 2074 -281 576 304 N ATOM 1268 CA LYS B 172 27.759 6.670 2.896 1.00 19.13 C ANISOU 1268 CA LYS B 172 2966 2303 1997 -313 598 336 C ATOM 1269 C LYS B 172 28.680 5.609 3.475 1.00 19.43 C ANISOU 1269 C LYS B 172 3095 2311 1977 -322 528 438 C ATOM 1270 O LYS B 172 28.343 4.431 3.499 1.00 20.04 O ANISOU 1270 O LYS B 172 3198 2322 2093 -351 527 495 O ATOM 1271 CB LYS B 172 26.663 7.034 3.903 1.00 20.20 C ANISOU 1271 CB LYS B 172 3110 2476 2091 -395 727 315 C ATOM 1272 CG LYS B 172 26.064 8.416 3.677 1.00 20.65 C ANISOU 1272 CG LYS B 172 3091 2571 2185 -371 799 217 C ATOM 1273 CD LYS B 172 24.780 8.626 4.462 1.00 23.22 C ANISOU 1273 CD LYS B 172 3392 2918 2512 -441 947 185 C ATOM 1274 CE LYS B 172 25.033 9.275 5.816 1.00 24.83 C ANISOU 1274 CE LYS B 172 3689 3175 2570 -499 1027 166 C ATOM 1275 NZ LYS B 172 23.754 9.780 6.402 1.00 25.96 N ANISOU 1275 NZ LYS B 172 3786 3340 2737 -546 1197 101 N ATOM 1276 N GLY B 173 29.853 6.034 3.926 1.00 19.36 N ANISOU 1276 N GLY B 173 3129 2345 1883 -298 464 466 N ATOM 1277 CA GLY B 173 30.782 5.134 4.587 1.00 20.11 C ANISOU 1277 CA GLY B 173 3299 2422 1920 -301 385 579 C ATOM 1278 C GLY B 173 30.485 5.047 6.066 1.00 21.35 C ANISOU 1278 C GLY B 173 3550 2623 1938 -402 433 640 C ATOM 1279 O GLY B 173 29.450 5.523 6.532 1.00 21.66 O ANISOU 1279 O GLY B 173 3594 2695 1942 -472 547 588 O ATOM 1280 N THR B 174 31.395 4.429 6.807 1.00 22.21 N ANISOU 1280 N THR B 174 3733 2737 1971 -411 346 756 N ATOM 1281 CA THR B 174 31.285 4.387 8.257 1.00 23.58 C ANISOU 1281 CA THR B 174 4012 2970 1977 -516 372 827 C ATOM 1282 C THR B 174 31.862 5.662 8.857 1.00 23.58 C ANISOU 1282 C THR B 174 4033 3082 1844 -546 360 770 C ATOM 1283 O THR B 174 31.416 6.105 9.913 1.00 24.51 O ANISOU 1283 O THR B 174 4227 3268 1818 -648 436 755 O ATOM 1284 CB THR B 174 31.988 3.159 8.851 1.00 24.81 C ANISOU 1284 CB THR B 174 4244 3083 2099 -518 270 997 C ATOM 1285 OG1 THR B 174 33.301 3.041 8.289 1.00 24.40 O ANISOU 1285 OG1 THR B 174 4143 3016 2111 -411 134 1033 O ATOM 1286 CG2 THR B 174 31.193 1.900 8.553 1.00 25.26 C ANISOU 1286 CG2 THR B 174 4314 3019 2262 -528 314 1053 C ATOM 1287 N ALA B 175 32.841 6.249 8.168 1.00 22.66 N ANISOU 1287 N ALA B 175 3852 2983 1776 -466 273 731 N ATOM 1288 CA ALA B 175 33.460 7.511 8.588 1.00 22.64 C ANISOU 1288 CA ALA B 175 3859 3074 1669 -497 255 665 C ATOM 1289 C ALA B 175 32.598 8.723 8.256 1.00 21.91 C ANISOU 1289 C ALA B 175 3730 2992 1604 -510 382 512 C ATOM 1290 O ALA B 175 31.970 8.779 7.197 1.00 20.91 O ANISOU 1290 O ALA B 175 3519 2805 1620 -446 430 454 O ATOM 1291 CB ALA B 175 34.835 7.664 7.956 1.00 22.09 C ANISOU 1291 CB ALA B 175 3722 3016 1654 -414 120 686 C ATOM 1292 N LYS B 176 32.578 9.692 9.166 1.00 22.61 N ANISOU 1292 N LYS B 176 3882 3152 1555 -593 433 450 N ATOM 1293 CA LYS B 176 31.842 10.928 8.940 1.00 22.19 C ANISOU 1293 CA LYS B 176 3798 3096 1536 -598 557 304 C ATOM 1294 C LYS B 176 32.660 11.860 8.073 1.00 21.16 C ANISOU 1294 C LYS B 176 3600 2962 1478 -532 492 244 C ATOM 1295 O LYS B 176 33.714 12.349 8.481 1.00 21.52 O ANISOU 1295 O LYS B 176 3678 3063 1433 -565 410 247 O ATOM 1296 CB LYS B 176 31.484 11.622 10.252 1.00 23.54 C ANISOU 1296 CB LYS B 176 4076 3333 1535 -717 658 242 C ATOM 1297 CG LYS B 176 30.391 10.933 11.057 1.00 24.65 C ANISOU 1297 CG LYS B 176 4276 3479 1611 -793 777 272 C ATOM 1298 CD LYS B 176 29.878 11.830 12.183 1.00 26.11 C ANISOU 1298 CD LYS B 176 4554 3723 1645 -902 920 167 C ATOM 1299 CE LYS B 176 30.979 12.215 13.175 1.00 27.06 C ANISOU 1299 CE LYS B 176 4792 3934 1554 -994 829 180 C ATOM 1300 NZ LYS B 176 30.428 12.928 14.361 1.00 28.68 N ANISOU 1300 NZ LYS B 176 5114 4199 1585 -1120 981 76 N ATOM 1301 N THR B 177 32.167 12.088 6.866 1.00 20.03 N ANISOU 1301 N THR B 177 3360 2756 1494 -446 524 196 N ATOM 1302 CA THR B 177 32.770 13.034 5.949 1.00 19.12 C ANISOU 1302 CA THR B 177 3181 2630 1455 -387 485 139 C ATOM 1303 C THR B 177 32.233 14.436 6.244 1.00 19.42 C ANISOU 1303 C THR B 177 3237 2663 1481 -421 595 18 C ATOM 1304 O THR B 177 31.291 14.606 7.021 1.00 20.25 O ANISOU 1304 O THR B 177 3385 2769 1539 -475 715 -29 O ATOM 1305 CB THR B 177 32.435 12.661 4.487 1.00 17.98 C ANISOU 1305 CB THR B 177 2935 2423 1474 -287 469 146 C ATOM 1306 OG1 THR B 177 31.039 12.867 4.246 1.00 17.95 O ANISOU 1306 OG1 THR B 177 2894 2380 1546 -280 582 92 O ATOM 1307 CG2 THR B 177 32.765 11.198 4.208 1.00 17.90 C ANISOU 1307 CG2 THR B 177 2916 2393 1492 -254 390 246 C ATOM 1308 N VAL B 178 32.838 15.443 5.623 1.00 18.91 N ANISOU 1308 N VAL B 178 3137 2584 1462 -390 565 -32 N ATOM 1309 CA VAL B 178 32.204 16.749 5.517 1.00 19.05 C ANISOU 1309 CA VAL B 178 3148 2558 1532 -387 673 -141 C ATOM 1310 C VAL B 178 30.894 16.515 4.760 1.00 18.61 C ANISOU 1310 C VAL B 178 3011 2445 1617 -316 749 -147 C ATOM 1311 O VAL B 178 30.772 15.522 4.028 1.00 17.94 O ANISOU 1311 O VAL B 178 2869 2353 1594 -267 692 -76 O ATOM 1312 CB VAL B 178 33.104 17.768 4.776 1.00 18.54 C ANISOU 1312 CB VAL B 178 3054 2474 1517 -361 615 -172 C ATOM 1313 CG1 VAL B 178 34.334 18.102 5.614 1.00 19.24 C ANISOU 1313 CG1 VAL B 178 3214 2626 1469 -450 543 -178 C ATOM 1314 CG2 VAL B 178 33.519 17.251 3.398 1.00 17.37 C ANISOU 1314 CG2 VAL B 178 2813 2310 1475 -271 524 -102 C ATOM 1315 N ASP B 179 29.906 17.388 4.938 1.00 19.16 N ANISOU 1315 N ASP B 179 3068 2470 1741 -312 878 -233 N ATOM 1316 CA ASP B 179 28.608 17.150 4.305 1.00 19.01 C ANISOU 1316 CA ASP B 179 2953 2409 1859 -250 945 -231 C ATOM 1317 C ASP B 179 28.718 17.171 2.783 1.00 17.90 C ANISOU 1317 C ASP B 179 2719 2236 1849 -158 855 -189 C ATOM 1318 O ASP B 179 29.026 18.212 2.206 1.00 17.69 O ANISOU 1318 O ASP B 179 2673 2171 1877 -120 843 -219 O ATOM 1319 CB ASP B 179 27.555 18.144 4.771 1.00 20.02 C ANISOU 1319 CB ASP B 179 3068 2493 2044 -248 1104 -329 C ATOM 1320 CG ASP B 179 26.166 17.745 4.331 1.00 20.19 C ANISOU 1320 CG ASP B 179 2979 2492 2200 -199 1173 -318 C ATOM 1321 OD1 ASP B 179 25.683 16.685 4.792 1.00 20.49 O ANISOU 1321 OD1 ASP B 179 3021 2569 2197 -245 1199 -279 O ATOM 1322 OD2 ASP B 179 25.562 18.483 3.521 1.00 20.14 O ANISOU 1322 OD2 ASP B 179 2879 2429 2344 -119 1195 -339 O ATOM 1323 N PRO B 180 28.471 16.017 2.135 1.00 17.35 N ANISOU 1323 N PRO B 180 2598 2177 1819 -132 795 -120 N ATOM 1324 CA PRO B 180 28.661 15.863 0.693 1.00 16.44 C ANISOU 1324 CA PRO B 180 2410 2044 1793 -62 703 -81 C ATOM 1325 C PRO B 180 27.955 16.923 -0.155 1.00 16.47 C ANISOU 1325 C PRO B 180 2335 2001 1920 1 732 -110 C ATOM 1326 O PRO B 180 28.613 17.614 -0.939 1.00 16.02 O ANISOU 1326 O PRO B 180 2272 1929 1885 37 675 -103 O ATOM 1327 CB PRO B 180 28.094 14.465 0.417 1.00 16.34 C ANISOU 1327 CB PRO B 180 2365 2039 1806 -66 677 -30 C ATOM 1328 CG PRO B 180 28.312 13.738 1.682 1.00 16.91 C ANISOU 1328 CG PRO B 180 2519 2138 1768 -138 705 -9 C ATOM 1329 CD PRO B 180 28.006 14.760 2.746 1.00 17.74 C ANISOU 1329 CD PRO B 180 2667 2250 1823 -180 814 -77 C ATOM 1330 N LEU B 181 26.639 17.061 0.008 1.00 17.14 N ANISOU 1330 N LEU B 181 2357 2065 2090 14 820 -135 N ATOM 1331 CA LEU B 181 25.872 17.952 -0.855 1.00 17.36 C ANISOU 1331 CA LEU B 181 2292 2048 2256 86 832 -142 C ATOM 1332 C LEU B 181 26.224 19.422 -0.646 1.00 17.75 C ANISOU 1332 C LEU B 181 2375 2042 2326 108 881 -192 C ATOM 1333 O LEU B 181 26.570 20.113 -1.605 1.00 17.43 O ANISOU 1333 O LEU B 181 2313 1971 2340 157 819 -165 O ATOM 1334 CB LEU B 181 24.364 17.711 -0.713 1.00 18.20 C ANISOU 1334 CB LEU B 181 2298 2150 2468 98 913 -152 C ATOM 1335 CG LEU B 181 23.462 18.201 -1.857 1.00 18.48 C ANISOU 1335 CG LEU B 181 2203 2158 2660 176 878 -122 C ATOM 1336 CD1 LEU B 181 23.824 17.531 -3.175 1.00 17.62 C ANISOU 1336 CD1 LEU B 181 2072 2081 2543 189 729 -54 C ATOM 1337 CD2 LEU B 181 21.994 17.976 -1.526 1.00 19.56 C ANISOU 1337 CD2 LEU B 181 2226 2299 2908 180 969 -136 C ATOM 1338 N SER B 182 26.163 19.893 0.596 1.00 18.56 N ANISOU 1338 N SER B 182 2542 2131 2378 63 994 -266 N ATOM 1339 CA SER B 182 26.413 21.309 0.871 1.00 19.18 C ANISOU 1339 CA SER B 182 2663 2140 2486 76 1058 -333 C ATOM 1340 C SER B 182 27.866 21.730 0.611 1.00 18.54 C ANISOU 1340 C SER B 182 2660 2061 2323 47 966 -321 C ATOM 1341 O SER B 182 28.118 22.865 0.198 1.00 18.78 O ANISOU 1341 O SER B 182 2697 2021 2418 77 970 -338 O ATOM 1342 CB SER B 182 25.958 21.700 2.281 1.00 20.44 C ANISOU 1342 CB SER B 182 2882 2284 2601 24 1215 -434 C ATOM 1343 OG SER B 182 26.579 20.891 3.257 1.00 20.37 O ANISOU 1343 OG SER B 182 2971 2354 2416 -75 1206 -439 O ATOM 1344 N THR B 183 28.811 20.822 0.841 1.00 17.87 N ANISOU 1344 N THR B 183 2627 2052 2109 -10 884 -286 N ATOM 1345 CA THR B 183 30.222 21.108 0.585 1.00 17.36 C ANISOU 1345 CA THR B 183 2614 2007 1976 -40 793 -268 C ATOM 1346 C THR B 183 30.480 21.277 -0.918 1.00 16.61 C ANISOU 1346 C THR B 183 2453 1893 1965 27 706 -202 C ATOM 1347 O THR B 183 31.085 22.271 -1.351 1.00 16.68 O ANISOU 1347 O THR B 183 2479 1861 1999 29 690 -207 O ATOM 1348 CB THR B 183 31.145 20.032 1.206 1.00 17.04 C ANISOU 1348 CB THR B 183 2626 2054 1795 -105 722 -234 C ATOM 1349 OG1 THR B 183 30.993 20.047 2.632 1.00 17.97 O ANISOU 1349 OG1 THR B 183 2824 2194 1810 -183 798 -292 O ATOM 1350 CG2 THR B 183 32.621 20.276 0.850 1.00 16.63 C ANISOU 1350 CG2 THR B 183 2595 2030 1693 -129 623 -208 C ATOM 1351 N LEU B 184 30.003 20.316 -1.706 1.00 16.05 N ANISOU 1351 N LEU B 184 2315 1852 1929 70 655 -142 N ATOM 1352 CA LEU B 184 30.107 20.388 -3.161 1.00 15.53 C ANISOU 1352 CA LEU B 184 2193 1781 1924 125 577 -82 C ATOM 1353 C LEU B 184 29.428 21.645 -3.707 1.00 16.11 C ANISOU 1353 C LEU B 184 2229 1776 2116 179 612 -82 C ATOM 1354 O LEU B 184 29.987 22.348 -4.552 1.00 16.02 O ANISOU 1354 O LEU B 184 2221 1740 2125 195 567 -47 O ATOM 1355 CB LEU B 184 29.525 19.124 -3.804 1.00 15.11 C ANISOU 1355 CB LEU B 184 2083 1771 1886 148 527 -37 C ATOM 1356 CG LEU B 184 30.489 17.981 -4.153 1.00 14.42 C ANISOU 1356 CG LEU B 184 2018 1741 1719 129 448 -4 C ATOM 1357 CD1 LEU B 184 31.356 18.359 -5.361 1.00 14.03 C ANISOU 1357 CD1 LEU B 184 1962 1702 1667 152 381 29 C ATOM 1358 CD2 LEU B 184 31.364 17.547 -2.969 1.00 14.44 C ANISOU 1358 CD2 LEU B 184 2088 1774 1624 75 455 -20 C ATOM 1359 N GLN B 185 28.232 21.931 -3.197 1.00 16.88 N ANISOU 1359 N GLN B 185 2288 1830 2296 206 699 -117 N ATOM 1360 CA GLN B 185 27.496 23.127 -3.576 1.00 17.73 C ANISOU 1360 CA GLN B 185 2349 1847 2539 271 742 -115 C ATOM 1361 C GLN B 185 28.338 24.385 -3.354 1.00 18.11 C ANISOU 1361 C GLN B 185 2476 1821 2583 251 772 -150 C ATOM 1362 O GLN B 185 28.445 25.236 -4.241 1.00 18.35 O ANISOU 1362 O GLN B 185 2493 1791 2688 293 736 -101 O ATOM 1363 CB GLN B 185 26.187 23.212 -2.792 1.00 18.71 C ANISOU 1363 CB GLN B 185 2419 1938 2752 298 859 -168 C ATOM 1364 CG GLN B 185 25.243 24.283 -3.286 1.00 19.77 C ANISOU 1364 CG GLN B 185 2472 1977 3063 390 897 -150 C ATOM 1365 CD GLN B 185 24.817 24.066 -4.720 1.00 19.56 C ANISOU 1365 CD GLN B 185 2350 1974 3108 450 775 -40 C ATOM 1366 OE1 GLN B 185 24.078 23.135 -5.020 1.00 19.45 O ANISOU 1366 OE1 GLN B 185 2253 2026 3111 455 737 -8 O ATOM 1367 NE2 GLN B 185 25.274 24.932 -5.612 1.00 19.66 N ANISOU 1367 NE2 GLN B 185 2379 1934 3156 484 711 21 N ATOM 1368 N MET B 186 28.943 24.475 -2.172 1.00 18.29 N ANISOU 1368 N MET B 186 2587 1851 2511 176 831 -231 N ATOM 1369 CA MET B 186 29.768 25.611 -1.786 1.00 18.83 C ANISOU 1369 CA MET B 186 2740 1852 2561 130 863 -285 C ATOM 1370 C MET B 186 30.898 25.869 -2.789 1.00 18.21 C ANISOU 1370 C MET B 186 2674 1786 2459 116 759 -215 C ATOM 1371 O MET B 186 31.181 27.025 -3.131 1.00 18.79 O ANISOU 1371 O MET B 186 2775 1769 2597 119 773 -214 O ATOM 1372 CB MET B 186 30.310 25.388 -0.372 1.00 19.11 C ANISOU 1372 CB MET B 186 2868 1932 2461 30 913 -375 C ATOM 1373 CG MET B 186 31.262 26.456 0.143 1.00 19.78 C ANISOU 1373 CG MET B 186 3049 1965 2501 -47 935 -444 C ATOM 1374 SD MET B 186 32.980 26.080 -0.254 1.00 18.87 S ANISOU 1374 SD MET B 186 2958 1944 2269 -122 794 -385 S ATOM 1375 CE MET B 186 33.254 24.603 0.721 1.00 18.44 C ANISOU 1375 CE MET B 186 2921 2029 2056 -180 755 -383 C ATOM 1376 N LEU B 187 31.522 24.788 -3.260 1.00 17.18 N ANISOU 1376 N LEU B 187 2523 1761 2243 99 665 -159 N ATOM 1377 CA LEU B 187 32.629 24.873 -4.209 1.00 16.66 C ANISOU 1377 CA LEU B 187 2459 1727 2144 81 579 -97 C ATOM 1378 C LEU B 187 32.166 25.432 -5.545 1.00 16.81 C ANISOU 1378 C LEU B 187 2432 1695 2261 150 548 -19 C ATOM 1379 O LEU B 187 32.887 26.196 -6.197 1.00 17.00 O ANISOU 1379 O LEU B 187 2479 1687 2293 131 523 19 O ATOM 1380 CB LEU B 187 33.276 23.500 -4.417 1.00 15.73 C ANISOU 1380 CB LEU B 187 2321 1726 1931 65 503 -62 C ATOM 1381 CG LEU B 187 33.941 22.773 -3.239 1.00 15.62 C ANISOU 1381 CG LEU B 187 2347 1779 1809 -1 499 -105 C ATOM 1382 CD1 LEU B 187 34.525 21.453 -3.709 1.00 14.86 C ANISOU 1382 CD1 LEU B 187 2216 1772 1659 10 421 -52 C ATOM 1383 CD2 LEU B 187 35.018 23.616 -2.551 1.00 16.15 C ANISOU 1383 CD2 LEU B 187 2474 1839 1823 -85 504 -150 C ATOM 1384 N HIS B 188 30.952 25.059 -5.937 1.00 16.88 N ANISOU 1384 N HIS B 188 2375 1700 2341 220 546 13 N ATOM 1385 CA HIS B 188 30.410 25.414 -7.247 1.00 17.15 C ANISOU 1385 CA HIS B 188 2355 1707 2453 284 492 104 C ATOM 1386 C HIS B 188 29.725 26.775 -7.254 1.00 18.33 C ANISOU 1386 C HIS B 188 2499 1724 2742 338 546 114 C ATOM 1387 O HIS B 188 29.647 27.429 -8.293 1.00 18.80 O ANISOU 1387 O HIS B 188 2544 1739 2859 374 497 203 O ATOM 1388 CB HIS B 188 29.466 24.313 -7.735 1.00 16.83 C ANISOU 1388 CB HIS B 188 2237 1736 2421 325 444 139 C ATOM 1389 CG HIS B 188 30.159 23.017 -8.005 1.00 15.85 C ANISOU 1389 CG HIS B 188 2123 1720 2179 284 385 141 C ATOM 1390 ND1 HIS B 188 30.393 22.549 -9.280 1.00 15.56 N ANISOU 1390 ND1 HIS B 188 2070 1742 2101 289 301 205 N ATOM 1391 CD2 HIS B 188 30.705 22.109 -7.164 1.00 15.27 C ANISOU 1391 CD2 HIS B 188 2080 1701 2022 237 401 89 C ATOM 1392 CE1 HIS B 188 31.044 21.401 -9.213 1.00 14.85 C ANISOU 1392 CE1 HIS B 188 1996 1727 1920 255 279 180 C ATOM 1393 NE2 HIS B 188 31.243 21.111 -7.939 1.00 14.66 N ANISOU 1393 NE2 HIS B 188 1997 1698 1875 227 332 119 N ATOM 1394 N GLY B 189 29.249 27.198 -6.089 1.00 18.98 N ANISOU 1394 N GLY B 189 2598 1737 2877 340 651 24 N ATOM 1395 CA GLY B 189 28.567 28.479 -5.944 1.00 20.33 C ANISOU 1395 CA GLY B 189 2764 1760 3200 400 727 13 C ATOM 1396 C GLY B 189 27.062 28.321 -5.977 1.00 21.02 C ANISOU 1396 C GLY B 189 2742 1826 3419 495 757 30 C ATOM 1397 O GLY B 189 26.516 27.364 -5.423 1.00 20.66 O ANISOU 1397 O GLY B 189 2653 1859 3340 486 784 -13 O ATOM 1398 N ALA B 190 26.389 29.262 -6.634 1.00 22.16 N ANISOU 1398 N ALA B 190 2835 1864 3721 584 751 101 N ATOM 1399 CA ALA B 190 24.936 29.229 -6.753 1.00 23.11 C ANISOU 1399 CA ALA B 190 2825 1960 3995 685 771 132 C ATOM 1400 C ALA B 190 24.447 28.131 -7.698 1.00 22.46 C ANISOU 1400 C ALA B 190 2646 2011 3875 697 642 225 C ATOM 1401 O ALA B 190 23.363 27.587 -7.500 1.00 22.84 O ANISOU 1401 O ALA B 190 2586 2098 3996 737 661 218 O ATOM 1402 CB ALA B 190 24.415 30.575 -7.194 1.00 24.73 C ANISOU 1402 CB ALA B 190 2999 2005 4392 784 790 194 C ATOM 1403 N GLU B 191 25.246 27.802 -8.712 1.00 21.61 N ANISOU 1403 N GLU B 191 2580 1976 3654 655 520 305 N ATOM 1404 CA GLU B 191 24.819 26.870 -9.762 1.00 21.34 C ANISOU 1404 CA GLU B 191 2472 2059 3578 659 392 392 C ATOM 1405 C GLU B 191 25.875 25.823 -10.154 1.00 19.80 C ANISOU 1405 C GLU B 191 2347 1986 3191 568 325 384 C ATOM 1406 O GLU B 191 27.071 26.126 -10.175 1.00 19.28 O ANISOU 1406 O GLU B 191 2378 1911 3036 517 331 372 O ATOM 1407 CB GLU B 191 24.385 27.648 -11.008 1.00 22.53 C ANISOU 1407 CB GLU B 191 2574 2168 3819 726 291 535 C ATOM 1408 CG GLU B 191 22.984 28.251 -10.938 1.00 24.33 C ANISOU 1408 CG GLU B 191 2670 2316 4258 838 310 578 C ATOM 1409 CD GLU B 191 22.538 28.838 -12.274 1.00 25.92 C ANISOU 1409 CD GLU B 191 2816 2501 4532 900 174 747 C ATOM 1410 OE1 GLU B 191 21.335 28.730 -12.603 1.00 27.77 O ANISOU 1410 OE1 GLU B 191 2907 2755 4890 971 117 811 O ATOM 1411 OE2 GLU B 191 23.392 29.400 -13.001 1.00 26.71 O ANISOU 1411 OE2 GLU B 191 3011 2575 4561 873 119 822 O ATOM 1412 N PRO B 192 25.440 24.590 -10.484 1.00 19.31 N ANISOU 1412 N PRO B 192 2232 2033 3074 548 263 388 N ATOM 1413 CA PRO B 192 24.062 24.097 -10.471 1.00 19.96 C ANISOU 1413 CA PRO B 192 2189 2142 3254 587 249 399 C ATOM 1414 C PRO B 192 23.536 23.923 -9.059 1.00 20.09 C ANISOU 1414 C PRO B 192 2178 2126 3330 590 382 298 C ATOM 1415 O PRO B 192 24.321 23.778 -8.121 1.00 19.39 O ANISOU 1415 O PRO B 192 2181 2030 3157 538 462 214 O ATOM 1416 CB PRO B 192 24.170 22.721 -11.143 1.00 19.20 C ANISOU 1416 CB PRO B 192 2090 2170 3036 526 155 407 C ATOM 1417 CG PRO B 192 25.520 22.691 -11.791 1.00 18.41 C ANISOU 1417 CG PRO B 192 2100 2101 2794 479 110 424 C ATOM 1418 CD PRO B 192 26.375 23.545 -10.933 1.00 18.17 C ANISOU 1418 CD PRO B 192 2148 1991 2766 475 206 377 C ATOM 1419 N VAL B 193 22.216 23.955 -8.912 1.00 21.15 N ANISOU 1419 N VAL B 193 2182 2247 3605 645 406 308 N ATOM 1420 CA VAL B 193 21.593 23.612 -7.643 1.00 21.42 C ANISOU 1420 CA VAL B 193 2179 2273 3686 636 539 214 C ATOM 1421 C VAL B 193 21.599 22.087 -7.540 1.00 20.52 C ANISOU 1421 C VAL B 193 2068 2270 3460 553 505 188 C ATOM 1422 O VAL B 193 20.837 21.398 -8.220 1.00 20.82 O ANISOU 1422 O VAL B 193 2008 2372 3530 549 421 236 O ATOM 1423 CB VAL B 193 20.160 24.195 -7.510 1.00 23.09 C ANISOU 1423 CB VAL B 193 2233 2431 4108 727 593 232 C ATOM 1424 CG1 VAL B 193 19.517 23.747 -6.201 1.00 23.47 C ANISOU 1424 CG1 VAL B 193 2243 2486 4189 703 748 128 C ATOM 1425 CG2 VAL B 193 20.188 25.716 -7.600 1.00 24.15 C ANISOU 1425 CG2 VAL B 193 2374 2430 4371 818 633 259 C ATOM 1426 N PHE B 194 22.494 21.572 -6.707 1.00 19.56 N ANISOU 1426 N PHE B 194 2061 2166 3206 484 561 118 N ATOM 1427 CA PHE B 194 22.696 20.137 -6.576 1.00 18.75 C ANISOU 1427 CA PHE B 194 1984 2145 2994 407 530 100 C ATOM 1428 C PHE B 194 21.585 19.477 -5.766 1.00 19.42 C ANISOU 1428 C PHE B 194 1988 2250 3140 385 615 62 C ATOM 1429 O PHE B 194 21.207 19.972 -4.702 1.00 20.08 O ANISOU 1429 O PHE B 194 2066 2291 3272 395 748 3 O ATOM 1430 CB PHE B 194 24.036 19.842 -5.897 1.00 17.74 C ANISOU 1430 CB PHE B 194 1997 2025 2717 348 557 53 C ATOM 1431 CG PHE B 194 25.239 20.185 -6.718 1.00 17.03 C ANISOU 1431 CG PHE B 194 1981 1938 2551 348 473 88 C ATOM 1432 CD1 PHE B 194 25.188 20.191 -8.104 1.00 17.02 C ANISOU 1432 CD1 PHE B 194 1944 1964 2559 372 362 160 C ATOM 1433 CD2 PHE B 194 26.450 20.453 -6.094 1.00 16.50 C ANISOU 1433 CD2 PHE B 194 2020 1859 2391 312 505 51 C ATOM 1434 CE1 PHE B 194 26.320 20.499 -8.855 1.00 16.50 C ANISOU 1434 CE1 PHE B 194 1949 1907 2415 363 302 191 C ATOM 1435 CE2 PHE B 194 27.589 20.754 -6.835 1.00 15.97 C ANISOU 1435 CE2 PHE B 194 2007 1801 2259 305 438 83 C ATOM 1436 CZ PHE B 194 27.524 20.779 -8.215 1.00 15.97 C ANISOU 1436 CZ PHE B 194 1973 1823 2271 331 346 152 C ATOM 1437 N ARG B 195 21.071 18.361 -6.272 1.00 19.66 N ANISOU 1437 N ARG B 195 1959 2345 3164 346 544 89 N ATOM 1438 CA ARG B 195 20.148 17.538 -5.503 1.00 20.95 C ANISOU 1438 CA ARG B 195 2059 2535 3367 299 622 56 C ATOM 1439 C ARG B 195 20.749 16.155 -5.222 1.00 20.25 C ANISOU 1439 C ARG B 195 2063 2485 3145 209 601 41 C ATOM 1440 O ARG B 195 21.670 15.712 -5.920 1.00 19.22 O ANISOU 1440 O ARG B 195 2010 2371 2920 193 503 61 O ATOM 1441 CB ARG B 195 18.785 17.428 -6.197 1.00 22.18 C ANISOU 1441 CB ARG B 195 2039 2721 3668 322 572 101 C ATOM 1442 CG ARG B 195 18.709 16.367 -7.269 1.00 23.23 C ANISOU 1442 CG ARG B 195 2153 2919 3755 267 428 141 C ATOM 1443 CD ARG B 195 17.268 15.930 -7.519 1.00 26.82 C ANISOU 1443 CD ARG B 195 2433 3417 4340 247 406 164 C ATOM 1444 NE ARG B 195 17.210 14.710 -8.329 1.00 28.15 N ANISOU 1444 NE ARG B 195 2607 3644 4446 162 287 177 N ATOM 1445 CZ ARG B 195 17.443 14.664 -9.641 1.00 29.32 C ANISOU 1445 CZ ARG B 195 2763 3829 4548 161 133 220 C ATOM 1446 NH1 ARG B 195 17.760 15.771 -10.319 1.00 28.93 N ANISOU 1446 NH1 ARG B 195 2716 3767 4508 242 73 273 N ATOM 1447 NH2 ARG B 195 17.368 13.504 -10.281 1.00 29.80 N ANISOU 1447 NH2 ARG B 195 2842 3935 4548 73 44 210 N ATOM 1448 N LEU B 196 20.231 15.486 -4.194 1.00 20.86 N ANISOU 1448 N LEU B 196 2134 2572 3221 152 701 8 N ATOM 1449 CA LEU B 196 20.723 14.166 -3.823 1.00 20.63 C ANISOU 1449 CA LEU B 196 2194 2562 3082 69 688 6 C ATOM 1450 C LEU B 196 19.832 13.056 -4.366 1.00 21.12 C ANISOU 1450 C LEU B 196 2171 2654 3198 15 636 28 C ATOM 1451 O LEU B 196 18.673 12.926 -3.969 1.00 22.18 O ANISOU 1451 O LEU B 196 2197 2803 3428 -11 708 21 O ATOM 1452 CB LEU B 196 20.869 14.040 -2.303 1.00 21.06 C ANISOU 1452 CB LEU B 196 2325 2607 3068 21 823 -32 C ATOM 1453 CG LEU B 196 21.689 12.845 -1.798 1.00 20.99 C ANISOU 1453 CG LEU B 196 2440 2605 2930 -51 802 -17 C ATOM 1454 CD1 LEU B 196 23.173 12.975 -2.173 1.00 20.03 C ANISOU 1454 CD1 LEU B 196 2425 2476 2709 -22 711 -4 C ATOM 1455 CD2 LEU B 196 21.522 12.673 -0.293 1.00 21.19 C ANISOU 1455 CD2 LEU B 196 2525 2635 2891 -113 935 -39 C ATOM 1456 N ALA B 197 20.387 12.267 -5.281 1.00 20.51 N ANISOU 1456 N ALA B 197 2142 2587 3064 -9 519 47 N ATOM 1457 CA ALA B 197 19.708 11.098 -5.818 1.00 21.19 C ANISOU 1457 CA ALA B 197 2178 2691 3181 -79 462 55 C ATOM 1458 C ALA B 197 19.471 10.072 -4.707 1.00 21.73 C ANISOU 1458 C ALA B 197 2288 2742 3229 -163 554 45 C ATOM 1459 O ALA B 197 20.310 9.902 -3.816 1.00 21.35 O ANISOU 1459 O ALA B 197 2358 2668 3088 -171 610 42 O ATOM 1460 CB ALA B 197 20.524 10.494 -6.939 1.00 20.47 C ANISOU 1460 CB ALA B 197 2161 2602 3014 -87 338 58 C ATOM 1461 N LYS B 198 18.330 9.392 -4.763 1.00 22.78 N ANISOU 1461 N LYS B 198 2321 2890 3445 -232 565 47 N ATOM 1462 CA LYS B 198 17.943 8.463 -3.699 1.00 23.53 C ANISOU 1462 CA LYS B 198 2443 2965 3531 -323 666 49 C ATOM 1463 C LYS B 198 18.897 7.272 -3.548 1.00 23.05 C ANISOU 1463 C LYS B 198 2538 2853 3366 -373 632 62 C ATOM 1464 O LYS B 198 19.185 6.849 -2.425 1.00 23.30 O ANISOU 1464 O LYS B 198 2657 2859 3337 -413 716 79 O ATOM 1465 CB LYS B 198 16.496 7.991 -3.874 1.00 24.76 C ANISOU 1465 CB LYS B 198 2444 3151 3812 -398 682 50 C ATOM 1466 CG LYS B 198 15.459 9.080 -3.651 1.00 25.90 C ANISOU 1466 CG LYS B 198 2421 3339 4081 -348 758 44 C ATOM 1467 CD LYS B 198 14.059 8.502 -3.731 1.00 29.32 C ANISOU 1467 CD LYS B 198 2687 3808 4645 -433 779 50 C ATOM 1468 CE LYS B 198 12.986 9.526 -3.387 1.00 31.13 C ANISOU 1468 CE LYS B 198 2730 4077 5020 -377 877 43 C ATOM 1469 NZ LYS B 198 12.588 10.348 -4.562 1.00 31.97 N ANISOU 1469 NZ LYS B 198 2698 4218 5231 -291 750 67 N ATOM 1470 N HIS B 199 19.393 6.750 -4.668 1.00 22.50 N ANISOU 1470 N HIS B 199 2504 2766 3277 -368 511 55 N ATOM 1471 CA HIS B 199 20.228 5.549 -4.660 1.00 22.25 C ANISOU 1471 CA HIS B 199 2605 2670 3179 -406 479 62 C ATOM 1472 C HIS B 199 21.242 5.585 -5.801 1.00 21.62 C ANISOU 1472 C HIS B 199 2584 2583 3048 -346 372 41 C ATOM 1473 O HIS B 199 20.923 6.039 -6.902 1.00 21.88 O ANISOU 1473 O HIS B 199 2547 2659 3107 -326 296 20 O ATOM 1474 CB HIS B 199 19.345 4.305 -4.783 1.00 23.26 C ANISOU 1474 CB HIS B 199 2705 2764 3370 -519 477 59 C ATOM 1475 CG HIS B 199 20.016 3.036 -4.351 1.00 23.16 C ANISOU 1475 CG HIS B 199 2830 2659 3311 -565 487 81 C ATOM 1476 ND1 HIS B 199 21.022 2.438 -5.080 1.00 21.86 N ANISOU 1476 ND1 HIS B 199 2763 2438 3106 -532 409 62 N ATOM 1477 CD2 HIS B 199 19.809 2.243 -3.273 1.00 23.29 C ANISOU 1477 CD2 HIS B 199 2900 2624 3323 -639 568 125 C ATOM 1478 CE1 HIS B 199 21.419 1.343 -4.459 1.00 22.39 C ANISOU 1478 CE1 HIS B 199 2934 2412 3159 -573 439 96 C ATOM 1479 NE2 HIS B 199 20.699 1.201 -3.361 1.00 23.13 N ANISOU 1479 NE2 HIS B 199 3010 2510 3270 -642 529 142 N ATOM 1480 N PHE B 200 22.452 5.091 -5.543 1.00 19.17 N ANISOU 1480 N PHE B 200 3204 1840 2241 -159 152 -3 N ATOM 1481 CA PHE B 200 23.539 5.158 -6.527 1.00 18.53 C ANISOU 1481 CA PHE B 200 3086 1729 2226 -222 68 -33 C ATOM 1482 C PHE B 200 23.269 4.369 -7.814 1.00 18.33 C ANISOU 1482 C PHE B 200 2943 1745 2278 -273 69 3 C ATOM 1483 O PHE B 200 23.697 4.778 -8.901 1.00 18.08 O ANISOU 1483 O PHE B 200 2859 1711 2300 -300 35 -9 O ATOM 1484 CB PHE B 200 24.898 4.794 -5.897 1.00 18.21 C ANISOU 1484 CB PHE B 200 3103 1663 2155 -251 -17 -70 C ATOM 1485 CG PHE B 200 25.199 3.321 -5.877 1.00 17.88 C ANISOU 1485 CG PHE B 200 3029 1644 2120 -277 -35 -39 C ATOM 1486 CD1 PHE B 200 24.713 2.508 -4.856 1.00 18.16 C ANISOU 1486 CD1 PHE B 200 3112 1690 2097 -253 4 -4 C ATOM 1487 CD2 PHE B 200 25.986 2.745 -6.876 1.00 17.11 C ANISOU 1487 CD2 PHE B 200 2865 1555 2081 -316 -88 -41 C ATOM 1488 CE1 PHE B 200 24.998 1.141 -4.836 1.00 17.53 C ANISOU 1488 CE1 PHE B 200 3027 1609 2025 -275 -15 29 C ATOM 1489 CE2 PHE B 200 26.273 1.380 -6.864 1.00 16.53 C ANISOU 1489 CE2 PHE B 200 2789 1484 2009 -321 -103 -17 C ATOM 1490 CZ PHE B 200 25.779 0.580 -5.841 1.00 16.86 C ANISOU 1490 CZ PHE B 200 2891 1515 1999 -303 -70 19 C ATOM 1491 N LEU B 201 22.556 3.250 -7.694 1.00 18.76 N ANISOU 1491 N LEU B 201 2963 1836 2329 -293 107 49 N ATOM 1492 CA LEU B 201 22.202 2.450 -8.866 1.00 18.81 C ANISOU 1492 CA LEU B 201 2878 1872 2395 -351 102 76 C ATOM 1493 C LEU B 201 21.214 3.183 -9.767 1.00 19.25 C ANISOU 1493 C LEU B 201 2848 1983 2485 -342 145 102 C ATOM 1494 O LEU B 201 21.255 3.025 -10.987 1.00 19.01 O ANISOU 1494 O LEU B 201 2746 1973 2502 -382 118 101 O ATOM 1495 CB LEU B 201 21.656 1.077 -8.470 1.00 19.07 C ANISOU 1495 CB LEU B 201 2916 1915 2416 -395 123 122 C ATOM 1496 CG LEU B 201 22.665 0.041 -7.962 1.00 18.91 C ANISOU 1496 CG LEU B 201 2971 1837 2377 -406 70 107 C ATOM 1497 CD1 LEU B 201 21.939 -1.205 -7.492 1.00 19.65 C ANISOU 1497 CD1 LEU B 201 3088 1924 2455 -454 102 167 C ATOM 1498 CD2 LEU B 201 23.691 -0.316 -9.035 1.00 18.08 C ANISOU 1498 CD2 LEU B 201 2846 1706 2316 -423 1 67 C ATOM 1499 N GLU B 202 20.341 3.985 -9.158 1.00 20.25 N ANISOU 1499 N GLU B 202 2982 2138 2573 -277 212 126 N ATOM 1500 CA GLU B 202 19.423 4.850 -9.894 1.00 20.93 C ANISOU 1500 CA GLU B 202 2993 2280 2679 -236 258 157 C ATOM 1501 C GLU B 202 20.219 5.822 -10.759 1.00 20.73 C ANISOU 1501 C GLU B 202 2979 2204 2692 -226 210 117 C ATOM 1502 O GLU B 202 19.953 5.974 -11.952 1.00 20.30 O ANISOU 1502 O GLU B 202 2839 2192 2682 -245 202 138 O ATOM 1503 CB GLU B 202 18.534 5.615 -8.910 1.00 21.93 C ANISOU 1503 CB GLU B 202 3155 2436 2743 -131 342 183 C ATOM 1504 CG GLU B 202 17.870 6.874 -9.466 1.00 22.77 C ANISOU 1504 CG GLU B 202 3230 2567 2854 -40 387 201 C ATOM 1505 CD GLU B 202 17.658 7.942 -8.400 1.00 24.49 C ANISOU 1505 CD GLU B 202 3565 2742 2999 89 443 180 C ATOM 1506 OE1 GLU B 202 17.379 7.580 -7.230 1.00 25.45 O ANISOU 1506 OE1 GLU B 202 3733 2885 3051 124 486 187 O ATOM 1507 OE2 GLU B 202 17.761 9.144 -8.737 1.00 24.38 O ANISOU 1507 OE2 GLU B 202 3606 2668 2990 160 444 158 O ATOM 1508 N MET B 203 21.207 6.456 -10.132 1.00 21.09 N ANISOU 1508 N MET B 203 3131 2166 2716 -207 173 64 N ATOM 1509 CA MET B 203 22.088 7.424 -10.769 1.00 21.26 C ANISOU 1509 CA MET B 203 3178 2130 2769 -218 122 33 C ATOM 1510 C MET B 203 22.880 6.803 -11.922 1.00 20.59 C ANISOU 1510 C MET B 203 3014 2072 2739 -295 62 31 C ATOM 1511 O MET B 203 23.048 7.422 -12.978 1.00 20.47 O ANISOU 1511 O MET B 203 2954 2064 2761 -306 48 43 O ATOM 1512 CB MET B 203 23.032 8.000 -9.708 1.00 21.82 C ANISOU 1512 CB MET B 203 3379 2115 2795 -214 80 -23 C ATOM 1513 CG MET B 203 24.202 8.825 -10.229 1.00 22.43 C ANISOU 1513 CG MET B 203 3485 2134 2903 -266 7 -52 C ATOM 1514 SD MET B 203 23.697 10.279 -11.164 1.00 24.40 S ANISOU 1514 SD MET B 203 3742 2341 3188 -228 36 -26 S ATOM 1515 CE MET B 203 22.599 11.093 -9.998 1.00 24.30 C ANISOU 1515 CE MET B 203 3857 2274 3102 -101 115 -39 C ATOM 1516 N LEU B 204 23.366 5.583 -11.703 1.00 20.36 N ANISOU 1516 N LEU B 204 2977 2055 2705 -337 31 19 N ATOM 1517 CA LEU B 204 24.086 4.823 -12.722 1.00 19.99 C ANISOU 1517 CA LEU B 204 2868 2035 2693 -386 -18 13 C ATOM 1518 C LEU B 204 23.180 4.512 -13.918 1.00 19.95 C ANISOU 1518 C LEU B 204 2770 2093 2719 -403 7 44 C ATOM 1519 O LEU B 204 23.568 4.727 -15.063 1.00 19.69 O ANISOU 1519 O LEU B 204 2682 2088 2712 -419 -18 44 O ATOM 1520 CB LEU B 204 24.655 3.531 -12.109 1.00 19.94 C ANISOU 1520 CB LEU B 204 2896 2016 2665 -402 -47 -3 C ATOM 1521 CG LEU B 204 25.512 2.557 -12.926 1.00 19.45 C ANISOU 1521 CG LEU B 204 2801 1970 2620 -423 -95 -18 C ATOM 1522 CD1 LEU B 204 26.364 1.753 -11.982 1.00 19.98 C ANISOU 1522 CD1 LEU B 204 2931 2007 2653 -407 -128 -32 C ATOM 1523 CD2 LEU B 204 24.674 1.621 -13.789 1.00 18.96 C ANISOU 1523 CD2 LEU B 204 2697 1931 2575 -452 -77 -4 C ATOM 1524 N ILE B 205 21.980 4.008 -13.643 1.00 20.46 N ANISOU 1524 N ILE B 205 2812 2192 2772 -405 54 76 N ATOM 1525 CA ILE B 205 21.013 3.677 -14.691 1.00 21.01 C ANISOU 1525 CA ILE B 205 2786 2336 2860 -436 69 110 C ATOM 1526 C ILE B 205 20.507 4.932 -15.424 1.00 21.52 C ANISOU 1526 C ILE B 205 2794 2444 2939 -391 95 141 C ATOM 1527 O ILE B 205 20.376 4.927 -16.645 1.00 21.45 O ANISOU 1527 O ILE B 205 2712 2489 2949 -413 76 153 O ATOM 1528 CB ILE B 205 19.826 2.848 -14.130 1.00 21.49 C ANISOU 1528 CB ILE B 205 2824 2440 2903 -469 110 152 C ATOM 1529 CG1 ILE B 205 20.334 1.541 -13.513 1.00 21.52 C ANISOU 1529 CG1 ILE B 205 2899 2384 2895 -518 81 132 C ATOM 1530 CG2 ILE B 205 18.816 2.545 -15.222 1.00 21.38 C ANISOU 1530 CG2 ILE B 205 2701 2518 2904 -520 112 190 C ATOM 1531 CD1 ILE B 205 19.353 0.876 -12.562 1.00 22.17 C ANISOU 1531 CD1 ILE B 205 2987 2488 2950 -549 128 183 C ATOM 1532 N MET B 206 20.250 6.004 -14.676 1.00 22.33 N ANISOU 1532 N MET B 206 2943 2517 3024 -318 136 153 N ATOM 1533 CA MET B 206 19.787 7.270 -15.245 1.00 23.08 C ANISOU 1533 CA MET B 206 3013 2629 3128 -253 165 186 C ATOM 1534 C MET B 206 20.823 7.954 -16.140 1.00 23.26 C ANISOU 1534 C MET B 206 3047 2609 3180 -270 117 170 C ATOM 1535 O MET B 206 20.553 9.014 -16.724 1.00 23.72 O ANISOU 1535 O MET B 206 3096 2667 3248 -222 134 204 O ATOM 1536 CB MET B 206 19.344 8.223 -14.136 1.00 23.74 C ANISOU 1536 CB MET B 206 3180 2665 3174 -157 222 191 C ATOM 1537 CG MET B 206 18.016 7.848 -13.497 1.00 24.31 C ANISOU 1537 CG MET B 206 3202 2824 3210 -111 295 239 C ATOM 1538 SD MET B 206 16.669 7.814 -14.684 1.00 24.00 S ANISOU 1538 SD MET B 206 2993 2940 3186 -99 327 324 S ATOM 1539 CE MET B 206 16.512 9.559 -15.039 1.00 25.39 C ANISOU 1539 CE MET B 206 3214 3074 3359 39 362 347 C ATOM 1540 N SER B 207 22.003 7.342 -16.248 1.00 23.17 N ANISOU 1540 N SER B 207 3054 2571 3180 -333 59 128 N ATOM 1541 CA SER B 207 23.029 7.789 -17.187 1.00 23.43 C ANISOU 1541 CA SER B 207 3069 2599 3236 -363 15 125 C ATOM 1542 C SER B 207 22.553 7.651 -18.625 1.00 23.43 C ANISOU 1542 C SER B 207 2967 2688 3248 -370 16 161 C ATOM 1543 O SER B 207 23.063 8.319 -19.524 1.00 23.40 O ANISOU 1543 O SER B 207 2938 2697 3257 -375 0 183 O ATOM 1544 CB SER B 207 24.315 6.990 -16.994 1.00 23.08 C ANISOU 1544 CB SER B 207 3040 2540 3189 -412 -40 82 C ATOM 1545 OG SER B 207 24.887 7.277 -15.731 1.00 24.23 O ANISOU 1545 OG SER B 207 3277 2612 3317 -410 -54 53 O ATOM 1546 N TYR B 208 21.570 6.777 -18.828 1.00 23.88 N ANISOU 1546 N TYR B 208 2966 2814 3294 -380 32 170 N ATOM 1547 CA TYR B 208 21.044 6.481 -20.150 1.00 24.21 C ANISOU 1547 CA TYR B 208 2913 2952 3332 -399 22 195 C ATOM 1548 C TYR B 208 22.209 6.307 -21.123 1.00 23.95 C ANISOU 1548 C TYR B 208 2868 2932 3301 -426 -23 171 C ATOM 1549 O TYR B 208 22.271 6.976 -22.162 1.00 24.25 O ANISOU 1549 O TYR B 208 2858 3019 3339 -411 -25 207 O ATOM 1550 CB TYR B 208 20.104 7.598 -20.625 1.00 24.80 C ANISOU 1550 CB TYR B 208 2938 3077 3409 -337 61 262 C ATOM 1551 CG TYR B 208 18.812 7.748 -19.848 1.00 25.86 C ANISOU 1551 CG TYR B 208 3053 3242 3529 -289 116 300 C ATOM 1552 CD1 TYR B 208 18.111 6.630 -19.375 1.00 26.30 C ANISOU 1552 CD1 TYR B 208 3074 3347 3571 -338 121 295 C ATOM 1553 CD2 TYR B 208 18.266 9.011 -19.616 1.00 26.77 C ANISOU 1553 CD2 TYR B 208 3187 3344 3642 -189 166 349 C ATOM 1554 CE1 TYR B 208 16.913 6.770 -18.674 1.00 26.75 C ANISOU 1554 CE1 TYR B 208 3093 3461 3610 -294 179 345 C ATOM 1555 CE2 TYR B 208 17.069 9.162 -18.917 1.00 27.56 C ANISOU 1555 CE2 TYR B 208 3258 3494 3718 -120 227 391 C ATOM 1556 CZ TYR B 208 16.401 8.039 -18.453 1.00 27.44 C ANISOU 1556 CZ TYR B 208 3186 3552 3688 -175 235 393 C ATOM 1557 OH TYR B 208 15.224 8.190 -17.765 1.00 28.48 O ANISOU 1557 OH TYR B 208 3271 3760 3791 -108 302 448 O ATOM 1558 N SER B 209 23.135 5.416 -20.767 1.00 23.35 N ANISOU 1558 N SER B 209 2833 2818 3219 -453 -54 119 N ATOM 1559 CA SER B 209 24.355 5.199 -21.545 1.00 22.96 C ANISOU 1559 CA SER B 209 2770 2794 3161 -459 -89 99 C ATOM 1560 C SER B 209 24.061 4.838 -22.997 1.00 23.07 C ANISOU 1560 C SER B 209 2716 2900 3149 -465 -101 104 C ATOM 1561 O SER B 209 24.903 5.037 -23.877 1.00 23.23 O ANISOU 1561 O SER B 209 2704 2968 3154 -453 -114 110 O ATOM 1562 CB SER B 209 25.212 4.117 -20.903 1.00 22.77 C ANISOU 1562 CB SER B 209 2798 2728 3124 -465 -115 46 C ATOM 1563 OG SER B 209 25.672 4.530 -19.636 1.00 22.86 O ANISOU 1563 OG SER B 209 2868 2671 3148 -460 -115 43 O ATOM 1564 N PHE B 210 22.856 4.326 -23.231 1.00 22.88 N ANISOU 1564 N PHE B 210 2667 2912 3113 -487 -97 105 N ATOM 1565 CA PHE B 210 22.400 3.962 -24.561 1.00 23.00 C ANISOU 1565 CA PHE B 210 2625 3021 3092 -503 -118 105 C ATOM 1566 C PHE B 210 22.191 5.156 -25.493 1.00 23.28 C ANISOU 1566 C PHE B 210 2589 3132 3124 -469 -103 171 C ATOM 1567 O PHE B 210 22.223 4.986 -26.705 1.00 23.80 O ANISOU 1567 O PHE B 210 2610 3283 3148 -470 -123 172 O ATOM 1568 CB PHE B 210 21.095 3.162 -24.468 1.00 23.20 C ANISOU 1568 CB PHE B 210 2634 3074 3106 -558 -127 100 C ATOM 1569 CG PHE B 210 19.971 3.905 -23.800 1.00 23.01 C ANISOU 1569 CG PHE B 210 2567 3071 3107 -547 -86 164 C ATOM 1570 CD1 PHE B 210 19.197 4.823 -24.513 1.00 23.07 C ANISOU 1570 CD1 PHE B 210 2487 3172 3106 -514 -70 231 C ATOM 1571 CD2 PHE B 210 19.676 3.682 -22.460 1.00 22.74 C ANISOU 1571 CD2 PHE B 210 2577 2970 3093 -554 -59 164 C ATOM 1572 CE1 PHE B 210 18.158 5.511 -23.898 1.00 23.07 C ANISOU 1572 CE1 PHE B 210 2446 3201 3120 -475 -24 294 C ATOM 1573 CE2 PHE B 210 18.634 4.360 -21.837 1.00 22.74 C ANISOU 1573 CE2 PHE B 210 2535 3003 3101 -523 -11 225 C ATOM 1574 CZ PHE B 210 17.874 5.279 -22.558 1.00 23.28 C ANISOU 1574 CZ PHE B 210 2515 3166 3163 -477 8 289 C ATOM 1575 N VAL B 211 21.965 6.349 -24.939 1.00 23.27 N ANISOU 1575 N VAL B 211 2589 3095 3156 -435 -67 227 N ATOM 1576 CA VAL B 211 21.501 7.490 -25.744 1.00 23.61 C ANISOU 1576 CA VAL B 211 2578 3197 3196 -394 -49 304 C ATOM 1577 C VAL B 211 22.363 7.736 -26.979 1.00 23.80 C ANISOU 1577 C VAL B 211 2569 3280 3193 -391 -66 322 C ATOM 1578 O VAL B 211 21.850 7.764 -28.097 1.00 24.17 O ANISOU 1578 O VAL B 211 2551 3433 3201 -381 -76 353 O ATOM 1579 CB VAL B 211 21.331 8.797 -24.912 1.00 23.81 C ANISOU 1579 CB VAL B 211 2650 3138 3260 -343 -7 354 C ATOM 1580 CG1 VAL B 211 21.046 9.999 -25.820 1.00 23.95 C ANISOU 1580 CG1 VAL B 211 2633 3195 3273 -291 10 440 C ATOM 1581 CG2 VAL B 211 20.210 8.641 -23.914 1.00 23.74 C ANISOU 1581 CG2 VAL B 211 2649 3116 3258 -320 24 355 C ATOM 1582 N HIS B 212 23.666 7.902 -26.781 1.00 23.65 N ANISOU 1582 N HIS B 212 2586 3213 3188 -401 -72 309 N ATOM 1583 CA HIS B 212 24.553 8.211 -27.903 1.00 24.10 C ANISOU 1583 CA HIS B 212 2600 3342 3215 -398 -78 342 C ATOM 1584 C HIS B 212 24.770 7.032 -28.872 1.00 23.98 C ANISOU 1584 C HIS B 212 2552 3426 3134 -396 -103 288 C ATOM 1585 O HIS B 212 24.688 7.225 -30.089 1.00 24.51 O ANISOU 1585 O HIS B 212 2565 3596 3152 -377 -104 324 O ATOM 1586 CB HIS B 212 25.863 8.847 -27.423 1.00 24.21 C ANISOU 1586 CB HIS B 212 2643 3296 3260 -420 -77 363 C ATOM 1587 CG HIS B 212 25.671 10.176 -26.759 1.00 25.11 C ANISOU 1587 CG HIS B 212 2808 3308 3423 -425 -59 419 C ATOM 1588 ND1 HIS B 212 25.959 10.393 -25.429 1.00 25.55 N ANISOU 1588 ND1 HIS B 212 2943 3249 3518 -447 -64 388 N ATOM 1589 CD2 HIS B 212 25.202 11.353 -27.240 1.00 26.17 C ANISOU 1589 CD2 HIS B 212 2944 3431 3568 -403 -38 503 C ATOM 1590 CE1 HIS B 212 25.689 11.650 -25.122 1.00 26.06 C ANISOU 1590 CE1 HIS B 212 3065 3225 3611 -440 -48 440 C ATOM 1591 NE2 HIS B 212 25.229 12.254 -26.203 1.00 26.16 N ANISOU 1591 NE2 HIS B 212 3035 3293 3611 -410 -30 514 N ATOM 1592 N PRO B 213 25.047 5.817 -28.347 1.00 23.46 N ANISOU 1592 N PRO B 213 2531 3324 3059 -407 -123 203 N ATOM 1593 CA PRO B 213 24.955 4.609 -29.181 1.00 23.76 C ANISOU 1593 CA PRO B 213 2574 3425 3030 -401 -151 137 C ATOM 1594 C PRO B 213 23.645 4.490 -29.979 1.00 24.19 C ANISOU 1594 C PRO B 213 2590 3554 3047 -423 -169 146 C ATOM 1595 O PRO B 213 23.678 4.083 -31.142 1.00 24.78 O ANISOU 1595 O PRO B 213 2646 3722 3048 -410 -190 124 O ATOM 1596 CB PRO B 213 25.071 3.473 -28.163 1.00 23.38 C ANISOU 1596 CB PRO B 213 2606 3281 2997 -417 -167 59 C ATOM 1597 CG PRO B 213 25.904 4.054 -27.080 1.00 22.95 C ANISOU 1597 CG PRO B 213 2570 3155 2997 -410 -149 83 C ATOM 1598 CD PRO B 213 25.521 5.497 -26.987 1.00 22.89 C ANISOU 1598 CD PRO B 213 2523 3145 3030 -419 -124 164 C ATOM 1599 N ALA B 214 22.515 4.848 -29.372 1.00 24.07 N ANISOU 1599 N ALA B 214 2559 3515 3072 -449 -162 179 N ATOM 1600 CA ALA B 214 21.229 4.815 -30.065 1.00 24.89 C ANISOU 1600 CA ALA B 214 2601 3714 3141 -472 -182 204 C ATOM 1601 C ALA B 214 21.222 5.770 -31.260 1.00 25.55 C ANISOU 1601 C ALA B 214 2614 3908 3185 -426 -175 279 C ATOM 1602 O ALA B 214 20.933 5.361 -32.386 1.00 26.05 O ANISOU 1602 O ALA B 214 2644 4080 3174 -434 -209 265 O ATOM 1603 CB ALA B 214 20.088 5.141 -29.107 1.00 24.70 C ANISOU 1603 CB ALA B 214 2555 3664 3167 -488 -162 245 C ATOM 1604 N ILE B 215 21.569 7.030 -31.000 1.00 25.64 N ANISOU 1604 N ILE B 215 2616 3883 3242 -382 -132 359 N ATOM 1605 CA ILE B 215 21.568 8.088 -32.012 1.00 26.45 C ANISOU 1605 CA ILE B 215 2664 4068 3317 -337 -117 453 C ATOM 1606 C ILE B 215 22.478 7.761 -33.205 1.00 27.10 C ANISOU 1606 C ILE B 215 2730 4242 3326 -328 -131 438 C ATOM 1607 O ILE B 215 22.074 7.913 -34.362 1.00 27.84 O ANISOU 1607 O ILE B 215 2769 4459 3349 -307 -145 477 O ATOM 1608 CB ILE B 215 21.917 9.466 -31.374 1.00 26.28 C ANISOU 1608 CB ILE B 215 2673 3948 3364 -304 -72 534 C ATOM 1609 CG1 ILE B 215 20.776 9.914 -30.459 1.00 26.04 C ANISOU 1609 CG1 ILE B 215 2652 3863 3378 -277 -51 561 C ATOM 1610 CG2 ILE B 215 22.178 10.525 -32.442 1.00 26.71 C ANISOU 1610 CG2 ILE B 215 2692 4065 3391 -267 -56 637 C ATOM 1611 CD1 ILE B 215 21.080 11.124 -29.639 1.00 25.73 C ANISOU 1611 CD1 ILE B 215 2683 3694 3401 -243 -12 612 C ATOM 1612 N LEU B 216 23.691 7.300 -32.916 1.00 27.13 N ANISOU 1612 N LEU B 216 2776 4198 3334 -335 -126 386 N ATOM 1613 CA LEU B 216 24.631 6.887 -33.954 1.00 27.94 C ANISOU 1613 CA LEU B 216 2861 4396 3357 -308 -129 368 C ATOM 1614 C LEU B 216 24.094 5.717 -34.769 1.00 28.71 C ANISOU 1614 C LEU B 216 2971 4575 3363 -308 -173 283 C ATOM 1615 O LEU B 216 24.290 5.664 -35.981 1.00 29.45 O ANISOU 1615 O LEU B 216 3034 4791 3364 -274 -178 292 O ATOM 1616 CB LEU B 216 25.981 6.506 -33.341 1.00 27.71 C ANISOU 1616 CB LEU B 216 2867 4311 3351 -302 -115 328 C ATOM 1617 CG LEU B 216 26.857 7.587 -32.709 1.00 27.19 C ANISOU 1617 CG LEU B 216 2789 4187 3355 -320 -84 407 C ATOM 1618 CD1 LEU B 216 27.984 6.911 -31.980 1.00 26.96 C ANISOU 1618 CD1 LEU B 216 2787 4119 3340 -318 -86 349 C ATOM 1619 CD2 LEU B 216 27.396 8.562 -33.744 1.00 27.43 C ANISOU 1619 CD2 LEU B 216 2753 4316 3351 -308 -58 516 C ATOM 1620 N PHE B 217 23.425 4.784 -34.092 1.00 28.88 N ANISOU 1620 N PHE B 217 3044 4526 3404 -353 -206 200 N ATOM 1621 CA PHE B 217 22.807 3.625 -34.741 1.00 29.76 C ANISOU 1621 CA PHE B 217 3188 4685 3433 -384 -262 112 C ATOM 1622 C PHE B 217 21.598 4.027 -35.586 1.00 30.52 C ANISOU 1622 C PHE B 217 3210 4904 3483 -407 -293 163 C ATOM 1623 O PHE B 217 21.384 3.487 -36.670 1.00 31.39 O ANISOU 1623 O PHE B 217 3323 5114 3489 -411 -337 120 O ATOM 1624 CB PHE B 217 22.405 2.566 -33.702 1.00 29.46 C ANISOU 1624 CB PHE B 217 3230 4525 3438 -447 -290 28 C ATOM 1625 CG PHE B 217 21.796 1.329 -34.299 1.00 30.52 C ANISOU 1625 CG PHE B 217 3424 4680 3493 -502 -357 -68 C ATOM 1626 CD1 PHE B 217 22.605 0.285 -34.746 1.00 31.60 C ANISOU 1626 CD1 PHE B 217 3664 4787 3556 -466 -375 -171 C ATOM 1627 CD2 PHE B 217 20.414 1.206 -34.425 1.00 30.62 C ANISOU 1627 CD2 PHE B 217 3392 4743 3498 -591 -404 -54 C ATOM 1628 CE1 PHE B 217 22.043 -0.863 -35.313 1.00 32.50 C ANISOU 1628 CE1 PHE B 217 3864 4895 3590 -525 -446 -269 C ATOM 1629 CE2 PHE B 217 19.846 0.068 -34.988 1.00 31.74 C ANISOU 1629 CE2 PHE B 217 3596 4900 3563 -670 -480 -143 C ATOM 1630 CZ PHE B 217 20.660 -0.969 -35.431 1.00 32.69 C ANISOU 1630 CZ PHE B 217 3848 4963 3611 -641 -503 -257 C ATOM 1631 N GLY B 218 20.810 4.973 -35.083 1.00 30.50 N ANISOU 1631 N GLY B 218 3143 4898 3548 -413 -272 255 N ATOM 1632 CA GLY B 218 19.616 5.435 -35.785 1.00 31.52 C ANISOU 1632 CA GLY B 218 3183 5156 3636 -419 -298 323 C ATOM 1633 C GLY B 218 19.905 6.169 -37.085 1.00 32.40 C ANISOU 1633 C GLY B 218 3243 5398 3670 -356 -291 395 C ATOM 1634 O GLY B 218 19.018 6.314 -37.927 1.00 33.31 O ANISOU 1634 O GLY B 218 3289 5649 3717 -357 -328 435 O ATOM 1635 N ARG B 219 21.145 6.627 -37.244 1.00 32.29 N ANISOU 1635 N ARG B 219 3253 5355 3661 -305 -244 420 N ATOM 1636 CA ARG B 219 21.567 7.359 -38.434 1.00 33.28 C ANISOU 1636 CA ARG B 219 3331 5601 3712 -246 -225 504 C ATOM 1637 C ARG B 219 22.591 6.589 -39.286 1.00 33.80 C ANISOU 1637 C ARG B 219 3432 5734 3676 -220 -229 431 C ATOM 1638 O ARG B 219 22.657 6.778 -40.504 1.00 34.47 O ANISOU 1638 O ARG B 219 3481 5963 3655 -179 -234 469 O ATOM 1639 CB ARG B 219 22.104 8.743 -38.037 1.00 33.05 C ANISOU 1639 CB ARG B 219 3288 5506 3765 -211 -161 627 C ATOM 1640 CG ARG B 219 22.483 9.674 -39.204 1.00 34.57 C ANISOU 1640 CG ARG B 219 3431 5812 3893 -160 -134 747 C ATOM 1641 CD ARG B 219 21.308 9.937 -40.149 1.00 36.45 C ANISOU 1641 CD ARG B 219 3604 6192 4052 -129 -167 806 C ATOM 1642 NE ARG B 219 21.708 10.705 -41.328 1.00 38.19 N ANISOU 1642 NE ARG B 219 3785 6531 4194 -76 -143 919 N ATOM 1643 CZ ARG B 219 22.203 10.182 -42.450 1.00 39.00 C ANISOU 1643 CZ ARG B 219 3874 6774 4170 -56 -155 891 C ATOM 1644 NH1 ARG B 219 22.378 8.870 -42.572 1.00 38.63 N ANISOU 1644 NH1 ARG B 219 3865 6754 4059 -79 -194 742 N ATOM 1645 NH2 ARG B 219 22.531 10.980 -43.459 1.00 40.00 N ANISOU 1645 NH2 ARG B 219 3960 7012 4227 -7 -124 1014 N ATOM 1646 N TRP B 220 23.377 5.723 -38.646 1.00 33.57 N ANISOU 1646 N TRP B 220 3475 5610 3670 -229 -224 332 N ATOM 1647 CA TRP B 220 24.428 4.971 -39.339 1.00 34.39 C ANISOU 1647 CA TRP B 220 3619 5772 3676 -176 -216 262 C ATOM 1648 C TRP B 220 24.317 3.453 -39.167 1.00 34.98 C ANISOU 1648 C TRP B 220 3798 5785 3706 -194 -266 103 C ATOM 1649 O TRP B 220 25.242 2.716 -39.530 1.00 35.55 O ANISOU 1649 O TRP B 220 3929 5875 3704 -130 -254 30 O ATOM 1650 CB TRP B 220 25.817 5.429 -38.875 1.00 33.88 C ANISOU 1650 CB TRP B 220 3540 5670 3664 -138 -152 311 C ATOM 1651 CG TRP B 220 26.048 6.908 -38.936 1.00 33.59 C ANISOU 1651 CG TRP B 220 3426 5657 3680 -141 -106 465 C ATOM 1652 CD1 TRP B 220 26.285 7.740 -37.885 1.00 32.67 C ANISOU 1652 CD1 TRP B 220 3306 5422 3687 -180 -80 530 C ATOM 1653 CD2 TRP B 220 26.071 7.729 -40.110 1.00 34.44 C ANISOU 1653 CD2 TRP B 220 3467 5904 3714 -107 -85 576 C ATOM 1654 NE1 TRP B 220 26.455 9.027 -38.326 1.00 32.98 N ANISOU 1654 NE1 TRP B 220 3292 5501 3739 -179 -46 671 N ATOM 1655 CE2 TRP B 220 26.327 9.050 -39.689 1.00 34.08 C ANISOU 1655 CE2 TRP B 220 3387 5801 3761 -133 -45 709 C ATOM 1656 CE3 TRP B 220 25.898 7.476 -41.479 1.00 35.57 C ANISOU 1656 CE3 TRP B 220 3587 6214 3714 -57 -97 575 C ATOM 1657 CZ2 TRP B 220 26.414 10.119 -40.583 1.00 34.91 C ANISOU 1657 CZ2 TRP B 220 3436 5999 3828 -114 -15 852 C ATOM 1658 CZ3 TRP B 220 25.983 8.542 -42.369 1.00 36.25 C ANISOU 1658 CZ3 TRP B 220 3604 6413 3757 -31 -64 719 C ATOM 1659 CH2 TRP B 220 26.239 9.846 -41.915 1.00 35.96 C ANISOU 1659 CH2 TRP B 220 3535 6306 3822 -60 -22 860 C ATOM 1660 N GLY B 221 23.196 2.991 -38.614 1.00 35.14 N ANISOU 1660 N GLY B 221 3847 5737 3768 -278 -319 57 N ATOM 1661 CA GLY B 221 22.993 1.568 -38.323 1.00 35.86 C ANISOU 1661 CA GLY B 221 4054 5739 3833 -323 -373 -83 C ATOM 1662 C GLY B 221 23.090 0.674 -39.544 1.00 37.46 C ANISOU 1662 C GLY B 221 4330 6022 3880 -293 -419 -182 C ATOM 1663 O GLY B 221 23.952 -0.207 -39.611 1.00 38.05 O ANISOU 1663 O GLY B 221 4511 6044 3901 -231 -411 -278 O ATOM 1664 N SER B 222 22.207 0.912 -40.509 1.00 38.40 N ANISOU 1664 N SER B 222 4399 6274 3918 -328 -468 -159 N ATOM 1665 CA SER B 222 22.178 0.151 -41.757 1.00 40.04 C ANISOU 1665 CA SER B 222 4680 6575 3959 -307 -522 -255 C ATOM 1666 C SER B 222 22.779 0.947 -42.923 1.00 40.56 C ANISOU 1666 C SER B 222 4672 6817 3923 -198 -476 -178 C ATOM 1667 O SER B 222 22.419 0.745 -44.089 1.00 41.70 O ANISOU 1667 O SER B 222 4828 7093 3923 -188 -525 -210 O ATOM 1668 CB SER B 222 20.748 -0.314 -42.063 1.00 41.03 C ANISOU 1668 CB SER B 222 4809 6738 4042 -439 -628 -296 C ATOM 1669 OG SER B 222 19.790 0.547 -41.465 1.00 40.55 O ANISOU 1669 OG SER B 222 4615 6703 4089 -507 -627 -178 O ATOM 1670 N TRP B 223 23.710 1.838 -42.579 1.00 39.78 N ANISOU 1670 N TRP B 223 4501 6720 3895 -125 -386 -73 N ATOM 1671 CA TRP B 223 24.411 2.716 -43.524 1.00 40.22 C ANISOU 1671 CA TRP B 223 4473 6932 3876 -32 -325 31 C ATOM 1672 C TRP B 223 25.021 1.932 -44.687 1.00 41.47 C ANISOU 1672 C TRP B 223 4706 7200 3849 63 -329 -61 C ATOM 1673 O TRP B 223 25.930 1.123 -44.502 1.00 41.58 O ANISOU 1673 O TRP B 223 4807 7157 3833 135 -302 -153 O ATOM 1674 CB TRP B 223 25.474 3.524 -42.763 1.00 39.37 C ANISOU 1674 CB TRP B 223 4306 6772 3883 5 -237 132 C ATOM 1675 CG TRP B 223 26.378 4.391 -43.599 1.00 40.23 C ANISOU 1675 CG TRP B 223 4329 7028 3929 85 -166 252 C ATOM 1676 CD1 TRP B 223 26.003 5.384 -44.463 1.00 40.87 C ANISOU 1676 CD1 TRP B 223 4325 7241 3962 92 -156 379 C ATOM 1677 CD2 TRP B 223 27.813 4.365 -43.616 1.00 40.68 C ANISOU 1677 CD2 TRP B 223 4368 7124 3965 166 -93 274 C ATOM 1678 NE1 TRP B 223 27.114 5.965 -45.029 1.00 41.27 N ANISOU 1678 NE1 TRP B 223 4313 7403 3963 161 -80 478 N ATOM 1679 CE2 TRP B 223 28.238 5.361 -44.529 1.00 41.12 C ANISOU 1679 CE2 TRP B 223 4324 7340 3959 204 -40 418 C ATOM 1680 CE3 TRP B 223 28.782 3.591 -42.956 1.00 40.41 C ANISOU 1680 CE3 TRP B 223 4384 7017 3952 214 -67 195 C ATOM 1681 CZ2 TRP B 223 29.592 5.603 -44.803 1.00 41.54 C ANISOU 1681 CZ2 TRP B 223 4315 7494 3973 275 38 488 C ATOM 1682 CZ3 TRP B 223 30.133 3.831 -43.230 1.00 40.79 C ANISOU 1682 CZ3 TRP B 223 4366 7174 3959 299 10 262 C ATOM 1683 CH2 TRP B 223 30.522 4.832 -44.146 1.00 41.48 C ANISOU 1683 CH2 TRP B 223 4342 7431 3987 322 62 409 C ATOM 1684 N ASP B 224 24.506 2.177 -45.888 1.00 42.55 N ANISOU 1684 N ASP B 224 4811 7501 3854 77 -361 -36 N ATOM 1685 CA ASP B 224 24.910 1.417 -47.076 1.00 44.01 C ANISOU 1685 CA ASP B 224 5082 7802 3838 167 -375 -135 C ATOM 1686 C ASP B 224 26.335 1.723 -47.555 1.00 44.21 C ANISOU 1686 C ASP B 224 5070 7933 3794 314 -269 -77 C ATOM 1687 O ASP B 224 26.741 1.285 -48.632 1.00 45.65 O ANISOU 1687 O ASP B 224 5303 8247 3794 416 -260 -132 O ATOM 1688 CB ASP B 224 23.883 1.589 -48.213 1.00 45.27 C ANISOU 1688 CB ASP B 224 5216 8121 3864 132 -451 -125 C ATOM 1689 CG ASP B 224 23.874 2.995 -48.808 1.00 45.38 C ANISOU 1689 CG ASP B 224 5075 8297 3870 168 -399 70 C ATOM 1690 OD1 ASP B 224 23.575 3.115 -50.016 1.00 46.48 O ANISOU 1690 OD1 ASP B 224 5200 8615 3847 206 -429 87 O ATOM 1691 OD2 ASP B 224 24.159 3.973 -48.082 1.00 44.23 O ANISOU 1691 OD2 ASP B 224 4835 8095 3874 158 -333 206 O ATOM 1692 N GLY B 225 27.085 2.468 -46.743 1.00 42.98 N ANISOU 1692 N GLY B 225 4825 7728 3778 319 -190 37 N ATOM 1693 CA GLY B 225 28.470 2.831 -47.053 1.00 43.05 C ANISOU 1693 CA GLY B 225 4768 7846 3743 433 -88 118 C ATOM 1694 C GLY B 225 28.613 4.109 -47.865 1.00 43.26 C ANISOU 1694 C GLY B 225 4659 8047 3732 446 -36 303 C ATOM 1695 O GLY B 225 29.716 4.641 -47.998 1.00 43.58 O ANISOU 1695 O GLY B 225 4614 8177 3767 504 51 411 O ATOM 1696 N LYS B 226 27.499 4.605 -48.400 1.00 43.19 N ANISOU 1696 N LYS B 226 4625 8089 3695 388 -92 350 N ATOM 1697 CA LYS B 226 27.508 5.778 -49.274 1.00 43.62 C ANISOU 1697 CA LYS B 226 4570 8308 3696 408 -51 528 C ATOM 1698 C LYS B 226 27.682 7.080 -48.492 1.00 42.13 C ANISOU 1698 C LYS B 226 4285 8036 3687 338 -2 704 C ATOM 1699 O LYS B 226 26.996 7.297 -47.489 1.00 41.08 O ANISOU 1699 O LYS B 226 4164 7740 3705 251 -40 697 O ATOM 1700 CB LYS B 226 26.237 5.832 -50.136 1.00 44.58 C ANISOU 1700 CB LYS B 226 4700 8526 3714 384 -133 521 C ATOM 1701 CG LYS B 226 26.108 4.694 -51.156 1.00 46.72 C ANISOU 1701 CG LYS B 226 5073 8910 3771 451 -185 362 C ATOM 1702 CD LYS B 226 27.147 4.789 -52.265 1.00 49.46 C ANISOU 1702 CD LYS B 226 5396 9458 3941 587 -103 412 C ATOM 1703 CE LYS B 226 27.209 3.503 -53.087 1.00 51.85 C ANISOU 1703 CE LYS B 226 5837 9832 4031 675 -146 219 C ATOM 1704 NZ LYS B 226 28.195 3.597 -54.216 1.00 53.67 N ANISOU 1704 NZ LYS B 226 6041 10283 4066 830 -57 270 N ATOM 1705 N PRO B 227 28.608 7.948 -48.949 1.00 42.20 N ANISOU 1705 N PRO B 227 4205 8157 3672 373 82 863 N ATOM 1706 CA PRO B 227 28.876 9.253 -48.337 1.00 41.14 C ANISOU 1706 CA PRO B 227 3996 7943 3690 299 126 1039 C ATOM 1707 C PRO B 227 27.688 10.226 -48.374 1.00 40.55 C ANISOU 1707 C PRO B 227 3908 7822 3675 246 87 1143 C ATOM 1708 O PRO B 227 26.799 10.100 -49.223 1.00 41.01 O ANISOU 1708 O PRO B 227 3973 7988 3623 280 40 1130 O ATOM 1709 CB PRO B 227 30.034 9.800 -49.178 1.00 42.33 C ANISOU 1709 CB PRO B 227 4060 8275 3749 350 215 1183 C ATOM 1710 CG PRO B 227 29.937 9.073 -50.471 1.00 43.81 C ANISOU 1710 CG PRO B 227 4268 8662 3716 462 211 1114 C ATOM 1711 CD PRO B 227 29.487 7.705 -50.108 1.00 43.62 C ANISOU 1711 CD PRO B 227 4356 8551 3666 485 141 885 C ATOM 1712 N VAL B 228 27.689 11.177 -47.441 1.00 39.27 N ANISOU 1712 N VAL B 228 3733 7504 3682 171 105 1242 N ATOM 1713 CA VAL B 228 26.674 12.233 -47.365 1.00 38.82 C ANISOU 1713 CA VAL B 228 3672 7385 3695 143 84 1359 C ATOM 1714 C VAL B 228 27.348 13.607 -47.495 1.00 39.15 C ANISOU 1714 C VAL B 228 3675 7413 3789 114 150 1568 C ATOM 1715 O VAL B 228 28.500 13.760 -47.101 1.00 39.02 O ANISOU 1715 O VAL B 228 3639 7364 3823 71 199 1602 O ATOM 1716 CB VAL B 228 25.811 12.134 -46.065 1.00 37.52 C ANISOU 1716 CB VAL B 228 3558 7016 3680 88 36 1277 C ATOM 1717 CG1 VAL B 228 24.978 10.856 -46.068 1.00 37.16 C ANISOU 1717 CG1 VAL B 228 3547 6996 3575 97 -38 1098 C ATOM 1718 CG2 VAL B 228 26.668 12.214 -44.800 1.00 36.30 C ANISOU 1718 CG2 VAL B 228 3432 6690 3670 24 66 1254 C ATOM 1719 N PRO B 229 26.640 14.606 -48.061 1.00 39.79 N ANISOU 1719 N PRO B 229 3745 7521 3853 135 150 1715 N ATOM 1720 CA PRO B 229 27.282 15.887 -48.392 1.00 40.58 C ANISOU 1720 CA PRO B 229 3823 7619 3978 107 212 1927 C ATOM 1721 C PRO B 229 28.003 16.557 -47.219 1.00 39.83 C ANISOU 1721 C PRO B 229 3764 7316 4055 3 239 1974 C ATOM 1722 O PRO B 229 29.112 17.068 -47.388 1.00 40.53 O ANISOU 1722 O PRO B 229 3817 7434 4149 -54 292 2089 O ATOM 1723 CB PRO B 229 26.111 16.755 -48.869 1.00 41.15 C ANISOU 1723 CB PRO B 229 3910 7693 4034 157 190 2047 C ATOM 1724 CG PRO B 229 25.105 15.785 -49.357 1.00 41.11 C ANISOU 1724 CG PRO B 229 3887 7817 3917 225 124 1915 C ATOM 1725 CD PRO B 229 25.212 14.608 -48.436 1.00 40.04 C ANISOU 1725 CD PRO B 229 3782 7595 3838 185 90 1704 C ATOM 1726 N GLU B 230 27.379 16.549 -46.047 1.00 38.47 N ANISOU 1726 N GLU B 230 3658 6945 4013 -26 201 1888 N ATOM 1727 CA GLU B 230 27.939 17.213 -44.874 1.00 37.90 C ANISOU 1727 CA GLU B 230 3641 6663 4098 -124 215 1919 C ATOM 1728 C GLU B 230 27.411 16.598 -43.586 1.00 36.20 C ANISOU 1728 C GLU B 230 3483 6288 3982 -137 172 1753 C ATOM 1729 O GLU B 230 26.399 15.890 -43.596 1.00 35.71 O ANISOU 1729 O GLU B 230 3422 6258 3886 -76 131 1646 O ATOM 1730 CB GLU B 230 27.634 18.714 -44.902 1.00 38.93 C ANISOU 1730 CB GLU B 230 3832 6668 4293 -144 234 2103 C ATOM 1731 CG GLU B 230 26.153 19.058 -45.028 1.00 39.69 C ANISOU 1731 CG GLU B 230 3969 6728 4383 -47 205 2120 C ATOM 1732 CD GLU B 230 25.795 20.352 -44.326 1.00 40.86 C ANISOU 1732 CD GLU B 230 4229 6645 4653 -63 215 2227 C ATOM 1733 OE1 GLU B 230 26.101 20.478 -43.118 1.00 40.18 O ANISOU 1733 OE1 GLU B 230 4215 6365 4685 -134 208 2162 O ATOM 1734 OE2 GLU B 230 25.201 21.237 -44.980 1.00 42.41 O ANISOU 1734 OE2 GLU B 230 4451 6848 4816 5 228 2374 O ATOM 1735 N ALA B 231 28.102 16.883 -42.485 1.00 35.37 N ANISOU 1735 N ALA B 231 3422 6021 3996 -226 177 1739 N ATOM 1736 CA ALA B 231 27.739 16.371 -41.169 1.00 33.71 C ANISOU 1736 CA ALA B 231 3271 5655 3882 -245 142 1595 C ATOM 1737 C ALA B 231 26.251 16.561 -40.886 1.00 33.26 C ANISOU 1737 C ALA B 231 3265 5521 3852 -178 116 1572 C ATOM 1738 O ALA B 231 25.758 17.693 -40.874 1.00 33.81 O ANISOU 1738 O ALA B 231 3388 5496 3963 -160 129 1688 O ATOM 1739 CB ALA B 231 28.578 17.043 -40.093 1.00 33.64 C ANISOU 1739 CB ALA B 231 3320 5471 3993 -352 148 1626 C ATOM 1740 N PRO B 232 25.523 15.447 -40.683 1.00 32.36 N ANISOU 1740 N PRO B 232 3134 5453 3709 -139 80 1428 N ATOM 1741 CA PRO B 232 24.101 15.526 -40.361 1.00 32.06 C ANISOU 1741 CA PRO B 232 3117 5372 3694 -83 55 1407 C ATOM 1742 C PRO B 232 23.882 15.940 -38.912 1.00 31.45 C ANISOU 1742 C PRO B 232 3125 5081 3744 -108 59 1375 C ATOM 1743 O PRO B 232 24.727 15.664 -38.052 1.00 30.81 O ANISOU 1743 O PRO B 232 3080 4902 3724 -177 60 1307 O ATOM 1744 CB PRO B 232 23.597 14.090 -40.578 1.00 31.42 C ANISOU 1744 CB PRO B 232 2990 5409 3538 -69 10 1260 C ATOM 1745 CG PRO B 232 24.755 13.312 -41.114 1.00 31.65 C ANISOU 1745 CG PRO B 232 2992 5538 3496 -92 17 1205 C ATOM 1746 CD PRO B 232 25.992 14.052 -40.746 1.00 31.77 C ANISOU 1746 CD PRO B 232 3023 5471 3576 -145 61 1284 C ATOM 1747 N LEU B 233 22.755 16.598 -38.653 1.00 31.74 N ANISOU 1747 N LEU B 233 3192 5058 3811 -41 61 1426 N ATOM 1748 CA LEU B 233 22.369 16.975 -37.301 1.00 31.28 C ANISOU 1748 CA LEU B 233 3219 4810 3853 -37 70 1391 C ATOM 1749 C LEU B 233 22.350 15.745 -36.399 1.00 30.15 C ANISOU 1749 C LEU B 233 3069 4653 3735 -81 44 1229 C ATOM 1750 O LEU B 233 22.033 14.640 -36.848 1.00 29.97 O ANISOU 1750 O LEU B 233 2973 4766 3647 -84 13 1151 O ATOM 1751 CB LEU B 233 20.999 17.652 -37.312 1.00 31.99 C ANISOU 1751 CB LEU B 233 3317 4896 3943 77 80 1464 C ATOM 1752 CG LEU B 233 20.925 19.034 -37.969 1.00 33.40 C ANISOU 1752 CG LEU B 233 3542 5034 4113 142 111 1636 C ATOM 1753 CD1 LEU B 233 19.502 19.343 -38.426 1.00 34.49 C ANISOU 1753 CD1 LEU B 233 3629 5274 4204 281 112 1710 C ATOM 1754 CD2 LEU B 233 21.453 20.126 -37.039 1.00 33.36 C ANISOU 1754 CD2 LEU B 233 3691 4779 4206 117 140 1677 C ATOM 1755 N PHE B 234 22.701 15.940 -35.131 1.00 29.63 N ANISOU 1755 N PHE B 234 3088 4414 3755 -120 53 1181 N ATOM 1756 CA PHE B 234 22.815 14.831 -34.187 1.00 28.51 C ANISOU 1756 CA PHE B 234 2952 4242 3639 -165 32 1041 C ATOM 1757 C PHE B 234 21.467 14.540 -33.543 1.00 28.21 C ANISOU 1757 C PHE B 234 2909 4195 3614 -109 30 999 C ATOM 1758 O PHE B 234 20.639 13.829 -34.121 1.00 28.10 O ANISOU 1758 O PHE B 234 2813 4323 3543 -86 7 978 O ATOM 1759 CB PHE B 234 23.876 15.146 -33.127 1.00 28.18 C ANISOU 1759 CB PHE B 234 2996 4039 3670 -236 37 1012 C ATOM 1760 CG PHE B 234 24.432 13.935 -32.440 1.00 27.30 C ANISOU 1760 CG PHE B 234 2877 3930 3567 -289 13 884 C ATOM 1761 CD1 PHE B 234 24.911 12.852 -33.178 1.00 27.21 C ANISOU 1761 CD1 PHE B 234 2793 4056 3491 -304 -4 831 C ATOM 1762 CD2 PHE B 234 24.517 13.891 -31.052 1.00 27.10 C ANISOU 1762 CD2 PHE B 234 2929 3763 3604 -315 10 819 C ATOM 1763 CE1 PHE B 234 25.442 11.724 -32.541 1.00 26.58 C ANISOU 1763 CE1 PHE B 234 2721 3964 3415 -335 -24 719 C ATOM 1764 CE2 PHE B 234 25.045 12.772 -30.404 1.00 26.71 C ANISOU 1764 CE2 PHE B 234 2877 3714 3558 -355 -12 712 C ATOM 1765 CZ PHE B 234 25.508 11.684 -31.153 1.00 26.27 C ANISOU 1765 CZ PHE B 234 2752 3787 3444 -363 -28 665 C ATOM 1766 N TYR B 235 21.268 15.109 -32.353 1.00 28.12 N ANISOU 1766 N TYR B 235 2986 4027 3671 -90 53 992 N ATOM 1767 CA TYR B 235 20.024 15.018 -31.594 1.00 28.01 C ANISOU 1767 CA TYR B 235 2972 4001 3672 -23 67 972 C ATOM 1768 C TYR B 235 18.822 15.438 -32.426 1.00 29.16 C ANISOU 1768 C TYR B 235 3039 4272 3769 77 76 1066 C ATOM 1769 O TYR B 235 17.835 14.707 -32.508 1.00 29.44 O ANISOU 1769 O TYR B 235 2982 4434 3770 93 60 1041 O ATOM 1770 CB TYR B 235 20.103 15.906 -30.354 1.00 27.94 C ANISOU 1770 CB TYR B 235 3093 3796 3727 8 100 974 C ATOM 1771 CG TYR B 235 21.234 15.573 -29.411 1.00 26.98 C ANISOU 1771 CG TYR B 235 3048 3554 3649 -89 84 886 C ATOM 1772 CD1 TYR B 235 22.356 16.390 -29.320 1.00 26.82 C ANISOU 1772 CD1 TYR B 235 3115 3414 3662 -147 79 918 C ATOM 1773 CD2 TYR B 235 21.178 14.439 -28.603 1.00 26.14 C ANISOU 1773 CD2 TYR B 235 2925 3459 3547 -128 69 779 C ATOM 1774 CE1 TYR B 235 23.396 16.084 -28.450 1.00 26.32 C ANISOU 1774 CE1 TYR B 235 3105 3263 3630 -239 55 844 C ATOM 1775 CE2 TYR B 235 22.209 14.123 -27.735 1.00 25.11 C ANISOU 1775 CE2 TYR B 235 2859 3232 3449 -205 51 707 C ATOM 1776 CZ TYR B 235 23.311 14.948 -27.664 1.00 25.66 C ANISOU 1776 CZ TYR B 235 3001 3202 3547 -258 42 738 C ATOM 1777 OH TYR B 235 24.325 14.629 -26.799 1.00 25.84 O ANISOU 1777 OH TYR B 235 3071 3152 3594 -337 16 671 O ATOM 1778 N GLN B 236 18.913 16.613 -33.044 1.00 30.21 N ANISOU 1778 N GLN B 236 3208 4374 3897 138 99 1182 N ATOM 1779 CA GLN B 236 17.839 17.137 -33.892 1.00 31.47 C ANISOU 1779 CA GLN B 236 3297 4657 4005 251 108 1292 C ATOM 1780 C GLN B 236 17.655 16.331 -35.182 1.00 31.62 C ANISOU 1780 C GLN B 236 3181 4898 3936 218 62 1294 C ATOM 1781 O GLN B 236 16.642 16.475 -35.871 1.00 32.49 O ANISOU 1781 O GLN B 236 3200 5155 3988 297 53 1367 O ATOM 1782 CB GLN B 236 18.073 18.620 -34.208 1.00 32.44 C ANISOU 1782 CB GLN B 236 3518 4665 4144 325 144 1423 C ATOM 1783 CG GLN B 236 17.943 19.530 -32.987 1.00 32.88 C ANISOU 1783 CG GLN B 236 3725 4501 4267 391 187 1426 C ATOM 1784 CD GLN B 236 17.887 21.007 -33.334 1.00 34.50 C ANISOU 1784 CD GLN B 236 4044 4586 4480 490 222 1563 C ATOM 1785 OE1 GLN B 236 18.227 21.419 -34.447 1.00 36.36 O ANISOU 1785 OE1 GLN B 236 4256 4876 4682 480 214 1663 O ATOM 1786 NE2 GLN B 236 17.461 21.816 -32.373 1.00 34.79 N ANISOU 1786 NE2 GLN B 236 4216 4449 4553 592 262 1570 N ATOM 1787 N GLY B 237 18.629 15.477 -35.487 1.00 30.97 N ANISOU 1787 N GLY B 237 3089 4844 3836 109 32 1212 N ATOM 1788 CA GLY B 237 18.618 14.683 -36.710 1.00 31.35 C ANISOU 1788 CA GLY B 237 3040 5084 3789 78 -12 1195 C ATOM 1789 C GLY B 237 18.010 13.297 -36.585 1.00 31.08 C ANISOU 1789 C GLY B 237 2939 5150 3719 21 -62 1079 C ATOM 1790 O GLY B 237 17.881 12.591 -37.583 1.00 31.32 O ANISOU 1790 O GLY B 237 2904 5335 3660 -7 -108 1051 O ATOM 1791 N ILE B 238 17.637 12.900 -35.369 1.00 30.70 N ANISOU 1791 N ILE B 238 2918 5012 3735 -1 -55 1010 N ATOM 1792 CA ILE B 238 17.025 11.582 -35.151 1.00 30.62 C ANISOU 1792 CA ILE B 238 2857 5078 3701 -73 -102 909 C ATOM 1793 C ILE B 238 15.686 11.475 -35.870 1.00 31.75 C ANISOU 1793 C ILE B 238 2876 5412 3773 -46 -140 964 C ATOM 1794 O ILE B 238 15.013 12.481 -36.103 1.00 32.70 O ANISOU 1794 O ILE B 238 2953 5585 3888 57 -113 1083 O ATOM 1795 CB ILE B 238 16.836 11.223 -33.637 1.00 29.80 C ANISOU 1795 CB ILE B 238 2802 4845 3676 -101 -80 844 C ATOM 1796 CG1 ILE B 238 15.791 12.127 -32.965 1.00 30.65 C ANISOU 1796 CG1 ILE B 238 2887 4940 3819 -2 -34 931 C ATOM 1797 CG2 ILE B 238 18.175 11.235 -32.901 1.00 28.66 C ANISOU 1797 CG2 ILE B 238 2770 4528 3591 -137 -57 784 C ATOM 1798 CD1 ILE B 238 15.068 11.484 -31.772 1.00 30.39 C ANISOU 1798 CD1 ILE B 238 2841 4884 3821 -30 -24 879 C ATOM 1799 N ASP B 239 15.314 10.253 -36.230 1.00 31.98 N ANISOU 1799 N ASP B 239 2858 5548 3746 -139 -206 880 N ATOM 1800 CA ASP B 239 13.999 9.994 -36.807 1.00 33.11 C ANISOU 1800 CA ASP B 239 2873 5886 3821 -148 -259 922 C ATOM 1801 C ASP B 239 13.102 9.340 -35.762 1.00 33.06 C ANISOU 1801 C ASP B 239 2826 5878 3859 -210 -267 886 C ATOM 1802 O ASP B 239 13.484 9.219 -34.592 1.00 32.23 O ANISOU 1802 O ASP B 239 2798 5613 3834 -223 -223 839 O ATOM 1803 CB ASP B 239 14.118 9.117 -38.058 1.00 33.71 C ANISOU 1803 CB ASP B 239 2926 6098 3785 -225 -341 858 C ATOM 1804 CG ASP B 239 14.949 7.859 -37.826 1.00 33.25 C ANISOU 1804 CG ASP B 239 2969 5938 3726 -333 -371 703 C ATOM 1805 OD1 ASP B 239 15.246 7.506 -36.658 1.00 32.08 O ANISOU 1805 OD1 ASP B 239 2887 5639 3664 -368 -341 646 O ATOM 1806 OD2 ASP B 239 15.310 7.219 -38.833 1.00 33.91 O ANISOU 1806 OD2 ASP B 239 3074 6097 3714 -372 -425 640 O ATOM 1807 N GLN B 240 11.916 8.913 -36.185 1.00 34.12 N ANISOU 1807 N GLN B 240 2832 6199 3933 -254 -325 915 N ATOM 1808 CA GLN B 240 10.962 8.286 -35.279 1.00 34.25 C ANISOU 1808 CA GLN B 240 2782 6251 3982 -327 -335 904 C ATOM 1809 C GLN B 240 11.478 6.951 -34.736 1.00 33.44 C ANISOU 1809 C GLN B 240 2776 6027 3902 -480 -371 762 C ATOM 1810 O GLN B 240 11.225 6.615 -33.580 1.00 33.07 O ANISOU 1810 O GLN B 240 2743 5903 3919 -517 -340 744 O ATOM 1811 CB GLN B 240 9.600 8.112 -35.961 1.00 35.82 C ANISOU 1811 CB GLN B 240 2803 6705 4102 -361 -402 978 C ATOM 1812 CG GLN B 240 8.449 7.841 -34.996 1.00 36.50 C ANISOU 1812 CG GLN B 240 2776 6870 4223 -399 -389 1024 C ATOM 1813 CD GLN B 240 8.226 8.973 -34.002 1.00 36.19 C ANISOU 1813 CD GLN B 240 2731 6766 4253 -223 -274 1120 C ATOM 1814 OE1 GLN B 240 7.848 10.085 -34.379 1.00 36.60 O ANISOU 1814 OE1 GLN B 240 2723 6899 4284 -61 -235 1237 O ATOM 1815 NE2 GLN B 240 8.456 8.689 -32.722 1.00 34.67 N ANISOU 1815 NE2 GLN B 240 2616 6423 4135 -247 -219 1070 N ATOM 1816 N ALA B 241 12.204 6.203 -35.568 1.00 33.35 N ANISOU 1816 N ALA B 241 2839 5999 3833 -554 -432 664 N ATOM 1817 CA ALA B 241 12.732 4.891 -35.176 1.00 32.79 C ANISOU 1817 CA ALA B 241 2881 5806 3772 -682 -471 527 C ATOM 1818 C ALA B 241 13.715 4.997 -34.007 1.00 31.38 C ANISOU 1818 C ALA B 241 2822 5414 3688 -640 -395 487 C ATOM 1819 O ALA B 241 13.705 4.158 -33.103 1.00 31.09 O ANISOU 1819 O ALA B 241 2842 5279 3693 -723 -399 424 O ATOM 1820 CB ALA B 241 13.378 4.182 -36.368 1.00 32.83 C ANISOU 1820 CB ALA B 241 2959 5836 3681 -729 -541 431 C ATOM 1821 N THR B 242 14.546 6.038 -34.030 1.00 30.65 N ANISOU 1821 N THR B 242 2765 5255 3624 -520 -331 530 N ATOM 1822 CA THR B 242 15.537 6.272 -32.985 1.00 29.46 C ANISOU 1822 CA THR B 242 2720 4918 3555 -482 -268 500 C ATOM 1823 C THR B 242 14.859 6.699 -31.690 1.00 29.34 C ANISOU 1823 C THR B 242 2683 4852 3613 -454 -214 551 C ATOM 1824 O THR B 242 15.288 6.302 -30.603 1.00 28.77 O ANISOU 1824 O THR B 242 2692 4646 3595 -481 -190 497 O ATOM 1825 CB THR B 242 16.570 7.323 -33.421 1.00 28.99 C ANISOU 1825 CB THR B 242 2698 4813 3503 -385 -225 545 C ATOM 1826 OG1 THR B 242 17.205 6.880 -34.623 1.00 29.59 O ANISOU 1826 OG1 THR B 242 2788 4957 3499 -403 -266 501 O ATOM 1827 CG2 THR B 242 17.632 7.532 -32.353 1.00 27.71 C ANISOU 1827 CG2 THR B 242 2639 4471 3418 -368 -175 511 C ATOM 1828 N ALA B 243 13.798 7.497 -31.812 1.00 30.03 N ANISOU 1828 N ALA B 243 2662 5057 3691 -386 -193 658 N ATOM 1829 CA ALA B 243 12.999 7.902 -30.655 1.00 29.98 C ANISOU 1829 CA ALA B 243 2621 5038 3734 -337 -136 714 C ATOM 1830 C ALA B 243 12.436 6.665 -29.963 1.00 30.01 C ANISOU 1830 C ALA B 243 2603 5054 3743 -466 -165 661 C ATOM 1831 O ALA B 243 12.610 6.493 -28.754 1.00 29.48 O ANISOU 1831 O ALA B 243 2601 4872 3728 -469 -121 635 O ATOM 1832 CB ALA B 243 11.882 8.854 -31.072 1.00 31.07 C ANISOU 1832 CB ALA B 243 2629 5334 3842 -229 -113 844 C ATOM 1833 N ASP B 244 11.790 5.802 -30.748 1.00 30.71 N ANISOU 1833 N ASP B 244 2612 5281 3774 -580 -244 646 N ATOM 1834 CA ASP B 244 11.255 4.528 -30.274 1.00 31.15 C ANISOU 1834 CA ASP B 244 2658 5349 3829 -737 -290 598 C ATOM 1835 C ASP B 244 12.327 3.659 -29.604 1.00 30.13 C ANISOU 1835 C ASP B 244 2695 5015 3738 -800 -291 483 C ATOM 1836 O ASP B 244 12.071 3.028 -28.570 1.00 30.01 O ANISOU 1836 O ASP B 244 2706 4938 3757 -869 -276 469 O ATOM 1837 CB ASP B 244 10.611 3.768 -31.438 1.00 32.36 C ANISOU 1837 CB ASP B 244 2733 5660 3901 -864 -395 582 C ATOM 1838 CG ASP B 244 9.383 4.476 -31.997 1.00 33.93 C ANISOU 1838 CG ASP B 244 2740 6096 4057 -817 -404 709 C ATOM 1839 OD1 ASP B 244 8.861 4.032 -33.043 1.00 34.99 O ANISOU 1839 OD1 ASP B 244 2798 6382 4113 -909 -496 706 O ATOM 1840 OD2 ASP B 244 8.936 5.475 -31.393 1.00 34.40 O ANISOU 1840 OD2 ASP B 244 2728 6192 4150 -681 -321 810 O ATOM 1841 N MET B 245 13.518 3.644 -30.206 1.00 29.30 N ANISOU 1841 N MET B 245 2694 4820 3618 -769 -306 411 N ATOM 1842 CA MET B 245 14.681 2.923 -29.691 1.00 28.32 C ANISOU 1842 CA MET B 245 2722 4518 3522 -794 -305 310 C ATOM 1843 C MET B 245 15.080 3.439 -28.309 1.00 27.17 C ANISOU 1843 C MET B 245 2627 4245 3450 -725 -227 329 C ATOM 1844 O MET B 245 15.352 2.653 -27.402 1.00 26.87 O ANISOU 1844 O MET B 245 2672 4098 3441 -778 -224 278 O ATOM 1845 CB MET B 245 15.846 3.056 -30.676 1.00 28.12 C ANISOU 1845 CB MET B 245 2761 4466 3458 -740 -321 258 C ATOM 1846 CG MET B 245 17.173 2.481 -30.201 1.00 28.19 C ANISOU 1846 CG MET B 245 2908 4313 3489 -729 -310 169 C ATOM 1847 SD MET B 245 17.289 0.697 -30.387 1.00 30.54 S ANISOU 1847 SD MET B 245 3319 4544 3740 -848 -386 46 S ATOM 1848 CE MET B 245 17.613 0.567 -32.142 1.00 31.14 C ANISOU 1848 CE MET B 245 3394 4730 3709 -829 -442 1 C ATOM 1849 N LEU B 246 15.102 4.762 -28.157 1.00 26.68 N ANISOU 1849 N LEU B 246 2531 4195 3413 -605 -167 403 N ATOM 1850 CA LEU B 246 15.392 5.406 -26.871 1.00 25.73 C ANISOU 1850 CA LEU B 246 2466 3959 3349 -532 -97 422 C ATOM 1851 C LEU B 246 14.324 5.098 -25.819 1.00 26.13 C ANISOU 1851 C LEU B 246 2471 4043 3415 -560 -66 459 C ATOM 1852 O LEU B 246 14.630 4.988 -24.633 1.00 25.68 O ANISOU 1852 O LEU B 246 2489 3877 3391 -550 -28 437 O ATOM 1853 CB LEU B 246 15.535 6.918 -27.049 1.00 25.58 C ANISOU 1853 CB LEU B 246 2436 3939 3344 -402 -47 495 C ATOM 1854 CG LEU B 246 16.729 7.402 -27.873 1.00 24.84 C ANISOU 1854 CG LEU B 246 2395 3799 3244 -373 -61 478 C ATOM 1855 CD1 LEU B 246 16.433 8.735 -28.531 1.00 25.10 C ANISOU 1855 CD1 LEU B 246 2381 3888 3268 -272 -33 576 C ATOM 1856 CD2 LEU B 246 17.975 7.491 -27.014 1.00 24.45 C ANISOU 1856 CD2 LEU B 246 2463 3588 3239 -369 -42 425 C ATOM 1857 N THR B 247 13.075 4.956 -26.261 1.00 27.06 N ANISOU 1857 N THR B 247 2456 4325 3500 -597 -84 522 N ATOM 1858 CA THR B 247 11.978 4.573 -25.372 1.00 27.61 C ANISOU 1858 CA THR B 247 2451 4465 3574 -640 -56 573 C ATOM 1859 C THR B 247 12.139 3.120 -24.920 1.00 27.59 C ANISOU 1859 C THR B 247 2517 4389 3578 -797 -101 502 C ATOM 1860 O THR B 247 11.931 2.810 -23.746 1.00 27.73 O ANISOU 1860 O THR B 247 2560 4358 3618 -815 -58 515 O ATOM 1861 CB THR B 247 10.598 4.775 -26.040 1.00 28.89 C ANISOU 1861 CB THR B 247 2428 4855 3695 -649 -72 671 C ATOM 1862 OG1 THR B 247 10.524 6.093 -26.597 1.00 28.99 O ANISOU 1862 OG1 THR B 247 2395 4924 3696 -491 -37 738 O ATOM 1863 CG2 THR B 247 9.474 4.599 -25.034 1.00 29.34 C ANISOU 1863 CG2 THR B 247 2386 5009 3755 -665 -23 749 C ATOM 1864 N ALA B 248 12.527 2.247 -25.852 1.00 27.47 N ANISOU 1864 N ALA B 248 2543 4358 3535 -901 -184 429 N ATOM 1865 CA ALA B 248 12.735 0.827 -25.563 1.00 27.46 C ANISOU 1865 CA ALA B 248 2638 4263 3534 -1046 -236 356 C ATOM 1866 C ALA B 248 13.850 0.613 -24.541 1.00 26.35 C ANISOU 1866 C ALA B 248 2648 3931 3434 -1000 -197 297 C ATOM 1867 O ALA B 248 13.679 -0.126 -23.567 1.00 26.51 O ANISOU 1867 O ALA B 248 2717 3883 3471 -1068 -186 296 O ATOM 1868 CB ALA B 248 13.027 0.060 -26.843 1.00 27.90 C ANISOU 1868 CB ALA B 248 2736 4325 3539 -1133 -330 277 C ATOM 1869 N CYS B 249 14.981 1.274 -24.770 1.00 25.28 N ANISOU 1869 N CYS B 249 2578 3720 3308 -889 -179 258 N ATOM 1870 CA CYS B 249 16.119 1.234 -23.856 1.00 24.33 C ANISOU 1870 CA CYS B 249 2581 3443 3219 -834 -148 210 C ATOM 1871 C CYS B 249 15.789 1.775 -22.465 1.00 24.16 C ANISOU 1871 C CYS B 249 2557 3393 3230 -782 -76 263 C ATOM 1872 O CYS B 249 16.195 1.190 -21.458 1.00 23.86 O ANISOU 1872 O CYS B 249 2609 3252 3206 -801 -64 235 O ATOM 1873 CB CYS B 249 17.269 2.039 -24.436 1.00 23.56 C ANISOU 1873 CB CYS B 249 2515 3312 3123 -735 -143 185 C ATOM 1874 SG CYS B 249 18.034 1.320 -25.870 1.00 23.90 S ANISOU 1874 SG CYS B 249 2599 3366 3117 -764 -212 107 S ATOM 1875 N SER B 250 15.072 2.900 -22.429 1.00 24.37 N ANISOU 1875 N SER B 250 2490 3513 3258 -701 -27 340 N ATOM 1876 CA SER B 250 14.632 3.532 -21.185 1.00 24.41 C ANISOU 1876 CA SER B 250 2491 3509 3275 -626 49 392 C ATOM 1877 C SER B 250 13.724 2.613 -20.367 1.00 25.28 C ANISOU 1877 C SER B 250 2567 3661 3377 -716 64 426 C ATOM 1878 O SER B 250 13.835 2.559 -19.139 1.00 25.12 O ANISOU 1878 O SER B 250 2608 3574 3361 -688 111 430 O ATOM 1879 CB SER B 250 13.916 4.846 -21.491 1.00 24.81 C ANISOU 1879 CB SER B 250 2447 3661 3316 -509 97 471 C ATOM 1880 OG SER B 250 13.063 5.235 -20.429 1.00 25.70 O ANISOU 1880 OG SER B 250 2525 3819 3421 -443 172 534 O ATOM 1881 N ASN B 251 12.826 1.904 -21.054 1.00 26.18 N ANISOU 1881 N ASN B 251 2582 3893 3473 -832 20 457 N ATOM 1882 CA ASN B 251 11.966 0.906 -20.419 1.00 27.12 C ANISOU 1882 CA ASN B 251 2663 4057 3584 -958 19 499 C ATOM 1883 C ASN B 251 12.780 -0.237 -19.832 1.00 26.79 C ANISOU 1883 C ASN B 251 2776 3847 3555 -1043 -11 427 C ATOM 1884 O ASN B 251 12.502 -0.705 -18.728 1.00 27.34 O ANISOU 1884 O ASN B 251 2873 3888 3627 -1079 27 461 O ATOM 1885 CB ASN B 251 10.938 0.363 -21.412 1.00 28.24 C ANISOU 1885 CB ASN B 251 2674 4355 3701 -1093 -44 539 C ATOM 1886 CG ASN B 251 9.917 1.402 -21.814 1.00 28.71 C ANISOU 1886 CG ASN B 251 2553 4615 3738 -1006 -7 639 C ATOM 1887 OD1 ASN B 251 10.035 2.575 -21.457 1.00 28.41 O ANISOU 1887 OD1 ASN B 251 2510 4579 3706 -833 66 669 O ATOM 1888 ND2 ASN B 251 8.908 0.981 -22.564 1.00 29.61 N ANISOU 1888 ND2 ASN B 251 2527 4899 3823 -1125 -62 691 N ATOM 1889 N GLU B 252 13.792 -0.669 -20.578 1.00 26.15 N ANISOU 1889 N GLU B 252 2798 3662 3478 -1060 -74 334 N ATOM 1890 CA GLU B 252 14.724 -1.687 -20.111 1.00 25.85 C ANISOU 1890 CA GLU B 252 2919 3456 3448 -1101 -103 262 C ATOM 1891 C GLU B 252 15.455 -1.223 -18.846 1.00 25.06 C ANISOU 1891 C GLU B 252 2896 3262 3363 -992 -41 260 C ATOM 1892 O GLU B 252 15.810 -2.041 -17.995 1.00 25.19 O ANISOU 1892 O GLU B 252 3015 3175 3382 -1027 -40 245 O ATOM 1893 CB GLU B 252 15.702 -2.077 -21.230 1.00 25.40 C ANISOU 1893 CB GLU B 252 2943 3329 3377 -1099 -171 167 C ATOM 1894 CG GLU B 252 15.036 -2.851 -22.378 1.00 26.25 C ANISOU 1894 CG GLU B 252 3021 3499 3453 -1231 -248 148 C ATOM 1895 CD GLU B 252 15.990 -3.257 -23.498 1.00 26.48 C ANISOU 1895 CD GLU B 252 3143 3466 3451 -1210 -309 48 C ATOM 1896 OE1 GLU B 252 17.141 -2.777 -23.546 1.00 26.17 O ANISOU 1896 OE1 GLU B 252 3153 3372 3417 -1085 -287 9 O ATOM 1897 OE2 GLU B 252 15.583 -4.071 -24.347 1.00 28.29 O ANISOU 1897 OE2 GLU B 252 3397 3710 3644 -1322 -381 10 O ATOM 1898 N CYS B 253 15.653 0.089 -18.722 1.00 24.45 N ANISOU 1898 N CYS B 253 2779 3219 3292 -863 7 278 N ATOM 1899 CA CYS B 253 16.223 0.691 -17.514 1.00 24.09 C ANISOU 1899 CA CYS B 253 2803 3099 3251 -763 61 276 C ATOM 1900 C CYS B 253 15.282 0.533 -16.326 1.00 25.07 C ANISOU 1900 C CYS B 253 2900 3266 3358 -776 123 346 C ATOM 1901 O CYS B 253 15.711 0.168 -15.226 1.00 25.04 O ANISOU 1901 O CYS B 253 2989 3179 3346 -766 143 336 O ATOM 1902 CB CYS B 253 16.526 2.178 -17.731 1.00 23.66 C ANISOU 1902 CB CYS B 253 2725 3063 3203 -638 92 281 C ATOM 1903 SG CYS B 253 17.946 2.526 -18.786 1.00 21.89 S ANISOU 1903 SG CYS B 253 2549 2775 2994 -606 36 210 S ATOM 1904 N LYS B 254 14.001 0.815 -16.559 1.00 26.05 N ANISOU 1904 N LYS B 254 2888 3539 3471 -793 155 425 N ATOM 1905 CA LYS B 254 12.960 0.643 -15.553 1.00 27.15 C ANISOU 1905 CA LYS B 254 2967 3763 3587 -809 221 511 C ATOM 1906 C LYS B 254 12.851 -0.829 -15.147 1.00 27.40 C ANISOU 1906 C LYS B 254 3049 3744 3618 -966 189 519 C ATOM 1907 O LYS B 254 12.664 -1.149 -13.971 1.00 27.76 O ANISOU 1907 O LYS B 254 3130 3773 3643 -969 239 560 O ATOM 1908 CB LYS B 254 11.618 1.156 -16.090 1.00 28.40 C ANISOU 1908 CB LYS B 254 2941 4119 3729 -802 252 603 C ATOM 1909 CG LYS B 254 10.509 1.296 -15.043 1.00 30.60 C ANISOU 1909 CG LYS B 254 3129 4527 3972 -770 344 708 C ATOM 1910 CD LYS B 254 10.416 2.716 -14.483 1.00 33.07 C ANISOU 1910 CD LYS B 254 3441 4866 4256 -557 433 727 C ATOM 1911 CE LYS B 254 9.539 3.636 -15.359 1.00 34.90 C ANISOU 1911 CE LYS B 254 3519 5262 4479 -470 454 793 C ATOM 1912 NZ LYS B 254 10.150 3.987 -16.687 1.00 34.11 N ANISOU 1912 NZ LYS B 254 3434 5114 4412 -475 378 734 N ATOM 1913 N ASP B 255 12.976 -1.714 -16.131 1.00 27.36 N ANISOU 1913 N ASP B 255 3060 3708 3629 -1093 104 479 N ATOM 1914 CA ASP B 255 12.917 -3.154 -15.897 1.00 28.12 C ANISOU 1914 CA ASP B 255 3235 3723 3727 -1251 60 479 C ATOM 1915 C ASP B 255 13.982 -3.618 -14.907 1.00 27.56 C ANISOU 1915 C ASP B 255 3334 3483 3657 -1204 69 434 C ATOM 1916 O ASP B 255 13.685 -4.359 -13.962 1.00 28.22 O ANISOU 1916 O ASP B 255 3462 3532 3728 -1272 93 486 O ATOM 1917 CB ASP B 255 13.055 -3.916 -17.219 1.00 28.20 C ANISOU 1917 CB ASP B 255 3272 3698 3743 -1367 -39 416 C ATOM 1918 CG ASP B 255 11.751 -3.997 -17.985 1.00 29.14 C ANISOU 1918 CG ASP B 255 3231 3990 3852 -1493 -68 482 C ATOM 1919 OD1 ASP B 255 10.689 -3.709 -17.391 1.00 28.69 O ANISOU 1919 OD1 ASP B 255 3040 4078 3785 -1513 -9 591 O ATOM 1920 OD2 ASP B 255 11.791 -4.357 -19.183 1.00 29.53 O ANISOU 1920 OD2 ASP B 255 3286 4041 3893 -1568 -150 428 O ATOM 1921 N VAL B 256 15.216 -3.168 -15.132 1.00 26.35 N ANISOU 1921 N VAL B 256 3264 3236 3512 -1091 50 348 N ATOM 1922 CA VAL B 256 16.346 -3.520 -14.278 1.00 25.79 C ANISOU 1922 CA VAL B 256 3340 3023 3436 -1030 49 304 C ATOM 1923 C VAL B 256 16.158 -2.910 -12.887 1.00 25.78 C ANISOU 1923 C VAL B 256 3336 3049 3409 -949 128 357 C ATOM 1924 O VAL B 256 16.369 -3.584 -11.878 1.00 26.11 O ANISOU 1924 O VAL B 256 3467 3021 3431 -964 141 377 O ATOM 1925 CB VAL B 256 17.693 -3.088 -14.908 1.00 24.61 C ANISOU 1925 CB VAL B 256 3248 2805 3297 -932 8 213 C ATOM 1926 CG1 VAL B 256 18.851 -3.336 -13.947 1.00 24.41 C ANISOU 1926 CG1 VAL B 256 3348 2667 3260 -859 7 180 C ATOM 1927 CG2 VAL B 256 17.924 -3.827 -16.206 1.00 24.52 C ANISOU 1927 CG2 VAL B 256 3260 2762 3293 -999 -64 157 C ATOM 1928 N ALA B 257 15.738 -1.647 -12.852 1.00 25.46 N ANISOU 1928 N ALA B 257 3204 3108 3360 -856 180 380 N ATOM 1929 CA ALA B 257 15.424 -0.955 -11.605 1.00 25.68 C ANISOU 1929 CA ALA B 257 3233 3176 3350 -763 261 424 C ATOM 1930 C ALA B 257 14.367 -1.697 -10.778 1.00 26.93 C ANISOU 1930 C ALA B 257 3350 3404 3478 -842 312 522 C ATOM 1931 O ALA B 257 14.548 -1.902 -9.574 1.00 27.31 O ANISOU 1931 O ALA B 257 3474 3414 3487 -809 352 543 O ATOM 1932 CB ALA B 257 14.980 0.478 -11.887 1.00 25.48 C ANISOU 1932 CB ALA B 257 3120 3244 3318 -649 308 437 C ATOM 1933 N ASN B 258 13.274 -2.104 -11.425 1.00 27.68 N ANISOU 1933 N ASN B 258 3321 3609 3585 -955 309 587 N ATOM 1934 CA ASN B 258 12.196 -2.823 -10.741 1.00 28.92 C ANISOU 1934 CA ASN B 258 3414 3857 3717 -1060 355 699 C ATOM 1935 C ASN B 258 12.647 -4.163 -10.170 1.00 29.16 C ANISOU 1935 C ASN B 258 3581 3751 3748 -1172 320 701 C ATOM 1936 O ASN B 258 12.268 -4.524 -9.051 1.00 29.95 O ANISOU 1936 O ASN B 258 3696 3873 3809 -1188 379 780 O ATOM 1937 CB ASN B 258 10.984 -3.013 -11.664 1.00 29.96 C ANISOU 1937 CB ASN B 258 3374 4145 3863 -1183 339 769 C ATOM 1938 CG ASN B 258 10.236 -1.712 -11.929 1.00 30.23 C ANISOU 1938 CG ASN B 258 3251 4355 3879 -1054 401 812 C ATOM 1939 OD1 ASN B 258 10.071 -0.874 -11.035 1.00 29.87 O ANISOU 1939 OD1 ASN B 258 3197 4361 3792 -902 492 843 O ATOM 1940 ND2 ASN B 258 9.771 -1.541 -13.165 1.00 30.09 N ANISOU 1940 ND2 ASN B 258 3118 4429 3883 -1104 352 815 N ATOM 1941 N ALA B 259 13.466 -4.882 -10.938 1.00 28.52 N ANISOU 1941 N ALA B 259 3605 3529 3704 -1235 229 619 N ATOM 1942 CA ALA B 259 13.956 -6.205 -10.543 1.00 28.85 C ANISOU 1942 CA ALA B 259 3798 3415 3748 -1328 187 615 C ATOM 1943 C ALA B 259 14.837 -6.144 -9.300 1.00 28.32 C ANISOU 1943 C ALA B 259 3854 3260 3646 -1209 222 604 C ATOM 1944 O ALA B 259 14.781 -7.035 -8.450 1.00 29.41 O ANISOU 1944 O ALA B 259 4077 3335 3762 -1269 235 662 O ATOM 1945 CB ALA B 259 14.700 -6.857 -11.681 1.00 28.32 C ANISOU 1945 CB ALA B 259 3825 3221 3716 -1377 89 518 C ATOM 1946 N ILE B 260 15.641 -5.091 -9.203 1.00 26.85 N ANISOU 1946 N ILE B 260 3679 3071 3452 -1049 232 534 N ATOM 1947 CA ILE B 260 16.504 -4.873 -8.052 1.00 26.27 C ANISOU 1947 CA ILE B 260 3710 2935 3335 -934 254 515 C ATOM 1948 C ILE B 260 15.663 -4.578 -6.803 1.00 27.39 C ANISOU 1948 C ILE B 260 3812 3177 3416 -905 349 609 C ATOM 1949 O ILE B 260 15.869 -5.189 -5.745 1.00 27.93 O ANISOU 1949 O ILE B 260 3974 3198 3442 -906 369 651 O ATOM 1950 CB ILE B 260 17.520 -3.750 -8.332 1.00 24.79 C ANISOU 1950 CB ILE B 260 3536 2729 3153 -797 231 420 C ATOM 1951 CG1 ILE B 260 18.461 -4.172 -9.461 1.00 23.74 C ANISOU 1951 CG1 ILE B 260 3447 2506 3067 -816 145 339 C ATOM 1952 CG2 ILE B 260 18.305 -3.394 -7.073 1.00 24.42 C ANISOU 1952 CG2 ILE B 260 3584 2643 3051 -689 249 404 C ATOM 1953 CD1 ILE B 260 19.185 -3.020 -10.122 1.00 23.34 C ANISOU 1953 CD1 ILE B 260 3359 2474 3034 -723 123 266 C ATOM 1954 N MET B 261 14.704 -3.664 -6.940 1.00 27.74 N ANISOU 1954 N MET B 261 3721 3369 3450 -871 411 648 N ATOM 1955 CA MET B 261 13.795 -3.318 -5.849 1.00 28.86 C ANISOU 1955 CA MET B 261 3807 3636 3524 -824 514 742 C ATOM 1956 C MET B 261 13.051 -4.535 -5.289 1.00 30.83 C ANISOU 1956 C MET B 261 4045 3913 3755 -968 541 860 C ATOM 1957 O MET B 261 12.890 -4.656 -4.075 1.00 31.77 O ANISOU 1957 O MET B 261 4203 4063 3805 -927 608 924 O ATOM 1958 CB MET B 261 12.798 -2.242 -6.293 1.00 29.09 C ANISOU 1958 CB MET B 261 3675 3829 3547 -760 575 774 C ATOM 1959 CG MET B 261 13.398 -0.847 -6.407 1.00 27.98 C ANISOU 1959 CG MET B 261 3569 3665 3398 -588 580 682 C ATOM 1960 SD MET B 261 12.184 0.436 -6.769 1.00 27.90 S ANISOU 1960 SD MET B 261 3396 3838 3367 -474 665 734 S ATOM 1961 CE MET B 261 12.173 0.412 -8.563 1.00 26.88 C ANISOU 1961 CE MET B 261 3172 3712 3329 -567 577 701 C ATOM 1962 N ALA B 262 12.612 -5.431 -6.174 1.00 31.74 N ANISOU 1962 N ALA B 262 4118 4016 3928 -1142 487 889 N ATOM 1963 CA ALA B 262 11.848 -6.616 -5.774 1.00 33.79 C ANISOU 1963 CA ALA B 262 4368 4291 4179 -1317 500 1009 C ATOM 1964 C ALA B 262 12.726 -7.680 -5.116 1.00 34.24 C ANISOU 1964 C ALA B 262 4621 4161 4226 -1350 462 1002 C ATOM 1965 O ALA B 262 12.287 -8.366 -4.190 1.00 35.38 O ANISOU 1965 O ALA B 262 4793 4318 4330 -1420 509 1112 O ATOM 1966 CB ALA B 262 11.096 -7.206 -6.977 1.00 34.48 C ANISOU 1966 CB ALA B 262 4360 4416 4325 -1509 439 1035 C ATOM 1967 N ALA B 263 13.958 -7.814 -5.604 1.00 33.56 N ANISOU 1967 N ALA B 263 4665 3912 4173 -1292 381 881 N ATOM 1968 CA ALA B 263 14.916 -8.771 -5.058 1.00 34.20 C ANISOU 1968 CA ALA B 263 4936 3816 4243 -1288 339 867 C ATOM 1969 C ALA B 263 15.594 -8.224 -3.809 1.00 34.29 C ANISOU 1969 C ALA B 263 5012 3833 4182 -1122 386 860 C ATOM 1970 O ALA B 263 16.108 -8.986 -2.990 1.00 34.81 O ANISOU 1970 O ALA B 263 5211 3803 4213 -1113 379 895 O ATOM 1971 CB ALA B 263 15.957 -9.134 -6.102 1.00 33.24 C ANISOU 1971 CB ALA B 263 4912 3542 4174 -1275 239 747 C ATOM 1972 N CYS B 264 15.592 -6.901 -3.671 1.00 34.17 N ANISOU 1972 N CYS B 264 4915 3928 4141 -990 428 816 N ATOM 1973 CA CYS B 264 16.293 -6.242 -2.578 1.00 34.53 C ANISOU 1973 CA CYS B 264 5032 3976 4111 -833 456 786 C ATOM 1974 C CYS B 264 15.467 -5.128 -1.926 1.00 35.26 C ANISOU 1974 C CYS B 264 5027 4231 4137 -741 556 822 C ATOM 1975 O CYS B 264 15.559 -3.962 -2.331 1.00 34.62 O ANISOU 1975 O CYS B 264 4895 4195 4064 -645 560 749 O ATOM 1976 CB CYS B 264 17.639 -5.699 -3.071 1.00 33.20 C ANISOU 1976 CB CYS B 264 4926 3719 3969 -732 377 652 C ATOM 1977 SG CYS B 264 18.713 -6.954 -3.799 1.00 33.66 S ANISOU 1977 SG CYS B 264 5102 3600 4086 -788 271 605 S ATOM 1978 N PRO B 265 14.648 -5.486 -0.918 1.00 36.95 N ANISOU 1978 N PRO B 265 5222 4535 4281 -764 642 942 N ATOM 1979 CA PRO B 265 13.966 -4.506 -0.061 1.00 37.65 C ANISOU 1979 CA PRO B 265 5250 4778 4278 -641 749 979 C ATOM 1980 C PRO B 265 14.939 -3.477 0.518 1.00 36.82 C ANISOU 1980 C PRO B 265 5251 4627 4111 -465 734 864 C ATOM 1981 O PRO B 265 16.110 -3.801 0.765 1.00 36.28 O ANISOU 1981 O PRO B 265 5311 4433 4039 -447 657 801 O ATOM 1982 CB PRO B 265 13.405 -5.366 1.077 1.00 39.29 C ANISOU 1982 CB PRO B 265 5480 5041 4409 -694 820 1118 C ATOM 1983 CG PRO B 265 13.224 -6.716 0.482 1.00 39.86 C ANISOU 1983 CG PRO B 265 5555 5030 4560 -896 766 1185 C ATOM 1984 CD PRO B 265 14.304 -6.875 -0.551 1.00 38.32 C ANISOU 1984 CD PRO B 265 5440 4666 4455 -910 644 1056 C ATOM 1985 N GLY B 266 14.452 -2.253 0.725 1.00 36.83 N ANISOU 1985 N GLY B 266 5201 4731 4060 -336 803 841 N ATOM 1986 CA GLY B 266 15.247 -1.179 1.332 1.00 36.16 C ANISOU 1986 CA GLY B 266 5231 4603 3905 -179 791 732 C ATOM 1987 C GLY B 266 16.168 -0.450 0.367 1.00 34.60 C ANISOU 1987 C GLY B 266 5061 4301 3786 -159 696 602 C ATOM 1988 O GLY B 266 17.020 0.334 0.788 1.00 34.31 O ANISOU 1988 O GLY B 266 5131 4202 3703 -67 657 506 O ATOM 1989 N ASN B 267 16.004 -0.717 -0.927 1.00 33.65 N ANISOU 1989 N ASN B 267 4845 4165 3777 -255 654 602 N ATOM 1990 CA ASN B 267 16.767 -0.042 -1.971 1.00 32.03 C ANISOU 1990 CA ASN B 267 4642 3881 3646 -244 575 498 C ATOM 1991 C ASN B 267 15.834 0.714 -2.914 1.00 31.91 C ANISOU 1991 C ASN B 267 4497 3952 3676 -227 617 514 C ATOM 1992 O ASN B 267 15.331 0.155 -3.892 1.00 31.69 O ANISOU 1992 O ASN B 267 4362 3958 3722 -331 601 556 O ATOM 1993 CB ASN B 267 17.633 -1.049 -2.732 1.00 31.16 C ANISOU 1993 CB ASN B 267 4555 3666 3618 -355 475 472 C ATOM 1994 CG ASN B 267 18.783 -1.574 -1.898 1.00 30.72 C ANISOU 1994 CG ASN B 267 4632 3522 3518 -336 419 441 C ATOM 1995 OD1 ASN B 267 19.781 -0.886 -1.691 1.00 29.29 O ANISOU 1995 OD1 ASN B 267 4520 3293 3315 -268 367 358 O ATOM 1996 ND2 ASN B 267 18.652 -2.804 -1.420 1.00 31.39 N ANISOU 1996 ND2 ASN B 267 4753 3587 3588 -402 425 516 N ATOM 1997 N ASP B 268 15.602 1.988 -2.600 1.00 32.08 N ANISOU 1997 N ASP B 268 4537 4006 3645 -89 668 480 N ATOM 1998 CA ASP B 268 14.639 2.815 -3.327 1.00 32.29 C ANISOU 1998 CA ASP B 268 4448 4127 3694 -31 724 508 C ATOM 1999 C ASP B 268 15.191 3.320 -4.665 1.00 30.98 C ANISOU 1999 C ASP B 268 4259 3891 3623 -59 645 441 C ATOM 2000 O ASP B 268 15.992 4.254 -4.712 1.00 30.60 O ANISOU 2000 O ASP B 268 4307 3749 3573 9 606 354 O ATOM 2001 CB ASP B 268 14.171 3.978 -2.441 1.00 33.37 C ANISOU 2001 CB ASP B 268 4640 4311 3728 151 816 499 C ATOM 2002 CG ASP B 268 13.119 4.856 -3.113 1.00 34.52 C ANISOU 2002 CG ASP B 268 4669 4564 3884 244 885 541 C ATOM 2003 OD1 ASP B 268 12.789 5.923 -2.544 1.00 35.92 O ANISOU 2003 OD1 ASP B 268 4910 4758 3981 417 957 521 O ATOM 2004 OD2 ASP B 268 12.618 4.489 -4.198 1.00 34.52 O ANISOU 2004 OD2 ASP B 268 4523 4631 3964 155 867 593 O ATOM 2005 N LEU B 269 14.749 2.689 -5.747 1.00 30.53 N ANISOU 2005 N LEU B 269 4076 3883 3641 -170 619 486 N ATOM 2006 CA LEU B 269 15.149 3.068 -7.098 1.00 29.56 C ANISOU 2006 CA LEU B 269 3914 3720 3598 -200 552 437 C ATOM 2007 C LEU B 269 13.940 3.539 -7.901 1.00 30.16 C ANISOU 2007 C LEU B 269 3836 3933 3691 -174 602 506 C ATOM 2008 O LEU B 269 13.860 3.315 -9.111 1.00 29.72 O ANISOU 2008 O LEU B 269 3695 3899 3699 -253 551 509 O ATOM 2009 CB LEU B 269 15.812 1.882 -7.807 1.00 28.78 C ANISOU 2009 CB LEU B 269 3816 3556 3564 -347 461 416 C ATOM 2010 CG LEU B 269 17.309 1.601 -7.663 1.00 27.74 C ANISOU 2010 CG LEU B 269 3810 3284 3444 -362 379 332 C ATOM 2011 CD1 LEU B 269 17.688 1.214 -6.245 1.00 28.45 C ANISOU 2011 CD1 LEU B 269 4009 3336 3466 -334 396 335 C ATOM 2012 CD2 LEU B 269 17.709 0.498 -8.630 1.00 27.17 C ANISOU 2012 CD2 LEU B 269 3718 3172 3434 -480 306 320 C ATOM 2013 N SER B 270 13.002 4.195 -7.222 1.00 31.33 N ANISOU 2013 N SER B 270 3947 4185 3772 -52 703 562 N ATOM 2014 CA SER B 270 11.753 4.631 -7.847 1.00 32.33 C ANISOU 2014 CA SER B 270 3909 4475 3900 -4 762 647 C ATOM 2015 C SER B 270 11.921 5.898 -8.691 1.00 32.16 C ANISOU 2015 C SER B 270 3899 4416 3904 107 750 605 C ATOM 2016 O SER B 270 11.035 6.249 -9.478 1.00 32.73 O ANISOU 2016 O SER B 270 3831 4616 3990 141 776 671 O ATOM 2017 CB SER B 270 10.661 4.824 -6.793 1.00 33.80 C ANISOU 2017 CB SER B 270 4041 4809 3995 105 886 737 C ATOM 2018 OG SER B 270 10.994 5.872 -5.902 1.00 34.20 O ANISOU 2018 OG SER B 270 4238 4785 3971 287 938 678 O ATOM 2019 N ASP B 271 13.058 6.573 -8.533 1.00 31.58 N ANISOU 2019 N ASP B 271 3989 4175 3836 156 705 503 N ATOM 2020 CA ASP B 271 13.353 7.764 -9.326 1.00 31.60 C ANISOU 2020 CA ASP B 271 4027 4113 3867 240 684 465 C ATOM 2021 C ASP B 271 13.916 7.434 -10.704 1.00 30.82 C ANISOU 2021 C ASP B 271 3870 3985 3854 117 590 444 C ATOM 2022 O ASP B 271 14.279 8.339 -11.451 1.00 30.77 O ANISOU 2022 O ASP B 271 3892 3921 3877 164 564 419 O ATOM 2023 CB ASP B 271 14.287 8.721 -8.578 1.00 31.52 C ANISOU 2023 CB ASP B 271 4219 3936 3820 331 673 372 C ATOM 2024 CG ASP B 271 13.564 9.561 -7.540 1.00 32.69 C ANISOU 2024 CG ASP B 271 4437 4111 3871 517 777 387 C ATOM 2025 OD1 ASP B 271 12.441 9.200 -7.127 1.00 34.06 O ANISOU 2025 OD1 ASP B 271 4501 4443 3996 569 866 472 O ATOM 2026 OD2 ASP B 271 14.134 10.585 -7.121 1.00 32.40 O ANISOU 2026 OD2 ASP B 271 4573 3938 3801 609 770 312 O ATOM 2027 N ASP B 272 13.995 6.147 -11.037 1.00 30.76 N ANISOU 2027 N ASP B 272 3794 4011 3881 -37 541 456 N ATOM 2028 CA ASP B 272 14.217 5.737 -12.419 1.00 30.69 C ANISOU 2028 CA ASP B 272 3707 4017 3935 -141 467 450 C ATOM 2029 C ASP B 272 12.968 6.041 -13.215 1.00 31.60 C ANISOU 2029 C ASP B 272 3660 4295 4050 -111 503 537 C ATOM 2030 O ASP B 272 11.913 5.441 -12.992 1.00 32.35 O ANISOU 2030 O ASP B 272 3638 4530 4123 -150 543 615 O ATOM 2031 CB ASP B 272 14.518 4.251 -12.519 1.00 30.56 C ANISOU 2031 CB ASP B 272 3682 3986 3942 -302 409 438 C ATOM 2032 CG ASP B 272 15.928 3.930 -12.150 1.00 30.91 C ANISOU 2032 CG ASP B 272 3866 3880 3999 -331 350 353 C ATOM 2033 OD1 ASP B 272 16.199 3.718 -10.942 1.00 31.50 O ANISOU 2033 OD1 ASP B 272 4030 3905 4035 -308 373 342 O ATOM 2034 OD2 ASP B 272 16.763 3.887 -13.079 1.00 32.00 O ANISOU 2034 OD2 ASP B 272 4018 3964 4177 -371 282 304 O ATOM 2035 N LYS B 273 13.096 6.987 -14.134 1.00 31.76 N ANISOU 2035 N LYS B 273 3668 4308 4093 -44 488 532 N ATOM 2036 CA LYS B 273 11.962 7.480 -14.894 1.00 33.11 C ANISOU 2036 CA LYS B 273 3690 4636 4254 19 522 618 C ATOM 2037 C LYS B 273 12.190 7.320 -16.391 1.00 32.96 C ANISOU 2037 C LYS B 273 3601 4645 4278 -64 443 613 C ATOM 2038 O LYS B 273 13.296 6.998 -16.829 1.00 31.88 O ANISOU 2038 O LYS B 273 3543 4394 4175 -145 372 538 O ATOM 2039 CB LYS B 273 11.659 8.939 -14.525 1.00 33.78 C ANISOU 2039 CB LYS B 273 3830 4701 4304 226 599 640 C ATOM 2040 CG LYS B 273 12.894 9.836 -14.362 1.00 33.29 C ANISOU 2040 CG LYS B 273 3961 4431 4258 278 571 552 C ATOM 2041 CD LYS B 273 12.553 11.169 -13.686 1.00 34.21 C ANISOU 2041 CD LYS B 273 4180 4496 4324 480 651 562 C ATOM 2042 CE LYS B 273 12.273 10.993 -12.194 1.00 34.50 C ANISOU 2042 CE LYS B 273 4285 4530 4294 544 721 549 C ATOM 2043 NZ LYS B 273 11.561 12.160 -11.607 1.00 35.34 N ANISOU 2043 NZ LYS B 273 4456 4641 4331 768 819 577 N ATOM 2044 N ASP B 274 11.124 7.520 -17.162 1.00 34.28 N ANISOU 2044 N ASP B 274 3610 4982 4432 -39 457 697 N ATOM 2045 CA ASP B 274 11.197 7.499 -18.608 1.00 34.51 C ANISOU 2045 CA ASP B 274 3565 5064 4483 -95 388 702 C ATOM 2046 C ASP B 274 12.116 8.600 -19.080 1.00 33.87 C ANISOU 2046 C ASP B 274 3595 4853 4423 -3 376 663 C ATOM 2047 O ASP B 274 12.138 9.688 -18.509 1.00 34.08 O ANISOU 2047 O ASP B 274 3702 4811 4436 144 436 674 O ATOM 2048 CB ASP B 274 9.808 7.703 -19.217 1.00 36.24 C ANISOU 2048 CB ASP B 274 3590 5508 4672 -56 411 814 C ATOM 2049 CG ASP B 274 9.098 6.396 -19.503 1.00 37.98 C ANISOU 2049 CG ASP B 274 3673 5870 4885 -238 362 846 C ATOM 2050 OD1 ASP B 274 8.016 6.168 -18.914 1.00 40.09 O ANISOU 2050 OD1 ASP B 274 3820 6290 5123 -235 415 932 O ATOM 2051 OD2 ASP B 274 9.624 5.597 -20.318 1.00 38.68 O ANISOU 2051 OD2 ASP B 274 3782 5921 4995 -385 271 787 O ATOM 2052 N ILE B 275 12.879 8.305 -20.126 1.00 33.36 N ANISOU 2052 N ILE B 275 3539 4753 4382 -92 299 620 N ATOM 2053 CA ILE B 275 13.733 9.296 -20.764 1.00 33.14 C ANISOU 2053 CA ILE B 275 3591 4628 4373 -30 283 602 C ATOM 2054 C ILE B 275 12.914 10.518 -21.205 1.00 34.42 C ANISOU 2054 C ILE B 275 3699 4865 4516 123 332 693 C ATOM 2055 O ILE B 275 13.372 11.656 -21.083 1.00 34.47 O ANISOU 2055 O ILE B 275 3815 4753 4530 227 359 695 O ATOM 2056 CB ILE B 275 14.538 8.676 -21.940 1.00 32.44 C ANISOU 2056 CB ILE B 275 3490 4538 4299 -146 199 557 C ATOM 2057 CG1 ILE B 275 15.620 9.643 -22.424 1.00 31.84 C ANISOU 2057 CG1 ILE B 275 3505 4351 4243 -101 186 542 C ATOM 2058 CG2 ILE B 275 13.613 8.208 -23.079 1.00 32.68 C ANISOU 2058 CG2 ILE B 275 3364 4750 4302 -195 164 609 C ATOM 2059 CD1 ILE B 275 16.807 8.950 -23.040 1.00 31.17 C ANISOU 2059 CD1 ILE B 275 3453 4220 4170 -205 120 474 C ATOM 2060 N TYR B 276 11.697 10.267 -21.688 1.00 35.64 N ANISOU 2060 N TYR B 276 3687 5215 4641 132 341 773 N ATOM 2061 CA TYR B 276 10.778 11.327 -22.091 1.00 37.12 C ANISOU 2061 CA TYR B 276 3798 5507 4800 295 391 876 C ATOM 2062 C TYR B 276 10.371 12.165 -20.889 1.00 38.33 C ANISOU 2062 C TYR B 276 4028 5603 4933 466 489 900 C ATOM 2063 O TYR B 276 10.376 13.397 -20.947 1.00 39.10 O ANISOU 2063 O TYR B 276 4206 5628 5023 628 531 934 O ATOM 2064 CB TYR B 276 9.544 10.732 -22.778 1.00 37.86 C ANISOU 2064 CB TYR B 276 3674 5852 4860 251 371 959 C ATOM 2065 CG TYR B 276 8.438 11.724 -23.068 1.00 38.88 C ANISOU 2065 CG TYR B 276 3693 6130 4948 437 430 1082 C ATOM 2066 CD1 TYR B 276 8.701 12.919 -23.736 1.00 38.85 C ANISOU 2066 CD1 TYR B 276 3753 6064 4943 576 441 1120 C ATOM 2067 CD2 TYR B 276 7.126 11.459 -22.691 1.00 39.96 C ANISOU 2067 CD2 TYR B 276 3657 6480 5044 476 475 1172 C ATOM 2068 CE1 TYR B 276 7.692 13.827 -24.010 1.00 40.25 C ANISOU 2068 CE1 TYR B 276 3839 6374 5079 767 497 1239 C ATOM 2069 CE2 TYR B 276 6.105 12.362 -22.965 1.00 41.67 C ANISOU 2069 CE2 TYR B 276 3760 6856 5218 668 532 1294 C ATOM 2070 CZ TYR B 276 6.400 13.545 -23.624 1.00 41.78 C ANISOU 2070 CZ TYR B 276 3855 6790 5231 822 543 1325 C ATOM 2071 OH TYR B 276 5.405 14.450 -23.896 1.00 43.46 O ANISOU 2071 OH TYR B 276 3966 7151 5395 1035 601 1451 O ATOM 2072 N GLN B 277 10.026 11.476 -19.806 1.00 38.89 N ANISOU 2072 N GLN B 277 4086 5703 4990 432 524 884 N ATOM 2073 CA GLN B 277 9.692 12.100 -18.537 1.00 40.19 C ANISOU 2073 CA GLN B 277 4334 5817 5120 587 619 892 C ATOM 2074 C GLN B 277 10.905 12.845 -17.980 1.00 39.66 C ANISOU 2074 C GLN B 277 4504 5492 5072 626 615 799 C ATOM 2075 O GLN B 277 10.759 13.858 -17.294 1.00 40.64 O ANISOU 2075 O GLN B 277 4746 5532 5165 797 683 803 O ATOM 2076 CB GLN B 277 9.219 11.026 -17.558 1.00 40.21 C ANISOU 2076 CB GLN B 277 4270 5905 5101 503 645 892 C ATOM 2077 CG GLN B 277 8.532 11.540 -16.309 1.00 41.92 C ANISOU 2077 CG GLN B 277 4518 6152 5259 676 758 928 C ATOM 2078 CD GLN B 277 7.913 10.418 -15.486 1.00 42.59 C ANISOU 2078 CD GLN B 277 4498 6368 5317 580 787 960 C ATOM 2079 OE1 GLN B 277 8.399 9.277 -15.487 1.00 42.16 O ANISOU 2079 OE1 GLN B 277 4443 6280 5296 380 720 913 O ATOM 2080 NE2 GLN B 277 6.833 10.738 -14.773 1.00 44.62 N ANISOU 2080 NE2 GLN B 277 4670 6776 5509 731 893 1047 N ATOM 2081 N TRP B 278 12.099 12.342 -18.291 1.00 38.58 N ANISOU 2081 N TRP B 278 4439 5238 4981 470 532 717 N ATOM 2082 CA TRP B 278 13.345 12.965 -17.854 1.00 38.21 C ANISOU 2082 CA TRP B 278 4594 4968 4955 469 510 634 C ATOM 2083 C TRP B 278 13.640 14.246 -18.626 1.00 38.95 C ANISOU 2083 C TRP B 278 4762 4973 5063 557 505 664 C ATOM 2084 O TRP B 278 14.046 15.246 -18.032 1.00 39.37 O ANISOU 2084 O TRP B 278 4989 4861 5108 645 529 635 O ATOM 2085 CB TRP B 278 14.521 11.986 -17.965 1.00 36.68 C ANISOU 2085 CB TRP B 278 4429 4708 4801 283 426 553 C ATOM 2086 CG TRP B 278 15.841 12.605 -17.607 1.00 35.97 C ANISOU 2086 CG TRP B 278 4514 4421 4731 262 391 480 C ATOM 2087 CD1 TRP B 278 16.381 12.722 -16.357 1.00 35.76 C ANISOU 2087 CD1 TRP B 278 4629 4272 4687 270 400 415 C ATOM 2088 CD2 TRP B 278 16.778 13.205 -18.507 1.00 35.49 C ANISOU 2088 CD2 TRP B 278 4500 4279 4707 220 339 475 C ATOM 2089 NE1 TRP B 278 17.599 13.352 -16.425 1.00 35.50 N ANISOU 2089 NE1 TRP B 278 4723 4087 4679 223 347 366 N ATOM 2090 CE2 TRP B 278 17.867 13.662 -17.732 1.00 35.42 C ANISOU 2090 CE2 TRP B 278 4653 4099 4704 190 313 407 C ATOM 2091 CE3 TRP B 278 16.803 13.406 -19.896 1.00 35.46 C ANISOU 2091 CE3 TRP B 278 4412 4339 4722 200 310 527 C ATOM 2092 CZ2 TRP B 278 18.973 14.306 -18.299 1.00 35.45 C ANISOU 2092 CZ2 TRP B 278 4727 4000 4740 128 260 398 C ATOM 2093 CZ3 TRP B 278 17.902 14.046 -20.460 1.00 35.26 C ANISOU 2093 CZ3 TRP B 278 4462 4209 4726 153 266 519 C ATOM 2094 CH2 TRP B 278 18.972 14.488 -19.661 1.00 35.30 C ANISOU 2094 CH2 TRP B 278 4620 4049 4744 111 242 458 C ATOM 2095 N TYR B 279 13.438 14.209 -19.943 1.00 39.45 N ANISOU 2095 N TYR B 279 4707 5141 5143 529 471 722 N ATOM 2096 CA TYR B 279 13.695 15.363 -20.813 1.00 40.45 C ANISOU 2096 CA TYR B 279 4891 5197 5280 603 465 770 C ATOM 2097 C TYR B 279 12.922 16.614 -20.413 1.00 42.30 C ANISOU 2097 C TYR B 279 5205 5388 5480 822 547 830 C ATOM 2098 O TYR B 279 13.489 17.707 -20.381 1.00 42.78 O ANISOU 2098 O TYR B 279 5437 5266 5551 883 550 824 O ATOM 2099 CB TYR B 279 13.410 15.027 -22.278 1.00 40.40 C ANISOU 2099 CB TYR B 279 4723 5351 5278 552 421 834 C ATOM 2100 CG TYR B 279 14.645 14.664 -23.058 1.00 39.32 C ANISOU 2100 CG TYR B 279 4609 5156 5175 399 343 786 C ATOM 2101 CD1 TYR B 279 15.507 15.652 -23.529 1.00 39.23 C ANISOU 2101 CD1 TYR B 279 4711 5009 5186 410 327 800 C ATOM 2102 CD2 TYR B 279 14.955 13.332 -23.326 1.00 38.53 C ANISOU 2102 CD2 TYR B 279 4423 5136 5081 246 287 731 C ATOM 2103 CE1 TYR B 279 16.645 15.324 -24.245 1.00 38.70 C ANISOU 2103 CE1 TYR B 279 4646 4915 5142 276 264 768 C ATOM 2104 CE2 TYR B 279 16.093 12.989 -24.043 1.00 37.83 C ANISOU 2104 CE2 TYR B 279 4353 5008 5012 132 225 688 C ATOM 2105 CZ TYR B 279 16.932 13.990 -24.497 1.00 38.04 C ANISOU 2105 CZ TYR B 279 4470 4928 5057 150 217 711 C ATOM 2106 OH TYR B 279 18.061 13.657 -25.204 1.00 37.77 O ANISOU 2106 OH TYR B 279 4436 4881 5034 43 164 681 O ATOM 2107 N LEU B 280 11.638 16.443 -20.106 1.00 43.64 N ANISOU 2107 N LEU B 280 5252 5725 5605 939 612 893 N ATOM 2108 CA LEU B 280 10.771 17.555 -19.724 1.00 45.75 C ANISOU 2108 CA LEU B 280 5576 5983 5824 1183 703 959 C ATOM 2109 C LEU B 280 11.141 18.164 -18.379 1.00 46.55 C ANISOU 2109 C LEU B 280 5903 5882 5901 1271 751 881 C ATOM 2110 O LEU B 280 11.002 19.367 -18.184 1.00 47.69 O ANISOU 2110 O LEU B 280 6204 5896 6019 1450 800 900 O ATOM 2111 CB LEU B 280 9.303 17.127 -19.728 1.00 46.75 C ANISOU 2111 CB LEU B 280 5482 6381 5901 1281 763 1056 C ATOM 2112 CG LEU B 280 8.565 17.337 -21.049 1.00 47.58 C ANISOU 2112 CG LEU B 280 5412 6670 5997 1335 748 1174 C ATOM 2113 CD1 LEU B 280 9.043 16.364 -22.111 1.00 46.49 C ANISOU 2113 CD1 LEU B 280 5152 6614 5897 1105 644 1155 C ATOM 2114 CD2 LEU B 280 7.065 17.218 -20.845 1.00 49.40 C ANISOU 2114 CD2 LEU B 280 5443 7161 6165 1480 823 1283 C ATOM 2115 N GLU B 281 11.608 17.328 -17.457 1.00 46.36 N ANISOU 2115 N GLU B 281 5908 5829 5879 1150 734 794 N ATOM 2116 CA GLU B 281 12.050 17.793 -16.143 1.00 47.55 C ANISOU 2116 CA GLU B 281 6275 5795 5995 1210 765 707 C ATOM 2117 C GLU B 281 13.233 18.750 -16.234 1.00 47.44 C ANISOU 2117 C GLU B 281 6492 5519 6013 1172 710 644 C ATOM 2118 O GLU B 281 13.322 19.702 -15.458 1.00 48.67 O ANISOU 2118 O GLU B 281 6860 5503 6128 1296 745 603 O ATOM 2119 CB GLU B 281 12.410 16.609 -15.237 1.00 46.45 C ANISOU 2119 CB GLU B 281 6108 5688 5852 1066 744 633 C ATOM 2120 CG GLU B 281 11.261 16.109 -14.361 1.00 48.01 C ANISOU 2120 CG GLU B 281 6203 6057 5983 1168 835 674 C ATOM 2121 CD GLU B 281 11.582 14.801 -13.628 1.00 47.40 C ANISOU 2121 CD GLU B 281 6078 6026 5907 1003 808 623 C ATOM 2122 OE1 GLU B 281 12.754 14.591 -13.219 1.00 46.98 O ANISOU 2122 OE1 GLU B 281 6159 5815 5877 882 742 527 O ATOM 2123 OE2 GLU B 281 10.646 13.981 -13.459 1.00 49.19 O ANISOU 2123 OE2 GLU B 281 6128 6453 6109 993 852 689 O ATOM 2124 N TYR B 282 14.128 18.508 -17.189 1.00 46.46 N ANISOU 2124 N TYR B 282 6331 5368 5956 999 622 640 N ATOM 2125 CA TYR B 282 15.411 19.200 -17.204 1.00 46.58 C ANISOU 2125 CA TYR B 282 6537 5156 6005 905 556 581 C ATOM 2126 C TYR B 282 15.755 19.929 -18.508 1.00 46.67 C ANISOU 2126 C TYR B 282 6551 5121 6060 884 521 652 C ATOM 2127 O TYR B 282 16.882 20.392 -18.685 1.00 46.63 O ANISOU 2127 O TYR B 282 6669 4956 6091 767 457 621 O ATOM 2128 CB TYR B 282 16.526 18.240 -16.743 1.00 45.52 C ANISOU 2128 CB TYR B 282 6401 4997 5898 698 481 489 C ATOM 2129 CG TYR B 282 16.182 17.557 -15.422 1.00 46.23 C ANISOU 2129 CG TYR B 282 6502 5126 5938 726 518 429 C ATOM 2130 CD1 TYR B 282 15.952 18.313 -14.261 1.00 47.99 C ANISOU 2130 CD1 TYR B 282 6912 5225 6098 861 569 383 C ATOM 2131 CD2 TYR B 282 16.053 16.170 -15.337 1.00 45.25 C ANISOU 2131 CD2 TYR B 282 6214 5158 5821 624 506 422 C ATOM 2132 CE1 TYR B 282 15.614 17.706 -13.052 1.00 47.91 C ANISOU 2132 CE1 TYR B 282 6911 5265 6029 895 611 337 C ATOM 2133 CE2 TYR B 282 15.717 15.553 -14.129 1.00 45.55 C ANISOU 2133 CE2 TYR B 282 6264 5235 5810 648 545 383 C ATOM 2134 CZ TYR B 282 15.498 16.329 -12.992 1.00 46.70 C ANISOU 2134 CZ TYR B 282 6581 5274 5888 785 599 344 C ATOM 2135 OH TYR B 282 15.168 15.735 -11.795 1.00 46.67 O ANISOU 2135 OH TYR B 282 6590 5320 5823 815 643 313 O ATOM 2136 N TYR B 283 14.778 20.054 -19.403 1.00 46.98 N ANISOU 2136 N TYR B 283 6452 5309 6089 996 561 757 N ATOM 2137 CA TYR B 283 14.954 20.836 -20.630 1.00 47.22 C ANISOU 2137 CA TYR B 283 6492 5305 6146 1011 539 842 C ATOM 2138 C TYR B 283 13.701 21.609 -21.058 1.00 48.56 C ANISOU 2138 C TYR B 283 6628 5547 6274 1247 615 955 C ATOM 2139 O TYR B 283 13.694 22.221 -22.127 1.00 49.25 O ANISOU 2139 O TYR B 283 6705 5632 6374 1279 603 1044 O ATOM 2140 CB TYR B 283 15.453 19.955 -21.786 1.00 46.08 C ANISOU 2140 CB TYR B 283 6165 5304 6040 834 470 864 C ATOM 2141 CG TYR B 283 16.934 19.651 -21.752 1.00 45.25 C ANISOU 2141 CG TYR B 283 6125 5089 5979 627 392 788 C ATOM 2142 CD1 TYR B 283 17.870 20.584 -22.208 1.00 45.81 C ANISOU 2142 CD1 TYR B 283 6327 4998 6080 567 355 813 C ATOM 2143 CD2 TYR B 283 17.403 18.426 -21.269 1.00 44.36 C ANISOU 2143 CD2 TYR B 283 5937 5043 5875 492 355 704 C ATOM 2144 CE1 TYR B 283 19.239 20.309 -22.178 1.00 45.15 C ANISOU 2144 CE1 TYR B 283 6277 4843 6033 376 284 757 C ATOM 2145 CE2 TYR B 283 18.770 18.139 -21.232 1.00 43.72 C ANISOU 2145 CE2 TYR B 283 5901 4883 5828 321 286 643 C ATOM 2146 CZ TYR B 283 19.681 19.084 -21.690 1.00 44.02 C ANISOU 2146 CZ TYR B 283 6048 4785 5894 263 251 672 C ATOM 2147 OH TYR B 283 21.029 18.804 -21.655 1.00 43.27 O ANISOU 2147 OH TYR B 283 5971 4641 5827 93 184 626 O ATOM 2148 N HIS B 284 12.659 21.597 -20.225 1.00 48.99 N ANISOU 2148 N HIS B 284 6664 5676 6274 1420 696 959 N ATOM 2149 CA HIS B 284 11.370 22.222 -20.567 1.00 50.32 C ANISOU 2149 CA HIS B 284 6766 5960 6392 1668 776 1076 C ATOM 2150 C HIS B 284 11.475 23.651 -21.120 1.00 51.47 C ANISOU 2150 C HIS B 284 7096 5923 6538 1809 790 1144 C ATOM 2151 O HIS B 284 10.799 23.995 -22.092 1.00 52.12 O ANISOU 2151 O HIS B 284 7069 6127 6606 1924 809 1266 O ATOM 2152 CB HIS B 284 10.376 22.162 -19.393 1.00 51.38 C ANISOU 2152 CB HIS B 284 6895 6170 6456 1853 873 1065 C ATOM 2153 CG HIS B 284 10.914 22.704 -18.103 1.00 52.23 C ANISOU 2153 CG HIS B 284 7274 6030 6539 1896 896 954 C ATOM 2154 ND1 HIS B 284 10.890 24.047 -17.791 1.00 54.19 N ANISOU 2154 ND1 HIS B 284 7781 6055 6753 2088 940 954 N ATOM 2155 CD2 HIS B 284 11.478 22.083 -17.040 1.00 51.77 C ANISOU 2155 CD2 HIS B 284 7281 5913 6476 1776 877 838 C ATOM 2156 CE1 HIS B 284 11.427 24.230 -16.598 1.00 54.35 C ANISOU 2156 CE1 HIS B 284 8015 5888 6746 2072 942 834 C ATOM 2157 NE2 HIS B 284 11.790 23.054 -16.119 1.00 52.93 N ANISOU 2157 NE2 HIS B 284 7715 5814 6582 1887 904 765 N ATOM 2158 N GLU B 285 12.335 24.466 -20.513 1.00 51.56 N ANISOU 2158 N GLU B 285 7389 5639 6563 1789 775 1070 N ATOM 2159 CA GLU B 285 12.514 25.866 -20.922 1.00 52.88 C ANISOU 2159 CA GLU B 285 7779 5581 6732 1905 784 1128 C ATOM 2160 C GLU B 285 13.180 26.017 -22.299 1.00 51.75 C ANISOU 2160 C GLU B 285 7580 5436 6645 1759 713 1207 C ATOM 2161 O GLU B 285 13.180 27.104 -22.876 1.00 53.00 O ANISOU 2161 O GLU B 285 7879 5453 6805 1858 723 1292 O ATOM 2162 CB GLU B 285 13.285 26.649 -19.844 1.00 53.69 C ANISOU 2162 CB GLU B 285 8213 5359 6829 1891 772 1016 C ATOM 2163 CG GLU B 285 14.648 26.056 -19.469 1.00 52.61 C ANISOU 2163 CG GLU B 285 8115 5131 6744 1592 675 901 C ATOM 2164 CD GLU B 285 15.214 26.629 -18.177 1.00 53.46 C ANISOU 2164 CD GLU B 285 8516 4974 6823 1585 663 776 C ATOM 2165 OE1 GLU B 285 14.900 26.093 -17.089 1.00 53.16 O ANISOU 2165 OE1 GLU B 285 8472 4992 6735 1633 698 691 O ATOM 2166 OE2 GLU B 285 15.988 27.609 -18.256 1.00 55.32 O ANISOU 2166 OE2 GLU B 285 8992 4947 7082 1520 615 765 O ATOM 2167 N ASP B 286 13.732 24.919 -22.815 1.00 49.33 N ANISOU 2167 N ASP B 286 7078 5287 6379 1533 645 1183 N ATOM 2168 CA ASP B 286 14.424 24.907 -24.106 1.00 48.21 C ANISOU 2168 CA ASP B 286 6863 5176 6279 1384 580 1249 C ATOM 2169 C ASP B 286 13.618 24.207 -25.200 1.00 47.39 C ANISOU 2169 C ASP B 286 6478 5376 6153 1414 582 1342 C ATOM 2170 O ASP B 286 13.830 24.450 -26.389 1.00 47.50 O ANISOU 2170 O ASP B 286 6436 5437 6174 1379 551 1433 O ATOM 2171 CB ASP B 286 15.800 24.247 -23.967 1.00 46.67 C ANISOU 2171 CB ASP B 286 6674 4922 6135 1107 497 1152 C ATOM 2172 CG ASP B 286 16.790 25.105 -23.193 1.00 47.17 C ANISOU 2172 CG ASP B 286 7016 4683 6224 1034 469 1086 C ATOM 2173 OD1 ASP B 286 17.042 26.255 -23.611 1.00 48.35 O ANISOU 2173 OD1 ASP B 286 7335 4651 6385 1069 467 1156 O ATOM 2174 OD2 ASP B 286 17.327 24.624 -22.174 1.00 45.99 O ANISOU 2174 OD2 ASP B 286 6919 4475 6080 932 444 967 O ATOM 2175 N ILE B 287 12.702 23.336 -24.786 1.00 46.50 N ANISOU 2175 N ILE B 287 6190 5472 6007 1469 613 1321 N ATOM 2176 CA ILE B 287 11.853 22.584 -25.709 1.00 45.83 C ANISOU 2176 CA ILE B 287 5832 5688 5892 1480 604 1398 C ATOM 2177 C ILE B 287 10.626 23.410 -26.120 1.00 47.45 C ANISOU 2177 C ILE B 287 5994 5992 6044 1745 670 1536 C ATOM 2178 O ILE B 287 9.846 23.837 -25.265 1.00 48.62 O ANISOU 2178 O ILE B 287 6197 6120 6155 1942 748 1545 O ATOM 2179 CB ILE B 287 11.399 21.243 -25.073 1.00 44.69 C ANISOU 2179 CB ILE B 287 5514 5729 5736 1397 602 1325 C ATOM 2180 CG1 ILE B 287 12.617 20.408 -24.659 1.00 42.85 C ANISOU 2180 CG1 ILE B 287 5330 5400 5551 1157 538 1195 C ATOM 2181 CG2 ILE B 287 10.516 20.462 -26.033 1.00 44.50 C ANISOU 2181 CG2 ILE B 287 5218 6011 5678 1381 578 1401 C ATOM 2182 CD1 ILE B 287 12.310 19.292 -23.675 1.00 41.86 C ANISOU 2182 CD1 ILE B 287 5122 5366 5418 1093 548 1112 C ATOM 2183 N GLN B 288 10.452 23.634 -27.423 1.00 47.44 N ANISOU 2183 N GLN B 288 5891 6105 6027 1762 642 1648 N ATOM 2184 CA GLN B 288 9.269 24.363 -27.900 1.00 49.02 C ANISOU 2184 CA GLN B 288 6025 6431 6170 2021 698 1794 C ATOM 2185 C GLN B 288 8.050 23.464 -28.154 1.00 48.76 C ANISOU 2185 C GLN B 288 5689 6755 6083 2061 701 1846 C ATOM 2186 O GLN B 288 6.912 23.893 -27.958 1.00 50.43 O ANISOU 2186 O GLN B 288 5830 7091 6241 2297 770 1939 O ATOM 2187 CB GLN B 288 9.580 25.239 -29.126 1.00 49.93 C ANISOU 2187 CB GLN B 288 6203 6488 6282 2061 674 1913 C ATOM 2188 CG GLN B 288 9.966 24.473 -30.374 1.00 49.12 C ANISOU 2188 CG GLN B 288 5918 6568 6176 1869 590 1935 C ATOM 2189 CD GLN B 288 9.028 24.738 -31.541 1.00 50.74 C ANISOU 2189 CD GLN B 288 5957 7009 6315 2015 588 2094 C ATOM 2190 OE1 GLN B 288 7.928 25.270 -31.368 1.00 51.85 O ANISOU 2190 OE1 GLN B 288 6056 7236 6408 2258 650 2188 O ATOM 2191 NE2 GLN B 288 9.456 24.350 -32.738 1.00 50.42 N ANISOU 2191 NE2 GLN B 288 5812 7088 6258 1875 518 2127 N ATOM 2192 N ASP B 289 8.295 22.229 -28.587 1.00 46.68 N ANISOU 2192 N ASP B 289 5250 6656 5831 1831 625 1790 N ATOM 2193 CA ASP B 289 7.233 21.258 -28.832 1.00 46.38 C ANISOU 2193 CA ASP B 289 4930 6945 5746 1809 608 1827 C ATOM 2194 C ASP B 289 7.544 19.975 -28.072 1.00 44.57 C ANISOU 2194 C ASP B 289 4650 6738 5548 1597 577 1693 C ATOM 2195 O ASP B 289 8.474 19.252 -28.425 1.00 42.98 O ANISOU 2195 O ASP B 289 4463 6487 5381 1378 503 1605 O ATOM 2196 CB ASP B 289 7.103 20.983 -30.335 1.00 46.49 C ANISOU 2196 CB ASP B 289 4780 7161 5725 1738 530 1906 C ATOM 2197 CG ASP B 289 5.876 20.147 -30.690 1.00 47.03 C ANISOU 2197 CG ASP B 289 4555 7582 5731 1729 503 1966 C ATOM 2198 OD1 ASP B 289 5.169 19.658 -29.781 1.00 47.30 O ANISOU 2198 OD1 ASP B 289 4497 7717 5759 1749 542 1948 O ATOM 2199 OD2 ASP B 289 5.618 19.977 -31.900 1.00 47.27 O ANISOU 2199 OD2 ASP B 289 4445 7800 5715 1694 438 2038 O ATOM 2200 N ASP B 290 6.753 19.690 -27.039 1.00 44.87 N ANISOU 2200 N ASP B 290 4625 6857 5566 1673 637 1685 N ATOM 2201 CA ASP B 290 7.050 18.593 -26.116 1.00 43.31 C ANISOU 2201 CA ASP B 290 4416 6642 5397 1497 624 1565 C ATOM 2202 C ASP B 290 5.960 17.526 -25.981 1.00 43.67 C ANISOU 2202 C ASP B 290 4207 6981 5407 1435 617 1600 C ATOM 2203 O ASP B 290 5.889 16.855 -24.949 1.00 43.28 O ANISOU 2203 O ASP B 290 4155 6925 5366 1367 643 1536 O ATOM 2204 CB ASP B 290 7.403 19.156 -24.727 1.00 43.36 C ANISOU 2204 CB ASP B 290 4640 6415 5421 1597 701 1495 C ATOM 2205 CG ASP B 290 6.232 19.873 -24.050 1.00 44.95 C ANISOU 2205 CG ASP B 290 4817 6700 5562 1874 811 1582 C ATOM 2206 OD1 ASP B 290 6.349 20.167 -22.842 1.00 44.75 O ANISOU 2206 OD1 ASP B 290 4946 6527 5531 1959 878 1520 O ATOM 2207 OD2 ASP B 290 5.202 20.141 -24.707 1.00 46.04 O ANISOU 2207 OD2 ASP B 290 4784 7059 5652 2017 832 1714 O ATOM 2208 N HIS B 291 5.133 17.352 -27.012 1.00 44.57 N ANISOU 2208 N HIS B 291 4107 7354 5475 1445 577 1704 N ATOM 2209 CA HIS B 291 4.003 16.412 -26.928 1.00 45.36 C ANISOU 2209 CA HIS B 291 3947 7753 5534 1377 564 1757 C ATOM 2210 C HIS B 291 4.407 14.932 -26.927 1.00 43.91 C ANISOU 2210 C HIS B 291 3709 7595 5378 1075 476 1651 C ATOM 2211 O HIS B 291 3.655 14.086 -26.443 1.00 44.33 O ANISOU 2211 O HIS B 291 3608 7819 5414 988 477 1668 O ATOM 2212 CB HIS B 291 2.910 16.718 -27.969 1.00 47.20 C ANISOU 2212 CB HIS B 291 3956 8278 5699 1486 544 1911 C ATOM 2213 CG HIS B 291 3.273 16.359 -29.379 1.00 46.78 C ANISOU 2213 CG HIS B 291 3845 8295 5634 1335 428 1908 C ATOM 2214 ND1 HIS B 291 3.010 15.119 -29.923 1.00 46.41 N ANISOU 2214 ND1 HIS B 291 3629 8438 5568 1098 327 1879 N ATOM 2215 CD2 HIS B 291 3.841 17.091 -30.367 1.00 46.38 C ANISOU 2215 CD2 HIS B 291 3887 8156 5578 1393 400 1935 C ATOM 2216 CE1 HIS B 291 3.417 15.097 -31.180 1.00 46.32 C ANISOU 2216 CE1 HIS B 291 3614 8453 5532 1026 241 1877 C ATOM 2217 NE2 HIS B 291 3.923 16.282 -31.474 1.00 46.47 N ANISOU 2217 NE2 HIS B 291 3781 8315 5560 1203 286 1917 N ATOM 2218 N ASP B 292 5.590 14.633 -27.460 1.00 42.34 N ANISOU 2218 N ASP B 292 3642 7226 5220 922 403 1549 N ATOM 2219 CA ASP B 292 6.196 13.300 -27.334 1.00 41.10 C ANISOU 2219 CA ASP B 292 3499 7025 5093 664 330 1428 C ATOM 2220 C ASP B 292 7.724 13.377 -27.342 1.00 39.25 C ANISOU 2220 C ASP B 292 3484 6515 4912 590 306 1310 C ATOM 2221 O ASP B 292 8.293 14.457 -27.513 1.00 39.25 O ANISOU 2221 O ASP B 292 3617 6369 4927 713 337 1327 O ATOM 2222 CB ASP B 292 5.680 12.328 -28.412 1.00 41.67 C ANISOU 2222 CB ASP B 292 3384 7326 5123 493 226 1446 C ATOM 2223 CG ASP B 292 6.001 12.778 -29.830 1.00 42.28 C ANISOU 2223 CG ASP B 292 3456 7439 5169 513 165 1476 C ATOM 2224 OD1 ASP B 292 5.264 12.362 -30.744 1.00 44.57 O ANISOU 2224 OD1 ASP B 292 3571 7965 5401 449 94 1533 O ATOM 2225 OD2 ASP B 292 6.975 13.533 -30.045 1.00 41.84 O ANISOU 2225 OD2 ASP B 292 3567 7190 5141 582 184 1450 O ATOM 2226 N LEU B 293 8.378 12.231 -27.160 1.00 37.87 N ANISOU 2226 N LEU B 293 3348 6277 4764 389 249 1199 N ATOM 2227 CA LEU B 293 9.838 12.173 -27.076 1.00 36.10 C ANISOU 2227 CA LEU B 293 3310 5821 4586 315 226 1090 C ATOM 2228 C LEU B 293 10.536 12.673 -28.344 1.00 35.73 C ANISOU 2228 C LEU B 293 3298 5749 4529 319 182 1103 C ATOM 2229 O LEU B 293 11.488 13.457 -28.260 1.00 35.27 O ANISOU 2229 O LEU B 293 3389 5510 4503 369 204 1085 O ATOM 2230 CB LEU B 293 10.304 10.759 -26.725 1.00 34.97 C ANISOU 2230 CB LEU B 293 3185 5642 4462 116 173 981 C ATOM 2231 CG LEU B 293 11.810 10.551 -26.549 1.00 33.83 C ANISOU 2231 CG LEU B 293 3211 5285 4359 42 149 871 C ATOM 2232 CD1 LEU B 293 12.354 11.301 -25.329 1.00 32.98 C ANISOU 2232 CD1 LEU B 293 3253 4987 4290 134 218 846 C ATOM 2233 CD2 LEU B 293 12.130 9.064 -26.468 1.00 33.21 C ANISOU 2233 CD2 LEU B 293 3133 5204 4283 -139 87 778 C ATOM 2234 N TYR B 294 10.058 12.228 -29.506 1.00 35.98 N ANISOU 2234 N TYR B 294 3193 5969 4509 260 116 1138 N ATOM 2235 CA TYR B 294 10.627 12.658 -30.779 1.00 35.73 C ANISOU 2235 CA TYR B 294 3178 5948 4450 269 76 1162 C ATOM 2236 C TYR B 294 10.710 14.180 -30.855 1.00 36.31 C ANISOU 2236 C TYR B 294 3326 5936 4533 456 140 1258 C ATOM 2237 O TYR B 294 11.789 14.738 -31.083 1.00 35.83 O ANISOU 2237 O TYR B 294 3398 5715 4499 458 145 1240 O ATOM 2238 CB TYR B 294 9.833 12.106 -31.967 1.00 36.47 C ANISOU 2238 CB TYR B 294 3102 6289 4468 210 0 1205 C ATOM 2239 CG TYR B 294 10.277 12.678 -33.293 1.00 36.56 C ANISOU 2239 CG TYR B 294 3120 6339 4433 251 -31 1252 C ATOM 2240 CD1 TYR B 294 11.485 12.285 -33.875 1.00 35.64 C ANISOU 2240 CD1 TYR B 294 3097 6130 4312 154 -71 1168 C ATOM 2241 CD2 TYR B 294 9.499 13.624 -33.963 1.00 37.88 C ANISOU 2241 CD2 TYR B 294 3198 6642 4554 399 -15 1390 C ATOM 2242 CE1 TYR B 294 11.907 12.815 -35.093 1.00 35.84 C ANISOU 2242 CE1 TYR B 294 3125 6205 4287 193 -91 1221 C ATOM 2243 CE2 TYR B 294 9.910 14.160 -35.184 1.00 38.20 C ANISOU 2243 CE2 TYR B 294 3249 6721 4545 438 -42 1445 C ATOM 2244 CZ TYR B 294 11.114 13.750 -35.740 1.00 37.31 C ANISOU 2244 CZ TYR B 294 3228 6520 4427 329 -78 1360 C ATOM 2245 OH TYR B 294 11.526 14.272 -36.941 1.00 37.74 O ANISOU 2245 OH TYR B 294 3288 6627 4425 367 -97 1423 O ATOM 2246 N HIS B 295 9.572 14.839 -30.648 1.00 37.42 N ANISOU 2246 N HIS B 295 3384 6182 4650 613 190 1364 N ATOM 2247 CA HIS B 295 9.499 16.294 -30.693 1.00 38.17 C ANISOU 2247 CA HIS B 295 3563 6190 4748 815 255 1464 C ATOM 2248 C HIS B 295 10.248 16.963 -29.539 1.00 37.71 C ANISOU 2248 C HIS B 295 3717 5858 4752 869 319 1409 C ATOM 2249 O HIS B 295 10.809 18.046 -29.711 1.00 38.09 O ANISOU 2249 O HIS B 295 3909 5745 4818 955 346 1448 O ATOM 2250 CB HIS B 295 8.045 16.753 -30.752 1.00 39.79 C ANISOU 2250 CB HIS B 295 3618 6598 4901 990 295 1594 C ATOM 2251 CG HIS B 295 7.359 16.396 -32.035 1.00 40.74 C ANISOU 2251 CG HIS B 295 3543 6987 4950 958 224 1670 C ATOM 2252 ND1 HIS B 295 6.691 15.203 -32.216 1.00 40.88 N ANISOU 2252 ND1 HIS B 295 3380 7221 4933 812 159 1645 N ATOM 2253 CD2 HIS B 295 7.254 17.068 -33.206 1.00 41.30 C ANISOU 2253 CD2 HIS B 295 3578 7141 4971 1045 202 1772 C ATOM 2254 CE1 HIS B 295 6.199 15.158 -33.442 1.00 41.69 C ANISOU 2254 CE1 HIS B 295 3343 7535 4963 807 94 1719 C ATOM 2255 NE2 HIS B 295 6.527 16.277 -34.063 1.00 41.83 N ANISOU 2255 NE2 HIS B 295 3442 7483 4969 955 121 1800 N ATOM 2256 N ALA B 296 10.276 16.311 -28.377 1.00 36.93 N ANISOU 2256 N ALA B 296 3646 5705 4682 806 338 1321 N ATOM 2257 CA ALA B 296 11.008 16.827 -27.220 1.00 36.32 C ANISOU 2257 CA ALA B 296 3770 5378 4652 838 387 1254 C ATOM 2258 C ALA B 296 12.497 16.989 -27.526 1.00 35.29 C ANISOU 2258 C ALA B 296 3784 5060 4564 722 343 1190 C ATOM 2259 O ALA B 296 13.114 17.986 -27.144 1.00 35.41 O ANISOU 2259 O ALA B 296 3975 4873 4608 781 372 1191 O ATOM 2260 CB ALA B 296 10.803 15.926 -26.010 1.00 35.68 C ANISOU 2260 CB ALA B 296 3674 5302 4582 771 404 1172 C ATOM 2261 N ILE B 297 13.058 16.009 -28.231 1.00 34.44 N ANISOU 2261 N ILE B 297 3603 5027 4454 556 273 1138 N ATOM 2262 CA ILE B 297 14.478 16.010 -28.594 1.00 33.54 C ANISOU 2262 CA ILE B 297 3590 4784 4371 441 233 1084 C ATOM 2263 C ILE B 297 14.774 16.891 -29.815 1.00 34.31 C ANISOU 2263 C ILE B 297 3696 4890 4449 485 223 1179 C ATOM 2264 O ILE B 297 15.717 17.681 -29.796 1.00 34.30 O ANISOU 2264 O ILE B 297 3829 4721 4480 475 230 1190 O ATOM 2265 CB ILE B 297 14.998 14.566 -28.814 1.00 32.38 C ANISOU 2265 CB ILE B 297 3375 4708 4219 269 170 986 C ATOM 2266 CG1 ILE B 297 14.955 13.793 -27.491 1.00 31.56 C ANISOU 2266 CG1 ILE B 297 3304 4546 4142 218 183 895 C ATOM 2267 CG2 ILE B 297 16.408 14.569 -29.406 1.00 31.54 C ANISOU 2267 CG2 ILE B 297 3335 4522 4126 176 134 952 C ATOM 2268 CD1 ILE B 297 15.181 12.309 -27.624 1.00 31.20 C ANISOU 2268 CD1 ILE B 297 3195 4573 4086 71 126 809 C ATOM 2269 N THR B 298 13.960 16.765 -30.860 1.00 35.20 N ANISOU 2269 N THR B 298 3666 5203 4505 528 204 1256 N ATOM 2270 CA THR B 298 14.211 17.459 -32.128 1.00 36.05 C ANISOU 2270 CA THR B 298 3765 5352 4580 563 190 1353 C ATOM 2271 C THR B 298 13.908 18.960 -32.102 1.00 37.45 C ANISOU 2271 C THR B 298 4043 5420 4766 735 247 1472 C ATOM 2272 O THR B 298 14.422 19.710 -32.935 1.00 38.09 O ANISOU 2272 O THR B 298 4177 5458 4838 750 243 1552 O ATOM 2273 CB THR B 298 13.457 16.802 -33.300 1.00 36.44 C ANISOU 2273 CB THR B 298 3631 5662 4551 548 139 1393 C ATOM 2274 OG1 THR B 298 12.083 16.620 -32.945 1.00 37.43 O ANISOU 2274 OG1 THR B 298 3638 5932 4651 632 154 1430 O ATOM 2275 CG2 THR B 298 14.066 15.454 -33.632 1.00 35.67 C ANISOU 2275 CG2 THR B 298 3485 5631 4436 373 74 1278 C ATOM 2276 N THR B 299 13.080 19.398 -31.158 1.00 38.19 N ANISOU 2276 N THR B 299 4171 5468 4870 870 303 1488 N ATOM 2277 CA THR B 299 12.777 20.823 -31.029 1.00 39.84 C ANISOU 2277 CA THR B 299 4509 5545 5083 1056 362 1590 C ATOM 2278 C THR B 299 13.463 21.441 -29.810 1.00 39.91 C ANISOU 2278 C THR B 299 4742 5271 5150 1059 398 1522 C ATOM 2279 O THR B 299 13.063 22.510 -29.335 1.00 41.25 O ANISOU 2279 O THR B 299 5048 5306 5320 1229 456 1575 O ATOM 2280 CB THR B 299 11.250 21.107 -30.987 1.00 41.30 C ANISOU 2280 CB THR B 299 4581 5894 5216 1263 409 1686 C ATOM 2281 OG1 THR B 299 10.697 20.637 -29.750 1.00 41.27 O ANISOU 2281 OG1 THR B 299 4559 5899 5222 1292 447 1614 O ATOM 2282 CG2 THR B 299 10.529 20.455 -32.168 1.00 41.29 C ANISOU 2282 CG2 THR B 299 4346 6193 5148 1242 358 1752 C ATOM 2283 N ASN B 300 14.494 20.762 -29.311 1.00 38.79 N ANISOU 2283 N ASN B 300 4645 5043 5050 878 361 1402 N ATOM 2284 CA ASN B 300 15.278 21.250 -28.181 1.00 39.01 C ANISOU 2284 CA ASN B 300 4879 4817 5127 845 376 1327 C ATOM 2285 C ASN B 300 16.280 22.304 -28.654 1.00 39.95 C ANISOU 2285 C ASN B 300 5157 4748 5275 800 360 1381 C ATOM 2286 O ASN B 300 17.187 22.001 -29.435 1.00 39.43 O ANISOU 2286 O ASN B 300 5043 4719 5218 653 313 1387 O ATOM 2287 CB ASN B 300 15.994 20.085 -27.485 1.00 37.40 C ANISOU 2287 CB ASN B 300 4645 4615 4948 671 337 1190 C ATOM 2288 CG ASN B 300 16.566 20.456 -26.112 1.00 37.27 C ANISOU 2288 CG ASN B 300 4819 4375 4966 653 350 1103 C ATOM 2289 OD1 ASN B 300 16.704 21.633 -25.768 1.00 37.94 O ANISOU 2289 OD1 ASN B 300 5088 4267 5062 732 376 1132 O ATOM 2290 ND2 ASN B 300 16.906 19.435 -25.325 1.00 35.74 N ANISOU 2290 ND2 ASN B 300 4594 4201 4783 548 329 994 N ATOM 2291 N LYS B 301 16.110 23.536 -28.175 1.00 41.64 N ANISOU 2291 N LYS B 301 5566 4759 5497 927 402 1424 N ATOM 2292 CA LYS B 301 16.932 24.664 -28.629 1.00 42.95 C ANISOU 2292 CA LYS B 301 5903 4727 5690 888 389 1497 C ATOM 2293 C LYS B 301 18.396 24.606 -28.180 1.00 42.19 C ANISOU 2293 C LYS B 301 5914 4471 5645 668 335 1415 C ATOM 2294 O LYS B 301 19.252 25.252 -28.790 1.00 43.02 O ANISOU 2294 O LYS B 301 6096 4477 5773 569 308 1484 O ATOM 2295 CB LYS B 301 16.287 26.010 -28.264 1.00 44.89 C ANISOU 2295 CB LYS B 301 6352 4780 5924 1097 447 1566 C ATOM 2296 CG LYS B 301 15.107 26.366 -29.160 1.00 46.40 C ANISOU 2296 CG LYS B 301 6439 5128 6063 1306 490 1705 C ATOM 2297 CD LYS B 301 14.592 27.781 -28.926 1.00 48.60 C ANISOU 2297 CD LYS B 301 6943 5196 6328 1527 548 1789 C ATOM 2298 CE LYS B 301 13.501 28.136 -29.936 1.00 49.78 C ANISOU 2298 CE LYS B 301 6972 5522 6421 1737 585 1947 C ATOM 2299 NZ LYS B 301 13.065 29.555 -29.831 1.00 52.14 N ANISOU 2299 NZ LYS B 301 7506 5603 6704 1967 643 2045 N ATOM 2300 N SER B 302 18.688 23.836 -27.133 1.00 40.94 N ANISOU 2300 N SER B 302 5752 4302 5501 588 319 1282 N ATOM 2301 CA SER B 302 20.081 23.621 -26.727 1.00 40.17 C ANISOU 2301 CA SER B 302 5715 4103 5445 377 260 1207 C ATOM 2302 C SER B 302 20.719 22.427 -27.455 1.00 38.57 C ANISOU 2302 C SER B 302 5306 4108 5241 231 217 1185 C ATOM 2303 O SER B 302 21.815 21.987 -27.106 1.00 37.89 O ANISOU 2303 O SER B 302 5222 3996 5180 71 172 1118 O ATOM 2304 CB SER B 302 20.221 23.507 -25.197 1.00 39.94 C ANISOU 2304 CB SER B 302 5816 3936 5425 365 257 1078 C ATOM 2305 OG SER B 302 19.359 22.523 -24.656 1.00 39.07 O ANISOU 2305 OG SER B 302 5583 3975 5285 446 288 1013 O ATOM 2306 N TYR B 303 20.026 21.917 -28.471 1.00 38.13 N ANISOU 2306 N TYR B 303 5077 4263 5148 294 231 1243 N ATOM 2307 CA TYR B 303 20.562 20.869 -29.333 1.00 36.76 C ANISOU 2307 CA TYR B 303 4730 4282 4957 181 194 1229 C ATOM 2308 C TYR B 303 20.814 21.367 -30.757 1.00 37.44 C ANISOU 2308 C TYR B 303 4765 4443 5018 172 190 1356 C ATOM 2309 O TYR B 303 21.229 20.584 -31.620 1.00 36.98 O ANISOU 2309 O TYR B 303 4568 4554 4928 99 165 1355 O ATOM 2310 CB TYR B 303 19.622 19.658 -29.384 1.00 35.82 C ANISOU 2310 CB TYR B 303 4446 4363 4799 229 197 1174 C ATOM 2311 CG TYR B 303 19.662 18.731 -28.183 1.00 34.94 C ANISOU 2311 CG TYR B 303 4336 4232 4705 183 188 1044 C ATOM 2312 CD1 TYR B 303 18.666 17.769 -27.999 1.00 34.47 C ANISOU 2312 CD1 TYR B 303 4160 4320 4618 227 197 1003 C ATOM 2313 CD2 TYR B 303 20.681 18.814 -27.227 1.00 34.58 C ANISOU 2313 CD2 TYR B 303 4408 4031 4700 86 168 970 C ATOM 2314 CE1 TYR B 303 18.685 16.906 -26.907 1.00 33.63 C ANISOU 2314 CE1 TYR B 303 4060 4195 4524 182 193 897 C ATOM 2315 CE2 TYR B 303 20.705 17.957 -26.124 1.00 33.45 C ANISOU 2315 CE2 TYR B 303 4268 3876 4564 52 161 860 C ATOM 2316 CZ TYR B 303 19.704 17.006 -25.973 1.00 33.15 C ANISOU 2316 CZ TYR B 303 4120 3976 4499 104 177 827 C ATOM 2317 OH TYR B 303 19.713 16.151 -24.892 1.00 32.16 O ANISOU 2317 OH TYR B 303 4003 3839 4379 68 173 731 O ATOM 2318 N LYS B 304 20.562 22.653 -31.011 1.00 38.66 N ANISOU 2318 N LYS B 304 5040 4471 5178 255 217 1467 N ATOM 2319 CA LYS B 304 20.689 23.188 -32.375 1.00 39.31 C ANISOU 2319 CA LYS B 304 5080 4628 5229 264 219 1608 C ATOM 2320 C LYS B 304 22.146 23.348 -32.803 1.00 38.98 C ANISOU 2320 C LYS B 304 5055 4549 5208 83 188 1640 C ATOM 2321 O LYS B 304 23.000 23.727 -32.001 1.00 39.17 O ANISOU 2321 O LYS B 304 5202 4395 5284 -28 169 1601 O ATOM 2322 CB LYS B 304 19.890 24.488 -32.576 1.00 41.06 C ANISOU 2322 CB LYS B 304 5427 4731 5444 429 261 1733 C ATOM 2323 CG LYS B 304 20.536 25.762 -32.042 1.00 42.51 C ANISOU 2323 CG LYS B 304 5853 4618 5680 389 264 1774 C ATOM 2324 CD LYS B 304 20.338 26.934 -33.012 1.00 45.13 C ANISOU 2324 CD LYS B 304 6268 4886 5995 471 288 1952 C ATOM 2325 CE LYS B 304 18.876 27.396 -33.085 1.00 46.57 C ANISOU 2325 CE LYS B 304 6466 5092 6136 731 339 2017 C ATOM 2326 NZ LYS B 304 18.657 28.449 -34.118 1.00 47.42 N ANISOU 2326 NZ LYS B 304 6640 5161 6217 827 362 2201 N ATOM 2327 N GLY B 305 22.412 23.044 -34.071 1.00 38.65 N ANISOU 2327 N GLY B 305 4879 4691 5115 53 183 1715 N ATOM 2328 CA GLY B 305 23.758 23.123 -34.637 1.00 38.16 C ANISOU 2328 CA GLY B 305 4793 4651 5057 -106 164 1765 C ATOM 2329 C GLY B 305 24.650 21.948 -34.275 1.00 36.33 C ANISOU 2329 C GLY B 305 4461 4514 4828 -229 133 1641 C ATOM 2330 O GLY B 305 25.786 21.863 -34.746 1.00 36.56 O ANISOU 2330 O GLY B 305 4437 4604 4849 -350 121 1679 O ATOM 2331 N LEU B 306 24.135 21.043 -33.442 1.00 34.56 N ANISOU 2331 N LEU B 306 4210 4311 4612 -190 123 1503 N ATOM 2332 CA LEU B 306 24.902 19.893 -32.961 1.00 32.79 C ANISOU 2332 CA LEU B 306 3913 4153 4391 -285 94 1379 C ATOM 2333 C LEU B 306 24.867 18.733 -33.956 1.00 31.90 C ANISOU 2333 C LEU B 306 3636 4280 4203 -269 88 1351 C ATOM 2334 O LEU B 306 23.807 18.163 -34.228 1.00 31.50 O ANISOU 2334 O LEU B 306 3524 4332 4112 -178 90 1318 O ATOM 2335 CB LEU B 306 24.417 19.443 -31.575 1.00 31.85 C ANISOU 2335 CB LEU B 306 3856 3934 4311 -259 87 1251 C ATOM 2336 CG LEU B 306 24.408 20.434 -30.401 1.00 32.30 C ANISOU 2336 CG LEU B 306 4095 3749 4428 -262 90 1241 C ATOM 2337 CD1 LEU B 306 24.297 19.677 -29.090 1.00 31.46 C ANISOU 2337 CD1 LEU B 306 4016 3597 4342 -268 77 1102 C ATOM 2338 CD2 LEU B 306 25.617 21.374 -30.369 1.00 33.13 C ANISOU 2338 CD2 LEU B 306 4296 3721 4570 -398 67 1308 C ATOM 2339 N VAL B 307 26.044 18.389 -34.479 1.00 31.53 N ANISOU 2339 N VAL B 307 3521 4327 4133 -360 79 1364 N ATOM 2340 CA VAL B 307 26.175 17.439 -35.591 1.00 30.82 C ANISOU 2340 CA VAL B 307 3297 4459 3954 -337 78 1350 C ATOM 2341 C VAL B 307 26.973 16.171 -35.254 1.00 29.76 C ANISOU 2341 C VAL B 307 3103 4398 3804 -385 59 1228 C ATOM 2342 O VAL B 307 27.665 16.102 -34.237 1.00 29.33 O ANISOU 2342 O VAL B 307 3092 4242 3809 -454 45 1175 O ATOM 2343 CB VAL B 307 26.816 18.115 -36.827 1.00 31.86 C ANISOU 2343 CB VAL B 307 3382 4687 4035 -362 101 1497 C ATOM 2344 CG1 VAL B 307 25.895 19.185 -37.389 1.00 32.32 C ANISOU 2344 CG1 VAL B 307 3489 4707 4085 -284 120 1624 C ATOM 2345 CG2 VAL B 307 28.181 18.697 -36.474 1.00 32.14 C ANISOU 2345 CG2 VAL B 307 3445 4646 4121 -493 101 1554 C ATOM 2346 N HIS B 308 26.864 15.174 -36.126 1.00 29.36 N ANISOU 2346 N HIS B 308 2964 4525 3667 -340 55 1183 N ATOM 2347 CA HIS B 308 27.621 13.934 -35.995 1.00 28.54 C ANISOU 2347 CA HIS B 308 2814 4500 3531 -357 41 1073 C ATOM 2348 C HIS B 308 29.113 14.177 -36.214 1.00 28.93 C ANISOU 2348 C HIS B 308 2817 4602 3574 -422 58 1136 C ATOM 2349 O HIS B 308 29.487 15.053 -37.001 1.00 29.99 O ANISOU 2349 O HIS B 308 2921 4788 3686 -445 83 1269 O ATOM 2350 CB HIS B 308 27.125 12.905 -37.013 1.00 28.56 C ANISOU 2350 CB HIS B 308 2756 4670 3427 -288 32 1015 C ATOM 2351 CG HIS B 308 25.907 12.159 -36.574 1.00 27.82 C ANISOU 2351 CG HIS B 308 2689 4544 3337 -256 0 912 C ATOM 2352 ND1 HIS B 308 24.633 12.661 -36.723 1.00 28.66 N ANISOU 2352 ND1 HIS B 308 2797 4644 3446 -217 -5 957 N ATOM 2353 CD2 HIS B 308 25.769 10.946 -35.992 1.00 27.02 C ANISOU 2353 CD2 HIS B 308 2608 4422 3235 -261 -27 777 C ATOM 2354 CE1 HIS B 308 23.760 11.788 -36.252 1.00 27.88 C ANISOU 2354 CE1 HIS B 308 2705 4538 3349 -211 -35 857 C ATOM 2355 NE2 HIS B 308 24.424 10.739 -35.801 1.00 27.36 N ANISOU 2355 NE2 HIS B 308 2659 4452 3283 -244 -49 747 N ATOM 2356 N PRO B 309 29.976 13.407 -35.519 1.00 28.24 N ANISOU 2356 N PRO B 309 2716 4513 3502 -452 46 1052 N ATOM 2357 CA PRO B 309 31.399 13.474 -35.858 1.00 28.49 C ANISOU 2357 CA PRO B 309 2666 4651 3506 -499 64 1115 C ATOM 2358 C PRO B 309 31.626 12.774 -37.192 1.00 28.66 C ANISOU 2358 C PRO B 309 2601 4886 3404 -417 92 1120 C ATOM 2359 O PRO B 309 31.244 11.613 -37.365 1.00 28.05 O ANISOU 2359 O PRO B 309 2530 4861 3267 -337 81 1000 O ATOM 2360 CB PRO B 309 32.091 12.713 -34.716 1.00 27.79 C ANISOU 2360 CB PRO B 309 2587 4514 3458 -524 39 1014 C ATOM 2361 CG PRO B 309 31.026 12.411 -33.704 1.00 27.13 C ANISOU 2361 CG PRO B 309 2605 4272 3432 -506 10 908 C ATOM 2362 CD PRO B 309 29.713 12.460 -34.419 1.00 27.23 C ANISOU 2362 CD PRO B 309 2637 4299 3410 -441 17 911 C ATOM 2363 N VAL B 310 32.218 13.496 -38.138 1.00 29.45 N ANISOU 2363 N VAL B 310 2630 5102 3457 -439 127 1259 N ATOM 2364 CA VAL B 310 32.418 12.979 -39.488 1.00 29.66 C ANISOU 2364 CA VAL B 310 2578 5343 3350 -352 161 1279 C ATOM 2365 C VAL B 310 33.862 13.163 -39.942 1.00 30.54 C ANISOU 2365 C VAL B 310 2576 5614 3415 -383 205 1383 C ATOM 2366 O VAL B 310 34.623 13.905 -39.321 1.00 30.87 O ANISOU 2366 O VAL B 310 2596 5597 3538 -497 202 1468 O ATOM 2367 CB VAL B 310 31.430 13.620 -40.509 1.00 30.18 C ANISOU 2367 CB VAL B 310 2657 5447 3364 -315 170 1361 C ATOM 2368 CG1 VAL B 310 29.987 13.272 -40.152 1.00 29.10 C ANISOU 2368 CG1 VAL B 310 2601 5204 3251 -271 128 1258 C ATOM 2369 CG2 VAL B 310 31.613 15.131 -40.593 1.00 30.62 C ANISOU 2369 CG2 VAL B 310 2720 5434 3480 -404 189 1541 C ATOM 2370 N LYS B 311 34.231 12.468 -41.013 1.00 30.94 N ANISOU 2370 N LYS B 311 2554 5873 3330 -282 243 1375 N ATOM 2371 CA LYS B 311 35.543 12.628 -41.633 1.00 32.09 C ANISOU 2371 CA LYS B 311 2569 6218 3407 -287 298 1491 C ATOM 2372 C LYS B 311 35.426 12.622 -43.153 1.00 32.96 C ANISOU 2372 C LYS B 311 2627 6529 3365 -196 347 1559 C ATOM 2373 O LYS B 311 34.421 12.164 -43.695 1.00 32.70 O ANISOU 2373 O LYS B 311 2661 6499 3266 -110 328 1475 O ATOM 2374 CB LYS B 311 36.517 11.551 -41.146 1.00 32.17 C ANISOU 2374 CB LYS B 311 2525 6308 3389 -227 307 1397 C ATOM 2375 CG LYS B 311 36.151 10.116 -41.502 1.00 32.06 C ANISOU 2375 CG LYS B 311 2563 6349 3269 -63 305 1224 C ATOM 2376 CD LYS B 311 36.978 9.151 -40.664 1.00 32.53 C ANISOU 2376 CD LYS B 311 2609 6411 3342 -12 300 1128 C ATOM 2377 CE LYS B 311 36.777 7.700 -41.080 1.00 32.89 C ANISOU 2377 CE LYS B 311 2721 6506 3268 160 304 964 C ATOM 2378 NZ LYS B 311 37.493 6.770 -40.155 1.00 32.16 N ANISOU 2378 NZ LYS B 311 2638 6383 3199 219 296 871 N ATOM 2379 N ALA B 312 36.448 13.133 -43.833 1.00 34.13 N ANISOU 2379 N ALA B 312 2653 6858 3454 -221 407 1717 N ATOM 2380 CA ALA B 312 36.423 13.262 -45.290 1.00 35.20 C ANISOU 2380 CA ALA B 312 2733 7202 3438 -140 461 1809 C ATOM 2381 C ALA B 312 36.656 11.929 -45.996 1.00 35.42 C ANISOU 2381 C ALA B 312 2741 7417 3301 40 492 1682 C ATOM 2382 O ALA B 312 37.584 11.190 -45.662 1.00 35.58 O ANISOU 2382 O ALA B 312 2704 7520 3296 95 516 1627 O ATOM 2383 CB ALA B 312 37.434 14.297 -45.750 1.00 36.80 C ANISOU 2383 CB ALA B 312 2812 7537 3634 -240 519 2038 C ATOM 2384 N VAL B 313 35.794 11.627 -46.962 1.00 35.60 N ANISOU 2384 N VAL B 313 2819 7503 3204 137 486 1633 N ATOM 2385 CA VAL B 313 35.895 10.396 -47.753 1.00 36.28 C ANISOU 2385 CA VAL B 313 2921 7752 3112 312 508 1501 C ATOM 2386 C VAL B 313 35.667 10.686 -49.232 1.00 37.78 C ANISOU 2386 C VAL B 313 3080 8144 3130 386 548 1591 C ATOM 2387 O VAL B 313 35.295 11.802 -49.599 1.00 38.06 O ANISOU 2387 O VAL B 313 3092 8173 3196 303 552 1749 O ATOM 2388 CB VAL B 313 34.880 9.296 -47.293 1.00 35.03 C ANISOU 2388 CB VAL B 313 2911 7435 2963 365 429 1270 C ATOM 2389 CG1 VAL B 313 35.309 8.658 -45.971 1.00 33.53 C ANISOU 2389 CG1 VAL B 313 2751 7098 2891 344 405 1161 C ATOM 2390 CG2 VAL B 313 33.456 9.849 -47.215 1.00 33.76 C ANISOU 2390 CG2 VAL B 313 2829 7125 2872 288 361 1269 C ATOM 2391 N ASP B 314 35.897 9.681 -50.073 1.00 38.89 N ANISOU 2391 N ASP B 314 3234 8459 3085 549 578 1490 N ATOM 2392 CA ASP B 314 35.516 9.754 -51.479 1.00 40.51 C ANISOU 2392 CA ASP B 314 3441 8851 3101 639 600 1531 C ATOM 2393 C ASP B 314 34.028 10.094 -51.609 1.00 39.88 C ANISOU 2393 C ASP B 314 3457 8642 3055 581 514 1501 C ATOM 2394 O ASP B 314 33.168 9.421 -51.035 1.00 38.58 O ANISOU 2394 O ASP B 314 3402 8312 2945 571 433 1330 O ATOM 2395 CB ASP B 314 35.847 8.441 -52.206 1.00 41.59 C ANISOU 2395 CB ASP B 314 3625 9146 3030 833 627 1372 C ATOM 2396 CG ASP B 314 35.133 8.309 -53.548 1.00 43.16 C ANISOU 2396 CG ASP B 314 3879 9492 3028 923 614 1350 C ATOM 2397 OD1 ASP B 314 35.169 9.259 -54.360 1.00 44.53 O ANISOU 2397 OD1 ASP B 314 3968 9811 3140 901 658 1537 O ATOM 2398 OD2 ASP B 314 34.532 7.244 -53.792 1.00 43.65 O ANISOU 2398 OD2 ASP B 314 4075 9521 2989 1011 556 1146 O ATOM 2399 N ALA B 315 33.758 11.161 -52.356 1.00 41.00 N ANISOU 2399 N ALA B 315 3547 8869 3163 543 536 1683 N ATOM 2400 CA ALA B 315 32.402 11.645 -52.655 1.00 41.06 C ANISOU 2400 CA ALA B 315 3616 8804 3179 510 466 1700 C ATOM 2401 C ALA B 315 31.600 12.188 -51.460 1.00 39.36 C ANISOU 2401 C ALA B 315 3454 8318 3183 384 400 1694 C ATOM 2402 O ALA B 315 30.371 12.233 -51.496 1.00 38.91 O ANISOU 2402 O ALA B 315 3458 8190 3138 378 330 1648 O ATOM 2403 CB ALA B 315 31.589 10.595 -53.470 1.00 41.79 C ANISOU 2403 CB ALA B 315 3796 8992 3092 622 407 1525 C ATOM 2404 N GLY B 316 32.298 12.624 -50.418 1.00 38.75 N ANISOU 2404 N GLY B 316 3347 8106 3269 288 424 1746 N ATOM 2405 CA GLY B 316 31.651 13.370 -49.346 1.00 37.68 C ANISOU 2405 CA GLY B 316 3262 7724 3329 174 378 1775 C ATOM 2406 C GLY B 316 32.220 13.194 -47.955 1.00 36.62 C ANISOU 2406 C GLY B 316 3143 7416 3357 94 369 1708 C ATOM 2407 O GLY B 316 33.430 13.305 -47.730 1.00 37.01 O ANISOU 2407 O GLY B 316 3119 7518 3426 58 419 1771 O ATOM 2408 N VAL B 317 31.314 12.916 -47.025 1.00 35.45 N ANISOU 2408 N VAL B 317 3081 7074 3316 65 302 1585 N ATOM 2409 CA VAL B 317 31.604 12.833 -45.600 1.00 34.41 C ANISOU 2409 CA VAL B 317 2983 6748 3342 -14 281 1519 C ATOM 2410 C VAL B 317 31.094 11.493 -45.043 1.00 33.58 C ANISOU 2410 C VAL B 317 2949 6576 3234 36 229 1300 C ATOM 2411 O VAL B 317 30.070 10.975 -45.500 1.00 33.51 O ANISOU 2411 O VAL B 317 2986 6589 3155 87 185 1214 O ATOM 2412 CB VAL B 317 30.996 14.072 -44.871 1.00 33.91 C ANISOU 2412 CB VAL B 317 2969 6483 3431 -113 260 1619 C ATOM 2413 CG1 VAL B 317 30.041 13.685 -43.745 1.00 32.01 C ANISOU 2413 CG1 VAL B 317 2819 6048 3296 -127 200 1480 C ATOM 2414 CG2 VAL B 317 32.094 15.021 -44.407 1.00 34.29 C ANISOU 2414 CG2 VAL B 317 2980 6479 3569 -226 297 1760 C ATOM 2415 N ALA B 318 31.827 10.927 -44.087 1.00 33.17 N ANISOU 2415 N ALA B 318 2903 6450 3251 16 230 1218 N ATOM 2416 CA ALA B 318 31.467 9.643 -43.480 1.00 32.72 C ANISOU 2416 CA ALA B 318 2924 6312 3197 57 185 1022 C ATOM 2417 C ALA B 318 31.589 9.701 -41.963 1.00 31.95 C ANISOU 2417 C ALA B 318 2864 6016 3259 -23 161 981 C ATOM 2418 O ALA B 318 32.430 10.441 -41.446 1.00 32.06 O ANISOU 2418 O ALA B 318 2828 6002 3351 -93 186 1081 O ATOM 2419 CB ALA B 318 32.330 8.525 -44.033 1.00 33.39 C ANISOU 2419 CB ALA B 318 2995 6545 3148 170 215 936 C ATOM 2420 N PRO B 319 30.749 8.925 -41.243 1.00 31.38 N ANISOU 2420 N PRO B 319 2881 5812 3231 -24 107 839 N ATOM 2421 CA PRO B 319 30.766 8.949 -39.782 1.00 30.64 C ANISOU 2421 CA PRO B 319 2831 5533 3277 -93 84 797 C ATOM 2422 C PRO B 319 32.137 8.631 -39.214 1.00 31.13 C ANISOU 2422 C PRO B 319 2855 5615 3358 -89 110 792 C ATOM 2423 O PRO B 319 32.833 7.742 -39.713 1.00 31.53 O ANISOU 2423 O PRO B 319 2884 5787 3310 2 132 737 O ATOM 2424 CB PRO B 319 29.765 7.852 -39.394 1.00 30.00 C ANISOU 2424 CB PRO B 319 2841 5365 3193 -72 32 640 C ATOM 2425 CG PRO B 319 29.591 7.025 -40.627 1.00 30.66 C ANISOU 2425 CG PRO B 319 2934 5593 3123 12 26 575 C ATOM 2426 CD PRO B 319 29.730 7.989 -41.750 1.00 31.35 C ANISOU 2426 CD PRO B 319 2941 5827 3142 27 62 716 C ATOM 2427 N ASP B 320 32.512 9.383 -38.185 1.00 31.45 N ANISOU 2427 N ASP B 320 2888 5542 3518 -182 105 850 N ATOM 2428 CA ASP B 320 33.770 9.195 -37.486 1.00 32.36 C ANISOU 2428 CA ASP B 320 2955 5674 3665 -200 116 857 C ATOM 2429 C ASP B 320 33.471 8.546 -36.148 1.00 32.03 C ANISOU 2429 C ASP B 320 3000 5466 3704 -215 73 737 C ATOM 2430 O ASP B 320 33.081 9.221 -35.192 1.00 31.42 O ANISOU 2430 O ASP B 320 2970 5236 3732 -303 46 753 O ATOM 2431 CB ASP B 320 34.474 10.544 -37.297 1.00 32.75 C ANISOU 2431 CB ASP B 320 2938 5723 3782 -318 130 1016 C ATOM 2432 CG ASP B 320 35.736 10.446 -36.452 1.00 33.11 C ANISOU 2432 CG ASP B 320 2921 5789 3868 -365 126 1031 C ATOM 2433 OD1 ASP B 320 36.087 11.454 -35.802 1.00 33.11 O ANISOU 2433 OD1 ASP B 320 2916 5708 3959 -495 106 1118 O ATOM 2434 OD2 ASP B 320 36.378 9.375 -36.429 1.00 33.25 O ANISOU 2434 OD2 ASP B 320 2904 5904 3826 -270 137 959 O ATOM 2435 N PHE B 321 33.631 7.227 -36.091 1.00 33.13 N ANISOU 2435 N PHE B 321 3173 5629 3785 -120 67 616 N ATOM 2436 CA PHE B 321 33.479 6.493 -34.834 1.00 33.48 C ANISOU 2436 CA PHE B 321 3299 5528 3894 -125 31 511 C ATOM 2437 C PHE B 321 34.773 6.607 -34.026 1.00 34.56 C ANISOU 2437 C PHE B 321 3372 5690 4070 -146 35 552 C ATOM 2438 O PHE B 321 35.654 7.403 -34.355 1.00 35.62 O ANISOU 2438 O PHE B 321 3399 5936 4200 -189 59 670 O ATOM 2439 CB PHE B 321 33.096 5.028 -35.086 1.00 33.44 C ANISOU 2439 CB PHE B 321 3379 5515 3811 -22 18 370 C ATOM 2440 CG PHE B 321 31.929 4.853 -36.025 1.00 33.52 C ANISOU 2440 CG PHE B 321 3435 5539 3761 -9 4 331 C ATOM 2441 CD1 PHE B 321 32.136 4.457 -37.342 1.00 34.48 C ANISOU 2441 CD1 PHE B 321 3537 5813 3750 80 27 320 C ATOM 2442 CD2 PHE B 321 30.626 5.087 -35.593 1.00 32.72 C ANISOU 2442 CD2 PHE B 321 3392 5316 3726 -83 -33 309 C ATOM 2443 CE1 PHE B 321 31.059 4.293 -38.219 1.00 35.04 C ANISOU 2443 CE1 PHE B 321 3650 5908 3754 82 2 282 C ATOM 2444 CE2 PHE B 321 29.542 4.926 -36.461 1.00 33.03 C ANISOU 2444 CE2 PHE B 321 3455 5391 3704 -80 -55 282 C ATOM 2445 CZ PHE B 321 29.760 4.528 -37.775 1.00 34.10 C ANISOU 2445 CZ PHE B 321 3576 5674 3708 -4 -43 266 C ATOM 2446 N GLY B 322 34.905 5.817 -32.975 1.00 35.00 N ANISOU 2446 N GLY B 322 3488 5653 4159 -124 8 465 N ATOM 2447 CA GLY B 322 36.008 6.029 -32.051 1.00 36.49 C ANISOU 2447 CA GLY B 322 3617 5856 4393 -162 -3 508 C ATOM 2448 C GLY B 322 35.485 7.026 -31.042 1.00 36.73 C ANISOU 2448 C GLY B 322 3696 5726 4534 -299 -40 536 C ATOM 2449 O GLY B 322 34.871 6.627 -30.038 1.00 36.23 O ANISOU 2449 O GLY B 322 3730 5514 4519 -308 -71 455 O ATOM 2450 N ASN B 323 35.677 8.319 -31.326 1.00 37.60 N ANISOU 2450 N ASN B 323 3752 5857 4679 -401 -35 652 N ATOM 2451 CA ASN B 323 35.140 9.409 -30.485 1.00 37.69 C ANISOU 2451 CA ASN B 323 3833 5701 4786 -522 -66 682 C ATOM 2452 C ASN B 323 35.065 9.084 -28.973 1.00 37.04 C ANISOU 2452 C ASN B 323 3833 5478 4761 -548 -110 602 C ATOM 2453 O ASN B 323 35.963 8.427 -28.435 1.00 37.40 O ANISOU 2453 O ASN B 323 3838 5580 4790 -523 -126 576 O ATOM 2454 CB ASN B 323 33.793 9.928 -31.033 1.00 37.42 C ANISOU 2454 CB ASN B 323 3866 5587 4763 -520 -52 689 C ATOM 2455 CG ASN B 323 32.741 8.823 -31.209 1.00 37.33 C ANISOU 2455 CG ASN B 323 3917 5552 4715 -424 -50 576 C ATOM 2456 OD1 ASN B 323 31.996 8.814 -32.192 1.00 38.42 O ANISOU 2456 OD1 ASN B 323 4052 5739 4808 -384 -33 584 O ATOM 2457 ND2 ASN B 323 32.671 7.902 -30.256 1.00 37.07 N ANISOU 2457 ND2 ASN B 323 3942 5445 4697 -397 -73 477 N ATOM 2458 N ARG B 324 34.021 9.551 -28.292 1.00 36.24 N ANISOU 2458 N ARG B 324 3842 5209 4719 -587 -125 570 N ATOM 2459 CA ARG B 324 33.807 9.189 -26.890 1.00 35.86 C ANISOU 2459 CA ARG B 324 3881 5034 4711 -597 -159 490 C ATOM 2460 C ARG B 324 32.373 8.757 -26.642 1.00 34.32 C ANISOU 2460 C ARG B 324 3781 4732 4527 -547 -148 415 C ATOM 2461 O ARG B 324 32.042 8.250 -25.568 1.00 33.93 O ANISOU 2461 O ARG B 324 3804 4591 4498 -538 -166 346 O ATOM 2462 CB ARG B 324 34.246 10.308 -25.937 1.00 36.24 C ANISOU 2462 CB ARG B 324 3966 4987 4817 -716 -197 534 C ATOM 2463 CG ARG B 324 35.748 10.242 -25.628 1.00 38.24 C ANISOU 2463 CG ARG B 324 4125 5348 5057 -769 -231 573 C ATOM 2464 CD ARG B 324 36.291 11.461 -24.883 1.00 39.35 C ANISOU 2464 CD ARG B 324 4295 5411 5245 -921 -282 628 C ATOM 2465 NE ARG B 324 37.755 11.502 -24.953 1.00 43.71 N ANISOU 2465 NE ARG B 324 4711 6119 5776 -989 -312 700 N ATOM 2466 CZ ARG B 324 38.537 12.338 -24.267 1.00 45.87 C ANISOU 2466 CZ ARG B 324 4981 6370 6079 -1139 -374 748 C ATOM 2467 NH1 ARG B 324 38.010 13.234 -23.436 1.00 46.48 N ANISOU 2467 NH1 ARG B 324 5208 6249 6202 -1230 -413 722 N ATOM 2468 NH2 ARG B 324 39.857 12.274 -24.413 1.00 47.08 N ANISOU 2468 NH2 ARG B 324 4980 6704 6205 -1198 -400 824 N ATOM 2469 N TYR B 325 31.536 8.936 -27.660 1.00 33.55 N ANISOU 2469 N TYR B 325 3673 4665 4409 -517 -120 438 N ATOM 2470 CA TYR B 325 30.191 8.383 -27.678 1.00 32.11 C ANISOU 2470 CA TYR B 325 3545 4433 4222 -471 -112 377 C ATOM 2471 C TYR B 325 30.223 6.867 -27.541 1.00 31.36 C ANISOU 2471 C TYR B 325 3468 4360 4086 -413 -122 283 C ATOM 2472 O TYR B 325 29.291 6.274 -27.004 1.00 30.99 O ANISOU 2472 O TYR B 325 3484 4239 4051 -405 -128 223 O ATOM 2473 CB TYR B 325 29.482 8.760 -28.976 1.00 32.39 C ANISOU 2473 CB TYR B 325 3541 4543 4223 -447 -89 426 C ATOM 2474 CG TYR B 325 29.352 10.247 -29.206 1.00 32.71 C ANISOU 2474 CG TYR B 325 3580 4548 4298 -490 -76 530 C ATOM 2475 CD1 TYR B 325 30.005 10.868 -30.268 1.00 33.23 C ANISOU 2475 CD1 TYR B 325 3577 4715 4336 -505 -60 622 C ATOM 2476 CD2 TYR B 325 28.573 11.034 -28.362 1.00 32.59 C ANISOU 2476 CD2 TYR B 325 3646 4397 4341 -507 -75 539 C ATOM 2477 CE1 TYR B 325 29.880 12.239 -30.484 1.00 34.15 C ANISOU 2477 CE1 TYR B 325 3712 4779 4485 -549 -49 726 C ATOM 2478 CE2 TYR B 325 28.444 12.396 -28.567 1.00 33.15 C ANISOU 2478 CE2 TYR B 325 3745 4411 4441 -534 -63 632 C ATOM 2479 CZ TYR B 325 29.097 12.998 -29.627 1.00 33.87 C ANISOU 2479 CZ TYR B 325 3774 4585 4509 -561 -52 727 C ATOM 2480 OH TYR B 325 28.969 14.356 -29.822 1.00 34.32 O ANISOU 2480 OH TYR B 325 3878 4566 4597 -592 -42 827 O ATOM 2481 N LEU B 326 31.297 6.249 -28.031 1.00 31.19 N ANISOU 2481 N LEU B 326 3394 4442 4015 -370 -120 276 N ATOM 2482 CA LEU B 326 31.447 4.796 -27.982 1.00 30.59 C ANISOU 2482 CA LEU B 326 3356 4376 3892 -296 -128 187 C ATOM 2483 C LEU B 326 32.630 4.328 -27.129 1.00 30.58 C ANISOU 2483 C LEU B 326 3347 4379 3891 -270 -142 174 C ATOM 2484 O LEU B 326 32.486 3.381 -26.354 1.00 30.54 O ANISOU 2484 O LEU B 326 3418 4297 3888 -238 -158 105 O ATOM 2485 CB LEU B 326 31.517 4.193 -29.390 1.00 31.05 C ANISOU 2485 CB LEU B 326 3382 4553 3863 -224 -111 170 C ATOM 2486 CG LEU B 326 30.360 4.439 -30.374 1.00 30.93 C ANISOU 2486 CG LEU B 326 3368 4561 3821 -238 -106 175 C ATOM 2487 CD1 LEU B 326 30.498 3.539 -31.589 1.00 31.27 C ANISOU 2487 CD1 LEU B 326 3412 4708 3760 -158 -101 126 C ATOM 2488 CD2 LEU B 326 28.988 4.238 -29.738 1.00 29.79 C ANISOU 2488 CD2 LEU B 326 3296 4301 3721 -285 -127 132 C ATOM 2489 N THR B 327 33.787 4.980 -27.245 1.00 30.59 N ANISOU 2489 N THR B 327 3255 4477 3891 -289 -140 247 N ATOM 2490 CA THR B 327 34.961 4.552 -26.462 1.00 30.32 C ANISOU 2490 CA THR B 327 3190 4481 3850 -261 -159 246 C ATOM 2491 C THR B 327 34.780 4.775 -24.962 1.00 29.31 C ANISOU 2491 C THR B 327 3132 4221 3783 -326 -197 226 C ATOM 2492 O THR B 327 35.527 4.217 -24.162 1.00 29.54 O ANISOU 2492 O THR B 327 3160 4262 3802 -293 -220 209 O ATOM 2493 CB THR B 327 36.297 5.205 -26.921 1.00 31.33 C ANISOU 2493 CB THR B 327 3175 4772 3956 -282 -153 345 C ATOM 2494 OG1 THR B 327 36.218 6.628 -26.779 1.00 31.60 O ANISOU 2494 OG1 THR B 327 3186 4770 4049 -418 -167 424 O ATOM 2495 CG2 THR B 327 36.632 4.840 -28.362 1.00 31.57 C ANISOU 2495 CG2 THR B 327 3130 4960 3904 -190 -106 366 C ATOM 2496 N GLU B 328 33.795 5.592 -24.590 1.00 28.21 N ANISOU 2496 N GLU B 328 3054 3966 3697 -405 -200 230 N ATOM 2497 CA GLU B 328 33.464 5.822 -23.178 1.00 27.29 C ANISOU 2497 CA GLU B 328 3022 3721 3625 -454 -229 202 C ATOM 2498 C GLU B 328 32.105 5.239 -22.817 1.00 26.00 C ANISOU 2498 C GLU B 328 2959 3449 3473 -429 -213 138 C ATOM 2499 O GLU B 328 32.004 4.429 -21.900 1.00 25.60 O ANISOU 2499 O GLU B 328 2972 3338 3418 -402 -226 89 O ATOM 2500 CB GLU B 328 33.503 7.310 -22.839 1.00 27.61 C ANISOU 2500 CB GLU B 328 3069 3710 3713 -561 -245 260 C ATOM 2501 CG GLU B 328 34.883 7.850 -22.511 1.00 29.25 C ANISOU 2501 CG GLU B 328 3206 3988 3921 -630 -286 314 C ATOM 2502 CD GLU B 328 35.059 8.175 -21.035 1.00 30.63 C ANISOU 2502 CD GLU B 328 3457 4063 4116 -691 -335 287 C ATOM 2503 OE1 GLU B 328 36.201 8.041 -20.533 1.00 31.32 O ANISOU 2503 OE1 GLU B 328 3486 4228 4186 -719 -380 305 O ATOM 2504 OE2 GLU B 328 34.062 8.573 -20.383 1.00 30.07 O ANISOU 2504 OE2 GLU B 328 3500 3853 4071 -705 -330 251 O ATOM 2505 N ASP B 329 31.072 5.638 -23.556 1.00 25.27 N ANISOU 2505 N ASP B 329 2869 3344 3389 -438 -187 151 N ATOM 2506 CA ASP B 329 29.695 5.235 -23.267 1.00 24.40 C ANISOU 2506 CA ASP B 329 2827 3155 3289 -431 -173 110 C ATOM 2507 C ASP B 329 29.441 3.726 -23.340 1.00 24.02 C ANISOU 2507 C ASP B 329 2817 3103 3206 -384 -177 43 C ATOM 2508 O ASP B 329 28.465 3.239 -22.771 1.00 23.77 O ANISOU 2508 O ASP B 329 2847 3000 3185 -396 -173 13 O ATOM 2509 CB ASP B 329 28.710 5.981 -24.174 1.00 24.56 C ANISOU 2509 CB ASP B 329 2818 3196 3316 -444 -148 150 C ATOM 2510 CG ASP B 329 28.615 7.472 -23.856 1.00 25.19 C ANISOU 2510 CG ASP B 329 2909 3225 3438 -485 -141 212 C ATOM 2511 OD1 ASP B 329 27.634 8.111 -24.303 1.00 25.20 O ANISOU 2511 OD1 ASP B 329 2907 3218 3448 -479 -118 247 O ATOM 2512 OD2 ASP B 329 29.512 8.010 -23.165 1.00 26.12 O ANISOU 2512 OD2 ASP B 329 3044 3308 3575 -524 -162 226 O ATOM 2513 N ILE B 330 30.301 2.985 -24.033 1.00 24.04 N ANISOU 2513 N ILE B 330 2791 3180 3161 -327 -183 25 N ATOM 2514 CA ILE B 330 30.189 1.523 -24.028 1.00 23.91 C ANISOU 2514 CA ILE B 330 2846 3131 3107 -274 -191 -45 C ATOM 2515 C ILE B 330 30.915 0.892 -22.821 1.00 23.94 C ANISOU 2515 C ILE B 330 2902 3080 3114 -240 -209 -65 C ATOM 2516 O ILE B 330 30.250 0.352 -21.931 1.00 23.79 O ANISOU 2516 O ILE B 330 2967 2961 3112 -261 -214 -92 O ATOM 2517 CB ILE B 330 30.599 0.859 -25.382 1.00 24.44 C ANISOU 2517 CB ILE B 330 2892 3289 3104 -203 -185 -72 C ATOM 2518 CG1 ILE B 330 29.811 1.454 -26.559 1.00 24.24 C ANISOU 2518 CG1 ILE B 330 2818 3326 3065 -236 -174 -50 C ATOM 2519 CG2 ILE B 330 30.421 -0.653 -25.321 1.00 24.57 C ANISOU 2519 CG2 ILE B 330 3020 3235 3080 -150 -199 -152 C ATOM 2520 CD1 ILE B 330 28.301 1.334 -26.442 1.00 23.97 C ANISOU 2520 CD1 ILE B 330 2829 3224 3053 -303 -183 -69 C ATOM 2521 N PRO B 331 32.266 0.976 -22.767 1.00 24.12 N ANISOU 2521 N PRO B 331 2866 3181 3116 -191 -217 -40 N ATOM 2522 CA PRO B 331 32.922 0.287 -21.655 1.00 24.21 C ANISOU 2522 CA PRO B 331 2925 3153 3119 -145 -238 -55 C ATOM 2523 C PRO B 331 32.648 0.926 -20.288 1.00 23.77 C ANISOU 2523 C PRO B 331 2902 3020 3109 -219 -256 -38 C ATOM 2524 O PRO B 331 32.595 0.217 -19.277 1.00 23.83 O ANISOU 2524 O PRO B 331 2988 2956 3111 -196 -269 -61 O ATOM 2525 CB PRO B 331 34.413 0.379 -22.011 1.00 24.83 C ANISOU 2525 CB PRO B 331 2901 3372 3161 -78 -243 -17 C ATOM 2526 CG PRO B 331 34.527 1.552 -22.882 1.00 24.61 C ANISOU 2526 CG PRO B 331 2769 3436 3147 -140 -230 38 C ATOM 2527 CD PRO B 331 33.243 1.656 -23.641 1.00 24.47 C ANISOU 2527 CD PRO B 331 2793 3365 3139 -175 -208 13 C ATOM 2528 N MET B 332 32.468 2.246 -20.269 1.00 23.30 N ANISOU 2528 N MET B 332 2796 2971 3086 -301 -256 2 N ATOM 2529 CA MET B 332 32.284 2.990 -19.025 1.00 22.84 C ANISOU 2529 CA MET B 332 2780 2841 3058 -363 -274 12 C ATOM 2530 C MET B 332 30.827 3.417 -18.867 1.00 22.06 C ANISOU 2530 C MET B 332 2740 2655 2989 -404 -244 3 C ATOM 2531 O MET B 332 30.508 4.308 -18.080 1.00 21.85 O ANISOU 2531 O MET B 332 2749 2571 2983 -449 -245 14 O ATOM 2532 CB MET B 332 33.214 4.210 -18.986 1.00 23.36 C ANISOU 2532 CB MET B 332 2775 2964 3136 -426 -302 62 C ATOM 2533 CG MET B 332 34.663 3.905 -19.321 1.00 24.12 C ANISOU 2533 CG MET B 332 2773 3193 3200 -391 -327 93 C ATOM 2534 SD MET B 332 35.547 3.191 -17.929 1.00 25.49 S ANISOU 2534 SD MET B 332 2972 3373 3342 -351 -376 78 S ATOM 2535 CE MET B 332 37.037 2.602 -18.718 1.00 26.19 C ANISOU 2535 CE MET B 332 2920 3649 3380 -262 -382 121 C ATOM 2536 N GLY B 333 29.946 2.763 -19.615 1.00 21.76 N ANISOU 2536 N GLY B 333 2710 2613 2945 -386 -218 -17 N ATOM 2537 CA GLY B 333 28.530 3.094 -19.597 1.00 21.29 C ANISOU 2537 CA GLY B 333 2676 2507 2908 -419 -188 -12 C ATOM 2538 C GLY B 333 27.622 1.894 -19.778 1.00 21.22 C ANISOU 2538 C GLY B 333 2707 2472 2885 -414 -179 -45 C ATOM 2539 O GLY B 333 27.120 1.339 -18.797 1.00 21.35 O ANISOU 2539 O GLY B 333 2788 2422 2902 -425 -173 -57 O ATOM 2540 N MET B 334 27.416 1.496 -21.032 1.00 21.07 N ANISOU 2540 N MET B 334 2653 2505 2846 -408 -180 -57 N ATOM 2541 CA MET B 334 26.453 0.445 -21.373 1.00 21.25 C ANISOU 2541 CA MET B 334 2718 2504 2853 -431 -182 -89 C ATOM 2542 C MET B 334 26.804 -0.913 -20.770 1.00 21.37 C ANISOU 2542 C MET B 334 2831 2443 2847 -409 -201 -132 C ATOM 2543 O MET B 334 25.925 -1.610 -20.251 1.00 21.52 O ANISOU 2543 O MET B 334 2909 2396 2870 -457 -200 -138 O ATOM 2544 CB MET B 334 26.273 0.324 -22.893 1.00 21.46 C ANISOU 2544 CB MET B 334 2699 2607 2847 -428 -191 -102 C ATOM 2545 CG MET B 334 25.524 1.486 -23.532 1.00 21.17 C ANISOU 2545 CG MET B 334 2578 2640 2827 -456 -173 -51 C ATOM 2546 SD MET B 334 24.849 1.080 -25.156 1.00 22.44 S ANISOU 2546 SD MET B 334 2700 2889 2936 -473 -192 -69 S ATOM 2547 CE MET B 334 23.482 0.014 -24.721 1.00 22.56 C ANISOU 2547 CE MET B 334 2769 2850 2952 -556 -212 -97 C ATOM 2548 N ILE B 335 28.085 -1.275 -20.831 1.00 21.34 N ANISOU 2548 N ILE B 335 2838 2451 2817 -335 -215 -150 N ATOM 2549 CA ILE B 335 28.560 -2.559 -20.308 1.00 21.58 C ANISOU 2549 CA ILE B 335 2970 2407 2820 -284 -231 -185 C ATOM 2550 C ILE B 335 28.296 -2.683 -18.810 1.00 21.27 C ANISOU 2550 C ILE B 335 2990 2289 2804 -310 -228 -164 C ATOM 2551 O ILE B 335 27.860 -3.730 -18.335 1.00 21.82 O ANISOU 2551 O ILE B 335 3158 2268 2864 -322 -233 -178 O ATOM 2552 CB ILE B 335 30.062 -2.798 -20.635 1.00 21.99 C ANISOU 2552 CB ILE B 335 3001 2520 2834 -172 -241 -194 C ATOM 2553 CG1 ILE B 335 30.291 -2.794 -22.153 1.00 22.14 C ANISOU 2553 CG1 ILE B 335 2972 2625 2814 -134 -236 -216 C ATOM 2554 CG2 ILE B 335 30.569 -4.105 -20.018 1.00 22.41 C ANISOU 2554 CG2 ILE B 335 3168 2490 2855 -94 -255 -222 C ATOM 2555 CD1 ILE B 335 29.335 -3.685 -22.942 1.00 22.04 C ANISOU 2555 CD1 ILE B 335 3044 2556 2774 -163 -245 -272 C ATOM 2556 N VAL B 336 28.544 -1.601 -18.080 1.00 20.71 N ANISOU 2556 N VAL B 336 2866 2247 2754 -322 -221 -128 N ATOM 2557 CA VAL B 336 28.287 -1.557 -16.643 1.00 20.49 C ANISOU 2557 CA VAL B 336 2891 2160 2733 -341 -216 -108 C ATOM 2558 C VAL B 336 26.809 -1.823 -16.378 1.00 20.28 C ANISOU 2558 C VAL B 336 2899 2084 2721 -411 -188 -97 C ATOM 2559 O VAL B 336 26.469 -2.635 -15.517 1.00 20.77 O ANISOU 2559 O VAL B 336 3041 2078 2773 -423 -183 -89 O ATOM 2560 CB VAL B 336 28.697 -0.197 -16.019 1.00 20.31 C ANISOU 2560 CB VAL B 336 2819 2173 2724 -353 -217 -83 C ATOM 2561 CG1 VAL B 336 28.415 -0.183 -14.518 1.00 20.24 C ANISOU 2561 CG1 VAL B 336 2880 2108 2705 -361 -212 -71 C ATOM 2562 CG2 VAL B 336 30.172 0.117 -16.300 1.00 20.33 C ANISOU 2562 CG2 VAL B 336 2763 2247 2713 -309 -252 -79 C ATOM 2563 N PHE B 337 25.943 -1.143 -17.126 1.00 19.68 N ANISOU 2563 N PHE B 337 2755 2056 2666 -457 -168 -85 N ATOM 2564 CA PHE B 337 24.502 -1.362 -17.042 1.00 19.65 C ANISOU 2564 CA PHE B 337 2750 2044 2672 -526 -143 -62 C ATOM 2565 C PHE B 337 24.139 -2.812 -17.386 1.00 20.24 C ANISOU 2565 C PHE B 337 2895 2064 2732 -569 -165 -86 C ATOM 2566 O PHE B 337 23.291 -3.415 -16.723 1.00 20.76 O ANISOU 2566 O PHE B 337 3003 2087 2798 -630 -152 -60 O ATOM 2567 CB PHE B 337 23.752 -0.380 -17.949 1.00 19.32 C ANISOU 2567 CB PHE B 337 2611 2084 2648 -549 -126 -40 C ATOM 2568 CG PHE B 337 22.262 -0.587 -17.975 1.00 19.37 C ANISOU 2568 CG PHE B 337 2584 2118 2659 -618 -103 -6 C ATOM 2569 CD1 PHE B 337 21.490 -0.346 -16.844 1.00 19.03 C ANISOU 2569 CD1 PHE B 337 2544 2069 2618 -629 -61 38 C ATOM 2570 CD2 PHE B 337 21.629 -1.009 -19.139 1.00 19.87 C ANISOU 2570 CD2 PHE B 337 2606 2230 2715 -672 -126 -13 C ATOM 2571 CE1 PHE B 337 20.113 -0.539 -16.868 1.00 19.68 C ANISOU 2571 CE1 PHE B 337 2571 2207 2700 -693 -36 85 C ATOM 2572 CE2 PHE B 337 20.249 -1.201 -19.171 1.00 19.89 C ANISOU 2572 CE2 PHE B 337 2557 2283 2718 -750 -113 28 C ATOM 2573 CZ PHE B 337 19.493 -0.967 -18.035 1.00 20.09 C ANISOU 2573 CZ PHE B 337 2568 2315 2751 -761 -66 83 C ATOM 2574 N LYS B 338 24.793 -3.361 -18.412 1.00 20.28 N ANISOU 2574 N LYS B 338 2920 2068 2717 -537 -197 -133 N ATOM 2575 CA LYS B 338 24.617 -4.761 -18.804 1.00 20.83 C ANISOU 2575 CA LYS B 338 3092 2059 2762 -566 -227 -171 C ATOM 2576 C LYS B 338 25.036 -5.715 -17.678 1.00 21.48 C ANISOU 2576 C LYS B 338 3296 2030 2834 -539 -231 -167 C ATOM 2577 O LYS B 338 24.411 -6.767 -17.474 1.00 22.21 O ANISOU 2577 O LYS B 338 3486 2031 2921 -607 -243 -167 O ATOM 2578 CB LYS B 338 25.405 -5.061 -20.086 1.00 20.82 C ANISOU 2578 CB LYS B 338 3101 2083 2725 -501 -254 -230 C ATOM 2579 CG LYS B 338 25.319 -6.508 -20.570 1.00 21.11 C ANISOU 2579 CG LYS B 338 3278 2019 2725 -513 -290 -287 C ATOM 2580 CD LYS B 338 23.919 -6.857 -21.039 1.00 20.55 C ANISOU 2580 CD LYS B 338 3212 1938 2657 -658 -311 -288 C ATOM 2581 CE LYS B 338 23.724 -8.349 -21.208 1.00 20.61 C ANISOU 2581 CE LYS B 338 3393 1805 2633 -705 -354 -339 C ATOM 2582 NZ LYS B 338 22.334 -8.653 -21.612 1.00 20.25 N ANISOU 2582 NZ LYS B 338 3339 1764 2591 -876 -386 -331 N ATOM 2583 N GLY B 339 26.090 -5.337 -16.955 1.00 21.09 N ANISOU 2583 N GLY B 339 3242 1992 2780 -448 -225 -157 N ATOM 2584 CA GLY B 339 26.560 -6.096 -15.800 1.00 21.73 C ANISOU 2584 CA GLY B 339 3424 1987 2844 -405 -229 -140 C ATOM 2585 C GLY B 339 25.519 -6.173 -14.699 1.00 22.06 C ANISOU 2585 C GLY B 339 3493 1989 2898 -490 -202 -87 C ATOM 2586 O GLY B 339 25.328 -7.231 -14.086 1.00 22.85 O ANISOU 2586 O GLY B 339 3707 1990 2985 -509 -206 -69 O ATOM 2587 N VAL B 340 24.841 -5.050 -14.458 1.00 21.45 N ANISOU 2587 N VAL B 340 3316 1990 2842 -533 -170 -56 N ATOM 2588 CA VAL B 340 23.761 -4.987 -13.480 1.00 21.86 C ANISOU 2588 CA VAL B 340 3370 2039 2896 -600 -130 1 C ATOM 2589 C VAL B 340 22.547 -5.781 -13.981 1.00 22.80 C ANISOU 2589 C VAL B 340 3500 2136 3027 -719 -130 20 C ATOM 2590 O VAL B 340 21.927 -6.525 -13.220 1.00 23.67 O ANISOU 2590 O VAL B 340 3671 2193 3129 -784 -115 67 O ATOM 2591 CB VAL B 340 23.359 -3.523 -13.153 1.00 21.39 C ANISOU 2591 CB VAL B 340 3211 2071 2847 -589 -91 24 C ATOM 2592 CG1 VAL B 340 22.324 -3.485 -12.028 1.00 21.59 C ANISOU 2592 CG1 VAL B 340 3241 2105 2856 -628 -40 86 C ATOM 2593 CG2 VAL B 340 24.583 -2.693 -12.776 1.00 20.40 C ANISOU 2593 CG2 VAL B 340 3080 1962 2710 -501 -108 0 C ATOM 2594 N ALA B 341 22.231 -5.635 -15.267 1.00 22.81 N ANISOU 2594 N ALA B 341 3443 2183 3042 -757 -151 -12 N ATOM 2595 CA ALA B 341 21.125 -6.364 -15.890 1.00 23.68 C ANISOU 2595 CA ALA B 341 3556 2286 3156 -886 -169 -2 C ATOM 2596 C ALA B 341 21.235 -7.894 -15.720 1.00 24.91 C ANISOU 2596 C ALA B 341 3874 2296 3297 -938 -205 -16 C ATOM 2597 O ALA B 341 20.237 -8.569 -15.427 1.00 25.73 O ANISOU 2597 O ALA B 341 4005 2368 3405 -1069 -206 32 O ATOM 2598 CB ALA B 341 21.017 -5.992 -17.357 1.00 23.40 C ANISOU 2598 CB ALA B 341 3447 2322 3121 -897 -199 -47 C ATOM 2599 N ILE B 342 22.447 -8.423 -15.901 1.00 24.94 N ANISOU 2599 N ILE B 342 3983 2214 3280 -833 -233 -73 N ATOM 2600 CA ILE B 342 22.711 -9.856 -15.748 1.00 26.06 C ANISOU 2600 CA ILE B 342 4307 2194 3402 -845 -266 -91 C ATOM 2601 C ILE B 342 22.514 -10.282 -14.295 1.00 26.52 C ANISOU 2601 C ILE B 342 4431 2186 3459 -867 -237 -14 C ATOM 2602 O ILE B 342 21.920 -11.331 -14.017 1.00 27.61 O ANISOU 2602 O ILE B 342 4682 2213 3594 -973 -250 18 O ATOM 2603 CB ILE B 342 24.126 -10.231 -16.266 1.00 26.12 C ANISOU 2603 CB ILE B 342 4399 2148 3377 -687 -292 -164 C ATOM 2604 CG1 ILE B 342 24.148 -10.188 -17.795 1.00 26.43 C ANISOU 2604 CG1 ILE B 342 4416 2226 3399 -688 -324 -240 C ATOM 2605 CG2 ILE B 342 24.559 -11.612 -15.785 1.00 26.71 C ANISOU 2605 CG2 ILE B 342 4677 2045 3425 -650 -313 -167 C ATOM 2606 CD1 ILE B 342 25.517 -9.911 -18.379 1.00 26.77 C ANISOU 2606 CD1 ILE B 342 4442 2316 3412 -513 -325 -292 C ATOM 2607 N ALA B 343 22.991 -9.444 -13.378 1.00 25.64 N ANISOU 2607 N ALA B 343 4253 2145 3345 -777 -199 18 N ATOM 2608 CA ALA B 343 22.883 -9.712 -11.948 1.00 25.84 C ANISOU 2608 CA ALA B 343 4333 2132 3355 -777 -168 91 C ATOM 2609 C ALA B 343 21.436 -9.673 -11.466 1.00 26.26 C ANISOU 2609 C ALA B 343 4330 2228 3419 -925 -128 171 C ATOM 2610 O ALA B 343 21.071 -10.398 -10.547 1.00 27.09 O ANISOU 2610 O ALA B 343 4517 2267 3508 -978 -110 241 O ATOM 2611 CB ALA B 343 23.728 -8.728 -11.170 1.00 24.86 C ANISOU 2611 CB ALA B 343 4148 2086 3213 -652 -147 94 C ATOM 2612 N ALA B 344 20.622 -8.822 -12.087 1.00 25.84 N ANISOU 2612 N ALA B 344 4131 2298 3388 -983 -111 172 N ATOM 2613 CA ALA B 344 19.197 -8.740 -11.778 1.00 26.50 C ANISOU 2613 CA ALA B 344 4130 2460 3479 -1116 -72 255 C ATOM 2614 C ALA B 344 18.405 -9.841 -12.480 1.00 27.81 C ANISOU 2614 C ALA B 344 4347 2563 3658 -1287 -117 266 C ATOM 2615 O ALA B 344 17.287 -10.151 -12.079 1.00 28.72 O ANISOU 2615 O ALA B 344 4419 2719 3775 -1425 -93 353 O ATOM 2616 CB ALA B 344 18.653 -7.382 -12.157 1.00 25.76 C ANISOU 2616 CB ALA B 344 3861 2529 3396 -1091 -37 259 C ATOM 2617 N GLY B 345 18.996 -10.423 -13.523 1.00 28.07 N ANISOU 2617 N GLY B 345 4472 2502 3694 -1279 -182 179 N ATOM 2618 CA GLY B 345 18.355 -11.478 -14.309 1.00 29.55 C ANISOU 2618 CA GLY B 345 4738 2606 3884 -1442 -242 165 C ATOM 2619 C GLY B 345 17.381 -10.955 -15.351 1.00 29.82 C ANISOU 2619 C GLY B 345 4619 2781 3929 -1551 -263 159 C ATOM 2620 O GLY B 345 16.503 -11.685 -15.807 1.00 31.16 O ANISOU 2620 O GLY B 345 4810 2929 4099 -1732 -309 177 O ATOM 2621 N VAL B 346 17.545 -9.690 -15.735 1.00 28.78 N ANISOU 2621 N VAL B 346 4338 2793 3803 -1444 -234 139 N ATOM 2622 CA VAL B 346 16.628 -9.022 -16.661 1.00 28.90 C ANISOU 2622 CA VAL B 346 4190 2968 3824 -1517 -245 148 C ATOM 2623 C VAL B 346 17.219 -8.967 -18.068 1.00 28.84 C ANISOU 2623 C VAL B 346 4205 2951 3801 -1470 -305 43 C ATOM 2624 O VAL B 346 18.341 -8.484 -18.268 1.00 27.85 O ANISOU 2624 O VAL B 346 4103 2808 3670 -1311 -295 -15 O ATOM 2625 CB VAL B 346 16.285 -7.578 -16.184 1.00 27.96 C ANISOU 2625 CB VAL B 346 3892 3018 3716 -1424 -169 208 C ATOM 2626 CG1 VAL B 346 15.244 -6.929 -17.092 1.00 27.93 C ANISOU 2626 CG1 VAL B 346 3714 3186 3713 -1489 -177 237 C ATOM 2627 CG2 VAL B 346 15.793 -7.589 -14.755 1.00 27.99 C ANISOU 2627 CG2 VAL B 346 3880 3038 3716 -1439 -101 305 C ATOM 2628 N ALA B 347 16.460 -9.469 -19.037 1.00 30.13 N ANISOU 2628 N ALA B 347 4360 3138 3950 -1615 -368 24 N ATOM 2629 CA ALA B 347 16.846 -9.384 -20.438 1.00 30.34 C ANISOU 2629 CA ALA B 347 4397 3184 3946 -1581 -424 -70 C ATOM 2630 C ALA B 347 16.658 -7.951 -20.927 1.00 29.68 C ANISOU 2630 C ALA B 347 4117 3292 3869 -1497 -388 -45 C ATOM 2631 O ALA B 347 15.688 -7.279 -20.556 1.00 29.76 O ANISOU 2631 O ALA B 347 3971 3439 3898 -1542 -350 45 O ATOM 2632 CB ALA B 347 16.031 -10.349 -21.273 1.00 31.82 C ANISOU 2632 CB ALA B 347 4644 3341 4105 -1774 -512 -99 C ATOM 2633 N ILE B 348 17.603 -7.483 -21.738 1.00 29.32 N ANISOU 2633 N ILE B 348 4081 3257 3804 -1365 -396 -116 N ATOM 2634 CA ILE B 348 17.564 -6.127 -22.291 1.00 28.71 C ANISOU 2634 CA ILE B 348 3841 3337 3729 -1279 -365 -92 C ATOM 2635 C ILE B 348 17.976 -6.122 -23.775 1.00 29.33 C ANISOU 2635 C ILE B 348 3932 3454 3760 -1247 -417 -170 C ATOM 2636 O ILE B 348 19.003 -5.541 -24.138 1.00 28.43 O ANISOU 2636 O ILE B 348 3815 3349 3636 -1108 -395 -202 O ATOM 2637 CB ILE B 348 18.423 -5.120 -21.454 1.00 27.38 C ANISOU 2637 CB ILE B 348 3643 3168 3592 -1122 -293 -67 C ATOM 2638 CG1 ILE B 348 19.877 -5.593 -21.317 1.00 26.76 C ANISOU 2638 CG1 ILE B 348 3701 2965 3503 -1015 -300 -137 C ATOM 2639 CG2 ILE B 348 17.789 -4.871 -20.078 1.00 27.25 C ANISOU 2639 CG2 ILE B 348 3585 3160 3607 -1146 -235 18 C ATOM 2640 CD1 ILE B 348 20.824 -4.554 -20.723 1.00 25.58 C ANISOU 2640 CD1 ILE B 348 3510 2834 3374 -879 -250 -119 C ATOM 2641 N PRO B 349 17.160 -6.761 -24.642 1.00 31.00 N ANISOU 2641 N PRO B 349 4150 3697 3933 -1383 -487 -195 N ATOM 2642 CA PRO B 349 17.534 -7.009 -26.046 1.00 31.76 C ANISOU 2642 CA PRO B 349 4295 3811 3961 -1363 -547 -284 C ATOM 2643 C PRO B 349 17.929 -5.766 -26.844 1.00 31.08 C ANISOU 2643 C PRO B 349 4081 3868 3859 -1236 -516 -270 C ATOM 2644 O PRO B 349 18.781 -5.860 -27.735 1.00 31.15 O ANISOU 2644 O PRO B 349 4151 3870 3815 -1148 -533 -343 O ATOM 2645 CB PRO B 349 16.273 -7.651 -26.645 1.00 33.31 C ANISOU 2645 CB PRO B 349 4475 4059 4124 -1563 -629 -284 C ATOM 2646 CG PRO B 349 15.173 -7.336 -25.685 1.00 33.46 C ANISOU 2646 CG PRO B 349 4360 4155 4198 -1664 -595 -166 C ATOM 2647 CD PRO B 349 15.817 -7.290 -24.341 1.00 32.22 C ANISOU 2647 CD PRO B 349 4261 3885 4095 -1574 -520 -137 C ATOM 2648 N SER B 350 17.323 -4.623 -26.526 1.00 30.65 N ANISOU 2648 N SER B 350 3859 3940 3844 -1219 -469 -174 N ATOM 2649 CA SER B 350 17.622 -3.368 -27.224 1.00 30.09 C ANISOU 2649 CA SER B 350 3675 3994 3764 -1106 -437 -143 C ATOM 2650 C SER B 350 18.975 -2.759 -26.831 1.00 29.08 C ANISOU 2650 C SER B 350 3581 3805 3662 -954 -379 -152 C ATOM 2651 O SER B 350 19.697 -2.254 -27.695 1.00 28.86 O ANISOU 2651 O SER B 350 3534 3828 3602 -868 -376 -170 O ATOM 2652 CB SER B 350 16.489 -2.362 -27.040 1.00 29.93 C ANISOU 2652 CB SER B 350 3482 4119 3772 -1126 -407 -35 C ATOM 2653 OG SER B 350 15.305 -2.855 -27.637 1.00 31.08 O ANISOU 2653 OG SER B 350 3566 4363 3879 -1265 -471 -21 O ATOM 2654 N ASN B 351 19.308 -2.799 -25.539 1.00 28.56 N ANISOU 2654 N ASN B 351 3561 3643 3649 -930 -337 -133 N ATOM 2655 CA ASN B 351 20.645 -2.414 -25.085 1.00 27.82 C ANISOU 2655 CA ASN B 351 3510 3487 3573 -810 -300 -148 C ATOM 2656 C ASN B 351 21.702 -3.344 -25.686 1.00 28.22 C ANISOU 2656 C ASN B 351 3676 3471 3574 -760 -332 -237 C ATOM 2657 O ASN B 351 22.729 -2.887 -26.188 1.00 27.82 O ANISOU 2657 O ASN B 351 3609 3457 3504 -659 -316 -249 O ATOM 2658 CB ASN B 351 20.746 -2.410 -23.552 1.00 27.49 C ANISOU 2658 CB ASN B 351 3505 3358 3582 -802 -260 -117 C ATOM 2659 CG ASN B 351 20.281 -1.095 -22.921 1.00 27.06 C ANISOU 2659 CG ASN B 351 3348 3365 3568 -772 -206 -37 C ATOM 2660 OD1 ASN B 351 21.093 -0.234 -22.582 1.00 26.21 O ANISOU 2660 OD1 ASN B 351 3234 3246 3479 -689 -176 -25 O ATOM 2661 ND2 ASN B 351 18.971 -0.948 -22.748 1.00 27.52 N ANISOU 2661 ND2 ASN B 351 3332 3490 3634 -838 -195 19 N ATOM 2662 N ASP B 352 21.430 -4.647 -25.646 1.00 29.21 N ANISOU 2662 N ASP B 352 3923 3501 3675 -830 -376 -293 N ATOM 2663 CA ASP B 352 22.310 -5.652 -26.246 1.00 30.13 C ANISOU 2663 CA ASP B 352 4178 3540 3732 -770 -407 -385 C ATOM 2664 C ASP B 352 22.566 -5.356 -27.727 1.00 30.52 C ANISOU 2664 C ASP B 352 4187 3698 3711 -721 -426 -423 C ATOM 2665 O ASP B 352 23.722 -5.280 -28.157 1.00 30.45 O ANISOU 2665 O ASP B 352 4197 3708 3665 -592 -406 -453 O ATOM 2666 CB ASP B 352 21.727 -7.064 -26.073 1.00 31.35 C ANISOU 2666 CB ASP B 352 4485 3560 3867 -879 -461 -437 C ATOM 2667 CG ASP B 352 21.610 -7.487 -24.605 1.00 31.47 C ANISOU 2667 CG ASP B 352 4558 3459 3939 -916 -438 -394 C ATOM 2668 OD1 ASP B 352 22.176 -6.805 -23.718 1.00 29.62 O ANISOU 2668 OD1 ASP B 352 4269 3237 3748 -834 -385 -345 O ATOM 2669 OD2 ASP B 352 20.943 -8.515 -24.342 1.00 32.58 O ANISOU 2669 OD2 ASP B 352 4808 3496 4077 -1036 -478 -408 O ATOM 2670 N LYS B 353 21.481 -5.174 -28.485 1.00 31.07 N ANISOU 2670 N LYS B 353 4191 3859 3757 -821 -464 -413 N ATOM 2671 CA LYS B 353 21.533 -4.796 -29.904 1.00 31.40 C ANISOU 2671 CA LYS B 353 4180 4028 3724 -786 -485 -435 C ATOM 2672 C LYS B 353 22.511 -3.645 -30.148 1.00 29.99 C ANISOU 2672 C LYS B 353 3901 3941 3552 -651 -424 -386 C ATOM 2673 O LYS B 353 23.295 -3.679 -31.100 1.00 30.38 O ANISOU 2673 O LYS B 353 3967 4046 3529 -560 -421 -425 O ATOM 2674 CB LYS B 353 20.127 -4.416 -30.404 1.00 32.15 C ANISOU 2674 CB LYS B 353 4166 4240 3811 -912 -524 -389 C ATOM 2675 CG LYS B 353 20.087 -3.679 -31.750 1.00 33.55 C ANISOU 2675 CG LYS B 353 4248 4581 3919 -867 -535 -376 C ATOM 2676 CD LYS B 353 19.742 -4.601 -32.914 1.00 37.23 C ANISOU 2676 CD LYS B 353 4802 5068 4276 -929 -618 -471 C ATOM 2677 CE LYS B 353 18.284 -4.434 -33.361 1.00 39.35 C ANISOU 2677 CE LYS B 353 4965 5459 4526 -1074 -680 -428 C ATOM 2678 NZ LYS B 353 17.294 -4.870 -32.327 1.00 40.08 N ANISOU 2678 NZ LYS B 353 5046 5492 4689 -1222 -700 -390 N ATOM 2679 N LEU B 354 22.459 -2.643 -29.272 1.00 28.45 N ANISOU 2679 N LEU B 354 3610 3762 3439 -643 -374 -298 N ATOM 2680 CA LEU B 354 23.304 -1.456 -29.373 1.00 27.10 C ANISOU 2680 CA LEU B 354 3348 3662 3287 -548 -323 -238 C ATOM 2681 C LEU B 354 24.756 -1.725 -29.027 1.00 26.61 C ANISOU 2681 C LEU B 354 3341 3548 3221 -446 -297 -267 C ATOM 2682 O LEU B 354 25.650 -1.192 -29.680 1.00 26.70 O ANISOU 2682 O LEU B 354 3300 3644 3200 -366 -273 -247 O ATOM 2683 CB LEU B 354 22.769 -0.341 -28.481 1.00 26.35 C ANISOU 2683 CB LEU B 354 3164 3574 3274 -573 -285 -147 C ATOM 2684 CG LEU B 354 21.595 0.457 -29.035 1.00 26.40 C ANISOU 2684 CG LEU B 354 3063 3689 3280 -616 -289 -82 C ATOM 2685 CD1 LEU B 354 21.074 1.430 -27.984 1.00 25.53 C ANISOU 2685 CD1 LEU B 354 2897 3561 3244 -617 -244 -2 C ATOM 2686 CD2 LEU B 354 22.012 1.183 -30.303 1.00 26.04 C ANISOU 2686 CD2 LEU B 354 2953 3760 3183 -557 -284 -54 C ATOM 2687 N ILE B 355 24.980 -2.535 -27.993 1.00 26.19 N ANISOU 2687 N ILE B 355 3383 3370 3196 -450 -301 -301 N ATOM 2688 CA ILE B 355 26.328 -2.913 -27.566 1.00 25.58 C ANISOU 2688 CA ILE B 355 3359 3251 3111 -345 -283 -323 C ATOM 2689 C ILE B 355 27.045 -3.652 -28.696 1.00 26.36 C ANISOU 2689 C ILE B 355 3516 3385 3112 -251 -293 -393 C ATOM 2690 O ILE B 355 28.140 -3.257 -29.107 1.00 26.22 O ANISOU 2690 O ILE B 355 3441 3457 3064 -149 -263 -373 O ATOM 2691 CB ILE B 355 26.306 -3.758 -26.252 1.00 25.55 C ANISOU 2691 CB ILE B 355 3461 3102 3145 -364 -290 -343 C ATOM 2692 CG1 ILE B 355 25.922 -2.875 -25.059 1.00 24.60 C ANISOU 2692 CG1 ILE B 355 3276 2966 3105 -417 -265 -270 C ATOM 2693 CG2 ILE B 355 27.658 -4.402 -25.996 1.00 25.51 C ANISOU 2693 CG2 ILE B 355 3524 3060 3109 -238 -281 -376 C ATOM 2694 CD1 ILE B 355 25.488 -3.626 -23.814 1.00 24.49 C ANISOU 2694 CD1 ILE B 355 3353 2828 3123 -465 -271 -274 C ATOM 2695 N MET B 356 26.405 -4.697 -29.217 1.00 27.11 N ANISOU 2695 N MET B 356 3726 3419 3154 -291 -338 -472 N ATOM 2696 CA MET B 356 26.991 -5.519 -30.274 1.00 28.31 C ANISOU 2696 CA MET B 356 3973 3585 3199 -194 -351 -557 C ATOM 2697 C MET B 356 27.413 -4.706 -31.497 1.00 28.57 C ANISOU 2697 C MET B 356 3893 3794 3168 -127 -326 -531 C ATOM 2698 O MET B 356 28.481 -4.945 -32.066 1.00 29.39 O ANISOU 2698 O MET B 356 4012 3957 3198 12 -299 -557 O ATOM 2699 CB MET B 356 26.035 -6.637 -30.687 1.00 29.29 C ANISOU 2699 CB MET B 356 4247 3609 3274 -285 -417 -647 C ATOM 2700 CG MET B 356 25.738 -7.645 -29.589 1.00 29.63 C ANISOU 2700 CG MET B 356 4433 3464 3363 -344 -441 -674 C ATOM 2701 SD MET B 356 27.211 -8.285 -28.765 1.00 30.46 S ANISOU 2701 SD MET B 356 4637 3472 3466 -165 -400 -690 S ATOM 2702 CE MET B 356 28.027 -9.189 -30.086 1.00 30.83 C ANISOU 2702 CE MET B 356 4823 3523 3368 0 -408 -803 C ATOM 2703 N TRP B 357 26.578 -3.747 -31.888 1.00 28.16 N ANISOU 2703 N TRP B 357 3724 3834 3140 -217 -332 -470 N ATOM 2704 CA TRP B 357 26.863 -2.892 -33.033 1.00 28.31 C ANISOU 2704 CA TRP B 357 3634 4021 3102 -168 -309 -426 C ATOM 2705 C TRP B 357 27.980 -1.908 -32.715 1.00 27.56 C ANISOU 2705 C TRP B 357 3423 4000 3049 -94 -248 -336 C ATOM 2706 O TRP B 357 28.925 -1.771 -33.489 1.00 28.20 O ANISOU 2706 O TRP B 357 3464 4193 3059 9 -215 -325 O ATOM 2707 CB TRP B 357 25.603 -2.141 -33.477 1.00 28.30 C ANISOU 2707 CB TRP B 357 3545 4092 3116 -278 -335 -375 C ATOM 2708 CG TRP B 357 25.829 -1.212 -34.643 1.00 28.71 C ANISOU 2708 CG TRP B 357 3488 4313 3108 -230 -311 -315 C ATOM 2709 CD1 TRP B 357 25.847 -1.549 -35.964 1.00 29.72 C ANISOU 2709 CD1 TRP B 357 3640 4541 3111 -186 -331 -363 C ATOM 2710 CD2 TRP B 357 26.072 0.202 -34.585 1.00 28.10 C ANISOU 2710 CD2 TRP B 357 3274 4318 3087 -222 -264 -192 C ATOM 2711 NE1 TRP B 357 26.084 -0.435 -36.734 1.00 29.98 N ANISOU 2711 NE1 TRP B 357 3548 4725 3118 -148 -295 -268 N ATOM 2712 CE2 TRP B 357 26.226 0.653 -35.915 1.00 28.58 C ANISOU 2712 CE2 TRP B 357 3274 4530 3054 -174 -254 -160 C ATOM 2713 CE3 TRP B 357 26.171 1.132 -33.539 1.00 27.14 C ANISOU 2713 CE3 TRP B 357 3089 4145 3077 -252 -232 -108 C ATOM 2714 CZ2 TRP B 357 26.472 1.995 -36.232 1.00 28.36 C ANISOU 2714 CZ2 TRP B 357 3126 4600 3050 -162 -212 -36 C ATOM 2715 CZ3 TRP B 357 26.418 2.473 -33.855 1.00 26.83 C ANISOU 2715 CZ3 TRP B 357 2943 4190 3060 -241 -194 3 C ATOM 2716 CH2 TRP B 357 26.563 2.887 -35.191 1.00 27.47 C ANISOU 2716 CH2 TRP B 357 2966 4416 3056 -200 -184 43 C ATOM 2717 N ALA B 358 27.863 -1.233 -31.573 1.00 26.44 N ANISOU 2717 N ALA B 358 3230 3801 3014 -152 -234 -270 N ATOM 2718 CA ALA B 358 28.798 -0.176 -31.183 1.00 25.68 C ANISOU 2718 CA ALA B 358 3027 3762 2966 -122 -191 -180 C ATOM 2719 C ALA B 358 30.234 -0.666 -31.026 1.00 25.91 C ANISOU 2719 C ALA B 358 3066 3818 2961 -9 -167 -195 C ATOM 2720 O ALA B 358 31.161 -0.036 -31.533 1.00 26.20 O ANISOU 2720 O ALA B 358 3003 3981 2970 44 -133 -133 O ATOM 2721 CB ALA B 358 28.328 0.509 -29.911 1.00 24.60 C ANISOU 2721 CB ALA B 358 2871 3536 2939 -205 -190 -129 C ATOM 2722 N GLN B 359 30.410 -1.792 -30.336 1.00 25.95 N ANISOU 2722 N GLN B 359 3184 3712 2962 31 -184 -267 N ATOM 2723 CA GLN B 359 31.743 -2.334 -30.079 1.00 26.31 C ANISOU 2723 CA GLN B 359 3240 3784 2973 158 -162 -277 C ATOM 2724 C GLN B 359 32.478 -2.708 -31.370 1.00 27.30 C ANISOU 2724 C GLN B 359 3354 4040 2979 291 -134 -304 C ATOM 2725 O GLN B 359 33.702 -2.573 -31.453 1.00 27.65 O ANISOU 2725 O GLN B 359 3317 4198 2990 395 -97 -259 O ATOM 2726 CB GLN B 359 31.686 -3.518 -29.099 1.00 26.42 C ANISOU 2726 CB GLN B 359 3398 3638 3001 184 -186 -346 C ATOM 2727 CG GLN B 359 31.038 -4.799 -29.635 1.00 27.19 C ANISOU 2727 CG GLN B 359 3666 3633 3032 203 -217 -455 C ATOM 2728 CD GLN B 359 31.007 -5.928 -28.608 1.00 27.75 C ANISOU 2728 CD GLN B 359 3891 3530 3124 221 -239 -506 C ATOM 2729 OE1 GLN B 359 31.065 -5.693 -27.396 1.00 27.62 O ANISOU 2729 OE1 GLN B 359 3852 3456 3184 180 -239 -458 O ATOM 2730 NE2 GLN B 359 30.908 -7.160 -29.092 1.00 28.59 N ANISOU 2730 NE2 GLN B 359 4168 3542 3154 283 -261 -602 N ATOM 2731 N GLU B 360 31.727 -3.162 -32.373 1.00 27.74 N ANISOU 2731 N GLU B 360 3485 4094 2962 285 -153 -372 N ATOM 2732 CA GLU B 360 32.310 -3.508 -33.667 1.00 28.96 C ANISOU 2732 CA GLU B 360 3644 4374 2984 415 -127 -406 C ATOM 2733 C GLU B 360 32.866 -2.259 -34.338 1.00 28.69 C ANISOU 2733 C GLU B 360 3426 4537 2938 420 -81 -291 C ATOM 2734 O GLU B 360 33.969 -2.289 -34.882 1.00 29.78 O ANISOU 2734 O GLU B 360 3500 4817 2999 550 -32 -263 O ATOM 2735 CB GLU B 360 31.293 -4.207 -34.576 1.00 29.67 C ANISOU 2735 CB GLU B 360 3863 4417 2993 386 -172 -508 C ATOM 2736 CG GLU B 360 31.905 -4.869 -35.821 1.00 31.99 C ANISOU 2736 CG GLU B 360 4222 4807 3126 547 -149 -579 C ATOM 2737 CD GLU B 360 32.141 -3.905 -36.993 1.00 33.34 C ANISOU 2737 CD GLU B 360 4246 5195 3227 572 -110 -504 C ATOM 2738 OE1 GLU B 360 31.459 -2.856 -37.072 1.00 33.00 O ANISOU 2738 OE1 GLU B 360 4093 5197 3248 441 -121 -421 O ATOM 2739 OE2 GLU B 360 33.007 -4.206 -37.848 1.00 34.54 O ANISOU 2739 OE2 GLU B 360 4397 5473 3252 733 -64 -522 O ATOM 2740 N LYS B 361 32.111 -1.163 -34.279 1.00 27.50 N ANISOU 2740 N LYS B 361 3191 4394 2863 282 -93 -217 N ATOM 2741 CA LYS B 361 32.520 0.088 -34.912 1.00 27.26 C ANISOU 2741 CA LYS B 361 3005 4523 2828 265 -54 -97 C ATOM 2742 C LYS B 361 33.877 0.565 -34.409 1.00 27.06 C ANISOU 2742 C LYS B 361 2866 4582 2834 306 -13 -9 C ATOM 2743 O LYS B 361 34.709 1.011 -35.193 1.00 28.04 O ANISOU 2743 O LYS B 361 2881 4879 2894 364 33 65 O ATOM 2744 CB LYS B 361 31.471 1.189 -34.720 1.00 26.32 C ANISOU 2744 CB LYS B 361 2838 4363 2799 120 -74 -28 C ATOM 2745 CG LYS B 361 30.031 0.813 -35.075 1.00 26.70 C ANISOU 2745 CG LYS B 361 2968 4347 2831 57 -123 -95 C ATOM 2746 CD LYS B 361 29.889 -0.003 -36.363 1.00 28.00 C ANISOU 2746 CD LYS B 361 3196 4590 2852 131 -135 -177 C ATOM 2747 CE LYS B 361 29.963 0.848 -37.607 1.00 28.42 C ANISOU 2747 CE LYS B 361 3147 4819 2830 153 -108 -97 C ATOM 2748 NZ LYS B 361 29.613 0.032 -38.802 1.00 29.99 N ANISOU 2748 NZ LYS B 361 3427 5084 2882 211 -134 -191 N ATOM 2749 N ILE B 362 34.099 0.451 -33.106 1.00 26.13 N ANISOU 2749 N ILE B 362 2770 4355 2805 272 -31 -12 N ATOM 2750 CA ILE B 362 35.351 0.897 -32.492 1.00 26.03 C ANISOU 2750 CA ILE B 362 2645 4421 2824 289 -10 71 C ATOM 2751 C ILE B 362 36.393 -0.222 -32.375 1.00 27.02 C ANISOU 2751 C ILE B 362 2793 4596 2875 454 10 24 C ATOM 2752 O ILE B 362 37.468 -0.022 -31.804 1.00 27.38 O ANISOU 2752 O ILE B 362 2742 4724 2939 482 22 89 O ATOM 2753 CB ILE B 362 35.107 1.587 -31.117 1.00 24.87 C ANISOU 2753 CB ILE B 362 2494 4149 2806 157 -44 109 C ATOM 2754 CG1 ILE B 362 34.489 0.614 -30.099 1.00 24.27 C ANISOU 2754 CG1 ILE B 362 2561 3893 2766 160 -81 10 C ATOM 2755 CG2 ILE B 362 34.220 2.814 -31.304 1.00 24.30 C ANISOU 2755 CG2 ILE B 362 2392 4044 2795 24 -51 171 C ATOM 2756 CD1 ILE B 362 34.388 1.157 -28.665 1.00 23.25 C ANISOU 2756 CD1 ILE B 362 2436 3656 2742 60 -110 40 C ATOM 2757 N GLY B 363 36.070 -1.395 -32.919 1.00 27.52 N ANISOU 2757 N GLY B 363 2991 4613 2852 566 9 -89 N ATOM 2758 CA GLY B 363 36.991 -2.533 -32.915 1.00 28.77 C ANISOU 2758 CA GLY B 363 3203 4804 2925 756 33 -143 C ATOM 2759 C GLY B 363 37.316 -3.087 -31.535 1.00 28.50 C ANISOU 2759 C GLY B 363 3223 4650 2955 774 7 -160 C ATOM 2760 O GLY B 363 38.428 -3.568 -31.294 1.00 29.44 O ANISOU 2760 O GLY B 363 3304 4854 3028 920 33 -141 O ATOM 2761 N LYS B 364 36.344 -3.014 -30.630 1.00 27.24 N ANISOU 2761 N LYS B 364 3147 4308 2895 634 -42 -188 N ATOM 2762 CA LYS B 364 36.469 -3.598 -29.299 1.00 26.87 C ANISOU 2762 CA LYS B 364 3176 4128 2903 642 -71 -209 C ATOM 2763 C LYS B 364 35.471 -4.740 -29.144 1.00 26.82 C ANISOU 2763 C LYS B 364 3384 3917 2888 641 -104 -324 C ATOM 2764 O LYS B 364 34.550 -4.885 -29.950 1.00 26.76 O ANISOU 2764 O LYS B 364 3448 3869 2853 590 -116 -381 O ATOM 2765 CB LYS B 364 36.220 -2.540 -28.222 1.00 25.76 C ANISOU 2765 CB LYS B 364 2958 3949 2882 477 -99 -136 C ATOM 2766 CG LYS B 364 37.116 -1.315 -28.298 1.00 26.11 C ANISOU 2766 CG LYS B 364 2808 4166 2947 431 -82 -20 C ATOM 2767 CD LYS B 364 38.522 -1.598 -27.807 1.00 28.01 C ANISOU 2767 CD LYS B 364 2960 4526 3156 542 -73 28 C ATOM 2768 CE LYS B 364 39.425 -0.413 -28.077 1.00 28.86 C ANISOU 2768 CE LYS B 364 2864 4829 3272 479 -59 152 C ATOM 2769 NZ LYS B 364 40.787 -0.645 -27.537 1.00 30.91 N ANISOU 2769 NZ LYS B 364 3012 5231 3502 570 -59 211 N ATOM 2770 N GLU B 365 35.659 -5.549 -28.106 1.00 27.00 N ANISOU 2770 N GLU B 365 3509 3818 2933 689 -122 -351 N ATOM 2771 CA GLU B 365 34.756 -6.665 -27.821 1.00 27.21 C ANISOU 2771 CA GLU B 365 3747 3634 2959 669 -156 -445 C ATOM 2772 C GLU B 365 34.496 -6.797 -26.324 1.00 26.62 C ANISOU 2772 C GLU B 365 3719 3424 2970 595 -184 -421 C ATOM 2773 O GLU B 365 35.419 -7.031 -25.539 1.00 26.87 O ANISOU 2773 O GLU B 365 3731 3476 3001 692 -179 -385 O ATOM 2774 CB GLU B 365 35.318 -7.972 -28.381 1.00 28.67 C ANISOU 2774 CB GLU B 365 4082 3780 3033 867 -142 -527 C ATOM 2775 CG GLU B 365 34.335 -9.125 -28.367 1.00 29.03 C ANISOU 2775 CG GLU B 365 4369 3599 3063 828 -184 -632 C ATOM 2776 CD GLU B 365 34.975 -10.428 -28.782 1.00 30.66 C ANISOU 2776 CD GLU B 365 4757 3736 3159 1040 -172 -716 C ATOM 2777 OE1 GLU B 365 35.804 -10.959 -28.013 1.00 31.05 O ANISOU 2777 OE1 GLU B 365 4841 3754 3202 1179 -157 -692 O ATOM 2778 OE2 GLU B 365 34.646 -10.921 -29.881 1.00 31.54 O ANISOU 2778 OE2 GLU B 365 4982 3822 3180 1076 -178 -806 O ATOM 2779 N TYR B 366 33.231 -6.646 -25.944 1.00 25.92 N ANISOU 2779 N TYR B 366 3684 3217 2948 428 -214 -434 N ATOM 2780 CA TYR B 366 32.839 -6.682 -24.545 1.00 25.59 C ANISOU 2780 CA TYR B 366 3681 3060 2982 345 -234 -405 C ATOM 2781 C TYR B 366 31.770 -7.736 -24.286 1.00 26.24 C ANISOU 2781 C TYR B 366 3950 2950 3070 276 -264 -467 C ATOM 2782 O TYR B 366 31.885 -8.523 -23.344 1.00 26.80 O ANISOU 2782 O TYR B 366 4134 2900 3150 308 -274 -469 O ATOM 2783 CB TYR B 366 32.341 -5.308 -24.098 1.00 24.25 C ANISOU 2783 CB TYR B 366 3375 2947 2893 200 -233 -336 C ATOM 2784 CG TYR B 366 33.282 -4.156 -24.404 1.00 23.96 C ANISOU 2784 CG TYR B 366 3160 3085 2857 225 -212 -268 C ATOM 2785 CD1 TYR B 366 34.510 -4.038 -23.756 1.00 23.60 C ANISOU 2785 CD1 TYR B 366 3048 3114 2807 305 -210 -221 C ATOM 2786 CD2 TYR B 366 32.932 -3.175 -25.331 1.00 23.77 C ANISOU 2786 CD2 TYR B 366 3035 3156 2839 158 -199 -241 C ATOM 2787 CE1 TYR B 366 35.364 -2.979 -24.027 1.00 23.64 C ANISOU 2787 CE1 TYR B 366 2886 3282 2815 298 -198 -149 C ATOM 2788 CE2 TYR B 366 33.784 -2.110 -25.609 1.00 23.18 C ANISOU 2788 CE2 TYR B 366 2808 3230 2769 161 -181 -166 C ATOM 2789 CZ TYR B 366 34.995 -2.021 -24.953 1.00 23.49 C ANISOU 2789 CZ TYR B 366 2781 3339 2806 221 -183 -121 C ATOM 2790 OH TYR B 366 35.843 -0.973 -25.227 1.00 23.97 O ANISOU 2790 OH TYR B 366 2685 3551 2871 199 -172 -39 O ATOM 2791 N LEU B 367 30.737 -7.742 -25.126 1.00 26.59 N ANISOU 2791 N LEU B 367 4023 2974 3105 175 -281 -508 N ATOM 2792 CA LEU B 367 29.634 -8.695 -25.028 1.00 27.31 C ANISOU 2792 CA LEU B 367 4277 2900 3199 72 -318 -562 C ATOM 2793 C LEU B 367 29.720 -9.736 -26.144 1.00 28.92 C ANISOU 2793 C LEU B 367 4634 3047 3307 147 -340 -661 C ATOM 2794 O LEU B 367 29.897 -9.386 -27.311 1.00 29.25 O ANISOU 2794 O LEU B 367 4617 3206 3291 190 -332 -689 O ATOM 2795 CB LEU B 367 28.295 -7.952 -25.102 1.00 26.51 C ANISOU 2795 CB LEU B 367 4092 2829 3153 -115 -333 -531 C ATOM 2796 CG LEU B 367 26.997 -8.667 -24.706 1.00 27.06 C ANISOU 2796 CG LEU B 367 4270 2762 3249 -271 -371 -547 C ATOM 2797 CD1 LEU B 367 26.872 -8.753 -23.197 1.00 26.78 C ANISOU 2797 CD1 LEU B 367 4255 2642 3277 -309 -357 -487 C ATOM 2798 CD2 LEU B 367 25.786 -7.953 -25.293 1.00 26.51 C ANISOU 2798 CD2 LEU B 367 4092 2780 3199 -418 -386 -526 C ATOM 2799 N VAL B 368 29.612 -11.011 -25.778 1.00 30.31 N ANISOU 2799 N VAL B 368 5019 3037 3461 167 -366 -714 N ATOM 2800 CA VAL B 368 29.565 -12.111 -26.747 1.00 32.28 C ANISOU 2800 CA VAL B 368 5466 3184 3616 223 -396 -823 C ATOM 2801 C VAL B 368 28.438 -13.066 -26.342 1.00 33.38 C ANISOU 2801 C VAL B 368 5792 3112 3779 55 -454 -857 C ATOM 2802 O VAL B 368 28.369 -13.486 -25.182 1.00 33.44 O ANISOU 2802 O VAL B 368 5867 2998 3841 26 -453 -812 O ATOM 2803 CB VAL B 368 30.918 -12.893 -26.836 1.00 33.49 C ANISOU 2803 CB VAL B 368 5732 3306 3688 479 -366 -862 C ATOM 2804 CG1 VAL B 368 30.844 -14.002 -27.881 1.00 35.00 C ANISOU 2804 CG1 VAL B 368 6153 3378 3768 551 -396 -987 C ATOM 2805 CG2 VAL B 368 32.082 -11.961 -27.157 1.00 32.87 C ANISOU 2805 CG2 VAL B 368 5444 3458 3586 633 -308 -808 C ATOM 2806 N ASP B 369 27.560 -13.394 -27.294 1.00 34.45 N ANISOU 2806 N ASP B 369 6005 3214 3871 -65 -507 -929 N ATOM 2807 CA ASP B 369 26.381 -14.240 -27.044 1.00 35.66 C ANISOU 2807 CA ASP B 369 6316 3189 4045 -269 -573 -955 C ATOM 2808 C ASP B 369 25.639 -13.853 -25.757 1.00 34.78 C ANISOU 2808 C ASP B 369 6104 3064 4045 -427 -564 -845 C ATOM 2809 O ASP B 369 25.312 -14.710 -24.927 1.00 35.61 O ANISOU 2809 O ASP B 369 6359 2992 4178 -500 -584 -830 O ATOM 2810 CB ASP B 369 26.764 -15.728 -27.021 1.00 37.67 C ANISOU 2810 CB ASP B 369 6877 3200 4235 -185 -603 -1041 C ATOM 2811 CG ASP B 369 27.238 -16.234 -28.372 1.00 39.35 C ANISOU 2811 CG ASP B 369 7228 3403 4319 -51 -622 -1169 C ATOM 2812 OD1 ASP B 369 26.697 -15.781 -29.403 1.00 39.88 O ANISOU 2812 OD1 ASP B 369 7217 3590 4343 -137 -653 -1209 O ATOM 2813 OD2 ASP B 369 28.147 -17.095 -28.402 1.00 40.34 O ANISOU 2813 OD2 ASP B 369 7547 3406 4376 151 -605 -1227 O ATOM 2814 N GLY B 370 25.399 -12.554 -25.594 1.00 33.25 N ANISOU 2814 N GLY B 370 5666 3058 3908 -469 -529 -766 N ATOM 2815 CA GLY B 370 24.694 -12.025 -24.427 1.00 32.49 C ANISOU 2815 CA GLY B 370 5458 2981 3905 -596 -509 -663 C ATOM 2816 C GLY B 370 25.450 -12.098 -23.109 1.00 32.13 C ANISOU 2816 C GLY B 370 5433 2876 3900 -496 -466 -605 C ATOM 2817 O GLY B 370 24.931 -11.668 -22.072 1.00 31.46 O ANISOU 2817 O GLY B 370 5267 2807 3879 -582 -444 -522 O ATOM 2818 N ALA B 371 26.672 -12.634 -23.147 1.00 32.55 N ANISOU 2818 N ALA B 371 5589 2873 3904 -303 -452 -645 N ATOM 2819 CA ALA B 371 27.473 -12.851 -21.941 1.00 32.30 C ANISOU 2819 CA ALA B 371 5592 2785 3894 -192 -421 -592 C ATOM 2820 C ALA B 371 28.732 -11.986 -21.925 1.00 31.40 C ANISOU 2820 C ALA B 371 5326 2834 3770 -16 -378 -566 C ATOM 2821 O ALA B 371 29.360 -11.767 -22.964 1.00 31.58 O ANISOU 2821 O ALA B 371 5305 2954 3740 90 -369 -611 O ATOM 2822 CB ALA B 371 27.829 -14.326 -21.796 1.00 33.83 C ANISOU 2822 CB ALA B 371 6048 2765 4040 -113 -445 -641 C ATOM 2823 N LEU B 372 29.096 -11.502 -20.738 1.00 30.57 N ANISOU 2823 N LEU B 372 5141 2765 3711 5 -353 -488 N ATOM 2824 CA LEU B 372 30.224 -10.582 -20.579 1.00 29.69 C ANISOU 2824 CA LEU B 372 4869 2815 3598 129 -324 -450 C ATOM 2825 C LEU B 372 31.568 -11.303 -20.607 1.00 30.63 C ANISOU 2825 C LEU B 372 5060 2925 3652 347 -316 -467 C ATOM 2826 O LEU B 372 32.239 -11.423 -19.581 1.00 30.69 O ANISOU 2826 O LEU B 372 5069 2929 3665 427 -311 -416 O ATOM 2827 CB LEU B 372 30.078 -9.770 -19.286 1.00 28.64 C ANISOU 2827 CB LEU B 372 4633 2725 3526 61 -311 -368 C ATOM 2828 CG LEU B 372 28.936 -8.753 -19.183 1.00 27.37 C ANISOU 2828 CG LEU B 372 4358 2620 3422 -109 -302 -335 C ATOM 2829 CD1 LEU B 372 28.912 -8.170 -17.789 1.00 26.96 C ANISOU 2829 CD1 LEU B 372 4255 2581 3408 -140 -288 -267 C ATOM 2830 CD2 LEU B 372 29.044 -7.646 -20.225 1.00 26.15 C ANISOU 2830 CD2 LEU B 372 4048 2618 3270 -114 -292 -342 C ATOM 2831 N THR B 373 31.947 -11.775 -21.794 1.00 31.49 N ANISOU 2831 N THR B 373 5228 3044 3693 451 -315 -537 N ATOM 2832 CA THR B 373 33.158 -12.584 -21.985 1.00 32.67 C ANISOU 2832 CA THR B 373 5465 3184 3764 686 -300 -562 C ATOM 2833 C THR B 373 33.993 -12.076 -23.165 1.00 32.82 C ANISOU 2833 C THR B 373 5357 3393 3721 814 -271 -584 C ATOM 2834 O THR B 373 34.784 -12.821 -23.743 1.00 33.99 O ANISOU 2834 O THR B 373 5594 3539 3781 1012 -253 -628 O ATOM 2835 CB THR B 373 32.818 -14.081 -22.237 1.00 34.25 C ANISOU 2835 CB THR B 373 5949 3151 3912 730 -324 -641 C ATOM 2836 OG1 THR B 373 32.259 -14.238 -23.549 1.00 34.84 O ANISOU 2836 OG1 THR B 373 6085 3211 3942 680 -340 -731 O ATOM 2837 CG2 THR B 373 31.844 -14.621 -21.192 1.00 34.03 C ANISOU 2837 CG2 THR B 373 6053 2931 3945 569 -354 -612 C ATOM 2838 N GLY B 374 33.810 -10.806 -23.516 1.00 31.73 N ANISOU 2838 N GLY B 374 5015 3418 3621 708 -260 -546 N ATOM 2839 CA GLY B 374 34.485 -10.213 -24.670 1.00 32.06 C ANISOU 2839 CA GLY B 374 4923 3652 3608 797 -230 -550 C ATOM 2840 C GLY B 374 35.984 -10.091 -24.484 1.00 32.66 C ANISOU 2840 C GLY B 374 4885 3884 3641 990 -197 -494 C ATOM 2841 O GLY B 374 36.486 -10.191 -23.367 1.00 32.84 O ANISOU 2841 O GLY B 374 4892 3893 3692 1029 -204 -440 O ATOM 2842 N LYS B 375 36.695 -9.866 -25.584 1.00 33.30 N ANISOU 2842 N LYS B 375 4875 4130 3646 1110 -160 -500 N ATOM 2843 CA LYS B 375 38.145 -9.724 -25.566 1.00 34.01 C ANISOU 2843 CA LYS B 375 4826 4413 3685 1296 -123 -435 C ATOM 2844 C LYS B 375 38.603 -8.649 -24.578 1.00 32.94 C ANISOU 2844 C LYS B 375 4488 4399 3628 1198 -137 -326 C ATOM 2845 O LYS B 375 39.538 -8.874 -23.812 1.00 33.48 O ANISOU 2845 O LYS B 375 4509 4528 3683 1311 -138 -272 O ATOM 2846 CB LYS B 375 38.659 -9.419 -26.975 1.00 34.84 C ANISOU 2846 CB LYS B 375 4832 4705 3702 1396 -77 -443 C ATOM 2847 CG LYS B 375 40.174 -9.333 -27.096 1.00 36.72 C ANISOU 2847 CG LYS B 375 4909 5175 3870 1601 -30 -368 C ATOM 2848 CD LYS B 375 40.591 -8.708 -28.427 1.00 38.59 C ANISOU 2848 CD LYS B 375 4997 5632 4034 1646 21 -346 C ATOM 2849 CE LYS B 375 42.058 -8.289 -28.406 1.00 40.03 C ANISOU 2849 CE LYS B 375 4947 6092 4171 1784 65 -231 C ATOM 2850 NZ LYS B 375 42.957 -9.442 -28.103 1.00 41.85 N ANISOU 2850 NZ LYS B 375 5257 6328 4316 2058 90 -244 N ATOM 2851 N ASP B 376 37.928 -7.499 -24.586 1.00 31.60 N ANISOU 2851 N ASP B 376 4214 4259 3535 992 -151 -294 N ATOM 2852 CA ASP B 376 38.343 -6.340 -23.786 1.00 30.82 C ANISOU 2852 CA ASP B 376 3936 4271 3503 883 -168 -199 C ATOM 2853 C ASP B 376 37.420 -6.045 -22.597 1.00 29.62 C ANISOU 2853 C ASP B 376 3848 3965 3443 714 -208 -197 C ATOM 2854 O ASP B 376 37.298 -4.888 -22.172 1.00 28.66 O ANISOU 2854 O ASP B 376 3613 3894 3383 574 -224 -144 O ATOM 2855 CB ASP B 376 38.453 -5.084 -24.664 1.00 30.41 C ANISOU 2855 CB ASP B 376 3706 4385 3462 791 -149 -148 C ATOM 2856 CG ASP B 376 39.142 -5.348 -25.983 1.00 31.77 C ANISOU 2856 CG ASP B 376 3823 4711 3536 944 -100 -153 C ATOM 2857 OD1 ASP B 376 40.368 -5.130 -26.068 1.00 32.41 O ANISOU 2857 OD1 ASP B 376 3752 4989 3575 1044 -78 -79 O ATOM 2858 OD2 ASP B 376 38.455 -5.779 -26.934 1.00 32.28 O ANISOU 2858 OD2 ASP B 376 3994 4713 3557 963 -85 -228 O ATOM 2859 N VAL B 377 36.781 -7.083 -22.054 1.00 29.65 N ANISOU 2859 N VAL B 377 4038 3778 3448 731 -223 -251 N ATOM 2860 CA VAL B 377 35.839 -6.901 -20.939 1.00 28.38 C ANISOU 2860 CA VAL B 377 3942 3480 3361 581 -251 -244 C ATOM 2861 C VAL B 377 36.534 -6.458 -19.645 1.00 28.04 C ANISOU 2861 C VAL B 377 3822 3490 3341 577 -275 -176 C ATOM 2862 O VAL B 377 35.912 -5.839 -18.784 1.00 27.34 O ANISOU 2862 O VAL B 377 3731 3349 3310 442 -293 -156 O ATOM 2863 CB VAL B 377 34.952 -8.154 -20.701 1.00 28.84 C ANISOU 2863 CB VAL B 377 4220 3325 3413 581 -260 -306 C ATOM 2864 CG1 VAL B 377 35.767 -9.317 -20.142 1.00 29.79 C ANISOU 2864 CG1 VAL B 377 4454 3385 3481 757 -264 -307 C ATOM 2865 CG2 VAL B 377 33.776 -7.817 -19.786 1.00 27.61 C ANISOU 2865 CG2 VAL B 377 4101 3058 3330 403 -276 -291 C ATOM 2866 N ALA B 378 37.824 -6.758 -19.524 1.00 28.70 N ANISOU 2866 N ALA B 378 3841 3691 3371 730 -275 -140 N ATOM 2867 CA ALA B 378 38.600 -6.348 -18.356 1.00 28.49 C ANISOU 2867 CA ALA B 378 3727 3745 3353 728 -310 -72 C ATOM 2868 C ALA B 378 38.926 -4.849 -18.362 1.00 27.53 C ANISOU 2868 C ALA B 378 3419 3772 3270 592 -327 -18 C ATOM 2869 O ALA B 378 39.365 -4.305 -17.348 1.00 27.37 O ANISOU 2869 O ALA B 378 3336 3800 3263 535 -369 29 O ATOM 2870 CB ALA B 378 39.874 -7.184 -18.234 1.00 30.05 C ANISOU 2870 CB ALA B 378 3903 4041 3475 943 -309 -41 C ATOM 2871 N THR B 379 38.707 -4.187 -19.497 1.00 26.73 N ANISOU 2871 N THR B 379 3242 3733 3180 534 -300 -23 N ATOM 2872 CA THR B 379 38.900 -2.738 -19.578 1.00 26.15 C ANISOU 2872 CA THR B 379 3019 3767 3149 390 -316 32 C ATOM 2873 C THR B 379 37.613 -1.978 -19.252 1.00 24.57 C ANISOU 2873 C THR B 379 2887 3430 3020 221 -322 7 C ATOM 2874 O THR B 379 37.584 -0.751 -19.320 1.00 24.29 O ANISOU 2874 O THR B 379 2767 3439 3022 98 -333 44 O ATOM 2875 CB THR B 379 39.451 -2.267 -20.964 1.00 26.77 C ANISOU 2875 CB THR B 379 2961 4012 3199 417 -281 65 C ATOM 2876 OG1 THR B 379 38.417 -2.333 -21.961 1.00 26.85 O ANISOU 2876 OG1 THR B 379 3045 3941 3217 390 -246 11 O ATOM 2877 CG2 THR B 379 40.659 -3.101 -21.402 1.00 28.15 C ANISOU 2877 CG2 THR B 379 3069 4339 3289 617 -259 88 C ATOM 2878 N THR B 380 36.554 -2.709 -18.903 1.00 23.71 N ANISOU 2878 N THR B 380 2932 3154 2924 218 -313 -49 N ATOM 2879 CA THR B 380 35.280 -2.097 -18.515 1.00 22.23 C ANISOU 2879 CA THR B 380 2803 2851 2794 79 -311 -65 C ATOM 2880 C THR B 380 35.135 -2.003 -16.990 1.00 21.91 C ANISOU 2880 C THR B 380 2820 2735 2768 35 -340 -55 C ATOM 2881 O THR B 380 36.035 -2.401 -16.238 1.00 22.58 O ANISOU 2881 O THR B 380 2898 2861 2820 104 -369 -33 O ATOM 2882 CB THR B 380 34.065 -2.870 -19.087 1.00 21.90 C ANISOU 2882 CB THR B 380 2875 2691 2756 74 -284 -121 C ATOM 2883 OG1 THR B 380 33.914 -4.118 -18.401 1.00 21.91 O ANISOU 2883 OG1 THR B 380 3010 2579 2735 137 -291 -149 O ATOM 2884 CG2 THR B 380 34.232 -3.127 -20.561 1.00 22.28 C ANISOU 2884 CG2 THR B 380 2890 2808 2768 134 -261 -144 C ATOM 2885 N ARG B 381 33.998 -1.475 -16.543 1.00 20.81 N ANISOU 2885 N ARG B 381 2735 2503 2671 -68 -330 -65 N ATOM 2886 CA ARG B 381 33.673 -1.438 -15.121 1.00 20.41 C ANISOU 2886 CA ARG B 381 2757 2376 2621 -102 -346 -61 C ATOM 2887 C ARG B 381 32.384 -2.184 -14.784 1.00 20.06 C ANISOU 2887 C ARG B 381 2832 2203 2587 -123 -316 -85 C ATOM 2888 O ARG B 381 31.682 -1.805 -13.847 1.00 19.63 O ANISOU 2888 O ARG B 381 2823 2093 2543 -181 -309 -77 O ATOM 2889 CB ARG B 381 33.532 -0.003 -14.638 1.00 20.03 C ANISOU 2889 CB ARG B 381 2669 2341 2600 -204 -360 -44 C ATOM 2890 CG ARG B 381 34.772 0.825 -14.654 1.00 19.39 C ANISOU 2890 CG ARG B 381 2484 2374 2510 -227 -405 -11 C ATOM 2891 CD ARG B 381 34.320 2.214 -14.921 1.00 17.86 C ANISOU 2891 CD ARG B 381 2264 2165 2356 -332 -400 -2 C ATOM 2892 NE ARG B 381 35.014 3.205 -14.122 1.00 17.41 N ANISOU 2892 NE ARG B 381 2190 2133 2292 -407 -455 16 N ATOM 2893 CZ ARG B 381 34.540 4.421 -13.890 1.00 16.60 C ANISOU 2893 CZ ARG B 381 2125 1969 2215 -498 -459 14 C ATOM 2894 NH1 ARG B 381 33.364 4.790 -14.382 1.00 15.21 N ANISOU 2894 NH1 ARG B 381 1989 1718 2073 -508 -405 3 N ATOM 2895 NH2 ARG B 381 35.244 5.262 -13.156 1.00 17.48 N ANISOU 2895 NH2 ARG B 381 2238 2092 2311 -575 -520 22 N ATOM 2896 N CYS B 382 32.058 -3.228 -15.537 1.00 20.23 N ANISOU 2896 N CYS B 382 2907 2179 2599 -80 -299 -111 N ATOM 2897 CA CYS B 382 30.941 -4.080 -15.145 1.00 20.39 C ANISOU 2897 CA CYS B 382 3044 2078 2626 -115 -281 -123 C ATOM 2898 C CYS B 382 31.329 -4.752 -13.830 1.00 20.77 C ANISOU 2898 C CYS B 382 3176 2072 2644 -66 -296 -100 C ATOM 2899 O CYS B 382 32.483 -5.158 -13.667 1.00 21.52 O ANISOU 2899 O CYS B 382 3266 2207 2702 36 -322 -92 O ATOM 2900 CB CYS B 382 30.608 -5.110 -16.226 1.00 20.83 C ANISOU 2900 CB CYS B 382 3161 2083 2669 -91 -274 -162 C ATOM 2901 SG CYS B 382 31.990 -6.139 -16.719 1.00 21.85 S ANISOU 2901 SG CYS B 382 3329 2232 2742 75 -292 -184 S ATOM 2902 N PRO B 383 30.380 -4.853 -12.877 1.00 20.49 N ANISOU 2902 N PRO B 383 3209 1961 2615 -131 -278 -81 N ATOM 2903 CA PRO B 383 30.724 -5.364 -11.548 1.00 20.79 C ANISOU 2903 CA PRO B 383 3324 1960 2617 -88 -292 -49 C ATOM 2904 C PRO B 383 31.350 -6.763 -11.594 1.00 21.55 C ANISOU 2904 C PRO B 383 3517 1991 2678 17 -307 -48 C ATOM 2905 O PRO B 383 32.213 -7.077 -10.770 1.00 21.94 O ANISOU 2905 O PRO B 383 3592 2058 2687 103 -333 -20 O ATOM 2906 CB PRO B 383 29.376 -5.378 -10.811 1.00 20.74 C ANISOU 2906 CB PRO B 383 3374 1885 2621 -180 -254 -25 C ATOM 2907 CG PRO B 383 28.338 -5.307 -11.875 1.00 20.51 C ANISOU 2907 CG PRO B 383 3316 1843 2634 -260 -227 -44 C ATOM 2908 CD PRO B 383 28.949 -4.516 -12.982 1.00 20.05 C ANISOU 2908 CD PRO B 383 3153 1872 2593 -238 -242 -77 C ATOM 2909 N GLN B 384 30.931 -7.576 -12.565 1.00 21.75 N ANISOU 2909 N GLN B 384 3605 1944 2715 16 -297 -79 N ATOM 2910 CA GLN B 384 31.491 -8.915 -12.771 1.00 22.86 C ANISOU 2910 CA GLN B 384 3866 1999 2819 129 -309 -90 C ATOM 2911 C GLN B 384 33.004 -8.902 -12.992 1.00 23.30 C ANISOU 2911 C GLN B 384 3859 2160 2834 287 -332 -90 C ATOM 2912 O GLN B 384 33.701 -9.822 -12.569 1.00 24.37 O ANISOU 2912 O GLN B 384 4081 2253 2926 415 -345 -70 O ATOM 2913 CB GLN B 384 30.792 -9.626 -13.929 1.00 23.14 C ANISOU 2913 CB GLN B 384 3981 1945 2866 89 -302 -140 C ATOM 2914 CG GLN B 384 29.399 -10.169 -13.600 1.00 23.75 C ANISOU 2914 CG GLN B 384 4161 1895 2970 -54 -290 -124 C ATOM 2915 CD GLN B 384 28.299 -9.108 -13.623 1.00 23.08 C ANISOU 2915 CD GLN B 384 3959 1882 2929 -201 -267 -110 C ATOM 2916 OE1 GLN B 384 28.525 -7.954 -13.994 1.00 21.98 O ANISOU 2916 OE1 GLN B 384 3681 1865 2805 -200 -261 -120 O ATOM 2917 NE2 GLN B 384 27.097 -9.507 -13.226 1.00 23.40 N ANISOU 2917 NE2 GLN B 384 4056 1848 2987 -326 -251 -78 N ATOM 2918 N ARG B 385 33.502 -7.852 -13.642 1.00 22.76 N ANISOU 2918 N ARG B 385 3635 2235 2778 279 -336 -101 N ATOM 2919 CA ARG B 385 34.938 -7.661 -13.863 1.00 23.31 C ANISOU 2919 CA ARG B 385 3601 2446 2809 407 -356 -84 C ATOM 2920 C ARG B 385 35.735 -7.598 -12.547 1.00 23.50 C ANISOU 2920 C ARG B 385 3605 2525 2800 460 -390 -30 C ATOM 2921 O ARG B 385 36.895 -7.999 -12.505 1.00 24.29 O ANISOU 2921 O ARG B 385 3667 2710 2851 603 -410 -4 O ATOM 2922 CB ARG B 385 35.172 -6.407 -14.727 1.00 22.79 C ANISOU 2922 CB ARG B 385 3367 2521 2769 345 -353 -90 C ATOM 2923 CG ARG B 385 36.625 -6.077 -15.095 1.00 23.90 C ANISOU 2923 CG ARG B 385 3367 2842 2874 447 -371 -60 C ATOM 2924 CD ARG B 385 37.263 -5.186 -14.045 1.00 24.72 C ANISOU 2924 CD ARG B 385 3372 3044 2976 397 -414 -10 C ATOM 2925 NE ARG B 385 38.196 -4.213 -14.608 1.00 26.02 N ANISOU 2925 NE ARG B 385 3358 3390 3140 377 -431 23 N ATOM 2926 CZ ARG B 385 39.501 -4.170 -14.347 1.00 26.82 C ANISOU 2926 CZ ARG B 385 3344 3649 3196 454 -467 75 C ATOM 2927 NH1 ARG B 385 40.252 -3.231 -14.912 1.00 26.85 N ANISOU 2927 NH1 ARG B 385 3178 3818 3204 404 -481 113 N ATOM 2928 NH2 ARG B 385 40.057 -5.055 -13.525 1.00 27.22 N ANISOU 2928 NH2 ARG B 385 3444 3702 3197 578 -489 98 N ATOM 2929 N TYR B 386 35.104 -7.106 -11.483 1.00 23.01 N ANISOU 2929 N TYR B 386 3565 2423 2754 353 -397 -10 N ATOM 2930 CA TYR B 386 35.758 -6.983 -10.176 1.00 23.46 C ANISOU 2930 CA TYR B 386 3613 2533 2768 387 -437 36 C ATOM 2931 C TYR B 386 35.381 -8.122 -9.240 1.00 24.35 C ANISOU 2931 C TYR B 386 3889 2514 2850 438 -430 65 C ATOM 2932 O TYR B 386 35.856 -8.184 -8.101 1.00 24.99 O ANISOU 2932 O TYR B 386 3983 2629 2883 479 -461 109 O ATOM 2933 CB TYR B 386 35.440 -5.630 -9.527 1.00 22.52 C ANISOU 2933 CB TYR B 386 3423 2465 2667 252 -453 37 C ATOM 2934 CG TYR B 386 35.791 -4.445 -10.393 1.00 21.76 C ANISOU 2934 CG TYR B 386 3183 2480 2604 186 -463 20 C ATOM 2935 CD1 TYR B 386 37.114 -4.029 -10.534 1.00 21.82 C ANISOU 2935 CD1 TYR B 386 3061 2645 2586 229 -510 47 C ATOM 2936 CD2 TYR B 386 34.801 -3.747 -11.088 1.00 20.72 C ANISOU 2936 CD2 TYR B 386 3038 2306 2528 80 -426 -11 C ATOM 2937 CE1 TYR B 386 37.447 -2.944 -11.335 1.00 21.66 C ANISOU 2937 CE1 TYR B 386 2909 2723 2596 154 -518 45 C ATOM 2938 CE2 TYR B 386 35.124 -2.657 -11.898 1.00 20.38 C ANISOU 2938 CE2 TYR B 386 2875 2356 2515 21 -433 -16 C ATOM 2939 CZ TYR B 386 36.448 -2.264 -12.013 1.00 21.14 C ANISOU 2939 CZ TYR B 386 2852 2594 2586 52 -479 13 C ATOM 2940 OH TYR B 386 36.782 -1.196 -12.811 1.00 21.26 O ANISOU 2940 OH TYR B 386 2750 2697 2629 -20 -486 22 O ATOM 2941 N GLY B 387 34.534 -9.026 -9.733 1.00 24.76 N ANISOU 2941 N GLY B 387 4068 2417 2923 428 -393 44 N ATOM 2942 CA GLY B 387 34.092 -10.188 -8.962 1.00 25.48 C ANISOU 2942 CA GLY B 387 4333 2358 2990 458 -383 79 C ATOM 2943 C GLY B 387 32.853 -9.906 -8.136 1.00 25.10 C ANISOU 2943 C GLY B 387 4332 2243 2963 310 -357 102 C ATOM 2944 O GLY B 387 32.513 -10.684 -7.246 1.00 26.02 O ANISOU 2944 O GLY B 387 4573 2263 3052 317 -349 151 O ATOM 2945 N PHE B 388 32.189 -8.784 -8.418 1.00 23.93 N ANISOU 2945 N PHE B 388 4083 2154 2857 186 -340 74 N ATOM 2946 CA PHE B 388 30.891 -8.481 -7.823 1.00 23.27 C ANISOU 2946 CA PHE B 388 4029 2023 2792 56 -302 94 C ATOM 2947 C PHE B 388 29.825 -9.096 -8.710 1.00 23.29 C ANISOU 2947 C PHE B 388 4087 1922 2839 -28 -271 76 C ATOM 2948 O PHE B 388 29.408 -8.491 -9.700 1.00 22.58 O ANISOU 2948 O PHE B 388 3915 1874 2792 -90 -261 34 O ATOM 2949 CB PHE B 388 30.669 -6.971 -7.701 1.00 22.12 C ANISOU 2949 CB PHE B 388 3759 1984 2662 -17 -297 74 C ATOM 2950 CG PHE B 388 31.704 -6.263 -6.873 1.00 22.17 C ANISOU 2950 CG PHE B 388 3712 2090 2620 36 -342 82 C ATOM 2951 CD1 PHE B 388 31.867 -6.565 -5.525 1.00 22.31 C ANISOU 2951 CD1 PHE B 388 3801 2100 2574 71 -354 126 C ATOM 2952 CD2 PHE B 388 32.503 -5.275 -7.438 1.00 21.30 C ANISOU 2952 CD2 PHE B 388 3481 2089 2525 37 -376 50 C ATOM 2953 CE1 PHE B 388 32.826 -5.905 -4.760 1.00 22.41 C ANISOU 2953 CE1 PHE B 388 3766 2216 2534 107 -409 129 C ATOM 2954 CE2 PHE B 388 33.463 -4.607 -6.676 1.00 21.19 C ANISOU 2954 CE2 PHE B 388 3416 2172 2465 58 -431 58 C ATOM 2955 CZ PHE B 388 33.623 -4.922 -5.338 1.00 21.90 C ANISOU 2955 CZ PHE B 388 3578 2256 2486 93 -451 93 C ATOM 2956 N ASN B 389 29.386 -10.300 -8.354 1.00 24.27 N ANISOU 2956 N ASN B 389 4357 1914 2951 -37 -262 113 N ATOM 2957 CA ASN B 389 28.521 -11.085 -9.233 1.00 24.70 C ANISOU 2957 CA ASN B 389 4490 1855 3040 -123 -251 93 C ATOM 2958 C ASN B 389 27.041 -11.103 -8.855 1.00 25.08 C ANISOU 2958 C ASN B 389 4549 1868 3113 -289 -213 139 C ATOM 2959 O ASN B 389 26.195 -11.452 -9.681 1.00 25.42 O ANISOU 2959 O ASN B 389 4610 1860 3190 -396 -211 120 O ATOM 2960 CB ASN B 389 29.069 -12.504 -9.378 1.00 25.67 C ANISOU 2960 CB ASN B 389 4786 1833 3136 -28 -274 94 C ATOM 2961 CG ASN B 389 30.491 -12.527 -9.915 1.00 25.36 C ANISOU 2961 CG ASN B 389 4718 1850 3066 153 -303 52 C ATOM 2962 OD1 ASN B 389 31.356 -13.212 -9.375 1.00 25.33 O ANISOU 2962 OD1 ASN B 389 4799 1810 3016 294 -320 83 O ATOM 2963 ND2 ASN B 389 30.739 -11.770 -10.979 1.00 23.95 N ANISOU 2963 ND2 ASN B 389 4414 1778 2909 157 -307 -9 N ATOM 2964 N THR B 390 26.728 -10.728 -7.618 1.00 25.40 N ANISOU 2964 N THR B 390 4573 1950 3128 -309 -184 202 N ATOM 2965 CA THR B 390 25.345 -10.754 -7.140 1.00 26.15 C ANISOU 2965 CA THR B 390 4664 2038 3234 -451 -137 263 C ATOM 2966 C THR B 390 24.830 -9.341 -6.893 1.00 25.43 C ANISOU 2966 C THR B 390 4423 2092 3147 -481 -99 260 C ATOM 2967 O THR B 390 25.619 -8.404 -6.803 1.00 24.95 O ANISOU 2967 O THR B 390 4293 2113 3072 -397 -115 219 O ATOM 2968 CB THR B 390 25.204 -11.588 -5.840 1.00 27.30 C ANISOU 2968 CB THR B 390 4932 2109 3332 -451 -118 356 C ATOM 2969 OG1 THR B 390 26.010 -11.013 -4.806 1.00 27.17 O ANISOU 2969 OG1 THR B 390 4894 2170 3258 -337 -120 369 O ATOM 2970 CG2 THR B 390 25.630 -13.036 -6.066 1.00 28.26 C ANISOU 2970 CG2 THR B 390 5232 2058 3449 -419 -152 367 C ATOM 2971 N LEU B 391 23.510 -9.189 -6.788 1.00 25.91 N ANISOU 2971 N LEU B 391 4437 2186 3223 -600 -51 307 N ATOM 2972 CA LEU B 391 22.906 -7.901 -6.424 1.00 25.59 C ANISOU 2972 CA LEU B 391 4274 2275 3174 -608 -3 315 C ATOM 2973 C LEU B 391 23.384 -7.419 -5.056 1.00 25.96 C ANISOU 2973 C LEU B 391 4349 2362 3152 -520 15 339 C ATOM 2974 O LEU B 391 23.595 -6.227 -4.854 1.00 25.33 O ANISOU 2974 O LEU B 391 4203 2364 3056 -467 22 302 O ATOM 2975 CB LEU B 391 21.374 -7.963 -6.463 1.00 25.88 C ANISOU 2975 CB LEU B 391 4250 2357 3226 -737 53 382 C ATOM 2976 CG LEU B 391 20.742 -7.996 -7.860 1.00 25.80 C ANISOU 2976 CG LEU B 391 4167 2362 3276 -831 34 351 C ATOM 2977 CD1 LEU B 391 19.238 -8.212 -7.776 1.00 26.39 C ANISOU 2977 CD1 LEU B 391 4173 2496 3357 -971 82 436 C ATOM 2978 CD2 LEU B 391 21.066 -6.730 -8.663 1.00 24.37 C ANISOU 2978 CD2 LEU B 391 3874 2266 3118 -766 25 278 C ATOM 2979 N ASP B 392 23.565 -8.353 -4.127 1.00 27.41 N ANISOU 2979 N ASP B 392 4643 2480 3290 -505 17 400 N ATOM 2980 CA ASP B 392 24.103 -8.029 -2.812 1.00 27.97 C ANISOU 2980 CA ASP B 392 4755 2590 3281 -417 22 423 C ATOM 2981 C ASP B 392 25.532 -7.509 -2.940 1.00 27.40 C ANISOU 2981 C ASP B 392 4673 2540 3196 -308 -47 348 C ATOM 2982 O ASP B 392 25.877 -6.485 -2.345 1.00 27.24 O ANISOU 2982 O ASP B 392 4618 2599 3132 -260 -52 319 O ATOM 2983 CB ASP B 392 24.050 -9.244 -1.887 1.00 29.32 C ANISOU 2983 CB ASP B 392 5054 2682 3404 -421 33 515 C ATOM 2984 CG ASP B 392 24.436 -8.907 -0.462 1.00 30.78 C ANISOU 2984 CG ASP B 392 5278 2925 3490 -336 45 549 C ATOM 2985 OD1 ASP B 392 24.028 -7.834 0.037 1.00 31.90 O ANISOU 2985 OD1 ASP B 392 5357 3171 3593 -325 84 534 O ATOM 2986 OD2 ASP B 392 25.148 -9.720 0.166 1.00 32.72 O ANISOU 2986 OD2 ASP B 392 5630 3114 3689 -273 14 590 O ATOM 2987 N ALA B 393 26.349 -8.203 -3.734 1.00 27.34 N ANISOU 2987 N ALA B 393 4698 2468 3224 -271 -100 318 N ATOM 2988 CA ALA B 393 27.724 -7.776 -3.984 1.00 27.06 C ANISOU 2988 CA ALA B 393 4626 2477 3178 -172 -164 260 C ATOM 2989 C ALA B 393 27.760 -6.373 -4.606 1.00 26.25 C ANISOU 2989 C ALA B 393 4399 2466 3109 -195 -169 194 C ATOM 2990 O ALA B 393 28.535 -5.512 -4.180 1.00 26.05 O ANISOU 2990 O ALA B 393 4336 2512 3050 -151 -204 165 O ATOM 2991 CB ALA B 393 28.439 -8.776 -4.863 1.00 27.16 C ANISOU 2991 CB ALA B 393 4686 2415 3219 -118 -203 243 C ATOM 2992 N ILE B 394 26.899 -6.159 -5.598 1.00 25.94 N ANISOU 2992 N ILE B 394 4303 2420 3131 -271 -137 175 N ATOM 2993 CA ILE B 394 26.748 -4.875 -6.275 1.00 25.19 C ANISOU 2993 CA ILE B 394 4101 2398 3072 -296 -133 126 C ATOM 2994 C ILE B 394 26.368 -3.757 -5.304 1.00 25.42 C ANISOU 2994 C ILE B 394 4116 2483 3058 -295 -103 130 C ATOM 2995 O ILE B 394 26.952 -2.673 -5.330 1.00 24.92 O ANISOU 2995 O ILE B 394 4013 2467 2990 -273 -132 86 O ATOM 2996 CB ILE B 394 25.687 -4.979 -7.390 1.00 24.92 C ANISOU 2996 CB ILE B 394 4016 2353 3099 -378 -99 124 C ATOM 2997 CG1 ILE B 394 26.231 -5.815 -8.554 1.00 24.72 C ANISOU 2997 CG1 ILE B 394 4006 2280 3108 -368 -139 91 C ATOM 2998 CG2 ILE B 394 25.237 -3.590 -7.855 1.00 24.03 C ANISOU 2998 CG2 ILE B 394 3802 2316 3012 -399 -77 97 C ATOM 2999 CD1 ILE B 394 25.212 -6.138 -9.608 1.00 24.47 C ANISOU 2999 CD1 ILE B 394 3946 2229 3121 -459 -122 87 C ATOM 3000 N LEU B 395 25.394 -4.038 -4.444 1.00 26.39 N ANISOU 3000 N LEU B 395 4282 2600 3145 -319 -45 185 N ATOM 3001 CA LEU B 395 24.867 -3.049 -3.514 1.00 26.82 C ANISOU 3001 CA LEU B 395 4338 2708 3145 -301 -1 189 C ATOM 3002 C LEU B 395 25.860 -2.683 -2.417 1.00 27.47 C ANISOU 3002 C LEU B 395 4484 2807 3147 -234 -47 167 C ATOM 3003 O LEU B 395 26.126 -1.508 -2.189 1.00 27.15 O ANISOU 3003 O LEU B 395 4436 2799 3081 -214 -63 116 O ATOM 3004 CB LEU B 395 23.561 -3.550 -2.888 1.00 27.42 C ANISOU 3004 CB LEU B 395 4430 2795 3192 -339 82 268 C ATOM 3005 CG LEU B 395 22.308 -3.613 -3.765 1.00 27.18 C ANISOU 3005 CG LEU B 395 4314 2789 3222 -417 135 300 C ATOM 3006 CD1 LEU B 395 21.237 -4.438 -3.082 1.00 28.02 C ANISOU 3006 CD1 LEU B 395 4439 2910 3298 -473 202 399 C ATOM 3007 CD2 LEU B 395 21.787 -2.225 -4.085 1.00 26.61 C ANISOU 3007 CD2 LEU B 395 4165 2788 3159 -391 171 266 C ATOM 3008 N THR B 396 26.417 -3.699 -1.762 1.00 28.67 N ANISOU 3008 N THR B 396 4707 2932 3256 -203 -74 206 N ATOM 3009 CA THR B 396 27.150 -3.511 -0.508 1.00 29.90 C ANISOU 3009 CA THR B 396 4930 3119 3313 -142 -112 205 C ATOM 3010 C THR B 396 28.666 -3.619 -0.641 1.00 30.41 C ANISOU 3010 C THR B 396 4984 3199 3370 -96 -211 174 C ATOM 3011 O THR B 396 29.396 -3.196 0.252 1.00 31.05 O ANISOU 3011 O THR B 396 5097 3329 3373 -59 -263 158 O ATOM 3012 CB THR B 396 26.678 -4.512 0.568 1.00 30.76 C ANISOU 3012 CB THR B 396 5127 3209 3352 -124 -69 292 C ATOM 3013 OG1 THR B 396 26.847 -5.846 0.079 1.00 31.25 O ANISOU 3013 OG1 THR B 396 5218 3197 3460 -133 -81 340 O ATOM 3014 CG2 THR B 396 25.208 -4.288 0.914 1.00 30.85 C ANISOU 3014 CG2 THR B 396 5132 3243 3347 -164 33 336 C ATOM 3015 N GLY B 397 29.136 -4.195 -1.743 1.00 30.73 N ANISOU 3015 N GLY B 397 4979 3212 3484 -95 -238 168 N ATOM 3016 CA GLY B 397 30.572 -4.325 -1.992 1.00 31.68 C ANISOU 3016 CA GLY B 397 5065 3374 3599 -38 -322 149 C ATOM 3017 C GLY B 397 31.215 -5.536 -1.336 1.00 33.22 C ANISOU 3017 C GLY B 397 5332 3551 3738 47 -351 207 C ATOM 3018 O GLY B 397 32.420 -5.753 -1.475 1.00 33.52 O ANISOU 3018 O GLY B 397 5335 3640 3761 116 -418 206 O ATOM 3019 N LYS B 398 30.412 -6.329 -0.629 1.00 34.48 N ANISOU 3019 N LYS B 398 5589 3645 3865 45 -298 269 N ATOM 3020 CA LYS B 398 30.915 -7.505 0.079 1.00 36.20 C ANISOU 3020 CA LYS B 398 5900 3829 4026 129 -318 339 C ATOM 3021 C LYS B 398 30.594 -8.805 -0.651 1.00 36.82 C ANISOU 3021 C LYS B 398 6045 3784 4161 135 -289 376 C ATOM 3022 O LYS B 398 29.434 -9.099 -0.948 1.00 36.66 O ANISOU 3022 O LYS B 398 6055 3689 4185 46 -227 395 O ATOM 3023 CB LYS B 398 30.411 -7.533 1.529 1.00 36.93 C ANISOU 3023 CB LYS B 398 6074 3936 4020 131 -289 395 C ATOM 3024 CG LYS B 398 31.183 -6.582 2.446 1.00 37.95 C ANISOU 3024 CG LYS B 398 6181 4181 4057 166 -352 361 C ATOM 3025 CD LYS B 398 30.458 -6.321 3.764 1.00 39.93 C ANISOU 3025 CD LYS B 398 6508 4456 4206 157 -307 395 C ATOM 3026 CE LYS B 398 31.171 -5.247 4.592 1.00 40.80 C ANISOU 3026 CE LYS B 398 6611 4673 4219 176 -379 338 C ATOM 3027 NZ LYS B 398 30.496 -4.978 5.907 1.00 42.30 N ANISOU 3027 NZ LYS B 398 6890 4894 4289 187 -334 362 N ATOM 3028 N LYS B 399 31.648 -9.564 -0.940 1.00 37.98 N ANISOU 3028 N LYS B 399 6216 3915 4301 243 -339 387 N ATOM 3029 CA LYS B 399 31.547 -10.867 -1.593 1.00 39.14 C ANISOU 3029 CA LYS B 399 6460 3925 4485 277 -324 414 C ATOM 3030 C LYS B 399 31.192 -11.976 -0.599 1.00 41.11 C ANISOU 3030 C LYS B 399 6867 4071 4682 301 -300 512 C ATOM 3031 O LYS B 399 31.107 -11.743 0.612 1.00 41.69 O ANISOU 3031 O LYS B 399 6960 4200 4680 306 -295 563 O ATOM 3032 CB LYS B 399 32.855 -11.198 -2.312 1.00 39.23 C ANISOU 3032 CB LYS B 399 6439 3968 4499 413 -378 386 C ATOM 3033 CG LYS B 399 33.229 -10.211 -3.400 1.00 37.59 C ANISOU 3033 CG LYS B 399 6078 3860 4344 386 -397 304 C ATOM 3034 CD LYS B 399 34.683 -10.351 -3.787 1.00 37.29 C ANISOU 3034 CD LYS B 399 5972 3917 4281 532 -453 298 C ATOM 3035 CE LYS B 399 35.041 -9.366 -4.874 1.00 36.68 C ANISOU 3035 CE LYS B 399 5739 3945 4252 492 -466 231 C ATOM 3036 NZ LYS B 399 36.428 -9.567 -5.365 1.00 37.57 N ANISOU 3036 NZ LYS B 399 5769 4168 4339 636 -509 236 N ATOM 3037 N HIS B 400 30.998 -13.183 -1.122 1.00 42.66 N ANISOU 3037 N HIS B 400 7187 4113 4911 316 -287 539 N ATOM 3038 CA HIS B 400 30.488 -14.312 -0.348 1.00 44.78 C ANISOU 3038 CA HIS B 400 7624 4247 5146 306 -258 641 C ATOM 3039 C HIS B 400 31.318 -15.567 -0.664 1.00 46.61 C ANISOU 3039 C HIS B 400 7995 4348 5365 452 -291 666 C ATOM 3040 O HIS B 400 31.599 -15.809 -1.842 1.00 46.54 O ANISOU 3040 O HIS B 400 7988 4286 5408 484 -306 597 O ATOM 3041 CB HIS B 400 29.010 -14.521 -0.710 1.00 44.57 C ANISOU 3041 CB HIS B 400 7630 4124 5180 119 -199 656 C ATOM 3042 CG HIS B 400 28.366 -15.676 -0.012 1.00 46.41 C ANISOU 3042 CG HIS B 400 8033 4212 5388 68 -166 770 C ATOM 3043 ND1 HIS B 400 27.721 -15.548 1.201 1.00 47.02 N ANISOU 3043 ND1 HIS B 400 8120 4338 5406 11 -120 863 N ATOM 3044 CD2 HIS B 400 28.254 -16.980 -0.362 1.00 47.66 C ANISOU 3044 CD2 HIS B 400 8368 4171 5568 61 -172 810 C ATOM 3045 CE1 HIS B 400 27.249 -16.725 1.572 1.00 48.67 C ANISOU 3045 CE1 HIS B 400 8493 4393 5607 -37 -98 967 C ATOM 3046 NE2 HIS B 400 27.558 -17.611 0.641 1.00 49.03 N ANISOU 3046 NE2 HIS B 400 8651 4275 5704 -13 -132 935 N ATOM 3047 N HIS B 401 31.745 -16.375 0.320 1.00 48.72 N ANISOU 3047 N HIS B 401 8388 4564 5559 559 -301 762 N ATOM 3048 CA HIS B 401 31.625 -16.227 1.796 1.00 49.87 C ANISOU 3048 CA HIS B 401 8550 4780 5616 562 -291 855 C ATOM 3049 C HIS B 401 31.023 -17.444 2.522 1.00 51.59 C ANISOU 3049 C HIS B 401 8970 4828 5803 537 -254 981 C ATOM 3050 O HIS B 401 30.066 -17.330 3.300 1.00 51.89 O ANISOU 3050 O HIS B 401 9024 4874 5817 414 -204 1050 O ATOM 3051 CB HIS B 401 30.996 -14.899 2.255 1.00 48.85 C ANISOU 3051 CB HIS B 401 8276 4809 5476 440 -266 821 C ATOM 3052 CG HIS B 401 31.978 -13.961 2.887 1.00 49.58 C ANISOU 3052 CG HIS B 401 8253 5091 5494 533 -322 791 C ATOM 3053 ND1 HIS B 401 32.812 -13.147 2.149 1.00 49.01 N ANISOU 3053 ND1 HIS B 401 8038 5131 5451 574 -373 697 N ATOM 3054 CD2 HIS B 401 32.271 -13.723 4.189 1.00 50.85 C ANISOU 3054 CD2 HIS B 401 8424 5352 5545 584 -340 847 C ATOM 3055 CE1 HIS B 401 33.570 -12.440 2.970 1.00 49.64 C ANISOU 3055 CE1 HIS B 401 8046 5368 5448 630 -427 695 C ATOM 3056 NE2 HIS B 401 33.262 -12.770 4.213 1.00 50.85 N ANISOU 3056 NE2 HIS B 401 8291 5516 5512 642 -411 779 N ATOM 3057 N HIS B 402 31.614 -18.609 2.249 1.00 52.99 N ANISOU 3057 N HIS B 402 9306 4852 5977 664 -278 1017 N ATOM 3058 CA HIS B 402 31.348 -19.870 2.958 1.00 55.02 C ANISOU 3058 CA HIS B 402 9784 4927 6194 684 -258 1148 C ATOM 3059 C HIS B 402 32.668 -20.642 2.964 1.00 56.34 C ANISOU 3059 C HIS B 402 10050 5047 6309 939 -309 1174 C ATOM 3060 O HIS B 402 33.288 -20.707 1.912 1.00 56.36 O ANISOU 3060 O HIS B 402 10030 5033 6353 1033 -336 1084 O ATOM 3061 CB HIS B 402 30.249 -20.679 2.253 1.00 55.63 C ANISOU 3061 CB HIS B 402 10005 4778 6354 511 -221 1158 C ATOM 3062 CG HIS B 402 30.308 -20.627 0.752 1.00 54.73 C ANISOU 3062 CG HIS B 402 9863 4604 6326 490 -241 1026 C ATOM 3063 ND1 HIS B 402 31.373 -21.118 0.025 1.00 55.13 N ANISOU 3063 ND1 HIS B 402 9980 4594 6375 686 -284 969 N ATOM 3064 CD2 HIS B 402 29.415 -20.169 -0.158 1.00 53.38 C ANISOU 3064 CD2 HIS B 402 9609 4435 6237 306 -223 947 C ATOM 3065 CE1 HIS B 402 31.141 -20.949 -1.265 1.00 54.06 C ANISOU 3065 CE1 HIS B 402 9807 4423 6311 620 -289 855 C ATOM 3066 NE2 HIS B 402 29.958 -20.377 -1.404 1.00 52.81 N ANISOU 3066 NE2 HIS B 402 9559 4300 6207 386 -257 840 N ATOM 3067 N HIS B 403 33.143 -21.248 4.063 1.00 57.89 N ANISOU 3067 N HIS B 403 10354 5232 6411 1071 -320 1297 N ATOM 3068 CA HIS B 403 32.487 -21.582 5.353 1.00 58.96 C ANISOU 3068 CA HIS B 403 10586 5337 6479 998 -283 1437 C ATOM 3069 C HIS B 403 31.998 -23.034 5.376 1.00 60.79 C ANISOU 3069 C HIS B 403 11093 5278 6727 974 -254 1545 C ATOM 3070 O HIS B 403 30.852 -23.336 5.037 1.00 60.92 O ANISOU 3070 O HIS B 403 11182 5152 6813 762 -210 1557 O ATOM 3071 CB HIS B 403 31.438 -20.561 5.830 1.00 57.81 C ANISOU 3071 CB HIS B 403 10299 5329 6335 789 -235 1427 C ATOM 3072 CG HIS B 403 32.019 -19.222 6.183 1.00 57.02 C ANISOU 3072 CG HIS B 403 9984 5497 6183 837 -271 1351 C ATOM 3073 ND1 HIS B 403 33.126 -19.081 6.993 1.00 57.78 N ANISOU 3073 ND1 HIS B 403 10048 5735 6172 1017 -329 1386 N ATOM 3074 CD2 HIS B 403 31.648 -17.966 5.832 1.00 55.41 C ANISOU 3074 CD2 HIS B 403 9597 5438 6018 723 -262 1243 C ATOM 3075 CE1 HIS B 403 33.418 -17.798 7.115 1.00 56.57 C ANISOU 3075 CE1 HIS B 403 9705 5795 5994 995 -360 1297 C ATOM 3076 NE2 HIS B 403 32.533 -17.100 6.426 1.00 54.87 N ANISOU 3076 NE2 HIS B 403 9405 5576 5868 823 -317 1210 N ATOM 3077 N HIS B 404 32.904 -23.930 5.770 1.00 62.37 N ANISOU 3077 N HIS B 404 11445 5393 6860 1196 -285 1628 N ATOM 3078 CA HIS B 404 32.679 -25.377 5.686 1.00 64.48 C ANISOU 3078 CA HIS B 404 12009 5352 7140 1219 -271 1722 C ATOM 3079 C HIS B 404 32.055 -25.998 6.939 1.00 66.00 C ANISOU 3079 C HIS B 404 12351 5460 7266 1145 -231 1907 C ATOM 3080 O HIS B 404 32.320 -25.572 8.061 1.00 65.99 O ANISOU 3080 O HIS B 404 12265 5645 7165 1208 -232 1985 O ATOM 3081 CB HIS B 404 33.974 -26.114 5.298 1.00 65.70 C ANISOU 3081 CB HIS B 404 12278 5427 7259 1523 -318 1715 C ATOM 3082 CG HIS B 404 35.022 -26.125 6.369 1.00 66.63 C ANISOU 3082 CG HIS B 404 12360 5704 7252 1763 -353 1815 C ATOM 3083 ND1 HIS B 404 36.068 -25.226 6.397 1.00 65.58 N ANISOU 3083 ND1 HIS B 404 11989 5857 7070 1916 -403 1750 N ATOM 3084 CD2 HIS B 404 35.196 -26.937 7.440 1.00 68.57 C ANISOU 3084 CD2 HIS B 404 12779 5870 7406 1873 -350 1983 C ATOM 3085 CE1 HIS B 404 36.835 -25.479 7.444 1.00 66.84 C ANISOU 3085 CE1 HIS B 404 12167 6117 7111 2107 -435 1869 C ATOM 3086 NE2 HIS B 404 36.327 -26.511 8.094 1.00 68.43 N ANISOU 3086 NE2 HIS B 404 12618 6100 7282 2094 -401 2012 N TER 3087 HIS B 404 HETATM 3088 PA NAI B 405 39.392 16.453 -20.897 1.00 20.55 P HETATM 3089 O1A NAI B 405 39.384 15.715 -22.184 1.00 20.64 O HETATM 3090 O2A NAI B 405 39.605 17.906 -21.077 1.00 20.35 O HETATM 3091 O5B NAI B 405 40.525 15.831 -19.953 1.00 21.17 O HETATM 3092 C5B NAI B 405 41.835 15.612 -20.411 1.00 23.16 C HETATM 3093 C4B NAI B 405 42.607 15.107 -19.204 1.00 24.74 C HETATM 3094 O4B NAI B 405 42.532 13.695 -19.120 1.00 26.22 O HETATM 3095 C3B NAI B 405 44.081 15.443 -19.251 1.00 24.73 C HETATM 3096 O3B NAI B 405 44.323 16.710 -18.709 1.00 23.95 O HETATM 3097 C2B NAI B 405 44.677 14.350 -18.398 1.00 25.62 C HETATM 3098 O2B NAI B 405 44.713 14.747 -17.046 1.00 24.55 O HETATM 3099 C1B NAI B 405 43.726 13.173 -18.580 1.00 27.21 C HETATM 3100 N9A NAI B 405 44.329 12.202 -19.517 1.00 28.07 N HETATM 3101 C8A NAI B 405 44.294 12.235 -20.892 1.00 28.37 C HETATM 3102 N7A NAI B 405 44.978 11.169 -21.373 1.00 28.26 N HETATM 3103 C5A NAI B 405 45.455 10.458 -20.329 1.00 28.30 C HETATM 3104 C6A NAI B 405 46.210 9.289 -20.258 1.00 28.41 C HETATM 3105 N6A NAI B 405 46.253 8.484 -21.314 1.00 29.11 N HETATM 3106 N1A NAI B 405 46.561 8.780 -19.017 1.00 28.52 N HETATM 3107 C2A NAI B 405 46.152 9.426 -17.858 1.00 28.65 C HETATM 3108 N3A NAI B 405 45.399 10.589 -17.938 1.00 28.53 N HETATM 3109 C4A NAI B 405 45.055 11.095 -19.155 1.00 28.33 C HETATM 3110 O3 NAI B 405 38.034 16.158 -20.083 1.00 20.82 O HETATM 3111 PN NAI B 405 37.059 17.331 -19.562 1.00 21.32 P HETATM 3112 O1N NAI B 405 36.741 18.218 -20.698 1.00 21.99 O HETATM 3113 O2N NAI B 405 37.586 17.938 -18.307 1.00 21.05 O HETATM 3114 O5D NAI B 405 35.749 16.473 -19.215 1.00 21.63 O HETATM 3115 C5D NAI B 405 35.760 15.559 -18.139 1.00 23.16 C HETATM 3116 C4D NAI B 405 34.623 14.562 -18.311 1.00 24.24 C HETATM 3117 O4D NAI B 405 33.390 15.253 -18.293 1.00 24.65 O HETATM 3118 C3D NAI B 405 34.719 13.830 -19.640 1.00 24.81 C HETATM 3119 O3D NAI B 405 34.478 12.464 -19.410 1.00 24.20 O HETATM 3120 C2D NAI B 405 33.619 14.415 -20.501 1.00 25.48 C HETATM 3121 O2D NAI B 405 32.994 13.408 -21.264 1.00 26.21 O HETATM 3122 C1D NAI B 405 32.659 15.038 -19.488 1.00 25.39 C HETATM 3123 N1N NAI B 405 32.030 16.295 -19.954 1.00 25.73 N HETATM 3124 C2N NAI B 405 32.748 17.304 -20.559 1.00 25.16 C HETATM 3125 C3N NAI B 405 32.110 18.477 -20.984 1.00 24.70 C HETATM 3126 C7N NAI B 405 32.910 19.734 -21.186 1.00 24.09 C HETATM 3127 O7N NAI B 405 34.319 19.697 -21.137 1.00 23.46 O HETATM 3128 N7N NAI B 405 32.260 20.876 -21.409 1.00 23.32 N HETATM 3129 C4N NAI B 405 30.732 18.612 -20.785 1.00 25.55 C HETATM 3130 C5N NAI B 405 30.008 17.596 -20.164 1.00 26.43 C HETATM 3131 C6N NAI B 405 30.677 16.441 -19.749 1.00 26.61 C HETATM 3132 N AG2 B 406 26.791 12.764 -22.056 0.50 35.37 N HETATM 3133 CA AG2 B 406 26.392 13.201 -20.689 0.50 35.42 C HETATM 3134 CB AG2 B 406 24.914 13.591 -20.669 0.50 35.43 C HETATM 3135 CG AG2 B 406 24.348 13.866 -19.285 0.50 35.68 C HETATM 3136 CD AG2 B 406 23.772 12.607 -18.649 0.50 36.22 C HETATM 3137 NE AG2 B 406 22.525 12.873 -17.934 0.50 36.54 N HETATM 3138 CZ AG2 B 406 22.100 12.184 -16.877 0.50 36.83 C HETATM 3139 NH1 AG2 B 406 22.819 11.178 -16.394 0.50 37.16 N HETATM 3140 NH2 AG2 B 406 20.951 12.504 -16.299 0.50 36.67 N CONECT 3088 3089 3090 3091 3110 CONECT 3089 3088 CONECT 3090 3088 CONECT 3091 3088 3092 CONECT 3092 3091 3093 CONECT 3093 3092 3094 3095 CONECT 3094 3093 3099 CONECT 3095 3093 3096 3097 CONECT 3096 3095 CONECT 3097 3095 3098 3099 CONECT 3098 3097 CONECT 3099 3094 3097 3100 CONECT 3100 3099 3101 3109 CONECT 3101 3100 3102 CONECT 3102 3101 3103 CONECT 3103 3102 3104 3109 CONECT 3104 3103 3105 3106 CONECT 3105 3104 CONECT 3106 3104 3107 CONECT 3107 3106 3108 CONECT 3108 3107 3109 CONECT 3109 3100 3103 3108 CONECT 3110 3088 3111 CONECT 3111 3110 3112 3113 3114 CONECT 3112 3111 CONECT 3113 3111 CONECT 3114 3111 3115 CONECT 3115 3114 3116 CONECT 3116 3115 3117 3118 CONECT 3117 3116 3122 CONECT 3118 3116 3119 3120 CONECT 3119 3118 CONECT 3120 3118 3121 3122 CONECT 3121 3120 CONECT 3122 3117 3120 3123 CONECT 3123 3122 3124 3131 CONECT 3124 3123 3125 CONECT 3125 3124 3126 3129 CONECT 3126 3125 3127 3128 CONECT 3127 3126 CONECT 3128 3126 CONECT 3129 3125 3130 CONECT 3130 3129 3131 CONECT 3131 3123 3130 CONECT 3132 3133 CONECT 3133 3132 3134 CONECT 3134 3133 3135 CONECT 3135 3134 3136 CONECT 3136 3135 3137 CONECT 3137 3136 3138 CONECT 3138 3137 3139 3140 CONECT 3139 3138 CONECT 3140 3138 MASTER 342 0 2 20 14 0 6 6 3139 1 53 32 END If you find 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