HEADER MEMBRANE PROTEIN 30-DEC-18 6J20
TITLE CRYSTAL STRUCTURE OF THE HUMAN NK1 SUBSTANCE P RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBSTANCE-P RECEPTOR,ENDOLYSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SPR,NK-1 RECEPTOR,NK-1R,TACHYKININ RECEPTOR 1,LYSIS PROTEIN,
COMPND 5 LYSOZYME,MURAMIDASE;
COMPND 6 EC: 3.2.1.17;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: THE FUSION PROTEIN OF SUBSTANCE-P RECEPTOR NK1R
COMPND 10 (RESIDUES 2-226), MINI-T4L (RESIDUES 1001-1010, 1017-1117), LINKER
COMPND 11 GGGSGG (RESIDUES 1011-1016), AND NK1R (RESIDUES 237-335)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;
SOURCE 3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;
SOURCE 4 ORGANISM_TAXID: 9606, 10665;
SOURCE 5 GENE: TACR1, NK1R, TAC1R, E, T4TP126;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS GPCR, COMPLEX, ANTAGONIST, SIGNALLING PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.CHEN,M.LU,H.ZHANG,B.WU,Q.ZHAO
REVDAT 1 06-MAR-19 6J20 0
JRNL AUTH S.CHEN,M.LU,D.LIU,L.YANG,C.YI,L.MA,H.ZHANG,Q.LIU,
JRNL AUTH 2 T.M.FRIMURER,M.W.WANG,T.W.SCHWARTZ,R.C.STEVENS,B.WU,
JRNL AUTH 3 K.WUTHRICH,Q.ZHAO
JRNL TITL HUMAN SUBSTANCE P RECEPTOR BINDING MODE OF THE ANTAGONIST
JRNL TITL 2 DRUG APREPITANT BY NMR AND CRYSTALLOGRAPHY.
JRNL REF NAT COMMUN V. 10 638 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 30733446
JRNL DOI 10.1038/S41467-019-08568-5
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 23622
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) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1201
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.68
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2774
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2100
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2648
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.54
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 126
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3147
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 101.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 114.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.12860
REMARK 3 B22 (A**2) : -9.12860
REMARK 3 B33 (A**2) : 18.25720
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.440
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.334
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.253
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.339
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.257
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3277 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4490 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1041 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 51 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 481 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3277 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 442 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3746 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.00
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.46
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.62
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -86.8273 55.3825 343.9060
REMARK 3 T TENSOR
REMARK 3 T11: -0.4676 T22: -0.2220
REMARK 3 T33: -0.4724 T12: 0.0604
REMARK 3 T13: -0.0147 T23: 0.1099
REMARK 3 L TENSOR
REMARK 3 L11: 0.0307 L22: 1.4075
REMARK 3 L33: 4.8976 L12: 0.4222
REMARK 3 L13: 0.5839 L23: 1.7571
REMARK 3 S TENSOR
REMARK 3 S11: 0.0360 S12: 0.0534 S13: 0.0278
REMARK 3 S21: -0.0904 S22: -0.1728 S23: -0.1261
REMARK 3 S31: -0.5015 S32: 0.7599 S33: 0.1368
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6J20 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1300010327.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26005
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.99000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4GRV, 4U15
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, PH 6.0-6.6, 25-35% PEG 400,
REMARK 280 200-350MM AMMONIUM TARTRATE DIBASIC, LIPIDIC CUBIC PHASE,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 51.25600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 51.25600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 78.48100
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 51.25600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 51.25600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 78.48100
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 51.25600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.25600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 78.48100
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 51.25600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.25600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 78.48100
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 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 2
REMARK 465 ASN A 3
REMARK 465 VAL A 4
REMARK 465 LEU A 5
REMARK 465 PRO A 6
REMARK 465 VAL A 7
REMARK 465 ASP A 8
REMARK 465 SER A 9
REMARK 465 ASP A 10
REMARK 465 LEU A 11
REMARK 465 SER A 12
REMARK 465 PRO A 13
REMARK 465 ASN A 14
REMARK 465 ILE A 15
REMARK 465 SER A 16
REMARK 465 THR A 17
REMARK 465 ASN A 18
REMARK 465 THR A 19
REMARK 465 SER A 20
REMARK 465 GLU A 21
REMARK 465 PRO A 22
REMARK 465 ASN A 23
REMARK 465 GLN A 24
REMARK 465 GLY A 1011
REMARK 465 GLY A 1012
REMARK 465 GLY A 1013
REMARK 465 SER A 1014
REMARK 465 GLY A 1015
REMARK 465 GLY A 1016
REMARK 465 CYS A 322
REMARK 465 CYS A 323
REMARK 465 PRO A 324
REMARK 465 PHE A 325
REMARK 465 ILE A 326
REMARK 465 SER A 327
REMARK 465 ALA A 328
REMARK 465 GLY A 329
REMARK 465 ASP A 330
REMARK 465 TYR A 331
REMARK 465 GLU A 332
REMARK 465 GLY A 333
REMARK 465 LEU A 334
REMARK 465 GLU A 335
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 25 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP A 30 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 30 CZ3 CH2
REMARK 470 LYS A 61 CG CD CE NZ
REMARK 470 ARG A 62 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 64 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 142 CG CD1 CD2
REMARK 470 SER A 176 OG
REMARK 470 LYS A 190 CG CD CE NZ
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 ASP A1017 CG OD1 OD2
REMARK 470 GLU A1018 CG CD OE1 OE2
REMARK 470 GLU A1020 CG CD OE1 OE2
REMARK 470 GLN A1025 CG CD OE1 NE2
REMARK 470 LYS A1103 CG CD CE NZ
REMARK 470 LYS A 243 CG CD CE NZ
REMARK 470 LEU A 277 CG CD1 CD2
REMARK 470 TYR A 278 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 279 CG CD1 CD2
REMARK 470 LYS A 280 CG CD CE NZ
REMARK 470 LYS A 281 CG CD CE NZ
REMARK 470 PHE A 282 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS A 318 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 320 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 321 CG CD NE CZ NH1 NH2
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 LYS A 61 -19.46 65.17
REMARK 500 ARG A 64 84.76 -66.64
REMARK 500 VAL A 66 -58.54 68.76
REMARK 500 HIS A 136 66.49 -119.80
REMARK 500 ASN A 189 12.97 -146.89
REMARK 500 TYR A 205 -82.53 -137.40
REMARK 500 ARG A1081 72.78 -102.69
REMARK 500 PRO A 271 -7.58 -53.18
REMARK 500 LYS A 281 -175.54 -67.10
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 GBQ A 1201
DBREF 6J20 A 2 226 UNP P25103 NK1R_HUMAN 2 226
DBREF 6J20 A 1001 1010 UNP D9IEF7 D9IEF7_BPT4 2 11
DBREF 6J20 A 1017 1117 UNP D9IEF7 D9IEF7_BPT4 61 161
DBREF 6J20 A 237 335 UNP P25103 NK1R_HUMAN 237 335
SEQADV 6J20 ASN A 78 UNP P25103 GLU 78 ENGINEERED MUTATION
SEQADV 6J20 TRP A 121 UNP P25103 TYR 121 ENGINEERED MUTATION
SEQADV 6J20 ARG A 222 UNP P25103 THR 222 ENGINEERED MUTATION
SEQADV 6J20 GLY A 1011 UNP D9IEF7 LINKER
SEQADV 6J20 GLY A 1012 UNP D9IEF7 LINKER
SEQADV 6J20 GLY A 1013 UNP D9IEF7 LINKER
SEQADV 6J20 SER A 1014 UNP D9IEF7 LINKER
SEQADV 6J20 GLY A 1015 UNP D9IEF7 LINKER
SEQADV 6J20 GLY A 1016 UNP D9IEF7 LINKER
SEQADV 6J20 ALA A 1053 UNP D9IEF7 CYS 97 ENGINEERED MUTATION
SEQRES 1 A 441 ASP ASN VAL LEU PRO VAL ASP SER ASP LEU SER PRO ASN
SEQRES 2 A 441 ILE SER THR ASN THR SER GLU PRO ASN GLN PHE VAL GLN
SEQRES 3 A 441 PRO ALA TRP GLN ILE VAL LEU TRP ALA ALA ALA TYR THR
SEQRES 4 A 441 VAL ILE VAL VAL THR SER VAL VAL GLY ASN VAL VAL VAL
SEQRES 5 A 441 MET TRP ILE ILE LEU ALA HIS LYS ARG MET ARG THR VAL
SEQRES 6 A 441 THR ASN TYR PHE LEU VAL ASN LEU ALA PHE ALA ASN ALA
SEQRES 7 A 441 SER MET ALA ALA PHE ASN THR VAL VAL ASN PHE THR TYR
SEQRES 8 A 441 ALA VAL HIS ASN GLU TRP TYR TYR GLY LEU PHE TYR CYS
SEQRES 9 A 441 LYS PHE HIS ASN PHE PHE PRO ILE ALA ALA VAL PHE ALA
SEQRES 10 A 441 SER ILE TRP SER MET THR ALA VAL ALA PHE ASP ARG TYR
SEQRES 11 A 441 MET ALA ILE ILE HIS PRO LEU GLN PRO ARG LEU SER ALA
SEQRES 12 A 441 THR ALA THR LYS VAL VAL ILE CYS VAL ILE TRP VAL LEU
SEQRES 13 A 441 ALA LEU LEU LEU ALA PHE PRO GLN GLY TYR TYR SER THR
SEQRES 14 A 441 THR GLU THR MET PRO SER ARG VAL VAL CYS MET ILE GLU
SEQRES 15 A 441 TRP PRO GLU HIS PRO ASN LYS ILE TYR GLU LYS VAL TYR
SEQRES 16 A 441 HIS ILE CYS VAL THR VAL LEU ILE TYR PHE LEU PRO LEU
SEQRES 17 A 441 LEU VAL ILE GLY TYR ALA TYR THR VAL VAL GLY ILE ARG
SEQRES 18 A 441 LEU TRP ALA SER ASN ILE PHE GLU MET LEU ARG ILE ASP
SEQRES 19 A 441 GLU GLY GLY GLY SER GLY GLY ASP GLU ALA GLU LYS LEU
SEQRES 20 A 441 PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU
SEQRES 21 A 441 ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP
SEQRES 22 A 441 ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN
SEQRES 23 A 441 MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU
SEQRES 24 A 441 ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL
SEQRES 25 A 441 ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN
SEQRES 26 A 441 ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR
SEQRES 27 A 441 TRP ASP ALA TYR HIS GLU GLN VAL SER ALA LYS ARG LYS
SEQRES 28 A 441 VAL VAL LYS MET MET ILE VAL VAL VAL CYS THR PHE ALA
SEQRES 29 A 441 ILE CYS TRP LEU PRO PHE HIS ILE PHE PHE LEU LEU PRO
SEQRES 30 A 441 TYR ILE ASN PRO ASP LEU TYR LEU LYS LYS PHE ILE GLN
SEQRES 31 A 441 GLN VAL TYR LEU ALA ILE MET TRP LEU ALA MET SER SER
SEQRES 32 A 441 THR MET TYR ASN PRO ILE ILE TYR CYS CYS LEU ASN ASP
SEQRES 33 A 441 ARG PHE ARG LEU GLY PHE LYS HIS ALA PHE ARG CYS CYS
SEQRES 34 A 441 PRO PHE ILE SER ALA GLY ASP TYR GLU GLY LEU GLU
HET GBQ A1201 37
HETNAM GBQ 5-[[(2~{R},3~{S})-2-[(1~{R})-1-[3,5-
HETNAM 2 GBQ BIS(TRIFLUOROMETHYL)PHENYL]ETHOXY]-3-(4-FLUOROPHENYL)
HETNAM 3 GBQ MORPHOLIN-4-YL]METHYL]-1,2-DIHYDRO-1,2,4-TRIAZOL-3-ONE
FORMUL 2 GBQ C23 H21 F7 N4 O3
HELIX 1 AA1 PRO A 28 LYS A 61 1 34
HELIX 2 AA2 VAL A 66 ASN A 96 1 31
HELIX 3 AA3 TYR A 100 HIS A 136 1 37
HELIX 4 AA4 SER A 143 TYR A 168 1 26
HELIX 5 AA5 LYS A 190 TYR A 205 1 16
HELIX 6 AA6 TYR A 205 ALA A 225 1 21
HELIX 7 AA7 ASN A 1001 GLU A 1010 1 10
HELIX 8 AA8 LEU A 1022 LEU A 1035 1 14
HELIX 9 AA9 LEU A 1040 LEU A 1047 1 8
HELIX 10 AB1 ASP A 1048 ALA A 1068 1 21
HELIX 11 AB2 PHE A 1070 GLN A 1079 1 10
HELIX 12 AB3 ARG A 1081 ALA A 1090 1 10
HELIX 13 AB4 SER A 1092 THR A 1098 1 7
HELIX 14 AB5 THR A 1098 GLY A 1112 1 15
HELIX 15 AB6 TRP A 1114 HIS A 237 5 5
HELIX 16 AB7 SER A 241 ASN A 274 1 34
HELIX 17 AB8 ASN A 274 LYS A 281 1 8
HELIX 18 AB9 PHE A 282 ASN A 309 1 28
HELIX 19 AC1 ASN A 309 ALA A 319 1 11
SHEET 1 AA1 2 SER A 169 THR A 173 0
SHEET 2 AA1 2 VAL A 178 ILE A 182 -1 O MET A 181 N THR A 170
SSBOND 1 CYS A 105 CYS A 180 1555 1555 2.04
SITE 1 AC1 16 ASN A 89 ASN A 109 PRO A 112 ILE A 113
SITE 2 AC1 16 VAL A 116 GLN A 165 ILE A 182 TRP A 184
SITE 3 AC1 16 GLU A 193 HIS A 197 VAL A 200 THR A 201
SITE 4 AC1 16 ILE A 204 TRP A 261 PHE A 264 HIS A 265
CRYST1 102.512 102.512 156.962 90.00 90.00 90.00 P 42 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 0.009755 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009755 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006371 0.00000
ATOM 1 N PHE A 25 -71.593 49.751 377.645 1.00165.50 N
ANISOU 1 N PHE A 25 21406 23646 17829 1023 -3522 990 N
ATOM 2 CA PHE A 25 -70.342 49.611 378.387 1.00168.60 C
ANISOU 2 CA PHE A 25 21658 24348 18053 1252 -3813 894 C
ATOM 3 C PHE A 25 -69.112 49.513 377.471 1.00174.72 C
ANISOU 3 C PHE A 25 21880 25707 18799 1541 -3925 758 C
ATOM 4 O PHE A 25 -68.002 49.825 377.912 1.00176.71 O
ANISOU 4 O PHE A 25 21823 26366 18951 1609 -4100 659 O
ATOM 5 CB PHE A 25 -70.410 48.415 379.348 1.00172.30 C
ANISOU 5 CB PHE A 25 22674 24481 18311 1574 -4069 872 C
ATOM 6 N VAL A 26 -69.311 49.089 376.200 1.00170.67 N
ANISOU 6 N VAL A 26 21229 25253 18363 1698 -3821 740 N
ATOM 7 CA VAL A 26 -68.248 48.951 375.191 1.00172.48 C
ANISOU 7 CA VAL A 26 20934 26032 18569 1963 -3892 600 C
ATOM 8 C VAL A 26 -67.813 50.362 374.724 1.00174.76 C
ANISOU 8 C VAL A 26 20694 26736 18969 1541 -3701 597 C
ATOM 9 O VAL A 26 -68.528 51.010 373.948 1.00171.43 O
ANISOU 9 O VAL A 26 20224 26199 18714 1217 -3427 693 O
ATOM 10 CB VAL A 26 -68.654 48.004 374.013 1.00175.78 C
ANISOU 10 CB VAL A 26 21424 26341 19025 2255 -3836 589 C
ATOM 11 CG1 VAL A 26 -67.526 47.856 372.993 1.00177.90 C
ANISOU 11 CG1 VAL A 26 21141 27201 19253 2541 -3914 426 C
ATOM 12 CG2 VAL A 26 -69.085 46.631 374.527 1.00176.46 C
ANISOU 12 CG2 VAL A 26 22104 25981 18963 2627 -4023 595 C
ATOM 13 N GLN A 27 -66.652 50.839 375.238 1.00172.88 N
ANISOU 13 N GLN A 27 20095 26974 18619 1536 -3856 480 N
ATOM 14 CA GLN A 27 -66.108 52.174 374.938 1.00171.94 C
ANISOU 14 CA GLN A 27 19505 27276 18547 1106 -3702 459 C
ATOM 15 C GLN A 27 -64.557 52.207 374.655 1.00177.34 C
ANISOU 15 C GLN A 27 19595 28706 19082 1290 -3873 234 C
ATOM 16 O GLN A 27 -63.872 53.079 375.205 1.00178.33 O
ANISOU 16 O GLN A 27 19463 29153 19141 1004 -3893 185 O
ATOM 17 CB GLN A 27 -66.501 53.171 376.058 1.00171.94 C
ANISOU 17 CB GLN A 27 19719 27035 18577 654 -3627 580 C
ATOM 18 CG GLN A 27 -66.163 52.706 377.483 1.00188.24 C
ANISOU 18 CG GLN A 27 22043 28988 20492 838 -3897 550 C
ATOM 19 CD GLN A 27 -66.569 53.711 378.527 1.00207.09 C
ANISOU 19 CD GLN A 27 24629 31146 22911 380 -3806 667 C
ATOM 20 OE1 GLN A 27 -67.754 53.889 378.828 1.00201.54 O
ANISOU 20 OE1 GLN A 27 24349 29919 22308 179 -3657 814 O
ATOM 21 NE2 GLN A 27 -65.589 54.373 379.126 1.00199.08 N
ANISOU 21 NE2 GLN A 27 23307 30536 21797 207 -3897 589 N
ATOM 22 N PRO A 28 -63.977 51.342 373.770 1.00173.64 N
ANISOU 22 N PRO A 28 18870 28556 18550 1732 -3982 80 N
ATOM 23 CA PRO A 28 -62.524 51.425 373.521 1.00176.38 C
ANISOU 23 CA PRO A 28 18610 29661 18744 1886 -4132 -165 C
ATOM 24 C PRO A 28 -62.138 52.489 372.491 1.00176.28 C
ANISOU 24 C PRO A 28 18089 30106 18785 1442 -3872 -208 C
ATOM 25 O PRO A 28 -62.900 52.750 371.556 1.00172.90 O
ANISOU 25 O PRO A 28 17741 29449 18503 1230 -3618 -86 O
ATOM 26 CB PRO A 28 -62.154 50.011 373.040 1.00180.46 C
ANISOU 26 CB PRO A 28 19119 30286 19163 2563 -4357 -316 C
ATOM 27 CG PRO A 28 -63.456 49.244 372.934 1.00182.15 C
ANISOU 27 CG PRO A 28 19957 29773 19479 2706 -4298 -129 C
ATOM 28 CD PRO A 28 -64.570 50.240 372.990 1.00173.88 C
ANISOU 28 CD PRO A 28 19136 28307 18622 2117 -3984 101 C
ATOM 29 N ALA A 29 -60.937 53.088 372.655 1.00173.11 N
ANISOU 29 N ALA A 29 17172 30359 18242 1296 -3941 -394 N
ATOM 30 CA ALA A 29 -60.395 54.123 371.766 1.00172.27 C
ANISOU 30 CA ALA A 29 16573 30758 18124 829 -3710 -468 C
ATOM 31 C ALA A 29 -60.195 53.625 370.326 1.00173.53 C
ANISOU 31 C ALA A 29 16431 31200 18302 1030 -3613 -576 C
ATOM 32 O ALA A 29 -60.336 54.410 369.386 1.00171.83 O
ANISOU 32 O ALA A 29 16049 31096 18142 603 -3342 -534 O
ATOM 33 CB ALA A 29 -59.089 54.662 372.323 1.00177.08 C
ANISOU 33 CB ALA A 29 16695 32048 18538 686 -3842 -684 C
ATOM 34 N TRP A 30 -59.901 52.314 370.161 1.00169.38 N
ANISOU 34 N TRP A 30 15884 30755 17717 1686 -3840 -711 N
ATOM 35 CA TRP A 30 -59.703 51.634 368.877 1.00168.64 C
ANISOU 35 CA TRP A 30 15541 30906 17628 1984 -3793 -828 C
ATOM 36 C TRP A 30 -60.962 51.678 368.013 1.00165.68 C
ANISOU 36 C TRP A 30 15533 29959 17457 1811 -3528 -592 C
ATOM 37 O TRP A 30 -60.867 51.585 366.790 1.00164.95 O
ANISOU 37 O TRP A 30 15199 30081 17392 1824 -3385 -651 O
ATOM 38 CB TRP A 30 -59.285 50.176 369.109 1.00169.92 C
ANISOU 38 CB TRP A 30 15744 31147 17670 2764 -4133 -997 C
ATOM 39 N GLN A 31 -62.137 51.823 368.658 1.00157.18 N
ANISOU 39 N GLN A 31 15027 28180 16513 1650 -3466 -343 N
ATOM 40 CA GLN A 31 -63.452 51.893 368.019 1.00151.94 C
ANISOU 40 CA GLN A 31 14750 26939 16042 1481 -3232 -122 C
ATOM 41 C GLN A 31 -63.890 53.330 367.712 1.00151.38 C
ANISOU 41 C GLN A 31 14662 26789 16067 813 -2938 14 C
ATOM 42 O GLN A 31 -64.455 53.560 366.645 1.00148.89 O
ANISOU 42 O GLN A 31 14371 26342 15858 652 -2722 92 O
ATOM 43 CB GLN A 31 -64.515 51.184 368.880 1.00151.03 C
ANISOU 43 CB GLN A 31 15264 26128 15992 1697 -3330 40 C
ATOM 44 CG GLN A 31 -64.440 49.654 368.842 1.00167.35 C
ANISOU 44 CG GLN A 31 17512 28095 17979 2351 -3566 -46 C
ATOM 45 CD GLN A 31 -65.400 48.972 369.795 1.00184.15 C
ANISOU 45 CD GLN A 31 20289 29560 20121 2509 -3670 97 C
ATOM 46 OE1 GLN A 31 -66.477 49.483 370.133 1.00176.06 O
ANISOU 46 OE1 GLN A 31 19618 28048 19227 2157 -3491 286 O
ATOM 47 NE2 GLN A 31 -65.032 47.782 370.243 1.00178.96 N
ANISOU 47 NE2 GLN A 31 19818 28870 19307 3049 -3964 -7 N
ATOM 48 N ILE A 32 -63.651 54.284 368.644 1.00147.02 N
ANISOU 48 N ILE A 32 14101 26297 15464 438 -2941 43 N
ATOM 49 CA ILE A 32 -64.040 55.702 368.519 1.00144.40 C
ANISOU 49 CA ILE A 32 13821 25859 15186 -196 -2694 170 C
ATOM 50 C ILE A 32 -63.378 56.373 367.304 1.00148.24 C
ANISOU 50 C ILE A 32 13867 26851 15605 -500 -2515 64 C
ATOM 51 O ILE A 32 -64.058 57.087 366.563 1.00145.11 O
ANISOU 51 O ILE A 32 13618 26220 15296 -840 -2281 189 O
ATOM 52 CB ILE A 32 -63.816 56.500 369.842 1.00148.17 C
ANISOU 52 CB ILE A 32 14394 26311 15594 -499 -2765 207 C
ATOM 53 CG1 ILE A 32 -64.514 55.809 371.043 1.00147.12 C
ANISOU 53 CG1 ILE A 32 14733 25652 15514 -216 -2932 312 C
ATOM 54 CG2 ILE A 32 -64.286 57.964 369.706 1.00147.13 C
ANISOU 54 CG2 ILE A 32 14388 26014 15500 -1138 -2517 344 C
ATOM 55 CD1 ILE A 32 -63.875 56.067 372.420 1.00155.39 C
ANISOU 55 CD1 ILE A 32 15766 26842 16435 -261 -3127 259 C
ATOM 56 N VAL A 33 -62.069 56.127 367.097 1.00148.42 N
ANISOU 56 N VAL A 33 13363 27570 15460 -367 -2628 -179 N
ATOM 57 CA VAL A 33 -61.298 56.668 365.968 1.00150.14 C
ANISOU 57 CA VAL A 33 13114 28360 15573 -653 -2466 -326 C
ATOM 58 C VAL A 33 -61.834 56.067 364.662 1.00152.12 C
ANISOU 58 C VAL A 33 13403 28464 15931 -439 -2343 -295 C
ATOM 59 O VAL A 33 -62.039 56.796 363.690 1.00151.18 O
ANISOU 59 O VAL A 33 13239 28381 15821 -827 -2107 -253 O
ATOM 60 CB VAL A 33 -59.769 56.457 366.140 1.00158.85 C
ANISOU 60 CB VAL A 33 13611 30288 16456 -519 -2634 -633 C
ATOM 61 CG1 VAL A 33 -58.992 57.019 364.951 1.00161.16 C
ANISOU 61 CG1 VAL A 33 13415 31198 16621 -858 -2442 -804 C
ATOM 62 CG2 VAL A 33 -59.270 57.081 367.440 1.00160.16 C
ANISOU 62 CG2 VAL A 33 13749 30591 16513 -757 -2753 -660 C
ATOM 63 N LEU A 34 -62.116 54.749 364.676 1.00147.66 N
ANISOU 63 N LEU A 34 12979 27688 15436 166 -2509 -306 N
ATOM 64 CA LEU A 34 -62.672 53.987 363.557 1.00145.66 C
ANISOU 64 CA LEU A 34 12812 27246 15286 449 -2430 -273 C
ATOM 65 C LEU A 34 -64.062 54.528 363.140 1.00143.88 C
ANISOU 65 C LEU A 34 13044 26378 15245 141 -2201 -16 C
ATOM 66 O LEU A 34 -64.382 54.533 361.949 1.00142.32 O
ANISOU 66 O LEU A 34 12812 26160 15104 74 -2031 7 O
ATOM 67 CB LEU A 34 -62.749 52.502 363.945 1.00146.29 C
ANISOU 67 CB LEU A 34 13054 27157 15372 1138 -2687 -322 C
ATOM 68 CG LEU A 34 -62.623 51.504 362.803 1.00151.96 C
ANISOU 68 CG LEU A 34 13651 27985 16100 1556 -2690 -413 C
ATOM 69 CD1 LEU A 34 -61.649 50.399 363.155 1.00155.61 C
ANISOU 69 CD1 LEU A 34 13860 28860 16404 2162 -2989 -653 C
ATOM 70 CD2 LEU A 34 -63.989 50.938 362.412 1.00151.75 C
ANISOU 70 CD2 LEU A 34 14159 27248 16252 1696 -2613 -199 C
ATOM 71 N TRP A 35 -64.862 55.004 364.120 1.00137.08 N
ANISOU 71 N TRP A 35 12599 25018 14467 -40 -2201 160 N
ATOM 72 CA TRP A 35 -66.183 55.600 363.894 1.00132.43 C
ANISOU 72 CA TRP A 35 12437 23841 14038 -322 -2008 378 C
ATOM 73 C TRP A 35 -66.054 57.045 363.393 1.00135.35 C
ANISOU 73 C TRP A 35 12715 24351 14360 -919 -1795 411 C
ATOM 74 O TRP A 35 -66.784 57.431 362.483 1.00132.95 O
ANISOU 74 O TRP A 35 12575 23799 14141 -1089 -1614 508 O
ATOM 75 CB TRP A 35 -67.041 55.576 365.172 1.00128.89 C
ANISOU 75 CB TRP A 35 12439 22865 13670 -307 -2087 520 C
ATOM 76 CG TRP A 35 -67.799 54.306 365.430 1.00128.18 C
ANISOU 76 CG TRP A 35 12670 22367 13666 159 -2201 568 C
ATOM 77 CD1 TRP A 35 -67.716 53.520 366.542 1.00131.78 C
ANISOU 77 CD1 TRP A 35 13300 22698 14071 471 -2420 546 C
ATOM 78 CD2 TRP A 35 -68.830 53.734 364.611 1.00125.45 C
ANISOU 78 CD2 TRP A 35 12566 21647 13454 318 -2096 653 C
ATOM 79 NE1 TRP A 35 -68.609 52.477 366.454 1.00129.37 N
ANISOU 79 NE1 TRP A 35 13346 21966 13844 798 -2452 609 N
ATOM 80 CE2 TRP A 35 -69.304 52.581 365.278 1.00128.71 C
ANISOU 80 CE2 TRP A 35 13291 21736 13878 710 -2253 672 C
ATOM 81 CE3 TRP A 35 -69.402 54.084 363.373 1.00125.02 C
ANISOU 81 CE3 TRP A 35 12510 21496 13495 161 -1890 709 C
ATOM 82 CZ2 TRP A 35 -70.313 51.769 364.746 1.00125.93 C
ANISOU 82 CZ2 TRP A 35 13229 20992 13625 922 -2199 739 C
ATOM 83 CZ3 TRP A 35 -70.399 53.275 362.844 1.00124.31 C
ANISOU 83 CZ3 TRP A 35 12684 21029 13519 403 -1847 774 C
ATOM 84 CH2 TRP A 35 -70.842 52.131 363.526 1.00124.51 C
ANISOU 84 CH2 TRP A 35 12998 20760 13550 768 -1994 786 C
ATOM 85 N ALA A 36 -65.135 57.846 363.994 1.00133.45 N
ANISOU 85 N ALA A 36 12239 24500 13965 -1242 -1824 327 N
ATOM 86 CA ALA A 36 -64.888 59.248 363.627 1.00133.36 C
ANISOU 86 CA ALA A 36 12171 24648 13852 -1854 -1638 345 C
ATOM 87 C ALA A 36 -64.472 59.371 362.167 1.00137.57 C
ANISOU 87 C ALA A 36 12432 25518 14319 -1982 -1479 254 C
ATOM 88 O ALA A 36 -64.873 60.320 361.491 1.00136.16 O
ANISOU 88 O ALA A 36 12435 25171 14128 -2396 -1286 346 O
ATOM 89 CB ALA A 36 -63.830 59.853 364.532 1.00137.07 C
ANISOU 89 CB ALA A 36 12381 25562 14139 -2118 -1724 230 C
ATOM 90 N ALA A 37 -63.700 58.378 361.679 1.00135.48 N
ANISOU 90 N ALA A 37 11764 25709 14005 -1602 -1569 70 N
ATOM 91 CA ALA A 37 -63.243 58.273 360.296 1.00136.00 C
ANISOU 91 CA ALA A 37 11527 26142 14004 -1644 -1436 -46 C
ATOM 92 C ALA A 37 -64.429 57.916 359.399 1.00134.66 C
ANISOU 92 C ALA A 37 11704 25442 14018 -1484 -1326 113 C
ATOM 93 O ALA A 37 -64.572 58.503 358.328 1.00134.04 O
ANISOU 93 O ALA A 37 11642 25377 13910 -1791 -1133 138 O
ATOM 94 CB ALA A 37 -62.155 57.216 360.184 1.00139.99 C
ANISOU 94 CB ALA A 37 11530 27247 14412 -1198 -1599 -297 C
ATOM 95 N ALA A 38 -65.302 56.988 359.858 1.00127.53 N
ANISOU 95 N ALA A 38 11104 24065 13288 -1034 -1446 219 N
ATOM 96 CA ALA A 38 -66.508 56.568 359.136 1.00123.66 C
ANISOU 96 CA ALA A 38 10954 23058 12975 -858 -1359 362 C
ATOM 97 C ALA A 38 -67.472 57.749 358.965 1.00125.33 C
ANISOU 97 C ALA A 38 11549 22820 13252 -1304 -1184 541 C
ATOM 98 O ALA A 38 -68.080 57.893 357.906 1.00123.18 O
ANISOU 98 O ALA A 38 11416 22342 13046 -1361 -1045 606 O
ATOM 99 CB ALA A 38 -67.193 55.421 359.868 1.00122.40 C
ANISOU 99 CB ALA A 38 11054 22511 12940 -359 -1528 421 C
ATOM 100 N TYR A 39 -67.560 58.619 359.988 1.00122.38 N
ANISOU 100 N TYR A 39 11344 22310 12843 -1609 -1201 609 N
ATOM 101 CA TYR A 39 -68.412 59.807 359.987 1.00120.15 C
ANISOU 101 CA TYR A 39 11446 21611 12593 -2014 -1067 761 C
ATOM 102 C TYR A 39 -67.864 60.944 359.115 1.00126.15 C
ANISOU 102 C TYR A 39 12113 22632 13186 -2523 -901 728 C
ATOM 103 O TYR A 39 -68.660 61.594 358.442 1.00124.10 O
ANISOU 103 O TYR A 39 12167 22024 12960 -2725 -772 835 O
ATOM 104 CB TYR A 39 -68.715 60.279 361.421 1.00120.06 C
ANISOU 104 CB TYR A 39 11676 21345 12597 -2129 -1154 840 C
ATOM 105 CG TYR A 39 -69.915 59.585 362.027 1.00117.73 C
ANISOU 105 CG TYR A 39 11725 20517 12490 -1794 -1223 946 C
ATOM 106 CD1 TYR A 39 -71.184 60.152 361.954 1.00116.83 C
ANISOU 106 CD1 TYR A 39 12019 19884 12487 -1919 -1125 1079 C
ATOM 107 CD2 TYR A 39 -69.791 58.335 362.630 1.00118.21 C
ANISOU 107 CD2 TYR A 39 11718 20601 12597 -1350 -1388 897 C
ATOM 108 CE1 TYR A 39 -72.298 59.504 362.487 1.00114.76 C
ANISOU 108 CE1 TYR A 39 12044 19178 12380 -1644 -1171 1149 C
ATOM 109 CE2 TYR A 39 -70.897 57.679 363.168 1.00116.40 C
ANISOU 109 CE2 TYR A 39 11830 19887 12509 -1094 -1435 985 C
ATOM 110 CZ TYR A 39 -72.149 58.268 363.095 1.00120.13 C
ANISOU 110 CZ TYR A 39 12663 19888 13094 -1259 -1316 1105 C
ATOM 111 OH TYR A 39 -73.241 57.626 363.620 1.00117.57 O
ANISOU 111 OH TYR A 39 12647 19132 12891 -1042 -1346 1165 O
ATOM 112 N THR A 40 -66.529 61.182 359.108 1.00126.77 N
ANISOU 112 N THR A 40 11778 23323 13066 -2735 -905 569 N
ATOM 113 CA THR A 40 -65.918 62.233 358.267 1.00129.19 C
ANISOU 113 CA THR A 40 11991 23929 13168 -3273 -734 514 C
ATOM 114 C THR A 40 -66.073 61.900 356.791 1.00132.89 C
ANISOU 114 C THR A 40 12397 24441 13654 -3194 -610 488 C
ATOM 115 O THR A 40 -66.271 62.808 355.981 1.00132.87 O
ANISOU 115 O THR A 40 12590 24345 13549 -3601 -451 534 O
ATOM 116 CB THR A 40 -64.453 62.521 358.627 1.00141.68 C
ANISOU 116 CB THR A 40 13112 26203 14516 -3539 -761 320 C
ATOM 117 OG1 THR A 40 -63.727 61.295 358.705 1.00143.50 O
ANISOU 117 OG1 THR A 40 12888 26868 14768 -3061 -903 149 O
ATOM 118 CG2 THR A 40 -64.308 63.322 359.914 1.00140.73 C
ANISOU 118 CG2 THR A 40 13135 26015 14321 -3831 -827 367 C
ATOM 119 N VAL A 41 -66.028 60.590 356.455 1.00128.62 N
ANISOU 119 N VAL A 41 11630 24008 13233 -2663 -692 418 N
ATOM 120 CA VAL A 41 -66.224 60.060 355.104 1.00127.71 C
ANISOU 120 CA VAL A 41 11451 23913 13161 -2495 -597 394 C
ATOM 121 C VAL A 41 -67.539 60.621 354.553 1.00128.50 C
ANISOU 121 C VAL A 41 12065 23386 13374 -2623 -486 587 C
ATOM 122 O VAL A 41 -67.560 61.105 353.419 1.00129.20 O
ANISOU 122 O VAL A 41 12211 23498 13380 -2877 -337 588 O
ATOM 123 CB VAL A 41 -66.163 58.505 355.103 1.00131.05 C
ANISOU 123 CB VAL A 41 11654 24430 13709 -1847 -742 316 C
ATOM 124 CG1 VAL A 41 -66.938 57.892 353.935 1.00128.51 C
ANISOU 124 CG1 VAL A 41 11473 23840 13514 -1600 -663 374 C
ATOM 125 CG2 VAL A 41 -64.715 58.019 355.109 1.00134.87 C
ANISOU 125 CG2 VAL A 41 11563 25653 14027 -1734 -818 69 C
ATOM 126 N ILE A 42 -68.600 60.635 355.398 1.00121.62 N
ANISOU 126 N ILE A 42 11570 21975 12666 -2476 -562 734 N
ATOM 127 CA ILE A 42 -69.926 61.178 355.078 1.00118.11 C
ANISOU 127 CA ILE A 42 11611 20932 12332 -2549 -490 895 C
ATOM 128 C ILE A 42 -69.846 62.690 354.786 1.00122.40 C
ANISOU 128 C ILE A 42 12397 21413 12697 -3123 -368 941 C
ATOM 129 O ILE A 42 -70.274 63.110 353.712 1.00121.86 O
ANISOU 129 O ILE A 42 12534 21166 12600 -3257 -258 983 O
ATOM 130 CB ILE A 42 -70.995 60.836 356.165 1.00117.94 C
ANISOU 130 CB ILE A 42 11884 20427 12499 -2275 -600 1002 C
ATOM 131 CG1 ILE A 42 -71.307 59.324 356.208 1.00116.61 C
ANISOU 131 CG1 ILE A 42 11606 20209 12492 -1725 -697 976 C
ATOM 132 CG2 ILE A 42 -72.277 61.668 355.972 1.00116.35 C
ANISOU 132 CG2 ILE A 42 12164 19675 12370 -2422 -530 1134 C
ATOM 133 CD1 ILE A 42 -72.219 58.900 357.385 1.00120.13 C
ANISOU 133 CD1 ILE A 42 12305 20258 13080 -1489 -807 1051 C
ATOM 134 N VAL A 43 -69.290 63.488 355.722 1.00119.34 N
ANISOU 134 N VAL A 43 12011 21160 12171 -3460 -394 930 N
ATOM 135 CA VAL A 43 -69.191 64.945 355.580 1.00120.14 C
ANISOU 135 CA VAL A 43 12401 21178 12069 -4028 -293 974 C
ATOM 136 C VAL A 43 -68.435 65.362 354.318 1.00127.82 C
ANISOU 136 C VAL A 43 13240 22496 12829 -4377 -143 888 C
ATOM 137 O VAL A 43 -68.857 66.307 353.651 1.00128.41 O
ANISOU 137 O VAL A 43 13705 22287 12797 -4685 -46 962 O
ATOM 138 CB VAL A 43 -68.637 65.690 356.823 1.00124.81 C
ANISOU 138 CB VAL A 43 13001 21893 12528 -4349 -347 967 C
ATOM 139 CG1 VAL A 43 -69.332 67.034 356.999 1.00123.85 C
ANISOU 139 CG1 VAL A 43 13431 21316 12309 -4731 -297 1091 C
ATOM 140 CG2 VAL A 43 -68.756 64.858 358.089 1.00123.21 C
ANISOU 140 CG2 VAL A 43 12671 21646 12496 -3961 -509 971 C
ATOM 141 N VAL A 44 -67.331 64.663 353.986 1.00125.75 N
ANISOU 141 N VAL A 44 12446 22842 12490 -4319 -131 721 N
ATOM 142 CA VAL A 44 -66.528 64.990 352.811 1.00127.52 C
ANISOU 142 CA VAL A 44 12481 23475 12494 -4665 23 607 C
ATOM 143 C VAL A 44 -67.258 64.582 351.515 1.00129.21 C
ANISOU 143 C VAL A 44 12856 23425 12814 -4449 97 660 C
ATOM 144 O VAL A 44 -67.570 65.468 350.721 1.00129.30 O
ANISOU 144 O VAL A 44 13221 23217 12690 -4808 215 720 O
ATOM 145 CB VAL A 44 -65.073 64.460 352.897 1.00134.07 C
ANISOU 145 CB VAL A 44 12659 25093 13188 -4680 13 376 C
ATOM 146 CG1 VAL A 44 -64.258 64.876 351.674 1.00136.78 C
ANISOU 146 CG1 VAL A 44 12805 25881 13284 -5086 196 239 C
ATOM 147 CG2 VAL A 44 -64.396 64.948 354.170 1.00135.67 C
ANISOU 147 CG2 VAL A 44 12733 25549 13266 -4938 -60 322 C
ATOM 148 N THR A 45 -67.572 63.276 351.325 1.00123.38 N
ANISOU 148 N THR A 45 11908 22672 12300 -3871 20 642 N
ATOM 149 CA THR A 45 -68.241 62.781 350.106 1.00121.75 C
ANISOU 149 CA THR A 45 11818 22242 12199 -3636 83 682 C
ATOM 150 C THR A 45 -69.598 63.466 349.824 1.00122.62 C
ANISOU 150 C THR A 45 12528 21670 12391 -3691 107 862 C
ATOM 151 O THR A 45 -69.962 63.608 348.655 1.00122.34 O
ANISOU 151 O THR A 45 12669 21492 12324 -3751 201 887 O
ATOM 152 CB THR A 45 -68.370 61.251 350.091 1.00130.41 C
ANISOU 152 CB THR A 45 12628 23414 13509 -3007 -19 635 C
ATOM 153 OG1 THR A 45 -69.113 60.841 351.231 1.00133.90 O
ANISOU 153 OG1 THR A 45 13228 23505 14142 -2685 -166 727 O
ATOM 154 CG2 THR A 45 -67.023 60.539 350.061 1.00130.31 C
ANISOU 154 CG2 THR A 45 12024 24102 13387 -2902 -41 425 C
ATOM 155 N SER A 46 -70.322 63.914 350.876 1.00116.68 N
ANISOU 155 N SER A 46 12088 20516 11728 -3670 18 972 N
ATOM 156 CA SER A 46 -71.603 64.610 350.714 1.00113.93 C
ANISOU 156 CA SER A 46 12292 19552 11444 -3692 18 1112 C
ATOM 157 C SER A 46 -71.424 66.070 350.292 1.00120.26 C
ANISOU 157 C SER A 46 13460 20255 11977 -4257 112 1143 C
ATOM 158 O SER A 46 -72.185 66.545 349.449 1.00119.09 O
ANISOU 158 O SER A 46 13697 19747 11806 -4297 152 1208 O
ATOM 159 CB SER A 46 -72.456 64.522 351.975 1.00113.72 C
ANISOU 159 CB SER A 46 12452 19160 11596 -3455 -106 1192 C
ATOM 160 OG SER A 46 -73.542 65.434 351.929 1.00117.68 O
ANISOU 160 OG SER A 46 13476 19139 12099 -3557 -109 1294 O
ATOM 161 N VAL A 47 -70.454 66.789 350.892 1.00119.61 N
ANISOU 161 N VAL A 47 13295 20472 11678 -4694 137 1095 N
ATOM 162 CA VAL A 47 -70.214 68.192 350.549 1.00121.77 C
ANISOU 162 CA VAL A 47 13960 20656 11652 -5283 226 1121 C
ATOM 163 C VAL A 47 -69.576 68.268 349.164 1.00129.43 C
ANISOU 163 C VAL A 47 14837 21917 12422 -5561 375 1040 C
ATOM 164 O VAL A 47 -70.130 68.927 348.285 1.00128.92 O
ANISOU 164 O VAL A 47 15234 21506 12245 -5734 429 1106 O
ATOM 165 CB VAL A 47 -69.453 68.986 351.652 1.00127.26 C
ANISOU 165 CB VAL A 47 14640 21551 12162 -5698 210 1097 C
ATOM 166 CG1 VAL A 47 -68.974 70.343 351.142 1.00130.30 C
ANISOU 166 CG1 VAL A 47 15388 21945 12175 -6375 327 1094 C
ATOM 167 CG2 VAL A 47 -70.330 69.173 352.887 1.00124.34 C
ANISOU 167 CG2 VAL A 47 14539 20743 11960 -5477 75 1204 C
ATOM 168 N VAL A 48 -68.464 67.529 348.957 1.00129.24 N
ANISOU 168 N VAL A 48 14224 22524 12359 -5557 430 887 N
ATOM 169 CA VAL A 48 -67.727 67.460 347.689 1.00131.91 C
ANISOU 169 CA VAL A 48 14372 23243 12506 -5808 583 775 C
ATOM 170 C VAL A 48 -68.672 67.096 346.536 1.00134.26 C
ANISOU 170 C VAL A 48 14919 23158 12935 -5512 605 851 C
ATOM 171 O VAL A 48 -68.778 67.866 345.588 1.00135.47 O
ANISOU 171 O VAL A 48 15443 23145 12885 -5863 707 878 O
ATOM 172 CB VAL A 48 -66.481 66.524 347.775 1.00137.89 C
ANISOU 172 CB VAL A 48 14388 24764 13240 -5721 607 570 C
ATOM 173 CG1 VAL A 48 -65.872 66.255 346.397 1.00139.79 C
ANISOU 173 CG1 VAL A 48 14399 25384 13330 -5873 763 442 C
ATOM 174 CG2 VAL A 48 -65.431 67.085 348.731 1.00140.52 C
ANISOU 174 CG2 VAL A 48 14495 25532 13364 -6138 609 467 C
ATOM 175 N GLY A 49 -69.386 65.979 346.676 1.00127.66 N
ANISOU 175 N GLY A 49 13929 22155 12421 -4892 502 888 N
ATOM 176 CA GLY A 49 -70.315 65.460 345.677 1.00125.01 C
ANISOU 176 CA GLY A 49 13771 21484 12244 -4547 506 950 C
ATOM 177 C GLY A 49 -71.491 66.347 345.322 1.00126.89 C
ANISOU 177 C GLY A 49 14668 21079 12467 -4621 485 1090 C
ATOM 178 O GLY A 49 -71.739 66.578 344.140 1.00126.57 O
ANISOU 178 O GLY A 49 14864 20901 12325 -4731 562 1103 O
ATOM 179 N ASN A 50 -72.232 66.840 346.332 1.00122.24 N
ANISOU 179 N ASN A 50 14383 20094 11967 -4542 373 1184 N
ATOM 180 CA ASN A 50 -73.426 67.664 346.105 1.00120.89 C
ANISOU 180 CA ASN A 50 14834 19308 11790 -4534 320 1295 C
ATOM 181 C ASN A 50 -73.126 69.103 345.667 1.00128.54 C
ANISOU 181 C ASN A 50 16289 20146 12404 -5115 388 1317 C
ATOM 182 O ASN A 50 -73.974 69.694 344.990 1.00128.47 O
ANISOU 182 O ASN A 50 16789 19689 12336 -5103 363 1380 O
ATOM 183 CB ASN A 50 -74.377 67.643 347.299 1.00117.95 C
ANISOU 183 CB ASN A 50 14610 18580 11625 -4233 181 1362 C
ATOM 184 CG ASN A 50 -75.140 66.341 347.451 1.00124.38 C
ANISOU 184 CG ASN A 50 15167 19319 12772 -3643 110 1362 C
ATOM 185 OD1 ASN A 50 -76.031 66.004 346.654 1.00113.85 O
ANISOU 185 OD1 ASN A 50 13979 17720 11558 -3361 98 1383 O
ATOM 186 ND2 ASN A 50 -74.820 65.586 348.493 1.00108.28 N
ANISOU 186 ND2 ASN A 50 12769 17501 10873 -3455 56 1333 N
ATOM 187 N VAL A 51 -71.942 69.664 346.019 1.00127.65 N
ANISOU 187 N VAL A 51 16047 20418 12036 -5624 467 1258 N
ATOM 188 CA VAL A 51 -71.568 71.016 345.567 1.00130.44 C
ANISOU 188 CA VAL A 51 16890 20670 12003 -6245 548 1271 C
ATOM 189 C VAL A 51 -71.294 70.950 344.049 1.00136.37 C
ANISOU 189 C VAL A 51 17684 21536 12593 -6418 677 1224 C
ATOM 190 O VAL A 51 -71.713 71.843 343.309 1.00137.44 O
ANISOU 190 O VAL A 51 18419 21290 12511 -6662 691 1281 O
ATOM 191 CB VAL A 51 -70.413 71.662 346.394 1.00136.93 C
ANISOU 191 CB VAL A 51 17577 21876 12575 -6784 604 1210 C
ATOM 192 CG1 VAL A 51 -69.793 72.860 345.678 1.00140.58 C
ANISOU 192 CG1 VAL A 51 18459 22366 12590 -7496 734 1188 C
ATOM 193 CG2 VAL A 51 -70.899 72.078 347.776 1.00135.21 C
ANISOU 193 CG2 VAL A 51 17555 21365 12453 -6683 469 1288 C
ATOM 194 N VAL A 52 -70.662 69.846 343.596 1.00132.89 N
ANISOU 194 N VAL A 52 16634 21591 12266 -6243 755 1120 N
ATOM 195 CA VAL A 52 -70.361 69.556 342.192 1.00133.99 C
ANISOU 195 CA VAL A 52 16704 21910 12297 -6339 883 1058 C
ATOM 196 C VAL A 52 -71.681 69.365 341.406 1.00135.12 C
ANISOU 196 C VAL A 52 17241 21488 12612 -5923 805 1162 C
ATOM 197 O VAL A 52 -71.829 69.950 340.333 1.00136.31 O
ANISOU 197 O VAL A 52 17809 21434 12549 -6173 869 1181 O
ATOM 198 CB VAL A 52 -69.389 68.345 342.062 1.00138.59 C
ANISOU 198 CB VAL A 52 16500 23177 12979 -6176 960 904 C
ATOM 199 CG1 VAL A 52 -69.318 67.821 340.627 1.00139.09 C
ANISOU 199 CG1 VAL A 52 16473 23360 13014 -6113 1069 851 C
ATOM 200 CG2 VAL A 52 -67.995 68.702 342.566 1.00141.99 C
ANISOU 200 CG2 VAL A 52 16580 24221 13150 -6692 1060 763 C
ATOM 201 N VAL A 53 -72.636 68.575 341.959 1.00127.48 N
ANISOU 201 N VAL A 53 16163 20268 12005 -5314 666 1220 N
ATOM 202 CA VAL A 53 -73.957 68.318 341.365 1.00124.29 C
ANISOU 202 CA VAL A 53 16073 19361 11791 -4877 577 1297 C
ATOM 203 C VAL A 53 -74.715 69.648 341.176 1.00129.29 C
ANISOU 203 C VAL A 53 17470 19430 12225 -5088 509 1383 C
ATOM 204 O VAL A 53 -75.234 69.889 340.088 1.00129.30 O
ANISOU 204 O VAL A 53 17835 19143 12149 -5054 507 1408 O
ATOM 205 CB VAL A 53 -74.764 67.237 342.152 1.00124.31 C
ANISOU 205 CB VAL A 53 15786 19261 12187 -4254 454 1320 C
ATOM 206 CG1 VAL A 53 -76.245 67.229 341.775 1.00121.39 C
ANISOU 206 CG1 VAL A 53 15804 18337 11982 -3862 344 1388 C
ATOM 207 CG2 VAL A 53 -74.167 65.852 341.944 1.00123.55 C
ANISOU 207 CG2 VAL A 53 15058 19628 12258 -3979 507 1238 C
ATOM 208 N MET A 54 -74.716 70.530 342.205 1.00126.93 N
ANISOU 208 N MET A 54 17430 18981 11817 -5312 446 1419 N
ATOM 209 CA MET A 54 -75.346 71.858 342.141 1.00128.10 C
ANISOU 209 CA MET A 54 18335 18600 11736 -5520 365 1488 C
ATOM 210 C MET A 54 -74.693 72.690 341.039 1.00136.77 C
ANISOU 210 C MET A 54 19821 19716 12429 -6080 482 1475 C
ATOM 211 O MET A 54 -75.396 73.370 340.291 1.00137.03 O
ANISOU 211 O MET A 54 20475 19282 12310 -6086 416 1521 O
ATOM 212 CB MET A 54 -75.235 72.600 343.484 1.00130.89 C
ANISOU 212 CB MET A 54 18832 18877 12023 -5707 297 1517 C
ATOM 213 CG MET A 54 -76.274 72.188 344.497 1.00131.08 C
ANISOU 213 CG MET A 54 18785 18644 12377 -5175 146 1549 C
ATOM 214 SD MET A 54 -76.078 73.063 346.069 1.00135.83 S
ANISOU 214 SD MET A 54 19553 19169 12888 -5413 76 1580 S
ATOM 215 CE MET A 54 -77.168 74.442 345.807 1.00133.36 C
ANISOU 215 CE MET A 54 20161 18157 12354 -5442 -61 1638 C
ATOM 216 N TRP A 55 -73.349 72.598 340.922 1.00136.76 N
ANISOU 216 N TRP A 55 19446 20274 12244 -6540 652 1395 N
ATOM 217 CA TRP A 55 -72.548 73.297 339.916 1.00140.82 C
ANISOU 217 CA TRP A 55 20239 20920 12348 -7155 804 1353 C
ATOM 218 C TRP A 55 -72.903 72.832 338.494 1.00142.86 C
ANISOU 218 C TRP A 55 20562 21089 12628 -6977 849 1345 C
ATOM 219 O TRP A 55 -73.166 73.677 337.643 1.00144.30 O
ANISOU 219 O TRP A 55 21379 20931 12516 -7261 859 1379 O
ATOM 220 CB TRP A 55 -71.043 73.139 340.211 1.00142.93 C
ANISOU 220 CB TRP A 55 19960 21897 12448 -7640 977 1232 C
ATOM 221 CG TRP A 55 -70.153 73.886 339.262 1.00148.73 C
ANISOU 221 CG TRP A 55 20946 22836 12730 -8350 1159 1163 C
ATOM 222 CD1 TRP A 55 -69.656 75.147 339.424 1.00155.36 C
ANISOU 222 CD1 TRP A 55 22296 23591 13141 -9029 1216 1167 C
ATOM 223 CD2 TRP A 55 -69.653 73.415 338.001 1.00150.17 C
ANISOU 223 CD2 TRP A 55 20891 23348 12818 -8479 1318 1070 C
ATOM 224 NE1 TRP A 55 -68.878 75.492 338.343 1.00158.64 N
ANISOU 224 NE1 TRP A 55 22817 24267 13191 -9599 1407 1079 N
ATOM 225 CE2 TRP A 55 -68.864 74.450 337.451 1.00158.83 C
ANISOU 225 CE2 TRP A 55 22379 24554 13417 -9270 1475 1017 C
ATOM 226 CE3 TRP A 55 -69.786 72.211 337.286 1.00149.49 C
ANISOU 226 CE3 TRP A 55 20317 23476 13007 -8015 1347 1023 C
ATOM 227 CZ2 TRP A 55 -68.219 74.323 336.213 1.00160.83 C
ANISOU 227 CZ2 TRP A 55 22530 25135 13444 -9614 1665 911 C
ATOM 228 CZ3 TRP A 55 -69.160 72.091 336.054 1.00153.54 C
ANISOU 228 CZ3 TRP A 55 20731 24299 13307 -8325 1525 925 C
ATOM 229 CH2 TRP A 55 -68.384 73.135 335.532 1.00158.76 C
ANISOU 229 CH2 TRP A 55 21765 25079 13476 -9119 1686 866 C
ATOM 230 N ILE A 56 -72.921 71.498 338.248 1.00136.06 N
ANISOU 230 N ILE A 56 19087 20512 12099 -6507 869 1300 N
ATOM 231 CA ILE A 56 -73.251 70.877 336.955 1.00134.66 C
ANISOU 231 CA ILE A 56 18887 20287 11989 -6277 911 1288 C
ATOM 232 C ILE A 56 -74.567 71.425 336.386 1.00138.32 C
ANISOU 232 C ILE A 56 20055 20055 12446 -6034 763 1386 C
ATOM 233 O ILE A 56 -74.603 71.842 335.230 1.00139.51 O
ANISOU 233 O ILE A 56 20606 20037 12366 -6246 812 1390 O
ATOM 234 CB ILE A 56 -73.244 69.314 337.042 1.00134.28 C
ANISOU 234 CB ILE A 56 18097 20590 12332 -5728 915 1235 C
ATOM 235 CG1 ILE A 56 -71.809 68.777 337.230 1.00136.70 C
ANISOU 235 CG1 ILE A 56 17734 21638 12568 -5989 1072 1099 C
ATOM 236 CG2 ILE A 56 -73.926 68.655 335.818 1.00132.34 C
ANISOU 236 CG2 ILE A 56 17910 20153 12219 -5366 909 1251 C
ATOM 237 CD1 ILE A 56 -71.714 67.339 337.692 1.00140.01 C
ANISOU 237 CD1 ILE A 56 17460 22393 13343 -5450 1033 1045 C
ATOM 238 N ILE A 57 -75.622 71.458 337.215 1.00132.87 N
ANISOU 238 N ILE A 57 19519 18978 11986 -5603 580 1450 N
ATOM 239 CA ILE A 57 -76.955 71.902 336.815 1.00131.66 C
ANISOU 239 CA ILE A 57 19961 18203 11862 -5276 410 1511 C
ATOM 240 C ILE A 57 -77.049 73.438 336.640 1.00140.75 C
ANISOU 240 C ILE A 57 21956 18923 12601 -5699 349 1555 C
ATOM 241 O ILE A 57 -77.409 73.894 335.550 1.00141.50 O
ANISOU 241 O ILE A 57 22571 18696 12495 -5756 319 1570 O
ATOM 242 CB ILE A 57 -78.043 71.328 337.774 1.00130.35 C
ANISOU 242 CB ILE A 57 19600 17841 12087 -4657 247 1529 C
ATOM 243 CG1 ILE A 57 -77.998 69.778 337.800 1.00127.67 C
ANISOU 243 CG1 ILE A 57 18526 17869 12112 -4245 302 1488 C
ATOM 244 CG2 ILE A 57 -79.447 71.829 337.395 1.00129.59 C
ANISOU 244 CG2 ILE A 57 20090 17143 12006 -4302 59 1556 C
ATOM 245 CD1 ILE A 57 -78.436 69.111 339.099 1.00130.72 C
ANISOU 245 CD1 ILE A 57 18528 18315 12824 -3861 220 1486 C
ATOM 246 N LEU A 58 -76.746 74.214 337.700 1.00140.32 N
ANISOU 246 N LEU A 58 22066 18840 12410 -5980 320 1574 N
ATOM 247 CA LEU A 58 -76.870 75.677 337.718 1.00144.04 C
ANISOU 247 CA LEU A 58 23372 18871 12485 -6358 241 1618 C
ATOM 248 C LEU A 58 -76.003 76.441 336.701 1.00155.46 C
ANISOU 248 C LEU A 58 25254 20359 13453 -7037 383 1607 C
ATOM 249 O LEU A 58 -76.485 77.415 336.116 1.00157.11 O
ANISOU 249 O LEU A 58 26273 20058 13362 -7155 282 1646 O
ATOM 250 CB LEU A 58 -76.618 76.236 339.130 1.00144.28 C
ANISOU 250 CB LEU A 58 23409 18926 12483 -6533 199 1636 C
ATOM 251 CG LEU A 58 -77.739 76.053 340.158 1.00145.29 C
ANISOU 251 CG LEU A 58 23482 18779 12944 -5945 9 1656 C
ATOM 252 CD1 LEU A 58 -77.180 76.021 341.561 1.00145.14 C
ANISOU 252 CD1 LEU A 58 23090 19047 13009 -6090 40 1655 C
ATOM 253 CD2 LEU A 58 -78.783 77.155 340.050 1.00147.78 C
ANISOU 253 CD2 LEU A 58 24646 18427 13077 -5793 -199 1688 C
ATOM 254 N ALA A 59 -74.736 76.036 336.514 1.00156.03 N
ANISOU 254 N ALA A 59 24821 21035 13430 -7485 609 1542 N
ATOM 255 CA ALA A 59 -73.811 76.739 335.621 1.00161.24 C
ANISOU 255 CA ALA A 59 25832 21819 13612 -8209 779 1507 C
ATOM 256 C ALA A 59 -74.016 76.461 334.130 1.00168.63 C
ANISOU 256 C ALA A 59 26959 22646 14467 -8163 828 1495 C
ATOM 257 O ALA A 59 -73.728 77.338 333.313 1.00171.92 O
ANISOU 257 O ALA A 59 28029 22853 14440 -8674 883 1500 O
ATOM 258 CB ALA A 59 -72.371 76.455 336.018 1.00163.86 C
ANISOU 258 CB ALA A 59 25519 22887 13855 -8710 1002 1406 C
ATOM 259 N HIS A 60 -74.496 75.258 333.775 1.00163.96 N
ANISOU 259 N HIS A 60 25832 22188 14276 -7580 811 1479 N
ATOM 260 CA HIS A 60 -74.689 74.858 332.380 1.00165.05 C
ANISOU 260 CA HIS A 60 26062 22264 14384 -7484 861 1464 C
ATOM 261 C HIS A 60 -75.815 75.593 331.650 1.00171.97 C
ANISOU 261 C HIS A 60 27819 22416 15107 -7292 671 1537 C
ATOM 262 O HIS A 60 -75.668 75.860 330.446 1.00174.59 O
ANISOU 262 O HIS A 60 28531 22635 15171 -7545 737 1529 O
ATOM 263 CB HIS A 60 -74.877 73.340 332.265 1.00162.23 C
ANISOU 263 CB HIS A 60 24902 22240 14497 -6900 885 1427 C
ATOM 264 CG HIS A 60 -73.601 72.557 332.363 1.00166.64 C
ANISOU 264 CG HIS A 60 24666 23550 15100 -7139 1104 1320 C
ATOM 265 ND1 HIS A 60 -72.681 72.786 333.379 1.00170.00 N
ANISOU 265 ND1 HIS A 60 24767 24384 15443 -7497 1186 1267 N
ATOM 266 CD2 HIS A 60 -73.152 71.541 331.591 1.00168.03 C
ANISOU 266 CD2 HIS A 60 24311 24131 15402 -7014 1235 1244 C
ATOM 267 CE1 HIS A 60 -71.696 71.928 333.171 1.00170.05 C
ANISOU 267 CE1 HIS A 60 24058 25040 15512 -7576 1358 1150 C
ATOM 268 NE2 HIS A 60 -71.936 71.155 332.110 1.00169.26 N
ANISOU 268 NE2 HIS A 60 23814 24959 15538 -7288 1394 1132 N
ATOM 269 N LYS A 61 -76.938 75.899 332.356 1.00167.10 N
ANISOU 269 N LYS A 61 27512 21324 14654 -6824 429 1593 N
ATOM 270 CA LYS A 61 -78.142 76.572 331.819 1.00167.35 C
ANISOU 270 CA LYS A 61 28348 20664 14575 -6514 195 1638 C
ATOM 271 C LYS A 61 -78.884 75.725 330.751 1.00168.61 C
ANISOU 271 C LYS A 61 28387 20721 14956 -6017 145 1623 C
ATOM 272 O LYS A 61 -80.064 75.965 330.486 1.00167.83 O
ANISOU 272 O LYS A 61 28781 20109 14877 -5589 -77 1636 O
ATOM 273 CB LYS A 61 -77.845 77.997 331.310 1.00174.91 C
ANISOU 273 CB LYS A 61 30271 21237 14948 -7115 178 1667 C
ATOM 274 N ARG A 62 -78.185 74.739 330.159 1.00163.09 N
ANISOU 274 N ARG A 62 27031 20524 14413 -6066 345 1583 N
ATOM 275 CA ARG A 62 -78.701 73.761 329.210 1.00160.15 C
ANISOU 275 CA ARG A 62 26404 20169 14278 -5635 341 1565 C
ATOM 276 C ARG A 62 -79.210 72.593 330.044 1.00158.48 C
ANISOU 276 C ARG A 62 25428 20199 14588 -5039 300 1547 C
ATOM 277 O ARG A 62 -80.090 71.853 329.602 1.00155.35 O
ANISOU 277 O ARG A 62 24858 19707 14461 -4525 224 1536 O
ATOM 278 CB ARG A 62 -77.572 73.279 328.294 1.00162.59 C
ANISOU 278 CB ARG A 62 26423 20928 14426 -6076 597 1521 C
ATOM 279 N MET A 63 -78.644 72.450 331.269 1.00153.59 N
ANISOU 279 N MET A 63 24383 19886 14088 -5134 350 1540 N
ATOM 280 CA MET A 63 -78.950 71.420 332.264 1.00148.84 C
ANISOU 280 CA MET A 63 23093 19530 13930 -4662 321 1523 C
ATOM 281 C MET A 63 -80.163 71.743 333.134 1.00149.20 C
ANISOU 281 C MET A 63 23375 19160 14154 -4216 94 1544 C
ATOM 282 O MET A 63 -80.699 70.832 333.764 1.00145.91 O
ANISOU 282 O MET A 63 22472 18859 14109 -3761 49 1525 O
ATOM 283 CB MET A 63 -77.724 71.142 333.145 1.00151.68 C
ANISOU 283 CB MET A 63 22888 20444 14299 -4997 483 1492 C
ATOM 284 CG MET A 63 -76.765 70.140 332.550 1.00155.56 C
ANISOU 284 CG MET A 63 22766 21495 14845 -5105 683 1426 C
ATOM 285 SD MET A 63 -77.381 68.443 332.625 1.00155.51 S
ANISOU 285 SD MET A 63 22093 21651 15344 -4373 643 1405 S
ATOM 286 CE MET A 63 -75.853 67.559 332.655 1.00153.34 C
ANISOU 286 CE MET A 63 21028 22143 15092 -4593 852 1310 C
ATOM 287 N ARG A 64 -80.588 73.025 333.185 1.00146.49 N
ANISOU 287 N ARG A 64 23785 18341 13532 -4350 -49 1571 N
ATOM 288 CA ARG A 64 -81.748 73.484 333.961 1.00144.59 C
ANISOU 288 CA ARG A 64 23842 17692 13405 -3940 -277 1566 C
ATOM 289 C ARG A 64 -83.040 72.882 333.359 1.00145.54 C
ANISOU 289 C ARG A 64 23950 17571 13776 -3309 -424 1523 C
ATOM 290 O ARG A 64 -83.687 73.520 332.526 1.00146.46 O
ANISOU 290 O ARG A 64 24684 17259 13704 -3189 -574 1511 O
ATOM 291 CB ARG A 64 -81.782 75.024 333.988 1.00147.84 C
ANISOU 291 CB ARG A 64 25121 17660 13391 -4270 -392 1595 C
ATOM 292 N THR A 65 -83.390 71.631 333.768 1.00138.55 N
ANISOU 292 N THR A 65 22373 16971 13298 -2913 -385 1491 N
ATOM 293 CA THR A 65 -84.512 70.859 333.199 1.00135.63 C
ANISOU 293 CA THR A 65 21868 16478 13187 -2355 -483 1438 C
ATOM 294 C THR A 65 -85.703 70.545 334.142 1.00134.69 C
ANISOU 294 C THR A 65 21594 16225 13358 -1837 -642 1370 C
ATOM 295 O THR A 65 -86.368 69.525 333.921 1.00133.19 O
ANISOU 295 O THR A 65 21047 16113 13447 -1430 -657 1319 O
ATOM 296 CB THR A 65 -83.994 69.529 332.583 1.00143.47 C
ANISOU 296 CB THR A 65 22237 17886 14389 -2305 -307 1439 C
ATOM 297 OG1 THR A 65 -83.500 68.663 333.611 1.00139.80 O
ANISOU 297 OG1 THR A 65 21134 17806 14178 -2259 -211 1437 O
ATOM 298 CG2 THR A 65 -82.950 69.736 331.486 1.00145.94 C
ANISOU 298 CG2 THR A 65 22661 18362 14429 -2769 -145 1474 C
ATOM 299 N VAL A 66 -86.015 71.421 335.128 1.00128.15 N
ANISOU 299 N VAL A 66 21051 15193 12447 -1857 -757 1359 N
ATOM 300 CA VAL A 66 -87.135 71.263 336.081 1.00124.62 C
ANISOU 300 CA VAL A 66 20488 14628 12234 -1409 -902 1275 C
ATOM 301 C VAL A 66 -86.865 70.095 337.044 1.00122.68 C
ANISOU 301 C VAL A 66 19510 14783 12321 -1322 -775 1276 C
ATOM 302 O VAL A 66 -86.834 70.338 338.249 1.00122.47 O
ANISOU 302 O VAL A 66 19403 14784 12345 -1355 -795 1272 O
ATOM 303 CB VAL A 66 -88.554 71.213 335.431 1.00127.64 C
ANISOU 303 CB VAL A 66 21094 14712 12690 -888 -1094 1162 C
ATOM 304 CG1 VAL A 66 -89.620 70.725 336.412 1.00125.14 C
ANISOU 304 CG1 VAL A 66 20472 14417 12660 -447 -1189 1048 C
ATOM 305 CG2 VAL A 66 -88.936 72.576 334.870 1.00130.44 C
ANISOU 305 CG2 VAL A 66 22267 14605 12688 -922 -1281 1145 C
ATOM 306 N THR A 67 -86.665 68.855 336.528 1.00114.32 N
ANISOU 306 N THR A 67 17958 14012 11465 -1215 -652 1281 N
ATOM 307 CA THR A 67 -86.312 67.670 337.323 1.00110.79 C
ANISOU 307 CA THR A 67 16863 13937 11296 -1141 -535 1286 C
ATOM 308 C THR A 67 -84.961 67.928 338.022 1.00114.56 C
ANISOU 308 C THR A 67 17192 14682 11653 -1591 -411 1361 C
ATOM 309 O THR A 67 -84.820 67.684 339.229 1.00112.90 O
ANISOU 309 O THR A 67 16708 14615 11572 -1580 -399 1360 O
ATOM 310 CB THR A 67 -86.362 66.400 336.447 1.00112.21 C
ANISOU 310 CB THR A 67 16661 14315 11657 -934 -449 1273 C
ATOM 311 OG1 THR A 67 -87.707 65.911 336.431 1.00110.58 O
ANISOU 311 OG1 THR A 67 16422 13945 11648 -479 -561 1180 O
ATOM 312 CG2 THR A 67 -85.430 65.288 336.937 1.00105.50 C
ANISOU 312 CG2 THR A 67 15222 13890 10974 -1003 -298 1306 C
ATOM 313 N ASN A 68 -84.004 68.496 337.262 1.00112.20 N
ANISOU 313 N ASN A 68 17110 14439 11080 -2003 -326 1413 N
ATOM 314 CA ASN A 68 -82.677 68.863 337.740 1.00112.80 C
ANISOU 314 CA ASN A 68 17084 14793 10982 -2490 -204 1461 C
ATOM 315 C ASN A 68 -82.707 70.038 338.736 1.00117.10 C
ANISOU 315 C ASN A 68 18007 15126 11361 -2696 -291 1479 C
ATOM 316 O ASN A 68 -81.840 70.101 339.616 1.00117.82 O
ANISOU 316 O ASN A 68 17871 15477 11419 -2977 -214 1502 O
ATOM 317 CB ASN A 68 -81.738 69.120 336.569 1.00112.28 C
ANISOU 317 CB ASN A 68 17147 14863 10652 -2886 -77 1484 C
ATOM 318 CG ASN A 68 -81.254 67.884 335.838 1.00120.69 C
ANISOU 318 CG ASN A 68 17696 16295 11864 -2790 58 1465 C
ATOM 319 OD1 ASN A 68 -80.512 67.986 334.859 1.00120.11 O
ANISOU 319 OD1 ASN A 68 17666 16378 11591 -3097 176 1466 O
ATOM 320 ND2 ASN A 68 -81.649 66.690 336.273 1.00103.75 N
ANISOU 320 ND2 ASN A 68 15077 14295 10048 -2377 48 1439 N
ATOM 321 N TYR A 69 -83.718 70.940 338.627 1.00112.37 N
ANISOU 321 N TYR A 69 17974 14062 10658 -2528 -462 1458 N
ATOM 322 CA TYR A 69 -83.907 72.054 339.563 1.00112.48 C
ANISOU 322 CA TYR A 69 18396 13823 10519 -2650 -571 1464 C
ATOM 323 C TYR A 69 -84.271 71.505 340.942 1.00112.07 C
ANISOU 323 C TYR A 69 17931 13898 10752 -2401 -597 1435 C
ATOM 324 O TYR A 69 -83.790 72.027 341.951 1.00112.97 O
ANISOU 324 O TYR A 69 18089 14051 10782 -2644 -591 1463 O
ATOM 325 CB TYR A 69 -84.997 73.016 339.084 1.00115.04 C
ANISOU 325 CB TYR A 69 19400 13629 10681 -2425 -774 1421 C
ATOM 326 CG TYR A 69 -84.479 74.251 338.382 1.00121.21 C
ANISOU 326 CG TYR A 69 20878 14153 11025 -2854 -796 1470 C
ATOM 327 CD1 TYR A 69 -83.801 75.245 339.084 1.00125.47 C
ANISOU 327 CD1 TYR A 69 21732 14639 11302 -3290 -783 1519 C
ATOM 328 CD2 TYR A 69 -84.734 74.466 337.029 1.00123.59 C
ANISOU 328 CD2 TYR A 69 21581 14226 11150 -2824 -843 1464 C
ATOM 329 CE1 TYR A 69 -83.338 76.395 338.443 1.00130.40 C
ANISOU 329 CE1 TYR A 69 23057 15004 11486 -3723 -801 1561 C
ATOM 330 CE2 TYR A 69 -84.297 75.622 336.384 1.00128.01 C
ANISOU 330 CE2 TYR A 69 22858 14508 11272 -3234 -871 1507 C
ATOM 331 CZ TYR A 69 -83.589 76.579 337.091 1.00138.44 C
ANISOU 331 CZ TYR A 69 24491 15788 12323 -3698 -845 1555 C
ATOM 332 OH TYR A 69 -83.148 77.713 336.452 1.00144.93 O
ANISOU 332 OH TYR A 69 26066 16323 12679 -4144 -867 1596 O
ATOM 333 N PHE A 70 -85.098 70.433 340.984 1.00103.38 N
ANISOU 333 N PHE A 70 16442 12866 9973 -1943 -618 1375 N
ATOM 334 CA PHE A 70 -85.465 69.768 342.235 1.00 99.50 C
ANISOU 334 CA PHE A 70 15549 12506 9750 -1714 -626 1339 C
ATOM 335 C PHE A 70 -84.280 68.965 342.759 1.00102.40 C
ANISOU 335 C PHE A 70 15391 13311 10204 -1940 -472 1393 C
ATOM 336 O PHE A 70 -84.084 68.907 343.970 1.00101.66 O
ANISOU 336 O PHE A 70 15110 13322 10193 -1974 -471 1397 O
ATOM 337 CB PHE A 70 -86.711 68.894 342.072 1.00 97.99 C
ANISOU 337 CB PHE A 70 15153 12250 9829 -1205 -690 1245 C
ATOM 338 CG PHE A 70 -87.988 69.672 341.864 1.00 98.70 C
ANISOU 338 CG PHE A 70 15694 11950 9858 -914 -871 1149 C
ATOM 339 CD1 PHE A 70 -88.484 70.507 342.862 1.00101.56 C
ANISOU 339 CD1 PHE A 70 16317 12110 10162 -868 -986 1101 C
ATOM 340 CD2 PHE A 70 -88.728 69.525 340.700 1.00 98.65 C
ANISOU 340 CD2 PHE A 70 15829 11794 9858 -647 -938 1089 C
ATOM 341 CE1 PHE A 70 -89.669 71.223 342.672 1.00102.60 C
ANISOU 341 CE1 PHE A 70 16853 11904 10225 -552 -1171 983 C
ATOM 342 CE2 PHE A 70 -89.914 70.236 340.513 1.00101.60 C
ANISOU 342 CE2 PHE A 70 16604 11834 10166 -335 -1128 973 C
ATOM 343 CZ PHE A 70 -90.372 71.088 341.494 1.00100.71 C
ANISOU 343 CZ PHE A 70 16749 11533 9982 -279 -1248 914 C
ATOM 344 N LEU A 71 -83.449 68.407 341.846 1.00 98.68 N
ANISOU 344 N LEU A 71 14700 13102 9692 -2096 -349 1424 N
ATOM 345 CA LEU A 71 -82.228 67.685 342.222 1.00 98.13 C
ANISOU 345 CA LEU A 71 14134 13484 9667 -2298 -215 1450 C
ATOM 346 C LEU A 71 -81.218 68.641 342.893 1.00106.11 C
ANISOU 346 C LEU A 71 15275 14604 10438 -2777 -177 1489 C
ATOM 347 O LEU A 71 -80.454 68.207 343.759 1.00105.01 O
ANISOU 347 O LEU A 71 14747 14790 10361 -2882 -121 1491 O
ATOM 348 CB LEU A 71 -81.583 66.983 341.014 1.00 97.90 C
ANISOU 348 CB LEU A 71 13863 13714 9619 -2345 -97 1449 C
ATOM 349 CG LEU A 71 -82.299 65.775 340.406 1.00 98.72 C
ANISOU 349 CG LEU A 71 13722 13818 9971 -1905 -104 1414 C
ATOM 350 CD1 LEU A 71 -81.408 65.090 339.387 1.00 98.74 C
ANISOU 350 CD1 LEU A 71 13463 14127 9928 -2003 24 1413 C
ATOM 351 CD2 LEU A 71 -82.757 64.774 341.477 1.00 96.59 C
ANISOU 351 CD2 LEU A 71 13071 13646 9981 -1581 -133 1387 C
ATOM 352 N VAL A 72 -81.230 69.942 342.491 1.00106.48 N
ANISOU 352 N VAL A 72 15894 14371 10192 -3065 -218 1513 N
ATOM 353 CA VAL A 72 -80.391 70.999 343.067 1.00109.24 C
ANISOU 353 CA VAL A 72 16484 14756 10267 -3557 -192 1548 C
ATOM 354 C VAL A 72 -80.854 71.233 344.500 1.00113.04 C
ANISOU 354 C VAL A 72 16973 15113 10863 -3427 -289 1548 C
ATOM 355 O VAL A 72 -80.013 71.330 345.398 1.00113.66 O
ANISOU 355 O VAL A 72 16857 15437 10892 -3701 -238 1565 O
ATOM 356 CB VAL A 72 -80.399 72.301 342.212 1.00115.78 C
ANISOU 356 CB VAL A 72 18013 15250 10729 -3875 -225 1573 C
ATOM 357 CG1 VAL A 72 -80.049 73.544 343.038 1.00117.84 C
ANISOU 357 CG1 VAL A 72 18693 15360 10721 -4267 -264 1606 C
ATOM 358 CG2 VAL A 72 -79.447 72.174 341.042 1.00117.44 C
ANISOU 358 CG2 VAL A 72 18158 15715 10750 -4215 -75 1574 C
ATOM 359 N ASN A 73 -82.196 71.287 344.705 1.00108.09 N
ANISOU 359 N ASN A 73 16550 14130 10388 -3002 -427 1514 N
ATOM 360 CA ASN A 73 -82.831 71.495 346.010 1.00106.63 C
ANISOU 360 CA ASN A 73 16393 13799 10321 -2826 -523 1492 C
ATOM 361 C ASN A 73 -82.554 70.323 346.938 1.00107.94 C
ANISOU 361 C ASN A 73 15945 14307 10761 -2683 -461 1483 C
ATOM 362 O ASN A 73 -82.355 70.512 348.139 1.00107.59 O
ANISOU 362 O ASN A 73 15827 14316 10737 -2777 -477 1494 O
ATOM 363 CB ASN A 73 -84.336 71.725 345.865 1.00105.50 C
ANISOU 363 CB ASN A 73 16553 13262 10270 -2386 -674 1420 C
ATOM 364 CG ASN A 73 -84.952 72.287 347.119 1.00122.74 C
ANISOU 364 CG ASN A 73 18901 15252 12484 -2278 -780 1383 C
ATOM 365 OD1 ASN A 73 -84.450 73.249 347.701 1.00115.56 O
ANISOU 365 OD1 ASN A 73 18277 14263 11367 -2596 -797 1426 O
ATOM 366 ND2 ASN A 73 -86.042 71.691 347.575 1.00112.85 N
ANISOU 366 ND2 ASN A 73 17476 13927 11476 -1844 -846 1292 N
ATOM 367 N LEU A 74 -82.527 69.117 346.364 1.00102.20 N
ANISOU 367 N LEU A 74 14809 13796 10225 -2458 -396 1464 N
ATOM 368 CA LEU A 74 -82.223 67.869 347.043 1.00 99.55 C
ANISOU 368 CA LEU A 74 13924 13779 10123 -2297 -344 1453 C
ATOM 369 C LEU A 74 -80.723 67.850 347.402 1.00105.59 C
ANISOU 369 C LEU A 74 14421 14937 10760 -2677 -251 1488 C
ATOM 370 O LEU A 74 -80.388 67.440 348.508 1.00105.57 O
ANISOU 370 O LEU A 74 14147 15111 10854 -2664 -257 1487 O
ATOM 371 CB LEU A 74 -82.637 66.689 346.133 1.00 97.42 C
ANISOU 371 CB LEU A 74 13391 13589 10037 -1968 -309 1421 C
ATOM 372 CG LEU A 74 -82.110 65.288 346.426 1.00100.14 C
ANISOU 372 CG LEU A 74 13200 14285 10564 -1820 -245 1412 C
ATOM 373 CD1 LEU A 74 -82.589 64.768 347.783 1.00 98.16 C
ANISOU 373 CD1 LEU A 74 12794 14001 10501 -1606 -298 1388 C
ATOM 374 CD2 LEU A 74 -82.512 64.340 345.324 1.00100.58 C
ANISOU 374 CD2 LEU A 74 13107 14377 10733 -1559 -208 1387 C
ATOM 375 N ALA A 75 -79.840 68.335 346.496 1.00104.06 N
ANISOU 375 N ALA A 75 14320 14884 10333 -3027 -170 1505 N
ATOM 376 CA ALA A 75 -78.388 68.414 346.710 1.00106.16 C
ANISOU 376 CA ALA A 75 14328 15572 10435 -3433 -72 1505 C
ATOM 377 C ALA A 75 -78.027 69.430 347.797 1.00111.49 C
ANISOU 377 C ALA A 75 15211 16198 10952 -3759 -107 1531 C
ATOM 378 O ALA A 75 -77.082 69.200 348.553 1.00111.81 O
ANISOU 378 O ALA A 75 14910 16592 10982 -3924 -71 1516 O
ATOM 379 CB ALA A 75 -77.673 68.765 345.411 1.00109.34 C
ANISOU 379 CB ALA A 75 14841 16107 10597 -3760 32 1498 C
ATOM 380 N PHE A 76 -78.780 70.544 347.879 1.00108.85 N
ANISOU 380 N PHE A 76 15445 15426 10488 -3829 -189 1562 N
ATOM 381 CA PHE A 76 -78.577 71.574 348.893 1.00110.38 C
ANISOU 381 CA PHE A 76 15916 15504 10521 -4117 -235 1591 C
ATOM 382 C PHE A 76 -78.974 71.028 350.268 1.00112.44 C
ANISOU 382 C PHE A 76 15916 15776 11030 -3835 -303 1582 C
ATOM 383 O PHE A 76 -78.186 71.129 351.206 1.00112.87 O
ANISOU 383 O PHE A 76 15788 16062 11036 -4065 -285 1590 O
ATOM 384 CB PHE A 76 -79.371 72.849 348.561 1.00113.67 C
ANISOU 384 CB PHE A 76 17048 15413 10730 -4189 -328 1614 C
ATOM 385 CG PHE A 76 -79.338 73.881 349.664 1.00117.13 C
ANISOU 385 CG PHE A 76 17818 15670 11017 -4418 -395 1641 C
ATOM 386 CD1 PHE A 76 -78.220 74.687 349.853 1.00123.55 C
ANISOU 386 CD1 PHE A 76 18772 16647 11526 -4987 -326 1670 C
ATOM 387 CD2 PHE A 76 -80.416 74.033 350.531 1.00118.55 C
ANISOU 387 CD2 PHE A 76 18162 15535 11345 -4079 -522 1624 C
ATOM 388 CE1 PHE A 76 -78.182 75.631 350.884 1.00125.80 C
ANISOU 388 CE1 PHE A 76 19381 16756 11662 -5207 -389 1698 C
ATOM 389 CE2 PHE A 76 -80.373 74.971 351.569 1.00122.67 C
ANISOU 389 CE2 PHE A 76 18993 15890 11725 -4281 -584 1646 C
ATOM 390 CZ PHE A 76 -79.258 75.766 351.735 1.00123.48 C
ANISOU 390 CZ PHE A 76 19257 16131 11528 -4840 -521 1690 C
ATOM 391 N ALA A 77 -80.196 70.448 350.373 1.00106.34 N
ANISOU 391 N ALA A 77 15130 14768 10508 -3355 -377 1555 N
ATOM 392 CA ALA A 77 -80.767 69.851 351.584 1.00103.43 C
ANISOU 392 CA ALA A 77 14551 14372 10376 -3063 -435 1533 C
ATOM 393 C ALA A 77 -79.844 68.780 352.138 1.00106.42 C
ANISOU 393 C ALA A 77 14380 15180 10876 -3061 -378 1530 C
ATOM 394 O ALA A 77 -79.622 68.749 353.351 1.00106.57 O
ANISOU 394 O ALA A 77 14286 15265 10940 -3094 -410 1535 O
ATOM 395 CB ALA A 77 -82.138 69.261 351.282 1.00101.79 C
ANISOU 395 CB ALA A 77 14369 13919 10387 -2591 -491 1479 C
ATOM 396 N ASN A 78 -79.264 67.942 351.243 1.00102.28 N
ANISOU 396 N ASN A 78 13532 14947 10383 -3020 -302 1515 N
ATOM 397 CA ASN A 78 -78.309 66.891 351.590 1.00101.90 C
ANISOU 397 CA ASN A 78 12968 15332 10418 -2980 -263 1492 C
ATOM 398 C ASN A 78 -77.049 67.520 352.197 1.00108.97 C
ANISOU 398 C ASN A 78 13772 16523 11107 -3411 -235 1495 C
ATOM 399 O ASN A 78 -76.830 67.376 353.397 1.00109.07 O
ANISOU 399 O ASN A 78 13656 16613 11173 -3403 -285 1496 O
ATOM 400 CB ASN A 78 -77.949 66.025 350.364 1.00100.40 C
ANISOU 400 CB ASN A 78 12506 15377 10265 -2854 -190 1460 C
ATOM 401 CG ASN A 78 -78.950 64.957 349.953 1.00112.30 C
ANISOU 401 CG ASN A 78 13928 16729 12011 -2389 -214 1443 C
ATOM 402 OD1 ASN A 78 -78.775 64.285 348.927 1.00111.41 O
ANISOU 402 OD1 ASN A 78 13647 16756 11929 -2270 -161 1421 O
ATOM 403 ND2 ASN A 78 -80.019 64.764 350.716 1.00 93.23 N
ANISOU 403 ND2 ASN A 78 11624 14040 9759 -2134 -287 1440 N
ATOM 404 N ALA A 79 -76.266 68.270 351.394 1.00107.77 N
ANISOU 404 N ALA A 79 13720 16524 10703 -3810 -154 1491 N
ATOM 405 CA ALA A 79 -75.022 68.928 351.814 1.00109.74 C
ANISOU 405 CA ALA A 79 13884 17099 10712 -4290 -106 1473 C
ATOM 406 C ALA A 79 -75.137 69.721 353.131 1.00112.95 C
ANISOU 406 C ALA A 79 14514 17337 11064 -4456 -178 1512 C
ATOM 407 O ALA A 79 -74.235 69.633 353.966 1.00113.43 O
ANISOU 407 O ALA A 79 14293 17733 11074 -4631 -179 1483 O
ATOM 408 CB ALA A 79 -74.496 69.814 350.695 1.00112.85 C
ANISOU 408 CB ALA A 79 14532 17535 10811 -4728 -7 1468 C
ATOM 409 N SER A 80 -76.251 70.461 353.321 1.00108.32 N
ANISOU 409 N SER A 80 14422 16246 10487 -4374 -248 1565 N
ATOM 410 CA SER A 80 -76.540 71.251 354.517 1.00108.41 C
ANISOU 410 CA SER A 80 14710 16029 10450 -4489 -323 1600 C
ATOM 411 C SER A 80 -76.602 70.363 355.764 1.00112.82 C
ANISOU 411 C SER A 80 14916 16710 11240 -4216 -381 1586 C
ATOM 412 O SER A 80 -75.953 70.683 356.763 1.00114.68 O
ANISOU 412 O SER A 80 15088 17093 11392 -4447 -401 1592 O
ATOM 413 CB SER A 80 -77.870 71.977 354.360 1.00110.44 C
ANISOU 413 CB SER A 80 15516 15738 10709 -4324 -399 1627 C
ATOM 414 OG SER A 80 -77.805 73.009 353.395 1.00123.24 O
ANISOU 414 OG SER A 80 17580 17180 12065 -4605 -373 1646 O
ATOM 415 N MET A 81 -77.362 69.241 355.697 1.00106.54 N
ANISOU 415 N MET A 81 13912 15853 10716 -3745 -409 1565 N
ATOM 416 CA MET A 81 -77.520 68.300 356.803 1.00104.95 C
ANISOU 416 CA MET A 81 13431 15725 10721 -3467 -466 1549 C
ATOM 417 C MET A 81 -76.209 67.661 357.219 1.00109.72 C
ANISOU 417 C MET A 81 13581 16815 11292 -3569 -456 1518 C
ATOM 418 O MET A 81 -76.011 67.441 358.417 1.00110.83 O
ANISOU 418 O MET A 81 13609 17021 11482 -3540 -517 1517 O
ATOM 419 CB MET A 81 -78.547 67.214 356.471 1.00105.09 C
ANISOU 419 CB MET A 81 13349 15592 10987 -2996 -481 1523 C
ATOM 420 CG MET A 81 -79.438 66.843 357.655 1.00107.13 C
ANISOU 420 CG MET A 81 13655 15633 11417 -2748 -548 1513 C
ATOM 421 SD MET A 81 -80.329 65.262 357.506 1.00109.15 S
ANISOU 421 SD MET A 81 13693 15841 11939 -2256 -553 1466 S
ATOM 422 CE MET A 81 -80.892 65.357 355.796 1.00106.36 C
ANISOU 422 CE MET A 81 13460 15370 11581 -2157 -499 1452 C
ATOM 423 N ALA A 82 -75.318 67.360 356.251 1.00105.41 N
ANISOU 423 N ALA A 82 12772 16623 10656 -3675 -385 1478 N
ATOM 424 CA ALA A 82 -74.009 66.761 356.532 1.00106.37 C
ANISOU 424 CA ALA A 82 12424 17270 10722 -3751 -382 1411 C
ATOM 425 C ALA A 82 -73.099 67.744 357.267 1.00111.59 C
ANISOU 425 C ALA A 82 13112 18129 11157 -4215 -380 1404 C
ATOM 426 O ALA A 82 -72.517 67.382 358.288 1.00111.72 O
ANISOU 426 O ALA A 82 12871 18387 11190 -4191 -446 1370 O
ATOM 427 CB ALA A 82 -73.344 66.295 355.245 1.00108.32 C
ANISOU 427 CB ALA A 82 12400 17848 10908 -3761 -297 1348 C
ATOM 428 N ALA A 83 -72.990 68.986 356.750 1.00109.13 N
ANISOU 428 N ALA A 83 13145 17701 10618 -4642 -311 1433 N
ATOM 429 CA ALA A 83 -72.155 70.050 357.301 1.00111.22 C
ANISOU 429 CA ALA A 83 13511 18125 10623 -5157 -290 1428 C
ATOM 430 C ALA A 83 -72.600 70.470 358.704 1.00114.61 C
ANISOU 430 C ALA A 83 14161 18286 11100 -5146 -386 1485 C
ATOM 431 O ALA A 83 -71.792 70.420 359.633 1.00114.66 O
ANISOU 431 O ALA A 83 13933 18586 11046 -5299 -422 1451 O
ATOM 432 CB ALA A 83 -72.145 71.245 356.361 1.00113.69 C
ANISOU 432 CB ALA A 83 14250 18279 10668 -5590 -200 1456 C
ATOM 433 N PHE A 84 -73.890 70.819 358.869 1.00110.39 N
ANISOU 433 N PHE A 84 14048 17217 10678 -4939 -433 1556 N
ATOM 434 CA PHE A 84 -74.443 71.270 360.146 1.00109.83 C
ANISOU 434 CA PHE A 84 14226 16855 10649 -4917 -516 1601 C
ATOM 435 C PHE A 84 -74.510 70.208 361.270 1.00111.98 C
ANISOU 435 C PHE A 84 14172 17229 11145 -4581 -596 1583 C
ATOM 436 O PHE A 84 -74.068 70.492 362.386 1.00111.77 O
ANISOU 436 O PHE A 84 14127 17279 11060 -4744 -646 1590 O
ATOM 437 CB PHE A 84 -75.840 71.908 359.954 1.00110.38 C
ANISOU 437 CB PHE A 84 14819 16358 10762 -4760 -547 1648 C
ATOM 438 CG PHE A 84 -75.901 73.229 359.216 1.00114.51 C
ANISOU 438 CG PHE A 84 15846 16647 11015 -5110 -515 1679 C
ATOM 439 CD1 PHE A 84 -75.169 74.330 359.657 1.00120.98 C
ANISOU 439 CD1 PHE A 84 16900 17514 11553 -5609 -503 1703 C
ATOM 440 CD2 PHE A 84 -76.756 73.399 358.131 1.00116.17 C
ANISOU 440 CD2 PHE A 84 16351 16553 11237 -4936 -510 1683 C
ATOM 441 CE1 PHE A 84 -75.236 75.558 358.978 1.00123.80 C
ANISOU 441 CE1 PHE A 84 17800 17614 11623 -5948 -481 1733 C
ATOM 442 CE2 PHE A 84 -76.828 74.626 357.457 1.00121.08 C
ANISOU 442 CE2 PHE A 84 17507 16918 11581 -5243 -501 1711 C
ATOM 443 CZ PHE A 84 -76.072 75.698 357.889 1.00122.04 C
ANISOU 443 CZ PHE A 84 17889 17075 11407 -5752 -487 1739 C
ATOM 444 N ASN A 85 -75.058 69.005 360.984 1.00106.75 N
ANISOU 444 N ASN A 85 13291 16553 10717 -4133 -612 1560 N
ATOM 445 CA ASN A 85 -75.342 67.994 362.001 1.00105.30 C
ANISOU 445 CA ASN A 85 12915 16365 10730 -3798 -692 1547 C
ATOM 446 C ASN A 85 -74.337 66.857 362.252 1.00110.81 C
ANISOU 446 C ASN A 85 13126 17510 11467 -3650 -735 1487 C
ATOM 447 O ASN A 85 -74.282 66.404 363.399 1.00110.01 O
ANISOU 447 O ASN A 85 12945 17424 11430 -3530 -820 1483 O
ATOM 448 CB ASN A 85 -76.695 67.352 361.721 1.00104.86 C
ANISOU 448 CB ASN A 85 12988 15962 10891 -3393 -696 1551 C
ATOM 449 CG ASN A 85 -77.845 68.307 361.867 1.00131.88 C
ANISOU 449 CG ASN A 85 16866 18935 14307 -3427 -696 1579 C
ATOM 450 OD1 ASN A 85 -78.235 68.684 362.976 1.00128.34 O
ANISOU 450 OD1 ASN A 85 16598 18297 13867 -3460 -743 1591 O
ATOM 451 ND2 ASN A 85 -78.417 68.717 360.748 1.00124.94 N
ANISOU 451 ND2 ASN A 85 16190 17879 13403 -3400 -653 1578 N
ATOM 452 N THR A 86 -73.612 66.346 361.234 1.00108.94 N
ANISOU 452 N THR A 86 12584 17615 11192 -3620 -689 1431 N
ATOM 453 CA THR A 86 -72.728 65.173 361.406 1.00109.87 C
ANISOU 453 CA THR A 86 12244 18154 11348 -3391 -751 1351 C
ATOM 454 C THR A 86 -71.722 65.284 362.587 1.00115.61 C
ANISOU 454 C THR A 86 12766 19197 11963 -3551 -838 1306 C
ATOM 455 O THR A 86 -71.696 64.370 363.416 1.00114.76 O
ANISOU 455 O THR A 86 12513 19135 11954 -3246 -950 1282 O
ATOM 456 CB THR A 86 -72.022 64.777 360.101 1.00120.09 C
ANISOU 456 CB THR A 86 13242 19805 12580 -3380 -679 1278 C
ATOM 457 OG1 THR A 86 -72.996 64.715 359.056 1.00115.98 O
ANISOU 457 OG1 THR A 86 12946 18967 12156 -3249 -605 1324 O
ATOM 458 CG2 THR A 86 -71.324 63.420 360.201 1.00119.85 C
ANISOU 458 CG2 THR A 86 12783 20136 12618 -3013 -763 1184 C
ATOM 459 N VAL A 87 -70.926 66.365 362.677 1.00114.13 N
ANISOU 459 N VAL A 87 12590 19214 11559 -4022 -795 1292 N
ATOM 460 CA VAL A 87 -69.947 66.505 363.769 1.00115.97 C
ANISOU 460 CA VAL A 87 12612 19778 11673 -4194 -880 1238 C
ATOM 461 C VAL A 87 -70.642 66.564 365.141 1.00117.02 C
ANISOU 461 C VAL A 87 13006 19550 11906 -4089 -976 1314 C
ATOM 462 O VAL A 87 -70.336 65.765 366.026 1.00116.31 O
ANISOU 462 O VAL A 87 12724 19594 11874 -3849 -1099 1275 O
ATOM 463 CB VAL A 87 -68.955 67.689 363.564 1.00123.35 C
ANISOU 463 CB VAL A 87 13510 21033 12326 -4778 -799 1195 C
ATOM 464 CG1 VAL A 87 -67.899 67.730 364.670 1.00125.35 C
ANISOU 464 CG1 VAL A 87 13481 21690 12456 -4930 -895 1113 C
ATOM 465 CG2 VAL A 87 -68.288 67.631 362.191 1.00125.11 C
ANISOU 465 CG2 VAL A 87 13487 21618 12431 -4916 -685 1107 C
ATOM 466 N VAL A 88 -71.595 67.494 365.275 1.00111.57 N
ANISOU 466 N VAL A 88 12769 18397 11224 -4252 -925 1412 N
ATOM 467 CA VAL A 88 -72.392 67.784 366.459 1.00109.29 C
ANISOU 467 CA VAL A 88 12792 17724 11009 -4214 -985 1480 C
ATOM 468 C VAL A 88 -73.148 66.535 366.988 1.00110.60 C
ANISOU 468 C VAL A 88 12925 17697 11402 -3730 -1063 1481 C
ATOM 469 O VAL A 88 -73.103 66.280 368.195 1.00109.80 O
ANISOU 469 O VAL A 88 12835 17560 11325 -3667 -1156 1486 O
ATOM 470 CB VAL A 88 -73.295 69.003 366.138 1.00112.09 C
ANISOU 470 CB VAL A 88 13629 17648 11311 -4438 -906 1555 C
ATOM 471 CG1 VAL A 88 -74.744 68.817 366.560 1.00109.10 C
ANISOU 471 CG1 VAL A 88 13553 16779 11121 -4142 -927 1598 C
ATOM 472 CG2 VAL A 88 -72.704 70.271 366.724 1.00113.93 C
ANISOU 472 CG2 VAL A 88 14047 17927 11314 -4921 -902 1578 C
ATOM 473 N ASN A 89 -73.788 65.747 366.093 1.00105.29 N
ANISOU 473 N ASN A 89 12222 16910 10873 -3415 -1024 1474 N
ATOM 474 CA ASN A 89 -74.513 64.529 366.474 1.00102.76 C
ANISOU 474 CA ASN A 89 11901 16407 10738 -2994 -1082 1468 C
ATOM 475 C ASN A 89 -73.561 63.423 366.924 1.00108.73 C
ANISOU 475 C ASN A 89 12321 17510 11482 -2773 -1201 1403 C
ATOM 476 O ASN A 89 -73.868 62.715 367.888 1.00108.08 O
ANISOU 476 O ASN A 89 12312 17285 11470 -2558 -1292 1406 O
ATOM 477 CB ASN A 89 -75.426 64.033 365.347 1.00 99.81 C
ANISOU 477 CB ASN A 89 11592 15836 10496 -2751 -1005 1469 C
ATOM 478 CG ASN A 89 -76.767 64.728 365.280 1.00124.21 C
ANISOU 478 CG ASN A 89 15061 18478 13656 -2782 -941 1510 C
ATOM 479 OD1 ASN A 89 -76.864 65.961 365.232 1.00120.97 O
ANISOU 479 OD1 ASN A 89 14876 17944 13144 -3069 -903 1542 O
ATOM 480 ND2 ASN A 89 -77.839 63.946 365.248 1.00115.83 N
ANISOU 480 ND2 ASN A 89 14086 17172 12754 -2480 -931 1495 N
ATOM 481 N PHE A 90 -72.404 63.282 366.242 1.00107.44 N
ANISOU 481 N PHE A 90 11805 17806 11210 -2826 -1206 1332 N
ATOM 482 CA PHE A 90 -71.408 62.265 366.574 1.00108.57 C
ANISOU 482 CA PHE A 90 11600 18336 11316 -2582 -1338 1239 C
ATOM 483 C PHE A 90 -70.771 62.503 367.944 1.00113.58 C
ANISOU 483 C PHE A 90 12201 19100 11853 -2702 -1462 1221 C
ATOM 484 O PHE A 90 -70.720 61.572 368.751 1.00113.18 O
ANISOU 484 O PHE A 90 12131 19032 11840 -2400 -1602 1195 O
ATOM 485 CB PHE A 90 -70.343 62.124 365.469 1.00112.28 C
ANISOU 485 CB PHE A 90 11674 19306 11682 -2615 -1303 1136 C
ATOM 486 CG PHE A 90 -69.249 61.129 365.788 1.00116.16 C
ANISOU 486 CG PHE A 90 11776 20251 12108 -2339 -1457 1006 C
ATOM 487 CD1 PHE A 90 -69.502 59.762 365.773 1.00118.47 C
ANISOU 487 CD1 PHE A 90 12041 20470 12503 -1843 -1560 977 C
ATOM 488 CD2 PHE A 90 -67.970 61.561 366.125 1.00121.66 C
ANISOU 488 CD2 PHE A 90 12150 21453 12621 -2568 -1508 899 C
ATOM 489 CE1 PHE A 90 -68.491 58.842 366.074 1.00121.68 C
ANISOU 489 CE1 PHE A 90 12124 21280 12827 -1540 -1730 843 C
ATOM 490 CE2 PHE A 90 -66.960 60.640 366.435 1.00126.77 C
ANISOU 490 CE2 PHE A 90 12422 22546 13197 -2266 -1674 750 C
ATOM 491 CZ PHE A 90 -67.227 59.287 366.404 1.00124.02 C
ANISOU 491 CZ PHE A 90 12075 22096 12951 -1734 -1793 724 C
ATOM 492 N THR A 91 -70.295 63.742 368.201 1.00111.17 N
ANISOU 492 N THR A 91 11923 18910 11407 -3150 -1414 1234 N
ATOM 493 CA THR A 91 -69.626 64.138 369.451 1.00112.39 C
ANISOU 493 CA THR A 91 12041 19216 11446 -3334 -1518 1216 C
ATOM 494 C THR A 91 -70.532 63.940 370.675 1.00113.10 C
ANISOU 494 C THR A 91 12473 18858 11642 -3198 -1589 1297 C
ATOM 495 O THR A 91 -70.086 63.353 371.665 1.00113.50 O
ANISOU 495 O THR A 91 12442 19018 11663 -3048 -1740 1259 O
ATOM 496 CB THR A 91 -69.054 65.557 369.346 1.00122.49 C
ANISOU 496 CB THR A 91 13336 20666 12539 -3882 -1427 1220 C
ATOM 497 OG1 THR A 91 -68.402 65.712 368.090 1.00125.32 O
ANISOU 497 OG1 THR A 91 13432 21384 12800 -4023 -1330 1146 O
ATOM 498 CG2 THR A 91 -68.054 65.857 370.430 1.00124.80 C
ANISOU 498 CG2 THR A 91 13461 21279 12678 -4081 -1538 1161 C
ATOM 499 N TYR A 92 -71.802 64.392 370.586 1.00106.17 N
ANISOU 499 N TYR A 92 11971 17494 10875 -3235 -1486 1391 N
ATOM 500 CA TYR A 92 -72.792 64.239 371.651 1.00103.48 C
ANISOU 500 CA TYR A 92 11958 16727 10632 -3129 -1522 1450 C
ATOM 501 C TYR A 92 -72.995 62.753 371.968 1.00106.57 C
ANISOU 501 C TYR A 92 12301 17071 11120 -2690 -1627 1416 C
ATOM 502 O TYR A 92 -72.894 62.384 373.134 1.00107.08 O
ANISOU 502 O TYR A 92 12449 17073 11162 -2612 -1744 1414 O
ATOM 503 CB TYR A 92 -74.127 64.936 371.283 1.00101.71 C
ANISOU 503 CB TYR A 92 12091 16056 10499 -3217 -1387 1517 C
ATOM 504 CG TYR A 92 -75.098 65.147 372.436 1.00101.13 C
ANISOU 504 CG TYR A 92 12355 15586 10482 -3227 -1397 1557 C
ATOM 505 CD1 TYR A 92 -76.445 65.412 372.200 1.00100.03 C
ANISOU 505 CD1 TYR A 92 12500 15057 10448 -3174 -1300 1576 C
ATOM 506 CD2 TYR A 92 -74.663 65.111 373.761 1.00102.97 C
ANISOU 506 CD2 TYR A 92 12618 15856 10651 -3293 -1504 1561 C
ATOM 507 CE1 TYR A 92 -77.337 65.630 373.251 1.00 97.36 C
ANISOU 507 CE1 TYR A 92 12448 14395 10151 -3193 -1299 1586 C
ATOM 508 CE2 TYR A 92 -75.553 65.296 374.821 1.00102.47 C
ANISOU 508 CE2 TYR A 92 12866 15438 10630 -3316 -1503 1589 C
ATOM 509 CZ TYR A 92 -76.887 65.565 374.559 1.00105.85 C
ANISOU 509 CZ TYR A 92 13555 15503 11162 -3273 -1394 1597 C
ATOM 510 OH TYR A 92 -77.754 65.772 375.604 1.00105.50 O
ANISOU 510 OH TYR A 92 13792 15148 11147 -3306 -1383 1600 O
ATOM 511 N ALA A 93 -73.194 61.903 370.932 1.00101.75 N
ANISOU 511 N ALA A 93 11569 16501 10590 -2416 -1596 1386 N
ATOM 512 CA ALA A 93 -73.383 60.451 371.050 1.00101.13 C
ANISOU 512 CA ALA A 93 11479 16366 10578 -1996 -1690 1351 C
ATOM 513 C ALA A 93 -72.193 59.723 371.689 1.00110.17 C
ANISOU 513 C ALA A 93 12393 17856 11609 -1808 -1886 1273 C
ATOM 514 O ALA A 93 -72.384 58.716 372.374 1.00110.06 O
ANISOU 514 O ALA A 93 12514 17698 11605 -1517 -2007 1259 O
ATOM 515 CB ALA A 93 -73.660 59.855 369.685 1.00100.77 C
ANISOU 515 CB ALA A 93 11323 16353 10612 -1792 -1612 1330 C
ATOM 516 N VAL A 94 -70.974 60.232 371.462 1.00110.58 N
ANISOU 516 N VAL A 94 12111 18370 11536 -1975 -1922 1208 N
ATOM 517 CA VAL A 94 -69.729 59.640 371.945 1.00113.53 C
ANISOU 517 CA VAL A 94 12191 19163 11781 -1791 -2116 1096 C
ATOM 518 C VAL A 94 -69.412 60.033 373.389 1.00120.21 C
ANISOU 518 C VAL A 94 13146 19988 12540 -1941 -2235 1108 C
ATOM 519 O VAL A 94 -68.994 59.173 374.166 1.00121.65 O
ANISOU 519 O VAL A 94 13321 20235 12666 -1651 -2431 1052 O
ATOM 520 CB VAL A 94 -68.570 59.966 370.952 1.00119.46 C
ANISOU 520 CB VAL A 94 12478 20486 12425 -1899 -2086 984 C
ATOM 521 CG1 VAL A 94 -67.188 59.840 371.592 1.00122.73 C
ANISOU 521 CG1 VAL A 94 12544 21417 12669 -1856 -2270 844 C
ATOM 522 CG2 VAL A 94 -68.662 59.085 369.715 1.00118.61 C
ANISOU 522 CG2 VAL A 94 12227 20455 12386 -1585 -2048 938 C
ATOM 523 N HIS A 95 -69.605 61.314 373.746 1.00117.29 N
ANISOU 523 N HIS A 95 12907 19512 12144 -2377 -2130 1178 N
ATOM 524 CA HIS A 95 -69.233 61.842 375.064 1.00118.55 C
ANISOU 524 CA HIS A 95 13154 19681 12207 -2578 -2228 1190 C
ATOM 525 C HIS A 95 -70.378 62.056 376.077 1.00119.21 C
ANISOU 525 C HIS A 95 13703 19222 12371 -2646 -2199 1301 C
ATOM 526 O HIS A 95 -70.095 62.184 377.273 1.00118.80 O
ANISOU 526 O HIS A 95 13745 19151 12243 -2720 -2313 1305 O
ATOM 527 CB HIS A 95 -68.453 63.154 374.888 1.00121.43 C
ANISOU 527 CB HIS A 95 13333 20368 12436 -3052 -2150 1170 C
ATOM 528 CG HIS A 95 -67.209 63.005 374.070 1.00127.90 C
ANISOU 528 CG HIS A 95 13664 21794 13138 -3048 -2177 1030 C
ATOM 529 ND1 HIS A 95 -67.146 63.462 372.766 1.00129.89 N
ANISOU 529 ND1 HIS A 95 13780 22185 13386 -3212 -2013 1018 N
ATOM 530 CD2 HIS A 95 -66.027 62.426 374.388 1.00132.79 C
ANISOU 530 CD2 HIS A 95 13908 22914 13631 -2886 -2354 881 C
ATOM 531 CE1 HIS A 95 -65.926 63.171 372.341 1.00132.33 C
ANISOU 531 CE1 HIS A 95 13625 23087 13567 -3176 -2076 861 C
ATOM 532 NE2 HIS A 95 -65.218 62.542 373.281 1.00134.57 N
ANISOU 532 NE2 HIS A 95 13733 23623 13776 -2966 -2285 765 N
ATOM 533 N ASN A 96 -71.647 62.106 375.604 1.00113.13 N
ANISOU 533 N ASN A 96 13204 18038 11742 -2627 -2049 1375 N
ATOM 534 CA ASN A 96 -72.861 62.357 376.402 1.00110.65 C
ANISOU 534 CA ASN A 96 13305 17231 11506 -2703 -1988 1452 C
ATOM 535 C ASN A 96 -72.800 63.730 377.105 1.00113.31 C
ANISOU 535 C ASN A 96 13781 17505 11768 -3117 -1942 1502 C
ATOM 536 O ASN A 96 -73.293 63.908 378.221 1.00111.42 O
ANISOU 536 O ASN A 96 13816 16989 11529 -3191 -1963 1539 O
ATOM 537 CB ASN A 96 -73.182 61.191 377.362 1.00113.30 C
ANISOU 537 CB ASN A 96 13831 17365 11851 -2413 -2121 1441 C
ATOM 538 CG ASN A 96 -74.025 60.107 376.732 1.00135.98 C
ANISOU 538 CG ASN A 96 16812 20024 14830 -2096 -2082 1430 C
ATOM 539 OD1 ASN A 96 -75.129 60.350 376.225 1.00129.89 O
ANISOU 539 OD1 ASN A 96 16197 18984 14172 -2144 -1922 1460 O
ATOM 540 ND2 ASN A 96 -73.535 58.878 376.772 1.00127.49 N
ANISOU 540 ND2 ASN A 96 15676 19060 13705 -1758 -2240 1377 N
ATOM 541 N GLU A 97 -72.183 64.702 376.414 1.00111.26 N
ANISOU 541 N GLU A 97 13347 17502 11423 -3404 -1874 1498 N
ATOM 542 CA GLU A 97 -71.989 66.075 376.870 1.00111.44 C
ANISOU 542 CA GLU A 97 13504 17503 11337 -3831 -1826 1540 C
ATOM 543 C GLU A 97 -72.283 67.035 375.738 1.00113.60 C
ANISOU 543 C GLU A 97 13834 17735 11594 -4066 -1668 1568 C
ATOM 544 O GLU A 97 -71.837 66.799 374.612 1.00115.11 O
ANISOU 544 O GLU A 97 13772 18192 11772 -4020 -1629 1526 O
ATOM 545 CB GLU A 97 -70.552 66.270 377.364 1.00115.94 C
ANISOU 545 CB GLU A 97 13792 18527 11732 -4004 -1950 1482 C
ATOM 546 CG GLU A 97 -70.295 65.614 378.709 1.00127.52 C
ANISOU 546 CG GLU A 97 15277 19993 13181 -3810 -2129 1460 C
ATOM 547 CD GLU A 97 -68.851 65.483 379.146 1.00151.51 C
ANISOU 547 CD GLU A 97 17993 23524 16050 -3897 -2285 1373 C
ATOM 548 OE1 GLU A 97 -67.949 65.992 378.440 1.00145.65 O
ANISOU 548 OE1 GLU A 97 16948 23199 15192 -4125 -2246 1310 O
ATOM 549 OE2 GLU A 97 -68.623 64.856 380.206 1.00146.84 O
ANISOU 549 OE2 GLU A 97 17453 22912 15427 -3739 -2449 1354 O
ATOM 550 N TRP A 98 -73.050 68.101 376.018 1.00107.49 N
ANISOU 550 N TRP A 98 13417 16617 10807 -4302 -1583 1632 N
ATOM 551 CA TRP A 98 -73.380 69.100 375.004 1.00106.77 C
ANISOU 551 CA TRP A 98 13476 16423 10668 -4525 -1454 1660 C
ATOM 552 C TRP A 98 -72.413 70.316 375.062 1.00113.41 C
ANISOU 552 C TRP A 98 14322 17489 11279 -5002 -1442 1670 C
ATOM 553 O TRP A 98 -72.406 71.084 376.032 1.00113.93 O
ANISOU 553 O TRP A 98 14604 17430 11253 -5235 -1473 1705 O
ATOM 554 CB TRP A 98 -74.858 69.495 375.053 1.00102.77 C
ANISOU 554 CB TRP A 98 13366 15413 10268 -4444 -1377 1698 C
ATOM 555 CG TRP A 98 -75.246 70.341 373.889 1.00103.55 C
ANISOU 555 CG TRP A 98 13631 15391 10324 -4576 -1272 1714 C
ATOM 556 CD1 TRP A 98 -75.487 71.681 373.902 1.00107.24 C
ANISOU 556 CD1 TRP A 98 14442 15649 10657 -4873 -1230 1751 C
ATOM 557 CD2 TRP A 98 -75.332 69.928 372.516 1.00102.85 C
ANISOU 557 CD2 TRP A 98 13394 15391 10292 -4426 -1209 1692 C
ATOM 558 NE1 TRP A 98 -75.728 72.130 372.623 1.00107.01 N
ANISOU 558 NE1 TRP A 98 14511 15558 10590 -4912 -1152 1752 N
ATOM 559 CE2 TRP A 98 -75.657 71.071 371.754 1.00107.50 C
ANISOU 559 CE2 TRP A 98 14266 15803 10777 -4644 -1133 1717 C
ATOM 560 CE3 TRP A 98 -75.175 68.698 371.854 1.00103.21 C
ANISOU 560 CE3 TRP A 98 13126 15632 10457 -4120 -1216 1651 C
ATOM 561 CZ2 TRP A 98 -75.823 71.025 370.362 1.00106.34 C
ANISOU 561 CZ2 TRP A 98 14087 15673 10644 -4576 -1062 1705 C
ATOM 562 CZ3 TRP A 98 -75.341 68.655 370.477 1.00104.36 C
ANISOU 562 CZ3 TRP A 98 13220 15805 10627 -4055 -1137 1640 C
ATOM 563 CH2 TRP A 98 -75.662 69.809 369.747 1.00105.32 C
ANISOU 563 CH2 TRP A 98 13617 15752 10647 -4286 -1060 1668 C
ATOM 564 N TYR A 99 -71.592 70.468 374.013 1.00110.21 N
ANISOU 564 N TYR A 99 13685 17425 10766 -5164 -1392 1631 N
ATOM 565 CA TYR A 99 -70.540 71.478 373.934 1.00112.18 C
ANISOU 565 CA TYR A 99 13885 17972 10765 -5650 -1368 1614 C
ATOM 566 C TYR A 99 -70.882 72.810 373.275 1.00114.58 C
ANISOU 566 C TYR A 99 14574 18042 10921 -6017 -1251 1669 C
ATOM 567 O TYR A 99 -70.234 73.811 373.575 1.00117.02 O
ANISOU 567 O TYR A 99 15001 18459 11004 -6466 -1238 1677 O
ATOM 568 CB TYR A 99 -69.322 70.881 373.198 1.00115.71 C
ANISOU 568 CB TYR A 99 13820 19009 11135 -5659 -1380 1507 C
ATOM 569 CG TYR A 99 -68.760 69.618 373.820 1.00118.64 C
ANISOU 569 CG TYR A 99 13807 19674 11595 -5298 -1526 1429 C
ATOM 570 CD1 TYR A 99 -68.336 69.597 375.147 1.00121.84 C
ANISOU 570 CD1 TYR A 99 14188 20155 11951 -5336 -1653 1418 C
ATOM 571 CD2 TYR A 99 -68.596 68.459 373.066 1.00119.13 C
ANISOU 571 CD2 TYR A 99 13549 19947 11768 -4919 -1549 1359 C
ATOM 572 CE1 TYR A 99 -67.806 68.442 375.722 1.00123.26 C
ANISOU 572 CE1 TYR A 99 14062 20586 12186 -4981 -1813 1340 C
ATOM 573 CE2 TYR A 99 -68.061 67.298 373.630 1.00120.61 C
ANISOU 573 CE2 TYR A 99 13434 20386 12007 -4559 -1707 1279 C
ATOM 574 CZ TYR A 99 -67.663 67.296 374.957 1.00128.35 C
ANISOU 574 CZ TYR A 99 14418 21420 12929 -4587 -1844 1268 C
ATOM 575 OH TYR A 99 -67.127 66.163 375.521 1.00129.11 O
ANISOU 575 OH TYR A 99 14263 21743 13051 -4212 -2024 1183 O
ATOM 576 N TYR A 100 -71.880 72.824 372.398 1.00107.58 N
ANISOU 576 N TYR A 100 13901 16832 10141 -5830 -1178 1700 N
ATOM 577 CA TYR A 100 -72.222 73.898 371.474 1.00107.38 C
ANISOU 577 CA TYR A 100 14232 16589 9979 -6082 -1082 1736 C
ATOM 578 C TYR A 100 -73.317 74.915 371.912 1.00108.77 C
ANISOU 578 C TYR A 100 14985 16217 10124 -6139 -1079 1803 C
ATOM 579 O TYR A 100 -73.772 75.714 371.080 1.00108.32 O
ANISOU 579 O TYR A 100 15275 15919 9963 -6259 -1022 1827 O
ATOM 580 CB TYR A 100 -72.597 73.239 370.133 1.00107.67 C
ANISOU 580 CB TYR A 100 14130 16636 10142 -5802 -1020 1712 C
ATOM 581 CG TYR A 100 -71.694 72.061 369.812 1.00110.82 C
ANISOU 581 CG TYR A 100 13969 17532 10607 -5632 -1041 1634 C
ATOM 582 CD1 TYR A 100 -70.455 72.251 369.206 1.00115.59 C
ANISOU 582 CD1 TYR A 100 14289 18614 11016 -5949 -996 1569 C
ATOM 583 CD2 TYR A 100 -72.037 70.765 370.205 1.00110.05 C
ANISOU 583 CD2 TYR A 100 13633 17442 10738 -5167 -1115 1610 C
ATOM 584 CE1 TYR A 100 -69.601 71.179 368.951 1.00117.30 C
ANISOU 584 CE1 TYR A 100 13971 19319 11277 -5762 -1031 1470 C
ATOM 585 CE2 TYR A 100 -71.181 69.687 369.971 1.00112.00 C
ANISOU 585 CE2 TYR A 100 13400 18133 11020 -4977 -1161 1528 C
ATOM 586 CZ TYR A 100 -69.970 69.899 369.330 1.00123.23 C
ANISOU 586 CZ TYR A 100 14518 20042 12260 -5253 -1123 1453 C
ATOM 587 OH TYR A 100 -69.126 68.846 369.074 1.00126.14 O
ANISOU 587 OH TYR A 100 14399 20876 12653 -5033 -1178 1347 O
ATOM 588 N GLY A 101 -73.667 74.936 373.194 1.00103.83 N
ANISOU 588 N GLY A 101 14476 15414 9561 -6069 -1147 1823 N
ATOM 589 CA GLY A 101 -74.636 75.892 373.724 1.00103.82 C
ANISOU 589 CA GLY A 101 14992 14935 9518 -6111 -1153 1864 C
ATOM 590 C GLY A 101 -76.094 75.671 373.361 1.00108.94 C
ANISOU 590 C GLY A 101 15852 15187 10355 -5710 -1136 1847 C
ATOM 591 O GLY A 101 -76.420 74.794 372.554 1.00107.51 O
ANISOU 591 O GLY A 101 15444 15068 10336 -5410 -1107 1814 O
ATOM 592 N LEU A 102 -76.985 76.495 373.956 1.00107.47 N
ANISOU 592 N LEU A 102 16100 14600 10132 -5702 -1158 1854 N
ATOM 593 CA LEU A 102 -78.445 76.432 373.819 1.00106.40 C
ANISOU 593 CA LEU A 102 16182 14094 10150 -5331 -1153 1804 C
ATOM 594 C LEU A 102 -78.956 76.705 372.388 1.00111.48 C
ANISOU 594 C LEU A 102 16987 14601 10771 -5218 -1116 1783 C
ATOM 595 O LEU A 102 -79.908 76.037 371.964 1.00110.13 O
ANISOU 595 O LEU A 102 16735 14317 10793 -4838 -1101 1722 O
ATOM 596 CB LEU A 102 -79.119 77.347 374.868 1.00107.09 C
ANISOU 596 CB LEU A 102 16682 13840 10166 -5375 -1194 1795 C
ATOM 597 CG LEU A 102 -80.245 78.287 374.437 1.00113.21 C
ANISOU 597 CG LEU A 102 17957 14208 10850 -5280 -1208 1754 C
ATOM 598 CD1 LEU A 102 -81.364 78.298 375.455 1.00112.38 C
ANISOU 598 CD1 LEU A 102 18025 13831 10844 -5041 -1236 1678 C
ATOM 599 CD2 LEU A 102 -79.710 79.702 374.140 1.00120.04 C
ANISOU 599 CD2 LEU A 102 19247 14970 11391 -5700 -1230 1819 C
ATOM 600 N PHE A 103 -78.352 77.669 371.653 1.00109.67 N
ANISOU 600 N PHE A 103 16998 14379 10293 -5556 -1102 1826 N
ATOM 601 CA PHE A 103 -78.798 77.945 370.287 1.00108.70 C
ANISOU 601 CA PHE A 103 17066 14111 10125 -5460 -1077 1809 C
ATOM 602 C PHE A 103 -78.583 76.728 369.378 1.00111.70 C
ANISOU 602 C PHE A 103 16976 14779 10687 -5247 -1023 1788 C
ATOM 603 O PHE A 103 -79.540 76.268 368.743 1.00109.88 O
ANISOU 603 O PHE A 103 16742 14394 10613 -4886 -1017 1738 O
ATOM 604 CB PHE A 103 -78.174 79.223 369.685 1.00112.62 C
ANISOU 604 CB PHE A 103 17980 14531 10280 -5903 -1070 1860 C
ATOM 605 CG PHE A 103 -78.529 79.370 368.219 1.00113.83 C
ANISOU 605 CG PHE A 103 18304 14565 10383 -5804 -1047 1844 C
ATOM 606 CD1 PHE A 103 -79.807 79.765 367.832 1.00115.77 C
ANISOU 606 CD1 PHE A 103 18931 14398 10660 -5472 -1104 1792 C
ATOM 607 CD2 PHE A 103 -77.623 79.009 367.227 1.00116.21 C
ANISOU 607 CD2 PHE A 103 18343 15190 10620 -6001 -972 1861 C
ATOM 608 CE1 PHE A 103 -80.161 79.820 366.480 1.00116.53 C
ANISOU 608 CE1 PHE A 103 19172 14386 10719 -5344 -1096 1771 C
ATOM 609 CE2 PHE A 103 -77.978 79.068 365.877 1.00118.92 C
ANISOU 609 CE2 PHE A 103 18838 15419 10927 -5895 -949 1847 C
ATOM 610 CZ PHE A 103 -79.243 79.476 365.513 1.00116.18 C
ANISOU 610 CZ PHE A 103 18896 14639 10610 -5567 -1016 1808 C
ATOM 611 N TYR A 104 -77.339 76.200 369.332 1.00108.93 N
ANISOU 611 N TYR A 104 16225 14858 10305 -5458 -991 1813 N
ATOM 612 CA TYR A 104 -77.029 75.041 368.502 1.00107.54 C
ANISOU 612 CA TYR A 104 15601 14979 10280 -5258 -948 1786 C
ATOM 613 C TYR A 104 -77.721 73.757 368.991 1.00110.16 C
ANISOU 613 C TYR A 104 15645 15302 10907 -4805 -970 1745 C
ATOM 614 O TYR A 104 -77.865 72.814 368.213 1.00109.16 O
ANISOU 614 O TYR A 104 15260 15289 10925 -4547 -940 1716 O
ATOM 615 CB TYR A 104 -75.527 74.841 368.291 1.00109.76 C
ANISOU 615 CB TYR A 104 15525 15750 10429 -5578 -916 1790 C
ATOM 616 CG TYR A 104 -75.259 74.377 366.879 1.00110.81 C
ANISOU 616 CG TYR A 104 15457 16078 10569 -5524 -849 1765 C
ATOM 617 CD1 TYR A 104 -75.277 75.276 365.815 1.00113.72 C
ANISOU 617 CD1 TYR A 104 16158 16312 10738 -5762 -796 1782 C
ATOM 618 CD2 TYR A 104 -75.102 73.025 366.587 1.00110.11 C
ANISOU 618 CD2 TYR A 104 14898 16254 10683 -5203 -844 1724 C
ATOM 619 CE1 TYR A 104 -75.095 74.848 364.502 1.00113.04 C
ANISOU 619 CE1 TYR A 104 15909 16383 10659 -5707 -730 1758 C
ATOM 620 CE2 TYR A 104 -74.925 72.585 365.275 1.00110.82 C
ANISOU 620 CE2 TYR A 104 14815 16504 10787 -5129 -780 1698 C
ATOM 621 CZ TYR A 104 -74.910 73.503 364.238 1.00116.61 C
ANISOU 621 CZ TYR A 104 15855 17125 11326 -5391 -719 1715 C
ATOM 622 OH TYR A 104 -74.720 73.080 362.950 1.00117.06 O
ANISOU 622 OH TYR A 104 15752 17340 11387 -5336 -651 1688 O
ATOM 623 N CYS A 105 -78.206 73.750 370.244 1.00106.05 N
ANISOU 623 N CYS A 105 15212 14623 10458 -4723 -1018 1739 N
ATOM 624 CA CYS A 105 -79.000 72.653 370.794 1.00103.95 C
ANISOU 624 CA CYS A 105 14774 14290 10433 -4343 -1031 1692 C
ATOM 625 C CYS A 105 -80.359 72.709 370.081 1.00104.57 C
ANISOU 625 C CYS A 105 15056 14061 10616 -4053 -1003 1634 C
ATOM 626 O CYS A 105 -80.768 71.715 369.494 1.00102.86 O
ANISOU 626 O CYS A 105 14620 13897 10564 -3766 -974 1593 O
ATOM 627 CB CYS A 105 -79.135 72.785 372.313 1.00104.63 C
ANISOU 627 CB CYS A 105 14956 14275 10525 -4395 -1080 1695 C
ATOM 628 SG CYS A 105 -80.400 71.719 373.057 1.00106.39 S
ANISOU 628 SG CYS A 105 15121 14312 10989 -3993 -1078 1619 S
ATOM 629 N LYS A 106 -81.000 73.893 370.047 1.00100.87 N
ANISOU 629 N LYS A 106 15014 13284 10027 -4127 -1019 1621 N
ATOM 630 CA LYS A 106 -82.272 74.111 369.353 1.00 99.63 C
ANISOU 630 CA LYS A 106 15081 12844 9931 -3847 -1016 1542 C
ATOM 631 C LYS A 106 -82.110 73.864 367.846 1.00104.38 C
ANISOU 631 C LYS A 106 15590 13536 10533 -3781 -981 1550 C
ATOM 632 O LYS A 106 -82.940 73.169 367.253 1.00103.65 O
ANISOU 632 O LYS A 106 15384 13395 10604 -3455 -961 1481 O
ATOM 633 CB LYS A 106 -82.803 75.534 369.603 1.00102.99 C
ANISOU 633 CB LYS A 106 16020 12936 10174 -3950 -1070 1524 C
ATOM 634 CG LYS A 106 -83.236 75.799 371.042 1.00109.11 C
ANISOU 634 CG LYS A 106 16920 13570 10967 -3942 -1102 1487 C
ATOM 635 CD LYS A 106 -83.853 77.185 371.201 1.00110.61 C
ANISOU 635 CD LYS A 106 17639 13413 10974 -3977 -1166 1447 C
ATOM 636 CE LYS A 106 -84.515 77.363 372.547 1.00111.30 C
ANISOU 636 CE LYS A 106 17834 13352 11104 -3893 -1190 1377 C
ATOM 637 NZ LYS A 106 -85.990 77.177 372.478 1.00109.72 N
ANISOU 637 NZ LYS A 106 17670 12981 11037 -3483 -1196 1209 N
ATOM 638 N PHE A 107 -81.014 74.389 367.246 1.00101.14 N
ANISOU 638 N PHE A 107 15213 13282 9933 -4111 -966 1626 N
ATOM 639 CA PHE A 107 -80.729 74.249 365.819 1.00100.65 C
ANISOU 639 CA PHE A 107 15087 13322 9833 -4114 -924 1637 C
ATOM 640 C PHE A 107 -80.489 72.805 365.350 1.00104.49 C
ANISOU 640 C PHE A 107 15077 14103 10522 -3890 -877 1621 C
ATOM 641 O PHE A 107 -81.036 72.434 364.314 1.00104.18 O
ANISOU 641 O PHE A 107 15009 14009 10564 -3666 -852 1588 O
ATOM 642 CB PHE A 107 -79.567 75.158 365.379 1.00104.25 C
ANISOU 642 CB PHE A 107 15701 13904 10006 -4582 -902 1705 C
ATOM 643 CG PHE A 107 -79.403 75.207 363.880 1.00105.52 C
ANISOU 643 CG PHE A 107 15903 14102 10086 -4613 -856 1708 C
ATOM 644 CD1 PHE A 107 -80.209 76.031 363.103 1.00108.13 C
ANISOU 644 CD1 PHE A 107 16703 14074 10309 -4539 -891 1690 C
ATOM 645 CD2 PHE A 107 -78.478 74.391 363.237 1.00107.21 C
ANISOU 645 CD2 PHE A 107 15692 14713 10331 -4687 -788 1716 C
ATOM 646 CE1 PHE A 107 -80.078 76.051 361.711 1.00108.98 C
ANISOU 646 CE1 PHE A 107 16873 14200 10336 -4567 -853 1694 C
ATOM 647 CE2 PHE A 107 -78.346 74.416 361.843 1.00109.83 C
ANISOU 647 CE2 PHE A 107 16063 15081 10586 -4722 -737 1714 C
ATOM 648 CZ PHE A 107 -79.143 75.249 361.093 1.00107.91 C
ANISOU 648 CZ PHE A 107 16307 14461 10233 -4676 -767 1710 C
ATOM 649 N HIS A 108 -79.668 72.010 366.067 1.00101.24 N
ANISOU 649 N HIS A 108 14301 13993 10172 -3940 -876 1640 N
ATOM 650 CA HIS A 108 -79.354 70.626 365.672 1.00100.28 C
ANISOU 650 CA HIS A 108 13742 14146 10212 -3715 -851 1621 C
ATOM 651 C HIS A 108 -80.564 69.663 365.775 1.00101.95 C
ANISOU 651 C HIS A 108 13892 14186 10657 -3297 -851 1561 C
ATOM 652 O HIS A 108 -80.498 68.522 365.286 1.00100.74 O
ANISOU 652 O HIS A 108 13451 14194 10630 -3078 -830 1541 O
ATOM 653 CB HIS A 108 -78.132 70.097 366.446 1.00102.04 C
ANISOU 653 CB HIS A 108 13636 14731 10404 -3855 -880 1641 C
ATOM 654 CG HIS A 108 -78.445 69.201 367.614 1.00103.87 C
ANISOU 654 CG HIS A 108 13736 14941 10789 -3631 -931 1621 C
ATOM 655 ND1 HIS A 108 -77.983 67.896 367.664 1.00105.08 N
ANISOU 655 ND1 HIS A 108 13535 15340 11049 -3413 -955 1598 N
ATOM 656 CD2 HIS A 108 -79.141 69.460 368.746 1.00104.62 C
ANISOU 656 CD2 HIS A 108 14039 14793 10919 -3610 -964 1615 C
ATOM 657 CE1 HIS A 108 -78.422 67.404 368.813 1.00103.47 C
ANISOU 657 CE1 HIS A 108 13366 15015 10932 -3281 -1003 1587 C
ATOM 658 NE2 HIS A 108 -79.126 68.309 369.496 1.00103.48 N
ANISOU 658 NE2 HIS A 108 13684 14734 10899 -3402 -1001 1594 N
ATOM 659 N ASN A 109 -81.642 70.118 366.442 1.00 96.62 N
ANISOU 659 N ASN A 109 13487 13202 10021 -3203 -872 1518 N
ATOM 660 CA ASN A 109 -82.878 69.356 366.594 1.00 93.49 C
ANISOU 660 CA ASN A 109 13061 12650 9812 -2864 -859 1433 C
ATOM 661 C ASN A 109 -83.945 69.820 365.610 1.00 96.60 C
ANISOU 661 C ASN A 109 13667 12815 10220 -2689 -847 1365 C
ATOM 662 O ASN A 109 -84.858 69.065 365.292 1.00 95.57 O
ANISOU 662 O ASN A 109 13438 12636 10239 -2407 -820 1284 O
ATOM 663 CB ASN A 109 -83.383 69.391 368.035 1.00 89.26 C
ANISOU 663 CB ASN A 109 12620 11983 9312 -2857 -883 1396 C
ATOM 664 CG ASN A 109 -82.651 68.438 368.956 1.00104.06 C
ANISOU 664 CG ASN A 109 14245 14063 11230 -2888 -902 1433 C
ATOM 665 OD1 ASN A 109 -82.206 67.352 368.557 1.00 87.84 O
ANISOU 665 OD1 ASN A 109 11917 12209 9250 -2761 -896 1444 O
ATOM 666 ND2 ASN A 109 -82.522 68.811 370.225 1.00101.19 N
ANISOU 666 ND2 ASN A 109 13994 13643 10812 -3038 -938 1447 N
ATOM 667 N PHE A 110 -83.816 71.053 365.116 1.00 93.37 N
ANISOU 667 N PHE A 110 13568 12270 9640 -2860 -873 1391 N
ATOM 668 CA PHE A 110 -84.741 71.651 364.167 1.00 92.68 C
ANISOU 668 CA PHE A 110 13750 11945 9520 -2697 -893 1325 C
ATOM 669 C PHE A 110 -84.334 71.291 362.740 1.00 97.10 C
ANISOU 669 C PHE A 110 14189 12631 10074 -2672 -857 1359 C
ATOM 670 O PHE A 110 -85.144 70.728 362.003 1.00 95.96 O
ANISOU 670 O PHE A 110 13969 12437 10055 -2385 -843 1287 O
ATOM 671 CB PHE A 110 -84.763 73.184 364.373 1.00 96.17 C
ANISOU 671 CB PHE A 110 14661 12142 9738 -2897 -958 1340 C
ATOM 672 CG PHE A 110 -85.448 74.017 363.313 1.00 98.32 C
ANISOU 672 CG PHE A 110 15302 12158 9898 -2778 -1010 1289 C
ATOM 673 CD1 PHE A 110 -86.764 74.429 363.473 1.00100.89 C
ANISOU 673 CD1 PHE A 110 15857 12223 10255 -2480 -1076 1153 C
ATOM 674 CD2 PHE A 110 -84.755 74.442 362.181 1.00100.95 C
ANISOU 674 CD2 PHE A 110 15775 12514 10066 -2974 -1002 1364 C
ATOM 675 CE1 PHE A 110 -87.390 75.217 362.499 1.00102.40 C
ANISOU 675 CE1 PHE A 110 16414 12170 10323 -2332 -1154 1093 C
ATOM 676 CE2 PHE A 110 -85.385 75.216 361.206 1.00104.17 C
ANISOU 676 CE2 PHE A 110 16577 12656 10348 -2857 -1067 1319 C
ATOM 677 CZ PHE A 110 -86.698 75.599 361.372 1.00101.97 C
ANISOU 677 CZ PHE A 110 16531 12107 10107 -2518 -1153 1185 C
ATOM 678 N PHE A 111 -83.083 71.630 362.347 1.00 95.10 N
ANISOU 678 N PHE A 111 13914 12556 9663 -2990 -835 1456 N
ATOM 679 CA PHE A 111 -82.584 71.451 360.987 1.00 95.22 C
ANISOU 679 CA PHE A 111 13850 12701 9628 -3033 -792 1486 C
ATOM 680 C PHE A 111 -82.748 70.029 360.372 1.00 98.75 C
ANISOU 680 C PHE A 111 13902 13333 10284 -2744 -743 1456 C
ATOM 681 O PHE A 111 -83.179 70.002 359.218 1.00 98.92 O
ANISOU 681 O PHE A 111 13996 13275 10315 -2608 -731 1431 O
ATOM 682 CB PHE A 111 -81.141 71.930 360.820 1.00 98.68 C
ANISOU 682 CB PHE A 111 14258 13380 9857 -3460 -758 1569 C
ATOM 683 CG PHE A 111 -80.854 72.183 359.359 1.00101.12 C
ANISOU 683 CG PHE A 111 14665 13716 10041 -3560 -717 1585 C
ATOM 684 CD1 PHE A 111 -81.470 73.233 358.683 1.00104.80 C
ANISOU 684 CD1 PHE A 111 15627 13849 10344 -3600 -758 1578 C
ATOM 685 CD2 PHE A 111 -80.027 71.331 358.639 1.00103.07 C
ANISOU 685 CD2 PHE A 111 14526 14307 10329 -3581 -645 1595 C
ATOM 686 CE1 PHE A 111 -81.253 73.432 357.316 1.00106.31 C
ANISOU 686 CE1 PHE A 111 15943 14041 10410 -3690 -723 1592 C
ATOM 687 CE2 PHE A 111 -79.806 71.537 357.274 1.00106.55 C
ANISOU 687 CE2 PHE A 111 15061 14771 10653 -3676 -598 1602 C
ATOM 688 CZ PHE A 111 -80.423 72.585 356.623 1.00105.20 C
ANISOU 688 CZ PHE A 111 15401 14254 10317 -3742 -634 1606 C
ATOM 689 N PRO A 112 -82.452 68.864 361.027 1.00 94.01 N
ANISOU 689 N PRO A 112 12933 12953 9835 -2637 -724 1455 N
ATOM 690 CA PRO A 112 -82.629 67.573 360.329 1.00 92.27 C
ANISOU 690 CA PRO A 112 12412 12870 9777 -2365 -686 1426 C
ATOM 691 C PRO A 112 -84.048 67.297 359.821 1.00 94.59 C
ANISOU 691 C PRO A 112 12809 12929 10203 -2045 -684 1340 C
ATOM 692 O PRO A 112 -84.185 66.792 358.708 1.00 94.18 O
ANISOU 692 O PRO A 112 12660 12925 10201 -1902 -653 1327 O
ATOM 693 CB PRO A 112 -82.160 66.540 361.358 1.00 93.11 C
ANISOU 693 CB PRO A 112 12227 13172 9979 -2308 -696 1433 C
ATOM 694 CG PRO A 112 -81.272 67.283 362.252 1.00 98.73 C
ANISOU 694 CG PRO A 112 12990 13974 10548 -2617 -727 1484 C
ATOM 695 CD PRO A 112 -81.900 68.639 362.376 1.00 95.10 C
ANISOU 695 CD PRO A 112 12937 13216 9979 -2752 -748 1480 C
ATOM 696 N ILE A 113 -85.095 67.681 360.591 1.00 89.65 N
ANISOU 696 N ILE A 113 12377 12069 9617 -1943 -719 1266 N
ATOM 697 CA ILE A 113 -86.503 67.497 360.192 1.00 87.52 C
ANISOU 697 CA ILE A 113 12189 11612 9454 -1645 -723 1145 C
ATOM 698 C ILE A 113 -86.809 68.292 358.925 1.00 92.06 C
ANISOU 698 C ILE A 113 13007 12038 9932 -1605 -752 1130 C
ATOM 699 O ILE A 113 -87.398 67.737 357.992 1.00 90.67 O
ANISOU 699 O ILE A 113 12752 11856 9844 -1382 -735 1073 O
ATOM 700 CB ILE A 113 -87.502 67.784 361.351 1.00 89.26 C
ANISOU 700 CB ILE A 113 12536 11663 9714 -1562 -749 1041 C
ATOM 701 CG1 ILE A 113 -87.291 66.779 362.497 1.00 87.58 C
ANISOU 701 CG1 ILE A 113 12088 11587 9602 -1578 -714 1049 C
ATOM 702 CG2 ILE A 113 -88.973 67.789 360.853 1.00 88.47 C
ANISOU 702 CG2 ILE A 113 12523 11404 9689 -1265 -762 878 C
ATOM 703 CD1 ILE A 113 -87.902 67.155 363.753 1.00 89.24 C
ANISOU 703 CD1 ILE A 113 12426 11675 9805 -1614 -731 983 C
ATOM 704 N ALA A 114 -86.362 69.570 358.884 1.00 90.61 N
ANISOU 704 N ALA A 114 13142 11735 9550 -1836 -799 1183 N
ATOM 705 CA ALA A 114 -86.535 70.475 357.743 1.00 91.72 C
ANISOU 705 CA ALA A 114 13614 11696 9541 -1846 -844 1180 C
ATOM 706 C ALA A 114 -85.780 69.975 356.509 1.00 96.53 C
ANISOU 706 C ALA A 114 14060 12487 10131 -1917 -783 1251 C
ATOM 707 O ALA A 114 -86.347 69.962 355.408 1.00 96.51 O
ANISOU 707 O ALA A 114 14159 12379 10133 -1739 -799 1207 O
ATOM 708 CB ALA A 114 -86.084 71.885 358.107 1.00 94.40 C
ANISOU 708 CB ALA A 114 14361 11869 9636 -2135 -903 1233 C
ATOM 709 N ALA A 115 -84.514 69.540 356.696 1.00 93.25 N
ANISOU 709 N ALA A 115 13375 12361 9693 -2159 -718 1344 N
ATOM 710 CA ALA A 115 -83.673 69.038 355.605 1.00 93.47 C
ANISOU 710 CA ALA A 115 13201 12621 9693 -2246 -650 1395 C
ATOM 711 C ALA A 115 -84.174 67.707 355.038 1.00 93.74 C
ANISOU 711 C ALA A 115 12927 12750 9939 -1912 -613 1348 C
ATOM 712 O ALA A 115 -84.122 67.528 353.823 1.00 92.08 O
ANISOU 712 O ALA A 115 12708 12570 9710 -1865 -584 1353 O
ATOM 713 CB ALA A 115 -82.221 68.931 356.050 1.00 95.54 C
ANISOU 713 CB ALA A 115 13227 13208 9865 -2565 -602 1469 C
ATOM 714 N VAL A 116 -84.683 66.786 355.904 1.00 88.71 N
ANISOU 714 N VAL A 116 12072 12147 9486 -1700 -614 1301 N
ATOM 715 CA VAL A 116 -85.227 65.505 355.431 1.00 86.62 C
ANISOU 715 CA VAL A 116 11561 11949 9402 -1403 -579 1251 C
ATOM 716 C VAL A 116 -86.567 65.747 354.710 1.00 90.15 C
ANISOU 716 C VAL A 116 12207 12151 9896 -1162 -608 1154 C
ATOM 717 O VAL A 116 -86.746 65.206 353.619 1.00 90.19 O
ANISOU 717 O VAL A 116 12123 12192 9953 -1014 -581 1139 O
ATOM 718 CB VAL A 116 -85.283 64.362 356.478 1.00 88.96 C
ANISOU 718 CB VAL A 116 11601 12360 9840 -1285 -565 1230 C
ATOM 719 CG1 VAL A 116 -85.814 63.079 355.856 1.00 87.60 C
ANISOU 719 CG1 VAL A 116 11237 12232 9814 -1010 -528 1180 C
ATOM 720 CG2 VAL A 116 -83.909 64.095 357.066 1.00 89.54 C
ANISOU 720 CG2 VAL A 116 11468 12700 9854 -1478 -560 1312 C
ATOM 721 N PHE A 117 -87.462 66.609 355.255 1.00 86.22 N
ANISOU 721 N PHE A 117 11982 11416 9361 -1116 -673 1078 N
ATOM 722 CA PHE A 117 -88.728 66.938 354.574 1.00 85.64 C
ANISOU 722 CA PHE A 117 12100 11131 9307 -861 -727 956 C
ATOM 723 C PHE A 117 -88.447 67.474 353.169 1.00 90.48 C
ANISOU 723 C PHE A 117 12909 11676 9794 -900 -747 1002 C
ATOM 724 O PHE A 117 -89.047 66.990 352.218 1.00 90.20 O
ANISOU 724 O PHE A 117 12822 11620 9829 -681 -746 943 O
ATOM 725 CB PHE A 117 -89.572 67.958 355.370 1.00 87.72 C
ANISOU 725 CB PHE A 117 12651 11169 9508 -809 -812 857 C
ATOM 726 CG PHE A 117 -90.949 68.258 354.805 1.00 88.70 C
ANISOU 726 CG PHE A 117 12933 11116 9654 -491 -886 687 C
ATOM 727 CD1 PHE A 117 -92.074 67.602 355.287 1.00 90.52 C
ANISOU 727 CD1 PHE A 117 12975 11384 10034 -254 -870 523 C
ATOM 728 CD2 PHE A 117 -91.122 69.221 353.816 1.00 92.07 C
ANISOU 728 CD2 PHE A 117 13710 11345 9927 -438 -979 674 C
ATOM 729 CE1 PHE A 117 -93.350 67.905 354.792 1.00 91.54 C
ANISOU 729 CE1 PHE A 117 13213 11397 10170 47 -947 333 C
ATOM 730 CE2 PHE A 117 -92.395 69.514 353.312 1.00 94.74 C
ANISOU 730 CE2 PHE A 117 14193 11532 10272 -105 -1074 496 C
ATOM 731 CZ PHE A 117 -93.501 68.856 353.805 1.00 91.60 C
ANISOU 731 CZ PHE A 117 13553 11215 10034 143 -1058 318 C
ATOM 732 N ALA A 118 -87.524 68.450 353.046 1.00 88.62 N
ANISOU 732 N ALA A 118 12905 11408 9357 -1201 -762 1102 N
ATOM 733 CA ALA A 118 -87.136 69.066 351.779 1.00 89.89 C
ANISOU 733 CA ALA A 118 13314 11495 9346 -1320 -773 1153 C
ATOM 734 C ALA A 118 -86.579 68.052 350.778 1.00 93.06 C
ANISOU 734 C ALA A 118 13410 12125 9822 -1301 -682 1198 C
ATOM 735 O ALA A 118 -86.947 68.116 349.614 1.00 93.45 O
ANISOU 735 O ALA A 118 13598 12075 9834 -1189 -700 1176 O
ATOM 736 CB ALA A 118 -86.135 70.183 352.019 1.00 92.88 C
ANISOU 736 CB ALA A 118 13961 11849 9479 -1723 -778 1250 C
ATOM 737 N SER A 119 -85.752 67.090 351.235 1.00 88.60 N
ANISOU 737 N SER A 119 12444 11860 9359 -1375 -598 1249 N
ATOM 738 CA SER A 119 -85.163 66.032 350.405 1.00 87.90 C
ANISOU 738 CA SER A 119 12037 12019 9342 -1331 -516 1281 C
ATOM 739 C SER A 119 -86.231 65.097 349.798 1.00 89.66 C
ANISOU 739 C SER A 119 12142 12178 9745 -964 -517 1201 C
ATOM 740 O SER A 119 -86.276 64.906 348.572 1.00 88.63 O
ANISOU 740 O SER A 119 12026 12050 9599 -894 -496 1203 O
ATOM 741 CB SER A 119 -84.180 65.200 351.229 1.00 91.58 C
ANISOU 741 CB SER A 119 12130 12797 9869 -1427 -463 1326 C
ATOM 742 OG SER A 119 -83.123 65.997 351.732 1.00105.74 O
ANISOU 742 OG SER A 119 13986 14697 11492 -1778 -458 1386 O
ATOM 743 N ILE A 120 -87.075 64.503 350.670 1.00 83.80 N
ANISOU 743 N ILE A 120 11284 11393 9162 -756 -535 1125 N
ATOM 744 CA ILE A 120 -88.093 63.549 350.255 1.00 81.57 C
ANISOU 744 CA ILE A 120 10870 11082 9040 -449 -524 1034 C
ATOM 745 C ILE A 120 -89.196 64.212 349.391 1.00 86.47 C
ANISOU 745 C ILE A 120 11759 11468 9629 -270 -594 938 C
ATOM 746 O ILE A 120 -89.694 63.560 348.474 1.00 85.38 O
ANISOU 746 O ILE A 120 11534 11339 9566 -76 -578 891 O
ATOM 747 CB ILE A 120 -88.635 62.728 351.467 1.00 82.59 C
ANISOU 747 CB ILE A 120 10817 11253 9312 -338 -508 969 C
ATOM 748 CG1 ILE A 120 -89.383 61.429 351.030 1.00 80.84 C
ANISOU 748 CG1 ILE A 120 10400 11079 9235 -90 -465 894 C
ATOM 749 CG2 ILE A 120 -89.474 63.566 352.422 1.00 83.17 C
ANISOU 749 CG2 ILE A 120 11085 11148 9369 -325 -569 879 C
ATOM 750 CD1 ILE A 120 -88.664 60.468 350.016 1.00 75.98 C
ANISOU 750 CD1 ILE A 120 9593 10633 8643 -48 -408 967 C
ATOM 751 N TRP A 121 -89.536 65.494 349.642 1.00 84.54 N
ANISOU 751 N TRP A 121 11851 11012 9257 -323 -682 905 N
ATOM 752 CA TRP A 121 -90.569 66.169 348.849 1.00 84.86 C
ANISOU 752 CA TRP A 121 12178 10822 9242 -112 -781 797 C
ATOM 753 C TRP A 121 -90.012 66.716 347.539 1.00 89.71 C
ANISOU 753 C TRP A 121 13032 11359 9694 -219 -798 876 C
ATOM 754 O TRP A 121 -90.780 66.900 346.597 1.00 90.21 O
ANISOU 754 O TRP A 121 13278 11269 9730 -9 -871 796 O
ATOM 755 CB TRP A 121 -91.352 67.209 349.664 1.00 84.32 C
ANISOU 755 CB TRP A 121 12384 10547 9106 -38 -890 690 C
ATOM 756 CG TRP A 121 -92.293 66.536 350.623 1.00 83.97 C
ANISOU 756 CG TRP A 121 12097 10576 9233 150 -871 550 C
ATOM 757 CD1 TRP A 121 -92.059 66.261 351.938 1.00 86.14 C
ANISOU 757 CD1 TRP A 121 12213 10948 9569 27 -819 566 C
ATOM 758 CD2 TRP A 121 -93.533 65.887 350.292 1.00 83.03 C
ANISOU 758 CD2 TRP A 121 11830 10479 9238 457 -882 373 C
ATOM 759 NE1 TRP A 121 -93.108 65.545 352.467 1.00 84.52 N
ANISOU 759 NE1 TRP A 121 11808 10802 9503 222 -795 408 N
ATOM 760 CE2 TRP A 121 -94.027 65.298 351.478 1.00 85.93 C
ANISOU 760 CE2 TRP A 121 11974 10952 9722 480 -828 281 C
ATOM 761 CE3 TRP A 121 -94.288 65.763 349.110 1.00 84.12 C
ANISOU 761 CE3 TRP A 121 12011 10564 9387 703 -933 273 C
ATOM 762 CZ2 TRP A 121 -95.245 64.604 351.521 1.00 84.51 C
ANISOU 762 CZ2 TRP A 121 11607 10845 9657 709 -811 84 C
ATOM 763 CZ3 TRP A 121 -95.495 65.082 349.155 1.00 84.67 C
ANISOU 763 CZ3 TRP A 121 11877 10712 9581 955 -928 77 C
ATOM 764 CH2 TRP A 121 -95.956 64.501 350.345 1.00 84.54 C
ANISOU 764 CH2 TRP A 121 11630 10821 9669 941 -860 -19 C
ATOM 765 N SER A 122 -88.679 66.885 347.438 1.00 86.23 N
ANISOU 765 N SER A 122 12566 11053 9144 -546 -725 1020 N
ATOM 766 CA SER A 122 -88.040 67.261 346.176 1.00 86.81 C
ANISOU 766 CA SER A 122 12824 11105 9053 -704 -707 1093 C
ATOM 767 C SER A 122 -88.055 66.016 345.282 1.00 90.62 C
ANISOU 767 C SER A 122 12984 11764 9683 -539 -628 1090 C
ATOM 768 O SER A 122 -88.324 66.138 344.090 1.00 90.97 O
ANISOU 768 O SER A 122 13193 11709 9664 -464 -649 1079 O
ATOM 769 CB SER A 122 -86.615 67.743 346.404 1.00 90.08 C
ANISOU 769 CB SER A 122 13265 11668 9295 -1132 -637 1215 C
ATOM 770 OG SER A 122 -86.637 68.979 347.097 1.00 95.77 O
ANISOU 770 OG SER A 122 14368 12181 9841 -1303 -717 1221 O
ATOM 771 N MET A 123 -87.838 64.812 345.883 1.00 87.03 N
ANISOU 771 N MET A 123 12106 11546 9414 -465 -550 1094 N
ATOM 772 CA MET A 123 -87.914 63.506 345.211 1.00 85.81 C
ANISOU 772 CA MET A 123 11646 11551 9405 -282 -481 1084 C
ATOM 773 C MET A 123 -89.356 63.277 344.682 1.00 89.38 C
ANISOU 773 C MET A 123 12178 11825 9956 50 -545 958 C
ATOM 774 O MET A 123 -89.515 62.798 343.546 1.00 90.49 O
ANISOU 774 O MET A 123 12286 11978 10119 169 -525 951 O
ATOM 775 CB MET A 123 -87.516 62.353 346.157 1.00 86.82 C
ANISOU 775 CB MET A 123 11397 11911 9678 -255 -416 1100 C
ATOM 776 CG MET A 123 -86.023 62.193 346.348 1.00 91.83 C
ANISOU 776 CG MET A 123 11848 12811 10234 -509 -350 1201 C
ATOM 777 SD MET A 123 -85.602 60.722 347.340 1.00 95.56 S
ANISOU 777 SD MET A 123 11917 13533 10859 -394 -308 1205 S
ATOM 778 CE MET A 123 -84.131 61.252 348.092 1.00 93.80 C
ANISOU 778 CE MET A 123 11600 13538 10500 -716 -294 1280 C
ATOM 779 N THR A 124 -90.390 63.658 345.489 1.00 82.64 N
ANISOU 779 N THR A 124 11424 10826 9149 194 -622 846 N
ATOM 780 CA THR A 124 -91.815 63.527 345.150 1.00 81.07 C
ANISOU 780 CA THR A 124 11271 10502 9030 507 -692 683 C
ATOM 781 C THR A 124 -92.168 64.432 343.990 1.00 88.00 C
ANISOU 781 C THR A 124 12499 11171 9766 591 -794 654 C
ATOM 782 O THR A 124 -92.929 64.025 343.101 1.00 88.10 O
ANISOU 782 O THR A 124 12489 11152 9833 823 -823 566 O
ATOM 783 CB THR A 124 -92.723 63.761 346.380 1.00 81.91 C
ANISOU 783 CB THR A 124 11373 10554 9195 609 -742 550 C
ATOM 784 OG1 THR A 124 -92.221 63.028 347.506 1.00 83.54 O
ANISOU 784 OG1 THR A 124 11319 10928 9493 478 -652 602 O
ATOM 785 CG2 THR A 124 -94.184 63.379 346.125 1.00 70.01 C
ANISOU 785 CG2 THR A 124 9799 9017 7784 925 -788 346 C
ATOM 786 N ALA A 125 -91.604 65.661 343.993 1.00 86.46 N
ANISOU 786 N ALA A 125 12655 10823 9371 390 -853 725 N
ATOM 787 CA ALA A 125 -91.815 66.656 342.939 1.00 87.28 C
ANISOU 787 CA ALA A 125 13197 10683 9283 424 -964 713 C
ATOM 788 C ALA A 125 -91.288 66.126 341.610 1.00 90.85 C
ANISOU 788 C ALA A 125 13593 11211 9715 374 -893 793 C
ATOM 789 O ALA A 125 -91.979 66.251 340.605 1.00 90.94 O
ANISOU 789 O ALA A 125 13787 11076 9689 584 -976 721 O
ATOM 790 CB ALA A 125 -91.143 67.961 343.311 1.00 89.74 C
ANISOU 790 CB ALA A 125 13899 10837 9361 140 -1013 796 C
ATOM 791 N VAL A 126 -90.114 65.461 341.625 1.00 87.42 N
ANISOU 791 N VAL A 126 12878 11026 9311 126 -745 921 N
ATOM 792 CA VAL A 126 -89.504 64.825 340.452 1.00 87.75 C
ANISOU 792 CA VAL A 126 12797 11200 9344 67 -654 990 C
ATOM 793 C VAL A 126 -90.448 63.731 339.954 1.00 92.92 C
ANISOU 793 C VAL A 126 13216 11896 10194 408 -652 898 C
ATOM 794 O VAL A 126 -90.754 63.698 338.769 1.00 93.36 O
ANISOU 794 O VAL A 126 13403 11862 10208 519 -680 878 O
ATOM 795 CB VAL A 126 -88.085 64.264 340.763 1.00 91.15 C
ANISOU 795 CB VAL A 126 12918 11941 9774 -224 -506 1109 C
ATOM 796 CG1 VAL A 126 -87.593 63.326 339.658 1.00 90.22 C
ANISOU 796 CG1 VAL A 126 12579 12006 9693 -204 -407 1146 C
ATOM 797 CG2 VAL A 126 -87.080 65.388 341.010 1.00 92.92 C
ANISOU 797 CG2 VAL A 126 13395 12148 9761 -616 -496 1191 C
ATOM 798 N ALA A 127 -90.919 62.855 340.868 1.00 90.33 N
ANISOU 798 N ALA A 127 12570 11693 10060 554 -621 836 N
ATOM 799 CA ALA A 127 -91.838 61.748 340.578 1.00 89.33 C
ANISOU 799 CA ALA A 127 12212 11624 10106 835 -606 735 C
ATOM 800 C ALA A 127 -93.131 62.265 339.946 1.00 95.80 C
ANISOU 800 C ALA A 127 13264 12235 10900 1101 -739 586 C
ATOM 801 O ALA A 127 -93.576 61.719 338.938 1.00 94.56 O
ANISOU 801 O ALA A 127 13064 12079 10784 1267 -740 543 O
ATOM 802 CB ALA A 127 -92.142 60.963 341.852 1.00 88.51 C
ANISOU 802 CB ALA A 127 11824 11649 10155 883 -559 683 C
ATOM 803 N PHE A 128 -93.701 63.344 340.508 1.00 95.57 N
ANISOU 803 N PHE A 128 13495 12030 10787 1153 -861 500 N
ATOM 804 CA PHE A 128 -94.914 63.968 339.996 1.00 97.50 C
ANISOU 804 CA PHE A 128 13986 12081 10978 1441 -1022 332 C
ATOM 805 C PHE A 128 -94.673 64.574 338.606 1.00101.90 C
ANISOU 805 C PHE A 128 14894 12459 11366 1439 -1093 388 C
ATOM 806 O PHE A 128 -95.568 64.506 337.763 1.00102.94 O
ANISOU 806 O PHE A 128 15104 12508 11500 1709 -1188 266 O
ATOM 807 CB PHE A 128 -95.452 65.009 340.995 1.00101.48 C
ANISOU 807 CB PHE A 128 14704 12445 11408 1495 -1141 229 C
ATOM 808 CG PHE A 128 -96.607 65.849 340.500 1.00106.21 C
ANISOU 808 CG PHE A 128 15616 12834 11906 1817 -1342 41 C
ATOM 809 CD1 PHE A 128 -96.397 67.145 340.033 1.00113.06 C
ANISOU 809 CD1 PHE A 128 17003 13420 12534 1791 -1485 78 C
ATOM 810 CD2 PHE A 128 -97.905 65.351 340.508 1.00109.49 C
ANISOU 810 CD2 PHE A 128 15823 13338 12441 2144 -1397 -189 C
ATOM 811 CE1 PHE A 128 -97.466 67.921 339.560 1.00116.55 C
ANISOU 811 CE1 PHE A 128 17770 13652 12860 2136 -1701 -109 C
ATOM 812 CE2 PHE A 128 -98.976 66.130 340.044 1.00114.97 C
ANISOU 812 CE2 PHE A 128 16783 13869 13030 2483 -1604 -393 C
ATOM 813 CZ PHE A 128 -98.749 67.411 339.575 1.00115.58 C
ANISOU 813 CZ PHE A 128 17396 13647 12872 2500 -1766 -350 C
ATOM 814 N ASP A 129 -93.466 65.144 338.366 1.00 97.38 N
ANISOU 814 N ASP A 129 14530 11840 10631 1118 -1045 560 N
ATOM 815 CA ASP A 129 -93.071 65.742 337.087 1.00 97.57 C
ANISOU 815 CA ASP A 129 14922 11696 10455 1029 -1088 630 C
ATOM 816 C ASP A 129 -92.942 64.677 335.996 1.00 98.69 C
ANISOU 816 C ASP A 129 14828 11977 10691 1088 -993 662 C
ATOM 817 O ASP A 129 -93.366 64.917 334.865 1.00 99.05 O
ANISOU 817 O ASP A 129 15125 11863 10646 1227 -1079 623 O
ATOM 818 CB ASP A 129 -91.771 66.559 337.220 1.00100.74 C
ANISOU 818 CB ASP A 129 15566 12065 10645 605 -1030 790 C
ATOM 819 CG ASP A 129 -91.362 67.282 335.945 1.00114.41 C
ANISOU 819 CG ASP A 129 17746 13601 12122 458 -1069 854 C
ATOM 820 OD1 ASP A 129 -92.021 68.289 335.591 1.00115.76 O
ANISOU 820 OD1 ASP A 129 18418 13452 12112 591 -1250 784 O
ATOM 821 OD2 ASP A 129 -90.391 66.836 335.296 1.00122.89 O
ANISOU 821 OD2 ASP A 129 18687 14842 13164 218 -926 962 O
ATOM 822 N ARG A 130 -92.361 63.511 336.328 1.00 92.38 N
ANISOU 822 N ARG A 130 13576 11463 10061 996 -828 729 N
ATOM 823 CA ARG A 130 -92.211 62.413 335.372 1.00 90.67 C
ANISOU 823 CA ARG A 130 13122 11392 9938 1061 -732 758 C
ATOM 824 C ARG A 130 -93.580 61.839 335.042 1.00 93.35 C
ANISOU 824 C ARG A 130 13363 11692 10415 1427 -809 599 C
ATOM 825 O ARG A 130 -93.900 61.702 333.867 1.00 92.83 O
ANISOU 825 O ARG A 130 13400 11554 10318 1554 -842 575 O
ATOM 826 CB ARG A 130 -91.245 61.318 335.880 1.00 88.40 C
ANISOU 826 CB ARG A 130 12410 11408 9770 903 -560 856 C
ATOM 827 CG ARG A 130 -89.846 61.796 336.288 1.00 96.64 C
ANISOU 827 CG ARG A 130 13467 12568 10683 539 -479 985 C
ATOM 828 CD ARG A 130 -88.959 62.255 335.140 1.00101.84 C
ANISOU 828 CD ARG A 130 14325 13226 11145 301 -428 1072 C
ATOM 829 NE ARG A 130 -89.324 63.588 334.665 1.00105.44 N
ANISOU 829 NE ARG A 130 15302 13371 11389 247 -553 1054 N
ATOM 830 CZ ARG A 130 -89.566 63.891 333.393 1.00115.61 C
ANISOU 830 CZ ARG A 130 16878 14493 12556 292 -599 1047 C
ATOM 831 NH1 ARG A 130 -89.453 62.963 332.449 1.00104.24 N
ANISOU 831 NH1 ARG A 130 15231 13183 11193 374 -516 1060 N
ATOM 832 NH2 ARG A 130 -89.912 65.127 333.053 1.00 94.13 N
ANISOU 832 NH2 ARG A 130 14687 11460 9620 259 -736 1026 N
ATOM 833 N TYR A 131 -94.413 61.581 336.080 1.00 89.06 N
ANISOU 833 N TYR A 131 12639 11197 10003 1582 -840 475 N
ATOM 834 CA TYR A 131 -95.784 61.065 335.975 1.00 87.76 C
ANISOU 834 CA TYR A 131 12342 11045 9957 1898 -905 283 C
ATOM 835 C TYR A 131 -96.590 61.935 335.017 1.00 95.25 C
ANISOU 835 C TYR A 131 13641 11770 10780 2124 -1085 170 C
ATOM 836 O TYR A 131 -97.260 61.420 334.116 1.00 94.31 O
ANISOU 836 O TYR A 131 13465 11664 10706 2328 -1116 82 O
ATOM 837 CB TYR A 131 -96.441 61.022 337.369 1.00 86.95 C
ANISOU 837 CB TYR A 131 12069 11017 9952 1958 -916 158 C
ATOM 838 CG TYR A 131 -97.836 60.442 337.381 1.00 86.22 C
ANISOU 838 CG TYR A 131 11791 11001 9969 2234 -958 -68 C
ATOM 839 CD1 TYR A 131 -98.041 59.069 337.472 1.00 86.24 C
ANISOU 839 CD1 TYR A 131 11453 11199 10115 2236 -831 -91 C
ATOM 840 CD2 TYR A 131 -98.956 61.269 337.342 1.00 88.01 C
ANISOU 840 CD2 TYR A 131 12186 11119 10135 2488 -1130 -277 C
ATOM 841 CE1 TYR A 131 -99.326 58.531 337.497 1.00 86.73 C
ANISOU 841 CE1 TYR A 131 11340 11359 10254 2439 -854 -314 C
ATOM 842 CE2 TYR A 131 -100.245 60.742 337.346 1.00 88.77 C
ANISOU 842 CE2 TYR A 131 12070 11340 10317 2730 -1164 -518 C
ATOM 843 CZ TYR A 131 -100.425 59.371 337.433 1.00 95.27 C
ANISOU 843 CZ TYR A 131 12545 12373 11280 2679 -1016 -535 C
ATOM 844 OH TYR A 131 -101.695 58.848 337.448 1.00 98.35 O
ANISOU 844 OH TYR A 131 12723 12912 11733 2868 -1035 -787 O
ATOM 845 N MET A 132 -96.482 63.260 335.200 1.00 94.98 N
ANISOU 845 N MET A 132 13999 11520 10569 2086 -1212 173 N
ATOM 846 CA MET A 132 -97.137 64.252 334.364 1.00 97.18 C
ANISOU 846 CA MET A 132 14707 11538 10678 2305 -1415 71 C
ATOM 847 C MET A 132 -96.612 64.205 332.919 1.00100.57 C
ANISOU 847 C MET A 132 15349 11868 10994 2232 -1403 183 C
ATOM 848 O MET A 132 -97.411 64.123 331.998 1.00101.74 O
ANISOU 848 O MET A 132 15601 11931 11124 2500 -1516 69 O
ATOM 849 CB MET A 132 -96.997 65.647 334.995 1.00101.83 C
ANISOU 849 CB MET A 132 15710 11903 11079 2248 -1547 66 C
ATOM 850 CG MET A 132 -98.326 66.288 335.336 1.00107.68 C
ANISOU 850 CG MET A 132 16599 12526 11787 2634 -1763 -184 C
ATOM 851 SD MET A 132 -99.460 65.197 336.226 1.00111.02 S
ANISOU 851 SD MET A 132 16436 13265 12480 2858 -1703 -406 S
ATOM 852 CE MET A 132 -100.990 65.978 335.842 1.00110.01 C
ANISOU 852 CE MET A 132 16541 13006 12251 3357 -1988 -725 C
ATOM 853 N ALA A 133 -95.286 64.189 332.725 1.00 94.55 N
ANISOU 853 N ALA A 133 14619 11149 10158 1872 -1259 390 N
ATOM 854 CA ALA A 133 -94.678 64.146 331.398 1.00 93.47 C
ANISOU 854 CA ALA A 133 14672 10946 9898 1749 -1219 497 C
ATOM 855 C ALA A 133 -94.953 62.864 330.618 1.00 94.42 C
ANISOU 855 C ALA A 133 14454 11236 10186 1898 -1133 476 C
ATOM 856 O ALA A 133 -95.052 62.937 329.393 1.00 95.91 O
ANISOU 856 O ALA A 133 14862 11301 10280 1973 -1186 475 O
ATOM 857 CB ALA A 133 -93.180 64.393 331.497 1.00 94.49 C
ANISOU 857 CB ALA A 133 14849 11150 9904 1305 -1068 690 C
ATOM 858 N ILE A 134 -95.078 61.705 331.311 1.00 87.69 N
ANISOU 858 N ILE A 134 13111 10645 9561 1934 -1008 458 N
ATOM 859 CA ILE A 134 -95.282 60.373 330.713 1.00 85.72 C
ANISOU 859 CA ILE A 134 12533 10569 9469 2048 -910 445 C
ATOM 860 C ILE A 134 -96.771 60.010 330.525 1.00 91.70 C
ANISOU 860 C ILE A 134 13207 11308 10326 2406 -1026 236 C
ATOM 861 O ILE A 134 -97.163 59.611 329.427 1.00 93.16 O
ANISOU 861 O ILE A 134 13427 11461 10508 2551 -1055 198 O
ATOM 862 CB ILE A 134 -94.520 59.222 331.473 1.00 86.47 C
ANISOU 862 CB ILE A 134 12193 10942 9720 1891 -718 537 C
ATOM 863 CG1 ILE A 134 -93.017 59.546 331.816 1.00 87.53 C
ANISOU 863 CG1 ILE A 134 12337 11163 9757 1542 -606 712 C
ATOM 864 CG2 ILE A 134 -94.627 57.884 330.753 1.00 84.92 C
ANISOU 864 CG2 ILE A 134 11729 10891 9646 1997 -622 536 C
ATOM 865 CD1 ILE A 134 -92.074 60.010 330.720 1.00 99.66 C
ANISOU 865 CD1 ILE A 134 14085 12663 11119 1337 -558 827 C
ATOM 866 N ILE A 135 -97.572 60.104 331.594 1.00 87.98 N
ANISOU 866 N ILE A 135 12602 10887 9938 2532 -1081 90 N
ATOM 867 CA ILE A 135 -98.987 59.705 331.633 1.00 87.52 C
ANISOU 867 CA ILE A 135 12381 10895 9977 2836 -1167 -146 C
ATOM 868 C ILE A 135 -99.938 60.789 331.076 1.00 95.73 C
ANISOU 868 C ILE A 135 13763 11730 10881 3124 -1407 -320 C
ATOM 869 O ILE A 135 -100.878 60.448 330.356 1.00 96.36 O
ANISOU 869 O ILE A 135 13786 11840 10987 3378 -1490 -480 O
ATOM 870 CB ILE A 135 -99.387 59.249 333.087 1.00 88.93 C
ANISOU 870 CB ILE A 135 12240 11258 10290 2810 -1097 -242 C
ATOM 871 CG1 ILE A 135 -98.338 58.285 333.736 1.00 86.47 C
ANISOU 871 CG1 ILE A 135 11663 11112 10079 2535 -889 -61 C
ATOM 872 CG2 ILE A 135 -100.803 58.671 333.178 1.00 89.79 C
ANISOU 872 CG2 ILE A 135 12114 11509 10495 3058 -1142 -504 C
ATOM 873 CD1 ILE A 135 -98.023 56.965 333.034 1.00 88.61 C
ANISOU 873 CD1 ILE A 135 11723 11512 10433 2501 -754 20 C
ATOM 874 N HIS A 136 -99.698 62.075 331.415 1.00 94.20 N
ANISOU 874 N HIS A 136 13936 11329 10527 3094 -1530 -299 N
ATOM 875 CA HIS A 136 -100.524 63.219 331.008 1.00 96.07 C
ANISOU 875 CA HIS A 136 14571 11335 10598 3388 -1788 -465 C
ATOM 876 C HIS A 136 -99.710 64.257 330.174 1.00100.90 C
ANISOU 876 C HIS A 136 15743 11635 10960 3250 -1870 -301 C
ATOM 877 O HIS A 136 -99.475 65.381 330.652 1.00100.03 O
ANISOU 877 O HIS A 136 15996 11326 10684 3193 -1975 -282 O
ATOM 878 CB HIS A 136 -101.168 63.865 332.254 1.00 97.90 C
ANISOU 878 CB HIS A 136 14790 11580 10829 3522 -1890 -635 C
ATOM 879 CG HIS A 136 -101.874 62.894 333.154 1.00100.36 C
ANISOU 879 CG HIS A 136 14579 12200 11352 3577 -1783 -790 C
ATOM 880 ND1 HIS A 136 -102.968 62.164 332.717 1.00102.14 N
ANISOU 880 ND1 HIS A 136 14532 12603 11674 3827 -1812 -1006 N
ATOM 881 CD2 HIS A 136 -101.614 62.562 334.441 1.00101.64 C
ANISOU 881 CD2 HIS A 136 14482 12515 11621 3389 -1649 -760 C
ATOM 882 CE1 HIS A 136 -103.336 61.416 333.743 1.00100.68 C
ANISOU 882 CE1 HIS A 136 13944 12672 11639 3758 -1685 -1101 C
ATOM 883 NE2 HIS A 136 -102.549 61.615 334.802 1.00100.60 N
ANISOU 883 NE2 HIS A 136 13935 12646 11643 3504 -1587 -955 N
ATOM 884 N PRO A 137 -99.253 63.890 328.938 1.00 98.99 N
ANISOU 884 N PRO A 137 15600 11342 10669 3166 -1817 -183 N
ATOM 885 CA PRO A 137 -98.418 64.820 328.151 1.00101.23 C
ANISOU 885 CA PRO A 137 16422 11348 10694 2965 -1865 -27 C
ATOM 886 C PRO A 137 -99.070 66.101 327.668 1.00111.05 C
ANISOU 886 C PRO A 137 18268 12242 11685 3219 -2153 -147 C
ATOM 887 O PRO A 137 -98.346 67.064 327.418 1.00112.65 O
ANISOU 887 O PRO A 137 18978 12188 11637 2997 -2195 -21 O
ATOM 888 CB PRO A 137 -97.968 63.970 326.961 1.00101.79 C
ANISOU 888 CB PRO A 137 16384 11493 10797 2858 -1734 86 C
ATOM 889 CG PRO A 137 -99.021 62.942 326.821 1.00104.51 C
ANISOU 889 CG PRO A 137 16329 12029 11352 3167 -1745 -80 C
ATOM 890 CD PRO A 137 -99.411 62.605 328.223 1.00 98.66 C
ANISOU 890 CD PRO A 137 15203 11495 10787 3211 -1697 -181 C
ATOM 891 N LEU A 138 -100.415 66.108 327.513 1.00110.62 N
ANISOU 891 N LEU A 138 18173 12184 11674 3676 -2353 -401 N
ATOM 892 CA LEU A 138 -101.191 67.243 326.985 1.00113.69 C
ANISOU 892 CA LEU A 138 19123 12252 11821 4020 -2669 -560 C
ATOM 893 C LEU A 138 -101.451 68.347 327.997 1.00123.42 C
ANISOU 893 C LEU A 138 20636 13332 12927 4126 -2831 -657 C
ATOM 894 O LEU A 138 -101.670 69.487 327.589 1.00125.59 O
ANISOU 894 O LEU A 138 21537 13259 12923 4294 -3077 -710 O
ATOM 895 CB LEU A 138 -102.502 66.774 326.343 1.00113.27 C
ANISOU 895 CB LEU A 138 18890 12295 11851 4487 -2828 -815 C
ATOM 896 CG LEU A 138 -102.393 65.613 325.368 1.00114.93 C
ANISOU 896 CG LEU A 138 18798 12670 12200 4420 -2677 -745 C
ATOM 897 CD1 LEU A 138 -103.736 65.151 324.947 1.00115.24 C
ANISOU 897 CD1 LEU A 138 18601 12853 12331 4860 -2826 -1022 C
ATOM 898 CD2 LEU A 138 -101.550 65.961 324.171 1.00116.99 C
ANISOU 898 CD2 LEU A 138 19534 12662 12253 4209 -2671 -543 C
ATOM 899 N GLN A 139 -101.427 68.023 329.299 1.00122.90 N
ANISOU 899 N GLN A 139 20150 13503 13042 4033 -2703 -681 N
ATOM 900 CA GLN A 139 -101.591 69.021 330.354 1.00126.59 C
ANISOU 900 CA GLN A 139 20851 13845 13401 4097 -2828 -759 C
ATOM 901 C GLN A 139 -100.212 69.351 330.951 1.00136.06 C
ANISOU 901 C GLN A 139 22189 14979 14527 3582 -2648 -487 C
ATOM 902 O GLN A 139 -99.668 68.546 331.710 1.00134.49 O
ANISOU 902 O GLN A 139 21505 15057 14537 3316 -2409 -383 O
ATOM 903 CB GLN A 139 -102.657 68.633 331.410 1.00127.14 C
ANISOU 903 CB GLN A 139 20434 14198 13674 4387 -2854 -1020 C
ATOM 904 CG GLN A 139 -102.534 67.224 331.988 1.00142.43 C
ANISOU 904 CG GLN A 139 21658 16537 15923 4190 -2572 -982 C
ATOM 905 CD GLN A 139 -103.587 66.897 333.021 1.00165.74 C
ANISOU 905 CD GLN A 139 24183 19759 19033 4427 -2590 -1251 C
ATOM 906 OE1 GLN A 139 -104.439 66.025 332.816 1.00160.15 O
ANISOU 906 OE1 GLN A 139 23067 19307 18474 4618 -2566 -1436 O
ATOM 907 NE2 GLN A 139 -103.527 67.554 334.175 1.00161.42 N
ANISOU 907 NE2 GLN A 139 23706 19179 18447 4382 -2615 -1281 N
ATOM 908 N PRO A 140 -99.575 70.475 330.541 1.00138.66 N
ANISOU 908 N PRO A 140 23189 14951 14544 3409 -2750 -363 N
ATOM 909 CA PRO A 140 -98.239 70.788 331.073 1.00139.44 C
ANISOU 909 CA PRO A 140 23401 15025 14555 2880 -2568 -119 C
ATOM 910 C PRO A 140 -98.293 71.474 332.434 1.00146.39 C
ANISOU 910 C PRO A 140 24341 15873 15407 2856 -2614 -162 C
ATOM 911 O PRO A 140 -99.187 72.288 332.674 1.00148.06 O
ANISOU 911 O PRO A 140 24881 15882 15492 3214 -2864 -350 O
ATOM 912 CB PRO A 140 -97.620 71.687 329.995 1.00143.93 C
ANISOU 912 CB PRO A 140 24686 15230 14771 2680 -2654 9 C
ATOM 913 CG PRO A 140 -98.757 72.040 329.033 1.00150.33 C
ANISOU 913 CG PRO A 140 25857 15803 15460 3181 -2944 -187 C
ATOM 914 CD PRO A 140 -100.037 71.531 329.619 1.00144.43 C
ANISOU 914 CD PRO A 140 24633 15281 14962 3669 -3042 -449 C
ATOM 915 N ARG A 141 -97.350 71.122 333.329 1.00143.40 N
ANISOU 915 N ARG A 141 23637 15705 15144 2455 -2380 -2 N
ATOM 916 CA ARG A 141 -97.251 71.675 334.693 1.00144.64 C
ANISOU 916 CA ARG A 141 23804 15862 15292 2363 -2384 -13 C
ATOM 917 C ARG A 141 -95.825 72.179 335.027 1.00149.35 C
ANISOU 917 C ARG A 141 24621 16405 15720 1801 -2236 229 C
ATOM 918 O ARG A 141 -95.573 72.673 336.136 1.00149.17 O
ANISOU 918 O ARG A 141 24641 16371 15664 1657 -2225 251 O
ATOM 919 CB ARG A 141 -97.766 70.663 335.749 1.00144.39 C
ANISOU 919 CB ARG A 141 23069 16193 15598 2495 -2265 -120 C
ATOM 920 CG ARG A 141 -99.275 70.421 335.677 1.00159.11 C
ANISOU 920 CG ARG A 141 24766 18116 17574 3033 -2435 -412 C
ATOM 921 CD ARG A 141 -99.850 69.799 336.936 1.00171.84 C
ANISOU 921 CD ARG A 141 25827 20030 19436 3129 -2347 -550 C
ATOM 922 NE ARG A 141 -101.270 69.481 336.759 1.00183.99 N
ANISOU 922 NE ARG A 141 27154 21684 21069 3603 -2484 -850 N
ATOM 923 CZ ARG A 141 -102.102 69.144 337.741 1.00196.58 C
ANISOU 923 CZ ARG A 141 28351 23517 22822 3777 -2468 -1058 C
ATOM 924 NH1 ARG A 141 -101.672 69.090 338.997 1.00181.25 N
ANISOU 924 NH1 ARG A 141 26206 21691 20968 3531 -2328 -987 N
ATOM 925 NH2 ARG A 141 -103.372 68.868 337.476 1.00182.59 N
ANISOU 925 NH2 ARG A 141 26381 21884 21109 4188 -2590 -1352 N
ATOM 926 N LEU A 142 -94.907 72.064 334.048 1.00145.97 N
ANISOU 926 N LEU A 142 24331 15957 15173 1479 -2121 395 N
ATOM 927 CA LEU A 142 -93.513 72.476 334.173 1.00146.08 C
ANISOU 927 CA LEU A 142 24524 15976 15004 912 -1964 602 C
ATOM 928 C LEU A 142 -93.352 73.935 333.768 1.00150.45 C
ANISOU 928 C LEU A 142 25934 16091 15139 777 -2140 628 C
ATOM 929 O LEU A 142 -93.704 74.307 332.642 1.00153.25 O
ANISOU 929 O LEU A 142 26754 16175 15298 923 -2285 593 O
ATOM 930 CB LEU A 142 -92.611 71.576 333.307 1.00145.29 C
ANISOU 930 CB LEU A 142 24129 16110 14965 629 -1745 738 C
ATOM 931 N SER A 143 -92.838 74.758 334.693 1.00143.72 N
ANISOU 931 N SER A 143 25321 15153 14133 501 -2136 688 N
ATOM 932 CA SER A 143 -92.579 76.186 334.493 1.00145.38 C
ANISOU 932 CA SER A 143 26384 14940 13914 301 -2288 727 C
ATOM 933 C SER A 143 -91.461 76.596 335.453 1.00148.25 C
ANISOU 933 C SER A 143 26741 15410 14178 -231 -2130 865 C
ATOM 934 O SER A 143 -91.512 76.224 336.627 1.00146.51 O
ANISOU 934 O SER A 143 26060 15416 14192 -180 -2064 841 O
ATOM 935 CB SER A 143 -93.844 77.005 334.744 1.00148.21 C
ANISOU 935 CB SER A 143 27192 14952 14170 828 -2608 535 C
ATOM 936 OG SER A 143 -93.611 78.398 334.632 1.00155.52 O
ANISOU 936 OG SER A 143 28996 15437 14659 651 -2772 571 O
ATOM 937 N ALA A 144 -90.440 77.326 334.956 1.00145.20 N
ANISOU 937 N ALA A 144 26855 14878 13435 -762 -2061 1002 N
ATOM 938 CA ALA A 144 -89.286 77.776 335.749 1.00144.69 C
ANISOU 938 CA ALA A 144 26829 14928 13220 -1338 -1904 1128 C
ATOM 939 C ALA A 144 -89.696 78.558 336.998 1.00146.27 C
ANISOU 939 C ALA A 144 27265 14944 13367 -1222 -2047 1074 C
ATOM 940 O ALA A 144 -89.163 78.296 338.077 1.00144.12 O
ANISOU 940 O ALA A 144 26574 14945 13239 -1443 -1906 1124 O
ATOM 941 CB ALA A 144 -88.346 78.607 334.892 1.00148.94 C
ANISOU 941 CB ALA A 144 28013 15266 13310 -1893 -1853 1240 C
ATOM 942 N THR A 145 -90.663 79.488 336.854 1.00143.31 N
ANISOU 942 N THR A 145 27551 14115 12787 -846 -2337 959 N
ATOM 943 CA THR A 145 -91.193 80.294 337.957 1.00143.50 C
ANISOU 943 CA THR A 145 27861 13924 12737 -657 -2508 878 C
ATOM 944 C THR A 145 -91.952 79.419 338.941 1.00141.87 C
ANISOU 944 C THR A 145 26904 14025 12974 -229 -2490 756 C
ATOM 945 O THR A 145 -91.735 79.544 340.151 1.00141.20 O
ANISOU 945 O THR A 145 26634 14051 12965 -349 -2437 770 O
ATOM 946 CB THR A 145 -92.037 81.482 337.461 1.00158.56 C
ANISOU 946 CB THR A 145 30698 15266 14282 -326 -2842 768 C
ATOM 947 OG1 THR A 145 -92.615 81.185 336.183 1.00163.19 O
ANISOU 947 OG1 THR A 145 31380 15746 14879 28 -2956 689 O
ATOM 948 CG2 THR A 145 -91.240 82.775 337.397 1.00160.59 C
ANISOU 948 CG2 THR A 145 31837 15153 14027 -853 -2876 892 C
ATOM 949 N ALA A 146 -92.814 78.511 338.422 1.00133.74 N
ANISOU 949 N ALA A 146 25445 13146 12226 234 -2523 635 N
ATOM 950 CA ALA A 146 -93.598 77.588 339.243 1.00129.21 C
ANISOU 950 CA ALA A 146 24159 12878 12057 622 -2494 500 C
ATOM 951 C ALA A 146 -92.693 76.645 340.039 1.00127.94 C
ANISOU 951 C ALA A 146 23292 13156 12163 259 -2207 628 C
ATOM 952 O ALA A 146 -92.944 76.454 341.227 1.00126.47 O
ANISOU 952 O ALA A 146 22782 13115 12156 350 -2183 572 O
ATOM 953 CB ALA A 146 -94.572 76.804 338.385 1.00128.56 C
ANISOU 953 CB ALA A 146 23798 12877 12172 1094 -2564 358 C
ATOM 954 N THR A 147 -91.606 76.122 339.410 1.00121.55 N
ANISOU 954 N THR A 147 22284 12550 11351 -157 -1998 791 N
ATOM 955 CA THR A 147 -90.611 75.239 340.040 1.00118.16 C
ANISOU 955 CA THR A 147 21220 12545 11132 -506 -1738 911 C
ATOM 956 C THR A 147 -89.979 75.959 341.245 1.00121.92 C
ANISOU 956 C THR A 147 21829 13010 11486 -840 -1707 979 C
ATOM 957 O THR A 147 -89.843 75.366 342.317 1.00119.03 O
ANISOU 957 O THR A 147 20954 12914 11358 -852 -1606 981 O
ATOM 958 CB THR A 147 -89.571 74.763 339.002 1.00120.01 C
ANISOU 958 CB THR A 147 21341 12957 11300 -874 -1559 1044 C
ATOM 959 OG1 THR A 147 -90.248 74.142 337.914 1.00116.83 O
ANISOU 959 OG1 THR A 147 20849 12535 11007 -537 -1604 975 O
ATOM 960 CG2 THR A 147 -88.577 73.772 339.576 1.00115.38 C
ANISOU 960 CG2 THR A 147 20078 12834 10926 -1165 -1314 1139 C
ATOM 961 N LYS A 148 -89.647 77.251 341.062 1.00121.30 N
ANISOU 961 N LYS A 148 22477 12593 11018 -1104 -1806 1028 N
ATOM 962 CA LYS A 148 -89.077 78.119 342.086 1.00122.31 C
ANISOU 962 CA LYS A 148 22872 12642 10958 -1447 -1802 1091 C
ATOM 963 C LYS A 148 -90.078 78.334 343.227 1.00125.62 C
ANISOU 963 C LYS A 148 23259 12957 11514 -1045 -1949 958 C
ATOM 964 O LYS A 148 -89.674 78.291 344.389 1.00124.70 O
ANISOU 964 O LYS A 148 22907 12998 11475 -1234 -1868 998 O
ATOM 965 CB LYS A 148 -88.610 79.451 341.476 1.00128.41 C
ANISOU 965 CB LYS A 148 24520 13027 11244 -1802 -1892 1159 C
ATOM 966 CG LYS A 148 -87.316 79.324 340.681 1.00142.25 C
ANISOU 966 CG LYS A 148 26256 14971 12823 -2390 -1684 1301 C
ATOM 967 CD LYS A 148 -87.095 80.502 339.742 1.00156.92 C
ANISOU 967 CD LYS A 148 29028 16405 14191 -2672 -1788 1342 C
ATOM 968 CE LYS A 148 -85.852 80.315 338.905 1.00171.88 C
ANISOU 968 CE LYS A 148 30864 18529 15912 -3260 -1564 1454 C
ATOM 969 NZ LYS A 148 -85.634 81.447 337.963 1.00187.20 N
ANISOU 969 NZ LYS A 148 33737 20044 17345 -3574 -1654 1490 N
ATOM 970 N VAL A 149 -91.383 78.505 342.901 1.00121.73 N
ANISOU 970 N VAL A 149 22962 12234 11055 -483 -2163 786 N
ATOM 971 CA VAL A 149 -92.459 78.674 343.893 1.00120.45 C
ANISOU 971 CA VAL A 149 22737 12006 11022 -44 -2310 612 C
ATOM 972 C VAL A 149 -92.699 77.344 344.651 1.00119.77 C
ANISOU 972 C VAL A 149 21780 12356 11370 99 -2148 564 C
ATOM 973 O VAL A 149 -92.997 77.384 345.845 1.00119.09 O
ANISOU 973 O VAL A 149 21513 12342 11395 174 -2151 502 O
ATOM 974 CB VAL A 149 -93.751 79.302 343.277 1.00125.96 C
ANISOU 974 CB VAL A 149 23917 12356 11587 518 -2600 411 C
ATOM 975 CG1 VAL A 149 -94.920 79.310 344.265 1.00124.94 C
ANISOU 975 CG1 VAL A 149 23576 12263 11632 1012 -2730 185 C
ATOM 976 CG2 VAL A 149 -93.481 80.719 342.779 1.00129.61 C
ANISOU 976 CG2 VAL A 149 25335 12335 11575 363 -2782 459 C
ATOM 977 N VAL A 150 -92.520 76.176 343.975 1.00112.76 N
ANISOU 977 N VAL A 150 20390 11747 10705 110 -2004 599 N
ATOM 978 CA VAL A 150 -92.670 74.849 344.590 1.00108.56 C
ANISOU 978 CA VAL A 150 19090 11607 10549 209 -1846 569 C
ATOM 979 C VAL A 150 -91.558 74.649 345.627 1.00111.32 C
ANISOU 979 C VAL A 150 19165 12183 10948 -228 -1670 719 C
ATOM 980 O VAL A 150 -91.865 74.363 346.785 1.00108.89 O
ANISOU 980 O VAL A 150 18563 12003 10809 -141 -1644 660 O
ATOM 981 CB VAL A 150 -92.768 73.686 343.562 1.00110.07 C
ANISOU 981 CB VAL A 150 18885 12005 10931 333 -1751 570 C
ATOM 982 CG1 VAL A 150 -92.763 72.322 344.251 1.00106.27 C
ANISOU 982 CG1 VAL A 150 17677 11910 10792 359 -1578 566 C
ATOM 983 CG2 VAL A 150 -94.015 73.828 342.691 1.00110.74 C
ANISOU 983 CG2 VAL A 150 19176 11901 11000 819 -1941 387 C
ATOM 984 N ILE A 151 -90.282 74.867 345.220 1.00109.18 N
ANISOU 984 N ILE A 151 19020 11961 10501 -702 -1557 895 N
ATOM 985 CA ILE A 151 -89.088 74.773 346.074 1.00108.92 C
ANISOU 985 CA ILE A 151 18758 12162 10464 -1150 -1401 1030 C
ATOM 986 C ILE A 151 -89.227 75.716 347.282 1.00116.61 C
ANISOU 986 C ILE A 151 20027 12958 11321 -1210 -1493 1007 C
ATOM 987 O ILE A 151 -88.892 75.336 348.403 1.00115.39 O
ANISOU 987 O ILE A 151 19517 13014 11311 -1322 -1406 1033 O
ATOM 988 CB ILE A 151 -87.804 75.044 345.236 1.00113.18 C
ANISOU 988 CB ILE A 151 19465 12769 10768 -1641 -1289 1179 C
ATOM 989 CG1 ILE A 151 -87.512 73.868 344.271 1.00111.07 C
ANISOU 989 CG1 ILE A 151 18747 12779 10674 -1597 -1157 1205 C
ATOM 990 CG2 ILE A 151 -86.590 75.341 346.137 1.00114.95 C
ANISOU 990 CG2 ILE A 151 19602 13185 10890 -2138 -1170 1291 C
ATOM 991 CD1 ILE A 151 -86.580 74.174 343.101 1.00112.15 C
ANISOU 991 CD1 ILE A 151 19147 12909 10557 -1953 -1087 1295 C
ATOM 992 N CYS A 152 -89.755 76.927 347.034 1.00118.02 N
ANISOU 992 N CYS A 152 20879 12735 11230 -1108 -1681 949 N
ATOM 993 CA CYS A 152 -90.046 77.994 347.994 1.00120.63 C
ANISOU 993 CA CYS A 152 21626 12813 11395 -1101 -1811 904 C
ATOM 994 C CYS A 152 -91.018 77.463 349.063 1.00120.18 C
ANISOU 994 C CYS A 152 21165 12872 11627 -706 -1842 753 C
ATOM 995 O CYS A 152 -90.707 77.540 350.251 1.00119.88 O
ANISOU 995 O CYS A 152 20989 12925 11635 -866 -1791 782 O
ATOM 996 CB CYS A 152 -90.623 79.203 347.252 1.00125.56 C
ANISOU 996 CB CYS A 152 23056 12968 11682 -945 -2036 840 C
ATOM 997 SG CYS A 152 -90.677 80.744 348.208 1.00133.12 S
ANISOU 997 SG CYS A 152 24694 13550 12336 -996 -2212 806 S
ATOM 998 N VAL A 153 -92.155 76.866 348.629 1.00113.37 N
ANISOU 998 N VAL A 153 20084 12037 10955 -221 -1911 589 N
ATOM 999 CA VAL A 153 -93.212 76.281 349.474 1.00110.53 C
ANISOU 999 CA VAL A 153 19322 11817 10857 162 -1931 407 C
ATOM 1000 C VAL A 153 -92.684 75.101 350.305 1.00110.17 C
ANISOU 1000 C VAL A 153 18614 12154 11091 -32 -1718 483 C
ATOM 1001 O VAL A 153 -92.886 75.099 351.524 1.00109.77 O
ANISOU 1001 O VAL A 153 18415 12168 11126 -22 -1702 432 O
ATOM 1002 CB VAL A 153 -94.475 75.927 348.631 1.00114.00 C
ANISOU 1002 CB VAL A 153 19696 12225 11394 678 -2049 203 C
ATOM 1003 CG1 VAL A 153 -95.375 74.902 349.320 1.00111.09 C
ANISOU 1003 CG1 VAL A 153 18733 12138 11339 966 -1986 31 C
ATOM 1004 CG2 VAL A 153 -95.265 77.188 348.283 1.00116.88 C
ANISOU 1004 CG2 VAL A 153 20719 12202 11488 989 -2314 58 C
ATOM 1005 N ILE A 154 -91.995 74.120 349.649 1.00103.37 N
ANISOU 1005 N ILE A 154 17391 11532 10352 -203 -1565 602 N
ATOM 1006 CA ILE A 154 -91.381 72.928 350.257 1.00 99.99 C
ANISOU 1006 CA ILE A 154 16373 11458 10159 -373 -1378 684 C
ATOM 1007 C ILE A 154 -90.594 73.325 351.520 1.00105.33 C
ANISOU 1007 C ILE A 154 17057 12184 10778 -700 -1329 779 C
ATOM 1008 O ILE A 154 -90.786 72.722 352.584 1.00103.47 O
ANISOU 1008 O ILE A 154 16480 12110 10724 -652 -1271 738 O
ATOM 1009 CB ILE A 154 -90.487 72.164 349.230 1.00101.80 C
ANISOU 1009 CB ILE A 154 16371 11885 10425 -559 -1250 816 C
ATOM 1010 CG1 ILE A 154 -91.342 71.383 348.204 1.00100.92 C
ANISOU 1010 CG1 ILE A 154 16087 11801 10457 -204 -1268 712 C
ATOM 1011 CG2 ILE A 154 -89.468 71.233 349.929 1.00100.51 C
ANISOU 1011 CG2 ILE A 154 15722 12060 10408 -819 -1082 931 C
ATOM 1012 CD1 ILE A 154 -90.583 70.825 346.982 1.00104.24 C
ANISOU 1012 CD1 ILE A 154 16386 12352 10869 -345 -1170 824 C
ATOM 1013 N TRP A 155 -89.745 74.367 351.396 1.00103.86 N
ANISOU 1013 N TRP A 155 17294 11850 10319 -1043 -1355 896 N
ATOM 1014 CA TRP A 155 -88.932 74.880 352.489 1.00104.15 C
ANISOU 1014 CA TRP A 155 17394 11921 10256 -1393 -1317 989 C
ATOM 1015 C TRP A 155 -89.730 75.583 353.572 1.00109.14 C
ANISOU 1015 C TRP A 155 18253 12353 10861 -1221 -1432 878 C
ATOM 1016 O TRP A 155 -89.370 75.448 354.740 1.00108.54 O
ANISOU 1016 O TRP A 155 17984 12403 10853 -1379 -1373 913 O
ATOM 1017 CB TRP A 155 -87.809 75.766 351.970 1.00104.86 C
ANISOU 1017 CB TRP A 155 17873 11931 10038 -1847 -1300 1131 C
ATOM 1018 CG TRP A 155 -86.621 74.968 351.532 1.00104.89 C
ANISOU 1018 CG TRP A 155 17478 12284 10091 -2154 -1132 1251 C
ATOM 1019 CD1 TRP A 155 -86.271 74.655 350.254 1.00107.96 C
ANISOU 1019 CD1 TRP A 155 17840 12745 10436 -2210 -1079 1288 C
ATOM 1020 CD2 TRP A 155 -85.667 74.314 352.384 1.00103.70 C
ANISOU 1020 CD2 TRP A 155 16872 12480 10051 -2406 -1005 1327 C
ATOM 1021 NE1 TRP A 155 -85.133 73.883 350.251 1.00106.79 N
ANISOU 1021 NE1 TRP A 155 17243 12980 10354 -2485 -922 1376 N
ATOM 1022 CE2 TRP A 155 -84.745 73.649 351.545 1.00107.50 C
ANISOU 1022 CE2 TRP A 155 17062 13246 10539 -2594 -883 1397 C
ATOM 1023 CE3 TRP A 155 -85.495 74.233 353.779 1.00104.15 C
ANISOU 1023 CE3 TRP A 155 16748 12635 10188 -2481 -991 1335 C
ATOM 1024 CZ2 TRP A 155 -83.651 72.933 352.051 1.00106.23 C
ANISOU 1024 CZ2 TRP A 155 16435 13476 10453 -2831 -762 1461 C
ATOM 1025 CZ3 TRP A 155 -84.416 73.517 354.279 1.00104.95 C
ANISOU 1025 CZ3 TRP A 155 16407 13103 10366 -2725 -874 1411 C
ATOM 1026 CH2 TRP A 155 -83.504 72.884 353.420 1.00105.74 C
ANISOU 1026 CH2 TRP A 155 16220 13493 10463 -2884 -768 1466 C
ATOM 1027 N VAL A 156 -90.814 76.299 353.212 1.00107.09 N
ANISOU 1027 N VAL A 156 18387 11799 10502 -878 -1600 732 N
ATOM 1028 CA VAL A 156 -91.666 76.988 354.192 1.00108.10 C
ANISOU 1028 CA VAL A 156 18732 11747 10595 -655 -1723 590 C
ATOM 1029 C VAL A 156 -92.366 75.950 355.092 1.00109.61 C
ANISOU 1029 C VAL A 156 18357 12191 11097 -425 -1645 466 C
ATOM 1030 O VAL A 156 -92.305 76.067 356.322 1.00109.26 O
ANISOU 1030 O VAL A 156 18240 12186 11087 -516 -1620 455 O
ATOM 1031 CB VAL A 156 -92.642 78.002 353.526 1.00114.79 C
ANISOU 1031 CB VAL A 156 20145 12234 11237 -300 -1945 438 C
ATOM 1032 CG1 VAL A 156 -93.744 78.450 354.487 1.00115.17 C
ANISOU 1032 CG1 VAL A 156 20267 12179 11312 61 -2070 224 C
ATOM 1033 CG2 VAL A 156 -91.882 79.213 352.985 1.00117.51 C
ANISOU 1033 CG2 VAL A 156 21172 12268 11208 -606 -2030 569 C
ATOM 1034 N LEU A 157 -92.954 74.901 354.469 1.00103.27 N
ANISOU 1034 N LEU A 157 17166 11565 10507 -173 -1594 382 N
ATOM 1035 CA LEU A 157 -93.635 73.802 355.162 1.00100.01 C
ANISOU 1035 CA LEU A 157 16234 11399 10367 12 -1505 260 C
ATOM 1036 C LEU A 157 -92.657 72.960 355.988 1.00101.35 C
ANISOU 1036 C LEU A 157 16019 11821 10669 -316 -1337 415 C
ATOM 1037 O LEU A 157 -93.040 72.459 357.045 1.00100.58 O
ANISOU 1037 O LEU A 157 15659 11845 10710 -273 -1282 338 O
ATOM 1038 CB LEU A 157 -94.375 72.910 354.155 1.00 98.93 C
ANISOU 1038 CB LEU A 157 15830 11376 10381 308 -1491 150 C
ATOM 1039 CG LEU A 157 -95.463 73.559 353.292 1.00104.65 C
ANISOU 1039 CG LEU A 157 16868 11896 10998 696 -1669 -35 C
ATOM 1040 CD1 LEU A 157 -95.861 72.641 352.179 1.00103.14 C
ANISOU 1040 CD1 LEU A 157 16410 11837 10941 889 -1634 -86 C
ATOM 1041 CD2 LEU A 157 -96.695 73.917 354.119 1.00107.98 C
ANISOU 1041 CD2 LEU A 157 17321 12278 11429 1022 -1774 -296 C
ATOM 1042 N ALA A 158 -91.399 72.811 355.508 1.00 96.82 N
ANISOU 1042 N ALA A 158 15419 11332 10035 -640 -1260 618 N
ATOM 1043 CA ALA A 158 -90.331 72.072 356.187 1.00 95.31 C
ANISOU 1043 CA ALA A 158 14885 11393 9934 -939 -1126 762 C
ATOM 1044 C ALA A 158 -89.875 72.781 357.476 1.00100.48 C
ANISOU 1044 C ALA A 158 15690 11996 10491 -1176 -1141 810 C
ATOM 1045 O ALA A 158 -89.672 72.116 358.493 1.00 98.60 O
ANISOU 1045 O ALA A 158 15151 11925 10386 -1240 -1069 821 O
ATOM 1046 CB ALA A 158 -89.144 71.882 355.254 1.00 96.31 C
ANISOU 1046 CB ALA A 158 14969 11641 9982 -1201 -1060 925 C
ATOM 1047 N LEU A 159 -89.705 74.123 357.432 1.00 99.50 N
ANISOU 1047 N LEU A 159 16061 11625 10118 -1314 -1239 840 N
ATOM 1048 CA LEU A 159 -89.283 74.915 358.594 1.00100.22 C
ANISOU 1048 CA LEU A 159 16361 11634 10083 -1553 -1264 887 C
ATOM 1049 C LEU A 159 -90.399 74.995 359.645 1.00104.47 C
ANISOU 1049 C LEU A 159 16889 12088 10716 -1284 -1316 718 C
ATOM 1050 O LEU A 159 -90.106 74.971 360.845 1.00102.87 O
ANISOU 1050 O LEU A 159 16596 11950 10541 -1442 -1279 747 O
ATOM 1051 CB LEU A 159 -88.793 76.317 358.185 1.00102.62 C
ANISOU 1051 CB LEU A 159 17253 11675 10063 -1788 -1356 960 C
ATOM 1052 CG LEU A 159 -87.646 76.381 357.158 1.00107.67 C
ANISOU 1052 CG LEU A 159 17957 12401 10553 -2128 -1294 1112 C
ATOM 1053 CD1 LEU A 159 -87.597 77.729 356.478 1.00109.89 C
ANISOU 1053 CD1 LEU A 159 18910 12344 10498 -2250 -1408 1132 C
ATOM 1054 CD2 LEU A 159 -86.298 76.020 357.772 1.00109.39 C
ANISOU 1054 CD2 LEU A 159 17880 12914 10768 -2552 -1171 1254 C
ATOM 1055 N LEU A 160 -91.677 75.036 359.189 1.00102.11 N
ANISOU 1055 N LEU A 160 16653 11676 10467 -876 -1398 527 N
ATOM 1056 CA LEU A 160 -92.864 75.052 360.055 1.00101.95 C
ANISOU 1056 CA LEU A 160 16575 11626 10534 -582 -1441 315 C
ATOM 1057 C LEU A 160 -92.998 73.732 360.816 1.00102.79 C
ANISOU 1057 C LEU A 160 16150 12016 10891 -590 -1298 285 C
ATOM 1058 O LEU A 160 -93.207 73.751 362.029 1.00102.45 O
ANISOU 1058 O LEU A 160 16049 11997 10881 -633 -1275 229 O
ATOM 1059 CB LEU A 160 -94.141 75.310 359.236 1.00103.06 C
ANISOU 1059 CB LEU A 160 16841 11652 10667 -139 -1559 97 C
ATOM 1060 CG LEU A 160 -94.424 76.758 358.834 1.00110.89 C
ANISOU 1060 CG LEU A 160 18441 12303 11390 7 -1754 29 C
ATOM 1061 CD1 LEU A 160 -95.320 76.812 357.601 1.00111.77 C
ANISOU 1061 CD1 LEU A 160 18654 12330 11483 402 -1870 -127 C
ATOM 1062 CD2 LEU A 160 -95.042 77.548 359.985 1.00114.08 C
ANISOU 1062 CD2 LEU A 160 19025 12594 11726 140 -1836 -126 C
ATOM 1063 N LEU A 161 -92.875 72.591 360.099 1.00 97.00 N
ANISOU 1063 N LEU A 161 15063 11478 10315 -553 -1206 320 N
ATOM 1064 CA LEU A 161 -92.951 71.239 360.659 1.00 94.26 C
ANISOU 1064 CA LEU A 161 14259 11377 10177 -565 -1076 304 C
ATOM 1065 C LEU A 161 -91.830 70.990 361.668 1.00 98.80 C
ANISOU 1065 C LEU A 161 14729 12056 10753 -903 -1005 476 C
ATOM 1066 O LEU A 161 -92.081 70.393 362.713 1.00 98.29 O
ANISOU 1066 O LEU A 161 14467 12089 10788 -924 -943 425 O
ATOM 1067 CB LEU A 161 -92.931 70.178 359.537 1.00 92.52 C
ANISOU 1067 CB LEU A 161 13769 11304 10080 -462 -1013 326 C
ATOM 1068 CG LEU A 161 -92.988 68.701 359.953 1.00 94.53 C
ANISOU 1068 CG LEU A 161 13607 11787 10524 -464 -887 314 C
ATOM 1069 CD1 LEU A 161 -94.377 68.304 360.436 1.00 94.22 C
ANISOU 1069 CD1 LEU A 161 13436 11786 10578 -235 -867 70 C
ATOM 1070 CD2 LEU A 161 -92.540 67.800 358.825 1.00 93.99 C
ANISOU 1070 CD2 LEU A 161 13341 11843 10529 -440 -834 403 C
ATOM 1071 N ALA A 162 -90.616 71.469 361.372 1.00 96.34 N
ANISOU 1071 N ALA A 162 14560 11733 10313 -1175 -1017 663 N
ATOM 1072 CA ALA A 162 -89.454 71.303 362.244 1.00 96.59 C
ANISOU 1072 CA ALA A 162 14486 11894 10321 -1498 -966 818 C
ATOM 1073 C ALA A 162 -89.506 72.171 363.504 1.00103.13 C
ANISOU 1073 C ALA A 162 15544 12592 11050 -1628 -1012 802 C
ATOM 1074 O ALA A 162 -88.906 71.802 364.516 1.00102.83 O
ANISOU 1074 O ALA A 162 15355 12674 11043 -1819 -968 875 O
ATOM 1075 CB ALA A 162 -88.187 71.603 361.467 1.00 98.19 C
ANISOU 1075 CB ALA A 162 14752 12162 10392 -1760 -960 986 C
ATOM 1076 N PHE A 163 -90.207 73.327 363.432 1.00101.56 N
ANISOU 1076 N PHE A 163 15728 12142 10719 -1509 -1111 702 N
ATOM 1077 CA PHE A 163 -90.308 74.337 364.487 1.00102.55 C
ANISOU 1077 CA PHE A 163 16152 12099 10714 -1607 -1173 677 C
ATOM 1078 C PHE A 163 -90.642 73.792 365.890 1.00106.22 C
ANISOU 1078 C PHE A 163 16394 12660 11304 -1608 -1114 608 C
ATOM 1079 O PHE A 163 -89.872 74.123 366.802 1.00107.01 O
ANISOU 1079 O PHE A 163 16564 12765 11329 -1882 -1109 716 O
ATOM 1080 CB PHE A 163 -91.267 75.484 364.111 1.00105.87 C
ANISOU 1080 CB PHE A 163 17003 12235 10986 -1363 -1306 531 C
ATOM 1081 CG PHE A 163 -91.265 76.617 365.111 1.00108.86 C
ANISOU 1081 CG PHE A 163 17754 12414 11192 -1475 -1383 519 C
ATOM 1082 CD1 PHE A 163 -90.265 77.584 365.089 1.00113.62 C
ANISOU 1082 CD1 PHE A 163 18727 12880 11563 -1806 -1428 681 C
ATOM 1083 CD2 PHE A 163 -92.250 76.705 366.091 1.00110.48 C
ANISOU 1083 CD2 PHE A 163 17943 12582 11452 -1270 -1402 335 C
ATOM 1084 CE1 PHE A 163 -90.248 78.618 366.034 1.00115.97 C
ANISOU 1084 CE1 PHE A 163 19394 12982 11689 -1922 -1500 674 C
ATOM 1085 CE2 PHE A 163 -92.234 77.740 367.030 1.00114.72 C
ANISOU 1085 CE2 PHE A 163 18831 12932 11825 -1366 -1474 322 C
ATOM 1086 CZ PHE A 163 -91.237 78.694 366.992 1.00114.46 C
ANISOU 1086 CZ PHE A 163 19187 12739 11565 -1684 -1527 498 C
ATOM 1087 N PRO A 164 -91.738 73.013 366.131 1.00100.44 N
ANISOU 1087 N PRO A 164 15420 12007 10737 -1346 -1069 430 N
ATOM 1088 CA PRO A 164 -92.022 72.567 367.509 1.00 99.10 C
ANISOU 1088 CA PRO A 164 15097 11911 10646 -1401 -1007 365 C
ATOM 1089 C PRO A 164 -90.881 71.817 368.188 1.00102.73 C
ANISOU 1089 C PRO A 164 15348 12532 11154 -1688 -936 545 C
ATOM 1090 O PRO A 164 -90.650 72.042 369.378 1.00103.17 O
ANISOU 1090 O PRO A 164 15460 12566 11173 -1849 -931 566 O
ATOM 1091 CB PRO A 164 -93.279 71.715 367.355 1.00 99.95 C
ANISOU 1091 CB PRO A 164 14956 12118 10901 -1116 -950 148 C
ATOM 1092 CG PRO A 164 -93.927 72.229 366.124 1.00105.15 C
ANISOU 1092 CG PRO A 164 15755 12681 11517 -848 -1032 43 C
ATOM 1093 CD PRO A 164 -92.787 72.538 365.205 1.00101.08 C
ANISOU 1093 CD PRO A 164 15372 12119 10916 -1014 -1068 264 C
ATOM 1094 N GLN A 165 -90.135 70.979 367.428 1.00 98.18 N
ANISOU 1094 N GLN A 165 14547 12115 10643 -1740 -896 668 N
ATOM 1095 CA GLN A 165 -88.976 70.225 367.930 1.00 97.22 C
ANISOU 1095 CA GLN A 165 14215 12174 10552 -1963 -854 825 C
ATOM 1096 C GLN A 165 -87.843 71.177 368.378 1.00103.26 C
ANISOU 1096 C GLN A 165 15169 12913 11151 -2273 -906 972 C
ATOM 1097 O GLN A 165 -87.213 70.931 369.406 1.00102.93 O
ANISOU 1097 O GLN A 165 15047 12959 11103 -2452 -899 1041 O
ATOM 1098 CB GLN A 165 -88.473 69.231 366.866 1.00 97.15 C
ANISOU 1098 CB GLN A 165 13944 12342 10627 -1903 -815 896 C
ATOM 1099 CG GLN A 165 -87.227 68.453 367.275 1.00 97.90 C
ANISOU 1099 CG GLN A 165 13814 12646 10736 -2078 -797 1035 C
ATOM 1100 CD GLN A 165 -87.385 66.959 367.243 1.00109.20 C
ANISOU 1100 CD GLN A 165 14969 14212 12309 -1926 -743 1008 C
ATOM 1101 OE1 GLN A 165 -88.466 66.406 367.471 1.00103.14 O
ANISOU 1101 OE1 GLN A 165 14174 13385 11631 -1761 -699 877 O
ATOM 1102 NE2 GLN A 165 -86.283 66.267 366.989 1.00 96.40 N
ANISOU 1102 NE2 GLN A 165 13148 12790 10691 -1986 -747 1119 N
ATOM 1103 N GLY A 166 -87.607 72.236 367.600 1.00101.14 N
ANISOU 1103 N GLY A 166 15170 12524 10735 -2342 -961 1011 N
ATOM 1104 CA GLY A 166 -86.589 73.240 367.884 1.00102.45 C
ANISOU 1104 CA GLY A 166 15568 12655 10705 -2671 -1005 1136 C
ATOM 1105 C GLY A 166 -86.982 74.140 369.037 1.00107.30 C
ANISOU 1105 C GLY A 166 16466 13075 11227 -2736 -1052 1088 C
ATOM 1106 O GLY A 166 -86.146 74.464 369.884 1.00107.76 O
ANISOU 1106 O GLY A 166 16571 13179 11193 -3018 -1062 1183 O
ATOM 1107 N TYR A 167 -88.273 74.527 369.080 1.00103.53 N
ANISOU 1107 N TYR A 167 16165 12402 10770 -2463 -1085 923 N
ATOM 1108 CA TYR A 167 -88.874 75.375 370.105 1.00104.07 C
ANISOU 1108 CA TYR A 167 16509 12278 10755 -2447 -1134 832 C
ATOM 1109 C TYR A 167 -88.724 74.759 371.503 1.00107.33 C
ANISOU 1109 C TYR A 167 16719 12802 11258 -2562 -1078 838 C
ATOM 1110 O TYR A 167 -88.272 75.449 372.415 1.00108.12 O
ANISOU 1110 O TYR A 167 17016 12825 11239 -2780 -1110 896 O
ATOM 1111 CB TYR A 167 -90.357 75.636 369.765 1.00105.70 C
ANISOU 1111 CB TYR A 167 16836 12333 10994 -2063 -1176 608 C
ATOM 1112 CG TYR A 167 -91.064 76.602 370.693 1.00109.69 C
ANISOU 1112 CG TYR A 167 17650 12638 11390 -1994 -1242 481 C
ATOM 1113 CD1 TYR A 167 -90.901 77.979 370.556 1.00113.96 C
ANISOU 1113 CD1 TYR A 167 18680 12925 11694 -2063 -1357 513 C
ATOM 1114 CD2 TYR A 167 -91.927 76.144 371.684 1.00110.11 C
ANISOU 1114 CD2 TYR A 167 17531 12751 11556 -1862 -1189 317 C
ATOM 1115 CE1 TYR A 167 -91.554 78.873 371.403 1.00116.47 C
ANISOU 1115 CE1 TYR A 167 19304 13051 11899 -1973 -1428 388 C
ATOM 1116 CE2 TYR A 167 -92.582 77.028 372.540 1.00112.57 C
ANISOU 1116 CE2 TYR A 167 18110 12899 11762 -1788 -1246 184 C
ATOM 1117 CZ TYR A 167 -92.395 78.394 372.394 1.00123.62 C
ANISOU 1117 CZ TYR A 167 19992 14044 12935 -1824 -1371 219 C
ATOM 1118 OH TYR A 167 -93.037 79.272 373.237 1.00127.65 O
ANISOU 1118 OH TYR A 167 20788 14385 13329 -1727 -1438 81 O
ATOM 1119 N TYR A 168 -89.065 73.461 371.661 1.00102.10 N
ANISOU 1119 N TYR A 168 15697 12310 10786 -2433 -998 783 N
ATOM 1120 CA TYR A 168 -89.002 72.750 372.943 1.00100.90 C
ANISOU 1120 CA TYR A 168 15381 12248 10710 -2526 -945 778 C
ATOM 1121 C TYR A 168 -87.622 72.140 373.280 1.00104.15 C
ANISOU 1121 C TYR A 168 15606 12845 11121 -2777 -939 964 C
ATOM 1122 O TYR A 168 -87.467 71.494 374.324 1.00103.80 O
ANISOU 1122 O TYR A 168 15447 12869 11125 -2851 -913 972 O
ATOM 1123 CB TYR A 168 -90.109 71.695 373.030 1.00101.13 C
ANISOU 1123 CB TYR A 168 15181 12344 10898 -2290 -866 608 C
ATOM 1124 CG TYR A 168 -91.507 72.269 372.960 1.00104.14 C
ANISOU 1124 CG TYR A 168 15698 12598 11272 -2044 -873 380 C
ATOM 1125 CD1 TYR A 168 -91.929 73.245 373.861 1.00107.50 C
ANISOU 1125 CD1 TYR A 168 16374 12876 11594 -2068 -912 291 C
ATOM 1126 CD2 TYR A 168 -92.430 71.794 372.032 1.00104.26 C
ANISOU 1126 CD2 TYR A 168 15573 12663 11377 -1772 -846 232 C
ATOM 1127 CE1 TYR A 168 -93.219 73.774 373.805 1.00109.75 C
ANISOU 1127 CE1 TYR A 168 16765 13076 11859 -1803 -933 49 C
ATOM 1128 CE2 TYR A 168 -93.726 72.306 371.974 1.00106.05 C
ANISOU 1128 CE2 TYR A 168 15889 12818 11588 -1519 -866 -12 C
ATOM 1129 CZ TYR A 168 -94.118 73.296 372.864 1.00116.49 C
ANISOU 1129 CZ TYR A 168 17453 14007 12801 -1523 -912 -110 C
ATOM 1130 OH TYR A 168 -95.400 73.795 372.818 1.00118.59 O
ANISOU 1130 OH TYR A 168 17786 14233 13039 -1238 -943 -381 O
ATOM 1131 N SER A 169 -86.612 72.392 372.437 1.00100.71 N
ANISOU 1131 N SER A 169 15159 12497 10610 -2914 -969 1097 N
ATOM 1132 CA SER A 169 -85.246 71.931 372.686 1.00100.34 C
ANISOU 1132 CA SER A 169 14918 12671 10535 -3143 -977 1244 C
ATOM 1133 C SER A 169 -84.575 72.883 373.665 1.00104.70 C
ANISOU 1133 C SER A 169 15681 13173 10927 -3442 -1027 1319 C
ATOM 1134 O SER A 169 -84.690 74.099 373.511 1.00106.25 O
ANISOU 1134 O SER A 169 16201 13195 10975 -3547 -1063 1323 O
ATOM 1135 CB SER A 169 -84.447 71.875 371.389 1.00103.29 C
ANISOU 1135 CB SER A 169 15173 13200 10874 -3190 -976 1327 C
ATOM 1136 OG SER A 169 -84.588 70.601 370.789 1.00109.53 O
ANISOU 1136 OG SER A 169 15652 14144 11822 -2979 -933 1304 O
ATOM 1137 N THR A 170 -83.891 72.344 374.672 1.00 99.76 N
ANISOU 1137 N THR A 170 14905 12685 10314 -3573 -1038 1375 N
ATOM 1138 CA THR A 170 -83.211 73.180 375.659 1.00100.83 C
ANISOU 1138 CA THR A 170 15216 12796 10300 -3869 -1087 1445 C
ATOM 1139 C THR A 170 -81.994 72.484 376.276 1.00104.67 C
ANISOU 1139 C THR A 170 15439 13553 10779 -4025 -1121 1533 C
ATOM 1140 O THR A 170 -81.813 71.277 376.112 1.00102.90 O
ANISOU 1140 O THR A 170 14926 13498 10674 -3863 -1113 1528 O
ATOM 1141 CB THR A 170 -84.214 73.694 376.728 1.00108.71 C
ANISOU 1141 CB THR A 170 16478 13539 11289 -3825 -1087 1354 C
ATOM 1142 OG1 THR A 170 -83.700 74.885 377.336 1.00112.77 O
ANISOU 1142 OG1 THR A 170 17270 13961 11616 -4111 -1138 1419 O
ATOM 1143 CG2 THR A 170 -84.547 72.650 377.785 1.00101.88 C
ANISOU 1143 CG2 THR A 170 15452 12711 10548 -3727 -1059 1302 C
ATOM 1144 N THR A 171 -81.170 73.258 376.994 1.00102.51 N
ANISOU 1144 N THR A 171 15283 13319 10349 -4330 -1170 1604 N
ATOM 1145 CA THR A 171 -80.027 72.720 377.713 1.00102.72 C
ANISOU 1145 CA THR A 171 15078 13607 10343 -4478 -1224 1667 C
ATOM 1146 C THR A 171 -80.365 72.638 379.207 1.00106.18 C
ANISOU 1146 C THR A 171 15640 13911 10791 -4503 -1254 1650 C
ATOM 1147 O THR A 171 -81.262 73.337 379.693 1.00106.40 O
ANISOU 1147 O THR A 171 15965 13667 10795 -4512 -1231 1605 O
ATOM 1148 CB THR A 171 -78.753 73.520 377.447 1.00110.94 C
ANISOU 1148 CB THR A 171 16106 14857 11188 -4830 -1257 1744 C
ATOM 1149 OG1 THR A 171 -79.000 74.891 377.749 1.00114.08 O
ANISOU 1149 OG1 THR A 171 16903 15015 11428 -5059 -1258 1762 O
ATOM 1150 CG2 THR A 171 -78.231 73.355 376.019 1.00107.43 C
ANISOU 1150 CG2 THR A 171 15467 14623 10728 -4826 -1223 1755 C
ATOM 1151 N GLU A 172 -79.682 71.735 379.914 1.00101.03 N
ANISOU 1151 N GLU A 172 14770 13448 10170 -4488 -1311 1673 N
ATOM 1152 CA GLU A 172 -79.801 71.548 381.350 1.00 99.45 C
ANISOU 1152 CA GLU A 172 14676 13151 9959 -4534 -1352 1668 C
ATOM 1153 C GLU A 172 -78.389 71.549 381.881 1.00102.21 C
ANISOU 1153 C GLU A 172 14874 13774 10189 -4749 -1454 1738 C
ATOM 1154 O GLU A 172 -77.533 70.814 381.374 1.00101.33 O
ANISOU 1154 O GLU A 172 14457 13958 10087 -4678 -1502 1750 O
ATOM 1155 CB GLU A 172 -80.555 70.259 381.719 1.00 99.41 C
ANISOU 1155 CB GLU A 172 14602 13071 10100 -4261 -1331 1602 C
ATOM 1156 CG GLU A 172 -82.060 70.309 381.471 1.00110.78 C
ANISOU 1156 CG GLU A 172 16198 14254 11641 -4084 -1224 1497 C
ATOM 1157 CD GLU A 172 -82.892 71.376 382.167 1.00132.50 C
ANISOU 1157 CD GLU A 172 19262 16746 14337 -4184 -1185 1440 C
ATOM 1158 OE1 GLU A 172 -84.024 71.632 381.697 1.00125.25 O
ANISOU 1158 OE1 GLU A 172 18440 15671 13478 -4029 -1111 1336 O
ATOM 1159 OE2 GLU A 172 -82.434 71.939 383.187 1.00130.18 O
ANISOU 1159 OE2 GLU A 172 19112 16414 13936 -4398 -1235 1487 O
ATOM 1160 N THR A 173 -78.118 72.442 382.836 1.00 98.74 N
ANISOU 1160 N THR A 173 14640 13256 9620 -5012 -1489 1772 N
ATOM 1161 CA THR A 173 -76.778 72.562 383.371 1.00100.14 C
ANISOU 1161 CA THR A 173 14675 13712 9663 -5246 -1590 1824 C
ATOM 1162 C THR A 173 -76.684 71.806 384.668 1.00105.29 C
ANISOU 1162 C THR A 173 15318 14347 10339 -5169 -1674 1817 C
ATOM 1163 O THR A 173 -77.482 72.003 385.589 1.00104.04 O
ANISOU 1163 O THR A 173 15426 13907 10198 -5175 -1649 1802 O
ATOM 1164 CB THR A 173 -76.327 74.019 383.418 1.00104.29 C
ANISOU 1164 CB THR A 173 15413 14217 9996 -5628 -1582 1872 C
ATOM 1165 OG1 THR A 173 -76.311 74.522 382.069 1.00104.37 O
ANISOU 1165 OG1 THR A 173 15424 14263 9968 -5678 -1514 1875 O
ATOM 1166 CG2 THR A 173 -74.959 74.176 384.042 1.00100.89 C
ANISOU 1166 CG2 THR A 173 14818 14106 9409 -5904 -1681 1906 C
ATOM 1167 N MET A 174 -75.694 70.914 384.715 1.00103.83 N
ANISOU 1167 N MET A 174 14832 14475 10144 -5082 -1780 1817 N
ATOM 1168 CA MET A 174 -75.421 70.028 385.838 1.00104.00 C
ANISOU 1168 CA MET A 174 14827 14523 10165 -4968 -1897 1807 C
ATOM 1169 C MET A 174 -73.972 70.156 386.335 1.00109.81 C
ANISOU 1169 C MET A 174 15362 15615 10747 -5148 -2042 1822 C
ATOM 1170 O MET A 174 -73.156 70.780 385.645 1.00110.91 O
ANISOU 1170 O MET A 174 15322 16026 10791 -5351 -2033 1828 O
ATOM 1171 CB MET A 174 -75.750 68.609 385.399 1.00105.38 C
ANISOU 1171 CB MET A 174 14854 14719 10468 -4597 -1912 1763 C
ATOM 1172 CG MET A 174 -77.229 68.401 385.252 1.00106.92 C
ANISOU 1172 CG MET A 174 15266 14564 10794 -4446 -1779 1728 C
ATOM 1173 SD MET A 174 -77.590 66.976 384.272 1.00110.37 S
ANISOU 1173 SD MET A 174 15517 15054 11364 -4072 -1762 1680 S
ATOM 1174 CE MET A 174 -76.987 65.616 385.388 1.00108.06 C
ANISOU 1174 CE MET A 174 15233 14814 11009 -3898 -1942 1671 C
ATOM 1175 N PRO A 175 -73.613 69.608 387.521 1.00106.71 N
ANISOU 1175 N PRO A 175 15000 15240 10306 -5100 -2177 1818 N
ATOM 1176 CA PRO A 175 -72.238 69.800 388.026 1.00108.54 C
ANISOU 1176 CA PRO A 175 15026 15837 10379 -5272 -2326 1812 C
ATOM 1177 C PRO A 175 -71.094 69.416 387.072 1.00114.01 C
ANISOU 1177 C PRO A 175 15271 17019 11027 -5192 -2398 1755 C
ATOM 1178 O PRO A 175 -70.213 70.238 386.850 1.00116.36 O
ANISOU 1178 O PRO A 175 15400 17625 11188 -5488 -2406 1745 O
ATOM 1179 CB PRO A 175 -72.198 68.972 389.318 1.00110.07 C
ANISOU 1179 CB PRO A 175 15346 15925 10551 -5125 -2472 1803 C
ATOM 1180 CG PRO A 175 -73.454 68.221 389.374 1.00112.08 C
ANISOU 1180 CG PRO A 175 15818 15820 10946 -4861 -2400 1796 C
ATOM 1181 CD PRO A 175 -74.448 68.903 388.514 1.00106.54 C
ANISOU 1181 CD PRO A 175 15231 14905 10345 -4929 -2198 1809 C
ATOM 1182 N SER A 176 -71.111 68.204 386.495 1.00109.16 N
ANISOU 1182 N SER A 176 14475 16488 10511 -4815 -2443 1708 N
ATOM 1183 CA SER A 176 -70.027 67.739 385.631 1.00109.77 C
ANISOU 1183 CA SER A 176 14115 17049 10545 -4689 -2521 1632 C
ATOM 1184 C SER A 176 -70.217 68.019 384.145 1.00110.82 C
ANISOU 1184 C SER A 176 14098 17270 10737 -4723 -2366 1628 C
ATOM 1185 O SER A 176 -69.232 67.957 383.403 1.00113.35 O
ANISOU 1185 O SER A 176 14050 18036 10980 -4754 -2398 1560 O
ATOM 1186 CB SER A 176 -69.772 66.250 385.852 1.00113.56 C
ANISOU 1186 CB SER A 176 14487 17599 11062 -4239 -2687 1572 C
ATOM 1187 N ARG A 177 -71.460 68.316 383.698 1.00101.69 N
ANISOU 1187 N ARG A 177 13215 15717 9706 -4712 -2203 1684 N
ATOM 1188 CA ARG A 177 -71.753 68.514 382.281 1.00 99.49 C
ANISOU 1188 CA ARG A 177 12838 15474 9488 -4704 -2066 1682 C
ATOM 1189 C ARG A 177 -72.952 69.414 381.951 1.00100.38 C
ANISOU 1189 C ARG A 177 13299 15180 9662 -4846 -1899 1739 C
ATOM 1190 O ARG A 177 -73.624 69.938 382.837 1.00 98.02 O
ANISOU 1190 O ARG A 177 13320 14565 9359 -4959 -1877 1776 O
ATOM 1191 CB ARG A 177 -71.941 67.135 381.603 1.00 98.82 C
ANISOU 1191 CB ARG A 177 12571 15444 9532 -4272 -2095 1635 C
ATOM 1192 CG ARG A 177 -73.233 66.370 381.956 1.00103.33 C
ANISOU 1192 CG ARG A 177 13426 15583 10252 -4003 -2060 1653 C
ATOM 1193 CD ARG A 177 -73.103 64.910 381.569 1.00110.46 C
ANISOU 1193 CD ARG A 177 14162 16590 11219 -3598 -2146 1601 C
ATOM 1194 NE ARG A 177 -74.363 64.322 381.111 1.00112.08 N
ANISOU 1194 NE ARG A 177 14552 16464 11571 -3391 -2036 1607 N
ATOM 1195 CZ ARG A 177 -75.235 63.708 381.901 1.00127.09 C
ANISOU 1195 CZ ARG A 177 16738 18034 13518 -3274 -2037 1608 C
ATOM 1196 NH1 ARG A 177 -75.009 63.611 383.207 1.00133.75 N
ANISOU 1196 NH1 ARG A 177 17743 18800 14276 -3333 -2146 1617 N
ATOM 1197 NH2 ARG A 177 -76.345 63.193 381.396 1.00 99.12 N
ANISOU 1197 NH2 ARG A 177 13325 14245 10092 -3118 -1925 1592 N
ATOM 1198 N VAL A 178 -73.196 69.573 380.638 1.00 97.94 N
ANISOU 1198 N VAL A 178 12918 14897 9397 -4820 -1791 1734 N
ATOM 1199 CA VAL A 178 -74.324 70.270 380.018 1.00 97.23 C
ANISOU 1199 CA VAL A 178 13115 14460 9368 -4863 -1651 1763 C
ATOM 1200 C VAL A 178 -75.040 69.227 379.145 1.00103.78 C
ANISOU 1200 C VAL A 178 13844 15216 10373 -4490 -1603 1729 C
ATOM 1201 O VAL A 178 -74.391 68.406 378.484 1.00104.37 O
ANISOU 1201 O VAL A 178 13602 15587 10467 -4330 -1640 1696 O
ATOM 1202 CB VAL A 178 -73.911 71.533 379.212 1.00101.11 C
ANISOU 1202 CB VAL A 178 13667 15043 9708 -5217 -1576 1787 C
ATOM 1203 CG1 VAL A 178 -75.092 72.109 378.425 1.00 98.56 C
ANISOU 1203 CG1 VAL A 178 13643 14361 9444 -5172 -1459 1801 C
ATOM 1204 CG2 VAL A 178 -73.335 72.594 380.137 1.00102.69 C
ANISOU 1204 CG2 VAL A 178 14026 15272 9719 -5610 -1616 1821 C
ATOM 1205 N VAL A 179 -76.374 69.249 379.167 1.00100.66 N
ANISOU 1205 N VAL A 179 13707 14444 10094 -4351 -1523 1723 N
ATOM 1206 CA VAL A 179 -77.193 68.292 378.434 1.00 98.90 C
ANISOU 1206 CA VAL A 179 13426 14122 10031 -4023 -1469 1683 C
ATOM 1207 C VAL A 179 -78.210 68.987 377.536 1.00103.10 C
ANISOU 1207 C VAL A 179 14143 14418 10612 -4019 -1349 1670 C
ATOM 1208 O VAL A 179 -78.922 69.877 377.985 1.00102.08 O
ANISOU 1208 O VAL A 179 14304 14029 10453 -4138 -1310 1667 O
ATOM 1209 CB VAL A 179 -77.819 67.295 379.450 1.00101.12 C
ANISOU 1209 CB VAL A 179 13801 14225 10395 -3812 -1506 1653 C
ATOM 1210 CG1 VAL A 179 -79.203 66.805 379.033 1.00 99.12 C
ANISOU 1210 CG1 VAL A 179 13669 13708 10283 -3591 -1402 1598 C
ATOM 1211 CG2 VAL A 179 -76.882 66.125 379.682 1.00101.74 C
ANISOU 1211 CG2 VAL A 179 13637 14565 10454 -3640 -1634 1645 C
ATOM 1212 N CYS A 180 -78.260 68.590 376.264 1.00101.51 N
ANISOU 1212 N CYS A 180 13782 14313 10476 -3866 -1302 1653 N
ATOM 1213 CA CYS A 180 -79.260 69.089 375.326 1.00101.34 C
ANISOU 1213 CA CYS A 180 13924 14075 10507 -3801 -1206 1627 C
ATOM 1214 C CYS A 180 -80.390 68.036 375.305 1.00105.15 C
ANISOU 1214 C CYS A 180 14401 14392 11160 -3477 -1164 1559 C
ATOM 1215 O CYS A 180 -80.144 66.878 374.956 1.00104.43 O
ANISOU 1215 O CYS A 180 14087 14450 11140 -3277 -1181 1548 O
ATOM 1216 CB CYS A 180 -78.661 69.311 373.938 1.00102.48 C
ANISOU 1216 CB CYS A 180 13919 14419 10601 -3861 -1176 1647 C
ATOM 1217 SG CYS A 180 -79.865 69.787 372.663 1.00105.48 S
ANISOU 1217 SG CYS A 180 14491 14542 11046 -3717 -1083 1609 S
ATOM 1218 N MET A 181 -81.595 68.415 375.767 1.00101.55 N
ANISOU 1218 N MET A 181 14193 13645 10748 -3435 -1114 1500 N
ATOM 1219 CA MET A 181 -82.743 67.523 375.745 1.00100.65 C
ANISOU 1219 CA MET A 181 14083 13390 10768 -3183 -1055 1409 C
ATOM 1220 C MET A 181 -84.018 68.280 375.360 1.00103.86 C
ANISOU 1220 C MET A 181 14693 13562 11206 -3119 -982 1317 C
ATOM 1221 O MET A 181 -84.145 69.474 375.639 1.00104.19 O
ANISOU 1221 O MET A 181 14955 13475 11158 -3267 -993 1318 O
ATOM 1222 CB MET A 181 -82.885 66.663 377.019 1.00103.27 C
ANISOU 1222 CB MET A 181 14443 13677 11119 -3151 -1081 1386 C
ATOM 1223 CG MET A 181 -83.301 67.372 378.283 1.00108.21 C
ANISOU 1223 CG MET A 181 15309 14120 11685 -3312 -1078 1360 C
ATOM 1224 SD MET A 181 -83.325 66.127 379.625 1.00113.42 S
ANISOU 1224 SD MET A 181 16004 14742 12348 -3274 -1112 1339 S
ATOM 1225 CE MET A 181 -84.506 66.859 380.750 1.00110.10 C
ANISOU 1225 CE MET A 181 15875 14060 11899 -3404 -1041 1245 C
ATOM 1226 N ILE A 182 -84.915 67.602 374.631 1.00 99.07 N
ANISOU 1226 N ILE A 182 14014 12915 10713 -2886 -919 1231 N
ATOM 1227 CA ILE A 182 -86.150 68.229 374.166 1.00 98.68 C
ANISOU 1227 CA ILE A 182 14115 12685 10694 -2771 -864 1112 C
ATOM 1228 C ILE A 182 -87.246 67.987 375.225 1.00103.30 C
ANISOU 1228 C ILE A 182 14798 13135 11317 -2725 -812 979 C
ATOM 1229 O ILE A 182 -87.507 66.838 375.599 1.00103.09 O
ANISOU 1229 O ILE A 182 14665 13151 11354 -2657 -774 940 O
ATOM 1230 CB ILE A 182 -86.544 67.888 372.668 1.00100.73 C
ANISOU 1230 CB ILE A 182 14257 12984 11032 -2564 -828 1074 C
ATOM 1231 CG1 ILE A 182 -88.052 67.724 372.480 1.00100.44 C
ANISOU 1231 CG1 ILE A 182 14271 12817 11075 -2356 -763 895 C
ATOM 1232 CG2 ILE A 182 -85.789 66.710 372.034 1.00100.01 C
ANISOU 1232 CG2 ILE A 182 13901 13096 11004 -2481 -828 1143 C
ATOM 1233 CD1 ILE A 182 -88.566 68.748 371.581 1.00113.63 C
ANISOU 1233 CD1 ILE A 182 16076 14386 12712 -2261 -781 844 C
ATOM 1234 N GLU A 183 -87.832 69.082 375.756 1.00100.26 N
ANISOU 1234 N GLU A 183 14637 12589 10868 -2780 -814 906 N
ATOM 1235 CA GLU A 183 -88.856 68.960 376.795 1.00 99.91 C
ANISOU 1235 CA GLU A 183 14680 12442 10838 -2760 -756 757 C
ATOM 1236 C GLU A 183 -90.142 69.752 376.496 1.00103.90 C
ANISOU 1236 C GLU A 183 15310 12825 11343 -2599 -725 569 C
ATOM 1237 O GLU A 183 -90.176 70.984 376.571 1.00103.30 O
ANISOU 1237 O GLU A 183 15453 12626 11172 -2632 -781 564 O
ATOM 1238 CB GLU A 183 -88.305 69.270 378.205 1.00101.94 C
ANISOU 1238 CB GLU A 183 15072 12652 11007 -2988 -792 823 C
ATOM 1239 CG GLU A 183 -87.422 70.498 378.314 1.00114.13 C
ANISOU 1239 CG GLU A 183 16786 14150 12428 -3173 -876 944 C
ATOM 1240 CD GLU A 183 -86.597 70.583 379.584 1.00129.48 C
ANISOU 1240 CD GLU A 183 18796 16111 14290 -3412 -926 1047 C
ATOM 1241 OE1 GLU A 183 -86.893 71.463 380.425 1.00128.53 O
ANISOU 1241 OE1 GLU A 183 18898 15849 14087 -3524 -935 1011 O
ATOM 1242 OE2 GLU A 183 -85.605 69.827 379.702 1.00111.55 O
ANISOU 1242 OE2 GLU A 183 16359 14001 12024 -3477 -970 1160 O
ATOM 1243 N TRP A 184 -91.203 68.992 376.170 1.00101.49 N
ANISOU 1243 N TRP A 184 14869 12564 11129 -2418 -642 401 N
ATOM 1244 CA TRP A 184 -92.559 69.454 375.869 1.00102.91 C
ANISOU 1244 CA TRP A 184 15087 12695 11321 -2217 -607 167 C
ATOM 1245 C TRP A 184 -93.313 69.768 377.173 1.00113.61 C
ANISOU 1245 C TRP A 184 16550 13992 12624 -2285 -560 7 C
ATOM 1246 O TRP A 184 -93.054 69.105 378.186 1.00112.79 O
ANISOU 1246 O TRP A 184 16427 13913 12515 -2464 -512 47 O
ATOM 1247 CB TRP A 184 -93.317 68.362 375.091 1.00100.24 C
ANISOU 1247 CB TRP A 184 14519 12478 11091 -2042 -526 44 C
ATOM 1248 CG TRP A 184 -92.928 68.261 373.645 1.00100.38 C
ANISOU 1248 CG TRP A 184 14450 12536 11155 -1907 -570 136 C
ATOM 1249 CD1 TRP A 184 -91.738 67.825 373.143 1.00102.62 C
ANISOU 1249 CD1 TRP A 184 14656 12880 11454 -1989 -606 350 C
ATOM 1250 CD2 TRP A 184 -93.743 68.596 372.513 1.00100.28 C
ANISOU 1250 CD2 TRP A 184 14413 12519 11170 -1659 -584 -1 C
ATOM 1251 NE1 TRP A 184 -91.754 67.881 371.771 1.00101.91 N
ANISOU 1251 NE1 TRP A 184 14506 12817 11400 -1830 -629 364 N
ATOM 1252 CE2 TRP A 184 -92.972 68.350 371.356 1.00103.73 C
ANISOU 1252 CE2 TRP A 184 14781 12995 11638 -1625 -621 158 C
ATOM 1253 CE3 TRP A 184 -95.047 69.098 372.364 1.00102.04 C
ANISOU 1253 CE3 TRP A 184 14663 12723 11383 -1448 -577 -258 C
ATOM 1254 CZ2 TRP A 184 -93.453 68.606 370.066 1.00102.90 C
ANISOU 1254 CZ2 TRP A 184 14664 12880 11554 -1405 -653 88 C
ATOM 1255 CZ3 TRP A 184 -95.528 69.336 371.087 1.00103.63 C
ANISOU 1255 CZ3 TRP A 184 14841 12928 11606 -1203 -622 -337 C
ATOM 1256 CH2 TRP A 184 -94.736 69.092 369.955 1.00103.63 C
ANISOU 1256 CH2 TRP A 184 14802 12936 11636 -1190 -659 -157 C
ATOM 1257 N PRO A 185 -94.282 70.726 377.173 1.00115.70 N
ANISOU 1257 N PRO A 185 16937 14185 12839 -2131 -576 -189 N
ATOM 1258 CA PRO A 185 -95.021 71.025 378.417 1.00117.85 C
ANISOU 1258 CA PRO A 185 17295 14428 13053 -2191 -524 -364 C
ATOM 1259 C PRO A 185 -95.690 69.808 379.052 1.00126.38 C
ANISOU 1259 C PRO A 185 18191 15644 14185 -2268 -380 -511 C
ATOM 1260 O PRO A 185 -96.094 68.883 378.350 1.00124.49 O
ANISOU 1260 O PRO A 185 17749 15527 14024 -2178 -314 -583 O
ATOM 1261 CB PRO A 185 -96.037 72.094 377.995 1.00120.67 C
ANISOU 1261 CB PRO A 185 17764 14729 13356 -1924 -577 -589 C
ATOM 1262 CG PRO A 185 -96.070 72.053 376.506 1.00124.46 C
ANISOU 1262 CG PRO A 185 18164 15236 13888 -1707 -629 -574 C
ATOM 1263 CD PRO A 185 -94.721 71.600 376.066 1.00118.37 C
ANISOU 1263 CD PRO A 185 17365 14461 13151 -1884 -657 -270 C
ATOM 1264 N GLU A 186 -95.760 69.798 380.391 1.00128.87 N
ANISOU 1264 N GLU A 186 18601 15926 14437 -2463 -330 -549 N
ATOM 1265 CA GLU A 186 -96.319 68.693 381.162 1.00131.10 C
ANISOU 1265 CA GLU A 186 18783 16306 14722 -2608 -188 -680 C
ATOM 1266 C GLU A 186 -97.820 68.522 380.957 1.00142.03 C
ANISOU 1266 C GLU A 186 20005 17844 16116 -2459 -75 -1026 C
ATOM 1267 O GLU A 186 -98.603 69.440 381.217 1.00142.83 O
ANISOU 1267 O GLU A 186 20149 17956 16165 -2334 -80 -1240 O
ATOM 1268 CB GLU A 186 -95.955 68.816 382.647 1.00133.08 C
ANISOU 1268 CB GLU A 186 19215 16467 14883 -2864 -173 -630 C
ATOM 1269 CG GLU A 186 -94.484 68.560 382.929 1.00142.75 C
ANISOU 1269 CG GLU A 186 20540 17603 16096 -3044 -265 -313 C
ATOM 1270 CD GLU A 186 -94.006 68.845 384.341 1.00170.65 C
ANISOU 1270 CD GLU A 186 24275 21032 19534 -3281 -282 -243 C
ATOM 1271 OE1 GLU A 186 -94.841 69.184 385.213 1.00170.81 O
ANISOU 1271 OE1 GLU A 186 24378 21032 19491 -3327 -210 -437 O
ATOM 1272 OE2 GLU A 186 -92.781 68.732 384.572 1.00167.27 O
ANISOU 1272 OE2 GLU A 186 23912 20557 19085 -3415 -372 -2 O
ATOM 1273 N HIS A 187 -98.198 67.342 380.449 1.00143.20 N
ANISOU 1273 N HIS A 187 19966 18125 16320 -2463 20 -1089 N
ATOM 1274 CA HIS A 187 -99.573 66.930 380.166 1.00146.41 C
ANISOU 1274 CA HIS A 187 20170 18728 16731 -2365 145 -1420 C
ATOM 1275 C HIS A 187 -99.863 65.544 380.783 1.00154.22 C
ANISOU 1275 C HIS A 187 21110 19807 17680 -2635 308 -1489 C
ATOM 1276 O HIS A 187 -98.898 64.852 381.121 1.00154.19 O
ANISOU 1276 O HIS A 187 21232 19689 17665 -2820 287 -1243 O
ATOM 1277 CB HIS A 187 -99.840 66.970 378.655 1.00147.38 C
ANISOU 1277 CB HIS A 187 20133 18924 16942 -2079 90 -1449 C
ATOM 1278 CG HIS A 187 -100.571 68.209 378.241 1.00152.58 C
ANISOU 1278 CG HIS A 187 20788 19605 17582 -1782 9 -1654 C
ATOM 1279 ND1 HIS A 187 -101.886 68.160 377.814 1.00155.85 N
ANISOU 1279 ND1 HIS A 187 20992 20231 17991 -1595 75 -2008 N
ATOM 1280 CD2 HIS A 187 -100.164 69.502 378.262 1.00155.08 C
ANISOU 1280 CD2 HIS A 187 21311 19754 17858 -1650 -139 -1565 C
ATOM 1281 CE1 HIS A 187 -102.229 69.416 377.570 1.00156.53 C
ANISOU 1281 CE1 HIS A 187 21166 20268 18040 -1314 -51 -2123 C
ATOM 1282 NE2 HIS A 187 -101.223 70.258 377.820 1.00156.42 N
ANISOU 1282 NE2 HIS A 187 21427 20009 17997 -1344 -181 -1858 N
ATOM 1283 N PRO A 188 -101.144 65.117 380.984 1.00153.21 N
ANISOU 1283 N PRO A 188 20825 19884 17505 -2677 465 -1826 N
ATOM 1284 CA PRO A 188 -101.398 63.815 381.643 1.00153.42 C
ANISOU 1284 CA PRO A 188 20874 19968 17449 -2994 627 -1887 C
ATOM 1285 C PRO A 188 -100.719 62.582 381.038 1.00154.99 C
ANISOU 1285 C PRO A 188 21099 20109 17683 -3060 620 -1670 C
ATOM 1286 O PRO A 188 -100.409 61.647 381.784 1.00155.23 O
ANISOU 1286 O PRO A 188 21293 20066 17622 -3333 687 -1595 O
ATOM 1287 CB PRO A 188 -102.927 63.677 381.592 1.00157.01 C
ANISOU 1287 CB PRO A 188 21103 20705 17848 -2991 790 -2315 C
ATOM 1288 CG PRO A 188 -103.381 64.667 380.560 1.00161.73 C
ANISOU 1288 CG PRO A 188 21517 21397 18535 -2596 686 -2437 C
ATOM 1289 CD PRO A 188 -102.419 65.804 380.688 1.00156.51 C
ANISOU 1289 CD PRO A 188 21052 20501 17913 -2454 501 -2186 C
ATOM 1290 N ASN A 189 -100.483 62.577 379.708 1.00148.55 N
ANISOU 1290 N ASN A 189 20149 19311 16981 -2806 533 -1573 N
ATOM 1291 CA ASN A 189 -99.879 61.438 379.005 1.00146.41 C
ANISOU 1291 CA ASN A 189 19884 19001 16746 -2822 520 -1386 C
ATOM 1292 C ASN A 189 -98.989 61.840 377.806 1.00146.31 C
ANISOU 1292 C ASN A 189 19811 18921 16859 -2554 359 -1148 C
ATOM 1293 O ASN A 189 -98.583 60.968 377.027 1.00144.54 O
ANISOU 1293 O ASN A 189 19550 18695 16675 -2510 344 -1024 O
ATOM 1294 CB ASN A 189 -100.957 60.404 378.591 1.00147.97 C
ANISOU 1294 CB ASN A 189 19939 19381 16900 -2898 682 -1635 C
ATOM 1295 CG ASN A 189 -102.248 60.954 378.009 1.00173.33 C
ANISOU 1295 CG ASN A 189 22886 22828 20142 -2718 744 -1970 C
ATOM 1296 OD1 ASN A 189 -102.462 62.169 377.873 1.00167.04 O
ANISOU 1296 OD1 ASN A 189 22021 22053 19393 -2495 659 -2046 O
ATOM 1297 ND2 ASN A 189 -103.157 60.051 377.667 1.00166.69 N
ANISOU 1297 ND2 ASN A 189 21906 22175 19252 -2813 889 -2196 N
ATOM 1298 N LYS A 190 -98.645 63.150 377.700 1.00140.85 N
ANISOU 1298 N LYS A 190 19143 18164 16208 -2398 239 -1082 N
ATOM 1299 CA LYS A 190 -97.792 63.731 376.650 1.00138.42 C
ANISOU 1299 CA LYS A 190 18819 17789 15987 -2191 92 -870 C
ATOM 1300 C LYS A 190 -98.245 63.332 375.232 1.00137.68 C
ANISOU 1300 C LYS A 190 18536 17803 15973 -1977 102 -940 C
ATOM 1301 O LYS A 190 -97.441 62.861 374.418 1.00135.77 O
ANISOU 1301 O LYS A 190 18268 17531 15787 -1916 43 -737 O
ATOM 1302 CB LYS A 190 -96.304 63.409 376.905 1.00140.34 C
ANISOU 1302 CB LYS A 190 19186 17910 16227 -2307 -2 -543 C
ATOM 1303 N ILE A 191 -99.556 63.506 374.964 1.00132.23 N
ANISOU 1303 N ILE A 191 17703 17259 15280 -1861 177 -1249 N
ATOM 1304 CA ILE A 191 -100.194 63.175 373.689 1.00130.37 C
ANISOU 1304 CA ILE A 191 17277 17151 15108 -1654 192 -1373 C
ATOM 1305 C ILE A 191 -99.612 64.019 372.550 1.00128.75 C
ANISOU 1305 C ILE A 191 17093 16855 14970 -1399 36 -1216 C
ATOM 1306 O ILE A 191 -99.227 63.443 371.533 1.00127.76 O
ANISOU 1306 O ILE A 191 16896 16738 14908 -1319 15 -1093 O
ATOM 1307 CB ILE A 191 -101.758 63.228 373.778 1.00135.34 C
ANISOU 1307 CB ILE A 191 17729 17999 15696 -1592 300 -1780 C
ATOM 1308 CG1 ILE A 191 -102.308 61.973 374.501 1.00136.73 C
ANISOU 1308 CG1 ILE A 191 17855 18299 15796 -1889 488 -1924 C
ATOM 1309 CG2 ILE A 191 -102.422 63.383 372.392 1.00136.47 C
ANISOU 1309 CG2 ILE A 191 17688 18263 15901 -1283 254 -1929 C
ATOM 1310 CD1 ILE A 191 -103.869 61.979 374.859 1.00148.58 C
ANISOU 1310 CD1 ILE A 191 19163 20074 17217 -1921 632 -2370 C
ATOM 1311 N TYR A 192 -99.509 65.355 372.732 1.00121.74 N
ANISOU 1311 N TYR A 192 16337 15868 14050 -1291 -71 -1216 N
ATOM 1312 CA TYR A 192 -98.997 66.275 371.710 1.00119.61 C
ANISOU 1312 CA TYR A 192 16160 15486 13799 -1082 -221 -1084 C
ATOM 1313 C TYR A 192 -97.588 65.931 371.202 1.00117.21 C
ANISOU 1313 C TYR A 192 15910 15090 13534 -1175 -278 -744 C
ATOM 1314 O TYR A 192 -97.342 66.086 370.005 1.00116.95 O
ANISOU 1314 O TYR A 192 15861 15038 13536 -1017 -347 -668 O
ATOM 1315 CB TYR A 192 -99.071 67.739 372.168 1.00122.42 C
ANISOU 1315 CB TYR A 192 16725 15718 14072 -1001 -325 -1134 C
ATOM 1316 CG TYR A 192 -100.466 68.197 372.534 1.00127.10 C
ANISOU 1316 CG TYR A 192 17250 16425 14617 -832 -297 -1502 C
ATOM 1317 CD1 TYR A 192 -101.487 68.222 371.584 1.00130.01 C
ANISOU 1317 CD1 TYR A 192 17472 16919 15005 -538 -322 -1742 C
ATOM 1318 CD2 TYR A 192 -100.762 68.632 373.822 1.00129.55 C
ANISOU 1318 CD2 TYR A 192 17634 16736 14853 -952 -254 -1626 C
ATOM 1319 CE1 TYR A 192 -102.777 68.634 371.919 1.00133.21 C
ANISOU 1319 CE1 TYR A 192 17777 17480 15355 -357 -306 -2117 C
ATOM 1320 CE2 TYR A 192 -102.044 69.058 374.165 1.00132.68 C
ANISOU 1320 CE2 TYR A 192 17940 17277 15194 -784 -227 -1994 C
ATOM 1321 CZ TYR A 192 -103.049 69.058 373.211 1.00143.54 C
ANISOU 1321 CZ TYR A 192 19143 18807 16588 -478 -255 -2248 C
ATOM 1322 OH TYR A 192 -104.312 69.480 373.556 1.00149.07 O
ANISOU 1322 OH TYR A 192 19721 19695 17223 -289 -238 -2644 O
ATOM 1323 N GLU A 193 -96.688 65.440 372.087 1.00108.24 N
ANISOU 1323 N GLU A 193 14832 13912 12381 -1421 -253 -557 N
ATOM 1324 CA GLU A 193 -95.324 65.051 371.723 1.00104.68 C
ANISOU 1324 CA GLU A 193 14396 13425 11953 -1505 -310 -267 C
ATOM 1325 C GLU A 193 -95.331 63.790 370.855 1.00103.41 C
ANISOU 1325 C GLU A 193 14065 13363 11863 -1440 -256 -244 C
ATOM 1326 O GLU A 193 -94.596 63.731 369.872 1.00102.40 O
ANISOU 1326 O GLU A 193 13897 13241 11771 -1365 -314 -87 O
ATOM 1327 CB GLU A 193 -94.446 64.868 372.978 1.00105.90 C
ANISOU 1327 CB GLU A 193 14656 13528 12054 -1751 -316 -114 C
ATOM 1328 CG GLU A 193 -92.976 64.629 372.662 1.00112.58 C
ANISOU 1328 CG GLU A 193 15496 14375 12903 -1821 -395 158 C
ATOM 1329 CD GLU A 193 -91.993 64.428 373.800 1.00122.15 C
ANISOU 1329 CD GLU A 193 16797 15560 14055 -2031 -431 309 C
ATOM 1330 OE1 GLU A 193 -92.382 64.553 374.984 1.00118.40 O
ANISOU 1330 OE1 GLU A 193 16427 15030 13529 -2157 -394 227 O
ATOM 1331 OE2 GLU A 193 -90.811 64.155 373.495 1.00113.50 O
ANISOU 1331 OE2 GLU A 193 15655 14513 12955 -2066 -501 500 O
ATOM 1332 N LYS A 194 -96.160 62.796 371.220 1.00 97.96 N
ANISOU 1332 N LYS A 194 13291 12755 11176 -1489 -139 -408 N
ATOM 1333 CA LYS A 194 -96.322 61.519 370.510 1.00 96.54 C
ANISOU 1333 CA LYS A 194 12986 12657 11038 -1451 -74 -418 C
ATOM 1334 C LYS A 194 -97.065 61.699 369.164 1.00 99.96 C
ANISOU 1334 C LYS A 194 13281 13164 11534 -1214 -79 -543 C
ATOM 1335 O LYS A 194 -96.730 61.028 368.188 1.00 98.93 O
ANISOU 1335 O LYS A 194 13073 13063 11453 -1129 -87 -446 O
ATOM 1336 CB LYS A 194 -97.024 60.473 371.405 1.00 98.46 C
ANISOU 1336 CB LYS A 194 13238 12951 11223 -1629 59 -574 C
ATOM 1337 N VAL A 195 -98.060 62.605 369.115 1.00 96.79 N
ANISOU 1337 N VAL A 195 12859 12796 11121 -1087 -84 -768 N
ATOM 1338 CA VAL A 195 -98.816 62.914 367.899 1.00 96.72 C
ANISOU 1338 CA VAL A 195 12742 12853 11153 -830 -116 -915 C
ATOM 1339 C VAL A 195 -97.879 63.610 366.896 1.00 99.23 C
ANISOU 1339 C VAL A 195 13151 13057 11495 -703 -247 -695 C
ATOM 1340 O VAL A 195 -97.814 63.189 365.735 1.00 98.38 O
ANISOU 1340 O VAL A 195 12956 12985 11440 -577 -259 -654 O
ATOM 1341 CB VAL A 195 -100.113 63.717 368.196 1.00102.09 C
ANISOU 1341 CB VAL A 195 13388 13610 11791 -695 -112 -1236 C
ATOM 1342 CG1 VAL A 195 -100.733 64.286 366.917 1.00102.31 C
ANISOU 1342 CG1 VAL A 195 13357 13673 11844 -378 -200 -1369 C
ATOM 1343 CG2 VAL A 195 -101.125 62.845 368.927 1.00102.53 C
ANISOU 1343 CG2 VAL A 195 13299 13841 11815 -839 47 -1490 C
ATOM 1344 N TYR A 196 -97.115 64.623 367.373 1.00 94.33 N
ANISOU 1344 N TYR A 196 12715 12304 10821 -772 -335 -553 N
ATOM 1345 CA TYR A 196 -96.125 65.359 366.587 1.00 93.30 C
ANISOU 1345 CA TYR A 196 12711 12067 10670 -735 -447 -342 C
ATOM 1346 C TYR A 196 -95.126 64.388 365.970 1.00 97.64 C
ANISOU 1346 C TYR A 196 13155 12671 11273 -805 -427 -129 C
ATOM 1347 O TYR A 196 -94.957 64.407 364.747 1.00 97.95 O
ANISOU 1347 O TYR A 196 13166 12713 11336 -678 -464 -75 O
ATOM 1348 CB TYR A 196 -95.398 66.409 367.455 1.00 93.89 C
ANISOU 1348 CB TYR A 196 13004 12014 10656 -886 -518 -224 C
ATOM 1349 CG TYR A 196 -94.264 67.134 366.760 1.00 93.82 C
ANISOU 1349 CG TYR A 196 13140 11915 10594 -936 -613 -1 C
ATOM 1350 CD1 TYR A 196 -94.518 68.157 365.853 1.00 96.22 C
ANISOU 1350 CD1 TYR A 196 13618 12109 10834 -777 -709 -38 C
ATOM 1351 CD2 TYR A 196 -92.935 66.830 367.046 1.00 93.67 C
ANISOU 1351 CD2 TYR A 196 13100 11929 10562 -1153 -614 231 C
ATOM 1352 CE1 TYR A 196 -93.479 68.823 365.204 1.00 97.43 C
ANISOU 1352 CE1 TYR A 196 13934 12179 10905 -874 -781 158 C
ATOM 1353 CE2 TYR A 196 -91.886 67.515 366.433 1.00 94.77 C
ANISOU 1353 CE2 TYR A 196 13352 12029 10629 -1244 -685 411 C
ATOM 1354 CZ TYR A 196 -92.164 68.509 365.507 1.00102.11 C
ANISOU 1354 CZ TYR A 196 14470 12840 11486 -1127 -759 378 C
ATOM 1355 OH TYR A 196 -91.139 69.166 364.872 1.00101.09 O
ANISOU 1355 OH TYR A 196 14480 12674 11257 -1262 -814 546 O
ATOM 1356 N HIS A 197 -94.506 63.512 366.802 1.00 93.13 N
ANISOU 1356 N HIS A 197 12536 12142 10709 -987 -374 -23 N
ATOM 1357 CA HIS A 197 -93.516 62.534 366.349 1.00 92.11 C
ANISOU 1357 CA HIS A 197 12310 12075 10611 -1027 -369 161 C
ATOM 1358 C HIS A 197 -94.046 61.603 365.259 1.00 96.22 C
ANISOU 1358 C HIS A 197 12686 12673 11200 -871 -318 93 C
ATOM 1359 O HIS A 197 -93.333 61.351 364.283 1.00 94.92 O
ANISOU 1359 O HIS A 197 12462 12544 11061 -808 -350 227 O
ATOM 1360 CB HIS A 197 -92.915 61.742 367.515 1.00 92.58 C
ANISOU 1360 CB HIS A 197 12385 12149 10641 -1207 -344 246 C
ATOM 1361 CG HIS A 197 -91.925 60.710 367.070 1.00 95.44 C
ANISOU 1361 CG HIS A 197 12659 12584 11019 -1197 -362 408 C
ATOM 1362 ND1 HIS A 197 -90.713 61.068 366.518 1.00 97.29 N
ANISOU 1362 ND1 HIS A 197 12858 12867 11239 -1205 -440 586 N
ATOM 1363 CD2 HIS A 197 -92.025 59.363 367.058 1.00 96.64 C
ANISOU 1363 CD2 HIS A 197 12761 12775 11182 -1172 -313 396 C
ATOM 1364 CE1 HIS A 197 -90.105 59.934 366.217 1.00 96.12 C
ANISOU 1364 CE1 HIS A 197 12615 12802 11104 -1156 -443 668 C
ATOM 1365 NE2 HIS A 197 -90.853 58.884 366.527 1.00 96.11 N
ANISOU 1365 NE2 HIS A 197 12625 12777 11114 -1126 -375 567 N
ATOM 1366 N ILE A 198 -95.295 61.116 365.412 1.00 93.63 N
ANISOU 1366 N ILE A 198 12296 12389 10891 -822 -234 -126 N
ATOM 1367 CA ILE A 198 -95.923 60.246 364.411 1.00 93.34 C
ANISOU 1367 CA ILE A 198 12126 12434 10906 -691 -179 -218 C
ATOM 1368 C ILE A 198 -96.167 61.030 363.097 1.00 96.46 C
ANISOU 1368 C ILE A 198 12500 12818 11333 -477 -248 -249 C
ATOM 1369 O ILE A 198 -95.806 60.544 362.023 1.00 94.79 O
ANISOU 1369 O ILE A 198 12219 12635 11161 -387 -256 -160 O
ATOM 1370 CB ILE A 198 -97.186 59.525 364.971 1.00 96.94 C
ANISOU 1370 CB ILE A 198 12519 12970 11345 -748 -60 -463 C
ATOM 1371 CG1 ILE A 198 -96.785 58.506 366.054 1.00 97.53 C
ANISOU 1371 CG1 ILE A 198 12669 13024 11365 -969 3 -391 C
ATOM 1372 CG2 ILE A 198 -97.983 58.826 363.849 1.00 97.33 C
ANISOU 1372 CG2 ILE A 198 12426 13118 11436 -610 -7 -595 C
ATOM 1373 CD1 ILE A 198 -97.934 58.081 367.008 1.00107.83 C
ANISOU 1373 CD1 ILE A 198 13982 14385 12602 -1127 126 -631 C
ATOM 1374 N CYS A 199 -96.726 62.254 363.205 1.00 93.95 N
ANISOU 1374 N CYS A 199 12271 12444 10981 -392 -308 -371 N
ATOM 1375 CA CYS A 199 -97.000 63.141 362.077 1.00 94.73 C
ANISOU 1375 CA CYS A 199 12428 12492 11073 -179 -400 -415 C
ATOM 1376 C CYS A 199 -95.768 63.454 361.242 1.00 97.72 C
ANISOU 1376 C CYS A 199 12894 12799 11438 -203 -470 -164 C
ATOM 1377 O CYS A 199 -95.850 63.417 360.012 1.00 97.62 O
ANISOU 1377 O CYS A 199 12860 12787 11444 -55 -500 -158 O
ATOM 1378 CB CYS A 199 -97.695 64.412 362.544 1.00 97.05 C
ANISOU 1378 CB CYS A 199 12865 12711 11298 -87 -473 -580 C
ATOM 1379 SG CYS A 199 -99.420 64.162 363.020 1.00102.44 S
ANISOU 1379 SG CYS A 199 13386 13549 11987 40 -403 -967 S
ATOM 1380 N VAL A 200 -94.627 63.745 361.909 1.00 92.69 N
ANISOU 1380 N VAL A 200 12345 12118 10755 -404 -491 29 N
ATOM 1381 CA VAL A 200 -93.339 64.034 361.265 1.00 91.24 C
ANISOU 1381 CA VAL A 200 12217 11917 10533 -490 -541 255 C
ATOM 1382 C VAL A 200 -92.916 62.788 360.480 1.00 92.98 C
ANISOU 1382 C VAL A 200 12244 12258 10825 -453 -487 339 C
ATOM 1383 O VAL A 200 -92.634 62.903 359.296 1.00 92.91 O
ANISOU 1383 O VAL A 200 12233 12255 10814 -375 -512 399 O
ATOM 1384 CB VAL A 200 -92.256 64.499 362.288 1.00 94.72 C
ANISOU 1384 CB VAL A 200 12751 12336 10902 -730 -567 407 C
ATOM 1385 CG1 VAL A 200 -90.866 64.542 361.661 1.00 94.39 C
ANISOU 1385 CG1 VAL A 200 12687 12359 10816 -853 -593 617 C
ATOM 1386 CG2 VAL A 200 -92.611 65.850 362.898 1.00 95.31 C
ANISOU 1386 CG2 VAL A 200 13065 12265 10885 -760 -634 340 C
ATOM 1387 N THR A 201 -92.946 61.606 361.129 1.00 88.48 N
ANISOU 1387 N THR A 201 11546 11771 10303 -502 -415 329 N
ATOM 1388 CA THR A 201 -92.586 60.292 360.578 1.00 87.49 C
ANISOU 1388 CA THR A 201 11273 11744 10227 -457 -369 395 C
ATOM 1389 C THR A 201 -93.421 59.959 359.344 1.00 91.74 C
ANISOU 1389 C THR A 201 11738 12299 10819 -266 -343 289 C
ATOM 1390 O THR A 201 -92.886 59.411 358.375 1.00 92.10 O
ANISOU 1390 O THR A 201 11705 12401 10888 -201 -340 383 O
ATOM 1391 CB THR A 201 -92.668 59.213 361.684 1.00 93.64 C
ANISOU 1391 CB THR A 201 12023 12551 11005 -551 -312 373 C
ATOM 1392 OG1 THR A 201 -91.816 59.595 362.767 1.00 95.62 O
ANISOU 1392 OG1 THR A 201 12348 12783 11199 -715 -354 478 O
ATOM 1393 CG2 THR A 201 -92.259 57.833 361.204 1.00 88.75 C
ANISOU 1393 CG2 THR A 201 11311 12004 10406 -493 -283 443 C
ATOM 1394 N VAL A 202 -94.716 60.307 359.364 1.00 87.48 N
ANISOU 1394 N VAL A 202 11216 11730 10292 -168 -329 80 N
ATOM 1395 CA VAL A 202 -95.586 60.063 358.221 1.00 86.80 C
ANISOU 1395 CA VAL A 202 11056 11676 10249 23 -318 -48 C
ATOM 1396 C VAL A 202 -95.213 61.014 357.077 1.00 91.08 C
ANISOU 1396 C VAL A 202 11694 12146 10766 133 -409 26 C
ATOM 1397 O VAL A 202 -95.007 60.545 355.958 1.00 91.94 O
ANISOU 1397 O VAL A 202 11741 12288 10905 225 -403 78 O
ATOM 1398 CB VAL A 202 -97.090 60.102 358.598 1.00 90.91 C
ANISOU 1398 CB VAL A 202 11527 12238 10775 99 -278 -330 C
ATOM 1399 CG1 VAL A 202 -97.988 60.141 357.356 1.00 90.67 C
ANISOU 1399 CG1 VAL A 202 11429 12248 10774 326 -300 -483 C
ATOM 1400 CG2 VAL A 202 -97.453 58.913 359.487 1.00 90.30 C
ANISOU 1400 CG2 VAL A 202 11364 12243 10701 -46 -161 -400 C
ATOM 1401 N LEU A 203 -95.066 62.323 357.374 1.00 86.68 N
ANISOU 1401 N LEU A 203 11320 11479 10134 105 -491 39 N
ATOM 1402 CA LEU A 203 -94.744 63.364 356.394 1.00 86.52 C
ANISOU 1402 CA LEU A 203 11479 11350 10044 173 -587 102 C
ATOM 1403 C LEU A 203 -93.341 63.293 355.790 1.00 88.73 C
ANISOU 1403 C LEU A 203 11768 11655 10289 31 -585 337 C
ATOM 1404 O LEU A 203 -93.160 63.732 354.648 1.00 88.57 O
ANISOU 1404 O LEU A 203 11849 11581 10222 95 -630 379 O
ATOM 1405 CB LEU A 203 -94.993 64.767 356.960 1.00 87.76 C
ANISOU 1405 CB LEU A 203 11885 11360 10098 169 -680 41 C
ATOM 1406 CG LEU A 203 -96.453 65.131 357.240 1.00 93.16 C
ANISOU 1406 CG LEU A 203 12587 12024 10785 382 -717 -233 C
ATOM 1407 CD1 LEU A 203 -96.546 66.417 358.024 1.00 94.64 C
ANISOU 1407 CD1 LEU A 203 13029 12067 10861 361 -808 -275 C
ATOM 1408 CD2 LEU A 203 -97.293 65.200 355.953 1.00 95.25 C
ANISOU 1408 CD2 LEU A 203 12854 12279 11057 659 -777 -375 C
ATOM 1409 N ILE A 204 -92.358 62.750 356.518 1.00 84.04 N
ANISOU 1409 N ILE A 204 11072 11155 9703 -156 -538 475 N
ATOM 1410 CA ILE A 204 -90.993 62.679 355.984 1.00 84.39 C
ANISOU 1410 CA ILE A 204 11080 11283 9702 -289 -536 665 C
ATOM 1411 C ILE A 204 -90.581 61.241 355.582 1.00 88.84 C
ANISOU 1411 C ILE A 204 11406 12004 10346 -233 -470 718 C
ATOM 1412 O ILE A 204 -89.467 61.055 355.087 1.00 89.59 O
ANISOU 1412 O ILE A 204 11425 12211 10406 -308 -465 848 O
ATOM 1413 CB ILE A 204 -89.935 63.372 356.904 1.00 88.24 C
ANISOU 1413 CB ILE A 204 11647 11786 10096 -539 -563 787 C
ATOM 1414 CG1 ILE A 204 -89.618 62.540 358.189 1.00 87.47 C
ANISOU 1414 CG1 ILE A 204 11406 11784 10046 -620 -528 808 C
ATOM 1415 CG2 ILE A 204 -90.349 64.825 357.234 1.00 90.01 C
ANISOU 1415 CG2 ILE A 204 12160 11825 10216 -591 -636 737 C
ATOM 1416 CD1 ILE A 204 -88.274 62.845 358.813 1.00 90.04 C
ANISOU 1416 CD1 ILE A 204 11712 12210 10289 -845 -550 950 C
ATOM 1417 N TYR A 205 -91.471 60.240 355.763 1.00 85.19 N
ANISOU 1417 N TYR A 205 10841 11558 9971 -105 -420 606 N
ATOM 1418 CA TYR A 205 -91.148 58.865 355.391 1.00 84.60 C
ANISOU 1418 CA TYR A 205 10599 11596 9948 -39 -368 649 C
ATOM 1419 C TYR A 205 -92.300 58.128 354.681 1.00 88.52 C
ANISOU 1419 C TYR A 205 11042 12077 10513 137 -323 511 C
ATOM 1420 O TYR A 205 -92.283 58.052 353.453 1.00 88.33 O
ANISOU 1420 O TYR A 205 10989 12068 10503 245 -325 529 O
ATOM 1421 CB TYR A 205 -90.608 58.050 356.590 1.00 85.80 C
ANISOU 1421 CB TYR A 205 10695 11811 10094 -135 -351 700 C
ATOM 1422 CG TYR A 205 -89.972 56.736 356.184 1.00 87.24 C
ANISOU 1422 CG TYR A 205 10755 12103 10291 -55 -330 771 C
ATOM 1423 CD1 TYR A 205 -88.671 56.692 355.682 1.00 89.34 C
ANISOU 1423 CD1 TYR A 205 10925 12502 10518 -68 -361 903 C
ATOM 1424 CD2 TYR A 205 -90.680 55.539 356.268 1.00 87.39 C
ANISOU 1424 CD2 TYR A 205 10764 12100 10341 30 -280 691 C
ATOM 1425 CE1 TYR A 205 -88.090 55.490 355.281 1.00 89.98 C
ANISOU 1425 CE1 TYR A 205 10896 12692 10601 48 -357 949 C
ATOM 1426 CE2 TYR A 205 -90.111 54.332 355.868 1.00 88.14 C
ANISOU 1426 CE2 TYR A 205 10795 12268 10427 126 -275 753 C
ATOM 1427 CZ TYR A 205 -88.814 54.311 355.377 1.00 96.83 C
ANISOU 1427 CZ TYR A 205 11794 13499 11498 157 -321 880 C
ATOM 1428 OH TYR A 205 -88.259 53.119 354.981 1.00 97.29 O
ANISOU 1428 OH TYR A 205 11793 13637 11537 291 -330 923 O
ATOM 1429 N PHE A 206 -93.268 57.572 355.436 1.00 84.53 N
ANISOU 1429 N PHE A 206 10523 11558 10035 143 -275 370 N
ATOM 1430 CA PHE A 206 -94.362 56.747 354.904 1.00 83.89 C
ANISOU 1430 CA PHE A 206 10374 11500 9999 261 -217 221 C
ATOM 1431 C PHE A 206 -95.220 57.403 353.805 1.00 87.03 C
ANISOU 1431 C PHE A 206 10779 11871 10419 427 -249 100 C
ATOM 1432 O PHE A 206 -95.362 56.789 352.746 1.00 85.69 O
ANISOU 1432 O PHE A 206 10544 11735 10279 538 -229 99 O
ATOM 1433 CB PHE A 206 -95.261 56.200 356.035 1.00 85.93 C
ANISOU 1433 CB PHE A 206 10633 11768 10248 174 -149 68 C
ATOM 1434 CG PHE A 206 -94.489 55.393 357.052 1.00 87.73 C
ANISOU 1434 CG PHE A 206 10897 12000 10438 34 -126 179 C
ATOM 1435 CD1 PHE A 206 -94.026 54.115 356.746 1.00 91.05 C
ANISOU 1435 CD1 PHE A 206 11300 12449 10847 65 -100 258 C
ATOM 1436 CD2 PHE A 206 -94.167 55.934 358.295 1.00 89.87 C
ANISOU 1436 CD2 PHE A 206 11243 12234 10670 -109 -148 209 C
ATOM 1437 CE1 PHE A 206 -93.265 53.386 357.674 1.00 92.05 C
ANISOU 1437 CE1 PHE A 206 11498 12562 10913 -24 -110 356 C
ATOM 1438 CE2 PHE A 206 -93.413 55.202 359.221 1.00 92.35 C
ANISOU 1438 CE2 PHE A 206 11611 12543 10934 -216 -150 311 C
ATOM 1439 CZ PHE A 206 -92.962 53.939 358.902 1.00 90.56 C
ANISOU 1439 CZ PHE A 206 11380 12341 10688 -162 -138 382 C
ATOM 1440 N LEU A 207 -95.789 58.614 354.037 1.00 84.24 N
ANISOU 1440 N LEU A 207 10520 11450 10038 464 -310 -9 N
ATOM 1441 CA LEU A 207 -96.655 59.259 353.040 1.00 84.62 C
ANISOU 1441 CA LEU A 207 10605 11461 10085 662 -371 -148 C
ATOM 1442 C LEU A 207 -95.926 59.570 351.703 1.00 89.39 C
ANISOU 1442 C LEU A 207 11281 12013 10670 731 -425 -1 C
ATOM 1443 O LEU A 207 -96.370 59.035 350.687 1.00 88.88 O
ANISOU 1443 O LEU A 207 11146 11983 10640 868 -412 -55 O
ATOM 1444 CB LEU A 207 -97.394 60.497 353.590 1.00 85.69 C
ANISOU 1444 CB LEU A 207 10862 11526 10171 726 -450 -307 C
ATOM 1445 CG LEU A 207 -98.159 61.365 352.567 1.00 91.48 C
ANISOU 1445 CG LEU A 207 11703 12189 10868 970 -562 -443 C
ATOM 1446 CD1 LEU A 207 -99.378 60.640 352.006 1.00 92.02 C
ANISOU 1446 CD1 LEU A 207 11594 12381 10987 1146 -530 -669 C
ATOM 1447 CD2 LEU A 207 -98.572 62.681 353.168 1.00 94.09 C
ANISOU 1447 CD2 LEU A 207 12216 12416 11117 1033 -664 -555 C
ATOM 1448 N PRO A 208 -94.825 60.368 351.644 1.00 86.28 N
ANISOU 1448 N PRO A 208 11023 11551 10210 618 -474 176 N
ATOM 1449 CA PRO A 208 -94.186 60.620 350.338 1.00 85.99 C
ANISOU 1449 CA PRO A 208 11057 11482 10132 650 -506 293 C
ATOM 1450 C PRO A 208 -93.687 59.365 349.611 1.00 89.82 C
ANISOU 1450 C PRO A 208 11363 12087 10676 666 -429 383 C
ATOM 1451 O PRO A 208 -93.745 59.340 348.384 1.00 89.94 O
ANISOU 1451 O PRO A 208 11404 12084 10685 770 -444 393 O
ATOM 1452 CB PRO A 208 -93.063 61.605 350.665 1.00 88.51 C
ANISOU 1452 CB PRO A 208 11536 11746 10346 451 -546 448 C
ATOM 1453 CG PRO A 208 -92.827 61.457 352.121 1.00 92.85 C
ANISOU 1453 CG PRO A 208 12023 12342 10913 309 -515 463 C
ATOM 1454 CD PRO A 208 -94.135 61.105 352.728 1.00 88.08 C
ANISOU 1454 CD PRO A 208 11354 11736 10377 434 -498 263 C
ATOM 1455 N LEU A 209 -93.268 58.307 350.347 1.00 85.88 N
ANISOU 1455 N LEU A 209 10712 11696 10224 585 -356 435 N
ATOM 1456 CA LEU A 209 -92.827 57.045 349.732 1.00 85.01 C
ANISOU 1456 CA LEU A 209 10459 11688 10153 631 -296 506 C
ATOM 1457 C LEU A 209 -94.000 56.288 349.085 1.00 90.90 C
ANISOU 1457 C LEU A 209 11147 12434 10957 795 -261 360 C
ATOM 1458 O LEU A 209 -93.800 55.531 348.135 1.00 90.50 O
ANISOU 1458 O LEU A 209 11031 12428 10926 876 -231 405 O
ATOM 1459 CB LEU A 209 -92.079 56.141 350.726 1.00 84.22 C
ANISOU 1459 CB LEU A 209 10268 11676 10055 531 -256 588 C
ATOM 1460 CG LEU A 209 -90.669 56.579 351.152 1.00 88.77 C
ANISOU 1460 CG LEU A 209 10833 12327 10570 386 -285 745 C
ATOM 1461 CD1 LEU A 209 -90.117 55.659 352.226 1.00 88.04 C
ANISOU 1461 CD1 LEU A 209 10674 12306 10473 333 -272 788 C
ATOM 1462 CD2 LEU A 209 -89.704 56.673 349.965 1.00 90.71 C
ANISOU 1462 CD2 LEU A 209 11019 12667 10780 400 -284 852 C
ATOM 1463 N LEU A 210 -95.217 56.504 349.591 1.00 88.90 N
ANISOU 1463 N LEU A 210 10907 12149 10722 837 -264 174 N
ATOM 1464 CA LEU A 210 -96.411 55.896 349.032 1.00 89.49 C
ANISOU 1464 CA LEU A 210 10908 12259 10835 969 -232 -2 C
ATOM 1465 C LEU A 210 -96.760 56.609 347.718 1.00 91.85 C
ANISOU 1465 C LEU A 210 11270 12502 11125 1141 -308 -45 C
ATOM 1466 O LEU A 210 -97.086 55.953 346.731 1.00 91.26 O
ANISOU 1466 O LEU A 210 11134 12462 11078 1250 -286 -81 O
ATOM 1467 CB LEU A 210 -97.559 56.030 350.029 1.00 91.00 C
ANISOU 1467 CB LEU A 210 11070 12479 11025 943 -212 -217 C
ATOM 1468 CG LEU A 210 -98.602 54.930 349.968 1.00 97.14 C
ANISOU 1468 CG LEU A 210 11730 13358 11822 956 -125 -393 C
ATOM 1469 CD1 LEU A 210 -98.218 53.769 350.901 1.00 97.15 C
ANISOU 1469 CD1 LEU A 210 11725 13385 11802 772 -30 -327 C
ATOM 1470 CD2 LEU A 210 -100.002 55.492 350.289 1.00100.83 C
ANISOU 1470 CD2 LEU A 210 12140 13892 12278 1022 -140 -680 C
ATOM 1471 N VAL A 211 -96.643 57.953 347.706 1.00 86.62 N
ANISOU 1471 N VAL A 211 10767 11736 10407 1159 -404 -35 N
ATOM 1472 CA VAL A 211 -96.909 58.807 346.548 1.00 85.34 C
ANISOU 1472 CA VAL A 211 10752 11476 10199 1316 -504 -69 C
ATOM 1473 C VAL A 211 -95.887 58.508 345.439 1.00 85.93 C
ANISOU 1473 C VAL A 211 10848 11546 10257 1282 -482 122 C
ATOM 1474 O VAL A 211 -96.297 58.217 344.317 1.00 84.71 O
ANISOU 1474 O VAL A 211 10687 11385 10114 1425 -495 77 O
ATOM 1475 CB VAL A 211 -97.011 60.312 346.943 1.00 90.02 C
ANISOU 1475 CB VAL A 211 11577 11928 10700 1330 -621 -107 C
ATOM 1476 CG1 VAL A 211 -97.183 61.201 345.718 1.00 91.12 C
ANISOU 1476 CG1 VAL A 211 11943 11924 10753 1491 -742 -128 C
ATOM 1477 CG2 VAL A 211 -98.159 60.548 347.923 1.00 90.02 C
ANISOU 1477 CG2 VAL A 211 11526 11963 10715 1407 -642 -335 C
ATOM 1478 N ILE A 212 -94.574 58.517 345.769 1.00 81.49 N
ANISOU 1478 N ILE A 212 10288 11013 9663 1091 -444 316 N
ATOM 1479 CA ILE A 212 -93.480 58.187 344.835 1.00 80.92 C
ANISOU 1479 CA ILE A 212 10193 10992 9562 1031 -407 482 C
ATOM 1480 C ILE A 212 -93.655 56.737 344.350 1.00 86.50 C
ANISOU 1480 C ILE A 212 10709 11805 10351 1130 -328 470 C
ATOM 1481 O ILE A 212 -93.512 56.474 343.160 1.00 87.03 O
ANISOU 1481 O ILE A 212 10778 11878 10411 1206 -320 506 O
ATOM 1482 CB ILE A 212 -92.059 58.442 345.440 1.00 83.51 C
ANISOU 1482 CB ILE A 212 10505 11394 9830 803 -379 650 C
ATOM 1483 CG1 ILE A 212 -91.859 59.917 345.811 1.00 84.72 C
ANISOU 1483 CG1 ILE A 212 10890 11426 9873 674 -455 670 C
ATOM 1484 CG2 ILE A 212 -90.951 57.980 344.495 1.00 83.34 C
ANISOU 1484 CG2 ILE A 212 10398 11491 9776 749 -328 783 C
ATOM 1485 CD1 ILE A 212 -90.678 60.190 346.752 1.00 91.20 C
ANISOU 1485 CD1 ILE A 212 11677 12339 10636 429 -430 796 C
ATOM 1486 N GLY A 213 -93.993 55.832 345.269 1.00 83.72 N
ANISOU 1486 N GLY A 213 10230 11521 10060 1117 -273 417 N
ATOM 1487 CA GLY A 213 -94.243 54.425 344.972 1.00 83.04 C
ANISOU 1487 CA GLY A 213 10018 11508 10024 1190 -202 394 C
ATOM 1488 C GLY A 213 -95.309 54.250 343.914 1.00 87.44 C
ANISOU 1488 C GLY A 213 10577 12037 10609 1353 -211 263 C
ATOM 1489 O GLY A 213 -95.093 53.528 342.943 1.00 87.60 O
ANISOU 1489 O GLY A 213 10557 12088 10640 1425 -180 311 O
ATOM 1490 N TYR A 214 -96.440 54.969 344.063 1.00 84.04 N
ANISOU 1490 N TYR A 214 10193 11557 10180 1426 -266 85 N
ATOM 1491 CA TYR A 214 -97.564 54.978 343.132 1.00 83.67 C
ANISOU 1491 CA TYR A 214 10139 11503 10148 1603 -302 -81 C
ATOM 1492 C TYR A 214 -97.116 55.479 341.758 1.00 88.78 C
ANISOU 1492 C TYR A 214 10903 12071 10759 1697 -363 11 C
ATOM 1493 O TYR A 214 -97.387 54.827 340.742 1.00 88.38 O
ANISOU 1493 O TYR A 214 10808 12043 10728 1801 -344 -12 O
ATOM 1494 CB TYR A 214 -98.721 55.865 343.662 1.00 85.48 C
ANISOU 1494 CB TYR A 214 10398 11717 10364 1688 -378 -305 C
ATOM 1495 CG TYR A 214 -99.754 56.158 342.595 1.00 89.15 C
ANISOU 1495 CG TYR A 214 10881 12173 10819 1914 -460 -479 C
ATOM 1496 CD1 TYR A 214 -100.744 55.230 342.281 1.00 91.19 C
ANISOU 1496 CD1 TYR A 214 10977 12557 11114 1984 -408 -649 C
ATOM 1497 CD2 TYR A 214 -99.682 57.318 341.828 1.00 91.62 C
ANISOU 1497 CD2 TYR A 214 11398 12346 11066 2048 -595 -468 C
ATOM 1498 CE1 TYR A 214 -101.646 55.455 341.240 1.00 93.62 C
ANISOU 1498 CE1 TYR A 214 11285 12877 11409 2202 -494 -813 C
ATOM 1499 CE2 TYR A 214 -100.568 57.548 340.774 1.00 93.72 C
ANISOU 1499 CE2 TYR A 214 11705 12593 11310 2282 -691 -622 C
ATOM 1500 CZ TYR A 214 -101.555 56.617 340.489 1.00100.86 C
ANISOU 1500 CZ TYR A 214 12406 13649 12268 2369 -643 -800 C
ATOM 1501 OH TYR A 214 -102.421 56.844 339.448 1.00 99.48 O
ANISOU 1501 OH TYR A 214 12256 13474 12066 2609 -749 -965 O
ATOM 1502 N ALA A 215 -96.471 56.665 341.738 1.00 85.57 N
ANISOU 1502 N ALA A 215 10670 11563 10281 1643 -434 106 N
ATOM 1503 CA ALA A 215 -96.030 57.339 340.528 1.00 85.64 C
ANISOU 1503 CA ALA A 215 10856 11469 10213 1683 -496 189 C
ATOM 1504 C ALA A 215 -95.118 56.493 339.661 1.00 89.19 C
ANISOU 1504 C ALA A 215 11225 11992 10671 1632 -412 342 C
ATOM 1505 O ALA A 215 -95.453 56.283 338.498 1.00 89.55 O
ANISOU 1505 O ALA A 215 11307 12006 10711 1756 -429 316 O
ATOM 1506 CB ALA A 215 -95.379 58.670 340.866 1.00 87.24 C
ANISOU 1506 CB ALA A 215 11284 11555 10307 1559 -566 272 C
ATOM 1507 N TYR A 216 -94.011 55.966 340.222 1.00 85.24 N
ANISOU 1507 N TYR A 216 10607 11601 10179 1473 -329 484 N
ATOM 1508 CA TYR A 216 -93.041 55.173 339.460 1.00 84.98 C
ANISOU 1508 CA TYR A 216 10478 11671 10140 1443 -254 613 C
ATOM 1509 C TYR A 216 -93.533 53.767 339.084 1.00 88.61 C
ANISOU 1509 C TYR A 216 10794 12196 10677 1576 -193 565 C
ATOM 1510 O TYR A 216 -93.007 53.216 338.113 1.00 87.49 O
ANISOU 1510 O TYR A 216 10616 12105 10523 1613 -153 638 O
ATOM 1511 CB TYR A 216 -91.654 55.123 340.127 1.00 85.79 C
ANISOU 1511 CB TYR A 216 10495 11899 10204 1261 -206 754 C
ATOM 1512 CG TYR A 216 -90.915 56.448 340.068 1.00 88.56 C
ANISOU 1512 CG TYR A 216 11002 12208 10437 1084 -244 829 C
ATOM 1513 CD1 TYR A 216 -90.955 57.246 338.922 1.00 91.26 C
ANISOU 1513 CD1 TYR A 216 11545 12442 10687 1077 -283 839 C
ATOM 1514 CD2 TYR A 216 -90.161 56.897 341.148 1.00 89.39 C
ANISOU 1514 CD2 TYR A 216 11086 12375 10502 904 -243 888 C
ATOM 1515 CE1 TYR A 216 -90.289 58.472 338.868 1.00 92.23 C
ANISOU 1515 CE1 TYR A 216 11872 12505 10665 875 -314 905 C
ATOM 1516 CE2 TYR A 216 -89.484 58.117 341.101 1.00 91.35 C
ANISOU 1516 CE2 TYR A 216 11504 12586 10618 702 -271 952 C
ATOM 1517 CZ TYR A 216 -89.560 58.906 339.963 1.00 98.32 C
ANISOU 1517 CZ TYR A 216 12614 13348 11396 678 -304 960 C
ATOM 1518 OH TYR A 216 -88.904 60.111 339.923 1.00101.20 O
ANISOU 1518 OH TYR A 216 13201 13655 11595 443 -329 1021 O
ATOM 1519 N THR A 217 -94.554 53.202 339.774 1.00 85.12 N
ANISOU 1519 N THR A 217 10289 11756 10298 1634 -183 432 N
ATOM 1520 CA THR A 217 -95.055 51.901 339.300 1.00 84.91 C
ANISOU 1520 CA THR A 217 10173 11775 10313 1730 -124 380 C
ATOM 1521 C THR A 217 -95.843 52.129 337.994 1.00 89.12 C
ANISOU 1521 C THR A 217 10766 12250 10847 1877 -167 294 C
ATOM 1522 O THR A 217 -95.515 51.511 336.982 1.00 89.97 O
ANISOU 1522 O THR A 217 10859 12376 10949 1936 -132 358 O
ATOM 1523 CB THR A 217 -95.811 51.071 340.355 1.00 91.67 C
ANISOU 1523 CB THR A 217 10961 12668 11200 1695 -78 266 C
ATOM 1524 OG1 THR A 217 -97.093 51.633 340.592 1.00103.35 O
ANISOU 1524 OG1 THR A 217 12450 14123 12695 1735 -120 73 O
ATOM 1525 CG2 THR A 217 -95.050 50.904 341.639 1.00 83.49 C
ANISOU 1525 CG2 THR A 217 9905 11667 10150 1562 -53 351 C
ATOM 1526 N VAL A 218 -96.812 53.085 338.009 1.00 83.66 N
ANISOU 1526 N VAL A 218 10153 11487 10148 1950 -255 149 N
ATOM 1527 CA VAL A 218 -97.626 53.480 336.860 1.00 82.96 C
ANISOU 1527 CA VAL A 218 10146 11333 10042 2119 -333 41 C
ATOM 1528 C VAL A 218 -96.709 53.878 335.683 1.00 89.13 C
ANISOU 1528 C VAL A 218 11061 12041 10762 2117 -350 198 C
ATOM 1529 O VAL A 218 -96.904 53.382 334.568 1.00 90.83 O
ANISOU 1529 O VAL A 218 11277 12254 10981 2216 -341 193 O
ATOM 1530 CB VAL A 218 -98.664 54.587 337.227 1.00 86.56 C
ANISOU 1530 CB VAL A 218 10689 11726 10473 2223 -455 -145 C
ATOM 1531 CG1 VAL A 218 -99.359 55.156 335.994 1.00 86.67 C
ANISOU 1531 CG1 VAL A 218 10833 11654 10443 2431 -572 -250 C
ATOM 1532 CG2 VAL A 218 -99.700 54.067 338.215 1.00 86.28 C
ANISOU 1532 CG2 VAL A 218 10486 11808 10488 2221 -419 -341 C
ATOM 1533 N VAL A 219 -95.708 54.740 335.941 1.00 84.80 N
ANISOU 1533 N VAL A 219 10626 11447 10146 1980 -367 329 N
ATOM 1534 CA VAL A 219 -94.743 55.206 334.943 1.00 84.86 C
ANISOU 1534 CA VAL A 219 10771 11409 10062 1907 -365 471 C
ATOM 1535 C VAL A 219 -93.886 54.021 334.445 1.00 90.44 C
ANISOU 1535 C VAL A 219 11310 12255 10797 1869 -247 587 C
ATOM 1536 O VAL A 219 -93.657 53.895 333.240 1.00 91.64 O
ANISOU 1536 O VAL A 219 11521 12391 10908 1905 -233 631 O
ATOM 1537 CB VAL A 219 -93.903 56.390 335.499 1.00 88.55 C
ANISOU 1537 CB VAL A 219 11393 11823 10430 1718 -397 562 C
ATOM 1538 CG1 VAL A 219 -92.626 56.628 334.700 1.00 88.94 C
ANISOU 1538 CG1 VAL A 219 11512 11910 10373 1546 -342 718 C
ATOM 1539 CG2 VAL A 219 -94.731 57.658 335.562 1.00 89.03 C
ANISOU 1539 CG2 VAL A 219 11716 11694 10418 1801 -541 452 C
ATOM 1540 N GLY A 220 -93.470 53.159 335.368 1.00 86.71 N
ANISOU 1540 N GLY A 220 10653 11910 10384 1816 -173 621 N
ATOM 1541 CA GLY A 220 -92.678 51.971 335.076 1.00 86.82 C
ANISOU 1541 CA GLY A 220 10518 12057 10413 1823 -81 709 C
ATOM 1542 C GLY A 220 -93.376 51.042 334.106 1.00 91.57 C
ANISOU 1542 C GLY A 220 11100 12639 11052 1982 -59 651 C
ATOM 1543 O GLY A 220 -92.777 50.633 333.102 1.00 92.27 O
ANISOU 1543 O GLY A 220 11174 12775 11110 2014 -16 723 O
ATOM 1544 N ILE A 221 -94.671 50.745 334.387 1.00 86.71 N
ANISOU 1544 N ILE A 221 10483 11971 10493 2072 -87 504 N
ATOM 1545 CA ILE A 221 -95.539 49.925 333.539 1.00 86.49 C
ANISOU 1545 CA ILE A 221 10440 11929 10492 2205 -73 415 C
ATOM 1546 C ILE A 221 -95.667 50.573 332.136 1.00 92.42 C
ANISOU 1546 C ILE A 221 11318 12596 11202 2290 -130 418 C
ATOM 1547 O ILE A 221 -95.556 49.873 331.129 1.00 93.81 O
ANISOU 1547 O ILE A 221 11486 12784 11372 2360 -91 450 O
ATOM 1548 CB ILE A 221 -96.918 49.663 334.215 1.00 89.02 C
ANISOU 1548 CB ILE A 221 10713 12253 10857 2239 -89 225 C
ATOM 1549 CG1 ILE A 221 -96.754 48.749 335.447 1.00 87.92 C
ANISOU 1549 CG1 ILE A 221 10491 12182 10731 2133 -15 234 C
ATOM 1550 CG2 ILE A 221 -97.944 49.060 333.221 1.00 89.49 C
ANISOU 1550 CG2 ILE A 221 10762 12313 10927 2363 -89 103 C
ATOM 1551 CD1 ILE A 221 -97.750 48.962 336.505 1.00 86.55 C
ANISOU 1551 CD1 ILE A 221 10282 12027 10577 2081 -27 66 C
ATOM 1552 N ARG A 222 -95.833 51.901 332.075 1.00 88.07 N
ANISOU 1552 N ARG A 222 10915 11944 10603 2281 -225 391 N
ATOM 1553 CA ARG A 222 -95.935 52.617 330.810 1.00 88.36 C
ANISOU 1553 CA ARG A 222 11140 11866 10568 2353 -297 395 C
ATOM 1554 C ARG A 222 -94.643 52.536 329.961 1.00 93.54 C
ANISOU 1554 C ARG A 222 11835 12552 11153 2247 -224 566 C
ATOM 1555 O ARG A 222 -94.724 52.300 328.755 1.00 92.89 O
ANISOU 1555 O ARG A 222 11819 12432 11042 2324 -222 575 O
ATOM 1556 CB ARG A 222 -96.380 54.079 331.041 1.00 87.36 C
ANISOU 1556 CB ARG A 222 11225 11595 10372 2372 -433 323 C
ATOM 1557 CG ARG A 222 -96.671 54.860 329.760 1.00 95.05 C
ANISOU 1557 CG ARG A 222 12466 12406 11243 2472 -541 303 C
ATOM 1558 CD ARG A 222 -97.878 54.344 328.975 1.00101.15 C
ANISOU 1558 CD ARG A 222 13211 13165 12057 2705 -604 145 C
ATOM 1559 NE ARG A 222 -99.143 54.857 329.502 1.00107.84 N
ANISOU 1559 NE ARG A 222 14057 13995 12924 2873 -729 -72 N
ATOM 1560 CZ ARG A 222 -99.671 56.029 329.161 1.00124.69 C
ANISOU 1560 CZ ARG A 222 16445 15971 14960 3018 -904 -173 C
ATOM 1561 NH1 ARG A 222 -99.050 56.816 328.289 1.00111.66 N
ANISOU 1561 NH1 ARG A 222 15114 14137 13174 2986 -969 -63 N
ATOM 1562 NH2 ARG A 222 -100.818 56.427 329.695 1.00115.25 N
ANISOU 1562 NH2 ARG A 222 15204 14803 13782 3197 -1018 -397 N
ATOM 1563 N LEU A 223 -93.467 52.709 330.592 1.00 91.06 N
ANISOU 1563 N LEU A 223 11464 12329 10805 2070 -163 686 N
ATOM 1564 CA LEU A 223 -92.178 52.707 329.900 1.00 91.66 C
ANISOU 1564 CA LEU A 223 11537 12495 10796 1940 -85 818 C
ATOM 1565 C LEU A 223 -91.629 51.330 329.553 1.00 97.69 C
ANISOU 1565 C LEU A 223 12098 13418 11602 2003 19 866 C
ATOM 1566 O LEU A 223 -90.911 51.201 328.566 1.00 98.60 O
ANISOU 1566 O LEU A 223 12223 13594 11648 1968 74 929 O
ATOM 1567 CB LEU A 223 -91.119 53.475 330.713 1.00 92.01 C
ANISOU 1567 CB LEU A 223 11577 12617 10767 1716 -64 900 C
ATOM 1568 CG LEU A 223 -91.240 54.999 330.821 1.00 96.60 C
ANISOU 1568 CG LEU A 223 12434 13034 11237 1591 -154 893 C
ATOM 1569 CD1 LEU A 223 -90.344 55.522 331.918 1.00 96.93 C
ANISOU 1569 CD1 LEU A 223 12421 13174 11234 1377 -128 955 C
ATOM 1570 CD2 LEU A 223 -90.842 55.685 329.534 1.00 98.21 C
ANISOU 1570 CD2 LEU A 223 12878 13150 11288 1495 -159 941 C
ATOM 1571 N TRP A 224 -91.906 50.319 330.375 1.00 95.10 N
ANISOU 1571 N TRP A 224 11611 13158 11364 2084 46 834 N
ATOM 1572 CA TRP A 224 -91.322 48.999 330.168 1.00 95.43 C
ANISOU 1572 CA TRP A 224 11505 13333 11421 2162 127 878 C
ATOM 1573 C TRP A 224 -92.304 47.914 329.721 1.00 98.98 C
ANISOU 1573 C TRP A 224 11960 13719 11928 2327 134 805 C
ATOM 1574 O TRP A 224 -91.905 47.042 328.953 1.00100.06 O
ANISOU 1574 O TRP A 224 12060 13913 12044 2410 188 843 O
ATOM 1575 CB TRP A 224 -90.550 48.558 331.425 1.00 94.50 C
ANISOU 1575 CB TRP A 224 11241 13352 11312 2113 154 919 C
ATOM 1576 CG TRP A 224 -89.207 49.231 331.554 1.00 96.86 C
ANISOU 1576 CG TRP A 224 11469 13803 11530 1958 179 1000 C
ATOM 1577 CD1 TRP A 224 -88.060 48.896 330.895 1.00100.65 C
ANISOU 1577 CD1 TRP A 224 11835 14470 11938 1947 243 1054 C
ATOM 1578 CD2 TRP A 224 -88.886 50.379 332.360 1.00 97.38 C
ANISOU 1578 CD2 TRP A 224 11568 13871 11561 1775 146 1018 C
ATOM 1579 NE1 TRP A 224 -87.041 49.753 331.247 1.00101.19 N
ANISOU 1579 NE1 TRP A 224 11843 14681 11924 1750 258 1095 N
ATOM 1580 CE2 TRP A 224 -87.521 50.678 332.139 1.00102.45 C
ANISOU 1580 CE2 TRP A 224 12107 14715 12103 1635 199 1083 C
ATOM 1581 CE3 TRP A 224 -89.617 51.184 333.252 1.00 98.31 C
ANISOU 1581 CE3 TRP A 224 11789 13852 11711 1714 79 974 C
ATOM 1582 CZ2 TRP A 224 -86.868 51.735 332.794 1.00102.60 C
ANISOU 1582 CZ2 TRP A 224 12137 14796 12050 1412 189 1113 C
ATOM 1583 CZ3 TRP A 224 -88.969 52.236 333.890 1.00100.45 C
ANISOU 1583 CZ3 TRP A 224 12091 14159 11916 1518 62 1014 C
ATOM 1584 CH2 TRP A 224 -87.613 52.505 333.656 1.00102.23 C
ANISOU 1584 CH2 TRP A 224 12227 14577 12037 1357 118 1087 C
ATOM 1585 N ALA A 225 -93.559 47.949 330.178 1.00 93.81 N
ANISOU 1585 N ALA A 225 11346 12968 11330 2367 85 689 N
ATOM 1586 CA ALA A 225 -94.534 46.925 329.800 1.00 92.72 C
ANISOU 1586 CA ALA A 225 11209 12795 11227 2480 100 599 C
ATOM 1587 C ALA A 225 -95.344 47.271 328.542 1.00 96.13 C
ANISOU 1587 C ALA A 225 11737 13135 11652 2573 51 529 C
ATOM 1588 O ALA A 225 -95.208 48.368 327.983 1.00 97.39 O
ANISOU 1588 O ALA A 225 12002 13230 11773 2557 -7 548 O
ATOM 1589 CB ALA A 225 -95.464 46.631 330.973 1.00 93.12 C
ANISOU 1589 CB ALA A 225 11224 12838 11320 2447 90 482 C
ATOM 1590 N SER A 226 -96.170 46.305 328.087 1.00 90.25 N
ANISOU 1590 N SER A 226 10984 12382 10926 2661 71 445 N
ATOM 1591 CA SER A 226 -97.095 46.397 326.946 1.00 89.25 C
ANISOU 1591 CA SER A 226 10927 12188 10795 2769 21 351 C
ATOM 1592 C SER A 226 -98.034 45.179 326.986 1.00 92.37 C
ANISOU 1592 C SER A 226 11272 12618 11208 2802 64 239 C
ATOM 1593 O SER A 226 -97.996 44.406 327.953 1.00 91.69 O
ANISOU 1593 O SER A 226 11133 12580 11124 2726 124 233 O
ATOM 1594 CB SER A 226 -96.339 46.475 325.621 1.00 92.07 C
ANISOU 1594 CB SER A 226 11367 12513 11102 2810 38 465 C
ATOM 1595 OG SER A 226 -97.213 46.627 324.515 1.00100.36 O
ANISOU 1595 OG SER A 226 12512 13483 12139 2919 -27 378 O
ATOM 1596 N ASN A1001 -98.889 45.024 325.968 1.00 88.86 N
ANISOU 1596 N ASN A1001 10864 12143 10755 2897 30 143 N
ATOM 1597 CA ASN A1001 -99.825 43.906 325.873 1.00 88.93 C
ANISOU 1597 CA ASN A1001 10838 12196 10756 2899 73 21 C
ATOM 1598 C ASN A1001 -100.138 43.587 324.410 1.00 94.36 C
ANISOU 1598 C ASN A1001 11591 12843 11419 3010 57 8 C
ATOM 1599 O ASN A1001 -99.694 44.303 323.511 1.00 94.62 O
ANISOU 1599 O ASN A1001 11705 12806 11439 3086 7 86 O
ATOM 1600 CB ASN A1001 -101.107 44.193 326.674 1.00 87.66 C
ANISOU 1600 CB ASN A1001 10585 12108 10614 2859 30 -202 C
ATOM 1601 CG ASN A1001 -101.760 45.499 326.315 1.00101.31 C
ANISOU 1601 CG ASN A1001 12319 13817 12357 2978 -107 -325 C
ATOM 1602 OD1 ASN A1001 -102.318 45.671 325.230 1.00 98.40 O
ANISOU 1602 OD1 ASN A1001 11990 13426 11971 3105 -178 -405 O
ATOM 1603 ND2 ASN A1001 -101.667 46.457 327.206 1.00 91.94 N
ANISOU 1603 ND2 ASN A1001 11120 12624 11189 2953 -160 -341 N
ATOM 1604 N ILE A1002 -100.925 42.529 324.186 1.00 91.36 N
ANISOU 1604 N ILE A1002 11195 12503 11014 2995 101 -97 N
ATOM 1605 CA ILE A1002 -101.340 42.049 322.868 1.00 91.36 C
ANISOU 1605 CA ILE A1002 11253 12476 10984 3085 93 -127 C
ATOM 1606 C ILE A1002 -102.120 43.108 322.077 1.00 97.27 C
ANISOU 1606 C ILE A1002 12011 13203 11744 3215 -42 -250 C
ATOM 1607 O ILE A1002 -101.948 43.185 320.859 1.00 98.02 O
ANISOU 1607 O ILE A1002 12206 13222 11815 3315 -73 -193 O
ATOM 1608 CB ILE A1002 -102.102 40.676 322.978 1.00 94.11 C
ANISOU 1608 CB ILE A1002 11594 12882 11281 2996 174 -234 C
ATOM 1609 CG1 ILE A1002 -102.411 40.047 321.588 1.00 94.13 C
ANISOU 1609 CG1 ILE A1002 11674 12850 11243 3078 177 -243 C
ATOM 1610 CG2 ILE A1002 -103.374 40.755 323.859 1.00 94.22 C
ANISOU 1610 CG2 ILE A1002 11483 13024 11292 2891 159 -476 C
ATOM 1611 CD1 ILE A1002 -101.209 39.861 320.648 1.00 95.65 C
ANISOU 1611 CD1 ILE A1002 11981 12940 11421 3173 207 -29 C
ATOM 1612 N PHE A1003 -102.955 43.921 322.755 1.00 94.23 N
ANISOU 1612 N PHE A1003 11541 12880 11382 3231 -130 -426 N
ATOM 1613 CA PHE A1003 -103.774 44.951 322.102 1.00 94.64 C
ANISOU 1613 CA PHE A1003 11621 12914 11425 3399 -291 -577 C
ATOM 1614 C PHE A1003 -102.920 46.088 321.584 1.00100.29 C
ANISOU 1614 C PHE A1003 12516 13469 12122 3478 -373 -426 C
ATOM 1615 O PHE A1003 -103.134 46.565 320.459 1.00 99.93 O
ANISOU 1615 O PHE A1003 12605 13331 12032 3617 -475 -446 O
ATOM 1616 CB PHE A1003 -104.885 45.446 323.034 1.00 96.60 C
ANISOU 1616 CB PHE A1003 11719 13299 11686 3413 -363 -830 C
ATOM 1617 CG PHE A1003 -105.799 44.341 323.509 1.00 97.81 C
ANISOU 1617 CG PHE A1003 11702 13635 11826 3284 -268 -1007 C
ATOM 1618 CD1 PHE A1003 -106.709 43.742 322.640 1.00101.16 C
ANISOU 1618 CD1 PHE A1003 12077 14149 12212 3331 -284 -1165 C
ATOM 1619 CD2 PHE A1003 -105.740 43.885 324.820 1.00 99.02 C
ANISOU 1619 CD2 PHE A1003 11767 13870 11987 3089 -159 -1018 C
ATOM 1620 CE1 PHE A1003 -107.549 42.712 323.079 1.00102.32 C
ANISOU 1620 CE1 PHE A1003 12085 14476 12315 3159 -183 -1338 C
ATOM 1621 CE2 PHE A1003 -106.582 42.855 325.258 1.00102.20 C
ANISOU 1621 CE2 PHE A1003 12057 14432 12341 2921 -60 -1186 C
ATOM 1622 CZ PHE A1003 -107.480 42.275 324.383 1.00100.95 C
ANISOU 1622 CZ PHE A1003 11850 14373 12135 2943 -67 -1347 C
ATOM 1623 N GLU A1004 -101.917 46.484 322.396 1.00 98.10 N
ANISOU 1623 N GLU A1004 12257 13158 11859 3369 -324 -276 N
ATOM 1624 CA GLU A1004 -100.935 47.511 322.061 1.00 98.88 C
ANISOU 1624 CA GLU A1004 12531 13124 11915 3366 -369 -119 C
ATOM 1625 C GLU A1004 -100.158 47.026 320.840 1.00103.46 C
ANISOU 1625 C GLU A1004 13213 13643 12453 3363 -303 37 C
ATOM 1626 O GLU A1004 -100.051 47.753 319.856 1.00104.76 O
ANISOU 1626 O GLU A1004 13568 13685 12550 3429 -384 66 O
ATOM 1627 CB GLU A1004 -99.985 47.736 323.247 1.00 99.95 C
ANISOU 1627 CB GLU A1004 12615 13290 12073 3211 -298 2 C
ATOM 1628 CG GLU A1004 -100.163 49.065 323.950 1.00115.62 C
ANISOU 1628 CG GLU A1004 14670 15220 14041 3222 -413 -62 C
ATOM 1629 CD GLU A1004 -101.273 49.105 324.982 1.00153.51 C
ANISOU 1629 CD GLU A1004 19321 20118 18888 3260 -459 -272 C
ATOM 1630 OE1 GLU A1004 -100.959 48.979 326.189 1.00153.49 O
ANISOU 1630 OE1 GLU A1004 19210 20185 18924 3132 -389 -245 O
ATOM 1631 OE2 GLU A1004 -102.450 49.287 324.590 1.00155.96 O
ANISOU 1631 OE2 GLU A1004 19621 20450 19187 3418 -569 -476 O
ATOM 1632 N MET A1005 -99.704 45.754 320.894 1.00 99.13 N
ANISOU 1632 N MET A1005 12560 13174 11929 3297 -162 118 N
ATOM 1633 CA MET A1005 -98.947 45.013 319.882 1.00 98.16 C
ANISOU 1633 CA MET A1005 12491 13034 11771 3300 -75 252 C
ATOM 1634 C MET A1005 -99.701 44.944 318.552 1.00100.77 C
ANISOU 1634 C MET A1005 12929 13293 12067 3425 -142 176 C
ATOM 1635 O MET A1005 -99.196 45.445 317.549 1.00100.51 O
ANISOU 1635 O MET A1005 13050 13167 11972 3448 -163 262 O
ATOM 1636 CB MET A1005 -98.651 43.594 320.409 1.00 99.70 C
ANISOU 1636 CB MET A1005 12569 13323 11988 3248 54 296 C
ATOM 1637 CG MET A1005 -97.553 42.890 319.679 1.00103.10 C
ANISOU 1637 CG MET A1005 13034 13763 12376 3256 151 451 C
ATOM 1638 SD MET A1005 -97.602 41.120 319.975 1.00106.77 S
ANISOU 1638 SD MET A1005 13460 14280 12829 3268 254 452 S
ATOM 1639 CE MET A1005 -95.893 40.724 319.854 1.00103.51 C
ANISOU 1639 CE MET A1005 13031 13931 12368 3287 345 634 C
ATOM 1640 N LEU A1006 -100.910 44.344 318.555 1.00 96.84 N
ANISOU 1640 N LEU A1006 12352 12848 11594 3488 -175 4 N
ATOM 1641 CA LEU A1006 -101.749 44.187 317.364 1.00 97.14 C
ANISOU 1641 CA LEU A1006 12462 12846 11599 3613 -248 -97 C
ATOM 1642 C LEU A1006 -102.133 45.515 316.697 1.00103.77 C
ANISOU 1642 C LEU A1006 13468 13568 12391 3746 -423 -164 C
ATOM 1643 O LEU A1006 -102.254 45.538 315.477 1.00103.73 O
ANISOU 1643 O LEU A1006 13604 13477 12333 3839 -474 -159 O
ATOM 1644 CB LEU A1006 -102.991 43.329 317.635 1.00 96.69 C
ANISOU 1644 CB LEU A1006 12260 12915 11562 3618 -243 -297 C
ATOM 1645 CG LEU A1006 -102.749 41.840 317.842 1.00 99.68 C
ANISOU 1645 CG LEU A1006 12586 13353 11935 3503 -86 -236 C
ATOM 1646 CD1 LEU A1006 -104.005 41.159 318.291 1.00100.08 C
ANISOU 1646 CD1 LEU A1006 12510 13538 11977 3443 -76 -454 C
ATOM 1647 CD2 LEU A1006 -102.201 41.166 316.581 1.00100.55 C
ANISOU 1647 CD2 LEU A1006 12823 13382 12001 3550 -31 -106 C
ATOM 1648 N ARG A1007 -102.287 46.615 317.475 1.00102.15 N
ANISOU 1648 N ARG A1007 13284 13341 12188 3762 -521 -221 N
ATOM 1649 CA ARG A1007 -102.571 47.951 316.937 1.00103.30 C
ANISOU 1649 CA ARG A1007 13655 13337 12256 3898 -706 -278 C
ATOM 1650 C ARG A1007 -101.350 48.485 316.150 1.00107.48 C
ANISOU 1650 C ARG A1007 14437 13703 12696 3813 -675 -62 C
ATOM 1651 O ARG A1007 -101.537 49.153 315.132 1.00109.23 O
ANISOU 1651 O ARG A1007 14915 13767 12819 3918 -801 -80 O
ATOM 1652 CB ARG A1007 -102.996 48.925 318.044 1.00105.00 C
ANISOU 1652 CB ARG A1007 13844 13570 12482 3935 -813 -397 C
ATOM 1653 CG ARG A1007 -104.512 49.008 318.212 1.00120.67 C
ANISOU 1653 CG ARG A1007 15693 15671 14484 4121 -950 -691 C
ATOM 1654 CD ARG A1007 -104.949 50.168 319.093 1.00133.87 C
ANISOU 1654 CD ARG A1007 17397 17331 16136 4218 -1097 -827 C
ATOM 1655 NE ARG A1007 -105.442 49.722 320.400 1.00145.71 N
ANISOU 1655 NE ARG A1007 18601 19043 17719 4139 -1024 -963 N
ATOM 1656 CZ ARG A1007 -104.701 49.644 321.505 1.00156.57 C
ANISOU 1656 CZ ARG A1007 19896 20449 19146 3946 -900 -842 C
ATOM 1657 NH1 ARG A1007 -103.417 49.978 321.477 1.00140.55 N
ANISOU 1657 NH1 ARG A1007 18028 18279 17097 3814 -834 -590 N
ATOM 1658 NH2 ARG A1007 -105.239 49.228 322.644 1.00140.32 N
ANISOU 1658 NH2 ARG A1007 17594 18576 17146 3871 -839 -982 N
ATOM 1659 N ILE A1008 -100.111 48.142 316.588 1.00101.88 N
ANISOU 1659 N ILE A1008 13659 13046 12005 3621 -508 124 N
ATOM 1660 CA ILE A1008 -98.865 48.540 315.914 1.00101.36 C
ANISOU 1660 CA ILE A1008 13774 12895 11844 3491 -441 309 C
ATOM 1661 C ILE A1008 -98.646 47.737 314.616 1.00105.46 C
ANISOU 1661 C ILE A1008 14345 13398 12328 3518 -371 371 C
ATOM 1662 O ILE A1008 -98.376 48.335 313.567 1.00105.98 O
ANISOU 1662 O ILE A1008 14665 13324 12278 3509 -416 422 O
ATOM 1663 CB ILE A1008 -97.626 48.501 316.860 1.00103.28 C
ANISOU 1663 CB ILE A1008 13887 13248 12106 3291 -300 451 C
ATOM 1664 CG1 ILE A1008 -97.808 49.454 318.060 1.00103.30 C
ANISOU 1664 CG1 ILE A1008 13889 13237 12124 3254 -381 398 C
ATOM 1665 CG2 ILE A1008 -96.332 48.831 316.093 1.00104.65 C
ANISOU 1665 CG2 ILE A1008 14204 13396 12163 3131 -211 611 C
ATOM 1666 CD1 ILE A1008 -96.788 49.299 319.218 1.00109.10 C
ANISOU 1666 CD1 ILE A1008 14434 14113 12906 3084 -256 498 C
ATOM 1667 N ASP A1009 -98.760 46.393 314.688 1.00101.38 N
ANISOU 1667 N ASP A1009 13620 13009 11892 3541 -262 365 N
ATOM 1668 CA ASP A1009 -98.558 45.501 313.538 1.00101.04 C
ANISOU 1668 CA ASP A1009 13611 12961 11820 3574 -186 420 C
ATOM 1669 C ASP A1009 -99.718 45.501 312.536 1.00106.84 C
ANISOU 1669 C ASP A1009 14466 13599 12529 3737 -315 290 C
ATOM 1670 O ASP A1009 -99.490 45.242 311.349 1.00107.53 O
ANISOU 1670 O ASP A1009 14688 13616 12552 3760 -293 346 O
ATOM 1671 CB ASP A1009 -98.220 44.080 314.002 1.00101.27 C
ANISOU 1671 CB ASP A1009 13427 13135 11915 3544 -35 464 C
ATOM 1672 CG ASP A1009 -96.864 43.967 314.682 1.00108.57 C
ANISOU 1672 CG ASP A1009 14249 14166 12838 3417 91 602 C
ATOM 1673 OD1 ASP A1009 -96.082 44.945 314.625 1.00109.53 O
ANISOU 1673 OD1 ASP A1009 14455 14266 12897 3316 90 678 O
ATOM 1674 OD2 ASP A1009 -96.570 42.894 315.242 1.00111.26 O
ANISOU 1674 OD2 ASP A1009 14443 14611 13218 3418 185 627 O
ATOM 1675 N GLU A1010 -100.950 45.794 313.004 1.00103.75 N
ANISOU 1675 N GLU A1010 14017 13225 12180 3854 -451 102 N
ATOM 1676 CA GLU A1010 -102.163 45.864 312.174 1.00129.81 C
ANISOU 1676 CA GLU A1010 17392 16478 15453 4035 -602 -69 C
ATOM 1677 C GLU A1010 -102.887 47.183 312.456 1.00157.58 C
ANISOU 1677 C GLU A1010 21025 19918 18930 4171 -814 -218 C
ATOM 1678 O GLU A1010 -103.969 47.428 311.932 1.00124.10 O
ANISOU 1678 O GLU A1010 16857 15645 14651 4364 -982 -390 O
ATOM 1679 CB GLU A1010 -103.103 44.665 312.436 1.00130.50 C
ANISOU 1679 CB GLU A1010 17242 16731 15612 4061 -554 -209 C
ATOM 1680 CG GLU A1010 -102.507 43.300 312.126 1.00138.24 C
ANISOU 1680 CG GLU A1010 18164 17758 16604 3963 -371 -81 C
ATOM 1681 CD GLU A1010 -103.503 42.160 312.034 1.00154.10 C
ANISOU 1681 CD GLU A1010 20037 19881 18632 3974 -341 -223 C
ATOM 1682 OE1 GLU A1010 -103.412 41.373 311.064 1.00144.66 O
ANISOU 1682 OE1 GLU A1010 18917 18649 17397 3992 -291 -177 O
ATOM 1683 OE2 GLU A1010 -104.382 42.059 312.921 1.00146.24 O
ANISOU 1683 OE2 GLU A1010 18869 19019 17675 3947 -362 -388 O
ATOM 1684 N ASP A1017 -111.643 57.974 306.760 1.00161.44 N
ANISOU 1684 N ASP A1017 24807 18717 17816 7716 -4189 -2239 N
ATOM 1685 CA ASP A1017 -110.381 57.333 306.392 1.00159.17 C
ANISOU 1685 CA ASP A1017 24566 18324 17588 7240 -3857 -1873 C
ATOM 1686 C ASP A1017 -110.529 55.802 306.235 1.00161.32 C
ANISOU 1686 C ASP A1017 24255 18951 18088 7071 -3601 -1871 C
ATOM 1687 O ASP A1017 -110.334 55.276 305.137 1.00160.64 O
ANISOU 1687 O ASP A1017 24276 18787 17971 7017 -3557 -1779 O
ATOM 1688 CB ASP A1017 -109.305 57.647 307.434 1.00 20.00 C
ATOM 1689 N GLU A1018 -110.874 55.105 307.345 1.00156.62 N
ANISOU 1689 N GLU A1018 23080 18728 17701 6979 -3436 -1975 N
ATOM 1690 CA GLU A1018 -111.105 53.656 307.483 1.00154.25 C
ANISOU 1690 CA GLU A1018 22222 18784 17603 6800 -3190 -2003 C
ATOM 1691 C GLU A1018 -111.719 53.381 308.874 1.00157.47 C
ANISOU 1691 C GLU A1018 22120 19555 18158 6798 -3125 -2210 C
ATOM 1692 O GLU A1018 -111.539 54.187 309.796 1.00157.28 O
ANISOU 1692 O GLU A1018 22166 19478 18117 6818 -3174 -2219 O
ATOM 1693 CB GLU A1018 -109.805 52.871 307.299 1.00 20.00 C
ATOM 1694 N ALA A1019 -112.445 52.253 309.020 1.00153.05 N
ANISOU 1694 N ALA A1019 21069 19358 17724 6752 -3011 -2380 N
ATOM 1695 CA ALA A1019 -113.087 51.862 310.282 1.00152.35 C
ANISOU 1695 CA ALA A1019 20485 19645 17757 6702 -2923 -2595 C
ATOM 1696 C ALA A1019 -112.068 51.353 311.322 1.00152.42 C
ANISOU 1696 C ALA A1019 20341 19671 17899 6292 -2603 -2330 C
ATOM 1697 O ALA A1019 -111.037 50.793 310.942 1.00150.66 O
ANISOU 1697 O ALA A1019 20240 19292 17711 6023 -2398 -2020 O
ATOM 1698 CB ALA A1019 -114.146 50.803 310.018 1.00153.53 C
ANISOU 1698 CB ALA A1019 20214 20163 17959 6726 -2889 -2853 C
ATOM 1699 N GLU A1020 -112.356 51.556 312.628 1.00147.23 N
ANISOU 1699 N GLU A1020 19417 19215 17308 6259 -2568 -2467 N
ATOM 1700 CA GLU A1020 -111.488 51.123 313.730 1.00144.15 C
ANISOU 1700 CA GLU A1020 18876 18860 17036 5902 -2294 -2252 C
ATOM 1701 C GLU A1020 -111.563 49.609 313.911 1.00145.60 C
ANISOU 1701 C GLU A1020 18702 19288 17330 5619 -2028 -2227 C
ATOM 1702 O GLU A1020 -112.666 49.053 313.947 1.00146.07 O
ANISOU 1702 O GLU A1020 18452 19649 17400 5679 -2051 -2512 O
ATOM 1703 CB GLU A1020 -111.874 51.832 315.030 1.00 20.00 C
ATOM 1704 N LYS A1021 -110.383 48.949 314.006 1.00139.23 N
ANISOU 1704 N LYS A1021 17956 18358 16587 5311 -1783 -1898 N
ATOM 1705 CA LYS A1021 -110.236 47.494 314.156 1.00136.98 C
ANISOU 1705 CA LYS A1021 17432 18233 16383 5036 -1530 -1822 C
ATOM 1706 C LYS A1021 -110.575 47.007 315.573 1.00140.57 C
ANISOU 1706 C LYS A1021 17548 18954 16910 4854 -1394 -1951 C
ATOM 1707 O LYS A1021 -110.042 47.519 316.565 1.00139.56 O
ANISOU 1707 O LYS A1021 17419 18789 16817 4778 -1357 -1878 O
ATOM 1708 CB LYS A1021 -108.841 47.010 313.705 1.00136.92 C
ANISOU 1708 CB LYS A1021 17621 18006 16395 4824 -1344 -1451 C
ATOM 1709 CG LYS A1021 -108.430 47.435 312.294 1.00145.65 C
ANISOU 1709 CG LYS A1021 19066 18859 17414 4946 -1442 -1316 C
ATOM 1710 CD LYS A1021 -109.032 46.557 311.206 1.00154.09 C
ANISOU 1710 CD LYS A1021 20092 19995 18460 4997 -1442 -1395 C
ATOM 1711 CE LYS A1021 -108.845 47.168 309.839 1.00161.31 C
ANISOU 1711 CE LYS A1021 21361 20662 19268 5165 -1592 -1320 C
ATOM 1712 NZ LYS A1021 -109.605 46.427 308.801 1.00167.68 N
ANISOU 1712 NZ LYS A1021 22121 21547 20044 5257 -1635 -1444 N
ATOM 1713 N LEU A1022 -111.472 46.006 315.639 1.00137.45 N
ANISOU 1713 N LEU A1022 16882 18823 16518 4761 -1314 -2147 N
ATOM 1714 CA LEU A1022 -112.034 45.372 316.842 1.00136.86 C
ANISOU 1714 CA LEU A1022 16486 19040 16474 4553 -1177 -2325 C
ATOM 1715 C LEU A1022 -111.243 44.113 317.274 1.00135.34 C
ANISOU 1715 C LEU A1022 16288 18815 16321 4205 -903 -2088 C
ATOM 1716 O LEU A1022 -111.614 42.987 316.930 1.00134.28 O
ANISOU 1716 O LEU A1022 16069 18797 16154 4049 -787 -2138 O
ATOM 1717 CB LEU A1022 -113.545 45.057 316.611 1.00139.31 C
ANISOU 1717 CB LEU A1022 16521 19686 16723 4637 -1261 -2720 C
ATOM 1718 CG LEU A1022 -114.050 44.942 315.134 1.00145.05 C
ANISOU 1718 CG LEU A1022 17340 20382 17389 4831 -1393 -2788 C
ATOM 1719 CD1 LEU A1022 -113.816 43.547 314.545 1.00143.61 C
ANISOU 1719 CD1 LEU A1022 17172 20193 17199 4572 -1192 -2646 C
ATOM 1720 CD2 LEU A1022 -115.518 45.313 315.024 1.00150.99 C
ANISOU 1720 CD2 LEU A1022 17840 21458 18073 5064 -1591 -3230 C
ATOM 1721 N PHE A1023 -110.143 44.317 318.023 1.00128.62 N
ANISOU 1721 N PHE A1023 15547 17801 15522 4092 -810 -1837 N
ATOM 1722 CA PHE A1023 -109.267 43.225 318.468 1.00126.05 C
ANISOU 1722 CA PHE A1023 15253 17418 15221 3817 -583 -1606 C
ATOM 1723 C PHE A1023 -109.766 42.477 319.685 1.00129.12 C
ANISOU 1723 C PHE A1023 15436 18022 15602 3573 -446 -1748 C
ATOM 1724 O PHE A1023 -109.545 41.270 319.779 1.00127.50 O
ANISOU 1724 O PHE A1023 15256 17823 15365 3357 -280 -1662 O
ATOM 1725 CB PHE A1023 -107.830 43.714 318.706 1.00126.19 C
ANISOU 1725 CB PHE A1023 15460 17203 15283 3799 -545 -1293 C
ATOM 1726 CG PHE A1023 -107.160 44.314 317.495 1.00127.50 C
ANISOU 1726 CG PHE A1023 15867 17147 15429 3958 -633 -1120 C
ATOM 1727 CD1 PHE A1023 -107.023 43.582 316.320 1.00130.41 C
ANISOU 1727 CD1 PHE A1023 16334 17450 15766 3967 -589 -1032 C
ATOM 1728 CD2 PHE A1023 -106.632 45.597 317.539 1.00129.69 C
ANISOU 1728 CD2 PHE A1023 16301 17274 15702 4072 -752 -1041 C
ATOM 1729 CE1 PHE A1023 -106.404 44.138 315.201 1.00131.43 C
ANISOU 1729 CE1 PHE A1023 16697 17379 15861 4088 -660 -880 C
ATOM 1730 CE2 PHE A1023 -106.009 46.151 316.421 1.00132.76 C
ANISOU 1730 CE2 PHE A1023 16949 17452 16040 4173 -822 -886 C
ATOM 1731 CZ PHE A1023 -105.899 45.420 315.259 1.00130.83 C
ANISOU 1731 CZ PHE A1023 16784 17159 15768 4178 -772 -809 C
ATOM 1732 N ASN A1024 -110.415 43.206 320.618 1.00126.63 N
ANISOU 1732 N ASN A1024 14949 17868 15297 3607 -518 -1966 N
ATOM 1733 CA ASN A1024 -110.974 42.743 321.896 1.00126.68 C
ANISOU 1733 CA ASN A1024 14750 18098 15283 3375 -403 -2142 C
ATOM 1734 C ASN A1024 -111.626 41.352 321.817 1.00128.80 C
ANISOU 1734 C ASN A1024 14930 18542 15467 3120 -252 -2268 C
ATOM 1735 O ASN A1024 -111.182 40.441 322.517 1.00127.80 O
ANISOU 1735 O ASN A1024 14872 18378 15310 2850 -78 -2145 O
ATOM 1736 CB ASN A1024 -111.952 43.784 322.497 1.00131.97 C
ANISOU 1736 CB ASN A1024 15208 18982 15951 3526 -547 -2461 C
ATOM 1737 CG ASN A1024 -111.877 45.196 321.924 1.00164.91 C
ANISOU 1737 CG ASN A1024 19497 23011 20149 3881 -781 -2455 C
ATOM 1738 OD1 ASN A1024 -112.107 45.437 320.726 1.00158.26 O
ANISOU 1738 OD1 ASN A1024 18754 22096 19281 4103 -918 -2476 O
ATOM 1739 ND2 ASN A1024 -111.630 46.173 322.791 1.00159.39 N
ANISOU 1739 ND2 ASN A1024 18811 22267 19482 3941 -839 -2447 N
ATOM 1740 N GLN A1025 -112.633 41.187 320.927 1.00124.48 N
ANISOU 1740 N GLN A1025 14265 18168 14862 3207 -329 -2505 N
ATOM 1741 CA GLN A1025 -113.391 39.948 320.715 1.00124.03 C
ANISOU 1741 CA GLN A1025 14124 18303 14699 2959 -202 -2665 C
ATOM 1742 C GLN A1025 -112.630 38.880 319.926 1.00123.41 C
ANISOU 1742 C GLN A1025 14304 17996 14592 2858 -92 -2387 C
ATOM 1743 O GLN A1025 -112.859 37.689 320.141 1.00122.96 O
ANISOU 1743 O GLN A1025 14280 18007 14432 2566 67 -2418 O
ATOM 1744 CB GLN A1025 -114.745 40.254 320.050 1.00127.75 C
ANISOU 1744 CB GLN A1025 14351 19072 15115 3108 -341 -3041 C
ATOM 1745 N ASP A1026 -111.736 39.299 319.015 1.00116.96 N
ANISOU 1745 N ASP A1026 13685 16911 13844 3089 -173 -2128 N
ATOM 1746 CA ASP A1026 -110.938 38.383 318.199 1.00114.98 C
ANISOU 1746 CA ASP A1026 13674 16446 13569 3041 -82 -1867 C
ATOM 1747 C ASP A1026 -109.779 37.734 318.964 1.00113.60 C
ANISOU 1747 C ASP A1026 13674 16093 13396 2871 73 -1592 C
ATOM 1748 O ASP A1026 -109.459 36.579 318.682 1.00112.37 O
ANISOU 1748 O ASP A1026 13681 15848 13165 2735 190 -1473 O
ATOM 1749 CB ASP A1026 -110.444 39.060 316.906 1.00117.03 C
ANISOU 1749 CB ASP A1026 14073 16514 13879 3333 -220 -1722 C
ATOM 1750 CG ASP A1026 -111.536 39.487 315.931 1.00131.93 C
ANISOU 1750 CG ASP A1026 15858 18536 15733 3521 -381 -1970 C
ATOM 1751 OD1 ASP A1026 -112.573 38.782 315.843 1.00133.51 O
ANISOU 1751 OD1 ASP A1026 15906 18968 15852 3387 -343 -2213 O
ATOM 1752 OD2 ASP A1026 -111.334 40.497 315.220 1.00140.04 O
ANISOU 1752 OD2 ASP A1026 16978 19435 16797 3791 -546 -1924 O
ATOM 1753 N VAL A1027 -109.151 38.468 319.921 1.00107.14 N
ANISOU 1753 N VAL A1027 12836 15222 12652 2892 62 -1499 N
ATOM 1754 CA VAL A1027 -108.042 37.972 320.762 1.00104.41 C
ANISOU 1754 CA VAL A1027 12632 14731 12308 2760 183 -1261 C
ATOM 1755 C VAL A1027 -108.515 36.759 321.580 1.00107.88 C
ANISOU 1755 C VAL A1027 13099 15264 12628 2451 332 -1359 C
ATOM 1756 O VAL A1027 -107.824 35.737 321.623 1.00106.26 O
ANISOU 1756 O VAL A1027 13108 14913 12353 2351 434 -1181 O
ATOM 1757 CB VAL A1027 -107.389 39.092 321.630 1.00106.43 C
ANISOU 1757 CB VAL A1027 12843 14938 12659 2840 127 -1173 C
ATOM 1758 CG1 VAL A1027 -106.453 38.524 322.695 1.00105.07 C
ANISOU 1758 CG1 VAL A1027 12773 14677 12473 2680 245 -994 C
ATOM 1759 CG2 VAL A1027 -106.636 40.087 320.758 1.00105.36 C
ANISOU 1759 CG2 VAL A1027 12789 14647 12597 3085 13 -1008 C
ATOM 1760 N ASP A1028 -109.727 36.854 322.154 1.00106.05 N
ANISOU 1760 N ASP A1028 12667 15281 12348 2302 338 -1661 N
ATOM 1761 CA ASP A1028 -110.336 35.777 322.939 1.00107.40 C
ANISOU 1761 CA ASP A1028 12868 15570 12370 1953 487 -1800 C
ATOM 1762 C ASP A1028 -110.717 34.598 322.050 1.00110.51 C
ANISOU 1762 C ASP A1028 13400 15955 12632 1828 557 -1827 C
ATOM 1763 O ASP A1028 -110.567 33.447 322.464 1.00110.36 O
ANISOU 1763 O ASP A1028 13602 15858 12471 1572 690 -1769 O
ATOM 1764 CB ASP A1028 -111.529 36.300 323.745 1.00111.40 C
ANISOU 1764 CB ASP A1028 13086 16388 12852 1821 479 -2143 C
ATOM 1765 CG ASP A1028 -111.132 37.324 324.795 1.00129.52 C
ANISOU 1765 CG ASP A1028 15290 18671 15252 1901 431 -2106 C
ATOM 1766 OD1 ASP A1028 -111.496 37.136 325.974 1.00133.93 O
ANISOU 1766 OD1 ASP A1028 15816 19328 15743 1648 530 -2205 O
ATOM 1767 OD2 ASP A1028 -110.437 38.310 324.441 1.00135.19 O
ANISOU 1767 OD2 ASP A1028 15998 19265 16102 2196 300 -1971 O
ATOM 1768 N ALA A1029 -111.142 34.891 320.808 1.00105.97 N
ANISOU 1768 N ALA A1029 12740 15431 12093 2019 458 -1899 N
ATOM 1769 CA ALA A1029 -111.484 33.886 319.809 1.00106.13 C
ANISOU 1769 CA ALA A1029 12888 15435 12001 1938 506 -1917 C
ATOM 1770 C ALA A1029 -110.216 33.142 319.369 1.00107.79 C
ANISOU 1770 C ALA A1029 13433 15325 12197 2002 560 -1573 C
ATOM 1771 O ALA A1029 -110.266 31.928 319.149 1.00108.01 O
ANISOU 1771 O ALA A1029 13680 15283 12076 1815 664 -1541 O
ATOM 1772 CB ALA A1029 -112.147 34.546 318.612 1.00107.38 C
ANISOU 1772 CB ALA A1029 12875 15709 12217 2178 359 -2063 C
ATOM 1773 N ALA A1030 -109.081 33.872 319.270 1.00101.63 N
ANISOU 1773 N ALA A1030 12695 14364 11554 2258 492 -1332 N
ATOM 1774 CA ALA A1030 -107.782 33.318 318.905 1.00100.19 C
ANISOU 1774 CA ALA A1030 12775 13925 11368 2359 532 -1026 C
ATOM 1775 C ALA A1030 -107.243 32.400 320.017 1.00105.39 C
ANISOU 1775 C ALA A1030 13640 14484 11921 2162 648 -925 C
ATOM 1776 O ALA A1030 -106.651 31.370 319.699 1.00105.76 O
ANISOU 1776 O ALA A1030 13955 14365 11865 2152 708 -776 O
ATOM 1777 CB ALA A1030 -106.798 34.435 318.609 1.00 99.51 C
ANISOU 1777 CB ALA A1030 12638 13735 11436 2634 437 -845 C
ATOM 1778 N VAL A1031 -107.475 32.750 321.309 1.00101.97 N
ANISOU 1778 N VAL A1031 13104 14145 11494 2015 670 -1017 N
ATOM 1779 CA VAL A1031 -107.058 31.924 322.449 1.00101.97 C
ANISOU 1779 CA VAL A1031 13320 14049 11374 1814 766 -945 C
ATOM 1780 C VAL A1031 -107.889 30.628 322.474 1.00110.05 C
ANISOU 1780 C VAL A1031 14547 15094 12174 1501 876 -1082 C
ATOM 1781 O VAL A1031 -107.308 29.549 322.574 1.00110.53 O
ANISOU 1781 O VAL A1031 14950 14957 12089 1435 935 -940 O
ATOM 1782 CB VAL A1031 -107.049 32.674 323.817 1.00104.52 C
ANISOU 1782 CB VAL A1031 13494 14458 11762 1736 760 -1000 C
ATOM 1783 CG1 VAL A1031 -106.638 31.746 324.962 1.00104.46 C
ANISOU 1783 CG1 VAL A1031 13755 14330 11604 1523 851 -929 C
ATOM 1784 CG2 VAL A1031 -106.130 33.891 323.778 1.00102.55 C
ANISOU 1784 CG2 VAL A1031 13103 14159 11704 2020 658 -843 C
ATOM 1785 N ARG A1032 -109.232 30.733 322.323 1.00109.40 N
ANISOU 1785 N ARG A1032 14265 15257 12046 1317 895 -1369 N
ATOM 1786 CA ARG A1032 -110.156 29.584 322.284 1.00111.47 C
ANISOU 1786 CA ARG A1032 14684 15592 12076 966 1008 -1543 C
ATOM 1787 C ARG A1032 -109.813 28.592 321.155 1.00116.01 C
ANISOU 1787 C ARG A1032 15552 15977 12551 1026 1024 -1402 C
ATOM 1788 O ARG A1032 -109.937 27.384 321.349 1.00117.19 O
ANISOU 1788 O ARG A1032 16034 16023 12471 763 1124 -1404 O
ATOM 1789 CB ARG A1032 -111.627 30.041 322.168 1.00112.95 C
ANISOU 1789 CB ARG A1032 14520 16142 12253 808 1005 -1903 C
ATOM 1790 CG ARG A1032 -112.211 30.604 323.467 1.00123.65 C
ANISOU 1790 CG ARG A1032 15653 17721 13609 612 1041 -2113 C
ATOM 1791 CD ARG A1032 -113.719 30.834 323.402 1.00133.25 C
ANISOU 1791 CD ARG A1032 16530 19339 14759 416 1058 -2516 C
ATOM 1792 NE ARG A1032 -114.085 32.066 322.694 1.00141.00 N
ANISOU 1792 NE ARG A1032 17145 20494 15934 768 893 -2634 N
ATOM 1793 CZ ARG A1032 -114.561 32.113 321.451 1.00156.92 C
ANISOU 1793 CZ ARG A1032 19060 22595 17966 919 814 -2723 C
ATOM 1794 NH1 ARG A1032 -114.745 30.994 320.758 1.00145.91 N
ANISOU 1794 NH1 ARG A1032 17879 21145 16416 737 895 -2706 N
ATOM 1795 NH2 ARG A1032 -114.864 33.279 320.894 1.00140.66 N
ANISOU 1795 NH2 ARG A1032 16715 20665 16063 1257 644 -2831 N
ATOM 1796 N GLY A1033 -109.368 29.115 320.012 1.00111.22 N
ANISOU 1796 N GLY A1033 14850 15313 12097 1361 926 -1282 N
ATOM 1797 CA GLY A1033 -109.001 28.320 318.847 1.00110.86 C
ANISOU 1797 CA GLY A1033 15044 15096 11982 1466 930 -1146 C
ATOM 1798 C GLY A1033 -107.697 27.558 318.989 1.00114.41 C
ANISOU 1798 C GLY A1033 15858 15247 12364 1582 955 -865 C
ATOM 1799 O GLY A1033 -107.590 26.424 318.509 1.00115.07 O
ANISOU 1799 O GLY A1033 16269 15179 12275 1516 1006 -803 O
ATOM 1800 N ILE A1034 -106.685 28.187 319.626 1.00109.18 N
ANISOU 1800 N ILE A1034 15143 14510 11829 1773 910 -704 N
ATOM 1801 CA ILE A1034 -105.367 27.588 319.858 1.00108.24 C
ANISOU 1801 CA ILE A1034 15315 14155 11658 1933 911 -459 C
ATOM 1802 C ILE A1034 -105.495 26.402 320.831 1.00115.18 C
ANISOU 1802 C ILE A1034 16568 14907 12287 1663 991 -480 C
ATOM 1803 O ILE A1034 -104.921 25.339 320.582 1.00115.66 O
ANISOU 1803 O ILE A1034 17006 14755 12184 1719 1005 -354 O
ATOM 1804 CB ILE A1034 -104.329 28.659 320.310 1.00109.21 C
ANISOU 1804 CB ILE A1034 15234 14283 11976 2179 840 -318 C
ATOM 1805 CG1 ILE A1034 -103.915 29.554 319.127 1.00107.87 C
ANISOU 1805 CG1 ILE A1034 14851 14151 11985 2458 767 -241 C
ATOM 1806 CG2 ILE A1034 -103.098 28.019 320.935 1.00109.92 C
ANISOU 1806 CG2 ILE A1034 15591 14191 11984 2295 840 -127 C
ATOM 1807 CD1 ILE A1034 -103.233 30.858 319.519 1.00110.48 C
ANISOU 1807 CD1 ILE A1034 14930 14544 12504 2620 699 -168 C
ATOM 1808 N LEU A1035 -106.302 26.572 321.896 1.00113.21 N
ANISOU 1808 N LEU A1035 16238 14788 11987 1363 1041 -653 N
ATOM 1809 CA LEU A1035 -106.546 25.544 322.912 1.00115.07 C
ANISOU 1809 CA LEU A1035 16843 14914 11963 1042 1124 -700 C
ATOM 1810 C LEU A1035 -107.455 24.384 322.422 1.00123.68 C
ANISOU 1810 C LEU A1035 18224 15975 12793 731 1215 -829 C
ATOM 1811 O LEU A1035 -107.600 23.388 323.133 1.00125.80 O
ANISOU 1811 O LEU A1035 18900 16104 12796 448 1286 -852 O
ATOM 1812 CB LEU A1035 -107.073 26.173 324.213 1.00114.92 C
ANISOU 1812 CB LEU A1035 16630 15061 11974 808 1158 -850 C
ATOM 1813 CG LEU A1035 -106.124 27.168 324.903 1.00117.30 C
ANISOU 1813 CG LEU A1035 16732 15354 12482 1061 1078 -714 C
ATOM 1814 CD1 LEU A1035 -106.855 27.989 325.933 1.00117.73 C
ANISOU 1814 CD1 LEU A1035 16490 15632 12609 858 1103 -904 C
ATOM 1815 CD2 LEU A1035 -104.920 26.473 325.522 1.00118.43 C
ANISOU 1815 CD2 LEU A1035 17255 15232 12510 1173 1052 -504 C
ATOM 1816 N ARG A1036 -108.031 24.506 321.206 1.00121.19 N
ANISOU 1816 N ARG A1036 17732 15778 12537 779 1207 -909 N
ATOM 1817 CA ARG A1036 -108.847 23.484 320.535 1.00123.18 C
ANISOU 1817 CA ARG A1036 18219 16021 12562 518 1282 -1025 C
ATOM 1818 C ARG A1036 -107.961 22.749 319.513 1.00127.02 C
ANISOU 1818 C ARG A1036 19027 16237 12996 796 1240 -802 C
ATOM 1819 O ARG A1036 -108.284 21.627 319.110 1.00128.85 O
ANISOU 1819 O ARG A1036 19637 16340 12982 607 1298 -822 O
ATOM 1820 CB ARG A1036 -110.027 24.128 319.783 1.00124.61 C
ANISOU 1820 CB ARG A1036 17974 16526 12848 433 1281 -1268 C
ATOM 1821 CG ARG A1036 -111.271 24.400 320.614 1.00137.76 C
ANISOU 1821 CG ARG A1036 19403 18501 14438 36 1359 -1580 C
ATOM 1822 CD ARG A1036 -112.435 24.764 319.705 1.00151.58 C
ANISOU 1822 CD ARG A1036 20802 20563 16227 -33 1348 -1838 C
ATOM 1823 NE ARG A1036 -113.336 25.751 320.308 1.00163.80 N
ANISOU 1823 NE ARG A1036 21882 22480 17875 -138 1339 -2119 N
ATOM 1824 CZ ARG A1036 -113.400 27.033 319.956 1.00177.09 C
ANISOU 1824 CZ ARG A1036 23138 24328 19819 189 1211 -2169 C
ATOM 1825 NH1 ARG A1036 -112.618 27.506 318.991 1.00160.30 N
ANISOU 1825 NH1 ARG A1036 20995 22032 17878 608 1093 -1953 N
ATOM 1826 NH2 ARG A1036 -114.251 27.851 320.560 1.00166.02 N
ANISOU 1826 NH2 ARG A1036 21345 23260 18475 96 1199 -2447 N
ATOM 1827 N ASN A1037 -106.869 23.414 319.071 1.00120.76 N
ANISOU 1827 N ASN A1037 18077 15377 12428 1233 1143 -604 N
ATOM 1828 CA ASN A1037 -105.890 22.928 318.098 1.00119.45 C
ANISOU 1828 CA ASN A1037 18129 15002 12253 1557 1097 -397 C
ATOM 1829 C ASN A1037 -104.838 22.054 318.795 1.00124.17 C
ANISOU 1829 C ASN A1037 19170 15328 12680 1661 1082 -228 C
ATOM 1830 O ASN A1037 -104.171 22.514 319.723 1.00123.72 O
ANISOU 1830 O ASN A1037 19040 15266 12703 1764 1044 -159 O
ATOM 1831 CB ASN A1037 -105.226 24.120 317.409 1.00115.58 C
ANISOU 1831 CB ASN A1037 17250 14605 12059 1930 1011 -295 C
ATOM 1832 CG ASN A1037 -104.456 23.780 316.164 1.00133.10 C
ANISOU 1832 CG ASN A1037 19595 16691 14287 2225 978 -139 C
ATOM 1833 OD1 ASN A1037 -103.464 23.041 316.193 1.00128.23 O
ANISOU 1833 OD1 ASN A1037 19284 15876 13562 2408 966 18 O
ATOM 1834 ND2 ASN A1037 -104.865 24.362 315.047 1.00122.73 N
ANISOU 1834 ND2 ASN A1037 18040 15490 13100 2303 954 -188 N
ATOM 1835 N ALA A1038 -104.697 20.797 318.342 1.00121.48 N
ANISOU 1835 N ALA A1038 19306 14760 12090 1647 1101 -169 N
ATOM 1836 CA ALA A1038 -103.753 19.821 318.901 1.00121.94 C
ANISOU 1836 CA ALA A1038 19868 14531 11933 1778 1063 -27 C
ATOM 1837 C ALA A1038 -102.287 20.150 318.594 1.00122.93 C
ANISOU 1837 C ALA A1038 19896 14601 12211 2285 962 168 C
ATOM 1838 O ALA A1038 -101.416 19.854 319.411 1.00123.14 O
ANISOU 1838 O ALA A1038 20139 14494 12153 2441 903 259 O
ATOM 1839 CB ALA A1038 -104.094 18.425 318.402 1.00124.76 C
ANISOU 1839 CB ALA A1038 20781 14658 11965 1627 1102 -36 C
ATOM 1840 N LYS A1039 -102.020 20.748 317.418 1.00116.69 N
ANISOU 1840 N LYS A1039 18787 13924 11624 2530 942 217 N
ATOM 1841 CA LYS A1039 -100.677 21.120 316.967 1.00115.02 C
ANISOU 1841 CA LYS A1039 18431 13717 11553 2972 868 374 C
ATOM 1842 C LYS A1039 -100.120 22.377 317.663 1.00116.77 C
ANISOU 1842 C LYS A1039 18226 14121 12020 3080 830 403 C
ATOM 1843 O LYS A1039 -98.897 22.538 317.734 1.00116.88 O
ANISOU 1843 O LYS A1039 18184 14136 12089 3396 770 519 O
ATOM 1844 CB LYS A1039 -100.664 21.331 315.440 1.00116.45 C
ANISOU 1844 CB LYS A1039 18452 13955 11839 3138 876 404 C
ATOM 1845 CG LYS A1039 -100.841 20.054 314.630 1.00131.34 C
ANISOU 1845 CG LYS A1039 20784 15637 13484 3152 895 423 C
ATOM 1846 CD LYS A1039 -100.737 20.299 313.134 1.00137.62 C
ANISOU 1846 CD LYS A1039 21406 16494 14391 3310 904 452 C
ATOM 1847 CE LYS A1039 -100.778 18.997 312.370 1.00151.64 C
ANISOU 1847 CE LYS A1039 23642 18057 15919 3340 919 477 C
ATOM 1848 NZ LYS A1039 -100.869 19.212 310.902 1.00161.21 N
ANISOU 1848 NZ LYS A1039 24697 19328 17229 3444 936 490 N
ATOM 1849 N LEU A1040 -101.007 23.271 318.156 1.00110.31 N
ANISOU 1849 N LEU A1040 17102 13472 11339 2823 862 285 N
ATOM 1850 CA LEU A1040 -100.603 24.550 318.742 1.00107.33 C
ANISOU 1850 CA LEU A1040 16325 13264 11193 2900 826 302 C
ATOM 1851 C LEU A1040 -100.724 24.666 320.259 1.00109.39 C
ANISOU 1851 C LEU A1040 16624 13528 11413 2717 827 256 C
ATOM 1852 O LEU A1040 -100.005 25.476 320.849 1.00107.25 O
ANISOU 1852 O LEU A1040 16128 13339 11285 2851 782 316 O
ATOM 1853 CB LEU A1040 -101.376 25.694 318.070 1.00105.77 C
ANISOU 1853 CB LEU A1040 15720 13264 11205 2829 833 207 C
ATOM 1854 CG LEU A1040 -101.123 25.897 316.572 1.00108.85 C
ANISOU 1854 CG LEU A1040 16011 13669 11678 3038 818 267 C
ATOM 1855 CD1 LEU A1040 -102.227 26.694 315.950 1.00108.39 C
ANISOU 1855 CD1 LEU A1040 15693 13755 11736 2908 817 129 C
ATOM 1856 CD2 LEU A1040 -99.805 26.589 316.318 1.00109.09 C
ANISOU 1856 CD2 LEU A1040 15854 13746 11849 3338 773 411 C
ATOM 1857 N LYS A1041 -101.618 23.875 320.885 1.00107.01 N
ANISOU 1857 N LYS A1041 16613 13142 10905 2393 883 145 N
ATOM 1858 CA LYS A1041 -101.861 23.886 322.330 1.00107.37 C
ANISOU 1858 CA LYS A1041 16742 13179 10874 2162 899 82 C
ATOM 1859 C LYS A1041 -100.621 23.565 323.192 1.00112.09 C
ANISOU 1859 C LYS A1041 17561 13628 11399 2384 823 224 C
ATOM 1860 O LYS A1041 -100.420 24.302 324.162 1.00111.67 O
ANISOU 1860 O LYS A1041 17312 13665 11454 2354 802 219 O
ATOM 1861 CB LYS A1041 -103.037 22.970 322.716 1.00111.71 C
ANISOU 1861 CB LYS A1041 17617 13661 11165 1734 989 -72 C
ATOM 1862 CG LYS A1041 -103.556 23.187 324.140 1.00121.51 C
ANISOU 1862 CG LYS A1041 18848 14965 12354 1415 1033 -189 C
ATOM 1863 CD LYS A1041 -104.236 21.948 324.686 1.00129.59 C
ANISOU 1863 CD LYS A1041 20382 15828 13027 1024 1112 -285 C
ATOM 1864 CE LYS A1041 -104.584 22.106 326.142 1.00138.00 C
ANISOU 1864 CE LYS A1041 21495 16923 14014 731 1152 -377 C
ATOM 1865 NZ LYS A1041 -104.858 20.793 326.776 1.00149.92 N
ANISOU 1865 NZ LYS A1041 23635 18193 15134 399 1208 -416 N
ATOM 1866 N PRO A1042 -99.803 22.497 322.929 1.00109.33 N
ANISOU 1866 N PRO A1042 17620 13062 10859 2615 769 335 N
ATOM 1867 CA PRO A1042 -98.653 22.222 323.820 1.00109.56 C
ANISOU 1867 CA PRO A1042 17845 12975 10806 2852 673 439 C
ATOM 1868 C PRO A1042 -97.616 23.347 323.872 1.00111.65 C
ANISOU 1868 C PRO A1042 17656 13433 11332 3150 610 523 C
ATOM 1869 O PRO A1042 -97.110 23.662 324.960 1.00111.70 O
ANISOU 1869 O PRO A1042 17631 13455 11355 3183 559 547 O
ATOM 1870 CB PRO A1042 -98.075 20.914 323.269 1.00112.81 C
ANISOU 1870 CB PRO A1042 18749 13146 10966 3085 618 513 C
ATOM 1871 CG PRO A1042 -99.172 20.316 322.448 1.00117.57 C
ANISOU 1871 CG PRO A1042 19537 13683 11451 2822 709 433 C
ATOM 1872 CD PRO A1042 -99.879 21.482 321.856 1.00111.37 C
ANISOU 1872 CD PRO A1042 18197 13169 10950 2689 780 360 C
ATOM 1873 N VAL A1043 -97.343 23.978 322.705 1.00105.70 N
ANISOU 1873 N VAL A1043 16563 12829 10770 3332 620 560 N
ATOM 1874 CA VAL A1043 -96.418 25.106 322.534 1.00103.70 C
ANISOU 1874 CA VAL A1043 15873 12777 10750 3566 581 629 C
ATOM 1875 C VAL A1043 -96.946 26.296 323.345 1.00104.83 C
ANISOU 1875 C VAL A1043 15683 13072 11076 3340 605 568 C
ATOM 1876 O VAL A1043 -96.264 26.765 324.256 1.00104.57 O
ANISOU 1876 O VAL A1043 15533 13100 11099 3413 556 608 O
ATOM 1877 CB VAL A1043 -96.262 25.492 321.040 1.00107.03 C
ANISOU 1877 CB VAL A1043 16071 13299 11295 3724 606 662 C
ATOM 1878 CG1 VAL A1043 -95.139 26.510 320.850 1.00105.51 C
ANISOU 1878 CG1 VAL A1043 15495 13305 11289 3947 573 733 C
ATOM 1879 CG2 VAL A1043 -96.046 24.256 320.166 1.00108.73 C
ANISOU 1879 CG2 VAL A1043 16642 13354 11316 3903 596 698 C
ATOM 1880 N TYR A1044 -98.175 26.755 323.017 1.00 98.91 N
ANISOU 1880 N TYR A1044 14788 12389 10403 3079 671 457 N
ATOM 1881 CA TYR A1044 -98.876 27.863 323.657 1.00 96.88 C
ANISOU 1881 CA TYR A1044 14225 12282 10304 2870 691 364 C
ATOM 1882 C TYR A1044 -98.926 27.748 325.194 1.00100.69 C
ANISOU 1882 C TYR A1044 14829 12722 10707 2704 685 333 C
ATOM 1883 O TYR A1044 -98.701 28.748 325.876 1.00 99.49 O
ANISOU 1883 O TYR A1044 14415 12687 10701 2697 661 335 O
ATOM 1884 CB TYR A1044 -100.289 27.985 323.084 1.00 97.65 C
ANISOU 1884 CB TYR A1044 14239 12445 10418 2630 751 211 C
ATOM 1885 CG TYR A1044 -101.017 29.228 323.545 1.00 98.66 C
ANISOU 1885 CG TYR A1044 14019 12754 10713 2478 754 91 C
ATOM 1886 CD1 TYR A1044 -100.861 30.438 322.876 1.00 99.36 C
ANISOU 1886 CD1 TYR A1044 13775 12968 11008 2626 709 110 C
ATOM 1887 CD2 TYR A1044 -101.880 29.192 324.641 1.00 99.58 C
ANISOU 1887 CD2 TYR A1044 14164 12912 10761 2183 797 -53 C
ATOM 1888 CE1 TYR A1044 -101.504 31.592 323.314 1.00 99.01 C
ANISOU 1888 CE1 TYR A1044 13452 13071 11098 2524 690 -6 C
ATOM 1889 CE2 TYR A1044 -102.546 30.336 325.074 1.00 99.56 C
ANISOU 1889 CE2 TYR A1044 13837 13089 10904 2073 791 -181 C
ATOM 1890 CZ TYR A1044 -102.360 31.534 324.402 1.00105.24 C
ANISOU 1890 CZ TYR A1044 14244 13915 11827 2263 729 -157 C
ATOM 1891 OH TYR A1044 -103.001 32.672 324.822 1.00105.10 O
ANISOU 1891 OH TYR A1044 13944 14054 11934 2191 703 -288 O
ATOM 1892 N ASP A1045 -99.225 26.544 325.728 1.00 98.27 N
ANISOU 1892 N ASP A1045 14948 12237 10153 2556 707 303 N
ATOM 1893 CA ASP A1045 -99.282 26.291 327.174 1.00 98.94 C
ANISOU 1893 CA ASP A1045 15233 12244 10116 2379 702 273 C
ATOM 1894 C ASP A1045 -97.920 26.480 327.828 1.00101.60 C
ANISOU 1894 C ASP A1045 15563 12557 10483 2662 602 406 C
ATOM 1895 O ASP A1045 -97.852 26.977 328.952 1.00100.89 O
ANISOU 1895 O ASP A1045 15393 12508 10433 2563 587 391 O
ATOM 1896 CB ASP A1045 -99.794 24.868 327.469 1.00103.12 C
ANISOU 1896 CB ASP A1045 16306 12548 10326 2167 739 224 C
ATOM 1897 CG ASP A1045 -101.303 24.695 327.472 1.00116.36 C
ANISOU 1897 CG ASP A1045 18009 14285 11919 1737 857 38 C
ATOM 1898 OD1 ASP A1045 -102.020 25.676 327.812 1.00116.61 O
ANISOU 1898 OD1 ASP A1045 17667 14529 12112 1554 902 -84 O
ATOM 1899 OD2 ASP A1045 -101.768 23.562 327.202 1.00123.21 O
ANISOU 1899 OD2 ASP A1045 19287 14993 12536 1572 902 -2 O
ATOM 1900 N SER A1046 -96.836 26.084 327.116 1.00 97.39 N
ANISOU 1900 N SER A1046 15096 11981 9927 3016 534 522 N
ATOM 1901 CA SER A1046 -95.449 26.164 327.582 1.00 96.69 C
ANISOU 1901 CA SER A1046 14980 11913 9846 3330 429 627 C
ATOM 1902 C SER A1046 -94.881 27.598 327.632 1.00100.50 C
ANISOU 1902 C SER A1046 14951 12640 10593 3416 416 661 C
ATOM 1903 O SER A1046 -93.849 27.827 328.272 1.00101.29 O
ANISOU 1903 O SER A1046 14977 12800 10708 3594 339 719 O
ATOM 1904 CB SER A1046 -94.554 25.269 326.724 1.00 97.97 C
ANISOU 1904 CB SER A1046 15353 11991 9880 3681 366 701 C
ATOM 1905 OG SER A1046 -93.834 25.990 325.738 1.00 97.61 O
ANISOU 1905 OG SER A1046 14931 12140 10017 3901 370 749 O
ATOM 1906 N LEU A1047 -95.532 28.546 326.942 1.00 95.14 N
ANISOU 1906 N LEU A1047 13947 12099 10103 3295 482 619 N
ATOM 1907 CA LEU A1047 -95.029 29.907 326.810 1.00 93.43 C
ANISOU 1907 CA LEU A1047 13306 12085 10109 3362 471 654 C
ATOM 1908 C LEU A1047 -95.470 30.879 327.874 1.00 98.90 C
ANISOU 1908 C LEU A1047 13816 12852 10909 3150 477 601 C
ATOM 1909 O LEU A1047 -96.588 30.797 328.381 1.00100.27 O
ANISOU 1909 O LEU A1047 14075 12977 11047 2891 523 496 O
ATOM 1910 CB LEU A1047 -95.382 30.473 325.422 1.00 91.96 C
ANISOU 1910 CB LEU A1047 12908 11985 10049 3383 514 643 C
ATOM 1911 CG LEU A1047 -94.792 29.743 324.211 1.00 95.96 C
ANISOU 1911 CG LEU A1047 13518 12459 10484 3619 512 705 C
ATOM 1912 CD1 LEU A1047 -95.549 30.090 322.948 1.00 94.67 C
ANISOU 1912 CD1 LEU A1047 13252 12319 10401 3556 563 665 C
ATOM 1913 CD2 LEU A1047 -93.316 30.028 324.056 1.00 97.66 C
ANISOU 1913 CD2 LEU A1047 13561 12809 10735 3886 466 795 C
ATOM 1914 N ASP A1048 -94.590 31.853 328.166 1.00 94.30 N
ANISOU 1914 N ASP A1048 12965 12410 10454 3250 436 662 N
ATOM 1915 CA ASP A1048 -94.846 32.968 329.070 1.00 92.18 C
ANISOU 1915 CA ASP A1048 12489 12228 10308 3085 434 626 C
ATOM 1916 C ASP A1048 -95.766 33.948 328.325 1.00 95.56 C
ANISOU 1916 C ASP A1048 12696 12732 10882 2968 473 553 C
ATOM 1917 O ASP A1048 -95.883 33.867 327.099 1.00 95.26 O
ANISOU 1917 O ASP A1048 12631 12700 10864 3052 491 560 O
ATOM 1918 CB ASP A1048 -93.530 33.646 329.479 1.00 93.34 C
ANISOU 1918 CB ASP A1048 12444 12503 10519 3235 376 718 C
ATOM 1919 CG ASP A1048 -92.731 34.215 328.325 1.00101.38 C
ANISOU 1919 CG ASP A1048 13245 13657 11617 3403 377 782 C
ATOM 1920 OD1 ASP A1048 -91.998 33.440 327.674 1.00101.80 O
ANISOU 1920 OD1 ASP A1048 13382 13716 11582 3615 363 827 O
ATOM 1921 OD2 ASP A1048 -92.828 35.438 328.083 1.00107.74 O
ANISOU 1921 OD2 ASP A1048 13819 14561 12556 3319 390 779 O
ATOM 1922 N ALA A1049 -96.410 34.862 329.063 1.00 91.82 N
ANISOU 1922 N ALA A1049 12080 12312 10496 2793 475 475 N
ATOM 1923 CA ALA A1049 -97.368 35.832 328.542 1.00 90.27 C
ANISOU 1923 CA ALA A1049 11696 12186 10417 2703 484 374 C
ATOM 1924 C ALA A1049 -96.863 36.679 327.377 1.00 93.19 C
ANISOU 1924 C ALA A1049 11903 12617 10888 2852 456 441 C
ATOM 1925 O ALA A1049 -97.640 36.939 326.452 1.00 93.61 O
ANISOU 1925 O ALA A1049 11915 12674 10977 2849 458 369 O
ATOM 1926 CB ALA A1049 -97.866 36.722 329.663 1.00 90.52 C
ANISOU 1926 CB ALA A1049 11606 12275 10514 2545 471 290 C
ATOM 1927 N VAL A1050 -95.581 37.109 327.413 1.00 87.98 N
ANISOU 1927 N VAL A1050 11158 12013 10256 2967 430 567 N
ATOM 1928 CA VAL A1050 -95.006 37.945 326.350 1.00 87.24 C
ANISOU 1928 CA VAL A1050 10935 11986 10228 3061 417 631 C
ATOM 1929 C VAL A1050 -94.921 37.162 325.030 1.00 93.03 C
ANISOU 1929 C VAL A1050 11757 12683 10907 3187 447 659 C
ATOM 1930 O VAL A1050 -95.393 37.664 324.000 1.00 92.94 O
ANISOU 1930 O VAL A1050 11712 12662 10939 3195 444 631 O
ATOM 1931 CB VAL A1050 -93.664 38.619 326.743 1.00 90.69 C
ANISOU 1931 CB VAL A1050 11244 12532 10683 3102 398 734 C
ATOM 1932 CG1 VAL A1050 -93.155 39.522 325.626 1.00 90.42 C
ANISOU 1932 CG1 VAL A1050 11107 12564 10685 3134 401 784 C
ATOM 1933 CG2 VAL A1050 -93.800 39.417 328.036 1.00 89.91 C
ANISOU 1933 CG2 VAL A1050 11074 12454 10632 2969 367 707 C
ATOM 1934 N ARG A1051 -94.370 35.916 325.083 1.00 89.31 N
ANISOU 1934 N ARG A1051 11428 12177 10329 3296 465 705 N
ATOM 1935 CA ARG A1051 -94.224 35.008 323.941 1.00 88.88 C
ANISOU 1935 CA ARG A1051 11492 12079 10200 3433 492 733 C
ATOM 1936 C ARG A1051 -95.553 34.487 323.415 1.00 94.12 C
ANISOU 1936 C ARG A1051 12288 12635 10837 3344 517 638 C
ATOM 1937 O ARG A1051 -95.662 34.213 322.218 1.00 94.55 O
ANISOU 1937 O ARG A1051 12384 12664 10875 3423 536 648 O
ATOM 1938 CB ARG A1051 -93.273 33.864 324.270 1.00 88.65 C
ANISOU 1938 CB ARG A1051 11605 12035 10043 3600 481 792 C
ATOM 1939 CG ARG A1051 -91.846 34.351 324.368 1.00 93.41 C
ANISOU 1939 CG ARG A1051 12025 12806 10660 3734 460 867 C
ATOM 1940 CD ARG A1051 -90.911 33.224 324.638 1.00 95.04 C
ANISOU 1940 CD ARG A1051 12361 13021 10729 3956 425 898 C
ATOM 1941 NE ARG A1051 -89.526 33.673 324.559 1.00103.08 N
ANISOU 1941 NE ARG A1051 13154 14261 11750 4096 409 937 N
ATOM 1942 CZ ARG A1051 -88.766 33.976 325.605 1.00113.59 C
ANISOU 1942 CZ ARG A1051 14374 15707 13077 4113 360 946 C
ATOM 1943 NH1 ARG A1051 -89.250 33.883 326.836 1.00 97.21 N
ANISOU 1943 NH1 ARG A1051 12415 13520 10999 4004 321 930 N
ATOM 1944 NH2 ARG A1051 -87.518 34.383 325.427 1.00100.45 N
ANISOU 1944 NH2 ARG A1051 12476 14287 11403 4223 355 959 N
ATOM 1945 N ARG A1052 -96.577 34.390 324.289 1.00 90.73 N
ANISOU 1945 N ARG A1052 11912 12164 10397 3164 521 533 N
ATOM 1946 CA ARG A1052 -97.928 33.986 323.898 1.00 90.52 C
ANISOU 1946 CA ARG A1052 11967 12089 10336 3034 550 404 C
ATOM 1947 C ARG A1052 -98.528 35.030 322.972 1.00 93.99 C
ANISOU 1947 C ARG A1052 12230 12591 10890 3042 522 342 C
ATOM 1948 O ARG A1052 -99.221 34.659 322.022 1.00 94.84 O
ANISOU 1948 O ARG A1052 12391 12675 10970 3040 535 278 O
ATOM 1949 CB ARG A1052 -98.819 33.803 325.122 1.00 91.22 C
ANISOU 1949 CB ARG A1052 12107 12172 10379 2812 569 282 C
ATOM 1950 CG ARG A1052 -98.629 32.450 325.771 1.00 99.81 C
ANISOU 1950 CG ARG A1052 13494 13141 11290 2764 600 307 C
ATOM 1951 CD ARG A1052 -99.389 32.349 327.067 1.00 99.45 C
ANISOU 1951 CD ARG A1052 13509 13093 11183 2508 629 188 C
ATOM 1952 NE ARG A1052 -99.333 30.982 327.572 1.00104.38 N
ANISOU 1952 NE ARG A1052 14497 13565 11596 2434 656 204 N
ATOM 1953 CZ ARG A1052 -99.990 30.545 328.637 1.00116.17 C
ANISOU 1953 CZ ARG A1052 16155 15018 12968 2177 698 106 C
ATOM 1954 NH1 ARG A1052 -100.776 31.365 329.323 1.00103.10 N
ANISOU 1954 NH1 ARG A1052 14287 13492 11394 1976 724 -30 N
ATOM 1955 NH2 ARG A1052 -99.873 29.282 329.021 1.00103.31 N
ANISOU 1955 NH2 ARG A1052 14926 13213 11115 2116 711 132 N
ATOM 1956 N ALA A1053 -98.233 36.334 323.229 1.00 88.59 N
ANISOU 1956 N ALA A1053 11366 11977 10318 3055 476 362 N
ATOM 1957 CA ALA A1053 -98.691 37.453 322.398 1.00 87.48 C
ANISOU 1957 CA ALA A1053 11111 11865 10263 3088 423 311 C
ATOM 1958 C ALA A1053 -98.038 37.424 321.014 1.00 90.42 C
ANISOU 1958 C ALA A1053 11523 12207 10624 3229 428 412 C
ATOM 1959 O ALA A1053 -98.704 37.736 320.029 1.00 89.31 O
ANISOU 1959 O ALA A1053 11390 12045 10499 3261 395 350 O
ATOM 1960 CB ALA A1053 -98.420 38.775 323.088 1.00 87.74 C
ANISOU 1960 CB ALA A1053 11011 11946 10379 3058 370 320 C
ATOM 1961 N ALA A1054 -96.753 37.003 320.937 1.00 87.63 N
ANISOU 1961 N ALA A1054 11198 11868 10231 3318 466 552 N
ATOM 1962 CA ALA A1054 -96.011 36.847 319.678 1.00 87.33 C
ANISOU 1962 CA ALA A1054 11191 11830 10162 3444 490 642 C
ATOM 1963 C ALA A1054 -96.649 35.728 318.840 1.00 90.82 C
ANISOU 1963 C ALA A1054 11783 12191 10534 3490 519 604 C
ATOM 1964 O ALA A1054 -96.838 35.921 317.639 1.00 90.19 O
ANISOU 1964 O ALA A1054 11727 12084 10456 3543 515 606 O
ATOM 1965 CB ALA A1054 -94.545 36.543 319.952 1.00 88.32 C
ANISOU 1965 CB ALA A1054 11279 12037 10242 3536 524 757 C
ATOM 1966 N LEU A1055 -97.049 34.599 319.485 1.00 87.27 N
ANISOU 1966 N LEU A1055 11461 11689 10007 3447 545 562 N
ATOM 1967 CA LEU A1055 -97.722 33.489 318.807 1.00 87.25 C
ANISOU 1967 CA LEU A1055 11638 11602 9912 3448 577 516 C
ATOM 1968 C LEU A1055 -99.116 33.893 318.301 1.00 92.22 C
ANISOU 1968 C LEU A1055 12222 12235 10581 3343 551 373 C
ATOM 1969 O LEU A1055 -99.454 33.552 317.165 1.00 92.01 O
ANISOU 1969 O LEU A1055 12268 12169 10524 3393 557 359 O
ATOM 1970 CB LEU A1055 -97.789 32.228 319.684 1.00 87.67 C
ANISOU 1970 CB LEU A1055 11895 11580 9836 3394 608 505 C
ATOM 1971 CG LEU A1055 -98.241 30.921 318.994 1.00 92.57 C
ANISOU 1971 CG LEU A1055 12770 12087 10314 3397 646 483 C
ATOM 1972 CD1 LEU A1055 -97.304 30.525 317.849 1.00 93.35 C
ANISOU 1972 CD1 LEU A1055 12934 12159 10374 3624 656 595 C
ATOM 1973 CD2 LEU A1055 -98.324 29.792 319.974 1.00 93.83 C
ANISOU 1973 CD2 LEU A1055 13187 12146 10317 3306 667 463 C
ATOM 1974 N ILE A1056 -99.901 34.648 319.118 1.00 89.05 N
ANISOU 1974 N ILE A1056 11693 11898 10245 3216 515 254 N
ATOM 1975 CA ILE A1056 -101.234 35.138 318.735 1.00 88.98 C
ANISOU 1975 CA ILE A1056 11598 11940 10269 3148 469 79 C
ATOM 1976 C ILE A1056 -101.122 36.171 317.618 1.00 92.63 C
ANISOU 1976 C ILE A1056 11994 12395 10805 3285 396 104 C
ATOM 1977 O ILE A1056 -101.943 36.155 316.698 1.00 93.00 O
ANISOU 1977 O ILE A1056 12055 12441 10839 3312 359 7 O
ATOM 1978 CB ILE A1056 -102.084 35.613 319.951 1.00 92.17 C
ANISOU 1978 CB ILE A1056 11877 12440 10705 2994 449 -78 C
ATOM 1979 CG1 ILE A1056 -102.930 34.450 320.452 1.00 93.30 C
ANISOU 1979 CG1 ILE A1056 12122 12600 10727 2802 521 -202 C
ATOM 1980 CG2 ILE A1056 -103.014 36.814 319.635 1.00 92.52 C
ANISOU 1980 CG2 ILE A1056 11751 12571 10830 3029 350 -237 C
ATOM 1981 CD1 ILE A1056 -102.595 34.061 321.691 1.00103.73 C
ANISOU 1981 CD1 ILE A1056 13502 13909 12003 2682 567 -177 C
ATOM 1982 N ASN A1057 -100.081 37.030 317.675 1.00 88.21 N
ANISOU 1982 N ASN A1057 11388 11828 10300 3358 376 232 N
ATOM 1983 CA ASN A1057 -99.796 38.033 316.649 1.00 87.88 C
ANISOU 1983 CA ASN A1057 11345 11753 10291 3455 315 278 C
ATOM 1984 C ASN A1057 -99.687 37.344 315.272 1.00 92.63 C
ANISOU 1984 C ASN A1057 12067 12293 10835 3541 345 326 C
ATOM 1985 O ASN A1057 -100.300 37.809 314.317 1.00 93.11 O
ANISOU 1985 O ASN A1057 12163 12316 10897 3594 277 263 O
ATOM 1986 CB ASN A1057 -98.510 38.787 316.997 1.00 86.85 C
ANISOU 1986 CB ASN A1057 11174 11640 10186 3462 327 420 C
ATOM 1987 CG ASN A1057 -98.243 40.029 316.187 1.00107.30 C
ANISOU 1987 CG ASN A1057 13796 14188 12785 3498 262 453 C
ATOM 1988 OD1 ASN A1057 -98.306 40.050 314.952 1.00106.81 O
ANISOU 1988 OD1 ASN A1057 13832 14065 12686 3562 248 469 O
ATOM 1989 ND2 ASN A1057 -97.822 41.066 316.865 1.00 95.30 N
ANISOU 1989 ND2 ASN A1057 12226 12689 11294 3442 226 478 N
ATOM 1990 N MET A1058 -98.964 36.203 315.203 1.00 89.88 N
ANISOU 1990 N MET A1058 11799 11930 10422 3568 436 424 N
ATOM 1991 CA MET A1058 -98.772 35.371 314.006 1.00 89.71 C
ANISOU 1991 CA MET A1058 11905 11849 10330 3654 479 476 C
ATOM 1992 C MET A1058 -100.106 34.792 313.514 1.00 95.20 C
ANISOU 1992 C MET A1058 12670 12510 10990 3612 458 339 C
ATOM 1993 O MET A1058 -100.331 34.759 312.304 1.00 95.31 O
ANISOU 1993 O MET A1058 12756 12477 10982 3678 440 336 O
ATOM 1994 CB MET A1058 -97.776 34.228 314.287 1.00 91.76 C
ANISOU 1994 CB MET A1058 12247 12106 10511 3714 563 581 C
ATOM 1995 CG MET A1058 -96.326 34.665 314.308 1.00 95.07 C
ANISOU 1995 CG MET A1058 12587 12599 10938 3795 592 707 C
ATOM 1996 SD MET A1058 -95.148 33.307 314.579 1.00 99.84 S
ANISOU 1996 SD MET A1058 13278 13227 11431 3938 657 793 S
ATOM 1997 CE MET A1058 -95.236 32.464 313.029 1.00 97.14 C
ANISOU 1997 CE MET A1058 13092 12813 11005 4055 698 816 C
ATOM 1998 N VAL A1059 -100.984 34.341 314.449 1.00 92.66 N
ANISOU 1998 N VAL A1059 12328 12228 10651 3483 464 216 N
ATOM 1999 CA VAL A1059 -102.309 33.768 314.139 1.00 93.29 C
ANISOU 1999 CA VAL A1059 12441 12328 10676 3391 456 50 C
ATOM 2000 C VAL A1059 -103.221 34.836 313.519 1.00 98.26 C
ANISOU 2000 C VAL A1059 12951 13013 11372 3436 343 -89 C
ATOM 2001 O VAL A1059 -103.968 34.538 312.589 1.00 98.79 O
ANISOU 2001 O VAL A1059 13059 13080 11398 3453 316 -179 O
ATOM 2002 CB VAL A1059 -102.971 33.015 315.332 1.00 97.14 C
ANISOU 2002 CB VAL A1059 12944 12866 11098 3195 507 -62 C
ATOM 2003 CG1 VAL A1059 -104.292 32.372 314.920 1.00 97.69 C
ANISOU 2003 CG1 VAL A1059 13044 12991 11083 3060 517 -248 C
ATOM 2004 CG2 VAL A1059 -102.035 31.954 315.902 1.00 96.80 C
ANISOU 2004 CG2 VAL A1059 13086 12731 10962 3187 589 78 C
ATOM 2005 N PHE A1060 -103.109 36.089 313.987 1.00 94.54 N
ANISOU 2005 N PHE A1060 12355 12577 10989 3476 267 -104 N
ATOM 2006 CA PHE A1060 -103.866 37.210 313.442 1.00 94.42 C
ANISOU 2006 CA PHE A1060 12271 12588 11018 3567 130 -232 C
ATOM 2007 C PHE A1060 -103.453 37.517 311.993 1.00100.85 C
ANISOU 2007 C PHE A1060 13218 13287 11813 3706 86 -135 C
ATOM 2008 O PHE A1060 -104.285 37.995 311.213 1.00103.20 O
ANISOU 2008 O PHE A1060 13525 13583 12102 3794 -29 -261 O
ATOM 2009 CB PHE A1060 -103.698 38.442 314.334 1.00 95.62 C
ANISOU 2009 CB PHE A1060 12319 12769 11242 3578 60 -248 C
ATOM 2010 CG PHE A1060 -104.780 38.560 315.377 1.00 97.60 C
ANISOU 2010 CG PHE A1060 12407 13167 11509 3490 27 -465 C
ATOM 2011 CD1 PHE A1060 -104.775 37.747 316.506 1.00100.45 C
ANISOU 2011 CD1 PHE A1060 12723 13595 11850 3318 135 -478 C
ATOM 2012 CD2 PHE A1060 -105.814 39.480 315.230 1.00100.45 C
ANISOU 2012 CD2 PHE A1060 12672 13605 11889 3586 -119 -672 C
ATOM 2013 CE1 PHE A1060 -105.790 37.844 317.461 1.00102.02 C
ANISOU 2013 CE1 PHE A1060 12767 13949 12047 3204 121 -695 C
ATOM 2014 CE2 PHE A1060 -106.826 39.582 316.191 1.00103.84 C
ANISOU 2014 CE2 PHE A1060 12918 14213 12323 3508 -143 -903 C
ATOM 2015 CZ PHE A1060 -106.807 38.762 317.299 1.00101.80 C
ANISOU 2015 CZ PHE A1060 12601 14033 12046 3299 -12 -913 C
ATOM 2016 N GLN A1061 -102.196 37.203 311.623 1.00 95.90 N
ANISOU 2016 N GLN A1061 12693 12578 11165 3729 175 69 N
ATOM 2017 CA GLN A1061 -101.677 37.454 310.285 1.00 95.78 C
ANISOU 2017 CA GLN A1061 12812 12464 11116 3826 161 170 C
ATOM 2018 C GLN A1061 -101.923 36.324 309.272 1.00101.67 C
ANISOU 2018 C GLN A1061 13671 13168 11792 3853 215 178 C
ATOM 2019 O GLN A1061 -102.297 36.615 308.141 1.00102.89 O
ANISOU 2019 O GLN A1061 13917 13258 11919 3930 148 149 O
ATOM 2020 CB GLN A1061 -100.183 37.797 310.357 1.00 96.38 C
ANISOU 2020 CB GLN A1061 12910 12519 11192 3824 233 358 C
ATOM 2021 CG GLN A1061 -99.636 38.433 309.078 1.00 92.98 C
ANISOU 2021 CG GLN A1061 12616 11999 10713 3882 213 444 C
ATOM 2022 CD GLN A1061 -98.138 38.607 309.049 1.00100.80 C
ANISOU 2022 CD GLN A1061 13604 13021 11674 3846 313 605 C
ATOM 2023 OE1 GLN A1061 -97.441 38.610 310.069 1.00 98.99 O
ANISOU 2023 OE1 GLN A1061 13258 12881 11474 3794 367 654 O
ATOM 2024 NE2 GLN A1061 -97.609 38.789 307.861 1.00 90.06 N
ANISOU 2024 NE2 GLN A1061 12368 11606 10245 3865 339 677 N
ATOM 2025 N MET A1062 -101.696 35.059 309.662 1.00 98.39 N
ANISOU 2025 N MET A1062 13283 12768 11332 3796 325 218 N
ATOM 2026 CA MET A1062 -101.768 33.882 308.783 1.00 98.52 C
ANISOU 2026 CA MET A1062 13446 12727 11261 3817 389 246 C
ATOM 2027 C MET A1062 -102.884 32.886 309.101 1.00101.48 C
ANISOU 2027 C MET A1062 13845 13139 11574 3699 407 102 C
ATOM 2028 O MET A1062 -103.117 31.957 308.322 1.00100.75 O
ANISOU 2028 O MET A1062 13893 12992 11395 3699 445 101 O
ATOM 2029 CB MET A1062 -100.427 33.127 308.857 1.00101.38 C
ANISOU 2029 CB MET A1062 13888 13057 11575 3868 502 419 C
ATOM 2030 CG MET A1062 -99.225 33.977 308.521 1.00105.92 C
ANISOU 2030 CG MET A1062 14430 13636 12177 3947 513 547 C
ATOM 2031 SD MET A1062 -97.691 33.264 309.146 1.00111.11 S
ANISOU 2031 SD MET A1062 15070 14353 12792 4008 622 688 S
ATOM 2032 CE MET A1062 -97.433 34.283 310.532 1.00107.63 C
ANISOU 2032 CE MET A1062 14451 14000 12442 3923 584 675 C
ATOM 2033 N GLY A1063 -103.493 33.022 310.272 1.00 98.22 N
ANISOU 2033 N GLY A1063 13312 12821 11186 3578 395 -16 N
ATOM 2034 CA GLY A1063 -104.523 32.100 310.728 1.00 99.01 C
ANISOU 2034 CA GLY A1063 13432 12986 11202 3405 433 -170 C
ATOM 2035 C GLY A1063 -103.941 30.864 311.383 1.00104.99 C
ANISOU 2035 C GLY A1063 14366 13672 11855 3316 547 -75 C
ATOM 2036 O GLY A1063 -102.781 30.500 311.141 1.00104.18 O
ANISOU 2036 O GLY A1063 14388 13467 11730 3439 593 105 O
ATOM 2037 N GLU A1064 -104.771 30.200 312.206 1.00103.32 N
ANISOU 2037 N GLU A1064 14177 13522 11556 3100 590 -214 N
ATOM 2038 CA GLU A1064 -104.481 28.974 312.962 1.00103.83 C
ANISOU 2038 CA GLU A1064 14471 13502 11477 2968 684 -165 C
ATOM 2039 C GLU A1064 -103.781 27.868 312.136 1.00109.12 C
ANISOU 2039 C GLU A1064 15434 14001 12024 3073 734 -19 C
ATOM 2040 O GLU A1064 -102.841 27.242 312.629 1.00109.47 O
ANISOU 2040 O GLU A1064 15658 13937 11998 3141 772 113 O
ATOM 2041 CB GLU A1064 -105.792 28.444 313.544 1.00106.12 C
ANISOU 2041 CB GLU A1064 14767 13900 11655 2670 723 -384 C
ATOM 2042 CG GLU A1064 -105.661 27.787 314.897 1.00116.68 C
ANISOU 2042 CG GLU A1064 16253 15201 12880 2477 795 -386 C
ATOM 2043 CD GLU A1064 -106.994 27.339 315.456 1.00141.28 C
ANISOU 2043 CD GLU A1064 19363 18453 15865 2132 850 -626 C
ATOM 2044 OE1 GLU A1064 -107.226 26.111 315.524 1.00147.40 O
ANISOU 2044 OE1 GLU A1064 20447 19131 16428 1934 930 -641 O
ATOM 2045 OE2 GLU A1064 -107.827 28.216 315.782 1.00132.66 O
ANISOU 2045 OE2 GLU A1064 17966 17575 14864 2055 811 -815 O
ATOM 2046 N THR A1065 -104.240 27.640 310.894 1.00106.44 N
ANISOU 2046 N THR A1065 15146 13643 11655 3105 723 -53 N
ATOM 2047 CA THR A1065 -103.726 26.619 309.973 1.00107.60 C
ANISOU 2047 CA THR A1065 15568 13635 11681 3205 766 63 C
ATOM 2048 C THR A1065 -102.300 26.954 309.454 1.00111.38 C
ANISOU 2048 C THR A1065 16037 14049 12234 3488 758 257 C
ATOM 2049 O THR A1065 -101.442 26.059 309.404 1.00111.66 O
ANISOU 2049 O THR A1065 16295 13969 12160 3602 801 374 O
ATOM 2050 CB THR A1065 -104.764 26.379 308.858 1.00118.44 C
ANISOU 2050 CB THR A1065 16968 15031 13001 3126 753 -56 C
ATOM 2051 OG1 THR A1065 -105.927 25.796 309.455 1.00121.18 O
ANISOU 2051 OG1 THR A1065 17352 15460 13230 2829 787 -242 O
ATOM 2052 CG2 THR A1065 -104.249 25.480 307.725 1.00115.61 C
ANISOU 2052 CG2 THR A1065 16886 14512 12530 3247 790 63 C
ATOM 2053 N GLY A1066 -102.081 28.219 309.078 1.00106.49 N
ANISOU 2053 N GLY A1066 15178 13511 11774 3592 700 273 N
ATOM 2054 CA GLY A1066 -100.794 28.723 308.606 1.00105.33 C
ANISOU 2054 CA GLY A1066 14981 13349 11691 3801 703 428 C
ATOM 2055 C GLY A1066 -99.704 28.677 309.664 1.00108.88 C
ANISOU 2055 C GLY A1066 15409 13818 12144 3868 731 524 C
ATOM 2056 O GLY A1066 -98.560 28.319 309.358 1.00109.35 O
ANISOU 2056 O GLY A1066 15538 13853 12157 4038 766 640 O
ATOM 2057 N VAL A1067 -100.061 29.009 310.931 1.00103.46 N
ANISOU 2057 N VAL A1067 14620 13190 11500 3740 712 461 N
ATOM 2058 CA VAL A1067 -99.141 28.998 312.073 1.00102.53 C
ANISOU 2058 CA VAL A1067 14475 13096 11384 3785 724 534 C
ATOM 2059 C VAL A1067 -98.735 27.554 312.443 1.00106.72 C
ANISOU 2059 C VAL A1067 15299 13512 11739 3833 763 580 C
ATOM 2060 O VAL A1067 -97.554 27.301 312.693 1.00106.88 O
ANISOU 2060 O VAL A1067 15352 13533 11724 4012 766 678 O
ATOM 2061 CB VAL A1067 -99.705 29.813 313.266 1.00105.74 C
ANISOU 2061 CB VAL A1067 14704 13590 11883 3626 690 446 C
ATOM 2062 CG1 VAL A1067 -98.782 29.764 314.479 1.00105.39 C
ANISOU 2062 CG1 VAL A1067 14648 13564 11833 3664 696 520 C
ATOM 2063 CG2 VAL A1067 -99.946 31.258 312.855 1.00104.94 C
ANISOU 2063 CG2 VAL A1067 14366 13576 11931 3635 630 411 C
ATOM 2064 N ALA A1068 -99.700 26.606 312.413 1.00102.73 N
ANISOU 2064 N ALA A1068 15020 12910 11101 3678 786 498 N
ATOM 2065 CA ALA A1068 -99.487 25.179 312.694 1.00102.80 C
ANISOU 2065 CA ALA A1068 15400 12763 10898 3694 814 528 C
ATOM 2066 C ALA A1068 -98.508 24.527 311.695 1.00107.03 C
ANISOU 2066 C ALA A1068 16097 13218 11352 3967 821 639 C
ATOM 2067 O ALA A1068 -97.978 23.447 311.965 1.00108.44 O
ANISOU 2067 O ALA A1068 16582 13266 11353 4078 819 684 O
ATOM 2068 CB ALA A1068 -100.817 24.444 312.691 1.00104.08 C
ANISOU 2068 CB ALA A1068 15762 12857 10926 3418 847 401 C
ATOM 2069 N GLY A1069 -98.263 25.212 310.574 1.00102.21 N
ANISOU 2069 N GLY A1069 15296 12685 10856 4079 824 673 N
ATOM 2070 CA GLY A1069 -97.333 24.795 309.532 1.00101.48 C
ANISOU 2070 CA GLY A1069 15288 12563 10707 4327 842 761 C
ATOM 2071 C GLY A1069 -95.871 24.898 309.931 1.00103.83 C
ANISOU 2071 C GLY A1069 15490 12949 11010 4570 832 842 C
ATOM 2072 O GLY A1069 -95.045 24.176 309.377 1.00105.07 O
ANISOU 2072 O GLY A1069 15782 13081 11059 4802 843 891 O
ATOM 2073 N PHE A1070 -95.530 25.778 310.910 1.00 98.07 N
ANISOU 2073 N PHE A1070 14523 12343 10397 4527 808 843 N
ATOM 2074 CA PHE A1070 -94.156 25.995 311.401 1.00 97.32 C
ANISOU 2074 CA PHE A1070 14284 12381 10313 4729 794 899 C
ATOM 2075 C PHE A1070 -93.770 24.962 312.471 1.00102.80 C
ANISOU 2075 C PHE A1070 15225 12983 10850 4839 749 901 C
ATOM 2076 O PHE A1070 -93.286 25.338 313.539 1.00103.91 O
ANISOU 2076 O PHE A1070 15243 13208 11030 4851 713 905 O
ATOM 2077 CB PHE A1070 -93.999 27.423 311.967 1.00 97.25 C
ANISOU 2077 CB PHE A1070 13934 12534 10484 4611 784 897 C
ATOM 2078 CG PHE A1070 -94.237 28.574 311.018 1.00 97.31 C
ANISOU 2078 CG PHE A1070 13731 12620 10621 4525 806 898 C
ATOM 2079 CD1 PHE A1070 -93.216 29.047 310.202 1.00100.21 C
ANISOU 2079 CD1 PHE A1070 13950 13121 11003 4648 842 947 C
ATOM 2080 CD2 PHE A1070 -95.460 29.234 310.992 1.00 97.80 C
ANISOU 2080 CD2 PHE A1070 13747 12637 10777 4320 782 836 C
ATOM 2081 CE1 PHE A1070 -93.424 30.140 309.350 1.00100.03 C
ANISOU 2081 CE1 PHE A1070 13794 13142 11071 4545 857 951 C
ATOM 2082 CE2 PHE A1070 -95.669 30.320 310.135 1.00 99.81 C
ANISOU 2082 CE2 PHE A1070 13859 12936 11127 4268 776 834 C
ATOM 2083 CZ PHE A1070 -94.647 30.771 309.327 1.00 97.98 C
ANISOU 2083 CZ PHE A1070 13536 12797 10896 4370 813 900 C
ATOM 2084 N THR A1071 -93.959 23.666 312.174 1.00 99.30 N
ANISOU 2084 N THR A1071 15159 12356 10214 4922 742 898 N
ATOM 2085 CA THR A1071 -93.756 22.533 313.088 1.00100.29 C
ANISOU 2085 CA THR A1071 15648 12323 10135 5017 685 895 C
ATOM 2086 C THR A1071 -92.388 22.520 313.799 1.00104.08 C
ANISOU 2086 C THR A1071 16039 12924 10584 5311 617 920 C
ATOM 2087 O THR A1071 -92.338 22.304 315.022 1.00104.55 O
ANISOU 2087 O THR A1071 16226 12923 10577 5287 559 910 O
ATOM 2088 CB THR A1071 -94.036 21.215 312.365 1.00109.52 C
ANISOU 2088 CB THR A1071 17252 13275 11086 5098 687 895 C
ATOM 2089 OG1 THR A1071 -95.269 21.343 311.658 1.00112.43 O
ANISOU 2089 OG1 THR A1071 17638 13582 11497 4820 749 859 O
ATOM 2090 CG2 THR A1071 -94.128 20.030 313.317 1.00107.76 C
ANISOU 2090 CG2 THR A1071 17511 12822 10612 5116 623 883 C
ATOM 2091 N ASN A1072 -91.303 22.766 313.050 1.00 99.11 N
ANISOU 2091 N ASN A1072 15183 12483 9991 5572 627 938 N
ATOM 2092 CA ASN A1072 -89.946 22.763 313.599 1.00 99.33 C
ANISOU 2092 CA ASN A1072 15070 12691 9981 5871 563 931 C
ATOM 2093 C ASN A1072 -89.748 23.927 314.572 1.00101.22 C
ANISOU 2093 C ASN A1072 14962 13108 10388 5723 557 932 C
ATOM 2094 O ASN A1072 -89.411 23.701 315.734 1.00 99.97 O
ANISOU 2094 O ASN A1072 14877 12941 10167 5801 478 920 O
ATOM 2095 CB ASN A1072 -88.907 22.775 312.474 1.00 99.23 C
ANISOU 2095 CB ASN A1072 14867 12882 9955 6145 596 921 C
ATOM 2096 CG ASN A1072 -89.027 21.613 311.511 1.00116.84 C
ANISOU 2096 CG ASN A1072 17440 14940 12012 6319 599 918 C
ATOM 2097 OD1 ASN A1072 -88.780 20.456 311.862 1.00117.32 O
ANISOU 2097 OD1 ASN A1072 17903 14812 11861 6520 515 904 O
ATOM 2098 ND2 ASN A1072 -89.374 21.897 310.264 1.00102.45 N
ANISOU 2098 ND2 ASN A1072 15494 13172 10262 6255 689 931 N
ATOM 2099 N SER A1073 -90.048 25.164 314.117 1.00 97.41 N
ANISOU 2099 N SER A1073 14146 12761 10106 5498 632 944 N
ATOM 2100 CA SER A1073 -89.951 26.389 314.929 1.00 95.24 C
ANISOU 2100 CA SER A1073 13553 12642 9993 5325 634 947 C
ATOM 2101 C SER A1073 -90.811 26.310 316.191 1.00 98.36 C
ANISOU 2101 C SER A1073 14102 12880 10391 5127 591 935 C
ATOM 2102 O SER A1073 -90.362 26.750 317.250 1.00 98.25 O
ANISOU 2102 O SER A1073 13954 12962 10415 5123 548 933 O
ATOM 2103 CB SER A1073 -90.304 27.618 314.098 1.00 94.37 C
ANISOU 2103 CB SER A1073 13173 12630 10052 5119 708 960 C
ATOM 2104 OG SER A1073 -89.498 27.675 312.933 1.00 99.89 O
ANISOU 2104 OG SER A1073 13744 13480 10729 5270 760 966 O
ATOM 2105 N LEU A1074 -92.017 25.707 316.090 1.00 94.88 N
ANISOU 2105 N LEU A1074 13946 12212 9891 4955 605 915 N
ATOM 2106 CA LEU A1074 -92.924 25.528 317.232 1.00 94.87 C
ANISOU 2106 CA LEU A1074 14119 12069 9858 4725 584 880 C
ATOM 2107 C LEU A1074 -92.348 24.540 318.261 1.00 99.67 C
ANISOU 2107 C LEU A1074 15030 12565 10274 4891 502 885 C
ATOM 2108 O LEU A1074 -92.565 24.726 319.454 1.00 99.46 O
ANISOU 2108 O LEU A1074 15034 12508 10249 4754 472 868 O
ATOM 2109 CB LEU A1074 -94.340 25.098 316.792 1.00 94.67 C
ANISOU 2109 CB LEU A1074 14310 11873 9788 4478 632 830 C
ATOM 2110 CG LEU A1074 -95.181 26.068 315.954 1.00 96.85 C
ANISOU 2110 CG LEU A1074 14332 12231 10236 4290 686 795 C
ATOM 2111 CD1 LEU A1074 -96.406 25.377 315.434 1.00 96.78 C
ANISOU 2111 CD1 LEU A1074 14564 12076 10132 4112 722 732 C
ATOM 2112 CD2 LEU A1074 -95.574 27.299 316.738 1.00 96.81 C
ANISOU 2112 CD2 LEU A1074 14042 12341 10399 4095 681 756 C
ATOM 2113 N ARG A1075 -91.590 23.517 317.810 1.00 97.27 N
ANISOU 2113 N ARG A1075 14968 12197 9795 5200 456 901 N
ATOM 2114 CA ARG A1075 -90.948 22.592 318.743 1.00 98.62 C
ANISOU 2114 CA ARG A1075 15460 12253 9758 5420 346 898 C
ATOM 2115 C ARG A1075 -89.740 23.268 319.410 1.00102.12 C
ANISOU 2115 C ARG A1075 15573 12946 10283 5626 283 900 C
ATOM 2116 O ARG A1075 -89.446 22.972 320.565 1.00103.61 O
ANISOU 2116 O ARG A1075 15920 13074 10374 5691 192 890 O
ATOM 2117 CB ARG A1075 -90.550 21.275 318.064 1.00101.67 C
ANISOU 2117 CB ARG A1075 16240 12482 9908 5717 296 898 C
ATOM 2118 CG ARG A1075 -89.935 20.242 319.021 1.00119.17 C
ANISOU 2118 CG ARG A1075 18894 14522 11865 5963 156 885 C
ATOM 2119 CD ARG A1075 -88.694 19.561 318.442 1.00143.77 C
ANISOU 2119 CD ARG A1075 22081 17711 14833 6471 60 865 C
ATOM 2120 NE ARG A1075 -87.572 20.479 318.182 1.00152.62 N
ANISOU 2120 NE ARG A1075 22640 19220 16129 6676 67 844 N
ATOM 2121 CZ ARG A1075 -86.313 20.093 317.969 1.00161.10 C
ANISOU 2121 CZ ARG A1075 23642 20470 17099 7125 -23 791 C
ATOM 2122 NH1 ARG A1075 -85.986 18.805 318.015 1.00144.13 N
ANISOU 2122 NH1 ARG A1075 21971 18120 14670 7468 -150 758 N
ATOM 2123 NH2 ARG A1075 -85.364 20.997 317.752 1.00140.76 N
ANISOU 2123 NH2 ARG A1075 20526 18282 14676 7233 7 755 N
ATOM 2124 N MET A1076 -89.051 24.181 318.696 1.00 96.69 N
ANISOU 2124 N MET A1076 14440 12539 9757 5702 333 906 N
ATOM 2125 CA MET A1076 -87.892 24.896 319.244 1.00 96.07 C
ANISOU 2125 CA MET A1076 14004 12747 9753 5851 292 892 C
ATOM 2126 C MET A1076 -88.317 25.802 320.390 1.00 96.06 C
ANISOU 2126 C MET A1076 13849 12765 9883 5572 292 903 C
ATOM 2127 O MET A1076 -87.664 25.800 321.433 1.00 94.75 O
ANISOU 2127 O MET A1076 13656 12670 9673 5688 206 889 O
ATOM 2128 CB MET A1076 -87.148 25.685 318.155 1.00 98.09 C
ANISOU 2128 CB MET A1076 13848 13296 10125 5916 370 886 C
ATOM 2129 CG MET A1076 -86.225 24.831 317.311 1.00103.57 C
ANISOU 2129 CG MET A1076 14605 14079 10667 6291 344 846 C
ATOM 2130 SD MET A1076 -85.903 25.621 315.716 1.00107.14 S
ANISOU 2130 SD MET A1076 14680 14789 11238 6238 482 842 S
ATOM 2131 CE MET A1076 -85.297 24.228 314.773 1.00105.83 C
ANISOU 2131 CE MET A1076 14753 14603 10854 6658 447 791 C
ATOM 2132 N LEU A1077 -89.443 26.534 320.208 1.00 91.17 N
ANISOU 2132 N LEU A1077 13148 12080 9413 5223 378 917 N
ATOM 2133 CA LEU A1077 -90.018 27.428 321.214 1.00 90.07 C
ANISOU 2133 CA LEU A1077 12873 11948 9401 4943 386 914 C
ATOM 2134 C LEU A1077 -90.476 26.625 322.439 1.00 96.94 C
ANISOU 2134 C LEU A1077 14103 12601 10128 4879 322 896 C
ATOM 2135 O LEU A1077 -90.185 27.016 323.571 1.00 97.60 O
ANISOU 2135 O LEU A1077 14110 12734 10239 4832 276 894 O
ATOM 2136 CB LEU A1077 -91.177 28.249 320.636 1.00 88.00 C
ANISOU 2136 CB LEU A1077 12475 11663 9297 4640 474 904 C
ATOM 2137 CG LEU A1077 -90.841 29.254 319.528 1.00 91.40 C
ANISOU 2137 CG LEU A1077 12584 12277 9865 4640 532 924 C
ATOM 2138 CD1 LEU A1077 -92.100 29.724 318.834 1.00 89.57 C
ANISOU 2138 CD1 LEU A1077 12353 11954 9725 4417 587 899 C
ATOM 2139 CD2 LEU A1077 -90.051 30.443 320.063 1.00 92.93 C
ANISOU 2139 CD2 LEU A1077 12441 12691 10176 4598 525 938 C
ATOM 2140 N GLN A1078 -91.122 25.466 322.204 1.00 93.92 N
ANISOU 2140 N GLN A1078 14140 11974 9570 4873 319 882 N
ATOM 2141 CA GLN A1078 -91.587 24.532 323.234 1.00 94.06 C
ANISOU 2141 CA GLN A1078 14602 11746 9391 4789 266 861 C
ATOM 2142 C GLN A1078 -90.398 24.050 324.065 1.00 98.78 C
ANISOU 2142 C GLN A1078 15327 12354 9850 5107 132 874 C
ATOM 2143 O GLN A1078 -90.500 23.983 325.287 1.00 99.30 O
ANISOU 2143 O GLN A1078 15540 12334 9854 5009 79 864 O
ATOM 2144 CB GLN A1078 -92.276 23.343 322.555 1.00 96.27 C
ANISOU 2144 CB GLN A1078 15321 11781 9476 4760 289 847 C
ATOM 2145 CG GLN A1078 -93.142 22.484 323.467 1.00103.89 C
ANISOU 2145 CG GLN A1078 16767 12474 10232 4512 281 809 C
ATOM 2146 CD GLN A1078 -93.804 21.350 322.712 1.00120.37 C
ANISOU 2146 CD GLN A1078 19293 14332 12112 4448 313 791 C
ATOM 2147 OE1 GLN A1078 -93.653 21.184 321.486 1.00116.64 O
ANISOU 2147 OE1 GLN A1078 18762 13893 11663 4597 341 809 O
ATOM 2148 NE2 GLN A1078 -94.556 20.534 323.433 1.00109.14 N
ANISOU 2148 NE2 GLN A1078 18341 12666 10463 4200 316 750 N
ATOM 2149 N GLN A1079 -89.262 23.748 323.401 1.00 95.75 N
ANISOU 2149 N GLN A1079 14864 12100 9416 5494 73 880 N
ATOM 2150 CA GLN A1079 -88.020 23.299 324.044 1.00 96.82 C
ANISOU 2150 CA GLN A1079 15064 12309 9416 5874 -74 863 C
ATOM 2151 C GLN A1079 -87.235 24.478 324.651 1.00100.85 C
ANISOU 2151 C GLN A1079 15083 13131 10106 5880 -87 858 C
ATOM 2152 O GLN A1079 -86.215 24.253 325.309 1.00102.24 O
ANISOU 2152 O GLN A1079 15248 13413 10185 6172 -214 827 O
ATOM 2153 CB GLN A1079 -87.139 22.531 323.056 1.00 99.20 C
ANISOU 2153 CB GLN A1079 15430 12675 9587 6294 -127 839 C
ATOM 2154 CG GLN A1079 -87.651 21.146 322.684 1.00113.93 C
ANISOU 2154 CG GLN A1079 17893 14199 11195 6385 -168 838 C
ATOM 2155 CD GLN A1079 -86.722 20.472 321.695 1.00136.03 C
ANISOU 2155 CD GLN A1079 20732 17085 13870 6833 -227 803 C
ATOM 2156 OE1 GLN A1079 -86.188 21.103 320.780 1.00127.72 O
ANISOU 2156 OE1 GLN A1079 19229 16334 12965 6940 -162 787 O
ATOM 2157 NE2 GLN A1079 -86.483 19.176 321.873 1.00132.57 N
ANISOU 2157 NE2 GLN A1079 20856 16379 13134 7103 -355 782 N
ATOM 2158 N LYS A1080 -87.724 25.729 324.443 1.00 95.47 N
ANISOU 2158 N LYS A1080 14018 12589 9666 5561 33 880 N
ATOM 2159 CA LYS A1080 -87.130 26.976 324.940 1.00 94.80 C
ANISOU 2159 CA LYS A1080 13484 12780 9755 5486 43 881 C
ATOM 2160 C LYS A1080 -85.765 27.282 324.279 1.00100.96 C
ANISOU 2160 C LYS A1080 13904 13902 10556 5769 30 852 C
ATOM 2161 O LYS A1080 -84.849 27.775 324.944 1.00102.54 O
ANISOU 2161 O LYS A1080 13847 14334 10779 5858 -26 826 O
ATOM 2162 CB LYS A1080 -87.059 27.003 326.491 1.00 97.63 C
ANISOU 2162 CB LYS A1080 13957 13072 10066 5435 -49 877 C
ATOM 2163 CG LYS A1080 -88.408 26.755 327.167 1.00105.18 C
ANISOU 2163 CG LYS A1080 15232 13736 10997 5102 -12 884 C
ATOM 2164 CD LYS A1080 -88.431 27.115 328.639 1.00108.62 C
ANISOU 2164 CD LYS A1080 15682 14148 11439 4965 -66 881 C
ATOM 2165 CE LYS A1080 -89.851 27.225 329.149 1.00122.72 C
ANISOU 2165 CE LYS A1080 17650 15731 13246 4563 14 865 C
ATOM 2166 NZ LYS A1080 -90.574 28.410 328.581 1.00136.82 N
ANISOU 2166 NZ LYS A1080 19071 17645 15268 4292 138 858 N
ATOM 2167 N ARG A1081 -85.642 26.977 322.965 1.00 96.68 N
ANISOU 2167 N ARG A1081 13337 13404 9993 5892 87 845 N
ATOM 2168 CA ARG A1081 -84.456 27.230 322.140 1.00 97.21 C
ANISOU 2168 CA ARG A1081 13063 13810 10064 6120 106 798 C
ATOM 2169 C ARG A1081 -84.793 28.466 321.304 1.00101.02 C
ANISOU 2169 C ARG A1081 13220 14421 10741 5812 253 832 C
ATOM 2170 O ARG A1081 -85.096 28.358 320.112 1.00100.43 O
ANISOU 2170 O ARG A1081 13170 14309 10679 5792 332 844 O
ATOM 2171 CB ARG A1081 -84.146 26.012 321.254 1.00 96.35 C
ANISOU 2171 CB ARG A1081 13192 13639 9778 6461 70 761 C
ATOM 2172 CG ARG A1081 -83.593 24.810 322.029 1.00101.18 C
ANISOU 2172 CG ARG A1081 14141 14147 10157 6842 -105 709 C
ATOM 2173 CD ARG A1081 -83.890 23.510 321.316 1.00101.84 C
ANISOU 2173 CD ARG A1081 14657 13985 10052 7068 -139 703 C
ATOM 2174 NE ARG A1081 -83.321 22.354 322.002 1.00106.41 N
ANISOU 2174 NE ARG A1081 15624 14432 10375 7460 -328 649 N
ATOM 2175 CZ ARG A1081 -82.179 21.766 321.664 1.00128.81 C
ANISOU 2175 CZ ARG A1081 18418 17467 13057 7938 -437 548 C
ATOM 2176 NH1 ARG A1081 -81.469 22.220 320.638 1.00121.80 N
ANISOU 2176 NH1 ARG A1081 17090 16942 12245 8054 -356 486 N
ATOM 2177 NH2 ARG A1081 -81.734 20.723 322.349 1.00118.91 N
ANISOU 2177 NH2 ARG A1081 17577 16053 11552 8309 -635 494 N
ATOM 2178 N TRP A1082 -84.812 29.641 321.975 1.00 97.48 N
ANISOU 2178 N TRP A1082 12513 14092 10432 5563 279 850 N
ATOM 2179 CA TRP A1082 -85.214 30.953 321.447 1.00 96.00 C
ANISOU 2179 CA TRP A1082 12081 13980 10415 5243 390 885 C
ATOM 2180 C TRP A1082 -84.436 31.405 320.232 1.00102.20 C
ANISOU 2180 C TRP A1082 12601 15028 11203 5280 476 860 C
ATOM 2181 O TRP A1082 -85.051 31.652 319.198 1.00101.80 O
ANISOU 2181 O TRP A1082 12587 14885 11208 5142 557 890 O
ATOM 2182 CB TRP A1082 -85.186 32.034 322.543 1.00 94.00 C
ANISOU 2182 CB TRP A1082 11641 13808 10268 5019 376 899 C
ATOM 2183 CG TRP A1082 -85.776 31.622 323.871 1.00 94.30 C
ANISOU 2183 CG TRP A1082 11911 13633 10285 4983 293 909 C
ATOM 2184 CD1 TRP A1082 -85.167 31.695 325.086 1.00 97.78 C
ANISOU 2184 CD1 TRP A1082 12294 14164 10693 5042 209 893 C
ATOM 2185 CD2 TRP A1082 -87.094 31.085 324.113 1.00 92.97 C
ANISOU 2185 CD2 TRP A1082 12075 13140 10110 4855 292 927 C
ATOM 2186 NE1 TRP A1082 -86.017 31.246 326.072 1.00 96.64 N
ANISOU 2186 NE1 TRP A1082 12444 13754 10522 4954 157 907 N
ATOM 2187 CE2 TRP A1082 -87.204 30.859 325.504 1.00 96.88 C
ANISOU 2187 CE2 TRP A1082 12710 13539 10561 4827 214 921 C
ATOM 2188 CE3 TRP A1082 -88.192 30.766 323.288 1.00 92.78 C
ANISOU 2188 CE3 TRP A1082 12237 12915 10099 4747 352 934 C
ATOM 2189 CZ2 TRP A1082 -88.365 30.332 326.092 1.00 95.09 C
ANISOU 2189 CZ2 TRP A1082 12805 13031 10295 4668 208 918 C
ATOM 2190 CZ3 TRP A1082 -89.325 30.207 323.867 1.00 93.39 C
ANISOU 2190 CZ3 TRP A1082 12614 12735 10136 4605 341 922 C
ATOM 2191 CH2 TRP A1082 -89.407 30.001 325.255 1.00 94.18 C
ANISOU 2191 CH2 TRP A1082 12850 12751 10184 4553 277 912 C
ATOM 2192 N ASP A1083 -83.100 31.499 320.339 1.00101.48 N
ANISOU 2192 N ASP A1083 12246 15274 11038 5460 458 792 N
ATOM 2193 CA ASP A1083 -82.214 31.894 319.236 1.00102.93 C
ANISOU 2193 CA ASP A1083 12152 15765 11190 5481 552 740 C
ATOM 2194 C ASP A1083 -82.364 30.979 318.018 1.00107.36 C
ANISOU 2194 C ASP A1083 12886 16233 11672 5670 587 729 C
ATOM 2195 O ASP A1083 -82.401 31.487 316.898 1.00107.75 O
ANISOU 2195 O ASP A1083 12843 16343 11753 5523 697 740 O
ATOM 2196 CB ASP A1083 -80.741 31.971 319.692 1.00107.49 C
ANISOU 2196 CB ASP A1083 12400 16767 11676 5662 516 630 C
ATOM 2197 CG ASP A1083 -80.489 32.907 320.863 1.00120.64 C
ANISOU 2197 CG ASP A1083 13867 18560 13410 5457 490 636 C
ATOM 2198 OD1 ASP A1083 -81.046 34.035 320.861 1.00120.32 O
ANISOU 2198 OD1 ASP A1083 13790 18436 13492 5094 562 707 O
ATOM 2199 OD2 ASP A1083 -79.751 32.510 321.790 1.00128.72 O
ANISOU 2199 OD2 ASP A1083 14793 19760 14355 5672 385 565 O
ATOM 2200 N GLU A1084 -82.477 29.641 318.243 1.00103.53 N
ANISOU 2200 N GLU A1084 12693 15576 11069 5983 488 711 N
ATOM 2201 CA GLU A1084 -82.670 28.598 317.220 1.00102.78 C
ANISOU 2201 CA GLU A1084 12835 15345 10873 6193 500 703 C
ATOM 2202 C GLU A1084 -83.981 28.834 316.485 1.00105.10 C
ANISOU 2202 C GLU A1084 13319 15346 11269 5915 582 792 C
ATOM 2203 O GLU A1084 -84.005 28.812 315.256 1.00105.80 O
ANISOU 2203 O GLU A1084 13390 15462 11348 5911 666 791 O
ATOM 2204 CB GLU A1084 -82.710 27.202 317.863 1.00104.70 C
ANISOU 2204 CB GLU A1084 13448 15379 10956 6525 357 681 C
ATOM 2205 CG GLU A1084 -81.415 26.429 317.833 1.00108.67 C
ANISOU 2205 CG GLU A1084 13858 16148 11282 6974 265 559 C
ATOM 2206 CD GLU A1084 -81.585 25.017 318.365 1.00132.94 C
ANISOU 2206 CD GLU A1084 17405 18940 14166 7309 110 546 C
ATOM 2207 OE1 GLU A1084 -82.110 24.157 317.618 1.00121.99 O
ANISOU 2207 OE1 GLU A1084 16349 17309 12692 7397 120 572 O
ATOM 2208 OE2 GLU A1084 -81.211 24.773 319.538 1.00130.32 O
ANISOU 2208 OE2 GLU A1084 17144 18616 13756 7473 -28 510 O
ATOM 2209 N ALA A1085 -85.066 29.084 317.234 1.00100.20 N
ANISOU 2209 N ALA A1085 12865 14467 10738 5684 557 853 N
ATOM 2210 CA ALA A1085 -86.374 29.368 316.654 1.00 98.64 C
ANISOU 2210 CA ALA A1085 12818 14023 10637 5423 617 909 C
ATOM 2211 C ALA A1085 -86.332 30.683 315.858 1.00103.46 C
ANISOU 2211 C ALA A1085 13161 14781 11369 5185 714 926 C
ATOM 2212 O ALA A1085 -86.826 30.719 314.729 1.00104.05 O
ANISOU 2212 O ALA A1085 13310 14766 11460 5117 774 944 O
ATOM 2213 CB ALA A1085 -87.420 29.441 317.747 1.00 98.01 C
ANISOU 2213 CB ALA A1085 12910 13715 10615 5231 569 934 C
ATOM 2214 N ALA A1086 -85.680 31.733 316.417 1.00 99.51 N
ANISOU 2214 N ALA A1086 12377 14504 10927 5063 724 917 N
ATOM 2215 CA ALA A1086 -85.505 33.057 315.802 1.00 98.58 C
ANISOU 2215 CA ALA A1086 12042 14528 10885 4816 807 930 C
ATOM 2216 C ALA A1086 -84.766 32.993 314.456 1.00101.87 C
ANISOU 2216 C ALA A1086 12356 15129 11221 4887 898 899 C
ATOM 2217 O ALA A1086 -85.105 33.726 313.523 1.00100.80 O
ANISOU 2217 O ALA A1086 12222 14955 11121 4690 968 925 O
ATOM 2218 CB ALA A1086 -84.760 33.977 316.762 1.00 99.91 C
ANISOU 2218 CB ALA A1086 11956 14920 11084 4699 795 914 C
ATOM 2219 N VAL A1087 -83.768 32.102 314.364 1.00 99.14 N
ANISOU 2219 N VAL A1087 11938 14980 10751 5182 888 833 N
ATOM 2220 CA VAL A1087 -82.940 31.890 313.175 1.00100.06 C
ANISOU 2220 CA VAL A1087 11931 15322 10766 5296 974 773 C
ATOM 2221 C VAL A1087 -83.734 31.182 312.054 1.00104.72 C
ANISOU 2221 C VAL A1087 12798 15655 11337 5361 1000 811 C
ATOM 2222 O VAL A1087 -83.632 31.568 310.876 1.00104.50 O
ANISOU 2222 O VAL A1087 12728 15686 11292 5252 1098 811 O
ATOM 2223 CB VAL A1087 -81.622 31.163 313.571 1.00105.06 C
ANISOU 2223 CB VAL A1087 12376 16278 11264 5632 932 660 C
ATOM 2224 CG1 VAL A1087 -80.994 30.421 312.395 1.00106.29 C
ANISOU 2224 CG1 VAL A1087 12508 16589 11290 5870 989 583 C
ATOM 2225 CG2 VAL A1087 -80.629 32.138 314.199 1.00105.51 C
ANISOU 2225 CG2 VAL A1087 12061 16707 11322 5497 957 596 C
ATOM 2226 N ASN A1088 -84.525 30.156 312.438 1.00100.57 N
ANISOU 2226 N ASN A1088 12574 14841 10796 5514 915 841 N
ATOM 2227 CA ASN A1088 -85.351 29.357 311.532 1.00 99.16 C
ANISOU 2227 CA ASN A1088 12691 14402 10585 5575 926 872 C
ATOM 2228 C ASN A1088 -86.537 30.150 310.980 1.00 99.99 C
ANISOU 2228 C ASN A1088 12886 14296 10810 5268 964 935 C
ATOM 2229 O ASN A1088 -86.893 29.985 309.810 1.00 98.28 O
ANISOU 2229 O ASN A1088 12779 13992 10572 5254 1016 948 O
ATOM 2230 CB ASN A1088 -85.829 28.097 312.248 1.00 97.56 C
ANISOU 2230 CB ASN A1088 12806 13962 10301 5778 823 876 C
ATOM 2231 CG ASN A1088 -86.350 27.012 311.337 1.00111.71 C
ANISOU 2231 CG ASN A1088 14900 15555 11988 5931 830 882 C
ATOM 2232 OD1 ASN A1088 -87.485 26.546 311.488 1.00115.96 O
ANISOU 2232 OD1 ASN A1088 15742 15796 12523 5846 799 918 O
ATOM 2233 ND2 ASN A1088 -85.526 26.548 310.404 1.00 91.56 N
ANISOU 2233 ND2 ASN A1088 12278 13177 9333 6154 872 833 N
ATOM 2234 N LEU A1089 -87.156 30.999 311.826 1.00 95.55 N
ANISOU 2234 N LEU A1089 12285 13655 10366 5042 929 964 N
ATOM 2235 CA LEU A1089 -88.301 31.814 311.416 1.00 93.70 C
ANISOU 2235 CA LEU A1089 12126 13237 10238 4787 937 997 C
ATOM 2236 C LEU A1089 -87.904 32.932 310.457 1.00 98.27 C
ANISOU 2236 C LEU A1089 12561 13942 10834 4624 1011 1007 C
ATOM 2237 O LEU A1089 -88.710 33.296 309.607 1.00 97.90 O
ANISOU 2237 O LEU A1089 12639 13737 10820 4506 1018 1025 O
ATOM 2238 CB LEU A1089 -89.083 32.354 312.618 1.00 92.32 C
ANISOU 2238 CB LEU A1089 11954 12955 10167 4623 870 1003 C
ATOM 2239 CG LEU A1089 -89.927 31.338 313.396 1.00 95.91 C
ANISOU 2239 CG LEU A1089 12633 13208 10600 4678 807 989 C
ATOM 2240 CD1 LEU A1089 -90.205 31.832 314.811 1.00 94.77 C
ANISOU 2240 CD1 LEU A1089 12423 13061 10525 4560 753 981 C
ATOM 2241 CD2 LEU A1089 -91.229 31.004 312.657 1.00 96.35 C
ANISOU 2241 CD2 LEU A1089 12896 13041 10670 4589 806 977 C
ATOM 2242 N ALA A1090 -86.653 33.438 310.548 1.00 95.04 N
ANISOU 2242 N ALA A1090 11908 13824 10379 4614 1065 983 N
ATOM 2243 CA ALA A1090 -86.146 34.480 309.648 1.00 94.72 C
ANISOU 2243 CA ALA A1090 11756 13925 10309 4419 1152 982 C
ATOM 2244 C ALA A1090 -85.831 33.933 308.244 1.00100.02 C
ANISOU 2244 C ALA A1090 12486 14638 10880 4516 1234 965 C
ATOM 2245 O ALA A1090 -85.543 34.712 307.333 1.00102.22 O
ANISOU 2245 O ALA A1090 12732 14995 11111 4337 1315 964 O
ATOM 2246 CB ALA A1090 -84.919 35.142 310.254 1.00 96.61 C
ANISOU 2246 CB ALA A1090 11709 14491 10509 4338 1194 942 C
ATOM 2247 N LYS A1091 -85.896 32.597 308.071 1.00 95.45 N
ANISOU 2247 N LYS A1091 12026 13991 10251 4789 1213 949 N
ATOM 2248 CA LYS A1091 -85.651 31.892 306.812 1.00 95.74 C
ANISOU 2248 CA LYS A1091 12145 14044 10186 4927 1280 929 C
ATOM 2249 C LYS A1091 -86.965 31.627 306.053 1.00100.22 C
ANISOU 2249 C LYS A1091 13010 14274 10795 4885 1249 982 C
ATOM 2250 O LYS A1091 -86.938 31.194 304.900 1.00101.18 O
ANISOU 2250 O LYS A1091 13237 14363 10844 4954 1303 978 O
ATOM 2251 CB LYS A1091 -84.926 30.561 307.087 1.00 98.91 C
ANISOU 2251 CB LYS A1091 12529 14571 10482 5282 1258 870 C
ATOM 2252 CG LYS A1091 -83.505 30.717 307.604 1.00 98.90 C
ANISOU 2252 CG LYS A1091 12202 14965 10409 5380 1287 781 C
ATOM 2253 CD LYS A1091 -82.875 29.382 307.866 1.00 98.98 C
ANISOU 2253 CD LYS A1091 12239 15068 10301 5785 1228 708 C
ATOM 2254 CE LYS A1091 -81.528 29.533 308.526 1.00104.00 C
ANISOU 2254 CE LYS A1091 12530 16118 10867 5912 1227 596 C
ATOM 2255 NZ LYS A1091 -81.088 28.268 309.172 1.00110.96 N
ANISOU 2255 NZ LYS A1091 13492 17031 11637 6344 1112 526 N
ATOM 2256 N SER A1092 -88.108 31.880 306.709 1.00 96.29 N
ANISOU 2256 N SER A1092 12632 13548 10405 4771 1163 1015 N
ATOM 2257 CA SER A1092 -89.457 31.644 306.193 1.00 94.81 C
ANISOU 2257 CA SER A1092 12690 13074 10259 4722 1117 1036 C
ATOM 2258 C SER A1092 -89.859 32.586 305.076 1.00 99.49 C
ANISOU 2258 C SER A1092 13339 13594 10870 4543 1139 1053 C
ATOM 2259 O SER A1092 -89.247 33.647 304.920 1.00 99.97 O
ANISOU 2259 O SER A1092 13275 13786 10924 4393 1181 1059 O
ATOM 2260 CB SER A1092 -90.472 31.755 307.330 1.00 95.58 C
ANISOU 2260 CB SER A1092 12842 13022 10453 4641 1024 1031 C
ATOM 2261 OG SER A1092 -90.627 33.101 307.747 1.00 98.54 O
ANISOU 2261 OG SER A1092 13094 13426 10919 4440 996 1035 O
ATOM 2262 N ARG A1093 -90.935 32.208 304.336 1.00 95.66 N
ANISOU 2262 N ARG A1093 13068 12888 10391 4546 1103 1055 N
ATOM 2263 CA ARG A1093 -91.569 32.995 303.270 1.00 95.07 C
ANISOU 2263 CA ARG A1093 13110 12686 10325 4411 1086 1062 C
ATOM 2264 C ARG A1093 -92.275 34.167 303.945 1.00 99.24 C
ANISOU 2264 C ARG A1093 13608 13146 10954 4245 994 1048 C
ATOM 2265 O ARG A1093 -92.254 35.279 303.422 1.00 99.27 O
ANISOU 2265 O ARG A1093 13649 13123 10946 4109 981 1057 O
ATOM 2266 CB ARG A1093 -92.595 32.140 302.503 1.00 94.70 C
ANISOU 2266 CB ARG A1093 13282 12440 10259 4484 1051 1048 C
ATOM 2267 CG ARG A1093 -92.365 32.088 300.996 1.00112.52 C
ANISOU 2267 CG ARG A1093 15657 14670 12426 4504 1114 1068 C
ATOM 2268 CD ARG A1093 -93.293 31.105 300.299 1.00130.23 C
ANISOU 2268 CD ARG A1093 18114 16728 14639 4583 1082 1054 C
ATOM 2269 NE ARG A1093 -94.651 31.637 300.141 1.00148.34 N
ANISOU 2269 NE ARG A1093 20504 18858 17001 4475 970 1014 N
ATOM 2270 CZ ARG A1093 -95.159 32.091 298.996 1.00168.39 C
ANISOU 2270 CZ ARG A1093 23180 21286 19514 4426 935 1009 C
ATOM 2271 NH1 ARG A1093 -94.434 32.072 297.884 1.00160.29 N
ANISOU 2271 NH1 ARG A1093 22225 20283 18395 4442 1020 1052 N
ATOM 2272 NH2 ARG A1093 -96.401 32.555 298.954 1.00155.20 N
ANISOU 2272 NH2 ARG A1093 21578 19493 17898 4369 810 946 N
ATOM 2273 N TRP A1094 -92.869 33.912 305.140 1.00 95.34 N
ANISOU 2273 N TRP A1094 13067 12621 10538 4257 928 1019 N
ATOM 2274 CA TRP A1094 -93.544 34.899 305.978 1.00 93.88 C
ANISOU 2274 CA TRP A1094 12830 12392 10447 4132 838 987 C
ATOM 2275 C TRP A1094 -92.606 36.064 306.261 1.00 96.96 C
ANISOU 2275 C TRP A1094 13095 12913 10834 4012 866 1021 C
ATOM 2276 O TRP A1094 -93.017 37.212 306.111 1.00 97.01 O
ANISOU 2276 O TRP A1094 13158 12841 10860 3890 800 1010 O
ATOM 2277 CB TRP A1094 -94.029 34.240 307.289 1.00 92.10 C
ANISOU 2277 CB TRP A1094 12557 12161 10277 4164 801 950 C
ATOM 2278 CG TRP A1094 -94.281 35.176 308.443 1.00 92.50 C
ANISOU 2278 CG TRP A1094 12490 12242 10415 4053 738 923 C
ATOM 2279 CD1 TRP A1094 -95.193 36.192 308.498 1.00 94.81 C
ANISOU 2279 CD1 TRP A1094 12801 12452 10769 3957 645 867 C
ATOM 2280 CD2 TRP A1094 -93.654 35.129 309.734 1.00 92.45 C
ANISOU 2280 CD2 TRP A1094 12344 12351 10433 4047 753 938 C
ATOM 2281 NE1 TRP A1094 -95.140 36.810 309.724 1.00 93.81 N
ANISOU 2281 NE1 TRP A1094 12553 12384 10705 3884 611 852 N
ATOM 2282 CE2 TRP A1094 -94.210 36.171 310.507 1.00 95.56 C
ANISOU 2282 CE2 TRP A1094 12675 12725 10910 3925 679 900 C
ATOM 2283 CE3 TRP A1094 -92.654 34.321 310.305 1.00 94.26 C
ANISOU 2283 CE3 TRP A1094 12504 12700 10612 4155 809 973 C
ATOM 2284 CZ2 TRP A1094 -93.809 36.418 311.827 1.00 94.52 C
ANISOU 2284 CZ2 TRP A1094 12412 12683 10818 3881 673 906 C
ATOM 2285 CZ3 TRP A1094 -92.260 34.570 311.610 1.00 95.50 C
ANISOU 2285 CZ3 TRP A1094 12533 12948 10806 4123 791 974 C
ATOM 2286 CH2 TRP A1094 -92.836 35.608 312.355 1.00 95.25 C
ANISOU 2286 CH2 TRP A1094 12438 12888 10863 3974 730 946 C
ATOM 2287 N TYR A1095 -91.349 35.771 306.651 1.00 93.72 N
ANISOU 2287 N TYR A1095 12527 12705 10377 4050 954 1049 N
ATOM 2288 CA TYR A1095 -90.349 36.801 306.930 1.00 94.14 C
ANISOU 2288 CA TYR A1095 12438 12929 10401 3907 1000 1068 C
ATOM 2289 C TYR A1095 -90.005 37.604 305.659 1.00100.80 C
ANISOU 2289 C TYR A1095 13385 13766 11150 3769 1051 1086 C
ATOM 2290 O TYR A1095 -89.836 38.817 305.740 1.00101.15 O
ANISOU 2290 O TYR A1095 13452 13811 11171 3577 1038 1096 O
ATOM 2291 CB TYR A1095 -89.082 36.213 307.593 1.00 94.86 C
ANISOU 2291 CB TYR A1095 12311 13281 10449 4002 1076 1064 C
ATOM 2292 CG TYR A1095 -88.040 37.261 307.933 1.00 96.32 C
ANISOU 2292 CG TYR A1095 12321 13683 10593 3824 1129 1065 C
ATOM 2293 CD1 TYR A1095 -87.978 37.828 309.202 1.00 98.16 C
ANISOU 2293 CD1 TYR A1095 12440 13964 10892 3744 1079 1065 C
ATOM 2294 CD2 TYR A1095 -87.111 37.685 306.985 1.00 97.89 C
ANISOU 2294 CD2 TYR A1095 12474 14047 10671 3709 1238 1059 C
ATOM 2295 CE1 TYR A1095 -87.037 38.810 309.512 1.00100.41 C
ANISOU 2295 CE1 TYR A1095 12578 14449 11125 3552 1129 1062 C
ATOM 2296 CE2 TYR A1095 -86.182 38.680 307.275 1.00 99.64 C
ANISOU 2296 CE2 TYR A1095 12551 14480 10829 3492 1297 1047 C
ATOM 2297 CZ TYR A1095 -86.140 39.232 308.542 1.00108.86 C
ANISOU 2297 CZ TYR A1095 13610 15687 12064 3416 1240 1050 C
ATOM 2298 OH TYR A1095 -85.198 40.188 308.827 1.00114.37 O
ANISOU 2298 OH TYR A1095 14169 16603 12683 3182 1303 1035 O
ATOM 2299 N ASN A1096 -89.914 36.932 304.506 1.00 98.50 N
ANISOU 2299 N ASN A1096 13188 13450 10787 3856 1109 1090 N
ATOM 2300 CA ASN A1096 -89.579 37.551 303.227 1.00100.40 C
ANISOU 2300 CA ASN A1096 13556 13676 10915 3724 1169 1104 C
ATOM 2301 C ASN A1096 -90.620 38.596 302.763 1.00106.10 C
ANISOU 2301 C ASN A1096 14528 14136 11648 3601 1053 1109 C
ATOM 2302 O ASN A1096 -90.247 39.702 302.351 1.00106.59 O
ANISOU 2302 O ASN A1096 14694 14187 11618 3399 1068 1124 O
ATOM 2303 CB ASN A1096 -89.375 36.462 302.167 1.00102.53 C
ANISOU 2303 CB ASN A1096 13881 13961 11115 3875 1246 1101 C
ATOM 2304 CG ASN A1096 -88.627 36.905 300.939 1.00122.65 C
ANISOU 2304 CG ASN A1096 16498 16585 13518 3737 1354 1105 C
ATOM 2305 OD1 ASN A1096 -87.658 37.673 301.007 1.00118.57 O
ANISOU 2305 OD1 ASN A1096 15877 16258 12916 3545 1438 1095 O
ATOM 2306 ND2 ASN A1096 -89.027 36.371 299.792 1.00112.18 N
ANISOU 2306 ND2 ASN A1096 15350 15127 12146 3816 1366 1112 N
ATOM 2307 N GLN A1097 -91.920 38.235 302.857 1.00102.42 N
ANISOU 2307 N GLN A1097 14168 13472 11276 3724 932 1082 N
ATOM 2308 CA GLN A1097 -93.074 39.049 302.465 1.00101.97 C
ANISOU 2308 CA GLN A1097 14329 13180 11235 3688 787 1052 C
ATOM 2309 C GLN A1097 -93.302 40.232 303.395 1.00104.79 C
ANISOU 2309 C GLN A1097 14678 13505 11633 3579 692 1034 C
ATOM 2310 O GLN A1097 -93.702 41.296 302.924 1.00105.60 O
ANISOU 2310 O GLN A1097 14997 13451 11675 3496 598 1024 O
ATOM 2311 CB GLN A1097 -94.347 38.182 302.381 1.00102.74 C
ANISOU 2311 CB GLN A1097 14478 13149 11410 3853 698 996 C
ATOM 2312 CG GLN A1097 -94.262 37.023 301.368 1.00127.36 C
ANISOU 2312 CG GLN A1097 17667 16254 14471 3958 776 1014 C
ATOM 2313 CD GLN A1097 -95.423 36.051 301.458 1.00154.57 C
ANISOU 2313 CD GLN A1097 21142 19612 17977 4085 712 955 C
ATOM 2314 OE1 GLN A1097 -95.867 35.646 302.545 1.00151.17 O
ANISOU 2314 OE1 GLN A1097 20593 19222 17622 4117 688 917 O
ATOM 2315 NE2 GLN A1097 -95.911 35.614 300.303 1.00148.88 N
ANISOU 2315 NE2 GLN A1097 20590 18775 17204 4139 695 943 N
ATOM 2316 N THR A1098 -93.090 40.040 304.712 1.00100.25 N
ANISOU 2316 N THR A1098 13886 13056 11147 3592 703 1028 N
ATOM 2317 CA THR A1098 -93.260 41.076 305.746 1.00 99.81 C
ANISOU 2317 CA THR A1098 13799 12988 11137 3495 621 1010 C
ATOM 2318 C THR A1098 -92.069 41.058 306.726 1.00103.80 C
ANISOU 2318 C THR A1098 14071 13723 11645 3411 727 1050 C
ATOM 2319 O THR A1098 -92.218 40.593 307.860 1.00102.46 O
ANISOU 2319 O THR A1098 13736 13623 11573 3481 712 1031 O
ATOM 2320 CB THR A1098 -94.625 40.957 306.456 1.00101.93 C
ANISOU 2320 CB THR A1098 14055 13148 11524 3606 482 924 C
ATOM 2321 OG1 THR A1098 -94.851 39.592 306.819 1.00100.60 O
ANISOU 2321 OG1 THR A1098 13751 13051 11421 3726 532 906 O
ATOM 2322 CG2 THR A1098 -95.773 41.480 305.614 1.00 97.43 C
ANISOU 2322 CG2 THR A1098 13712 12375 10931 3667 337 855 C
ATOM 2323 N PRO A1099 -90.888 41.578 306.312 1.00100.81 N
ANISOU 2323 N PRO A1099 13680 13478 11147 3246 832 1092 N
ATOM 2324 CA PRO A1099 -89.712 41.548 307.205 1.00100.85 C
ANISOU 2324 CA PRO A1099 13429 13747 11141 3171 930 1107 C
ATOM 2325 C PRO A1099 -89.791 42.377 308.483 1.00104.47 C
ANISOU 2325 C PRO A1099 13821 14214 11659 3072 862 1103 C
ATOM 2326 O PRO A1099 -89.269 41.938 309.505 1.00104.60 O
ANISOU 2326 O PRO A1099 13607 14407 11729 3115 897 1100 O
ATOM 2327 CB PRO A1099 -88.575 42.036 306.306 1.00104.32 C
ANISOU 2327 CB PRO A1099 13891 14334 11412 2977 1059 1125 C
ATOM 2328 CG PRO A1099 -89.249 42.844 305.249 1.00108.74 C
ANISOU 2328 CG PRO A1099 14792 14635 11891 2875 991 1136 C
ATOM 2329 CD PRO A1099 -90.542 42.149 304.993 1.00102.79 C
ANISOU 2329 CD PRO A1099 14143 13665 11247 3109 876 1115 C
ATOM 2330 N ASN A1100 -90.408 43.565 308.431 1.00101.41 N
ANISOU 2330 N ASN A1100 13651 13634 11248 2952 757 1098 N
ATOM 2331 CA ASN A1100 -90.490 44.481 309.574 1.00101.28 C
ANISOU 2331 CA ASN A1100 13610 13604 11267 2848 687 1092 C
ATOM 2332 C ASN A1100 -91.341 43.937 310.724 1.00103.46 C
ANISOU 2332 C ASN A1100 13750 13851 11708 3016 603 1049 C
ATOM 2333 O ASN A1100 -90.888 43.992 311.877 1.00103.45 O
ANISOU 2333 O ASN A1100 13571 13983 11754 2972 622 1056 O
ATOM 2334 CB ASN A1100 -90.941 45.869 309.135 1.00103.17 C
ANISOU 2334 CB ASN A1100 14172 13619 11408 2708 581 1088 C
ATOM 2335 CG ASN A1100 -89.946 46.541 308.218 1.00119.04 C
ANISOU 2335 CG ASN A1100 16342 15670 13219 2461 680 1131 C
ATOM 2336 OD1 ASN A1100 -88.928 47.088 308.658 1.00106.78 O
ANISOU 2336 OD1 ASN A1100 14710 14285 11575 2231 769 1154 O
ATOM 2337 ND2 ASN A1100 -90.199 46.470 306.918 1.00113.52 N
ANISOU 2337 ND2 ASN A1100 15859 14837 12435 2485 678 1134 N
ATOM 2338 N ARG A1101 -92.541 43.370 310.407 1.00 97.51 N
ANISOU 2338 N ARG A1101 13077 12945 11029 3190 520 997 N
ATOM 2339 CA ARG A1101 -93.441 42.750 311.390 1.00 94.93 C
ANISOU 2339 CA ARG A1101 12636 12601 10832 3318 456 934 C
ATOM 2340 C ARG A1101 -92.760 41.520 311.969 1.00 97.46 C
ANISOU 2340 C ARG A1101 12752 13095 11185 3389 561 964 C
ATOM 2341 O ARG A1101 -92.645 41.419 313.192 1.00 96.48 O
ANISOU 2341 O ARG A1101 12492 13046 11121 3381 555 955 O
ATOM 2342 CB ARG A1101 -94.786 42.353 310.756 1.00 93.31 C
ANISOU 2342 CB ARG A1101 12554 12238 10663 3455 362 852 C
ATOM 2343 CG ARG A1101 -95.832 41.849 311.763 1.00 98.53 C
ANISOU 2343 CG ARG A1101 13108 12897 11431 3532 298 756 C
ATOM 2344 CD ARG A1101 -97.221 41.772 311.148 1.00101.57 C
ANISOU 2344 CD ARG A1101 13598 13163 11832 3637 190 640 C
ATOM 2345 NE ARG A1101 -98.217 41.209 312.065 1.00102.15 N
ANISOU 2345 NE ARG A1101 13549 13278 11984 3673 155 524 N
ATOM 2346 CZ ARG A1101 -99.515 41.107 311.795 1.00113.31 C
ANISOU 2346 CZ ARG A1101 14986 14653 13415 3746 60 379 C
ATOM 2347 NH1 ARG A1101 -99.995 41.534 310.632 1.00104.15 N
ANISOU 2347 NH1 ARG A1101 13978 13390 12206 3827 -30 337 N
ATOM 2348 NH2 ARG A1101 -100.343 40.578 312.685 1.00 96.48 N
ANISOU 2348 NH2 ARG A1101 12726 12598 11333 3731 54 261 N
ATOM 2349 N ALA A1102 -92.283 40.602 311.076 1.00 93.38 N
ANISOU 2349 N ALA A1102 12236 12631 10612 3471 648 994 N
ATOM 2350 CA ALA A1102 -91.603 39.356 311.432 1.00 91.88 C
ANISOU 2350 CA ALA A1102 11907 12586 10418 3590 731 1013 C
ATOM 2351 C ALA A1102 -90.399 39.597 312.313 1.00 96.66 C
ANISOU 2351 C ALA A1102 12319 13406 11003 3530 785 1042 C
ATOM 2352 O ALA A1102 -90.285 38.901 313.316 1.00 96.98 O
ANISOU 2352 O ALA A1102 12258 13508 11082 3619 778 1033 O
ATOM 2353 CB ALA A1102 -91.231 38.567 310.199 1.00 92.70 C
ANISOU 2353 CB ALA A1102 12069 12710 10443 3686 806 1033 C
ATOM 2354 N LYS A1103 -89.570 40.633 312.034 1.00 93.55 N
ANISOU 2354 N LYS A1103 11890 13116 10537 3358 829 1068 N
ATOM 2355 CA LYS A1103 -88.433 40.958 312.906 1.00 94.36 C
ANISOU 2355 CA LYS A1103 11787 13455 10610 3269 879 1077 C
ATOM 2356 C LYS A1103 -88.880 41.335 314.347 1.00 99.41 C
ANISOU 2356 C LYS A1103 12377 14049 11346 3234 795 1068 C
ATOM 2357 O LYS A1103 -88.237 40.900 315.303 1.00 99.51 O
ANISOU 2357 O LYS A1103 12213 14225 11370 3283 811 1065 O
ATOM 2358 CB LYS A1103 -87.516 42.026 312.290 1.00 97.90 C
ANISOU 2358 CB LYS A1103 12234 14029 10935 3034 953 1093 C
ATOM 2359 N ARG A1104 -90.008 42.084 314.492 1.00 96.30 N
ANISOU 2359 N ARG A1104 12139 13436 11013 3174 697 1050 N
ATOM 2360 CA ARG A1104 -90.606 42.496 315.776 1.00 95.61 C
ANISOU 2360 CA ARG A1104 12023 13289 11015 3141 615 1024 C
ATOM 2361 C ARG A1104 -91.133 41.285 316.566 1.00 98.59 C
ANISOU 2361 C ARG A1104 12340 13651 11470 3298 597 991 C
ATOM 2362 O ARG A1104 -90.917 41.211 317.782 1.00 98.94 O
ANISOU 2362 O ARG A1104 12278 13763 11551 3284 583 988 O
ATOM 2363 CB ARG A1104 -91.770 43.492 315.555 1.00 96.32 C
ANISOU 2363 CB ARG A1104 12303 13161 11132 3086 504 981 C
ATOM 2364 CG ARG A1104 -91.348 44.940 315.362 1.00107.19 C
ANISOU 2364 CG ARG A1104 13792 14511 12423 2893 485 1009 C
ATOM 2365 CD ARG A1104 -92.510 45.930 315.506 1.00108.20 C
ANISOU 2365 CD ARG A1104 14113 14423 12576 2890 339 948 C
ATOM 2366 NE ARG A1104 -93.447 45.881 314.380 1.00100.65 N
ANISOU 2366 NE ARG A1104 13344 13294 11603 3004 267 900 N
ATOM 2367 CZ ARG A1104 -93.261 46.501 313.219 1.00111.20 C
ANISOU 2367 CZ ARG A1104 14905 14525 12820 2942 253 926 C
ATOM 2368 NH1 ARG A1104 -92.171 47.233 313.015 1.00 94.66 N
ANISOU 2368 NH1 ARG A1104 12881 12485 10599 2734 321 997 N
ATOM 2369 NH2 ARG A1104 -94.154 46.378 312.244 1.00 99.66 N
ANISOU 2369 NH2 ARG A1104 13608 12909 11348 3071 174 873 N
ATOM 2370 N VAL A1105 -91.860 40.362 315.875 1.00 93.06 N
ANISOU 2370 N VAL A1105 11737 12847 10774 3427 595 964 N
ATOM 2371 CA VAL A1105 -92.443 39.137 316.446 1.00 91.32 C
ANISOU 2371 CA VAL A1105 11531 12583 10585 3542 587 927 C
ATOM 2372 C VAL A1105 -91.319 38.189 316.872 1.00 95.16 C
ANISOU 2372 C VAL A1105 11923 13219 11014 3650 645 969 C
ATOM 2373 O VAL A1105 -91.353 37.664 317.989 1.00 95.06 O
ANISOU 2373 O VAL A1105 11889 13215 11016 3682 623 956 O
ATOM 2374 CB VAL A1105 -93.451 38.458 315.479 1.00 94.24 C
ANISOU 2374 CB VAL A1105 12047 12814 10945 3620 575 883 C
ATOM 2375 CG1 VAL A1105 -93.999 37.152 316.055 1.00 93.29 C
ANISOU 2375 CG1 VAL A1105 11982 12646 10818 3692 580 844 C
ATOM 2376 CG2 VAL A1105 -94.591 39.403 315.121 1.00 93.65 C
ANISOU 2376 CG2 VAL A1105 12051 12615 10917 3554 491 814 C
ATOM 2377 N ILE A1106 -90.314 38.004 315.990 1.00 91.46 N
ANISOU 2377 N ILE A1106 11406 12877 10469 3711 712 1007 N
ATOM 2378 CA ILE A1106 -89.145 37.159 316.229 1.00 92.23 C
ANISOU 2378 CA ILE A1106 11394 13158 10492 3860 756 1020 C
ATOM 2379 C ILE A1106 -88.382 37.639 317.463 1.00 96.90 C
ANISOU 2379 C ILE A1106 11813 13910 11095 3802 738 1023 C
ATOM 2380 O ILE A1106 -88.045 36.813 318.311 1.00 97.64 O
ANISOU 2380 O ILE A1106 11883 14054 11163 3940 710 1012 O
ATOM 2381 CB ILE A1106 -88.269 37.029 314.944 1.00 96.40 C
ANISOU 2381 CB ILE A1106 11876 13823 10928 3917 838 1030 C
ATOM 2382 CG1 ILE A1106 -88.908 36.026 313.944 1.00 95.86 C
ANISOU 2382 CG1 ILE A1106 11993 13601 10830 4057 849 1026 C
ATOM 2383 CG2 ILE A1106 -86.815 36.657 315.261 1.00 98.85 C
ANISOU 2383 CG2 ILE A1106 11980 14425 11153 4032 880 1013 C
ATOM 2384 CD1 ILE A1106 -88.448 36.146 312.464 1.00 99.31 C
ANISOU 2384 CD1 ILE A1106 12442 14097 11193 4056 926 1035 C
ATOM 2385 N THR A1107 -88.176 38.971 317.598 1.00 93.17 N
ANISOU 2385 N THR A1107 11258 13495 10648 3595 742 1035 N
ATOM 2386 CA THR A1107 -87.477 39.597 318.734 1.00 93.29 C
ANISOU 2386 CA THR A1107 11112 13663 10671 3497 727 1039 C
ATOM 2387 C THR A1107 -88.228 39.344 320.034 1.00 96.37 C
ANISOU 2387 C THR A1107 11556 13921 11138 3515 650 1026 C
ATOM 2388 O THR A1107 -87.604 39.104 321.074 1.00 96.17 O
ANISOU 2388 O THR A1107 11424 14015 11101 3557 628 1023 O
ATOM 2389 CB THR A1107 -87.200 41.071 318.437 1.00101.22 C
ANISOU 2389 CB THR A1107 12086 14717 11657 3247 752 1056 C
ATOM 2390 OG1 THR A1107 -86.338 41.127 317.296 1.00105.74 O
ANISOU 2390 OG1 THR A1107 12604 15446 12125 3218 842 1056 O
ATOM 2391 CG2 THR A1107 -86.548 41.804 319.592 1.00 97.94 C
ANISOU 2391 CG2 THR A1107 11520 14452 11241 3113 738 1058 C
ATOM 2392 N THR A1108 -89.564 39.327 319.958 1.00 92.12 N
ANISOU 2392 N THR A1108 11182 13155 10666 3489 609 1004 N
ATOM 2393 CA THR A1108 -90.420 39.036 321.109 1.00 90.91 C
ANISOU 2393 CA THR A1108 11091 12881 10570 3476 553 968 C
ATOM 2394 C THR A1108 -90.201 37.566 321.548 1.00 93.63 C
ANISOU 2394 C THR A1108 11501 13223 10853 3651 551 964 C
ATOM 2395 O THR A1108 -90.053 37.321 322.740 1.00 93.65 O
ANISOU 2395 O THR A1108 11493 13238 10851 3654 516 959 O
ATOM 2396 CB THR A1108 -91.867 39.455 320.810 1.00 97.95 C
ANISOU 2396 CB THR A1108 12102 13587 11526 3396 515 911 C
ATOM 2397 OG1 THR A1108 -91.857 40.837 320.420 1.00 95.67 O
ANISOU 2397 OG1 THR A1108 11795 13295 11260 3274 495 919 O
ATOM 2398 CG2 THR A1108 -92.802 39.254 322.004 1.00 94.33 C
ANISOU 2398 CG2 THR A1108 11680 13045 11117 3339 471 847 C
ATOM 2399 N PHE A1109 -90.091 36.619 320.588 1.00 89.30 N
ANISOU 2399 N PHE A1109 11042 12652 10237 3802 582 969 N
ATOM 2400 CA PHE A1109 -89.809 35.209 320.879 1.00 88.86 C
ANISOU 2400 CA PHE A1109 11108 12569 10084 3996 568 965 C
ATOM 2401 C PHE A1109 -88.375 35.039 321.399 1.00 95.55 C
ANISOU 2401 C PHE A1109 11806 13633 10864 4140 553 980 C
ATOM 2402 O PHE A1109 -88.141 34.243 322.306 1.00 95.70 O
ANISOU 2402 O PHE A1109 11916 13628 10816 4265 498 969 O
ATOM 2403 CB PHE A1109 -90.003 34.331 319.632 1.00 90.08 C
ANISOU 2403 CB PHE A1109 11405 12648 10174 4126 603 965 C
ATOM 2404 CG PHE A1109 -91.414 33.952 319.237 1.00 89.86 C
ANISOU 2404 CG PHE A1109 11573 12406 10164 4044 604 928 C
ATOM 2405 CD1 PHE A1109 -92.280 33.363 320.155 1.00 91.06 C
ANISOU 2405 CD1 PHE A1109 11882 12419 10296 3971 574 885 C
ATOM 2406 CD2 PHE A1109 -91.840 34.077 317.915 1.00 91.18 C
ANISOU 2406 CD2 PHE A1109 11778 12525 10342 4037 638 926 C
ATOM 2407 CE1 PHE A1109 -93.570 32.974 319.774 1.00 91.28 C
ANISOU 2407 CE1 PHE A1109 12066 12296 10319 3872 585 825 C
ATOM 2408 CE2 PHE A1109 -93.128 33.678 317.533 1.00 92.70 C
ANISOU 2408 CE2 PHE A1109 12132 12552 10538 3968 633 874 C
ATOM 2409 CZ PHE A1109 -93.986 33.134 318.465 1.00 90.45 C
ANISOU 2409 CZ PHE A1109 11969 12164 10235 3880 610 817 C
ATOM 2410 N ARG A1110 -87.419 35.787 320.831 1.00 93.95 N
ANISOU 2410 N ARG A1110 11386 13651 10661 4116 597 990 N
ATOM 2411 CA ARG A1110 -86.018 35.709 321.234 1.00 96.07 C
ANISOU 2411 CA ARG A1110 11454 14193 10855 4241 589 972 C
ATOM 2412 C ARG A1110 -85.770 36.257 322.640 1.00103.65 C
ANISOU 2412 C ARG A1110 12312 15219 11851 4147 534 972 C
ATOM 2413 O ARG A1110 -85.185 35.555 323.458 1.00104.50 O
ANISOU 2413 O ARG A1110 12418 15397 11890 4325 469 948 O
ATOM 2414 CB ARG A1110 -85.110 36.393 320.195 1.00 96.04 C
ANISOU 2414 CB ARG A1110 11239 14436 10816 4185 673 961 C
ATOM 2415 CG ARG A1110 -83.609 36.242 320.470 1.00105.22 C
ANISOU 2415 CG ARG A1110 12143 15955 11881 4323 675 904 C
ATOM 2416 CD ARG A1110 -82.715 36.765 319.359 1.00115.92 C
ANISOU 2416 CD ARG A1110 13294 17582 13168 4250 780 868 C
ATOM 2417 NE ARG A1110 -83.137 38.073 318.844 1.00133.90 N
ANISOU 2417 NE ARG A1110 15582 19794 15500 3913 846 913 N
ATOM 2418 CZ ARG A1110 -82.823 39.246 319.389 1.00152.42 C
ANISOU 2418 CZ ARG A1110 17798 22256 17857 3659 861 918 C
ATOM 2419 NH1 ARG A1110 -82.077 39.300 320.489 1.00136.69 N
ANISOU 2419 NH1 ARG A1110 15616 20477 15842 3691 821 881 N
ATOM 2420 NH2 ARG A1110 -83.261 40.375 318.845 1.00141.96 N
ANISOU 2420 NH2 ARG A1110 16562 20822 16553 3378 905 958 N
ATOM 2421 N THR A1111 -86.216 37.493 322.921 1.00102.49 N
ANISOU 2421 N THR A1111 12106 15037 11798 3884 549 994 N
ATOM 2422 CA THR A1111 -85.974 38.178 324.197 1.00103.46 C
ANISOU 2422 CA THR A1111 12126 15227 11958 3763 506 997 C
ATOM 2423 C THR A1111 -87.015 37.896 325.302 1.00108.92 C
ANISOU 2423 C THR A1111 12996 15686 12704 3721 444 996 C
ATOM 2424 O THR A1111 -86.663 37.934 326.485 1.00109.14 O
ANISOU 2424 O THR A1111 12980 15764 12724 3717 392 992 O
ATOM 2425 CB THR A1111 -85.817 39.698 323.970 1.00112.72 C
ANISOU 2425 CB THR A1111 13168 16486 13173 3497 550 1015 C
ATOM 2426 OG1 THR A1111 -87.039 40.239 323.469 1.00112.63 O
ANISOU 2426 OG1 THR A1111 13318 16238 13238 3364 555 1028 O
ATOM 2427 CG2 THR A1111 -84.667 40.043 323.019 1.00112.15 C
ANISOU 2427 CG2 THR A1111 12912 16685 13015 3474 627 1001 C
ATOM 2428 N GLY A1112 -88.271 37.663 324.920 1.00106.00 N
ANISOU 2428 N GLY A1112 12811 15087 12379 3671 454 986 N
ATOM 2429 CA GLY A1112 -89.367 37.440 325.862 1.00105.39 C
ANISOU 2429 CA GLY A1112 12888 14817 12339 3585 417 958 C
ATOM 2430 C GLY A1112 -89.805 38.727 326.537 1.00109.34 C
ANISOU 2430 C GLY A1112 13301 15309 12935 3369 404 948 C
ATOM 2431 O GLY A1112 -90.390 38.699 327.625 1.00108.12 O
ANISOU 2431 O GLY A1112 13210 15068 12804 3287 372 918 O
ATOM 2432 N THR A1113 -89.513 39.869 325.877 1.00106.22 N
ANISOU 2432 N THR A1113 12786 14997 12577 3269 428 969 N
ATOM 2433 CA THR A1113 -89.790 41.236 326.330 1.00105.47 C
ANISOU 2433 CA THR A1113 12636 14890 12546 3077 407 965 C
ATOM 2434 C THR A1113 -90.608 42.014 325.281 1.00109.12 C
ANISOU 2434 C THR A1113 13175 15240 13045 3005 410 942 C
ATOM 2435 O THR A1113 -90.830 41.516 324.173 1.00109.99 O
ANISOU 2435 O THR A1113 13351 15308 13134 3092 437 939 O
ATOM 2436 CB THR A1113 -88.457 41.977 326.620 1.00112.97 C
ANISOU 2436 CB THR A1113 13412 16053 13457 3006 419 1010 C
ATOM 2437 OG1 THR A1113 -87.743 42.204 325.397 1.00115.21 O
ANISOU 2437 OG1 THR A1113 13632 16461 13682 3015 475 1033 O
ATOM 2438 CG2 THR A1113 -87.573 41.259 327.639 1.00107.87 C
ANISOU 2438 CG2 THR A1113 12678 15542 12767 3105 392 1016 C
ATOM 2439 N TRP A1114 -91.024 43.247 325.626 1.00104.36 N
ANISOU 2439 N TRP A1114 12583 14585 12485 2861 370 923 N
ATOM 2440 CA TRP A1114 -91.784 44.135 324.743 1.00103.42 C
ANISOU 2440 CA TRP A1114 12570 14344 12379 2814 338 890 C
ATOM 2441 C TRP A1114 -90.873 45.170 324.053 1.00110.83 C
ANISOU 2441 C TRP A1114 13514 15349 13248 2701 358 952 C
ATOM 2442 O TRP A1114 -91.376 46.140 323.484 1.00110.87 O
ANISOU 2442 O TRP A1114 13656 15234 13237 2640 310 932 O
ATOM 2443 CB TRP A1114 -92.895 44.840 325.535 1.00100.59 C
ANISOU 2443 CB TRP A1114 12263 13872 12084 2754 263 805 C
ATOM 2444 CG TRP A1114 -93.928 43.917 326.106 1.00100.09 C
ANISOU 2444 CG TRP A1114 12207 13756 12066 2811 257 714 C
ATOM 2445 CD1 TRP A1114 -94.087 43.573 327.417 1.00102.56 C
ANISOU 2445 CD1 TRP A1114 12478 14089 12401 2764 257 684 C
ATOM 2446 CD2 TRP A1114 -94.949 43.223 325.381 1.00 99.31 C
ANISOU 2446 CD2 TRP A1114 12176 13583 11974 2893 256 633 C
ATOM 2447 NE1 TRP A1114 -95.157 42.722 327.557 1.00101.35 N
ANISOU 2447 NE1 TRP A1114 12372 13880 12256 2788 265 583 N
ATOM 2448 CE2 TRP A1114 -95.701 42.484 326.320 1.00102.63 C
ANISOU 2448 CE2 TRP A1114 12590 13994 12410 2865 266 547 C
ATOM 2449 CE3 TRP A1114 -95.305 43.154 324.021 1.00100.61 C
ANISOU 2449 CE3 TRP A1114 12414 13693 12121 2971 250 618 C
ATOM 2450 CZ2 TRP A1114 -96.793 41.693 325.946 1.00101.75 C
ANISOU 2450 CZ2 TRP A1114 12532 13839 12290 2891 277 440 C
ATOM 2451 CZ3 TRP A1114 -96.384 42.367 323.651 1.00101.76 C
ANISOU 2451 CZ3 TRP A1114 12602 13790 12272 3026 250 517 C
ATOM 2452 CH2 TRP A1114 -97.124 41.661 324.608 1.00102.17 C
ANISOU 2452 CH2 TRP A1114 12635 13853 12333 2976 266 424 C
ATOM 2453 N ASP A1115 -89.541 44.935 324.069 1.00110.25 N
ANISOU 2453 N ASP A1115 13306 15474 13111 2674 424 1013 N
ATOM 2454 CA ASP A1115 -88.497 45.804 323.511 1.00112.29 C
ANISOU 2454 CA ASP A1115 13535 15859 13270 2516 472 1058 C
ATOM 2455 C ASP A1115 -88.730 46.267 322.083 1.00116.84 C
ANISOU 2455 C ASP A1115 14274 16335 13784 2477 487 1064 C
ATOM 2456 O ASP A1115 -88.395 47.409 321.769 1.00118.38 O
ANISOU 2456 O ASP A1115 14572 16513 13893 2287 487 1084 O
ATOM 2457 CB ASP A1115 -87.123 45.137 323.621 1.00116.31 C
ANISOU 2457 CB ASP A1115 13827 16650 13715 2551 547 1079 C
ATOM 2458 CG ASP A1115 -86.409 45.427 324.928 1.00132.42 C
ANISOU 2458 CG ASP A1115 15714 18846 15752 2469 532 1085 C
ATOM 2459 OD1 ASP A1115 -86.553 44.623 325.874 1.00131.87 O
ANISOU 2459 OD1 ASP A1115 15586 18781 15736 2609 495 1071 O
ATOM 2460 OD2 ASP A1115 -85.695 46.451 324.999 1.00142.65 O
ANISOU 2460 OD2 ASP A1115 16970 20256 16973 2251 557 1101 O
ATOM 2461 N ALA A1116 -89.294 45.396 321.222 1.00112.11 N
ANISOU 2461 N ALA A1116 13728 15657 13210 2643 495 1045 N
ATOM 2462 CA ALA A1116 -89.582 45.700 319.812 1.00111.85 C
ANISOU 2462 CA ALA A1116 13865 15514 13119 2634 502 1047 C
ATOM 2463 C ALA A1116 -90.742 46.700 319.630 1.00114.32 C
ANISOU 2463 C ALA A1116 14408 15582 13448 2603 390 1005 C
ATOM 2464 O ALA A1116 -90.857 47.330 318.571 1.00113.97 O
ANISOU 2464 O ALA A1116 14556 15428 13321 2551 371 1011 O
ATOM 2465 CB ALA A1116 -89.878 44.413 319.057 1.00112.18 C
ANISOU 2465 CB ALA A1116 13895 15544 13185 2831 535 1034 C
ATOM 2466 N TYR A1117 -91.593 46.842 320.665 1.00109.90 N
ANISOU 2466 N TYR A1117 13837 14940 12979 2645 308 949 N
ATOM 2467 CA TYR A1117 -92.760 47.726 320.648 1.00109.57 C
ANISOU 2467 CA TYR A1117 13978 14699 12954 2669 182 873 C
ATOM 2468 C TYR A1117 -92.599 48.907 321.637 1.00114.82 C
ANISOU 2468 C TYR A1117 14689 15340 13599 2529 126 875 C
ATOM 2469 O TYR A1117 -93.546 49.309 322.322 1.00114.21 O
ANISOU 2469 O TYR A1117 14650 15167 13579 2586 29 789 O
ATOM 2470 CB TYR A1117 -94.055 46.908 320.864 1.00108.79 C
ANISOU 2470 CB TYR A1117 13834 14540 12960 2843 133 766 C
ATOM 2471 CG TYR A1117 -94.227 45.771 319.876 1.00108.29 C
ANISOU 2471 CG TYR A1117 13761 14484 12899 2961 185 766 C
ATOM 2472 CD1 TYR A1117 -93.619 44.536 320.089 1.00109.17 C
ANISOU 2472 CD1 TYR A1117 13732 14721 13026 3003 284 814 C
ATOM 2473 CD2 TYR A1117 -95.004 45.928 318.731 1.00108.73 C
ANISOU 2473 CD2 TYR A1117 13974 14412 12928 3047 123 714 C
ATOM 2474 CE1 TYR A1117 -93.752 43.496 319.173 1.00108.82 C
ANISOU 2474 CE1 TYR A1117 13710 14670 12967 3113 330 816 C
ATOM 2475 CE2 TYR A1117 -95.165 44.886 317.819 1.00109.23 C
ANISOU 2475 CE2 TYR A1117 14037 14478 12987 3146 172 716 C
ATOM 2476 CZ TYR A1117 -94.534 43.671 318.043 1.00115.86 C
ANISOU 2476 CZ TYR A1117 14743 15438 13839 3173 281 770 C
ATOM 2477 OH TYR A1117 -94.686 42.630 317.158 1.00116.10 O
ANISOU 2477 OH TYR A1117 14802 15457 13852 3274 326 771 O
ATOM 2478 N HIS A 237 -91.371 49.455 321.682 1.00112.71 N
ANISOU 2478 N HIS A 237 14410 15180 13236 2336 194 961 N
ATOM 2479 CA HIS A 237 -90.928 50.588 322.498 1.00113.46 C
ANISOU 2479 CA HIS A 237 14565 15274 13272 2149 165 985 C
ATOM 2480 C HIS A 237 -89.725 51.217 321.799 1.00122.49 C
ANISOU 2480 C HIS A 237 15789 16503 14248 1914 246 1062 C
ATOM 2481 O HIS A 237 -89.043 50.518 321.043 1.00122.68 O
ANISOU 2481 O HIS A 237 15705 16672 14237 1913 349 1093 O
ATOM 2482 CB HIS A 237 -90.518 50.120 323.901 1.00112.84 C
ANISOU 2482 CB HIS A 237 14237 15358 13279 2133 202 994 C
ATOM 2483 CG HIS A 237 -91.649 49.989 324.876 1.00114.52 C
ANISOU 2483 CG HIS A 237 14429 15474 13611 2257 117 910 C
ATOM 2484 ND1 HIS A 237 -92.438 51.072 325.220 1.00116.16 N
ANISOU 2484 ND1 HIS A 237 14811 15517 13808 2243 3 848 N
ATOM 2485 CD2 HIS A 237 -92.037 48.918 325.607 1.00114.75 C
ANISOU 2485 CD2 HIS A 237 14291 15562 13747 2378 137 870 C
ATOM 2486 CE1 HIS A 237 -93.307 50.615 326.106 1.00114.40 C
ANISOU 2486 CE1 HIS A 237 14485 15287 13696 2355 -33 760 C
ATOM 2487 NE2 HIS A 237 -93.103 49.326 326.372 1.00113.94 N
ANISOU 2487 NE2 HIS A 237 14234 15353 13705 2418 50 775 N
ATOM 2488 N GLU A 238 -89.456 52.522 322.040 1.00122.77 N
ANISOU 2488 N GLU A 238 16025 16458 14163 1701 206 1081 N
ATOM 2489 CA GLU A 238 -88.317 53.220 321.418 1.00125.72 C
ANISOU 2489 CA GLU A 238 16510 16919 14340 1408 293 1140 C
ATOM 2490 C GLU A 238 -86.966 52.657 321.883 1.00132.25 C
ANISOU 2490 C GLU A 238 16990 18106 15154 1274 439 1172 C
ATOM 2491 O GLU A 238 -86.839 52.220 323.032 1.00131.51 O
ANISOU 2491 O GLU A 238 16657 18140 15170 1339 437 1165 O
ATOM 2492 CB GLU A 238 -88.396 54.753 321.578 1.00128.60 C
ANISOU 2492 CB GLU A 238 17235 17082 14547 1194 206 1149 C
ATOM 2493 CG GLU A 238 -88.216 55.281 322.993 1.00139.42 C
ANISOU 2493 CG GLU A 238 18531 18493 15950 1102 172 1151 C
ATOM 2494 CD GLU A 238 -88.225 56.792 323.135 1.00170.37 C
ANISOU 2494 CD GLU A 238 22845 22199 19689 887 84 1161 C
ATOM 2495 OE1 GLU A 238 -87.608 57.481 322.289 1.00168.16 O
ANISOU 2495 OE1 GLU A 238 22844 21861 19190 639 120 1197 O
ATOM 2496 OE2 GLU A 238 -88.806 57.285 324.129 1.00172.44 O
ANISOU 2496 OE2 GLU A 238 23153 22357 20011 948 -17 1131 O
ATOM 2497 N GLN A 239 -85.977 52.640 320.974 1.00131.27 N
ANISOU 2497 N GLN A 239 16838 18155 14885 1099 561 1191 N
ATOM 2498 CA GLN A 239 -84.652 52.082 321.244 1.00132.62 C
ANISOU 2498 CA GLN A 239 16655 18717 15016 996 697 1187 C
ATOM 2499 C GLN A 239 -83.849 52.890 322.266 1.00137.89 C
ANISOU 2499 C GLN A 239 17245 19547 15600 724 719 1192 C
ATOM 2500 O GLN A 239 -83.454 52.337 323.294 1.00137.09 O
ANISOU 2500 O GLN A 239 16840 19657 15591 809 728 1177 O
ATOM 2501 CB GLN A 239 -83.860 51.864 319.937 1.00135.90 C
ANISOU 2501 CB GLN A 239 17054 19300 15282 872 827 1177 C
ATOM 2502 CG GLN A 239 -84.390 50.716 319.064 1.00154.31 C
ANISOU 2502 CG GLN A 239 19347 21571 17714 1173 831 1167 C
ATOM 2503 CD GLN A 239 -84.415 49.375 319.776 1.00175.68 C
ANISOU 2503 CD GLN A 239 21735 24416 20598 1487 821 1145 C
ATOM 2504 OE1 GLN A 239 -83.382 48.852 320.216 1.00172.11 O
ANISOU 2504 OE1 GLN A 239 20973 24291 20131 1493 893 1117 O
ATOM 2505 NE2 GLN A 239 -85.605 48.795 319.912 1.00165.61 N
ANISOU 2505 NE2 GLN A 239 20549 22901 19476 1752 725 1145 N
ATOM 2506 N VAL A 240 -83.640 54.193 322.000 1.00136.37 N
ANISOU 2506 N VAL A 240 17359 19239 15217 398 718 1212 N
ATOM 2507 CA VAL A 240 -82.878 55.095 322.877 1.00137.57 C
ANISOU 2507 CA VAL A 240 17497 19523 15251 82 742 1218 C
ATOM 2508 C VAL A 240 -83.841 56.065 323.605 1.00138.96 C
ANISOU 2508 C VAL A 240 18005 19342 15453 89 588 1244 C
ATOM 2509 O VAL A 240 -84.417 56.951 322.961 1.00139.25 O
ANISOU 2509 O VAL A 240 18473 19067 15370 13 514 1258 O
ATOM 2510 CB VAL A 240 -81.734 55.845 322.115 1.00144.76 C
ANISOU 2510 CB VAL A 240 18499 20628 15875 -362 881 1207 C
ATOM 2511 CG1 VAL A 240 -80.742 56.483 323.089 1.00146.08 C
ANISOU 2511 CG1 VAL A 240 18541 21039 15924 -692 931 1194 C
ATOM 2512 CG2 VAL A 240 -81.003 54.923 321.134 1.00145.48 C
ANISOU 2512 CG2 VAL A 240 18304 21041 15931 -331 1025 1160 C
ATOM 2513 N SER A 241 -84.020 55.888 324.939 1.00132.37 N
ANISOU 2513 N SER A 241 16982 18549 14763 200 531 1240 N
ATOM 2514 CA SER A 241 -84.906 56.756 325.727 1.00130.62 C
ANISOU 2514 CA SER A 241 17027 18029 14573 228 389 1246 C
ATOM 2515 C SER A 241 -84.270 57.313 327.004 1.00132.97 C
ANISOU 2515 C SER A 241 17228 18463 14832 13 396 1258 C
ATOM 2516 O SER A 241 -83.971 56.567 327.951 1.00130.93 O
ANISOU 2516 O SER A 241 16614 18424 14708 119 420 1247 O
ATOM 2517 CB SER A 241 -86.234 56.073 326.041 1.00130.99 C
ANISOU 2517 CB SER A 241 17029 17891 14851 624 279 1210 C
ATOM 2518 OG SER A 241 -86.043 54.941 326.869 1.00137.59 O
ANISOU 2518 OG SER A 241 17468 18956 15855 793 323 1198 O
ATOM 2519 N ALA A 242 -84.111 58.657 327.024 1.00129.68 N
ANISOU 2519 N ALA A 242 17175 17885 14212 -288 363 1280 N
ATOM 2520 CA ALA A 242 -83.586 59.440 328.142 1.00129.48 C
ANISOU 2520 CA ALA A 242 17160 17928 14107 -540 358 1295 C
ATOM 2521 C ALA A 242 -84.576 59.376 329.320 1.00129.58 C
ANISOU 2521 C ALA A 242 17154 17764 14316 -275 226 1280 C
ATOM 2522 O ALA A 242 -84.191 59.626 330.467 1.00129.20 O
ANISOU 2522 O ALA A 242 16979 17829 14283 -387 225 1288 O
ATOM 2523 CB ALA A 242 -83.372 60.882 327.707 1.00132.48 C
ANISOU 2523 CB ALA A 242 18034 18105 14196 -909 340 1321 C
ATOM 2524 N LYS A 243 -85.845 59.009 329.018 1.00122.53 N
ANISOU 2524 N LYS A 243 16371 16618 13566 68 120 1245 N
ATOM 2525 CA LYS A 243 -86.943 58.827 329.960 1.00119.44 C
ANISOU 2525 CA LYS A 243 15951 16073 13359 342 4 1198 C
ATOM 2526 C LYS A 243 -86.671 57.627 330.882 1.00120.30 C
ANISOU 2526 C LYS A 243 15607 16441 13662 480 64 1192 C
ATOM 2527 O LYS A 243 -86.775 57.770 332.100 1.00119.49 O
ANISOU 2527 O LYS A 243 15429 16346 13626 480 25 1182 O
ATOM 2528 CB LYS A 243 -88.272 58.652 329.205 1.00120.26 C
ANISOU 2528 CB LYS A 243 16243 15913 13537 651 -104 1134 C
ATOM 2529 N ARG A 244 -86.300 56.460 330.306 1.00114.81 N
ANISOU 2529 N ARG A 244 14642 15945 13037 598 153 1195 N
ATOM 2530 CA ARG A 244 -86.002 55.241 331.069 1.00112.63 C
ANISOU 2530 CA ARG A 244 13992 15892 12910 755 196 1186 C
ATOM 2531 C ARG A 244 -84.759 55.384 331.955 1.00115.68 C
ANISOU 2531 C ARG A 244 14162 16558 13232 544 253 1214 C
ATOM 2532 O ARG A 244 -84.732 54.823 333.053 1.00114.73 O
ANISOU 2532 O ARG A 244 13847 16527 13220 649 233 1204 O
ATOM 2533 CB ARG A 244 -85.869 54.021 330.144 1.00112.33 C
ANISOU 2533 CB ARG A 244 13779 15977 12926 939 263 1179 C
ATOM 2534 CG ARG A 244 -87.191 53.471 329.625 1.00121.57 C
ANISOU 2534 CG ARG A 244 15057 16921 14214 1212 203 1135 C
ATOM 2535 CD ARG A 244 -86.988 52.139 328.931 1.00138.00 C
ANISOU 2535 CD ARG A 244 16944 19138 16353 1398 271 1131 C
ATOM 2536 NE ARG A 244 -87.818 52.011 327.735 1.00154.48 N
ANISOU 2536 NE ARG A 244 19201 21048 18446 1523 251 1108 N
ATOM 2537 CZ ARG A 244 -87.354 52.056 326.489 1.00174.42 C
ANISOU 2537 CZ ARG A 244 21774 23625 20874 1468 314 1132 C
ATOM 2538 NH1 ARG A 244 -86.054 52.203 326.261 1.00163.49 N
ANISOU 2538 NH1 ARG A 244 20254 22491 19372 1281 412 1165 N
ATOM 2539 NH2 ARG A 244 -88.184 51.949 325.464 1.00164.99 N
ANISOU 2539 NH2 ARG A 244 20752 22250 19687 1593 280 1108 N
ATOM 2540 N LYS A 245 -83.739 56.134 331.477 1.00112.53 N
ANISOU 2540 N LYS A 245 13807 16307 12643 234 324 1238 N
ATOM 2541 CA LYS A 245 -82.482 56.395 332.191 1.00112.77 C
ANISOU 2541 CA LYS A 245 13625 16649 12575 -15 385 1242 C
ATOM 2542 C LYS A 245 -82.734 57.161 333.491 1.00112.59 C
ANISOU 2542 C LYS A 245 13710 16506 12562 -120 307 1257 C
ATOM 2543 O LYS A 245 -82.192 56.768 334.526 1.00112.86 O
ANISOU 2543 O LYS A 245 13489 16747 12646 -114 309 1250 O
ATOM 2544 CB LYS A 245 -81.475 57.160 331.301 1.00118.22 C
ANISOU 2544 CB LYS A 245 14385 17511 13024 -380 489 1244 C
ATOM 2545 CG LYS A 245 -80.357 56.289 330.724 1.00133.54 C
ANISOU 2545 CG LYS A 245 15953 19865 14922 -373 607 1198 C
ATOM 2546 CD LYS A 245 -78.957 56.791 331.098 1.00144.25 C
ANISOU 2546 CD LYS A 245 17106 21613 16089 -739 699 1159 C
ATOM 2547 CE LYS A 245 -77.882 55.811 330.670 1.00153.29 C
ANISOU 2547 CE LYS A 245 17816 23221 17208 -660 796 1077 C
ATOM 2548 NZ LYS A 245 -76.595 56.015 331.396 1.00158.48 N
ANISOU 2548 NZ LYS A 245 18160 24323 17734 -910 852 1006 N
ATOM 2549 N VAL A 246 -83.569 58.231 333.436 1.00105.03 N
ANISOU 2549 N VAL A 246 13145 15210 11552 -191 227 1271 N
ATOM 2550 CA VAL A 246 -83.933 59.073 334.582 1.00103.33 C
ANISOU 2550 CA VAL A 246 13095 14835 11332 -278 143 1278 C
ATOM 2551 C VAL A 246 -84.776 58.292 335.605 1.00104.48 C
ANISOU 2551 C VAL A 246 13086 14911 11702 27 75 1246 C
ATOM 2552 O VAL A 246 -84.442 58.292 336.792 1.00103.61 O
ANISOU 2552 O VAL A 246 12840 14902 11626 -30 63 1252 O
ATOM 2553 CB VAL A 246 -84.601 60.414 334.160 1.00106.97 C
ANISOU 2553 CB VAL A 246 14054 14944 11644 -400 60 1284 C
ATOM 2554 CG1 VAL A 246 -85.159 61.168 335.368 1.00106.26 C
ANISOU 2554 CG1 VAL A 246 14136 14665 11573 -409 -44 1274 C
ATOM 2555 CG2 VAL A 246 -83.630 61.296 333.384 1.00108.92 C
ANISOU 2555 CG2 VAL A 246 14501 15263 11620 -796 137 1320 C
ATOM 2556 N VAL A 247 -85.843 57.611 335.135 1.00 99.02 N
ANISOU 2556 N VAL A 247 12416 14062 11146 328 37 1205 N
ATOM 2557 CA VAL A 247 -86.765 56.828 335.965 1.00 96.61 C
ANISOU 2557 CA VAL A 247 11993 13685 11028 589 -14 1155 C
ATOM 2558 C VAL A 247 -86.005 55.728 336.734 1.00101.96 C
ANISOU 2558 C VAL A 247 12328 14629 11782 641 41 1171 C
ATOM 2559 O VAL A 247 -86.220 55.616 337.943 1.00101.13 O
ANISOU 2559 O VAL A 247 12165 14511 11749 671 4 1156 O
ATOM 2560 CB VAL A 247 -87.997 56.323 335.161 1.00 98.20 C
ANISOU 2560 CB VAL A 247 12284 13704 11325 857 -53 1091 C
ATOM 2561 CG1 VAL A 247 -88.805 55.288 335.931 1.00 96.00 C
ANISOU 2561 CG1 VAL A 247 11839 13421 11215 1082 -67 1029 C
ATOM 2562 CG2 VAL A 247 -88.891 57.493 334.781 1.00 98.23 C
ANISOU 2562 CG2 VAL A 247 12641 13425 11258 861 -155 1046 C
ATOM 2563 N LYS A 248 -85.059 55.002 336.076 1.00100.20 N
ANISOU 2563 N LYS A 248 11898 14652 11520 643 119 1193 N
ATOM 2564 CA LYS A 248 -84.232 53.974 336.749 1.00100.35 C
ANISOU 2564 CA LYS A 248 11613 14937 11579 728 146 1194 C
ATOM 2565 C LYS A 248 -83.374 54.617 337.851 1.00104.30 C
ANISOU 2565 C LYS A 248 12029 15594 12008 510 135 1212 C
ATOM 2566 O LYS A 248 -83.377 54.137 338.989 1.00103.50 O
ANISOU 2566 O LYS A 248 11820 15529 11977 599 93 1204 O
ATOM 2567 CB LYS A 248 -83.332 53.221 335.753 1.00104.11 C
ANISOU 2567 CB LYS A 248 11892 15667 11999 784 222 1190 C
ATOM 2568 CG LYS A 248 -83.922 51.915 335.243 1.00122.80 C
ANISOU 2568 CG LYS A 248 14210 17976 14473 1095 222 1167 C
ATOM 2569 CD LYS A 248 -83.045 51.324 334.140 1.00139.10 C
ANISOU 2569 CD LYS A 248 16110 20277 16464 1146 297 1158 C
ATOM 2570 CE LYS A 248 -83.621 50.078 333.507 1.00152.78 C
ANISOU 2570 CE LYS A 248 17838 21931 18282 1443 297 1140 C
ATOM 2571 NZ LYS A 248 -82.903 49.714 332.252 1.00162.26 N
ANISOU 2571 NZ LYS A 248 18921 23329 19402 1479 373 1126 N
ATOM 2572 N MET A 249 -82.697 55.741 337.516 1.00100.73 N
ANISOU 2572 N MET A 249 11661 15213 11397 205 170 1234 N
ATOM 2573 CA MET A 249 -81.853 56.523 338.418 1.00101.14 C
ANISOU 2573 CA MET A 249 11665 15419 11346 -67 169 1248 C
ATOM 2574 C MET A 249 -82.643 56.952 339.680 1.00103.65 C
ANISOU 2574 C MET A 249 12134 15504 11744 -49 82 1256 C
ATOM 2575 O MET A 249 -82.218 56.650 340.799 1.00103.34 O
ANISOU 2575 O MET A 249 11931 15599 11733 -51 57 1255 O
ATOM 2576 CB MET A 249 -81.289 57.740 337.659 1.00105.13 C
ANISOU 2576 CB MET A 249 12347 15954 11643 -426 226 1267 C
ATOM 2577 CG MET A 249 -80.274 58.538 338.434 1.00110.41 C
ANISOU 2577 CG MET A 249 12961 16824 12167 -763 244 1272 C
ATOM 2578 SD MET A 249 -79.441 59.807 337.445 1.00117.13 S
ANISOU 2578 SD MET A 249 14011 17772 12720 -1248 341 1279 S
ATOM 2579 CE MET A 249 -80.667 61.084 337.424 1.00113.11 C
ANISOU 2579 CE MET A 249 14085 16726 12164 -1308 247 1328 C
ATOM 2580 N MET A 250 -83.821 57.584 339.479 1.00 98.29 N
ANISOU 2580 N MET A 250 11759 14487 11099 0 30 1250 N
ATOM 2581 CA MET A 250 -84.705 58.090 340.532 1.00 96.15 C
ANISOU 2581 CA MET A 250 11652 13988 10892 29 -50 1233 C
ATOM 2582 C MET A 250 -85.350 57.000 341.368 1.00 98.53 C
ANISOU 2582 C MET A 250 11802 14269 11365 282 -77 1194 C
ATOM 2583 O MET A 250 -85.606 57.235 342.547 1.00 97.85 O
ANISOU 2583 O MET A 250 11744 14121 11314 252 -121 1183 O
ATOM 2584 CB MET A 250 -85.749 59.051 339.962 1.00 98.08 C
ANISOU 2584 CB MET A 250 12255 13913 11098 43 -111 1207 C
ATOM 2585 CG MET A 250 -85.151 60.285 339.296 1.00103.78 C
ANISOU 2585 CG MET A 250 13234 14591 11605 -253 -101 1249 C
ATOM 2586 SD MET A 250 -84.299 61.462 340.382 1.00109.93 S
ANISOU 2586 SD MET A 250 14117 15425 12226 -620 -111 1292 S
ATOM 2587 CE MET A 250 -82.673 60.806 340.393 1.00108.16 C
ANISOU 2587 CE MET A 250 13504 15659 11932 -823 7 1322 C
ATOM 2588 N ILE A 251 -85.596 55.810 340.786 1.00 94.48 N
ANISOU 2588 N ILE A 251 11155 13802 10941 512 -49 1172 N
ATOM 2589 CA ILE A 251 -86.146 54.670 341.530 1.00 92.70 C
ANISOU 2589 CA ILE A 251 10825 13556 10841 721 -66 1135 C
ATOM 2590 C ILE A 251 -85.070 54.188 342.517 1.00 98.25 C
ANISOU 2590 C ILE A 251 11328 14483 11518 678 -69 1166 C
ATOM 2591 O ILE A 251 -85.381 53.932 343.682 1.00 98.11 O
ANISOU 2591 O ILE A 251 11319 14408 11551 705 -107 1149 O
ATOM 2592 CB ILE A 251 -86.664 53.540 340.589 1.00 94.19 C
ANISOU 2592 CB ILE A 251 10968 13721 11099 956 -36 1104 C
ATOM 2593 CG1 ILE A 251 -88.014 53.934 339.974 1.00 93.58 C
ANISOU 2593 CG1 ILE A 251 11085 13402 11069 1036 -60 1042 C
ATOM 2594 CG2 ILE A 251 -86.774 52.185 341.313 1.00 92.98 C
ANISOU 2594 CG2 ILE A 251 10705 13607 11017 1128 -41 1082 C
ATOM 2595 CD1 ILE A 251 -88.452 53.064 338.802 1.00 99.07 C
ANISOU 2595 CD1 ILE A 251 11759 14076 11806 1223 -28 1015 C
ATOM 2596 N VAL A 252 -83.809 54.111 342.052 1.00 95.40 N
ANISOU 2596 N VAL A 252 10791 14390 11066 606 -33 1196 N
ATOM 2597 CA VAL A 252 -82.664 53.690 342.857 1.00 96.19 C
ANISOU 2597 CA VAL A 252 10671 14759 11119 587 -51 1202 C
ATOM 2598 C VAL A 252 -82.477 54.647 344.053 1.00 99.91 C
ANISOU 2598 C VAL A 252 11201 15211 11550 365 -90 1220 C
ATOM 2599 O VAL A 252 -82.413 54.176 345.189 1.00 98.92 O
ANISOU 2599 O VAL A 252 11022 15102 11460 432 -142 1214 O
ATOM 2600 CB VAL A 252 -81.390 53.516 341.979 1.00102.40 C
ANISOU 2600 CB VAL A 252 11230 15881 11797 547 2 1194 C
ATOM 2601 CG1 VAL A 252 -80.141 53.288 342.827 1.00104.00 C
ANISOU 2601 CG1 VAL A 252 11180 16409 11925 515 -32 1172 C
ATOM 2602 CG2 VAL A 252 -81.567 52.370 340.984 1.00101.81 C
ANISOU 2602 CG2 VAL A 252 11092 15823 11767 814 28 1172 C
ATOM 2603 N VAL A 253 -82.458 55.982 343.788 1.00 97.01 N
ANISOU 2603 N VAL A 253 10988 14775 11097 104 -70 1243 N
ATOM 2604 CA VAL A 253 -82.326 57.076 344.769 1.00 97.01 C
ANISOU 2604 CA VAL A 253 11102 14722 11034 -139 -103 1264 C
ATOM 2605 C VAL A 253 -83.371 56.937 345.892 1.00100.93 C
ANISOU 2605 C VAL A 253 11723 14979 11646 -23 -164 1245 C
ATOM 2606 O VAL A 253 -83.010 56.981 347.071 1.00102.48 O
ANISOU 2606 O VAL A 253 11864 15237 11835 -93 -201 1253 O
ATOM 2607 CB VAL A 253 -82.376 58.471 344.077 1.00101.07 C
ANISOU 2607 CB VAL A 253 11865 15119 11419 -404 -80 1287 C
ATOM 2608 CG1 VAL A 253 -82.601 59.604 345.075 1.00100.80 C
ANISOU 2608 CG1 VAL A 253 12047 14921 11332 -602 -131 1303 C
ATOM 2609 CG2 VAL A 253 -81.121 58.726 343.252 1.00102.85 C
ANISOU 2609 CG2 VAL A 253 11953 15642 11482 -629 -5 1297 C
ATOM 2610 N VAL A 254 -84.642 56.728 345.520 1.00 95.58 N
ANISOU 2610 N VAL A 254 11193 14056 11066 150 -172 1206 N
ATOM 2611 CA VAL A 254 -85.764 56.551 346.443 1.00 94.67 C
ANISOU 2611 CA VAL A 254 11182 13737 11051 254 -210 1154 C
ATOM 2612 C VAL A 254 -85.621 55.268 347.268 1.00 98.94 C
ANISOU 2612 C VAL A 254 11573 14365 11655 398 -219 1144 C
ATOM 2613 O VAL A 254 -85.844 55.302 348.477 1.00 99.08 O
ANISOU 2613 O VAL A 254 11629 14324 11691 357 -251 1130 O
ATOM 2614 CB VAL A 254 -87.110 56.651 345.688 1.00 98.40 C
ANISOU 2614 CB VAL A 254 11816 13983 11587 396 -213 1085 C
ATOM 2615 CG1 VAL A 254 -88.281 56.143 346.522 1.00 96.76 C
ANISOU 2615 CG1 VAL A 254 11645 13640 11481 523 -230 996 C
ATOM 2616 CG2 VAL A 254 -87.357 58.089 345.227 1.00 99.43 C
ANISOU 2616 CG2 VAL A 254 12184 13966 11629 263 -246 1084 C
ATOM 2617 N CYS A 255 -85.212 54.158 346.630 1.00 96.01 N
ANISOU 2617 N CYS A 255 11061 14123 11297 562 -196 1150 N
ATOM 2618 CA CYS A 255 -85.000 52.874 347.308 1.00 95.63 C
ANISOU 2618 CA CYS A 255 10925 14139 11271 724 -222 1140 C
ATOM 2619 C CYS A 255 -83.850 52.979 348.303 1.00 97.83 C
ANISOU 2619 C CYS A 255 11084 14609 11478 635 -272 1173 C
ATOM 2620 O CYS A 255 -83.933 52.407 349.389 1.00 97.14 O
ANISOU 2620 O CYS A 255 11029 14480 11399 695 -320 1162 O
ATOM 2621 CB CYS A 255 -84.786 51.746 346.303 1.00 96.63 C
ANISOU 2621 CB CYS A 255 10961 14351 11402 933 -198 1135 C
ATOM 2622 SG CYS A 255 -86.278 51.302 345.370 1.00 99.56 S
ANISOU 2622 SG CYS A 255 11479 14488 11863 1069 -151 1078 S
ATOM 2623 N THR A 256 -82.816 53.775 347.956 1.00 93.28 N
ANISOU 2623 N THR A 256 10387 14241 10816 469 -262 1205 N
ATOM 2624 CA THR A 256 -81.664 54.045 348.813 1.00 93.67 C
ANISOU 2624 CA THR A 256 10291 14520 10778 348 -307 1220 C
ATOM 2625 C THR A 256 -82.147 54.823 350.044 1.00 95.30 C
ANISOU 2625 C THR A 256 10656 14555 10998 183 -340 1232 C
ATOM 2626 O THR A 256 -81.766 54.473 351.161 1.00 95.67 O
ANISOU 2626 O THR A 256 10661 14661 11028 201 -403 1231 O
ATOM 2627 CB THR A 256 -80.574 54.787 348.026 1.00103.35 C
ANISOU 2627 CB THR A 256 11357 16022 11890 157 -263 1228 C
ATOM 2628 OG1 THR A 256 -80.237 54.022 346.874 1.00105.78 O
ANISOU 2628 OG1 THR A 256 11525 16475 12190 326 -225 1205 O
ATOM 2629 CG2 THR A 256 -79.326 55.029 348.840 1.00103.22 C
ANISOU 2629 CG2 THR A 256 11142 16308 11769 29 -308 1218 C
ATOM 2630 N PHE A 257 -83.023 55.841 349.837 1.00 88.42 N
ANISOU 2630 N PHE A 257 9986 13461 10150 48 -310 1234 N
ATOM 2631 CA PHE A 257 -83.588 56.662 350.906 1.00 86.07 C
ANISOU 2631 CA PHE A 257 9860 12983 9859 -93 -339 1232 C
ATOM 2632 C PHE A 257 -84.391 55.806 351.883 1.00 90.07 C
ANISOU 2632 C PHE A 257 10425 13346 10451 56 -366 1191 C
ATOM 2633 O PHE A 257 -84.141 55.872 353.089 1.00 90.17 O
ANISOU 2633 O PHE A 257 10451 13369 10442 -21 -409 1200 O
ATOM 2634 CB PHE A 257 -84.449 57.787 350.325 1.00 86.27 C
ANISOU 2634 CB PHE A 257 10108 12789 9883 -184 -318 1216 C
ATOM 2635 CG PHE A 257 -85.047 58.729 351.345 1.00 86.44 C
ANISOU 2635 CG PHE A 257 10322 12626 9895 -312 -354 1198 C
ATOM 2636 CD1 PHE A 257 -84.429 59.937 351.647 1.00 89.81 C
ANISOU 2636 CD1 PHE A 257 10846 13076 10203 -570 -372 1243 C
ATOM 2637 CD2 PHE A 257 -86.256 58.430 351.971 1.00 85.72 C
ANISOU 2637 CD2 PHE A 257 10328 12345 9898 -187 -365 1124 C
ATOM 2638 CE1 PHE A 257 -84.993 60.816 352.576 1.00 90.23 C
ANISOU 2638 CE1 PHE A 257 11100 12945 10238 -672 -411 1223 C
ATOM 2639 CE2 PHE A 257 -86.813 59.306 352.906 1.00 87.81 C
ANISOU 2639 CE2 PHE A 257 10760 12457 10148 -291 -397 1091 C
ATOM 2640 CZ PHE A 257 -86.182 60.492 353.198 1.00 87.26 C
ANISOU 2640 CZ PHE A 257 10796 12391 9966 -516 -425 1145 C
ATOM 2641 N ALA A 258 -85.350 55.012 351.363 1.00 86.93 N
ANISOU 2641 N ALA A 258 10077 12820 10133 243 -336 1142 N
ATOM 2642 CA ALA A 258 -86.218 54.118 352.144 1.00 86.69 C
ANISOU 2642 CA ALA A 258 10131 12651 10158 351 -340 1085 C
ATOM 2643 C ALA A 258 -85.402 53.160 353.036 1.00 93.48 C
ANISOU 2643 C ALA A 258 10929 13620 10970 417 -395 1114 C
ATOM 2644 O ALA A 258 -85.741 52.989 354.211 1.00 92.03 O
ANISOU 2644 O ALA A 258 10851 13335 10781 374 -420 1091 O
ATOM 2645 CB ALA A 258 -87.136 53.329 351.211 1.00 86.20 C
ANISOU 2645 CB ALA A 258 10102 12494 10157 519 -291 1027 C
ATOM 2646 N ILE A 259 -84.297 52.585 352.483 1.00 92.59 N
ANISOU 2646 N ILE A 259 10651 13723 10807 528 -424 1152 N
ATOM 2647 CA ILE A 259 -83.405 51.664 353.196 1.00 93.98 C
ANISOU 2647 CA ILE A 259 10765 14028 10914 651 -507 1163 C
ATOM 2648 C ILE A 259 -82.700 52.378 354.356 1.00 99.98 C
ANISOU 2648 C ILE A 259 11489 14882 11618 485 -569 1188 C
ATOM 2649 O ILE A 259 -82.814 51.924 355.492 1.00101.21 O
ANISOU 2649 O ILE A 259 11753 14955 11747 511 -629 1181 O
ATOM 2650 CB ILE A 259 -82.416 50.919 352.233 1.00 98.04 C
ANISOU 2650 CB ILE A 259 11090 14781 11380 848 -530 1166 C
ATOM 2651 CG1 ILE A 259 -83.178 49.890 351.361 1.00 97.55 C
ANISOU 2651 CG1 ILE A 259 11122 14583 11361 1047 -489 1140 C
ATOM 2652 CG2 ILE A 259 -81.261 50.230 353.011 1.00 99.67 C
ANISOU 2652 CG2 ILE A 259 11197 15185 11487 985 -650 1159 C
ATOM 2653 CD1 ILE A 259 -82.483 49.473 350.045 1.00102.73 C
ANISOU 2653 CD1 ILE A 259 11600 15440 11992 1202 -472 1139 C
ATOM 2654 N CYS A 260 -82.011 53.500 354.067 1.00 96.04 N
ANISOU 2654 N CYS A 260 10866 14541 11085 294 -551 1217 N
ATOM 2655 CA CYS A 260 -81.246 54.312 355.011 1.00 96.29 C
ANISOU 2655 CA CYS A 260 10844 14695 11046 95 -600 1240 C
ATOM 2656 C CYS A 260 -82.030 54.821 356.212 1.00 97.24 C
ANISOU 2656 C CYS A 260 11172 14579 11195 -40 -610 1242 C
ATOM 2657 O CYS A 260 -81.457 54.895 357.295 1.00 98.89 O
ANISOU 2657 O CYS A 260 11367 14859 11349 -107 -680 1254 O
ATOM 2658 CB CYS A 260 -80.571 55.465 354.283 1.00 98.01 C
ANISOU 2658 CB CYS A 260 10945 15093 11202 -128 -553 1262 C
ATOM 2659 SG CYS A 260 -79.232 54.953 353.183 1.00104.11 S
ANISOU 2659 SG CYS A 260 11396 16272 11890 -32 -550 1236 S
ATOM 2660 N TRP A 261 -83.308 55.198 356.034 1.00 89.86 N
ANISOU 2660 N TRP A 261 10417 13387 10337 -76 -545 1216 N
ATOM 2661 CA TRP A 261 -84.130 55.764 357.111 1.00 87.83 C
ANISOU 2661 CA TRP A 261 10346 12924 10103 -204 -544 1193 C
ATOM 2662 C TRP A 261 -84.997 54.761 357.882 1.00 90.77 C
ANISOU 2662 C TRP A 261 10853 13124 10510 -97 -543 1138 C
ATOM 2663 O TRP A 261 -85.465 55.099 358.970 1.00 90.81 O
ANISOU 2663 O TRP A 261 10987 13007 10510 -212 -550 1114 O
ATOM 2664 CB TRP A 261 -84.998 56.916 356.571 1.00 85.44 C
ANISOU 2664 CB TRP A 261 10163 12467 9834 -311 -488 1166 C
ATOM 2665 CG TRP A 261 -84.191 58.142 356.281 1.00 86.84 C
ANISOU 2665 CG TRP A 261 10319 12748 9929 -514 -497 1221 C
ATOM 2666 CD1 TRP A 261 -83.794 58.587 355.056 1.00 89.91 C
ANISOU 2666 CD1 TRP A 261 10659 13224 10278 -552 -466 1246 C
ATOM 2667 CD2 TRP A 261 -83.530 58.982 357.247 1.00 87.32 C
ANISOU 2667 CD2 TRP A 261 10409 12861 9907 -734 -539 1261 C
ATOM 2668 NE1 TRP A 261 -82.987 59.695 355.193 1.00 90.30 N
ANISOU 2668 NE1 TRP A 261 10730 13365 10213 -806 -478 1293 N
ATOM 2669 CE2 TRP A 261 -82.802 59.953 356.527 1.00 91.69 C
ANISOU 2669 CE2 TRP A 261 10946 13528 10364 -919 -524 1304 C
ATOM 2670 CE3 TRP A 261 -83.528 59.038 358.656 1.00 88.13 C
ANISOU 2670 CE3 TRP A 261 10576 12914 9996 -812 -583 1261 C
ATOM 2671 CZ2 TRP A 261 -82.071 60.963 357.164 1.00 91.93 C
ANISOU 2671 CZ2 TRP A 261 11019 13631 10280 -1189 -550 1344 C
ATOM 2672 CZ3 TRP A 261 -82.827 60.054 359.283 1.00 90.27 C
ANISOU 2672 CZ3 TRP A 261 10878 13251 10171 -1054 -615 1305 C
ATOM 2673 CH2 TRP A 261 -82.101 60.994 358.542 1.00 92.12 C
ANISOU 2673 CH2 TRP A 261 11090 13605 10305 -1244 -598 1345 C
ATOM 2674 N LEU A 262 -85.208 53.546 357.356 1.00 86.72 N
ANISOU 2674 N LEU A 262 10335 12600 10015 99 -532 1114 N
ATOM 2675 CA LEU A 262 -86.041 52.557 358.042 1.00 86.37 C
ANISOU 2675 CA LEU A 262 10462 12386 9967 159 -521 1057 C
ATOM 2676 C LEU A 262 -85.510 52.173 359.463 1.00 91.96 C
ANISOU 2676 C LEU A 262 11267 13083 10591 121 -605 1078 C
ATOM 2677 O LEU A 262 -86.297 52.286 360.410 1.00 91.89 O
ANISOU 2677 O LEU A 262 11422 12913 10578 -3 -577 1030 O
ATOM 2678 CB LEU A 262 -86.301 51.313 357.163 1.00 86.00 C
ANISOU 2678 CB LEU A 262 10428 12323 9925 361 -499 1033 C
ATOM 2679 CG LEU A 262 -87.341 50.282 357.660 1.00 89.46 C
ANISOU 2679 CG LEU A 262 11083 12569 10338 379 -459 957 C
ATOM 2680 CD1 LEU A 262 -88.680 50.939 358.023 1.00 88.16 C
ANISOU 2680 CD1 LEU A 262 10999 12268 10229 212 -367 856 C
ATOM 2681 CD2 LEU A 262 -87.535 49.176 356.635 1.00 89.90 C
ANISOU 2681 CD2 LEU A 262 11156 12616 10386 563 -437 942 C
ATOM 2682 N PRO A 263 -84.220 51.780 359.670 1.00 88.79 N
ANISOU 2682 N PRO A 263 10765 12858 10113 220 -712 1135 N
ATOM 2683 CA PRO A 263 -83.774 51.436 361.038 1.00 89.02 C
ANISOU 2683 CA PRO A 263 10912 12859 10052 199 -810 1146 C
ATOM 2684 C PRO A 263 -83.886 52.607 362.007 1.00 92.31 C
ANISOU 2684 C PRO A 263 11363 13234 10478 -48 -801 1157 C
ATOM 2685 O PRO A 263 -84.235 52.409 363.181 1.00 91.61 O
ANISOU 2685 O PRO A 263 11463 13001 10343 -126 -824 1138 O
ATOM 2686 CB PRO A 263 -82.313 51.012 360.848 1.00 92.45 C
ANISOU 2686 CB PRO A 263 11163 13557 10408 375 -934 1181 C
ATOM 2687 CG PRO A 263 -82.185 50.681 359.405 1.00 97.02 C
ANISOU 2687 CG PRO A 263 11590 14247 11025 532 -889 1175 C
ATOM 2688 CD PRO A 263 -83.121 51.603 358.696 1.00 91.03 C
ANISOU 2688 CD PRO A 263 10821 13392 10375 365 -754 1169 C
ATOM 2689 N PHE A 264 -83.622 53.836 361.488 1.00 87.83 N
ANISOU 2689 N PHE A 264 10642 12776 9952 -182 -763 1183 N
ATOM 2690 CA PHE A 264 -83.708 55.102 362.218 1.00 86.35 C
ANISOU 2690 CA PHE A 264 10498 12547 9763 -420 -752 1196 C
ATOM 2691 C PHE A 264 -85.114 55.285 362.810 1.00 88.66 C
ANISOU 2691 C PHE A 264 11000 12583 10103 -509 -676 1125 C
ATOM 2692 O PHE A 264 -85.264 55.368 364.032 1.00 85.98 O
ANISOU 2692 O PHE A 264 10793 12151 9724 -618 -700 1113 O
ATOM 2693 CB PHE A 264 -83.328 56.284 361.296 1.00 87.14 C
ANISOU 2693 CB PHE A 264 10464 12770 9874 -538 -716 1229 C
ATOM 2694 CG PHE A 264 -83.246 57.618 362.004 1.00 87.52 C
ANISOU 2694 CG PHE A 264 10587 12780 9888 -788 -720 1251 C
ATOM 2695 CD1 PHE A 264 -82.062 58.030 362.611 1.00 89.88 C
ANISOU 2695 CD1 PHE A 264 10790 13267 10095 -920 -793 1301 C
ATOM 2696 CD2 PHE A 264 -84.363 58.447 362.097 1.00 87.17 C
ANISOU 2696 CD2 PHE A 264 10713 12521 9887 -880 -659 1205 C
ATOM 2697 CE1 PHE A 264 -81.993 59.247 363.287 1.00 90.23 C
ANISOU 2697 CE1 PHE A 264 10931 13260 10091 -1166 -797 1324 C
ATOM 2698 CE2 PHE A 264 -84.292 59.662 362.781 1.00 89.56 C
ANISOU 2698 CE2 PHE A 264 11122 12766 10140 -1093 -673 1222 C
ATOM 2699 CZ PHE A 264 -83.107 60.054 363.367 1.00 88.35 C
ANISOU 2699 CZ PHE A 264 10897 12778 9895 -1247 -738 1290 C
ATOM 2700 N HIS A 265 -86.138 55.292 361.939 1.00 85.86 N
ANISOU 2700 N HIS A 265 10665 12134 9823 -455 -587 1061 N
ATOM 2701 CA HIS A 265 -87.522 55.460 362.361 1.00 85.59 C
ANISOU 2701 CA HIS A 265 10778 11915 9828 -521 -509 953 C
ATOM 2702 C HIS A 265 -87.999 54.351 363.309 1.00 91.38 C
ANISOU 2702 C HIS A 265 11668 12538 10513 -522 -497 898 C
ATOM 2703 O HIS A 265 -88.746 54.664 364.230 1.00 90.98 O
ANISOU 2703 O HIS A 265 11742 12374 10451 -656 -453 820 O
ATOM 2704 CB HIS A 265 -88.454 55.651 361.158 1.00 85.24 C
ANISOU 2704 CB HIS A 265 10693 11833 9860 -438 -433 878 C
ATOM 2705 CG HIS A 265 -88.230 56.967 360.463 1.00 88.41 C
ANISOU 2705 CG HIS A 265 11044 12270 10277 -486 -445 911 C
ATOM 2706 ND1 HIS A 265 -88.448 58.179 361.110 1.00 90.37 N
ANISOU 2706 ND1 HIS A 265 11391 12442 10505 -629 -457 890 N
ATOM 2707 CD2 HIS A 265 -87.803 57.219 359.207 1.00 89.31 C
ANISOU 2707 CD2 HIS A 265 11059 12472 10403 -420 -449 962 C
ATOM 2708 CE1 HIS A 265 -88.143 59.116 360.231 1.00 89.33 C
ANISOU 2708 CE1 HIS A 265 11246 12337 10360 -649 -474 932 C
ATOM 2709 NE2 HIS A 265 -87.752 58.589 359.073 1.00 89.47 N
ANISOU 2709 NE2 HIS A 265 11143 12455 10395 -537 -465 975 N
ATOM 2710 N ILE A 266 -87.526 53.089 363.139 1.00 89.10 N
ANISOU 2710 N ILE A 266 11400 12280 10173 -381 -543 936 N
ATOM 2711 CA ILE A 266 -87.884 51.973 364.036 1.00 89.47 C
ANISOU 2711 CA ILE A 266 11670 12194 10130 -392 -547 894 C
ATOM 2712 C ILE A 266 -87.250 52.225 365.415 1.00 93.75 C
ANISOU 2712 C ILE A 266 12318 12712 10591 -506 -632 939 C
ATOM 2713 O ILE A 266 -87.951 52.152 366.431 1.00 93.16 O
ANISOU 2713 O ILE A 266 12437 12494 10467 -657 -589 873 O
ATOM 2714 CB ILE A 266 -87.532 50.565 363.449 1.00 93.09 C
ANISOU 2714 CB ILE A 266 12180 12661 10529 -185 -591 919 C
ATOM 2715 CG1 ILE A 266 -88.395 50.241 362.204 1.00 92.22 C
ANISOU 2715 CG1 ILE A 266 12018 12532 10488 -114 -487 852 C
ATOM 2716 CG2 ILE A 266 -87.676 49.457 364.520 1.00 95.01 C
ANISOU 2716 CG2 ILE A 266 12729 12745 10627 -207 -635 898 C
ATOM 2717 CD1 ILE A 266 -87.842 49.127 361.301 1.00 98.59 C
ANISOU 2717 CD1 ILE A 266 12810 13391 11260 117 -535 895 C
ATOM 2718 N PHE A 267 -85.936 52.579 365.428 1.00 90.02 N
ANISOU 2718 N PHE A 267 11704 12401 10098 -451 -745 1038 N
ATOM 2719 CA PHE A 267 -85.169 52.926 366.629 1.00 89.27 C
ANISOU 2719 CA PHE A 267 11662 12328 9927 -546 -844 1087 C
ATOM 2720 C PHE A 267 -85.907 53.984 367.454 1.00 94.33 C
ANISOU 2720 C PHE A 267 12387 12858 10597 -788 -773 1045 C
ATOM 2721 O PHE A 267 -86.035 53.815 368.658 1.00 95.64 O
ANISOU 2721 O PHE A 267 12738 12912 10688 -895 -799 1031 O
ATOM 2722 CB PHE A 267 -83.761 53.420 366.250 1.00 90.89 C
ANISOU 2722 CB PHE A 267 11622 12791 10121 -483 -947 1169 C
ATOM 2723 CG PHE A 267 -82.873 53.717 367.427 1.00 92.94 C
ANISOU 2723 CG PHE A 267 11903 13118 10292 -564 -1065 1211 C
ATOM 2724 CD1 PHE A 267 -82.055 52.733 367.968 1.00 96.82 C
ANISOU 2724 CD1 PHE A 267 12463 13656 10670 -396 -1211 1224 C
ATOM 2725 CD2 PHE A 267 -82.866 54.977 368.014 1.00 94.41 C
ANISOU 2725 CD2 PHE A 267 12065 13312 10493 -796 -1043 1231 C
ATOM 2726 CE1 PHE A 267 -81.252 53.002 369.078 1.00 98.29 C
ANISOU 2726 CE1 PHE A 267 12668 13911 10767 -459 -1334 1252 C
ATOM 2727 CE2 PHE A 267 -82.084 55.234 369.142 1.00 97.66 C
ANISOU 2727 CE2 PHE A 267 12505 13783 10818 -884 -1151 1266 C
ATOM 2728 CZ PHE A 267 -81.271 54.252 369.654 1.00 96.74 C
ANISOU 2728 CZ PHE A 267 12428 13732 10598 -715 -1297 1275 C
ATOM 2729 N PHE A 268 -86.405 55.053 366.816 1.00 91.37 N
ANISOU 2729 N PHE A 268 11902 12501 10314 -861 -691 1019 N
ATOM 2730 CA PHE A 268 -87.128 56.111 367.514 1.00 91.43 C
ANISOU 2730 CA PHE A 268 11992 12407 10340 -1050 -634 963 C
ATOM 2731 C PHE A 268 -88.611 55.807 367.731 1.00101.11 C
ANISOU 2731 C PHE A 268 13347 13483 11588 -1097 -516 816 C
ATOM 2732 O PHE A 268 -89.235 56.466 368.564 1.00100.79 O
ANISOU 2732 O PHE A 268 13399 13360 11538 -1244 -474 744 O
ATOM 2733 CB PHE A 268 -86.920 57.466 366.832 1.00 91.71 C
ANISOU 2733 CB PHE A 268 11905 12517 10424 -1102 -630 996 C
ATOM 2734 CG PHE A 268 -85.564 58.039 367.156 1.00 92.78 C
ANISOU 2734 CG PHE A 268 11959 12795 10497 -1187 -729 1110 C
ATOM 2735 CD1 PHE A 268 -85.303 58.588 368.408 1.00 94.27 C
ANISOU 2735 CD1 PHE A 268 12252 12941 10627 -1358 -771 1131 C
ATOM 2736 CD2 PHE A 268 -84.536 58.006 366.222 1.00 94.46 C
ANISOU 2736 CD2 PHE A 268 11981 13209 10700 -1109 -775 1183 C
ATOM 2737 CE1 PHE A 268 -84.039 59.088 368.718 1.00 95.60 C
ANISOU 2737 CE1 PHE A 268 12331 13269 10725 -1453 -862 1222 C
ATOM 2738 CE2 PHE A 268 -83.274 58.519 366.532 1.00 97.84 C
ANISOU 2738 CE2 PHE A 268 12304 13820 11052 -1214 -859 1260 C
ATOM 2739 CZ PHE A 268 -83.033 59.053 367.779 1.00 95.88 C
ANISOU 2739 CZ PHE A 268 12157 13530 10744 -1387 -904 1280 C
ATOM 2740 N LEU A 269 -89.164 54.798 367.037 1.00103.10 N
ANISOU 2740 N LEU A 269 13605 13716 11853 -984 -461 758 N
ATOM 2741 CA LEU A 269 -90.566 54.403 367.207 1.00105.74 C
ANISOU 2741 CA LEU A 269 14039 13954 12185 -1052 -338 594 C
ATOM 2742 C LEU A 269 -90.709 53.459 368.394 1.00117.69 C
ANISOU 2742 C LEU A 269 15789 15353 13574 -1172 -331 564 C
ATOM 2743 O LEU A 269 -91.696 53.556 369.127 1.00118.37 O
ANISOU 2743 O LEU A 269 15983 15368 13624 -1340 -235 428 O
ATOM 2744 CB LEU A 269 -91.135 53.764 365.923 1.00105.34 C
ANISOU 2744 CB LEU A 269 13899 13940 12187 -908 -277 538 C
ATOM 2745 CG LEU A 269 -92.090 54.606 365.016 1.00109.58 C
ANISOU 2745 CG LEU A 269 14295 14517 12823 -863 -205 421 C
ATOM 2746 CD1 LEU A 269 -91.695 56.072 364.928 1.00109.68 C
ANISOU 2746 CD1 LEU A 269 14234 14557 12882 -873 -258 470 C
ATOM 2747 CD2 LEU A 269 -92.172 54.027 363.599 1.00110.51 C
ANISOU 2747 CD2 LEU A 269 14301 14693 12993 -685 -190 431 C
ATOM 2748 N LEU A 270 -89.694 52.590 368.614 1.00119.32 N
ANISOU 2748 N LEU A 270 16090 15548 13698 -1083 -440 680 N
ATOM 2749 CA LEU A 270 -89.645 51.591 369.692 1.00122.07 C
ANISOU 2749 CA LEU A 270 16731 15758 13892 -1164 -472 675 C
ATOM 2750 C LEU A 270 -89.814 52.150 371.126 1.00130.84 C
ANISOU 2750 C LEU A 270 17994 16781 14938 -1385 -467 646 C
ATOM 2751 O LEU A 270 -90.549 51.487 371.852 1.00130.84 O
ANISOU 2751 O LEU A 270 18243 16647 14823 -1541 -397 554 O
ATOM 2752 CB LEU A 270 -88.397 50.699 369.613 1.00122.97 C
ANISOU 2752 CB LEU A 270 16909 15891 13922 -962 -633 802 C
ATOM 2753 CG LEU A 270 -88.460 49.572 368.570 1.00127.66 C
ANISOU 2753 CG LEU A 270 17533 16479 14494 -776 -629 797 C
ATOM 2754 CD1 LEU A 270 -87.106 48.938 368.377 1.00129.05 C
ANISOU 2754 CD1 LEU A 270 17685 16738 14611 -519 -807 911 C
ATOM 2755 CD2 LEU A 270 -89.485 48.508 368.943 1.00130.38 C
ANISOU 2755 CD2 LEU A 270 18208 16629 14700 -905 -543 694 C
ATOM 2756 N PRO A 271 -89.258 53.327 371.565 1.00131.73 N
ANISOU 2756 N PRO A 271 17995 16957 15101 -1437 -523 709 N
ATOM 2757 CA PRO A 271 -89.505 53.800 372.948 1.00134.11 C
ANISOU 2757 CA PRO A 271 18465 17161 15331 -1654 -511 673 C
ATOM 2758 C PRO A 271 -90.973 53.908 373.397 1.00144.63 C
ANISOU 2758 C PRO A 271 19897 18411 16643 -1855 -341 486 C
ATOM 2759 O PRO A 271 -91.218 54.144 374.582 1.00145.65 O
ANISOU 2759 O PRO A 271 20206 18449 16687 -2048 -318 440 O
ATOM 2760 CB PRO A 271 -88.812 55.168 372.982 1.00135.02 C
ANISOU 2760 CB PRO A 271 18401 17377 15524 -1667 -574 754 C
ATOM 2761 CG PRO A 271 -87.723 55.043 372.008 1.00138.69 C
ANISOU 2761 CG PRO A 271 18672 17989 16034 -1467 -675 873 C
ATOM 2762 CD PRO A 271 -88.324 54.244 370.881 1.00133.45 C
ANISOU 2762 CD PRO A 271 17958 17332 15415 -1329 -601 815 C
ATOM 2763 N TYR A 272 -91.940 53.721 372.473 1.00144.83 N
ANISOU 2763 N TYR A 272 19801 18490 16738 -1813 -224 363 N
ATOM 2764 CA TYR A 272 -93.371 53.711 372.771 1.00146.78 C
ANISOU 2764 CA TYR A 272 20087 18724 16957 -1986 -57 144 C
ATOM 2765 C TYR A 272 -93.890 52.271 372.960 1.00154.97 C
ANISOU 2765 C TYR A 272 21357 19675 17850 -2098 19 66 C
ATOM 2766 O TYR A 272 -94.742 52.051 373.819 1.00155.47 O
ANISOU 2766 O TYR A 272 21577 19691 17805 -2341 136 -88 O
ATOM 2767 CB TYR A 272 -94.176 54.492 371.710 1.00147.40 C
ANISOU 2767 CB TYR A 272 19902 18931 17174 -1877 16 26 C
ATOM 2768 CG TYR A 272 -93.703 55.919 371.510 1.00148.97 C
ANISOU 2768 CG TYR A 272 19946 19178 17476 -1782 -64 100 C
ATOM 2769 CD1 TYR A 272 -93.548 56.784 372.593 1.00151.46 C
ANISOU 2769 CD1 TYR A 272 20341 19446 17760 -1910 -95 118 C
ATOM 2770 CD2 TYR A 272 -93.417 56.409 370.238 1.00148.95 C
ANISOU 2770 CD2 TYR A 272 19754 19257 17585 -1585 -104 149 C
ATOM 2771 CE1 TYR A 272 -93.096 58.092 372.418 1.00152.13 C
ANISOU 2771 CE1 TYR A 272 20335 19556 17911 -1849 -169 188 C
ATOM 2772 CE2 TYR A 272 -92.976 57.721 370.049 1.00149.52 C
ANISOU 2772 CE2 TYR A 272 19746 19349 17716 -1532 -176 215 C
ATOM 2773 CZ TYR A 272 -92.818 58.559 371.143 1.00157.12 C
ANISOU 2773 CZ TYR A 272 20807 20257 18636 -1668 -208 235 C
ATOM 2774 OH TYR A 272 -92.386 59.852 370.973 1.00157.23 O
ANISOU 2774 OH TYR A 272 20790 20271 18678 -1642 -279 300 O
ATOM 2775 N ILE A 273 -93.341 51.295 372.201 1.00154.37 N
ANISOU 2775 N ILE A 273 21328 19574 17750 -1935 -47 166 N
ATOM 2776 CA ILE A 273 -93.720 49.873 372.279 1.00156.77 C
ANISOU 2776 CA ILE A 273 21913 19764 17889 -2027 4 113 C
ATOM 2777 C ILE A 273 -92.982 49.146 373.433 1.00165.55 C
ANISOU 2777 C ILE A 273 23398 20691 18814 -2102 -107 215 C
ATOM 2778 O ILE A 273 -93.635 48.523 374.274 1.00166.77 O
ANISOU 2778 O ILE A 273 23857 20718 18791 -2359 -21 111 O
ATOM 2779 CB ILE A 273 -93.570 49.143 370.905 1.00159.48 C
ANISOU 2779 CB ILE A 273 22173 20149 18274 -1812 -14 153 C
ATOM 2780 CG1 ILE A 273 -94.307 49.908 369.780 1.00158.81 C
ANISOU 2780 CG1 ILE A 273 21731 20239 18370 -1721 75 56 C
ATOM 2781 CG2 ILE A 273 -94.061 47.684 370.987 1.00161.31 C
ANISOU 2781 CG2 ILE A 273 22738 20245 18307 -1947 55 77 C
ATOM 2782 CD1 ILE A 273 -93.769 49.670 368.365 1.00166.40 C
ANISOU 2782 CD1 ILE A 273 22534 21266 19423 -1452 16 150 C
ATOM 2783 N ASN A 274 -91.633 49.217 373.459 1.00164.20 N
ANISOU 2783 N ASN A 274 23205 20518 18664 -1885 -301 403 N
ATOM 2784 CA ASN A 274 -90.796 48.590 374.491 1.00166.29 C
ANISOU 2784 CA ASN A 274 23799 20628 18756 -1883 -452 503 C
ATOM 2785 C ASN A 274 -89.807 49.632 375.073 1.00171.82 C
ANISOU 2785 C ASN A 274 24342 21408 19533 -1829 -580 615 C
ATOM 2786 O ASN A 274 -88.674 49.735 374.589 1.00171.30 O
ANISOU 2786 O ASN A 274 24099 21457 19530 -1582 -730 742 O
ATOM 2787 CB ASN A 274 -90.059 47.362 373.931 1.00167.99 C
ANISOU 2787 CB ASN A 274 24180 20778 18870 -1629 -593 597 C
ATOM 2788 CG ASN A 274 -90.955 46.256 373.438 1.00190.39 C
ANISOU 2788 CG ASN A 274 27259 23498 21584 -1709 -483 499 C
ATOM 2789 OD1 ASN A 274 -91.438 45.420 374.209 1.00185.39 O
ANISOU 2789 OD1 ASN A 274 27052 22660 20728 -1914 -450 439 O
ATOM 2790 ND2 ASN A 274 -91.153 46.198 372.130 1.00180.64 N
ANISOU 2790 ND2 ASN A 274 25782 22382 20470 -1561 -428 483 N
ATOM 2791 N PRO A 275 -90.222 50.433 376.091 1.00169.86 N
ANISOU 2791 N PRO A 275 24146 21121 19271 -2067 -518 560 N
ATOM 2792 CA PRO A 275 -89.320 51.473 376.630 1.00170.36 C
ANISOU 2792 CA PRO A 275 24071 21259 19398 -2038 -635 665 C
ATOM 2793 C PRO A 275 -88.056 50.963 377.338 1.00178.34 C
ANISOU 2793 C PRO A 275 25276 22208 20276 -1923 -851 795 C
ATOM 2794 O PRO A 275 -87.024 51.639 377.290 1.00177.85 O
ANISOU 2794 O PRO A 275 25008 22287 20281 -1800 -981 899 O
ATOM 2795 CB PRO A 275 -90.223 52.276 377.579 1.00171.80 C
ANISOU 2795 CB PRO A 275 24305 21395 19578 -2327 -499 549 C
ATOM 2796 CG PRO A 275 -91.630 51.892 377.214 1.00175.62 C
ANISOU 2796 CG PRO A 275 24840 21852 20037 -2478 -298 362 C
ATOM 2797 CD PRO A 275 -91.535 50.475 376.764 1.00171.70 C
ANISOU 2797 CD PRO A 275 24547 21267 19425 -2382 -333 386 C
ATOM 2798 N ASP A 276 -88.134 49.781 377.985 1.00178.24 N
ANISOU 2798 N ASP A 276 25675 21991 20056 -1966 -894 776 N
ATOM 2799 CA ASP A 276 -87.020 49.163 378.722 1.00180.46 C
ANISOU 2799 CA ASP A 276 26215 22180 20171 -1828 -1122 875 C
ATOM 2800 C ASP A 276 -86.017 48.410 377.826 1.00185.80 C
ANISOU 2800 C ASP A 276 26808 22952 20836 -1453 -1301 958 C
ATOM 2801 O ASP A 276 -84.850 48.279 378.212 1.00186.70 O
ANISOU 2801 O ASP A 276 26931 23125 20883 -1258 -1518 1039 O
ATOM 2802 CB ASP A 276 -87.546 48.223 379.830 1.00184.09 C
ANISOU 2802 CB ASP A 276 27223 22347 20377 -2029 -1108 815 C
ATOM 2803 CG ASP A 276 -88.364 48.888 380.926 1.00194.75 C
ANISOU 2803 CG ASP A 276 28699 23605 21691 -2400 -959 727 C
ATOM 2804 OD1 ASP A 276 -89.459 48.374 381.243 1.00195.97 O
ANISOU 2804 OD1 ASP A 276 29137 23607 21716 -2661 -798 604 O
ATOM 2805 OD2 ASP A 276 -87.884 49.892 381.503 1.00200.43 O
ANISOU 2805 OD2 ASP A 276 29254 24408 22491 -2443 -1006 775 O
ATOM 2806 N LEU A 277 -86.473 47.905 376.651 1.00181.97 N
ANISOU 2806 N LEU A 277 26240 22497 20405 -1347 -1215 922 N
ATOM 2807 CA LEU A 277 -85.679 47.125 375.687 1.00182.31 C
ANISOU 2807 CA LEU A 277 26210 22626 20432 -993 -1356 978 C
ATOM 2808 C LEU A 277 -84.416 47.819 375.169 1.00185.93 C
ANISOU 2808 C LEU A 277 26237 23382 21025 -754 -1490 1062 C
ATOM 2809 O LEU A 277 -83.420 47.140 374.910 1.00187.06 O
ANISOU 2809 O LEU A 277 26381 23605 21087 -445 -1683 1104 O
ATOM 2810 CB LEU A 277 -86.543 46.673 374.506 1.00181.29 C
ANISOU 2810 CB LEU A 277 26029 22489 20364 -980 -1199 916 C
ATOM 2811 N TYR A 278 -84.458 49.156 375.011 1.00180.62 N
ANISOU 2811 N TYR A 278 25212 22882 20534 -898 -1392 1072 N
ATOM 2812 CA TYR A 278 -83.326 49.939 374.515 1.00180.06 C
ANISOU 2812 CA TYR A 278 24738 23104 20571 -755 -1487 1140 C
ATOM 2813 C TYR A 278 -82.228 50.153 375.578 1.00184.77 C
ANISOU 2813 C TYR A 278 25362 23775 21067 -719 -1683 1191 C
ATOM 2814 O TYR A 278 -81.161 49.548 375.471 1.00185.84 O
ANISOU 2814 O TYR A 278 25423 24061 21126 -442 -1874 1216 O
ATOM 2815 CB TYR A 278 -83.803 51.270 373.902 1.00179.34 C
ANISOU 2815 CB TYR A 278 24330 23136 20675 -933 -1317 1130 C
ATOM 2816 N LEU A 279 -82.516 50.971 376.618 1.00180.42 N
ANISOU 2816 N LEU A 279 24922 23125 20503 -984 -1642 1190 N
ATOM 2817 CA LEU A 279 -81.626 51.372 377.722 1.00181.05 C
ANISOU 2817 CA LEU A 279 25034 23261 20496 -1015 -1804 1233 C
ATOM 2818 C LEU A 279 -80.743 50.265 378.340 1.00185.45 C
ANISOU 2818 C LEU A 279 25814 23792 20855 -747 -2058 1245 C
ATOM 2819 O LEU A 279 -79.652 50.576 378.824 1.00186.52 O
ANISOU 2819 O LEU A 279 25790 24131 20949 -648 -2232 1273 O
ATOM 2820 CB LEU A 279 -82.445 52.045 378.833 1.00180.71 C
ANISOU 2820 CB LEU A 279 25219 23011 20432 -1347 -1697 1211 C
ATOM 2821 N LYS A 280 -81.209 48.998 378.329 1.00180.83 N
ANISOU 2821 N LYS A 280 25613 22963 20130 -634 -2088 1213 N
ATOM 2822 CA LYS A 280 -80.507 47.853 378.919 1.00182.20 C
ANISOU 2822 CA LYS A 280 26114 23038 20076 -359 -2342 1212 C
ATOM 2823 C LYS A 280 -79.171 47.490 378.235 1.00184.57 C
ANISOU 2823 C LYS A 280 26122 23646 20360 56 -2558 1215 C
ATOM 2824 O LYS A 280 -78.117 47.667 378.850 1.00186.03 O
ANISOU 2824 O LYS A 280 26214 24003 20467 193 -2765 1218 O
ATOM 2825 CB LYS A 280 -81.434 46.629 378.997 1.00185.48 C
ANISOU 2825 CB LYS A 280 27050 23096 20327 -371 -2299 1173 C
ATOM 2826 N LYS A 281 -79.215 46.979 376.981 1.00177.83 N
ANISOU 2826 N LYS A 281 25119 22880 19568 255 -2511 1197 N
ATOM 2827 CA LYS A 281 -78.045 46.536 376.210 1.00177.71 C
ANISOU 2827 CA LYS A 281 24826 23167 19529 661 -2694 1175 C
ATOM 2828 C LYS A 281 -77.083 47.674 375.803 1.00177.97 C
ANISOU 2828 C LYS A 281 24274 23645 19701 648 -2707 1180 C
ATOM 2829 O LYS A 281 -77.280 48.823 376.211 1.00176.44 O
ANISOU 2829 O LYS A 281 23921 23496 19621 319 -2577 1215 O
ATOM 2830 CB LYS A 281 -78.503 45.729 374.981 1.00179.49 C
ANISOU 2830 CB LYS A 281 25062 23343 19792 822 -2603 1156 C
ATOM 2831 N PHE A 282 -76.032 47.348 375.011 1.00172.91 N
ANISOU 2831 N PHE A 282 23327 23341 19029 996 -2864 1133 N
ATOM 2832 CA PHE A 282 -75.062 48.325 374.506 1.00171.17 C
ANISOU 2832 CA PHE A 282 22542 23588 18905 973 -2870 1114 C
ATOM 2833 C PHE A 282 -75.627 48.982 373.228 1.00167.58 C
ANISOU 2833 C PHE A 282 21789 23230 18655 794 -2615 1142 C
ATOM 2834 O PHE A 282 -75.193 48.689 372.107 1.00167.27 O
ANISOU 2834 O PHE A 282 21480 23428 18646 1008 -2619 1103 O
ATOM 2835 CB PHE A 282 -73.681 47.680 374.282 1.00176.01 C
ANISOU 2835 CB PHE A 282 22938 24557 19380 1414 -3139 1018 C
ATOM 2836 N ILE A 283 -76.630 49.859 373.423 1.00157.70 N
ANISOU 2836 N ILE A 283 20611 21777 17530 412 -2399 1200 N
ATOM 2837 CA ILE A 283 -77.323 50.581 372.356 1.00153.24 C
ANISOU 2837 CA ILE A 283 19840 21238 17145 220 -2164 1225 C
ATOM 2838 C ILE A 283 -76.504 51.728 371.767 1.00151.85 C
ANISOU 2838 C ILE A 283 19201 21452 17044 101 -2128 1228 C
ATOM 2839 O ILE A 283 -76.932 52.289 370.762 1.00150.60 O
ANISOU 2839 O ILE A 283 18874 21339 17010 -10 -1962 1243 O
ATOM 2840 CB ILE A 283 -78.748 51.063 372.754 1.00154.33 C
ANISOU 2840 CB ILE A 283 20232 21036 17372 -105 -1963 1256 C
ATOM 2841 CG1 ILE A 283 -78.805 51.643 374.191 1.00155.26 C
ANISOU 2841 CG1 ILE A 283 20537 21026 17429 -334 -2003 1276 C
ATOM 2842 CG2 ILE A 283 -79.779 49.964 372.538 1.00154.44 C
ANISOU 2842 CG2 ILE A 283 20574 20742 17363 -22 -1892 1232 C
ATOM 2843 CD1 ILE A 283 -78.618 53.161 374.278 1.00162.78 C
ANISOU 2843 CD1 ILE A 283 21238 22141 18470 -619 -1924 1309 C
ATOM 2844 N GLN A 284 -75.357 52.094 372.371 1.00145.34 N
ANISOU 2844 N GLN A 284 18188 20905 16129 104 -2279 1206 N
ATOM 2845 CA GLN A 284 -74.523 53.167 371.834 1.00143.52 C
ANISOU 2845 CA GLN A 284 17530 21071 15930 -57 -2240 1193 C
ATOM 2846 C GLN A 284 -73.869 52.773 370.508 1.00143.11 C
ANISOU 2846 C GLN A 284 17148 21343 15884 173 -2247 1133 C
ATOM 2847 O GLN A 284 -73.816 53.597 369.602 1.00141.28 O
ANISOU 2847 O GLN A 284 16665 21287 15728 -16 -2104 1143 O
ATOM 2848 CB GLN A 284 -73.493 53.654 372.852 1.00146.97 C
ANISOU 2848 CB GLN A 284 17843 21748 16252 -137 -2396 1167 C
ATOM 2849 CG GLN A 284 -73.776 55.083 373.308 1.00159.95 C
ANISOU 2849 CG GLN A 284 19562 23267 17944 -564 -2276 1236 C
ATOM 2850 CD GLN A 284 -72.556 55.802 373.835 1.00178.93 C
ANISOU 2850 CD GLN A 284 21686 26044 20257 -742 -2361 1207 C
ATOM 2851 OE1 GLN A 284 -71.447 55.710 373.287 1.00173.77 O
ANISOU 2851 OE1 GLN A 284 20662 25831 19530 -628 -2447 1124 O
ATOM 2852 NE2 GLN A 284 -72.750 56.586 374.883 1.00171.51 N
ANISOU 2852 NE2 GLN A 284 20904 24952 19310 -1047 -2328 1261 N
ATOM 2853 N GLN A 285 -73.416 51.507 370.384 1.00138.37 N
ANISOU 2853 N GLN A 285 16587 20797 15190 583 -2413 1067 N
ATOM 2854 CA GLN A 285 -72.814 50.958 369.161 1.00137.56 C
ANISOU 2854 CA GLN A 285 16200 20989 15078 859 -2436 994 C
ATOM 2855 C GLN A 285 -73.901 50.681 368.120 1.00135.77 C
ANISOU 2855 C GLN A 285 16102 20504 14980 849 -2249 1045 C
ATOM 2856 O GLN A 285 -73.624 50.718 366.920 1.00135.55 O
ANISOU 2856 O GLN A 285 15799 20707 14998 907 -2174 1014 O
ATOM 2857 CB GLN A 285 -72.000 49.688 369.471 1.00141.38 C
ANISOU 2857 CB GLN A 285 16737 21584 15396 1336 -2702 896 C
ATOM 2858 CG GLN A 285 -70.476 49.887 369.456 1.00153.51 C
ANISOU 2858 CG GLN A 285 17826 23687 16814 1481 -2872 766 C
ATOM 2859 CD GLN A 285 -69.926 50.820 370.521 1.00170.36 C
ANISOU 2859 CD GLN A 285 19853 25974 18902 1199 -2922 767 C
ATOM 2860 OE1 GLN A 285 -70.483 50.979 371.618 1.00164.88 O
ANISOU 2860 OE1 GLN A 285 19506 24943 18199 1060 -2948 843 O
ATOM 2861 NE2 GLN A 285 -68.790 51.437 370.227 1.00162.44 N
ANISOU 2861 NE2 GLN A 285 18367 25503 17851 1099 -2936 672 N
ATOM 2862 N VAL A 286 -75.142 50.420 368.595 1.00127.72 N
ANISOU 2862 N VAL A 286 15496 19023 14009 757 -2170 1111 N
ATOM 2863 CA VAL A 286 -76.349 50.196 367.786 1.00123.73 C
ANISOU 2863 CA VAL A 286 15150 18243 13620 709 -1989 1149 C
ATOM 2864 C VAL A 286 -76.746 51.549 367.176 1.00122.49 C
ANISOU 2864 C VAL A 286 14792 18144 13603 368 -1788 1191 C
ATOM 2865 O VAL A 286 -76.851 51.656 365.956 1.00121.23 O
ANISOU 2865 O VAL A 286 14455 18090 13518 392 -1685 1186 O
ATOM 2866 CB VAL A 286 -77.501 49.568 368.628 1.00126.43 C
ANISOU 2866 CB VAL A 286 15976 18124 13936 670 -1968 1175 C
ATOM 2867 CG1 VAL A 286 -78.838 49.620 367.890 1.00123.70 C
ANISOU 2867 CG1 VAL A 286 15749 17536 13717 543 -1758 1194 C
ATOM 2868 CG2 VAL A 286 -77.171 48.136 369.040 1.00128.15 C
ANISOU 2868 CG2 VAL A 286 16469 18240 13983 1021 -2170 1135 C
ATOM 2869 N TYR A 287 -76.924 52.582 368.031 1.00115.95 N
ANISOU 2869 N TYR A 287 14017 17245 12793 61 -1747 1229 N
ATOM 2870 CA TYR A 287 -77.272 53.936 367.618 1.00113.09 C
ANISOU 2870 CA TYR A 287 13541 16902 12526 -263 -1586 1267 C
ATOM 2871 C TYR A 287 -76.225 54.536 366.685 1.00114.37 C
ANISOU 2871 C TYR A 287 13320 17468 12667 -313 -1576 1247 C
ATOM 2872 O TYR A 287 -76.614 55.174 365.717 1.00113.54 O
ANISOU 2872 O TYR A 287 13143 17359 12637 -453 -1435 1267 O
ATOM 2873 CB TYR A 287 -77.572 54.863 368.817 1.00114.11 C
ANISOU 2873 CB TYR A 287 13835 16876 12647 -552 -1572 1303 C
ATOM 2874 CG TYR A 287 -77.965 56.265 368.397 1.00115.50 C
ANISOU 2874 CG TYR A 287 13956 17035 12893 -864 -1425 1337 C
ATOM 2875 CD1 TYR A 287 -79.084 56.488 367.595 1.00116.27 C
ANISOU 2875 CD1 TYR A 287 14150 16927 13101 -904 -1275 1340 C
ATOM 2876 CD2 TYR A 287 -77.185 57.362 368.745 1.00117.21 C
ANISOU 2876 CD2 TYR A 287 14040 17447 13046 -1110 -1448 1357 C
ATOM 2877 CE1 TYR A 287 -79.420 57.768 367.158 1.00117.59 C
ANISOU 2877 CE1 TYR A 287 14311 17060 13307 -1150 -1168 1363 C
ATOM 2878 CE2 TYR A 287 -77.519 58.651 368.329 1.00117.69 C
ANISOU 2878 CE2 TYR A 287 14116 17461 13138 -1394 -1328 1389 C
ATOM 2879 CZ TYR A 287 -78.642 58.851 367.540 1.00127.80 C
ANISOU 2879 CZ TYR A 287 15523 18512 14522 -1396 -1196 1392 C
ATOM 2880 OH TYR A 287 -78.974 60.119 367.111 1.00132.33 O
ANISOU 2880 OH TYR A 287 16159 19018 15103 -1639 -1102 1416 O
ATOM 2881 N LEU A 288 -74.920 54.295 366.930 1.00109.79 N
ANISOU 2881 N LEU A 288 12500 17246 11971 -195 -1727 1192 N
ATOM 2882 CA LEU A 288 -73.858 54.804 366.054 1.00109.74 C
ANISOU 2882 CA LEU A 288 12098 17682 11916 -265 -1709 1143 C
ATOM 2883 C LEU A 288 -73.871 54.149 364.676 1.00113.02 C
ANISOU 2883 C LEU A 288 12370 18201 12373 -47 -1652 1108 C
ATOM 2884 O LEU A 288 -73.444 54.777 363.709 1.00113.29 O
ANISOU 2884 O LEU A 288 12159 18482 12403 -202 -1554 1090 O
ATOM 2885 CB LEU A 288 -72.464 54.724 366.694 1.00112.13 C
ANISOU 2885 CB LEU A 288 12138 18395 12071 -196 -1885 1058 C
ATOM 2886 CG LEU A 288 -72.130 55.795 367.727 1.00116.25 C
ANISOU 2886 CG LEU A 288 12664 18972 12534 -535 -1903 1084 C
ATOM 2887 CD1 LEU A 288 -71.004 55.342 368.613 1.00119.26 C
ANISOU 2887 CD1 LEU A 288 12887 19652 12774 -362 -2122 994 C
ATOM 2888 CD2 LEU A 288 -71.803 57.132 367.078 1.00117.04 C
ANISOU 2888 CD2 LEU A 288 12561 19294 12616 -932 -1757 1094 C
ATOM 2889 N ALA A 289 -74.385 52.910 364.575 1.00108.62 N
ANISOU 2889 N ALA A 289 11995 17436 11838 285 -1706 1099 N
ATOM 2890 CA ALA A 289 -74.522 52.219 363.293 1.00107.94 C
ANISOU 2890 CA ALA A 289 11823 17395 11794 504 -1650 1072 C
ATOM 2891 C ALA A 289 -75.770 52.762 362.569 1.00110.12 C
ANISOU 2891 C ALA A 289 12262 17368 12210 306 -1452 1145 C
ATOM 2892 O ALA A 289 -75.668 53.156 361.408 1.00109.86 O
ANISOU 2892 O ALA A 289 12050 17478 12213 242 -1346 1139 O
ATOM 2893 CB ALA A 289 -74.635 50.719 363.509 1.00109.04 C
ANISOU 2893 CB ALA A 289 12154 17394 11881 912 -1789 1036 C
ATOM 2894 N ILE A 290 -76.926 52.838 363.287 1.00104.90 N
ANISOU 2894 N ILE A 290 11935 16308 11613 201 -1406 1197 N
ATOM 2895 CA ILE A 290 -78.233 53.336 362.818 1.00101.94 C
ANISOU 2895 CA ILE A 290 11739 15634 11360 39 -1241 1238 C
ATOM 2896 C ILE A 290 -78.162 54.814 362.364 1.00105.74 C
ANISOU 2896 C ILE A 290 12100 16205 11870 -278 -1133 1268 C
ATOM 2897 O ILE A 290 -78.717 55.155 361.319 1.00104.88 O
ANISOU 2897 O ILE A 290 11989 16028 11831 -323 -1019 1277 O
ATOM 2898 CB ILE A 290 -79.345 53.080 363.892 1.00103.78 C
ANISOU 2898 CB ILE A 290 12323 15490 11620 -9 -1232 1251 C
ATOM 2899 CG1 ILE A 290 -79.517 51.570 364.274 1.00104.87 C
ANISOU 2899 CG1 ILE A 290 12667 15485 11693 273 -1329 1222 C
ATOM 2900 CG2 ILE A 290 -80.680 53.691 363.521 1.00102.35 C
ANISOU 2900 CG2 ILE A 290 12287 15050 11551 -173 -1074 1257 C
ATOM 2901 CD1 ILE A 290 -79.480 50.488 363.160 1.00114.11 C
ANISOU 2901 CD1 ILE A 290 13802 16691 12865 559 -1331 1195 C
ATOM 2902 N MET A 291 -77.473 55.676 363.131 1.00103.67 N
ANISOU 2902 N MET A 291 11768 16086 11536 -497 -1177 1281 N
ATOM 2903 CA MET A 291 -77.298 57.084 362.781 1.00103.86 C
ANISOU 2903 CA MET A 291 11731 16190 11541 -824 -1091 1309 C
ATOM 2904 C MET A 291 -76.328 57.230 361.598 1.00108.67 C
ANISOU 2904 C MET A 291 12038 17164 12089 -846 -1060 1278 C
ATOM 2905 O MET A 291 -76.506 58.148 360.792 1.00107.28 O
ANISOU 2905 O MET A 291 11876 16976 11908 -1064 -953 1301 O
ATOM 2906 CB MET A 291 -76.854 57.912 363.988 1.00107.53 C
ANISOU 2906 CB MET A 291 12238 16689 11928 -1070 -1146 1329 C
ATOM 2907 CG MET A 291 -76.972 59.402 363.770 1.00112.42 C
ANISOU 2907 CG MET A 291 12928 17270 12516 -1426 -1053 1367 C
ATOM 2908 SD MET A 291 -76.541 60.402 365.216 1.00119.34 S
ANISOU 2908 SD MET A 291 13904 18143 13296 -1730 -1113 1396 S
ATOM 2909 CE MET A 291 -74.773 60.024 365.402 1.00118.89 C
ANISOU 2909 CE MET A 291 13456 18624 13092 -1724 -1232 1336 C
ATOM 2910 N TRP A 292 -75.328 56.312 361.473 1.00107.10 N
ANISOU 2910 N TRP A 292 11585 17283 11825 -610 -1158 1213 N
ATOM 2911 CA TRP A 292 -74.388 56.332 360.347 1.00108.58 C
ANISOU 2911 CA TRP A 292 11452 17860 11945 -609 -1124 1154 C
ATOM 2912 C TRP A 292 -75.142 56.059 359.049 1.00111.14 C
ANISOU 2912 C TRP A 292 11841 18026 12361 -507 -1011 1173 C
ATOM 2913 O TRP A 292 -74.915 56.761 358.065 1.00111.55 O
ANISOU 2913 O TRP A 292 11792 18214 12379 -699 -909 1171 O
ATOM 2914 CB TRP A 292 -73.232 55.327 360.512 1.00109.72 C
ANISOU 2914 CB TRP A 292 11308 18385 11997 -316 -1270 1052 C
ATOM 2915 CG TRP A 292 -72.186 55.487 359.445 1.00112.83 C
ANISOU 2915 CG TRP A 292 11327 19248 12297 -364 -1226 962 C
ATOM 2916 CD1 TRP A 292 -71.084 56.288 359.499 1.00118.17 C
ANISOU 2916 CD1 TRP A 292 11719 20346 12834 -640 -1219 894 C
ATOM 2917 CD2 TRP A 292 -72.220 54.943 358.115 1.00112.56 C
ANISOU 2917 CD2 TRP A 292 11175 19301 12291 -190 -1156 928 C
ATOM 2918 NE1 TRP A 292 -70.402 56.239 358.305 1.00119.07 N
ANISOU 2918 NE1 TRP A 292 11533 20829 12880 -650 -1147 806 N
ATOM 2919 CE2 TRP A 292 -71.086 55.434 357.431 1.00118.85 C
ANISOU 2919 CE2 TRP A 292 11606 20594 12958 -369 -1108 831 C
ATOM 2920 CE3 TRP A 292 -73.097 54.075 357.434 1.00111.87 C
ANISOU 2920 CE3 TRP A 292 11257 18934 12315 85 -1125 961 C
ATOM 2921 CZ2 TRP A 292 -70.802 55.087 356.103 1.00118.72 C
ANISOU 2921 CZ2 TRP A 292 11390 20794 12924 -271 -1029 768 C
ATOM 2922 CZ3 TRP A 292 -72.818 53.736 356.118 1.00113.63 C
ANISOU 2922 CZ3 TRP A 292 11290 19357 12527 193 -1056 910 C
ATOM 2923 CH2 TRP A 292 -71.678 54.231 355.470 1.00116.71 C
ANISOU 2923 CH2 TRP A 292 11318 20235 12791 24 -1010 815 C
ATOM 2924 N LEU A 293 -76.017 55.030 359.046 1.00105.95 N
ANISOU 2924 N LEU A 293 11368 17088 11802 -219 -1032 1185 N
ATOM 2925 CA LEU A 293 -76.846 54.641 357.906 1.00104.32 C
ANISOU 2925 CA LEU A 293 11245 16705 11688 -94 -937 1198 C
ATOM 2926 C LEU A 293 -77.721 55.821 357.446 1.00106.96 C
ANISOU 2926 C LEU A 293 11755 16803 12081 -366 -809 1251 C
ATOM 2927 O LEU A 293 -77.671 56.191 356.276 1.00106.72 O
ANISOU 2927 O LEU A 293 11661 16836 12050 -425 -722 1251 O
ATOM 2928 CB LEU A 293 -77.743 53.441 358.288 1.00103.17 C
ANISOU 2928 CB LEU A 293 11323 16266 11611 193 -984 1199 C
ATOM 2929 CG LEU A 293 -77.854 52.244 357.311 1.00107.73 C
ANISOU 2929 CG LEU A 293 11870 16847 12214 499 -978 1168 C
ATOM 2930 CD1 LEU A 293 -79.245 51.645 357.354 1.00105.82 C
ANISOU 2930 CD1 LEU A 293 11934 16212 12061 587 -934 1187 C
ATOM 2931 CD2 LEU A 293 -77.499 52.612 355.861 1.00109.64 C
ANISOU 2931 CD2 LEU A 293 11913 17280 12465 441 -875 1159 C
ATOM 2932 N ALA A 294 -78.503 56.413 358.378 1.00102.35 N
ANISOU 2932 N ALA A 294 11408 15948 11534 -515 -806 1286 N
ATOM 2933 CA ALA A 294 -79.394 57.551 358.150 1.00100.90 C
ANISOU 2933 CA ALA A 294 11432 15516 11388 -731 -718 1318 C
ATOM 2934 C ALA A 294 -78.657 58.731 357.513 1.00107.62 C
ANISOU 2934 C ALA A 294 12204 16552 12135 -1018 -668 1336 C
ATOM 2935 O ALA A 294 -79.111 59.278 356.503 1.00106.96 O
ANISOU 2935 O ALA A 294 12216 16364 12059 -1087 -591 1346 O
ATOM 2936 CB ALA A 294 -80.016 57.981 359.466 1.00100.77 C
ANISOU 2936 CB ALA A 294 11631 15266 11392 -838 -747 1331 C
ATOM 2937 N MET A 295 -77.501 59.089 358.084 1.00106.89 N
ANISOU 2937 N MET A 295 11947 16744 11924 -1191 -715 1330 N
ATOM 2938 CA MET A 295 -76.677 60.195 357.609 1.00108.71 C
ANISOU 2938 CA MET A 295 12103 17191 12011 -1527 -663 1334 C
ATOM 2939 C MET A 295 -75.936 59.881 356.311 1.00110.75 C
ANISOU 2939 C MET A 295 12109 17762 12210 -1500 -609 1290 C
ATOM 2940 O MET A 295 -75.529 60.815 355.626 1.00111.37 O
ANISOU 2940 O MET A 295 12199 17951 12167 -1799 -532 1293 O
ATOM 2941 CB MET A 295 -75.720 60.683 358.710 1.00113.45 C
ANISOU 2941 CB MET A 295 12604 18008 12492 -1751 -728 1327 C
ATOM 2942 CG MET A 295 -76.448 61.338 359.872 1.00117.01 C
ANISOU 2942 CG MET A 295 13351 18137 12972 -1874 -757 1377 C
ATOM 2943 SD MET A 295 -76.069 63.092 360.136 1.00124.02 S
ANISOU 2943 SD MET A 295 14407 19034 13680 -2376 -718 1414 S
ATOM 2944 CE MET A 295 -76.637 63.822 358.541 1.00120.07 C
ANISOU 2944 CE MET A 295 14115 18361 13145 -2492 -603 1435 C
ATOM 2945 N SER A 296 -75.771 58.586 355.957 1.00105.30 N
ANISOU 2945 N SER A 296 11222 17203 11584 -1157 -645 1244 N
ATOM 2946 CA SER A 296 -75.089 58.218 354.712 1.00105.72 C
ANISOU 2946 CA SER A 296 11026 17560 11583 -1102 -591 1189 C
ATOM 2947 C SER A 296 -75.964 58.472 353.463 1.00108.95 C
ANISOU 2947 C SER A 296 11622 17726 12049 -1111 -485 1227 C
ATOM 2948 O SER A 296 -75.417 58.653 352.378 1.00109.59 O
ANISOU 2948 O SER A 296 11569 18027 12045 -1218 -410 1196 O
ATOM 2949 CB SER A 296 -74.539 56.794 354.763 1.00108.08 C
ANISOU 2949 CB SER A 296 11070 18090 11905 -717 -681 1117 C
ATOM 2950 OG SER A 296 -75.532 55.783 354.812 1.00109.75 O
ANISOU 2950 OG SER A 296 11463 17980 12256 -386 -716 1145 O
ATOM 2951 N SER A 297 -77.315 58.579 353.638 1.00103.83 N
ANISOU 2951 N SER A 297 11286 16640 11525 -1026 -480 1281 N
ATOM 2952 CA SER A 297 -78.316 58.887 352.596 1.00102.21 C
ANISOU 2952 CA SER A 297 11295 16162 11378 -1009 -406 1306 C
ATOM 2953 C SER A 297 -78.007 60.232 351.902 1.00107.82 C
ANISOU 2953 C SER A 297 12130 16893 11944 -1370 -335 1328 C
ATOM 2954 O SER A 297 -78.442 60.477 350.770 1.00108.01 O
ANISOU 2954 O SER A 297 12282 16794 11961 -1378 -275 1336 O
ATOM 2955 CB SER A 297 -79.716 58.944 353.211 1.00102.32 C
ANISOU 2955 CB SER A 297 11593 15765 11520 -896 -430 1327 C
ATOM 2956 OG SER A 297 -79.930 60.116 353.983 1.00106.34 O
ANISOU 2956 OG SER A 297 12307 16123 11976 -1142 -446 1354 O
ATOM 2957 N THR A 298 -77.252 61.079 352.618 1.00105.06 N
ANISOU 2957 N THR A 298 11770 16687 11461 -1677 -348 1335 N
ATOM 2958 CA THR A 298 -76.770 62.417 352.297 1.00106.88 C
ANISOU 2958 CA THR A 298 12150 16959 11501 -2096 -292 1354 C
ATOM 2959 C THR A 298 -75.595 62.390 351.274 1.00113.97 C
ANISOU 2959 C THR A 298 12786 18275 12244 -2279 -211 1301 C
ATOM 2960 O THR A 298 -75.351 63.401 350.607 1.00115.35 O
ANISOU 2960 O THR A 298 13136 18446 12245 -2624 -137 1313 O
ATOM 2961 CB THR A 298 -76.354 63.075 353.635 1.00117.03 C
ANISOU 2961 CB THR A 298 13483 18272 12711 -2324 -346 1371 C
ATOM 2962 OG1 THR A 298 -77.413 62.967 354.580 1.00117.36 O
ANISOU 2962 OG1 THR A 298 13736 17958 12896 -2137 -412 1402 O
ATOM 2963 CG2 THR A 298 -76.008 64.498 353.510 1.00117.49 C
ANISOU 2963 CG2 THR A 298 13774 18309 12558 -2773 -301 1397 C
ATOM 2964 N MET A 299 -74.874 61.251 351.157 1.00110.79 N
ANISOU 2964 N MET A 299 11985 18229 11880 -2053 -225 1231 N
ATOM 2965 CA MET A 299 -73.719 61.148 350.262 1.00112.93 C
ANISOU 2965 CA MET A 299 11949 18957 12001 -2203 -148 1148 C
ATOM 2966 C MET A 299 -73.923 60.280 349.000 1.00116.23 C
ANISOU 2966 C MET A 299 12261 19411 12492 -1936 -97 1119 C
ATOM 2967 O MET A 299 -73.163 60.443 348.042 1.00117.47 O
ANISOU 2967 O MET A 299 12253 19876 12506 -2121 -4 1057 O
ATOM 2968 CB MET A 299 -72.478 60.667 351.040 1.00117.39 C
ANISOU 2968 CB MET A 299 12096 20013 12495 -2191 -207 1049 C
ATOM 2969 CG MET A 299 -72.468 59.178 351.346 1.00120.44 C
ANISOU 2969 CG MET A 299 12239 20493 13029 -1687 -310 1002 C
ATOM 2970 SD MET A 299 -71.010 58.664 352.273 1.00128.11 S
ANISOU 2970 SD MET A 299 12745 22039 13892 -1625 -416 864 S
ATOM 2971 CE MET A 299 -71.423 56.950 352.612 1.00123.30 C
ANISOU 2971 CE MET A 299 12069 21319 13461 -982 -558 846 C
ATOM 2972 N TYR A 300 -74.911 59.361 349.007 1.00110.27 N
ANISOU 2972 N TYR A 300 11599 18361 11939 -1529 -151 1156 N
ATOM 2973 CA TYR A 300 -75.146 58.406 347.920 1.00109.31 C
ANISOU 2973 CA TYR A 300 11382 18256 11896 -1240 -117 1130 C
ATOM 2974 C TYR A 300 -75.602 58.983 346.575 1.00113.50 C
ANISOU 2974 C TYR A 300 12129 18617 12380 -1388 -15 1162 C
ATOM 2975 O TYR A 300 -75.166 58.468 345.547 1.00114.01 O
ANISOU 2975 O TYR A 300 12012 18896 12409 -1315 47 1111 O
ATOM 2976 CB TYR A 300 -76.126 57.315 348.357 1.00107.63 C
ANISOU 2976 CB TYR A 300 11248 17762 11886 -812 -199 1157 C
ATOM 2977 CG TYR A 300 -75.621 56.480 349.511 1.00109.44 C
ANISOU 2977 CG TYR A 300 11279 18159 12143 -600 -311 1117 C
ATOM 2978 CD1 TYR A 300 -74.355 55.900 349.478 1.00113.53 C
ANISOU 2978 CD1 TYR A 300 11426 19146 12566 -510 -343 1018 C
ATOM 2979 CD2 TYR A 300 -76.419 56.241 350.624 1.00108.31 C
ANISOU 2979 CD2 TYR A 300 11328 17714 12110 -471 -392 1162 C
ATOM 2980 CE1 TYR A 300 -73.886 55.126 350.537 1.00114.57 C
ANISOU 2980 CE1 TYR A 300 11408 19418 12704 -278 -473 971 C
ATOM 2981 CE2 TYR A 300 -75.968 55.451 351.680 1.00109.72 C
ANISOU 2981 CE2 TYR A 300 11378 18015 12294 -273 -505 1127 C
ATOM 2982 CZ TYR A 300 -74.694 54.907 351.639 1.00118.50 C
ANISOU 2982 CZ TYR A 300 12147 19572 13304 -166 -556 1035 C
ATOM 2983 OH TYR A 300 -74.237 54.139 352.681 1.00118.87 O
ANISOU 2983 OH TYR A 300 12098 19728 13338 60 -695 992 O
ATOM 2984 N ASN A 301 -76.489 59.998 346.571 1.00109.49 N
ANISOU 2984 N ASN A 301 12017 17721 11865 -1565 -9 1235 N
ATOM 2985 CA ASN A 301 -77.060 60.598 345.353 1.00109.20 C
ANISOU 2985 CA ASN A 301 12266 17452 11774 -1673 56 1266 C
ATOM 2986 C ASN A 301 -76.027 60.990 344.262 1.00115.76 C
ANISOU 2986 C ASN A 301 12987 18603 12393 -1981 170 1222 C
ATOM 2987 O ASN A 301 -76.218 60.510 343.142 1.00113.82 O
ANISOU 2987 O ASN A 301 12725 18347 12173 -1845 220 1209 O
ATOM 2988 CB ASN A 301 -77.982 61.769 345.681 1.00108.03 C
ANISOU 2988 CB ASN A 301 12567 16881 11597 -1830 17 1329 C
ATOM 2989 CG ASN A 301 -79.274 61.337 346.323 1.00116.37 C
ANISOU 2989 CG ASN A 301 13762 17589 12863 -1498 -69 1348 C
ATOM 2990 OD1 ASN A 301 -79.530 60.144 346.538 1.00103.02 O
ANISOU 2990 OD1 ASN A 301 11872 15936 11336 -1168 -94 1326 O
ATOM 2991 ND2 ASN A 301 -80.117 62.304 346.649 1.00107.47 N
ANISOU 2991 ND2 ASN A 301 12996 16122 11714 -1586 -116 1377 N
ATOM 2992 N PRO A 302 -74.933 61.772 344.511 1.00116.07 N
ANISOU 2992 N PRO A 302 12934 18949 12217 -2398 222 1185 N
ATOM 2993 CA PRO A 302 -73.977 62.047 343.416 1.00119.08 C
ANISOU 2993 CA PRO A 302 13192 19669 12384 -2707 351 1119 C
ATOM 2994 C PRO A 302 -73.366 60.768 342.829 1.00124.79 C
ANISOU 2994 C PRO A 302 13460 20784 13170 -2426 385 1023 C
ATOM 2995 O PRO A 302 -73.179 60.691 341.610 1.00125.40 O
ANISOU 2995 O PRO A 302 13522 20963 13160 -2501 483 989 O
ATOM 2996 CB PRO A 302 -72.916 62.946 344.068 1.00123.55 C
ANISOU 2996 CB PRO A 302 13680 20542 12722 -3180 388 1075 C
ATOM 2997 CG PRO A 302 -73.055 62.723 345.521 1.00126.79 C
ANISOU 2997 CG PRO A 302 13996 20911 13267 -3004 269 1095 C
ATOM 2998 CD PRO A 302 -74.507 62.439 345.759 1.00118.65 C
ANISOU 2998 CD PRO A 302 13264 19348 12468 -2634 177 1192 C
ATOM 2999 N ILE A 303 -73.112 59.749 343.694 1.00121.13 N
ANISOU 2999 N ILE A 303 12664 20509 12849 -2080 295 978 N
ATOM 3000 CA ILE A 303 -72.578 58.432 343.315 1.00121.32 C
ANISOU 3000 CA ILE A 303 12284 20875 12937 -1727 288 880 C
ATOM 3001 C ILE A 303 -73.570 57.738 342.371 1.00122.64 C
ANISOU 3001 C ILE A 303 12617 20724 13257 -1399 295 933 C
ATOM 3002 O ILE A 303 -73.155 57.263 341.314 1.00123.53 O
ANISOU 3002 O ILE A 303 12552 21064 13319 -1337 370 867 O
ATOM 3003 CB ILE A 303 -72.201 57.559 344.555 1.00124.13 C
ANISOU 3003 CB ILE A 303 12354 21421 13388 -1416 156 830 C
ATOM 3004 CG1 ILE A 303 -71.132 58.261 345.432 1.00126.76 C
ANISOU 3004 CG1 ILE A 303 12482 22131 13551 -1756 149 757 C
ATOM 3005 CG2 ILE A 303 -71.750 56.140 344.142 1.00124.99 C
ANISOU 3005 CG2 ILE A 303 12119 21818 13555 -979 118 728 C
ATOM 3006 CD1 ILE A 303 -71.181 57.909 346.921 1.00130.03 C
ANISOU 3006 CD1 ILE A 303 12840 22505 14060 -1552 -1 769 C
ATOM 3007 N ILE A 304 -74.873 57.737 342.723 1.00115.68 N
ANISOU 3007 N ILE A 304 12074 19336 12545 -1217 225 1040 N
ATOM 3008 CA ILE A 304 -75.933 57.145 341.893 1.00113.34 C
ANISOU 3008 CA ILE A 304 11958 18716 12391 -927 226 1085 C
ATOM 3009 C ILE A 304 -75.999 57.823 340.502 1.00118.48 C
ANISOU 3009 C ILE A 304 12796 19303 12919 -1166 335 1096 C
ATOM 3010 O ILE A 304 -76.134 57.121 339.502 1.00117.85 O
ANISOU 3010 O ILE A 304 12656 19242 12880 -971 375 1076 O
ATOM 3011 CB ILE A 304 -77.315 57.129 342.617 1.00113.38 C
ANISOU 3011 CB ILE A 304 12265 18239 12575 -734 134 1165 C
ATOM 3012 CG1 ILE A 304 -77.238 56.396 343.972 1.00112.69 C
ANISOU 3012 CG1 ILE A 304 12023 18206 12587 -515 33 1152 C
ATOM 3013 CG2 ILE A 304 -78.411 56.501 341.730 1.00112.20 C
ANISOU 3013 CG2 ILE A 304 12275 17797 12559 -450 137 1189 C
ATOM 3014 CD1 ILE A 304 -78.193 56.904 345.011 1.00115.94 C
ANISOU 3014 CD1 ILE A 304 12706 18258 13089 -533 -35 1210 C
ATOM 3015 N TYR A 305 -75.866 59.171 340.448 1.00116.74 N
ANISOU 3015 N TYR A 305 12825 19005 12527 -1596 379 1126 N
ATOM 3016 CA TYR A 305 -75.930 59.955 339.209 1.00117.88 C
ANISOU 3016 CA TYR A 305 13237 19044 12508 -1874 470 1142 C
ATOM 3017 C TYR A 305 -74.804 59.624 338.240 1.00127.21 C
ANISOU 3017 C TYR A 305 14114 20684 13537 -2021 596 1047 C
ATOM 3018 O TYR A 305 -75.041 59.595 337.037 1.00126.59 O
ANISOU 3018 O TYR A 305 14177 20514 13408 -2043 663 1052 O
ATOM 3019 CB TYR A 305 -75.987 61.481 339.466 1.00119.43 C
ANISOU 3019 CB TYR A 305 13826 19037 12514 -2315 475 1192 C
ATOM 3020 CG TYR A 305 -77.088 61.990 340.380 1.00118.06 C
ANISOU 3020 CG TYR A 305 13985 18418 12456 -2203 353 1268 C
ATOM 3021 CD1 TYR A 305 -78.249 61.245 340.599 1.00116.59 C
ANISOU 3021 CD1 TYR A 305 13843 17938 12516 -1762 264 1294 C
ATOM 3022 CD2 TYR A 305 -76.995 63.239 340.984 1.00119.94 C
ANISOU 3022 CD2 TYR A 305 14507 18531 12534 -2554 332 1301 C
ATOM 3023 CE1 TYR A 305 -79.247 61.697 341.463 1.00114.68 C
ANISOU 3023 CE1 TYR A 305 13868 17337 12369 -1663 161 1335 C
ATOM 3024 CE2 TYR A 305 -77.994 63.708 341.836 1.00119.16 C
ANISOU 3024 CE2 TYR A 305 14702 18042 12532 -2434 219 1354 C
ATOM 3025 CZ TYR A 305 -79.118 62.933 342.074 1.00121.31 C
ANISOU 3025 CZ TYR A 305 14969 18065 13057 -1984 136 1363 C
ATOM 3026 OH TYR A 305 -80.090 63.398 342.924 1.00118.37 O
ANISOU 3026 OH TYR A 305 14855 17353 12768 -1876 34 1388 O
ATOM 3027 N CYS A 306 -73.587 59.377 338.755 1.00128.61 N
ANISOU 3027 N CYS A 306 13866 21368 13632 -2114 626 945 N
ATOM 3028 CA CYS A 306 -72.431 59.027 337.928 1.00132.23 C
ANISOU 3028 CA CYS A 306 13960 22347 13934 -2241 746 814 C
ATOM 3029 C CYS A 306 -72.529 57.622 337.363 1.00137.93 C
ANISOU 3029 C CYS A 306 14424 23167 14815 -1754 727 768 C
ATOM 3030 O CYS A 306 -72.148 57.398 336.216 1.00139.52 O
ANISOU 3030 O CYS A 306 14533 23554 14925 -1802 832 706 O
ATOM 3031 CB CYS A 306 -71.131 59.225 338.695 1.00135.45 C
ANISOU 3031 CB CYS A 306 13980 23295 14189 -2485 769 691 C
ATOM 3032 SG CYS A 306 -70.590 60.946 338.783 1.00142.25 S
ANISOU 3032 SG CYS A 306 15111 24198 14738 -3227 868 698 S
ATOM 3033 N CYS A 307 -73.043 56.681 338.160 1.00133.63 N
ANISOU 3033 N CYS A 307 13794 22489 14489 -1302 596 796 N
ATOM 3034 CA CYS A 307 -73.175 55.286 337.766 1.00133.17 C
ANISOU 3034 CA CYS A 307 13542 22485 14573 -818 556 758 C
ATOM 3035 C CYS A 307 -74.281 55.038 336.747 1.00135.71 C
ANISOU 3035 C CYS A 307 14167 22395 15001 -653 577 843 C
ATOM 3036 O CYS A 307 -74.081 54.253 335.817 1.00135.71 O
ANISOU 3036 O CYS A 307 14017 22539 15007 -448 620 789 O
ATOM 3037 CB CYS A 307 -73.336 54.399 338.995 1.00132.51 C
ANISOU 3037 CB CYS A 307 13340 22363 14646 -436 406 761 C
ATOM 3038 SG CYS A 307 -71.949 54.492 340.157 1.00139.55 S
ANISOU 3038 SG CYS A 307 13820 23794 15410 -542 353 633 S
ATOM 3039 N LEU A 308 -75.433 55.712 336.906 1.00130.72 N
ANISOU 3039 N LEU A 308 13953 21272 14442 -730 540 961 N
ATOM 3040 CA LEU A 308 -76.597 55.492 336.050 1.00128.85 C
ANISOU 3040 CA LEU A 308 14005 20636 14315 -546 535 1029 C
ATOM 3041 C LEU A 308 -76.919 56.619 335.033 1.00134.38 C
ANISOU 3041 C LEU A 308 15060 21122 14877 -876 609 1073 C
ATOM 3042 O LEU A 308 -77.923 56.507 334.319 1.00132.45 O
ANISOU 3042 O LEU A 308 15066 20544 14714 -716 590 1120 O
ATOM 3043 CB LEU A 308 -77.823 55.183 336.929 1.00126.11 C
ANISOU 3043 CB LEU A 308 13853 19889 14175 -269 414 1099 C
ATOM 3044 CG LEU A 308 -77.695 53.977 337.874 1.00130.22 C
ANISOU 3044 CG LEU A 308 14127 20528 14823 80 330 1067 C
ATOM 3045 CD1 LEU A 308 -78.805 53.969 338.897 1.00128.25 C
ANISOU 3045 CD1 LEU A 308 14092 19916 14722 207 232 1125 C
ATOM 3046 CD2 LEU A 308 -77.673 52.656 337.107 1.00132.46 C
ANISOU 3046 CD2 LEU A 308 14265 20894 15169 431 339 1027 C
ATOM 3047 N ASN A 309 -76.067 57.663 334.926 1.00133.99 N
ANISOU 3047 N ASN A 309 15045 21266 14598 -1336 689 1048 N
ATOM 3048 CA ASN A 309 -76.289 58.761 333.975 1.00135.17 C
ANISOU 3048 CA ASN A 309 15591 21201 14566 -1681 753 1086 C
ATOM 3049 C ASN A 309 -75.004 59.218 333.290 1.00145.14 C
ANISOU 3049 C ASN A 309 16708 22885 15553 -2117 907 1001 C
ATOM 3050 O ASN A 309 -74.002 59.485 333.960 1.00146.87 O
ANISOU 3050 O ASN A 309 16674 23478 15653 -2367 947 933 O
ATOM 3051 CB ASN A 309 -77.002 59.931 334.637 1.00132.35 C
ANISOU 3051 CB ASN A 309 15669 20442 14176 -1857 669 1168 C
ATOM 3052 CG ASN A 309 -78.198 60.424 333.878 1.00139.22 C
ANISOU 3052 CG ASN A 309 17020 20818 15060 -1777 613 1234 C
ATOM 3053 OD1 ASN A 309 -79.253 59.775 333.834 1.00121.90 O
ANISOU 3053 OD1 ASN A 309 14864 18373 13078 -1378 532 1256 O
ATOM 3054 ND2 ASN A 309 -78.066 61.610 333.302 1.00133.39 N
ANISOU 3054 ND2 ASN A 309 16681 19927 14076 -2163 647 1257 N
ATOM 3055 N ASP A 310 -75.049 59.310 331.945 1.00144.20 N
ANISOU 3055 N ASP A 310 16750 22716 15323 -2220 995 994 N
ATOM 3056 CA ASP A 310 -73.933 59.688 331.071 1.00148.13 C
ANISOU 3056 CA ASP A 310 17143 23598 15541 -2648 1164 901 C
ATOM 3057 C ASP A 310 -73.514 61.153 331.243 1.00153.78 C
ANISOU 3057 C ASP A 310 18181 24285 15965 -3247 1221 912 C
ATOM 3058 O ASP A 310 -72.333 61.428 331.463 1.00156.26 O
ANISOU 3058 O ASP A 310 18216 25076 16080 -3616 1331 805 O
ATOM 3059 CB ASP A 310 -74.263 59.408 329.582 1.00150.88 C
ANISOU 3059 CB ASP A 310 17663 23814 15852 -2588 1233 907 C
ATOM 3060 CG ASP A 310 -75.147 58.203 329.309 1.00164.42 C
ANISOU 3060 CG ASP A 310 19266 25356 17849 -2007 1152 937 C
ATOM 3061 OD1 ASP A 310 -74.622 57.067 329.316 1.00166.51 O
ANISOU 3061 OD1 ASP A 310 19069 25991 18206 -1742 1178 851 O
ATOM 3062 OD2 ASP A 310 -76.357 58.400 329.051 1.00169.08 O
ANISOU 3062 OD2 ASP A 310 20244 25451 18549 -1821 1058 1034 O
ATOM 3063 N ARG A 311 -74.477 62.089 331.112 1.00148.84 N
ANISOU 3063 N ARG A 311 18154 23108 15292 -3345 1141 1027 N
ATOM 3064 CA ARG A 311 -74.237 63.535 331.205 1.00150.59 C
ANISOU 3064 CA ARG A 311 18818 23188 15211 -3897 1171 1055 C
ATOM 3065 C ARG A 311 -73.772 63.977 332.593 1.00153.86 C
ANISOU 3065 C ARG A 311 19090 23762 15607 -4067 1134 1045 C
ATOM 3066 O ARG A 311 -73.007 64.939 332.684 1.00156.58 O
ANISOU 3066 O ARG A 311 19579 24262 15654 -4616 1221 1011 O
ATOM 3067 CB ARG A 311 -75.440 64.367 330.713 1.00150.11 C
ANISOU 3067 CB ARG A 311 19465 22470 15100 -3872 1060 1168 C
ATOM 3068 CG ARG A 311 -76.816 63.725 330.916 1.00157.52 C
ANISOU 3068 CG ARG A 311 20469 23008 16373 -3262 890 1236 C
ATOM 3069 CD ARG A 311 -77.692 63.798 329.669 1.00165.92 C
ANISOU 3069 CD ARG A 311 21941 23684 17416 -3111 849 1275 C
ATOM 3070 NE ARG A 311 -77.118 63.091 328.517 1.00175.68 N
ANISOU 3070 NE ARG A 311 22940 25208 18601 -3145 990 1218 N
ATOM 3071 CZ ARG A 311 -77.239 61.785 328.288 1.00188.02 C
ANISOU 3071 CZ ARG A 311 24080 26950 20408 -2731 1003 1187 C
ATOM 3072 NH1 ARG A 311 -77.903 61.011 329.140 1.00173.10 N
ANISOU 3072 NH1 ARG A 311 21963 24985 18824 -2273 889 1207 N
ATOM 3073 NH2 ARG A 311 -76.685 61.240 327.213 1.00174.15 N
ANISOU 3073 NH2 ARG A 311 22146 25450 18574 -2788 1134 1130 N
ATOM 3074 N PHE A 312 -74.193 63.260 333.663 1.00146.33 N
ANISOU 3074 N PHE A 312 17862 22787 14951 -3627 1013 1067 N
ATOM 3075 CA PHE A 312 -73.760 63.559 335.028 1.00145.65 C
ANISOU 3075 CA PHE A 312 17608 22859 14872 -3739 967 1057 C
ATOM 3076 C PHE A 312 -72.329 63.088 335.268 1.00151.77 C
ANISOU 3076 C PHE A 312 17790 24323 15554 -3914 1079 913 C
ATOM 3077 O PHE A 312 -71.548 63.839 335.861 1.00153.43 O
ANISOU 3077 O PHE A 312 17963 24768 15566 -4335 1123 870 O
ATOM 3078 CB PHE A 312 -74.721 62.979 336.084 1.00143.51 C
ANISOU 3078 CB PHE A 312 17290 22311 14925 -3233 801 1124 C
ATOM 3079 CG PHE A 312 -75.799 63.936 336.542 1.00143.01 C
ANISOU 3079 CG PHE A 312 17777 21690 14869 -3245 681 1228 C
ATOM 3080 CD1 PHE A 312 -75.501 64.988 337.401 1.00146.62 C
ANISOU 3080 CD1 PHE A 312 18438 22104 15166 -3598 659 1249 C
ATOM 3081 CD2 PHE A 312 -77.115 63.779 336.122 1.00142.12 C
ANISOU 3081 CD2 PHE A 312 17972 21114 14914 -2890 582 1288 C
ATOM 3082 CE1 PHE A 312 -76.496 65.881 337.811 1.00146.24 C
ANISOU 3082 CE1 PHE A 312 18912 21542 15110 -3579 537 1330 C
ATOM 3083 CE2 PHE A 312 -78.110 64.666 336.541 1.00143.71 C
ANISOU 3083 CE2 PHE A 312 18661 20834 15109 -2864 458 1353 C
ATOM 3084 CZ PHE A 312 -77.794 65.710 337.382 1.00143.05 C
ANISOU 3084 CZ PHE A 312 18791 20700 14863 -3197 434 1374 C
ATOM 3085 N ARG A 313 -71.973 61.864 334.789 1.00148.50 N
ANISOU 3085 N ARG A 313 16918 24244 15263 -3592 1119 826 N
ATOM 3086 CA ARG A 313 -70.620 61.319 334.964 1.00151.24 C
ANISOU 3086 CA ARG A 313 16662 25284 15520 -3679 1207 655 C
ATOM 3087 C ARG A 313 -69.574 62.108 334.170 1.00159.77 C
ANISOU 3087 C ARG A 313 17731 26742 16234 -4306 1398 542 C
ATOM 3088 O ARG A 313 -68.459 62.272 334.662 1.00162.17 O
ANISOU 3088 O ARG A 313 17664 27578 16377 -4593 1465 404 O
ATOM 3089 CB ARG A 313 -70.525 59.795 334.711 1.00150.08 C
ANISOU 3089 CB ARG A 313 16059 25377 15586 -3123 1176 581 C
ATOM 3090 CG ARG A 313 -70.673 59.305 333.277 1.00158.34 C
ANISOU 3090 CG ARG A 313 17141 26405 16617 -3022 1267 560 C
ATOM 3091 CD ARG A 313 -70.271 57.845 333.140 1.00164.87 C
ANISOU 3091 CD ARG A 313 17460 27594 17590 -2538 1247 448 C
ATOM 3092 NE ARG A 313 -71.316 56.933 333.609 1.00167.68 N
ANISOU 3092 NE ARG A 313 17888 27568 18253 -1960 1087 551 N
ATOM 3093 CZ ARG A 313 -72.240 56.377 332.830 1.00179.61 C
ANISOU 3093 CZ ARG A 313 19610 28722 19910 -1655 1064 630 C
ATOM 3094 NH1 ARG A 313 -72.254 56.621 331.525 1.00163.52 N
ANISOU 3094 NH1 ARG A 313 17737 26644 17751 -1839 1180 626 N
ATOM 3095 NH2 ARG A 313 -73.154 55.567 333.349 1.00166.68 N
ANISOU 3095 NH2 ARG A 313 18031 26774 18526 -1183 927 707 N
ATOM 3096 N LEU A 314 -69.951 62.648 332.988 1.00157.09 N
ANISOU 3096 N LEU A 314 17821 26123 15744 -4543 1482 594 N
ATOM 3097 CA LEU A 314 -69.072 63.478 332.159 1.00161.16 C
ANISOU 3097 CA LEU A 314 18439 26920 15875 -5195 1675 498 C
ATOM 3098 C LEU A 314 -68.850 64.857 332.806 1.00166.85 C
ANISOU 3098 C LEU A 314 19535 27525 16334 -5773 1689 536 C
ATOM 3099 O LEU A 314 -67.806 65.476 332.587 1.00170.00 O
ANISOU 3099 O LEU A 314 19847 28346 16400 -6367 1850 411 O
ATOM 3100 CB LEU A 314 -69.633 63.632 330.733 1.00161.25 C
ANISOU 3100 CB LEU A 314 18869 26596 15801 -5248 1739 556 C
ATOM 3101 CG LEU A 314 -69.521 62.412 329.810 1.00165.45 C
ANISOU 3101 CG LEU A 314 19018 27381 16466 -4875 1796 474 C
ATOM 3102 CD1 LEU A 314 -70.582 62.453 328.726 1.00163.70 C
ANISOU 3102 CD1 LEU A 314 19295 26610 16294 -4713 1766 597 C
ATOM 3103 CD2 LEU A 314 -68.137 62.311 329.184 1.00172.28 C
ANISOU 3103 CD2 LEU A 314 19453 28952 17054 -5281 2009 258 C
ATOM 3104 N GLY A 315 -69.830 65.302 333.597 1.00161.38 N
ANISOU 3104 N GLY A 315 19254 26280 15782 -5599 1524 696 N
ATOM 3105 CA GLY A 315 -69.800 66.560 334.338 1.00162.90 C
ANISOU 3105 CA GLY A 315 19860 26269 15766 -6050 1499 754 C
ATOM 3106 C GLY A 315 -68.844 66.535 335.517 1.00168.40 C
ANISOU 3106 C GLY A 315 20089 27461 16436 -6208 1508 655 C
ATOM 3107 O GLY A 315 -68.216 67.553 335.832 1.00170.83 O
ANISOU 3107 O GLY A 315 20573 27893 16441 -6794 1581 621 O
ATOM 3108 N PHE A 316 -68.730 65.364 336.179 1.00162.96 N
ANISOU 3108 N PHE A 316 18825 27046 16048 -5686 1426 603 N
ATOM 3109 CA PHE A 316 -67.816 65.149 337.301 1.00164.00 C
ANISOU 3109 CA PHE A 316 18449 27679 16185 -5729 1407 491 C
ATOM 3110 C PHE A 316 -66.374 65.087 336.798 1.00171.30 C
ANISOU 3110 C PHE A 316 18881 29369 16835 -6140 1591 264 C
ATOM 3111 O PHE A 316 -65.474 65.596 337.469 1.00173.36 O
ANISOU 3111 O PHE A 316 18930 30035 16905 -6533 1635 158 O
ATOM 3112 CB PHE A 316 -68.184 63.869 338.065 1.00162.88 C
ANISOU 3112 CB PHE A 316 17912 27551 16423 -5015 1249 503 C
ATOM 3113 CG PHE A 316 -69.094 64.090 339.252 1.00161.85 C
ANISOU 3113 CG PHE A 316 18053 26950 16493 -4781 1077 651 C
ATOM 3114 CD1 PHE A 316 -68.595 64.055 340.548 1.00165.60 C
ANISOU 3114 CD1 PHE A 316 18248 27677 16996 -4786 1004 606 C
ATOM 3115 CD2 PHE A 316 -70.454 64.319 339.074 1.00161.22 C
ANISOU 3115 CD2 PHE A 316 18495 26193 16568 -4545 984 819 C
ATOM 3116 CE1 PHE A 316 -69.438 64.252 341.645 1.00164.00 C
ANISOU 3116 CE1 PHE A 316 18298 27045 16970 -4581 854 736 C
ATOM 3117 CE2 PHE A 316 -71.296 64.510 340.171 1.00161.64 C
ANISOU 3117 CE2 PHE A 316 18770 25849 16797 -4331 834 930 C
ATOM 3118 CZ PHE A 316 -70.782 64.480 341.449 1.00160.23 C
ANISOU 3118 CZ PHE A 316 18324 25914 16641 -4361 776 893 C
ATOM 3119 N LYS A 317 -66.170 64.486 335.598 1.00168.54 N
ANISOU 3119 N LYS A 317 18353 29230 16454 -6062 1701 176 N
ATOM 3120 CA LYS A 317 -64.871 64.356 334.922 1.00172.37 C
ANISOU 3120 CA LYS A 317 18363 30458 16672 -6430 1894 -65 C
ATOM 3121 C LYS A 317 -64.328 65.730 334.538 1.00180.12 C
ANISOU 3121 C LYS A 317 19714 31507 17217 -7290 2068 -102 C
ATOM 3122 O LYS A 317 -63.127 65.960 334.667 1.00184.03 O
ANISOU 3122 O LYS A 317 19808 32666 17448 -7743 2202 -311 O
ATOM 3123 CB LYS A 317 -64.961 63.454 333.667 1.00174.08 C
ANISOU 3123 CB LYS A 317 18401 30779 16964 -6128 1966 -126 C
ATOM 3124 CG LYS A 317 -65.357 61.992 333.916 1.00180.31 C
ANISOU 3124 CG LYS A 317 18816 31557 18136 -5304 1812 -117 C
ATOM 3125 CD LYS A 317 -64.293 61.149 334.626 1.00191.34 C
ANISOU 3125 CD LYS A 317 19465 33660 19576 -5054 1773 -335 C
ATOM 3126 CE LYS A 317 -64.845 59.812 335.061 1.00197.18 C
ANISOU 3126 CE LYS A 317 19996 34246 20679 -4243 1587 -287 C
ATOM 3127 NZ LYS A 317 -63.872 59.047 335.884 1.00203.93 N
ANISOU 3127 NZ LYS A 317 20309 35489 21687 -3872 1497 -467 N
ATOM 3128 N HIS A 318 -65.219 66.647 334.095 1.00175.70 N
ANISOU 3128 N HIS A 318 19934 30263 16562 -7513 2056 91 N
ATOM 3129 CA HIS A 318 -64.881 68.022 333.708 1.00179.14 C
ANISOU 3129 CA HIS A 318 20902 30604 16559 -8321 2195 94 C
ATOM 3130 C HIS A 318 -64.377 68.858 334.897 1.00183.82 C
ANISOU 3130 C HIS A 318 21577 31075 17193 -8465 2160 104 C
ATOM 3131 O HIS A 318 -63.593 69.789 334.698 1.00184.18 O
ANISOU 3131 O HIS A 318 21854 30916 17210 -8690 2283 73 O
ATOM 3132 CB HIS A 318 -66.068 68.707 333.015 1.00177.97 C
ANISOU 3132 CB HIS A 318 21616 29624 16379 -8319 2130 309 C
ATOM 3133 N ALA A 319 -64.814 68.514 336.128 1.00179.22 N
ANISOU 3133 N ALA A 319 20793 30596 16705 -8284 1986 159 N
ATOM 3134 CA ALA A 319 -64.392 69.177 337.360 1.00180.28 C
ANISOU 3134 CA ALA A 319 20917 30852 16729 -8594 1945 148 C
ATOM 3135 C ALA A 319 -63.173 68.427 337.925 1.00183.88 C
ANISOU 3135 C ALA A 319 20650 31560 17657 -7985 1956 -30 C
ATOM 3136 O ALA A 319 -63.269 67.725 338.935 1.00184.79 O
ANISOU 3136 O ALA A 319 20281 32225 17704 -7938 1825 -75 O
ATOM 3137 CB ALA A 319 -65.537 69.201 338.361 1.00176.60 C
ANISOU 3137 CB ALA A 319 20776 29751 16574 -8116 1715 358 C
ATOM 3138 N PHE A 320 -62.028 68.549 337.215 1.00182.03 N
ANISOU 3138 N PHE A 320 20233 31426 17503 -7995 2126 -175 N
ATOM 3139 CA PHE A 320 -60.748 67.909 337.547 1.00182.82 C
ANISOU 3139 CA PHE A 320 19684 31900 17880 -7664 2153 -373 C
ATOM 3140 C PHE A 320 -59.553 68.670 336.960 1.00186.37 C
ANISOU 3140 C PHE A 320 20310 31861 18641 -7526 2304 -395 C
ATOM 3141 O PHE A 320 -59.558 69.021 335.773 1.00186.00 O
ANISOU 3141 O PHE A 320 20566 31584 18521 -7649 2437 -355 O
ATOM 3142 CB PHE A 320 -60.727 66.443 337.073 1.00184.31 C
ANISOU 3142 CB PHE A 320 19328 32468 18233 -7177 2123 -488 C
ATOM 3143 N ARG A 321 -58.528 68.908 337.803 1.00184.19 N
ANISOU 3143 N ARG A 321 19712 31843 18428 -7600 2301 -512 N
ATOM 3144 CA ARG A 321 -57.290 69.598 337.435 1.00200.66 C
ANISOU 3144 CA ARG A 321 22236 32331 21675 -6417 2308 -305 C
ATOM 3145 C ARG A 321 -56.065 68.826 337.923 1.00211.16 C
ANISOU 3145 C ARG A 321 23296 33031 23905 -5429 2193 -292 C
ATOM 3146 O ARG A 321 -56.135 67.616 338.139 1.00182.87 O
ANISOU 3146 O ARG A 321 18526 32040 18915 -6854 2301 -821 O
ATOM 3147 CB ARG A 321 -57.279 71.026 338.000 1.00200.74 C
ANISOU 3147 CB ARG A 321 22661 31987 21624 -6651 2306 -194 C
TER 3148 ARG A 321
HETATM 3149 C13 GBQ A1201 -85.225 63.138 361.031 1.00 93.66 C
HETATM 3150 C21 GBQ A1201 -85.653 63.260 369.418 1.00 96.24 C
HETATM 3151 C22 GBQ A1201 -84.332 63.864 368.957 1.00 94.92 C
HETATM 3152 C24 GBQ A1201 -87.723 62.196 368.917 1.00104.83 C
HETATM 3153 C01 GBQ A1201 -83.487 66.036 365.333 1.00 91.00 C
HETATM 3154 C02 GBQ A1201 -83.476 64.511 365.389 1.00 93.37 C
HETATM 3155 C03 GBQ A1201 -83.296 63.982 364.105 1.00 95.50 C
HETATM 3156 C04 GBQ A1201 -84.362 63.813 363.206 1.00 94.86 C
HETATM 3157 C05 GBQ A1201 -84.140 63.284 361.929 1.00 94.77 C
HETATM 3158 C06 GBQ A1201 -82.819 62.965 361.550 1.00 96.66 C
HETATM 3159 C07 GBQ A1201 -81.741 63.110 362.445 1.00 99.87 C
HETATM 3160 C08 GBQ A1201 -82.000 63.635 363.716 1.00 97.81 C
HETATM 3161 C09 GBQ A1201 -80.400 62.793 362.092 1.00105.55 C
HETATM 3162 C18 GBQ A1201 -84.537 62.781 366.759 1.00 94.48 C
HETATM 3163 C19 GBQ A1201 -85.948 62.168 367.136 1.00 94.73 C
HETATM 3164 C25 GBQ A1201 -88.769 63.279 369.143 1.00113.11 C
HETATM 3165 C27 GBQ A1201 -89.854 64.912 369.950 1.00116.09 C
HETATM 3166 C31 GBQ A1201 -86.772 62.102 365.963 1.00 90.34 C
HETATM 3167 C32 GBQ A1201 -87.635 63.156 365.586 1.00 87.03 C
HETATM 3168 C33 GBQ A1201 -88.435 63.065 364.449 1.00 84.98 C
HETATM 3169 C34 GBQ A1201 -88.362 61.907 363.662 1.00 87.13 C
HETATM 3170 C35 GBQ A1201 -87.500 60.849 364.003 1.00 86.58 C
HETATM 3171 C36 GBQ A1201 -86.717 60.945 365.159 1.00 88.17 C
HETATM 3172 F10 GBQ A1201 -79.691 63.976 361.912 1.00107.79 F
HETATM 3173 F11 GBQ A1201 -79.749 62.055 363.105 1.00106.20 F
HETATM 3174 F12 GBQ A1201 -80.352 62.044 360.935 1.00107.47 F
HETATM 3175 F14 GBQ A1201 -86.162 62.473 361.528 1.00 93.85 F
HETATM 3176 F15 GBQ A1201 -84.829 62.506 359.918 1.00 92.24 F
HETATM 3177 F16 GBQ A1201 -85.727 64.321 360.739 1.00 94.36 F
HETATM 3178 F37 GBQ A1201 -89.153 61.816 362.521 1.00 88.34 F
HETATM 3179 N20 GBQ A1201 -86.566 62.884 368.302 1.00 98.57 N
HETATM 3180 N26 GBQ A1201 -88.879 64.047 370.232 1.00115.51 N
HETATM 3181 N29 GBQ A1201 -90.310 64.716 368.718 1.00119.40 N
HETATM 3182 N30 GBQ A1201 -89.598 63.698 368.194 1.00118.07 N
HETATM 3183 O17 GBQ A1201 -84.679 64.054 366.032 1.00 94.62 O
HETATM 3184 O23 GBQ A1201 -83.727 62.964 367.976 1.00 95.05 O
HETATM 3185 O28 GBQ A1201 -90.279 65.785 370.697 1.00113.39 O
CONECT 628 1217
CONECT 1217 628
CONECT 3149 3157 3175 3176 3177
CONECT 3150 3151 3179
CONECT 3151 3150 3184
CONECT 3152 3164 3179
CONECT 3153 3154
CONECT 3154 3153 3155 3183
CONECT 3155 3154 3156 3160
CONECT 3156 3155 3157
CONECT 3157 3149 3156 3158
CONECT 3158 3157 3159
CONECT 3159 3158 3160 3161
CONECT 3160 3155 3159
CONECT 3161 3159 3172 3173 3174
CONECT 3162 3163 3183 3184
CONECT 3163 3162 3166 3179
CONECT 3164 3152 3180 3182
CONECT 3165 3180 3181 3185
CONECT 3166 3163 3167 3171
CONECT 3167 3166 3168
CONECT 3168 3167 3169
CONECT 3169 3168 3170 3178
CONECT 3170 3169 3171
CONECT 3171 3166 3170
CONECT 3172 3161
CONECT 3173 3161
CONECT 3174 3161
CONECT 3175 3149
CONECT 3176 3149
CONECT 3177 3149
CONECT 3178 3169
CONECT 3179 3150 3152 3163
CONECT 3180 3164 3165
CONECT 3181 3165 3182
CONECT 3182 3164 3181
CONECT 3183 3154 3162
CONECT 3184 3151 3162
CONECT 3185 3165
MASTER 356 0 1 19 2 0 4 6 3184 1 39 34
END