HEADER MEMBRANE PROTEIN 25-OCT-20 7ARO
TITLE CRYSTAL STRUCTURE OF THE NON-RIBOSE PARTIAL AGONIST LUF5833 BOUND TO
TITLE 2 THE ADENOSINE A2A RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE
COMPND 3 RECEPTOR A2A;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: CYTOCHROME B-562;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 562;
SOURCE 5 GENE: ADORA2A, ADORA2, CYBC;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS G PROTEIN-COUPLED RECEPTOR, GPCR, RECEPTOR, PARTIAL AGONIST, MEMBRANE
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.VERDON,T.AMELIA,J.VAN VELDHOVEN,M.FALSINI,R.LIU,L.HEITMAN,G.VAN
AUTHOR 2 WESTEN,E.SEGALA,R.CHENG,R.COOKE,D.VAN DER ES,A.IJZERMAN
REVDAT 2 21-APR-21 7ARO 1 JRNL
REVDAT 1 07-APR-21 7ARO 0
JRNL AUTH T.AMELIA,J.P.D.VAN VELDHOVEN,M.FALSINI,R.LIU,L.H.HEITMAN,
JRNL AUTH 2 G.J.P.VAN WESTEN,E.SEGALA,G.VERDON,R.K.Y.CHENG,R.M.COOKE,
JRNL AUTH 3 D.VAN DER ES,A.P.IJZERMAN
JRNL TITL CRYSTAL STRUCTURE AND SUBSEQUENT LIGAND DESIGN OF A
JRNL TITL 2 NONRIBOSIDE PARTIAL AGONIST BOUND TO THE ADENOSINE A 2A
JRNL TITL 3 RECEPTOR.
JRNL REF J.MED.CHEM. V. 64 3827 2021
JRNL REFN ISSN 0022-2623
JRNL PMID 33764785
JRNL DOI 10.1021/ACS.JMEDCHEM.0C01856
REMARK 2
REMARK 2 RESOLUTION. 3.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
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) : 3.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.5
REMARK 3 NUMBER OF REFLECTIONS : 7990
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 394
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.12
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.31
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 27.12
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2244
REMARK 3 BIN FREE R VALUE : 0.2655
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 19
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2932
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.23290
REMARK 3 B22 (A**2) : -8.36560
REMARK 3 B33 (A**2) : 1.13260
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) : 0.470
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.509
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.884
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3096 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4211 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1055 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 508 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3096 ; 10.000 ; 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 : 417 ; 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 : 2581 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 0.81
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.82
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.98
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|-1 - A|208 A|219 - A|305 A|1201 - A|1201 }
REMARK 3 ORIGIN FOR THE GROUP (A): 22.013 188.233 158.975
REMARK 3 T TENSOR
REMARK 3 T11: 0.0266 T22: -0.1933
REMARK 3 T33: -0.0002 T12: -0.0292
REMARK 3 T13: -0.0511 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.0944 L22: 1.5453
REMARK 3 L33: 1.8306 L12: -0.0075
REMARK 3 L13: -0.1243 L23: -0.2963
REMARK 3 S TENSOR
REMARK 3 S11: -0.0657 S12: -0.0422 S13: -0.0648
REMARK 3 S21: -0.0422 S22: 0.0302 S23: 0.1097
REMARK 3 S31: -0.0648 S32: 0.1097 S33: 0.0355
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|1001 - A|1106 }
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1505 236.372 161.072
REMARK 3 T TENSOR
REMARK 3 T11: -0.2627 T22: -0.304
REMARK 3 T33: 0.304 T12: 0.152
REMARK 3 T13: 0.0268 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 8.3155 L22: 8.3155
REMARK 3 L33: 2.5133 L12: -1.851
REMARK 3 L13: 0.1062 L23: -1.0301
REMARK 3 S TENSOR
REMARK 3 S11: 0 S12: -0.5442 S13: 0.3636
REMARK 3 S21: -0.5442 S22: 0.5442 S23: -0.2389
REMARK 3 S31: 0.3636 S32: -0.2389 S33: -0.5442
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7ARO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1292111975.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7990
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.120
REMARK 200 RESOLUTION RANGE LOW (A) : 43.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 5IU4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29-32% PEG 400, 0.1M TRI-SODIUM
REMARK 280 CITRATE PH = 5.3-5.4, 0.05M SODIUM THIOCYANATE, 2.5 % 2,5-
REMARK 280 HEXANEDIOL, LIPIDIC CUBIC PHASE, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.42650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.42650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 19.77050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.51350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.77050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.51350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.42650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.77050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.51350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.42650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.77050
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.51350
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 362.05400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 281.70600
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 -8
REMARK 465 TYR A -7
REMARK 465 LYS A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 LYS A 1042
REMARK 465 ALA A 1043
REMARK 465 THR A 1044
REMARK 465 PRO A 1045
REMARK 465 PRO A 1046
REMARK 465 LYS A 1047
REMARK 465 LEU A 1048
REMARK 465 GLU A 1049
REMARK 465 ASP A 1050
REMARK 465 LYS A 1051
REMARK 465 SER A 1052
REMARK 465 PRO A 1053
REMARK 465 ASP A 1054
REMARK 465 SER A 1055
REMARK 465 PRO A 1056
REMARK 465 GLU A 1057
REMARK 465 MET A 1058
REMARK 465 LYS A 1059
REMARK 465 ASP A 1060
REMARK 465 PHE A 1061
REMARK 465 ARG A 1062
REMARK 465 HIS A 1063
REMARK 465 HIS A 306
REMARK 465 VAL A 307
REMARK 465 LEU A 308
REMARK 465 ARG A 309
REMARK 465 GLN A 310
REMARK 465 GLN A 311
REMARK 465 GLU A 312
REMARK 465 PRO A 313
REMARK 465 PHE A 314
REMARK 465 LYS A 315
REMARK 465 ALA A 316
REMARK 465 ALA A 317
REMARK 465 ALA A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
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 TYR A1101 -61.73 -123.91
REMARK 500 ALA A 265 73.79 52.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLA A 1202
REMARK 610 OLA A 1203
REMARK 610 OLA A 1204
REMARK 610 OLA A 1205
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1207 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 52 OD1
REMARK 620 2 SER A 91 OG 119.2
REMARK 620 N 1
DBREF 7ARO A 2 208 UNP P29274 AA2AR_HUMAN 2 208
DBREF 7ARO A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
DBREF 7ARO A 219 317 UNP P29274 AA2AR_HUMAN 219 317
SEQADV 7ARO ASP A -8 UNP P29274 EXPRESSION TAG
SEQADV 7ARO TYR A -7 UNP P29274 EXPRESSION TAG
SEQADV 7ARO LYS A -6 UNP P29274 EXPRESSION TAG
SEQADV 7ARO ASP A -5 UNP P29274 EXPRESSION TAG
SEQADV 7ARO ASP A -4 UNP P29274 EXPRESSION TAG
SEQADV 7ARO ASP A -3 UNP P29274 EXPRESSION TAG
SEQADV 7ARO ASP A -2 UNP P29274 EXPRESSION TAG
SEQADV 7ARO GLY A -1 UNP P29274 EXPRESSION TAG
SEQADV 7ARO ALA A 0 UNP P29274 EXPRESSION TAG
SEQADV 7ARO PRO A 1 UNP P29274 EXPRESSION TAG
SEQADV 7ARO LEU A 54 UNP P29274 ALA 54 CONFLICT
SEQADV 7ARO ALA A 88 UNP P29274 THR 88 CONFLICT
SEQADV 7ARO ALA A 107 UNP P29274 ARG 107 CONFLICT
SEQADV 7ARO ALA A 122 UNP P29274 LYS 122 CONFLICT
SEQADV 7ARO ALA A 154 UNP P29274 ASN 154 CONFLICT
SEQADV 7ARO ALA A 202 UNP P29274 LEU 202 CONFLICT
SEQADV 7ARO TRP A 1007 UNP P0ABE7 MET 29 CONFLICT
SEQADV 7ARO ILE A 1102 UNP P0ABE7 HIS 124 CONFLICT
SEQADV 7ARO LEU A 1106 UNP P0ABE7 ARG 128 CONFLICT
SEQADV 7ARO ALA A 235 UNP P29274 LEU 235 CONFLICT
SEQADV 7ARO ALA A 239 UNP P29274 VAL 239 CONFLICT
SEQADV 7ARO ALA A 277 UNP P29274 SER 277 CONFLICT
SEQADV 7ARO ALA A 318 UNP P29274 EXPRESSION TAG
SEQADV 7ARO HIS A 319 UNP P29274 EXPRESSION TAG
SEQADV 7ARO HIS A 320 UNP P29274 EXPRESSION TAG
SEQADV 7ARO HIS A 321 UNP P29274 EXPRESSION TAG
SEQADV 7ARO HIS A 322 UNP P29274 EXPRESSION TAG
SEQADV 7ARO HIS A 323 UNP P29274 EXPRESSION TAG
SEQADV 7ARO HIS A 324 UNP P29274 EXPRESSION TAG
SEQADV 7ARO HIS A 325 UNP P29274 EXPRESSION TAG
SEQADV 7ARO HIS A 326 UNP P29274 EXPRESSION TAG
SEQADV 7ARO HIS A 327 UNP P29274 EXPRESSION TAG
SEQADV 7ARO HIS A 328 UNP P29274 EXPRESSION TAG
SEQRES 1 A 433 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE MET
SEQRES 2 A 433 GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE ALA
SEQRES 3 A 433 VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP ALA
SEQRES 4 A 433 VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN TYR
SEQRES 5 A 433 PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL GLY
SEQRES 6 A 433 VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR GLY
SEQRES 7 A 433 PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA CYS
SEQRES 8 A 433 PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER LEU
SEQRES 9 A 433 LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA ILE
SEQRES 10 A 433 PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG ALA
SEQRES 11 A 433 ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE ALA
SEQRES 12 A 433 ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS GLY
SEQRES 13 A 433 GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS GLY
SEQRES 14 A 433 GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL PRO
SEQRES 15 A 433 MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS VAL
SEQRES 16 A 433 LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU ARG
SEQRES 17 A 433 ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU GLU
SEQRES 18 A 433 ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE
SEQRES 19 A 433 GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU
SEQRES 20 A 433 THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA
SEQRES 21 A 433 THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO
SEQRES 22 A 433 GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL
SEQRES 23 A 433 GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY
SEQRES 24 A 433 LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS
SEQRES 25 A 433 THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU ARG
SEQRES 26 A 433 ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS
SEQRES 27 A 433 SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP
SEQRES 28 A 433 LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS
SEQRES 29 A 433 PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU
SEQRES 30 A 433 ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO
SEQRES 31 A 433 PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR
SEQRES 32 A 433 PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN
SEQRES 33 A 433 GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS
SEQRES 34 A 433 HIS HIS HIS HIS
HET RVZ A1201 24
HET OLA A1202 12
HET OLA A1203 11
HET OLA A1204 10
HET OLA A1205 6
HET CLR A1206 28
HET NA A1207 1
HETNAM RVZ 2-AZANYL-6-(1~{H}-IMIDAZOL-2-YLMETHYLSULFANYL)-4-
HETNAM 2 RVZ PHENYL-PYRIDINE-3,5-DICARBONITRILE
HETNAM OLA OLEIC ACID
HETNAM CLR CHOLESTEROL
HETNAM NA SODIUM ION
FORMUL 2 RVZ C17 H12 N6 S
FORMUL 3 OLA 4(C18 H34 O2)
FORMUL 7 CLR C27 H46 O
FORMUL 8 NA NA 1+
FORMUL 9 HOH *(H2 O)
HELIX 1 AA1 PRO A 1 ASN A 34 1 34
HELIX 2 AA2 SER A 35 GLN A 38 5 4
HELIX 3 AA3 ASN A 39 LEU A 58 1 20
HELIX 4 AA4 LEU A 58 SER A 67 1 10
HELIX 5 AA5 CYS A 74 ILE A 108 1 35
HELIX 6 AA6 ARG A 111 VAL A 116 1 6
HELIX 7 AA7 THR A 117 LEU A 137 1 21
HELIX 8 AA8 THR A 138 GLY A 142 5 5
HELIX 9 AA9 LYS A 150 GLN A 157 1 8
HELIX 10 AB1 LEU A 167 VAL A 172 1 6
HELIX 11 AB2 PRO A 173 PHE A 180 1 8
HELIX 12 AB3 VAL A 186 LYS A 1019 1 42
HELIX 13 AB4 ASN A 1022 GLN A 1041 1 20
HELIX 14 AB5 PHE A 1065 GLU A 1081 1 17
HELIX 15 AB6 LYS A 1083 TYR A 1101 1 19
HELIX 16 AB7 TYR A 1101 CYS A 259 1 47
HELIX 17 AB8 PRO A 266 ILE A 292 1 27
HELIX 18 AB9 ILE A 292 SER A 305 1 14
SHEET 1 AA1 2 CYS A 71 ALA A 73 0
SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72
SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.04
SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.04
SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03
LINK OD1 ASP A 52 NA NA A1207 1555 1555 2.41
LINK OG SER A 91 NA NA A1207 1555 1555 2.68
CRYST1 39.541 181.027 140.853 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.025290 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005524 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007100 0.00000
ATOM 1 N GLY A -1 20.404 157.363 141.647 1.00 94.14 N
ANISOU 1 N GLY A -1 17303 7824 10641 -479 126 -262 N
ATOM 2 CA GLY A -1 21.350 157.843 142.647 1.00 94.76 C
ANISOU 2 CA GLY A -1 17148 8043 10815 -276 235 -234 C
ATOM 3 C GLY A -1 22.696 158.245 142.074 1.00 95.19 C
ANISOU 3 C GLY A -1 17207 8125 10838 -71 365 -228 C
ATOM 4 O GLY A -1 23.686 157.533 142.250 1.00 95.26 O
ANISOU 4 O GLY A -1 17346 8073 10776 116 508 -212 O
ATOM 5 N ALA A 0 22.747 159.399 141.390 1.00 95.30 N
ANISOU 5 N ALA A 0 17075 8232 10905 -102 322 -238 N
ATOM 6 CA ALA A 0 23.970 159.924 140.781 1.00 95.76 C
ANISOU 6 CA ALA A 0 17113 8329 10943 69 445 -231 C
ATOM 7 C ALA A 0 25.054 160.173 141.827 1.00 96.15 C
ANISOU 7 C ALA A 0 16918 8527 11090 262 551 -197 C
ATOM 8 O ALA A 0 24.728 160.514 142.969 1.00 96.50 O
ANISOU 8 O ALA A 0 16719 8692 11253 225 488 -185 O
ATOM 9 CB ALA A 0 23.664 161.215 140.044 1.00 95.79 C
ANISOU 9 CB ALA A 0 16993 8409 10994 -31 359 -248 C
ATOM 10 N PRO A 1 26.355 160.035 141.452 1.00 95.85 N
ANISOU 10 N PRO A 1 16930 8485 11003 469 712 -179 N
ATOM 11 CA PRO A 1 27.445 160.285 142.422 1.00 95.53 C
ANISOU 11 CA PRO A 1 16643 8596 11057 652 805 -141 C
ATOM 12 C PRO A 1 27.257 161.568 143.236 1.00 95.01 C
ANISOU 12 C PRO A 1 16213 8730 11156 586 712 -134 C
ATOM 13 O PRO A 1 26.876 162.611 142.696 1.00 95.06 O
ANISOU 13 O PRO A 1 16111 8797 11211 468 632 -152 O
ATOM 14 CB PRO A 1 28.700 160.355 141.546 1.00 96.33 C
ANISOU 14 CB PRO A 1 16805 8694 11100 835 967 -126 C
ATOM 15 CG PRO A 1 28.369 159.571 140.338 1.00 96.78 C
ANISOU 15 CG PRO A 1 17207 8560 11004 779 986 -154 C
ATOM 16 CD PRO A 1 26.883 159.641 140.130 1.00 95.30 C
ANISOU 16 CD PRO A 1 17149 8273 10787 545 819 -188 C
ATOM 17 N PRO A 2 27.413 161.473 144.559 1.00 94.26 N
ANISOU 17 N PRO A 2 15950 8726 11140 653 712 -109 N
ATOM 18 CA PRO A 2 27.130 162.635 145.412 1.00 93.57 C
ANISOU 18 CA PRO A 2 15546 8809 11197 583 620 -103 C
ATOM 19 C PRO A 2 27.937 163.881 145.090 1.00 92.28 C
ANISOU 19 C PRO A 2 15165 8791 11105 638 654 -93 C
ATOM 20 O PRO A 2 27.444 164.990 145.298 1.00 92.55 O
ANISOU 20 O PRO A 2 15005 8931 11231 528 560 -102 O
ATOM 21 CB PRO A 2 27.394 162.112 146.826 1.00 94.65 C
ANISOU 21 CB PRO A 2 15602 8987 11373 674 638 -75 C
ATOM 22 CG PRO A 2 27.273 160.611 146.714 1.00 95.33 C
ANISOU 22 CG PRO A 2 15997 8893 11331 724 697 -75 C
ATOM 23 CD PRO A 2 27.810 160.295 145.354 1.00 93.81 C
ANISOU 23 CD PRO A 2 16001 8608 11035 792 791 -84 C
ATOM 24 N ILE A 3 29.150 163.711 144.554 1.00 90.73 N
ANISOU 24 N ILE A 3 15008 8600 10864 803 793 -74 N
ATOM 25 CA ILE A 3 29.992 164.851 144.211 1.00 89.75 C
ANISOU 25 CA ILE A 3 14684 8613 10804 849 839 -62 C
ATOM 26 C ILE A 3 29.426 165.710 143.058 1.00 88.01 C
ANISOU 26 C ILE A 3 14511 8365 10565 706 784 -94 C
ATOM 27 O ILE A 3 29.817 166.865 142.919 1.00 88.17 O
ANISOU 27 O ILE A 3 14341 8505 10655 685 777 -90 O
ATOM 28 CB ILE A 3 31.434 164.410 143.938 1.00 90.53 C
ANISOU 28 CB ILE A 3 14797 8733 10867 1066 1011 -26 C
ATOM 29 CG1 ILE A 3 32.392 165.625 143.971 1.00 91.57 C
ANISOU 29 CG1 ILE A 3 14686 9029 11079 1106 1061 -7 C
ATOM 30 CG2 ILE A 3 31.497 163.654 142.630 1.00 91.17 C
ANISOU 30 CG2 ILE A 3 15201 8635 10803 1115 1104 -39 C
ATOM 31 CD1 ILE A 3 33.821 165.344 143.688 1.00 92.97 C
ANISOU 31 CD1 ILE A 3 14788 9277 11257 1328 1224 41 C
ATOM 32 N MET A 4 28.485 165.178 142.266 1.00 86.18 N
ANISOU 32 N MET A 4 14530 7976 10239 596 730 -126 N
ATOM 33 CA MET A 4 27.886 165.937 141.168 1.00 84.82 C
ANISOU 33 CA MET A 4 14419 7769 10040 460 661 -156 C
ATOM 34 C MET A 4 26.889 167.010 141.650 1.00 82.21 C
ANISOU 34 C MET A 4 13893 7531 9813 297 499 -170 C
ATOM 35 O MET A 4 27.080 168.199 141.381 1.00 82.15 O
ANISOU 35 O MET A 4 13742 7615 9858 263 477 -172 O
ATOM 36 CB MET A 4 27.228 164.994 140.163 1.00 86.28 C
ANISOU 36 CB MET A 4 14941 7756 10083 395 647 -182 C
ATOM 37 CG MET A 4 28.178 164.025 139.555 1.00 90.03 C
ANISOU 37 CG MET A 4 15640 8125 10444 557 811 -170 C
ATOM 38 SD MET A 4 27.282 162.942 138.428 1.00 98.87 S
ANISOU 38 SD MET A 4 17180 8998 11390 448 765 -206 S
ATOM 39 CE MET A 4 26.899 164.121 137.085 1.00 98.15 C
ANISOU 39 CE MET A 4 17129 8894 11267 315 694 -235 C
ATOM 40 N GLY A 5 25.854 166.596 142.378 1.00 79.86 N
ANISOU 40 N GLY A 5 13593 7208 9542 202 394 -177 N
ATOM 41 CA GLY A 5 24.868 167.525 142.912 1.00 77.89 C
ANISOU 41 CA GLY A 5 13157 7046 9392 63 251 -185 C
ATOM 42 C GLY A 5 25.491 168.496 143.887 1.00 75.28 C
ANISOU 42 C GLY A 5 12539 6886 9178 124 267 -164 C
ATOM 43 O GLY A 5 25.170 169.689 143.870 1.00 75.07 O
ANISOU 43 O GLY A 5 12363 6944 9218 50 194 -170 O
ATOM 44 N SER A 6 26.428 167.994 144.705 1.00 73.17 N
ANISOU 44 N SER A 6 12207 6665 8929 267 363 -136 N
ATOM 45 CA SER A 6 27.124 168.857 145.635 1.00 71.77 C
ANISOU 45 CA SER A 6 11769 6648 8852 328 378 -113 C
ATOM 46 C SER A 6 28.071 169.814 144.900 1.00 70.13 C
ANISOU 46 C SER A 6 11482 6512 8652 368 442 -109 C
ATOM 47 O SER A 6 28.276 170.903 145.414 1.00 70.47 O
ANISOU 47 O SER A 6 11318 6678 8778 343 407 -102 O
ATOM 48 CB SER A 6 27.798 168.082 146.765 1.00 72.62 C
ANISOU 48 CB SER A 6 11822 6793 8979 462 442 -83 C
ATOM 49 OG SER A 6 28.464 166.914 146.327 1.00 74.29 O
ANISOU 49 OG SER A 6 12227 6902 9097 582 550 -73 O
ATOM 50 N SER A 7 28.559 169.483 143.668 1.00 68.13 N
ANISOU 50 N SER A 7 11405 6174 8307 414 531 -115 N
ATOM 51 CA SER A 7 29.375 170.425 142.874 1.00 66.45 C
ANISOU 51 CA SER A 7 11133 6020 8096 433 596 -111 C
ATOM 52 C SER A 7 28.562 171.661 142.483 1.00 64.36 C
ANISOU 52 C SER A 7 10814 5778 7863 281 480 -136 C
ATOM 53 O SER A 7 29.103 172.767 142.434 1.00 64.46 O
ANISOU 53 O SER A 7 10681 5890 7922 273 496 -129 O
ATOM 54 CB SER A 7 29.934 169.768 141.622 1.00 67.71 C
ANISOU 54 CB SER A 7 11519 6067 8140 509 719 -114 C
ATOM 55 OG SER A 7 30.931 168.829 141.985 1.00 70.42 O
ANISOU 55 OG SER A 7 11868 6420 8467 681 849 -82 O
ATOM 56 N VAL A 8 27.258 171.486 142.238 1.00 62.28 N
ANISOU 56 N VAL A 8 10661 5427 7574 160 360 -162 N
ATOM 57 CA VAL A 8 26.378 172.607 141.952 1.00 60.60 C
ANISOU 57 CA VAL A 8 10390 5239 7396 26 236 -182 C
ATOM 58 C VAL A 8 26.235 173.436 143.228 1.00 59.29 C
ANISOU 58 C VAL A 8 9969 5210 7349 7 175 -169 C
ATOM 59 O VAL A 8 26.444 174.642 143.199 1.00 59.24 O
ANISOU 59 O VAL A 8 9836 5286 7389 -24 152 -168 O
ATOM 60 CB VAL A 8 25.010 172.118 141.441 1.00 60.58 C
ANISOU 60 CB VAL A 8 10555 5119 7342 -93 118 -206 C
ATOM 61 CG1 VAL A 8 24.007 173.259 141.390 1.00 60.92 C
ANISOU 61 CG1 VAL A 8 10498 5207 7440 -216 -22 -219 C
ATOM 62 CG2 VAL A 8 25.149 171.454 140.089 1.00 60.78 C
ANISOU 62 CG2 VAL A 8 10852 5003 7239 -88 168 -222 C
ATOM 63 N TYR A 9 25.944 172.780 144.355 1.00 58.21 N
ANISOU 63 N TYR A 9 9773 5090 7253 30 156 -157 N
ATOM 64 CA TYR A 9 25.802 173.455 145.639 1.00 58.01 C
ANISOU 64 CA TYR A 9 9532 5182 7329 19 104 -144 C
ATOM 65 C TYR A 9 27.066 174.240 146.015 1.00 57.11 C
ANISOU 65 C TYR A 9 9249 5190 7261 94 174 -124 C
ATOM 66 O TYR A 9 26.973 175.413 146.364 1.00 57.47 O
ANISOU 66 O TYR A 9 9156 5317 7363 41 121 -124 O
ATOM 67 CB TYR A 9 25.444 172.443 146.745 1.00 58.37 C
ANISOU 67 CB TYR A 9 9573 5212 7392 52 100 -132 C
ATOM 68 CG TYR A 9 25.520 173.006 148.152 1.00 59.22 C
ANISOU 68 CG TYR A 9 9474 5435 7592 62 66 -115 C
ATOM 69 CD1 TYR A 9 24.648 174.000 148.574 1.00 60.16 C
ANISOU 69 CD1 TYR A 9 9486 5600 7772 -36 -34 -124 C
ATOM 70 CD2 TYR A 9 26.461 172.542 149.058 1.00 59.96 C
ANISOU 70 CD2 TYR A 9 9488 5588 7706 176 133 -89 C
ATOM 71 CE1 TYR A 9 24.688 174.494 149.872 1.00 60.89 C
ANISOU 71 CE1 TYR A 9 9414 5784 7937 -26 -60 -110 C
ATOM 72 CE2 TYR A 9 26.522 173.040 150.354 1.00 60.77 C
ANISOU 72 CE2 TYR A 9 9421 5786 7881 181 95 -74 C
ATOM 73 CZ TYR A 9 25.638 174.023 150.756 1.00 61.68 C
ANISOU 73 CZ TYR A 9 9449 5937 8050 78 2 -86 C
ATOM 74 OH TYR A 9 25.700 174.531 152.033 1.00 63.26 O
ANISOU 74 OH TYR A 9 9505 6221 8312 84 -30 -72 O
ATOM 75 N ILE A 10 28.233 173.600 145.932 1.00 55.58 N
ANISOU 75 N ILE A 10 9069 5009 7041 216 292 -103 N
ATOM 76 CA ILE A 10 29.506 174.219 146.269 1.00 54.31 C
ANISOU 76 CA ILE A 10 8743 4969 6923 290 364 -77 C
ATOM 77 C ILE A 10 29.816 175.401 145.370 1.00 53.41 C
ANISOU 77 C ILE A 10 8604 4885 6804 231 376 -86 C
ATOM 78 O ILE A 10 30.193 176.449 145.881 1.00 53.48 O
ANISOU 78 O ILE A 10 8445 5001 6874 202 354 -76 O
ATOM 79 CB ILE A 10 30.639 173.172 146.291 1.00 54.05 C
ANISOU 79 CB ILE A 10 8745 4935 6857 444 493 -49 C
ATOM 80 CG1 ILE A 10 30.397 172.183 147.431 1.00 54.68 C
ANISOU 80 CG1 ILE A 10 8821 5002 6950 504 472 -35 C
ATOM 81 CG2 ILE A 10 32.011 173.841 146.411 1.00 54.21 C
ANISOU 81 CG2 ILE A 10 8591 5086 6920 513 576 -18 C
ATOM 82 CD1 ILE A 10 31.329 171.059 147.476 1.00 56.03 C
ANISOU 82 CD1 ILE A 10 9067 5146 7077 655 583 -11 C
ATOM 83 N THR A 11 29.611 175.265 144.052 1.00 52.43 N
ANISOU 83 N THR A 11 8661 4659 6600 204 405 -105 N
ATOM 84 CA THR A 11 29.871 176.370 143.126 1.00 51.84 C
ANISOU 84 CA THR A 11 8593 4596 6506 145 420 -114 C
ATOM 85 C THR A 11 28.954 177.573 143.413 1.00 52.21 C
ANISOU 85 C THR A 11 8556 4679 6602 24 288 -131 C
ATOM 86 O THR A 11 29.402 178.729 143.409 1.00 52.26 O
ANISOU 86 O THR A 11 8454 4762 6640 -11 292 -126 O
ATOM 87 CB THR A 11 29.761 175.906 141.688 1.00 51.51 C
ANISOU 87 CB THR A 11 8788 4423 6359 142 467 -133 C
ATOM 88 OG1 THR A 11 30.590 174.759 141.504 1.00 51.99 O
ANISOU 88 OG1 THR A 11 8925 4455 6376 271 602 -114 O
ATOM 89 CG2 THR A 11 30.170 176.976 140.725 1.00 51.35 C
ANISOU 89 CG2 THR A 11 8795 4406 6308 91 496 -140 C
ATOM 90 N VAL A 12 27.675 177.297 143.703 1.00 51.84 N
ANISOU 90 N VAL A 12 8556 4578 6563 -38 174 -148 N
ATOM 91 CA VAL A 12 26.728 178.350 144.037 1.00 51.72 C
ANISOU 91 CA VAL A 12 8461 4595 6597 -133 54 -160 C
ATOM 92 C VAL A 12 27.143 179.025 145.350 1.00 51.21 C
ANISOU 92 C VAL A 12 8187 4653 6616 -116 45 -141 C
ATOM 93 O VAL A 12 27.179 180.251 145.419 1.00 51.72 O
ANISOU 93 O VAL A 12 8171 4773 6708 -165 12 -143 O
ATOM 94 CB VAL A 12 25.298 177.782 144.073 1.00 52.62 C
ANISOU 94 CB VAL A 12 8657 4633 6705 -195 -54 -176 C
ATOM 95 CG1 VAL A 12 24.332 178.732 144.775 1.00 53.40 C
ANISOU 95 CG1 VAL A 12 8634 4785 6873 -265 -167 -179 C
ATOM 96 CG2 VAL A 12 24.817 177.466 142.661 1.00 53.20 C
ANISOU 96 CG2 VAL A 12 8937 4587 6689 -241 -75 -197 C
ATOM 97 N GLU A 13 27.540 178.236 146.355 1.00 50.07 N
ANISOU 97 N GLU A 13 7974 4547 6504 -44 78 -123 N
ATOM 98 CA GLU A 13 27.985 178.786 147.627 1.00 49.54 C
ANISOU 98 CA GLU A 13 7725 4591 6507 -26 66 -104 C
ATOM 99 C GLU A 13 29.210 179.663 147.460 1.00 48.40 C
ANISOU 99 C GLU A 13 7478 4535 6375 -13 128 -88 C
ATOM 100 O GLU A 13 29.253 180.757 148.015 1.00 48.55 O
ANISOU 100 O GLU A 13 7385 4625 6436 -64 81 -86 O
ATOM 101 CB GLU A 13 28.266 177.669 148.634 1.00 52.32 C
ANISOU 101 CB GLU A 13 8046 4956 6878 58 93 -85 C
ATOM 102 CG GLU A 13 27.014 176.998 149.168 1.00 58.44 C
ANISOU 102 CG GLU A 13 8880 5667 7660 22 19 -96 C
ATOM 103 CD GLU A 13 26.286 177.710 150.293 1.00 66.26 C
ANISOU 103 CD GLU A 13 9758 6707 8712 -33 -68 -97 C
ATOM 104 OE1 GLU A 13 26.203 177.139 151.406 1.00 68.33 O
ANISOU 104 OE1 GLU A 13 9977 6987 9000 4 -74 -83 O
ATOM 105 OE2 GLU A 13 25.793 178.839 150.066 1.00 68.75 O
ANISOU 105 OE2 GLU A 13 10040 7037 9043 -107 -127 -109 O
ATOM 106 N LEU A 14 30.175 179.220 146.656 1.00 47.26 N
ANISOU 106 N LEU A 14 7380 4385 6192 48 236 -77 N
ATOM 107 CA LEU A 14 31.380 180.005 146.419 1.00 46.83 C
ANISOU 107 CA LEU A 14 7222 4420 6150 54 309 -58 C
ATOM 108 C LEU A 14 31.103 181.269 145.623 1.00 46.27 C
ANISOU 108 C LEU A 14 7190 4333 6058 -49 282 -77 C
ATOM 109 O LEU A 14 31.737 182.286 145.889 1.00 46.22 O
ANISOU 109 O LEU A 14 7068 4412 6081 -89 292 -65 O
ATOM 110 CB LEU A 14 32.474 179.177 145.761 1.00 47.01 C
ANISOU 110 CB LEU A 14 7278 4444 6139 159 447 -37 C
ATOM 111 CG LEU A 14 32.985 178.007 146.590 1.00 48.06 C
ANISOU 111 CG LEU A 14 7361 4606 6292 281 486 -11 C
ATOM 112 CD1 LEU A 14 33.914 177.133 145.770 1.00 48.31 C
ANISOU 112 CD1 LEU A 14 7469 4612 6275 398 629 8 C
ATOM 113 CD2 LEU A 14 33.622 178.479 147.895 1.00 48.49 C
ANISOU 113 CD2 LEU A 14 7201 4798 6424 293 450 17 C
ATOM 114 N ALA A 15 30.129 181.238 144.696 1.00 45.70 N
ANISOU 114 N ALA A 15 7283 4150 5932 -97 239 -105 N
ATOM 115 CA ALA A 15 29.755 182.443 143.946 1.00 45.75 C
ANISOU 115 CA ALA A 15 7343 4129 5910 -189 200 -123 C
ATOM 116 C ALA A 15 29.181 183.498 144.901 1.00 45.63 C
ANISOU 116 C ALA A 15 7219 4167 5950 -256 92 -127 C
ATOM 117 O ALA A 15 29.544 184.675 144.820 1.00 45.08 O
ANISOU 117 O ALA A 15 7107 4139 5884 -313 91 -125 O
ATOM 118 CB ALA A 15 28.741 182.097 142.863 1.00 45.79 C
ANISOU 118 CB ALA A 15 7545 4006 5846 -220 156 -149 C
ATOM 119 N ILE A 16 28.330 183.050 145.844 1.00 46.07 N
ANISOU 119 N ILE A 16 7239 4219 6045 -247 13 -130 N
ATOM 120 CA ILE A 16 27.735 183.904 146.857 1.00 46.97 C
ANISOU 120 CA ILE A 16 7259 4377 6209 -291 -78 -132 C
ATOM 121 C ILE A 16 28.828 184.468 147.757 1.00 47.69 C
ANISOU 121 C ILE A 16 7202 4577 6341 -284 -44 -110 C
ATOM 122 O ILE A 16 28.807 185.661 148.047 1.00 48.24 O
ANISOU 122 O ILE A 16 7230 4679 6421 -345 -85 -112 O
ATOM 123 CB ILE A 16 26.660 183.145 147.661 1.00 47.73 C
ANISOU 123 CB ILE A 16 7349 4448 6338 -273 -145 -135 C
ATOM 124 CG1 ILE A 16 25.481 182.781 146.757 1.00 49.05 C
ANISOU 124 CG1 ILE A 16 7652 4516 6469 -307 -202 -155 C
ATOM 125 CG2 ILE A 16 26.187 183.959 148.865 1.00 48.07 C
ANISOU 125 CG2 ILE A 16 7284 4545 6434 -299 -215 -131 C
ATOM 126 CD1 ILE A 16 24.496 181.826 147.397 1.00 50.62 C
ANISOU 126 CD1 ILE A 16 7852 4686 6695 -300 -254 -156 C
ATOM 127 N ALA A 17 29.802 183.636 148.172 1.00 47.28 N
ANISOU 127 N ALA A 17 7075 4580 6307 -212 27 -87 N
ATOM 128 CA ALA A 17 30.891 184.120 149.025 1.00 47.26 C
ANISOU 128 CA ALA A 17 6921 4691 6345 -209 48 -62 C
ATOM 129 C ALA A 17 31.706 185.217 148.337 1.00 47.05 C
ANISOU 129 C ALA A 17 6875 4702 6300 -277 92 -58 C
ATOM 130 O ALA A 17 32.056 186.199 148.987 1.00 47.72 O
ANISOU 130 O ALA A 17 6872 4851 6407 -337 56 -51 O
ATOM 131 CB ALA A 17 31.793 182.978 149.453 1.00 47.28 C
ANISOU 131 CB ALA A 17 6851 4746 6367 -107 117 -34 C
ATOM 132 N VAL A 18 31.951 185.097 147.017 1.00 45.94 N
ANISOU 132 N VAL A 18 6835 4511 6111 -276 166 -65 N
ATOM 133 CA VAL A 18 32.708 186.115 146.287 1.00 45.53 C
ANISOU 133 CA VAL A 18 6780 4485 6035 -346 219 -61 C
ATOM 134 C VAL A 18 31.983 187.464 146.346 1.00 45.91 C
ANISOU 134 C VAL A 18 6870 4504 6070 -448 128 -81 C
ATOM 135 O VAL A 18 32.579 188.495 146.670 1.00 45.94 O
ANISOU 135 O VAL A 18 6801 4571 6085 -518 124 -71 O
ATOM 136 CB VAL A 18 32.980 185.676 144.828 1.00 45.40 C
ANISOU 136 CB VAL A 18 6895 4399 5956 -322 319 -66 C
ATOM 137 CG1 VAL A 18 33.529 186.829 143.998 1.00 45.66 C
ANISOU 137 CG1 VAL A 18 6945 4448 5957 -404 376 -63 C
ATOM 138 CG2 VAL A 18 33.935 184.496 144.783 1.00 45.55 C
ANISOU 138 CG2 VAL A 18 6873 4451 5984 -210 425 -41 C
ATOM 139 N LEU A 19 30.677 187.429 146.089 1.00 45.78 N
ANISOU 139 N LEU A 19 6971 4394 6030 -453 51 -107 N
ATOM 140 CA LEU A 19 29.836 188.618 146.089 1.00 45.83 C
ANISOU 140 CA LEU A 19 7034 4360 6020 -525 -38 -125 C
ATOM 141 C LEU A 19 29.641 189.214 147.479 1.00 46.56 C
ANISOU 141 C LEU A 19 7021 4510 6159 -545 -109 -119 C
ATOM 142 O LEU A 19 29.599 190.433 147.624 1.00 46.73 O
ANISOU 142 O LEU A 19 7056 4534 6167 -612 -145 -123 O
ATOM 143 CB LEU A 19 28.490 188.260 145.480 1.00 45.30 C
ANISOU 143 CB LEU A 19 7096 4192 5925 -509 -105 -147 C
ATOM 144 CG LEU A 19 28.512 188.140 144.001 1.00 45.92 C
ANISOU 144 CG LEU A 19 7323 4192 5934 -520 -61 -158 C
ATOM 145 CD1 LEU A 19 27.355 187.329 143.512 1.00 46.23 C
ANISOU 145 CD1 LEU A 19 7467 4147 5953 -488 -111 -173 C
ATOM 146 CD2 LEU A 19 28.488 189.500 143.391 1.00 46.64 C
ANISOU 146 CD2 LEU A 19 7493 4248 5980 -591 -90 -168 C
ATOM 147 N ALA A 20 29.498 188.362 148.498 1.00 46.88 N
ANISOU 147 N ALA A 20 6977 4587 6247 -486 -127 -109 N
ATOM 148 CA ALA A 20 29.310 188.832 149.865 1.00 47.49 C
ANISOU 148 CA ALA A 20 6969 4713 6363 -498 -190 -103 C
ATOM 149 C ALA A 20 30.563 189.574 150.338 1.00 48.10 C
ANISOU 149 C ALA A 20 6948 4880 6449 -549 -162 -84 C
ATOM 150 O ALA A 20 30.456 190.641 150.935 1.00 48.34 O
ANISOU 150 O ALA A 20 6972 4921 6473 -611 -214 -86 O
ATOM 151 CB ALA A 20 29.002 187.665 150.783 1.00 47.36 C
ANISOU 151 CB ALA A 20 6897 4711 6387 -423 -204 -95 C
ATOM 152 N ILE A 21 31.745 189.044 150.016 1.00 48.13 N
ANISOU 152 N ILE A 21 6882 4944 6461 -527 -79 -63 N
ATOM 153 CA ILE A 21 32.998 189.692 150.376 1.00 48.80 C
ANISOU 153 CA ILE A 21 6855 5129 6560 -584 -52 -40 C
ATOM 154 C ILE A 21 33.182 191.009 149.616 1.00 49.76 C
ANISOU 154 C ILE A 21 7044 5225 6636 -693 -42 -50 C
ATOM 155 O ILE A 21 33.397 192.042 150.245 1.00 50.22 O
ANISOU 155 O ILE A 21 7075 5316 6692 -775 -88 -47 O
ATOM 156 CB ILE A 21 34.190 188.733 150.153 1.00 48.94 C
ANISOU 156 CB ILE A 21 6766 5225 6603 -520 44 -10 C
ATOM 157 CG1 ILE A 21 34.083 187.533 151.085 1.00 50.09 C
ANISOU 157 CG1 ILE A 21 6849 5395 6786 -412 26 3 C
ATOM 158 CG2 ILE A 21 35.515 189.460 150.335 1.00 48.95 C
ANISOU 158 CG2 ILE A 21 6639 5338 6623 -595 71 18 C
ATOM 159 CD1 ILE A 21 35.017 186.412 150.739 1.00 51.36 C
ANISOU 159 CD1 ILE A 21 6938 5611 6965 -318 121 31 C
ATOM 160 N LEU A 22 33.089 190.975 148.273 1.00 49.69 N
ANISOU 160 N LEU A 22 7142 5152 6585 -696 19 -61 N
ATOM 161 CA LEU A 22 33.300 192.149 147.442 1.00 50.04 C
ANISOU 161 CA LEU A 22 7268 5166 6579 -796 42 -68 C
ATOM 162 C LEU A 22 32.399 193.339 147.794 1.00 50.98 C
ANISOU 162 C LEU A 22 7479 5225 6668 -860 -54 -89 C
ATOM 163 O LEU A 22 32.895 194.434 148.077 1.00 51.24 O
ANISOU 163 O LEU A 22 7495 5287 6686 -954 -68 -83 O
ATOM 164 CB LEU A 22 33.150 191.770 145.968 1.00 49.85 C
ANISOU 164 CB LEU A 22 7369 5066 6505 -772 116 -79 C
ATOM 165 CG LEU A 22 34.340 191.087 145.368 1.00 50.81 C
ANISOU 165 CG LEU A 22 7419 5250 6637 -743 244 -54 C
ATOM 166 CD1 LEU A 22 33.989 190.473 144.041 1.00 51.21 C
ANISOU 166 CD1 LEU A 22 7611 5211 6638 -686 307 -67 C
ATOM 167 CD2 LEU A 22 35.461 192.060 145.196 1.00 51.23 C
ANISOU 167 CD2 LEU A 22 7426 5362 6678 -849 304 -37 C
ATOM 168 N GLY A 23 31.092 193.112 147.790 1.00 51.19 N
ANISOU 168 N GLY A 23 7596 5169 6685 -807 -121 -110 N
ATOM 169 CA GLY A 23 30.124 194.160 148.054 1.00 51.71 C
ANISOU 169 CA GLY A 23 7755 5171 6722 -840 -206 -128 C
ATOM 170 C GLY A 23 30.269 194.786 149.417 1.00 52.22 C
ANISOU 170 C GLY A 23 7748 5284 6808 -875 -259 -120 C
ATOM 171 O GLY A 23 30.215 196.008 149.543 1.00 52.04 O
ANISOU 171 O GLY A 23 7796 5234 6744 -947 -289 -126 O
ATOM 172 N ASN A 24 30.446 193.952 150.447 1.00 52.66 N
ANISOU 172 N ASN A 24 7684 5406 6920 -823 -270 -107 N
ATOM 173 CA ASN A 24 30.525 194.446 151.813 1.00 53.24 C
ANISOU 173 CA ASN A 24 7702 5518 7007 -848 -327 -100 C
ATOM 174 C ASN A 24 31.873 195.036 152.144 1.00 54.38 C
ANISOU 174 C ASN A 24 7768 5745 7149 -941 -306 -81 C
ATOM 175 O ASN A 24 31.924 195.960 152.958 1.00 54.77 O
ANISOU 175 O ASN A 24 7836 5797 7177 -1006 -359 -81 O
ATOM 176 CB ASN A 24 30.083 193.406 152.805 1.00 53.64 C
ANISOU 176 CB ASN A 24 7679 5593 7109 -760 -357 -95 C
ATOM 177 CG ASN A 24 28.601 193.186 152.684 1.00 55.82 C
ANISOU 177 CG ASN A 24 8039 5785 7384 -699 -396 -113 C
ATOM 178 OD1 ASN A 24 27.790 194.033 153.072 1.00 55.79 O
ANISOU 178 OD1 ASN A 24 8106 5733 7358 -711 -447 -123 O
ATOM 179 ND2 ASN A 24 28.219 192.072 152.083 1.00 56.86 N
ANISOU 179 ND2 ASN A 24 8172 5896 7536 -634 -372 -116 N
ATOM 180 N VAL A 25 32.957 194.618 151.451 1.00 54.67 N
ANISOU 180 N VAL A 25 7729 5844 7199 -959 -227 -64 N
ATOM 181 CA VAL A 25 34.253 195.297 151.614 1.00 55.34 C
ANISOU 181 CA VAL A 25 7731 6014 7282 -1068 -204 -42 C
ATOM 182 C VAL A 25 34.097 196.746 151.083 1.00 56.51 C
ANISOU 182 C VAL A 25 8019 6093 7361 -1184 -216 -58 C
ATOM 183 O VAL A 25 34.554 197.691 151.728 1.00 56.72 O
ANISOU 183 O VAL A 25 8041 6143 7366 -1285 -258 -52 O
ATOM 184 CB VAL A 25 35.431 194.534 150.952 1.00 55.22 C
ANISOU 184 CB VAL A 25 7597 6085 7299 -1054 -102 -15 C
ATOM 185 CG1 VAL A 25 36.604 195.463 150.658 1.00 55.47 C
ANISOU 185 CG1 VAL A 25 7576 6184 7317 -1192 -64 4 C
ATOM 186 CG2 VAL A 25 35.889 193.391 151.842 1.00 55.54 C
ANISOU 186 CG2 VAL A 25 7483 6216 7404 -959 -106 9 C
ATOM 187 N LEU A 26 33.360 196.903 149.961 1.00 56.92 N
ANISOU 187 N LEU A 26 8210 6047 7369 -1163 -189 -79 N
ATOM 188 CA LEU A 26 33.062 198.185 149.348 1.00 57.57 C
ANISOU 188 CA LEU A 26 8453 6043 7377 -1248 -199 -95 C
ATOM 189 C LEU A 26 32.229 199.086 150.283 1.00 58.10 C
ANISOU 189 C LEU A 26 8610 6052 7414 -1260 -295 -109 C
ATOM 190 O LEU A 26 32.465 200.289 150.344 1.00 58.24 O
ANISOU 190 O LEU A 26 8716 6038 7375 -1364 -311 -112 O
ATOM 191 CB LEU A 26 32.342 197.940 148.031 1.00 57.94 C
ANISOU 191 CB LEU A 26 8625 6001 7391 -1192 -166 -112 C
ATOM 192 CG LEU A 26 32.277 199.112 147.092 1.00 60.05 C
ANISOU 192 CG LEU A 26 9058 6184 7575 -1277 -149 -123 C
ATOM 193 CD1 LEU A 26 33.643 199.529 146.654 1.00 60.61 C
ANISOU 193 CD1 LEU A 26 9083 6316 7631 -1396 -62 -104 C
ATOM 194 CD2 LEU A 26 31.450 198.780 145.878 1.00 61.12 C
ANISOU 194 CD2 LEU A 26 9324 6225 7673 -1209 -137 -140 C
ATOM 195 N VAL A 27 31.296 198.505 151.045 1.00 58.22 N
ANISOU 195 N VAL A 27 8606 6051 7463 -1157 -351 -116 N
ATOM 196 CA VAL A 27 30.512 199.252 152.028 1.00 58.79 C
ANISOU 196 CA VAL A 27 8752 6075 7512 -1150 -428 -126 C
ATOM 197 C VAL A 27 31.443 199.809 153.107 1.00 60.82 C
ANISOU 197 C VAL A 27 8953 6394 7762 -1246 -454 -112 C
ATOM 198 O VAL A 27 31.387 200.997 153.393 1.00 61.25 O
ANISOU 198 O VAL A 27 9123 6396 7754 -1322 -487 -119 O
ATOM 199 CB VAL A 27 29.399 198.372 152.652 1.00 58.21 C
ANISOU 199 CB VAL A 27 8645 5987 7486 -1022 -466 -131 C
ATOM 200 CG1 VAL A 27 28.812 199.001 153.908 1.00 57.99 C
ANISOU 200 CG1 VAL A 27 8661 5931 7442 -1011 -528 -134 C
ATOM 201 CG2 VAL A 27 28.309 198.098 151.642 1.00 58.67 C
ANISOU 201 CG2 VAL A 27 8786 5969 7537 -948 -466 -145 C
ATOM 202 N CYS A 28 32.304 198.958 153.691 1.00 61.92 N
ANISOU 202 N CYS A 28 8925 6642 7961 -1242 -444 -91 N
ATOM 203 CA CYS A 28 33.217 199.364 154.755 1.00 63.24 C
ANISOU 203 CA CYS A 28 9022 6880 8126 -1332 -484 -74 C
ATOM 204 C CYS A 28 34.175 200.421 154.265 1.00 65.41 C
ANISOU 204 C CYS A 28 9333 7168 8354 -1488 -463 -68 C
ATOM 205 O CYS A 28 34.439 201.377 154.988 1.00 65.68 O
ANISOU 205 O CYS A 28 9427 7189 8341 -1588 -517 -68 O
ATOM 206 CB CYS A 28 33.964 198.160 155.319 1.00 63.03 C
ANISOU 206 CB CYS A 28 8803 6973 8174 -1284 -476 -49 C
ATOM 207 SG CYS A 28 32.906 196.932 156.121 1.00 63.22 S
ANISOU 207 SG CYS A 28 8792 6981 8248 -1115 -501 -54 S
ATOM 208 N TRP A 29 34.696 200.247 153.038 1.00 66.95 N
ANISOU 208 N TRP A 29 9500 7384 8556 -1514 -381 -62 N
ATOM 209 CA TRP A 29 35.643 201.155 152.381 1.00 69.12 C
ANISOU 209 CA TRP A 29 9799 7675 8790 -1667 -337 -52 C
ATOM 210 C TRP A 29 35.039 202.548 152.226 1.00 69.50 C
ANISOU 210 C TRP A 29 10067 7598 8741 -1746 -368 -75 C
ATOM 211 O TRP A 29 35.714 203.543 152.489 1.00 69.39 O
ANISOU 211 O TRP A 29 10094 7591 8680 -1897 -384 -68 O
ATOM 212 CB TRP A 29 35.950 200.628 150.981 1.00 70.35 C
ANISOU 212 CB TRP A 29 9930 7841 8961 -1640 -231 -47 C
ATOM 213 CG TRP A 29 37.345 200.185 150.723 1.00 72.47 C
ANISOU 213 CG TRP A 29 10012 8242 9282 -1690 -158 -13 C
ATOM 214 CD1 TRP A 29 37.888 198.979 151.050 1.00 74.01 C
ANISOU 214 CD1 TRP A 29 10022 8541 9556 -1595 -133 10 C
ATOM 215 CD2 TRP A 29 38.279 200.822 149.847 1.00 73.31 C
ANISOU 215 CD2 TRP A 29 10111 8380 9363 -1822 -77 3 C
ATOM 216 NE1 TRP A 29 39.144 198.866 150.506 1.00 74.74 N
ANISOU 216 NE1 TRP A 29 9977 8740 9680 -1656 -45 42 N
ATOM 217 CE2 TRP A 29 39.412 199.991 149.767 1.00 74.52 C
ANISOU 217 CE2 TRP A 29 10049 8673 9592 -1803 -6 39 C
ATOM 218 CE3 TRP A 29 38.298 202.048 149.180 1.00 74.06 C
ANISOU 218 CE3 TRP A 29 10363 8399 9378 -1957 -54 -7 C
ATOM 219 CZ2 TRP A 29 40.548 200.348 149.038 1.00 75.33 C
ANISOU 219 CZ2 TRP A 29 10073 8851 9699 -1917 90 67 C
ATOM 220 CZ3 TRP A 29 39.416 202.393 148.448 1.00 75.15 C
ANISOU 220 CZ3 TRP A 29 10436 8603 9514 -2081 40 18 C
ATOM 221 CH2 TRP A 29 40.531 201.557 148.397 1.00 75.39 C
ANISOU 221 CH2 TRP A 29 10234 8783 9627 -2064 112 56 C
ATOM 222 N ALA A 30 33.766 202.615 151.788 1.00 69.69 N
ANISOU 222 N ALA A 30 10237 7508 8734 -1643 -379 -100 N
ATOM 223 CA ALA A 30 33.059 203.871 151.586 1.00 70.30 C
ANISOU 223 CA ALA A 30 10535 7457 8719 -1681 -409 -120 C
ATOM 224 C ALA A 30 32.911 204.643 152.893 1.00 71.07 C
ANISOU 224 C ALA A 30 10695 7530 8778 -1727 -488 -123 C
ATOM 225 O ALA A 30 33.158 205.842 152.925 1.00 70.96 O
ANISOU 225 O ALA A 30 10819 7459 8683 -1847 -501 -127 O
ATOM 226 CB ALA A 30 31.694 203.614 150.950 1.00 70.26 C
ANISOU 226 CB ALA A 30 10634 7357 8705 -1539 -416 -139 C
ATOM 227 N VAL A 31 32.534 203.956 153.971 1.00 71.86 N
ANISOU 227 N VAL A 31 10706 7668 8929 -1637 -536 -120 N
ATOM 228 CA VAL A 31 32.366 204.589 155.266 1.00 73.21 C
ANISOU 228 CA VAL A 31 10944 7811 9060 -1667 -607 -123 C
ATOM 229 C VAL A 31 33.717 205.078 155.785 1.00 74.99 C
ANISOU 229 C VAL A 31 11116 8110 9266 -1842 -628 -105 C
ATOM 230 O VAL A 31 33.803 206.191 156.295 1.00 75.44 O
ANISOU 230 O VAL A 31 11322 8103 9240 -1945 -669 -112 O
ATOM 231 CB VAL A 31 31.651 203.647 156.254 1.00 73.62 C
ANISOU 231 CB VAL A 31 10911 7890 9172 -1527 -641 -122 C
ATOM 232 CG1 VAL A 31 31.524 204.284 157.629 1.00 74.23 C
ANISOU 232 CG1 VAL A 31 11065 7938 9203 -1557 -709 -123 C
ATOM 233 CG2 VAL A 31 30.279 203.260 155.725 1.00 73.86 C
ANISOU 233 CG2 VAL A 31 11000 7846 9218 -1375 -626 -137 C
ATOM 234 N TRP A 32 34.781 204.285 155.601 1.00 75.70 N
ANISOU 234 N TRP A 32 11001 8332 9428 -1880 -598 -82 N
ATOM 235 CA TRP A 32 36.114 204.681 156.038 1.00 76.86 C
ANISOU 235 CA TRP A 32 11059 8572 9571 -2049 -623 -58 C
ATOM 236 C TRP A 32 36.607 205.933 155.295 1.00 77.00 C
ANISOU 236 C TRP A 32 11201 8542 9512 -2222 -592 -60 C
ATOM 237 O TRP A 32 37.229 206.810 155.903 1.00 77.13 O
ANISOU 237 O TRP A 32 11259 8570 9479 -2384 -642 -52 O
ATOM 238 CB TRP A 32 37.110 203.524 155.847 1.00 77.52 C
ANISOU 238 CB TRP A 32 10885 8813 9757 -2025 -585 -28 C
ATOM 239 CG TRP A 32 38.530 203.888 156.183 1.00 79.12 C
ANISOU 239 CG TRP A 32 10957 9135 9972 -2196 -605 4 C
ATOM 240 CD1 TRP A 32 39.428 204.528 155.376 1.00 80.29 C
ANISOU 240 CD1 TRP A 32 11074 9324 10108 -2343 -545 19 C
ATOM 241 CD2 TRP A 32 39.204 203.662 157.434 1.00 79.77 C
ANISOU 241 CD2 TRP A 32 10909 9318 10082 -2240 -693 27 C
ATOM 242 NE1 TRP A 32 40.608 204.735 156.051 1.00 80.85 N
ANISOU 242 NE1 TRP A 32 10989 9525 10206 -2481 -590 53 N
ATOM 243 CE2 TRP A 32 40.502 204.201 157.314 1.00 80.75 C
ANISOU 243 CE2 TRP A 32 10916 9550 10216 -2420 -689 58 C
ATOM 244 CE3 TRP A 32 38.834 203.059 158.646 1.00 80.41 C
ANISOU 244 CE3 TRP A 32 10967 9409 10179 -2148 -775 27 C
ATOM 245 CZ2 TRP A 32 41.432 204.145 158.358 1.00 81.50 C
ANISOU 245 CZ2 TRP A 32 10864 9766 10337 -2509 -778 90 C
ATOM 246 CZ3 TRP A 32 39.755 203.010 159.678 1.00 81.28 C
ANISOU 246 CZ3 TRP A 32 10949 9627 10306 -2232 -861 56 C
ATOM 247 CH2 TRP A 32 41.035 203.546 159.529 1.00 81.50 C
ANISOU 247 CH2 TRP A 32 10855 9765 10345 -2410 -868 87 C
ATOM 248 N LEU A 33 36.350 206.011 153.986 1.00 76.76 N
ANISOU 248 N LEU A 33 11242 8456 9467 -2196 -512 -70 N
ATOM 249 CA LEU A 33 36.839 207.131 153.176 1.00 76.92 C
ANISOU 249 CA LEU A 33 11389 8426 9410 -2358 -468 -71 C
ATOM 250 C LEU A 33 36.026 208.422 153.239 1.00 76.66 C
ANISOU 250 C LEU A 33 11642 8227 9257 -2392 -503 -97 C
ATOM 251 O LEU A 33 36.601 209.510 153.220 1.00 76.66 O
ANISOU 251 O LEU A 33 11758 8190 9180 -2567 -506 -95 O
ATOM 252 CB LEU A 33 36.962 206.711 151.713 1.00 77.23 C
ANISOU 252 CB LEU A 33 11394 8476 9475 -2325 -360 -67 C
ATOM 253 CG LEU A 33 38.032 205.696 151.366 1.00 78.90 C
ANISOU 253 CG LEU A 33 11348 8847 9784 -2334 -294 -36 C
ATOM 254 CD1 LEU A 33 38.005 205.414 149.886 1.00 79.64 C
ANISOU 254 CD1 LEU A 33 11462 8918 9880 -2291 -181 -37 C
ATOM 255 CD2 LEU A 33 39.416 206.187 151.777 1.00 79.41 C
ANISOU 255 CD2 LEU A 33 11302 9018 9852 -2537 -300 -5 C
ATOM 256 N ASN A 34 34.701 208.310 153.242 1.00 76.24 N
ANISOU 256 N ASN A 34 11709 8071 9186 -2229 -519 -120 N
ATOM 257 CA ASN A 34 33.832 209.474 153.202 1.00 76.33 C
ANISOU 257 CA ASN A 34 11992 7925 9084 -2238 -544 -141 C
ATOM 258 C ASN A 34 33.380 209.885 154.576 1.00 76.81 C
ANISOU 258 C ASN A 34 12120 7951 9112 -2223 -624 -146 C
ATOM 259 O ASN A 34 32.615 209.157 155.205 1.00 77.17 O
ANISOU 259 O ASN A 34 12066 8035 9221 -2091 -655 -146 O
ATOM 260 CB ASN A 34 32.627 209.173 152.322 1.00 76.88 C
ANISOU 260 CB ASN A 34 12158 7904 9149 -2063 -523 -157 C
ATOM 261 CG ASN A 34 31.825 210.387 151.944 1.00 79.36 C
ANISOU 261 CG ASN A 34 12753 8056 9344 -2059 -543 -175 C
ATOM 262 OD1 ASN A 34 31.975 211.475 152.511 1.00 80.29 O
ANISOU 262 OD1 ASN A 34 13000 8118 9387 -2139 -585 -178 O
ATOM 263 ND2 ASN A 34 30.947 210.228 150.974 1.00 79.87 N
ANISOU 263 ND2 ASN A 34 12925 8039 9382 -1962 -517 -184 N
ATOM 264 N SER A 35 33.801 211.074 155.029 1.00 76.75 N
ANISOU 264 N SER A 35 12307 7857 8996 -2355 -655 -152 N
ATOM 265 CA SER A 35 33.377 211.552 156.342 1.00 77.30 C
ANISOU 265 CA SER A 35 12475 7879 9016 -2350 -730 -158 C
ATOM 266 C SER A 35 31.894 211.954 156.401 1.00 77.11 C
ANISOU 266 C SER A 35 12661 7709 8928 -2191 -742 -178 C
ATOM 267 O SER A 35 31.345 212.048 157.501 1.00 77.60 O
ANISOU 267 O SER A 35 12849 7707 8930 -2182 -790 -184 O
ATOM 268 CB SER A 35 34.285 212.656 156.853 1.00 79.38 C
ANISOU 268 CB SER A 35 12844 8125 9192 -2578 -768 -153 C
ATOM 269 OG SER A 35 35.415 212.046 157.457 1.00 82.53 O
ANISOU 269 OG SER A 35 13001 8686 9669 -2707 -772 -128 O
ATOM 270 N ASN A 36 31.230 212.128 155.232 1.00 76.08 N
ANISOU 270 N ASN A 36 12578 7523 8805 -2068 -698 -186 N
ATOM 271 CA ASN A 36 29.782 212.369 155.161 1.00 75.49 C
ANISOU 271 CA ASN A 36 12667 7329 8689 -1892 -707 -199 C
ATOM 272 C ASN A 36 28.988 211.095 155.516 1.00 74.08 C
ANISOU 272 C ASN A 36 12305 7221 8623 -1705 -712 -195 C
ATOM 273 O ASN A 36 27.821 211.186 155.888 1.00 74.17 O
ANISOU 273 O ASN A 36 12394 7165 8624 -1551 -723 -200 O
ATOM 274 CB ASN A 36 29.375 212.854 153.780 1.00 77.12 C
ANISOU 274 CB ASN A 36 13016 7443 8844 -1853 -669 -206 C
ATOM 275 CG ASN A 36 29.770 214.277 153.537 1.00 81.33 C
ANISOU 275 CG ASN A 36 13819 7848 9233 -1984 -667 -212 C
ATOM 276 OD1 ASN A 36 29.548 215.154 154.385 1.00 82.61 O
ANISOU 276 OD1 ASN A 36 14195 7889 9304 -1929 -692 -220 O
ATOM 277 ND2 ASN A 36 30.365 214.540 152.376 1.00 82.41 N
ANISOU 277 ND2 ASN A 36 13959 8008 9346 -2156 -631 -208 N
ATOM 278 N LEU A 37 29.614 209.914 155.371 1.00 72.69 N
ANISOU 278 N LEU A 37 11887 7179 8553 -1719 -696 -185 N
ATOM 279 CA LEU A 37 29.035 208.620 155.710 1.00 71.68 C
ANISOU 279 CA LEU A 37 11579 7123 8533 -1567 -697 -180 C
ATOM 280 C LEU A 37 29.418 208.163 157.120 1.00 70.65 C
ANISOU 280 C LEU A 37 11324 7077 8444 -1593 -732 -171 C
ATOM 281 O LEU A 37 28.997 207.090 157.521 1.00 70.71 O
ANISOU 281 O LEU A 37 11152 7170 8545 -1511 -728 -163 O
ATOM 282 CB LEU A 37 29.491 207.560 154.704 1.00 71.77 C
ANISOU 282 CB LEU A 37 11424 7221 8626 -1557 -652 -174 C
ATOM 283 CG LEU A 37 28.958 207.714 153.289 1.00 73.00 C
ANISOU 283 CG LEU A 37 11677 7307 8752 -1521 -617 -182 C
ATOM 284 CD1 LEU A 37 29.656 206.756 152.341 1.00 73.45 C
ANISOU 284 CD1 LEU A 37 11580 7454 8874 -1558 -565 -174 C
ATOM 285 CD2 LEU A 37 27.460 207.514 153.255 1.00 73.57 C
ANISOU 285 CD2 LEU A 37 11786 7322 8845 -1337 -637 -188 C
ATOM 286 N GLN A 38 30.219 208.936 157.862 1.00 69.68 N
ANISOU 286 N GLN A 38 11306 6924 8244 -1714 -770 -171 N
ATOM 287 CA GLN A 38 30.625 208.563 159.208 1.00 69.24 C
ANISOU 287 CA GLN A 38 11156 6939 8213 -1746 -817 -161 C
ATOM 288 C GLN A 38 29.682 209.157 160.236 1.00 68.48 C
ANISOU 288 C GLN A 38 11233 6737 8049 -1663 -844 -171 C
ATOM 289 O GLN A 38 29.881 210.269 160.722 1.00 68.99 O
ANISOU 289 O GLN A 38 11490 6716 8006 -1755 -873 -177 O
ATOM 290 CB GLN A 38 32.081 208.963 159.475 1.00 70.60 C
ANISOU 290 CB GLN A 38 11310 7166 8350 -1960 -849 -151 C
ATOM 291 CG GLN A 38 33.054 208.247 158.550 1.00 73.21 C
ANISOU 291 CG GLN A 38 11478 7597 8741 -2045 -804 -138 C
ATOM 292 CD GLN A 38 34.445 208.813 158.581 1.00 76.85 C
ANISOU 292 CD GLN A 38 11843 8157 9201 -2240 -839 -118 C
ATOM 293 OE1 GLN A 38 34.819 209.562 159.479 1.00 78.82 O
ANISOU 293 OE1 GLN A 38 12063 8442 9443 -2282 -907 -110 O
ATOM 294 NE2 GLN A 38 35.251 208.462 157.594 1.00 76.99 N
ANISOU 294 NE2 GLN A 38 11809 8218 9224 -2363 -793 -108 N
ATOM 295 N ASN A 39 28.631 208.417 160.530 1.00 67.15 N
ANISOU 295 N ASN A 39 11004 6569 7940 -1485 -828 -171 N
ATOM 296 CA ASN A 39 27.630 208.769 161.520 1.00 66.75 C
ANISOU 296 CA ASN A 39 11089 6431 7841 -1380 -836 -175 C
ATOM 297 C ASN A 39 27.197 207.487 162.239 1.00 66.02 C
ANISOU 297 C ASN A 39 10831 6412 7841 -1259 -833 -166 C
ATOM 298 O ASN A 39 27.507 206.395 161.772 1.00 66.29 O
ANISOU 298 O ASN A 39 10664 6549 7972 -1244 -823 -158 O
ATOM 299 CB ASN A 39 26.450 209.471 160.870 1.00 67.86 C
ANISOU 299 CB ASN A 39 11397 6453 7932 -1268 -803 -184 C
ATOM 300 CG ASN A 39 25.746 208.632 159.851 1.00 70.78 C
ANISOU 300 CG ASN A 39 11637 6862 8395 -1143 -769 -181 C
ATOM 301 OD1 ASN A 39 26.191 208.477 158.712 1.00 72.27 O
ANISOU 301 OD1 ASN A 39 11792 7069 8599 -1191 -755 -184 O
ATOM 302 ND2 ASN A 39 24.616 208.083 160.247 1.00 70.94 N
ANISOU 302 ND2 ASN A 39 11595 6887 8472 -985 -754 -176 N
ATOM 303 N VAL A 40 26.497 207.600 163.375 1.00 64.99 N
ANISOU 303 N VAL A 40 10794 6223 7675 -1174 -836 -166 N
ATOM 304 CA VAL A 40 26.090 206.435 164.156 1.00 64.20 C
ANISOU 304 CA VAL A 40 10554 6185 7654 -1068 -828 -156 C
ATOM 305 C VAL A 40 25.337 205.390 163.359 1.00 63.11 C
ANISOU 305 C VAL A 40 10253 6100 7628 -943 -785 -152 C
ATOM 306 O VAL A 40 25.659 204.206 163.462 1.00 63.24 O
ANISOU 306 O VAL A 40 10089 6212 7728 -929 -786 -143 O
ATOM 307 CB VAL A 40 25.302 206.860 165.397 1.00 65.04 C
ANISOU 307 CB VAL A 40 10813 6203 7695 -985 -820 -157 C
ATOM 308 CG1 VAL A 40 24.710 205.654 166.113 1.00 65.58 C
ANISOU 308 CG1 VAL A 40 10746 6327 7845 -867 -797 -145 C
ATOM 309 CG2 VAL A 40 26.188 207.655 166.334 1.00 65.78 C
ANISOU 309 CG2 VAL A 40 11057 6256 7680 -1124 -876 -160 C
ATOM 310 N THR A 41 24.371 205.807 162.536 1.00 62.00 N
ANISOU 310 N THR A 41 10177 5897 7483 -858 -754 -156 N
ATOM 311 CA THR A 41 23.583 204.871 161.723 1.00 61.58 C
ANISOU 311 CA THR A 41 9982 5888 7528 -749 -724 -152 C
ATOM 312 C THR A 41 24.479 203.988 160.855 1.00 60.99 C
ANISOU 312 C THR A 41 9743 5909 7521 -822 -729 -151 C
ATOM 313 O THR A 41 24.280 202.777 160.784 1.00 61.18 O
ANISOU 313 O THR A 41 9611 6000 7633 -762 -715 -144 O
ATOM 314 CB THR A 41 22.580 205.599 160.819 1.00 62.82 C
ANISOU 314 CB THR A 41 10242 5966 7660 -667 -708 -155 C
ATOM 315 OG1 THR A 41 22.160 206.842 161.397 1.00 63.90 O
ANISOU 315 OG1 THR A 41 10522 6016 7742 -569 -691 -151 O
ATOM 316 CG2 THR A 41 21.388 204.724 160.454 1.00 62.99 C
ANISOU 316 CG2 THR A 41 10119 6036 7778 -582 -695 -150 C
ATOM 317 N ASN A 42 25.512 204.591 160.266 1.00 60.04 N
ANISOU 317 N ASN A 42 9659 5795 7357 -954 -742 -156 N
ATOM 318 CA ASN A 42 26.425 203.861 159.407 1.00 59.58 C
ANISOU 318 CA ASN A 42 9453 5828 7358 -1020 -733 -152 C
ATOM 319 C ASN A 42 27.476 203.050 160.166 1.00 58.90 C
ANISOU 319 C ASN A 42 9226 5842 7310 -1082 -751 -140 C
ATOM 320 O ASN A 42 28.087 202.178 159.553 1.00 59.61 O
ANISOU 320 O ASN A 42 9182 6014 7454 -1119 -735 -133 O
ATOM 321 CB ASN A 42 27.047 204.777 158.378 1.00 60.58 C
ANISOU 321 CB ASN A 42 9661 5926 7430 -1127 -724 -159 C
ATOM 322 CG ASN A 42 26.051 205.247 157.338 1.00 63.72 C
ANISOU 322 CG ASN A 42 10204 6222 7784 -1058 -713 -169 C
ATOM 323 OD1 ASN A 42 24.950 204.701 157.184 1.00 64.65 O
ANISOU 323 OD1 ASN A 42 10289 6328 7949 -929 -705 -168 O
ATOM 324 ND2 ASN A 42 26.417 206.274 156.592 1.00 64.71 N
ANISOU 324 ND2 ASN A 42 10495 6275 7818 -1146 -717 -176 N
ATOM 325 N TYR A 43 27.648 203.260 161.481 1.00 57.39 N
ANISOU 325 N TYR A 43 9077 5644 7084 -1101 -786 -137 N
ATOM 326 CA TYR A 43 28.523 202.378 162.254 1.00 56.60 C
ANISOU 326 CA TYR A 43 8834 5643 7028 -1133 -812 -122 C
ATOM 327 C TYR A 43 27.830 201.038 162.424 1.00 54.88 C
ANISOU 327 C TYR A 43 8493 5463 6897 -996 -784 -115 C
ATOM 328 O TYR A 43 28.484 200.009 162.317 1.00 55.04 O
ANISOU 328 O TYR A 43 8360 5574 6980 -995 -780 -103 O
ATOM 329 CB TYR A 43 28.923 202.991 163.585 1.00 57.33 C
ANISOU 329 CB TYR A 43 9021 5713 7049 -1199 -867 -119 C
ATOM 330 CG TYR A 43 29.617 204.328 163.423 1.00 59.20 C
ANISOU 330 CG TYR A 43 9395 5906 7193 -1352 -899 -125 C
ATOM 331 CD1 TYR A 43 30.384 204.609 162.296 1.00 60.33 C
ANISOU 331 CD1 TYR A 43 9499 6083 7342 -1454 -883 -124 C
ATOM 332 CD2 TYR A 43 29.520 205.307 164.403 1.00 60.57 C
ANISOU 332 CD2 TYR A 43 9751 5997 7266 -1401 -940 -131 C
ATOM 333 CE1 TYR A 43 31.005 205.839 162.133 1.00 61.30 C
ANISOU 333 CE1 TYR A 43 9755 6161 7376 -1608 -907 -129 C
ATOM 334 CE2 TYR A 43 30.150 206.536 164.258 1.00 61.62 C
ANISOU 334 CE2 TYR A 43 10026 6080 7305 -1554 -972 -137 C
ATOM 335 CZ TYR A 43 30.892 206.798 163.120 1.00 62.60 C
ANISOU 335 CZ TYR A 43 10103 6242 7441 -1661 -955 -135 C
ATOM 336 OH TYR A 43 31.523 208.008 162.967 1.00 64.68 O
ANISOU 336 OH TYR A 43 10514 6454 7610 -1825 -981 -140 O
ATOM 337 N PHE A 44 26.498 201.034 162.591 1.00 53.23 N
ANISOU 337 N PHE A 44 8350 5185 6691 -880 -760 -122 N
ATOM 338 CA PHE A 44 25.731 199.802 162.621 1.00 52.15 C
ANISOU 338 CA PHE A 44 8105 5076 6634 -763 -729 -116 C
ATOM 339 C PHE A 44 25.723 199.170 161.233 1.00 51.05 C
ANISOU 339 C PHE A 44 7875 4969 6552 -749 -701 -119 C
ATOM 340 O PHE A 44 25.806 197.953 161.144 1.00 51.28 O
ANISOU 340 O PHE A 44 7782 5055 6648 -705 -685 -111 O
ATOM 341 CB PHE A 44 24.310 200.051 163.119 1.00 52.01 C
ANISOU 341 CB PHE A 44 8173 4981 6606 -654 -707 -118 C
ATOM 342 CG PHE A 44 24.284 200.443 164.571 1.00 52.64 C
ANISOU 342 CG PHE A 44 8341 5027 6631 -648 -721 -114 C
ATOM 343 CD1 PHE A 44 24.660 199.543 165.555 1.00 53.33 C
ANISOU 343 CD1 PHE A 44 8352 5165 6746 -634 -730 -103 C
ATOM 344 CD2 PHE A 44 23.915 201.719 164.953 1.00 53.30 C
ANISOU 344 CD2 PHE A 44 8604 5021 6628 -656 -725 -121 C
ATOM 345 CE1 PHE A 44 24.661 199.915 166.893 1.00 53.88 C
ANISOU 345 CE1 PHE A 44 8522 5197 6754 -635 -747 -99 C
ATOM 346 CE2 PHE A 44 23.926 202.089 166.287 1.00 53.93 C
ANISOU 346 CE2 PHE A 44 8787 5060 6643 -656 -737 -118 C
ATOM 347 CZ PHE A 44 24.300 201.185 167.249 1.00 53.74 C
ANISOU 347 CZ PHE A 44 8684 5088 6646 -647 -749 -107 C
ATOM 348 N VAL A 45 25.680 199.979 160.153 1.00 49.77 N
ANISOU 348 N VAL A 45 7788 4765 6357 -788 -695 -129 N
ATOM 349 CA VAL A 45 25.774 199.503 158.770 1.00 48.87 C
ANISOU 349 CA VAL A 45 7616 4672 6280 -788 -670 -132 C
ATOM 350 C VAL A 45 27.112 198.776 158.560 1.00 48.98 C
ANISOU 350 C VAL A 45 7504 4780 6328 -853 -658 -123 C
ATOM 351 O VAL A 45 27.138 197.742 157.897 1.00 49.47 O
ANISOU 351 O VAL A 45 7473 4878 6446 -808 -629 -120 O
ATOM 352 CB VAL A 45 25.570 200.649 157.766 1.00 48.40 C
ANISOU 352 CB VAL A 45 7687 4542 6160 -828 -670 -144 C
ATOM 353 CG1 VAL A 45 26.022 200.252 156.373 1.00 48.71 C
ANISOU 353 CG1 VAL A 45 7681 4607 6221 -857 -642 -146 C
ATOM 354 CG2 VAL A 45 24.116 201.063 157.743 1.00 48.63 C
ANISOU 354 CG2 VAL A 45 7807 4494 6178 -726 -676 -148 C
ATOM 355 N VAL A 46 28.207 199.285 159.157 1.00 48.30 N
ANISOU 355 N VAL A 46 7412 4733 6208 -954 -681 -115 N
ATOM 356 CA VAL A 46 29.511 198.639 159.080 1.00 48.00 C
ANISOU 356 CA VAL A 46 7234 4796 6206 -1008 -672 -99 C
ATOM 357 C VAL A 46 29.529 197.333 159.871 1.00 48.29 C
ANISOU 357 C VAL A 46 7151 4893 6303 -925 -676 -85 C
ATOM 358 O VAL A 46 30.123 196.363 159.408 1.00 48.32 O
ANISOU 358 O VAL A 46 7037 4965 6359 -901 -645 -74 O
ATOM 359 CB VAL A 46 30.624 199.597 159.495 1.00 48.37 C
ANISOU 359 CB VAL A 46 7301 4875 6204 -1147 -705 -92 C
ATOM 360 CG1 VAL A 46 31.926 198.854 159.778 1.00 48.98 C
ANISOU 360 CG1 VAL A 46 7203 5076 6330 -1187 -705 -67 C
ATOM 361 CG2 VAL A 46 30.829 200.639 158.415 1.00 48.92 C
ANISOU 361 CG2 VAL A 46 7473 4895 6221 -1236 -683 -102 C
ATOM 362 N SER A 47 28.863 197.290 161.038 1.00 48.29 N
ANISOU 362 N SER A 47 7196 4857 6294 -868 -703 -87 N
ATOM 363 CA SER A 47 28.761 196.055 161.830 1.00 48.64 C
ANISOU 363 CA SER A 47 7152 4945 6386 -790 -706 -74 C
ATOM 364 C SER A 47 27.991 194.974 161.056 1.00 48.68 C
ANISOU 364 C SER A 47 7114 4935 6447 -688 -661 -77 C
ATOM 365 O SER A 47 28.334 193.801 161.098 1.00 48.70 O
ANISOU 365 O SER A 47 7041 4972 6489 -626 -651 -66 O
ATOM 366 CB SER A 47 28.068 196.321 163.160 1.00 49.96 C
ANISOU 366 CB SER A 47 7398 5068 6515 -766 -739 -74 C
ATOM 367 OG SER A 47 27.906 195.113 163.888 1.00 52.59 O
ANISOU 367 OG SER A 47 7664 5426 6891 -680 -730 -63 O
ATOM 368 N LEU A 48 26.956 195.380 160.348 1.00 48.74 N
ANISOU 368 N LEU A 48 7186 4882 6450 -671 -641 -92 N
ATOM 369 CA LEU A 48 26.148 194.494 159.531 1.00 49.07 C
ANISOU 369 CA LEU A 48 7203 4905 6538 -597 -609 -97 C
ATOM 370 C LEU A 48 26.966 194.013 158.318 1.00 49.88 C
ANISOU 370 C LEU A 48 7249 5045 6657 -625 -577 -96 C
ATOM 371 O LEU A 48 26.903 192.830 157.975 1.00 50.57 O
ANISOU 371 O LEU A 48 7276 5151 6786 -571 -549 -92 O
ATOM 372 CB LEU A 48 24.895 195.272 159.103 1.00 48.84 C
ANISOU 372 CB LEU A 48 7272 4796 6489 -570 -616 -110 C
ATOM 373 CG LEU A 48 23.838 194.567 158.305 1.00 49.79 C
ANISOU 373 CG LEU A 48 7379 4889 6651 -506 -602 -114 C
ATOM 374 CD1 LEU A 48 23.363 193.328 159.005 1.00 50.24 C
ANISOU 374 CD1 LEU A 48 7362 4967 6761 -443 -587 -105 C
ATOM 375 CD2 LEU A 48 22.684 195.506 158.046 1.00 50.33 C
ANISOU 375 CD2 LEU A 48 7536 4891 6698 -476 -620 -120 C
ATOM 376 N ALA A 49 27.777 194.898 157.710 1.00 49.46 N
ANISOU 376 N ALA A 49 7223 5003 6568 -711 -574 -99 N
ATOM 377 CA ALA A 49 28.623 194.503 156.586 1.00 49.76 C
ANISOU 377 CA ALA A 49 7210 5079 6617 -738 -530 -95 C
ATOM 378 C ALA A 49 29.760 193.585 157.037 1.00 50.02 C
ANISOU 378 C ALA A 49 7112 5207 6687 -729 -511 -73 C
ATOM 379 O ALA A 49 30.141 192.684 156.291 1.00 50.07 O
ANISOU 379 O ALA A 49 7063 5242 6720 -694 -461 -67 O
ATOM 380 CB ALA A 49 29.187 195.724 155.896 1.00 49.93 C
ANISOU 380 CB ALA A 49 7296 5087 6587 -839 -525 -100 C
ATOM 381 N ALA A 50 30.280 193.782 158.262 1.00 49.94 N
ANISOU 381 N ALA A 50 7060 5243 6673 -752 -553 -60 N
ATOM 382 CA ALA A 50 31.337 192.929 158.804 1.00 50.26 C
ANISOU 382 CA ALA A 50 6970 5378 6747 -733 -551 -34 C
ATOM 383 C ALA A 50 30.806 191.499 158.997 1.00 51.08 C
ANISOU 383 C ALA A 50 7039 5476 6893 -614 -527 -30 C
ATOM 384 O ALA A 50 31.516 190.533 158.694 1.00 51.12 O
ANISOU 384 O ALA A 50 6956 5538 6929 -568 -488 -13 O
ATOM 385 CB ALA A 50 31.840 193.489 160.120 1.00 49.95 C
ANISOU 385 CB ALA A 50 6918 5374 6685 -785 -619 -22 C
ATOM 386 N ALA A 51 29.540 191.366 159.457 1.00 51.25 N
ANISOU 386 N ALA A 51 7136 5425 6913 -564 -544 -44 N
ATOM 387 CA ALA A 51 28.891 190.066 159.624 1.00 51.52 C
ANISOU 387 CA ALA A 51 7157 5437 6980 -468 -522 -42 C
ATOM 388 C ALA A 51 28.744 189.404 158.268 1.00 51.83 C
ANISOU 388 C ALA A 51 7203 5455 7036 -442 -469 -50 C
ATOM 389 O ALA A 51 28.977 188.205 158.162 1.00 52.53 O
ANISOU 389 O ALA A 51 7254 5558 7148 -377 -436 -40 O
ATOM 390 CB ALA A 51 27.519 190.224 160.270 1.00 51.59 C
ANISOU 390 CB ALA A 51 7242 5376 6986 -439 -543 -54 C
ATOM 391 N ASP A 52 28.391 190.169 157.225 1.00 51.28 N
ANISOU 391 N ASP A 52 7195 5345 6944 -490 -462 -67 N
ATOM 392 CA ASP A 52 28.237 189.609 155.890 1.00 51.57 C
ANISOU 392 CA ASP A 52 7259 5352 6984 -471 -416 -75 C
ATOM 393 C ASP A 52 29.571 189.204 155.257 1.00 51.12 C
ANISOU 393 C ASP A 52 7136 5358 6931 -473 -359 -60 C
ATOM 394 O ASP A 52 29.640 188.181 154.569 1.00 50.52 O
ANISOU 394 O ASP A 52 7059 5272 6863 -417 -310 -57 O
ATOM 395 CB ASP A 52 27.433 190.555 155.010 1.00 53.98 C
ANISOU 395 CB ASP A 52 7661 5589 7259 -512 -433 -95 C
ATOM 396 CG ASP A 52 25.974 190.637 155.425 1.00 59.97 C
ANISOU 396 CG ASP A 52 8470 6288 8027 -481 -476 -106 C
ATOM 397 OD1 ASP A 52 25.463 189.649 156.020 1.00 60.89 O
ANISOU 397 OD1 ASP A 52 8556 6404 8176 -425 -476 -100 O
ATOM 398 OD2 ASP A 52 25.336 191.680 155.149 1.00 62.69 O
ANISOU 398 OD2 ASP A 52 8885 6587 8345 -508 -505 -117 O
ATOM 399 N ILE A 53 30.653 189.942 155.564 1.00 50.99 N
ANISOU 399 N ILE A 53 7059 5410 6906 -535 -362 -46 N
ATOM 400 CA ILE A 53 31.994 189.581 155.107 1.00 51.02 C
ANISOU 400 CA ILE A 53 6969 5494 6923 -534 -304 -24 C
ATOM 401 C ILE A 53 32.379 188.235 155.737 1.00 51.03 C
ANISOU 401 C ILE A 53 6889 5541 6959 -434 -287 -2 C
ATOM 402 O ILE A 53 32.902 187.371 155.037 1.00 51.88 O
ANISOU 402 O ILE A 53 6972 5665 7077 -375 -218 9 O
ATOM 403 CB ILE A 53 33.025 190.678 155.452 1.00 51.45 C
ANISOU 403 CB ILE A 53 6959 5621 6968 -635 -323 -9 C
ATOM 404 CG1 ILE A 53 32.778 191.929 154.614 1.00 52.74 C
ANISOU 404 CG1 ILE A 53 7222 5729 7086 -731 -321 -29 C
ATOM 405 CG2 ILE A 53 34.461 190.180 155.257 1.00 51.63 C
ANISOU 405 CG2 ILE A 53 6847 5752 7020 -624 -266 24 C
ATOM 406 CD1 ILE A 53 33.554 193.147 155.082 1.00 54.30 C
ANISOU 406 CD1 ILE A 53 7394 5976 7262 -851 -355 -20 C
ATOM 407 N LEU A 54 32.074 188.035 157.038 1.00 49.75 N
ANISOU 407 N LEU A 54 6705 5388 6808 -406 -346 4 N
ATOM 408 CA LEU A 54 32.359 186.769 157.720 1.00 48.91 C
ANISOU 408 CA LEU A 54 6543 5314 6727 -306 -338 25 C
ATOM 409 C LEU A 54 31.478 185.606 157.231 1.00 48.25 C
ANISOU 409 C LEU A 54 6537 5150 6644 -225 -297 13 C
ATOM 410 O LEU A 54 31.834 184.447 157.427 1.00 47.72 O
ANISOU 410 O LEU A 54 6444 5098 6589 -136 -266 30 O
ATOM 411 CB LEU A 54 32.260 186.941 159.224 1.00 49.00 C
ANISOU 411 CB LEU A 54 6537 5343 6737 -309 -412 33 C
ATOM 412 CG LEU A 54 33.305 187.867 159.822 1.00 50.57 C
ANISOU 412 CG LEU A 54 6645 5635 6933 -376 -456 55 C
ATOM 413 CD1 LEU A 54 33.005 188.175 161.283 1.00 51.10 C
ANISOU 413 CD1 LEU A 54 6743 5692 6979 -403 -539 54 C
ATOM 414 CD2 LEU A 54 34.674 187.261 159.712 1.00 51.23 C
ANISOU 414 CD2 LEU A 54 6603 5817 7046 -310 -432 91 C
ATOM 415 N VAL A 55 30.332 185.907 156.593 1.00 47.95 N
ANISOU 415 N VAL A 55 6600 5027 6592 -257 -303 -16 N
ATOM 416 CA VAL A 55 29.507 184.872 155.978 1.00 47.91 C
ANISOU 416 CA VAL A 55 6673 4946 6584 -205 -273 -28 C
ATOM 417 C VAL A 55 30.276 184.316 154.777 1.00 47.28 C
ANISOU 417 C VAL A 55 6599 4872 6492 -174 -196 -22 C
ATOM 418 O VAL A 55 30.336 183.113 154.600 1.00 47.40 O
ANISOU 418 O VAL A 55 6643 4862 6505 -99 -154 -16 O
ATOM 419 CB VAL A 55 28.091 185.369 155.574 1.00 48.87 C
ANISOU 419 CB VAL A 55 6887 4986 6697 -251 -310 -55 C
ATOM 420 CG1 VAL A 55 27.397 184.384 154.626 1.00 49.30 C
ANISOU 420 CG1 VAL A 55 7024 4967 6741 -222 -281 -67 C
ATOM 421 CG2 VAL A 55 27.227 185.621 156.806 1.00 49.38 C
ANISOU 421 CG2 VAL A 55 6951 5036 6776 -253 -365 -56 C
ATOM 422 N GLY A 56 30.873 185.189 153.983 1.00 46.63 N
ANISOU 422 N GLY A 56 6503 4816 6396 -232 -172 -24 N
ATOM 423 CA GLY A 56 31.651 184.770 152.830 1.00 46.67 C
ANISOU 423 CA GLY A 56 6517 4828 6386 -205 -86 -17 C
ATOM 424 C GLY A 56 32.961 184.125 153.222 1.00 46.58 C
ANISOU 424 C GLY A 56 6389 4910 6398 -133 -34 19 C
ATOM 425 O GLY A 56 33.322 183.086 152.679 1.00 47.19 O
ANISOU 425 O GLY A 56 6490 4973 6467 -46 36 29 O
ATOM 426 N VAL A 57 33.677 184.717 154.176 1.00 45.89 N
ANISOU 426 N VAL A 57 6182 4919 6337 -165 -72 39 N
ATOM 427 CA VAL A 57 34.976 184.210 154.598 1.00 45.94 C
ANISOU 427 CA VAL A 57 6052 5032 6371 -100 -37 79 C
ATOM 428 C VAL A 57 34.878 182.920 155.419 1.00 46.76 C
ANISOU 428 C VAL A 57 6155 5127 6485 20 -45 94 C
ATOM 429 O VAL A 57 35.642 181.999 155.181 1.00 47.12 O
ANISOU 429 O VAL A 57 6165 5203 6535 121 25 118 O
ATOM 430 CB VAL A 57 35.790 185.311 155.339 1.00 46.00 C
ANISOU 430 CB VAL A 57 5932 5147 6400 -186 -94 99 C
ATOM 431 CG1 VAL A 57 37.073 184.754 155.940 1.00 46.21 C
ANISOU 431 CG1 VAL A 57 5799 5296 6462 -114 -80 145 C
ATOM 432 CG2 VAL A 57 36.104 186.476 154.419 1.00 46.18 C
ANISOU 432 CG2 VAL A 57 5957 5181 6407 -302 -66 90 C
ATOM 433 N LEU A 58 33.947 182.844 156.371 1.00 46.85 N
ANISOU 433 N LEU A 58 6215 5091 6494 15 -120 80 N
ATOM 434 CA LEU A 58 33.864 181.698 157.276 1.00 47.22 C
ANISOU 434 CA LEU A 58 6267 5129 6545 118 -131 96 C
ATOM 435 C LEU A 58 32.578 180.843 157.180 1.00 47.24 C
ANISOU 435 C LEU A 58 6413 5010 6527 149 -127 71 C
ATOM 436 O LEU A 58 32.694 179.626 157.036 1.00 47.31 O
ANISOU 436 O LEU A 58 6466 4986 6523 246 -78 82 O
ATOM 437 CB LEU A 58 34.071 182.183 158.728 1.00 47.34 C
ANISOU 437 CB LEU A 58 6208 5206 6574 93 -221 111 C
ATOM 438 CG LEU A 58 35.459 182.740 159.077 1.00 48.08 C
ANISOU 438 CG LEU A 58 6148 5432 6690 69 -242 144 C
ATOM 439 CD1 LEU A 58 35.437 183.456 160.396 1.00 48.27 C
ANISOU 439 CD1 LEU A 58 6138 5490 6712 20 -343 151 C
ATOM 440 CD2 LEU A 58 36.451 181.641 159.189 1.00 48.58 C
ANISOU 440 CD2 LEU A 58 6124 5565 6770 193 -190 183 C
ATOM 441 N ALA A 59 31.376 181.448 157.283 1.00 46.86 N
ANISOU 441 N ALA A 59 6434 4896 6473 69 -178 42 N
ATOM 442 CA ALA A 59 30.142 180.657 157.276 1.00 47.10 C
ANISOU 442 CA ALA A 59 6578 4825 6491 85 -180 23 C
ATOM 443 C ALA A 59 29.929 179.792 156.043 1.00 46.83 C
ANISOU 443 C ALA A 59 6639 4722 6433 119 -116 13 C
ATOM 444 O ALA A 59 29.541 178.643 156.190 1.00 46.84 O
ANISOU 444 O ALA A 59 6711 4667 6420 178 -95 16 O
ATOM 445 CB ALA A 59 28.934 181.540 157.499 1.00 47.71 C
ANISOU 445 CB ALA A 59 6694 4859 6574 -3 -239 -2 C
ATOM 446 N ILE A 60 30.174 180.319 154.839 1.00 46.57 N
ANISOU 446 N ILE A 60 6626 4683 6387 79 -84 1 N
ATOM 447 CA ILE A 60 29.999 179.558 153.598 1.00 46.62 C
ANISOU 447 CA ILE A 60 6744 4612 6356 104 -24 -10 C
ATOM 448 C ILE A 60 31.016 178.407 153.517 1.00 46.61 C
ANISOU 448 C ILE A 60 6740 4630 6341 224 59 16 C
ATOM 449 O ILE A 60 30.558 177.263 153.417 1.00 46.47 O
ANISOU 449 O ILE A 60 6832 4531 6294 275 82 12 O
ATOM 450 CB ILE A 60 29.954 180.467 152.372 1.00 47.02 C
ANISOU 450 CB ILE A 60 6832 4646 6389 31 -13 -29 C
ATOM 451 CG1 ILE A 60 28.631 181.244 152.391 1.00 48.34 C
ANISOU 451 CG1 ILE A 60 7039 4766 6562 -60 -97 -55 C
ATOM 452 CG2 ILE A 60 30.105 179.662 151.100 1.00 47.32 C
ANISOU 452 CG2 ILE A 60 6989 4612 6379 69 60 -36 C
ATOM 453 CD1 ILE A 60 28.468 182.283 151.303 1.00 50.12 C
ANISOU 453 CD1 ILE A 60 7306 4972 6764 -136 -105 -73 C
ATOM 454 N PRO A 61 32.352 178.622 153.702 1.00 46.37 N
ANISOU 454 N PRO A 61 6585 4705 6330 274 99 47 N
ATOM 455 CA PRO A 61 33.264 177.463 153.809 1.00 46.39 C
ANISOU 455 CA PRO A 61 6572 4730 6323 412 171 78 C
ATOM 456 C PRO A 61 32.842 176.447 154.894 1.00 47.27 C
ANISOU 456 C PRO A 61 6725 4806 6431 480 138 87 C
ATOM 457 O PRO A 61 32.972 175.247 154.665 1.00 47.24 O
ANISOU 457 O PRO A 61 6808 4747 6393 582 199 97 O
ATOM 458 CB PRO A 61 34.602 178.110 154.173 1.00 46.43 C
ANISOU 458 CB PRO A 61 6393 4879 6368 429 182 113 C
ATOM 459 CG PRO A 61 34.520 179.462 153.595 1.00 46.68 C
ANISOU 459 CG PRO A 61 6393 4933 6409 302 161 94 C
ATOM 460 CD PRO A 61 33.106 179.892 153.807 1.00 45.39 C
ANISOU 460 CD PRO A 61 6327 4684 6236 210 79 57 C
ATOM 461 N PHE A 62 32.303 176.906 156.048 1.00 48.01 N
ANISOU 461 N PHE A 62 6774 4917 6549 426 50 83 N
ATOM 462 CA PHE A 62 31.834 175.988 157.084 1.00 49.57 C
ANISOU 462 CA PHE A 62 7026 5072 6738 481 24 91 C
ATOM 463 C PHE A 62 30.628 175.179 156.605 1.00 50.85 C
ANISOU 463 C PHE A 62 7357 5100 6864 458 37 64 C
ATOM 464 O PHE A 62 30.577 173.977 156.870 1.00 51.39 O
ANISOU 464 O PHE A 62 7514 5109 6902 538 69 74 O
ATOM 465 CB PHE A 62 31.448 176.729 158.370 1.00 50.03 C
ANISOU 465 CB PHE A 62 7016 5170 6823 422 -65 90 C
ATOM 466 CG PHE A 62 32.568 177.252 159.244 1.00 51.25 C
ANISOU 466 CG PHE A 62 7025 5446 7004 449 -103 122 C
ATOM 467 CD1 PHE A 62 33.893 177.125 158.857 1.00 52.13 C
ANISOU 467 CD1 PHE A 62 7035 5646 7126 516 -58 152 C
ATOM 468 CD2 PHE A 62 32.292 177.943 160.413 1.00 52.03 C
ANISOU 468 CD2 PHE A 62 7084 5572 7115 397 -183 122 C
ATOM 469 CE1 PHE A 62 34.914 177.654 159.639 1.00 52.64 C
ANISOU 469 CE1 PHE A 62 6951 5833 7218 523 -106 182 C
ATOM 470 CE2 PHE A 62 33.318 178.462 161.193 1.00 52.54 C
ANISOU 470 CE2 PHE A 62 7022 5746 7196 404 -232 150 C
ATOM 471 CZ PHE A 62 34.620 178.312 160.803 1.00 52.26 C
ANISOU 471 CZ PHE A 62 6876 5804 7175 463 -199 181 C
ATOM 472 N ALA A 63 29.665 175.826 155.892 1.00 51.03 N
ANISOU 472 N ALA A 63 7426 5073 6888 346 9 31 N
ATOM 473 CA ALA A 63 28.442 175.188 155.355 1.00 51.41 C
ANISOU 473 CA ALA A 63 7620 5004 6908 296 3 6 C
ATOM 474 C ALA A 63 28.773 174.098 154.349 1.00 51.20 C
ANISOU 474 C ALA A 63 7725 4901 6826 361 80 6 C
ATOM 475 O ALA A 63 28.140 173.043 154.330 1.00 50.51 O
ANISOU 475 O ALA A 63 7768 4718 6704 367 88 -1 O
ATOM 476 CB ALA A 63 27.527 176.228 154.710 1.00 51.65 C
ANISOU 476 CB ALA A 63 7652 5019 6953 176 -48 -22 C
ATOM 477 N ILE A 64 29.773 174.360 153.510 1.00 51.66 N
ANISOU 477 N ILE A 64 7756 5000 6873 406 141 14 N
ATOM 478 CA ILE A 64 30.241 173.391 152.533 1.00 52.35 C
ANISOU 478 CA ILE A 64 7968 5021 6903 486 231 17 C
ATOM 479 C ILE A 64 30.855 172.200 153.273 1.00 53.40 C
ANISOU 479 C ILE A 64 8124 5147 7016 621 278 46 C
ATOM 480 O ILE A 64 30.561 171.046 152.949 1.00 53.72 O
ANISOU 480 O ILE A 64 8332 5079 6999 664 317 42 O
ATOM 481 CB ILE A 64 31.262 174.058 151.582 1.00 52.43 C
ANISOU 481 CB ILE A 64 7915 5094 6912 508 297 25 C
ATOM 482 CG1 ILE A 64 30.604 175.159 150.719 1.00 52.75 C
ANISOU 482 CG1 ILE A 64 7975 5115 6954 377 254 -6 C
ATOM 483 CG2 ILE A 64 31.950 173.014 150.721 1.00 52.97 C
ANISOU 483 CG2 ILE A 64 8097 5107 6920 625 411 38 C
ATOM 484 CD1 ILE A 64 31.571 175.997 149.940 1.00 53.63 C
ANISOU 484 CD1 ILE A 64 8015 5295 7069 378 315 3 C
ATOM 485 N THR A 65 31.665 172.487 154.296 1.00 53.81 N
ANISOU 485 N THR A 65 8023 5311 7113 683 264 77 N
ATOM 486 CA THR A 65 32.333 171.464 155.080 1.00 55.06 C
ANISOU 486 CA THR A 65 8188 5477 7254 824 299 110 C
ATOM 487 C THR A 65 31.379 170.519 155.820 1.00 56.36 C
ANISOU 487 C THR A 65 8490 5538 7388 818 268 101 C
ATOM 488 O THR A 65 31.491 169.306 155.668 1.00 56.27 O
ANISOU 488 O THR A 65 8624 5440 7319 908 327 109 O
ATOM 489 CB THR A 65 33.339 172.101 156.028 1.00 56.49 C
ANISOU 489 CB THR A 65 8168 5805 7490 872 267 144 C
ATOM 490 OG1 THR A 65 34.211 172.944 155.286 1.00 57.76 O
ANISOU 490 OG1 THR A 65 8203 6061 7681 857 299 153 O
ATOM 491 CG2 THR A 65 34.160 171.076 156.742 1.00 57.09 C
ANISOU 491 CG2 THR A 65 8243 5902 7548 1037 306 185 C
ATOM 492 N ILE A 66 30.460 171.051 156.630 1.00 57.41 N
ANISOU 492 N ILE A 66 8585 5674 7553 714 183 87 N
ATOM 493 CA ILE A 66 29.534 170.224 157.402 1.00 58.82 C
ANISOU 493 CA ILE A 66 8879 5762 7707 696 159 82 C
ATOM 494 C ILE A 66 28.540 169.446 156.507 1.00 60.78 C
ANISOU 494 C ILE A 66 9316 5872 7906 626 178 53 C
ATOM 495 O ILE A 66 28.007 168.424 156.947 1.00 60.71 O
ANISOU 495 O ILE A 66 9436 5771 7859 628 184 54 O
ATOM 496 CB ILE A 66 28.839 171.077 158.485 1.00 58.81 C
ANISOU 496 CB ILE A 66 8777 5812 7757 607 76 77 C
ATOM 497 CG1 ILE A 66 28.238 170.208 159.584 1.00 59.44 C
ANISOU 497 CG1 ILE A 66 8942 5829 7815 625 64 86 C
ATOM 498 CG2 ILE A 66 27.823 172.028 157.877 1.00 59.24 C
ANISOU 498 CG2 ILE A 66 8811 5857 7842 461 29 45 C
ATOM 499 CD1 ILE A 66 27.840 170.935 160.747 1.00 60.49 C
ANISOU 499 CD1 ILE A 66 8979 6017 7986 579 2 91 C
ATOM 500 N SER A 67 28.339 169.890 155.233 1.00 62.32 N
ANISOU 500 N SER A 67 9540 6046 8093 565 189 31 N
ATOM 501 CA SER A 67 27.464 169.181 154.289 1.00 64.11 C
ANISOU 501 CA SER A 67 9952 6142 8264 495 198 5 C
ATOM 502 C SER A 67 28.060 167.821 153.850 1.00 65.92 C
ANISOU 502 C SER A 67 10361 6276 8410 614 287 17 C
ATOM 503 O SER A 67 27.326 166.960 153.365 1.00 66.10 O
ANISOU 503 O SER A 67 10570 6171 8373 564 292 0 O
ATOM 504 CB SER A 67 27.128 170.045 153.078 1.00 65.44 C
ANISOU 504 CB SER A 67 10113 6312 8438 403 176 -21 C
ATOM 505 OG SER A 67 28.158 170.022 152.104 1.00 67.90 O
ANISOU 505 OG SER A 67 10464 6624 8710 486 257 -15 O
ATOM 506 N THR A 68 29.380 167.625 154.028 1.00 66.96 N
ANISOU 506 N THR A 68 10437 6468 8535 771 357 48 N
ATOM 507 CA THR A 68 30.048 166.351 153.728 1.00 68.13 C
ANISOU 507 CA THR A 68 10746 6535 8605 916 452 66 C
ATOM 508 C THR A 68 29.809 165.307 154.850 1.00 68.96 C
ANISOU 508 C THR A 68 10934 6585 8682 975 446 84 C
ATOM 509 O THR A 68 29.836 164.104 154.587 1.00 69.23 O
ANISOU 509 O THR A 68 11167 6504 8634 1055 509 90 O
ATOM 510 CB THR A 68 31.568 166.571 153.491 1.00 69.37 C
ANISOU 510 CB THR A 68 10789 6794 8774 1073 533 99 C
ATOM 511 OG1 THR A 68 32.249 166.780 154.739 1.00 70.50 O
ANISOU 511 OG1 THR A 68 10764 7054 8970 1162 509 135 O
ATOM 512 CG2 THR A 68 31.850 167.720 152.523 1.00 69.46 C
ANISOU 512 CG2 THR A 68 10694 6877 8821 1007 539 86 C
ATOM 513 N GLY A 69 29.586 165.775 156.076 1.00 69.13 N
ANISOU 513 N GLY A 69 10820 6683 8762 946 379 94 N
ATOM 514 CA GLY A 69 29.408 164.893 157.214 1.00 69.99 C
ANISOU 514 CA GLY A 69 11013 6739 8841 999 375 111 C
ATOM 515 C GLY A 69 30.712 164.311 157.719 1.00 70.76 C
ANISOU 515 C GLY A 69 11088 6882 8917 1204 431 154 C
ATOM 516 O GLY A 69 30.717 163.242 158.330 1.00 71.34 O
ANISOU 516 O GLY A 69 11297 6877 8932 1293 459 172 O
ATOM 517 N PHE A 70 31.820 165.024 157.501 1.00 70.70 N
ANISOU 517 N PHE A 70 10894 7009 8958 1279 442 175 N
ATOM 518 CA PHE A 70 33.170 164.626 157.893 1.00 71.23 C
ANISOU 518 CA PHE A 70 10889 7155 9023 1478 487 223 C
ATOM 519 C PHE A 70 33.292 164.258 159.373 1.00 71.36 C
ANISOU 519 C PHE A 70 10887 7191 9038 1547 437 251 C
ATOM 520 O PHE A 70 32.548 164.775 160.195 1.00 71.18 O
ANISOU 520 O PHE A 70 10816 7180 9047 1430 356 237 O
ATOM 521 CB PHE A 70 34.160 165.746 157.532 1.00 71.67 C
ANISOU 521 CB PHE A 70 10702 7376 9152 1492 484 239 C
ATOM 522 CG PHE A 70 34.085 166.957 158.438 1.00 72.89 C
ANISOU 522 CG PHE A 70 10659 7650 9387 1384 377 236 C
ATOM 523 CD1 PHE A 70 32.995 167.812 158.395 1.00 73.66 C
ANISOU 523 CD1 PHE A 70 10745 7728 9513 1198 315 196 C
ATOM 524 CD2 PHE A 70 35.093 167.226 159.348 1.00 74.10 C
ANISOU 524 CD2 PHE A 70 10644 7931 9578 1472 336 277 C
ATOM 525 CE1 PHE A 70 32.909 168.900 159.255 1.00 74.19 C
ANISOU 525 CE1 PHE A 70 10657 7890 9642 1108 225 194 C
ATOM 526 CE2 PHE A 70 35.008 168.322 160.201 1.00 74.73 C
ANISOU 526 CE2 PHE A 70 10571 8105 9717 1367 236 273 C
ATOM 527 CZ PHE A 70 33.917 169.153 160.146 1.00 74.19 C
ANISOU 527 CZ PHE A 70 10513 8005 9672 1189 187 231 C
ATOM 528 N CYS A 71 34.229 163.363 159.713 1.00 71.64 N
ANISOU 528 N CYS A 71 10956 7231 9034 1741 483 294 N
ATOM 529 CA CYS A 71 34.441 162.949 161.103 1.00 72.46 C
ANISOU 529 CA CYS A 71 11055 7348 9129 1808 428 321 C
ATOM 530 C CYS A 71 35.000 164.092 161.905 1.00 71.97 C
ANISOU 530 C CYS A 71 10737 7460 9147 1805 346 344 C
ATOM 531 O CYS A 71 35.925 164.762 161.448 1.00 72.29 O
ANISOU 531 O CYS A 71 10613 7622 9233 1863 365 365 O
ATOM 532 CB CYS A 71 35.344 161.724 161.186 1.00 74.40 C
ANISOU 532 CB CYS A 71 11415 7548 9304 2032 496 364 C
ATOM 533 SG CYS A 71 34.598 160.219 160.517 1.00 82.83 S
ANISOU 533 SG CYS A 71 12824 8392 10257 2047 597 340 S
ATOM 534 N ALA A 72 34.433 164.337 163.088 1.00 70.98 N
ANISOU 534 N ALA A 72 10586 7346 9034 1738 260 343 N
ATOM 535 CA ALA A 72 34.899 165.434 163.923 1.00 70.63 C
ANISOU 535 CA ALA A 72 10323 7459 9056 1726 170 365 C
ATOM 536 C ALA A 72 34.553 165.205 165.375 1.00 70.12 C
ANISOU 536 C ALA A 72 10313 7362 8966 1711 97 372 C
ATOM 537 O ALA A 72 33.575 164.529 165.677 1.00 70.56 O
ANISOU 537 O ALA A 72 10550 7284 8974 1655 114 350 O
ATOM 538 CB ALA A 72 34.271 166.742 163.449 1.00 70.75 C
ANISOU 538 CB ALA A 72 10199 7544 9140 1550 131 331 C
ATOM 539 N ALA A 73 35.300 165.830 166.294 1.00 69.19 N
ANISOU 539 N ALA A 73 10040 7368 8881 1746 12 402 N
ATOM 540 CA ALA A 73 34.952 165.800 167.719 1.00 69.12 C
ANISOU 540 CA ALA A 73 10077 7339 8846 1729 -66 411 C
ATOM 541 C ALA A 73 33.644 166.587 167.853 1.00 68.79 C
ANISOU 541 C ALA A 73 10070 7242 8824 1525 -88 362 C
ATOM 542 O ALA A 73 33.515 167.628 167.212 1.00 68.99 O
ANISOU 542 O ALA A 73 9978 7327 8907 1411 -99 337 O
ATOM 543 CB ALA A 73 36.040 166.479 168.528 1.00 69.51 C
ANISOU 543 CB ALA A 73 9931 7548 8933 1778 -165 449 C
ATOM 544 N CYS A 74 32.651 166.072 168.583 1.00 68.27 N
ANISOU 544 N CYS A 74 10170 7059 8711 1481 -85 350 N
ATOM 545 CA CYS A 74 31.331 166.709 168.614 1.00 68.50 C
ANISOU 545 CA CYS A 74 10230 7035 8763 1297 -89 308 C
ATOM 546 C CYS A 74 31.341 168.225 168.874 1.00 67.98 C
ANISOU 546 C CYS A 74 9991 7078 8759 1189 -164 296 C
ATOM 547 O CYS A 74 30.609 168.932 168.186 1.00 68.21 O
ANISOU 547 O CYS A 74 9984 7102 8829 1059 -152 261 O
ATOM 548 CB CYS A 74 30.368 166.000 169.559 1.00 69.78 C
ANISOU 548 CB CYS A 74 10572 7072 8868 1267 -74 305 C
ATOM 549 SG CYS A 74 28.618 166.403 169.260 1.00 72.98 S
ANISOU 549 SG CYS A 74 11035 7392 9301 1057 -42 257 S
ATOM 550 N HIS A 75 32.164 168.724 169.806 1.00 67.22 N
ANISOU 550 N HIS A 75 9796 7078 8666 1240 -243 324 N
ATOM 551 CA HIS A 75 32.171 170.156 170.093 1.00 67.10 C
ANISOU 551 CA HIS A 75 9643 7154 8697 1131 -315 312 C
ATOM 552 C HIS A 75 32.791 171.002 168.991 1.00 65.80 C
ANISOU 552 C HIS A 75 9315 7093 8594 1094 -316 305 C
ATOM 553 O HIS A 75 32.335 172.121 168.748 1.00 65.79 O
ANISOU 553 O HIS A 75 9250 7117 8631 964 -337 277 O
ATOM 554 CB HIS A 75 32.795 170.447 171.444 1.00 68.72 C
ANISOU 554 CB HIS A 75 9816 7416 8876 1175 -407 343 C
ATOM 555 CG HIS A 75 31.772 170.431 172.529 1.00 72.16 C
ANISOU 555 CG HIS A 75 10386 7760 9272 1113 -414 330 C
ATOM 556 ND1 HIS A 75 31.220 169.242 172.982 1.00 74.31 N
ANISOU 556 ND1 HIS A 75 10837 7913 9483 1171 -364 337 N
ATOM 557 CD2 HIS A 75 31.198 171.464 173.190 1.00 73.62 C
ANISOU 557 CD2 HIS A 75 10559 7949 9466 997 -454 310 C
ATOM 558 CE1 HIS A 75 30.351 169.587 173.918 1.00 75.06 C
ANISOU 558 CE1 HIS A 75 11011 7953 9557 1088 -373 324 C
ATOM 559 NE2 HIS A 75 30.305 170.914 174.082 1.00 75.04 N
ANISOU 559 NE2 HIS A 75 10898 8019 9593 989 -424 308 N
ATOM 560 N GLY A 76 33.777 170.457 168.300 1.00 64.63 N
ANISOU 560 N GLY A 76 9110 6993 8451 1207 -283 330 N
ATOM 561 CA GLY A 76 34.380 171.148 167.166 1.00 64.13 C
ANISOU 561 CA GLY A 76 8905 7022 8442 1177 -264 325 C
ATOM 562 C GLY A 76 33.382 171.248 166.032 1.00 63.57 C
ANISOU 562 C GLY A 76 8904 6867 8382 1075 -197 281 C
ATOM 563 O GLY A 76 33.246 172.296 165.397 1.00 63.79 O
ANISOU 563 O GLY A 76 8846 6940 8452 965 -209 258 O
ATOM 564 N CYS A 77 32.620 170.168 165.833 1.00 62.76 N
ANISOU 564 N CYS A 77 8973 6637 8237 1101 -135 268 N
ATOM 565 CA CYS A 77 31.545 170.046 164.865 1.00 62.53 C
ANISOU 565 CA CYS A 77 9043 6509 8206 1006 -81 229 C
ATOM 566 C CYS A 77 30.490 171.131 165.142 1.00 61.09 C
ANISOU 566 C CYS A 77 8832 6324 8057 848 -129 198 C
ATOM 567 O CYS A 77 30.082 171.862 164.238 1.00 61.33 O
ANISOU 567 O CYS A 77 8820 6363 8120 752 -124 171 O
ATOM 568 CB CYS A 77 30.944 168.650 164.975 1.00 64.17 C
ANISOU 568 CB CYS A 77 9448 6581 8352 1059 -27 230 C
ATOM 569 SG CYS A 77 29.512 168.386 163.928 1.00 71.72 S
ANISOU 569 SG CYS A 77 10540 7409 9300 924 21 185 S
ATOM 570 N LEU A 78 30.108 171.260 166.417 1.00 59.38 N
ANISOU 570 N LEU A 78 8638 6096 7827 831 -175 205 N
ATOM 571 CA LEU A 78 29.145 172.211 166.954 1.00 57.89 C
ANISOU 571 CA LEU A 78 8433 5901 7660 708 -214 183 C
ATOM 572 C LEU A 78 29.568 173.669 166.755 1.00 56.79 C
ANISOU 572 C LEU A 78 8146 5866 7565 641 -269 175 C
ATOM 573 O LEU A 78 28.712 174.554 166.766 1.00 56.92 O
ANISOU 573 O LEU A 78 8152 5873 7601 538 -291 153 O
ATOM 574 CB LEU A 78 29.004 171.901 168.439 1.00 57.62 C
ANISOU 574 CB LEU A 78 8466 5839 7589 743 -243 202 C
ATOM 575 CG LEU A 78 27.641 171.920 169.105 1.00 58.70 C
ANISOU 575 CG LEU A 78 8690 5895 7717 655 -230 185 C
ATOM 576 CD1 LEU A 78 26.522 171.396 168.216 1.00 58.92 C
ANISOU 576 CD1 LEU A 78 8791 5836 7758 580 -168 159 C
ATOM 577 CD2 LEU A 78 27.704 171.134 170.368 1.00 59.35 C
ANISOU 577 CD2 LEU A 78 8878 5928 7743 724 -232 209 C
ATOM 578 N PHE A 79 30.878 173.927 166.600 1.00 55.44 N
ANISOU 578 N PHE A 79 7864 5793 7407 699 -288 196 N
ATOM 579 CA PHE A 79 31.338 175.275 166.338 1.00 54.59 C
ANISOU 579 CA PHE A 79 7625 5779 7336 624 -335 190 C
ATOM 580 C PHE A 79 31.089 175.583 164.880 1.00 55.50 C
ANISOU 580 C PHE A 79 7727 5883 7478 568 -285 165 C
ATOM 581 O PHE A 79 30.500 176.624 164.587 1.00 56.02 O
ANISOU 581 O PHE A 79 7771 5948 7565 460 -306 139 O
ATOM 582 CB PHE A 79 32.810 175.491 166.697 1.00 53.12 C
ANISOU 582 CB PHE A 79 7312 5714 7158 691 -382 227 C
ATOM 583 CG PHE A 79 33.228 176.907 166.386 1.00 52.54 C
ANISOU 583 CG PHE A 79 7116 5729 7118 590 -426 219 C
ATOM 584 CD1 PHE A 79 32.799 177.960 167.170 1.00 52.83 C
ANISOU 584 CD1 PHE A 79 7157 5767 7150 492 -492 205 C
ATOM 585 CD2 PHE A 79 33.983 177.194 165.264 1.00 52.79 C
ANISOU 585 CD2 PHE A 79 7045 5831 7180 589 -393 225 C
ATOM 586 CE1 PHE A 79 33.160 179.265 166.864 1.00 53.28 C
ANISOU 586 CE1 PHE A 79 7123 5892 7228 392 -531 196 C
ATOM 587 CE2 PHE A 79 34.329 178.500 164.953 1.00 53.09 C
ANISOU 587 CE2 PHE A 79 6985 5941 7244 483 -429 217 C
ATOM 588 CZ PHE A 79 33.927 179.525 165.759 1.00 52.86 C
ANISOU 588 CZ PHE A 79 6968 5910 7206 384 -502 202 C
ATOM 589 N ILE A 80 31.546 174.709 163.949 1.00 55.62 N
ANISOU 589 N ILE A 80 7764 5883 7486 644 -219 172 N
ATOM 590 CA ILE A 80 31.342 174.990 162.513 1.00 55.90 C
ANISOU 590 CA ILE A 80 7800 5902 7536 591 -172 148 C
ATOM 591 C ILE A 80 29.855 174.842 162.082 1.00 55.59 C
ANISOU 591 C ILE A 80 7879 5751 7490 504 -157 112 C
ATOM 592 O ILE A 80 29.497 175.269 160.980 1.00 56.08 O
ANISOU 592 O ILE A 80 7945 5797 7564 435 -142 89 O
ATOM 593 CB ILE A 80 32.297 174.226 161.562 1.00 56.42 C
ANISOU 593 CB ILE A 80 7860 5985 7593 692 -98 166 C
ATOM 594 CG1 ILE A 80 31.910 172.766 161.404 1.00 57.42 C
ANISOU 594 CG1 ILE A 80 8142 6003 7674 774 -38 167 C
ATOM 595 CG2 ILE A 80 33.753 174.381 161.970 1.00 56.89 C
ANISOU 595 CG2 ILE A 80 7776 6170 7668 779 -113 207 C
ATOM 596 CD1 ILE A 80 32.244 172.303 160.060 1.00 58.93 C
ANISOU 596 CD1 ILE A 80 8370 6171 7849 815 41 164 C
ATOM 597 N ALA A 81 28.998 174.274 162.954 1.00 54.23 N
ANISOU 597 N ALA A 81 7798 5508 7300 502 -165 111 N
ATOM 598 CA ALA A 81 27.580 174.168 162.691 1.00 53.29 C
ANISOU 598 CA ALA A 81 7766 5299 7182 415 -158 84 C
ATOM 599 C ALA A 81 26.888 175.473 163.105 1.00 52.66 C
ANISOU 599 C ALA A 81 7622 5249 7136 315 -210 69 C
ATOM 600 O ALA A 81 26.023 175.973 162.382 1.00 52.69 O
ANISOU 600 O ALA A 81 7635 5225 7160 232 -214 45 O
ATOM 601 CB ALA A 81 27.000 173.002 163.485 1.00 53.12 C
ANISOU 601 CB ALA A 81 7861 5196 7128 451 -136 94 C
ATOM 602 N CYS A 82 27.291 176.037 164.258 1.00 51.97 N
ANISOU 602 N CYS A 82 7479 5217 7050 330 -253 84 N
ATOM 603 CA CYS A 82 26.640 177.181 164.875 1.00 51.84 C
ANISOU 603 CA CYS A 82 7431 5215 7051 253 -295 73 C
ATOM 604 C CYS A 82 27.209 178.546 164.545 1.00 51.26 C
ANISOU 604 C CYS A 82 7263 5219 6996 205 -336 67 C
ATOM 605 O CYS A 82 26.549 179.542 164.874 1.00 51.69 O
ANISOU 605 O CYS A 82 7312 5270 7060 139 -363 54 O
ATOM 606 CB CYS A 82 26.603 176.986 166.382 1.00 52.64 C
ANISOU 606 CB CYS A 82 7565 5310 7128 286 -315 91 C
ATOM 607 SG CYS A 82 25.561 175.614 166.922 1.00 56.45 S
ANISOU 607 SG CYS A 82 8177 5685 7587 307 -262 95 S
ATOM 608 N PHE A 83 28.410 178.637 163.947 1.00 49.94 N
ANISOU 608 N PHE A 83 7026 5119 6830 237 -335 78 N
ATOM 609 CA PHE A 83 28.998 179.954 163.696 1.00 49.21 C
ANISOU 609 CA PHE A 83 6848 5098 6751 176 -373 74 C
ATOM 610 C PHE A 83 28.086 180.900 162.904 1.00 48.37 C
ANISOU 610 C PHE A 83 6761 4957 6659 84 -375 44 C
ATOM 611 O PHE A 83 28.004 182.082 163.243 1.00 48.52 O
ANISOU 611 O PHE A 83 6758 4999 6677 23 -416 37 O
ATOM 612 CB PHE A 83 30.373 179.861 163.057 1.00 49.01 C
ANISOU 612 CB PHE A 83 6738 5152 6733 217 -357 92 C
ATOM 613 CG PHE A 83 31.037 181.215 163.029 1.00 49.69 C
ANISOU 613 CG PHE A 83 6737 5315 6829 140 -401 92 C
ATOM 614 CD1 PHE A 83 31.338 181.884 164.205 1.00 50.63 C
ANISOU 614 CD1 PHE A 83 6828 5473 6936 108 -471 102 C
ATOM 615 CD2 PHE A 83 31.323 181.838 161.831 1.00 50.31 C
ANISOU 615 CD2 PHE A 83 6781 5417 6919 92 -373 81 C
ATOM 616 CE1 PHE A 83 31.948 183.136 164.179 1.00 51.17 C
ANISOU 616 CE1 PHE A 83 6832 5604 7005 23 -515 101 C
ATOM 617 CE2 PHE A 83 31.938 183.083 161.810 1.00 50.98 C
ANISOU 617 CE2 PHE A 83 6796 5567 7008 10 -411 82 C
ATOM 618 CZ PHE A 83 32.236 183.730 162.982 1.00 50.77 C
ANISOU 618 CZ PHE A 83 6741 5578 6969 -28 -483 92 C
ATOM 619 N VAL A 84 27.347 180.364 161.910 1.00 46.98 N
ANISOU 619 N VAL A 84 6640 4720 6490 76 -335 27 N
ATOM 620 CA VAL A 84 26.420 181.160 161.097 1.00 45.59 C
ANISOU 620 CA VAL A 84 6487 4509 6326 0 -343 2 C
ATOM 621 C VAL A 84 25.308 181.780 161.949 1.00 44.64 C
ANISOU 621 C VAL A 84 6388 4361 6214 -39 -373 -5 C
ATOM 622 O VAL A 84 24.842 182.879 161.644 1.00 45.11 O
ANISOU 622 O VAL A 84 6441 4419 6278 -93 -398 -19 O
ATOM 623 CB VAL A 84 25.847 180.331 159.938 1.00 45.54 C
ANISOU 623 CB VAL A 84 6546 4440 6319 0 -307 -11 C
ATOM 624 CG1 VAL A 84 25.100 179.112 160.454 1.00 45.67 C
ANISOU 624 CG1 VAL A 84 6627 4397 6330 37 -284 -5 C
ATOM 625 CG2 VAL A 84 24.959 181.178 159.037 1.00 45.95 C
ANISOU 625 CG2 VAL A 84 6619 4457 6382 -74 -330 -34 C
ATOM 626 N LEU A 85 24.916 181.110 163.043 1.00 42.96 N
ANISOU 626 N LEU A 85 6204 4122 5997 -4 -366 6 N
ATOM 627 CA LEU A 85 23.902 181.629 163.937 1.00 41.76 C
ANISOU 627 CA LEU A 85 6074 3943 5850 -30 -378 4 C
ATOM 628 C LEU A 85 24.416 182.872 164.662 1.00 41.60 C
ANISOU 628 C LEU A 85 6028 3966 5812 -49 -419 6 C
ATOM 629 O LEU A 85 23.623 183.772 164.928 1.00 41.66 O
ANISOU 629 O LEU A 85 6053 3953 5822 -82 -429 -2 O
ATOM 630 CB LEU A 85 23.454 180.551 164.918 1.00 41.40 C
ANISOU 630 CB LEU A 85 6076 3857 5796 11 -350 18 C
ATOM 631 CG LEU A 85 22.995 179.232 164.278 1.00 42.19 C
ANISOU 631 CG LEU A 85 6223 3905 5902 24 -310 18 C
ATOM 632 CD1 LEU A 85 22.648 178.210 165.325 1.00 42.78 C
ANISOU 632 CD1 LEU A 85 6357 3936 5960 58 -280 33 C
ATOM 633 CD2 LEU A 85 21.814 179.444 163.374 1.00 42.31 C
ANISOU 633 CD2 LEU A 85 6242 3885 5948 -39 -307 1 C
ATOM 634 N VAL A 86 25.741 182.957 164.941 1.00 41.21 N
ANISOU 634 N VAL A 86 5939 3974 5745 -32 -443 18 N
ATOM 635 CA VAL A 86 26.345 184.143 165.563 1.00 41.07 C
ANISOU 635 CA VAL A 86 5903 3998 5704 -67 -492 21 C
ATOM 636 C VAL A 86 26.228 185.323 164.622 1.00 41.45 C
ANISOU 636 C VAL A 86 5938 4054 5755 -134 -505 4 C
ATOM 637 O VAL A 86 25.861 186.419 165.044 1.00 42.15 O
ANISOU 637 O VAL A 86 6057 4133 5825 -174 -531 -3 O
ATOM 638 CB VAL A 86 27.821 183.928 165.923 1.00 41.20 C
ANISOU 638 CB VAL A 86 5857 4089 5707 -43 -521 42 C
ATOM 639 CG1 VAL A 86 28.414 185.185 166.533 1.00 41.11 C
ANISOU 639 CG1 VAL A 86 5825 4121 5673 -109 -578 42 C
ATOM 640 CG2 VAL A 86 27.980 182.738 166.849 1.00 42.08 C
ANISOU 640 CG2 VAL A 86 5991 4195 5802 29 -524 64 C
ATOM 641 N LEU A 87 26.532 185.102 163.341 1.00 40.74 N
ANISOU 641 N LEU A 87 5818 3979 5683 -142 -483 -3 N
ATOM 642 CA LEU A 87 26.466 186.148 162.349 1.00 40.47 C
ANISOU 642 CA LEU A 87 5785 3944 5647 -204 -490 -19 C
ATOM 643 C LEU A 87 25.037 186.589 162.111 1.00 40.53 C
ANISOU 643 C LEU A 87 5850 3887 5664 -220 -488 -36 C
ATOM 644 O LEU A 87 24.792 187.790 162.009 1.00 41.00 O
ANISOU 644 O LEU A 87 5937 3936 5706 -263 -512 -46 O
ATOM 645 CB LEU A 87 27.132 185.694 161.049 1.00 40.14 C
ANISOU 645 CB LEU A 87 5712 3923 5616 -200 -457 -21 C
ATOM 646 CG LEU A 87 28.568 185.223 161.171 1.00 40.77 C
ANISOU 646 CG LEU A 87 5718 4078 5696 -171 -447 1 C
ATOM 647 CD1 LEU A 87 29.104 184.856 159.825 1.00 41.21 C
ANISOU 647 CD1 LEU A 87 5757 4142 5757 -165 -398 -1 C
ATOM 648 CD2 LEU A 87 29.462 186.273 161.832 1.00 40.98 C
ANISOU 648 CD2 LEU A 87 5694 4170 5706 -225 -496 12 C
ATOM 649 N ALA A 88 24.087 185.645 162.076 1.00 40.09 N
ANISOU 649 N ALA A 88 5813 3788 5631 -186 -462 -37 N
ATOM 650 CA ALA A 88 22.686 186.007 161.888 1.00 40.74 C
ANISOU 650 CA ALA A 88 5926 3822 5731 -199 -463 -47 C
ATOM 651 C ALA A 88 22.181 186.821 163.061 1.00 41.92 C
ANISOU 651 C ALA A 88 6099 3960 5867 -195 -473 -42 C
ATOM 652 O ALA A 88 21.443 187.784 162.862 1.00 41.83 O
ANISOU 652 O ALA A 88 6111 3927 5854 -210 -484 -50 O
ATOM 653 CB ALA A 88 21.839 184.767 161.717 1.00 40.76 C
ANISOU 653 CB ALA A 88 5936 3789 5763 -178 -436 -44 C
ATOM 654 N GLN A 89 22.610 186.463 164.282 1.00 42.91 N
ANISOU 654 N GLN A 89 6231 4098 5976 -169 -469 -29 N
ATOM 655 CA GLN A 89 22.201 187.175 165.484 1.00 44.15 C
ANISOU 655 CA GLN A 89 6432 4235 6108 -161 -473 -24 C
ATOM 656 C GLN A 89 22.794 188.551 165.533 1.00 44.74 C
ANISOU 656 C GLN A 89 6534 4324 6143 -203 -512 -31 C
ATOM 657 O GLN A 89 22.095 189.494 165.893 1.00 45.03 O
ANISOU 657 O GLN A 89 6623 4325 6162 -204 -510 -36 O
ATOM 658 CB GLN A 89 22.555 186.400 166.753 1.00 46.40 C
ANISOU 658 CB GLN A 89 6735 4523 6374 -124 -465 -7 C
ATOM 659 CG GLN A 89 21.754 186.876 167.965 1.00 51.00 C
ANISOU 659 CG GLN A 89 7381 5065 6932 -106 -446 -2 C
ATOM 660 CD GLN A 89 20.280 186.652 167.748 1.00 56.62 C
ANISOU 660 CD GLN A 89 8088 5738 7686 -90 -395 -1 C
ATOM 661 OE1 GLN A 89 19.859 185.589 167.278 1.00 58.82 O
ANISOU 661 OE1 GLN A 89 8331 6012 8005 -85 -370 1 O
ATOM 662 NE2 GLN A 89 19.471 187.658 168.047 1.00 57.45 N
ANISOU 662 NE2 GLN A 89 8231 5817 7781 -83 -380 -2 N
ATOM 663 N SER A 90 24.064 188.692 165.128 1.00 44.90 N
ANISOU 663 N SER A 90 6523 4391 6147 -237 -543 -31 N
ATOM 664 CA SER A 90 24.696 190.002 165.069 1.00 45.72 C
ANISOU 664 CA SER A 90 6659 4503 6209 -296 -581 -38 C
ATOM 665 C SER A 90 23.978 190.906 164.065 1.00 46.68 C
ANISOU 665 C SER A 90 6814 4588 6335 -318 -573 -54 C
ATOM 666 O SER A 90 23.812 192.095 164.320 1.00 46.89 O
ANISOU 666 O SER A 90 6909 4583 6323 -341 -589 -61 O
ATOM 667 CB SER A 90 26.154 189.871 164.678 1.00 46.83 C
ANISOU 667 CB SER A 90 6740 4712 6342 -338 -609 -32 C
ATOM 668 OG SER A 90 26.688 191.178 164.565 1.00 49.62 O
ANISOU 668 OG SER A 90 7120 5067 6666 -412 -633 -42 O
ATOM 669 N SER A 91 23.547 190.330 162.936 1.00 46.98 N
ANISOU 669 N SER A 91 6813 4626 6409 -310 -554 -60 N
ATOM 670 CA SER A 91 22.800 191.041 161.916 1.00 47.64 C
ANISOU 670 CA SER A 91 6931 4674 6496 -323 -555 -73 C
ATOM 671 C SER A 91 21.474 191.557 162.498 1.00 48.35 C
ANISOU 671 C SER A 91 7068 4716 6588 -282 -547 -72 C
ATOM 672 O SER A 91 21.125 192.718 162.295 1.00 48.49 O
ANISOU 672 O SER A 91 7147 4702 6576 -292 -560 -78 O
ATOM 673 CB SER A 91 22.546 190.132 160.715 1.00 48.80 C
ANISOU 673 CB SER A 91 7040 4822 6681 -313 -539 -78 C
ATOM 674 OG SER A 91 23.758 189.787 160.063 1.00 51.09 O
ANISOU 674 OG SER A 91 7296 5151 6964 -341 -533 -78 O
ATOM 675 N ILE A 92 20.759 190.711 163.257 1.00 48.65 N
ANISOU 675 N ILE A 92 7082 4747 6657 -235 -520 -61 N
ATOM 676 CA ILE A 92 19.483 191.069 163.879 1.00 49.38 C
ANISOU 676 CA ILE A 92 7200 4803 6758 -191 -498 -54 C
ATOM 677 C ILE A 92 19.665 192.238 164.819 1.00 50.20 C
ANISOU 677 C ILE A 92 7386 4883 6804 -189 -501 -53 C
ATOM 678 O ILE A 92 18.866 193.172 164.786 1.00 50.35 O
ANISOU 678 O ILE A 92 7453 4865 6813 -154 -486 -51 O
ATOM 679 CB ILE A 92 18.843 189.826 164.554 1.00 49.82 C
ANISOU 679 CB ILE A 92 7215 4858 6855 -152 -457 -40 C
ATOM 680 CG1 ILE A 92 18.091 189.005 163.517 1.00 50.42 C
ANISOU 680 CG1 ILE A 92 7230 4945 6984 -161 -455 -41 C
ATOM 681 CG2 ILE A 92 17.928 190.168 165.744 1.00 50.34 C
ANISOU 681 CG2 ILE A 92 7300 4894 6932 -104 -420 -28 C
ATOM 682 CD1 ILE A 92 17.898 187.669 163.908 1.00 51.46 C
ANISOU 682 CD1 ILE A 92 7332 5074 7146 -142 -417 -28 C
ATOM 683 N PHE A 93 20.728 192.205 165.628 1.00 50.62 N
ANISOU 683 N PHE A 93 7461 4956 6817 -222 -523 -53 N
ATOM 684 CA PHE A 93 21.002 193.294 166.552 1.00 51.52 C
ANISOU 684 CA PHE A 93 7670 5040 6865 -233 -535 -53 C
ATOM 685 C PHE A 93 21.327 194.600 165.798 1.00 51.84 C
ANISOU 685 C PHE A 93 7777 5060 6861 -280 -566 -66 C
ATOM 686 O PHE A 93 20.857 195.665 166.202 1.00 52.10 O
ANISOU 686 O PHE A 93 7908 5039 6847 -264 -559 -68 O
ATOM 687 CB PHE A 93 22.124 192.927 167.524 1.00 51.75 C
ANISOU 687 CB PHE A 93 7697 5103 6864 -262 -564 -47 C
ATOM 688 CG PHE A 93 21.729 191.967 168.622 1.00 52.95 C
ANISOU 688 CG PHE A 93 7858 5241 7019 -207 -532 -33 C
ATOM 689 CD1 PHE A 93 20.507 192.080 169.262 1.00 54.02 C
ANISOU 689 CD1 PHE A 93 8045 5325 7154 -151 -479 -27 C
ATOM 690 CD2 PHE A 93 22.608 190.997 169.064 1.00 54.03 C
ANISOU 690 CD2 PHE A 93 7956 5416 7157 -209 -550 -22 C
ATOM 691 CE1 PHE A 93 20.160 191.210 170.296 1.00 54.86 C
ANISOU 691 CE1 PHE A 93 8170 5416 7260 -106 -439 -13 C
ATOM 692 CE2 PHE A 93 22.257 190.127 170.092 1.00 54.89 C
ANISOU 692 CE2 PHE A 93 8091 5505 7261 -159 -519 -9 C
ATOM 693 CZ PHE A 93 21.038 190.242 170.706 1.00 54.67 C
ANISOU 693 CZ PHE A 93 8121 5422 7230 -113 -461 -5 C
ATOM 694 N SER A 94 22.093 194.520 164.690 1.00 51.26 N
ANISOU 694 N SER A 94 7659 5021 6795 -338 -593 -75 N
ATOM 695 CA SER A 94 22.409 195.711 163.908 1.00 50.82 C
ANISOU 695 CA SER A 94 7673 4943 6695 -392 -617 -86 C
ATOM 696 C SER A 94 21.156 196.272 163.262 1.00 50.55 C
ANISOU 696 C SER A 94 7681 4856 6669 -337 -598 -90 C
ATOM 697 O SER A 94 20.933 197.473 163.330 1.00 50.98 O
ANISOU 697 O SER A 94 7841 4855 6672 -323 -598 -92 O
ATOM 698 CB SER A 94 23.461 195.407 162.855 1.00 51.78 C
ANISOU 698 CB SER A 94 7727 5113 6836 -452 -631 -91 C
ATOM 699 OG SER A 94 24.695 195.126 163.489 1.00 54.24 O
ANISOU 699 OG SER A 94 7996 5479 7135 -504 -654 -84 O
ATOM 700 N LEU A 95 20.309 195.416 162.687 1.00 49.68 N
ANISOU 700 N LEU A 95 7491 4762 6624 -297 -583 -87 N
ATOM 701 CA LEU A 95 19.072 195.855 162.062 1.00 49.38 C
ANISOU 701 CA LEU A 95 7467 4689 6607 -240 -576 -85 C
ATOM 702 C LEU A 95 18.144 196.514 163.080 1.00 49.68 C
ANISOU 702 C LEU A 95 7560 4684 6631 -166 -547 -74 C
ATOM 703 O LEU A 95 17.527 197.530 162.781 1.00 50.13 O
ANISOU 703 O LEU A 95 7674 4703 6671 -126 -550 -73 O
ATOM 704 CB LEU A 95 18.379 194.660 161.423 1.00 49.19 C
ANISOU 704 CB LEU A 95 7336 4695 6658 -214 -566 -80 C
ATOM 705 CG LEU A 95 19.010 194.173 160.163 1.00 50.34 C
ANISOU 705 CG LEU A 95 7448 4858 6821 -254 -590 -90 C
ATOM 706 CD1 LEU A 95 18.442 192.843 159.760 1.00 50.77 C
ANISOU 706 CD1 LEU A 95 7421 4926 6942 -222 -582 -81 C
ATOM 707 CD2 LEU A 95 18.763 195.143 159.066 1.00 51.24 C
ANISOU 707 CD2 LEU A 95 7640 4931 6898 -256 -616 -97 C
ATOM 708 N LEU A 96 18.055 195.943 164.282 1.00 49.26 N
ANISOU 708 N LEU A 96 7488 4639 6590 -137 -514 -64 N
ATOM 709 CA LEU A 96 17.217 196.482 165.342 1.00 49.33 C
ANISOU 709 CA LEU A 96 7549 4608 6584 -61 -470 -50 C
ATOM 710 C LEU A 96 17.771 197.842 165.810 1.00 49.63 C
ANISOU 710 C LEU A 96 7737 4593 6528 -78 -478 -58 C
ATOM 711 O LEU A 96 17.003 198.783 166.007 1.00 50.02 O
ANISOU 711 O LEU A 96 7868 4592 6545 -10 -442 -49 O
ATOM 712 CB LEU A 96 17.150 195.452 166.489 1.00 49.09 C
ANISOU 712 CB LEU A 96 7466 4600 6586 -38 -429 -38 C
ATOM 713 CG LEU A 96 16.335 195.765 167.730 1.00 49.81 C
ANISOU 713 CG LEU A 96 7631 4651 6643 21 -373 -24 C
ATOM 714 CD1 LEU A 96 14.940 196.206 167.382 1.00 50.48 C
ANISOU 714 CD1 LEU A 96 7722 4709 6750 112 -324 -9 C
ATOM 715 CD2 LEU A 96 16.266 194.552 168.620 1.00 50.00 C
ANISOU 715 CD2 LEU A 96 7594 4701 6703 29 -337 -13 C
ATOM 716 N ALA A 97 19.101 197.968 165.907 1.00 49.12 N
ANISOU 716 N ALA A 97 7710 4538 6415 -170 -524 -72 N
ATOM 717 CA ALA A 97 19.722 199.227 166.310 1.00 49.13 C
ANISOU 717 CA ALA A 97 7863 4486 6319 -208 -542 -79 C
ATOM 718 C ALA A 97 19.499 200.307 165.273 1.00 48.66 C
ANISOU 718 C ALA A 97 7893 4382 6214 -232 -564 -90 C
ATOM 719 O ALA A 97 19.261 201.451 165.634 1.00 48.94 O
ANISOU 719 O ALA A 97 8079 4352 6163 -247 -570 -95 O
ATOM 720 CB ALA A 97 21.208 199.031 166.536 1.00 49.46 C
ANISOU 720 CB ALA A 97 7898 4565 6330 -305 -586 -84 C
ATOM 721 N ILE A 98 19.556 199.953 163.989 1.00 47.94 N
ANISOU 721 N ILE A 98 7723 4321 6173 -237 -578 -93 N
ATOM 722 CA ILE A 98 19.324 200.913 162.920 1.00 47.93 C
ANISOU 722 CA ILE A 98 7810 4273 6127 -255 -598 -102 C
ATOM 723 C ILE A 98 17.887 201.435 162.983 1.00 48.48 C
ANISOU 723 C ILE A 98 7930 4292 6200 -136 -570 -91 C
ATOM 724 O ILE A 98 17.671 202.641 162.851 1.00 48.80 O
ANISOU 724 O ILE A 98 8094 4270 6178 -122 -579 -95 O
ATOM 725 CB ILE A 98 19.696 200.297 161.563 1.00 47.93 C
ANISOU 725 CB ILE A 98 7713 4320 6179 -294 -621 -108 C
ATOM 726 CG1 ILE A 98 21.221 200.180 161.457 1.00 48.60 C
ANISOU 726 CG1 ILE A 98 7764 4451 6250 -412 -645 -118 C
ATOM 727 CG2 ILE A 98 19.131 201.102 160.405 1.00 48.25 C
ANISOU 727 CG2 ILE A 98 7841 4306 6184 -276 -636 -113 C
ATOM 728 CD1 ILE A 98 21.735 199.319 160.322 1.00 49.74 C
ANISOU 728 CD1 ILE A 98 7807 4645 6448 -440 -650 -121 C
ATOM 729 N ALA A 99 16.919 200.545 163.260 1.00 48.36 N
ANISOU 729 N ALA A 99 7813 4305 6256 -48 -533 -74 N
ATOM 730 CA ALA A 99 15.520 200.941 163.375 1.00 48.62 C
ANISOU 730 CA ALA A 99 7852 4310 6310 74 -501 -56 C
ATOM 731 C ALA A 99 15.338 201.877 164.555 1.00 49.01 C
ANISOU 731 C ALA A 99 8031 4296 6294 141 -452 -47 C
ATOM 732 O ALA A 99 14.689 202.907 164.410 1.00 49.44 O
ANISOU 732 O ALA A 99 8127 4314 6344 250 -420 -31 O
ATOM 733 CB ALA A 99 14.629 199.721 163.526 1.00 48.60 C
ANISOU 733 CB ALA A 99 7677 4374 6416 123 -478 -38 C
ATOM 734 N ILE A 100 15.956 201.568 165.699 1.00 49.00 N
ANISOU 734 N ILE A 100 8092 4283 6243 83 -445 -55 N
ATOM 735 CA ILE A 100 15.827 202.414 166.886 1.00 49.39 C
ANISOU 735 CA ILE A 100 8292 4260 6214 136 -398 -50 C
ATOM 736 C ILE A 100 16.509 203.768 166.687 1.00 50.25 C
ANISOU 736 C ILE A 100 8586 4295 6211 70 -437 -67 C
ATOM 737 O ILE A 100 15.970 204.798 167.095 1.00 50.44 O
ANISOU 737 O ILE A 100 8780 4234 6152 127 -407 -65 O
ATOM 738 CB ILE A 100 16.294 201.670 168.143 1.00 49.20 C
ANISOU 738 CB ILE A 100 8261 4254 6180 95 -384 -50 C
ATOM 739 CG1 ILE A 100 15.329 200.528 168.428 1.00 50.07 C
ANISOU 739 CG1 ILE A 100 8235 4410 6380 180 -321 -28 C
ATOM 740 CG2 ILE A 100 16.369 202.601 169.331 1.00 49.31 C
ANISOU 740 CG2 ILE A 100 8483 4175 6076 108 -360 -52 C
ATOM 741 CD1 ILE A 100 15.857 199.540 169.343 1.00 51.74 C
ANISOU 741 CD1 ILE A 100 8399 4657 6602 126 -322 -29 C
ATOM 742 N ASP A 101 17.633 203.785 165.970 1.00 50.55 N
ANISOU 742 N ASP A 101 8599 4366 6243 -57 -500 -85 N
ATOM 743 CA ASP A 101 18.343 205.014 165.679 1.00 51.67 C
ANISOU 743 CA ASP A 101 8916 4437 6278 -137 -537 -101 C
ATOM 744 C ASP A 101 17.459 205.931 164.837 1.00 53.38 C
ANISOU 744 C ASP A 101 9217 4592 6472 -45 -523 -96 C
ATOM 745 O ASP A 101 17.338 207.117 165.142 1.00 53.24 O
ANISOU 745 O ASP A 101 9399 4476 6354 -15 -508 -97 O
ATOM 746 CB ASP A 101 19.665 204.700 164.959 1.00 52.86 C
ANISOU 746 CB ASP A 101 8996 4648 6440 -289 -598 -116 C
ATOM 747 CG ASP A 101 20.416 205.929 164.495 1.00 57.51 C
ANISOU 747 CG ASP A 101 9754 5171 6925 -392 -634 -131 C
ATOM 748 OD1 ASP A 101 21.022 206.599 165.335 1.00 58.56 O
ANISOU 748 OD1 ASP A 101 10031 5253 6967 -458 -649 -137 O
ATOM 749 OD2 ASP A 101 20.381 206.224 163.293 1.00 59.68 O
ANISOU 749 OD2 ASP A 101 10031 5441 7205 -410 -647 -136 O
ATOM 750 N ARG A 102 16.798 205.369 163.817 1.00 54.84 N
ANISOU 750 N ARG A 102 9259 4831 6748 7 -529 -88 N
ATOM 751 CA ARG A 102 15.923 206.154 162.961 1.00 56.93 C
ANISOU 751 CA ARG A 102 9582 5049 7001 104 -528 -78 C
ATOM 752 C ARG A 102 14.677 206.647 163.684 1.00 59.13 C
ANISOU 752 C ARG A 102 9935 5273 7261 265 -464 -56 C
ATOM 753 O ARG A 102 14.188 207.737 163.376 1.00 59.52 O
ANISOU 753 O ARG A 102 10145 5237 7234 336 -456 -51 O
ATOM 754 CB ARG A 102 15.569 205.393 161.689 1.00 58.50 C
ANISOU 754 CB ARG A 102 9599 5323 7305 125 -555 -72 C
ATOM 755 CG ARG A 102 16.773 205.054 160.804 1.00 62.44 C
ANISOU 755 CG ARG A 102 10102 5834 7789 6 -611 -91 C
ATOM 756 CD ARG A 102 17.445 206.264 160.168 1.00 66.74 C
ANISOU 756 CD ARG A 102 10865 6281 8212 -37 -626 -103 C
ATOM 757 NE ARG A 102 18.393 206.897 161.086 1.00 70.47 N
ANISOU 757 NE ARG A 102 11413 6744 8619 -185 -636 -122 N
ATOM 758 CZ ARG A 102 18.505 208.209 161.273 1.00 72.51 C
ANISOU 758 CZ ARG A 102 11879 6911 8760 -230 -634 -130 C
ATOM 759 NH1 ARG A 102 17.757 209.052 160.575 1.00 72.56 N
ANISOU 759 NH1 ARG A 102 12051 6820 8697 -124 -615 -122 N
ATOM 760 NH2 ARG A 102 19.388 208.688 162.139 1.00 71.92 N
ANISOU 760 NH2 ARG A 102 11848 6842 8636 -380 -655 -144 N
ATOM 761 N TYR A 103 14.174 205.870 164.659 1.00 60.32 N
ANISOU 761 N TYR A 103 9974 5469 7476 328 -413 -40 N
ATOM 762 CA TYR A 103 13.024 206.296 165.452 1.00 61.91 C
ANISOU 762 CA TYR A 103 10229 5628 7667 487 -335 -14 C
ATOM 763 C TYR A 103 13.409 207.482 166.337 1.00 63.36 C
ANISOU 763 C TYR A 103 10675 5692 7706 488 -307 -24 C
ATOM 764 O TYR A 103 12.631 208.423 166.453 1.00 63.63 O
ANISOU 764 O TYR A 103 10841 5650 7685 616 -261 -9 O
ATOM 765 CB TYR A 103 12.466 205.158 166.318 1.00 62.16 C
ANISOU 765 CB TYR A 103 10100 5730 7790 534 -276 4 C
ATOM 766 CG TYR A 103 11.322 205.607 167.202 1.00 63.46 C
ANISOU 766 CG TYR A 103 10320 5850 7940 696 -179 33 C
ATOM 767 CD1 TYR A 103 10.068 205.869 166.669 1.00 64.76 C
ANISOU 767 CD1 TYR A 103 10418 6030 8159 842 -150 64 C
ATOM 768 CD2 TYR A 103 11.514 205.847 168.554 1.00 64.51 C
ANISOU 768 CD2 TYR A 103 10592 5923 7997 708 -116 32 C
ATOM 769 CE1 TYR A 103 9.020 206.312 167.467 1.00 65.81 C
ANISOU 769 CE1 TYR A 103 10599 6127 8280 1004 -50 95 C
ATOM 770 CE2 TYR A 103 10.476 206.299 169.361 1.00 65.65 C
ANISOU 770 CE2 TYR A 103 10807 6019 8119 866 -12 60 C
ATOM 771 CZ TYR A 103 9.224 206.520 168.816 1.00 66.72 C
ANISOU 771 CZ TYR A 103 10855 6178 8318 1018 27 93 C
ATOM 772 OH TYR A 103 8.177 206.949 169.602 1.00 68.31 O
ANISOU 772 OH TYR A 103 11107 6342 8506 1188 142 126 O
ATOM 773 N ILE A 104 14.598 207.446 166.970 1.00 64.03 N
ANISOU 773 N ILE A 104 10841 5760 7726 349 -335 -47 N
ATOM 774 CA ILE A 104 15.044 208.563 167.809 1.00 65.09 C
ANISOU 774 CA ILE A 104 11241 5777 7714 325 -322 -58 C
ATOM 775 C ILE A 104 15.202 209.822 166.960 1.00 66.94 C
ANISOU 775 C ILE A 104 11654 5924 7856 310 -355 -68 C
ATOM 776 O ILE A 104 14.778 210.896 167.372 1.00 67.31 O
ANISOU 776 O ILE A 104 11922 5856 7795 389 -315 -64 O
ATOM 777 CB ILE A 104 16.358 208.225 168.553 1.00 64.97 C
ANISOU 777 CB ILE A 104 11258 5775 7654 160 -370 -79 C
ATOM 778 CG1 ILE A 104 16.171 207.038 169.485 1.00 65.54 C
ANISOU 778 CG1 ILE A 104 11194 5913 7797 189 -332 -67 C
ATOM 779 CG2 ILE A 104 16.901 209.436 169.309 1.00 65.22 C
ANISOU 779 CG2 ILE A 104 11578 5680 7522 101 -379 -93 C
ATOM 780 CD1 ILE A 104 17.451 206.487 169.951 1.00 66.73 C
ANISOU 780 CD1 ILE A 104 11314 6106 7934 37 -395 -83 C
ATOM 781 N ALA A 105 15.758 209.678 165.756 1.00 68.07 N
ANISOU 781 N ALA A 105 11712 6114 8036 218 -421 -80 N
ATOM 782 CA ALA A 105 15.962 210.812 164.868 1.00 69.82 C
ANISOU 782 CA ALA A 105 12103 6255 8172 193 -454 -90 C
ATOM 783 C ALA A 105 14.673 211.485 164.432 1.00 71.45 C
ANISOU 783 C ALA A 105 12375 6403 8368 384 -412 -67 C
ATOM 784 O ALA A 105 14.645 212.709 164.318 1.00 71.64 O
ANISOU 784 O ALA A 105 12641 6309 8272 413 -405 -70 O
ATOM 785 CB ALA A 105 16.766 210.388 163.656 1.00 70.10 C
ANISOU 785 CB ALA A 105 12015 6360 8260 66 -521 -104 C
ATOM 786 N ILE A 106 13.611 210.713 164.202 1.00 72.59 N
ANISOU 786 N ILE A 106 12316 6630 8636 515 -386 -41 N
ATOM 787 CA ILE A 106 12.352 211.302 163.768 1.00 74.45 C
ANISOU 787 CA ILE A 106 12584 6828 8874 705 -354 -13 C
ATOM 788 C ILE A 106 11.464 211.755 164.928 1.00 75.93 C
ANISOU 788 C ILE A 106 12869 6958 9024 869 -256 11 C
ATOM 789 O ILE A 106 10.748 212.742 164.788 1.00 76.15 O
ANISOU 789 O ILE A 106 13044 6902 8987 1014 -223 29 O
ATOM 790 CB ILE A 106 11.598 210.372 162.802 1.00 75.40 C
ANISOU 790 CB ILE A 106 12447 7063 9138 764 -385 6 C
ATOM 791 CG1 ILE A 106 10.567 211.171 161.990 1.00 76.41 C
ANISOU 791 CG1 ILE A 106 12632 7149 9252 928 -391 33 C
ATOM 792 CG2 ILE A 106 10.935 209.210 163.546 1.00 76.10 C
ANISOU 792 CG2 ILE A 106 12311 7254 9351 818 -336 27 C
ATOM 793 CD1 ILE A 106 10.349 210.632 160.696 1.00 77.76 C
ANISOU 793 CD1 ILE A 106 12650 7391 9503 910 -466 37 C
ATOM 794 N ALA A 107 11.504 211.052 166.064 1.00 76.84 N
ANISOU 794 N ALA A 107 12915 7109 9171 855 -206 13 N
ATOM 795 CA ALA A 107 10.622 211.357 167.185 1.00 78.35 C
ANISOU 795 CA ALA A 107 13185 7251 9333 1014 -98 38 C
ATOM 796 C ALA A 107 11.144 212.458 168.090 1.00 79.86 C
ANISOU 796 C ALA A 107 13698 7293 9351 996 -66 22 C
ATOM 797 O ALA A 107 10.371 213.296 168.547 1.00 79.95 O
ANISOU 797 O ALA A 107 13872 7213 9291 1159 12 42 O
ATOM 798 CB ALA A 107 10.321 210.099 167.985 1.00 78.50 C
ANISOU 798 CB ALA A 107 12998 7367 9459 1017 -49 50 C
ATOM 799 N ILE A 108 12.448 212.472 168.342 1.00 80.97 N
ANISOU 799 N ILE A 108 13935 7408 9421 799 -128 -13 N
ATOM 800 CA ILE A 108 13.062 213.497 169.179 1.00 82.54 C
ANISOU 800 CA ILE A 108 14451 7464 9447 746 -119 -31 C
ATOM 801 C ILE A 108 14.326 214.050 168.520 1.00 84.16 C
ANISOU 801 C ILE A 108 14775 7630 9572 545 -220 -64 C
ATOM 802 O ILE A 108 15.425 213.873 169.047 1.00 84.27 O
ANISOU 802 O ILE A 108 14829 7649 9543 367 -272 -87 O
ATOM 803 CB ILE A 108 13.340 212.974 170.608 1.00 83.23 C
ANISOU 803 CB ILE A 108 14573 7545 9506 709 -79 -35 C
ATOM 804 CG1 ILE A 108 13.973 211.567 170.592 1.00 84.27 C
ANISOU 804 CG1 ILE A 108 14449 7816 9755 570 -136 -45 C
ATOM 805 CG2 ILE A 108 12.084 213.018 171.465 1.00 83.86 C
ANISOU 805 CG2 ILE A 108 14679 7592 9592 924 51 -2 C
ATOM 806 CD1 ILE A 108 14.735 211.238 171.806 1.00 85.77 C
ANISOU 806 CD1 ILE A 108 14765 7971 9853 408 -181 -68 C
ATOM 807 N PRO A 109 14.206 214.731 167.366 1.00 85.32 N
ANISOU 807 N PRO A 109 14982 7741 9696 566 -251 -64 N
ATOM 808 CA PRO A 109 15.412 215.252 166.697 1.00 86.47 C
ANISOU 808 CA PRO A 109 15237 7851 9766 365 -338 -94 C
ATOM 809 C PRO A 109 16.207 216.280 167.501 1.00 88.12 C
ANISOU 809 C PRO A 109 15763 7922 9797 246 -349 -115 C
ATOM 810 O PRO A 109 17.393 216.472 167.235 1.00 88.25 O
ANISOU 810 O PRO A 109 15833 7934 9764 39 -423 -139 O
ATOM 811 CB PRO A 109 14.871 215.855 165.399 1.00 86.86 C
ANISOU 811 CB PRO A 109 15318 7870 9815 454 -350 -84 C
ATOM 812 CG PRO A 109 13.433 216.105 165.661 1.00 87.00 C
ANISOU 812 CG PRO A 109 15351 7856 9849 711 -266 -50 C
ATOM 813 CD PRO A 109 12.987 215.030 166.592 1.00 85.08 C
ANISOU 813 CD PRO A 109 14910 7707 9710 769 -213 -35 C
ATOM 814 N LEU A 110 15.572 216.930 168.484 1.00 89.18 N
ANISOU 814 N LEU A 110 16108 7943 9832 370 -276 -105 N
ATOM 815 CA LEU A 110 16.254 217.928 169.302 1.00 90.71 C
ANISOU 815 CA LEU A 110 16631 7991 9844 259 -288 -126 C
ATOM 816 C LEU A 110 17.291 217.314 170.227 1.00 91.83 C
ANISOU 816 C LEU A 110 16716 8189 9987 76 -340 -143 C
ATOM 817 O LEU A 110 18.322 217.933 170.490 1.00 92.07 O
ANISOU 817 O LEU A 110 16904 8166 9913 -128 -413 -165 O
ATOM 818 CB LEU A 110 15.243 218.747 170.111 1.00 91.21 C
ANISOU 818 CB LEU A 110 16954 7908 9794 462 -185 -109 C
ATOM 819 CG LEU A 110 14.283 219.587 169.289 1.00 93.03 C
ANISOU 819 CG LEU A 110 17277 8068 10001 660 -134 -88 C
ATOM 820 CD1 LEU A 110 13.270 220.258 170.176 1.00 93.85 C
ANISOU 820 CD1 LEU A 110 17596 8049 10013 885 -16 -65 C
ATOM 821 CD2 LEU A 110 15.029 220.609 168.442 1.00 93.66 C
ANISOU 821 CD2 LEU A 110 17564 8053 9969 531 -203 -108 C
ATOM 822 N ARG A 111 17.023 216.106 170.724 1.00 92.38 N
ANISOU 822 N ARG A 111 16560 8367 10175 143 -308 -129 N
ATOM 823 CA ARG A 111 17.955 215.435 171.623 1.00 93.60 C
ANISOU 823 CA ARG A 111 16648 8580 10336 -9 -360 -141 C
ATOM 824 C ARG A 111 18.709 214.286 170.966 1.00 94.41 C
ANISOU 824 C ARG A 111 16450 8847 10574 -154 -442 -148 C
ATOM 825 O ARG A 111 19.388 213.558 171.680 1.00 94.42 O
ANISOU 825 O ARG A 111 16370 8911 10594 -266 -488 -154 O
ATOM 826 CB ARG A 111 17.256 214.897 172.882 1.00 95.38 C
ANISOU 826 CB ARG A 111 16807 8829 10606 135 -277 -122 C
ATOM 827 CG ARG A 111 15.917 215.523 173.254 1.00 98.98 C
ANISOU 827 CG ARG A 111 17487 9152 10971 340 -160 -105 C
ATOM 828 CD ARG A 111 15.108 214.548 174.087 1.00102.66 C
ANISOU 828 CD ARG A 111 17813 9678 11516 462 -77 -84 C
ATOM 829 NE ARG A 111 14.673 215.135 175.361 1.00105.97 N
ANISOU 829 NE ARG A 111 18513 9954 11798 572 16 -77 N
ATOM 830 CZ ARG A 111 14.159 214.440 176.372 1.00108.41 C
ANISOU 830 CZ ARG A 111 18781 10277 12133 674 103 -60 C
ATOM 831 NH1 ARG A 111 14.027 213.119 176.281 1.00108.01 N
ANISOU 831 NH1 ARG A 111 18421 10376 12240 671 103 -48 N
ATOM 832 NH2 ARG A 111 13.785 215.055 177.486 1.00108.46 N
ANISOU 832 NH2 ARG A 111 19070 10140 12000 777 196 -53 N
ATOM 833 N TYR A 112 18.585 214.088 169.640 1.00 94.90 N
ANISOU 833 N TYR A 112 16345 8981 10733 -138 -456 -145 N
ATOM 834 CA TYR A 112 19.280 212.998 168.962 1.00 95.90 C
ANISOU 834 CA TYR A 112 16190 9259 10988 -257 -519 -150 C
ATOM 835 C TYR A 112 20.801 213.107 169.129 1.00 96.53 C
ANISOU 835 C TYR A 112 16308 9358 11011 -499 -611 -169 C
ATOM 836 O TYR A 112 21.425 212.150 169.552 1.00 96.71 O
ANISOU 836 O TYR A 112 16165 9482 11100 -576 -649 -168 O
ATOM 837 CB TYR A 112 18.889 212.918 167.469 1.00 96.14 C
ANISOU 837 CB TYR A 112 16088 9339 11104 -207 -520 -145 C
ATOM 838 CG TYR A 112 19.666 211.873 166.692 1.00 97.19 C
ANISOU 838 CG TYR A 112 15957 9615 11357 -324 -575 -150 C
ATOM 839 CD1 TYR A 112 20.910 212.162 166.147 1.00 98.27 C
ANISOU 839 CD1 TYR A 112 16113 9769 11457 -523 -642 -167 C
ATOM 840 CD2 TYR A 112 19.169 210.592 166.523 1.00 98.14 C
ANISOU 840 CD2 TYR A 112 15813 9851 11624 -239 -555 -137 C
ATOM 841 CE1 TYR A 112 21.647 211.197 165.473 1.00 99.21 C
ANISOU 841 CE1 TYR A 112 15994 10019 11683 -619 -681 -169 C
ATOM 842 CE2 TYR A 112 19.877 209.631 165.811 1.00 99.13 C
ANISOU 842 CE2 TYR A 112 15719 10097 11849 -337 -598 -141 C
ATOM 843 CZ TYR A 112 21.123 209.935 165.294 1.00100.05 C
ANISOU 843 CZ TYR A 112 15858 10230 11927 -520 -658 -157 C
ATOM 844 OH TYR A 112 21.853 209.000 164.602 1.00101.57 O
ANISOU 844 OH TYR A 112 15840 10539 12213 -608 -689 -159 O
ATOM 845 N ASN A 113 21.393 214.259 168.809 1.00 96.70 N
ANISOU 845 N ASN A 113 16548 9284 10910 -619 -648 -183 N
ATOM 846 CA ASN A 113 22.845 214.452 168.894 1.00 97.28 C
ANISOU 846 CA ASN A 113 16650 9380 10930 -865 -738 -198 C
ATOM 847 C ASN A 113 23.416 214.165 170.297 1.00 97.06 C
ANISOU 847 C ASN A 113 16648 9366 10863 -944 -781 -198 C
ATOM 848 O ASN A 113 24.514 213.619 170.423 1.00 97.20 O
ANISOU 848 O ASN A 113 16522 9487 10921 -1106 -857 -200 O
ATOM 849 CB ASN A 113 23.221 215.871 168.448 1.00 98.89 C
ANISOU 849 CB ASN A 113 17141 9449 10984 -971 -758 -211 C
ATOM 850 CG ASN A 113 22.616 216.293 167.128 1.00102.53 C
ANISOU 850 CG ASN A 113 17610 9881 11465 -890 -721 -210 C
ATOM 851 OD1 ASN A 113 22.593 215.527 166.150 1.00103.95 O
ANISOU 851 OD1 ASN A 113 17546 10176 11773 -877 -723 -205 O
ATOM 852 ND2 ASN A 113 22.116 217.529 167.074 1.00102.99 N
ANISOU 852 ND2 ASN A 113 17965 9779 11390 -829 -688 -213 N
ATOM 853 N GLY A 114 22.663 214.534 171.330 1.00 96.46 N
ANISOU 853 N GLY A 114 16756 9188 10708 -822 -729 -195 N
ATOM 854 CA GLY A 114 23.069 214.314 172.711 1.00 96.05 C
ANISOU 854 CA GLY A 114 16765 9128 10603 -874 -763 -195 C
ATOM 855 C GLY A 114 22.806 212.905 173.218 1.00 95.14 C
ANISOU 855 C GLY A 114 16403 9129 10618 -768 -734 -180 C
ATOM 856 O GLY A 114 23.460 212.443 174.155 1.00 95.36 O
ANISOU 856 O GLY A 114 16411 9191 10630 -839 -784 -178 O
ATOM 857 N LEU A 115 21.837 212.211 172.622 1.00 93.64 N
ANISOU 857 N LEU A 115 16031 8996 10551 -601 -657 -167 N
ATOM 858 CA LEU A 115 21.491 210.855 173.036 1.00 92.60 C
ANISOU 858 CA LEU A 115 15668 8969 10546 -498 -619 -152 C
ATOM 859 C LEU A 115 22.351 209.841 172.276 1.00 90.62 C
ANISOU 859 C LEU A 115 15131 8877 10423 -605 -686 -152 C
ATOM 860 O LEU A 115 22.947 208.957 172.887 1.00 91.02 O
ANISOU 860 O LEU A 115 15048 9010 10527 -634 -715 -145 O
ATOM 861 CB LEU A 115 19.991 210.615 172.745 1.00 93.22 C
ANISOU 861 CB LEU A 115 15675 9042 10703 -279 -509 -136 C
ATOM 862 CG LEU A 115 19.253 209.435 173.398 1.00 95.26 C
ANISOU 862 CG LEU A 115 15734 9381 11080 -148 -444 -116 C
ATOM 863 CD1 LEU A 115 17.766 209.649 173.310 1.00 95.89 C
ANISOU 863 CD1 LEU A 115 15882 9394 11160 66 -324 -97 C
ATOM 864 CD2 LEU A 115 19.571 208.098 172.724 1.00 96.12 C
ANISOU 864 CD2 LEU A 115 15535 9641 11344 -188 -480 -113 C
ATOM 865 N VAL A 116 22.420 209.982 170.950 1.00 88.33 N
ANISOU 865 N VAL A 116 14759 8625 10179 -654 -705 -157 N
ATOM 866 CA VAL A 116 23.083 209.060 170.036 1.00 86.37 C
ANISOU 866 CA VAL A 116 14250 8516 10052 -731 -746 -156 C
ATOM 867 C VAL A 116 24.500 209.522 169.671 1.00 84.39 C
ANISOU 867 C VAL A 116 14023 8291 9751 -947 -836 -166 C
ATOM 868 O VAL A 116 24.681 210.359 168.787 1.00 84.29 O
ANISOU 868 O VAL A 116 14104 8232 9691 -1016 -845 -176 O
ATOM 869 CB VAL A 116 22.192 208.801 168.801 1.00 86.55 C
ANISOU 869 CB VAL A 116 14156 8563 10165 -616 -693 -152 C
ATOM 870 CG1 VAL A 116 22.761 207.680 167.975 1.00 86.92 C
ANISOU 870 CG1 VAL A 116 13952 8744 10332 -681 -725 -150 C
ATOM 871 CG2 VAL A 116 20.756 208.465 169.214 1.00 86.80 C
ANISOU 871 CG2 VAL A 116 14149 8579 10250 -414 -609 -136 C
ATOM 872 N THR A 117 25.496 208.959 170.382 1.00 82.54 N
ANISOU 872 N THR A 117 13704 8132 9526 -1052 -902 -162 N
ATOM 873 CA THR A 117 26.919 209.276 170.301 1.00 81.29 C
ANISOU 873 CA THR A 117 13538 8019 9328 -1263 -996 -164 C
ATOM 874 C THR A 117 27.696 208.183 169.568 1.00 79.74 C
ANISOU 874 C THR A 117 13052 7983 9263 -1315 -1021 -154 C
ATOM 875 O THR A 117 27.324 207.016 169.639 1.00 79.98 O
ANISOU 875 O THR A 117 12900 8090 9398 -1204 -989 -144 O
ATOM 876 CB THR A 117 27.417 209.504 171.742 1.00 82.33 C
ANISOU 876 CB THR A 117 13801 8115 9366 -1330 -1060 -162 C
ATOM 877 OG1 THR A 117 26.835 210.711 172.236 1.00 83.45 O
ANISOU 877 OG1 THR A 117 14250 8092 9365 -1304 -1034 -174 O
ATOM 878 CG2 THR A 117 28.926 209.567 171.868 1.00 82.53 C
ANISOU 878 CG2 THR A 117 13767 8221 9370 -1547 -1174 -157 C
ATOM 879 N GLY A 118 28.746 208.570 168.855 1.00 78.22 N
ANISOU 879 N GLY A 118 12824 7836 9060 -1482 -1069 -155 N
ATOM 880 CA GLY A 118 29.573 207.631 168.115 1.00 77.41 C
ANISOU 880 CA GLY A 118 12458 7882 9072 -1537 -1084 -143 C
ATOM 881 C GLY A 118 30.272 206.622 168.998 1.00 76.30 C
ANISOU 881 C GLY A 118 12156 7853 8983 -1557 -1142 -125 C
ATOM 882 O GLY A 118 30.350 205.440 168.647 1.00 76.74 O
ANISOU 882 O GLY A 118 11989 8016 9153 -1492 -1121 -113 O
ATOM 883 N THR A 119 30.767 207.067 170.158 1.00 74.70 N
ANISOU 883 N THR A 119 12076 7618 8689 -1643 -1219 -122 N
ATOM 884 CA THR A 119 31.457 206.158 171.066 1.00 73.63 C
ANISOU 884 CA THR A 119 11800 7584 8592 -1661 -1287 -103 C
ATOM 885 C THR A 119 30.448 205.238 171.787 1.00 72.07 C
ANISOU 885 C THR A 119 11586 7365 8432 -1470 -1236 -100 C
ATOM 886 O THR A 119 30.780 204.090 172.056 1.00 72.08 O
ANISOU 886 O THR A 119 11404 7469 8516 -1424 -1252 -83 O
ATOM 887 CB THR A 119 32.433 206.906 171.975 1.00 74.90 C
ANISOU 887 CB THR A 119 12075 7736 8648 -1843 -1404 -97 C
ATOM 888 OG1 THR A 119 33.486 206.014 172.354 1.00 75.79 O
ANISOU 888 OG1 THR A 119 11971 7998 8829 -1899 -1483 -71 O
ATOM 889 CG2 THR A 119 31.767 207.571 173.181 1.00 75.20 C
ANISOU 889 CG2 THR A 119 12394 7627 8552 -1816 -1421 -110 C
ATOM 890 N ARG A 120 29.212 205.701 172.029 1.00 70.71 N
ANISOU 890 N ARG A 120 11593 7066 8208 -1353 -1166 -115 N
ATOM 891 CA ARG A 120 28.176 204.854 172.618 1.00 70.01 C
ANISOU 891 CA ARG A 120 11480 6958 8161 -1175 -1100 -110 C
ATOM 892 C ARG A 120 27.745 203.796 171.594 1.00 68.36 C
ANISOU 892 C ARG A 120 11045 6836 8094 -1073 -1033 -105 C
ATOM 893 O ARG A 120 27.493 202.658 171.974 1.00 68.34 O
ANISOU 893 O ARG A 120 10918 6887 8161 -983 -1013 -93 O
ATOM 894 CB ARG A 120 26.957 205.682 173.038 1.00 72.31 C
ANISOU 894 CB ARG A 120 12005 7100 8369 -1072 -1027 -122 C
ATOM 895 CG ARG A 120 27.227 206.666 174.167 1.00 76.81 C
ANISOU 895 CG ARG A 120 12835 7561 8787 -1135 -1075 -128 C
ATOM 896 CD ARG A 120 26.301 207.871 174.081 1.00 80.54 C
ANISOU 896 CD ARG A 120 13564 7882 9156 -1093 -1015 -143 C
ATOM 897 NE ARG A 120 25.652 208.148 175.361 1.00 83.28 N
ANISOU 897 NE ARG A 120 14115 8114 9412 -988 -967 -143 N
ATOM 898 CZ ARG A 120 24.936 209.236 175.621 1.00 85.12 C
ANISOU 898 CZ ARG A 120 14602 8202 9538 -928 -910 -152 C
ATOM 899 NH1 ARG A 120 24.378 209.398 176.809 1.00 85.51 N
ANISOU 899 NH1 ARG A 120 14827 8153 9509 -823 -854 -149 N
ATOM 900 NH2 ARG A 120 24.769 210.167 174.692 1.00 84.16 N
ANISOU 900 NH2 ARG A 120 14569 8027 9381 -965 -900 -163 N
ATOM 901 N ALA A 121 27.692 204.151 170.294 1.00 66.73 N
ANISOU 901 N ALA A 121 10796 6636 7922 -1094 -1001 -113 N
ATOM 902 CA ALA A 121 27.362 203.211 169.232 1.00 65.67 C
ANISOU 902 CA ALA A 121 10467 6575 7908 -1016 -948 -110 C
ATOM 903 C ALA A 121 28.386 202.077 169.199 1.00 64.81 C
ANISOU 903 C ALA A 121 10146 6600 7880 -1055 -988 -93 C
ATOM 904 O ALA A 121 27.984 200.918 169.117 1.00 65.04 O
ANISOU 904 O ALA A 121 10043 6676 7993 -951 -948 -85 O
ATOM 905 CB ALA A 121 27.336 203.921 167.897 1.00 65.52 C
ANISOU 905 CB ALA A 121 10469 6537 7889 -1062 -927 -121 C
ATOM 906 N ALA A 122 29.698 202.392 169.346 1.00 63.69 N
ANISOU 906 N ALA A 122 9973 6519 7707 -1204 -1068 -85 N
ATOM 907 CA ALA A 122 30.756 201.367 169.379 1.00 62.95 C
ANISOU 907 CA ALA A 122 9674 6560 7684 -1238 -1112 -63 C
ATOM 908 C ALA A 122 30.627 200.425 170.592 1.00 62.52 C
ANISOU 908 C ALA A 122 9594 6525 7638 -1154 -1137 -49 C
ATOM 909 O ALA A 122 30.977 199.247 170.503 1.00 62.47 O
ANISOU 909 O ALA A 122 9415 6612 7710 -1104 -1138 -32 O
ATOM 910 CB ALA A 122 32.127 202.013 169.364 1.00 62.81 C
ANISOU 910 CB ALA A 122 9636 6601 7626 -1419 -1196 -53 C
ATOM 911 N GLY A 123 30.120 200.949 171.705 1.00 61.81 N
ANISOU 911 N GLY A 123 9689 6337 7459 -1136 -1151 -56 N
ATOM 912 CA GLY A 123 29.885 200.169 172.913 1.00 61.36 C
ANISOU 912 CA GLY A 123 9650 6273 7391 -1055 -1165 -45 C
ATOM 913 C GLY A 123 28.697 199.247 172.740 1.00 60.42 C
ANISOU 913 C GLY A 123 9478 6134 7344 -893 -1064 -47 C
ATOM 914 O GLY A 123 28.744 198.082 173.141 1.00 60.45 O
ANISOU 914 O GLY A 123 9380 6189 7398 -822 -1060 -31 O
ATOM 915 N ILE A 124 27.633 199.747 172.101 1.00 59.47 N
ANISOU 915 N ILE A 124 9420 5945 7233 -835 -985 -62 N
ATOM 916 CA ILE A 124 26.455 198.931 171.832 1.00 59.35 C
ANISOU 916 CA ILE A 124 9344 5917 7290 -695 -896 -61 C
ATOM 917 C ILE A 124 26.826 197.804 170.870 1.00 59.05 C
ANISOU 917 C ILE A 124 9100 5978 7357 -681 -886 -54 C
ATOM 918 O ILE A 124 26.484 196.652 171.116 1.00 59.08 O
ANISOU 918 O ILE A 124 9019 6012 7416 -600 -855 -43 O
ATOM 919 CB ILE A 124 25.322 199.800 171.265 1.00 59.91 C
ANISOU 919 CB ILE A 124 9499 5910 7356 -643 -827 -76 C
ATOM 920 CG1 ILE A 124 24.856 200.809 172.298 1.00 61.25 C
ANISOU 920 CG1 ILE A 124 9890 5966 7416 -631 -818 -82 C
ATOM 921 CG2 ILE A 124 24.157 198.947 170.802 1.00 60.25 C
ANISOU 921 CG2 ILE A 124 9448 5959 7486 -516 -746 -71 C
ATOM 922 CD1 ILE A 124 24.073 201.933 171.722 1.00 62.87 C
ANISOU 922 CD1 ILE A 124 10198 6091 7598 -586 -763 -93 C
ATOM 923 N ILE A 125 27.599 198.122 169.815 1.00 58.48 N
ANISOU 923 N ILE A 125 8960 5953 7305 -761 -906 -58 N
ATOM 924 CA ILE A 125 28.046 197.112 168.854 1.00 58.26 C
ANISOU 924 CA ILE A 125 8753 6015 7369 -746 -889 -51 C
ATOM 925 C ILE A 125 28.860 196.021 169.547 1.00 57.76 C
ANISOU 925 C ILE A 125 8578 6034 7334 -735 -928 -29 C
ATOM 926 O ILE A 125 28.609 194.840 169.319 1.00 58.09 O
ANISOU 926 O ILE A 125 8508 6117 7445 -663 -892 -21 O
ATOM 927 CB ILE A 125 28.826 197.753 167.685 1.00 58.77 C
ANISOU 927 CB ILE A 125 8774 6121 7434 -854 -910 -55 C
ATOM 928 CG1 ILE A 125 27.931 198.716 166.898 1.00 59.58 C
ANISOU 928 CG1 ILE A 125 9005 6137 7496 -870 -880 -75 C
ATOM 929 CG2 ILE A 125 29.404 196.679 166.765 1.00 59.20 C
ANISOU 929 CG2 ILE A 125 8661 6256 7577 -823 -876 -47 C
ATOM 930 CD1 ILE A 125 28.644 199.565 165.897 1.00 60.65 C
ANISOU 930 CD1 ILE A 125 9098 6308 7639 -965 -882 -79 C
ATOM 931 N ALA A 126 29.771 196.416 170.450 1.00 56.78 N
ANISOU 931 N ALA A 126 8494 5928 7151 -804 -1006 -19 N
ATOM 932 CA ALA A 126 30.578 195.468 171.210 1.00 56.37 C
ANISOU 932 CA ALA A 126 8338 5959 7120 -789 -1057 6 C
ATOM 933 C ALA A 126 29.691 194.550 172.058 1.00 55.72 C
ANISOU 933 C ALA A 126 8298 5834 7039 -674 -1026 11 C
ATOM 934 O ALA A 126 29.864 193.333 172.018 1.00 55.82 O
ANISOU 934 O ALA A 126 8213 5902 7094 -615 -1030 29 O
ATOM 935 CB ALA A 126 31.573 196.211 172.089 1.00 56.44 C
ANISOU 935 CB ALA A 126 8390 5996 7058 -906 -1164 17 C
ATOM 936 N ILE A 127 28.702 195.121 172.765 1.00 54.84 N
ANISOU 936 N ILE A 127 8340 5619 6877 -639 -988 -3 N
ATOM 937 CA ILE A 127 27.780 194.338 173.585 1.00 54.34 C
ANISOU 937 CA ILE A 127 8334 5505 6809 -536 -943 3 C
ATOM 938 C ILE A 127 26.980 193.368 172.710 1.00 53.65 C
ANISOU 938 C ILE A 127 8160 5416 6807 -443 -851 0 C
ATOM 939 O ILE A 127 26.816 192.196 173.056 1.00 53.44 O
ANISOU 939 O ILE A 127 8122 5381 6803 -365 -813 10 O
ATOM 940 CB ILE A 127 26.866 195.295 174.385 1.00 54.67 C
ANISOU 940 CB ILE A 127 8569 5434 6768 -525 -917 -10 C
ATOM 941 CG1 ILE A 127 27.650 195.967 175.511 1.00 55.62 C
ANISOU 941 CG1 ILE A 127 8810 5537 6787 -630 -1012 -10 C
ATOM 942 CG2 ILE A 127 25.643 194.578 174.936 1.00 55.04 C
ANISOU 942 CG2 ILE A 127 8673 5431 6810 -421 -857 -1 C
ATOM 943 CD1 ILE A 127 26.933 197.121 176.152 1.00 57.01 C
ANISOU 943 CD1 ILE A 127 9199 5600 6864 -602 -993 -15 C
ATOM 944 N CYS A 128 26.505 193.867 171.569 1.00 52.95 N
ANISOU 944 N CYS A 128 8019 5336 6763 -461 -819 -13 N
ATOM 945 CA CYS A 128 25.718 193.085 170.644 1.00 52.73 C
ANISOU 945 CA CYS A 128 7918 5305 6811 -388 -744 -17 C
ATOM 946 C CYS A 128 26.496 191.925 170.059 1.00 52.32 C
ANISOU 946 C CYS A 128 7723 5334 6821 -382 -751 -7 C
ATOM 947 O CYS A 128 25.923 190.847 169.898 1.00 52.88 O
ANISOU 947 O CYS A 128 7738 5406 6949 -323 -698 -6 O
ATOM 948 CB CYS A 128 25.110 193.972 169.564 1.00 53.34 C
ANISOU 948 CB CYS A 128 8021 5346 6898 -405 -713 -35 C
ATOM 949 SG CYS A 128 23.778 195.050 170.160 1.00 55.86 S
ANISOU 949 SG CYS A 128 8504 5560 7160 -365 -671 -43 S
ATOM 950 N TRP A 129 27.803 192.109 169.791 1.00 51.06 N
ANISOU 950 N TRP A 129 7506 5246 6650 -443 -815 3 N
ATOM 951 CA TRP A 129 28.615 191.014 169.263 1.00 50.37 C
ANISOU 951 CA TRP A 129 7280 5238 6619 -421 -812 17 C
ATOM 952 C TRP A 129 28.887 189.955 170.320 1.00 49.59 C
ANISOU 952 C TRP A 129 7163 5162 6517 -357 -832 39 C
ATOM 953 O TRP A 129 28.842 188.767 170.008 1.00 49.45 O
ANISOU 953 O TRP A 129 7077 5168 6545 -290 -798 49 O
ATOM 954 CB TRP A 129 29.912 191.526 168.664 1.00 50.14 C
ANISOU 954 CB TRP A 129 7175 5287 6588 -511 -863 23 C
ATOM 955 CG TRP A 129 29.784 191.915 167.229 1.00 50.39 C
ANISOU 955 CG TRP A 129 7170 5324 6654 -542 -820 9 C
ATOM 956 CD1 TRP A 129 29.593 193.172 166.733 1.00 51.30 C
ANISOU 956 CD1 TRP A 129 7348 5405 6737 -620 -825 -8 C
ATOM 957 CD2 TRP A 129 29.837 191.039 166.096 1.00 50.35 C
ANISOU 957 CD2 TRP A 129 7073 5350 6709 -495 -765 11 C
ATOM 958 NE1 TRP A 129 29.546 193.136 165.358 1.00 51.54 N
ANISOU 958 NE1 TRP A 129 7329 5446 6806 -626 -778 -16 N
ATOM 959 CE2 TRP A 129 29.716 191.840 164.939 1.00 51.14 C
ANISOU 959 CE2 TRP A 129 7183 5434 6811 -550 -741 -6 C
ATOM 960 CE3 TRP A 129 29.994 189.657 165.945 1.00 50.72 C
ANISOU 960 CE3 TRP A 129 7047 5426 6800 -409 -733 25 C
ATOM 961 CZ2 TRP A 129 29.777 191.306 163.647 1.00 51.50 C
ANISOU 961 CZ2 TRP A 129 7171 5495 6901 -526 -687 -9 C
ATOM 962 CZ3 TRP A 129 30.035 189.130 164.664 1.00 51.64 C
ANISOU 962 CZ3 TRP A 129 7108 5554 6958 -384 -678 21 C
ATOM 963 CH2 TRP A 129 29.920 189.951 163.533 1.00 51.63 C
ANISOU 963 CH2 TRP A 129 7121 5539 6958 -443 -656 4 C
ATOM 964 N VAL A 130 29.108 190.368 171.575 1.00 48.95 N
ANISOU 964 N VAL A 130 7162 5064 6374 -376 -888 47 N
ATOM 965 CA VAL A 130 29.315 189.398 172.651 1.00 48.63 C
ANISOU 965 CA VAL A 130 7124 5036 6318 -312 -914 69 C
ATOM 966 C VAL A 130 28.013 188.603 172.917 1.00 48.93 C
ANISOU 966 C VAL A 130 7227 4996 6368 -225 -832 64 C
ATOM 967 O VAL A 130 28.038 187.372 173.006 1.00 49.13 O
ANISOU 967 O VAL A 130 7224 5031 6414 -154 -812 78 O
ATOM 968 CB VAL A 130 29.893 190.033 173.920 1.00 48.24 C
ANISOU 968 CB VAL A 130 7169 4974 6184 -362 -1001 77 C
ATOM 969 CG1 VAL A 130 30.060 188.983 174.995 1.00 48.57 C
ANISOU 969 CG1 VAL A 130 7201 5046 6209 -300 -1047 104 C
ATOM 970 CG2 VAL A 130 31.230 190.688 173.627 1.00 48.27 C
ANISOU 970 CG2 VAL A 130 7131 5041 6170 -479 -1080 78 C
ATOM 971 N LEU A 131 26.868 189.299 172.944 1.00 48.50 N
ANISOU 971 N LEU A 131 7262 4866 6299 -232 -783 45 N
ATOM 972 CA LEU A 131 25.568 188.666 173.120 1.00 48.54 C
ANISOU 972 CA LEU A 131 7321 4802 6318 -163 -700 43 C
ATOM 973 C LEU A 131 25.289 187.680 172.000 1.00 49.02 C
ANISOU 973 C LEU A 131 7291 4878 6457 -123 -641 41 C
ATOM 974 O LEU A 131 24.739 186.611 172.269 1.00 49.56 O
ANISOU 974 O LEU A 131 7378 4912 6543 -68 -586 48 O
ATOM 975 CB LEU A 131 24.463 189.723 173.100 1.00 48.48 C
ANISOU 975 CB LEU A 131 7402 4727 6291 -179 -659 26 C
ATOM 976 CG LEU A 131 24.224 190.457 174.376 1.00 49.68 C
ANISOU 976 CG LEU A 131 7702 4804 6370 -160 -643 28 C
ATOM 977 CD1 LEU A 131 23.156 191.479 174.182 1.00 50.34 C
ANISOU 977 CD1 LEU A 131 7838 4830 6459 -149 -578 14 C
ATOM 978 CD2 LEU A 131 23.826 189.503 175.476 1.00 50.12 C
ANISOU 978 CD2 LEU A 131 7784 4833 6426 -91 -597 44 C
ATOM 979 N SER A 132 25.643 188.050 170.740 1.00 48.42 N
ANISOU 979 N SER A 132 7130 4845 6420 -159 -648 31 N
ATOM 980 CA SER A 132 25.431 187.217 169.564 1.00 48.31 C
ANISOU 980 CA SER A 132 7044 4839 6471 -133 -598 27 C
ATOM 981 C SER A 132 26.218 185.935 169.661 1.00 48.85 C
ANISOU 981 C SER A 132 7057 4947 6557 -85 -600 44 C
ATOM 982 O SER A 132 25.702 184.882 169.294 1.00 49.26 O
ANISOU 982 O SER A 132 7096 4977 6643 -44 -549 44 O
ATOM 983 CB SER A 132 25.816 187.967 168.303 1.00 48.84 C
ANISOU 983 CB SER A 132 7063 4935 6561 -187 -608 12 C
ATOM 984 OG SER A 132 25.001 189.117 168.213 1.00 50.58 O
ANISOU 984 OG SER A 132 7349 5122 6746 -234 -623 -1 O
ATOM 985 N PHE A 133 27.455 185.998 170.189 1.00 48.54 N
ANISOU 985 N PHE A 133 6987 4965 6491 -88 -661 60 N
ATOM 986 CA PHE A 133 28.249 184.793 170.380 1.00 48.70 C
ANISOU 986 CA PHE A 133 6956 5024 6522 -23 -663 82 C
ATOM 987 C PHE A 133 27.564 183.866 171.392 1.00 49.03 C
ANISOU 987 C PHE A 133 7084 5002 6546 40 -628 90 C
ATOM 988 O PHE A 133 27.435 182.678 171.135 1.00 49.10 O
ANISOU 988 O PHE A 133 7091 4987 6577 92 -579 94 O
ATOM 989 CB PHE A 133 29.668 185.143 170.826 1.00 48.52 C
ANISOU 989 CB PHE A 133 6880 5082 6474 -38 -747 103 C
ATOM 990 CG PHE A 133 30.605 185.287 169.657 1.00 49.33 C
ANISOU 990 CG PHE A 133 6864 5268 6611 -72 -760 106 C
ATOM 991 CD1 PHE A 133 30.920 184.198 168.865 1.00 50.19 C
ANISOU 991 CD1 PHE A 133 6896 5415 6758 -7 -721 119 C
ATOM 992 CD2 PHE A 133 31.171 186.508 169.348 1.00 50.12 C
ANISOU 992 CD2 PHE A 133 6941 5403 6701 -168 -802 98 C
ATOM 993 CE1 PHE A 133 31.764 184.336 167.770 1.00 50.78 C
ANISOU 993 CE1 PHE A 133 6864 5566 6865 -32 -718 125 C
ATOM 994 CE2 PHE A 133 32.022 186.640 168.260 1.00 50.69 C
ANISOU 994 CE2 PHE A 133 6904 5552 6805 -205 -803 104 C
ATOM 995 CZ PHE A 133 32.310 185.555 167.477 1.00 50.45 C
ANISOU 995 CZ PHE A 133 6788 5563 6816 -135 -757 118 C
ATOM 996 N ALA A 134 27.062 184.424 172.505 1.00 48.88 N
ANISOU 996 N ALA A 134 7153 4944 6477 30 -649 92 N
ATOM 997 CA ALA A 134 26.370 183.643 173.521 1.00 48.95 C
ANISOU 997 CA ALA A 134 7256 4885 6457 82 -609 101 C
ATOM 998 C ALA A 134 25.107 183.004 172.970 1.00 49.29 C
ANISOU 998 C ALA A 134 7313 4871 6543 95 -518 90 C
ATOM 999 O ALA A 134 24.850 181.845 173.255 1.00 49.81 O
ANISOU 999 O ALA A 134 7411 4902 6611 143 -475 101 O
ATOM 1000 CB ALA A 134 26.029 184.519 174.709 1.00 49.02 C
ANISOU 1000 CB ALA A 134 7370 4852 6405 57 -630 99 C
ATOM 1001 N ILE A 135 24.331 183.733 172.167 1.00 49.00 N
ANISOU 1001 N ILE A 135 7260 4821 6538 50 -490 71 N
ATOM 1002 CA ILE A 135 23.100 183.202 171.590 1.00 49.21 C
ANISOU 1002 CA ILE A 135 7283 4804 6611 51 -415 63 C
ATOM 1003 C ILE A 135 23.385 182.132 170.530 1.00 48.80 C
ANISOU 1003 C ILE A 135 7166 4773 6602 59 -404 61 C
ATOM 1004 O ILE A 135 22.823 181.041 170.591 1.00 48.93 O
ANISOU 1004 O ILE A 135 7197 4751 6643 72 -353 63 O
ATOM 1005 CB ILE A 135 22.234 184.362 171.020 1.00 50.07 C
ANISOU 1005 CB ILE A 135 7377 4903 6744 8 -402 46 C
ATOM 1006 CG1 ILE A 135 21.694 185.264 172.136 1.00 51.18 C
ANISOU 1006 CG1 ILE A 135 7599 5011 6836 5 -401 47 C
ATOM 1007 CG2 ILE A 135 21.107 183.841 170.133 1.00 50.48 C
ANISOU 1007 CG2 ILE A 135 7405 4924 6853 6 -338 42 C
ATOM 1008 CD1 ILE A 135 21.161 186.567 171.635 1.00 52.41 C
ANISOU 1008 CD1 ILE A 135 7751 5169 6993 -33 -418 31 C
ATOM 1009 N GLY A 136 24.233 182.463 169.563 1.00 48.16 N
ANISOU 1009 N GLY A 136 7020 4750 6528 45 -449 57 N
ATOM 1010 CA GLY A 136 24.555 181.577 168.457 1.00 48.14 C
ANISOU 1010 CA GLY A 136 6968 4764 6558 58 -432 54 C
ATOM 1011 C GLY A 136 25.289 180.330 168.887 1.00 48.00 C
ANISOU 1011 C GLY A 136 6972 4742 6526 126 -418 73 C
ATOM 1012 O GLY A 136 25.074 179.263 168.314 1.00 48.66 O
ANISOU 1012 O GLY A 136 7082 4784 6625 143 -372 72 O
ATOM 1013 N LEU A 137 26.148 180.444 169.908 1.00 46.80 N
ANISOU 1013 N LEU A 137 6814 4629 6338 165 -464 92 N
ATOM 1014 CA LEU A 137 26.906 179.298 170.391 1.00 45.82 C
ANISOU 1014 CA LEU A 137 6712 4505 6193 247 -459 115 C
ATOM 1015 C LEU A 137 26.340 178.704 171.661 1.00 45.20 C
ANISOU 1015 C LEU A 137 6736 4365 6075 289 -441 129 C
ATOM 1016 O LEU A 137 27.034 177.933 172.316 1.00 45.19 O
ANISOU 1016 O LEU A 137 6760 4368 6041 361 -457 152 O
ATOM 1017 CB LEU A 137 28.408 179.602 170.537 1.00 45.65 C
ANISOU 1017 CB LEU A 137 6607 4574 6162 279 -522 135 C
ATOM 1018 CG LEU A 137 29.077 180.240 169.306 1.00 46.45 C
ANISOU 1018 CG LEU A 137 6604 4747 6298 231 -538 126 C
ATOM 1019 CD1 LEU A 137 30.508 180.627 169.576 1.00 46.62 C
ANISOU 1019 CD1 LEU A 137 6552 4859 6304 222 -618 145 C
ATOM 1020 CD2 LEU A 137 28.983 179.346 168.102 1.00 46.81 C
ANISOU 1020 CD2 LEU A 137 6616 4802 6368 284 -489 130 C
ATOM 1021 N THR A 138 25.055 178.973 171.983 1.00 44.76 N
ANISOU 1021 N THR A 138 6739 4248 6019 247 -402 118 N
ATOM 1022 CA THR A 138 24.403 178.320 173.135 1.00 45.06 C
ANISOU 1022 CA THR A 138 6884 4221 6018 278 -369 131 C
ATOM 1023 C THR A 138 24.487 176.780 173.034 1.00 45.85 C
ANISOU 1023 C THR A 138 7042 4275 6105 335 -327 145 C
ATOM 1024 O THR A 138 24.748 176.164 174.057 1.00 46.20 O
ANISOU 1024 O THR A 138 7177 4277 6101 380 -319 163 O
ATOM 1025 CB THR A 138 22.964 178.838 173.372 1.00 45.47 C
ANISOU 1025 CB THR A 138 6975 4218 6085 223 -312 119 C
ATOM 1026 OG1 THR A 138 23.022 180.029 174.153 1.00 46.16 O
ANISOU 1026 OG1 THR A 138 7072 4321 6146 199 -347 116 O
ATOM 1027 CG2 THR A 138 22.071 177.838 174.109 1.00 45.17 C
ANISOU 1027 CG2 THR A 138 7040 4104 6017 247 -250 133 C
ATOM 1028 N PRO A 139 24.375 176.137 171.843 1.00 46.03 N
ANISOU 1028 N PRO A 139 7033 4294 6163 332 -297 136 N
ATOM 1029 CA PRO A 139 24.522 174.680 171.790 1.00 46.29 C
ANISOU 1029 CA PRO A 139 7146 4271 6172 388 -255 149 C
ATOM 1030 C PRO A 139 25.853 174.174 172.333 1.00 46.88 C
ANISOU 1030 C PRO A 139 7232 4380 6202 490 -301 175 C
ATOM 1031 O PRO A 139 25.880 173.123 172.961 1.00 47.11 O
ANISOU 1031 O PRO A 139 7360 4353 6186 554 -277 193 O
ATOM 1032 CB PRO A 139 24.370 174.378 170.304 1.00 46.81 C
ANISOU 1032 CB PRO A 139 7169 4340 6277 367 -232 134 C
ATOM 1033 CG PRO A 139 23.487 175.468 169.818 1.00 47.20 C
ANISOU 1033 CG PRO A 139 7143 4415 6375 278 -240 110 C
ATOM 1034 CD PRO A 139 24.046 176.666 170.505 1.00 45.52 C
ANISOU 1034 CD PRO A 139 6902 4240 6153 261 -281 112 C
ATOM 1035 N MET A 140 26.944 174.919 172.130 1.00 46.89 N
ANISOU 1035 N MET A 140 7132 4473 6213 504 -368 180 N
ATOM 1036 CA MET A 140 28.250 174.523 172.664 1.00 47.47 C
ANISOU 1036 CA MET A 140 7193 4595 6249 604 -423 211 C
ATOM 1037 C MET A 140 28.319 174.596 174.204 1.00 48.46 C
ANISOU 1037 C MET A 140 7400 4698 6315 628 -466 230 C
ATOM 1038 O MET A 140 29.182 173.966 174.811 1.00 48.75 O
ANISOU 1038 O MET A 140 7483 4735 6306 724 -496 259 O
ATOM 1039 CB MET A 140 29.355 175.355 172.033 1.00 47.47 C
ANISOU 1039 CB MET A 140 7045 4710 6282 603 -482 216 C
ATOM 1040 CG MET A 140 29.548 175.044 170.598 1.00 48.65 C
ANISOU 1040 CG MET A 140 7137 4876 6473 611 -434 206 C
ATOM 1041 SD MET A 140 30.783 176.125 169.897 1.00 51.72 S
ANISOU 1041 SD MET A 140 7351 5401 6900 594 -491 214 S
ATOM 1042 CE MET A 140 32.224 175.665 170.862 1.00 48.87 C
ANISOU 1042 CE MET A 140 6948 5112 6507 732 -548 264 C
ATOM 1043 N LEU A 141 27.420 175.370 174.829 1.00 48.70 N
ANISOU 1043 N LEU A 141 7460 4704 6340 548 -468 214 N
ATOM 1044 CA LEU A 141 27.331 175.459 176.281 1.00 49.28 C
ANISOU 1044 CA LEU A 141 7638 4737 6348 562 -494 228 C
ATOM 1045 C LEU A 141 26.601 174.242 176.896 1.00 50.78 C
ANISOU 1045 C LEU A 141 7977 4820 6496 605 -419 238 C
ATOM 1046 O LEU A 141 26.528 174.156 178.125 1.00 51.40 O
ANISOU 1046 O LEU A 141 8166 4854 6509 631 -432 253 O
ATOM 1047 CB LEU A 141 26.661 176.775 176.733 1.00 48.87 C
ANISOU 1047 CB LEU A 141 7594 4677 6297 472 -497 208 C
ATOM 1048 CG LEU A 141 27.136 178.079 176.063 1.00 49.57 C
ANISOU 1048 CG LEU A 141 7560 4852 6423 409 -557 193 C
ATOM 1049 CD1 LEU A 141 26.515 179.289 176.720 1.00 49.73 C
ANISOU 1049 CD1 LEU A 141 7622 4843 6429 336 -552 176 C
ATOM 1050 CD2 LEU A 141 28.631 178.234 176.139 1.00 50.21 C
ANISOU 1050 CD2 LEU A 141 7578 5019 6479 443 -665 215 C
ATOM 1051 N GLY A 142 26.076 173.322 176.068 1.00 51.14 N
ANISOU 1051 N GLY A 142 8040 4821 6572 608 -343 231 N
ATOM 1052 CA GLY A 142 25.423 172.125 176.577 1.00 52.34 C
ANISOU 1052 CA GLY A 142 8339 4869 6679 638 -273 242 C
ATOM 1053 C GLY A 142 24.127 171.708 175.916 1.00 53.48 C
ANISOU 1053 C GLY A 142 8514 4943 6861 559 -176 223 C
ATOM 1054 O GLY A 142 23.736 170.538 176.024 1.00 54.26 O
ANISOU 1054 O GLY A 142 8731 4957 6927 578 -116 232 O
ATOM 1055 N TRP A 143 23.440 172.642 175.236 1.00 53.26 N
ANISOU 1055 N TRP A 143 8389 4948 6899 467 -162 198 N
ATOM 1056 CA TRP A 143 22.178 172.317 174.574 1.00 53.59 C
ANISOU 1056 CA TRP A 143 8440 4937 6985 384 -84 183 C
ATOM 1057 C TRP A 143 22.481 171.751 173.211 1.00 55.37 C
ANISOU 1057 C TRP A 143 8623 5173 7242 384 -84 173 C
ATOM 1058 O TRP A 143 22.353 172.431 172.199 1.00 55.35 O
ANISOU 1058 O TRP A 143 8515 5220 7294 335 -102 153 O
ATOM 1059 CB TRP A 143 21.298 173.556 174.463 1.00 52.68 C
ANISOU 1059 CB TRP A 143 8243 4851 6920 300 -73 167 C
ATOM 1060 CG TRP A 143 19.850 173.321 174.133 1.00 52.02 C
ANISOU 1060 CG TRP A 143 8161 4721 6881 213 4 159 C
ATOM 1061 CD1 TRP A 143 19.240 172.144 173.805 1.00 52.46 C
ANISOU 1061 CD1 TRP A 143 8283 4712 6938 180 62 163 C
ATOM 1062 CD2 TRP A 143 18.841 174.328 174.065 1.00 51.62 C
ANISOU 1062 CD2 TRP A 143 8034 4696 6885 145 27 149 C
ATOM 1063 NE1 TRP A 143 17.908 172.360 173.549 1.00 52.49 N
ANISOU 1063 NE1 TRP A 143 8240 4705 6998 86 114 158 N
ATOM 1064 CE2 TRP A 143 17.638 173.695 173.696 1.00 52.20 C
ANISOU 1064 CE2 TRP A 143 8111 4727 6997 72 95 150 C
ATOM 1065 CE3 TRP A 143 18.839 175.710 174.282 1.00 51.93 C
ANISOU 1065 CE3 TRP A 143 8007 4785 6938 140 -5 141 C
ATOM 1066 CZ2 TRP A 143 16.440 174.394 173.567 1.00 52.73 C
ANISOU 1066 CZ2 TRP A 143 8100 4812 7125 6 133 147 C
ATOM 1067 CZ3 TRP A 143 17.657 176.400 174.142 1.00 52.71 C
ANISOU 1067 CZ3 TRP A 143 8047 4892 7090 83 37 136 C
ATOM 1068 CH2 TRP A 143 16.475 175.747 173.781 1.00 52.82 C
ANISOU 1068 CH2 TRP A 143 8047 4873 7149 22 105 141 C
ATOM 1069 N ASN A 144 22.895 170.492 173.193 1.00 56.83 N
ANISOU 1069 N ASN A 144 8907 5304 7382 448 -62 186 N
ATOM 1070 CA ASN A 144 23.287 169.810 171.976 1.00 58.75 C
ANISOU 1070 CA ASN A 144 9149 5539 7635 470 -54 180 C
ATOM 1071 C ASN A 144 22.989 168.308 172.064 1.00 61.06 C
ANISOU 1071 C ASN A 144 9608 5721 7873 493 7 191 C
ATOM 1072 O ASN A 144 22.646 167.798 173.135 1.00 61.58 O
ANISOU 1072 O ASN A 144 9782 5726 7888 511 35 208 O
ATOM 1073 CB ASN A 144 24.772 170.059 171.741 1.00 59.69 C
ANISOU 1073 CB ASN A 144 9194 5739 7746 573 -114 191 C
ATOM 1074 CG ASN A 144 25.636 169.529 172.850 1.00 63.84 C
ANISOU 1074 CG ASN A 144 9791 6259 8207 687 -141 222 C
ATOM 1075 OD1 ASN A 144 25.597 168.347 173.197 1.00 65.69 O
ANISOU 1075 OD1 ASN A 144 10165 6409 8384 741 -101 237 O
ATOM 1076 ND2 ASN A 144 26.438 170.388 173.443 1.00 64.99 N
ANISOU 1076 ND2 ASN A 144 9852 6490 8352 722 -214 233 N
ATOM 1077 N ASN A 145 23.148 167.589 170.951 1.00 62.40 N
ANISOU 1077 N ASN A 145 9813 5857 8039 502 29 183 N
ATOM 1078 CA ASN A 145 22.922 166.144 170.930 1.00 64.14 C
ANISOU 1078 CA ASN A 145 10210 5963 8199 521 86 193 C
ATOM 1079 C ASN A 145 24.241 165.365 171.008 1.00 65.32 C
ANISOU 1079 C ASN A 145 10425 6107 8288 680 75 214 C
ATOM 1080 O ASN A 145 24.314 164.249 170.498 1.00 65.34 O
ANISOU 1080 O ASN A 145 10542 6035 8250 715 115 215 O
ATOM 1081 CB ASN A 145 22.150 165.734 169.670 1.00 65.84 C
ANISOU 1081 CB ASN A 145 10456 6123 8436 416 120 170 C
ATOM 1082 CG ASN A 145 20.782 166.363 169.540 1.00 69.63 C
ANISOU 1082 CG ASN A 145 10878 6604 8975 263 134 156 C
ATOM 1083 OD1 ASN A 145 20.059 166.538 170.524 1.00 70.55 O
ANISOU 1083 OD1 ASN A 145 10985 6724 9097 236 148 165 O
ATOM 1084 ND2 ASN A 145 20.384 166.703 168.314 1.00 70.80 N
ANISOU 1084 ND2 ASN A 145 10987 6749 9164 167 130 135 N
ATOM 1085 N CYS A 146 25.283 165.944 171.625 1.00 66.21 N
ANISOU 1085 N CYS A 146 10459 6302 8396 779 19 233 N
ATOM 1086 CA CYS A 146 26.566 165.260 171.760 1.00 67.71 C
ANISOU 1086 CA CYS A 146 10689 6504 8535 945 3 262 C
ATOM 1087 C CYS A 146 26.494 164.072 172.706 1.00 69.04 C
ANISOU 1087 C CYS A 146 11056 6563 8614 1019 36 286 C
ATOM 1088 O CYS A 146 27.253 163.130 172.536 1.00 69.35 O
ANISOU 1088 O CYS A 146 11182 6566 8600 1148 52 307 O
ATOM 1089 CB CYS A 146 27.683 166.224 172.149 1.00 68.68 C
ANISOU 1089 CB CYS A 146 10650 6761 8684 1018 -80 278 C
ATOM 1090 SG CYS A 146 28.057 167.474 170.893 1.00 72.75 S
ANISOU 1090 SG CYS A 146 10953 7400 9288 964 -111 256 S
ATOM 1091 N GLY A 147 25.577 164.100 173.667 1.00 69.80 N
ANISOU 1091 N GLY A 147 11231 6600 8689 943 55 286 N
ATOM 1092 CA GLY A 147 25.393 162.987 174.590 1.00 71.18 C
ANISOU 1092 CA GLY A 147 11616 6658 8773 999 95 309 C
ATOM 1093 C GLY A 147 24.763 161.752 173.964 1.00 72.49 C
ANISOU 1093 C GLY A 147 11957 6690 8895 961 178 301 C
ATOM 1094 O GLY A 147 24.906 160.643 174.484 1.00 72.50 O
ANISOU 1094 O GLY A 147 12152 6589 8808 1042 212 323 O
ATOM 1095 N GLN A 148 24.063 161.922 172.835 1.00 73.47 N
ANISOU 1095 N GLN A 148 12029 6810 9075 834 205 271 N
ATOM 1096 CA GLN A 148 23.410 160.813 172.135 1.00 74.86 C
ANISOU 1096 CA GLN A 148 12370 6861 9212 769 273 261 C
ATOM 1097 C GLN A 148 23.930 160.732 170.688 1.00 75.67 C
ANISOU 1097 C GLN A 148 12428 6988 9337 797 267 245 C
ATOM 1098 O GLN A 148 23.174 160.981 169.738 1.00 75.74 O
ANISOU 1098 O GLN A 148 12392 6992 9393 663 276 218 O
ATOM 1099 CB GLN A 148 21.876 160.992 172.145 1.00 77.15 C
ANISOU 1099 CB GLN A 148 12660 7110 9543 567 312 242 C
ATOM 1100 CG GLN A 148 21.297 161.546 173.448 1.00 82.32 C
ANISOU 1100 CG GLN A 148 13295 7779 10205 526 320 254 C
ATOM 1101 CD GLN A 148 20.387 160.556 174.137 1.00 88.93 C
ANISOU 1101 CD GLN A 148 14313 8488 10990 430 400 263 C
ATOM 1102 OE1 GLN A 148 20.777 159.421 174.454 1.00 91.36 O
ANISOU 1102 OE1 GLN A 148 14830 8682 11202 494 438 280 O
ATOM 1103 NE2 GLN A 148 19.148 160.966 174.394 1.00 89.73 N
ANISOU 1103 NE2 GLN A 148 14339 8604 11150 278 432 255 N
ATOM 1104 N PRO A 149 25.232 160.419 170.492 1.00 76.05 N
ANISOU 1104 N PRO A 149 12481 7064 9349 976 252 265 N
ATOM 1105 CA PRO A 149 25.763 160.384 169.128 1.00 76.58 C
ANISOU 1105 CA PRO A 149 12508 7155 9433 1013 260 252 C
ATOM 1106 C PRO A 149 25.142 159.298 168.287 1.00 77.60 C
ANISOU 1106 C PRO A 149 12842 7141 9503 958 324 238 C
ATOM 1107 O PRO A 149 24.747 158.260 168.816 1.00 77.67 O
ANISOU 1107 O PRO A 149 13058 7023 9431 964 368 250 O
ATOM 1108 CB PRO A 149 27.258 160.114 169.340 1.00 77.06 C
ANISOU 1108 CB PRO A 149 12547 7272 9460 1232 243 286 C
ATOM 1109 CG PRO A 149 27.340 159.430 170.636 1.00 77.24 C
ANISOU 1109 CG PRO A 149 12707 7230 9410 1313 246 316 C
ATOM 1110 CD PRO A 149 26.279 160.071 171.474 1.00 75.54 C
ANISOU 1110 CD PRO A 149 12461 7014 9227 1157 229 302 C
ATOM 1111 N LYS A 150 25.046 159.538 166.976 1.00 78.42 N
ANISOU 1111 N LYS A 150 12902 7257 9638 900 328 213 N
ATOM 1112 CA LYS A 150 24.562 158.514 166.060 1.00 79.74 C
ANISOU 1112 CA LYS A 150 13273 7284 9739 850 381 198 C
ATOM 1113 C LYS A 150 25.769 157.600 165.835 1.00 81.27 C
ANISOU 1113 C LYS A 150 13599 7431 9849 1065 425 223 C
ATOM 1114 O LYS A 150 26.616 157.880 164.981 1.00 81.36 O
ANISOU 1114 O LYS A 150 13526 7509 9878 1164 428 224 O
ATOM 1115 CB LYS A 150 24.063 159.126 164.743 1.00 80.92 C
ANISOU 1115 CB LYS A 150 13336 7463 9945 720 362 164 C
ATOM 1116 CG LYS A 150 22.766 159.895 164.904 1.00 84.04 C
ANISOU 1116 CG LYS A 150 13612 7899 10420 518 322 143 C
ATOM 1117 CD LYS A 150 22.018 159.981 163.589 1.00 88.08 C
ANISOU 1117 CD LYS A 150 14138 8378 10951 373 309 113 C
ATOM 1118 CE LYS A 150 20.622 160.533 163.757 1.00 92.14 C
ANISOU 1118 CE LYS A 150 14554 8919 11538 173 273 98 C
ATOM 1119 NZ LYS A 150 20.625 161.967 164.162 1.00 94.51 N
ANISOU 1119 NZ LYS A 150 14601 9370 11939 162 220 93 N
ATOM 1120 N GLU A 151 25.891 156.553 166.673 1.00 82.21 N
ANISOU 1120 N GLU A 151 13919 7442 9877 1149 462 247 N
ATOM 1121 CA GLU A 151 27.038 155.658 166.626 1.00 83.41 C
ANISOU 1121 CA GLU A 151 14201 7547 9944 1376 504 278 C
ATOM 1122 C GLU A 151 27.105 154.820 165.374 1.00 83.86 C
ANISOU 1122 C GLU A 151 14447 7487 9929 1399 569 265 C
ATOM 1123 O GLU A 151 28.202 154.529 164.920 1.00 83.90 O
ANISOU 1123 O GLU A 151 14469 7508 9901 1591 603 285 O
ATOM 1124 CB GLU A 151 27.159 154.785 167.879 1.00 86.37 C
ANISOU 1124 CB GLU A 151 14743 7839 10234 1475 519 311 C
ATOM 1125 CG GLU A 151 28.090 155.371 168.937 1.00 92.26 C
ANISOU 1125 CG GLU A 151 15316 8721 11016 1623 460 345 C
ATOM 1126 CD GLU A 151 29.452 155.890 168.493 1.00 99.75 C
ANISOU 1126 CD GLU A 151 16072 9816 12013 1795 434 366 C
ATOM 1127 OE1 GLU A 151 30.030 155.352 167.518 1.00101.04 O
ANISOU 1127 OE1 GLU A 151 16303 9946 12142 1899 489 369 O
ATOM 1128 OE2 GLU A 151 29.950 156.837 169.145 1.00102.30 O
ANISOU 1128 OE2 GLU A 151 16179 10287 12405 1825 362 380 O
ATOM 1129 N GLY A 152 25.965 154.488 164.794 1.00 84.10 N
ANISOU 1129 N GLY A 152 14606 7408 9938 1205 584 232 N
ATOM 1130 CA GLY A 152 25.937 153.742 163.544 1.00 84.92 C
ANISOU 1130 CA GLY A 152 14904 7392 9968 1199 636 215 C
ATOM 1131 C GLY A 152 26.506 154.556 162.404 1.00 85.60 C
ANISOU 1131 C GLY A 152 14819 7586 10117 1230 625 201 C
ATOM 1132 O GLY A 152 27.246 154.030 161.574 1.00 85.68 O
ANISOU 1132 O GLY A 152 14943 7547 10066 1363 683 206 O
ATOM 1133 N LYS A 153 26.205 155.859 162.385 1.00 85.93 N
ANISOU 1133 N LYS A 153 14592 7780 10280 1129 559 187 N
ATOM 1134 CA LYS A 153 26.726 156.779 161.379 1.00 86.65 C
ANISOU 1134 CA LYS A 153 14496 7987 10440 1142 542 174 C
ATOM 1135 C LYS A 153 28.234 156.985 161.575 1.00 87.22 C
ANISOU 1135 C LYS A 153 14442 8171 10526 1374 563 208 C
ATOM 1136 O LYS A 153 28.977 157.007 160.595 1.00 87.50 O
ANISOU 1136 O LYS A 153 14440 8242 10563 1457 598 209 O
ATOM 1137 CB LYS A 153 25.990 158.122 161.457 1.00 88.11 C
ANISOU 1137 CB LYS A 153 14443 8295 10742 971 463 152 C
ATOM 1138 CG LYS A 153 26.114 158.944 160.191 1.00 91.93 C
ANISOU 1138 CG LYS A 153 14802 8850 11279 917 445 128 C
ATOM 1139 CD LYS A 153 25.123 160.100 160.164 1.00 96.04 C
ANISOU 1139 CD LYS A 153 15168 9434 11889 713 372 102 C
ATOM 1140 CE LYS A 153 23.686 159.637 160.224 1.00 99.54 C
ANISOU 1140 CE LYS A 153 15773 9750 12297 529 363 79 C
ATOM 1141 NZ LYS A 153 22.772 160.560 159.508 1.00101.75 N
ANISOU 1141 NZ LYS A 153 15957 10069 12635 373 309 49 N
ATOM 1142 N ALA A 154 28.686 157.105 162.841 1.00 87.27 N
ANISOU 1142 N ALA A 154 14390 8231 10539 1481 542 241 N
ATOM 1143 CA ALA A 154 30.106 157.271 163.163 1.00 87.72 C
ANISOU 1143 CA ALA A 154 14310 8406 10614 1699 547 281 C
ATOM 1144 C ALA A 154 30.911 156.034 162.796 1.00 87.93 C
ANISOU 1144 C ALA A 154 14537 8335 10536 1911 632 310 C
ATOM 1145 O ALA A 154 32.006 156.168 162.261 1.00 88.24 O
ANISOU 1145 O ALA A 154 14475 8464 10588 2096 660 341 O
ATOM 1146 CB ALA A 154 30.289 157.582 164.639 1.00 88.10 C
ANISOU 1146 CB ALA A 154 14235 8542 10699 1734 481 307 C
ATOM 1147 N HIS A 155 30.378 154.836 163.063 1.00 87.52 N
ANISOU 1147 N HIS A 155 14773 8099 10380 1885 676 303 N
ATOM 1148 CA HIS A 155 31.073 153.602 162.709 1.00 87.61 C
ANISOU 1148 CA HIS A 155 15022 7989 10275 2083 763 329 C
ATOM 1149 C HIS A 155 31.123 153.432 161.200 1.00 86.92 C
ANISOU 1149 C HIS A 155 15033 7837 10154 2068 829 305 C
ATOM 1150 O HIS A 155 32.149 153.014 160.675 1.00 87.17 O
ANISOU 1150 O HIS A 155 15115 7865 10142 2265 904 329 O
ATOM 1151 CB HIS A 155 30.411 152.376 163.354 1.00 88.93 C
ANISOU 1151 CB HIS A 155 15482 7972 10336 2038 783 328 C
ATOM 1152 CG HIS A 155 30.679 152.245 164.821 1.00 92.23 C
ANISOU 1152 CG HIS A 155 15878 8420 10745 2137 746 365 C
ATOM 1153 ND1 HIS A 155 31.967 152.106 165.311 1.00 94.44 N
ANISOU 1153 ND1 HIS A 155 16138 8750 10996 2403 762 415 N
ATOM 1154 CD2 HIS A 155 29.811 152.214 165.859 1.00 93.60 C
ANISOU 1154 CD2 HIS A 155 16049 8582 10934 2010 693 361 C
ATOM 1155 CE1 HIS A 155 31.842 152.015 166.626 1.00 95.11 C
ANISOU 1155 CE1 HIS A 155 16219 8848 11072 2433 710 439 C
ATOM 1156 NE2 HIS A 155 30.562 152.078 167.002 1.00 94.93 N
ANISOU 1156 NE2 HIS A 155 16212 8783 11072 2197 674 406 N
ATOM 1157 N SER A 156 30.039 153.783 160.495 1.00 86.13 N
ANISOU 1157 N SER A 156 14949 7698 10079 1832 800 259 N
ATOM 1158 CA SER A 156 29.979 153.671 159.039 1.00 86.12 C
ANISOU 1158 CA SER A 156 15051 7628 10042 1785 848 231 C
ATOM 1159 C SER A 156 31.072 154.494 158.372 1.00 85.84 C
ANISOU 1159 C SER A 156 14811 7737 10066 1921 878 246 C
ATOM 1160 O SER A 156 31.777 153.997 157.498 1.00 85.97 O
ANISOU 1160 O SER A 156 14953 7695 10016 2053 966 253 O
ATOM 1161 CB SER A 156 28.585 154.052 158.527 1.00 87.74 C
ANISOU 1161 CB SER A 156 15227 7817 10294 1504 781 184 C
ATOM 1162 OG SER A 156 28.536 154.936 157.415 1.00 90.33 O
ANISOU 1162 OG SER A 156 15620 8105 10597 1463 812 158 O
ATOM 1163 N GLN A 157 31.230 155.737 158.806 1.00 85.39 N
ANISOU 1163 N GLN A 157 14443 7868 10132 1891 809 252 N
ATOM 1164 CA GLN A 157 32.240 156.619 158.245 1.00 85.61 C
ANISOU 1164 CA GLN A 157 14255 8047 10227 2000 833 268 C
ATOM 1165 C GLN A 157 33.662 156.401 158.771 1.00 85.66 C
ANISOU 1165 C GLN A 157 14191 8130 10226 2260 871 325 C
ATOM 1166 O GLN A 157 34.553 157.181 158.440 1.00 86.06 O
ANISOU 1166 O GLN A 157 14064 8310 10326 2385 905 350 O
ATOM 1167 CB GLN A 157 31.838 158.066 158.448 1.00 86.91 C
ANISOU 1167 CB GLN A 157 14125 8377 10521 1849 739 252 C
ATOM 1168 CG GLN A 157 30.701 158.496 157.562 1.00 90.20 C
ANISOU 1168 CG GLN A 157 14577 8735 10958 1591 678 202 C
ATOM 1169 CD GLN A 157 30.641 159.995 157.518 1.00 95.47 C
ANISOU 1169 CD GLN A 157 15041 9521 11713 1487 643 180 C
ATOM 1170 OE1 GLN A 157 31.671 160.691 157.538 1.00 96.97 O
ANISOU 1170 OE1 GLN A 157 15145 9783 11916 1594 694 193 O
ATOM 1171 NE2 GLN A 157 29.430 160.536 157.457 1.00 96.57 N
ANISOU 1171 NE2 GLN A 157 15103 9679 11909 1283 561 149 N
ATOM 1172 N GLY A 158 33.871 155.377 159.587 1.00 85.15 N
ANISOU 1172 N GLY A 158 14262 7990 10101 2340 864 348 N
ATOM 1173 CA GLY A 158 35.186 155.085 160.133 1.00 85.33 C
ANISOU 1173 CA GLY A 158 14228 8081 10111 2597 890 405 C
ATOM 1174 C GLY A 158 35.714 156.177 161.035 1.00 85.15 C
ANISOU 1174 C GLY A 158 13858 8285 10211 2624 813 431 C
ATOM 1175 O GLY A 158 36.920 156.442 161.054 1.00 85.24 O
ANISOU 1175 O GLY A 158 13714 8417 10256 2797 848 470 O
ATOM 1176 N CYS A 159 34.812 156.845 161.764 1.00 84.72 N
ANISOU 1176 N CYS A 159 13678 8289 10224 2445 709 410 N
ATOM 1177 CA CYS A 159 35.222 157.904 162.687 1.00 84.63 C
ANISOU 1177 CA CYS A 159 13360 8479 10317 2456 625 433 C
ATOM 1178 C CYS A 159 35.981 157.302 163.855 1.00 84.86 C
ANISOU 1178 C CYS A 159 13399 8530 10314 2629 589 483 C
ATOM 1179 O CYS A 159 35.738 156.153 164.232 1.00 84.86 O
ANISOU 1179 O CYS A 159 13635 8385 10222 2671 608 488 O
ATOM 1180 CB CYS A 159 34.026 158.719 163.176 1.00 84.23 C
ANISOU 1180 CB CYS A 159 13190 8474 10339 2215 529 394 C
ATOM 1181 SG CYS A 159 33.196 159.693 161.895 1.00 83.90 S
ANISOU 1181 SG CYS A 159 13172 8380 10326 1976 543 331 S
ATOM 1182 N GLY A 160 36.873 158.087 164.434 1.00 84.93 N
ANISOU 1182 N GLY A 160 13151 8721 10397 2710 525 521 N
ATOM 1183 CA GLY A 160 37.631 157.643 165.591 1.00 85.67 C
ANISOU 1183 CA GLY A 160 13238 8850 10462 2876 472 572 C
ATOM 1184 C GLY A 160 36.820 157.692 166.873 1.00 86.16 C
ANISOU 1184 C GLY A 160 13388 8853 10497 2776 387 562 C
ATOM 1185 O GLY A 160 35.672 158.154 166.881 1.00 86.40 O
ANISOU 1185 O GLY A 160 13485 8810 10533 2567 368 515 O
ATOM 1186 N GLU A 161 37.404 157.201 167.972 1.00 86.09 N
ANISOU 1186 N GLU A 161 13378 8876 10456 2936 334 611 N
ATOM 1187 CA GLU A 161 36.725 157.233 169.262 1.00 86.58 C
ANISOU 1187 CA GLU A 161 13536 8878 10482 2854 260 605 C
ATOM 1188 C GLU A 161 36.675 158.683 169.725 1.00 86.32 C
ANISOU 1188 C GLU A 161 13249 9002 10547 2715 149 596 C
ATOM 1189 O GLU A 161 37.663 159.407 169.604 1.00 86.70 O
ANISOU 1189 O GLU A 161 13079 9214 10648 2807 79 634 O
ATOM 1190 CB GLU A 161 37.432 156.337 170.289 1.00 89.67 C
ANISOU 1190 CB GLU A 161 14050 9231 10788 3079 241 660 C
ATOM 1191 CG GLU A 161 37.575 154.887 169.846 1.00 95.86 C
ANISOU 1191 CG GLU A 161 15116 9844 11463 3229 357 671 C
ATOM 1192 CD GLU A 161 36.278 154.153 169.560 1.00103.25 C
ANISOU 1192 CD GLU A 161 16324 10576 12331 3050 419 618 C
ATOM 1193 OE1 GLU A 161 35.291 154.378 170.299 1.00104.85 O
ANISOU 1193 OE1 GLU A 161 16573 10736 12531 2891 366 596 O
ATOM 1194 OE2 GLU A 161 36.250 153.346 168.602 1.00105.26 O
ANISOU 1194 OE2 GLU A 161 16749 10712 12534 3065 522 601 O
ATOM 1195 N GLY A 162 35.510 159.114 170.182 1.00 85.49 N
ANISOU 1195 N GLY A 162 13173 8846 10464 2488 133 545 N
ATOM 1196 CA GLY A 162 35.307 160.504 170.573 1.00 84.90 C
ANISOU 1196 CA GLY A 162 12892 8896 10470 2344 36 532 C
ATOM 1197 C GLY A 162 34.888 161.394 169.413 1.00 83.87 C
ANISOU 1197 C GLY A 162 12618 8826 10424 2188 57 490 C
ATOM 1198 O GLY A 162 34.774 162.609 169.584 1.00 84.26 O
ANISOU 1198 O GLY A 162 12461 9007 10549 2102 -14 485 O
ATOM 1199 N GLN A 163 34.642 160.807 168.221 1.00 82.28 N
ANISOU 1199 N GLN A 163 12536 8525 10201 2157 153 463 N
ATOM 1200 CA GLN A 163 34.223 161.560 167.044 1.00 81.24 C
ANISOU 1200 CA GLN A 163 12298 8432 10135 2016 176 424 C
ATOM 1201 C GLN A 163 32.833 161.142 166.560 1.00 79.94 C
ANISOU 1201 C GLN A 163 12329 8110 9935 1873 232 379 C
ATOM 1202 O GLN A 163 32.397 160.016 166.798 1.00 80.18 O
ANISOU 1202 O GLN A 163 12583 7999 9884 1907 273 381 O
ATOM 1203 CB GLN A 163 35.215 161.362 165.891 1.00 82.42 C
ANISOU 1203 CB GLN A 163 12373 8643 10300 2144 241 443 C
ATOM 1204 CG GLN A 163 36.616 161.873 166.145 1.00 84.62 C
ANISOU 1204 CG GLN A 163 12456 9082 10614 2312 200 498 C
ATOM 1205 CD GLN A 163 37.402 161.853 164.868 1.00 87.77 C
ANISOU 1205 CD GLN A 163 12753 9554 11042 2409 278 513 C
ATOM 1206 OE1 GLN A 163 37.282 160.940 164.043 1.00 88.82 O
ANISOU 1206 OE1 GLN A 163 13018 9588 11143 2395 372 488 O
ATOM 1207 NE2 GLN A 163 38.220 162.866 164.673 1.00 88.36 N
ANISOU 1207 NE2 GLN A 163 12592 9803 11177 2501 237 556 N
ATOM 1208 N VAL A 164 32.155 162.053 165.850 1.00 78.35 N
ANISOU 1208 N VAL A 164 12047 7932 9791 1711 231 339 N
ATOM 1209 CA VAL A 164 30.849 161.833 165.235 1.00 77.13 C
ANISOU 1209 CA VAL A 164 12052 7642 9610 1562 271 298 C
ATOM 1210 C VAL A 164 30.915 162.282 163.777 1.00 75.06 C
ANISOU 1210 C VAL A 164 11716 7411 9392 1480 294 268 C
ATOM 1211 O VAL A 164 31.791 163.072 163.397 1.00 74.89 O
ANISOU 1211 O VAL A 164 11497 7523 9434 1495 269 274 O
ATOM 1212 CB VAL A 164 29.729 162.634 165.963 1.00 78.29 C
ANISOU 1212 CB VAL A 164 12174 7781 9791 1387 216 274 C
ATOM 1213 CG1 VAL A 164 29.574 162.197 167.413 1.00 79.20 C
ANISOU 1213 CG1 VAL A 164 12438 7812 9844 1423 213 293 C
ATOM 1214 CG2 VAL A 164 29.971 164.136 165.866 1.00 78.71 C
ANISOU 1214 CG2 VAL A 164 11983 7993 9930 1341 141 274 C
ATOM 1215 N ALA A 165 29.944 161.831 162.960 1.00 73.37 N
ANISOU 1215 N ALA A 165 11669 7069 9138 1385 338 237 N
ATOM 1216 CA ALA A 165 29.803 162.325 161.595 1.00 72.32 C
ANISOU 1216 CA ALA A 165 11500 6943 9033 1294 355 207 C
ATOM 1217 C ALA A 165 29.207 163.716 161.771 1.00 71.31 C
ANISOU 1217 C ALA A 165 11179 6919 8994 1150 278 188 C
ATOM 1218 O ALA A 165 28.163 163.858 162.404 1.00 71.60 O
ANISOU 1218 O ALA A 165 11232 6927 9045 1036 239 176 O
ATOM 1219 CB ALA A 165 28.845 161.453 160.812 1.00 72.13 C
ANISOU 1219 CB ALA A 165 11698 6758 8949 1186 390 177 C
ATOM 1220 N CYS A 166 29.936 164.738 161.347 1.00 69.98 N
ANISOU 1220 N CYS A 166 10831 6873 8885 1158 262 188 N
ATOM 1221 CA CYS A 166 29.517 166.108 161.547 1.00 69.10 C
ANISOU 1221 CA CYS A 166 10555 6851 8850 1026 191 171 C
ATOM 1222 C CYS A 166 28.416 166.517 160.605 1.00 67.68 C
ANISOU 1222 C CYS A 166 10416 6617 8684 870 187 131 C
ATOM 1223 O CYS A 166 28.667 166.905 159.467 1.00 68.10 O
ANISOU 1223 O CYS A 166 10470 6671 8734 868 218 119 O
ATOM 1224 CB CYS A 166 30.702 167.056 161.469 1.00 69.98 C
ANISOU 1224 CB CYS A 166 10462 7113 9014 1083 169 189 C
ATOM 1225 SG CYS A 166 30.352 168.710 162.096 1.00 72.75 S
ANISOU 1225 SG CYS A 166 10633 7565 9444 934 79 170 S
ATOM 1226 N LEU A 167 27.189 166.427 161.086 1.00 65.85 N
ANISOU 1226 N LEU A 167 10214 6340 8467 740 148 113 N
ATOM 1227 CA LEU A 167 26.002 166.779 160.326 1.00 64.58 C
ANISOU 1227 CA LEU A 167 10079 6134 8326 586 129 79 C
ATOM 1228 C LEU A 167 25.232 167.760 161.181 1.00 62.70 C
ANISOU 1228 C LEU A 167 9719 5954 8150 483 68 73 C
ATOM 1229 O LEU A 167 24.973 167.458 162.343 1.00 62.71 O
ANISOU 1229 O LEU A 167 9733 5949 8147 497 61 87 O
ATOM 1230 CB LEU A 167 25.150 165.516 160.129 1.00 64.89 C
ANISOU 1230 CB LEU A 167 10325 6028 8301 540 161 71 C
ATOM 1231 CG LEU A 167 25.099 164.904 158.740 1.00 66.02 C
ANISOU 1231 CG LEU A 167 10609 6082 8394 517 195 52 C
ATOM 1232 CD1 LEU A 167 26.443 164.454 158.310 1.00 66.25 C
ANISOU 1232 CD1 LEU A 167 10678 6117 8376 685 261 69 C
ATOM 1233 CD2 LEU A 167 24.143 163.730 158.722 1.00 66.68 C
ANISOU 1233 CD2 LEU A 167 10895 6023 8416 447 212 46 C
ATOM 1234 N PHE A 168 24.830 168.914 160.626 1.00 61.03 N
ANISOU 1234 N PHE A 168 9405 5792 7990 384 27 52 N
ATOM 1235 CA PHE A 168 24.117 169.923 161.408 1.00 59.97 C
ANISOU 1235 CA PHE A 168 9158 5715 7913 304 -23 48 C
ATOM 1236 C PHE A 168 22.936 169.382 162.213 1.00 59.11 C
ANISOU 1236 C PHE A 168 9114 5541 7804 229 -22 49 C
ATOM 1237 O PHE A 168 22.880 169.568 163.427 1.00 59.30 O
ANISOU 1237 O PHE A 168 9108 5588 7836 246 -28 63 O
ATOM 1238 CB PHE A 168 23.667 171.106 160.536 1.00 59.64 C
ANISOU 1238 CB PHE A 168 9019 5723 7919 215 -64 26 C
ATOM 1239 CG PHE A 168 23.011 172.223 161.323 1.00 60.29 C
ANISOU 1239 CG PHE A 168 8987 5865 8054 154 -109 24 C
ATOM 1240 CD1 PHE A 168 21.665 172.176 161.640 1.00 61.17 C
ANISOU 1240 CD1 PHE A 168 9115 5939 8187 68 -119 20 C
ATOM 1241 CD2 PHE A 168 23.746 173.305 161.767 1.00 61.10 C
ANISOU 1241 CD2 PHE A 168 8971 6062 8183 181 -137 28 C
ATOM 1242 CE1 PHE A 168 21.075 173.181 162.390 1.00 61.89 C
ANISOU 1242 CE1 PHE A 168 9111 6081 8323 26 -148 21 C
ATOM 1243 CE2 PHE A 168 23.142 174.324 162.492 1.00 61.77 C
ANISOU 1243 CE2 PHE A 168 8975 6189 8304 129 -174 26 C
ATOM 1244 CZ PHE A 168 21.810 174.259 162.791 1.00 61.61 C
ANISOU 1244 CZ PHE A 168 8979 6128 8304 60 -176 23 C
ATOM 1245 N GLU A 169 22.024 168.694 161.550 1.00 58.11 N
ANISOU 1245 N GLU A 169 9095 5326 7659 148 -10 36 N
ATOM 1246 CA GLU A 169 20.813 168.216 162.191 1.00 57.87 C
ANISOU 1246 CA GLU A 169 9117 5236 7633 53 -5 38 C
ATOM 1247 C GLU A 169 21.083 167.130 163.254 1.00 57.36 C
ANISOU 1247 C GLU A 169 9167 5111 7515 122 41 60 C
ATOM 1248 O GLU A 169 20.242 166.921 164.131 1.00 57.54 O
ANISOU 1248 O GLU A 169 9207 5108 7549 59 52 68 O
ATOM 1249 CB GLU A 169 19.747 167.796 161.149 1.00 60.01 C
ANISOU 1249 CB GLU A 169 9464 5436 7901 -73 -18 19 C
ATOM 1250 CG GLU A 169 20.260 167.408 159.755 1.00 64.59 C
ANISOU 1250 CG GLU A 169 10126 5977 8438 -52 -16 3 C
ATOM 1251 CD GLU A 169 20.575 168.491 158.728 1.00 68.51 C
ANISOU 1251 CD GLU A 169 10519 6543 8969 -59 -55 -13 C
ATOM 1252 OE1 GLU A 169 19.626 169.058 158.138 1.00 67.80 O
ANISOU 1252 OE1 GLU A 169 10380 6462 8917 -173 -106 -28 O
ATOM 1253 OE2 GLU A 169 21.779 168.740 158.483 1.00 70.34 O
ANISOU 1253 OE2 GLU A 169 10722 6818 9185 48 -32 -9 O
ATOM 1254 N ASP A 170 22.268 166.501 163.231 1.00 56.55 N
ANISOU 1254 N ASP A 170 9141 4989 7356 254 71 73 N
ATOM 1255 CA ASP A 170 22.612 165.487 164.227 1.00 56.41 C
ANISOU 1255 CA ASP A 170 9239 4914 7281 337 109 97 C
ATOM 1256 C ASP A 170 23.170 166.085 165.522 1.00 55.04 C
ANISOU 1256 C ASP A 170 8973 4817 7123 412 88 118 C
ATOM 1257 O ASP A 170 23.104 165.433 166.567 1.00 55.24 O
ANISOU 1257 O ASP A 170 9086 4794 7108 446 110 136 O
ATOM 1258 CB ASP A 170 23.652 164.500 163.669 1.00 58.79 C
ANISOU 1258 CB ASP A 170 9653 5170 7513 474 148 108 C
ATOM 1259 CG ASP A 170 23.164 163.580 162.580 1.00 64.21 C
ANISOU 1259 CG ASP A 170 10494 5749 8154 419 178 91 C
ATOM 1260 OD1 ASP A 170 21.960 163.643 162.243 1.00 65.75 O
ANISOU 1260 OD1 ASP A 170 10704 5907 8371 265 160 71 O
ATOM 1261 OD2 ASP A 170 23.985 162.794 162.062 1.00 66.11 O
ANISOU 1261 OD2 ASP A 170 10844 5943 8333 533 220 99 O
ATOM 1262 N VAL A 171 23.791 167.269 165.448 1.00 53.34 N
ANISOU 1262 N VAL A 171 8594 4716 6958 436 44 116 N
ATOM 1263 CA VAL A 171 24.431 167.853 166.621 1.00 51.94 C
ANISOU 1263 CA VAL A 171 8336 4612 6788 501 12 135 C
ATOM 1264 C VAL A 171 23.650 169.045 167.190 1.00 50.53 C
ANISOU 1264 C VAL A 171 8041 4493 6665 410 -24 126 C
ATOM 1265 O VAL A 171 23.668 169.247 168.398 1.00 50.49 O
ANISOU 1265 O VAL A 171 8022 4512 6651 440 -41 141 O
ATOM 1266 CB VAL A 171 25.923 168.190 166.351 1.00 52.21 C
ANISOU 1266 CB VAL A 171 8284 4734 6821 622 -12 150 C
ATOM 1267 CG1 VAL A 171 26.703 166.942 165.978 1.00 52.50 C
ANISOU 1267 CG1 VAL A 171 8439 4711 6798 738 35 165 C
ATOM 1268 CG2 VAL A 171 26.079 169.247 165.264 1.00 52.55 C
ANISOU 1268 CG2 VAL A 171 8200 4849 6917 568 -34 129 C
ATOM 1269 N VAL A 172 22.959 169.817 166.340 1.00 49.21 N
ANISOU 1269 N VAL A 172 7800 4346 6550 308 -38 102 N
ATOM 1270 CA VAL A 172 22.184 170.972 166.791 1.00 48.66 C
ANISOU 1270 CA VAL A 172 7632 4328 6531 233 -66 95 C
ATOM 1271 C VAL A 172 20.723 170.566 167.027 1.00 48.64 C
ANISOU 1271 C VAL A 172 7679 4259 6543 132 -32 91 C
ATOM 1272 O VAL A 172 20.041 170.163 166.076 1.00 48.97 O
ANISOU 1272 O VAL A 172 7739 4264 6601 57 -25 77 O
ATOM 1273 CB VAL A 172 22.298 172.158 165.805 1.00 48.65 C
ANISOU 1273 CB VAL A 172 7510 4397 6577 192 -106 76 C
ATOM 1274 CG1 VAL A 172 21.567 173.387 166.329 1.00 48.81 C
ANISOU 1274 CG1 VAL A 172 7444 4464 6638 135 -131 71 C
ATOM 1275 CG2 VAL A 172 23.753 172.485 165.545 1.00 48.92 C
ANISOU 1275 CG2 VAL A 172 7489 4499 6598 281 -130 83 C
ATOM 1276 N PRO A 173 20.240 170.669 168.292 1.00 47.81 N
ANISOU 1276 N PRO A 173 7600 4136 6429 124 -9 105 N
ATOM 1277 CA PRO A 173 18.856 170.276 168.598 1.00 47.32 C
ANISOU 1277 CA PRO A 173 7580 4016 6383 27 37 107 C
ATOM 1278 C PRO A 173 17.817 171.086 167.833 1.00 47.24 C
ANISOU 1278 C PRO A 173 7465 4040 6443 -76 20 92 C
ATOM 1279 O PRO A 173 17.970 172.291 167.646 1.00 47.56 O
ANISOU 1279 O PRO A 173 7398 4151 6521 -72 -18 83 O
ATOM 1280 CB PRO A 173 18.749 170.522 170.108 1.00 47.84 C
ANISOU 1280 CB PRO A 173 7655 4088 6435 54 58 124 C
ATOM 1281 CG PRO A 173 20.139 170.564 170.605 1.00 48.24 C
ANISOU 1281 CG PRO A 173 7731 4163 6436 172 26 135 C
ATOM 1282 CD PRO A 173 20.938 171.147 169.499 1.00 46.97 C
ANISOU 1282 CD PRO A 173 7476 4069 6300 197 -27 120 C
ATOM 1283 N MET A 174 16.752 170.421 167.404 1.00 46.80 N
ANISOU 1283 N MET A 174 7442 3934 6406 -175 46 91 N
ATOM 1284 CA MET A 174 15.697 171.075 166.656 1.00 47.13 C
ANISOU 1284 CA MET A 174 7375 4015 6517 -269 20 81 C
ATOM 1285 C MET A 174 14.847 172.007 167.524 1.00 48.02 C
ANISOU 1285 C MET A 174 7390 4176 6680 -292 38 92 C
ATOM 1286 O MET A 174 14.387 173.034 167.018 1.00 48.57 O
ANISOU 1286 O MET A 174 7352 4297 6807 -334 6 85 O
ATOM 1287 CB MET A 174 14.857 170.050 165.901 1.00 47.54 C
ANISOU 1287 CB MET A 174 7480 4006 6577 -381 29 80 C
ATOM 1288 CG MET A 174 13.867 170.647 164.961 1.00 49.49 C
ANISOU 1288 CG MET A 174 7611 4300 6893 -471 -20 71 C
ATOM 1289 SD MET A 174 14.569 171.802 163.795 1.00 56.59 S
ANISOU 1289 SD MET A 174 8453 5256 7793 -405 -89 47 S
ATOM 1290 CE MET A 174 15.251 170.677 162.611 1.00 58.16 C
ANISOU 1290 CE MET A 174 8777 5380 7942 -440 -111 31 C
ATOM 1291 N ASN A 175 14.700 171.705 168.845 1.00 47.94 N
ANISOU 1291 N ASN A 175 7425 4145 6645 -259 92 110 N
ATOM 1292 CA ASN A 175 13.982 172.579 169.807 1.00 48.24 C
ANISOU 1292 CA ASN A 175 7387 4221 6720 -268 125 122 C
ATOM 1293 C ASN A 175 14.756 173.881 170.072 1.00 47.55 C
ANISOU 1293 C ASN A 175 7246 4193 6627 -189 85 114 C
ATOM 1294 O ASN A 175 14.145 174.927 170.316 1.00 47.41 O
ANISOU 1294 O ASN A 175 7160 4212 6642 -191 99 120 O
ATOM 1295 CB ASN A 175 13.663 171.862 171.115 1.00 50.27 C
ANISOU 1295 CB ASN A 175 7735 4423 6944 -269 207 145 C
ATOM 1296 CG ASN A 175 14.822 171.054 171.623 1.00 55.44 C
ANISOU 1296 CG ASN A 175 8530 5022 7514 -191 211 149 C
ATOM 1297 OD1 ASN A 175 15.934 171.562 171.783 1.00 57.45 O
ANISOU 1297 OD1 ASN A 175 8790 5305 7734 -101 168 144 O
ATOM 1298 ND2 ASN A 175 14.612 169.761 171.821 1.00 56.49 N
ANISOU 1298 ND2 ASN A 175 8777 5076 7611 -227 261 160 N
ATOM 1299 N TYR A 176 16.107 173.820 169.986 1.00 46.90 N
ANISOU 1299 N TYR A 176 7197 4121 6502 -119 37 104 N
ATOM 1300 CA TYR A 176 16.953 175.007 170.075 1.00 46.33 C
ANISOU 1300 CA TYR A 176 7075 4107 6421 -61 -10 97 C
ATOM 1301 C TYR A 176 16.674 175.851 168.822 1.00 45.45 C
ANISOU 1301 C TYR A 176 6864 4042 6362 -102 -54 80 C
ATOM 1302 O TYR A 176 16.405 177.037 168.937 1.00 45.07 O
ANISOU 1302 O TYR A 176 6753 4032 6339 -106 -65 77 O
ATOM 1303 CB TYR A 176 18.472 174.655 170.180 1.00 46.13 C
ANISOU 1303 CB TYR A 176 7094 4090 6343 17 -51 96 C
ATOM 1304 CG TYR A 176 19.353 175.861 169.913 1.00 46.70 C
ANISOU 1304 CG TYR A 176 7098 4232 6415 50 -111 87 C
ATOM 1305 CD1 TYR A 176 19.624 176.784 170.914 1.00 47.44 C
ANISOU 1305 CD1 TYR A 176 7205 4344 6477 88 -125 96 C
ATOM 1306 CD2 TYR A 176 19.815 176.141 168.634 1.00 47.60 C
ANISOU 1306 CD2 TYR A 176 7145 4387 6554 36 -154 70 C
ATOM 1307 CE1 TYR A 176 20.380 177.924 170.662 1.00 48.02 C
ANISOU 1307 CE1 TYR A 176 7223 4476 6546 101 -183 88 C
ATOM 1308 CE2 TYR A 176 20.529 177.301 168.361 1.00 48.41 C
ANISOU 1308 CE2 TYR A 176 7189 4550 6654 53 -204 63 C
ATOM 1309 CZ TYR A 176 20.797 178.198 169.377 1.00 49.00 C
ANISOU 1309 CZ TYR A 176 7277 4643 6700 81 -220 72 C
ATOM 1310 OH TYR A 176 21.496 179.349 169.113 1.00 50.33 O
ANISOU 1310 OH TYR A 176 7396 4866 6860 82 -274 66 O
ATOM 1311 N MET A 177 16.728 175.231 167.644 1.00 44.99 N
ANISOU 1311 N MET A 177 6810 3972 6313 -133 -76 69 N
ATOM 1312 CA MET A 177 16.533 175.936 166.398 1.00 45.61 C
ANISOU 1312 CA MET A 177 6814 4085 6431 -173 -122 52 C
ATOM 1313 C MET A 177 15.163 176.592 166.243 1.00 46.33 C
ANISOU 1313 C MET A 177 6828 4194 6582 -233 -116 57 C
ATOM 1314 O MET A 177 15.073 177.704 165.712 1.00 46.98 O
ANISOU 1314 O MET A 177 6841 4319 6691 -234 -153 48 O
ATOM 1315 CB MET A 177 16.828 175.016 165.217 1.00 46.43 C
ANISOU 1315 CB MET A 177 6968 4150 6525 -204 -134 43 C
ATOM 1316 CG MET A 177 18.281 174.681 165.075 1.00 49.22 C
ANISOU 1316 CG MET A 177 7372 4501 6828 -133 -146 37 C
ATOM 1317 SD MET A 177 19.284 176.162 164.850 1.00 56.47 S
ANISOU 1317 SD MET A 177 8205 5501 7751 -85 -190 30 S
ATOM 1318 CE MET A 177 18.691 176.696 163.267 1.00 55.74 C
ANISOU 1318 CE MET A 177 8068 5425 7687 -138 -233 8 C
ATOM 1319 N VAL A 178 14.099 175.925 166.700 1.00 45.84 N
ANISOU 1319 N VAL A 178 6775 4100 6541 -283 -67 72 N
ATOM 1320 CA VAL A 178 12.754 176.481 166.567 1.00 45.67 C
ANISOU 1320 CA VAL A 178 6659 4107 6585 -337 -56 83 C
ATOM 1321 C VAL A 178 12.354 177.456 167.702 1.00 45.76 C
ANISOU 1321 C VAL A 178 6628 4147 6611 -294 -12 98 C
ATOM 1322 O VAL A 178 11.959 178.585 167.403 1.00 45.84 O
ANISOU 1322 O VAL A 178 6563 4201 6655 -281 -36 96 O
ATOM 1323 CB VAL A 178 11.731 175.355 166.390 1.00 45.80 C
ANISOU 1323 CB VAL A 178 6686 4088 6628 -426 -22 98 C
ATOM 1324 CG1 VAL A 178 10.309 175.910 166.381 1.00 46.32 C
ANISOU 1324 CG1 VAL A 178 6628 4199 6771 -478 -14 115 C
ATOM 1325 CG2 VAL A 178 12.021 174.594 165.109 1.00 45.90 C
ANISOU 1325 CG2 VAL A 178 6752 4066 6622 -476 -72 82 C
ATOM 1326 N TYR A 179 12.428 177.027 168.988 1.00 45.24 N
ANISOU 1326 N TYR A 179 6626 4050 6514 -267 56 114 N
ATOM 1327 CA TYR A 179 12.002 177.887 170.092 1.00 45.06 C
ANISOU 1327 CA TYR A 179 6588 4041 6492 -222 109 128 C
ATOM 1328 C TYR A 179 12.988 178.995 170.441 1.00 43.78 C
ANISOU 1328 C TYR A 179 6453 3897 6284 -147 70 115 C
ATOM 1329 O TYR A 179 12.602 180.155 170.595 1.00 43.12 O
ANISOU 1329 O TYR A 179 6326 3841 6215 -120 74 117 O
ATOM 1330 CB TYR A 179 11.703 177.065 171.354 1.00 45.85 C
ANISOU 1330 CB TYR A 179 6768 4092 6562 -220 199 150 C
ATOM 1331 CG TYR A 179 10.562 176.074 171.258 1.00 47.57 C
ANISOU 1331 CG TYR A 179 6962 4288 6823 -308 255 168 C
ATOM 1332 CD1 TYR A 179 9.290 176.480 170.870 1.00 48.58 C
ANISOU 1332 CD1 TYR A 179 6965 4460 7032 -359 280 185 C
ATOM 1333 CD2 TYR A 179 10.720 174.763 171.687 1.00 48.97 C
ANISOU 1333 CD2 TYR A 179 7246 4402 6958 -338 288 174 C
ATOM 1334 CE1 TYR A 179 8.228 175.582 170.827 1.00 49.64 C
ANISOU 1334 CE1 TYR A 179 7066 4584 7212 -455 328 205 C
ATOM 1335 CE2 TYR A 179 9.662 173.865 171.674 1.00 50.04 C
ANISOU 1335 CE2 TYR A 179 7372 4512 7128 -433 345 192 C
ATOM 1336 CZ TYR A 179 8.421 174.270 171.220 1.00 50.94 C
ANISOU 1336 CZ TYR A 179 7347 4679 7329 -500 362 208 C
ATOM 1337 OH TYR A 179 7.391 173.356 171.182 1.00 52.73 O
ANISOU 1337 OH TYR A 179 7554 4888 7593 -611 411 229 O
ATOM 1338 N PHE A 180 14.248 178.632 170.610 1.00 43.43 N
ANISOU 1338 N PHE A 180 6484 3837 6181 -113 35 105 N
ATOM 1339 CA PHE A 180 15.258 179.587 171.017 1.00 43.70 C
ANISOU 1339 CA PHE A 180 6546 3891 6167 -57 -8 95 C
ATOM 1340 C PHE A 180 15.725 180.438 169.856 1.00 42.99 C
ANISOU 1340 C PHE A 180 6393 3845 6096 -66 -81 75 C
ATOM 1341 O PHE A 180 15.529 181.645 169.901 1.00 43.14 O
ANISOU 1341 O PHE A 180 6384 3886 6122 -55 -93 71 O
ATOM 1342 CB PHE A 180 16.422 178.875 171.732 1.00 44.11 C
ANISOU 1342 CB PHE A 180 6690 3918 6151 -14 -20 99 C
ATOM 1343 CG PHE A 180 17.375 179.747 172.519 1.00 45.10 C
ANISOU 1343 CG PHE A 180 6858 4058 6219 35 -59 97 C
ATOM 1344 CD1 PHE A 180 18.410 180.415 171.890 1.00 46.19 C
ANISOU 1344 CD1 PHE A 180 6961 4243 6347 42 -136 83 C
ATOM 1345 CD2 PHE A 180 17.277 179.842 173.893 1.00 45.92 C
ANISOU 1345 CD2 PHE A 180 7045 4128 6275 65 -18 112 C
ATOM 1346 CE1 PHE A 180 19.308 181.183 172.622 1.00 46.97 C
ANISOU 1346 CE1 PHE A 180 7099 4357 6391 70 -181 83 C
ATOM 1347 CE2 PHE A 180 18.168 180.617 174.618 1.00 46.72 C
ANISOU 1347 CE2 PHE A 180 7198 4238 6316 99 -65 110 C
ATOM 1348 CZ PHE A 180 19.175 181.285 173.979 1.00 46.60 C
ANISOU 1348 CZ PHE A 180 7140 4273 6294 97 -150 96 C
ATOM 1349 N ASN A 181 16.328 179.834 168.823 1.00 42.11 N
ANISOU 1349 N ASN A 181 6270 3740 5989 -84 -123 63 N
ATOM 1350 CA ASN A 181 16.851 180.607 167.713 1.00 41.99 C
ANISOU 1350 CA ASN A 181 6208 3763 5984 -94 -185 44 C
ATOM 1351 C ASN A 181 15.771 181.309 166.914 1.00 42.28 C
ANISOU 1351 C ASN A 181 6176 3815 6074 -131 -195 40 C
ATOM 1352 O ASN A 181 15.791 182.535 166.852 1.00 42.75 O
ANISOU 1352 O ASN A 181 6214 3897 6131 -117 -220 34 O
ATOM 1353 CB ASN A 181 17.762 179.797 166.826 1.00 42.56 C
ANISOU 1353 CB ASN A 181 6294 3834 6041 -95 -214 35 C
ATOM 1354 CG ASN A 181 18.630 180.697 166.007 1.00 44.82 C
ANISOU 1354 CG ASN A 181 6549 4163 6320 -91 -268 19 C
ATOM 1355 OD1 ASN A 181 18.300 181.035 164.872 1.00 46.38 O
ANISOU 1355 OD1 ASN A 181 6711 4368 6543 -126 -293 7 O
ATOM 1356 ND2 ASN A 181 19.736 181.149 166.581 1.00 44.58 N
ANISOU 1356 ND2 ASN A 181 6530 4159 6249 -56 -289 21 N
ATOM 1357 N PHE A 182 14.797 180.573 166.368 1.00 41.93 N
ANISOU 1357 N PHE A 182 6099 3756 6074 -176 -177 47 N
ATOM 1358 CA PHE A 182 13.739 181.206 165.591 1.00 42.00 C
ANISOU 1358 CA PHE A 182 6033 3789 6137 -207 -199 48 C
ATOM 1359 C PHE A 182 12.776 182.077 166.402 1.00 40.87 C
ANISOU 1359 C PHE A 182 5845 3661 6023 -182 -158 65 C
ATOM 1360 O PHE A 182 12.781 183.274 166.211 1.00 40.69 O
ANISOU 1360 O PHE A 182 5801 3659 6001 -154 -182 61 O
ATOM 1361 CB PHE A 182 12.956 180.189 164.760 1.00 42.72 C
ANISOU 1361 CB PHE A 182 6100 3866 6267 -276 -205 52 C
ATOM 1362 CG PHE A 182 11.949 180.826 163.829 1.00 44.38 C
ANISOU 1362 CG PHE A 182 6228 4105 6531 -310 -249 54 C
ATOM 1363 CD1 PHE A 182 12.234 182.016 163.185 1.00 45.62 C
ANISOU 1363 CD1 PHE A 182 6368 4284 6679 -285 -303 40 C
ATOM 1364 CD2 PHE A 182 10.755 180.195 163.538 1.00 45.81 C
ANISOU 1364 CD2 PHE A 182 6349 4291 6767 -372 -242 71 C
ATOM 1365 CE1 PHE A 182 11.323 182.589 162.314 1.00 46.67 C
ANISOU 1365 CE1 PHE A 182 6435 4441 6856 -307 -351 44 C
ATOM 1366 CE2 PHE A 182 9.844 180.770 162.665 1.00 46.91 C
ANISOU 1366 CE2 PHE A 182 6404 4464 6955 -399 -295 77 C
ATOM 1367 CZ PHE A 182 10.140 181.959 162.050 1.00 46.79 C
ANISOU 1367 CZ PHE A 182 6381 4468 6929 -360 -351 63 C
ATOM 1368 N PHE A 183 11.943 181.495 167.267 1.00 40.07 N
ANISOU 1368 N PHE A 183 5736 3546 5942 -191 -89 87 N
ATOM 1369 CA PHE A 183 10.908 182.247 167.973 1.00 39.57 C
ANISOU 1369 CA PHE A 183 5626 3500 5911 -159 -31 109 C
ATOM 1370 C PHE A 183 11.450 183.390 168.845 1.00 39.88 C
ANISOU 1370 C PHE A 183 5725 3531 5896 -85 -16 105 C
ATOM 1371 O PHE A 183 11.069 184.550 168.645 1.00 39.50 O
ANISOU 1371 O PHE A 183 5647 3502 5859 -49 -27 106 O
ATOM 1372 CB PHE A 183 9.977 181.305 168.783 1.00 38.56 C
ANISOU 1372 CB PHE A 183 5483 3356 5812 -188 57 136 C
ATOM 1373 CG PHE A 183 9.082 180.373 167.982 1.00 38.13 C
ANISOU 1373 CG PHE A 183 5354 3313 5820 -276 46 146 C
ATOM 1374 CD1 PHE A 183 8.922 180.534 166.618 1.00 38.57 C
ANISOU 1374 CD1 PHE A 183 5350 3397 5910 -316 -40 135 C
ATOM 1375 CD2 PHE A 183 8.376 179.363 168.601 1.00 38.25 C
ANISOU 1375 CD2 PHE A 183 5369 3309 5856 -326 120 169 C
ATOM 1376 CE1 PHE A 183 8.102 179.680 165.890 1.00 38.71 C
ANISOU 1376 CE1 PHE A 183 5308 3421 5978 -408 -62 145 C
ATOM 1377 CE2 PHE A 183 7.553 178.516 167.865 1.00 38.54 C
ANISOU 1377 CE2 PHE A 183 5341 3356 5947 -424 103 180 C
ATOM 1378 CZ PHE A 183 7.424 178.681 166.519 1.00 38.14 C
ANISOU 1378 CZ PHE A 183 5231 3332 5927 -465 8 168 C
ATOM 1379 N ALA A 184 12.357 183.077 169.774 1.00 40.28 N
ANISOU 1379 N ALA A 184 5872 3550 5883 -62 3 101 N
ATOM 1380 CA ALA A 184 12.865 184.089 170.688 1.00 41.05 C
ANISOU 1380 CA ALA A 184 6044 3633 5919 -5 12 98 C
ATOM 1381 C ALA A 184 13.898 185.062 170.100 1.00 42.25 C
ANISOU 1381 C ALA A 184 6220 3801 6034 2 -70 75 C
ATOM 1382 O ALA A 184 13.760 186.268 170.278 1.00 42.47 O
ANISOU 1382 O ALA A 184 6269 3825 6041 34 -71 73 O
ATOM 1383 CB ALA A 184 13.421 183.427 171.937 1.00 41.00 C
ANISOU 1383 CB ALA A 184 6136 3588 5854 13 51 105 C
ATOM 1384 N CYS A 185 14.920 184.560 169.398 1.00 42.87 N
ANISOU 1384 N CYS A 185 6299 3891 6099 -27 -131 59 N
ATOM 1385 CA CYS A 185 16.028 185.389 168.932 1.00 43.65 C
ANISOU 1385 CA CYS A 185 6416 4009 6162 -31 -201 39 C
ATOM 1386 C CYS A 185 15.908 185.942 167.511 1.00 44.25 C
ANISOU 1386 C CYS A 185 6437 4108 6268 -58 -251 25 C
ATOM 1387 O CYS A 185 16.713 186.792 167.136 1.00 44.43 O
ANISOU 1387 O CYS A 185 6481 4143 6259 -66 -298 11 O
ATOM 1388 CB CYS A 185 17.333 184.628 169.109 1.00 44.65 C
ANISOU 1388 CB CYS A 185 6574 4143 6249 -36 -234 34 C
ATOM 1389 SG CYS A 185 17.653 184.112 170.820 1.00 49.43 S
ANISOU 1389 SG CYS A 185 7265 4715 6800 1 -195 51 S
ATOM 1390 N VAL A 186 14.941 185.473 166.717 1.00 44.38 N
ANISOU 1390 N VAL A 186 6389 4130 6343 -79 -245 30 N
ATOM 1391 CA VAL A 186 14.762 185.974 165.355 1.00 44.90 C
ANISOU 1391 CA VAL A 186 6414 4212 6432 -103 -298 18 C
ATOM 1392 C VAL A 186 13.373 186.613 165.164 1.00 45.42 C
ANISOU 1392 C VAL A 186 6425 4285 6546 -84 -284 32 C
ATOM 1393 O VAL A 186 13.266 187.782 164.796 1.00 45.47 O
ANISOU 1393 O VAL A 186 6442 4295 6541 -60 -310 27 O
ATOM 1394 CB VAL A 186 15.065 184.879 164.300 1.00 45.60 C
ANISOU 1394 CB VAL A 186 6483 4303 6539 -149 -327 9 C
ATOM 1395 CG1 VAL A 186 14.624 185.310 162.894 1.00 45.83 C
ANISOU 1395 CG1 VAL A 186 6477 4341 6595 -177 -379 0 C
ATOM 1396 CG2 VAL A 186 16.542 184.499 164.320 1.00 46.37 C
ANISOU 1396 CG2 VAL A 186 6626 4404 6589 -148 -343 -4 C
ATOM 1397 N LEU A 187 12.316 185.850 165.437 1.00 45.59 N
ANISOU 1397 N LEU A 187 6390 4312 6621 -93 -242 52 N
ATOM 1398 CA LEU A 187 10.954 186.297 165.266 1.00 46.04 C
ANISOU 1398 CA LEU A 187 6367 4390 6735 -76 -228 73 C
ATOM 1399 C LEU A 187 10.602 187.456 166.167 1.00 46.33 C
ANISOU 1399 C LEU A 187 6429 4421 6753 0 -178 85 C
ATOM 1400 O LEU A 187 10.152 188.469 165.640 1.00 47.10 O
ANISOU 1400 O LEU A 187 6508 4528 6858 36 -206 87 O
ATOM 1401 CB LEU A 187 9.969 185.140 165.413 1.00 46.41 C
ANISOU 1401 CB LEU A 187 6340 4450 6845 -120 -192 94 C
ATOM 1402 CG LEU A 187 8.526 185.439 165.026 1.00 48.29 C
ANISOU 1402 CG LEU A 187 6461 4728 7160 -119 -195 120 C
ATOM 1403 CD1 LEU A 187 8.432 185.990 163.606 1.00 49.15 C
ANISOU 1403 CD1 LEU A 187 6545 4854 7276 -117 -289 109 C
ATOM 1404 CD2 LEU A 187 7.659 184.198 165.183 1.00 48.99 C
ANISOU 1404 CD2 LEU A 187 6479 4830 7306 -196 -175 138 C
ATOM 1405 N VAL A 188 10.863 187.371 167.491 1.00 45.48 N
ANISOU 1405 N VAL A 188 6384 4288 6609 29 -109 92 N
ATOM 1406 CA VAL A 188 10.551 188.496 168.380 1.00 45.23 C
ANISOU 1406 CA VAL A 188 6403 4238 6546 105 -56 103 C
ATOM 1407 C VAL A 188 11.294 189.789 167.968 1.00 45.78 C
ANISOU 1407 C VAL A 188 6551 4289 6553 128 -115 82 C
ATOM 1408 O VAL A 188 10.617 190.795 167.746 1.00 46.00 O
ANISOU 1408 O VAL A 188 6574 4317 6589 183 -108 91 O
ATOM 1409 CB VAL A 188 10.712 188.157 169.860 1.00 45.05 C
ANISOU 1409 CB VAL A 188 6452 4181 6482 129 26 114 C
ATOM 1410 CG1 VAL A 188 10.589 189.403 170.721 1.00 45.14 C
ANISOU 1410 CG1 VAL A 188 6553 4159 6439 206 73 120 C
ATOM 1411 CG2 VAL A 188 9.661 187.146 170.258 1.00 45.42 C
ANISOU 1411 CG2 VAL A 188 6418 4244 6596 114 102 142 C
ATOM 1412 N PRO A 189 12.628 189.786 167.755 1.00 45.63 N
ANISOU 1412 N PRO A 189 6598 4261 6481 85 -175 56 N
ATOM 1413 CA PRO A 189 13.284 191.016 167.284 1.00 45.30 C
ANISOU 1413 CA PRO A 189 6626 4203 6384 89 -228 38 C
ATOM 1414 C PRO A 189 12.759 191.525 165.934 1.00 44.92 C
ANISOU 1414 C PRO A 189 6524 4171 6371 89 -278 35 C
ATOM 1415 O PRO A 189 12.645 192.741 165.779 1.00 45.61 O
ANISOU 1415 O PRO A 189 6671 4237 6423 125 -291 32 O
ATOM 1416 CB PRO A 189 14.763 190.631 167.212 1.00 46.11 C
ANISOU 1416 CB PRO A 189 6770 4309 6440 30 -278 17 C
ATOM 1417 CG PRO A 189 14.900 189.470 168.115 1.00 46.84 C
ANISOU 1417 CG PRO A 189 6851 4404 6541 23 -240 26 C
ATOM 1418 CD PRO A 189 13.615 188.713 167.988 1.00 45.25 C
ANISOU 1418 CD PRO A 189 6565 4215 6415 36 -190 46 C
ATOM 1419 N LEU A 190 12.422 190.643 164.977 1.00 43.73 N
ANISOU 1419 N LEU A 190 6282 4053 6282 48 -309 35 N
ATOM 1420 CA LEU A 190 11.893 191.113 163.694 1.00 43.71 C
ANISOU 1420 CA LEU A 190 6239 4062 6305 48 -366 34 C
ATOM 1421 C LEU A 190 10.515 191.769 163.903 1.00 43.92 C
ANISOU 1421 C LEU A 190 6218 4098 6372 125 -334 62 C
ATOM 1422 O LEU A 190 10.232 192.811 163.314 1.00 43.76 O
ANISOU 1422 O LEU A 190 6225 4067 6335 167 -367 62 O
ATOM 1423 CB LEU A 190 11.829 189.976 162.669 1.00 43.92 C
ANISOU 1423 CB LEU A 190 6195 4113 6379 -16 -409 29 C
ATOM 1424 CG LEU A 190 13.172 189.550 162.078 1.00 45.31 C
ANISOU 1424 CG LEU A 190 6422 4280 6513 -75 -448 3 C
ATOM 1425 CD1 LEU A 190 13.054 188.262 161.297 1.00 45.92 C
ANISOU 1425 CD1 LEU A 190 6452 4368 6627 -131 -469 0 C
ATOM 1426 CD2 LEU A 190 13.736 190.614 161.203 1.00 45.86 C
ANISOU 1426 CD2 LEU A 190 6547 4337 6540 -80 -501 -14 C
ATOM 1427 N LEU A 191 9.684 191.204 164.795 1.00 44.10 N
ANISOU 1427 N LEU A 191 6175 4137 6442 152 -261 88 N
ATOM 1428 CA LEU A 191 8.380 191.789 165.107 1.00 44.72 C
ANISOU 1428 CA LEU A 191 6192 4234 6565 236 -212 121 C
ATOM 1429 C LEU A 191 8.562 193.153 165.785 1.00 46.22 C
ANISOU 1429 C LEU A 191 6501 4378 6683 321 -176 120 C
ATOM 1430 O LEU A 191 7.846 194.093 165.450 1.00 46.37 O
ANISOU 1430 O LEU A 191 6512 4398 6709 396 -182 134 O
ATOM 1431 CB LEU A 191 7.555 190.852 165.998 1.00 44.31 C
ANISOU 1431 CB LEU A 191 6056 4208 6571 238 -124 149 C
ATOM 1432 CG LEU A 191 7.161 189.515 165.385 1.00 45.35 C
ANISOU 1432 CG LEU A 191 6084 4377 6771 148 -149 155 C
ATOM 1433 CD1 LEU A 191 6.395 188.661 166.370 1.00 45.48 C
ANISOU 1433 CD1 LEU A 191 6035 4411 6836 147 -48 185 C
ATOM 1434 CD2 LEU A 191 6.390 189.694 164.094 1.00 46.23 C
ANISOU 1434 CD2 LEU A 191 6098 4530 6940 124 -238 161 C
ATOM 1435 N LEU A 192 9.556 193.273 166.696 1.00 46.93 N
ANISOU 1435 N LEU A 192 6711 4423 6697 308 -146 102 N
ATOM 1436 CA LEU A 192 9.901 194.526 167.357 1.00 47.82 C
ANISOU 1436 CA LEU A 192 6969 4478 6722 366 -121 96 C
ATOM 1437 C LEU A 192 10.332 195.547 166.325 1.00 48.81 C
ANISOU 1437 C LEU A 192 7158 4583 6804 360 -200 77 C
ATOM 1438 O LEU A 192 9.890 196.689 166.394 1.00 49.12 O
ANISOU 1438 O LEU A 192 7269 4587 6808 440 -182 85 O
ATOM 1439 CB LEU A 192 11.041 194.317 168.347 1.00 48.14 C
ANISOU 1439 CB LEU A 192 7120 4483 6689 319 -110 77 C
ATOM 1440 CG LEU A 192 10.709 193.553 169.597 1.00 50.29 C
ANISOU 1440 CG LEU A 192 7390 4750 6968 336 -25 94 C
ATOM 1441 CD1 LEU A 192 11.936 193.420 170.458 1.00 51.22 C
ANISOU 1441 CD1 LEU A 192 7629 4832 7002 290 -42 74 C
ATOM 1442 CD2 LEU A 192 9.631 194.254 170.400 1.00 51.20 C
ANISOU 1442 CD2 LEU A 192 7538 4839 7077 443 74 121 C
ATOM 1443 N MET A 193 11.151 195.133 165.340 1.00 49.23 N
ANISOU 1443 N MET A 193 7193 4653 6858 271 -281 53 N
ATOM 1444 CA MET A 193 11.602 195.997 164.253 1.00 50.37 C
ANISOU 1444 CA MET A 193 7399 4778 6962 253 -353 35 C
ATOM 1445 C MET A 193 10.416 196.509 163.467 1.00 51.32 C
ANISOU 1445 C MET A 193 7463 4910 7125 327 -370 56 C
ATOM 1446 O MET A 193 10.345 197.704 163.187 1.00 51.86 O
ANISOU 1446 O MET A 193 7627 4936 7140 378 -386 54 O
ATOM 1447 CB MET A 193 12.551 195.252 163.307 1.00 51.19 C
ANISOU 1447 CB MET A 193 7471 4906 7074 151 -419 11 C
ATOM 1448 CG MET A 193 13.963 195.245 163.779 1.00 54.26 C
ANISOU 1448 CG MET A 193 7938 5279 7398 85 -427 -10 C
ATOM 1449 SD MET A 193 14.925 193.830 163.217 1.00 60.80 S
ANISOU 1449 SD MET A 193 8692 6151 8257 -7 -460 -25 S
ATOM 1450 CE MET A 193 14.738 194.002 161.481 1.00 57.92 C
ANISOU 1450 CE MET A 193 8302 5792 7913 -30 -523 -34 C
ATOM 1451 N LEU A 194 9.448 195.626 163.168 1.00 51.23 N
ANISOU 1451 N LEU A 194 7302 4956 7209 335 -369 78 N
ATOM 1452 CA LEU A 194 8.252 196.018 162.434 1.00 51.77 C
ANISOU 1452 CA LEU A 194 7290 5050 7329 405 -396 104 C
ATOM 1453 C LEU A 194 7.468 197.096 163.180 1.00 52.31 C
ANISOU 1453 C LEU A 194 7403 5094 7378 537 -327 130 C
ATOM 1454 O LEU A 194 7.067 198.091 162.577 1.00 52.13 O
ANISOU 1454 O LEU A 194 7418 5053 7334 609 -361 139 O
ATOM 1455 CB LEU A 194 7.374 194.797 162.162 1.00 51.84 C
ANISOU 1455 CB LEU A 194 7125 5129 7443 373 -402 126 C
ATOM 1456 CG LEU A 194 6.099 195.068 161.386 1.00 52.80 C
ANISOU 1456 CG LEU A 194 7133 5296 7632 438 -440 160 C
ATOM 1457 CD1 LEU A 194 6.401 195.672 160.017 1.00 53.05 C
ANISOU 1457 CD1 LEU A 194 7215 5310 7630 423 -549 144 C
ATOM 1458 CD2 LEU A 194 5.300 193.803 161.231 1.00 53.35 C
ANISOU 1458 CD2 LEU A 194 7030 5435 7803 390 -436 185 C
ATOM 1459 N GLY A 195 7.335 196.915 164.493 1.00 52.75 N
ANISOU 1459 N GLY A 195 7472 5142 7431 570 -230 142 N
ATOM 1460 CA GLY A 195 6.668 197.865 165.372 1.00 53.52 C
ANISOU 1460 CA GLY A 195 7632 5205 7497 698 -142 167 C
ATOM 1461 C GLY A 195 7.362 199.209 165.372 1.00 54.25 C
ANISOU 1461 C GLY A 195 7927 5213 7475 729 -160 145 C
ATOM 1462 O GLY A 195 6.702 200.247 165.290 1.00 54.48 O
ANISOU 1462 O GLY A 195 8006 5214 7480 845 -142 164 O
ATOM 1463 N VAL A 196 8.701 199.199 165.420 1.00 54.50 N
ANISOU 1463 N VAL A 196 8072 5203 7431 625 -200 107 N
ATOM 1464 CA VAL A 196 9.485 200.428 165.379 1.00 55.20 C
ANISOU 1464 CA VAL A 196 8357 5212 7406 622 -227 84 C
ATOM 1465 C VAL A 196 9.290 201.134 164.048 1.00 56.04 C
ANISOU 1465 C VAL A 196 8476 5310 7507 642 -302 82 C
ATOM 1466 O VAL A 196 9.026 202.333 164.037 1.00 56.25 O
ANISOU 1466 O VAL A 196 8628 5276 7470 729 -290 89 O
ATOM 1467 CB VAL A 196 10.976 200.181 165.675 1.00 55.87 C
ANISOU 1467 CB VAL A 196 8526 5275 7427 491 -263 48 C
ATOM 1468 CG1 VAL A 196 11.787 201.457 165.493 1.00 56.28 C
ANISOU 1468 CG1 VAL A 196 8773 5248 7364 465 -299 26 C
ATOM 1469 CG2 VAL A 196 11.164 199.631 167.083 1.00 56.44 C
ANISOU 1469 CG2 VAL A 196 8615 5342 7487 483 -195 52 C
ATOM 1470 N TYR A 197 9.355 200.399 162.931 1.00 56.56 N
ANISOU 1470 N TYR A 197 8426 5432 7634 571 -377 75 N
ATOM 1471 CA TYR A 197 9.163 201.015 161.621 1.00 57.71 C
ANISOU 1471 CA TYR A 197 8592 5566 7768 588 -454 74 C
ATOM 1472 C TYR A 197 7.785 201.613 161.472 1.00 58.91 C
ANISOU 1472 C TYR A 197 8699 5727 7956 738 -438 113 C
ATOM 1473 O TYR A 197 7.673 202.736 160.991 1.00 58.98 O
ANISOU 1473 O TYR A 197 8829 5680 7901 803 -463 115 O
ATOM 1474 CB TYR A 197 9.516 200.066 160.484 1.00 57.78 C
ANISOU 1474 CB TYR A 197 8501 5625 7828 484 -534 59 C
ATOM 1475 CG TYR A 197 11.011 200.027 160.275 1.00 58.84 C
ANISOU 1475 CG TYR A 197 8733 5728 7894 361 -561 21 C
ATOM 1476 CD1 TYR A 197 11.717 201.176 159.939 1.00 59.80 C
ANISOU 1476 CD1 TYR A 197 9024 5780 7916 343 -583 3 C
ATOM 1477 CD2 TYR A 197 11.731 198.865 160.497 1.00 59.86 C
ANISOU 1477 CD2 TYR A 197 8790 5897 8055 264 -557 6 C
ATOM 1478 CE1 TYR A 197 13.101 201.157 159.794 1.00 60.64 C
ANISOU 1478 CE1 TYR A 197 9205 5870 7967 222 -601 -28 C
ATOM 1479 CE2 TYR A 197 13.115 198.836 160.361 1.00 60.80 C
ANISOU 1479 CE2 TYR A 197 8981 6000 8118 161 -575 -23 C
ATOM 1480 CZ TYR A 197 13.797 199.980 160.001 1.00 61.41 C
ANISOU 1480 CZ TYR A 197 9207 6020 8107 136 -598 -39 C
ATOM 1481 OH TYR A 197 15.165 199.915 159.877 1.00 62.30 O
ANISOU 1481 OH TYR A 197 9368 6130 8173 25 -613 -63 O
ATOM 1482 N LEU A 198 6.753 200.938 161.988 1.00 59.79 N
ANISOU 1482 N LEU A 198 8652 5905 8162 798 -386 147 N
ATOM 1483 CA LEU A 198 5.399 201.487 161.957 1.00 61.20 C
ANISOU 1483 CA LEU A 198 8761 6107 8385 952 -360 191 C
ATOM 1484 C LEU A 198 5.318 202.805 162.743 1.00 62.72 C
ANISOU 1484 C LEU A 198 9132 6215 8485 1076 -283 199 C
ATOM 1485 O LEU A 198 4.728 203.776 162.265 1.00 62.92 O
ANISOU 1485 O LEU A 198 9209 6214 8486 1196 -299 220 O
ATOM 1486 CB LEU A 198 4.400 200.474 162.513 1.00 61.37 C
ANISOU 1486 CB LEU A 198 8573 6220 8526 974 -304 227 C
ATOM 1487 CG LEU A 198 4.205 199.248 161.651 1.00 62.92 C
ANISOU 1487 CG LEU A 198 8595 6495 8814 868 -386 227 C
ATOM 1488 CD1 LEU A 198 3.355 198.220 162.365 1.00 63.80 C
ANISOU 1488 CD1 LEU A 198 8524 6687 9032 864 -318 259 C
ATOM 1489 CD2 LEU A 198 3.630 199.612 160.290 1.00 63.32 C
ANISOU 1489 CD2 LEU A 198 8596 6572 8890 904 -495 242 C
ATOM 1490 N ARG A 199 5.959 202.854 163.915 1.00 63.42 N
ANISOU 1490 N ARG A 199 9333 6253 8512 1049 -205 183 N
ATOM 1491 CA ARG A 199 5.980 204.062 164.727 1.00 64.49 C
ANISOU 1491 CA ARG A 199 9668 6293 8542 1152 -131 186 C
ATOM 1492 C ARG A 199 6.751 205.198 164.050 1.00 65.53 C
ANISOU 1492 C ARG A 199 10010 6332 8556 1131 -197 158 C
ATOM 1493 O ARG A 199 6.350 206.353 164.173 1.00 65.72 O
ANISOU 1493 O ARG A 199 10176 6285 8511 1257 -163 173 O
ATOM 1494 CB ARG A 199 6.510 203.759 166.129 1.00 65.76 C
ANISOU 1494 CB ARG A 199 9906 6420 8660 1113 -44 174 C
ATOM 1495 CG ARG A 199 5.508 202.960 166.956 1.00 68.96 C
ANISOU 1495 CG ARG A 199 10149 6892 9160 1184 56 212 C
ATOM 1496 CD ARG A 199 6.078 202.422 168.257 1.00 72.94 C
ANISOU 1496 CD ARG A 199 10720 7368 9626 1127 131 199 C
ATOM 1497 NE ARG A 199 6.264 203.456 169.276 1.00 76.95 N
ANISOU 1497 NE ARG A 199 11464 7766 10008 1200 205 194 N
ATOM 1498 CZ ARG A 199 7.180 203.401 170.242 1.00 79.85 C
ANISOU 1498 CZ ARG A 199 11986 8071 10284 1118 218 166 C
ATOM 1499 NH1 ARG A 199 8.012 202.367 170.322 1.00 79.59 N
ANISOU 1499 NH1 ARG A 199 11885 8078 10276 973 164 142 N
ATOM 1500 NH2 ARG A 199 7.285 204.389 171.122 1.00 80.05 N
ANISOU 1500 NH2 ARG A 199 12241 7987 10186 1184 279 163 N
ATOM 1501 N ILE A 200 7.826 204.875 163.308 1.00 66.10 N
ANISOU 1501 N ILE A 200 10104 6404 8606 976 -286 121 N
ATOM 1502 CA ILE A 200 8.598 205.874 162.568 1.00 67.13 C
ANISOU 1502 CA ILE A 200 10422 6454 8632 931 -350 95 C
ATOM 1503 C ILE A 200 7.705 206.524 161.502 1.00 68.00 C
ANISOU 1503 C ILE A 200 10523 6561 8755 1047 -397 119 C
ATOM 1504 O ILE A 200 7.614 207.748 161.444 1.00 68.34 O
ANISOU 1504 O ILE A 200 10752 6513 8702 1130 -388 123 O
ATOM 1505 CB ILE A 200 9.865 205.241 161.908 1.00 67.81 C
ANISOU 1505 CB ILE A 200 10491 6561 8713 743 -428 56 C
ATOM 1506 CG1 ILE A 200 10.935 204.886 162.932 1.00 68.71 C
ANISOU 1506 CG1 ILE A 200 10656 6663 8787 631 -397 31 C
ATOM 1507 CG2 ILE A 200 10.445 206.151 160.809 1.00 68.41 C
ANISOU 1507 CG2 ILE A 200 10719 6571 8703 700 -498 36 C
ATOM 1508 CD1 ILE A 200 12.060 204.049 162.343 1.00 69.91 C
ANISOU 1508 CD1 ILE A 200 10738 6864 8962 468 -461 2 C
ATOM 1509 N PHE A 201 7.063 205.707 160.659 1.00 68.20 N
ANISOU 1509 N PHE A 201 10345 6678 8890 1049 -454 137 N
ATOM 1510 CA PHE A 201 6.250 206.222 159.578 1.00 69.21 C
ANISOU 1510 CA PHE A 201 10452 6812 9032 1147 -519 161 C
ATOM 1511 C PHE A 201 5.018 206.929 160.066 1.00 70.44 C
ANISOU 1511 C PHE A 201 10599 6963 9200 1352 -457 208 C
ATOM 1512 O PHE A 201 4.619 207.914 159.455 1.00 70.38 O
ANISOU 1512 O PHE A 201 10695 6905 9140 1461 -491 224 O
ATOM 1513 CB PHE A 201 5.922 205.126 158.569 1.00 69.02 C
ANISOU 1513 CB PHE A 201 10219 6888 9118 1080 -605 167 C
ATOM 1514 CG PHE A 201 7.160 204.604 157.884 1.00 69.32 C
ANISOU 1514 CG PHE A 201 10302 6914 9124 900 -665 122 C
ATOM 1515 CD1 PHE A 201 8.105 205.473 157.368 1.00 69.91 C
ANISOU 1515 CD1 PHE A 201 10581 6899 9084 845 -697 92 C
ATOM 1516 CD2 PHE A 201 7.369 203.247 157.741 1.00 69.83 C
ANISOU 1516 CD2 PHE A 201 10206 7054 9270 788 -684 112 C
ATOM 1517 CE1 PHE A 201 9.240 204.991 156.741 1.00 70.54 C
ANISOU 1517 CE1 PHE A 201 10688 6976 9140 685 -740 55 C
ATOM 1518 CE2 PHE A 201 8.508 202.771 157.123 1.00 70.47 C
ANISOU 1518 CE2 PHE A 201 10330 7126 9322 639 -727 74 C
ATOM 1519 CZ PHE A 201 9.436 203.643 156.627 1.00 70.31 C
ANISOU 1519 CZ PHE A 201 10495 7026 9195 590 -753 47 C
ATOM 1520 N ALA A 202 4.432 206.469 161.181 1.00 71.60 N
ANISOU 1520 N ALA A 202 10637 7158 9411 1411 -359 233 N
ATOM 1521 CA ALA A 202 3.270 207.147 161.747 1.00 73.28 C
ANISOU 1521 CA ALA A 202 10838 7369 9638 1617 -276 281 C
ATOM 1522 C ALA A 202 3.693 208.518 162.302 1.00 74.93 C
ANISOU 1522 C ALA A 202 11342 7436 9693 1694 -217 269 C
ATOM 1523 O ALA A 202 2.966 209.494 162.117 1.00 74.92 O
ANISOU 1523 O ALA A 202 11421 7391 9652 1863 -205 299 O
ATOM 1524 CB ALA A 202 2.638 206.301 162.841 1.00 73.46 C
ANISOU 1524 CB ALA A 202 10689 7467 9754 1645 -170 308 C
ATOM 1525 N ALA A 203 4.887 208.598 162.940 1.00 76.02 N
ANISOU 1525 N ALA A 203 11649 7498 9737 1566 -190 225 N
ATOM 1526 CA ALA A 203 5.414 209.856 163.467 1.00 77.39 C
ANISOU 1526 CA ALA A 203 12125 7528 9753 1599 -145 206 C
ATOM 1527 C ALA A 203 5.671 210.829 162.324 1.00 79.02 C
ANISOU 1527 C ALA A 203 12493 7658 9871 1606 -231 195 C
ATOM 1528 O ALA A 203 5.281 211.985 162.419 1.00 79.15 O
ANISOU 1528 O ALA A 203 12700 7579 9795 1746 -194 210 O
ATOM 1529 CB ALA A 203 6.694 209.615 164.261 1.00 77.47 C
ANISOU 1529 CB ALA A 203 12248 7493 9693 1426 -132 162 C
ATOM 1530 N ALA A 204 6.266 210.354 161.225 1.00 80.17 N
ANISOU 1530 N ALA A 204 12571 7843 10045 1466 -341 170 N
ATOM 1531 CA ALA A 204 6.526 211.197 160.069 1.00 81.91 C
ANISOU 1531 CA ALA A 204 12943 7995 10186 1459 -423 159 C
ATOM 1532 C ALA A 204 5.218 211.676 159.449 1.00 84.18 C
ANISOU 1532 C ALA A 204 13180 8297 10506 1664 -441 207 C
ATOM 1533 O ALA A 204 5.098 212.852 159.119 1.00 84.48 O
ANISOU 1533 O ALA A 204 13431 8230 10436 1758 -448 212 O
ATOM 1534 CB ALA A 204 7.338 210.433 159.041 1.00 81.87 C
ANISOU 1534 CB ALA A 204 12847 8042 10219 1277 -523 128 C
ATOM 1535 N ARG A 205 4.227 210.786 159.317 1.00 85.76 N
ANISOU 1535 N ARG A 205 13104 8626 10852 1729 -451 243 N
ATOM 1536 CA ARG A 205 2.945 211.132 158.719 1.00 87.68 C
ANISOU 1536 CA ARG A 205 13251 8913 11151 1923 -478 296 C
ATOM 1537 C ARG A 205 2.240 212.201 159.535 1.00 88.48 C
ANISOU 1537 C ARG A 205 13499 8937 11182 2139 -374 330 C
ATOM 1538 O ARG A 205 1.705 213.150 158.963 1.00 88.72 O
ANISOU 1538 O ARG A 205 13630 8918 11161 2292 -406 357 O
ATOM 1539 CB ARG A 205 2.076 209.871 158.570 1.00 90.48 C
ANISOU 1539 CB ARG A 205 13268 9429 11680 1933 -493 331 C
ATOM 1540 CG ARG A 205 0.646 210.107 158.072 1.00 95.59 C
ANISOU 1540 CG ARG A 205 13773 10145 12401 2120 -540 391 C
ATOM 1541 CD ARG A 205 -0.212 208.850 158.183 1.00100.18 C
ANISOU 1541 CD ARG A 205 14017 10890 13156 2097 -562 424 C
ATOM 1542 NE ARG A 205 -0.161 208.271 159.531 1.00104.29 N
ANISOU 1542 NE ARG A 205 14436 11453 13735 2076 -432 429 N
ATOM 1543 CZ ARG A 205 -0.841 207.197 159.916 1.00107.29 C
ANISOU 1543 CZ ARG A 205 14566 11952 14246 2155 -379 479 C
ATOM 1544 NH1 ARG A 205 -1.650 206.575 159.069 1.00107.72 N
ANISOU 1544 NH1 ARG A 205 14430 12103 14395 2258 -452 531 N
ATOM 1545 NH2 ARG A 205 -0.723 206.741 161.157 1.00107.14 N
ANISOU 1545 NH2 ARG A 205 14488 11957 14265 2127 -254 480 N
ATOM 1546 N ARG A 206 2.293 212.081 160.872 1.00 88.76 N
ANISOU 1546 N ARG A 206 13560 8956 11208 2161 -249 331 N
ATOM 1547 CA ARG A 206 1.661 213.057 161.751 1.00 89.59 C
ANISOU 1547 CA ARG A 206 13820 8980 11241 2371 -135 363 C
ATOM 1548 C ARG A 206 2.351 214.417 161.718 1.00 89.99 C
ANISOU 1548 C ARG A 206 14237 8853 11102 2370 -136 332 C
ATOM 1549 O ARG A 206 1.668 215.435 161.703 1.00 90.19 O
ANISOU 1549 O ARG A 206 14416 8799 11053 2560 -105 361 O
ATOM 1550 CB ARG A 206 1.590 212.553 163.192 1.00 91.13 C
ANISOU 1550 CB ARG A 206 13965 9194 11465 2391 4 371 C
ATOM 1551 CG ARG A 206 0.612 213.378 164.010 1.00 94.59 C
ANISOU 1551 CG ARG A 206 14485 9585 11868 2646 134 420 C
ATOM 1552 CD ARG A 206 0.949 213.401 165.486 1.00 98.45 C
ANISOU 1552 CD ARG A 206 15126 9998 12283 2639 273 406 C
ATOM 1553 NE ARG A 206 -0.091 214.081 166.264 1.00101.94 N
ANISOU 1553 NE ARG A 206 15568 10432 12732 2892 418 463 N
ATOM 1554 CZ ARG A 206 -0.955 213.461 167.064 1.00104.44 C
ANISOU 1554 CZ ARG A 206 15680 10845 13158 2953 530 498 C
ATOM 1555 NH1 ARG A 206 -0.912 212.141 167.208 1.00103.82 N
ANISOU 1555 NH1 ARG A 206 15391 10870 13185 2779 508 481 N
ATOM 1556 NH2 ARG A 206 -1.867 214.158 167.730 1.00104.75 N
ANISOU 1556 NH2 ARG A 206 15731 10873 13197 3195 671 553 N
ATOM 1557 N GLN A 207 3.688 214.442 161.691 1.00 89.87 N
ANISOU 1557 N GLN A 207 14344 8786 11018 2146 -188 275 N
ATOM 1558 CA GLN A 207 4.425 215.700 161.658 1.00 90.28 C
ANISOU 1558 CA GLN A 207 14735 8675 10892 2090 -204 240 C
ATOM 1559 C GLN A 207 4.176 216.479 160.372 1.00 91.50 C
ANISOU 1559 C GLN A 207 14961 8794 11010 2171 -295 254 C
ATOM 1560 O GLN A 207 4.092 217.706 160.410 1.00 91.77 O
ANISOU 1560 O GLN A 207 15285 8685 10898 2246 -281 252 O
ATOM 1561 CB GLN A 207 5.915 215.454 161.836 1.00 90.62 C
ANISOU 1561 CB GLN A 207 14832 8704 10897 1817 -253 182 C
ATOM 1562 CG GLN A 207 6.284 214.873 163.183 1.00 92.20 C
ANISOU 1562 CG GLN A 207 15011 8917 11103 1731 -175 164 C
ATOM 1563 CD GLN A 207 7.776 214.691 163.326 1.00 94.84 C
ANISOU 1563 CD GLN A 207 15514 9183 11338 1499 -212 111 C
ATOM 1564 OE1 GLN A 207 8.587 215.304 162.618 1.00 95.76 O
ANISOU 1564 OE1 GLN A 207 15813 9216 11354 1417 -272 88 O
ATOM 1565 NE2 GLN A 207 8.174 213.844 164.259 1.00 95.21 N
ANISOU 1565 NE2 GLN A 207 15498 9268 11411 1392 -176 94 N
ATOM 1566 N LEU A 208 4.047 215.778 159.242 1.00 92.07 N
ANISOU 1566 N LEU A 208 14790 8988 11205 2156 -391 270 N
ATOM 1567 CA LEU A 208 3.767 216.426 157.967 1.00 93.30 C
ANISOU 1567 CA LEU A 208 15024 9106 11319 2238 -485 285 C
ATOM 1568 C LEU A 208 2.345 217.016 157.986 1.00 94.71 C
ANISOU 1568 C LEU A 208 15166 9296 11522 2526 -449 349 C
ATOM 1569 O LEU A 208 2.129 218.133 157.507 1.00 94.88 O
ANISOU 1569 O LEU A 208 15411 9208 11432 2659 -464 364 O
ATOM 1570 CB LEU A 208 3.928 215.415 156.830 1.00 93.60 C
ANISOU 1570 CB LEU A 208 14845 9256 11462 2107 -610 276 C
ATOM 1571 CG LEU A 208 3.957 215.995 155.428 1.00 95.62 C
ANISOU 1571 CG LEU A 208 15197 9468 11664 2144 -725 283 C
ATOM 1572 CD1 LEU A 208 5.079 215.385 154.609 1.00 96.03 C
ANISOU 1572 CD1 LEU A 208 15189 9558 11740 1919 -824 242 C
ATOM 1573 CD2 LEU A 208 2.620 215.805 154.726 1.00 96.84 C
ANISOU 1573 CD2 LEU A 208 15170 9711 11914 2365 -771 346 C
ATOM 1574 N ALA A1001 1.388 216.281 158.573 1.00 95.52 N
ANISOU 1574 N ALA A1001 12058 4423 19812 1235 -1592 134 N
ATOM 1575 CA ALA A1001 0.014 216.750 158.704 1.00 96.65 C
ANISOU 1575 CA ALA A1001 12009 4755 19957 951 -1804 428 C
ATOM 1576 C ALA A1001 -0.032 217.978 159.609 1.00 97.65 C
ANISOU 1576 C ALA A1001 11894 5617 19592 1039 -1528 776 C
ATOM 1577 O ALA A1001 -0.746 218.916 159.301 1.00 97.69 O
ANISOU 1577 O ALA A1001 11908 5938 19271 903 -1600 725 O
ATOM 1578 CB ALA A1001 -0.867 215.646 159.267 1.00 96.84 C
ANISOU 1578 CB ALA A1001 11698 4311 20785 751 -2017 924 C
ATOM 1579 N ASP A1002 0.757 217.996 160.693 1.00 98.44 N
ANISOU 1579 N ASP A1002 11804 6060 19538 1315 -1200 1056 N
ATOM 1580 CA ASP A1002 0.826 219.139 161.609 1.00 99.81 C
ANISOU 1580 CA ASP A1002 11765 6921 19238 1429 -965 1312 C
ATOM 1581 C ASP A1002 1.408 220.380 160.926 1.00100.41 C
ANISOU 1581 C ASP A1002 12082 7327 18743 1493 -849 811 C
ATOM 1582 O ASP A1002 0.974 221.490 161.219 1.00100.31 O
ANISOU 1582 O ASP A1002 11963 7755 18397 1450 -783 886 O
ATOM 1583 CB ASP A1002 1.649 218.797 162.861 1.00102.52 C
ANISOU 1583 CB ASP A1002 11887 7464 19600 1710 -756 1671 C
ATOM 1584 CG ASP A1002 1.008 217.763 163.768 1.00108.10 C
ANISOU 1584 CG ASP A1002 12289 8030 20754 1683 -784 2360 C
ATOM 1585 OD1 ASP A1002 -0.231 217.590 163.690 1.00109.14 O
ANISOU 1585 OD1 ASP A1002 12288 8031 21151 1436 -900 2629 O
ATOM 1586 OD2 ASP A1002 1.746 217.125 164.558 1.00110.29 O
ANISOU 1586 OD2 ASP A1002 12437 8321 21145 1918 -685 2669 O
ATOM 1587 N LEU A1003 2.368 220.202 160.007 1.00100.95 N
ANISOU 1587 N LEU A1003 12413 7240 18702 1635 -754 372 N
ATOM 1588 CA LEU A1003 2.941 221.327 159.266 1.00102.08 C
ANISOU 1588 CA LEU A1003 12774 7659 18351 1698 -590 -47 C
ATOM 1589 C LEU A1003 1.864 221.936 158.377 1.00103.20 C
ANISOU 1589 C LEU A1003 13109 7819 18285 1461 -792 -200 C
ATOM 1590 O LEU A1003 1.696 223.149 158.361 1.00103.30 O
ANISOU 1590 O LEU A1003 13070 8226 17955 1441 -700 -195 O
ATOM 1591 CB LEU A1003 4.121 220.876 158.386 1.00102.27 C
ANISOU 1591 CB LEU A1003 13084 7411 18365 1883 -425 -500 C
ATOM 1592 CG LEU A1003 5.468 220.668 159.061 1.00103.85 C
ANISOU 1592 CG LEU A1003 13073 7694 18691 2168 -174 -431 C
ATOM 1593 CD1 LEU A1003 6.431 219.968 158.123 1.00104.47 C
ANISOU 1593 CD1 LEU A1003 13410 7382 18904 2341 -12 -853 C
ATOM 1594 CD2 LEU A1003 6.068 221.987 159.493 1.00104.49 C
ANISOU 1594 CD2 LEU A1003 12966 8313 18422 2270 39 -423 C
ATOM 1595 N GLU A1004 1.123 221.092 157.654 1.00104.04 N
ANISOU 1595 N GLU A1004 13411 7478 18641 1282 -1105 -328 N
ATOM 1596 CA GLU A1004 0.069 221.571 156.773 1.00105.14 C
ANISOU 1596 CA GLU A1004 13730 7610 18610 1058 -1393 -470 C
ATOM 1597 C GLU A1004 -1.110 222.143 157.552 1.00105.99 C
ANISOU 1597 C GLU A1004 13453 7975 18843 885 -1503 -9 C
ATOM 1598 O GLU A1004 -1.728 223.089 157.091 1.00106.06 O
ANISOU 1598 O GLU A1004 13506 8202 18591 786 -1599 -55 O
ATOM 1599 CB GLU A1004 -0.366 220.476 155.784 1.00107.54 C
ANISOU 1599 CB GLU A1004 14349 7348 19163 919 -1770 -799 C
ATOM 1600 CG GLU A1004 -1.332 220.940 154.700 1.00111.87 C
ANISOU 1600 CG GLU A1004 15121 7877 19507 699 -2168 -993 C
ATOM 1601 CD GLU A1004 -0.888 222.070 153.786 1.00117.47 C
ANISOU 1601 CD GLU A1004 16209 8911 19515 796 -2052 -1315 C
ATOM 1602 OE1 GLU A1004 -1.766 222.636 153.096 1.00118.21 O
ANISOU 1602 OE1 GLU A1004 16488 9008 19419 635 -2421 -1427 O
ATOM 1603 OE2 GLU A1004 0.325 222.384 153.742 1.00119.47 O
ANISOU 1603 OE2 GLU A1004 16553 9398 19443 1033 -1607 -1426 O
ATOM 1604 N ASP A1005 -1.392 221.618 158.742 1.00106.51 N
ANISOU 1604 N ASP A1005 13137 8039 19294 880 -1447 462 N
ATOM 1605 CA ASP A1005 -2.474 222.108 159.586 1.00107.69 C
ANISOU 1605 CA ASP A1005 12890 8444 19585 759 -1455 941 C
ATOM 1606 C ASP A1005 -2.160 223.529 160.040 1.00108.32 C
ANISOU 1606 C ASP A1005 12871 9110 19176 904 -1166 955 C
ATOM 1607 O ASP A1005 -3.046 224.385 160.013 1.00108.61 O
ANISOU 1607 O ASP A1005 12773 9348 19144 793 -1223 1057 O
ATOM 1608 CB ASP A1005 -2.670 221.150 160.777 1.00110.06 C
ANISOU 1608 CB ASP A1005 12855 8615 20348 785 -1371 1463 C
ATOM 1609 CG ASP A1005 -3.441 221.670 161.971 1.00115.80 C
ANISOU 1609 CG ASP A1005 13149 9688 21161 765 -1208 2041 C
ATOM 1610 OD1 ASP A1005 -4.359 222.502 161.771 1.00116.86 O
ANISOU 1610 OD1 ASP A1005 13180 10096 21124 679 -1215 2050 O
ATOM 1611 OD2 ASP A1005 -3.139 221.234 163.106 1.00118.27 O
ANISOU 1611 OD2 ASP A1005 13227 9995 21718 854 -1054 2509 O
ATOM 1612 N ASN A1006 -0.911 223.787 160.447 1.00108.41 N
ANISOU 1612 N ASN A1006 12928 9358 18905 1152 -881 828 N
ATOM 1613 CA ASN A1006 -0.519 225.130 160.881 1.00108.87 C
ANISOU 1613 CA ASN A1006 12885 9918 18564 1289 -637 771 C
ATOM 1614 C ASN A1006 -0.507 226.121 159.715 1.00109.32 C
ANISOU 1614 C ASN A1006 13197 10009 18331 1229 -665 402 C
ATOM 1615 O ASN A1006 -0.843 227.287 159.898 1.00109.19 O
ANISOU 1615 O ASN A1006 13054 10296 18137 1228 -579 432 O
ATOM 1616 CB ASN A1006 0.838 225.100 161.574 1.00109.70 C
ANISOU 1616 CB ASN A1006 12938 10215 18528 1552 -401 710 C
ATOM 1617 CG ASN A1006 0.809 224.834 163.065 1.00112.27 C
ANISOU 1617 CG ASN A1006 12951 10805 18901 1687 -305 1138 C
ATOM 1618 OD1 ASN A1006 1.847 224.546 163.666 1.00113.17 O
ANISOU 1618 OD1 ASN A1006 13017 11013 18971 1897 -212 1146 O
ATOM 1619 ND2 ASN A1006 -0.350 224.939 163.713 1.00112.76 N
ANISOU 1619 ND2 ASN A1006 12788 11017 19040 1596 -314 1522 N
ATOM 1620 N TRP A1007 -0.130 225.651 158.520 1.00109.75 N
ANISOU 1620 N TRP A1007 13621 9743 18334 1198 -772 68 N
ATOM 1621 CA TRP A1007 -0.116 226.459 157.307 1.00110.58 C
ANISOU 1621 CA TRP A1007 14038 9864 18114 1160 -800 -235 C
ATOM 1622 C TRP A1007 -1.542 226.815 156.911 1.00111.39 C
ANISOU 1622 C TRP A1007 14109 9939 18274 939 -1125 -96 C
ATOM 1623 O TRP A1007 -1.810 227.956 156.548 1.00111.41 O
ANISOU 1623 O TRP A1007 14136 10146 18047 924 -1100 -117 O
ATOM 1624 CB TRP A1007 0.572 225.692 156.168 1.00110.63 C
ANISOU 1624 CB TRP A1007 14481 9534 18018 1209 -833 -615 C
ATOM 1625 CG TRP A1007 0.574 226.409 154.854 1.00111.13 C
ANISOU 1625 CG TRP A1007 14936 9624 17666 1195 -855 -891 C
ATOM 1626 CD1 TRP A1007 -0.150 226.092 153.743 1.00112.06 C
ANISOU 1626 CD1 TRP A1007 15408 9519 17650 1065 -1210 -1075 C
ATOM 1627 CD2 TRP A1007 1.351 227.560 154.513 1.00111.23 C
ANISOU 1627 CD2 TRP A1007 15029 9896 17337 1329 -513 -994 C
ATOM 1628 NE1 TRP A1007 0.141 226.966 152.725 1.00112.33 N
ANISOU 1628 NE1 TRP A1007 15780 9704 17197 1135 -1093 -1258 N
ATOM 1629 CE2 TRP A1007 1.061 227.879 153.173 1.00112.01 C
ANISOU 1629 CE2 TRP A1007 15560 9940 17060 1290 -637 -1184 C
ATOM 1630 CE3 TRP A1007 2.277 228.346 155.207 1.00111.61 C
ANISOU 1630 CE3 TRP A1007 14814 10206 17386 1475 -136 -940 C
ATOM 1631 CZ2 TRP A1007 1.641 228.965 152.526 1.00112.54 C
ANISOU 1631 CZ2 TRP A1007 15792 10202 16766 1396 -334 -1244 C
ATOM 1632 CZ3 TRP A1007 2.865 229.407 154.556 1.00112.32 C
ANISOU 1632 CZ3 TRP A1007 15036 10435 17207 1556 139 -1049 C
ATOM 1633 CH2 TRP A1007 2.551 229.703 153.230 1.00112.48 C
ANISOU 1633 CH2 TRP A1007 15480 10392 16866 1519 72 -1165 C
ATOM 1634 N GLU A1008 -2.459 225.848 156.991 1.00111.97 N
ANISOU 1634 N GLU A1008 14092 9727 18722 766 -1443 67 N
ATOM 1635 CA GLU A1008 -3.856 226.070 156.649 1.00113.13 C
ANISOU 1635 CA GLU A1008 14134 9804 19044 541 -1806 220 C
ATOM 1636 C GLU A1008 -4.475 227.018 157.648 1.00113.77 C
ANISOU 1636 C GLU A1008 13777 10242 19210 551 -1630 584 C
ATOM 1637 O GLU A1008 -5.178 227.924 157.235 1.00113.85 O
ANISOU 1637 O GLU A1008 13748 10369 19140 481 -1751 615 O
ATOM 1638 CB GLU A1008 -4.637 224.746 156.624 1.00115.73 C
ANISOU 1638 CB GLU A1008 14387 9690 19895 341 -2179 323 C
ATOM 1639 CG GLU A1008 -5.814 224.757 155.669 1.00120.68 C
ANISOU 1639 CG GLU A1008 15087 10104 20662 101 -2706 256 C
ATOM 1640 CD GLU A1008 -5.420 224.711 154.208 1.00126.49 C
ANISOU 1640 CD GLU A1008 16403 10709 20948 117 -2960 -249 C
ATOM 1641 OE1 GLU A1008 -4.619 223.822 153.840 1.00127.63 O
ANISOU 1641 OE1 GLU A1008 16890 10618 20986 213 -2908 -589 O
ATOM 1642 OE2 GLU A1008 -5.912 225.564 153.431 1.00128.16 O
ANISOU 1642 OE2 GLU A1008 16731 11059 20904 55 -3202 -291 O
ATOM 1643 N THR A1009 -4.193 226.836 158.951 1.00114.22 N
ANISOU 1643 N THR A1009 13525 10483 19391 667 -1335 849 N
ATOM 1644 CA THR A1009 -4.715 227.699 160.012 1.00115.14 C
ANISOU 1644 CA THR A1009 13251 10972 19524 729 -1108 1149 C
ATOM 1645 C THR A1009 -4.290 229.153 159.787 1.00116.14 C
ANISOU 1645 C THR A1009 13449 11401 19278 851 -922 924 C
ATOM 1646 O THR A1009 -5.092 230.067 159.964 1.00116.35 O
ANISOU 1646 O THR A1009 13252 11596 19357 826 -899 1058 O
ATOM 1647 CB THR A1009 -4.299 227.167 161.390 1.00116.17 C
ANISOU 1647 CB THR A1009 13136 11280 19724 879 -833 1435 C
ATOM 1648 OG1 THR A1009 -4.981 225.936 161.638 1.00117.04 O
ANISOU 1648 OG1 THR A1009 13098 11073 20297 734 -997 1761 O
ATOM 1649 CG2 THR A1009 -4.614 228.140 162.507 1.00116.45 C
ANISOU 1649 CG2 THR A1009 12844 11763 19638 1007 -547 1651 C
ATOM 1650 N LEU A1010 -3.049 229.362 159.352 1.00116.51 N
ANISOU 1650 N LEU A1010 13779 11469 19021 979 -781 596 N
ATOM 1651 CA LEU A1010 -2.551 230.697 159.052 1.00117.37 C
ANISOU 1651 CA LEU A1010 13948 11785 18864 1077 -595 395 C
ATOM 1652 C LEU A1010 -3.356 231.341 157.899 1.00118.10 C
ANISOU 1652 C LEU A1010 14196 11766 18910 940 -831 372 C
ATOM 1653 O LEU A1010 -3.848 232.456 158.050 1.00118.27 O
ANISOU 1653 O LEU A1010 14034 11950 18952 954 -767 456 O
ATOM 1654 CB LEU A1010 -1.049 230.617 158.712 1.00117.69 C
ANISOU 1654 CB LEU A1010 14228 11802 18686 1224 -389 90 C
ATOM 1655 CG LEU A1010 -0.409 231.839 158.068 1.00119.33 C
ANISOU 1655 CG LEU A1010 14567 12093 18681 1291 -203 -123 C
ATOM 1656 CD1 LEU A1010 -0.523 233.035 158.964 1.00120.04 C
ANISOU 1656 CD1 LEU A1010 14330 12460 18822 1365 -29 -75 C
ATOM 1657 CD2 LEU A1010 1.046 231.579 157.741 1.00119.96 C
ANISOU 1657 CD2 LEU A1010 14834 12103 18643 1427 22 -379 C
ATOM 1658 N ASN A1011 -3.506 230.642 156.772 1.00118.42 N
ANISOU 1658 N ASN A1011 14579 11531 18885 827 -1121 250 N
ATOM 1659 CA ASN A1011 -4.215 231.181 155.613 1.00119.13 C
ANISOU 1659 CA ASN A1011 14873 11542 18848 721 -1412 231 C
ATOM 1660 C ASN A1011 -5.719 231.342 155.813 1.00119.53 C
ANISOU 1660 C ASN A1011 14601 11570 19246 560 -1723 530 C
ATOM 1661 O ASN A1011 -6.300 232.323 155.353 1.00119.42 O
ANISOU 1661 O ASN A1011 14543 11632 19199 541 -1826 624 O
ATOM 1662 CB ASN A1011 -3.918 230.340 154.380 1.00120.36 C
ANISOU 1662 CB ASN A1011 15524 11436 18771 673 -1667 -38 C
ATOM 1663 CG ASN A1011 -2.484 230.456 153.954 1.00123.31 C
ANISOU 1663 CG ASN A1011 16222 11848 18782 858 -1304 -319 C
ATOM 1664 OD1 ASN A1011 -1.875 231.525 154.054 1.00124.39 O
ANISOU 1664 OD1 ASN A1011 16300 12189 18773 979 -964 -312 O
ATOM 1665 ND2 ASN A1011 -1.917 229.362 153.477 1.00123.80 N
ANISOU 1665 ND2 ASN A1011 16598 11680 18760 884 -1355 -574 N
ATOM 1666 N ASP A1012 -6.344 230.391 156.496 1.00119.87 N
ANISOU 1666 N ASP A1012 14385 11486 19675 450 -1857 718 N
ATOM 1667 CA ASP A1012 -7.769 230.443 156.758 1.00120.85 C
ANISOU 1667 CA ASP A1012 14122 11558 20237 292 -2112 1040 C
ATOM 1668 C ASP A1012 -8.099 231.606 157.660 1.00121.39 C
ANISOU 1668 C ASP A1012 13792 11935 20396 410 -1779 1255 C
ATOM 1669 O ASP A1012 -9.036 232.339 157.367 1.00121.60 O
ANISOU 1669 O ASP A1012 13618 11972 20612 349 -1950 1415 O
ATOM 1670 CB ASP A1012 -8.260 229.132 157.375 1.00123.05 C
ANISOU 1670 CB ASP A1012 14181 11600 20973 153 -2251 1236 C
ATOM 1671 CG ASP A1012 -8.112 227.931 156.457 1.00128.55 C
ANISOU 1671 CG ASP A1012 15258 11908 21676 26 -2636 969 C
ATOM 1672 OD1 ASP A1012 -7.997 228.132 155.223 1.00129.29 O
ANISOU 1672 OD1 ASP A1012 15792 11937 21394 25 -2876 648 O
ATOM 1673 OD2 ASP A1012 -8.096 226.791 156.970 1.00131.15 O
ANISOU 1673 OD2 ASP A1012 15463 11994 22376 -53 -2678 1080 O
ATOM 1674 N ASN A1013 -7.310 231.818 158.723 1.00121.68 N
ANISOU 1674 N ASN A1013 13723 12221 20291 597 -1328 1228 N
ATOM 1675 CA ASN A1013 -7.562 232.930 159.638 1.00122.49 C
ANISOU 1675 CA ASN A1013 13484 12623 20435 742 -1000 1339 C
ATOM 1676 C ASN A1013 -7.312 234.296 158.996 1.00123.19 C
ANISOU 1676 C ASN A1013 13688 12780 20339 819 -948 1160 C
ATOM 1677 O ASN A1013 -7.956 235.268 159.383 1.00123.32 O
ANISOU 1677 O ASN A1013 13407 12924 20526 887 -816 1267 O
ATOM 1678 CB ASN A1013 -6.807 232.771 160.946 1.00123.61 C
ANISOU 1678 CB ASN A1013 13504 13031 20433 931 -605 1326 C
ATOM 1679 CG ASN A1013 -7.540 231.947 161.972 1.00126.47 C
ANISOU 1679 CG ASN A1013 13531 13457 21065 917 -511 1699 C
ATOM 1680 OD1 ASN A1013 -8.770 231.966 162.049 1.00127.62 O
ANISOU 1680 OD1 ASN A1013 13362 13556 21573 820 -580 1990 O
ATOM 1681 ND2 ASN A1013 -6.803 231.215 162.791 1.00126.93 N
ANISOU 1681 ND2 ASN A1013 13622 13626 20980 1027 -331 1740 N
ATOM 1682 N LEU A1014 -6.439 234.369 157.980 1.00123.39 N
ANISOU 1682 N LEU A1014 14132 12696 20055 817 -1029 915 N
ATOM 1683 CA LEU A1014 -6.241 235.613 157.237 1.00124.19 C
ANISOU 1683 CA LEU A1014 14354 12814 20020 874 -985 834 C
ATOM 1684 C LEU A1014 -7.536 235.939 156.468 1.00124.99 C
ANISOU 1684 C LEU A1014 14376 12789 20327 745 -1376 1071 C
ATOM 1685 O LEU A1014 -7.963 237.092 156.450 1.00125.18 O
ANISOU 1685 O LEU A1014 14205 12861 20497 807 -1312 1180 O
ATOM 1686 CB LEU A1014 -5.059 235.491 156.266 1.00124.38 C
ANISOU 1686 CB LEU A1014 14848 12757 19654 910 -935 585 C
ATOM 1687 CG LEU A1014 -3.674 235.670 156.884 1.00126.00 C
ANISOU 1687 CG LEU A1014 15060 13086 19729 1068 -522 354 C
ATOM 1688 CD1 LEU A1014 -2.572 235.298 155.898 1.00126.60 C
ANISOU 1688 CD1 LEU A1014 15567 13048 19487 1100 -451 143 C
ATOM 1689 CD2 LEU A1014 -3.478 237.080 157.361 1.00126.69 C
ANISOU 1689 CD2 LEU A1014 14905 13298 19933 1180 -253 324 C
ATOM 1690 N LYS A1015 -8.183 234.917 155.881 1.00125.47 N
ANISOU 1690 N LYS A1015 14550 12663 20461 570 -1809 1145 N
ATOM 1691 CA LYS A1015 -9.448 235.086 155.169 1.00126.43 C
ANISOU 1691 CA LYS A1015 14556 12654 20827 433 -2281 1366 C
ATOM 1692 C LYS A1015 -10.558 235.510 156.130 1.00127.53 C
ANISOU 1692 C LYS A1015 14087 12861 21508 432 -2189 1670 C
ATOM 1693 O LYS A1015 -11.371 236.357 155.773 1.00127.67 O
ANISOU 1693 O LYS A1015 13898 12857 21752 434 -2354 1859 O
ATOM 1694 CB LYS A1015 -9.840 233.795 154.441 1.00128.10 C
ANISOU 1694 CB LYS A1015 14987 12623 21065 235 -2799 1311 C
ATOM 1695 CG LYS A1015 -8.866 233.395 153.341 1.00131.86 C
ANISOU 1695 CG LYS A1015 16101 13023 20977 259 -2912 979 C
ATOM 1696 CD LYS A1015 -9.219 232.037 152.746 1.00135.83 C
ANISOU 1696 CD LYS A1015 16809 13248 21554 74 -3426 839 C
ATOM 1697 CE LYS A1015 -8.270 231.608 151.650 1.00139.04 C
ANISOU 1697 CE LYS A1015 17882 13581 21367 133 -3516 456 C
ATOM 1698 NZ LYS A1015 -8.423 232.430 150.419 1.00140.92 N
ANISOU 1698 NZ LYS A1015 18487 13905 21151 180 -3790 444 N
ATOM 1699 N VAL A1016 -10.580 234.945 157.351 1.00128.10 N
ANISOU 1699 N VAL A1016 13871 13019 21782 454 -1902 1743 N
ATOM 1700 CA VAL A1016 -11.549 235.288 158.399 1.00129.14 C
ANISOU 1700 CA VAL A1016 13435 13264 22369 500 -1682 2031 C
ATOM 1701 C VAL A1016 -11.441 236.778 158.767 1.00130.52 C
ANISOU 1701 C VAL A1016 13453 13628 22510 713 -1328 1971 C
ATOM 1702 O VAL A1016 -12.463 237.445 158.932 1.00130.60 O
ANISOU 1702 O VAL A1016 13068 13631 22923 739 -1332 2192 O
ATOM 1703 CB VAL A1016 -11.369 234.377 159.639 1.00129.44 C
ANISOU 1703 CB VAL A1016 13294 13414 22475 533 -1366 2127 C
ATOM 1704 CG1 VAL A1016 -12.158 234.893 160.840 1.00129.94 C
ANISOU 1704 CG1 VAL A1016 12830 13692 22849 666 -976 2387 C
ATOM 1705 CG2 VAL A1016 -11.751 232.940 159.317 1.00129.70 C
ANISOU 1705 CG2 VAL A1016 13356 13165 22761 300 -1737 2262 C
ATOM 1706 N ILE A1017 -10.207 237.299 158.869 1.00131.50 N
ANISOU 1706 N ILE A1017 13859 13879 22227 862 -1037 1665 N
ATOM 1707 CA ILE A1017 -9.969 238.708 159.184 1.00132.85 C
ANISOU 1707 CA ILE A1017 13903 14160 22412 1051 -724 1541 C
ATOM 1708 C ILE A1017 -10.481 239.612 158.065 1.00134.39 C
ANISOU 1708 C ILE A1017 14118 14176 22768 1017 -988 1668 C
ATOM 1709 O ILE A1017 -11.111 240.628 158.347 1.00134.61 O
ANISOU 1709 O ILE A1017 13811 14204 23131 1127 -855 1764 O
ATOM 1710 CB ILE A1017 -8.473 238.952 159.495 1.00133.21 C
ANISOU 1710 CB ILE A1017 14213 14328 22072 1181 -415 1182 C
ATOM 1711 CG1 ILE A1017 -8.095 238.276 160.816 1.00134.08 C
ANISOU 1711 CG1 ILE A1017 14201 14676 22066 1281 -137 1102 C
ATOM 1712 CG2 ILE A1017 -8.130 240.445 159.527 1.00133.60 C
ANISOU 1712 CG2 ILE A1017 14183 14374 22204 1330 -187 1019 C
ATOM 1713 CD1 ILE A1017 -6.647 238.177 161.043 1.00135.36 C
ANISOU 1713 CD1 ILE A1017 14617 14930 21884 1369 32 787 C
ATOM 1714 N GLU A1018 -10.244 239.232 156.804 1.00135.22 N
ANISOU 1714 N GLU A1018 14623 14133 22620 892 -1352 1671 N
ATOM 1715 CA GLU A1018 -10.706 240.017 155.660 1.00136.47 C
ANISOU 1715 CA GLU A1018 14871 14151 22832 875 -1650 1843 C
ATOM 1716 C GLU A1018 -12.238 240.154 155.619 1.00137.25 C
ANISOU 1716 C GLU A1018 14532 14159 23456 810 -1965 2179 C
ATOM 1717 O GLU A1018 -12.751 241.229 155.315 1.00137.32 O
ANISOU 1717 O GLU A1018 14317 14103 23755 901 -1980 2354 O
ATOM 1718 CB GLU A1018 -10.220 239.390 154.353 1.00139.01 C
ANISOU 1718 CB GLU A1018 15753 14384 22682 768 -2005 1780 C
ATOM 1719 CG GLU A1018 -8.724 239.500 154.132 1.00144.19 C
ANISOU 1719 CG GLU A1018 16814 15104 22867 840 -1671 1473 C
ATOM 1720 CD GLU A1018 -8.228 238.767 152.901 1.00150.92 C
ANISOU 1720 CD GLU A1018 18238 15886 23219 793 -1937 1416 C
ATOM 1721 OE1 GLU A1018 -9.065 238.373 152.055 1.00152.25 O
ANISOU 1721 OE1 GLU A1018 18528 15971 23350 691 -2455 1575 O
ATOM 1722 OE2 GLU A1018 -6.996 238.582 152.782 1.00153.13 O
ANISOU 1722 OE2 GLU A1018 18843 16201 23138 871 -1631 1204 O
ATOM 1723 N LYS A1019 -12.960 239.067 155.931 1.00137.64 N
ANISOU 1723 N LYS A1019 14423 14170 23702 654 -2215 2286 N
ATOM 1724 CA LYS A1019 -14.422 239.042 155.913 1.00138.45 C
ANISOU 1724 CA LYS A1019 14040 14163 24403 567 -2528 2624 C
ATOM 1725 C LYS A1019 -15.041 239.269 157.293 1.00139.17 C
ANISOU 1725 C LYS A1019 13564 14376 24938 675 -2054 2740 C
ATOM 1726 O LYS A1019 -16.145 238.786 157.552 1.00139.29 O
ANISOU 1726 O LYS A1019 13341 14392 25191 570 -2043 2869 O
ATOM 1727 CB LYS A1019 -14.939 237.725 155.307 1.00140.19 C
ANISOU 1727 CB LYS A1019 14356 14213 24695 312 -3118 2697 C
ATOM 1728 CG LYS A1019 -14.287 237.351 153.975 1.00143.93 C
ANISOU 1728 CG LYS A1019 15499 14617 24571 235 -3515 2474 C
ATOM 1729 CD LYS A1019 -14.771 236.000 153.462 1.00147.93 C
ANISOU 1729 CD LYS A1019 16111 14928 25169 -10 -4079 2435 C
ATOM 1730 CE LYS A1019 -14.207 235.680 152.099 1.00151.36 C
ANISOU 1730 CE LYS A1019 17213 15300 24998 -56 -4556 2205 C
ATOM 1731 NZ LYS A1019 -14.724 234.387 151.575 1.00153.46 N
ANISOU 1731 NZ LYS A1019 17587 15330 25390 -294 -5177 2088 N
ATOM 1732 N ALA A1020 -14.335 239.980 158.182 1.00139.53 N
ANISOU 1732 N ALA A1020 13402 14514 25100 898 -1644 2694 N
ATOM 1733 CA ALA A1020 -14.883 240.309 159.496 1.00140.42 C
ANISOU 1733 CA ALA A1020 13025 14782 25546 1062 -1138 2747 C
ATOM 1734 C ALA A1020 -15.489 241.719 159.456 1.00141.33 C
ANISOU 1734 C ALA A1020 12867 14871 25961 1289 -879 2728 C
ATOM 1735 O ALA A1020 -15.074 242.561 158.658 1.00141.34 O
ANISOU 1735 O ALA A1020 13142 14846 25714 1394 -769 2491 O
ATOM 1736 CB ALA A1020 -13.811 240.224 160.575 1.00140.56 C
ANISOU 1736 CB ALA A1020 13235 15051 25122 1156 -686 2471 C
ATOM 1737 N ASP A1021 -16.501 241.969 160.285 1.00141.89 N
ANISOU 1737 N ASP A1021 12365 14915 26632 1370 -761 2987 N
ATOM 1738 CA ASP A1021 -17.148 243.286 160.351 1.00142.92 C
ANISOU 1738 CA ASP A1021 12172 14972 27157 1610 -499 2971 C
ATOM 1739 C ASP A1021 -16.949 243.964 161.724 1.00142.98 C
ANISOU 1739 C ASP A1021 12074 15223 27029 1882 192 2636 C
ATOM 1740 O ASP A1021 -17.055 245.192 161.826 1.00143.32 O
ANISOU 1740 O ASP A1021 12096 15209 27149 2090 446 2382 O
ATOM 1741 CB ASP A1021 -18.652 243.189 160.012 1.00145.36 C
ANISOU 1741 CB ASP A1021 11878 15113 28239 1597 -699 3405 C
ATOM 1742 CG ASP A1021 -19.034 243.706 158.631 1.00151.14 C
ANISOU 1742 CG ASP A1021 12705 15583 29140 1414 -1433 3683 C
ATOM 1743 OD1 ASP A1021 -18.118 244.070 157.854 1.00152.07 O
ANISOU 1743 OD1 ASP A1021 13328 15641 28811 1384 -1654 3541 O
ATOM 1744 OD2 ASP A1021 -20.251 243.739 158.324 1.00153.83 O
ANISOU 1744 OD2 ASP A1021 12606 15785 30058 1308 -1791 4057 O
ATOM 1745 N ASN A1022 -16.675 243.162 162.776 1.00142.42 N
ANISOU 1745 N ASN A1022 11944 15412 26756 1887 475 2637 N
ATOM 1746 CA AASN A1022 -16.470 243.668 164.131 0.50142.64 C
ANISOU 1746 CA AASN A1022 11920 15749 26528 2167 1104 2319 C
ATOM 1747 CA BASN A1022 -16.464 243.675 164.125 0.50142.52 C
ANISOU 1747 CA BASN A1022 11904 15733 26513 2168 1104 2318 C
ATOM 1748 C ASN A1022 -15.026 243.458 164.577 1.00142.57 C
ANISOU 1748 C ASN A1022 12389 16012 25771 2221 1295 1896 C
ATOM 1749 O ASN A1022 -14.357 242.548 164.088 1.00142.75 O
ANISOU 1749 O ASN A1022 12784 16110 25343 2050 1101 1876 O
ATOM 1750 CB AASN A1022 -17.428 242.980 165.111 0.50143.75 C
ANISOU 1750 CB AASN A1022 11571 16071 26979 2262 1468 2634 C
ATOM 1751 CB BASN A1022 -17.454 243.055 165.122 0.50143.32 C
ANISOU 1751 CB BASN A1022 11514 16015 26925 2265 1471 2631 C
ATOM 1752 CG AASN A1022 -17.671 243.772 166.372 0.50146.84 C
ANISOU 1752 CG AASN A1022 11693 16660 27439 2642 2099 2385 C
ATOM 1753 CG BASN A1022 -17.545 241.549 165.074 0.50145.86 C
ANISOU 1753 CG BASN A1022 11868 16392 27158 2017 1285 2975 C
ATOM 1754 OD1AASN A1022 -17.871 244.992 166.338 0.50148.04 O
ANISOU 1754 OD1AASN A1022 11824 16662 27764 2808 2163 2090 O
ATOM 1755 OD1BASN A1022 -17.736 240.943 164.017 0.50146.81 O
ANISOU 1755 OD1BASN A1022 12082 16258 27442 1724 723 3188 O
ATOM 1756 ND2AASN A1022 -17.666 243.094 167.512 0.50147.38 N
ANISOU 1756 ND2AASN A1022 11564 17060 27374 2797 2586 2504 N
ATOM 1757 ND2BASN A1022 -17.442 240.913 166.228 0.50146.35 N
ANISOU 1757 ND2BASN A1022 11865 16782 26959 2147 1751 3029 N
ATOM 1758 N ALA A1023 -14.550 244.286 165.515 1.00141.96 N
ANISOU 1758 N ALA A1023 12296 16084 25557 2503 1702 1481 N
ATOM 1759 CA ALA A1023 -13.188 244.171 166.026 1.00141.87 C
ANISOU 1759 CA ALA A1023 12654 16335 24916 2604 1870 1033 C
ATOM 1760 C ALA A1023 -12.985 242.887 166.835 1.00141.56 C
ANISOU 1760 C ALA A1023 12712 16647 24427 2598 2012 1171 C
ATOM 1761 O ALA A1023 -11.872 242.372 166.879 1.00141.68 O
ANISOU 1761 O ALA A1023 13087 16791 23953 2560 1925 955 O
ATOM 1762 CB ALA A1023 -12.834 245.390 166.862 1.00141.99 C
ANISOU 1762 CB ALA A1023 12587 16444 24919 2921 2245 526 C
ATOM 1763 N ALA A1024 -14.054 242.355 167.451 1.00141.07 N
ANISOU 1763 N ALA A1024 12304 16719 24578 2639 2239 1573 N
ATOM 1764 CA ALA A1024 -13.974 241.119 168.222 1.00141.03 C
ANISOU 1764 CA ALA A1024 12349 17019 24218 2639 2410 1819 C
ATOM 1765 C ALA A1024 -13.667 239.933 167.309 1.00140.59 C
ANISOU 1765 C ALA A1024 12530 16755 24132 2300 1943 2073 C
ATOM 1766 O ALA A1024 -12.902 239.055 167.701 1.00140.75 O
ANISOU 1766 O ALA A1024 12817 16959 23702 2291 1953 2051 O
ATOM 1767 CB ALA A1024 -15.274 240.882 168.976 1.00141.24 C
ANISOU 1767 CB ALA A1024 11886 17175 24605 2747 2800 2268 C
ATOM 1768 N GLN A1025 -14.231 239.917 166.084 1.00139.86 N
ANISOU 1768 N GLN A1025 12356 16275 24512 2040 1508 2290 N
ATOM 1769 CA GLN A1025 -13.972 238.834 165.132 1.00139.49 C
ANISOU 1769 CA GLN A1025 12558 15991 24449 1726 1025 2458 C
ATOM 1770 C GLN A1025 -12.529 238.865 164.643 1.00138.85 C
ANISOU 1770 C GLN A1025 13003 15887 23866 1695 836 2048 C
ATOM 1771 O GLN A1025 -11.896 237.817 164.523 1.00138.89 O
ANISOU 1771 O GLN A1025 13278 15877 23615 1571 679 2068 O
ATOM 1772 CB GLN A1025 -14.964 238.864 163.959 1.00140.84 C
ANISOU 1772 CB GLN A1025 12522 15792 25200 1488 566 2750 C
ATOM 1773 CG GLN A1025 -16.266 238.109 164.253 1.00143.41 C
ANISOU 1773 CG GLN A1025 12354 16048 26085 1375 585 3266 C
ATOM 1774 CD GLN A1025 -16.163 236.598 164.115 1.00146.77 C
ANISOU 1774 CD GLN A1025 12909 16348 26510 1121 318 3488 C
ATOM 1775 OE1 GLN A1025 -15.669 235.887 165.003 1.00147.77 O
ANISOU 1775 OE1 GLN A1025 13133 16682 26329 1193 619 3540 O
ATOM 1776 NE2 GLN A1025 -16.654 236.066 163.004 1.00147.12 N
ANISOU 1776 NE2 GLN A1025 12950 16031 26918 829 -277 3627 N
ATOM 1777 N VAL A1026 -11.993 240.067 164.404 1.00138.05 N
ANISOU 1777 N VAL A1026 13012 15759 23680 1818 887 1687 N
ATOM 1778 CA VAL A1026 -10.599 240.229 163.993 1.00137.70 C
ANISOU 1778 CA VAL A1026 13395 15688 23238 1807 784 1310 C
ATOM 1779 C VAL A1026 -9.686 239.755 165.135 1.00136.83 C
ANISOU 1779 C VAL A1026 13416 15913 22660 1967 1051 1093 C
ATOM 1780 O VAL A1026 -8.734 239.018 164.890 1.00137.01 O
ANISOU 1780 O VAL A1026 13743 15925 22389 1883 906 1005 O
ATOM 1781 CB VAL A1026 -10.300 241.695 163.582 1.00138.50 C
ANISOU 1781 CB VAL A1026 13505 15645 23473 1906 822 1020 C
ATOM 1782 CG1 VAL A1026 -8.822 241.895 163.272 1.00139.16 C
ANISOU 1782 CG1 VAL A1026 13957 15700 23218 1901 788 655 C
ATOM 1783 CG2 VAL A1026 -11.153 242.114 162.393 1.00138.97 C
ANISOU 1783 CG2 VAL A1026 13468 15386 23947 1765 510 1296 C
ATOM 1784 N LYS A1027 -10.019 240.122 166.383 1.00135.84 N
ANISOU 1784 N LYS A1027 13060 16096 22456 2213 1434 1030 N
ATOM 1785 CA LYS A1027 -9.242 239.709 167.547 1.00135.26 C
ANISOU 1785 CA LYS A1027 13115 16401 21878 2403 1656 853 C
ATOM 1786 C LYS A1027 -9.232 238.189 167.694 1.00134.53 C
ANISOU 1786 C LYS A1027 13100 16363 21650 2279 1571 1248 C
ATOM 1787 O LYS A1027 -8.169 237.604 167.899 1.00134.67 O
ANISOU 1787 O LYS A1027 13382 16481 21308 2294 1489 1118 O
ATOM 1788 CB LYS A1027 -9.773 240.364 168.834 1.00136.74 C
ANISOU 1788 CB LYS A1027 13064 16940 21949 2720 2095 735 C
ATOM 1789 CG LYS A1027 -8.960 239.966 170.062 1.00139.80 C
ANISOU 1789 CG LYS A1027 13630 17777 21711 2947 2274 548 C
ATOM 1790 CD LYS A1027 -9.581 240.396 171.374 1.00143.43 C
ANISOU 1790 CD LYS A1027 13915 18657 21925 3292 2731 466 C
ATOM 1791 CE LYS A1027 -8.677 240.033 172.528 1.00146.24 C
ANISOU 1791 CE LYS A1027 14512 19485 21568 3531 2817 252 C
ATOM 1792 NZ LYS A1027 -9.435 239.825 173.789 1.00148.20 N
ANISOU 1792 NZ LYS A1027 14634 20218 21456 3849 3296 438 N
ATOM 1793 N ASP A1028 -10.402 237.546 167.562 1.00133.46 N
ANISOU 1793 N ASP A1028 12706 16118 21886 2150 1571 1741 N
ATOM 1794 CA ASP A1028 -10.513 236.093 167.678 1.00132.89 C
ANISOU 1794 CA ASP A1028 12651 16008 21835 2008 1486 2159 C
ATOM 1795 C ASP A1028 -9.589 235.359 166.705 1.00131.84 C
ANISOU 1795 C ASP A1028 12882 15592 21622 1793 1076 2040 C
ATOM 1796 O ASP A1028 -8.887 234.440 167.119 1.00131.98 O
ANISOU 1796 O ASP A1028 13068 15697 21383 1817 1080 2104 O
ATOM 1797 CB ASP A1028 -11.969 235.634 167.483 1.00134.52 C
ANISOU 1797 CB ASP A1028 12457 16024 22631 1848 1481 2682 C
ATOM 1798 CG ASP A1028 -12.795 235.614 168.757 1.00138.39 C
ANISOU 1798 CG ASP A1028 12586 16850 23147 2067 2002 3018 C
ATOM 1799 OD1 ASP A1028 -12.681 234.635 169.523 1.00138.91 O
ANISOU 1799 OD1 ASP A1028 12626 17055 23100 2086 2167 3383 O
ATOM 1800 OD2 ASP A1028 -13.565 236.569 168.978 1.00140.26 O
ANISOU 1800 OD2 ASP A1028 12563 17199 23531 2235 2271 2937 O
ATOM 1801 N ALA A1029 -9.552 235.784 165.434 1.00130.65 N
ANISOU 1801 N ALA A1029 12864 15117 21660 1617 748 1870 N
ATOM 1802 CA ALA A1029 -8.695 235.138 164.443 1.00129.99 C
ANISOU 1802 CA ALA A1029 13153 14776 21462 1445 410 1728 C
ATOM 1803 C ALA A1029 -7.210 235.414 164.678 1.00129.09 C
ANISOU 1803 C ALA A1029 13326 14812 20910 1594 507 1321 C
ATOM 1804 O ALA A1029 -6.384 234.530 164.460 1.00129.18 O
ANISOU 1804 O ALA A1029 13581 14734 20768 1542 384 1275 O
ATOM 1805 CB ALA A1029 -9.098 235.559 163.041 1.00130.10 C
ANISOU 1805 CB ALA A1029 13255 14461 21714 1253 59 1690 C
ATOM 1806 N LEU A1030 -6.869 236.619 165.142 1.00128.07 N
ANISOU 1806 N LEU A1030 13138 14879 20644 1781 717 1015 N
ATOM 1807 CA LEU A1030 -5.474 236.973 165.409 1.00127.52 C
ANISOU 1807 CA LEU A1030 13266 14930 20255 1912 778 608 C
ATOM 1808 C LEU A1030 -4.903 236.206 166.605 1.00126.57 C
ANISOU 1808 C LEU A1030 13157 15132 19802 2081 908 635 C
ATOM 1809 O LEU A1030 -3.741 235.801 166.556 1.00126.75 O
ANISOU 1809 O LEU A1030 13373 15153 19635 2108 823 452 O
ATOM 1810 CB LEU A1030 -5.318 238.484 165.630 1.00127.83 C
ANISOU 1810 CB LEU A1030 13199 15038 20335 2054 929 250 C
ATOM 1811 CG LEU A1030 -5.446 239.377 164.398 1.00129.29 C
ANISOU 1811 CG LEU A1030 13427 14895 20804 1927 806 179 C
ATOM 1812 CD1 LEU A1030 -5.700 240.809 164.803 1.00129.86 C
ANISOU 1812 CD1 LEU A1030 13284 15005 21051 2083 995 -72 C
ATOM 1813 CD2 LEU A1030 -4.208 239.290 163.526 1.00129.90 C
ANISOU 1813 CD2 LEU A1030 13798 14784 20776 1840 685 -15 C
ATOM 1814 N THR A1031 -5.711 235.986 167.665 1.00125.38 N
ANISOU 1814 N THR A1031 12791 15262 19584 2213 1127 900 N
ATOM 1815 CA THR A1031 -5.261 235.228 168.841 1.00124.69 C
ANISOU 1815 CA THR A1031 12729 15524 19123 2401 1256 1025 C
ATOM 1816 C THR A1031 -4.937 233.781 168.464 1.00123.52 C
ANISOU 1816 C THR A1031 12728 15155 19049 2247 1057 1320 C
ATOM 1817 O THR A1031 -3.954 233.221 168.955 1.00123.61 O
ANISOU 1817 O THR A1031 12888 15283 18796 2355 1000 1231 O
ATOM 1818 CB THR A1031 -6.278 235.305 169.988 1.00125.95 C
ANISOU 1818 CB THR A1031 12640 16030 19187 2580 1595 1339 C
ATOM 1819 OG1 THR A1031 -7.579 234.972 169.501 1.00126.96 O
ANISOU 1819 OG1 THR A1031 12543 15911 19785 2385 1614 1788 O
ATOM 1820 CG2 THR A1031 -6.295 236.667 170.662 1.00126.30 C
ANISOU 1820 CG2 THR A1031 12591 16375 19023 2832 1831 938 C
ATOM 1821 N LYS A1032 -5.747 233.194 167.564 1.00122.27 N
ANISOU 1821 N LYS A1032 12519 14638 19301 1995 912 1631 N
ATOM 1822 CA LYS A1032 -5.535 231.840 167.059 1.00121.41 C
ANISOU 1822 CA LYS A1032 12542 14217 19372 1823 692 1864 C
ATOM 1823 C LYS A1032 -4.298 231.791 166.143 1.00120.32 C
ANISOU 1823 C LYS A1032 12721 13850 19143 1767 476 1473 C
ATOM 1824 O LYS A1032 -3.567 230.801 166.153 1.00120.54 O
ANISOU 1824 O LYS A1032 12891 13765 19143 1773 388 1527 O
ATOM 1825 CB LYS A1032 -6.782 231.330 166.317 1.00122.74 C
ANISOU 1825 CB LYS A1032 12558 14034 20043 1558 530 2203 C
ATOM 1826 CG LYS A1032 -7.988 231.093 167.216 1.00125.73 C
ANISOU 1826 CG LYS A1032 12563 14579 20629 1596 784 2701 C
ATOM 1827 CD LYS A1032 -9.191 230.637 166.404 1.00129.02 C
ANISOU 1827 CD LYS A1032 12765 14602 21654 1308 559 2997 C
ATOM 1828 CE LYS A1032 -10.447 230.608 167.232 1.00132.10 C
ANISOU 1828 CE LYS A1032 12704 15154 22332 1353 873 3475 C
ATOM 1829 NZ LYS A1032 -11.616 230.177 166.428 1.00134.03 N
ANISOU 1829 NZ LYS A1032 12678 14972 23275 1049 596 3787 N
ATOM 1830 N MET A1033 -4.057 232.856 165.366 1.00118.89 N
ANISOU 1830 N MET A1033 12633 13591 18948 1731 426 1113 N
ATOM 1831 CA MET A1033 -2.884 232.929 164.502 1.00117.84 C
ANISOU 1831 CA MET A1033 12776 13271 18728 1703 314 771 C
ATOM 1832 C MET A1033 -1.613 233.055 165.325 1.00116.68 C
ANISOU 1832 C MET A1033 12643 13374 18315 1919 430 535 C
ATOM 1833 O MET A1033 -0.598 232.464 164.964 1.00116.78 O
ANISOU 1833 O MET A1033 12824 13244 18305 1928 359 418 O
ATOM 1834 CB MET A1033 -2.983 234.129 163.558 1.00118.33 C
ANISOU 1834 CB MET A1033 12898 13208 18853 1631 285 532 C
ATOM 1835 CG MET A1033 -3.912 233.902 162.416 1.00119.99 C
ANISOU 1835 CG MET A1033 13190 13121 19281 1414 55 704 C
ATOM 1836 SD MET A1033 -4.077 235.330 161.329 1.00122.30 S
ANISOU 1836 SD MET A1033 13554 13292 19624 1360 12 536 S
ATOM 1837 CE MET A1033 -2.426 235.458 160.725 1.00120.29 C
ANISOU 1837 CE MET A1033 13609 12956 19141 1423 108 187 C
ATOM 1838 N ARG A1034 -1.660 233.824 166.421 1.00115.33 N
ANISOU 1838 N ARG A1034 12291 13572 17957 2107 591 441 N
ATOM 1839 CA ARG A1034 -0.495 234.045 167.263 1.00114.77 C
ANISOU 1839 CA ARG A1034 12212 13771 17625 2321 623 173 C
ATOM 1840 C ARG A1034 -0.043 232.772 167.965 1.00114.23 C
ANISOU 1840 C ARG A1034 12173 13822 17406 2426 573 447 C
ATOM 1841 O ARG A1034 1.151 232.471 167.988 1.00114.52 O
ANISOU 1841 O ARG A1034 12277 13850 17385 2512 480 279 O
ATOM 1842 CB ARG A1034 -0.758 235.155 168.274 1.00115.58 C
ANISOU 1842 CB ARG A1034 12146 14239 17530 2508 767 -42 C
ATOM 1843 CG ARG A1034 0.530 235.727 168.813 1.00117.80 C
ANISOU 1843 CG ARG A1034 12421 14697 17640 2676 702 -486 C
ATOM 1844 CD ARG A1034 0.309 236.629 170.003 1.00119.99 C
ANISOU 1844 CD ARG A1034 12571 15379 17642 2906 796 -748 C
ATOM 1845 NE ARG A1034 1.545 237.311 170.378 1.00121.63 N
ANISOU 1845 NE ARG A1034 12746 15673 17794 3023 651 -1257 N
ATOM 1846 CZ ARG A1034 2.464 236.813 171.198 1.00122.89 C
ANISOU 1846 CZ ARG A1034 12923 16097 17674 3195 484 -1329 C
ATOM 1847 NH1 ARG A1034 2.295 235.618 171.748 1.00121.99 N
ANISOU 1847 NH1 ARG A1034 12880 16191 17278 3288 475 -887 N
ATOM 1848 NH2 ARG A1034 3.560 237.506 171.474 1.00122.85 N
ANISOU 1848 NH2 ARG A1034 12835 16124 17719 3275 303 -1819 N
ATOM 1849 N ALA A1035 -0.994 232.006 168.510 1.00113.38 N
ANISOU 1849 N ALA A1035 11985 13796 17300 2420 644 912 N
ATOM 1850 CA ALA A1035 -0.677 230.735 169.156 1.00112.85 C
ANISOU 1850 CA ALA A1035 11932 13790 17155 2513 614 1284 C
ATOM 1851 C ALA A1035 -0.126 229.732 168.134 1.00112.19 C
ANISOU 1851 C ALA A1035 12011 13236 17381 2356 430 1306 C
ATOM 1852 O ALA A1035 0.748 228.941 168.474 1.00112.12 O
ANISOU 1852 O ALA A1035 12046 13226 17329 2478 359 1384 O
ATOM 1853 CB ALA A1035 -1.914 230.169 169.832 1.00113.01 C
ANISOU 1853 CB ALA A1035 11795 13923 17223 2505 779 1835 C
ATOM 1854 N ALA A1036 -0.616 229.781 166.882 1.00111.52 N
ANISOU 1854 N ALA A1036 12024 12758 17589 2112 344 1218 N
ATOM 1855 CA ALA A1036 -0.148 228.912 165.804 1.00111.43 C
ANISOU 1855 CA ALA A1036 12220 12294 17824 1977 184 1146 C
ATOM 1856 C ALA A1036 1.266 229.288 165.340 1.00111.11 C
ANISOU 1856 C ALA A1036 12315 12216 17685 2076 185 716 C
ATOM 1857 O ALA A1036 2.058 228.399 165.032 1.00111.28 O
ANISOU 1857 O ALA A1036 12449 12002 17829 2109 126 693 O
ATOM 1858 CB ALA A1036 -1.112 228.963 164.630 1.00111.47 C
ANISOU 1858 CB ALA A1036 12321 11964 18068 1718 58 1130 C
ATOM 1859 N ALA A1037 1.593 230.586 165.305 1.00110.56 N
ANISOU 1859 N ALA A1037 12201 12340 17468 2126 270 386 N
ATOM 1860 CA ALA A1037 2.925 231.027 164.895 1.00110.38 C
ANISOU 1860 CA ALA A1037 12231 12266 17443 2207 305 11 C
ATOM 1861 C ALA A1037 3.981 230.518 165.878 1.00110.20 C
ANISOU 1861 C ALA A1037 12088 12440 17342 2428 264 23 C
ATOM 1862 O ALA A1037 5.010 229.997 165.455 1.00110.23 O
ANISOU 1862 O ALA A1037 12145 12246 17490 2481 250 -95 O
ATOM 1863 CB ALA A1037 2.974 232.544 164.793 1.00110.49 C
ANISOU 1863 CB ALA A1037 12159 12412 17409 2205 399 -294 C
ATOM 1864 N LEU A1038 3.706 230.612 167.184 1.00109.85 N
ANISOU 1864 N LEU A1038 11886 12792 17058 2579 245 185 N
ATOM 1865 CA LEU A1038 4.628 230.105 168.196 1.00110.01 C
ANISOU 1865 CA LEU A1038 11808 13054 16939 2813 143 251 C
ATOM 1866 C LEU A1038 4.700 228.582 168.168 1.00109.76 C
ANISOU 1866 C LEU A1038 11842 12785 17078 2828 81 646 C
ATOM 1867 O LEU A1038 5.762 228.026 168.426 1.00110.01 O
ANISOU 1867 O LEU A1038 11827 12792 17180 2982 -18 637 O
ATOM 1868 CB LEU A1038 4.224 230.586 169.588 1.00110.49 C
ANISOU 1868 CB LEU A1038 11748 13639 16595 2997 145 346 C
ATOM 1869 CG LEU A1038 4.066 232.094 169.753 1.00112.42 C
ANISOU 1869 CG LEU A1038 11913 14104 16697 3011 202 -74 C
ATOM 1870 CD1 LEU A1038 3.696 232.435 171.179 1.00113.14 C
ANISOU 1870 CD1 LEU A1038 11932 14736 16321 3241 220 -9 C
ATOM 1871 CD2 LEU A1038 5.336 232.843 169.337 1.00113.17 C
ANISOU 1871 CD2 LEU A1038 11935 14095 16970 3027 105 -579 C
ATOM 1872 N ASP A1039 3.585 227.911 167.828 1.00109.16 N
ANISOU 1872 N ASP A1039 11841 12488 17145 2663 122 987 N
ATOM 1873 CA ASP A1039 3.492 226.457 167.695 1.00108.99 C
ANISOU 1873 CA ASP A1039 11874 12129 17408 2628 60 1361 C
ATOM 1874 C ASP A1039 4.402 225.992 166.545 1.00109.09 C
ANISOU 1874 C ASP A1039 12043 11686 17722 2580 15 1064 C
ATOM 1875 O ASP A1039 5.077 224.972 166.670 1.00109.21 O
ANISOU 1875 O ASP A1039 12054 11492 17947 2688 -45 1213 O
ATOM 1876 CB ASP A1039 2.039 226.071 167.394 1.00110.05 C
ANISOU 1876 CB ASP A1039 12021 12065 17728 2403 87 1673 C
ATOM 1877 CG ASP A1039 1.524 224.816 168.052 1.00113.61 C
ANISOU 1877 CG ASP A1039 12385 12384 18399 2410 73 2256 C
ATOM 1878 OD1 ASP A1039 2.161 224.345 169.016 1.00113.95 O
ANISOU 1878 OD1 ASP A1039 12337 12677 18283 2643 87 2538 O
ATOM 1879 OD2 ASP A1039 0.462 224.323 167.625 1.00115.71 O
ANISOU 1879 OD2 ASP A1039 12653 12299 19011 2184 34 2458 O
ATOM 1880 N ALA A1040 4.435 226.746 165.434 1.00108.86 N
ANISOU 1880 N ALA A1040 12151 11502 17709 2442 72 664 N
ATOM 1881 CA ALA A1040 5.302 226.422 164.296 1.00109.14 C
ANISOU 1881 CA ALA A1040 12362 11157 17949 2430 110 357 C
ATOM 1882 C ALA A1040 6.766 226.829 164.517 1.00109.43 C
ANISOU 1882 C ALA A1040 12262 11326 17988 2633 177 95 C
ATOM 1883 O ALA A1040 7.621 226.454 163.725 1.00109.44 O
ANISOU 1883 O ALA A1040 12352 11033 18198 2681 263 -108 O
ATOM 1884 CB ALA A1040 4.773 227.067 163.027 1.00109.14 C
ANISOU 1884 CB ALA A1040 12585 10973 17909 2229 163 98 C
ATOM 1885 N GLN A1041 7.056 227.604 165.567 1.00109.67 N
ANISOU 1885 N GLN A1041 12070 11787 17814 2758 137 71 N
ATOM 1886 CA GLN A1041 8.406 228.045 165.889 1.00110.38 C
ANISOU 1886 CA GLN A1041 11961 12011 17967 2936 122 -183 C
ATOM 1887 C GLN A1041 9.121 227.025 166.784 1.00110.60 C
ANISOU 1887 C GLN A1041 11842 12115 18064 3163 -46 85 C
ATOM 1888 O GLN A1041 8.490 226.244 167.500 1.00110.63 O
ANISOU 1888 O GLN A1041 11850 12263 17920 3212 -146 491 O
ATOM 1889 CB GLN A1041 8.363 229.423 166.569 1.00112.40 C
ANISOU 1889 CB GLN A1041 12050 12668 17987 2958 90 -407 C
ATOM 1890 CG GLN A1041 9.707 230.147 166.609 1.00116.16 C
ANISOU 1890 CG GLN A1041 12296 13194 18647 3066 68 -774 C
ATOM 1891 CD GLN A1041 9.587 231.570 167.112 1.00120.98 C
ANISOU 1891 CD GLN A1041 12758 14100 19108 3051 26 -1066 C
ATOM 1892 OE1 GLN A1041 8.601 231.958 167.756 1.00122.66 O
ANISOU 1892 OE1 GLN A1041 13011 14596 18997 3046 -21 -980 O
ATOM 1893 NE2 GLN A1041 10.598 232.386 166.833 1.00121.53 N
ANISOU 1893 NE2 GLN A1041 12628 14080 19466 3050 62 -1425 N
ATOM 1894 N GLY A1064 12.183 235.915 160.494 1.00 95.68 N
ANISOU 1894 N GLY A1064 9538 9296 17520 2418 1749 -1975 N
ATOM 1895 CA GLY A1064 10.931 235.684 159.784 1.00 96.36 C
ANISOU 1895 CA GLY A1064 10088 9357 17169 2338 1767 -1767 C
ATOM 1896 C GLY A1064 9.748 235.525 160.713 1.00 96.92 C
ANISOU 1896 C GLY A1064 10220 9670 16936 2303 1420 -1684 C
ATOM 1897 O GLY A1064 8.716 236.170 160.526 1.00 97.04 O
ANISOU 1897 O GLY A1064 10359 9717 16796 2191 1388 -1599 O
ATOM 1898 N PHE A1065 9.884 234.655 161.721 1.00 97.21 N
ANISOU 1898 N PHE A1065 10151 9879 16904 2415 1177 -1667 N
ATOM 1899 CA PHE A1065 8.817 234.453 162.701 1.00 97.79 C
ANISOU 1899 CA PHE A1065 10250 10217 16690 2414 909 -1539 C
ATOM 1900 C PHE A1065 8.686 235.668 163.619 1.00 98.21 C
ANISOU 1900 C PHE A1065 10040 10499 16775 2429 806 -1734 C
ATOM 1901 O PHE A1065 7.580 235.973 164.041 1.00 98.25 O
ANISOU 1901 O PHE A1065 10103 10662 16567 2388 728 -1648 O
ATOM 1902 CB PHE A1065 9.024 233.166 163.513 1.00 97.76 C
ANISOU 1902 CB PHE A1065 10219 10334 16590 2553 712 -1394 C
ATOM 1903 CG PHE A1065 8.466 231.923 162.861 1.00 98.41 C
ANISOU 1903 CG PHE A1065 10609 10210 16573 2503 723 -1149 C
ATOM 1904 CD1 PHE A1065 9.233 231.175 161.988 1.00 99.20 C
ANISOU 1904 CD1 PHE A1065 10844 10008 16839 2540 878 -1195 C
ATOM 1905 CD2 PHE A1065 7.180 231.496 163.132 1.00 99.19 C
ANISOU 1905 CD2 PHE A1065 10839 10390 16460 2425 584 -894 C
ATOM 1906 CE1 PHE A1065 8.721 230.029 161.397 1.00 99.83 C
ANISOU 1906 CE1 PHE A1065 11216 9856 16857 2499 850 -1045 C
ATOM 1907 CE2 PHE A1065 6.673 230.347 162.540 1.00 99.81 C
ANISOU 1907 CE2 PHE A1065 11164 10220 16540 2357 544 -702 C
ATOM 1908 CZ PHE A1065 7.448 229.619 161.682 1.00 99.59 C
ANISOU 1908 CZ PHE A1065 11297 9878 16662 2393 655 -806 C
ATOM 1909 N ASP A1066 9.792 236.388 163.893 1.00 98.27 N
ANISOU 1909 N ASP A1066 9743 10495 17100 2486 811 -2018 N
ATOM 1910 CA ASP A1066 9.752 237.598 164.711 1.00 98.80 C
ANISOU 1910 CA ASP A1066 9558 10715 17266 2500 691 -2300 C
ATOM 1911 C ASP A1066 8.929 238.679 164.015 1.00 98.76 C
ANISOU 1911 C ASP A1066 9635 10539 17348 2349 878 -2286 C
ATOM 1912 O ASP A1066 8.148 239.378 164.664 1.00 99.03 O
ANISOU 1912 O ASP A1066 9613 10727 17287 2357 785 -2391 O
ATOM 1913 CB ASP A1066 11.164 238.115 164.993 1.00101.05 C
ANISOU 1913 CB ASP A1066 9470 10923 18001 2556 634 -2620 C
ATOM 1914 CG ASP A1066 11.805 237.459 166.190 1.00106.67 C
ANISOU 1914 CG ASP A1066 10019 11898 18615 2742 314 -2697 C
ATOM 1915 OD1 ASP A1066 11.716 236.219 166.302 1.00107.80 O
ANISOU 1915 OD1 ASP A1066 10345 12115 18499 2820 277 -2412 O
ATOM 1916 OD2 ASP A1066 12.398 238.186 167.019 1.00109.08 O
ANISOU 1916 OD2 ASP A1066 10004 12317 19124 2815 69 -3041 O
ATOM 1917 N ILE A1067 9.084 238.806 162.690 1.00 98.10 N
ANISOU 1917 N ILE A1067 9696 10148 17431 2237 1154 -2141 N
ATOM 1918 CA ILE A1067 8.307 239.762 161.914 1.00 97.96 C
ANISOU 1918 CA ILE A1067 9783 9956 17482 2109 1321 -2039 C
ATOM 1919 C ILE A1067 6.834 239.346 161.950 1.00 98.06 C
ANISOU 1919 C ILE A1067 10049 10108 17101 2070 1196 -1804 C
ATOM 1920 O ILE A1067 5.971 240.168 162.233 1.00 98.18 O
ANISOU 1920 O ILE A1067 9993 10168 17141 2043 1156 -1822 O
ATOM 1921 CB ILE A1067 8.843 239.821 160.466 1.00 98.06 C
ANISOU 1921 CB ILE A1067 9954 9667 17637 2040 1651 -1878 C
ATOM 1922 CG1 ILE A1067 10.341 240.150 160.448 1.00 98.62 C
ANISOU 1922 CG1 ILE A1067 9695 9582 18195 2080 1821 -2071 C
ATOM 1923 CG2 ILE A1067 8.036 240.802 159.630 1.00 98.64 C
ANISOU 1923 CG2 ILE A1067 10176 9578 17725 1927 1800 -1689 C
ATOM 1924 CD1 ILE A1067 10.991 239.959 159.140 1.00 99.65 C
ANISOU 1924 CD1 ILE A1067 9968 9475 18421 2069 2206 -1902 C
ATOM 1925 N LEU A1068 6.565 238.058 161.734 1.00 97.93 N
ANISOU 1925 N LEU A1068 10277 10137 16794 2076 1127 -1598 N
ATOM 1926 CA LEU A1068 5.218 237.525 161.731 1.00 98.46 C
ANISOU 1926 CA LEU A1068 10539 10288 16585 2017 993 -1348 C
ATOM 1927 C LEU A1068 4.482 237.764 163.051 1.00 98.89 C
ANISOU 1927 C LEU A1068 10400 10639 16534 2092 847 -1378 C
ATOM 1928 O LEU A1068 3.379 238.303 163.048 1.00 99.08 O
ANISOU 1928 O LEU A1068 10414 10688 16545 2039 838 -1276 O
ATOM 1929 CB LEU A1068 5.254 236.032 161.413 1.00 98.90 C
ANISOU 1929 CB LEU A1068 10826 10292 16460 2020 922 -1181 C
ATOM 1930 CG LEU A1068 3.894 235.454 161.134 1.00100.72 C
ANISOU 1930 CG LEU A1068 11242 10514 16513 1917 770 -912 C
ATOM 1931 CD1 LEU A1068 3.395 235.929 159.792 1.00101.38 C
ANISOU 1931 CD1 LEU A1068 11564 10385 16571 1783 809 -826 C
ATOM 1932 CD2 LEU A1068 3.912 233.941 161.235 1.00101.42 C
ANISOU 1932 CD2 LEU A1068 11457 10559 16517 1939 651 -772 C
ATOM 1933 N VAL A1069 5.092 237.379 164.175 1.00 98.81 N
ANISOU 1933 N VAL A1069 10238 10868 16437 2238 742 -1507 N
ATOM 1934 CA VAL A1069 4.496 237.552 165.491 1.00 99.19 C
ANISOU 1934 CA VAL A1069 10146 11264 16278 2362 638 -1545 C
ATOM 1935 C VAL A1069 4.314 239.030 165.814 1.00 99.22 C
ANISOU 1935 C VAL A1069 9961 11297 16443 2388 686 -1853 C
ATOM 1936 O VAL A1069 3.262 239.421 166.312 1.00 99.38 O
ANISOU 1936 O VAL A1069 9940 11471 16348 2426 710 -1811 O
ATOM 1937 CB VAL A1069 5.317 236.799 166.559 1.00100.21 C
ANISOU 1937 CB VAL A1069 10192 11657 16225 2542 485 -1601 C
ATOM 1938 CG1 VAL A1069 4.853 237.145 167.969 1.00100.91 C
ANISOU 1938 CG1 VAL A1069 10155 12168 16019 2722 394 -1721 C
ATOM 1939 CG2 VAL A1069 5.251 235.293 166.324 1.00100.80 C
ANISOU 1939 CG2 VAL A1069 10442 11676 16180 2528 445 -1228 C
ATOM 1940 N GLY A1070 5.297 239.849 165.457 1.00 98.93 N
ANISOU 1940 N GLY A1070 9788 11061 16740 2361 729 -2145 N
ATOM 1941 CA GLY A1070 5.211 241.286 165.670 1.00 99.15 C
ANISOU 1941 CA GLY A1070 9613 11012 17046 2368 769 -2462 C
ATOM 1942 C GLY A1070 4.077 241.916 164.889 1.00 98.99 C
ANISOU 1942 C GLY A1070 9668 10791 17151 2255 913 -2253 C
ATOM 1943 O GLY A1070 3.358 242.765 165.414 1.00 99.20 O
ANISOU 1943 O GLY A1070 9570 10879 17241 2315 927 -2397 O
ATOM 1944 N GLN A1071 3.898 241.500 163.634 1.00 98.58 N
ANISOU 1944 N GLN A1071 9827 10507 17122 2112 1005 -1922 N
ATOM 1945 CA GLN A1071 2.822 242.022 162.797 1.00 98.72 C
ANISOU 1945 CA GLN A1071 9932 10344 17234 2009 1075 -1671 C
ATOM 1946 C GLN A1071 1.445 241.572 163.293 1.00 98.89 C
ANISOU 1946 C GLN A1071 9980 10574 17019 2036 983 -1458 C
ATOM 1947 O GLN A1071 0.468 242.295 163.116 1.00 98.79 O
ANISOU 1947 O GLN A1071 9890 10482 17164 2017 1013 -1360 O
ATOM 1948 CB GLN A1071 3.042 241.648 161.331 1.00100.10 C
ANISOU 1948 CB GLN A1071 10371 10266 17395 1878 1156 -1397 C
ATOM 1949 CG GLN A1071 4.247 242.335 160.693 1.00102.96 C
ANISOU 1949 CG GLN A1071 10664 10380 18077 1853 1355 -1523 C
ATOM 1950 CD GLN A1071 4.514 241.854 159.288 1.00107.00 C
ANISOU 1950 CD GLN A1071 11489 10711 18454 1774 1493 -1257 C
ATOM 1951 OE1 GLN A1071 4.858 242.631 158.394 1.00108.23 O
ANISOU 1951 OE1 GLN A1071 11653 10633 18837 1734 1715 -1171 O
ATOM 1952 NE2 GLN A1071 4.370 240.561 159.056 1.00107.88 N
ANISOU 1952 NE2 GLN A1071 11875 10918 18197 1764 1383 -1121 N
ATOM 1953 N ILE A1072 1.369 240.395 163.927 1.00 98.97 N
ANISOU 1953 N ILE A1072 10062 10830 16713 2087 889 -1353 N
ATOM 1954 CA ILE A1072 0.143 239.900 164.533 1.00 99.63 C
ANISOU 1954 CA ILE A1072 10113 11123 16618 2122 852 -1113 C
ATOM 1955 C ILE A1072 -0.172 240.769 165.762 1.00100.28 C
ANISOU 1955 C ILE A1072 9960 11460 16681 2306 934 -1380 C
ATOM 1956 O ILE A1072 -1.309 241.202 165.930 1.00100.24 O
ANISOU 1956 O ILE A1072 9842 11492 16752 2332 1012 -1263 O
ATOM 1957 CB ILE A1072 0.277 238.391 164.872 1.00100.02 C
ANISOU 1957 CB ILE A1072 10289 11316 16396 2130 758 -889 C
ATOM 1958 CG1 ILE A1072 0.276 237.556 163.585 1.00100.83 C
ANISOU 1958 CG1 ILE A1072 10644 11128 16541 1951 670 -657 C
ATOM 1959 CG2 ILE A1072 -0.827 237.926 165.817 1.00100.58 C
ANISOU 1959 CG2 ILE A1072 10252 11656 16307 2207 782 -640 C
ATOM 1960 CD1 ILE A1072 0.644 236.123 163.773 1.00102.10 C
ANISOU 1960 CD1 ILE A1072 10927 11317 16550 1959 581 -504 C
ATOM 1961 N ASP A1073 0.844 241.082 166.577 1.00100.87 N
ANISOU 1961 N ASP A1073 9952 11692 16681 2444 908 -1771 N
ATOM 1962 CA ASP A1073 0.685 241.946 167.747 1.00101.98 C
ANISOU 1962 CA ASP A1073 9917 12080 16751 2645 950 -2141 C
ATOM 1963 C ASP A1073 0.250 243.360 167.354 1.00102.81 C
ANISOU 1963 C ASP A1073 9869 11910 17283 2619 1058 -2343 C
ATOM 1964 O ASP A1073 -0.578 243.962 168.043 1.00103.11 O
ANISOU 1964 O ASP A1073 9783 12087 17306 2762 1167 -2468 O
ATOM 1965 CB ASP A1073 1.990 242.007 168.554 1.00103.82 C
ANISOU 1965 CB ASP A1073 10097 12487 16861 2775 799 -2568 C
ATOM 1966 CG ASP A1073 2.359 240.694 169.206 1.00108.44 C
ANISOU 1966 CG ASP A1073 10797 13396 17010 2870 682 -2369 C
ATOM 1967 OD1 ASP A1073 1.447 239.882 169.453 1.00109.28 O
ANISOU 1967 OD1 ASP A1073 10986 13694 16840 2901 761 -1972 O
ATOM 1968 OD2 ASP A1073 3.564 240.477 169.463 1.00110.47 O
ANISOU 1968 OD2 ASP A1073 11027 13689 17258 2913 510 -2580 O
ATOM 1969 N ASP A1074 0.785 243.884 166.238 1.00102.85 N
ANISOU 1969 N ASP A1074 9879 11513 17686 2455 1061 -2340 N
ATOM 1970 CA ASP A1074 0.421 245.210 165.748 1.00103.23 C
ANISOU 1970 CA ASP A1074 9777 11233 18213 2421 1163 -2444 C
ATOM 1971 C ASP A1074 -1.073 245.261 165.422 1.00104.48 C
ANISOU 1971 C ASP A1074 9925 11364 18408 2405 1237 -2075 C
ATOM 1972 O ASP A1074 -1.765 246.187 165.840 1.00104.54 O
ANISOU 1972 O ASP A1074 9745 11338 18638 2521 1337 -2236 O
ATOM 1973 CB ASP A1074 1.240 245.563 164.495 1.00103.60 C
ANISOU 1973 CB ASP A1074 9868 10876 18621 2245 1194 -2347 C
ATOM 1974 CG ASP A1074 2.708 245.830 164.739 1.00105.55 C
ANISOU 1974 CG ASP A1074 10004 11047 19053 2250 1156 -2725 C
ATOM 1975 OD1 ASP A1074 3.115 245.893 165.918 1.00105.65 O
ANISOU 1975 OD1 ASP A1074 9896 11308 18940 2395 1038 -3141 O
ATOM 1976 OD2 ASP A1074 3.453 245.968 163.754 1.00106.78 O
ANISOU 1976 OD2 ASP A1074 10188 10909 19475 2120 1243 -2595 O
ATOM 1977 N ALA A1075 -1.571 244.239 164.716 1.00105.36 N
ANISOU 1977 N ALA A1075 10216 11486 18331 2275 1169 -1609 N
ATOM 1978 CA ALA A1075 -2.977 244.164 164.338 1.00106.82 C
ANISOU 1978 CA ALA A1075 10355 11629 18603 2232 1169 -1226 C
ATOM 1979 C ALA A1075 -3.868 243.910 165.544 1.00108.22 C
ANISOU 1979 C ALA A1075 10375 12149 18595 2401 1275 -1226 C
ATOM 1980 O ALA A1075 -4.964 244.461 165.619 1.00108.39 O
ANISOU 1980 O ALA A1075 10203 12126 18854 2457 1370 -1101 O
ATOM 1981 CB ALA A1075 -3.180 243.078 163.295 1.00107.02 C
ANISOU 1981 CB ALA A1075 10618 11561 18485 2041 1004 -801 C
ATOM 1982 N LEU A1076 -3.397 243.096 166.497 1.00109.17 N
ANISOU 1982 N LEU A1076 10563 12614 18301 2504 1281 -1336 N
ATOM 1983 CA LEU A1076 -4.139 242.792 167.716 1.00110.58 C
ANISOU 1983 CA LEU A1076 10627 13180 18208 2699 1439 -1297 C
ATOM 1984 C LEU A1076 -4.350 244.053 168.544 1.00111.77 C
ANISOU 1984 C LEU A1076 10592 13427 18447 2932 1623 -1741 C
ATOM 1985 O LEU A1076 -5.426 244.240 169.100 1.00111.72 O
ANISOU 1985 O LEU A1076 10429 13602 18419 3083 1838 -1641 O
ATOM 1986 CB LEU A1076 -3.394 241.750 168.546 1.00111.01 C
ANISOU 1986 CB LEU A1076 10827 13586 17767 2783 1386 -1293 C
ATOM 1987 CG LEU A1076 -4.176 241.213 169.719 1.00112.74 C
ANISOU 1987 CG LEU A1076 10982 14285 17569 3024 1579 -1206 C
ATOM 1988 CD1 LEU A1076 -5.327 240.355 169.244 1.00113.29 C
ANISOU 1988 CD1 LEU A1076 10921 14372 17750 2967 1736 -639 C
ATOM 1989 CD2 LEU A1076 -3.276 240.460 170.667 1.00113.59 C
ANISOU 1989 CD2 LEU A1076 11253 14701 17204 3121 1464 -1231 C
ATOM 1990 N LYS A1077 -3.340 244.939 168.593 1.00112.67 N
ANISOU 1990 N LYS A1077 10701 13388 18722 2965 1554 -2240 N
ATOM 1991 CA LYS A1077 -3.450 246.200 169.325 1.00113.94 C
ANISOU 1991 CA LYS A1077 10691 13553 19047 3179 1686 -2759 C
ATOM 1992 C LYS A1077 -4.504 247.090 168.688 1.00114.85 C
ANISOU 1992 C LYS A1077 10607 13320 19713 3149 1824 -2598 C
ATOM 1993 O LYS A1077 -5.297 247.693 169.402 1.00114.81 O
ANISOU 1993 O LYS A1077 10432 13416 19776 3367 2041 -2784 O
ATOM 1994 CB LYS A1077 -2.101 246.934 169.382 1.00115.92 C
ANISOU 1994 CB LYS A1077 10940 13632 19471 3174 1524 -3323 C
ATOM 1995 CG LYS A1077 -2.158 248.241 170.176 1.00119.61 C
ANISOU 1995 CG LYS A1077 11243 14082 20120 3404 1608 -3967 C
ATOM 1996 CD LYS A1077 -1.732 248.070 171.638 1.00123.08 C
ANISOU 1996 CD LYS A1077 11774 15051 19940 3675 1553 -4436 C
ATOM 1997 CE LYS A1077 -0.236 247.915 171.768 1.00125.94 C
ANISOU 1997 CE LYS A1077 12196 15424 20230 3612 1231 -4786 C
ATOM 1998 NZ LYS A1077 0.166 247.615 173.163 1.00127.45 N
ANISOU 1998 NZ LYS A1077 12504 16176 19746 3888 1103 -5189 N
ATOM 1999 N LEU A1078 -4.535 247.151 167.350 1.00115.65 N
ANISOU 1999 N LEU A1078 10732 13023 20185 2907 1705 -2241 N
ATOM 2000 CA LEU A1078 -5.535 247.943 166.639 1.00117.03 C
ANISOU 2000 CA LEU A1078 10721 12852 20894 2873 1770 -1995 C
ATOM 2001 C LEU A1078 -6.928 247.378 166.863 1.00118.20 C
ANISOU 2001 C LEU A1078 10735 13191 20983 2926 1879 -1580 C
ATOM 2002 O LEU A1078 -7.867 248.145 167.084 1.00118.34 O
ANISOU 2002 O LEU A1078 10493 13103 21368 3067 2052 -1587 O
ATOM 2003 CB LEU A1078 -5.224 248.013 165.144 1.00117.40 C
ANISOU 2003 CB LEU A1078 10887 12508 21213 2620 1587 -1649 C
ATOM 2004 CG LEU A1078 -3.979 248.800 164.795 1.00119.14 C
ANISOU 2004 CG LEU A1078 11138 12430 21701 2565 1562 -1970 C
ATOM 2005 CD1 LEU A1078 -3.627 248.629 163.344 1.00119.84 C
ANISOU 2005 CD1 LEU A1078 11409 12234 21889 2341 1444 -1554 C
ATOM 2006 CD2 LEU A1078 -4.151 250.264 165.137 1.00119.84 C
ANISOU 2006 CD2 LEU A1078 10956 12224 22355 2708 1697 -2317 C
ATOM 2007 N ALA A1079 -7.056 246.041 166.855 1.00118.83 N
ANISOU 2007 N ALA A1079 10957 13524 20669 2823 1795 -1223 N
ATOM 2008 CA ALA A1079 -8.329 245.372 167.112 1.00119.98 C
ANISOU 2008 CA ALA A1079 10935 13838 20816 2845 1901 -787 C
ATOM 2009 C ALA A1079 -8.846 245.728 168.519 1.00120.99 C
ANISOU 2009 C ALA A1079 10865 14304 20803 3167 2272 -1039 C
ATOM 2010 O ALA A1079 -10.007 246.116 168.664 1.00121.09 O
ANISOU 2010 O ALA A1079 10583 14273 21153 3272 2475 -858 O
ATOM 2011 CB ALA A1079 -8.171 243.863 166.964 1.00120.19 C
ANISOU 2011 CB ALA A1079 11150 14037 20478 2681 1747 -427 C
ATOM 2012 N ASN A1080 -7.961 245.687 169.535 1.00121.49 N
ANISOU 2012 N ASN A1080 11086 14697 20377 3347 2355 -1488 N
ATOM 2013 CA ASN A1080 -8.315 246.032 170.916 1.00122.40 C
ANISOU 2013 CA ASN A1080 11105 15202 20200 3697 2702 -1812 C
ATOM 2014 C ASN A1080 -8.707 247.504 171.091 1.00122.96 C
ANISOU 2014 C ASN A1080 10959 15043 20718 3892 2886 -2256 C
ATOM 2015 O ASN A1080 -9.423 247.838 172.031 1.00123.10 O
ANISOU 2015 O ASN A1080 10824 15305 20641 4188 3246 -2412 O
ATOM 2016 CB ASN A1080 -7.209 245.624 171.885 1.00123.73 C
ANISOU 2016 CB ASN A1080 11534 15785 19693 3841 2643 -2194 C
ATOM 2017 CG ASN A1080 -7.005 244.127 171.956 1.00126.98 C
ANISOU 2017 CG ASN A1080 12116 16453 19678 3721 2540 -1712 C
ATOM 2018 OD1 ASN A1080 -7.957 243.338 171.909 1.00128.14 O
ANISOU 2018 OD1 ASN A1080 12152 16661 19872 3655 2674 -1132 O
ATOM 2019 ND2 ASN A1080 -5.751 243.701 172.054 1.00127.55 N
ANISOU 2019 ND2 ASN A1080 12424 16633 19408 3684 2284 -1931 N
ATOM 2020 N GLU A1081 -8.257 248.374 170.184 1.00123.30 N
ANISOU 2020 N GLU A1081 10980 14598 21268 3742 2674 -2437 N
ATOM 2021 CA GLU A1081 -8.643 249.782 170.168 1.00124.27 C
ANISOU 2021 CA GLU A1081 10869 14371 21978 3890 2812 -2786 C
ATOM 2022 C GLU A1081 -9.962 250.026 169.385 1.00125.07 C
ANISOU 2022 C GLU A1081 10668 14167 22688 3833 2894 -2251 C
ATOM 2023 O GLU A1081 -10.388 251.176 169.266 1.00125.33 O
ANISOU 2023 O GLU A1081 10463 13856 23299 3962 3012 -2446 O
ATOM 2024 CB GLU A1081 -7.528 250.637 169.554 1.00126.47 C
ANISOU 2024 CB GLU A1081 11223 14220 22611 3750 2561 -3152 C
ATOM 2025 CG GLU A1081 -6.300 250.761 170.435 1.00131.43 C
ANISOU 2025 CG GLU A1081 12027 15066 22845 3860 2471 -3829 C
ATOM 2026 CD GLU A1081 -5.049 251.262 169.735 1.00137.61 C
ANISOU 2026 CD GLU A1081 12870 15451 23966 3650 2198 -4057 C
ATOM 2027 OE1 GLU A1081 -3.976 251.272 170.382 1.00138.42 O
ANISOU 2027 OE1 GLU A1081 13094 15728 23770 3688 2043 -4535 O
ATOM 2028 OE2 GLU A1081 -5.133 251.629 168.541 1.00139.91 O
ANISOU 2028 OE2 GLU A1081 13072 15263 24825 3456 2139 -3726 O
ATOM 2029 N GLY A1082 -10.576 248.968 168.849 1.00125.21 N
ANISOU 2029 N GLY A1082 10673 14275 22627 3645 2796 -1597 N
ATOM 2030 CA GLY A1082 -11.809 249.055 168.076 1.00125.70 C
ANISOU 2030 CA GLY A1082 10434 14073 23254 3563 2773 -1051 C
ATOM 2031 C GLY A1082 -11.626 249.590 166.668 1.00125.87 C
ANISOU 2031 C GLY A1082 10484 13592 23748 3328 2421 -825 C
ATOM 2032 O GLY A1082 -12.595 250.029 166.044 1.00126.13 O
ANISOU 2032 O GLY A1082 10241 13345 24336 3311 2363 -459 O
ATOM 2033 N LYS A1083 -10.383 249.558 166.151 1.00125.46 N
ANISOU 2033 N LYS A1083 10755 13433 23482 3162 2191 -1006 N
ATOM 2034 CA LYS A1083 -10.065 250.047 164.810 1.00125.39 C
ANISOU 2034 CA LYS A1083 10834 12990 23819 2961 1913 -775 C
ATOM 2035 C LYS A1083 -10.043 248.858 163.858 1.00125.16 C
ANISOU 2035 C LYS A1083 11049 13028 23476 2685 1594 -282 C
ATOM 2036 O LYS A1083 -8.982 248.326 163.557 1.00125.36 O
ANISOU 2036 O LYS A1083 11396 13117 23118 2547 1469 -373 O
ATOM 2037 CB LYS A1083 -8.709 250.778 164.821 1.00127.01 C
ANISOU 2037 CB LYS A1083 11203 13013 24041 2958 1918 -1260 C
ATOM 2038 CG LYS A1083 -8.613 251.861 165.895 1.00130.51 C
ANISOU 2038 CG LYS A1083 11438 13400 24750 3233 2189 -1888 C
ATOM 2039 CD LYS A1083 -7.272 252.576 165.882 1.00134.10 C
ANISOU 2039 CD LYS A1083 11996 13611 25346 3193 2136 -2367 C
ATOM 2040 CE LYS A1083 -7.236 253.704 166.882 1.00137.28 C
ANISOU 2040 CE LYS A1083 12184 13878 26098 3457 2340 -3041 C
ATOM 2041 NZ LYS A1083 -5.910 254.374 166.907 1.00139.19 N
ANISOU 2041 NZ LYS A1083 12478 13855 26554 3392 2242 -3537 N
ATOM 2042 N VAL A1084 -11.220 248.435 163.405 1.00124.55 N
ANISOU 2042 N VAL A1084 10799 12923 23600 2615 1453 212 N
ATOM 2043 CA VAL A1084 -11.396 247.257 162.559 1.00124.58 C
ANISOU 2043 CA VAL A1084 11007 12977 23351 2361 1106 640 C
ATOM 2044 C VAL A1084 -10.700 247.378 161.208 1.00124.09 C
ANISOU 2044 C VAL A1084 11275 12660 23214 2176 797 781 C
ATOM 2045 O VAL A1084 -9.870 246.535 160.880 1.00124.28 O
ANISOU 2045 O VAL A1084 11652 12787 22780 2033 673 744 O
ATOM 2046 CB VAL A1084 -12.886 246.855 162.382 1.00125.57 C
ANISOU 2046 CB VAL A1084 10805 13090 23816 2319 972 1117 C
ATOM 2047 CG1 VAL A1084 -12.999 245.420 161.888 1.00126.24 C
ANISOU 2047 CG1 VAL A1084 11091 13288 23586 2073 655 1416 C
ATOM 2048 CG2 VAL A1084 -13.703 247.068 163.659 1.00126.12 C
ANISOU 2048 CG2 VAL A1084 10456 13349 24114 2566 1392 1026 C
ATOM 2049 N LYS A1085 -11.023 248.421 160.430 1.00123.55 N
ANISOU 2049 N LYS A1085 11096 12260 23586 2200 699 968 N
ATOM 2050 CA LYS A1085 -10.443 248.637 159.103 1.00123.50 C
ANISOU 2050 CA LYS A1085 11409 12029 23489 2060 451 1183 C
ATOM 2051 C LYS A1085 -8.913 248.726 159.159 1.00123.43 C
ANISOU 2051 C LYS A1085 11701 12026 23169 2036 633 825 C
ATOM 2052 O LYS A1085 -8.217 248.153 158.320 1.00123.35 O
ANISOU 2052 O LYS A1085 12064 12030 22774 1891 483 938 O
ATOM 2053 CB LYS A1085 -11.026 249.913 158.473 1.00125.00 C
ANISOU 2053 CB LYS A1085 11370 11855 24269 2151 397 1447 C
ATOM 2054 CG LYS A1085 -12.549 249.982 158.490 1.00128.20 C
ANISOU 2054 CG LYS A1085 11387 12214 25109 2203 219 1804 C
ATOM 2055 CD LYS A1085 -13.179 249.378 157.246 1.00131.71 C
ANISOU 2055 CD LYS A1085 12000 12597 25446 2032 -310 2329 C
ATOM 2056 CE LYS A1085 -14.644 249.747 157.162 1.00134.59 C
ANISOU 2056 CE LYS A1085 11896 12809 26431 2110 -517 2712 C
ATOM 2057 NZ LYS A1085 -15.171 249.666 155.775 1.00136.35 N
ANISOU 2057 NZ LYS A1085 12285 12904 26616 1991 -1089 3220 N
ATOM 2058 N GLU A1086 -8.398 249.433 160.162 1.00123.14 N
ANISOU 2058 N GLU A1086 11488 11979 23321 2188 950 369 N
ATOM 2059 CA GLU A1086 -6.967 249.597 160.368 1.00123.25 C
ANISOU 2059 CA GLU A1086 11678 11976 23174 2174 1107 -15 C
ATOM 2060 C GLU A1086 -6.319 248.270 160.754 1.00122.77 C
ANISOU 2060 C GLU A1086 11867 12269 22510 2097 1071 -169 C
ATOM 2061 O GLU A1086 -5.207 247.993 160.318 1.00122.71 O
ANISOU 2061 O GLU A1086 12109 12238 22278 2006 1071 -250 O
ATOM 2062 CB GLU A1086 -6.727 250.641 161.456 1.00125.73 C
ANISOU 2062 CB GLU A1086 11702 12187 23882 2366 1374 -520 C
ATOM 2063 CG GLU A1086 -5.342 251.248 161.430 1.00130.56 C
ANISOU 2063 CG GLU A1086 12381 12592 24634 2336 1484 -856 C
ATOM 2064 CD GLU A1086 -5.189 252.420 162.376 1.00136.49 C
ANISOU 2064 CD GLU A1086 12829 13160 25870 2517 1677 -1398 C
ATOM 2065 OE1 GLU A1086 -6.210 253.079 162.680 1.00137.00 O
ANISOU 2065 OE1 GLU A1086 12632 13111 26310 2672 1757 -1403 O
ATOM 2066 OE2 GLU A1086 -4.044 252.687 162.807 1.00139.10 O
ANISOU 2066 OE2 GLU A1086 13169 13440 26244 2509 1734 -1842 O
ATOM 2067 N ALA A1087 -7.020 247.441 161.547 1.00122.35 N
ANISOU 2067 N ALA A1087 11726 12523 22237 2142 1064 -161 N
ATOM 2068 CA ALA A1087 -6.525 246.123 161.943 1.00122.39 C
ANISOU 2068 CA ALA A1087 11943 12838 21723 2081 1019 -226 C
ATOM 2069 C ALA A1087 -6.473 245.185 160.742 1.00122.05 C
ANISOU 2069 C ALA A1087 12214 12729 21430 1872 746 128 C
ATOM 2070 O ALA A1087 -5.507 244.440 160.602 1.00122.23 O
ANISOU 2070 O ALA A1087 12499 12832 21110 1805 725 18 O
ATOM 2071 CB ALA A1087 -7.400 245.523 163.035 1.00122.50 C
ANISOU 2071 CB ALA A1087 11758 13161 21626 2186 1115 -197 C
ATOM 2072 N GLN A1088 -7.489 245.236 159.862 1.00121.48 N
ANISOU 2072 N GLN A1088 12114 12503 21538 1786 517 527 N
ATOM 2073 CA GLN A1088 -7.518 244.408 158.656 1.00121.24 C
ANISOU 2073 CA GLN A1088 12416 12405 21247 1603 195 817 C
ATOM 2074 C GLN A1088 -6.384 244.803 157.697 1.00120.61 C
ANISOU 2074 C GLN A1088 12663 12163 20998 1567 240 768 C
ATOM 2075 O GLN A1088 -5.784 243.931 157.069 1.00120.76 O
ANISOU 2075 O GLN A1088 13038 12219 20625 1471 137 778 O
ATOM 2076 CB GLN A1088 -8.882 244.504 157.960 1.00123.00 C
ANISOU 2076 CB GLN A1088 12497 12502 21736 1539 -123 1230 C
ATOM 2077 CG GLN A1088 -10.023 243.926 158.781 1.00127.00 C
ANISOU 2077 CG GLN A1088 12657 13148 22449 1544 -158 1355 C
ATOM 2078 CD GLN A1088 -11.371 244.256 158.179 1.00132.25 C
ANISOU 2078 CD GLN A1088 13057 13653 23537 1505 -456 1748 C
ATOM 2079 OE1 GLN A1088 -11.770 245.422 158.079 1.00134.00 O
ANISOU 2079 OE1 GLN A1088 13055 13712 24145 1619 -396 1835 O
ATOM 2080 NE2 GLN A1088 -12.112 243.237 157.769 1.00133.22 N
ANISOU 2080 NE2 GLN A1088 13161 13787 23669 1343 -808 1997 N
ATOM 2081 N ALA A1089 -6.066 246.106 157.614 1.00119.59 N
ANISOU 2081 N ALA A1089 12399 11838 21203 1656 434 711 N
ATOM 2082 CA ALA A1089 -4.970 246.585 156.774 1.00119.16 C
ANISOU 2082 CA ALA A1089 12584 11607 21084 1632 562 720 C
ATOM 2083 C ALA A1089 -3.632 246.121 157.346 1.00118.59 C
ANISOU 2083 C ALA A1089 12604 11652 20804 1639 782 337 C
ATOM 2084 O ALA A1089 -2.754 245.703 156.593 1.00118.63 O
ANISOU 2084 O ALA A1089 12912 11627 20533 1580 832 375 O
ATOM 2085 CB ALA A1089 -5.003 248.100 156.680 1.00119.20 C
ANISOU 2085 CB ALA A1089 12339 11318 21632 1721 729 772 C
ATOM 2086 N ALA A1090 -3.484 246.161 158.676 1.00118.08 N
ANISOU 2086 N ALA A1090 12280 11736 20851 1731 908 -30 N
ATOM 2087 CA ALA A1090 -2.272 245.687 159.344 1.00118.01 C
ANISOU 2087 CA ALA A1090 12310 11868 20661 1756 1043 -396 C
ATOM 2088 C ALA A1090 -2.083 244.188 159.131 1.00117.67 C
ANISOU 2088 C ALA A1090 12555 12017 20137 1679 906 -309 C
ATOM 2089 O ALA A1090 -0.956 243.724 158.985 1.00117.64 O
ANISOU 2089 O ALA A1090 12705 12026 19968 1665 994 -452 O
ATOM 2090 CB ALA A1090 -2.349 245.982 160.832 1.00118.33 C
ANISOU 2090 CB ALA A1090 12050 12089 20821 1899 1131 -780 C
ATOM 2091 N ALA A1091 -3.184 243.429 159.130 1.00117.20 N
ANISOU 2091 N ALA A1091 12528 12073 19930 1633 696 -79 N
ATOM 2092 CA ALA A1091 -3.148 241.987 158.922 1.00117.23 C
ANISOU 2092 CA ALA A1091 12779 12189 19576 1547 530 15 C
ATOM 2093 C ALA A1091 -2.768 241.625 157.488 1.00117.05 C
ANISOU 2093 C ALA A1091 13146 12002 19323 1446 427 168 C
ATOM 2094 O ALA A1091 -2.180 240.572 157.269 1.00117.20 O
ANISOU 2094 O ALA A1091 13411 12057 19063 1413 398 96 O
ATOM 2095 CB ALA A1091 -4.488 241.369 159.286 1.00117.35 C
ANISOU 2095 CB ALA A1091 12658 12302 19629 1504 331 245 C
ATOM 2096 N GLU A1092 -3.082 242.487 156.513 1.00116.72 N
ANISOU 2096 N GLU A1092 13180 11788 19382 1423 387 382 N
ATOM 2097 CA GLU A1092 -2.708 242.237 155.121 1.00116.87 C
ANISOU 2097 CA GLU A1092 13620 11700 19085 1368 321 538 C
ATOM 2098 C GLU A1092 -1.179 242.206 154.940 1.00116.43 C
ANISOU 2098 C GLU A1092 13718 11612 18908 1418 656 335 C
ATOM 2099 O GLU A1092 -0.678 241.519 154.053 1.00116.48 O
ANISOU 2099 O GLU A1092 14104 11605 18547 1401 660 356 O
ATOM 2100 CB GLU A1092 -3.343 243.275 154.192 1.00119.74 C
ANISOU 2100 CB GLU A1092 14015 11911 19568 1367 225 868 C
ATOM 2101 CG GLU A1092 -3.667 242.728 152.816 1.00125.47 C
ANISOU 2101 CG GLU A1092 15190 12624 19857 1302 -82 1106 C
ATOM 2102 CD GLU A1092 -4.807 241.727 152.800 1.00133.10 C
ANISOU 2102 CD GLU A1092 16172 13662 20739 1196 -538 1154 C
ATOM 2103 OE1 GLU A1092 -5.768 241.902 153.584 1.00134.41 O
ANISOU 2103 OE1 GLU A1092 15943 13839 21289 1180 -666 1239 O
ATOM 2104 OE2 GLU A1092 -4.740 240.767 151.999 1.00135.93 O
ANISOU 2104 OE2 GLU A1092 16918 14041 20688 1134 -753 1095 O
ATOM 2105 N GLN A1093 -0.436 242.926 155.790 1.00115.86 N
ANISOU 2105 N GLN A1093 13336 11520 19165 1489 931 111 N
ATOM 2106 CA GLN A1093 1.025 242.915 155.741 1.00115.74 C
ANISOU 2106 CA GLN A1093 13359 11454 19162 1530 1236 -83 C
ATOM 2107 C GLN A1093 1.582 241.519 156.007 1.00115.24 C
ANISOU 2107 C GLN A1093 13458 11531 18796 1538 1192 -262 C
ATOM 2108 O GLN A1093 2.654 241.196 155.506 1.00115.31 O
ANISOU 2108 O GLN A1093 13630 11482 18700 1569 1407 -331 O
ATOM 2109 CB GLN A1093 1.613 243.906 156.757 1.00117.54 C
ANISOU 2109 CB GLN A1093 13164 11625 19871 1590 1429 -351 C
ATOM 2110 CG GLN A1093 1.005 245.305 156.682 1.00121.05 C
ANISOU 2110 CG GLN A1093 13377 11879 20736 1599 1464 -229 C
ATOM 2111 CD GLN A1093 1.218 245.953 155.338 1.00125.07 C
ANISOU 2111 CD GLN A1093 14078 12156 21285 1569 1618 133 C
ATOM 2112 OE1 GLN A1093 2.325 246.375 154.997 1.00126.67 O
ANISOU 2112 OE1 GLN A1093 14293 12212 21622 1572 1919 134 O
ATOM 2113 NE2 GLN A1093 0.156 246.051 154.548 1.00125.34 N
ANISOU 2113 NE2 GLN A1093 14249 12156 21218 1550 1419 485 N
ATOM 2114 N LEU A1094 0.853 240.690 156.781 1.00114.58 N
ANISOU 2114 N LEU A1094 13310 11610 18616 1522 946 -303 N
ATOM 2115 CA LEU A1094 1.234 239.322 157.103 1.00114.55 C
ANISOU 2115 CA LEU A1094 13430 11702 18391 1531 869 -414 C
ATOM 2116 C LEU A1094 1.483 238.481 155.856 1.00114.75 C
ANISOU 2116 C LEU A1094 13896 11614 18089 1493 836 -344 C
ATOM 2117 O LEU A1094 2.336 237.604 155.884 1.00114.95 O
ANISOU 2117 O LEU A1094 14036 11629 18013 1544 932 -496 O
ATOM 2118 CB LEU A1094 0.150 238.662 157.954 1.00114.38 C
ANISOU 2118 CB LEU A1094 13275 11826 18358 1500 616 -330 C
ATOM 2119 CG LEU A1094 0.012 239.215 159.350 1.00115.52 C
ANISOU 2119 CG LEU A1094 13041 12156 18697 1592 686 -458 C
ATOM 2120 CD1 LEU A1094 -1.273 238.764 159.987 1.00116.11 C
ANISOU 2120 CD1 LEU A1094 12983 12361 18772 1566 511 -270 C
ATOM 2121 CD2 LEU A1094 1.167 238.797 160.199 1.00116.01 C
ANISOU 2121 CD2 LEU A1094 13015 12342 18724 1699 795 -704 C
ATOM 2122 N LYS A1095 0.751 238.745 154.769 1.00114.69 N
ANISOU 2122 N LYS A1095 14144 11525 17909 1426 688 -133 N
ATOM 2123 CA LYS A1095 0.878 238.014 153.504 1.00115.06 C
ANISOU 2123 CA LYS A1095 14676 11490 17551 1412 616 -108 C
ATOM 2124 C LYS A1095 2.293 238.140 152.910 1.00115.54 C
ANISOU 2124 C LYS A1095 14909 11492 17500 1522 1045 -220 C
ATOM 2125 O LYS A1095 2.862 237.151 152.452 1.00115.60 O
ANISOU 2125 O LYS A1095 15205 11459 17257 1572 1109 -370 O
ATOM 2126 CB LYS A1095 -0.200 238.523 152.528 1.00116.45 C
ANISOU 2126 CB LYS A1095 15056 11632 17558 1343 338 159 C
ATOM 2127 CG LYS A1095 -0.295 237.831 151.185 1.00119.48 C
ANISOU 2127 CG LYS A1095 16000 11971 17426 1350 210 179 C
ATOM 2128 CD LYS A1095 -1.661 238.080 150.548 1.00122.51 C
ANISOU 2128 CD LYS A1095 16512 12352 17683 1261 -266 425 C
ATOM 2129 CE LYS A1095 -1.838 237.331 149.253 1.00125.25 C
ANISOU 2129 CE LYS A1095 17455 12687 17448 1270 -517 374 C
ATOM 2130 NZ LYS A1095 -3.235 237.427 148.756 1.00126.86 N
ANISOU 2130 NZ LYS A1095 17722 12883 17597 1156 -1131 557 N
ATOM 2131 N THR A1096 2.878 239.339 152.971 1.00115.60 N
ANISOU 2131 N THR A1096 14690 11463 17772 1566 1361 -159 N
ATOM 2132 CA THR A1096 4.229 239.564 152.468 1.00116.19 C
ANISOU 2132 CA THR A1096 14819 11456 17873 1662 1823 -211 C
ATOM 2133 C THR A1096 5.236 238.740 153.261 1.00116.18 C
ANISOU 2133 C THR A1096 14644 11473 18026 1728 1951 -504 C
ATOM 2134 O THR A1096 6.129 238.139 152.674 1.00116.39 O
ANISOU 2134 O THR A1096 14882 11443 17895 1818 2212 -590 O
ATOM 2135 CB THR A1096 4.571 241.053 152.543 1.00117.89 C
ANISOU 2135 CB THR A1096 14704 11571 18518 1663 2087 -77 C
ATOM 2136 OG1 THR A1096 4.622 241.445 153.919 1.00119.13 O
ANISOU 2136 OG1 THR A1096 14376 11760 19128 1646 2006 -295 O
ATOM 2137 CG2 THR A1096 3.574 241.921 151.777 1.00118.33 C
ANISOU 2137 CG2 THR A1096 14879 11585 18497 1616 1936 265 C
ATOM 2138 N THR A1097 5.084 238.703 154.591 1.00115.89 N
ANISOU 2138 N THR A1097 14228 11526 18279 1709 1769 -646 N
ATOM 2139 CA THR A1097 5.974 237.930 155.458 1.00116.12 C
ANISOU 2139 CA THR A1097 14060 11603 18459 1787 1810 -880 C
ATOM 2140 C THR A1097 5.798 236.430 155.243 1.00115.61 C
ANISOU 2140 C THR A1097 14297 11532 18099 1805 1640 -924 C
ATOM 2141 O THR A1097 6.770 235.680 155.264 1.00115.59 O
ANISOU 2141 O THR A1097 14302 11472 18143 1905 1795 -1068 O
ATOM 2142 CB THR A1097 5.722 238.277 156.921 1.00117.83 C
ANISOU 2142 CB THR A1097 13858 11969 18944 1786 1623 -991 C
ATOM 2143 OG1 THR A1097 5.797 239.695 157.088 1.00118.79 O
ANISOU 2143 OG1 THR A1097 13709 12039 19388 1766 1751 -1005 O
ATOM 2144 CG2 THR A1097 6.700 237.578 157.864 1.00118.47 C
ANISOU 2144 CG2 THR A1097 13719 12131 19165 1891 1621 -1200 C
ATOM 2145 N ARG A1098 4.557 235.996 155.036 1.00115.08 N
ANISOU 2145 N ARG A1098 14440 11483 17802 1707 1309 -801 N
ATOM 2146 CA ARG A1098 4.242 234.599 154.797 1.00114.97 C
ANISOU 2146 CA ARG A1098 14703 11394 17585 1692 1092 -848 C
ATOM 2147 C ARG A1098 4.898 234.128 153.500 1.00115.05 C
ANISOU 2147 C ARG A1098 15151 11259 17303 1770 1303 -957 C
ATOM 2148 O ARG A1098 5.498 233.059 153.471 1.00115.09 O
ANISOU 2148 O ARG A1098 15275 11157 17296 1853 1358 -1125 O
ATOM 2149 CB ARG A1098 2.724 234.418 154.740 1.00115.78 C
ANISOU 2149 CB ARG A1098 14885 11511 17594 1545 680 -678 C
ATOM 2150 CG ARG A1098 2.289 232.998 154.500 1.00117.78 C
ANISOU 2150 CG ARG A1098 15386 11624 17741 1492 399 -729 C
ATOM 2151 CD ARG A1098 0.921 232.973 153.881 1.00119.82 C
ANISOU 2151 CD ARG A1098 15825 11831 17871 1338 3 -589 C
ATOM 2152 NE ARG A1098 0.923 233.609 152.567 1.00121.57 N
ANISOU 2152 NE ARG A1098 16401 12043 17747 1355 50 -579 N
ATOM 2153 CZ ARG A1098 -0.162 234.064 151.953 1.00123.05 C
ANISOU 2153 CZ ARG A1098 16704 12241 17809 1252 -271 -408 C
ATOM 2154 NH1 ARG A1098 -1.352 233.971 152.533 1.00122.19 N
ANISOU 2154 NH1 ARG A1098 16341 12127 17958 1111 -645 -249 N
ATOM 2155 NH2 ARG A1098 -0.066 234.615 150.753 1.00123.17 N
ANISOU 2155 NH2 ARG A1098 17073 12275 17451 1302 -213 -359 N
ATOM 2156 N ASN A1099 4.843 234.949 152.453 1.00114.91 N
ANISOU 2156 N ASN A1099 15366 11239 17055 1772 1462 -852 N
ATOM 2157 CA ASN A1099 5.444 234.601 151.169 1.00115.25 C
ANISOU 2157 CA ASN A1099 15872 11199 16718 1884 1725 -937 C
ATOM 2158 C ASN A1099 6.977 234.644 151.201 1.00115.16 C
ANISOU 2158 C ASN A1099 15706 11135 16915 2046 2262 -1058 C
ATOM 2159 O ASN A1099 7.629 233.729 150.699 1.00115.32 O
ANISOU 2159 O ASN A1099 15978 11056 16783 2174 2444 -1253 O
ATOM 2160 CB ASN A1099 4.905 235.514 150.065 1.00116.49 C
ANISOU 2160 CB ASN A1099 16326 11411 16523 1861 1745 -708 C
ATOM 2161 CG ASN A1099 3.411 235.432 149.914 1.00119.73 C
ANISOU 2161 CG ASN A1099 16881 11856 16756 1713 1177 -588 C
ATOM 2162 OD1 ASN A1099 2.779 234.446 150.311 1.00121.06 O
ANISOU 2162 OD1 ASN A1099 17060 11971 16965 1628 787 -712 O
ATOM 2163 ND2 ASN A1099 2.812 236.471 149.348 1.00120.21 N
ANISOU 2163 ND2 ASN A1099 17009 11979 16684 1678 1115 -310 N
ATOM 2164 N ALA A1100 7.552 235.697 151.787 1.00114.73 N
ANISOU 2164 N ALA A1100 15213 11116 17265 2045 2507 -965 N
ATOM 2165 CA ALA A1100 9.003 235.854 151.816 1.00114.73 C
ANISOU 2165 CA ALA A1100 14975 11040 17578 2178 2998 -1050 C
ATOM 2166 C ALA A1100 9.715 234.970 152.824 1.00114.41 C
ANISOU 2166 C ALA A1100 14632 10968 17869 2251 2936 -1270 C
ATOM 2167 O ALA A1100 10.882 234.650 152.619 1.00114.27 O
ANISOU 2167 O ALA A1100 14540 10851 18026 2397 3306 -1378 O
ATOM 2168 CB ALA A1100 9.368 237.309 152.054 1.00114.87 C
ANISOU 2168 CB ALA A1100 14591 11050 18005 2129 3226 -893 C
ATOM 2169 N TYR A1101 9.039 234.589 153.915 1.00114.12 N
ANISOU 2169 N TYR A1101 14404 11020 17935 2172 2493 -1301 N
ATOM 2170 CA TYR A1101 9.688 233.811 154.966 1.00114.17 C
ANISOU 2170 CA TYR A1101 14105 11030 18244 2258 2399 -1438 C
ATOM 2171 C TYR A1101 9.023 232.481 155.317 1.00113.75 C
ANISOU 2171 C TYR A1101 14227 10950 18042 2247 2039 -1457 C
ATOM 2172 O TYR A1101 9.654 231.433 155.197 1.00113.93 O
ANISOU 2172 O TYR A1101 14320 10829 18138 2371 2116 -1572 O
ATOM 2173 CB TYR A1101 9.844 234.658 156.249 1.00114.44 C
ANISOU 2173 CB TYR A1101 13618 11219 18647 2225 2268 -1446 C
ATOM 2174 CG TYR A1101 10.640 235.930 156.077 1.00115.33 C
ANISOU 2174 CG TYR A1101 13443 11281 19094 2227 2595 -1462 C
ATOM 2175 CD1 TYR A1101 10.021 237.116 155.713 1.00116.25 C
ANISOU 2175 CD1 TYR A1101 13574 11403 19195 2113 2638 -1333 C
ATOM 2176 CD2 TYR A1101 12.007 235.955 156.315 1.00116.27 C
ANISOU 2176 CD2 TYR A1101 13231 11311 19634 2340 2854 -1584 C
ATOM 2177 CE1 TYR A1101 10.747 238.288 155.558 1.00117.26 C
ANISOU 2177 CE1 TYR A1101 13411 11419 19725 2102 2949 -1316 C
ATOM 2178 CE2 TYR A1101 12.742 237.122 156.171 1.00117.21 C
ANISOU 2178 CE2 TYR A1101 13030 11331 20175 2318 3157 -1580 C
ATOM 2179 CZ TYR A1101 12.108 238.291 155.799 1.00118.27 C
ANISOU 2179 CZ TYR A1101 13193 11444 20301 2192 3208 -1444 C
ATOM 2180 OH TYR A1101 12.832 239.450 155.652 1.00120.06 O
ANISOU 2180 OH TYR A1101 13071 11510 21036 2157 3515 -1412 O
ATOM 2181 N ILE A1102 7.779 232.524 155.788 1.00112.98 N
ANISOU 2181 N ILE A1102 14146 10959 17821 2107 1668 -1326 N
ATOM 2182 CA ILE A1102 7.075 231.370 156.331 1.00112.94 C
ANISOU 2182 CA ILE A1102 14194 10920 17797 2070 1326 -1270 C
ATOM 2183 C ILE A1102 6.971 230.200 155.356 1.00112.77 C
ANISOU 2183 C ILE A1102 14607 10641 17599 2085 1282 -1378 C
ATOM 2184 O ILE A1102 7.204 229.059 155.755 1.00112.95 O
ANISOU 2184 O ILE A1102 14608 10522 17785 2147 1176 -1409 O
ATOM 2185 CB ILE A1102 5.697 231.765 156.907 1.00113.45 C
ANISOU 2185 CB ILE A1102 14156 11143 17808 1914 1005 -1072 C
ATOM 2186 CG1 ILE A1102 5.783 233.055 157.759 1.00114.65 C
ANISOU 2186 CG1 ILE A1102 13923 11532 18105 1924 1074 -1047 C
ATOM 2187 CG2 ILE A1102 5.102 230.621 157.720 1.00113.85 C
ANISOU 2187 CG2 ILE A1102 14145 11168 17947 1884 715 -940 C
ATOM 2188 CD1 ILE A1102 6.758 232.973 158.933 1.00116.00 C
ANISOU 2188 CD1 ILE A1102 13734 11832 18509 2068 1126 -1142 C
ATOM 2189 N GLN A1103 6.665 230.470 154.088 1.00112.37 N
ANISOU 2189 N GLN A1103 14958 10521 17218 2049 1359 -1444 N
ATOM 2190 CA GLN A1103 6.557 229.410 153.087 1.00112.41 C
ANISOU 2190 CA GLN A1103 15435 10287 16987 2082 1295 -1637 C
ATOM 2191 C GLN A1103 7.905 228.713 152.866 1.00111.99 C
ANISOU 2191 C GLN A1103 15416 10063 17072 2306 1665 -1860 C
ATOM 2192 O GLN A1103 7.932 227.500 152.666 1.00111.95 O
ANISOU 2192 O GLN A1103 15620 9807 17107 2360 1552 -2033 O
ATOM 2193 CB GLN A1103 5.927 229.955 151.788 1.00114.34 C
ANISOU 2193 CB GLN A1103 16133 10564 16749 2023 1264 -1655 C
ATOM 2194 CG GLN A1103 6.226 229.194 150.488 1.00118.47 C
ANISOU 2194 CG GLN A1103 17228 10904 16884 2142 1363 -1949 C
ATOM 2195 CD GLN A1103 5.320 228.012 150.232 1.00123.56 C
ANISOU 2195 CD GLN A1103 18164 11325 17460 2035 856 -2114 C
ATOM 2196 OE1 GLN A1103 4.440 227.678 151.036 1.00125.44 O
ANISOU 2196 OE1 GLN A1103 18137 11515 18011 1862 449 -1961 O
ATOM 2197 NE2 GLN A1103 5.521 227.351 149.094 1.00124.05 N
ANISOU 2197 NE2 GLN A1103 18776 11234 17123 2142 882 -2440 N
ATOM 2198 N LYS A1104 9.020 229.455 152.967 1.00111.50 N
ANISOU 2198 N LYS A1104 15090 10097 17179 2434 2091 -1852 N
ATOM 2199 CA LYS A1104 10.346 228.862 152.819 1.00111.69 C
ANISOU 2199 CA LYS A1104 15039 9960 17440 2660 2467 -2029 C
ATOM 2200 C LYS A1104 10.628 227.888 153.956 1.00111.15 C
ANISOU 2200 C LYS A1104 14659 9787 17786 2710 2223 -2007 C
ATOM 2201 O LYS A1104 11.174 226.813 153.720 1.00111.41 O
ANISOU 2201 O LYS A1104 14813 9561 17956 2859 2305 -2174 O
ATOM 2202 CB LYS A1104 11.429 229.943 152.777 1.00114.18 C
ANISOU 2202 CB LYS A1104 15019 10387 17977 2752 2931 -1976 C
ATOM 2203 CG LYS A1104 11.335 230.851 151.569 1.00119.48 C
ANISOU 2203 CG LYS A1104 15996 11122 18279 2749 3284 -1931 C
ATOM 2204 CD LYS A1104 12.432 231.904 151.607 1.00124.94 C
ANISOU 2204 CD LYS A1104 16261 11868 19344 2811 3745 -1828 C
ATOM 2205 CE LYS A1104 12.381 232.850 150.431 1.00129.56 C
ANISOU 2205 CE LYS A1104 17118 12500 19608 2821 4162 -1687 C
ATOM 2206 NZ LYS A1104 12.880 234.208 150.798 1.00132.02 N
ANISOU 2206 NZ LYS A1104 16936 12864 20363 2751 4385 -1490 N
ATOM 2207 N TYR A1105 10.239 228.250 155.185 1.00110.26 N
ANISOU 2207 N TYR A1105 14222 9855 17815 2585 1881 -1791 N
ATOM 2208 CA TYR A1105 10.424 227.367 156.332 1.00109.80 C
ANISOU 2208 CA TYR A1105 13894 9743 18083 2642 1635 -1681 C
ATOM 2209 C TYR A1105 9.562 226.124 156.163 1.00108.66 C
ANISOU 2209 C TYR A1105 14020 9325 17940 2578 1328 -1665 C
ATOM 2210 O TYR A1105 10.040 225.014 156.369 1.00108.10 O
ANISOU 2210 O TYR A1105 13826 9057 18189 2695 1260 -1626 O
ATOM 2211 CB TYR A1105 10.075 228.085 157.650 1.00110.10 C
ANISOU 2211 CB TYR A1105 13531 10108 18195 2565 1408 -1451 C
ATOM 2212 CG TYR A1105 10.111 227.164 158.851 1.00111.25 C
ANISOU 2212 CG TYR A1105 13388 10279 18601 2662 1184 -1272 C
ATOM 2213 CD1 TYR A1105 11.286 226.531 159.231 1.00112.26 C
ANISOU 2213 CD1 TYR A1105 13286 10311 19057 2880 1309 -1326 C
ATOM 2214 CD2 TYR A1105 8.961 226.894 159.581 1.00112.31 C
ANISOU 2214 CD2 TYR A1105 13462 10541 18669 2554 862 -1003 C
ATOM 2215 CE1 TYR A1105 11.322 225.665 160.317 1.00113.26 C
ANISOU 2215 CE1 TYR A1105 13160 10476 19397 2993 1075 -1105 C
ATOM 2216 CE2 TYR A1105 8.985 226.031 160.672 1.00113.33 C
ANISOU 2216 CE2 TYR A1105 13352 10722 18987 2666 687 -765 C
ATOM 2217 CZ TYR A1105 10.170 225.419 161.040 1.00114.28 C
ANISOU 2217 CZ TYR A1105 13277 10755 19390 2888 772 -811 C
ATOM 2218 OH TYR A1105 10.211 224.563 162.118 1.00115.85 O
ANISOU 2218 OH TYR A1105 13246 11018 19753 3022 569 -520 O
ATOM 2219 N LEU A1106 8.300 226.307 155.754 1.00107.99 N
ANISOU 2219 N LEU A1106 14271 9201 17560 2393 1120 -1684 N
ATOM 2220 CA LEU A1106 7.372 225.205 155.536 1.00107.49 C
ANISOU 2220 CA LEU A1106 14439 8848 17555 2279 771 -1690 C
ATOM 2221 C LEU A1106 7.931 224.213 154.519 1.00106.99 C
ANISOU 2221 C LEU A1106 14761 8398 17494 2417 902 -2053 C
ATOM 2222 O LEU A1106 7.916 223.013 154.776 1.00107.25 O
ANISOU 2222 O LEU A1106 14793 8090 17867 2460 754 -2083 O
ATOM 2223 CB LEU A1106 6.004 225.737 155.064 1.00107.74 C
ANISOU 2223 CB LEU A1106 14657 8976 17302 2035 471 -1613 C
ATOM 2224 CG LEU A1106 5.024 224.679 154.552 1.00109.10 C
ANISOU 2224 CG LEU A1106 15166 8798 17491 1898 98 -1745 C
ATOM 2225 CD1 LEU A1106 4.339 223.975 155.697 1.00110.10 C
ANISOU 2225 CD1 LEU A1106 14995 8765 18074 1778 -218 -1448 C
ATOM 2226 CD2 LEU A1106 4.045 225.260 153.561 1.00109.47 C
ANISOU 2226 CD2 LEU A1106 15513 8940 17140 1725 -133 -1804 C
ATOM 2227 N GLU A 219 8.430 224.710 153.389 1.00106.14 N
ANISOU 2227 N GLU A 219 19197 9495 11636 1890 -667 122 N
ATOM 2228 CA GLU A 219 8.966 223.847 152.346 1.00105.35 C
ANISOU 2228 CA GLU A 219 18930 9487 11610 1704 -755 100 C
ATOM 2229 C GLU A 219 10.248 223.140 152.763 1.00103.87 C
ANISOU 2229 C GLU A 219 18660 9353 11453 1406 -738 52 C
ATOM 2230 O GLU A 219 10.439 221.984 152.395 1.00103.79 O
ANISOU 2230 O GLU A 219 18372 9487 11577 1301 -783 43 O
ATOM 2231 CB GLU A 219 9.151 224.607 151.034 1.00107.72 C
ANISOU 2231 CB GLU A 219 19479 9666 11783 1698 -819 99 C
ATOM 2232 CG GLU A 219 8.491 223.911 149.856 1.00112.73 C
ANISOU 2232 CG GLU A 219 19901 10410 12521 1721 -924 115 C
ATOM 2233 CD GLU A 219 8.310 224.784 148.629 1.00119.36 C
ANISOU 2233 CD GLU A 219 20991 11126 13235 1798 -990 128 C
ATOM 2234 OE1 GLU A 219 8.244 226.026 148.787 1.00121.08 O
ANISOU 2234 OE1 GLU A 219 21538 11174 13291 1900 -953 136 O
ATOM 2235 OE2 GLU A 219 8.227 224.225 147.511 1.00121.83 O
ANISOU 2235 OE2 GLU A 219 21185 11503 13601 1759 -1080 130 O
ATOM 2236 N ARG A 220 11.109 223.809 153.545 1.00102.60 N
ANISOU 2236 N ARG A 220 18739 9078 11166 1270 -679 23 N
ATOM 2237 CA ARG A 220 12.341 223.180 154.006 1.00101.99 C
ANISOU 2237 CA ARG A 220 18573 9060 11119 993 -669 -18 C
ATOM 2238 C ARG A 220 12.041 222.112 155.046 1.00100.87 C
ANISOU 2238 C ARG A 220 18142 9061 11124 1018 -635 -13 C
ATOM 2239 O ARG A 220 12.633 221.035 154.996 1.00101.06 O
ANISOU 2239 O ARG A 220 17925 9214 11260 862 -658 -31 O
ATOM 2240 CB ARG A 220 13.322 224.209 154.569 1.00103.63 C
ANISOU 2240 CB ARG A 220 19116 9110 11150 830 -629 -47 C
ATOM 2241 CG ARG A 220 14.210 224.845 153.510 1.00107.29 C
ANISOU 2241 CG ARG A 220 19759 9496 11512 629 -667 -72 C
ATOM 2242 CD ARG A 220 15.450 225.476 154.131 1.00110.96 C
ANISOU 2242 CD ARG A 220 20463 9856 11842 392 -635 -105 C
ATOM 2243 NE ARG A 220 15.983 226.576 153.321 1.00114.09 N
ANISOU 2243 NE ARG A 220 21190 10090 12069 295 -644 -116 N
ATOM 2244 CZ ARG A 220 17.065 227.286 153.636 1.00116.17 C
ANISOU 2244 CZ ARG A 220 21699 10245 12196 69 -625 -143 C
ATOM 2245 NH1 ARG A 220 17.748 227.015 154.743 1.00115.74 N
ANISOU 2245 NH1 ARG A 220 21593 10229 12153 -82 -606 -161 N
ATOM 2246 NH2 ARG A 220 17.473 228.271 152.844 1.00116.00 N
ANISOU 2246 NH2 ARG A 220 21979 10074 12020 -13 -630 -150 N
ATOM 2247 N ALA A 221 11.104 222.391 155.970 1.00 99.57 N
ANISOU 2247 N ALA A 221 18006 8870 10957 1222 -574 14 N
ATOM 2248 CA ALA A 221 10.701 221.432 156.996 1.00 98.62 C
ANISOU 2248 CA ALA A 221 17626 8876 10969 1266 -530 24 C
ATOM 2249 C ALA A 221 10.055 220.208 156.346 1.00 97.66 C
ANISOU 2249 C ALA A 221 17135 8933 11037 1326 -580 45 C
ATOM 2250 O ALA A 221 10.346 219.090 156.750 1.00 98.02 O
ANISOU 2250 O ALA A 221 16934 9106 11203 1223 -579 34 O
ATOM 2251 CB ALA A 221 9.738 222.075 157.982 1.00 98.65 C
ANISOU 2251 CB ALA A 221 17753 8806 10923 1497 -444 54 C
ATOM 2252 N ARG A 222 9.224 220.412 155.317 1.00 96.31 N
ANISOU 2252 N ARG A 222 16939 8767 10886 1482 -632 75 N
ATOM 2253 CA ARG A 222 8.582 219.326 154.582 1.00 95.71 C
ANISOU 2253 CA ARG A 222 16541 8848 10975 1533 -697 97 C
ATOM 2254 C ARG A 222 9.630 218.496 153.846 1.00 94.61 C
ANISOU 2254 C ARG A 222 16288 8776 10881 1291 -760 60 C
ATOM 2255 O ARG A 222 9.561 217.269 153.855 1.00 94.66 O
ANISOU 2255 O ARG A 222 16006 8926 11032 1240 -781 61 O
ATOM 2256 CB ARG A 222 7.574 219.918 153.592 1.00 97.46 C
ANISOU 2256 CB ARG A 222 16821 9035 11175 1743 -751 136 C
ATOM 2257 CG ARG A 222 6.831 218.932 152.703 1.00101.40 C
ANISOU 2257 CG ARG A 222 17018 9683 11826 1798 -839 162 C
ATOM 2258 CD ARG A 222 5.701 219.650 151.973 1.00105.38 C
ANISOU 2258 CD ARG A 222 17596 10147 12299 2034 -893 209 C
ATOM 2259 NE ARG A 222 4.695 220.154 152.915 1.00109.22 N
ANISOU 2259 NE ARG A 222 18085 10622 12791 2278 -815 253 N
ATOM 2260 CZ ARG A 222 3.872 221.171 152.674 1.00111.96 C
ANISOU 2260 CZ ARG A 222 18572 10897 13072 2515 -824 295 C
ATOM 2261 NH1 ARG A 222 3.941 221.831 151.526 1.00112.12 N
ANISOU 2261 NH1 ARG A 222 18750 10842 13008 2539 -916 299 N
ATOM 2262 NH2 ARG A 222 2.991 221.550 153.589 1.00111.85 N
ANISOU 2262 NH2 ARG A 222 18545 10881 13072 2738 -737 337 N
ATOM 2263 N SER A 223 10.624 219.160 153.245 1.00 93.58 N
ANISOU 2263 N SER A 223 16392 8541 10625 1139 -779 30 N
ATOM 2264 CA SER A 223 11.680 218.461 152.524 1.00 93.13 C
ANISOU 2264 CA SER A 223 16247 8539 10599 913 -822 -2 C
ATOM 2265 C SER A 223 12.561 217.644 153.462 1.00 92.29 C
ANISOU 2265 C SER A 223 16001 8511 10553 736 -781 -30 C
ATOM 2266 O SER A 223 13.009 216.571 153.077 1.00 92.36 O
ANISOU 2266 O SER A 223 15802 8630 10660 616 -810 -43 O
ATOM 2267 CB SER A 223 12.520 219.433 151.704 1.00 94.47 C
ANISOU 2267 CB SER A 223 16705 8573 10615 798 -842 -24 C
ATOM 2268 OG SER A 223 13.202 218.755 150.659 1.00 96.59 O
ANISOU 2268 OG SER A 223 16867 8905 10929 649 -892 -41 O
ATOM 2269 N THR A 224 12.787 218.123 154.690 1.00 91.47 N
ANISOU 2269 N THR A 224 16015 8351 10389 726 -716 -36 N
ATOM 2270 CA THR A 224 13.582 217.380 155.662 1.00 91.35 C
ANISOU 2270 CA THR A 224 15873 8410 10427 574 -685 -58 C
ATOM 2271 C THR A 224 12.845 216.121 156.098 1.00 91.01 C
ANISOU 2271 C THR A 224 15513 8515 10551 665 -677 -39 C
ATOM 2272 O THR A 224 13.452 215.051 156.178 1.00 91.55 O
ANISOU 2272 O THR A 224 15384 8690 10711 534 -686 -55 O
ATOM 2273 CB THR A 224 13.962 218.267 156.837 1.00 92.83 C
ANISOU 2273 CB THR A 224 16295 8486 10491 543 -629 -69 C
ATOM 2274 OG1 THR A 224 14.885 219.249 156.370 1.00 94.08 O
ANISOU 2274 OG1 THR A 224 16720 8523 10504 399 -644 -91 O
ATOM 2275 CG2 THR A 224 14.582 217.487 157.983 1.00 93.24 C
ANISOU 2275 CG2 THR A 224 16211 8616 10599 421 -602 -85 C
ATOM 2276 N LEU A 225 11.538 216.226 156.330 1.00 89.98 N
ANISOU 2276 N LEU A 225 15329 8395 10464 888 -658 -3 N
ATOM 2277 CA LEU A 225 10.740 215.071 156.719 1.00 89.50 C
ANISOU 2277 CA LEU A 225 14970 8474 10563 972 -647 19 C
ATOM 2278 C LEU A 225 10.702 214.027 155.613 1.00 88.92 C
ANISOU 2278 C LEU A 225 14672 8512 10602 916 -722 19 C
ATOM 2279 O LEU A 225 10.857 212.844 155.899 1.00 89.07 O
ANISOU 2279 O LEU A 225 14464 8645 10735 847 -720 15 O
ATOM 2280 CB LEU A 225 9.330 215.514 157.083 1.00 89.71 C
ANISOU 2280 CB LEU A 225 14991 8488 10607 1224 -605 63 C
ATOM 2281 CG LEU A 225 8.982 215.487 158.558 1.00 91.39 C
ANISOU 2281 CG LEU A 225 15204 8696 10823 1297 -508 73 C
ATOM 2282 CD1 LEU A 225 9.965 216.293 159.401 1.00 92.04 C
ANISOU 2282 CD1 LEU A 225 15554 8657 10761 1177 -466 40 C
ATOM 2283 CD2 LEU A 225 7.586 215.984 158.765 1.00 92.11 C
ANISOU 2283 CD2 LEU A 225 15305 8769 10924 1560 -458 121 C
ATOM 2284 N GLN A 226 10.563 214.457 154.349 1.00 88.04 N
ANISOU 2284 N GLN A 226 14645 8359 10448 933 -788 22 N
ATOM 2285 CA GLN A 226 10.548 213.524 153.228 1.00 87.66 C
ANISOU 2285 CA GLN A 226 14419 8399 10486 871 -863 20 C
ATOM 2286 C GLN A 226 11.879 212.786 153.087 1.00 86.69 C
ANISOU 2286 C GLN A 226 14243 8318 10378 643 -862 -18 C
ATOM 2287 O GLN A 226 11.881 211.598 152.766 1.00 86.97 O
ANISOU 2287 O GLN A 226 14060 8460 10523 590 -889 -21 O
ATOM 2288 CB GLN A 226 10.208 214.246 151.929 1.00 89.72 C
ANISOU 2288 CB GLN A 226 14828 8588 10674 927 -933 29 C
ATOM 2289 CG GLN A 226 8.804 214.819 151.890 1.00 94.12 C
ANISOU 2289 CG GLN A 226 15394 9130 11238 1166 -957 74 C
ATOM 2290 CD GLN A 226 8.587 215.582 150.605 1.00 99.53 C
ANISOU 2290 CD GLN A 226 16220 9747 11848 1194 -1042 79 C
ATOM 2291 OE1 GLN A 226 8.346 216.795 150.601 1.00101.37 O
ANISOU 2291 OE1 GLN A 226 16709 9853 11953 1277 -1038 86 O
ATOM 2292 NE2 GLN A 226 8.695 214.884 149.478 1.00100.23 N
ANISOU 2292 NE2 GLN A 226 16167 9909 12004 1118 -1119 74 N
ATOM 2293 N LYS A 227 13.005 213.467 153.352 1.00 85.44 N
ANISOU 2293 N LYS A 227 14278 8077 10110 508 -830 -46 N
ATOM 2294 CA LYS A 227 14.318 212.825 153.299 1.00 84.85 C
ANISOU 2294 CA LYS A 227 14141 8048 10049 297 -823 -78 C
ATOM 2295 C LYS A 227 14.441 211.772 154.394 1.00 84.07 C
ANISOU 2295 C LYS A 227 13832 8055 10056 271 -788 -79 C
ATOM 2296 O LYS A 227 15.008 210.705 154.157 1.00 84.19 O
ANISOU 2296 O LYS A 227 13677 8161 10150 167 -799 -90 O
ATOM 2297 CB LYS A 227 15.442 213.852 153.467 1.00 86.54 C
ANISOU 2297 CB LYS A 227 14597 8159 10126 157 -796 -102 C
ATOM 2298 CG LYS A 227 15.602 214.827 152.311 1.00 90.57 C
ANISOU 2298 CG LYS A 227 15335 8557 10520 139 -823 -106 C
ATOM 2299 CD LYS A 227 16.874 215.671 152.488 1.00 94.81 C
ANISOU 2299 CD LYS A 227 16071 9014 10938 -52 -794 -131 C
ATOM 2300 CE LYS A 227 16.656 217.162 152.361 1.00 98.48 C
ANISOU 2300 CE LYS A 227 16860 9317 11243 -21 -791 -130 C
ATOM 2301 NZ LYS A 227 16.173 217.769 153.632 1.00100.66 N
ANISOU 2301 NZ LYS A 227 17270 9515 11462 120 -760 -117 N
ATOM 2302 N GLU A 228 13.908 212.070 155.590 1.00 83.21 N
ANISOU 2302 N GLU A 228 13749 7927 9941 370 -740 -65 N
ATOM 2303 CA GLU A 228 13.922 211.138 156.712 1.00 82.98 C
ANISOU 2303 CA GLU A 228 13545 7984 10000 361 -701 -63 C
ATOM 2304 C GLU A 228 13.053 209.917 156.403 1.00 81.87 C
ANISOU 2304 C GLU A 228 13143 7960 10004 435 -722 -44 C
ATOM 2305 O GLU A 228 13.452 208.791 156.705 1.00 82.00 O
ANISOU 2305 O GLU A 228 12988 8065 10104 355 -716 -52 O
ATOM 2306 CB GLU A 228 13.449 211.827 157.997 1.00 85.75 C
ANISOU 2306 CB GLU A 228 14010 8273 10300 470 -639 -50 C
ATOM 2307 CG GLU A 228 14.568 212.445 158.811 1.00 91.67 C
ANISOU 2307 CG GLU A 228 14952 8944 10935 343 -614 -74 C
ATOM 2308 CD GLU A 228 14.100 213.033 160.129 1.00 99.77 C
ANISOU 2308 CD GLU A 228 16094 9906 11907 447 -549 -63 C
ATOM 2309 OE1 GLU A 228 13.459 214.110 160.108 1.00101.17 O
ANISOU 2309 OE1 GLU A 228 16462 9980 11998 577 -524 -49 O
ATOM 2310 OE2 GLU A 228 14.368 212.409 161.182 1.00102.70 O
ANISOU 2310 OE2 GLU A 228 16374 10329 12318 405 -519 -67 O
ATOM 2311 N VAL A 229 11.886 210.131 155.776 1.00 80.43 N
ANISOU 2311 N VAL A 229 12935 7776 9850 584 -752 -17 N
ATOM 2312 CA VAL A 229 11.019 209.023 155.391 1.00 79.72 C
ANISOU 2312 CA VAL A 229 12602 7795 9892 640 -785 4 C
ATOM 2313 C VAL A 229 11.716 208.160 154.343 1.00 78.61 C
ANISOU 2313 C VAL A 229 12378 7703 9788 501 -842 -17 C
ATOM 2314 O VAL A 229 11.680 206.932 154.441 1.00 78.74 O
ANISOU 2314 O VAL A 229 12200 7812 9904 458 -845 -17 O
ATOM 2315 CB VAL A 229 9.648 209.511 154.892 1.00 80.50 C
ANISOU 2315 CB VAL A 229 12688 7887 10011 827 -817 42 C
ATOM 2316 CG1 VAL A 229 8.818 208.359 154.336 1.00 81.26 C
ANISOU 2316 CG1 VAL A 229 12534 8100 10243 855 -870 64 C
ATOM 2317 CG2 VAL A 229 8.897 210.212 156.003 1.00 80.90 C
ANISOU 2317 CG2 VAL A 229 12794 7902 10040 980 -742 68 C
ATOM 2318 N HIS A 230 12.402 208.792 153.381 1.00 77.49 N
ANISOU 2318 N HIS A 230 12396 7492 9555 426 -876 -36 N
ATOM 2319 CA HIS A 230 13.122 208.040 152.356 1.00 76.90 C
ANISOU 2319 CA HIS A 230 12264 7454 9502 298 -916 -56 C
ATOM 2320 C HIS A 230 14.219 207.168 152.964 1.00 74.73 C
ANISOU 2320 C HIS A 230 11892 7238 9264 157 -873 -78 C
ATOM 2321 O HIS A 230 14.377 206.016 152.558 1.00 74.72 O
ANISOU 2321 O HIS A 230 11738 7311 9340 104 -889 -83 O
ATOM 2322 CB HIS A 230 13.715 208.966 151.285 1.00 78.91 C
ANISOU 2322 CB HIS A 230 12723 7615 9642 239 -945 -70 C
ATOM 2323 CG HIS A 230 14.209 208.220 150.075 1.00 82.95 C
ANISOU 2323 CG HIS A 230 13180 8161 10177 139 -984 -85 C
ATOM 2324 ND1 HIS A 230 15.512 207.736 149.996 1.00 85.08 N
ANISOU 2324 ND1 HIS A 230 13425 8458 10445 -21 -947 -110 N
ATOM 2325 CD2 HIS A 230 13.550 207.876 148.942 1.00 84.56 C
ANISOU 2325 CD2 HIS A 230 13353 8374 10403 184 -1055 -75 C
ATOM 2326 CE1 HIS A 230 15.604 207.137 148.818 1.00 85.69 C
ANISOU 2326 CE1 HIS A 230 13468 8552 10537 -61 -984 -116 C
ATOM 2327 NE2 HIS A 230 14.450 207.191 148.149 1.00 85.74 N
ANISOU 2327 NE2 HIS A 230 13477 8544 10555 52 -1054 -96 N
ATOM 2328 N ALA A 231 14.972 207.716 153.937 1.00 72.63 N
ANISOU 2328 N ALA A 231 11721 6936 8938 99 -822 -90 N
ATOM 2329 CA ALA A 231 16.040 206.980 154.605 1.00 70.76 C
ANISOU 2329 CA ALA A 231 11397 6756 8731 -26 -788 -107 C
ATOM 2330 C ALA A 231 15.469 205.844 155.450 1.00 68.83 C
ANISOU 2330 C ALA A 231 10954 6601 8598 29 -769 -94 C
ATOM 2331 O ALA A 231 16.049 204.758 155.462 1.00 68.88 O
ANISOU 2331 O ALA A 231 10827 6679 8665 -50 -764 -103 O
ATOM 2332 CB ALA A 231 16.868 207.918 155.463 1.00 70.73 C
ANISOU 2332 CB ALA A 231 11551 6691 8633 -96 -754 -119 C
ATOM 2333 N ALA A 232 14.317 206.069 156.118 1.00 66.80 N
ANISOU 2333 N ALA A 232 10676 6337 8367 170 -752 -70 N
ATOM 2334 CA ALA A 232 13.676 205.025 156.921 1.00 65.36 C
ANISOU 2334 CA ALA A 232 10312 6234 8288 225 -724 -54 C
ATOM 2335 C ALA A 232 13.119 203.904 156.044 1.00 63.70 C
ANISOU 2335 C ALA A 232 9929 6098 8175 230 -767 -46 C
ATOM 2336 O ALA A 232 13.171 202.743 156.440 1.00 63.70 O
ANISOU 2336 O ALA A 232 9784 6168 8252 192 -752 -46 O
ATOM 2337 CB ALA A 232 12.584 205.610 157.798 1.00 65.23 C
ANISOU 2337 CB ALA A 232 10323 6191 8270 374 -682 -28 C
ATOM 2338 N LYS A 233 12.632 204.236 154.844 1.00 62.40 N
ANISOU 2338 N LYS A 233 9797 5912 8000 267 -826 -39 N
ATOM 2339 CA LYS A 233 12.154 203.213 153.919 1.00 61.84 C
ANISOU 2339 CA LYS A 233 9586 5902 8008 257 -880 -33 C
ATOM 2340 C LYS A 233 13.316 202.362 153.445 1.00 60.70 C
ANISOU 2340 C LYS A 233 9417 5781 7865 116 -882 -60 C
ATOM 2341 O LYS A 233 13.180 201.147 153.374 1.00 60.98 O
ANISOU 2341 O LYS A 233 9311 5881 7978 85 -886 -59 O
ATOM 2342 CB LYS A 233 11.425 203.818 152.719 1.00 64.32 C
ANISOU 2342 CB LYS A 233 9958 6183 8299 326 -955 -19 C
ATOM 2343 CG LYS A 233 10.005 204.240 153.047 1.00 69.24 C
ANISOU 2343 CG LYS A 233 10502 6832 8976 480 -969 19 C
ATOM 2344 CD LYS A 233 9.261 204.737 151.815 1.00 74.21 C
ANISOU 2344 CD LYS A 233 11195 7428 9575 556 -1056 36 C
ATOM 2345 CE LYS A 233 7.944 205.388 152.183 1.00 78.41 C
ANISOU 2345 CE LYS A 233 11691 7967 10133 732 -1055 78 C
ATOM 2346 NZ LYS A 233 7.373 206.184 151.056 1.00 80.71 N
ANISOU 2346 NZ LYS A 233 12110 8198 10357 825 -1128 93 N
ATOM 2347 N SER A 234 14.477 202.977 153.163 1.00 59.27 N
ANISOU 2347 N SER A 234 9373 5549 7597 29 -871 -83 N
ATOM 2348 CA SER A 234 15.659 202.229 152.736 1.00 58.21 C
ANISOU 2348 CA SER A 234 9213 5442 7463 -97 -860 -105 C
ATOM 2349 C SER A 234 16.085 201.240 153.826 1.00 56.93 C
ANISOU 2349 C SER A 234 8921 5347 7364 -134 -815 -107 C
ATOM 2350 O SER A 234 16.333 200.073 153.524 1.00 57.37 O
ANISOU 2350 O SER A 234 8871 5453 7474 -173 -818 -111 O
ATOM 2351 CB SER A 234 16.816 203.173 152.422 1.00 59.15 C
ANISOU 2351 CB SER A 234 9488 5502 7482 -188 -841 -124 C
ATOM 2352 OG SER A 234 16.488 204.084 151.390 1.00 61.06 O
ANISOU 2352 OG SER A 234 9873 5673 7655 -164 -879 -124 O
ATOM 2353 N ALA A 235 16.112 201.689 155.095 1.00 54.94 N
ANISOU 2353 N ALA A 235 8687 5090 7098 -113 -775 -103 N
ATOM 2354 CA ALA A 235 16.495 200.824 156.202 1.00 53.34 C
ANISOU 2354 CA ALA A 235 8381 4945 6943 -147 -736 -104 C
ATOM 2355 C ALA A 235 15.486 199.701 156.395 1.00 51.57 C
ANISOU 2355 C ALA A 235 8009 4771 6813 -74 -731 -86 C
ATOM 2356 O ALA A 235 15.886 198.569 156.657 1.00 51.89 O
ANISOU 2356 O ALA A 235 7949 4862 6903 -112 -712 -88 O
ATOM 2357 CB ALA A 235 16.637 201.637 157.470 1.00 53.37 C
ANISOU 2357 CB ALA A 235 8470 4918 6890 -157 -702 -106 C
ATOM 2358 N ALA A 236 14.189 199.995 156.223 1.00 49.69 N
ANISOU 2358 N ALA A 236 7754 4524 6603 23 -753 -66 N
ATOM 2359 CA ALA A 236 13.143 198.984 156.349 1.00 48.39 C
ANISOU 2359 CA ALA A 236 7438 4414 6533 77 -754 -46 C
ATOM 2360 C ALA A 236 13.230 197.948 155.232 1.00 46.97 C
ANISOU 2360 C ALA A 236 7183 4268 6397 17 -801 -52 C
ATOM 2361 O ALA A 236 12.953 196.781 155.480 1.00 46.80 O
ANISOU 2361 O ALA A 236 7045 4293 6443 3 -790 -46 O
ATOM 2362 CB ALA A 236 11.774 199.633 156.357 1.00 48.36 C
ANISOU 2362 CB ALA A 236 7427 4400 6548 196 -769 -18 C
ATOM 2363 N ILE A 237 13.638 198.354 154.019 1.00 45.75 N
ANISOU 2363 N ILE A 237 7112 4079 6194 -20 -848 -66 N
ATOM 2364 CA ILE A 237 13.813 197.414 152.913 1.00 45.45 C
ANISOU 2364 CA ILE A 237 7037 4056 6176 -79 -888 -75 C
ATOM 2365 C ILE A 237 14.918 196.412 153.253 1.00 45.15 C
ANISOU 2365 C ILE A 237 6958 4047 6148 -159 -840 -91 C
ATOM 2366 O ILE A 237 14.782 195.219 152.979 1.00 45.49 O
ANISOU 2366 O ILE A 237 6925 4120 6240 -185 -847 -91 O
ATOM 2367 CB ILE A 237 14.115 198.164 151.602 1.00 46.00 C
ANISOU 2367 CB ILE A 237 7233 4072 6174 -102 -935 -87 C
ATOM 2368 CG1 ILE A 237 12.869 198.893 151.117 1.00 47.24 C
ANISOU 2368 CG1 ILE A 237 7410 4208 6332 -13 -1000 -66 C
ATOM 2369 CG2 ILE A 237 14.662 197.219 150.510 1.00 46.47 C
ANISOU 2369 CG2 ILE A 237 7293 4134 6231 -180 -954 -103 C
ATOM 2370 CD1 ILE A 237 13.140 199.815 149.951 1.00 48.97 C
ANISOU 2370 CD1 ILE A 237 7782 4359 6464 -24 -1050 -76 C
ATOM 2371 N ILE A 238 16.001 196.896 153.878 1.00 44.34 N
ANISOU 2371 N ILE A 238 6910 3937 6000 -195 -794 -103 N
ATOM 2372 CA ILE A 238 17.123 196.080 154.311 1.00 44.09 C
ANISOU 2372 CA ILE A 238 6835 3940 5977 -257 -750 -113 C
ATOM 2373 C ILE A 238 16.617 195.007 155.299 1.00 44.45 C
ANISOU 2373 C ILE A 238 6766 4029 6094 -227 -726 -100 C
ATOM 2374 O ILE A 238 16.847 193.815 155.079 1.00 45.04 O
ANISOU 2374 O ILE A 238 6781 4130 6204 -255 -719 -103 O
ATOM 2375 CB ILE A 238 18.200 197.004 154.929 1.00 44.09 C
ANISOU 2375 CB ILE A 238 6908 3928 5916 -298 -720 -121 C
ATOM 2376 CG1 ILE A 238 18.850 197.921 153.852 1.00 44.47 C
ANISOU 2376 CG1 ILE A 238 7072 3932 5891 -351 -735 -134 C
ATOM 2377 CG2 ILE A 238 19.228 196.223 155.747 1.00 44.50 C
ANISOU 2377 CG2 ILE A 238 6893 4030 5986 -341 -681 -123 C
ATOM 2378 CD1 ILE A 238 19.930 197.331 153.016 1.00 45.22 C
ANISOU 2378 CD1 ILE A 238 7158 4045 5977 -421 -720 -145 C
ATOM 2379 N ALA A 239 15.826 195.422 156.305 1.00 43.79 N
ANISOU 2379 N ALA A 239 6664 3946 6029 -165 -711 -85 N
ATOM 2380 CA ALA A 239 15.252 194.512 157.300 1.00 43.54 C
ANISOU 2380 CA ALA A 239 6535 3948 6059 -134 -678 -70 C
ATOM 2381 C ALA A 239 14.257 193.527 156.675 1.00 43.13 C
ANISOU 2381 C ALA A 239 6395 3918 6073 -127 -708 -59 C
ATOM 2382 O ALA A 239 14.254 192.344 157.015 1.00 43.02 O
ANISOU 2382 O ALA A 239 6315 3930 6101 -150 -686 -56 O
ATOM 2383 CB ALA A 239 14.578 195.305 158.403 1.00 43.46 C
ANISOU 2383 CB ALA A 239 6541 3925 6045 -62 -647 -54 C
ATOM 2384 N GLY A 240 13.451 194.014 155.742 1.00 42.81 N
ANISOU 2384 N GLY A 240 6366 3863 6035 -102 -762 -53 N
ATOM 2385 CA GLY A 240 12.470 193.199 155.045 1.00 43.10 C
ANISOU 2385 CA GLY A 240 6326 3920 6129 -107 -810 -40 C
ATOM 2386 C GLY A 240 13.125 192.114 154.231 1.00 43.74 C
ANISOU 2386 C GLY A 240 6416 3999 6206 -184 -826 -58 C
ATOM 2387 O GLY A 240 12.643 190.984 154.196 1.00 43.97 O
ANISOU 2387 O GLY A 240 6376 4048 6284 -210 -833 -50 O
ATOM 2388 N LEU A 241 14.256 192.435 153.608 1.00 44.18 N
ANISOU 2388 N LEU A 241 6561 4026 6198 -222 -822 -80 N
ATOM 2389 CA LEU A 241 15.011 191.453 152.835 1.00 44.90 C
ANISOU 2389 CA LEU A 241 6676 4110 6274 -283 -818 -96 C
ATOM 2390 C LEU A 241 15.647 190.386 153.732 1.00 45.62 C
ANISOU 2390 C LEU A 241 6716 4228 6389 -298 -757 -96 C
ATOM 2391 O LEU A 241 15.707 189.225 153.327 1.00 46.14 O
ANISOU 2391 O LEU A 241 6770 4291 6470 -328 -756 -100 O
ATOM 2392 CB LEU A 241 16.046 192.129 151.937 1.00 44.69 C
ANISOU 2392 CB LEU A 241 6754 4052 6175 -315 -816 -115 C
ATOM 2393 CG LEU A 241 15.425 192.854 150.763 1.00 45.28 C
ANISOU 2393 CG LEU A 241 6901 4087 6217 -308 -884 -116 C
ATOM 2394 CD1 LEU A 241 16.418 193.749 150.106 1.00 45.82 C
ANISOU 2394 CD1 LEU A 241 7079 4120 6209 -337 -869 -131 C
ATOM 2395 CD2 LEU A 241 14.798 191.886 149.783 1.00 45.28 C
ANISOU 2395 CD2 LEU A 241 6899 4074 6232 -334 -939 -116 C
ATOM 2396 N PHE A 242 16.051 190.749 154.969 1.00 45.16 N
ANISOU 2396 N PHE A 242 6638 4190 6332 -274 -710 -92 N
ATOM 2397 CA PHE A 242 16.576 189.775 155.928 1.00 45.40 C
ANISOU 2397 CA PHE A 242 6624 4244 6383 -277 -659 -89 C
ATOM 2398 C PHE A 242 15.469 188.780 156.273 1.00 46.32 C
ANISOU 2398 C PHE A 242 6672 4369 6559 -269 -659 -73 C
ATOM 2399 O PHE A 242 15.702 187.568 156.264 1.00 46.27 O
ANISOU 2399 O PHE A 242 6652 4362 6565 -293 -641 -74 O
ATOM 2400 CB PHE A 242 17.077 190.465 157.212 1.00 44.75 C
ANISOU 2400 CB PHE A 242 6546 4175 6282 -254 -622 -84 C
ATOM 2401 CG PHE A 242 17.670 189.534 158.249 1.00 44.58 C
ANISOU 2401 CG PHE A 242 6490 4177 6272 -251 -578 -79 C
ATOM 2402 CD1 PHE A 242 16.873 188.939 159.210 1.00 44.94 C
ANISOU 2402 CD1 PHE A 242 6489 4228 6358 -223 -552 -64 C
ATOM 2403 CD2 PHE A 242 19.031 189.300 158.295 1.00 45.01 C
ANISOU 2403 CD2 PHE A 242 6557 4249 6295 -273 -560 -86 C
ATOM 2404 CE1 PHE A 242 17.422 188.088 160.158 1.00 45.41 C
ANISOU 2404 CE1 PHE A 242 6535 4300 6418 -217 -514 -58 C
ATOM 2405 CE2 PHE A 242 19.579 188.472 159.265 1.00 45.46 C
ANISOU 2405 CE2 PHE A 242 6587 4328 6359 -259 -528 -78 C
ATOM 2406 CZ PHE A 242 18.771 187.857 160.176 1.00 45.13 C
ANISOU 2406 CZ PHE A 242 6517 4280 6349 -230 -507 -65 C
ATOM 2407 N ALA A 243 14.260 189.295 156.548 1.00 47.04 N
ANISOU 2407 N ALA A 243 6721 4467 6685 -235 -676 -57 N
ATOM 2408 CA ALA A 243 13.123 188.447 156.880 1.00 48.16 C
ANISOU 2408 CA ALA A 243 6781 4626 6890 -235 -674 -37 C
ATOM 2409 C ALA A 243 12.755 187.543 155.703 1.00 49.14 C
ANISOU 2409 C ALA A 243 6903 4740 7030 -291 -728 -41 C
ATOM 2410 O ALA A 243 12.609 186.344 155.894 1.00 49.39 O
ANISOU 2410 O ALA A 243 6911 4771 7085 -327 -710 -37 O
ATOM 2411 CB ALA A 243 11.934 189.296 157.312 1.00 48.22 C
ANISOU 2411 CB ALA A 243 6735 4652 6934 -179 -678 -14 C
ATOM 2412 N LEU A 244 12.682 188.092 154.487 1.00 49.51 N
ANISOU 2412 N LEU A 244 6993 4767 7049 -302 -793 -49 N
ATOM 2413 CA LEU A 244 12.368 187.291 153.313 1.00 50.66 C
ANISOU 2413 CA LEU A 244 7160 4892 7194 -360 -852 -55 C
ATOM 2414 C LEU A 244 13.419 186.172 153.077 1.00 51.75 C
ANISOU 2414 C LEU A 244 7363 5003 7297 -402 -813 -73 C
ATOM 2415 O LEU A 244 13.033 185.042 152.770 1.00 52.05 O
ANISOU 2415 O LEU A 244 7398 5026 7351 -448 -824 -71 O
ATOM 2416 CB LEU A 244 12.187 188.194 152.071 1.00 50.96 C
ANISOU 2416 CB LEU A 244 7255 4909 7199 -358 -931 -60 C
ATOM 2417 CG LEU A 244 12.166 187.508 150.683 1.00 52.44 C
ANISOU 2417 CG LEU A 244 7523 5055 7348 -419 -990 -75 C
ATOM 2418 CD1 LEU A 244 10.965 186.595 150.520 1.00 53.02 C
ANISOU 2418 CD1 LEU A 244 7541 5136 7470 -473 -1047 -60 C
ATOM 2419 CD2 LEU A 244 12.241 188.528 149.546 1.00 52.86 C
ANISOU 2419 CD2 LEU A 244 7660 5077 7348 -407 -1054 -83 C
ATOM 2420 N CYS A 245 14.725 186.457 153.273 1.00 51.96 N
ANISOU 2420 N CYS A 245 7442 5023 7277 -384 -761 -88 N
ATOM 2421 CA CYS A 245 15.780 185.468 153.016 1.00 52.57 C
ANISOU 2421 CA CYS A 245 7575 5080 7321 -403 -718 -102 C
ATOM 2422 C CYS A 245 15.922 184.406 154.076 1.00 52.55 C
ANISOU 2422 C CYS A 245 7536 5087 7342 -396 -663 -93 C
ATOM 2423 O CYS A 245 16.276 183.266 153.749 1.00 52.68 O
ANISOU 2423 O CYS A 245 7600 5075 7342 -416 -644 -98 O
ATOM 2424 CB CYS A 245 17.112 186.153 152.760 1.00 53.81 C
ANISOU 2424 CB CYS A 245 7781 5238 7426 -389 -685 -115 C
ATOM 2425 SG CYS A 245 17.117 187.174 151.271 1.00 58.91 S
ANISOU 2425 SG CYS A 245 8509 5850 8022 -410 -739 -128 S
ATOM 2426 N TRP A 246 15.693 184.771 155.340 1.00 52.14 N
ANISOU 2426 N TRP A 246 7421 5068 7321 -362 -633 -80 N
ATOM 2427 CA TRP A 246 15.844 183.813 156.422 1.00 52.36 C
ANISOU 2427 CA TRP A 246 7427 5100 7365 -351 -579 -70 C
ATOM 2428 C TRP A 246 14.595 183.052 156.778 1.00 52.58 C
ANISOU 2428 C TRP A 246 7412 5124 7442 -380 -584 -54 C
ATOM 2429 O TRP A 246 14.717 181.940 157.265 1.00 52.96 O
ANISOU 2429 O TRP A 246 7476 5157 7491 -388 -545 -49 O
ATOM 2430 CB TRP A 246 16.410 184.472 157.665 1.00 52.28 C
ANISOU 2430 CB TRP A 246 7393 5121 7350 -305 -539 -64 C
ATOM 2431 CG TRP A 246 17.875 184.741 157.580 1.00 52.69 C
ANISOU 2431 CG TRP A 246 7479 5184 7356 -289 -520 -74 C
ATOM 2432 CD1 TRP A 246 18.470 185.921 157.259 1.00 53.52 C
ANISOU 2432 CD1 TRP A 246 7599 5303 7433 -288 -535 -83 C
ATOM 2433 CD2 TRP A 246 18.933 183.808 157.827 1.00 52.69 C
ANISOU 2433 CD2 TRP A 246 7498 5187 7336 -272 -480 -74 C
ATOM 2434 NE1 TRP A 246 19.836 185.790 157.319 1.00 53.81 N
ANISOU 2434 NE1 TRP A 246 7646 5360 7438 -281 -508 -86 N
ATOM 2435 CE2 TRP A 246 20.147 184.498 157.656 1.00 53.55 C
ANISOU 2435 CE2 TRP A 246 7611 5323 7411 -263 -475 -80 C
ATOM 2436 CE3 TRP A 246 18.973 182.451 158.162 1.00 53.02 C
ANISOU 2436 CE3 TRP A 246 7556 5208 7381 -263 -448 -67 C
ATOM 2437 CZ2 TRP A 246 21.385 183.872 157.801 1.00 54.25 C
ANISOU 2437 CZ2 TRP A 246 7701 5432 7479 -236 -440 -76 C
ATOM 2438 CZ3 TRP A 246 20.198 181.838 158.322 1.00 53.76 C
ANISOU 2438 CZ3 TRP A 246 7670 5312 7446 -227 -413 -64 C
ATOM 2439 CH2 TRP A 246 21.386 182.542 158.139 1.00 54.11 C
ANISOU 2439 CH2 TRP A 246 7698 5395 7465 -210 -411 -67 C
ATOM 2440 N LEU A 247 13.405 183.631 156.581 1.00 52.35 N
ANISOU 2440 N LEU A 247 7328 5111 7453 -393 -630 -43 N
ATOM 2441 CA LEU A 247 12.162 182.948 156.940 1.00 52.46 C
ANISOU 2441 CA LEU A 247 7277 5133 7523 -430 -633 -22 C
ATOM 2442 C LEU A 247 11.985 181.556 156.318 1.00 52.75 C
ANISOU 2442 C LEU A 247 7360 5129 7552 -502 -647 -26 C
ATOM 2443 O LEU A 247 11.593 180.658 157.067 1.00 53.27 O
ANISOU 2443 O LEU A 247 7407 5192 7644 -527 -606 -13 O
ATOM 2444 CB LEU A 247 10.923 183.802 156.676 1.00 52.36 C
ANISOU 2444 CB LEU A 247 7182 5154 7560 -427 -687 -5 C
ATOM 2445 CG LEU A 247 10.629 184.801 157.766 1.00 53.96 C
ANISOU 2445 CG LEU A 247 7323 5391 7787 -356 -644 11 C
ATOM 2446 CD1 LEU A 247 9.610 185.793 157.316 1.00 54.84 C
ANISOU 2446 CD1 LEU A 247 7371 5533 7934 -331 -700 27 C
ATOM 2447 CD2 LEU A 247 10.201 184.121 159.037 1.00 54.67 C
ANISOU 2447 CD2 LEU A 247 7365 5493 7913 -354 -568 31 C
ATOM 2448 N PRO A 248 12.273 181.299 155.011 1.00 51.81 N
ANISOU 2448 N PRO A 248 7320 4974 7392 -539 -698 -44 N
ATOM 2449 CA PRO A 248 12.040 179.948 154.475 1.00 50.89 C
ANISOU 2449 CA PRO A 248 7267 4808 7261 -613 -713 -47 C
ATOM 2450 C PRO A 248 12.769 178.861 155.242 1.00 50.08 C
ANISOU 2450 C PRO A 248 7221 4675 7133 -599 -633 -49 C
ATOM 2451 O PRO A 248 12.176 177.836 155.543 1.00 50.37 O
ANISOU 2451 O PRO A 248 7268 4687 7184 -654 -621 -38 O
ATOM 2452 CB PRO A 248 12.518 180.051 153.030 1.00 51.54 C
ANISOU 2452 CB PRO A 248 7448 4850 7287 -632 -767 -69 C
ATOM 2453 CG PRO A 248 12.378 181.469 152.702 1.00 52.33 C
ANISOU 2453 CG PRO A 248 7500 4987 7397 -595 -809 -69 C
ATOM 2454 CD PRO A 248 12.742 182.206 153.946 1.00 51.06 C
ANISOU 2454 CD PRO A 248 7273 4870 7257 -523 -745 -61 C
ATOM 2455 N LEU A 249 14.023 179.106 155.609 1.00 49.04 N
ANISOU 2455 N LEU A 249 7121 4546 6965 -526 -580 -58 N
ATOM 2456 CA LEU A 249 14.827 178.143 156.354 1.00 48.49 C
ANISOU 2456 CA LEU A 249 7105 4453 6866 -491 -508 -56 C
ATOM 2457 C LEU A 249 14.198 177.877 157.723 1.00 48.18 C
ANISOU 2457 C LEU A 249 7006 4431 6868 -490 -467 -35 C
ATOM 2458 O LEU A 249 14.077 176.726 158.140 1.00 48.08 O
ANISOU 2458 O LEU A 249 7045 4380 6845 -513 -430 -28 O
ATOM 2459 CB LEU A 249 16.271 178.704 156.461 1.00 48.25 C
ANISOU 2459 CB LEU A 249 7086 4446 6800 -412 -476 -66 C
ATOM 2460 CG LEU A 249 17.449 177.839 156.906 1.00 49.01 C
ANISOU 2460 CG LEU A 249 7218 4539 6865 -348 -411 -61 C
ATOM 2461 CD1 LEU A 249 17.780 178.050 158.355 1.00 49.39 C
ANISOU 2461 CD1 LEU A 249 7216 4611 6940 -324 -379 -44 C
ATOM 2462 CD2 LEU A 249 17.304 176.403 156.509 1.00 49.69 C
ANISOU 2462 CD2 LEU A 249 7413 4562 6905 -350 -385 -66 C
ATOM 2463 N HIS A 250 13.746 178.932 158.386 1.00 48.14 N
ANISOU 2463 N HIS A 250 6907 4479 6905 -466 -469 -25 N
ATOM 2464 CA HIS A 250 13.131 178.809 159.693 1.00 49.11 C
ANISOU 2464 CA HIS A 250 6977 4619 7063 -458 -419 -3 C
ATOM 2465 C HIS A 250 11.817 178.082 159.609 1.00 50.12 C
ANISOU 2465 C HIS A 250 7071 4736 7236 -541 -428 13 C
ATOM 2466 O HIS A 250 11.538 177.226 160.442 1.00 50.45 O
ANISOU 2466 O HIS A 250 7132 4756 7282 -562 -374 26 O
ATOM 2467 CB HIS A 250 12.947 180.187 160.328 1.00 49.68 C
ANISOU 2467 CB HIS A 250 6973 4742 7161 -405 -416 4 C
ATOM 2468 CG HIS A 250 14.226 180.770 160.840 1.00 51.35 C
ANISOU 2468 CG HIS A 250 7220 4963 7327 -336 -395 -7 C
ATOM 2469 ND1 HIS A 250 14.983 180.123 161.804 1.00 52.97 N
ANISOU 2469 ND1 HIS A 250 7472 5154 7501 -302 -345 -3 N
ATOM 2470 CD2 HIS A 250 14.853 181.914 160.491 1.00 52.22 C
ANISOU 2470 CD2 HIS A 250 7328 5096 7417 -305 -424 -19 C
ATOM 2471 CE1 HIS A 250 16.029 180.899 162.018 1.00 53.32 C
ANISOU 2471 CE1 HIS A 250 7527 5221 7513 -254 -351 -11 C
ATOM 2472 NE2 HIS A 250 15.995 181.986 161.250 1.00 53.22 N
ANISOU 2472 NE2 HIS A 250 7488 5229 7505 -260 -394 -22 N
ATOM 2473 N ILE A 251 11.010 178.410 158.605 1.00 50.52 N
ANISOU 2473 N ILE A 251 7074 4803 7318 -594 -500 13 N
ATOM 2474 CA ILE A 251 9.715 177.782 158.402 1.00 51.32 C
ANISOU 2474 CA ILE A 251 7125 4907 7469 -688 -526 32 C
ATOM 2475 C ILE A 251 9.884 176.286 158.111 1.00 52.15 C
ANISOU 2475 C ILE A 251 7341 4940 7533 -762 -516 25 C
ATOM 2476 O ILE A 251 9.176 175.472 158.704 1.00 52.45 O
ANISOU 2476 O ILE A 251 7365 4967 7596 -823 -480 44 O
ATOM 2477 CB ILE A 251 8.926 178.531 157.314 1.00 51.80 C
ANISOU 2477 CB ILE A 251 7117 5001 7563 -722 -623 34 C
ATOM 2478 CG1 ILE A 251 8.541 179.923 157.812 1.00 52.83 C
ANISOU 2478 CG1 ILE A 251 7138 5197 7737 -644 -619 48 C
ATOM 2479 CG2 ILE A 251 7.688 177.749 156.906 1.00 52.36 C
ANISOU 2479 CG2 ILE A 251 7138 5076 7680 -838 -671 54 C
ATOM 2480 CD1 ILE A 251 8.014 180.815 156.744 1.00 54.34 C
ANISOU 2480 CD1 ILE A 251 7285 5417 7946 -647 -716 49 C
ATOM 2481 N ILE A 252 10.885 175.900 157.292 1.00 52.03 N
ANISOU 2481 N ILE A 252 7450 4871 7449 -751 -536 0 N
ATOM 2482 CA ILE A 252 11.159 174.490 157.025 1.00 52.45 C
ANISOU 2482 CA ILE A 252 7637 4843 7447 -803 -518 -8 C
ATOM 2483 C ILE A 252 11.489 173.771 158.330 1.00 53.73 C
ANISOU 2483 C ILE A 252 7836 4983 7597 -769 -426 4 C
ATOM 2484 O ILE A 252 10.910 172.729 158.605 1.00 54.36 O
ANISOU 2484 O ILE A 252 7963 5018 7674 -846 -405 15 O
ATOM 2485 CB ILE A 252 12.284 174.310 155.978 1.00 52.35 C
ANISOU 2485 CB ILE A 252 7754 4779 7358 -767 -534 -35 C
ATOM 2486 CG1 ILE A 252 11.847 174.834 154.606 1.00 52.83 C
ANISOU 2486 CG1 ILE A 252 7811 4843 7419 -817 -629 -46 C
ATOM 2487 CG2 ILE A 252 12.729 172.839 155.888 1.00 52.68 C
ANISOU 2487 CG2 ILE A 252 7956 4728 7333 -792 -495 -41 C
ATOM 2488 CD1 ILE A 252 12.931 174.842 153.559 1.00 53.69 C
ANISOU 2488 CD1 ILE A 252 8039 4907 7452 -774 -635 -71 C
ATOM 2489 N ASN A 253 12.322 174.379 159.183 1.00 54.20 N
ANISOU 2489 N ASN A 253 7872 5074 7650 -664 -375 4 N
ATOM 2490 CA ASN A 253 12.635 173.796 160.481 1.00 55.48 C
ANISOU 2490 CA ASN A 253 8069 5216 7794 -624 -296 18 C
ATOM 2491 C ASN A 253 11.384 173.622 161.329 1.00 56.63 C
ANISOU 2491 C ASN A 253 8140 5379 7997 -688 -264 43 C
ATOM 2492 O ASN A 253 11.260 172.617 162.000 1.00 56.33 O
ANISOU 2492 O ASN A 253 8172 5293 7939 -716 -209 54 O
ATOM 2493 CB ASN A 253 13.669 174.629 161.220 1.00 57.01 C
ANISOU 2493 CB ASN A 253 8239 5449 7973 -509 -267 15 C
ATOM 2494 CG ASN A 253 15.060 174.466 160.678 1.00 60.67 C
ANISOU 2494 CG ASN A 253 8783 5893 8375 -441 -270 -2 C
ATOM 2495 OD1 ASN A 253 15.364 173.518 159.942 1.00 61.88 O
ANISOU 2495 OD1 ASN A 253 9039 5986 8485 -460 -271 -11 O
ATOM 2496 ND2 ASN A 253 15.937 175.394 161.034 1.00 61.70 N
ANISOU 2496 ND2 ASN A 253 8871 6073 8501 -361 -268 -5 N
ATOM 2497 N CYS A 254 10.433 174.552 161.243 1.00 58.20 N
ANISOU 2497 N CYS A 254 8204 5644 8266 -713 -294 55 N
ATOM 2498 CA CYS A 254 9.177 174.457 161.981 1.00 60.35 C
ANISOU 2498 CA CYS A 254 8383 5946 8602 -771 -256 84 C
ATOM 2499 C CYS A 254 8.387 173.245 161.527 1.00 62.61 C
ANISOU 2499 C CYS A 254 8704 6188 8895 -905 -271 93 C
ATOM 2500 O CYS A 254 7.800 172.570 162.360 1.00 63.05 O
ANISOU 2500 O CYS A 254 8757 6231 8969 -957 -207 115 O
ATOM 2501 CB CYS A 254 8.346 175.729 161.842 1.00 61.25 C
ANISOU 2501 CB CYS A 254 8342 6143 8788 -756 -289 97 C
ATOM 2502 SG CYS A 254 9.047 177.187 162.658 1.00 64.83 S
ANISOU 2502 SG CYS A 254 8762 6639 9232 -614 -256 93 S
ATOM 2503 N PHE A 255 8.340 172.975 160.216 1.00 63.88 N
ANISOU 2503 N PHE A 255 8906 6327 9040 -969 -357 77 N
ATOM 2504 CA PHE A 255 7.625 171.800 159.705 1.00 65.58 C
ANISOU 2504 CA PHE A 255 9178 6490 9250 -1112 -386 83 C
ATOM 2505 C PHE A 255 8.294 170.503 160.155 1.00 66.85 C
ANISOU 2505 C PHE A 255 9518 6551 9331 -1119 -319 76 C
ATOM 2506 O PHE A 255 7.613 169.578 160.583 1.00 67.09 O
ANISOU 2506 O PHE A 255 9579 6546 9366 -1216 -281 93 O
ATOM 2507 CB PHE A 255 7.500 171.849 158.179 1.00 65.74 C
ANISOU 2507 CB PHE A 255 9226 6498 9255 -1175 -501 65 C
ATOM 2508 CG PHE A 255 6.320 172.662 157.707 1.00 66.54 C
ANISOU 2508 CG PHE A 255 9153 6688 9443 -1229 -579 85 C
ATOM 2509 CD1 PHE A 255 6.425 174.029 157.528 1.00 67.29 C
ANISOU 2509 CD1 PHE A 255 9138 6854 9573 -1131 -605 84 C
ATOM 2510 CD2 PHE A 255 5.103 172.060 157.451 1.00 67.45 C
ANISOU 2510 CD2 PHE A 255 9209 6814 9604 -1378 -627 107 C
ATOM 2511 CE1 PHE A 255 5.334 174.777 157.110 1.00 68.01 C
ANISOU 2511 CE1 PHE A 255 9068 7028 9744 -1162 -674 107 C
ATOM 2512 CE2 PHE A 255 4.016 172.811 157.023 1.00 68.10 C
ANISOU 2512 CE2 PHE A 255 9111 6990 9773 -1417 -703 132 C
ATOM 2513 CZ PHE A 255 4.140 174.161 156.847 1.00 67.79 C
ANISOU 2513 CZ PHE A 255 8969 7021 9767 -1300 -725 132 C
ATOM 2514 N THR A 256 9.627 170.451 160.105 1.00 67.62 N
ANISOU 2514 N THR A 256 9731 6606 9356 -1011 -299 53 N
ATOM 2515 CA THR A 256 10.385 169.287 160.548 1.00 68.89 C
ANISOU 2515 CA THR A 256 10066 6673 9435 -983 -236 48 C
ATOM 2516 C THR A 256 10.133 169.025 162.038 1.00 70.18 C
ANISOU 2516 C THR A 256 10214 6838 9613 -968 -145 73 C
ATOM 2517 O THR A 256 9.947 167.882 162.446 1.00 70.77 O
ANISOU 2517 O THR A 256 10400 6837 9651 -1032 -98 82 O
ATOM 2518 CB THR A 256 11.890 169.535 160.328 1.00 70.42 C
ANISOU 2518 CB THR A 256 10335 6855 9567 -841 -227 27 C
ATOM 2519 OG1 THR A 256 12.153 169.774 158.946 1.00 71.64 O
ANISOU 2519 OG1 THR A 256 10519 7001 9701 -851 -297 6 O
ATOM 2520 CG2 THR A 256 12.757 168.400 160.853 1.00 70.90 C
ANISOU 2520 CG2 THR A 256 10562 6831 9547 -778 -157 28 C
ATOM 2521 N PHE A 257 10.090 170.087 162.841 1.00 70.44 N
ANISOU 2521 N PHE A 257 10120 6950 9695 -892 -118 83 N
ATOM 2522 CA PHE A 257 9.933 169.988 164.283 1.00 71.21 C
ANISOU 2522 CA PHE A 257 10211 7048 9796 -857 -30 105 C
ATOM 2523 C PHE A 257 8.508 169.726 164.753 1.00 72.93 C
ANISOU 2523 C PHE A 257 10349 7284 10078 -975 10 133 C
ATOM 2524 O PHE A 257 8.262 168.780 165.506 1.00 73.34 O
ANISOU 2524 O PHE A 257 10490 7275 10101 -1023 80 149 O
ATOM 2525 CB PHE A 257 10.489 171.261 164.932 1.00 70.24 C
ANISOU 2525 CB PHE A 257 10003 6995 9690 -731 -20 103 C
ATOM 2526 CG PHE A 257 10.463 171.289 166.429 1.00 69.92 C
ANISOU 2526 CG PHE A 257 9973 6952 9640 -677 66 123 C
ATOM 2527 CD1 PHE A 257 11.239 170.417 167.167 1.00 70.29 C
ANISOU 2527 CD1 PHE A 257 10165 6930 9611 -624 114 124 C
ATOM 2528 CD2 PHE A 257 9.702 172.217 167.102 1.00 70.33 C
ANISOU 2528 CD2 PHE A 257 9902 7068 9753 -670 99 141 C
ATOM 2529 CE1 PHE A 257 11.231 170.455 168.547 1.00 70.79 C
ANISOU 2529 CE1 PHE A 257 10255 6984 9656 -575 187 142 C
ATOM 2530 CE2 PHE A 257 9.688 172.247 168.484 1.00 70.93 C
ANISOU 2530 CE2 PHE A 257 10008 7131 9810 -621 184 159 C
ATOM 2531 CZ PHE A 257 10.442 171.356 169.199 1.00 70.58 C
ANISOU 2531 CZ PHE A 257 10114 7015 9687 -579 225 159 C
ATOM 2532 N PHE A 258 7.575 170.563 164.326 1.00 73.81 N
ANISOU 2532 N PHE A 258 10292 7478 10273 -1019 -32 144 N
ATOM 2533 CA PHE A 258 6.204 170.481 164.768 1.00 75.37 C
ANISOU 2533 CA PHE A 258 10374 7717 10547 -1119 7 177 C
ATOM 2534 C PHE A 258 5.420 169.341 164.140 1.00 77.72 C
ANISOU 2534 C PHE A 258 10712 7971 10849 -1289 -21 185 C
ATOM 2535 O PHE A 258 4.455 168.882 164.743 1.00 78.06 O
ANISOU 2535 O PHE A 258 10711 8018 10930 -1384 41 215 O
ATOM 2536 CB PHE A 258 5.506 171.824 164.568 1.00 75.04 C
ANISOU 2536 CB PHE A 258 10133 7785 10594 -1088 -27 190 C
ATOM 2537 CG PHE A 258 5.984 172.913 165.504 1.00 75.50 C
ANISOU 2537 CG PHE A 258 10156 7880 10650 -942 29 191 C
ATOM 2538 CD1 PHE A 258 5.999 172.716 166.878 1.00 76.18 C
ANISOU 2538 CD1 PHE A 258 10289 7942 10715 -901 140 207 C
ATOM 2539 CD2 PHE A 258 6.374 174.146 165.016 1.00 76.03 C
ANISOU 2539 CD2 PHE A 258 10156 8001 10731 -853 -30 176 C
ATOM 2540 CE1 PHE A 258 6.424 173.723 167.740 1.00 76.57 C
ANISOU 2540 CE1 PHE A 258 10322 8018 10754 -776 184 208 C
ATOM 2541 CE2 PHE A 258 6.805 175.146 165.881 1.00 76.55 C
ANISOU 2541 CE2 PHE A 258 10207 8093 10787 -732 17 177 C
ATOM 2542 CZ PHE A 258 6.824 174.929 167.236 1.00 76.24 C
ANISOU 2542 CZ PHE A 258 10216 8027 10724 -695 121 193 C
ATOM 2543 N CYS A 259 5.830 168.863 162.963 1.00 79.33 N
ANISOU 2543 N CYS A 259 11010 8125 11007 -1334 -109 160 N
ATOM 2544 CA CYS A 259 5.144 167.750 162.320 1.00 81.49 C
ANISOU 2544 CA CYS A 259 11352 8342 11268 -1505 -147 164 C
ATOM 2545 C CYS A 259 6.123 166.621 162.036 1.00 82.83 C
ANISOU 2545 C CYS A 259 11770 8382 11319 -1493 -139 138 C
ATOM 2546 O CYS A 259 6.658 166.503 160.932 1.00 82.80 O
ANISOU 2546 O CYS A 259 11854 8340 11266 -1479 -213 111 O
ATOM 2547 CB CYS A 259 4.424 168.203 161.061 1.00 83.40 C
ANISOU 2547 CB CYS A 259 11479 8643 11565 -1593 -271 164 C
ATOM 2548 SG CYS A 259 3.350 166.934 160.351 1.00 90.86 S
ANISOU 2548 SG CYS A 259 12492 9529 12501 -1832 -336 174 S
ATOM 2549 N PRO A 260 6.409 165.800 163.052 1.00 83.97 N
ANISOU 2549 N PRO A 260 12041 8452 11411 -1489 -44 147 N
ATOM 2550 CA PRO A 260 7.410 164.737 162.879 1.00 84.88 C
ANISOU 2550 CA PRO A 260 12399 8442 11410 -1448 -24 126 C
ATOM 2551 C PRO A 260 7.042 163.661 161.877 1.00 85.85 C
ANISOU 2551 C PRO A 260 12671 8468 11478 -1601 -72 118 C
ATOM 2552 O PRO A 260 7.928 162.964 161.376 1.00 85.99 O
ANISOU 2552 O PRO A 260 12906 8373 11392 -1564 -56 101 O
ATOM 2553 CB PRO A 260 7.568 164.170 164.290 1.00 85.63 C
ANISOU 2553 CB PRO A 260 12571 8492 11472 -1408 91 146 C
ATOM 2554 CG PRO A 260 6.272 164.474 164.953 1.00 85.94 C
ANISOU 2554 CG PRO A 260 12462 8592 11600 -1536 127 178 C
ATOM 2555 CD PRO A 260 5.867 165.811 164.421 1.00 83.92 C
ANISOU 2555 CD PRO A 260 11974 8465 11448 -1541 52 181 C
ATOM 2556 N ASP A 261 5.749 163.507 161.602 1.00 86.28 N
ANISOU 2556 N ASP A 261 12618 8565 11600 -1771 -132 133 N
ATOM 2557 CA ASP A 261 5.326 162.536 160.613 1.00 87.30 C
ANISOU 2557 CA ASP A 261 12897 8600 11672 -1934 -192 124 C
ATOM 2558 C ASP A 261 5.033 163.168 159.249 1.00 87.57 C
ANISOU 2558 C ASP A 261 12828 8695 11750 -1999 -325 114 C
ATOM 2559 O ASP A 261 4.598 162.468 158.341 1.00 87.54 O
ANISOU 2559 O ASP A 261 12850 8665 11747 -2177 -401 119 O
ATOM 2560 CB ASP A 261 4.176 161.693 161.144 1.00 89.82 C
ANISOU 2560 CB ASP A 261 13225 8891 12012 -2118 -145 155 C
ATOM 2561 CG ASP A 261 4.629 160.793 162.286 1.00 95.68 C
ANISOU 2561 CG ASP A 261 14166 9521 12667 -2075 -24 159 C
ATOM 2562 OD1 ASP A 261 5.805 160.336 162.261 1.00 96.37 O
ANISOU 2562 OD1 ASP A 261 14476 9499 12643 -1979 -11 134 O
ATOM 2563 OD2 ASP A 261 3.818 160.545 163.202 1.00 98.59 O
ANISOU 2563 OD2 ASP A 261 14472 9910 13076 -2128 62 189 O
ATOM 2564 N CYS A 262 5.347 164.458 159.071 1.00 87.92 N
ANISOU 2564 N CYS A 262 12762 8818 11827 -1855 -358 101 N
ATOM 2565 CA CYS A 262 5.173 165.114 157.791 1.00 88.65 C
ANISOU 2565 CA CYS A 262 12766 8965 11953 -1888 -482 90 C
ATOM 2566 C CYS A 262 6.272 164.720 156.860 1.00 89.18 C
ANISOU 2566 C CYS A 262 13034 8939 11911 -1809 -509 53 C
ATOM 2567 O CYS A 262 7.430 165.095 157.055 1.00 89.29 O
ANISOU 2567 O CYS A 262 13073 8956 11895 -1637 -461 37 O
ATOM 2568 CB CYS A 262 5.101 166.631 157.928 1.00 89.22 C
ANISOU 2568 CB CYS A 262 12608 9174 12119 -1769 -492 98 C
ATOM 2569 SG CYS A 262 3.458 167.258 158.346 1.00 91.38 S
ANISOU 2569 SG CYS A 262 12594 9588 12538 -1872 -518 143 S
ATOM 2570 N SER A 263 5.891 164.009 155.793 1.00 89.20 N
ANISOU 2570 N SER A 263 13189 8853 11850 -1938 -582 40 N
ATOM 2571 CA SER A 263 6.769 163.640 154.691 1.00 89.61 C
ANISOU 2571 CA SER A 263 13440 8812 11795 -1870 -607 7 C
ATOM 2572 C SER A 263 6.956 164.961 153.957 1.00 89.36 C
ANISOU 2572 C SER A 263 13241 8888 11825 -1793 -678 0 C
ATOM 2573 O SER A 263 6.028 165.440 153.299 1.00 89.66 O
ANISOU 2573 O SER A 263 13143 8996 11930 -1901 -779 12 O
ATOM 2574 CB SER A 263 6.074 162.626 153.785 1.00 91.21 C
ANISOU 2574 CB SER A 263 13810 8914 11930 -2053 -695 -2 C
ATOM 2575 OG SER A 263 4.756 163.034 153.444 1.00 93.55 O
ANISOU 2575 OG SER A 263 13922 9301 12320 -2211 -803 19 O
ATOM 2576 N HIS A 264 8.071 165.629 154.240 1.00 88.60 N
ANISOU 2576 N HIS A 264 13146 8810 11708 -1610 -627 -16 N
ATOM 2577 CA HIS A 264 8.309 166.962 153.711 1.00 88.39 C
ANISOU 2577 CA HIS A 264 12979 8876 11729 -1530 -684 -24 C
ATOM 2578 C HIS A 264 9.826 167.280 153.699 1.00 87.49 C
ANISOU 2578 C HIS A 264 12949 8739 11553 -1353 -621 -46 C
ATOM 2579 O HIS A 264 10.652 166.441 154.085 1.00 87.63 O
ANISOU 2579 O HIS A 264 13118 8678 11499 -1287 -538 -52 O
ATOM 2580 CB HIS A 264 7.498 167.986 154.566 1.00 89.38 C
ANISOU 2580 CB HIS A 264 12847 9138 11976 -1504 -676 2 C
ATOM 2581 CG HIS A 264 7.050 169.220 153.834 1.00 91.50 C
ANISOU 2581 CG HIS A 264 12958 9497 12309 -1519 -780 6 C
ATOM 2582 ND1 HIS A 264 7.684 170.441 154.021 1.00 93.30 N
ANISOU 2582 ND1 HIS A 264 13079 9801 12570 -1386 -774 1 N
ATOM 2583 CD2 HIS A 264 6.028 169.389 152.961 1.00 92.52 C
ANISOU 2583 CD2 HIS A 264 13023 9655 12476 -1652 -897 17 C
ATOM 2584 CE1 HIS A 264 7.039 171.303 153.250 1.00 93.81 C
ANISOU 2584 CE1 HIS A 264 13031 9929 12684 -1426 -877 7 C
ATOM 2585 NE2 HIS A 264 6.036 170.717 152.590 1.00 93.66 N
ANISOU 2585 NE2 HIS A 264 13028 9887 12671 -1583 -957 18 N
ATOM 2586 N ALA A 265 10.173 168.490 153.226 1.00 86.25 N
ANISOU 2586 N ALA A 265 12691 8653 11425 -1279 -661 -55 N
ATOM 2587 CA ALA A 265 11.520 169.034 153.122 1.00 85.37 C
ANISOU 2587 CA ALA A 265 12620 8544 11272 -1123 -608 -72 C
ATOM 2588 C ALA A 265 12.528 168.137 152.398 1.00 83.80 C
ANISOU 2588 C ALA A 265 12647 8232 10959 -1081 -572 -92 C
ATOM 2589 O ALA A 265 13.453 167.604 153.019 1.00 83.95 O
ANISOU 2589 O ALA A 265 12755 8208 10934 -994 -482 -91 O
ATOM 2590 CB ALA A 265 12.052 169.443 154.493 1.00 85.68 C
ANISOU 2590 CB ALA A 265 12560 8644 11350 -1007 -518 -58 C
ATOM 2591 N PRO A 266 12.418 168.042 151.059 1.00 82.03 N
ANISOU 2591 N PRO A 266 12524 7958 10684 -1135 -642 -110 N
ATOM 2592 CA PRO A 266 13.446 167.311 150.299 1.00 80.96 C
ANISOU 2592 CA PRO A 266 12614 7714 10435 -1084 -602 -130 C
ATOM 2593 C PRO A 266 14.817 168.007 150.391 1.00 79.69 C
ANISOU 2593 C PRO A 266 12414 7598 10266 -910 -521 -135 C
ATOM 2594 O PRO A 266 14.878 169.215 150.617 1.00 79.91 O
ANISOU 2594 O PRO A 266 12284 7723 10356 -874 -547 -134 O
ATOM 2595 CB PRO A 266 12.900 167.314 148.873 1.00 81.77 C
ANISOU 2595 CB PRO A 266 12785 7782 10504 -1182 -711 -146 C
ATOM 2596 CG PRO A 266 11.958 168.460 148.810 1.00 82.27 C
ANISOU 2596 CG PRO A 266 12643 7946 10669 -1276 -814 -131 C
ATOM 2597 CD PRO A 266 11.400 168.647 150.177 1.00 81.04 C
ANISOU 2597 CD PRO A 266 12342 7855 10597 -1280 -767 -107 C
ATOM 2598 N LEU A 267 15.920 167.255 150.229 1.00 78.32 N
ANISOU 2598 N LEU A 267 12384 7356 10017 -806 -425 -138 N
ATOM 2599 CA LEU A 267 17.265 167.823 150.400 1.00 77.38 C
ANISOU 2599 CA LEU A 267 12208 7293 9898 -641 -345 -136 C
ATOM 2600 C LEU A 267 17.596 168.949 149.443 1.00 75.87 C
ANISOU 2600 C LEU A 267 11959 7153 9715 -616 -377 -149 C
ATOM 2601 O LEU A 267 18.304 169.871 149.841 1.00 76.09 O
ANISOU 2601 O LEU A 267 11849 7273 9787 -524 -343 -143 O
ATOM 2602 CB LEU A 267 18.381 166.774 150.380 1.00 77.67 C
ANISOU 2602 CB LEU A 267 12417 7248 9846 -523 -240 -135 C
ATOM 2603 CG LEU A 267 19.529 167.094 151.343 1.00 79.16 C
ANISOU 2603 CG LEU A 267 12489 7521 10067 -364 -159 -118 C
ATOM 2604 CD1 LEU A 267 19.064 167.047 152.796 1.00 79.60 C
ANISOU 2604 CD1 LEU A 267 12428 7629 10187 -372 -158 -99 C
ATOM 2605 CD2 LEU A 267 20.714 166.181 151.117 1.00 79.90 C
ANISOU 2605 CD2 LEU A 267 12736 7549 10075 -226 -58 -113 C
ATOM 2606 N TRP A 268 17.043 168.926 148.229 1.00 74.13 N
ANISOU 2606 N TRP A 268 11844 6872 9449 -706 -447 -166 N
ATOM 2607 CA TRP A 268 17.277 170.015 147.285 1.00 72.84 C
ANISOU 2607 CA TRP A 268 11642 6747 9285 -690 -480 -178 C
ATOM 2608 C TRP A 268 16.634 171.320 147.801 1.00 70.71 C
ANISOU 2608 C TRP A 268 11147 6598 9121 -723 -551 -169 C
ATOM 2609 O TRP A 268 17.198 172.395 147.616 1.00 70.62 O
ANISOU 2609 O TRP A 268 11052 6651 9130 -663 -542 -172 O
ATOM 2610 CB TRP A 268 16.760 169.641 145.886 1.00 73.03 C
ANISOU 2610 CB TRP A 268 11854 6667 9226 -784 -548 -197 C
ATOM 2611 CG TRP A 268 15.267 169.505 145.781 1.00 73.50 C
ANISOU 2611 CG TRP A 268 11896 6716 9317 -946 -676 -195 C
ATOM 2612 CD1 TRP A 268 14.530 168.364 145.915 1.00 74.20 C
ANISOU 2612 CD1 TRP A 268 12088 6728 9378 -1049 -703 -192 C
ATOM 2613 CD2 TRP A 268 14.338 170.551 145.464 1.00 73.62 C
ANISOU 2613 CD2 TRP A 268 11782 6799 9392 -1025 -795 -193 C
ATOM 2614 NE1 TRP A 268 13.197 168.639 145.719 1.00 74.54 N
ANISOU 2614 NE1 TRP A 268 12056 6796 9468 -1195 -835 -187 N
ATOM 2615 CE2 TRP A 268 13.052 169.977 145.443 1.00 74.36 C
ANISOU 2615 CE2 TRP A 268 11886 6865 9501 -1174 -894 -186 C
ATOM 2616 CE3 TRP A 268 14.471 171.924 145.208 1.00 74.11 C
ANISOU 2616 CE3 TRP A 268 11721 6942 9495 -983 -828 -194 C
ATOM 2617 CZ2 TRP A 268 11.908 170.730 145.183 1.00 74.97 C
ANISOU 2617 CZ2 TRP A 268 11838 7005 9641 -1270 -1026 -177 C
ATOM 2618 CZ3 TRP A 268 13.336 172.667 144.968 1.00 74.90 C
ANISOU 2618 CZ3 TRP A 268 11718 7093 9650 -1071 -955 -188 C
ATOM 2619 CH2 TRP A 268 12.075 172.070 144.945 1.00 75.03 C
ANISOU 2619 CH2 TRP A 268 11731 7091 9687 -1207 -1054 -178 C
ATOM 2620 N LEU A 269 15.463 171.218 148.457 1.00 68.84 N
ANISOU 2620 N LEU A 269 10820 6389 8948 -816 -615 -157 N
ATOM 2621 CA LEU A 269 14.762 172.367 149.014 1.00 67.60 C
ANISOU 2621 CA LEU A 269 10458 6339 8889 -838 -672 -145 C
ATOM 2622 C LEU A 269 15.499 172.895 150.245 1.00 67.25 C
ANISOU 2622 C LEU A 269 10279 6377 8896 -730 -592 -133 C
ATOM 2623 O LEU A 269 15.571 174.113 150.445 1.00 67.73 O
ANISOU 2623 O LEU A 269 10208 6520 9007 -694 -609 -129 O
ATOM 2624 CB LEU A 269 13.330 171.997 149.375 1.00 67.09 C
ANISOU 2624 CB LEU A 269 10337 6278 8874 -963 -746 -131 C
ATOM 2625 CG LEU A 269 12.427 173.170 149.659 1.00 68.01 C
ANISOU 2625 CG LEU A 269 10261 6496 9084 -990 -817 -117 C
ATOM 2626 CD1 LEU A 269 11.831 173.686 148.393 1.00 68.25 C
ANISOU 2626 CD1 LEU A 269 10318 6514 9102 -1073 -937 -123 C
ATOM 2627 CD2 LEU A 269 11.317 172.784 150.581 1.00 68.85 C
ANISOU 2627 CD2 LEU A 269 10248 6645 9266 -1045 -813 -93 C
ATOM 2628 N MET A 270 16.099 171.996 151.046 1.00 66.16 N
ANISOU 2628 N MET A 270 10189 6211 8737 -673 -507 -125 N
ATOM 2629 CA MET A 270 16.896 172.426 152.179 1.00 65.51 C
ANISOU 2629 CA MET A 270 10002 6201 8690 -568 -439 -113 C
ATOM 2630 C MET A 270 18.125 173.208 151.691 1.00 65.06 C
ANISOU 2630 C MET A 270 9929 6181 8611 -476 -405 -121 C
ATOM 2631 O MET A 270 18.396 174.275 152.231 1.00 65.49 O
ANISOU 2631 O MET A 270 9852 6320 8713 -437 -406 -116 O
ATOM 2632 CB MET A 270 17.277 171.257 153.090 1.00 65.91 C
ANISOU 2632 CB MET A 270 10125 6206 8711 -521 -363 -102 C
ATOM 2633 CG MET A 270 17.921 171.692 154.403 1.00 68.06 C
ANISOU 2633 CG MET A 270 10282 6555 9024 -427 -312 -85 C
ATOM 2634 SD MET A 270 17.197 173.136 155.244 1.00 72.23 S
ANISOU 2634 SD MET A 270 10604 7192 9648 -451 -357 -76 S
ATOM 2635 CE MET A 270 16.350 172.359 156.552 1.00 71.33 C
ANISOU 2635 CE MET A 270 10481 7058 9562 -498 -334 -56 C
ATOM 2636 N TYR A 271 18.797 172.749 150.607 1.00 63.96 N
ANISOU 2636 N TYR A 271 9930 5975 8396 -451 -377 -134 N
ATOM 2637 CA TYR A 271 19.946 173.475 150.050 1.00 63.11 C
ANISOU 2637 CA TYR A 271 9815 5900 8264 -374 -335 -140 C
ATOM 2638 C TYR A 271 19.518 174.803 149.435 1.00 60.91 C
ANISOU 2638 C TYR A 271 9460 5668 8015 -423 -404 -149 C
ATOM 2639 O TYR A 271 20.270 175.766 149.503 1.00 60.95 O
ANISOU 2639 O TYR A 271 9386 5737 8035 -372 -379 -148 O
ATOM 2640 CB TYR A 271 20.679 172.656 148.980 1.00 63.93 C
ANISOU 2640 CB TYR A 271 10105 5910 8275 -345 -285 -151 C
ATOM 2641 CG TYR A 271 21.467 171.473 149.487 1.00 65.84 C
ANISOU 2641 CG TYR A 271 10431 6110 8474 -252 -191 -140 C
ATOM 2642 CD1 TYR A 271 22.582 171.649 150.293 1.00 67.25 C
ANISOU 2642 CD1 TYR A 271 10508 6364 8679 -137 -122 -121 C
ATOM 2643 CD2 TYR A 271 21.189 170.192 149.042 1.00 67.37 C
ANISOU 2643 CD2 TYR A 271 10820 6185 8592 -271 -173 -146 C
ATOM 2644 CE1 TYR A 271 23.347 170.566 150.716 1.00 68.44 C
ANISOU 2644 CE1 TYR A 271 10737 6480 8789 -34 -38 -107 C
ATOM 2645 CE2 TYR A 271 21.930 169.101 149.473 1.00 68.66 C
ANISOU 2645 CE2 TYR A 271 11080 6301 8707 -170 -82 -134 C
ATOM 2646 CZ TYR A 271 23.011 169.289 150.309 1.00 69.72 C
ANISOU 2646 CZ TYR A 271 11098 6518 8874 -45 -15 -113 C
ATOM 2647 OH TYR A 271 23.752 168.198 150.705 1.00 71.64 O
ANISOU 2647 OH TYR A 271 11436 6717 9068 70 71 -97 O
ATOM 2648 N LEU A 272 18.328 174.857 148.832 1.00 59.04 N
ANISOU 2648 N LEU A 272 9255 5397 7782 -523 -495 -157 N
ATOM 2649 CA LEU A 272 17.809 176.090 148.242 1.00 57.96 C
ANISOU 2649 CA LEU A 272 9057 5296 7667 -564 -572 -163 C
ATOM 2650 C LEU A 272 17.519 177.124 149.323 1.00 56.64 C
ANISOU 2650 C LEU A 272 8712 5226 7583 -547 -589 -150 C
ATOM 2651 O LEU A 272 17.829 178.305 149.149 1.00 56.25 O
ANISOU 2651 O LEU A 272 8605 5223 7544 -524 -599 -153 O
ATOM 2652 CB LEU A 272 16.543 175.795 147.426 1.00 57.94 C
ANISOU 2652 CB LEU A 272 9124 5238 7651 -672 -675 -170 C
ATOM 2653 CG LEU A 272 15.953 176.943 146.617 1.00 58.67 C
ANISOU 2653 CG LEU A 272 9198 5347 7747 -712 -767 -176 C
ATOM 2654 CD1 LEU A 272 16.970 177.533 145.656 1.00 58.82 C
ANISOU 2654 CD1 LEU A 272 9299 5348 7703 -659 -723 -190 C
ATOM 2655 CD2 LEU A 272 14.742 176.471 145.853 1.00 59.13 C
ANISOU 2655 CD2 LEU A 272 9340 5344 7781 -819 -874 -179 C
ATOM 2656 N ALA A 273 16.967 176.672 150.453 1.00 55.73 N
ANISOU 2656 N ALA A 273 8525 5132 7518 -558 -584 -135 N
ATOM 2657 CA ALA A 273 16.691 177.550 151.585 1.00 55.55 C
ANISOU 2657 CA ALA A 273 8351 5190 7565 -534 -585 -121 C
ATOM 2658 C ALA A 273 17.982 178.103 152.219 1.00 55.27 C
ANISOU 2658 C ALA A 273 8267 5206 7526 -444 -516 -119 C
ATOM 2659 O ALA A 273 17.998 179.268 152.624 1.00 55.57 O
ANISOU 2659 O ALA A 273 8214 5304 7598 -427 -531 -115 O
ATOM 2660 CB ALA A 273 15.881 176.809 152.632 1.00 55.48 C
ANISOU 2660 CB ALA A 273 8301 5181 7598 -564 -576 -105 C
ATOM 2661 N ILE A 274 19.057 177.268 152.303 1.00 54.27 N
ANISOU 2661 N ILE A 274 8205 5058 7358 -387 -443 -118 N
ATOM 2662 CA ILE A 274 20.376 177.644 152.838 1.00 53.14 C
ANISOU 2662 CA ILE A 274 8013 4968 7210 -304 -381 -112 C
ATOM 2663 C ILE A 274 21.009 178.672 151.902 1.00 52.39 C
ANISOU 2663 C ILE A 274 7917 4895 7093 -301 -385 -122 C
ATOM 2664 O ILE A 274 21.492 179.707 152.360 1.00 52.00 O
ANISOU 2664 O ILE A 274 7781 4910 7065 -283 -384 -118 O
ATOM 2665 CB ILE A 274 21.286 176.392 152.996 1.00 53.21 C
ANISOU 2665 CB ILE A 274 8098 4943 7178 -238 -307 -105 C
ATOM 2666 CG1 ILE A 274 20.761 175.458 154.078 1.00 53.82 C
ANISOU 2666 CG1 ILE A 274 8180 4997 7270 -237 -298 -92 C
ATOM 2667 CG2 ILE A 274 22.735 176.778 153.284 1.00 53.65 C
ANISOU 2667 CG2 ILE A 274 8097 5062 7227 -152 -250 -94 C
ATOM 2668 CD1 ILE A 274 21.388 174.104 154.037 1.00 54.89 C
ANISOU 2668 CD1 ILE A 274 8428 5073 7354 -181 -236 -86 C
ATOM 2669 N VAL A 275 20.972 178.395 150.582 1.00 52.00 N
ANISOU 2669 N VAL A 275 7978 4785 6995 -327 -390 -136 N
ATOM 2670 CA VAL A 275 21.509 179.283 149.552 1.00 52.22 C
ANISOU 2670 CA VAL A 275 8034 4818 6991 -332 -388 -147 C
ATOM 2671 C VAL A 275 20.778 180.641 149.588 1.00 52.38 C
ANISOU 2671 C VAL A 275 7983 4874 7046 -377 -462 -150 C
ATOM 2672 O VAL A 275 21.423 181.690 149.488 1.00 52.72 O
ANISOU 2672 O VAL A 275 7983 4960 7087 -365 -447 -150 O
ATOM 2673 CB VAL A 275 21.539 178.601 148.147 1.00 52.55 C
ANISOU 2673 CB VAL A 275 8235 4771 6961 -351 -378 -161 C
ATOM 2674 CG1 VAL A 275 21.487 179.614 147.003 1.00 52.89 C
ANISOU 2674 CG1 VAL A 275 8322 4802 6972 -386 -410 -174 C
ATOM 2675 CG2 VAL A 275 22.766 177.704 148.009 1.00 52.90 C
ANISOU 2675 CG2 VAL A 275 8341 4796 6961 -273 -274 -155 C
ATOM 2676 N LEU A 276 19.457 180.625 149.812 1.00 51.78 N
ANISOU 2676 N LEU A 276 7887 4784 7003 -425 -536 -149 N
ATOM 2677 CA LEU A 276 18.689 181.862 149.902 1.00 51.57 C
ANISOU 2677 CA LEU A 276 7792 4791 7010 -450 -602 -147 C
ATOM 2678 C LEU A 276 19.086 182.677 151.120 1.00 51.87 C
ANISOU 2678 C LEU A 276 7722 4899 7087 -411 -575 -137 C
ATOM 2679 O LEU A 276 19.192 183.894 151.015 1.00 52.18 O
ANISOU 2679 O LEU A 276 7740 4962 7123 -410 -594 -139 O
ATOM 2680 CB LEU A 276 17.193 181.561 149.932 1.00 51.46 C
ANISOU 2680 CB LEU A 276 7759 4760 7033 -501 -680 -142 C
ATOM 2681 CG LEU A 276 16.274 182.767 150.034 1.00 52.13 C
ANISOU 2681 CG LEU A 276 7771 4881 7157 -511 -749 -135 C
ATOM 2682 CD1 LEU A 276 16.438 183.686 148.856 1.00 52.00 C
ANISOU 2682 CD1 LEU A 276 7824 4842 7094 -519 -789 -147 C
ATOM 2683 CD2 LEU A 276 14.842 182.327 150.159 1.00 52.83 C
ANISOU 2683 CD2 LEU A 276 7813 4968 7292 -557 -815 -122 C
ATOM 2684 N ALA A 277 19.318 182.023 152.269 1.00 51.71 N
ANISOU 2684 N ALA A 277 7651 4903 7094 -379 -532 -125 N
ATOM 2685 CA ALA A 277 19.730 182.720 153.490 1.00 52.15 C
ANISOU 2685 CA ALA A 277 7622 5018 7176 -345 -510 -115 C
ATOM 2686 C ALA A 277 21.114 183.352 153.315 1.00 52.53 C
ANISOU 2686 C ALA A 277 7667 5099 7193 -322 -472 -117 C
ATOM 2687 O ALA A 277 21.331 184.489 153.743 1.00 52.88 O
ANISOU 2687 O ALA A 277 7669 5181 7242 -324 -484 -116 O
ATOM 2688 CB ALA A 277 19.749 181.761 154.658 1.00 52.34 C
ANISOU 2688 CB ALA A 277 7617 5049 7221 -315 -473 -101 C
ATOM 2689 N HIS A 278 22.042 182.633 152.657 1.00 52.10 N
ANISOU 2689 N HIS A 278 7662 5031 7104 -302 -423 -120 N
ATOM 2690 CA HIS A 278 23.380 183.159 152.393 1.00 52.08 C
ANISOU 2690 CA HIS A 278 7644 5068 7077 -285 -377 -118 C
ATOM 2691 C HIS A 278 23.306 184.355 151.438 1.00 52.68 C
ANISOU 2691 C HIS A 278 7756 5133 7128 -331 -404 -131 C
ATOM 2692 O HIS A 278 24.062 185.300 151.611 1.00 52.80 O
ANISOU 2692 O HIS A 278 7733 5193 7138 -341 -391 -128 O
ATOM 2693 CB HIS A 278 24.292 182.072 151.805 1.00 52.16 C
ANISOU 2693 CB HIS A 278 7706 5059 7054 -243 -309 -115 C
ATOM 2694 CG HIS A 278 24.656 180.979 152.766 1.00 52.90 C
ANISOU 2694 CG HIS A 278 7771 5168 7161 -181 -271 -99 C
ATOM 2695 ND1 HIS A 278 25.096 179.751 152.320 1.00 54.12 N
ANISOU 2695 ND1 HIS A 278 7994 5284 7284 -132 -214 -95 N
ATOM 2696 CD2 HIS A 278 24.655 180.972 154.118 1.00 53.85 C
ANISOU 2696 CD2 HIS A 278 7815 5331 7314 -157 -282 -85 C
ATOM 2697 CE1 HIS A 278 25.352 179.036 153.403 1.00 54.50 C
ANISOU 2697 CE1 HIS A 278 8005 5354 7348 -76 -194 -78 C
ATOM 2698 NE2 HIS A 278 25.105 179.728 154.510 1.00 54.63 N
ANISOU 2698 NE2 HIS A 278 7934 5421 7403 -91 -235 -72 N
ATOM 2699 N THR A 279 22.373 184.326 150.455 1.00 53.19 N
ANISOU 2699 N THR A 279 7899 5136 7174 -363 -447 -144 N
ATOM 2700 CA THR A 279 22.124 185.403 149.472 1.00 54.03 C
ANISOU 2700 CA THR A 279 8062 5218 7248 -403 -484 -155 C
ATOM 2701 C THR A 279 21.896 186.745 150.137 1.00 54.75 C
ANISOU 2701 C THR A 279 8101 5344 7358 -415 -520 -152 C
ATOM 2702 O THR A 279 22.273 187.776 149.581 1.00 54.91 O
ANISOU 2702 O THR A 279 8159 5360 7345 -440 -522 -158 O
ATOM 2703 CB THR A 279 20.884 185.105 148.632 1.00 55.13 C
ANISOU 2703 CB THR A 279 8276 5294 7376 -432 -553 -164 C
ATOM 2704 OG1 THR A 279 20.982 183.788 148.104 1.00 56.56 O
ANISOU 2704 OG1 THR A 279 8526 5430 7534 -428 -527 -168 O
ATOM 2705 CG2 THR A 279 20.672 186.117 147.520 1.00 55.09 C
ANISOU 2705 CG2 THR A 279 8351 5255 7326 -463 -591 -175 C
ATOM 2706 N ASN A 280 21.306 186.746 151.340 1.00 54.93 N
ANISOU 2706 N ASN A 280 8050 5394 7427 -397 -543 -143 N
ATOM 2707 CA ASN A 280 21.080 187.982 152.080 1.00 55.57 C
ANISOU 2707 CA ASN A 280 8095 5499 7518 -399 -569 -139 C
ATOM 2708 C ASN A 280 22.387 188.771 152.309 1.00 55.99 C
ANISOU 2708 C ASN A 280 8139 5591 7544 -415 -529 -138 C
ATOM 2709 O ASN A 280 22.361 189.999 152.380 1.00 56.23 O
ANISOU 2709 O ASN A 280 8190 5620 7554 -436 -551 -141 O
ATOM 2710 CB ASN A 280 20.382 187.695 153.402 1.00 56.51 C
ANISOU 2710 CB ASN A 280 8145 5641 7686 -370 -577 -127 C
ATOM 2711 CG ASN A 280 20.015 188.950 154.130 1.00 59.20 C
ANISOU 2711 CG ASN A 280 8467 5998 8029 -363 -595 -122 C
ATOM 2712 OD1 ASN A 280 20.546 189.247 155.204 1.00 60.01 O
ANISOU 2712 OD1 ASN A 280 8530 6132 8139 -348 -572 -114 O
ATOM 2713 ND2 ASN A 280 19.148 189.742 153.519 1.00 59.87 N
ANISOU 2713 ND2 ASN A 280 8593 6054 8101 -368 -640 -126 N
ATOM 2714 N SER A 281 23.527 188.070 152.374 1.00 55.91 N
ANISOU 2714 N SER A 281 8099 5615 7531 -405 -472 -133 N
ATOM 2715 CA SER A 281 24.810 188.737 152.554 1.00 56.43 C
ANISOU 2715 CA SER A 281 8134 5730 7578 -430 -438 -127 C
ATOM 2716 C SER A 281 25.302 189.478 151.313 1.00 56.89 C
ANISOU 2716 C SER A 281 8260 5767 7590 -476 -420 -136 C
ATOM 2717 O SER A 281 26.261 190.226 151.403 1.00 57.07 O
ANISOU 2717 O SER A 281 8263 5827 7595 -517 -397 -131 O
ATOM 2718 CB SER A 281 25.861 187.757 153.059 1.00 57.83 C
ANISOU 2718 CB SER A 281 8239 5961 7772 -394 -385 -112 C
ATOM 2719 OG SER A 281 25.535 187.302 154.363 1.00 60.19 O
ANISOU 2719 OG SER A 281 8483 6282 8104 -360 -404 -102 O
ATOM 2720 N VAL A 282 24.649 189.289 150.167 1.00 57.01 N
ANISOU 2720 N VAL A 282 8362 5720 7581 -478 -433 -148 N
ATOM 2721 CA VAL A 282 25.019 189.923 148.903 1.00 57.62 C
ANISOU 2721 CA VAL A 282 8528 5761 7604 -518 -415 -158 C
ATOM 2722 C VAL A 282 24.201 191.191 148.625 1.00 58.33 C
ANISOU 2722 C VAL A 282 8689 5808 7666 -548 -478 -166 C
ATOM 2723 O VAL A 282 24.698 192.131 148.001 1.00 58.37 O
ANISOU 2723 O VAL A 282 8757 5797 7624 -593 -461 -170 O
ATOM 2724 CB VAL A 282 24.796 188.907 147.744 1.00 57.82 C
ANISOU 2724 CB VAL A 282 8634 5730 7604 -500 -398 -166 C
ATOM 2725 CG1 VAL A 282 25.034 189.542 146.379 1.00 58.18 C
ANISOU 2725 CG1 VAL A 282 8796 5725 7584 -540 -380 -176 C
ATOM 2726 CG2 VAL A 282 25.648 187.658 147.920 1.00 58.11 C
ANISOU 2726 CG2 VAL A 282 8624 5798 7656 -458 -324 -156 C
ATOM 2727 N VAL A 283 22.935 191.197 149.059 1.00 58.53 N
ANISOU 2727 N VAL A 283 8707 5813 7720 -519 -547 -167 N
ATOM 2728 CA VAL A 283 21.960 192.204 148.683 1.00 58.87 C
ANISOU 2728 CA VAL A 283 8820 5808 7739 -521 -613 -172 C
ATOM 2729 C VAL A 283 22.131 193.593 149.297 1.00 59.74 C
ANISOU 2729 C VAL A 283 8945 5924 7828 -539 -621 -169 C
ATOM 2730 O VAL A 283 21.816 194.550 148.594 1.00 60.09 O
ANISOU 2730 O VAL A 283 9088 5919 7824 -553 -651 -175 O
ATOM 2731 CB VAL A 283 20.519 191.705 148.901 1.00 59.02 C
ANISOU 2731 CB VAL A 283 8811 5812 7801 -479 -680 -167 C
ATOM 2732 CG1 VAL A 283 20.302 190.363 148.226 1.00 59.27 C
ANISOU 2732 CG1 VAL A 283 8855 5824 7842 -478 -682 -171 C
ATOM 2733 CG2 VAL A 283 20.175 191.614 150.373 1.00 59.54 C
ANISOU 2733 CG2 VAL A 283 8777 5922 7922 -447 -678 -156 C
ATOM 2734 N ASN A 284 22.587 193.736 150.554 1.00 59.87 N
ANISOU 2734 N ASN A 284 8887 5991 7871 -539 -600 -162 N
ATOM 2735 CA ASN A 284 22.675 195.067 151.178 1.00 60.72 C
ANISOU 2735 CA ASN A 284 9032 6091 7947 -560 -614 -161 C
ATOM 2736 C ASN A 284 23.518 196.115 150.398 1.00 61.02 C
ANISOU 2736 C ASN A 284 9168 6102 7916 -631 -594 -168 C
ATOM 2737 O ASN A 284 22.997 197.204 150.166 1.00 60.87 O
ANISOU 2737 O ASN A 284 9247 6028 7851 -633 -628 -171 O
ATOM 2738 CB ASN A 284 23.119 194.972 152.631 1.00 62.07 C
ANISOU 2738 CB ASN A 284 9122 6316 8147 -560 -598 -151 C
ATOM 2739 CG ASN A 284 22.147 194.192 153.495 1.00 65.06 C
ANISOU 2739 CG ASN A 284 9430 6707 8582 -492 -615 -144 C
ATOM 2740 OD1 ASN A 284 21.053 193.793 153.068 1.00 65.91 O
ANISOU 2740 OD1 ASN A 284 9538 6790 8716 -450 -643 -143 O
ATOM 2741 ND2 ASN A 284 22.521 193.966 154.741 1.00 65.58 N
ANISOU 2741 ND2 ASN A 284 9437 6813 8666 -486 -602 -135 N
ATOM 2742 N PRO A 285 24.739 195.817 149.903 1.00 61.40 N
ANISOU 2742 N PRO A 285 9197 6182 7950 -686 -535 -167 N
ATOM 2743 CA PRO A 285 25.477 196.824 149.110 1.00 61.48 C
ANISOU 2743 CA PRO A 285 9303 6164 7894 -762 -508 -172 C
ATOM 2744 C PRO A 285 24.717 197.339 147.890 1.00 61.63 C
ANISOU 2744 C PRO A 285 9462 6097 7860 -752 -537 -182 C
ATOM 2745 O PRO A 285 24.919 198.477 147.477 1.00 61.79 O
ANISOU 2745 O PRO A 285 9593 6071 7814 -803 -535 -186 O
ATOM 2746 CB PRO A 285 26.741 196.081 148.675 1.00 62.25 C
ANISOU 2746 CB PRO A 285 9332 6317 8002 -799 -430 -165 C
ATOM 2747 CG PRO A 285 26.910 195.009 149.688 1.00 62.92 C
ANISOU 2747 CG PRO A 285 9278 6473 8155 -752 -424 -154 C
ATOM 2748 CD PRO A 285 25.529 194.581 150.063 1.00 61.30 C
ANISOU 2748 CD PRO A 285 9077 6233 7981 -676 -484 -159 C
ATOM 2749 N PHE A 286 23.845 196.512 147.317 1.00 61.51 N
ANISOU 2749 N PHE A 286 9450 6057 7866 -692 -569 -186 N
ATOM 2750 CA PHE A 286 23.035 196.926 146.181 1.00 61.87 C
ANISOU 2750 CA PHE A 286 9624 6023 7861 -676 -616 -193 C
ATOM 2751 C PHE A 286 21.958 197.883 146.623 1.00 61.17 C
ANISOU 2751 C PHE A 286 9581 5898 7763 -633 -688 -190 C
ATOM 2752 O PHE A 286 21.723 198.866 145.938 1.00 61.39 O
ANISOU 2752 O PHE A 286 9741 5861 7725 -642 -714 -193 O
ATOM 2753 CB PHE A 286 22.423 195.721 145.471 1.00 62.40 C
ANISOU 2753 CB PHE A 286 9681 6076 7952 -635 -641 -196 C
ATOM 2754 CG PHE A 286 23.468 195.026 144.649 1.00 63.78 C
ANISOU 2754 CG PHE A 286 9879 6254 8102 -673 -563 -200 C
ATOM 2755 CD1 PHE A 286 23.739 195.439 143.358 1.00 64.84 C
ANISOU 2755 CD1 PHE A 286 10153 6325 8157 -710 -541 -208 C
ATOM 2756 CD2 PHE A 286 24.245 194.020 145.198 1.00 64.96 C
ANISOU 2756 CD2 PHE A 286 9915 6467 8299 -666 -500 -194 C
ATOM 2757 CE1 PHE A 286 24.723 194.819 142.613 1.00 65.72 C
ANISOU 2757 CE1 PHE A 286 10288 6439 8243 -739 -451 -209 C
ATOM 2758 CE2 PHE A 286 25.251 193.419 144.458 1.00 65.85 C
ANISOU 2758 CE2 PHE A 286 10046 6585 8388 -687 -414 -194 C
ATOM 2759 CZ PHE A 286 25.490 193.831 143.173 1.00 65.68 C
ANISOU 2759 CZ PHE A 286 10161 6503 8291 -724 -385 -202 C
ATOM 2760 N ILE A 287 21.327 197.630 147.773 1.00 60.17 N
ANISOU 2760 N ILE A 287 9356 5810 7698 -581 -715 -182 N
ATOM 2761 CA ILE A 287 20.296 198.517 148.283 1.00 60.11 C
ANISOU 2761 CA ILE A 287 9383 5770 7684 -523 -769 -175 C
ATOM 2762 C ILE A 287 20.865 199.897 148.588 1.00 61.43 C
ANISOU 2762 C ILE A 287 9654 5904 7784 -565 -751 -177 C
ATOM 2763 O ILE A 287 20.259 200.898 148.217 1.00 61.67 O
ANISOU 2763 O ILE A 287 9802 5869 7762 -534 -790 -176 O
ATOM 2764 CB ILE A 287 19.587 197.900 149.490 1.00 59.64 C
ANISOU 2764 CB ILE A 287 9197 5761 7704 -462 -782 -164 C
ATOM 2765 CG1 ILE A 287 19.055 196.510 149.153 1.00 59.93 C
ANISOU 2765 CG1 ILE A 287 9145 5825 7800 -439 -799 -161 C
ATOM 2766 CG2 ILE A 287 18.482 198.819 150.007 1.00 59.99 C
ANISOU 2766 CG2 ILE A 287 9276 5774 7743 -388 -826 -153 C
ATOM 2767 CD1 ILE A 287 18.070 196.482 148.023 1.00 60.80 C
ANISOU 2767 CD1 ILE A 287 9314 5891 7897 -412 -868 -160 C
ATOM 2768 N TYR A 288 22.063 199.959 149.192 1.00 62.16 N
ANISOU 2768 N TYR A 288 9712 6036 7871 -640 -695 -180 N
ATOM 2769 CA TYR A 288 22.695 201.247 149.484 1.00 63.14 C
ANISOU 2769 CA TYR A 288 9940 6127 7925 -704 -679 -182 C
ATOM 2770 C TYR A 288 23.027 201.972 148.189 1.00 64.64 C
ANISOU 2770 C TYR A 288 10276 6250 8034 -758 -669 -190 C
ATOM 2771 O TYR A 288 22.769 203.157 148.085 1.00 64.42 O
ANISOU 2771 O TYR A 288 10389 6151 7936 -761 -690 -191 O
ATOM 2772 CB TYR A 288 23.966 201.082 150.330 1.00 62.93 C
ANISOU 2772 CB TYR A 288 9829 6168 7913 -787 -632 -180 C
ATOM 2773 CG TYR A 288 23.752 200.326 151.622 1.00 63.36 C
ANISOU 2773 CG TYR A 288 9751 6285 8039 -738 -639 -172 C
ATOM 2774 CD1 TYR A 288 22.685 200.623 152.456 1.00 63.94 C
ANISOU 2774 CD1 TYR A 288 9838 6332 8123 -658 -675 -168 C
ATOM 2775 CD2 TYR A 288 24.642 199.346 152.031 1.00 64.19 C
ANISOU 2775 CD2 TYR A 288 9724 6472 8195 -768 -604 -167 C
ATOM 2776 CE1 TYR A 288 22.484 199.931 153.644 1.00 64.69 C
ANISOU 2776 CE1 TYR A 288 9825 6477 8277 -615 -673 -160 C
ATOM 2777 CE2 TYR A 288 24.452 198.648 153.216 1.00 64.99 C
ANISOU 2777 CE2 TYR A 288 9719 6622 8351 -722 -611 -159 C
ATOM 2778 CZ TYR A 288 23.376 198.947 154.025 1.00 65.66 C
ANISOU 2778 CZ TYR A 288 9828 6675 8443 -651 -644 -156 C
ATOM 2779 OH TYR A 288 23.215 198.263 155.207 1.00 67.10 O
ANISOU 2779 OH TYR A 288 9920 6900 8674 -611 -643 -148 O
ATOM 2780 N ALA A 289 23.572 201.266 147.197 1.00 66.06 N
ANISOU 2780 N ALA A 289 10438 6444 8216 -794 -634 -194 N
ATOM 2781 CA ALA A 289 23.924 201.879 145.922 1.00 67.93 C
ANISOU 2781 CA ALA A 289 10824 6614 8371 -846 -614 -200 C
ATOM 2782 C ALA A 289 22.709 202.390 145.160 1.00 69.96 C
ANISOU 2782 C ALA A 289 11213 6785 8584 -771 -686 -202 C
ATOM 2783 O ALA A 289 22.765 203.470 144.587 1.00 70.25 O
ANISOU 2783 O ALA A 289 11416 6744 8534 -800 -690 -205 O
ATOM 2784 CB ALA A 289 24.691 200.899 145.068 1.00 68.11 C
ANISOU 2784 CB ALA A 289 10799 6672 8409 -885 -552 -202 C
ATOM 2785 N TYR A 290 21.611 201.635 145.160 1.00 71.32 N
ANISOU 2785 N TYR A 290 11313 6971 8814 -677 -746 -198 N
ATOM 2786 CA TYR A 290 20.412 202.044 144.443 1.00 73.17 C
ANISOU 2786 CA TYR A 290 11645 7138 9016 -599 -829 -194 C
ATOM 2787 C TYR A 290 19.577 203.074 145.188 1.00 73.58 C
ANISOU 2787 C TYR A 290 11744 7158 9054 -529 -875 -184 C
ATOM 2788 O TYR A 290 18.823 203.798 144.541 1.00 74.11 O
ANISOU 2788 O TYR A 290 11941 7153 9063 -477 -931 -179 O
ATOM 2789 CB TYR A 290 19.554 200.828 144.043 1.00 74.38 C
ANISOU 2789 CB TYR A 290 11703 7321 9235 -540 -882 -190 C
ATOM 2790 CG TYR A 290 20.052 200.134 142.792 1.00 76.82 C
ANISOU 2790 CG TYR A 290 12064 7610 9514 -588 -861 -200 C
ATOM 2791 CD1 TYR A 290 19.867 200.699 141.538 1.00 78.49 C
ANISOU 2791 CD1 TYR A 290 12448 7737 9638 -593 -894 -204 C
ATOM 2792 CD2 TYR A 290 20.713 198.917 142.864 1.00 78.55 C
ANISOU 2792 CD2 TYR A 290 12177 7885 9782 -621 -801 -204 C
ATOM 2793 CE1 TYR A 290 20.333 200.072 140.385 1.00 79.97 C
ANISOU 2793 CE1 TYR A 290 12704 7895 9785 -636 -866 -213 C
ATOM 2794 CE2 TYR A 290 21.189 198.282 141.720 1.00 80.03 C
ANISOU 2794 CE2 TYR A 290 12430 8046 9932 -657 -768 -213 C
ATOM 2795 CZ TYR A 290 21.000 198.863 140.478 1.00 81.29 C
ANISOU 2795 CZ TYR A 290 12766 8118 10002 -667 -798 -218 C
ATOM 2796 OH TYR A 290 21.481 198.242 139.343 1.00 83.23 O
ANISOU 2796 OH TYR A 290 13096 8328 10201 -701 -758 -227 O
ATOM 2797 N ARG A 291 19.709 203.171 146.524 1.00 73.19 N
ANISOU 2797 N ARG A 291 11607 7155 9048 -521 -851 -179 N
ATOM 2798 CA ARG A 291 18.855 204.079 147.289 1.00 73.34 C
ANISOU 2798 CA ARG A 291 11675 7141 9052 -438 -884 -168 C
ATOM 2799 C ARG A 291 19.542 205.242 147.996 1.00 73.95 C
ANISOU 2799 C ARG A 291 11865 7176 9058 -493 -844 -173 C
ATOM 2800 O ARG A 291 18.857 206.190 148.371 1.00 74.27 O
ANISOU 2800 O ARG A 291 12014 7155 9052 -423 -869 -165 O
ATOM 2801 CB ARG A 291 18.039 203.289 148.315 1.00 73.91 C
ANISOU 2801 CB ARG A 291 11577 7281 9224 -356 -900 -156 C
ATOM 2802 CG ARG A 291 16.982 202.389 147.699 1.00 75.51 C
ANISOU 2802 CG ARG A 291 11691 7510 9490 -287 -961 -145 C
ATOM 2803 CD ARG A 291 15.941 201.968 148.717 1.00 77.76 C
ANISOU 2803 CD ARG A 291 11837 7847 9860 -194 -978 -127 C
ATOM 2804 NE ARG A 291 15.331 203.113 149.396 1.00 80.28 N
ANISOU 2804 NE ARG A 291 12227 8128 10149 -110 -982 -113 N
ATOM 2805 CZ ARG A 291 14.168 203.662 149.056 1.00 82.39 C
ANISOU 2805 CZ ARG A 291 12521 8369 10414 1 -1041 -93 C
ATOM 2806 NH1 ARG A 291 13.466 203.173 148.043 1.00 81.95 N
ANISOU 2806 NH1 ARG A 291 12420 8327 10389 30 -1113 -83 N
ATOM 2807 NH2 ARG A 291 13.695 204.701 149.732 1.00 82.47 N
ANISOU 2807 NH2 ARG A 291 12606 8340 10390 87 -1029 -79 N
ATOM 2808 N ILE A 292 20.852 205.175 148.224 1.00 74.03 N
ANISOU 2808 N ILE A 292 11851 7218 9057 -613 -784 -183 N
ATOM 2809 CA ILE A 292 21.562 206.219 148.967 1.00 74.76 C
ANISOU 2809 CA ILE A 292 12044 7277 9084 -687 -754 -187 C
ATOM 2810 C ILE A 292 22.651 206.894 148.141 1.00 75.70 C
ANISOU 2810 C ILE A 292 12294 7352 9117 -819 -715 -196 C
ATOM 2811 O ILE A 292 23.703 206.302 147.908 1.00 75.83 O
ANISOU 2811 O ILE A 292 12225 7429 9158 -916 -668 -200 O
ATOM 2812 CB ILE A 292 22.117 205.677 150.306 1.00 75.11 C
ANISOU 2812 CB ILE A 292 11947 7403 9188 -723 -727 -185 C
ATOM 2813 CG1 ILE A 292 21.038 204.904 151.090 1.00 76.08 C
ANISOU 2813 CG1 ILE A 292 11943 7569 9396 -598 -753 -175 C
ATOM 2814 CG2 ILE A 292 22.705 206.803 151.142 1.00 75.54 C
ANISOU 2814 CG2 ILE A 292 12118 7416 9168 -800 -712 -188 C
ATOM 2815 CD1 ILE A 292 21.524 204.194 152.314 1.00 77.32 C
ANISOU 2815 CD1 ILE A 292 11957 7806 9615 -625 -728 -172 C
ATOM 2816 N ARG A 293 22.404 208.147 147.724 1.00 76.08 N
ANISOU 2816 N ARG A 293 12553 7292 9061 -819 -729 -197 N
ATOM 2817 CA ARG A 293 23.317 208.952 146.908 1.00 76.70 C
ANISOU 2817 CA ARG A 293 12794 7307 9041 -946 -691 -205 C
ATOM 2818 C ARG A 293 24.756 208.967 147.407 1.00 75.78 C
ANISOU 2818 C ARG A 293 12616 7251 8926 -1110 -631 -208 C
ATOM 2819 O ARG A 293 25.665 208.684 146.623 1.00 75.88 O
ANISOU 2819 O ARG A 293 12603 7293 8936 -1208 -580 -210 O
ATOM 2820 CB ARG A 293 22.771 210.387 146.763 1.00 79.27 C
ANISOU 2820 CB ARG A 293 13365 7503 9251 -911 -718 -204 C
ATOM 2821 CG ARG A 293 23.725 211.417 146.136 1.00 84.23 C
ANISOU 2821 CG ARG A 293 14198 8047 9758 -1056 -676 -211 C
ATOM 2822 CD ARG A 293 22.995 212.705 145.765 1.00 88.99 C
ANISOU 2822 CD ARG A 293 15061 8505 10244 -979 -712 -208 C
ATOM 2823 NE ARG A 293 21.884 212.449 144.839 1.00 92.99 N
ANISOU 2823 NE ARG A 293 15570 8991 10769 -832 -767 -201 N
ATOM 2824 CZ ARG A 293 20.755 213.150 144.805 1.00 95.64 C
ANISOU 2824 CZ ARG A 293 16042 9242 11055 -686 -826 -191 C
ATOM 2825 NH1 ARG A 293 20.576 214.174 145.633 1.00 95.68 N
ANISOU 2825 NH1 ARG A 293 16213 9162 10980 -661 -825 -188 N
ATOM 2826 NH2 ARG A 293 19.798 212.836 143.941 1.00 95.39 N
ANISOU 2826 NH2 ARG A 293 15986 9208 11050 -564 -887 -181 N
ATOM 2827 N GLU A 294 24.972 209.292 148.694 1.00 74.68 N
ANISOU 2827 N GLU A 294 12451 7133 8791 -1140 -637 -206 N
ATOM 2828 CA GLU A 294 26.334 209.360 149.211 1.00 74.20 C
ANISOU 2828 CA GLU A 294 12328 7134 8731 -1304 -596 -206 C
ATOM 2829 C GLU A 294 27.072 208.027 149.103 1.00 73.23 C
ANISOU 2829 C GLU A 294 11973 7141 8711 -1333 -559 -200 C
ATOM 2830 O GLU A 294 28.274 208.028 148.852 1.00 73.27 O
ANISOU 2830 O GLU A 294 11935 7194 8711 -1468 -509 -196 O
ATOM 2831 CB GLU A 294 26.394 209.932 150.629 1.00 76.71 C
ANISOU 2831 CB GLU A 294 12674 7445 9026 -1332 -621 -205 C
ATOM 2832 CG GLU A 294 26.741 211.417 150.706 1.00 81.93 C
ANISOU 2832 CG GLU A 294 13571 8000 9559 -1443 -619 -210 C
ATOM 2833 CD GLU A 294 27.955 211.906 149.933 1.00 88.63 C
ANISOU 2833 CD GLU A 294 14483 8843 10351 -1626 -571 -210 C
ATOM 2834 OE1 GLU A 294 27.778 212.388 148.790 1.00 90.62 O
ANISOU 2834 OE1 GLU A 294 14871 9017 10542 -1619 -550 -214 O
ATOM 2835 OE2 GLU A 294 29.079 211.840 150.480 1.00 90.18 O
ANISOU 2835 OE2 GLU A 294 14596 9111 10558 -1778 -554 -205 O
ATOM 2836 N PHE A 295 26.359 206.903 149.235 1.00 72.19 N
ANISOU 2836 N PHE A 295 11697 7061 8669 -1207 -580 -198 N
ATOM 2837 CA PHE A 295 26.992 205.599 149.083 1.00 71.82 C
ANISOU 2837 CA PHE A 295 11452 7124 8712 -1217 -543 -193 C
ATOM 2838 C PHE A 295 27.287 205.365 147.612 1.00 71.52 C
ANISOU 2838 C PHE A 295 11456 7068 8653 -1243 -498 -195 C
ATOM 2839 O PHE A 295 28.412 205.048 147.253 1.00 71.50 O
ANISOU 2839 O PHE A 295 11377 7126 8665 -1334 -434 -189 O
ATOM 2840 CB PHE A 295 26.106 204.472 149.636 1.00 71.43 C
ANISOU 2840 CB PHE A 295 11264 7123 8755 -1082 -577 -190 C
ATOM 2841 CG PHE A 295 26.404 204.099 151.060 1.00 71.56 C
ANISOU 2841 CG PHE A 295 11156 7211 8822 -1087 -588 -183 C
ATOM 2842 CD1 PHE A 295 27.601 203.499 151.397 1.00 72.06 C
ANISOU 2842 CD1 PHE A 295 11079 7373 8929 -1165 -553 -174 C
ATOM 2843 CD2 PHE A 295 25.485 204.341 152.062 1.00 72.08 C
ANISOU 2843 CD2 PHE A 295 11251 7246 8889 -1006 -631 -183 C
ATOM 2844 CE1 PHE A 295 27.881 203.166 152.712 1.00 72.57 C
ANISOU 2844 CE1 PHE A 295 11040 7500 9033 -1168 -573 -167 C
ATOM 2845 CE2 PHE A 295 25.764 204.002 153.376 1.00 72.56 C
ANISOU 2845 CE2 PHE A 295 11218 7365 8987 -1011 -640 -176 C
ATOM 2846 CZ PHE A 295 26.959 203.416 153.692 1.00 72.26 C
ANISOU 2846 CZ PHE A 295 11048 7421 8988 -1094 -617 -169 C
ATOM 2847 N ARG A 296 26.289 205.573 146.755 1.00 71.30 N
ANISOU 2847 N ARG A 296 11553 6953 8585 -1161 -530 -202 N
ATOM 2848 CA ARG A 296 26.403 205.370 145.321 1.00 71.74 C
ANISOU 2848 CA ARG A 296 11681 6972 8607 -1171 -498 -205 C
ATOM 2849 C ARG A 296 27.569 206.139 144.720 1.00 72.16 C
ANISOU 2849 C ARG A 296 11831 7001 8585 -1319 -425 -204 C
ATOM 2850 O ARG A 296 28.341 205.570 143.962 1.00 71.97 O
ANISOU 2850 O ARG A 296 11754 7017 8573 -1370 -354 -201 O
ATOM 2851 CB ARG A 296 25.085 205.767 144.655 1.00 73.18 C
ANISOU 2851 CB ARG A 296 12008 7054 8743 -1063 -567 -210 C
ATOM 2852 CG ARG A 296 25.073 205.607 143.150 1.00 76.79 C
ANISOU 2852 CG ARG A 296 12576 7455 9148 -1068 -550 -214 C
ATOM 2853 CD ARG A 296 23.666 205.680 142.587 1.00 80.56 C
ANISOU 2853 CD ARG A 296 13149 7858 9603 -942 -641 -214 C
ATOM 2854 NE ARG A 296 23.013 206.969 142.832 1.00 83.92 N
ANISOU 2854 NE ARG A 296 13728 8200 9959 -904 -691 -212 N
ATOM 2855 CZ ARG A 296 22.026 207.161 143.701 1.00 85.81 C
ANISOU 2855 CZ ARG A 296 13925 8445 10236 -798 -754 -205 C
ATOM 2856 NH1 ARG A 296 21.487 208.364 143.846 1.00 85.65 N
ANISOU 2856 NH1 ARG A 296 14063 8338 10140 -755 -788 -200 N
ATOM 2857 NH2 ARG A 296 21.573 206.152 144.435 1.00 85.32 N
ANISOU 2857 NH2 ARG A 296 13669 8469 10281 -733 -776 -200 N
ATOM 2858 N GLN A 297 27.735 207.407 145.121 1.00 72.48 N
ANISOU 2858 N GLN A 297 12007 6982 8550 -1392 -436 -206 N
ATOM 2859 CA GLN A 297 28.803 208.272 144.641 1.00 73.13 C
ANISOU 2859 CA GLN A 297 12197 7036 8554 -1551 -371 -203 C
ATOM 2860 C GLN A 297 30.162 207.789 145.109 1.00 73.31 C
ANISOU 2860 C GLN A 297 12032 7184 8638 -1671 -305 -191 C
ATOM 2861 O GLN A 297 31.108 207.760 144.324 1.00 73.38 O
ANISOU 2861 O GLN A 297 12034 7215 8630 -1768 -222 -184 O
ATOM 2862 CB GLN A 297 28.550 209.723 145.079 1.00 75.13 C
ANISOU 2862 CB GLN A 297 12651 7186 8707 -1596 -409 -208 C
ATOM 2863 CG GLN A 297 27.368 210.368 144.347 1.00 79.32 C
ANISOU 2863 CG GLN A 297 13396 7583 9158 -1485 -459 -215 C
ATOM 2864 CD GLN A 297 27.092 211.787 144.792 1.00 83.91 C
ANISOU 2864 CD GLN A 297 14196 8051 9635 -1500 -494 -218 C
ATOM 2865 OE1 GLN A 297 27.502 212.219 145.881 1.00 85.93 O
ANISOU 2865 OE1 GLN A 297 14437 8324 9887 -1563 -502 -217 O
ATOM 2866 NE2 GLN A 297 26.384 212.539 143.955 1.00 83.74 N
ANISOU 2866 NE2 GLN A 297 14394 7903 9518 -1438 -519 -221 N
ATOM 2867 N THR A 298 30.258 207.380 146.373 1.00 73.48 N
ANISOU 2867 N THR A 298 11896 7291 8732 -1655 -340 -186 N
ATOM 2868 CA THR A 298 31.518 206.888 146.922 1.00 74.03 C
ANISOU 2868 CA THR A 298 11770 7490 8867 -1755 -295 -169 C
ATOM 2869 C THR A 298 31.934 205.600 146.251 1.00 74.59 C
ANISOU 2869 C THR A 298 11686 7642 9011 -1707 -230 -161 C
ATOM 2870 O THR A 298 33.110 205.422 145.963 1.00 74.43 O
ANISOU 2870 O THR A 298 11575 7696 9007 -1806 -151 -145 O
ATOM 2871 CB THR A 298 31.460 206.722 148.441 1.00 75.23 C
ANISOU 2871 CB THR A 298 11802 7709 9074 -1736 -357 -165 C
ATOM 2872 OG1 THR A 298 30.821 207.847 149.044 1.00 76.58 O
ANISOU 2872 OG1 THR A 298 12139 7784 9173 -1733 -422 -176 O
ATOM 2873 CG2 THR A 298 32.831 206.572 149.031 1.00 75.39 C
ANISOU 2873 CG2 THR A 298 11668 7846 9131 -1872 -328 -145 C
ATOM 2874 N PHE A 299 30.973 204.711 145.966 1.00 75.26 N
ANISOU 2874 N PHE A 299 11748 7711 9137 -1557 -258 -169 N
ATOM 2875 CA PHE A 299 31.255 203.448 145.285 1.00 76.45 C
ANISOU 2875 CA PHE A 299 11782 7919 9345 -1500 -198 -164 C
ATOM 2876 C PHE A 299 31.847 203.718 143.894 1.00 78.23 C
ANISOU 2876 C PHE A 299 12113 8103 9508 -1570 -107 -162 C
ATOM 2877 O PHE A 299 32.826 203.071 143.535 1.00 78.60 O
ANISOU 2877 O PHE A 299 12044 8229 9591 -1607 -17 -147 O
ATOM 2878 CB PHE A 299 29.993 202.569 145.163 1.00 75.89 C
ANISOU 2878 CB PHE A 299 11709 7816 9311 -1344 -256 -175 C
ATOM 2879 CG PHE A 299 29.421 201.985 146.438 1.00 75.72 C
ANISOU 2879 CG PHE A 299 11562 7845 9364 -1260 -323 -174 C
ATOM 2880 CD1 PHE A 299 30.143 202.003 147.615 1.00 76.22 C
ANISOU 2880 CD1 PHE A 299 11500 7992 9467 -1312 -326 -162 C
ATOM 2881 CD2 PHE A 299 28.152 201.441 146.459 1.00 76.00 C
ANISOU 2881 CD2 PHE A 299 11609 7842 9426 -1137 -385 -183 C
ATOM 2882 CE1 PHE A 299 29.617 201.462 148.778 1.00 76.62 C
ANISOU 2882 CE1 PHE A 299 11453 8081 9577 -1234 -382 -161 C
ATOM 2883 CE2 PHE A 299 27.628 200.906 147.623 1.00 76.45 C
ANISOU 2883 CE2 PHE A 299 11556 7944 9549 -1066 -434 -180 C
ATOM 2884 CZ PHE A 299 28.362 200.923 148.775 1.00 76.27 C
ANISOU 2884 CZ PHE A 299 11425 7996 9559 -1113 -429 -170 C
ATOM 2885 N ARG A 300 31.312 204.721 143.142 1.00 79.14 N
ANISOU 2885 N ARG A 300 12453 8093 9524 -1590 -125 -175 N
ATOM 2886 CA ARG A 300 31.830 205.094 141.813 1.00 80.34 C
ANISOU 2886 CA ARG A 300 12740 8187 9599 -1661 -39 -174 C
ATOM 2887 C ARG A 300 33.296 205.495 141.931 1.00 81.41 C
ANISOU 2887 C ARG A 300 12794 8402 9737 -1822 58 -154 C
ATOM 2888 O ARG A 300 34.126 205.028 141.156 1.00 81.62 O
ANISOU 2888 O ARG A 300 12750 8481 9782 -1851 164 -141 O
ATOM 2889 CB ARG A 300 31.073 206.301 141.214 1.00 81.88 C
ANISOU 2889 CB ARG A 300 13202 8233 9676 -1673 -84 -188 C
ATOM 2890 CG ARG A 300 29.569 206.258 141.308 1.00 85.61 C
ANISOU 2890 CG ARG A 300 13760 8627 10139 -1529 -201 -202 C
ATOM 2891 CD ARG A 300 28.943 205.879 139.988 1.00 89.41 C
ANISOU 2891 CD ARG A 300 14333 9045 10595 -1435 -213 -210 C
ATOM 2892 NE ARG A 300 27.533 206.261 139.930 1.00 92.69 N
ANISOU 2892 NE ARG A 300 14876 9368 10973 -1325 -327 -218 N
ATOM 2893 CZ ARG A 300 26.798 206.248 138.823 1.00 95.48 C
ANISOU 2893 CZ ARG A 300 15407 9620 11251 -1275 -361 -224 C
ATOM 2894 NH1 ARG A 300 25.529 206.631 138.860 1.00 95.79 N
ANISOU 2894 NH1 ARG A 300 15539 9592 11266 -1168 -472 -226 N
ATOM 2895 NH2 ARG A 300 27.330 205.865 137.666 1.00 95.25 N
ANISOU 2895 NH2 ARG A 300 15466 9557 11166 -1327 -282 -225 N
ATOM 2896 N LYS A 301 33.610 206.341 142.928 1.00 81.86 N
ANISOU 2896 N LYS A 301 12844 8476 9782 -1920 19 -150 N
ATOM 2897 CA LYS A 301 34.953 206.847 143.141 1.00 82.80 C
ANISOU 2897 CA LYS A 301 12889 8670 9901 -2094 89 -130 C
ATOM 2898 C LYS A 301 35.928 205.772 143.582 1.00 83.78 C
ANISOU 2898 C LYS A 301 12735 8961 10138 -2097 140 -105 C
ATOM 2899 O LYS A 301 37.087 205.819 143.185 1.00 83.92 O
ANISOU 2899 O LYS A 301 12672 9050 10164 -2209 241 -82 O
ATOM 2900 CB LYS A 301 34.919 208.044 144.085 1.00 84.65 C
ANISOU 2900 CB LYS A 301 13219 8863 10081 -2196 16 -134 C
ATOM 2901 CG LYS A 301 34.408 209.263 143.323 1.00 89.03 C
ANISOU 2901 CG LYS A 301 14070 9250 10507 -2217 5 -151 C
ATOM 2902 CD LYS A 301 33.550 210.240 144.116 1.00 93.30 C
ANISOU 2902 CD LYS A 301 14783 9696 10972 -2245 -85 -164 C
ATOM 2903 CE LYS A 301 32.775 211.139 143.168 1.00 96.35 C
ANISOU 2903 CE LYS A 301 15459 9913 11235 -2215 -93 -179 C
ATOM 2904 NZ LYS A 301 31.927 210.359 142.218 1.00 97.51 N
ANISOU 2904 NZ LYS A 301 15628 10021 11401 -2039 -109 -188 N
ATOM 2905 N ILE A 302 35.462 204.773 144.334 1.00 84.44 N
ANISOU 2905 N ILE A 302 12674 9104 10305 -1968 81 -107 N
ATOM 2906 CA ILE A 302 36.323 203.659 144.733 1.00 85.48 C
ANISOU 2906 CA ILE A 302 12552 9388 10541 -1945 128 -82 C
ATOM 2907 C ILE A 302 36.606 202.752 143.520 1.00 86.05 C
ANISOU 2907 C ILE A 302 12598 9469 10625 -1879 242 -75 C
ATOM 2908 O ILE A 302 37.728 202.264 143.360 1.00 86.09 O
ANISOU 2908 O ILE A 302 12443 9587 10681 -1918 338 -46 O
ATOM 2909 CB ILE A 302 35.731 202.865 145.922 1.00 86.14 C
ANISOU 2909 CB ILE A 302 12507 9522 10700 -1827 34 -85 C
ATOM 2910 CG1 ILE A 302 35.667 203.727 147.185 1.00 86.95 C
ANISOU 2910 CG1 ILE A 302 12624 9625 10787 -1902 -63 -87 C
ATOM 2911 CG2 ILE A 302 36.543 201.598 146.185 1.00 86.78 C
ANISOU 2911 CG2 ILE A 302 12346 9746 10881 -1776 87 -58 C
ATOM 2912 CD1 ILE A 302 34.779 203.154 148.215 1.00 88.13 C
ANISOU 2912 CD1 ILE A 302 12725 9776 10983 -1774 -156 -98 C
ATOM 2913 N ILE A 303 35.599 202.542 142.661 1.00 86.36 N
ANISOU 2913 N ILE A 303 12803 9394 10617 -1780 232 -98 N
ATOM 2914 CA ILE A 303 35.775 201.718 141.473 1.00 87.40 C
ANISOU 2914 CA ILE A 303 12949 9514 10743 -1719 336 -94 C
ATOM 2915 C ILE A 303 36.699 202.425 140.456 1.00 88.75 C
ANISOU 2915 C ILE A 303 13219 9659 10844 -1848 457 -83 C
ATOM 2916 O ILE A 303 37.581 201.783 139.882 1.00 88.90 O
ANISOU 2916 O ILE A 303 13163 9733 10882 -1844 584 -63 O
ATOM 2917 CB ILE A 303 34.406 201.280 140.913 1.00 87.84 C
ANISOU 2917 CB ILE A 303 13137 9465 10774 -1579 273 -121 C
ATOM 2918 CG1 ILE A 303 33.685 200.382 141.935 1.00 88.65 C
ANISOU 2918 CG1 ILE A 303 13113 9613 10957 -1470 172 -126 C
ATOM 2919 CG2 ILE A 303 34.561 200.541 139.595 1.00 88.33 C
ANISOU 2919 CG2 ILE A 303 13228 9509 10823 -1518 377 -117 C
ATOM 2920 CD1 ILE A 303 32.186 200.416 141.867 1.00 89.84 C
ANISOU 2920 CD1 ILE A 303 13392 9660 11082 -1373 63 -151 C
ATOM 2921 N ARG A 304 36.563 203.759 140.312 1.00 89.45 N
ANISOU 2921 N ARG A 304 13468 9670 10851 -1966 428 -91 N
ATOM 2922 CA ARG A 304 37.433 204.591 139.464 1.00 90.55 C
ANISOU 2922 CA ARG A 304 13709 9781 10917 -2117 538 -79 C
ATOM 2923 C ARG A 304 38.891 204.486 139.974 1.00 91.46 C
ANISOU 2923 C ARG A 304 13579 10062 11109 -2228 628 -41 C
ATOM 2924 O ARG A 304 39.789 204.173 139.201 1.00 91.90 O
ANISOU 2924 O ARG A 304 13582 10166 11171 -2263 771 -18 O
ATOM 2925 CB ARG A 304 36.930 206.059 139.466 1.00 91.82 C
ANISOU 2925 CB ARG A 304 14086 9824 10977 -2217 464 -96 C
ATOM 2926 CG ARG A 304 37.990 207.152 139.271 1.00 94.84 C
ANISOU 2926 CG ARG A 304 14515 10215 11304 -2425 548 -77 C
ATOM 2927 CD ARG A 304 37.721 208.343 140.173 1.00 98.09 C
ANISOU 2927 CD ARG A 304 15037 10570 11662 -2525 445 -88 C
ATOM 2928 NE ARG A 304 38.754 209.376 140.062 1.00101.58 N
ANISOU 2928 NE ARG A 304 15519 11024 12052 -2743 520 -69 N
ATOM 2929 CZ ARG A 304 38.738 210.364 139.168 1.00104.46 C
ANISOU 2929 CZ ARG A 304 16134 11260 12296 -2838 573 -75 C
ATOM 2930 NH1 ARG A 304 39.715 211.265 139.146 1.00104.19 N
ANISOU 2930 NH1 ARG A 304 16123 11245 12220 -3052 643 -56 N
ATOM 2931 NH2 ARG A 304 37.750 210.456 138.286 1.00104.66 N
ANISOU 2931 NH2 ARG A 304 16391 11137 12238 -2725 552 -100 N
ATOM 2932 N SER A 305 39.108 204.720 141.274 1.00 91.76 N
ANISOU 2932 N SER A 305 13467 10190 11207 -2275 542 -32 N
ATOM 2933 CA SER A 305 40.420 204.614 141.903 1.00 92.59 C
ANISOU 2933 CA SER A 305 13319 10465 11395 -2374 587 6 C
ATOM 2934 C SER A 305 40.841 203.133 141.985 1.00 93.18 C
ANISOU 2934 C SER A 305 13167 10661 11576 -2230 641 27 C
ATOM 2935 O SER A 305 40.091 202.279 142.474 1.00 93.31 O
ANISOU 2935 O SER A 305 13129 10683 11640 -2084 559 14 O
ATOM 2936 CB SER A 305 40.381 205.235 143.300 1.00 94.14 C
ANISOU 2936 CB SER A 305 13464 10697 11609 -2448 452 4 C
ATOM 2937 OG SER A 305 41.530 204.957 144.084 1.00 96.52 O
ANISOU 2937 OG SER A 305 13505 11170 11998 -2526 459 41 O
TER 2938 SER A 305
HETATM 2939 C10 RVZ A1201 21.615 178.722 159.314 1.00 60.42 C
ANISOU 2939 C10 RVZ A1201 8603 6116 8238 -116 -312 -40 C
HETATM 2940 C13 RVZ A1201 22.505 173.854 157.851 1.00 61.58 C
ANISOU 2940 C13 RVZ A1201 9106 6040 8250 -7 -171 -32 C
HETATM 2941 C21 RVZ A1201 21.175 170.896 153.227 1.00 67.05 C
ANISOU 2941 C21 RVZ A1201 10349 6377 8750 -176 -159 -91 C
HETATM 2942 C22 RVZ A1201 20.727 169.667 153.591 1.00 67.06 C
ANISOU 2942 C22 RVZ A1201 10460 6300 8721 -194 -141 -85 C
HETATM 2943 C02 RVZ A1201 20.257 172.470 158.420 1.00 61.24 C
ANISOU 2943 C02 RVZ A1201 9178 5876 8214 -138 -184 -32 C
HETATM 2944 C03 RVZ A1201 20.299 173.808 158.737 1.00 60.83 C
ANISOU 2944 C03 RVZ A1201 8998 5907 8208 -139 -215 -32 C
HETATM 2945 C04 RVZ A1201 19.083 174.448 159.390 1.00 60.63 C
ANISOU 2945 C04 RVZ A1201 8894 5906 8236 -207 -246 -29 C
HETATM 2946 C06 RVZ A1201 21.457 174.524 158.473 1.00 60.92 C
ANISOU 2946 C06 RVZ A1201 8957 5978 8213 -76 -212 -33 C
HETATM 2947 C07 RVZ A1201 21.531 176.015 158.785 1.00 60.54 C
ANISOU 2947 C07 RVZ A1201 8789 6010 8204 -87 -248 -35 C
HETATM 2948 C08 RVZ A1201 22.030 176.897 157.840 1.00 60.44 C
ANISOU 2948 C08 RVZ A1201 8745 6031 8190 -96 -265 -47 C
HETATM 2949 C09 RVZ A1201 22.103 178.249 158.111 1.00 60.43 C
ANISOU 2949 C09 RVZ A1201 8655 6091 8213 -112 -297 -49 C
HETATM 2950 C11 RVZ A1201 21.086 177.850 160.249 1.00 60.40 C
ANISOU 2950 C11 RVZ A1201 8628 6082 8239 -105 -291 -28 C
HETATM 2951 C12 RVZ A1201 21.058 176.495 159.993 1.00 60.41 C
ANISOU 2951 C12 RVZ A1201 8713 6024 8216 -93 -259 -25 C
HETATM 2952 C14 RVZ A1201 23.822 174.565 157.531 1.00 61.33 C
ANISOU 2952 C14 RVZ A1201 9003 6083 8216 58 -157 -28 C
HETATM 2953 C16 RVZ A1201 22.381 172.505 157.553 1.00 62.55 C
ANISOU 2953 C16 RVZ A1201 9364 6075 8326 5 -135 -31 C
HETATM 2954 C18 RVZ A1201 23.440 170.099 155.975 1.00 65.76 C
ANISOU 2954 C18 RVZ A1201 10075 6320 8592 118 -24 -34 C
HETATM 2955 C19 RVZ A1201 22.384 170.201 154.867 1.00 66.69 C
ANISOU 2955 C19 RVZ A1201 10261 6375 8703 -11 -71 -59 C
HETATM 2956 N01 RVZ A1201 19.040 171.767 158.767 1.00 61.21 N
ANISOU 2956 N01 RVZ A1201 9221 5816 8221 -222 -189 -29 N
HETATM 2957 N05 RVZ A1201 18.200 174.951 159.882 1.00 60.58 N
ANISOU 2957 N05 RVZ A1201 8826 5921 8271 -250 -264 -25 N
HETATM 2958 N15 RVZ A1201 24.793 175.092 157.296 1.00 61.27 N
ANISOU 2958 N15 RVZ A1201 8938 6134 8209 100 -145 -23 N
HETATM 2959 N20 RVZ A1201 22.209 171.209 153.991 1.00 66.97 N
ANISOU 2959 N20 RVZ A1201 10249 6439 8756 -69 -113 -76 N
HETATM 2960 N23 RVZ A1201 21.464 169.266 154.595 1.00 66.99 N
ANISOU 2960 N23 RVZ A1201 10428 6315 8709 -89 -85 -66 N
HETATM 2961 N24 RVZ A1201 21.281 171.837 157.868 1.00 61.81 N
ANISOU 2961 N24 RVZ A1201 9332 5918 8233 -64 -145 -32 N
HETATM 2962 S17 RVZ A1201 23.813 171.691 156.785 1.00 64.35 S
ANISOU 2962 S17 RVZ A1201 9677 6282 8492 124 -66 -25 S
HETATM 2963 C1 OLA A1202 21.834 169.281 145.684 1.00 74.07 C
HETATM 2964 O1 OLA A1202 20.775 168.621 145.839 1.00 74.24 O
HETATM 2965 O2 OLA A1202 22.891 168.995 146.299 1.00 74.24 O
HETATM 2966 C2 OLA A1202 21.835 170.461 144.722 1.00 73.44 C
HETATM 2967 C3 OLA A1202 21.878 171.775 145.495 1.00 72.82 C
HETATM 2968 C4 OLA A1202 21.876 172.986 144.572 1.00 72.39 C
HETATM 2969 C5 OLA A1202 21.831 174.276 145.386 1.00 72.15 C
HETATM 2970 C6 OLA A1202 22.104 175.510 144.527 1.00 71.92 C
HETATM 2971 C7 OLA A1202 20.828 176.244 144.109 1.00 71.49 C
HETATM 2972 C8 OLA A1202 20.976 176.851 142.715 1.00 71.03 C
HETATM 2973 C9 OLA A1202 20.146 178.103 142.603 1.00 70.76 C
HETATM 2974 C10 OLA A1202 20.739 179.291 142.525 1.00 70.66 C
HETATM 2975 C1 OLA A1203 35.172 201.231 159.314 1.00 58.36 C
HETATM 2976 O1 OLA A1203 34.677 201.368 158.166 1.00 58.85 O
HETATM 2977 O2 OLA A1203 34.987 202.063 160.240 1.00 58.36 O
HETATM 2978 C2 OLA A1203 36.038 200.014 159.587 1.00 57.56 C
HETATM 2979 C3 OLA A1203 35.526 198.789 158.828 1.00 56.72 C
HETATM 2980 C4 OLA A1203 36.280 197.529 159.239 1.00 55.93 C
HETATM 2981 C5 OLA A1203 35.381 196.526 159.948 1.00 55.17 C
HETATM 2982 C6 OLA A1203 35.013 195.362 159.036 1.00 54.67 C
HETATM 2983 C7 OLA A1203 36.052 194.244 159.067 1.00 54.28 C
HETATM 2984 C8 OLA A1203 35.522 192.992 159.765 1.00 54.05 C
HETATM 2985 C9 OLA A1203 36.026 191.740 159.080 1.00 53.89 C
HETATM 2986 C1 OLA A1204 31.791 174.462 177.270 1.00 52.54 C
HETATM 2987 O1 OLA A1204 30.931 173.578 177.043 1.00 53.17 O
HETATM 2988 O2 OLA A1204 32.943 174.172 177.652 1.00 52.72 O
HETATM 2989 C2 OLA A1204 31.421 175.918 177.065 1.00 51.55 C
HETATM 2990 C3 OLA A1204 32.241 176.847 177.963 1.00 50.58 C
HETATM 2991 C4 OLA A1204 31.423 178.078 178.338 1.00 49.65 C
HETATM 2992 C5 OLA A1204 32.241 179.167 179.020 1.00 48.83 C
HETATM 2993 C6 OLA A1204 31.299 180.218 179.597 1.00 48.17 C
HETATM 2994 C7 OLA A1204 31.348 181.533 178.827 1.00 47.55 C
HETATM 2995 C8 OLA A1204 30.079 182.350 179.054 1.00 47.06 C
HETATM 2996 C4 OLA A1205 33.652 192.404 169.015 1.00 49.64 C
HETATM 2997 C5 OLA A1205 33.544 190.884 169.108 1.00 49.96 C
HETATM 2998 C6 OLA A1205 33.762 190.387 170.538 1.00 50.40 C
HETATM 2999 C7 OLA A1205 33.595 188.866 170.695 1.00 50.59 C
HETATM 3000 C8 OLA A1205 34.174 188.352 172.026 1.00 50.43 C
HETATM 3001 C9 OLA A1205 33.639 186.980 172.390 1.00 50.13 C
HETATM 3002 C1 CLR A1206 2.918 173.564 162.695 1.00 82.18 C
HETATM 3003 C2 CLR A1206 2.703 172.051 162.580 1.00 82.16 C
HETATM 3004 C3 CLR A1206 1.749 171.667 161.454 1.00 82.05 C
HETATM 3005 C4 CLR A1206 2.292 172.186 160.128 1.00 82.20 C
HETATM 3006 C5 CLR A1206 2.658 173.660 160.217 1.00 82.26 C
HETATM 3007 C6 CLR A1206 2.300 174.445 159.176 1.00 82.29 C
HETATM 3008 C7 CLR A1206 2.385 175.956 159.225 1.00 82.24 C
HETATM 3009 C8 CLR A1206 3.515 176.403 160.144 1.00 82.20 C
HETATM 3010 C9 CLR A1206 3.375 175.725 161.535 1.00 82.09 C
HETATM 3011 C10 CLR A1206 3.461 174.189 161.407 1.00 82.11 C
HETATM 3012 C11 CLR A1206 4.354 176.277 162.619 1.00 82.07 C
HETATM 3013 C12 CLR A1206 4.402 177.824 162.603 1.00 82.14 C
HETATM 3014 C13 CLR A1206 4.616 178.421 161.189 1.00 82.42 C
HETATM 3015 C14 CLR A1206 3.495 177.936 160.255 1.00 82.37 C
HETATM 3016 C15 CLR A1206 3.605 178.777 158.985 1.00 82.41 C
HETATM 3017 C16 CLR A1206 4.067 180.131 159.536 1.00 82.39 C
HETATM 3018 C17 CLR A1206 4.427 179.939 161.027 1.00 82.36 C
HETATM 3019 C18 CLR A1206 6.021 178.032 160.686 1.00 82.67 C
HETATM 3020 C19 CLR A1206 4.895 173.730 161.166 1.00 81.92 C
HETATM 3021 C20 CLR A1206 5.511 180.845 161.661 1.00 82.14 C
HETATM 3022 C21 CLR A1206 4.963 181.401 162.983 1.00 81.98 C
HETATM 3023 C22 CLR A1206 6.148 181.854 160.678 1.00 82.07 C
HETATM 3024 C23 CLR A1206 6.489 183.250 161.210 1.00 82.08 C
HETATM 3025 C24 CLR A1206 5.505 184.307 160.715 1.00 82.09 C
HETATM 3026 C25 CLR A1206 5.127 185.288 161.824 1.00 82.28 C
HETATM 3027 C26 CLR A1206 4.852 186.665 161.234 1.00 82.49 C
HETATM 3028 C27 CLR A1206 3.942 184.834 162.680 1.00 82.23 C
HETATM 3029 O1 CLR A1206 1.678 170.241 161.390 1.00 81.91 O
HETATM 3030 NA NA A1207 23.528 189.378 157.423 1.00 38.98 NA1+
HETATM 3031 O HOH A1301 24.631 163.767 143.055 1.00 40.07 O
CONECT 397 3030
CONECT 533 1181
CONECT 549 1090
CONECT 569 1225
CONECT 674 3030
CONECT 1090 549
CONECT 1181 533
CONECT 1225 569
CONECT 2548 2569
CONECT 2569 2548
CONECT 2939 2949 2950
CONECT 2940 2946 2952 2953
CONECT 2941 2942 2959
CONECT 2942 2941 2960
CONECT 2943 2944 2956 2961
CONECT 2944 2943 2945 2946
CONECT 2945 2944 2957
CONECT 2946 2940 2944 2947
CONECT 2947 2946 2948 2951
CONECT 2948 2947 2949
CONECT 2949 2939 2948
CONECT 2950 2939 2951
CONECT 2951 2947 2950
CONECT 2952 2940 2958
CONECT 2953 2940 2961 2962
CONECT 2954 2955 2962
CONECT 2955 2954 2959 2960
CONECT 2956 2943
CONECT 2957 2945
CONECT 2958 2952
CONECT 2959 2941 2955
CONECT 2960 2942 2955
CONECT 2961 2943 2953
CONECT 2962 2953 2954
CONECT 2963 2964 2965 2966
CONECT 2964 2963
CONECT 2965 2963
CONECT 2966 2963 2967
CONECT 2967 2966 2968
CONECT 2968 2967 2969
CONECT 2969 2968 2970
CONECT 2970 2969 2971
CONECT 2971 2970 2972
CONECT 2972 2971 2973
CONECT 2973 2972 2974
CONECT 2974 2973
CONECT 2975 2976 2977 2978
CONECT 2976 2975
CONECT 2977 2975
CONECT 2978 2975 2979
CONECT 2979 2978 2980
CONECT 2980 2979 2981
CONECT 2981 2980 2982
CONECT 2982 2981 2983
CONECT 2983 2982 2984
CONECT 2984 2983 2985
CONECT 2985 2984
CONECT 2986 2987 2988 2989
CONECT 2987 2986
CONECT 2988 2986
CONECT 2989 2986 2990
CONECT 2990 2989 2991
CONECT 2991 2990 2992
CONECT 2992 2991 2993
CONECT 2993 2992 2994
CONECT 2994 2993 2995
CONECT 2995 2994
CONECT 2996 2997
CONECT 2997 2996 2998
CONECT 2998 2997 2999
CONECT 2999 2998 3000
CONECT 3000 2999 3001
CONECT 3001 3000
CONECT 3002 3003 3011
CONECT 3003 3002 3004
CONECT 3004 3003 3005 3029
CONECT 3005 3004 3006
CONECT 3006 3005 3007 3011
CONECT 3007 3006 3008
CONECT 3008 3007 3009
CONECT 3009 3008 3010 3015
CONECT 3010 3009 3011 3012
CONECT 3011 3002 3006 3010 3020
CONECT 3012 3010 3013
CONECT 3013 3012 3014
CONECT 3014 3013 3015 3018 3019
CONECT 3015 3009 3014 3016
CONECT 3016 3015 3017
CONECT 3017 3016 3018
CONECT 3018 3014 3017 3021
CONECT 3019 3014
CONECT 3020 3011
CONECT 3021 3018 3022 3023
CONECT 3022 3021
CONECT 3023 3021 3024
CONECT 3024 3023 3025
CONECT 3025 3024 3026
CONECT 3026 3025 3027 3028
CONECT 3027 3026
CONECT 3028 3026
CONECT 3029 3004
CONECT 3030 397 674
MASTER 367 0 7 18 2 0 0 6 3025 1 102 34
END