HEADER MEMBRANE PROTEIN 08-SEP-22 8GTG
TITLE CORTICOTROPIN-RELEASING HORMONE RECEPTOR 1(CRF1R) BOUND WITH BMK-I-152
TITLE 2 BY XFEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOFORM CRF-R2 OF CORTICOTROPIN-RELEASING FACTOR RECEPTOR
COMPND 3 1;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: CRF-R-1,CRF-R1,CRFR-1,CORTICOTROPIN-RELEASING HORMONE
COMPND 6 RECEPTOR 1,CRH-R-1,CRH-R1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ENDOLYSIN;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: LYSIS PROTEIN,LYSOZYME,MURAMIDASE;
COMPND 13 EC: 3.2.1.17;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CRHR1, CRFR, CRFR1, CRHR;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE T6;
SOURCE 10 ORGANISM_TAXID: 10666;
SOURCE 11 GENE: E, ECT6_00117;
SOURCE 12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.S.CHO,H.KIM
REVDAT 3 18-OCT-23 8GTG 1 JRNL
REVDAT 2 20-SEP-23 8GTG 1 JRNL
REVDAT 1 13-SEP-23 8GTG 0
JRNL AUTH H.KIM,T.LIM,G.E.HA,J.Y.LEE,J.W.KIM,N.CHANG,S.H.KIM,K.H.KIM,
JRNL AUTH 2 J.LEE,Y.CHO,B.W.KIM,A.ABRAHAMSSON,S.H.KIM,H.J.KIM,S.PARK,
JRNL AUTH 3 S.J.LEE,J.PARK,E.CHEONG,B.M.KIM,H.S.CHO
JRNL TITL STRUCTURE-BASED DRUG DISCOVERY OF A CORTICOTROPIN-RELEASING
JRNL TITL 2 HORMONE RECEPTOR 1 ANTAGONIST USING AN X-RAY FREE-ELECTRON
JRNL TITL 3 LASER.
JRNL REF EXP.MOL.MED. V. 55 2039 2023
JRNL REFN ISSN 1226-3613
JRNL PMID 37653040
JRNL DOI 10.1038/S12276-023-01082-1
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 15048
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.910
REMARK 3 FREE R VALUE TEST SET COUNT : 438
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 44.1100 - 3.9700 1.00 4916 147 0.2062 0.2233
REMARK 3 2 3.9700 - 3.1500 1.00 4862 146 0.2645 0.3206
REMARK 3 3 3.1500 - 2.7500 1.00 4832 145 0.3483 0.3977
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.534
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.809
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 81.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 3325
REMARK 3 ANGLE : 1.045 4547
REMARK 3 CHIRALITY : 0.055 534
REMARK 3 PLANARITY : 0.008 564
REMARK 3 DIHEDRAL : 13.456 454
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6934 0.1502 12.8241
REMARK 3 T TENSOR
REMARK 3 T11: 0.5561 T22: 0.3391
REMARK 3 T33: 0.5082 T12: 0.0227
REMARK 3 T13: -0.1032 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.9650 L22: 0.8636
REMARK 3 L33: 4.9235 L12: 0.1409
REMARK 3 L13: -2.1319 L23: -0.0170
REMARK 3 S TENSOR
REMARK 3 S11: 0.1658 S12: -0.1571 S13: 0.1885
REMARK 3 S21: -0.0235 S22: -0.0635 S23: -0.0198
REMARK 3 S31: -0.3520 S32: 0.1987 S33: -0.1253
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8GTG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1300032096.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-19
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER
REMARK 200 BEAMLINE : NCI
REMARK 200 X-RAY GENERATOR MODEL : PAL-XFEL BEAMLINE NCI
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.278
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15559
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 44.110
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 264.7
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 180.9
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.170
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.19.2_4158
REMARK 200 STARTING MODEL: 4K5Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M NA-CITRATE(4.5), 0.06M NACL
REMARK 280 20~30% PEG 400(W/V), PH 4.5, LIPIDIC CUBIC PHASE, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 47.83000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.32500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 47.83000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.32500
REMARK 290 SMTRY3 4 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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 TYR A 221
REMARK 465 SER A 222
REMARK 465 THR A 223
REMARK 465 GLU A 369
REMARK 465 VAL A 370
REMARK 465 ARG A 371
REMARK 465 SER A 372
REMARK 465 ALA A 373
REMARK 465 ALA A 374
REMARK 465 ALA A 375
REMARK 465 ALA A 376
REMARK 465 HIS A 377
REMARK 465 HIS A 378
REMARK 465 HIS A 379
REMARK 465 HIS A 380
REMARK 465 HIS A 381
REMARK 465 HIS A 382
REMARK 465 HIS A 383
REMARK 465 HIS A 384
REMARK 465 HIS A 385
REMARK 465 HIS A 386
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 103 CG SD CE
REMARK 470 ILE A 105 CG1 CG2 CD1
REMARK 470 GLU A 108 CG CD OE1 OE2
REMARK 470 GLU A 109 CG CD OE1 OE2
REMARK 470 LYS A 110 CG CD CE NZ
REMARK 470 LYS A 111 CG CD CE NZ
REMARK 470 LYS A 113 CG CD CE NZ
REMARK 470 ARG A 143 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 145 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 148 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 225 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 262 CG CD CE NZ
REMARK 470 ARG A 263 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 267 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 297 CG CD CE NZ
REMARK 470 ARG A 299 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 310 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 311 CG CD CE NZ
REMARK 470 LYS A 314 CG CD CE NZ
REMARK 470 ASN A 333 CG OD1 ND2
REMARK 470 GLU A 336 CG CD OE1 OE2
REMARK 470 GLU A 338 CG CD OE1 OE2
REMARK 470 ARG A 341 CG CD NE CZ NH1 NH2
REMARK 470 ARG B1006 CG CD NE CZ NH1 NH2
REMARK 470 ARG B1012 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1014 CG CD CE NZ
REMARK 470 LYS B1017 CG CD CE NZ
REMARK 470 TYR B1023 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B1033 CG CD CE NZ
REMARK 470 LYS B1041 CG CD CE NZ
REMARK 470 GLU B1043 CG CD OE1 OE2
REMARK 470 LYS B1046 CG CD CE NZ
REMARK 470 ARG B1050 CG CD NE CZ NH1 NH2
REMARK 470 GLU B1060 CG CD OE1 OE2
REMARK 470 ARG B1074 CG CD NE CZ NH1 NH2
REMARK 470 ARG B1078 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1081 CG CD CE NZ
REMARK 470 ARG B1117 CG CD NE CZ NH1 NH2
REMARK 470 GLU B1126 CG CD OE1 OE2
REMARK 470 LYS B1133 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N ASP A 224 O TYR B 1159 2.11
REMARK 500 OD2 ASP B 1045 CB SER B 1052 2.17
REMARK 500 OD1 ASP B 1008 OH TYR B 1159 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 333 73.54 59.75
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8GTG A 104 373 UNP P34998-2 CRFR1_HUMAN 104 373
DBREF1 8GTG B 1000 1159 UNP A0A346FJK3_BPT6
DBREF2 8GTG B A0A346FJK3 2 161
SEQADV 8GTG MET A 103 UNP P34998-2 INITIATING METHIONINE
SEQADV 8GTG ALA A 120 UNP P34998-2 VAL 120 ENGINEERED MUTATION
SEQADV 8GTG ALA A 144 UNP P34998-2 LEU 144 ENGINEERED MUTATION
SEQADV 8GTG ALA A 156 UNP P34998-2 TRP 156 ENGINEERED MUTATION
SEQADV 8GTG ALA A 160 UNP P34998-2 SER 160 ENGINEERED MUTATION
SEQADV 8GTG ALA A 228 UNP P34998-2 LYS 228 ENGINEERED MUTATION
SEQADV 8GTG ALA A 260 UNP P34998-2 PHE 260 ENGINEERED MUTATION
SEQADV 8GTG ALA A 277 UNP P34998-2 ILE 277 ENGINEERED MUTATION
SEQADV 8GTG ALA A 309 UNP P34998-2 TYR 309 ENGINEERED MUTATION
SEQADV 8GTG ALA A 330 UNP P34998-2 PHE 330 ENGINEERED MUTATION
SEQADV 8GTG ALA A 349 UNP P34998-2 SER 349 ENGINEERED MUTATION
SEQADV 8GTG ALA A 363 UNP P34998-2 TYR 363 ENGINEERED MUTATION
SEQADV 8GTG ALA A 374 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG ALA A 375 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG ALA A 376 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG HIS A 377 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG HIS A 378 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG HIS A 379 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG HIS A 380 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG HIS A 381 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG HIS A 382 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG HIS A 383 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG HIS A 384 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG HIS A 385 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG HIS A 386 UNP P34998-2 EXPRESSION TAG
SEQADV 8GTG SER B 1052 UNP A0A346FJK CYS 54 ENGINEERED MUTATION
SEQADV 8GTG SER B 1095 UNP A0A346FJK CYS 97 ENGINEERED MUTATION
SEQRES 1 A 284 MET GLU ILE LEU ASN GLU GLU LYS LYS SER LYS VAL HIS
SEQRES 2 A 284 TYR HIS VAL ALA ALA ILE ILE ASN TYR LEU GLY HIS CYS
SEQRES 3 A 284 ILE SER LEU VAL ALA LEU LEU VAL ALA PHE VAL LEU PHE
SEQRES 4 A 284 LEU ARG ALA ARG SER ILE ARG CYS LEU ARG ASN ILE ILE
SEQRES 5 A 284 HIS ALA ASN LEU ILE ALA ALA PHE ILE LEU ARG ASN ALA
SEQRES 6 A 284 THR TRP PHE VAL VAL GLN LEU THR MET SER PRO GLU VAL
SEQRES 7 A 284 HIS GLN SER ASN VAL GLY TRP CYS ARG LEU VAL THR ALA
SEQRES 8 A 284 ALA TYR ASN TYR PHE HIS VAL THR ASN PHE PHE TRP MET
SEQRES 9 A 284 PHE GLY GLU GLY CYS TYR LEU HIS THR ALA ILE VAL LEU
SEQRES 10 A 284 THR TYR SER THR ASP ARG LEU ARG ALA TRP MET PHE ILE
SEQRES 11 A 284 CYS ILE GLY TRP GLY VAL PRO PHE PRO ILE ILE VAL ALA
SEQRES 12 A 284 TRP ALA ILE GLY LYS LEU TYR TYR ASP ASN GLU LYS CYS
SEQRES 13 A 284 TRP ALA GLY LYS ARG PRO GLY VAL TYR THR ASP TYR ILE
SEQRES 14 A 284 TYR GLN GLY PRO MET ALA LEU VAL LEU LEU ILE ASN PHE
SEQRES 15 A 284 ILE PHE LEU PHE ASN ILE VAL ARG ILE LEU MET THR LYS
SEQRES 16 A 284 LEU ARG ALA SER THR THR SER GLU THR ILE GLN ALA ARG
SEQRES 17 A 284 LYS ALA VAL LYS ALA THR LEU VAL LEU LEU PRO LEU LEU
SEQRES 18 A 284 GLY ILE THR TYR MET LEU ALA PHE VAL ASN PRO GLY GLU
SEQRES 19 A 284 ASP GLU VAL SER ARG VAL VAL PHE ILE TYR PHE ASN ALA
SEQRES 20 A 284 PHE LEU GLU SER PHE GLN GLY PHE PHE VAL SER VAL PHE
SEQRES 21 A 284 ALA CYS PHE LEU ASN SER GLU VAL ARG SER ALA ALA ALA
SEQRES 22 A 284 ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 160 ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG
SEQRES 2 B 160 LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE
SEQRES 3 B 160 GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU SER
SEQRES 4 B 160 VAL ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN
SEQRES 5 B 160 SER ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU
SEQRES 6 B 160 PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU
SEQRES 7 B 160 ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP
SEQRES 8 B 160 ALA VAL ARG ARG SER ALA LEU ILE ASN MET VAL PHE GLN
SEQRES 9 B 160 MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU
SEQRES 10 B 160 ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL
SEQRES 11 B 160 ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN
SEQRES 12 B 160 ARG ALA LYS ARG VAL ILE ALA THR PHE ARG THR GLY THR
SEQRES 13 B 160 TRP ASP ALA TYR
HET CW9 A 401 59
HETNAM CW9 8-(4-BROMANYL-2,6-DIMETHOXY-PHENYL)-~{N},~{N}-BIS(2-
HETNAM 2 CW9 METHOXYETHYL)-2,7-DIMETHYL-PYRAZOLO[1,5-A][1,3,
HETNAM 3 CW9 5]TRIAZIN-4-AMINE
FORMUL 3 CW9 C21 H28 BR N5 O4
HELIX 1 AA1 MET A 103 ALA A 144 1 42
HELIX 2 AA2 ARG A 145 ARG A 148 5 4
HELIX 3 AA3 CYS A 149 MET A 176 1 28
HELIX 4 AA4 SER A 177 ASN A 184 1 8
HELIX 5 AA5 VAL A 185 ILE A 217 1 33
HELIX 6 AA6 ARG A 227 TRP A 236 1 10
HELIX 7 AA7 VAL A 238 ASP A 254 1 17
HELIX 8 AA8 GLU A 256 ALA A 260 5 5
HELIX 9 AA9 ASP A 269 THR A 296 1 28
HELIX 10 AB1 THR A 303 ALA A 330 1 28
HELIX 11 AB2 ASP A 337 PHE A 354 1 18
HELIX 12 AB3 PHE A 354 LEU A 366 1 13
HELIX 13 AB4 ILE B 1001 GLU B 1009 1 9
HELIX 14 AB5 SER B 1036 GLY B 1049 1 14
HELIX 15 AB6 THR B 1057 ASN B 1079 1 23
HELIX 16 AB7 LYS B 1081 LEU B 1089 1 9
HELIX 17 AB8 ASP B 1090 GLY B 1111 1 22
HELIX 18 AB9 PHE B 1112 GLN B 1121 1 10
HELIX 19 AC1 ARG B 1123 LYS B 1133 1 11
HELIX 20 AC2 SER B 1134 THR B 1140 1 7
HELIX 21 AC3 THR B 1140 GLY B 1154 1 15
SHEET 1 AA1 3 ARG B1012 LYS B1017 0
SHEET 2 AA1 3 TYR B1023 GLY B1026 -1 O THR B1024 N TYR B1016
SHEET 3 AA1 3 HIS B1029 THR B1032 -1 O LEU B1031 N TYR B1023
SSBOND 1 CYS A 188 CYS A 258 1555 1555 2.00
CRYST1 95.660 70.650 86.750 90.00 97.82 90.00 C 1 2 1 4
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 0.010454 0.000000 0.001436 0.00000
SCALE2 0.000000 0.014154 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011636 0.00000
ATOM 1 N MET A 103 40.086 3.260 -38.716 1.00135.51 N
ANISOU 1 N MET A 103 20135 17551 13800 -593 2828 1417 N
ATOM 2 CA MET A 103 41.489 3.634 -38.771 1.00138.32 C
ANISOU 2 CA MET A 103 20390 17978 14189 -778 3053 1394 C
ATOM 3 C MET A 103 41.956 3.968 -37.362 1.00145.07 C
ANISOU 3 C MET A 103 21066 18781 15273 -898 3038 1344 C
ATOM 4 O MET A 103 41.765 3.169 -36.450 1.00146.64 O
ANISOU 4 O MET A 103 21088 19008 15622 -801 2891 1240 O
ATOM 5 CB MET A 103 41.675 4.812 -39.711 1.00137.81 C
ANISOU 5 CB MET A 103 20564 17847 13950 -896 3237 1557 C
ATOM 6 N GLU A 104 42.566 5.140 -37.168 1.00152.81 N
ANISOU 6 N GLU A 104 22100 19689 16269 -1123 3202 1412 N
ATOM 7 CA GLU A 104 42.898 5.559 -35.811 1.00154.05 C
ANISOU 7 CA GLU A 104 22109 19803 16619 -1270 3183 1358 C
ATOM 8 C GLU A 104 41.642 5.672 -34.959 1.00152.93 C
ANISOU 8 C GLU A 104 22057 19462 16585 -1139 2967 1396 C
ATOM 9 O GLU A 104 41.686 5.423 -33.748 1.00153.20 O
ANISOU 9 O GLU A 104 21906 19509 16793 -1155 2861 1309 O
ATOM 10 CB GLU A 104 43.662 6.886 -35.827 1.00155.84 C
ANISOU 10 CB GLU A 104 22439 19959 16815 -1580 3422 1413 C
ATOM 11 CG GLU A 104 45.125 6.776 -36.246 1.00159.31 C
ANISOU 11 CG GLU A 104 22678 20658 17194 -1777 3636 1331 C
ATOM 12 CD GLU A 104 45.972 6.021 -35.236 1.00161.24 C
ANISOU 12 CD GLU A 104 22514 21172 17579 -1810 3585 1171 C
ATOM 13 OE1 GLU A 104 45.664 6.071 -34.026 1.00159.97 O
ANISOU 13 OE1 GLU A 104 22254 20957 17570 -1821 3450 1126 O
ATOM 14 OE2 GLU A 104 46.950 5.372 -35.654 1.00166.99 O1-
ANISOU 14 OE2 GLU A 104 23015 22181 18253 -1805 3686 1098 O1-
ATOM 15 N ILE A 105 40.510 6.016 -35.576 1.00156.39 N
ANISOU 15 N ILE A 105 22762 19750 16909 -993 2896 1531 N
ATOM 16 CA ILE A 105 39.240 6.008 -34.860 1.00153.20 C
ANISOU 16 CA ILE A 105 22421 19204 16585 -833 2682 1569 C
ATOM 17 C ILE A 105 38.974 4.627 -34.273 1.00153.34 C
ANISOU 17 C ILE A 105 22202 19349 16712 -688 2482 1419 C
ATOM 18 O ILE A 105 38.527 4.496 -33.126 1.00150.90 O
ANISOU 18 O ILE A 105 21801 18970 16563 -654 2340 1374 O
ATOM 19 CB ILE A 105 38.104 6.460 -35.796 1.00146.29 C
ANISOU 19 CB ILE A 105 21826 18241 15518 -662 2641 1745 C
ATOM 20 N LEU A 106 39.255 3.574 -35.047 1.00138.36 N
ANISOU 20 N LEU A 106 20223 17624 14722 -604 2489 1337 N
ATOM 21 CA LEU A 106 39.022 2.210 -34.576 1.00140.24 C
ANISOU 21 CA LEU A 106 20289 17949 15047 -464 2345 1193 C
ATOM 22 C LEU A 106 39.963 1.845 -33.433 1.00141.48 C
ANISOU 22 C LEU A 106 20182 18179 15397 -523 2368 1087 C
ATOM 23 O LEU A 106 39.567 1.138 -32.497 1.00140.97 O
ANISOU 23 O LEU A 106 20002 18097 15465 -422 2224 1013 O
ATOM 24 CB LEU A 106 39.169 1.218 -35.731 1.00138.95 C
ANISOU 24 CB LEU A 106 20145 17927 14722 -375 2396 1124 C
ATOM 25 CG LEU A 106 38.627 -0.192 -35.470 1.00139.56 C
ANISOU 25 CG LEU A 106 20152 18039 14836 -224 2266 984 C
ATOM 26 CD1 LEU A 106 37.161 -0.159 -35.037 1.00137.79 C
ANISOU 26 CD1 LEU A 106 20017 17712 14623 -146 2047 1013 C
ATOM 27 CD2 LEU A 106 38.800 -1.049 -36.705 1.00136.07 C
ANISOU 27 CD2 LEU A 106 19778 17716 14208 -173 2359 909 C
ATOM 28 N ASN A 107 41.219 2.298 -33.499 1.00140.20 N
ANISOU 28 N ASN A 107 19908 18127 15235 -688 2554 1080 N
ATOM 29 CA ASN A 107 42.151 2.053 -32.402 1.00139.77 C
ANISOU 29 CA ASN A 107 19565 18210 15330 -754 2576 992 C
ATOM 30 C ASN A 107 41.699 2.759 -31.122 1.00138.01 C
ANISOU 30 C ASN A 107 19329 17853 15254 -843 2466 1009 C
ATOM 31 O ASN A 107 41.857 2.223 -30.018 1.00136.97 O
ANISOU 31 O ASN A 107 18986 17798 15259 -794 2373 934 O
ATOM 32 CB ASN A 107 43.562 2.491 -32.809 1.00141.93 C
ANISOU 32 CB ASN A 107 19709 18680 15538 -946 2805 980 C
ATOM 33 CG ASN A 107 44.617 2.116 -31.780 1.00143.42 C
ANISOU 33 CG ASN A 107 19542 19114 15837 -992 2832 888 C
ATOM 34 OD1 ASN A 107 44.319 1.959 -30.591 1.00142.72 O
ANISOU 34 OD1 ASN A 107 19338 19004 15887 -954 2692 854 O
ATOM 35 ND2 ASN A 107 45.853 1.956 -32.235 1.00143.37 N
ANISOU 35 ND2 ASN A 107 19347 19373 15754 -1060 3013 852 N
ATOM 36 N GLU A 108 41.154 3.974 -31.248 1.00147.73 N
ANISOU 36 N GLU A 108 20797 18883 16452 -963 2493 1114 N
ATOM 37 CA GLU A 108 40.560 4.637 -30.091 1.00144.72 C
ANISOU 37 CA GLU A 108 20453 18334 16198 -1023 2395 1131 C
ATOM 38 C GLU A 108 39.347 3.867 -29.581 1.00143.58 C
ANISOU 38 C GLU A 108 20317 18106 16129 -787 2157 1118 C
ATOM 39 O GLU A 108 39.141 3.758 -28.369 1.00144.34 O
ANISOU 39 O GLU A 108 20294 18176 16370 -785 2045 1067 O
ATOM 40 CB GLU A 108 40.176 6.076 -30.439 1.00139.93 C
ANISOU 40 CB GLU A 108 20152 17494 15520 -1158 2510 1263 C
ATOM 41 N GLU A 109 38.528 3.330 -30.491 1.00140.96 N
ANISOU 41 N GLU A 109 20122 17751 15687 -608 2083 1155 N
ATOM 42 CA GLU A 109 37.382 2.527 -30.073 1.00141.22 C
ANISOU 42 CA GLU A 109 20152 17738 15768 -418 1871 1122 C
ATOM 43 C GLU A 109 37.821 1.264 -29.332 1.00146.16 C
ANISOU 43 C GLU A 109 20537 18484 16511 -338 1812 983 C
ATOM 44 O GLU A 109 37.193 0.874 -28.341 1.00147.00 O
ANISOU 44 O GLU A 109 20583 18532 16738 -262 1663 944 O
ATOM 45 CB GLU A 109 36.512 2.175 -31.282 1.00135.86 C
ANISOU 45 CB GLU A 109 19643 17072 14906 -286 1822 1168 C
ATOM 46 N LYS A 110 38.888 0.601 -29.797 1.00143.03 N
ANISOU 46 N LYS A 110 20012 18257 16076 -334 1941 918 N
ATOM 47 CA LYS A 110 39.363 -0.606 -29.114 1.00143.98 C
ANISOU 47 CA LYS A 110 19921 18490 16293 -211 1919 813 C
ATOM 48 C LYS A 110 39.952 -0.285 -27.739 1.00144.51 C
ANISOU 48 C LYS A 110 19771 18625 16513 -289 1896 795 C
ATOM 49 O LYS A 110 39.848 -1.098 -26.814 1.00143.93 O
ANISOU 49 O LYS A 110 19565 18576 16544 -161 1806 741 O
ATOM 50 CB LYS A 110 40.383 -1.354 -29.981 1.00142.25 C
ANISOU 50 CB LYS A 110 19625 18445 15980 -154 2088 764 C
ATOM 51 N LYS A 111 40.584 0.885 -27.582 1.00155.18 N
ANISOU 51 N LYS A 111 21087 20013 17863 -511 1990 834 N
ATOM 52 CA LYS A 111 41.154 1.251 -26.285 1.00151.47 C
ANISOU 52 CA LYS A 111 20402 19644 17508 -631 1973 798 C
ATOM 53 C LYS A 111 40.067 1.455 -25.233 1.00151.36 C
ANISOU 53 C LYS A 111 20458 19441 17612 -599 1793 806 C
ATOM 54 O LYS A 111 40.288 1.200 -24.046 1.00147.34 O
ANISOU 54 O LYS A 111 19754 19022 17207 -592 1721 757 O
ATOM 55 CB LYS A 111 42.017 2.509 -26.416 1.00148.78 C
ANISOU 55 CB LYS A 111 20045 19370 17115 -934 2140 816 C
ATOM 56 N SER A 112 38.891 1.940 -25.642 1.00157.00 N
ANISOU 56 N SER A 112 21438 19917 18297 -571 1722 875 N
ATOM 57 CA SER A 112 37.800 2.141 -24.689 1.00156.06 C
ANISOU 57 CA SER A 112 21386 19628 18280 -524 1557 887 C
ATOM 58 C SER A 112 37.122 0.828 -24.305 1.00153.78 C
ANISOU 58 C SER A 112 21034 19345 18048 -301 1402 832 C
ATOM 59 O SER A 112 36.595 0.711 -23.194 1.00153.68 O
ANISOU 59 O SER A 112 20967 19274 18149 -265 1277 809 O
ATOM 60 CB SER A 112 36.766 3.123 -25.253 1.00157.25 C
ANISOU 60 CB SER A 112 21828 19557 18362 -536 1546 998 C
ATOM 61 OG SER A 112 35.963 2.526 -26.257 1.00155.84 O
ANISOU 61 OG SER A 112 21775 19362 18074 -365 1482 1031 O
ATOM 62 N LYS A 113 37.087 -0.152 -25.209 1.00141.12 N
ANISOU 62 N LYS A 113 19463 17795 16361 -166 1424 804 N
ATOM 63 CA LYS A 113 36.454 -1.425 -24.883 1.00136.86 C
ANISOU 63 CA LYS A 113 18905 17232 15862 15 1316 736 C
ATOM 64 C LYS A 113 37.247 -2.176 -23.823 1.00131.19 C
ANISOU 64 C LYS A 113 17956 16635 15257 89 1327 679 C
ATOM 65 O LYS A 113 36.666 -2.877 -22.989 1.00127.61 O
ANISOU 65 O LYS A 113 17477 16120 14888 200 1220 643 O
ATOM 66 CB LYS A 113 36.294 -2.281 -26.139 1.00136.52 C
ANISOU 66 CB LYS A 113 18979 17211 15684 108 1373 700 C
ATOM 67 N VAL A 114 38.575 -2.063 -23.859 1.00131.78 N
ANISOU 67 N VAL A 114 17851 16905 15315 38 1463 677 N
ATOM 68 CA VAL A 114 39.408 -2.748 -22.876 1.00129.65 C
ANISOU 68 CA VAL A 114 17326 16816 15119 139 1481 646 C
ATOM 69 C VAL A 114 39.185 -2.156 -21.484 1.00128.08 C
ANISOU 69 C VAL A 114 17019 16612 15033 47 1361 650 C
ATOM 70 O VAL A 114 39.040 -2.886 -20.497 1.00125.30 O
ANISOU 70 O VAL A 114 16564 16284 14761 188 1282 632 O
ATOM 71 CB VAL A 114 40.887 -2.686 -23.298 1.00128.55 C
ANISOU 71 CB VAL A 114 16986 16951 14906 100 1657 648 C
ATOM 72 CG1 VAL A 114 41.529 -1.404 -22.815 1.00132.15 C
ANISOU 72 CG1 VAL A 114 17305 17538 15369 -171 1686 660 C
ATOM 73 CG2 VAL A 114 41.650 -3.891 -22.803 1.00125.95 C
ANISOU 73 CG2 VAL A 114 16445 16818 14594 341 1712 632 C
ATOM 74 N HIS A 115 39.155 -0.818 -21.390 1.00119.83 N
ANISOU 74 N HIS A 115 16021 15523 13988 -192 1364 674 N
ATOM 75 CA HIS A 115 38.943 -0.144 -20.107 1.00118.68 C
ANISOU 75 CA HIS A 115 15801 15356 13934 -314 1273 664 C
ATOM 76 C HIS A 115 37.548 -0.418 -19.546 1.00115.08 C
ANISOU 76 C HIS A 115 15493 14671 13562 -198 1104 670 C
ATOM 77 O HIS A 115 37.386 -0.577 -18.330 1.00109.24 O
ANISOU 77 O HIS A 115 14640 13955 12911 -174 1008 646 O
ATOM 78 CB HIS A 115 39.169 1.369 -20.253 1.00121.66 C
ANISOU 78 CB HIS A 115 16266 15681 14278 -608 1360 681 C
ATOM 79 CG HIS A 115 40.562 1.757 -20.667 1.00124.69 C
ANISOU 79 CG HIS A 115 16486 16315 14575 -788 1536 658 C
ATOM 80 ND1 HIS A 115 40.817 2.560 -21.761 1.00129.01 N
ANISOU 80 ND1 HIS A 115 17196 16796 15026 -946 1683 693 N
ATOM 81 CD2 HIS A 115 41.769 1.482 -20.118 1.00124.39 C
ANISOU 81 CD2 HIS A 115 16124 16620 14517 -839 1592 608 C
ATOM 82 CE1 HIS A 115 42.120 2.742 -21.882 1.00125.78 C
ANISOU 82 CE1 HIS A 115 16574 16668 14549 -1108 1827 653 C
ATOM 83 NE2 HIS A 115 42.721 2.099 -20.897 1.00126.23 N
ANISOU 83 NE2 HIS A 115 16318 16998 14645 -1044 1771 600 N
ATOM 84 N TYR A 116 36.524 -0.443 -20.409 1.00117.19 N
ANISOU 84 N TYR A 116 15998 14743 13785 -134 1065 702 N
ATOM 85 CA TYR A 116 35.192 -0.861 -19.974 1.00113.81 C
ANISOU 85 CA TYR A 116 15681 14149 13412 -16 909 698 C
ATOM 86 C TYR A 116 35.196 -2.310 -19.501 1.00107.25 C
ANISOU 86 C TYR A 116 14753 13372 12627 173 868 641 C
ATOM 87 O TYR A 116 34.498 -2.657 -18.543 1.00102.85 O
ANISOU 87 O TYR A 116 14183 12741 12154 235 752 623 O
ATOM 88 CB TYR A 116 34.175 -0.689 -21.104 1.00117.27 C
ANISOU 88 CB TYR A 116 16353 14453 13752 18 882 739 C
ATOM 89 CG TYR A 116 33.762 0.735 -21.424 1.00120.28 C
ANISOU 89 CG TYR A 116 16893 14717 14091 -100 903 828 C
ATOM 90 CD1 TYR A 116 34.626 1.803 -21.217 1.00121.50 C
ANISOU 90 CD1 TYR A 116 17022 14884 14257 -283 1022 852 C
ATOM 91 CD2 TYR A 116 32.487 1.010 -21.906 1.00124.26 C
ANISOU 91 CD2 TYR A 116 17577 15107 14530 -27 818 890 C
ATOM 92 CE1 TYR A 116 34.232 3.106 -21.498 1.00122.69 C
ANISOU 92 CE1 TYR A 116 17373 14878 14366 -380 1079 940 C
ATOM 93 CE2 TYR A 116 32.087 2.302 -22.187 1.00124.65 C
ANISOU 93 CE2 TYR A 116 17795 15038 14530 -81 859 998 C
ATOM 94 CZ TYR A 116 32.961 3.347 -21.983 1.00124.18 C
ANISOU 94 CZ TYR A 116 17754 14933 14493 -253 1001 1025 C
ATOM 95 OH TYR A 116 32.555 4.633 -22.265 1.00125.04 O
ANISOU 95 OH TYR A 116 18082 14878 14549 -296 1080 1140 O
ATOM 96 N HIS A 117 35.941 -3.180 -20.191 1.00110.49 N
ANISOU 96 N HIS A 117 15118 13888 12974 274 982 618 N
ATOM 97 CA HIS A 117 36.075 -4.564 -19.746 1.00106.77 C
ANISOU 97 CA HIS A 117 14585 13445 12538 476 995 577 C
ATOM 98 C HIS A 117 36.804 -4.640 -18.409 1.00104.68 C
ANISOU 98 C HIS A 117 14079 13338 12358 519 978 591 C
ATOM 99 O HIS A 117 36.538 -5.541 -17.602 1.00102.67 O
ANISOU 99 O HIS A 117 13798 13050 12161 677 936 580 O
ATOM 100 CB HIS A 117 36.798 -5.397 -20.811 1.00110.77 C
ANISOU 100 CB HIS A 117 15115 14025 12946 588 1157 555 C
ATOM 101 CG HIS A 117 36.535 -6.873 -20.712 1.00109.72 C
ANISOU 101 CG HIS A 117 15063 13806 12819 798 1201 505 C
ATOM 102 ND1 HIS A 117 37.486 -7.777 -20.283 1.00107.03 N
ANISOU 102 ND1 HIS A 117 14589 13585 12493 1001 1320 518 N
ATOM 103 CD2 HIS A 117 35.419 -7.598 -20.973 1.00108.03 C
ANISOU 103 CD2 HIS A 117 15062 13400 12585 829 1160 441 C
ATOM 104 CE1 HIS A 117 36.969 -8.993 -20.289 1.00105.18 C
ANISOU 104 CE1 HIS A 117 14521 13187 12256 1157 1370 469 C
ATOM 105 NE2 HIS A 117 35.717 -8.912 -20.703 1.00106.70 N
ANISOU 105 NE2 HIS A 117 14921 13191 12427 1030 1274 408 N
ATOM 106 N VAL A 118 37.748 -3.717 -18.171 1.00106.77 N
ANISOU 106 N VAL A 118 14164 13791 12611 369 1022 612 N
ATOM 107 CA VAL A 118 38.403 -3.619 -16.863 1.00105.53 C
ANISOU 107 CA VAL A 118 13752 13839 12505 361 988 618 C
ATOM 108 C VAL A 118 37.421 -3.142 -15.799 1.00102.31 C
ANISOU 108 C VAL A 118 13401 13281 12192 283 832 608 C
ATOM 109 O VAL A 118 37.332 -3.722 -14.710 1.00 98.99 O
ANISOU 109 O VAL A 118 12873 12911 11828 402 762 609 O
ATOM 110 CB VAL A 118 39.638 -2.704 -16.938 1.00109.00 C
ANISOU 110 CB VAL A 118 13984 14548 12881 159 1086 616 C
ATOM 111 CG1 VAL A 118 39.900 -2.053 -15.589 1.00108.20 C
ANISOU 111 CG1 VAL A 118 13688 14602 12821 9 1012 596 C
ATOM 112 CG2 VAL A 118 40.849 -3.513 -17.355 1.00109.68 C
ANISOU 112 CG2 VAL A 118 13871 14913 12887 324 1224 634 C
ATOM 113 N ALA A 119 36.672 -2.072 -16.092 1.00108.58 N
ANISOU 113 N ALA A 119 14372 13890 12995 101 788 609 N
ATOM 114 CA ALA A 119 35.636 -1.626 -15.164 1.00104.39 C
ANISOU 114 CA ALA A 119 13920 13197 12548 52 653 603 C
ATOM 115 C ALA A 119 34.692 -2.774 -14.820 1.00100.45 C
ANISOU 115 C ALA A 119 13494 12573 12100 259 556 594 C
ATOM 116 O ALA A 119 34.335 -2.973 -13.652 1.00 95.51 O
ANISOU 116 O ALA A 119 12804 11939 11548 298 464 584 O
ATOM 117 CB ALA A 119 34.866 -0.443 -15.760 1.00101.13 C
ANISOU 117 CB ALA A 119 13731 12578 12116 -99 649 630 C
ATOM 118 N ALA A 120 34.323 -3.567 -15.828 1.00 95.98 N
ANISOU 118 N ALA A 120 13067 11918 11481 376 592 587 N
ATOM 119 CA ALA A 120 33.416 -4.692 -15.630 1.00 91.08 C
ANISOU 119 CA ALA A 120 12551 11169 10888 529 534 556 C
ATOM 120 C ALA A 120 34.020 -5.755 -14.718 1.00 87.31 C
ANISOU 120 C ALA A 120 11934 10787 10453 704 568 556 C
ATOM 121 O ALA A 120 33.295 -6.445 -13.994 1.00 85.47 O
ANISOU 121 O ALA A 120 11755 10447 10274 795 505 539 O
ATOM 122 CB ALA A 120 33.047 -5.298 -16.987 1.00 91.80 C
ANISOU 122 CB ALA A 120 12820 11178 10883 574 598 526 C
ATOM 123 N ILE A 121 35.337 -5.937 -14.776 1.00 91.73 N
ANISOU 123 N ILE A 121 12318 11561 10976 771 681 584 N
ATOM 124 CA ILE A 121 35.989 -6.901 -13.898 1.00 90.96 C
ANISOU 124 CA ILE A 121 12068 11597 10894 984 726 615 C
ATOM 125 C ILE A 121 36.008 -6.400 -12.449 1.00 91.02 C
ANISOU 125 C ILE A 121 11900 11719 10965 929 610 635 C
ATOM 126 O ILE A 121 35.804 -7.176 -11.501 1.00 86.35 O
ANISOU 126 O ILE A 121 11281 11118 10412 1093 580 659 O
ATOM 127 CB ILE A 121 37.398 -7.217 -14.433 1.00 93.51 C
ANISOU 127 CB ILE A 121 12226 12168 11135 1096 886 651 C
ATOM 128 CG1 ILE A 121 37.309 -7.853 -15.832 1.00 95.83 C
ANISOU 128 CG1 ILE A 121 12725 12324 11363 1169 1014 620 C
ATOM 129 CG2 ILE A 121 38.152 -8.115 -13.472 1.00 92.48 C
ANISOU 129 CG2 ILE A 121 11905 12234 11000 1357 938 715 C
ATOM 130 CD1 ILE A 121 38.581 -8.574 -16.275 1.00 96.50 C
ANISOU 130 CD1 ILE A 121 12685 12612 11370 1376 1201 660 C
ATOM 131 N ILE A 122 36.256 -5.101 -12.252 1.00 90.12 N
ANISOU 131 N ILE A 122 11684 11706 10851 689 561 622 N
ATOM 132 CA ILE A 122 36.234 -4.543 -10.905 1.00 89.65 C
ANISOU 132 CA ILE A 122 11478 11750 10837 594 459 618 C
ATOM 133 C ILE A 122 34.849 -4.692 -10.288 1.00 86.69 C
ANISOU 133 C ILE A 122 11277 11113 10547 614 335 602 C
ATOM 134 O ILE A 122 34.707 -4.971 -9.090 1.00 84.68 O
ANISOU 134 O ILE A 122 10930 10912 10332 677 264 613 O
ATOM 135 CB ILE A 122 36.663 -3.068 -10.931 1.00 91.96 C
ANISOU 135 CB ILE A 122 11698 12139 11103 288 466 584 C
ATOM 136 CG1 ILE A 122 38.121 -2.936 -11.384 1.00 93.64 C
ANISOU 136 CG1 ILE A 122 11687 12675 11217 241 593 590 C
ATOM 137 CG2 ILE A 122 36.384 -2.427 -9.549 1.00 90.80 C
ANISOU 137 CG2 ILE A 122 11466 12033 11002 154 361 554 C
ATOM 138 CD1 ILE A 122 39.076 -3.938 -10.754 1.00 92.38 C
ANISOU 138 CD1 ILE A 122 11252 12842 11007 475 626 638 C
ATOM 139 N ASN A 123 33.809 -4.471 -11.089 1.00 82.58 N
ANISOU 139 N ASN A 123 10994 10339 10042 556 306 579 N
ATOM 140 CA ASN A 123 32.452 -4.565 -10.583 1.00 79.53 C
ANISOU 140 CA ASN A 123 10753 9742 9722 562 191 561 C
ATOM 141 C ASN A 123 32.085 -6.001 -10.209 1.00 78.39 C
ANISOU 141 C ASN A 123 10658 9529 9597 771 197 560 C
ATOM 142 O ASN A 123 31.398 -6.228 -9.206 1.00 76.87 O
ANISOU 142 O ASN A 123 10476 9268 9463 800 112 554 O
ATOM 143 CB ASN A 123 31.484 -3.972 -11.611 1.00 78.73 C
ANISOU 143 CB ASN A 123 10859 9457 9597 466 165 549 C
ATOM 144 CG ASN A 123 30.462 -3.010 -10.973 1.00 80.16 C
ANISOU 144 CG ASN A 123 11108 9518 9832 356 54 548 C
ATOM 145 OD1 ASN A 123 30.585 -2.623 -9.795 1.00 82.59 O
ANISOU 145 OD1 ASN A 123 11312 9872 10195 305 6 542 O
ATOM 146 ND2 ASN A 123 29.458 -2.613 -11.752 1.00 76.96 N
ANISOU 146 ND2 ASN A 123 10872 8977 9394 330 20 559 N
ATOM 147 N TYR A 124 32.516 -6.988 -11.002 1.00 80.24 N
ANISOU 147 N TYR A 124 10949 9761 9779 915 317 562 N
ATOM 148 CA TYR A 124 32.141 -8.374 -10.705 1.00 78.23 C
ANISOU 148 CA TYR A 124 10802 9387 9533 1104 368 555 C
ATOM 149 C TYR A 124 32.835 -8.881 -9.437 1.00 77.54 C
ANISOU 149 C TYR A 124 10544 9447 9469 1277 384 622 C
ATOM 150 O TYR A 124 32.218 -9.596 -8.632 1.00 74.41 O
ANISOU 150 O TYR A 124 10224 8935 9112 1373 362 627 O
ATOM 151 CB TYR A 124 32.445 -9.281 -11.912 1.00 74.72 C
ANISOU 151 CB TYR A 124 10499 8877 9015 1210 526 531 C
ATOM 152 CG TYR A 124 31.330 -9.423 -12.967 1.00 74.53 C
ANISOU 152 CG TYR A 124 10714 8658 8948 1091 515 445 C
ATOM 153 CD1 TYR A 124 30.284 -10.346 -12.810 1.00 72.96 C
ANISOU 153 CD1 TYR A 124 10703 8267 8750 1105 520 379 C
ATOM 154 CD2 TYR A 124 31.344 -8.648 -14.137 1.00 78.56 C
ANISOU 154 CD2 TYR A 124 11256 9202 9393 956 511 429 C
ATOM 155 CE1 TYR A 124 29.276 -10.471 -13.784 1.00 74.88 C
ANISOU 155 CE1 TYR A 124 11128 8400 8921 968 505 287 C
ATOM 156 CE2 TYR A 124 30.347 -8.764 -15.115 1.00 75.72 C
ANISOU 156 CE2 TYR A 124 11083 8728 8960 856 492 358 C
ATOM 157 CZ TYR A 124 29.320 -9.676 -14.937 1.00 76.45 C
ANISOU 157 CZ TYR A 124 11329 8674 9044 855 484 282 C
ATOM 158 OH TYR A 124 28.337 -9.798 -15.903 1.00 75.74 O
ANISOU 158 OH TYR A 124 11392 8535 8852 730 461 198 O
ATOM 159 N LEU A 125 34.121 -8.523 -9.251 1.00 80.65 N
ANISOU 159 N LEU A 125 10696 10124 9822 1315 426 677 N
ATOM 160 CA LEU A 125 34.900 -8.971 -8.097 1.00 80.53 C
ANISOU 160 CA LEU A 125 10470 10337 9790 1498 440 756 C
ATOM 161 C LEU A 125 34.472 -8.259 -6.815 1.00 80.72 C
ANISOU 161 C LEU A 125 10385 10420 9864 1366 284 748 C
ATOM 162 O LEU A 125 34.397 -8.882 -5.745 1.00 79.06 O
ANISOU 162 O LEU A 125 10127 10249 9661 1524 264 800 O
ATOM 163 CB LEU A 125 36.384 -8.742 -8.360 1.00 84.33 C
ANISOU 163 CB LEU A 125 10690 11169 10184 1551 527 806 C
ATOM 164 CG LEU A 125 37.347 -9.393 -7.366 1.00 87.30 C
ANISOU 164 CG LEU A 125 10817 11856 10496 1814 573 914 C
ATOM 165 CD1 LEU A 125 37.274 -10.913 -7.490 1.00 84.41 C
ANISOU 165 CD1 LEU A 125 10633 11322 10118 2170 724 986 C
ATOM 166 CD2 LEU A 125 38.770 -8.904 -7.590 1.00 90.87 C
ANISOU 166 CD2 LEU A 125 10949 12734 10843 1795 630 946 C
ATOM 167 N GLY A 126 34.204 -6.951 -6.906 1.00 81.32 N
ANISOU 167 N GLY A 126 10439 10495 9964 1085 191 688 N
ATOM 168 CA GLY A 126 33.663 -6.227 -5.771 1.00 79.15 C
ANISOU 168 CA GLY A 126 10114 10223 9738 941 61 662 C
ATOM 169 C GLY A 126 32.312 -6.759 -5.327 1.00 77.06 C
ANISOU 169 C GLY A 126 10048 9683 9547 997 -9 646 C
ATOM 170 O GLY A 126 31.999 -6.765 -4.133 1.00 77.58 O
ANISOU 170 O GLY A 126 10055 9781 9642 1008 -87 656 O
ATOM 171 N HIS A 127 31.492 -7.212 -6.277 1.00 74.59 N
ANISOU 171 N HIS A 127 9966 9122 9251 1016 21 615 N
ATOM 172 CA HIS A 127 30.179 -7.747 -5.931 1.00 72.73 C
ANISOU 172 CA HIS A 127 9911 8656 9068 1037 -34 584 C
ATOM 173 C HIS A 127 30.273 -9.151 -5.316 1.00 74.52 C
ANISOU 173 C HIS A 127 10178 8846 9288 1270 44 629 C
ATOM 174 O HIS A 127 29.489 -9.491 -4.423 1.00 74.36 O
ANISOU 174 O HIS A 127 10218 8726 9310 1288 -9 625 O
ATOM 175 CB HIS A 127 29.279 -7.727 -7.165 1.00 69.22 C
ANISOU 175 CB HIS A 127 9672 8018 8610 948 -28 525 C
ATOM 176 CG HIS A 127 28.574 -6.417 -7.380 1.00 71.91 C
ANISOU 176 CG HIS A 127 10036 8317 8970 756 -133 499 C
ATOM 177 ND1 HIS A 127 29.162 -5.348 -8.025 1.00 75.79 N
ANISOU 177 ND1 HIS A 127 10478 8887 9432 641 -115 511 N
ATOM 178 CD2 HIS A 127 27.324 -6.009 -7.052 1.00 70.47 C
ANISOU 178 CD2 HIS A 127 9934 8019 8823 675 -236 471 C
ATOM 179 CE1 HIS A 127 28.311 -4.337 -8.073 1.00 73.75 C
ANISOU 179 CE1 HIS A 127 10292 8539 9192 517 -191 502 C
ATOM 180 NE2 HIS A 127 27.188 -4.714 -7.492 1.00 70.10 N
ANISOU 180 NE2 HIS A 127 9895 7972 8766 547 -271 480 N
ATOM 181 N CYS A 128 31.222 -9.981 -5.768 1.00 72.23 N
ANISOU 181 N CYS A 128 9874 8629 8942 1463 190 680 N
ATOM 182 CA CYS A 128 31.442 -11.275 -5.118 1.00 73.82 C
ANISOU 182 CA CYS A 128 10127 8796 9126 1728 300 752 C
ATOM 183 C CYS A 128 31.939 -11.098 -3.688 1.00 73.77 C
ANISOU 183 C CYS A 128 9895 9022 9113 1819 230 836 C
ATOM 184 O CYS A 128 31.486 -11.786 -2.765 1.00 69.55 O
ANISOU 184 O CYS A 128 9433 8399 8594 1940 236 877 O
ATOM 185 CB CYS A 128 32.439 -12.121 -5.921 1.00 71.33 C
ANISOU 185 CB CYS A 128 9839 8525 8739 1951 494 804 C
ATOM 186 SG CYS A 128 31.801 -12.641 -7.520 1.00 76.95 S
ANISOU 186 SG CYS A 128 10862 8944 9431 1866 611 694 S
ATOM 187 N ILE A 129 32.915 -10.210 -3.493 1.00 75.67 N
ANISOU 187 N ILE A 129 9858 9580 9312 1754 176 862 N
ATOM 188 CA ILE A 129 33.453 -10.004 -2.155 1.00 75.73 C
ANISOU 188 CA ILE A 129 9621 9874 9281 1814 106 929 C
ATOM 189 C ILE A 129 32.385 -9.416 -1.239 1.00 74.76 C
ANISOU 189 C ILE A 129 9546 9631 9229 1627 -43 869 C
ATOM 190 O ILE A 129 32.240 -9.837 -0.086 1.00 73.21 O
ANISOU 190 O ILE A 129 9306 9491 9021 1743 -75 925 O
ATOM 191 CB ILE A 129 34.694 -9.106 -2.214 1.00 78.27 C
ANISOU 191 CB ILE A 129 9629 10587 9522 1712 86 934 C
ATOM 192 CG1 ILE A 129 35.735 -9.705 -3.158 1.00 79.47 C
ANISOU 192 CG1 ILE A 129 9723 10872 9600 1911 242 996 C
ATOM 193 CG2 ILE A 129 35.232 -8.926 -0.799 1.00 79.53 C
ANISOU 193 CG2 ILE A 129 9515 11092 9610 1753 8 991 C
ATOM 194 CD1 ILE A 129 36.818 -8.736 -3.526 1.00 82.69 C
ANISOU 194 CD1 ILE A 129 9860 11626 9933 1739 236 969 C
ATOM 195 N SER A 130 31.616 -8.437 -1.735 1.00 75.63 N
ANISOU 195 N SER A 130 9752 9580 9404 1357 -126 765 N
ATOM 196 CA SER A 130 30.524 -7.887 -0.935 1.00 72.05 C
ANISOU 196 CA SER A 130 9364 8996 9016 1204 -249 710 C
ATOM 197 C SER A 130 29.529 -8.963 -0.537 1.00 69.08 C
ANISOU 197 C SER A 130 9183 8386 8680 1337 -231 725 C
ATOM 198 O SER A 130 29.052 -8.978 0.599 1.00 69.70 O
ANISOU 198 O SER A 130 9238 8467 8778 1337 -300 734 O
ATOM 199 CB SER A 130 29.814 -6.764 -1.691 1.00 70.45 C
ANISOU 199 CB SER A 130 9266 8637 8863 956 -307 621 C
ATOM 200 OG SER A 130 30.552 -5.567 -1.625 1.00 72.25 O
ANISOU 200 OG SER A 130 9336 9054 9060 775 -329 594 O
ATOM 201 N LEU A 131 29.179 -9.857 -1.461 1.00 68.22 N
ANISOU 201 N LEU A 131 9277 8068 8574 1425 -128 714 N
ATOM 202 CA LEU A 131 28.151 -10.850 -1.163 1.00 67.83 C
ANISOU 202 CA LEU A 131 9444 7774 8553 1488 -89 700 C
ATOM 203 C LEU A 131 28.610 -11.838 -0.081 1.00 68.53 C
ANISOU 203 C LEU A 131 9509 7922 8607 1740 -10 810 C
ATOM 204 O LEU A 131 27.868 -12.127 0.876 1.00 63.93 O
ANISOU 204 O LEU A 131 8989 7250 8050 1742 -47 815 O
ATOM 205 CB LEU A 131 27.729 -11.566 -2.455 1.00 64.51 C
ANISOU 205 CB LEU A 131 9256 7134 8119 1482 26 640 C
ATOM 206 CG LEU A 131 26.586 -12.583 -2.276 1.00 64.98 C
ANISOU 206 CG LEU A 131 9564 6934 8191 1476 89 589 C
ATOM 207 CD1 LEU A 131 25.270 -11.846 -2.006 1.00 65.45 C
ANISOU 207 CD1 LEU A 131 9632 6936 8298 1248 -69 503 C
ATOM 208 CD2 LEU A 131 26.394 -13.458 -3.491 1.00 61.80 C
ANISOU 208 CD2 LEU A 131 9394 6345 7742 1475 244 521 C
ATOM 209 N VAL A 132 29.835 -12.362 -0.215 1.00 68.89 N
ANISOU 209 N VAL A 132 9459 8134 8582 1972 106 911 N
ATOM 210 CA VAL A 132 30.374 -13.271 0.796 1.00 67.97 C
ANISOU 210 CA VAL A 132 9304 8117 8407 2266 192 1050 C
ATOM 211 C VAL A 132 30.406 -12.570 2.153 1.00 68.76 C
ANISOU 211 C VAL A 132 9178 8454 8494 2206 34 1080 C
ATOM 212 O VAL A 132 29.924 -13.101 3.164 1.00 67.60 O
ANISOU 212 O VAL A 132 9100 8240 8345 2301 36 1132 O
ATOM 213 CB VAL A 132 31.775 -13.773 0.367 1.00 68.83 C
ANISOU 213 CB VAL A 132 9292 8440 8422 2544 335 1166 C
ATOM 214 CG1 VAL A 132 32.441 -14.589 1.481 1.00 70.84 C
ANISOU 214 CG1 VAL A 132 9454 8876 8585 2894 416 1346 C
ATOM 215 CG2 VAL A 132 31.718 -14.601 -0.942 1.00 64.73 C
ANISOU 215 CG2 VAL A 132 9040 7649 7904 2622 525 1132 C
ATOM 216 N ALA A 133 30.907 -11.331 2.176 1.00 70.07 N
ANISOU 216 N ALA A 133 9096 8880 8648 2014 -94 1032 N
ATOM 217 CA ALA A 133 31.002 -10.561 3.415 1.00 69.34 C
ANISOU 217 CA ALA A 133 8787 9033 8527 1908 -233 1032 C
ATOM 218 C ALA A 133 29.642 -10.412 4.091 1.00 66.66 C
ANISOU 218 C ALA A 133 8607 8450 8270 1768 -319 965 C
ATOM 219 O ALA A 133 29.494 -10.669 5.292 1.00 68.52 O
ANISOU 219 O ALA A 133 8794 8768 8473 1848 -355 1020 O
ATOM 220 CB ALA A 133 31.605 -9.190 3.110 1.00 68.24 C
ANISOU 220 CB ALA A 133 8434 9126 8368 1648 -320 949 C
ATOM 221 N LEU A 134 28.627 -10.016 3.333 1.00 65.09 N
ANISOU 221 N LEU A 134 8591 7974 8164 1570 -350 853 N
ATOM 222 CA LEU A 134 27.300 -9.886 3.921 1.00 64.41 C
ANISOU 222 CA LEU A 134 8638 7686 8147 1446 -425 790 C
ATOM 223 C LEU A 134 26.821 -11.214 4.507 1.00 64.56 C
ANISOU 223 C LEU A 134 8824 7548 8158 1638 -334 857 C
ATOM 224 O LEU A 134 26.223 -11.253 5.587 1.00 65.48 O
ANISOU 224 O LEU A 134 8947 7648 8283 1621 -387 864 O
ATOM 225 CB LEU A 134 26.336 -9.344 2.870 1.00 62.38 C
ANISOU 225 CB LEU A 134 8533 7208 7963 1247 -458 679 C
ATOM 226 CG LEU A 134 26.675 -7.903 2.442 1.00 65.33 C
ANISOU 226 CG LEU A 134 8782 7696 8344 1050 -534 622 C
ATOM 227 CD1 LEU A 134 25.777 -7.366 1.305 1.00 63.25 C
ANISOU 227 CD1 LEU A 134 8669 7238 8128 905 -554 545 C
ATOM 228 CD2 LEU A 134 26.588 -6.969 3.647 1.00 66.83 C
ANISOU 228 CD2 LEU A 134 8843 8014 8537 926 -636 596 C
ATOM 229 N LEU A 135 27.102 -12.315 3.823 1.00 65.33 N
ANISOU 229 N LEU A 135 9074 7517 8231 1819 -174 907 N
ATOM 230 CA LEU A 135 26.709 -13.630 4.314 1.00 65.36 C
ANISOU 230 CA LEU A 135 9288 7328 8216 2003 -37 974 C
ATOM 231 C LEU A 135 27.405 -13.976 5.629 1.00 66.48 C
ANISOU 231 C LEU A 135 9290 7690 8280 2240 -27 1125 C
ATOM 232 O LEU A 135 26.786 -14.514 6.560 1.00 66.41 O
ANISOU 232 O LEU A 135 9392 7573 8267 2293 -3 1164 O
ATOM 233 CB LEU A 135 27.045 -14.674 3.249 1.00 66.73 C
ANISOU 233 CB LEU A 135 9668 7322 8364 2157 167 995 C
ATOM 234 CG LEU A 135 25.945 -15.006 2.265 1.00 66.59 C
ANISOU 234 CG LEU A 135 9917 6992 8393 1961 223 852 C
ATOM 235 CD1 LEU A 135 26.553 -15.827 1.145 1.00 66.45 C
ANISOU 235 CD1 LEU A 135 10059 6859 8332 2099 421 864 C
ATOM 236 CD2 LEU A 135 24.803 -15.749 2.997 1.00 68.10 C
ANISOU 236 CD2 LEU A 135 10325 6949 8601 1910 278 822 C
ATOM 237 N VAL A 136 28.718 -13.739 5.689 1.00 68.58 N
ANISOU 237 N VAL A 136 9308 8285 8462 2394 -31 1220 N
ATOM 238 CA VAL A 136 29.485 -14.042 6.890 1.00 68.90 C
ANISOU 238 CA VAL A 136 9167 8623 8391 2639 -29 1378 C
ATOM 239 C VAL A 136 28.988 -13.195 8.053 1.00 71.58 C
ANISOU 239 C VAL A 136 9362 9100 8734 2444 -208 1326 C
ATOM 240 O VAL A 136 28.876 -13.672 9.189 1.00 70.44 O
ANISOU 240 O VAL A 136 9216 9020 8530 2591 -200 1424 O
ATOM 241 CB VAL A 136 30.991 -13.847 6.621 1.00 68.20 C
ANISOU 241 CB VAL A 136 8791 8932 8190 2806 -11 1470 C
ATOM 242 CG1 VAL A 136 31.732 -13.566 7.909 1.00 72.37 C
ANISOU 242 CG1 VAL A 136 9004 9909 8583 2914 -104 1576 C
ATOM 243 CG2 VAL A 136 31.584 -15.087 5.975 1.00 66.90 C
ANISOU 243 CG2 VAL A 136 8781 8663 7976 3160 218 1601 C
ATOM 244 N ALA A 137 28.654 -11.930 7.785 1.00 68.69 N
ANISOU 244 N ALA A 137 8901 8765 8435 2117 -355 1174 N
ATOM 245 CA ALA A 137 28.044 -11.114 8.825 1.00 69.02 C
ANISOU 245 CA ALA A 137 8860 8874 8491 1916 -499 1104 C
ATOM 246 C ALA A 137 26.679 -11.657 9.214 1.00 68.77 C
ANISOU 246 C ALA A 137 9084 8509 8536 1887 -478 1075 C
ATOM 247 O ALA A 137 26.321 -11.675 10.399 1.00 70.59 O
ANISOU 247 O ALA A 137 9284 8801 8735 1895 -528 1102 O
ATOM 248 CB ALA A 137 27.936 -9.671 8.353 1.00 71.61 C
ANISOU 248 CB ALA A 137 9092 9242 8874 1593 -614 953 C
ATOM 249 N PHE A 138 25.900 -12.092 8.224 1.00 66.92 N
ANISOU 249 N PHE A 138 9093 7946 8388 1833 -403 1010 N
ATOM 250 CA PHE A 138 24.546 -12.555 8.492 1.00 65.38 C
ANISOU 250 CA PHE A 138 9123 7462 8255 1750 -380 955 C
ATOM 251 C PHE A 138 24.542 -13.783 9.400 1.00 70.74 C
ANISOU 251 C PHE A 138 9929 8077 8872 1987 -255 1085 C
ATOM 252 O PHE A 138 23.722 -13.875 10.324 1.00 70.87 O
ANISOU 252 O PHE A 138 10006 8024 8899 1929 -284 1073 O
ATOM 253 CB PHE A 138 23.845 -12.852 7.175 1.00 62.18 C
ANISOU 253 CB PHE A 138 8928 6782 7915 1638 -312 856 C
ATOM 254 CG PHE A 138 22.381 -13.122 7.312 1.00 60.31 C
ANISOU 254 CG PHE A 138 8876 6311 7730 1480 -310 763 C
ATOM 255 CD1 PHE A 138 21.505 -12.117 7.691 1.00 60.98 C
ANISOU 255 CD1 PHE A 138 8877 6429 7864 1274 -460 673 C
ATOM 256 CD2 PHE A 138 21.873 -14.389 7.049 1.00 61.03 C
ANISOU 256 CD2 PHE A 138 9232 6149 7808 1529 -140 761 C
ATOM 257 CE1 PHE A 138 20.139 -12.361 7.799 1.00 59.93 C
ANISOU 257 CE1 PHE A 138 8880 6128 7764 1132 -459 588 C
ATOM 258 CE2 PHE A 138 20.514 -14.646 7.151 1.00 60.57 C
ANISOU 258 CE2 PHE A 138 9323 5912 7778 1344 -132 658 C
ATOM 259 CZ PHE A 138 19.643 -13.634 7.529 1.00 60.75 C
ANISOU 259 CZ PHE A 138 9219 6016 7847 1152 -301 575 C
ATOM 260 N VAL A 139 25.444 -14.745 9.157 1.00 67.95 N
ANISOU 260 N VAL A 139 9632 7739 8448 2273 -96 1219 N
ATOM 261 CA VAL A 139 25.458 -15.942 10.000 1.00 70.39 C
ANISOU 261 CA VAL A 139 10101 7958 8686 2538 59 1368 C
ATOM 262 C VAL A 139 26.015 -15.641 11.396 1.00 73.06 C
ANISOU 262 C VAL A 139 10197 8640 8921 2671 -39 1490 C
ATOM 263 O VAL A 139 25.600 -16.267 12.387 1.00 72.86 O
ANISOU 263 O VAL A 139 10288 8543 8854 2783 21 1575 O
ATOM 264 CB VAL A 139 26.228 -17.089 9.318 1.00 69.78 C
ANISOU 264 CB VAL A 139 10194 7768 8553 2843 293 1490 C
ATOM 265 CG1 VAL A 139 25.639 -17.376 7.946 1.00 69.83 C
ANISOU 265 CG1 VAL A 139 10444 7447 8641 2672 391 1345 C
ATOM 266 CG2 VAL A 139 27.691 -16.744 9.199 1.00 71.01 C
ANISOU 266 CG2 VAL A 139 10053 8310 8618 3052 258 1603 C
ATOM 267 N LEU A 140 26.968 -14.706 11.499 1.00 73.17 N
ANISOU 267 N LEU A 140 9879 9044 8878 2648 -178 1496 N
ATOM 268 CA LEU A 140 27.465 -14.299 12.809 1.00 73.24 C
ANISOU 268 CA LEU A 140 9629 9431 8768 2710 -290 1576 C
ATOM 269 C LEU A 140 26.348 -13.712 13.665 1.00 75.46 C
ANISOU 269 C LEU A 140 9943 9623 9105 2456 -410 1464 C
ATOM 270 O LEU A 140 26.308 -13.934 14.882 1.00 77.94 O
ANISOU 270 O LEU A 140 10207 10078 9328 2558 -429 1553 O
ATOM 271 CB LEU A 140 28.620 -13.307 12.654 1.00 71.80 C
ANISOU 271 CB LEU A 140 9086 9686 8508 2641 -411 1553 C
ATOM 272 CG LEU A 140 29.953 -14.008 12.398 1.00 72.58 C
ANISOU 272 CG LEU A 140 9051 10053 8472 2999 -298 1736 C
ATOM 273 CD1 LEU A 140 31.085 -13.052 12.078 1.00 74.48 C
ANISOU 273 CD1 LEU A 140 8933 10732 8634 2890 -400 1691 C
ATOM 274 CD2 LEU A 140 30.321 -14.857 13.593 1.00 76.32 C
ANISOU 274 CD2 LEU A 140 9481 10732 8786 3348 -235 1951 C
ATOM 275 N PHE A 141 25.425 -12.965 13.053 1.00 75.15 N
ANISOU 275 N PHE A 141 9985 9364 9204 2144 -486 1279 N
ATOM 276 CA PHE A 141 24.344 -12.354 13.829 1.00 76.19 C
ANISOU 276 CA PHE A 141 10140 9422 9388 1918 -590 1173 C
ATOM 277 C PHE A 141 23.330 -13.393 14.309 1.00 77.99 C
ANISOU 277 C PHE A 141 10633 9363 9638 1990 -481 1214 C
ATOM 278 O PHE A 141 22.774 -13.269 15.405 1.00 80.77 O
ANISOU 278 O PHE A 141 10973 9750 9965 1940 -530 1213 O
ATOM 279 CB PHE A 141 23.651 -11.285 12.991 1.00 73.79 C
ANISOU 279 CB PHE A 141 9850 8979 9208 1615 -681 989 C
ATOM 280 CG PHE A 141 24.207 -9.907 13.185 1.00 76.15 C
ANISOU 280 CG PHE A 141 9910 9544 9482 1435 -814 909 C
ATOM 281 CD1 PHE A 141 24.993 -9.326 12.193 1.00 74.66 C
ANISOU 281 CD1 PHE A 141 9619 9448 9299 1373 -823 872 C
ATOM 282 CD2 PHE A 141 23.914 -9.175 14.330 1.00 78.03 C
ANISOU 282 CD2 PHE A 141 10046 9917 9685 1303 -909 857 C
ATOM 283 CE1 PHE A 141 25.504 -8.051 12.344 1.00 75.68 C
ANISOU 283 CE1 PHE A 141 9562 9796 9398 1171 -913 784 C
ATOM 284 CE2 PHE A 141 24.414 -7.897 14.498 1.00 80.49 C
ANISOU 284 CE2 PHE A 141 10176 10442 9963 1100 -998 761 C
ATOM 285 CZ PHE A 141 25.214 -7.329 13.495 1.00 82.24 C
ANISOU 285 CZ PHE A 141 10311 10747 10191 1025 -994 722 C
ATOM 286 N LEU A 142 23.061 -14.413 13.487 1.00 77.56 N
ANISOU 286 N LEU A 142 10830 9016 9623 2081 -317 1236 N
ATOM 287 CA LEU A 142 21.990 -15.380 13.730 1.00 78.06 C
ANISOU 287 CA LEU A 142 11186 8759 9714 2071 -183 1233 C
ATOM 288 C LEU A 142 22.360 -16.388 14.804 1.00 81.34 C
ANISOU 288 C LEU A 142 11690 9202 10015 2362 -52 1426 C
ATOM 289 O LEU A 142 21.478 -16.941 15.477 1.00 80.12 O
ANISOU 289 O LEU A 142 11721 8860 9860 2326 23 1430 O
ATOM 290 CB LEU A 142 21.660 -16.104 12.425 1.00 73.99 C
ANISOU 290 CB LEU A 142 10920 7934 9256 2035 -31 1170 C
ATOM 291 CG LEU A 142 20.758 -15.323 11.474 1.00 73.15 C
ANISOU 291 CG LEU A 142 10807 7732 9255 1716 -136 971 C
ATOM 292 CD1 LEU A 142 20.684 -16.013 10.101 1.00 69.56 C
ANISOU 292 CD1 LEU A 142 10560 7048 8821 1693 9 913 C
ATOM 293 CD2 LEU A 142 19.393 -15.191 12.091 1.00 71.67 C
ANISOU 293 CD2 LEU A 142 10687 7438 9106 1508 -182 874 C
ATOM 294 N ARG A 143 23.659 -16.658 14.934 1.00 81.44 N
ANISOU 294 N ARG A 143 11572 9455 9918 2662 -12 1594 N
ATOM 295 CA ARG A 143 24.152 -17.556 15.965 1.00 82.44 C
ANISOU 295 CA ARG A 143 11748 9672 9904 3001 110 1816 C
ATOM 296 C ARG A 143 24.032 -16.926 17.348 1.00 86.59 C
ANISOU 296 C ARG A 143 12063 10483 10352 2947 -51 1837 C
ATOM 297 O ARG A 143 23.755 -17.631 18.328 1.00 88.68 O
ANISOU 297 O ARG A 143 12459 10698 10537 3103 42 1964 O
ATOM 298 CB ARG A 143 25.604 -17.953 15.652 1.00 77.97 C
ANISOU 298 CB ARG A 143 11056 9348 9222 3361 191 1998 C
ATOM 299 N ALA A 144 24.196 -15.605 17.439 1.00 87.93 N
ANISOU 299 N ALA A 144 11936 10932 10540 2711 -273 1707 N
ATOM 300 CA ALA A 144 24.153 -14.918 18.726 1.00 90.11 C
ANISOU 300 CA ALA A 144 12006 11503 10730 2630 -422 1702 C
ATOM 301 C ALA A 144 22.794 -15.073 19.405 1.00 91.44 C
ANISOU 301 C ALA A 144 12375 11408 10960 2472 -406 1633 C
ATOM 302 O ALA A 144 21.741 -14.985 18.762 1.00 88.52 O
ANISOU 302 O ALA A 144 12181 10714 10737 2247 -387 1484 O
ATOM 303 CB ALA A 144 24.479 -13.434 18.536 1.00 90.40 C
ANISOU 303 CB ALA A 144 11754 11804 10790 2349 -622 1536 C
ATOM 304 N ARG A 145 22.826 -15.313 20.724 1.00 93.40 N
ANISOU 304 N ARG A 145 12578 11832 11077 2597 -412 1748 N
ATOM 305 CA ARG A 145 21.615 -15.270 21.537 1.00 95.00 C
ANISOU 305 CA ARG A 145 12910 11868 11319 2425 -422 1676 C
ATOM 306 C ARG A 145 21.116 -13.848 21.738 1.00 96.49 C
ANISOU 306 C ARG A 145 12914 12174 11575 2083 -618 1465 C
ATOM 307 O ARG A 145 20.009 -13.664 22.257 1.00 98.43 O
ANISOU 307 O ARG A 145 13254 12270 11874 1909 -634 1373 O
ATOM 308 CB ARG A 145 21.859 -15.935 22.895 1.00 95.08 C
ANISOU 308 CB ARG A 145 12926 12048 11150 2675 -363 1874 C
ATOM 309 N SER A 146 21.908 -12.849 21.339 1.00102.93 N
ANISOU 309 N SER A 146 13482 13245 12380 1985 -747 1389 N
ATOM 310 CA SER A 146 21.498 -11.449 21.321 1.00103.27 C
ANISOU 310 CA SER A 146 13400 13342 12496 1661 -893 1183 C
ATOM 311 C SER A 146 20.652 -11.105 20.104 1.00101.68 C
ANISOU 311 C SER A 146 13341 12808 12483 1473 -882 1036 C
ATOM 312 O SER A 146 20.304 -9.931 19.924 1.00101.68 O
ANISOU 312 O SER A 146 13268 12815 12551 1237 -978 880 O
ATOM 313 CB SER A 146 22.728 -10.535 21.365 1.00105.78 C
ANISOU 313 CB SER A 146 13421 14061 12709 1607 -1002 1155 C
ATOM 314 OG SER A 146 23.550 -10.838 22.481 1.00109.21 O
ANISOU 314 OG SER A 146 13678 14881 12934 1782 -1025 1292 O
ATOM 315 N ILE A 147 20.344 -12.097 19.262 1.00 89.95 N
ANISOU 315 N ILE A 147 12065 11046 11067 1577 -756 1085 N
ATOM 316 CA ILE A 147 19.443 -11.924 18.129 1.00 85.76 C
ANISOU 316 CA ILE A 147 11671 10228 10684 1404 -740 953 C
ATOM 317 C ILE A 147 18.018 -11.638 18.586 1.00 83.88 C
ANISOU 317 C ILE A 147 11518 9839 10512 1214 -765 842 C
ATOM 318 O ILE A 147 17.169 -11.258 17.767 1.00 79.55 O
ANISOU 318 O ILE A 147 11028 9130 10066 1051 -782 720 O
ATOM 319 CB ILE A 147 19.504 -13.166 17.208 1.00 85.79 C
ANISOU 319 CB ILE A 147 11889 9997 10712 1548 -576 1024 C
ATOM 320 CG1 ILE A 147 18.872 -12.862 15.838 1.00 83.05 C
ANISOU 320 CG1 ILE A 147 11621 9450 10485 1366 -582 884 C
ATOM 321 CG2 ILE A 147 18.862 -14.386 17.874 1.00 85.33 C
ANISOU 321 CG2 ILE A 147 12061 9743 10616 1646 -424 1108 C
ATOM 322 CD1 ILE A 147 19.559 -11.746 15.064 1.00 76.38 C
ANISOU 322 CD1 ILE A 147 10594 8757 9671 1289 -694 821 C
ATOM 323 N ARG A 148 17.734 -11.819 19.885 1.00 88.28 N
ANISOU 323 N ARG A 148 12072 10473 10997 1245 -764 888 N
ATOM 324 CA ARG A 148 16.433 -11.484 20.454 1.00 80.45 C
ANISOU 324 CA ARG A 148 11131 9384 10052 1072 -789 785 C
ATOM 325 C ARG A 148 16.290 -9.988 20.750 1.00 77.81 C
ANISOU 325 C ARG A 148 10629 9195 9742 900 -927 659 C
ATOM 326 O ARG A 148 15.166 -9.468 20.720 1.00 72.79 O
ANISOU 326 O ARG A 148 10027 8450 9179 750 -949 547 O
ATOM 327 CB ARG A 148 16.211 -12.324 21.706 1.00 81.02 C
ANISOU 327 CB ARG A 148 11288 9468 10028 1180 -712 892 C
ATOM 328 N CYS A 149 17.407 -9.290 21.011 1.00 76.19 N
ANISOU 328 N CYS A 149 10248 9237 9463 916 -1002 671 N
ATOM 329 CA CYS A 149 17.418 -7.830 21.120 1.00 75.38 C
ANISOU 329 CA CYS A 149 10026 9236 9380 730 -1096 536 C
ATOM 330 C CYS A 149 16.822 -7.179 19.878 1.00 74.46 C
ANISOU 330 C CYS A 149 9971 8923 9398 616 -1103 432 C
ATOM 331 O CYS A 149 17.202 -7.495 18.745 1.00 75.25 O
ANISOU 331 O CYS A 149 10100 8949 9542 667 -1078 461 O
ATOM 332 CB CYS A 149 18.848 -7.308 21.293 1.00 78.32 C
ANISOU 332 CB CYS A 149 10209 9906 9642 734 -1150 554 C
ATOM 333 SG CYS A 149 19.607 -7.487 22.906 1.00 84.17 S
ANISOU 333 SG CYS A 149 10791 11015 10175 803 -1187 632 S
ATOM 334 N LEU A 150 15.928 -6.217 20.089 1.00 71.19 N
ANISOU 334 N LEU A 150 9572 8441 9035 476 -1130 320 N
ATOM 335 CA LEU A 150 15.359 -5.518 18.949 1.00 69.53 C
ANISOU 335 CA LEU A 150 9411 8076 8929 403 -1132 244 C
ATOM 336 C LEU A 150 16.462 -5.014 18.023 1.00 72.67 C
ANISOU 336 C LEU A 150 9753 8527 9330 389 -1146 243 C
ATOM 337 O LEU A 150 16.390 -5.174 16.797 1.00 69.66 O
ANISOU 337 O LEU A 150 9422 8035 9012 414 -1130 253 O
ATOM 338 CB LEU A 150 14.484 -4.367 19.441 1.00 67.32 C
ANISOU 338 CB LEU A 150 9144 7757 8678 293 -1144 140 C
ATOM 339 CG LEU A 150 13.845 -3.400 18.451 1.00 68.58 C
ANISOU 339 CG LEU A 150 9354 7783 8921 248 -1135 76 C
ATOM 340 CD1 LEU A 150 12.865 -4.115 17.504 1.00 67.09 C
ANISOU 340 CD1 LEU A 150 9218 7482 8791 304 -1124 101 C
ATOM 341 CD2 LEU A 150 13.151 -2.274 19.224 1.00 67.10 C
ANISOU 341 CD2 LEU A 150 9190 7572 8734 177 -1116 -9 C
ATOM 342 N ARG A 151 17.519 -4.442 18.593 1.00 74.33 N
ANISOU 342 N ARG A 151 9851 8934 9457 333 -1172 228 N
ATOM 343 CA ARG A 151 18.519 -3.791 17.756 1.00 74.79 C
ANISOU 343 CA ARG A 151 9850 9056 9512 272 -1174 204 C
ATOM 344 C ARG A 151 19.174 -4.786 16.797 1.00 74.34 C
ANISOU 344 C ARG A 151 9782 9001 9460 415 -1154 304 C
ATOM 345 O ARG A 151 19.492 -4.437 15.652 1.00 74.30 O
ANISOU 345 O ARG A 151 9794 8932 9503 388 -1140 288 O
ATOM 346 CB ARG A 151 19.574 -3.113 18.626 1.00 76.82 C
ANISOU 346 CB ARG A 151 9964 9579 9646 154 -1197 156 C
ATOM 347 CG ARG A 151 20.698 -4.035 19.025 1.00 79.59 C
ANISOU 347 CG ARG A 151 10161 10206 9873 282 -1219 267 C
ATOM 348 CD ARG A 151 21.990 -3.261 19.047 1.00 83.12 C
ANISOU 348 CD ARG A 151 10439 10932 10212 140 -1235 211 C
ATOM 349 NE ARG A 151 21.938 -2.293 20.128 1.00 87.56 N
ANISOU 349 NE ARG A 151 10959 11618 10690 -70 -1249 85 N
ATOM 350 CZ ARG A 151 22.384 -2.534 21.352 1.00 91.00 C
ANISOU 350 CZ ARG A 151 11251 12359 10967 -70 -1290 104 C
ATOM 351 NH1 ARG A 151 22.174 -1.680 22.344 1.00 90.55 N
ANISOU 351 NH1 ARG A 151 11188 12381 10834 -274 -1292 -26 N
ATOM 352 NH2 ARG A 151 23.056 -3.662 21.586 1.00 90.95 N
ANISOU 352 NH2 ARG A 151 11111 12585 10860 153 -1317 262 N
ATOM 353 N ASN A 152 19.430 -6.012 17.260 1.00 76.21 N
ANISOU 353 N ASN A 152 10007 9310 9641 578 -1135 415 N
ATOM 354 CA ASN A 152 20.019 -7.013 16.384 1.00 73.60 C
ANISOU 354 CA ASN A 152 9702 8952 9311 737 -1083 514 C
ATOM 355 C ASN A 152 18.996 -7.553 15.396 1.00 70.47 C
ANISOU 355 C ASN A 152 9482 8274 9020 749 -1034 498 C
ATOM 356 O ASN A 152 19.366 -8.059 14.336 1.00 68.27 O
ANISOU 356 O ASN A 152 9251 7926 8763 819 -986 532 O
ATOM 357 CB ASN A 152 20.611 -8.141 17.215 1.00 79.28 C
ANISOU 357 CB ASN A 152 10383 9818 9921 938 -1046 653 C
ATOM 358 CG ASN A 152 21.909 -7.745 17.875 1.00 83.79 C
ANISOU 358 CG ASN A 152 10729 10757 10352 956 -1094 689 C
ATOM 359 OD1 ASN A 152 22.677 -6.969 17.321 1.00 82.96 O
ANISOU 359 OD1 ASN A 152 10506 10781 10235 853 -1124 633 O
ATOM 360 ND2 ASN A 152 22.156 -8.266 19.076 1.00 90.49 N
ANISOU 360 ND2 ASN A 152 11507 11798 11076 1075 -1099 781 N
ATOM 361 N ILE A 153 17.710 -7.485 15.737 1.00 70.79 N
ANISOU 361 N ILE A 153 9611 8178 9110 676 -1040 440 N
ATOM 362 CA ILE A 153 16.665 -7.777 14.761 1.00 66.76 C
ANISOU 362 CA ILE A 153 9224 7466 8676 636 -1009 396 C
ATOM 363 C ILE A 153 16.773 -6.800 13.602 1.00 66.61 C
ANISOU 363 C ILE A 153 9180 7421 8706 561 -1044 338 C
ATOM 364 O ILE A 153 16.702 -7.182 12.425 1.00 62.06 O
ANISOU 364 O ILE A 153 8668 6757 8156 576 -1012 339 O
ATOM 365 CB ILE A 153 15.277 -7.717 15.442 1.00 65.87 C
ANISOU 365 CB ILE A 153 9159 7282 8585 559 -1017 340 C
ATOM 366 CG1 ILE A 153 15.240 -8.629 16.672 1.00 68.62 C
ANISOU 366 CG1 ILE A 153 9541 7658 8872 629 -973 405 C
ATOM 367 CG2 ILE A 153 14.161 -8.105 14.503 1.00 60.31 C
ANISOU 367 CG2 ILE A 153 8547 6442 7926 502 -988 289 C
ATOM 368 CD1 ILE A 153 13.897 -8.698 17.348 1.00 66.48 C
ANISOU 368 CD1 ILE A 153 9318 7326 8615 547 -964 352 C
ATOM 369 N ILE A 154 16.966 -5.517 13.928 1.00 67.17 N
ANISOU 369 N ILE A 154 9178 7564 8779 473 -1092 287 N
ATOM 370 CA ILE A 154 17.094 -4.470 12.920 1.00 64.72 C
ANISOU 370 CA ILE A 154 8872 7211 8506 405 -1100 243 C
ATOM 371 C ILE A 154 18.333 -4.691 12.055 1.00 62.73 C
ANISOU 371 C ILE A 154 8581 7022 8233 442 -1079 286 C
ATOM 372 O ILE A 154 18.297 -4.489 10.833 1.00 61.20 O
ANISOU 372 O ILE A 154 8434 6749 8071 436 -1064 280 O
ATOM 373 CB ILE A 154 17.136 -3.095 13.613 1.00 65.60 C
ANISOU 373 CB ILE A 154 8955 7361 8610 293 -1114 175 C
ATOM 374 CG1 ILE A 154 16.115 -3.015 14.779 1.00 66.51 C
ANISOU 374 CG1 ILE A 154 9088 7458 8724 277 -1126 141 C
ATOM 375 CG2 ILE A 154 17.006 -1.995 12.581 1.00 63.93 C
ANISOU 375 CG2 ILE A 154 8805 7047 8438 240 -1090 141 C
ATOM 376 CD1 ILE A 154 14.688 -2.638 14.414 1.00 62.24 C
ANISOU 376 CD1 ILE A 154 8623 6787 8239 288 -1119 111 C
ATOM 377 N HIS A 155 19.456 -5.055 12.685 1.00 66.50 N
ANISOU 377 N HIS A 155 8955 7671 8641 488 -1076 333 N
ATOM 378 CA HIS A 155 20.693 -5.286 11.946 1.00 67.42 C
ANISOU 378 CA HIS A 155 9004 7892 8722 540 -1049 381 C
ATOM 379 C HIS A 155 20.548 -6.458 10.970 1.00 64.52 C
ANISOU 379 C HIS A 155 8737 7396 8380 670 -991 438 C
ATOM 380 O HIS A 155 20.928 -6.351 9.797 1.00 60.14 O
ANISOU 380 O HIS A 155 8202 6805 7842 668 -966 435 O
ATOM 381 CB HIS A 155 21.869 -5.540 12.904 1.00 70.08 C
ANISOU 381 CB HIS A 155 9176 8502 8950 596 -1058 436 C
ATOM 382 CG HIS A 155 22.287 -4.343 13.705 1.00 73.52 C
ANISOU 382 CG HIS A 155 9495 9111 9329 418 -1100 354 C
ATOM 383 ND1 HIS A 155 22.544 -4.398 15.060 1.00 77.93 N
ANISOU 383 ND1 HIS A 155 9943 9876 9790 411 -1135 362 N
ATOM 384 CD2 HIS A 155 22.454 -3.049 13.345 1.00 74.65 C
ANISOU 384 CD2 HIS A 155 9640 9237 9488 223 -1095 255 C
ATOM 385 CE1 HIS A 155 22.883 -3.195 15.491 1.00 79.44 C
ANISOU 385 CE1 HIS A 155 10063 10186 9934 198 -1151 253 C
ATOM 386 NE2 HIS A 155 22.833 -2.359 14.469 1.00 76.81 N
ANISOU 386 NE2 HIS A 155 9812 9700 9674 79 -1117 187 N
ATOM 387 N ALA A 156 19.993 -7.586 11.441 1.00 61.33 N
ANISOU 387 N ALA A 156 8419 6914 7970 770 -953 483 N
ATOM 388 CA ALA A 156 19.860 -8.766 10.596 1.00 60.57 C
ANISOU 388 CA ALA A 156 8457 6673 7882 868 -863 520 C
ATOM 389 C ALA A 156 18.972 -8.489 9.380 1.00 59.91 C
ANISOU 389 C ALA A 156 8468 6439 7856 758 -869 438 C
ATOM 390 O ALA A 156 19.201 -9.036 8.290 1.00 58.22 O
ANISOU 390 O ALA A 156 8330 6153 7639 793 -806 443 O
ATOM 391 CB ALA A 156 19.312 -9.937 11.417 1.00 59.11 C
ANISOU 391 CB ALA A 156 8385 6400 7674 955 -794 568 C
ATOM 392 N ASN A 157 17.938 -7.670 9.545 1.00 58.13 N
ANISOU 392 N ASN A 157 8238 6182 7667 640 -936 368 N
ATOM 393 CA ASN A 157 17.076 -7.362 8.410 1.00 57.56 C
ANISOU 393 CA ASN A 157 8223 6027 7620 563 -949 309 C
ATOM 394 C ASN A 157 17.740 -6.420 7.414 1.00 57.00 C
ANISOU 394 C ASN A 157 8112 5991 7556 542 -968 309 C
ATOM 395 O ASN A 157 17.490 -6.529 6.207 1.00 54.89 O
ANISOU 395 O ASN A 157 7899 5676 7280 527 -952 292 O
ATOM 396 CB ASN A 157 15.756 -6.774 8.879 1.00 56.49 C
ANISOU 396 CB ASN A 157 8080 5878 7504 486 -1004 256 C
ATOM 397 CG ASN A 157 14.783 -7.842 9.238 1.00 55.91 C
ANISOU 397 CG ASN A 157 8080 5750 7416 461 -965 230 C
ATOM 398 OD1 ASN A 157 13.940 -8.221 8.415 1.00 53.87 O
ANISOU 398 OD1 ASN A 157 7870 5460 7137 397 -950 180 O
ATOM 399 ND2 ASN A 157 14.896 -8.365 10.461 1.00 57.41 N
ANISOU 399 ND2 ASN A 157 8277 5941 7597 497 -941 261 N
ATOM 400 N LEU A 158 18.538 -5.462 7.900 1.00 57.42 N
ANISOU 400 N LEU A 158 8076 6133 7610 517 -994 318 N
ATOM 401 CA LEU A 158 19.338 -4.641 6.997 1.00 59.29 C
ANISOU 401 CA LEU A 158 8286 6398 7841 480 -984 319 C
ATOM 402 C LEU A 158 20.299 -5.497 6.155 1.00 56.93 C
ANISOU 402 C LEU A 158 7986 6130 7514 558 -927 362 C
ATOM 403 O LEU A 158 20.352 -5.351 4.936 1.00 53.69 O
ANISOU 403 O LEU A 158 7623 5674 7102 547 -905 357 O
ATOM 404 CB LEU A 158 20.096 -3.583 7.803 1.00 58.48 C
ANISOU 404 CB LEU A 158 8095 6400 7725 397 -996 300 C
ATOM 405 CG LEU A 158 20.911 -2.566 6.985 1.00 57.87 C
ANISOU 405 CG LEU A 158 8007 6344 7636 310 -962 286 C
ATOM 406 CD1 LEU A 158 19.965 -1.562 6.350 1.00 54.71 C
ANISOU 406 CD1 LEU A 158 7725 5792 7270 269 -954 264 C
ATOM 407 CD2 LEU A 158 21.973 -1.873 7.828 1.00 59.48 C
ANISOU 407 CD2 LEU A 158 8098 6709 7791 196 -952 253 C
ATOM 408 N ILE A 159 21.071 -6.384 6.797 1.00 56.40 N
ANISOU 408 N ILE A 159 7867 6150 7413 659 -893 415 N
ATOM 409 CA ILE A 159 22.014 -7.246 6.082 1.00 57.03 C
ANISOU 409 CA ILE A 159 7950 6261 7458 775 -816 470 C
ATOM 410 C ILE A 159 21.285 -8.083 5.035 1.00 58.48 C
ANISOU 410 C ILE A 159 8298 6270 7653 793 -758 447 C
ATOM 411 O ILE A 159 21.728 -8.210 3.877 1.00 54.87 O
ANISOU 411 O ILE A 159 7876 5793 7181 808 -709 446 O
ATOM 412 CB ILE A 159 22.770 -8.146 7.082 1.00 57.24 C
ANISOU 412 CB ILE A 159 7910 6407 7430 932 -774 556 C
ATOM 413 CG1 ILE A 159 23.613 -7.291 8.032 1.00 60.64 C
ANISOU 413 CG1 ILE A 159 8142 7084 7813 885 -836 565 C
ATOM 414 CG2 ILE A 159 23.600 -9.202 6.360 1.00 58.68 C
ANISOU 414 CG2 ILE A 159 8135 6588 7574 1105 -661 628 C
ATOM 415 CD1 ILE A 159 24.598 -6.396 7.313 1.00 64.93 C
ANISOU 415 CD1 ILE A 159 8573 7764 8334 794 -838 541 C
ATOM 416 N ALA A 160 20.168 -8.696 5.447 1.00 56.69 N
ANISOU 416 N ALA A 160 8171 5929 7439 774 -753 417 N
ATOM 417 CA ALA A 160 19.387 -9.511 4.530 1.00 54.95 C
ANISOU 417 CA ALA A 160 8103 5570 7206 738 -691 366 C
ATOM 418 C ALA A 160 18.955 -8.686 3.323 1.00 53.40 C
ANISOU 418 C ALA A 160 7901 5382 7008 635 -744 312 C
ATOM 419 O ALA A 160 19.083 -9.132 2.177 1.00 53.89 O
ANISOU 419 O ALA A 160 8040 5403 7034 628 -685 290 O
ATOM 420 CB ALA A 160 18.176 -10.099 5.265 1.00 52.02 C
ANISOU 420 CB ALA A 160 7812 5114 6837 680 -685 324 C
ATOM 421 N ALA A 161 18.488 -7.460 3.570 1.00 54.28 N
ANISOU 421 N ALA A 161 7931 5547 7145 569 -840 300 N
ATOM 422 CA ALA A 161 18.033 -6.577 2.499 1.00 55.36 C
ANISOU 422 CA ALA A 161 8070 5698 7266 510 -882 278 C
ATOM 423 C ALA A 161 19.139 -6.332 1.464 1.00 54.49 C
ANISOU 423 C ALA A 161 7957 5611 7136 535 -839 308 C
ATOM 424 O ALA A 161 18.860 -6.238 0.266 1.00 53.33 O
ANISOU 424 O ALA A 161 7858 5460 6947 508 -832 292 O
ATOM 425 CB ALA A 161 17.540 -5.249 3.099 1.00 51.35 C
ANISOU 425 CB ALA A 161 7504 5217 6790 479 -954 283 C
ATOM 426 N PHE A 162 20.391 -6.194 1.919 1.00 52.30 N
ANISOU 426 N PHE A 162 7607 5392 6873 578 -811 350 N
ATOM 427 CA PHE A 162 21.516 -5.944 1.040 1.00 54.98 C
ANISOU 427 CA PHE A 162 7919 5783 7188 593 -763 377 C
ATOM 428 C PHE A 162 21.987 -7.235 0.367 1.00 58.93 C
ANISOU 428 C PHE A 162 8486 6254 7653 682 -669 386 C
ATOM 429 O PHE A 162 22.611 -7.196 -0.708 1.00 55.71 O
ANISOU 429 O PHE A 162 8092 5864 7212 691 -618 393 O
ATOM 430 CB PHE A 162 22.659 -5.298 1.829 1.00 56.67 C
ANISOU 430 CB PHE A 162 7999 6126 7408 581 -765 407 C
ATOM 431 CG PHE A 162 22.567 -3.803 1.934 1.00 61.01 C
ANISOU 431 CG PHE A 162 8529 6679 7973 457 -800 385 C
ATOM 432 CD1 PHE A 162 21.673 -3.191 2.818 1.00 60.30 C
ANISOU 432 CD1 PHE A 162 8457 6539 7915 408 -853 358 C
ATOM 433 CD2 PHE A 162 23.387 -2.987 1.136 1.00 61.32 C
ANISOU 433 CD2 PHE A 162 8555 6756 7989 387 -754 390 C
ATOM 434 CE1 PHE A 162 21.602 -1.800 2.905 1.00 58.57 C
ANISOU 434 CE1 PHE A 162 8265 6285 7705 305 -847 338 C
ATOM 435 CE2 PHE A 162 23.316 -1.611 1.221 1.00 60.52 C
ANISOU 435 CE2 PHE A 162 8485 6616 7894 265 -746 369 C
ATOM 436 CZ PHE A 162 22.422 -1.016 2.109 1.00 61.48 C
ANISOU 436 CZ PHE A 162 8647 6664 8049 231 -785 344 C
ATOM 437 N ILE A 163 21.713 -8.381 0.993 1.00 57.77 N
ANISOU 437 N ILE A 163 8399 6046 7505 752 -624 388 N
ATOM 438 CA ILE A 163 21.983 -9.652 0.338 1.00 56.10 C
ANISOU 438 CA ILE A 163 8313 5750 7254 834 -498 386 C
ATOM 439 C ILE A 163 21.087 -9.815 -0.886 1.00 54.79 C
ANISOU 439 C ILE A 163 8268 5502 7047 721 -487 302 C
ATOM 440 O ILE A 163 21.559 -10.126 -1.987 1.00 57.32 O
ANISOU 440 O ILE A 163 8650 5807 7323 735 -411 289 O
ATOM 441 CB ILE A 163 21.820 -10.820 1.333 1.00 54.08 C
ANISOU 441 CB ILE A 163 8140 5410 6997 931 -421 412 C
ATOM 442 CG1 ILE A 163 22.945 -10.789 2.368 1.00 55.63 C
ANISOU 442 CG1 ILE A 163 8198 5746 7193 1086 -416 517 C
ATOM 443 CG2 ILE A 163 21.793 -12.157 0.577 1.00 53.32 C
ANISOU 443 CG2 ILE A 163 8250 5155 6854 980 -255 383 C
ATOM 444 CD1 ILE A 163 22.919 -11.936 3.393 1.00 57.80 C
ANISOU 444 CD1 ILE A 163 8559 5952 7450 1235 -324 580 C
ATOM 445 N LEU A 164 19.783 -9.610 -0.722 1.00 51.08 N
ANISOU 445 N LEU A 164 7819 5013 6576 606 -562 242 N
ATOM 446 CA LEU A 164 18.911 -9.864 -1.852 1.00 55.46 C
ANISOU 446 CA LEU A 164 8460 5553 7058 492 -553 158 C
ATOM 447 C LEU A 164 19.256 -8.946 -3.014 1.00 57.61 C
ANISOU 447 C LEU A 164 8684 5909 7295 479 -593 177 C
ATOM 448 O LEU A 164 19.274 -9.376 -4.175 1.00 55.98 O
ANISOU 448 O LEU A 164 8558 5699 7012 439 -534 132 O
ATOM 449 CB LEU A 164 17.458 -9.720 -1.444 1.00 54.09 C
ANISOU 449 CB LEU A 164 8268 5413 6870 380 -635 100 C
ATOM 450 CG LEU A 164 17.216 -10.909 -0.547 1.00 56.01 C
ANISOU 450 CG LEU A 164 8614 5542 7126 374 -545 68 C
ATOM 451 CD1 LEU A 164 15.745 -11.174 -0.438 1.00 58.08 C
ANISOU 451 CD1 LEU A 164 8893 5838 7338 215 -577 -27 C
ATOM 452 CD2 LEU A 164 18.000 -12.128 -1.022 1.00 53.10 C
ANISOU 452 CD2 LEU A 164 8411 5040 6725 429 -371 57 C
ATOM 453 N ARG A 165 19.557 -7.680 -2.708 1.00 56.08 N
ANISOU 453 N ARG A 165 8380 5780 7149 503 -674 241 N
ATOM 454 CA ARG A 165 19.961 -6.731 -3.737 1.00 56.24 C
ANISOU 454 CA ARG A 165 8377 5855 7135 495 -687 276 C
ATOM 455 C ARG A 165 21.221 -7.192 -4.465 1.00 58.45 C
ANISOU 455 C ARG A 165 8682 6131 7393 545 -585 292 C
ATOM 456 O ARG A 165 21.240 -7.290 -5.705 1.00 57.04 O
ANISOU 456 O ARG A 165 8564 5968 7140 519 -549 271 O
ATOM 457 CB ARG A 165 20.199 -5.359 -3.116 1.00 55.09 C
ANISOU 457 CB ARG A 165 8149 5736 7046 498 -745 334 C
ATOM 458 CG ARG A 165 20.256 -4.229 -4.142 1.00 54.59 C
ANISOU 458 CG ARG A 165 8105 5698 6939 480 -750 376 C
ATOM 459 CD ARG A 165 20.809 -2.951 -3.546 1.00 55.95 C
ANISOU 459 CD ARG A 165 8241 5854 7164 459 -747 421 C
ATOM 460 NE ARG A 165 21.422 -2.101 -4.562 1.00 59.11 N
ANISOU 460 NE ARG A 165 8683 6253 7523 437 -691 465 N
ATOM 461 CZ ARG A 165 22.174 -1.036 -4.303 1.00 60.66 C
ANISOU 461 CZ ARG A 165 8877 6427 7744 376 -642 490 C
ATOM 462 NH1 ARG A 165 22.378 -0.621 -3.058 1.00 61.49 N
ANISOU 462 NH1 ARG A 165 8931 6523 7908 325 -651 468 N
ATOM 463 NH2 ARG A 165 22.752 -0.382 -5.316 1.00 57.96 N
ANISOU 463 NH2 ARG A 165 8591 6076 7354 344 -570 528 N
ATOM 464 N ASN A 166 22.290 -7.489 -3.720 1.00 57.74 N
ANISOU 464 N ASN A 166 8536 6051 7352 626 -534 332 N
ATOM 465 CA ASN A 166 23.501 -7.933 -4.406 1.00 57.23 C
ANISOU 465 CA ASN A 166 8473 6015 7255 700 -428 357 C
ATOM 466 C ASN A 166 23.296 -9.267 -5.096 1.00 57.87 C
ANISOU 466 C ASN A 166 8708 5999 7281 732 -317 304 C
ATOM 467 O ASN A 166 23.963 -9.560 -6.089 1.00 60.09 O
ANISOU 467 O ASN A 166 9034 6286 7511 764 -226 301 O
ATOM 468 CB ASN A 166 24.681 -8.035 -3.447 1.00 56.52 C
ANISOU 468 CB ASN A 166 8258 6016 7200 805 -394 422 C
ATOM 469 CG ASN A 166 25.171 -6.677 -2.998 1.00 59.36 C
ANISOU 469 CG ASN A 166 8473 6494 7586 726 -465 450 C
ATOM 470 OD1 ASN A 166 24.440 -5.938 -2.314 1.00 62.29 O
ANISOU 470 OD1 ASN A 166 8830 6841 7996 646 -553 435 O
ATOM 471 ND2 ASN A 166 26.379 -6.293 -3.445 1.00 62.95 N
ANISOU 471 ND2 ASN A 166 8834 7073 8012 728 -411 480 N
ATOM 472 N ALA A 167 22.417 -10.110 -4.574 1.00 57.68 N
ANISOU 472 N ALA A 167 8780 5876 7258 711 -302 253 N
ATOM 473 CA ALA A 167 22.153 -11.357 -5.276 1.00 59.06 C
ANISOU 473 CA ALA A 167 9141 5933 7365 694 -168 177 C
ATOM 474 C ALA A 167 21.507 -11.067 -6.623 1.00 58.74 C
ANISOU 474 C ALA A 167 9149 5938 7234 550 -198 98 C
ATOM 475 O ALA A 167 21.902 -11.637 -7.651 1.00 58.79 O
ANISOU 475 O ALA A 167 9262 5910 7167 547 -85 55 O
ATOM 476 CB ALA A 167 21.264 -12.293 -4.436 1.00 55.52 C
ANISOU 476 CB ALA A 167 8807 5363 6924 655 -127 124 C
ATOM 477 N THR A 168 20.494 -10.189 -6.637 1.00 56.47 N
ANISOU 477 N THR A 168 8781 5742 6932 444 -344 83 N
ATOM 478 CA THR A 168 19.754 -10.019 -7.875 1.00 61.00 C
ANISOU 478 CA THR A 168 9390 6403 7386 324 -376 17 C
ATOM 479 C THR A 168 20.541 -9.163 -8.873 1.00 62.74 C
ANISOU 479 C THR A 168 9565 6699 7575 368 -382 81 C
ATOM 480 O THR A 168 20.204 -9.151 -10.062 1.00 64.25 O
ANISOU 480 O THR A 168 9800 6967 7646 295 -378 37 O
ATOM 481 CB THR A 168 18.344 -9.437 -7.616 1.00 58.42 C
ANISOU 481 CB THR A 168 8983 6189 7026 230 -516 -6 C
ATOM 482 OG1 THR A 168 18.432 -8.029 -7.462 1.00 60.89 O
ANISOU 482 OG1 THR A 168 9176 6575 7383 302 -623 100 O
ATOM 483 CG2 THR A 168 17.710 -10.015 -6.342 1.00 59.71 C
ANISOU 483 CG2 THR A 168 9154 6282 7251 202 -521 -42 C
ATOM 484 N TRP A 169 21.599 -8.478 -8.419 1.00 61.71 N
ANISOU 484 N TRP A 169 9348 6566 7534 470 -383 178 N
ATOM 485 CA TRP A 169 22.475 -7.759 -9.339 1.00 62.44 C
ANISOU 485 CA TRP A 169 9413 6717 7595 493 -355 233 C
ATOM 486 C TRP A 169 23.080 -8.713 -10.362 1.00 67.35 C
ANISOU 486 C TRP A 169 10140 7312 8139 507 -218 182 C
ATOM 487 O TRP A 169 23.281 -8.349 -11.531 1.00 66.03 O
ANISOU 487 O TRP A 169 9998 7206 7886 476 -198 186 O
ATOM 488 CB TRP A 169 23.574 -7.038 -8.558 1.00 59.78 C
ANISOU 488 CB TRP A 169 8959 6399 7354 560 -354 318 C
ATOM 489 CG TRP A 169 24.544 -6.255 -9.410 1.00 67.06 C
ANISOU 489 CG TRP A 169 9849 7386 8245 555 -308 369 C
ATOM 490 CD1 TRP A 169 24.439 -4.939 -9.771 1.00 67.56 C
ANISOU 490 CD1 TRP A 169 9896 7480 8293 499 -353 422 C
ATOM 491 CD2 TRP A 169 25.785 -6.722 -9.986 1.00 68.79 C
ANISOU 491 CD2 TRP A 169 10057 7643 8438 612 -186 379 C
ATOM 492 NE1 TRP A 169 25.524 -4.563 -10.542 1.00 68.10 N
ANISOU 492 NE1 TRP A 169 9951 7597 8328 490 -268 455 N
ATOM 493 CE2 TRP A 169 26.361 -5.635 -10.684 1.00 70.47 C
ANISOU 493 CE2 TRP A 169 10235 7920 8620 558 -173 427 C
ATOM 494 CE3 TRP A 169 26.458 -7.947 -9.981 1.00 67.86 C
ANISOU 494 CE3 TRP A 169 9968 7504 8312 718 -68 358 C
ATOM 495 CZ2 TRP A 169 27.571 -5.741 -11.368 1.00 72.65 C
ANISOU 495 CZ2 TRP A 169 10477 8267 8858 586 -61 445 C
ATOM 496 CZ3 TRP A 169 27.662 -8.046 -10.661 1.00 71.35 C
ANISOU 496 CZ3 TRP A 169 10374 8020 8717 778 44 386 C
ATOM 497 CH2 TRP A 169 28.203 -6.955 -11.346 1.00 71.93 C
ANISOU 497 CH2 TRP A 169 10386 8183 8760 702 40 424 C
ATOM 498 N PHE A 170 23.377 -9.939 -9.939 1.00 62.67 N
ANISOU 498 N PHE A 170 9628 6616 7567 565 -106 140 N
ATOM 499 CA PHE A 170 23.902 -10.919 -10.872 1.00 65.57 C
ANISOU 499 CA PHE A 170 10133 6924 7856 589 57 84 C
ATOM 500 C PHE A 170 22.872 -11.255 -11.948 1.00 67.96 C
ANISOU 500 C PHE A 170 10557 7244 8022 423 57 -36 C
ATOM 501 O PHE A 170 23.188 -11.269 -13.149 1.00 69.72 O
ANISOU 501 O PHE A 170 10834 7512 8145 392 118 -66 O
ATOM 502 CB PHE A 170 24.357 -12.158 -10.100 1.00 63.97 C
ANISOU 502 CB PHE A 170 10027 6579 7699 715 205 80 C
ATOM 503 CG PHE A 170 25.721 -12.002 -9.489 1.00 67.22 C
ANISOU 503 CG PHE A 170 10311 7047 8184 912 251 201 C
ATOM 504 CD1 PHE A 170 26.877 -12.175 -10.284 1.00 69.05 C
ANISOU 504 CD1 PHE A 170 10539 7325 8374 1019 378 233 C
ATOM 505 CD2 PHE A 170 25.866 -11.654 -8.145 1.00 63.26 C
ANISOU 505 CD2 PHE A 170 9670 6592 7773 983 168 279 C
ATOM 506 CE1 PHE A 170 28.152 -12.017 -9.733 1.00 69.03 C
ANISOU 506 CE1 PHE A 170 10373 7441 8412 1196 418 345 C
ATOM 507 CE2 PHE A 170 27.128 -11.495 -7.585 1.00 64.47 C
ANISOU 507 CE2 PHE A 170 9669 6867 7961 1147 202 384 C
ATOM 508 CZ PHE A 170 28.276 -11.669 -8.377 1.00 69.05 C
ANISOU 508 CZ PHE A 170 10222 7523 8492 1254 324 419 C
ATOM 509 N VAL A 171 21.626 -11.497 -11.547 1.00 66.97 N
ANISOU 509 N VAL A 171 10457 7118 7872 302 -13 -110 N
ATOM 510 CA VAL A 171 20.605 -11.790 -12.547 1.00 68.83 C
ANISOU 510 CA VAL A 171 10767 7441 7945 116 -25 -235 C
ATOM 511 C VAL A 171 20.399 -10.594 -13.463 1.00 70.71 C
ANISOU 511 C VAL A 171 10891 7877 8099 98 -152 -174 C
ATOM 512 O VAL A 171 20.047 -10.757 -14.636 1.00 72.30 O
ANISOU 512 O VAL A 171 11144 8188 8137 -10 -135 -249 O
ATOM 513 CB VAL A 171 19.287 -12.209 -11.873 1.00 70.16 C
ANISOU 513 CB VAL A 171 10944 7621 8091 -24 -82 -325 C
ATOM 514 CG1 VAL A 171 18.301 -12.666 -12.918 1.00 70.13 C
ANISOU 514 CG1 VAL A 171 11006 7753 7889 -248 -73 -479 C
ATOM 515 CG2 VAL A 171 19.518 -13.298 -10.820 1.00 65.55 C
ANISOU 515 CG2 VAL A 171 10490 6814 7601 18 54 -355 C
ATOM 516 N VAL A 172 20.595 -9.375 -12.942 1.00 70.17 N
ANISOU 516 N VAL A 172 10681 7854 8125 198 -267 -38 N
ATOM 517 CA VAL A 172 20.406 -8.163 -13.736 1.00 72.60 C
ANISOU 517 CA VAL A 172 10914 8313 8356 211 -361 47 C
ATOM 518 C VAL A 172 21.444 -8.074 -14.859 1.00 75.43 C
ANISOU 518 C VAL A 172 11326 8679 8654 241 -262 71 C
ATOM 519 O VAL A 172 21.129 -7.650 -15.977 1.00 74.66 O
ANISOU 519 O VAL A 172 11238 8718 8410 203 -289 82 O
ATOM 520 CB VAL A 172 20.443 -6.918 -12.828 1.00 70.50 C
ANISOU 520 CB VAL A 172 10537 8037 8212 303 -458 176 C
ATOM 521 CG1 VAL A 172 20.755 -5.680 -13.659 1.00 75.34 C
ANISOU 521 CG1 VAL A 172 11133 8723 8770 352 -477 289 C
ATOM 522 CG2 VAL A 172 19.122 -6.719 -12.126 1.00 67.83 C
ANISOU 522 CG2 VAL A 172 10136 7766 7871 274 -577 165 C
ATOM 523 N GLN A 173 22.699 -8.448 -14.572 1.00 73.73 N
ANISOU 523 N GLN A 173 11132 8344 8537 322 -145 90 N
ATOM 524 CA GLN A 173 23.742 -8.416 -15.592 1.00 73.78 C
ANISOU 524 CA GLN A 173 11177 8367 8487 354 -36 109 C
ATOM 525 C GLN A 173 23.353 -9.268 -16.790 1.00 77.23 C
ANISOU 525 C GLN A 173 11747 8844 8754 256 40 -12 C
ATOM 526 O GLN A 173 23.616 -8.897 -17.941 1.00 79.47 O
ANISOU 526 O GLN A 173 12052 9221 8921 235 65 5 O
ATOM 527 CB GLN A 173 25.079 -8.879 -15.007 1.00 72.96 C
ANISOU 527 CB GLN A 173 11053 8171 8498 473 87 140 C
ATOM 528 CG GLN A 173 25.588 -7.969 -13.929 1.00 72.31 C
ANISOU 528 CG GLN A 173 10821 8102 8550 534 18 245 C
ATOM 529 CD GLN A 173 25.360 -6.502 -14.280 1.00 75.80 C
ANISOU 529 CD GLN A 173 11209 8621 8971 480 -77 326 C
ATOM 530 OE1 GLN A 173 24.646 -5.765 -13.557 1.00 75.64 O
ANISOU 530 OE1 GLN A 173 11143 8596 9002 461 -189 364 O
ATOM 531 NE2 GLN A 173 25.973 -6.060 -15.384 1.00 76.57 N
ANISOU 531 NE2 GLN A 173 11330 8775 8987 467 -13 359 N
ATOM 532 N LEU A 174 22.725 -10.415 -16.534 1.00 77.48 N
ANISOU 532 N LEU A 174 11880 8805 8756 176 91 -142 N
ATOM 533 CA LEU A 174 22.213 -11.267 -17.604 1.00 77.65 C
ANISOU 533 CA LEU A 174 12042 8870 8593 25 172 -294 C
ATOM 534 C LEU A 174 21.040 -10.609 -18.340 1.00 80.84 C
ANISOU 534 C LEU A 174 12371 9521 8825 -102 18 -309 C
ATOM 535 O LEU A 174 20.694 -11.029 -19.449 1.00 84.02 O
ANISOU 535 O LEU A 174 12849 10042 9033 -236 60 -417 O
ATOM 536 CB LEU A 174 21.805 -12.611 -17.013 1.00 75.37 C
ANISOU 536 CB LEU A 174 11901 8418 8316 -56 287 -434 C
ATOM 537 CG LEU A 174 22.955 -13.471 -16.465 1.00 75.71 C
ANISOU 537 CG LEU A 174 12060 8225 8481 106 484 -416 C
ATOM 538 CD1 LEU A 174 22.386 -14.614 -15.617 1.00 73.16 C
ANISOU 538 CD1 LEU A 174 11889 7720 8189 46 584 -518 C
ATOM 539 CD2 LEU A 174 23.834 -14.016 -17.568 1.00 75.83 C
ANISOU 539 CD2 LEU A 174 12214 8192 8405 137 673 -464 C
ATOM 540 N THR A 175 20.404 -9.598 -17.731 1.00 81.33 N
ANISOU 540 N THR A 175 12284 9680 8940 -54 -152 -200 N
ATOM 541 CA THR A 175 19.355 -8.807 -18.389 1.00 82.89 C
ANISOU 541 CA THR A 175 12383 10141 8969 -99 -298 -162 C
ATOM 542 C THR A 175 19.915 -7.806 -19.400 1.00 84.26 C
ANISOU 542 C THR A 175 12540 10410 9065 -7 -306 -32 C
ATOM 543 O THR A 175 19.200 -7.371 -20.311 1.00 82.32 O
ANISOU 543 O THR A 175 12252 10404 8620 -36 -382 -8 O
ATOM 544 CB THR A 175 18.534 -8.075 -17.318 1.00 79.30 C
ANISOU 544 CB THR A 175 11797 9729 8606 -37 -445 -76 C
ATOM 545 OG1 THR A 175 17.556 -8.965 -16.766 1.00 82.21 O
ANISOU 545 OG1 THR A 175 12162 10131 8944 -180 -465 -216 O
ATOM 546 CG2 THR A 175 17.889 -6.799 -17.834 1.00 76.54 C
ANISOU 546 CG2 THR A 175 11339 9599 8143 50 -574 65 C
ATOM 547 N MET A 176 21.163 -7.399 -19.225 1.00 82.82 N
ANISOU 547 N MET A 176 12379 10066 9024 106 -226 60 N
ATOM 548 CA MET A 176 21.722 -6.280 -19.962 1.00 84.58 C
ANISOU 548 CA MET A 176 12590 10342 9203 190 -223 203 C
ATOM 549 C MET A 176 22.238 -6.702 -21.344 1.00 89.59 C
ANISOU 549 C MET A 176 13316 11051 9675 136 -118 148 C
ATOM 550 O MET A 176 22.811 -5.877 -22.062 1.00 89.09 O
ANISOU 550 O MET A 176 13264 11024 9563 195 -87 259 O
ATOM 551 CB MET A 176 22.829 -5.621 -19.121 1.00 83.65 C
ANISOU 551 CB MET A 176 12440 10051 9294 289 -177 308 C
ATOM 552 CG MET A 176 22.320 -5.003 -17.809 1.00 82.10 C
ANISOU 552 CG MET A 176 12161 9793 9240 337 -279 371 C
ATOM 553 SD MET A 176 22.686 -3.267 -17.462 1.00 86.67 S
ANISOU 553 SD MET A 176 12715 10315 9900 423 -296 554 S
ATOM 554 CE MET A 176 24.484 -3.291 -17.458 1.00 85.55 C
ANISOU 554 CE MET A 176 12574 10071 9861 408 -145 557 C
ATOM 555 N SER A 177 22.029 -7.957 -21.732 1.00 93.64 N
ANISOU 555 N SER A 177 13913 11575 10093 14 -45 -27 N
ATOM 556 CA SER A 177 22.226 -8.356 -23.106 1.00 96.19 C
ANISOU 556 CA SER A 177 14326 12009 10214 -66 41 -102 C
ATOM 557 C SER A 177 21.297 -7.526 -23.992 1.00 98.27 C
ANISOU 557 C SER A 177 14521 12561 10255 -83 -91 -27 C
ATOM 558 O SER A 177 20.125 -7.334 -23.666 1.00 96.69 O
ANISOU 558 O SER A 177 14228 12520 9990 -111 -230 -25 O
ATOM 559 CB SER A 177 21.957 -9.847 -23.278 1.00 96.15 C
ANISOU 559 CB SER A 177 14449 11957 10128 -228 152 -326 C
ATOM 560 OG SER A 177 22.487 -10.333 -24.477 1.00 98.22 O
ANISOU 560 OG SER A 177 14831 12252 10237 -291 289 -410 O
ATOM 561 N PRO A 178 21.794 -7.014 -25.118 1.00 98.27 N
ANISOU 561 N PRO A 178 14558 12657 10123 -48 -46 47 N
ATOM 562 CA PRO A 178 20.985 -6.071 -25.936 1.00 96.56 C
ANISOU 562 CA PRO A 178 14276 12724 9689 -3 -165 172 C
ATOM 563 C PRO A 178 19.810 -6.735 -26.639 1.00 96.81 C
ANISOU 563 C PRO A 178 14272 13070 9444 -163 -240 30 C
ATOM 564 O PRO A 178 18.799 -6.075 -26.895 1.00 94.67 O
ANISOU 564 O PRO A 178 13885 13082 9005 -110 -381 127 O
ATOM 565 CB PRO A 178 22.008 -5.494 -26.955 1.00 97.76 C
ANISOU 565 CB PRO A 178 14506 12860 9776 63 -58 276 C
ATOM 566 CG PRO A 178 23.255 -6.415 -26.848 1.00 99.33 C
ANISOU 566 CG PRO A 178 14801 12825 10115 11 121 152 C
ATOM 567 CD PRO A 178 22.939 -7.513 -25.863 1.00 99.62 C
ANISOU 567 CD PRO A 178 14843 12734 10276 -68 128 -10 C
ATOM 568 N GLU A 179 19.928 -8.021 -26.978 1.00 99.52 N
ANISOU 568 N GLU A 179 14713 13386 9716 -357 -132 -199 N
ATOM 569 CA GLU A 179 18.799 -8.777 -27.511 1.00 98.73 C
ANISOU 569 CA GLU A 179 14583 13579 9351 -579 -184 -383 C
ATOM 570 C GLU A 179 17.727 -8.966 -26.452 1.00 96.57 C
ANISOU 570 C GLU A 179 14194 13361 9138 -637 -302 -432 C
ATOM 571 O GLU A 179 16.533 -8.850 -26.748 1.00 96.24 O
ANISOU 571 O GLU A 179 14011 13687 8870 -722 -438 -459 O
ATOM 572 CB GLU A 179 19.283 -10.131 -28.044 1.00100.75 C
ANISOU 572 CB GLU A 179 15027 13717 9537 -790 10 -632 C
ATOM 573 CG GLU A 179 20.402 -10.762 -27.189 1.00102.15 C
ANISOU 573 CG GLU A 179 15348 13454 10011 -720 184 -668 C
ATOM 574 CD GLU A 179 21.813 -10.244 -27.515 1.00102.33 C
ANISOU 574 CD GLU A 179 15423 13306 10154 -532 291 -526 C
ATOM 575 OE1 GLU A 179 21.939 -9.196 -28.206 1.00102.14 O
ANISOU 575 OE1 GLU A 179 15328 13446 10036 -433 219 -363 O
ATOM 576 OE2 GLU A 179 22.798 -10.870 -27.036 1.00102.19 O1-
ANISOU 576 OE2 GLU A 179 15511 12997 10320 -471 455 -566 O1-
ATOM 577 N VAL A 180 18.137 -9.276 -25.213 1.00 95.73 N
ANISOU 577 N VAL A 180 14132 12922 9318 -591 -250 -444 N
ATOM 578 CA VAL A 180 17.193 -9.310 -24.096 1.00 94.55 C
ANISOU 578 CA VAL A 180 13871 12799 9254 -614 -362 -459 C
ATOM 579 C VAL A 180 16.634 -7.915 -23.824 1.00 92.53 C
ANISOU 579 C VAL A 180 13437 12714 9004 -403 -538 -224 C
ATOM 580 O VAL A 180 15.422 -7.749 -23.639 1.00 93.07 O
ANISOU 580 O VAL A 180 13353 13062 8947 -437 -674 -226 O
ATOM 581 CB VAL A 180 17.848 -9.921 -22.840 1.00 91.35 C
ANISOU 581 CB VAL A 180 13565 12000 9146 -586 -257 -503 C
ATOM 582 CG1 VAL A 180 16.778 -10.453 -21.879 1.00 89.72 C
ANISOU 582 CG1 VAL A 180 13298 11829 8964 -715 -320 -611 C
ATOM 583 CG2 VAL A 180 18.815 -11.037 -23.222 1.00 91.80 C
ANISOU 583 CG2 VAL A 180 13836 11819 9225 -672 -35 -652 C
ATOM 584 N HIS A 181 17.495 -6.888 -23.826 1.00 90.69 N
ANISOU 584 N HIS A 181 13229 12328 8901 -184 -520 -20 N
ATOM 585 CA HIS A 181 17.055 -5.528 -23.498 1.00 92.70 C
ANISOU 585 CA HIS A 181 13375 12667 9181 33 -638 211 C
ATOM 586 C HIS A 181 15.883 -5.083 -24.379 1.00 95.34 C
ANISOU 586 C HIS A 181 13578 13446 9201 62 -765 276 C
ATOM 587 O HIS A 181 14.861 -4.597 -23.875 1.00 94.21 O
ANISOU 587 O HIS A 181 13291 13484 9019 153 -889 356 O
ATOM 588 CB HIS A 181 18.234 -4.557 -23.633 1.00 94.24 C
ANISOU 588 CB HIS A 181 13661 12637 9509 204 -554 391 C
ATOM 589 CG HIS A 181 18.080 -3.269 -22.871 1.00 96.27 C
ANISOU 589 CG HIS A 181 13880 12803 9896 407 -608 599 C
ATOM 590 ND1 HIS A 181 17.798 -3.220 -21.518 1.00 98.19 N
ANISOU 590 ND1 HIS A 181 14070 12898 10339 433 -654 591 N
ATOM 591 CD2 HIS A 181 18.197 -1.979 -23.276 1.00 96.46 C
ANISOU 591 CD2 HIS A 181 13941 12837 9873 591 -597 817 C
ATOM 592 CE1 HIS A 181 17.744 -1.957 -21.126 1.00 97.95 C
ANISOU 592 CE1 HIS A 181 14045 12792 10379 614 -669 784 C
ATOM 593 NE2 HIS A 181 17.984 -1.185 -22.172 1.00 97.85 N
ANISOU 593 NE2 HIS A 181 14099 12859 10221 715 -625 926 N
ATOM 594 N GLN A 182 16.012 -5.252 -25.704 1.00 97.09 N
ANISOU 594 N GLN A 182 13834 13877 9177 -4 -734 246 N
ATOM 595 CA GLN A 182 14.949 -4.861 -26.626 1.00 95.19 C
ANISOU 595 CA GLN A 182 13451 14121 8596 32 -855 314 C
ATOM 596 C GLN A 182 13.732 -5.797 -26.550 1.00 96.91 C
ANISOU 596 C GLN A 182 13517 14681 8624 -205 -948 103 C
ATOM 597 O GLN A 182 12.614 -5.369 -26.861 1.00 97.30 O
ANISOU 597 O GLN A 182 13370 15173 8427 -140 -1088 181 O
ATOM 598 CB GLN A 182 15.500 -4.804 -28.060 1.00 98.03 C
ANISOU 598 CB GLN A 182 13897 14614 8736 15 -786 335 C
ATOM 599 CG GLN A 182 16.639 -3.779 -28.302 1.00 97.46 C
ANISOU 599 CG GLN A 182 13967 14266 8799 234 -685 556 C
ATOM 600 CD GLN A 182 16.992 -3.586 -29.808 1.00 96.57 C
ANISOU 600 CD GLN A 182 13918 14357 8416 242 -633 610 C
ATOM 601 OE1 GLN A 182 16.291 -4.080 -30.700 1.00 94.98 O
ANISOU 601 OE1 GLN A 182 13634 14554 7899 114 -695 510 O
ATOM 602 NE2 GLN A 182 18.102 -2.888 -30.077 1.00 93.90 N
ANISOU 602 NE2 GLN A 182 13727 13759 8193 367 -511 757 N
ATOM 603 N SER A 183 13.907 -7.065 -26.134 1.00100.18 N
ANISOU 603 N SER A 183 14018 14913 9132 -478 -860 -161 N
ATOM 604 CA SER A 183 12.816 -8.040 -26.240 1.00 99.21 C
ANISOU 604 CA SER A 183 13789 15118 8788 -777 -909 -400 C
ATOM 605 C SER A 183 11.694 -7.819 -25.226 1.00100.13 C
ANISOU 605 C SER A 183 13706 15399 8940 -744 -1045 -370 C
ATOM 606 O SER A 183 10.561 -8.252 -25.485 1.00101.95 O
ANISOU 606 O SER A 183 13763 16067 8905 -943 -1132 -504 O
ATOM 607 CB SER A 183 13.340 -9.476 -26.101 1.00 99.41 C
ANISOU 607 CB SER A 183 14021 14852 8897 -1079 -730 -691 C
ATOM 608 OG SER A 183 14.043 -9.697 -24.889 1.00 97.14 O
ANISOU 608 OG SER A 183 13859 14080 8970 -1001 -641 -679 O
ATOM 609 N ASN A 184 11.978 -7.179 -24.081 1.00 96.39 N
ANISOU 609 N ASN A 184 13245 14608 8769 -519 -1058 -211 N
ATOM 610 CA ASN A 184 10.949 -6.799 -23.103 1.00 94.70 C
ANISOU 610 CA ASN A 184 12843 14540 8598 -436 -1183 -147 C
ATOM 611 C ASN A 184 10.188 -8.020 -22.573 1.00 93.22 C
ANISOU 611 C ASN A 184 12607 14445 8367 -772 -1174 -421 C
ATOM 612 O ASN A 184 8.971 -7.985 -22.396 1.00 93.16 O
ANISOU 612 O ASN A 184 12375 14835 8188 -831 -1294 -448 O
ATOM 613 CB ASN A 184 9.987 -5.772 -23.712 1.00 95.72 C
ANISOU 613 CB ASN A 184 12745 15168 8455 -221 -1335 55 C
ATOM 614 CG ASN A 184 9.642 -4.625 -22.760 1.00 96.21 C
ANISOU 614 CG ASN A 184 12723 15152 8682 110 -1406 301 C
ATOM 615 OD1 ASN A 184 10.512 -3.846 -22.374 1.00 96.73 O
ANISOU 615 OD1 ASN A 184 12941 14828 8986 328 -1338 470 O
ATOM 616 ND2 ASN A 184 8.359 -4.470 -22.453 1.00 95.22 N
ANISOU 616 ND2 ASN A 184 12352 15428 8401 146 -1533 323 N
ATOM 617 N VAL A 185 10.909 -9.110 -22.289 1.00 91.62 N
ANISOU 617 N VAL A 185 12624 13872 8316 -987 -1015 -621 N
ATOM 618 CA VAL A 185 10.260 -10.330 -21.819 1.00 87.66 C
ANISOU 618 CA VAL A 185 12139 13396 7770 -1328 -958 -891 C
ATOM 619 C VAL A 185 9.655 -10.108 -20.437 1.00 85.39 C
ANISOU 619 C VAL A 185 11739 13038 7666 -1250 -1032 -835 C
ATOM 620 O VAL A 185 10.091 -9.245 -19.666 1.00 84.59 O
ANISOU 620 O VAL A 185 11635 12697 7808 -955 -1070 -625 O
ATOM 621 CB VAL A 185 11.245 -11.511 -21.796 1.00 85.41 C
ANISOU 621 CB VAL A 185 12163 12672 7618 -1516 -732 -1083 C
ATOM 622 CG1 VAL A 185 10.479 -12.808 -22.010 1.00 84.58 C
ANISOU 622 CG1 VAL A 185 12110 12723 7303 -1949 -640 -1402 C
ATOM 623 CG2 VAL A 185 12.316 -11.315 -22.836 1.00 87.53 C
ANISOU 623 CG2 VAL A 185 12570 12833 7855 -1416 -650 -1024 C
ATOM 624 N GLY A 186 8.646 -10.913 -20.109 1.00 85.48 N
ANISOU 624 N GLY A 186 11666 13260 7551 -1545 -1037 -1040 N
ATOM 625 CA GLY A 186 8.004 -10.760 -18.822 1.00 80.80 C
ANISOU 625 CA GLY A 186 10960 12630 7109 -1494 -1100 -1002 C
ATOM 626 C GLY A 186 8.980 -10.916 -17.680 1.00 80.02 C
ANISOU 626 C GLY A 186 11074 11948 7382 -1366 -990 -949 C
ATOM 627 O GLY A 186 9.029 -10.077 -16.781 1.00 80.61 O
ANISOU 627 O GLY A 186 11075 11901 7652 -1105 -1066 -762 O
ATOM 628 N TRP A 187 9.801 -11.971 -17.715 1.00 80.10 N
ANISOU 628 N TRP A 187 11356 11597 7481 -1531 -797 -1105 N
ATOM 629 CA TRP A 187 10.718 -12.200 -16.604 1.00 78.79 C
ANISOU 629 CA TRP A 187 11373 10926 7638 -1397 -688 -1049 C
ATOM 630 C TRP A 187 11.752 -11.090 -16.527 1.00 77.86 C
ANISOU 630 C TRP A 187 11253 10621 7709 -1040 -736 -798 C
ATOM 631 O TRP A 187 12.350 -10.869 -15.467 1.00 75.08 O
ANISOU 631 O TRP A 187 10951 9963 7612 -873 -713 -696 O
ATOM 632 CB TRP A 187 11.391 -13.574 -16.730 1.00 80.45 C
ANISOU 632 CB TRP A 187 11885 10804 7877 -1605 -448 -1248 C
ATOM 633 CG TRP A 187 12.192 -13.735 -17.978 1.00 82.69 C
ANISOU 633 CG TRP A 187 12302 11064 8054 -1614 -355 -1281 C
ATOM 634 CD1 TRP A 187 11.725 -14.103 -19.204 1.00 82.73 C
ANISOU 634 CD1 TRP A 187 12301 11371 7762 -1858 -338 -1441 C
ATOM 635 CD2 TRP A 187 13.599 -13.475 -18.144 1.00 82.18 C
ANISOU 635 CD2 TRP A 187 12372 10695 8159 -1371 -270 -1148 C
ATOM 636 NE1 TRP A 187 12.753 -14.122 -20.112 1.00 82.22 N
ANISOU 636 NE1 TRP A 187 12381 11176 7681 -1777 -239 -1418 N
ATOM 637 CE2 TRP A 187 13.911 -13.740 -19.489 1.00 81.24 C
ANISOU 637 CE2 TRP A 187 12339 10684 7842 -1477 -195 -1237 C
ATOM 638 CE3 TRP A 187 14.623 -13.061 -17.282 1.00 82.01 C
ANISOU 638 CE3 TRP A 187 12390 10350 8418 -1091 -248 -972 C
ATOM 639 CZ2 TRP A 187 15.201 -13.597 -20.000 1.00 84.28 C
ANISOU 639 CZ2 TRP A 187 12851 10857 8313 -1301 -95 -1149 C
ATOM 640 CZ3 TRP A 187 15.908 -12.920 -17.791 1.00 82.19 C
ANISOU 640 CZ3 TRP A 187 12521 10191 8516 -930 -153 -890 C
ATOM 641 CH2 TRP A 187 16.184 -13.188 -19.137 1.00 84.56 C
ANISOU 641 CH2 TRP A 187 12909 10595 8627 -1029 -75 -976 C
ATOM 642 N CYS A 188 11.954 -10.385 -17.645 1.00 79.06 N
ANISOU 642 N CYS A 188 11346 10973 7719 -940 -794 -703 N
ATOM 643 CA CYS A 188 12.926 -9.299 -17.731 1.00 78.31 C
ANISOU 643 CA CYS A 188 11266 10720 7767 -642 -815 -477 C
ATOM 644 C CYS A 188 12.443 -8.047 -16.996 1.00 75.55 C
ANISOU 644 C CYS A 188 10751 10449 7506 -406 -958 -272 C
ATOM 645 O CYS A 188 13.239 -7.349 -16.357 1.00 74.71 O
ANISOU 645 O CYS A 188 10693 10077 7618 -208 -941 -126 O
ATOM 646 CB CYS A 188 13.189 -8.994 -19.213 1.00 82.14 C
ANISOU 646 CB CYS A 188 11761 11409 8040 -633 -814 -447 C
ATOM 647 SG CYS A 188 14.617 -7.934 -19.618 1.00 87.06 S
ANISOU 647 SG CYS A 188 12473 11802 8803 -353 -768 -223 S
ATOM 648 N ARG A 189 11.153 -7.711 -17.124 1.00 78.62 N
ANISOU 648 N ARG A 189 10939 11224 7707 -421 -1089 -259 N
ATOM 649 CA ARG A 189 10.600 -6.592 -16.363 1.00 81.01 C
ANISOU 649 CA ARG A 189 11101 11594 8088 -183 -1200 -72 C
ATOM 650 C ARG A 189 10.442 -6.955 -14.885 1.00 76.62 C
ANISOU 650 C ARG A 189 10552 10813 7748 -223 -1185 -128 C
ATOM 651 O ARG A 189 10.659 -6.112 -14.006 1.00 72.27 O
ANISOU 651 O ARG A 189 9995 10082 7382 -18 -1208 20 O
ATOM 652 CB ARG A 189 9.247 -6.179 -16.930 1.00 81.79 C
ANISOU 652 CB ARG A 189 10961 12214 7900 -156 -1335 -30 C
ATOM 653 CG ARG A 189 9.161 -6.054 -18.404 1.00 84.17 C
ANISOU 653 CG ARG A 189 11221 12838 7920 -168 -1360 -12 C
ATOM 654 CD ARG A 189 7.786 -6.542 -18.765 1.00 87.39 C
ANISOU 654 CD ARG A 189 11396 13781 8027 -358 -1459 -140 C
ATOM 655 NE ARG A 189 7.458 -6.564 -20.184 1.00 87.58 N
ANISOU 655 NE ARG A 189 11326 14241 7710 -422 -1505 -158 N
ATOM 656 CZ ARG A 189 6.219 -6.613 -20.658 1.00 89.16 C
ANISOU 656 CZ ARG A 189 11258 15034 7586 -503 -1623 -198 C
ATOM 657 NH1 ARG A 189 5.172 -6.691 -19.853 1.00 88.57 N
ANISOU 657 NH1 ARG A 189 10980 15188 7486 -546 -1700 -236 N
ATOM 658 NH2 ARG A 189 6.023 -6.587 -21.976 1.00 92.62 N
ANISOU 658 NH2 ARG A 189 11612 15878 7700 -548 -1664 -201 N
ATOM 659 N LEU A 190 10.029 -8.202 -14.618 1.00 74.00 N
ANISOU 659 N LEU A 190 10247 10494 7377 -501 -1134 -345 N
ATOM 660 CA LEU A 190 9.922 -8.750 -13.268 1.00 72.56 C
ANISOU 660 CA LEU A 190 10106 10083 7382 -570 -1094 -416 C
ATOM 661 C LEU A 190 11.264 -8.749 -12.541 1.00 71.96 C
ANISOU 661 C LEU A 190 10210 9550 7582 -442 -994 -349 C
ATOM 662 O LEU A 190 11.329 -8.468 -11.335 1.00 71.60 O
ANISOU 662 O LEU A 190 10152 9332 7722 -342 -1009 -285 O
ATOM 663 CB LEU A 190 9.354 -10.164 -13.354 1.00 72.08 C
ANISOU 663 CB LEU A 190 10098 10093 7194 -920 -1010 -672 C
ATOM 664 CG LEU A 190 9.357 -10.975 -12.066 1.00 76.11 C
ANISOU 664 CG LEU A 190 10717 10320 7882 -1024 -918 -764 C
ATOM 665 CD1 LEU A 190 8.462 -10.320 -11.002 1.00 77.21 C
ANISOU 665 CD1 LEU A 190 10663 10590 8082 -923 -1040 -678 C
ATOM 666 CD2 LEU A 190 8.906 -12.404 -12.340 1.00 78.33 C
ANISOU 666 CD2 LEU A 190 11120 10626 8017 -1395 -784 -1027 C
ATOM 667 N VAL A 191 12.343 -9.075 -13.250 1.00 73.17 N
ANISOU 667 N VAL A 191 10517 9532 7750 -447 -890 -367 N
ATOM 668 CA VAL A 191 13.673 -8.983 -12.660 1.00 71.08 C
ANISOU 668 CA VAL A 191 10380 8912 7716 -305 -803 -286 C
ATOM 669 C VAL A 191 14.040 -7.526 -12.352 1.00 70.19 C
ANISOU 669 C VAL A 191 10187 8770 7713 -62 -885 -79 C
ATOM 670 O VAL A 191 14.732 -7.247 -11.367 1.00 67.50 O
ANISOU 670 O VAL A 191 9875 8203 7568 41 -860 -11 O
ATOM 671 CB VAL A 191 14.700 -9.670 -13.584 1.00 71.00 C
ANISOU 671 CB VAL A 191 10536 8772 7670 -358 -662 -354 C
ATOM 672 CG1 VAL A 191 16.111 -9.322 -13.185 1.00 70.73 C
ANISOU 672 CG1 VAL A 191 10570 8472 7831 -177 -594 -237 C
ATOM 673 CG2 VAL A 191 14.531 -11.171 -13.513 1.00 70.26 C
ANISOU 673 CG2 VAL A 191 10593 8572 7530 -578 -522 -556 C
ATOM 674 N THR A 192 13.609 -6.574 -13.192 1.00 72.34 N
ANISOU 674 N THR A 192 10371 9270 7846 31 -967 26 N
ATOM 675 CA THR A 192 13.976 -5.176 -12.956 1.00 70.63 C
ANISOU 675 CA THR A 192 10134 8981 7722 253 -1001 221 C
ATOM 676 C THR A 192 13.223 -4.606 -11.755 1.00 67.16 C
ANISOU 676 C THR A 192 9601 8540 7375 341 -1074 280 C
ATOM 677 O THR A 192 13.800 -3.875 -10.943 1.00 63.83 O
ANISOU 677 O THR A 192 9218 7912 7124 454 -1052 372 O
ATOM 678 CB THR A 192 13.734 -4.352 -14.236 1.00 70.43 C
ANISOU 678 CB THR A 192 10078 9179 7504 354 -1038 334 C
ATOM 679 OG1 THR A 192 14.671 -4.773 -15.229 1.00 75.02 O
ANISOU 679 OG1 THR A 192 10767 9702 8035 286 -950 291 O
ATOM 680 CG2 THR A 192 13.949 -2.847 -14.031 1.00 69.79 C
ANISOU 680 CG2 THR A 192 10014 9011 7493 585 -1042 543 C
ATOM 681 N ALA A 193 11.928 -4.916 -11.641 1.00 67.99 N
ANISOU 681 N ALA A 193 9578 8899 7357 277 -1155 219 N
ATOM 682 CA ALA A 193 11.149 -4.475 -10.489 1.00 68.94 C
ANISOU 682 CA ALA A 193 9602 9037 7556 355 -1215 262 C
ATOM 683 C ALA A 193 11.653 -5.122 -9.193 1.00 66.20 C
ANISOU 683 C ALA A 193 9325 8409 7418 272 -1162 180 C
ATOM 684 O ALA A 193 11.611 -4.506 -8.123 1.00 62.16 O
ANISOU 684 O ALA A 193 8796 7781 7042 376 -1178 249 O
ATOM 685 CB ALA A 193 9.661 -4.772 -10.721 1.00 68.30 C
ANISOU 685 CB ALA A 193 9338 9343 7269 281 -1308 202 C
ATOM 686 N ALA A 194 12.132 -6.365 -9.264 1.00 65.75 N
ANISOU 686 N ALA A 194 9363 8242 7379 97 -1083 38 N
ATOM 687 CA ALA A 194 12.713 -6.981 -8.076 1.00 63.25 C
ANISOU 687 CA ALA A 194 9126 7661 7244 63 -1017 -9 C
ATOM 688 C ALA A 194 13.929 -6.200 -7.611 1.00 62.99 C
ANISOU 688 C ALA A 194 9147 7410 7379 217 -986 110 C
ATOM 689 O ALA A 194 14.055 -5.873 -6.425 1.00 64.09 O
ANISOU 689 O ALA A 194 9266 7431 7652 276 -997 150 O
ATOM 690 CB ALA A 194 13.070 -8.447 -8.343 1.00 61.77 C
ANISOU 690 CB ALA A 194 9071 7371 7028 -113 -901 -162 C
ATOM 691 N TYR A 195 14.803 -5.833 -8.539 1.00 62.97 N
ANISOU 691 N TYR A 195 9200 7376 7351 267 -944 165 N
ATOM 692 CA TYR A 195 15.999 -5.093 -8.159 1.00 60.65 C
ANISOU 692 CA TYR A 195 8944 6908 7193 369 -901 260 C
ATOM 693 C TYR A 195 15.631 -3.710 -7.629 1.00 59.49 C
ANISOU 693 C TYR A 195 8749 6764 7091 485 -957 376 C
ATOM 694 O TYR A 195 16.273 -3.192 -6.696 1.00 58.10 O
ANISOU 694 O TYR A 195 8584 6444 7048 521 -932 414 O
ATOM 695 CB TYR A 195 16.974 -5.016 -9.355 1.00 61.93 C
ANISOU 695 CB TYR A 195 9173 7057 7300 378 -832 286 C
ATOM 696 CG TYR A 195 18.189 -4.173 -9.066 1.00 56.64 C
ANISOU 696 CG TYR A 195 8524 6254 6742 449 -780 375 C
ATOM 697 CD1 TYR A 195 18.088 -2.783 -9.033 1.00 58.56 C
ANISOU 697 CD1 TYR A 195 8766 6489 6995 527 -801 487 C
ATOM 698 CD2 TYR A 195 19.403 -4.756 -8.728 1.00 54.73 C
ANISOU 698 CD2 TYR A 195 8303 5904 6587 436 -698 347 C
ATOM 699 CE1 TYR A 195 19.166 -2.001 -8.704 1.00 60.40 C
ANISOU 699 CE1 TYR A 195 9026 6603 7319 538 -736 542 C
ATOM 700 CE2 TYR A 195 20.501 -3.981 -8.418 1.00 53.90 C
ANISOU 700 CE2 TYR A 195 8182 5735 6564 466 -654 412 C
ATOM 701 CZ TYR A 195 20.378 -2.604 -8.404 1.00 59.04 C
ANISOU 701 CZ TYR A 195 8840 6373 7221 491 -672 497 C
ATOM 702 OH TYR A 195 21.450 -1.789 -8.079 1.00 65.93 O
ANISOU 702 OH TYR A 195 9709 7183 8159 469 -609 540 O
ATOM 703 N ASN A 196 14.616 -3.083 -8.227 1.00 60.16 N
ANISOU 703 N ASN A 196 8785 7024 7050 551 -1018 434 N
ATOM 704 CA ASN A 196 14.204 -1.767 -7.746 1.00 62.48 C
ANISOU 704 CA ASN A 196 9068 7297 7375 695 -1038 555 C
ATOM 705 C ASN A 196 13.586 -1.853 -6.358 1.00 61.80 C
ANISOU 705 C ASN A 196 8921 7176 7384 691 -1077 519 C
ATOM 706 O ASN A 196 13.881 -1.019 -5.496 1.00 58.32 O
ANISOU 706 O ASN A 196 8519 6587 7054 753 -1048 573 O
ATOM 707 CB ASN A 196 13.248 -1.124 -8.741 1.00 63.61 C
ANISOU 707 CB ASN A 196 9168 7663 7337 816 -1083 652 C
ATOM 708 CG ASN A 196 13.987 -0.458 -9.916 1.00 63.97 C
ANISOU 708 CG ASN A 196 9313 7679 7313 883 -1019 751 C
ATOM 709 OD1 ASN A 196 15.204 -0.202 -9.839 1.00 58.51 O
ANISOU 709 OD1 ASN A 196 8724 6777 6730 846 -933 761 O
ATOM 710 ND2 ASN A 196 13.242 -0.160 -10.997 1.00 64.73 N
ANISOU 710 ND2 ASN A 196 9368 8015 7212 980 -1057 830 N
ATOM 711 N TYR A 197 12.747 -2.873 -6.127 1.00 61.52 N
ANISOU 711 N TYR A 197 8803 7272 7299 594 -1129 415 N
ATOM 712 CA TYR A 197 12.120 -3.075 -4.830 1.00 60.10 C
ANISOU 712 CA TYR A 197 8565 7072 7197 573 -1160 372 C
ATOM 713 C TYR A 197 13.162 -3.226 -3.729 1.00 60.55 C
ANISOU 713 C TYR A 197 8689 6890 7428 542 -1108 351 C
ATOM 714 O TYR A 197 13.069 -2.583 -2.666 1.00 59.17 O
ANISOU 714 O TYR A 197 8504 6636 7343 596 -1113 385 O
ATOM 715 CB TYR A 197 11.235 -4.316 -4.873 1.00 62.98 C
ANISOU 715 CB TYR A 197 8859 7599 7472 420 -1192 242 C
ATOM 716 CG TYR A 197 10.833 -4.750 -3.493 1.00 63.11 C
ANISOU 716 CG TYR A 197 8847 7548 7584 367 -1197 184 C
ATOM 717 CD1 TYR A 197 9.805 -4.086 -2.815 1.00 63.81 C
ANISOU 717 CD1 TYR A 197 8830 7751 7664 451 -1253 227 C
ATOM 718 CD2 TYR A 197 11.496 -5.796 -2.843 1.00 61.43 C
ANISOU 718 CD2 TYR A 197 8719 7158 7465 259 -1132 102 C
ATOM 719 CE1 TYR A 197 9.421 -4.463 -1.515 1.00 62.81 C
ANISOU 719 CE1 TYR A 197 8677 7566 7620 398 -1254 174 C
ATOM 720 CE2 TYR A 197 11.124 -6.186 -1.544 1.00 62.19 C
ANISOU 720 CE2 TYR A 197 8799 7192 7638 220 -1130 62 C
ATOM 721 CZ TYR A 197 10.076 -5.507 -0.888 1.00 60.88 C
ANISOU 721 CZ TYR A 197 8522 7146 7463 276 -1195 92 C
ATOM 722 OH TYR A 197 9.706 -5.861 0.381 1.00 56.97 O
ANISOU 722 OH TYR A 197 8012 6598 7038 235 -1189 54 O
ATOM 723 N PHE A 198 14.151 -4.100 -3.957 1.00 58.39 N
ANISOU 723 N PHE A 198 8477 6522 7186 460 -1051 295 N
ATOM 724 CA PHE A 198 15.239 -4.261 -2.998 1.00 54.88 C
ANISOU 724 CA PHE A 198 8066 5911 6874 456 -1002 292 C
ATOM 725 C PHE A 198 16.043 -2.985 -2.828 1.00 54.81 C
ANISOU 725 C PHE A 198 8077 5821 6928 520 -978 377 C
ATOM 726 O PHE A 198 16.583 -2.747 -1.744 1.00 55.11 O
ANISOU 726 O PHE A 198 8103 5779 7058 513 -964 378 O
ATOM 727 CB PHE A 198 16.163 -5.390 -3.429 1.00 55.21 C
ANISOU 727 CB PHE A 198 8169 5895 6914 405 -928 241 C
ATOM 728 CG PHE A 198 15.544 -6.735 -3.309 1.00 59.27 C
ANISOU 728 CG PHE A 198 8716 6417 7387 315 -903 142 C
ATOM 729 CD1 PHE A 198 14.790 -7.071 -2.180 1.00 58.86 C
ANISOU 729 CD1 PHE A 198 8635 6356 7373 282 -929 107 C
ATOM 730 CD2 PHE A 198 15.708 -7.674 -4.318 1.00 59.98 C
ANISOU 730 CD2 PHE A 198 8887 6511 7391 245 -833 73 C
ATOM 731 CE1 PHE A 198 14.210 -8.306 -2.064 1.00 58.70 C
ANISOU 731 CE1 PHE A 198 8673 6325 7307 172 -879 8 C
ATOM 732 CE2 PHE A 198 15.130 -8.935 -4.210 1.00 59.94 C
ANISOU 732 CE2 PHE A 198 8954 6482 7337 127 -774 -37 C
ATOM 733 CZ PHE A 198 14.376 -9.250 -3.081 1.00 58.77 C
ANISOU 733 CZ PHE A 198 8784 6318 7228 85 -794 -69 C
ATOM 734 N HIS A 199 16.189 -2.174 -3.889 1.00 57.83 N
ANISOU 734 N HIS A 199 8499 6225 7247 566 -959 443 N
ATOM 735 CA HIS A 199 16.891 -0.901 -3.708 1.00 56.40 C
ANISOU 735 CA HIS A 199 8373 5941 7117 597 -905 514 C
ATOM 736 C HIS A 199 16.129 0.038 -2.780 1.00 55.88 C
ANISOU 736 C HIS A 199 8315 5830 7088 655 -918 548 C
ATOM 737 O HIS A 199 16.730 0.699 -1.923 1.00 53.88 O
ANISOU 737 O HIS A 199 8094 5466 6912 617 -870 545 O
ATOM 738 CB HIS A 199 17.176 -0.235 -5.054 1.00 56.34 C
ANISOU 738 CB HIS A 199 8437 5944 7024 638 -857 589 C
ATOM 739 CG HIS A 199 18.388 0.656 -5.033 1.00 57.74 C
ANISOU 739 CG HIS A 199 8687 6000 7252 594 -760 623 C
ATOM 740 ND1 HIS A 199 18.362 1.960 -5.480 1.00 59.22 N
ANISOU 740 ND1 HIS A 199 8990 6105 7404 647 -686 715 N
ATOM 741 CD2 HIS A 199 19.633 0.467 -4.521 1.00 61.32 C
ANISOU 741 CD2 HIS A 199 9111 6412 7776 494 -713 576 C
ATOM 742 CE1 HIS A 199 19.549 2.520 -5.293 1.00 61.63 C
ANISOU 742 CE1 HIS A 199 9346 6311 7758 542 -590 704 C
ATOM 743 NE2 HIS A 199 20.337 1.639 -4.702 1.00 61.07 N
ANISOU 743 NE2 HIS A 199 9165 6291 7747 447 -616 619 N
ATOM 744 N VAL A 200 14.810 0.104 -2.926 1.00 56.08 N
ANISOU 744 N VAL A 200 8302 5961 7044 741 -974 574 N
ATOM 745 CA VAL A 200 14.035 0.937 -2.031 1.00 59.01 C
ANISOU 745 CA VAL A 200 8680 6296 7446 823 -973 610 C
ATOM 746 C VAL A 200 14.138 0.415 -0.597 1.00 57.65 C
ANISOU 746 C VAL A 200 8457 6074 7375 737 -996 524 C
ATOM 747 O VAL A 200 14.349 1.187 0.341 1.00 53.07 O
ANISOU 747 O VAL A 200 7923 5380 6862 734 -952 527 O
ATOM 748 CB VAL A 200 12.583 1.024 -2.527 1.00 60.33 C
ANISOU 748 CB VAL A 200 8776 6652 7494 953 -1033 662 C
ATOM 749 CG1 VAL A 200 11.739 1.801 -1.530 1.00 58.04 C
ANISOU 749 CG1 VAL A 200 8483 6334 7234 1062 -1021 700 C
ATOM 750 CG2 VAL A 200 12.544 1.686 -3.911 1.00 59.30 C
ANISOU 750 CG2 VAL A 200 8704 6584 7244 1070 -1001 774 C
ATOM 751 N THR A 201 14.056 -0.902 -0.403 1.00 56.58 N
ANISOU 751 N THR A 201 8245 6010 7241 656 -1047 445 N
ATOM 752 CA THR A 201 14.113 -1.399 0.968 1.00 56.12 C
ANISOU 752 CA THR A 201 8150 5910 7264 598 -1060 384 C
ATOM 753 C THR A 201 15.422 -1.008 1.652 1.00 56.23 C
ANISOU 753 C THR A 201 8196 5813 7356 545 -1009 379 C
ATOM 754 O THR A 201 15.442 -0.779 2.872 1.00 56.14 O
ANISOU 754 O THR A 201 8168 5766 7398 520 -1009 354 O
ATOM 755 CB THR A 201 13.919 -2.929 1.038 1.00 54.25 C
ANISOU 755 CB THR A 201 7871 5730 7010 522 -1086 309 C
ATOM 756 OG1 THR A 201 15.111 -3.604 0.626 1.00 52.88 O
ANISOU 756 OG1 THR A 201 7736 5506 6852 482 -1039 296 O
ATOM 757 CG2 THR A 201 12.699 -3.397 0.242 1.00 55.55 C
ANISOU 757 CG2 THR A 201 7992 6049 7067 511 -1128 283 C
ATOM 758 N ASN A 202 16.524 -0.946 0.903 1.00 55.68 N
ANISOU 758 N ASN A 202 8156 5720 7278 515 -964 396 N
ATOM 759 CA ASN A 202 17.795 -0.550 1.511 1.00 56.00 C
ANISOU 759 CA ASN A 202 8192 5719 7366 442 -914 383 C
ATOM 760 C ASN A 202 17.715 0.866 2.080 1.00 55.24 C
ANISOU 760 C ASN A 202 8164 5534 7291 416 -864 392 C
ATOM 761 O ASN A 202 18.401 1.178 3.063 1.00 55.46 O
ANISOU 761 O ASN A 202 8169 5555 7350 323 -837 349 O
ATOM 762 CB ASN A 202 18.966 -0.627 0.494 1.00 57.99 C
ANISOU 762 CB ASN A 202 8455 5988 7592 410 -861 401 C
ATOM 763 CG ASN A 202 19.287 -2.058 -0.004 1.00 55.72 C
ANISOU 763 CG ASN A 202 8125 5763 7282 436 -873 384 C
ATOM 764 OD1 ASN A 202 18.493 -2.994 0.151 1.00 54.99 O
ANISOU 764 OD1 ASN A 202 8027 5685 7182 464 -911 357 O
ATOM 765 ND2 ASN A 202 20.497 -2.225 -0.570 1.00 54.73 N
ANISOU 765 ND2 ASN A 202 7982 5671 7142 416 -818 394 N
ATOM 766 N PHE A 203 16.938 1.747 1.439 1.00 54.20 N
ANISOU 766 N PHE A 203 8127 5340 7127 500 -833 451 N
ATOM 767 CA PHE A 203 16.800 3.121 1.918 1.00 58.20 C
ANISOU 767 CA PHE A 203 8753 5714 7646 498 -743 467 C
ATOM 768 C PHE A 203 15.914 3.195 3.163 1.00 58.68 C
ANISOU 768 C PHE A 203 8789 5766 7740 529 -773 434 C
ATOM 769 O PHE A 203 16.151 4.001 4.068 1.00 59.17 O
ANISOU 769 O PHE A 203 8922 5731 7829 457 -700 393 O
ATOM 770 CB PHE A 203 16.203 3.992 0.819 1.00 58.46 C
ANISOU 770 CB PHE A 203 8911 5682 7618 633 -681 570 C
ATOM 771 CG PHE A 203 17.215 4.611 -0.066 1.00 61.07 C
ANISOU 771 CG PHE A 203 9349 5931 7923 568 -579 603 C
ATOM 772 CD1 PHE A 203 17.559 5.961 0.101 1.00 64.20 C
ANISOU 772 CD1 PHE A 203 9933 6139 8322 522 -422 619 C
ATOM 773 CD2 PHE A 203 17.840 3.865 -1.064 1.00 61.94 C
ANISOU 773 CD2 PHE A 203 9396 6138 8002 540 -615 609 C
ATOM 774 CE1 PHE A 203 18.521 6.539 -0.709 1.00 64.88 C
ANISOU 774 CE1 PHE A 203 10130 6145 8378 431 -308 642 C
ATOM 775 CE2 PHE A 203 18.805 4.434 -1.876 1.00 62.20 C
ANISOU 775 CE2 PHE A 203 9520 6106 8006 469 -514 636 C
ATOM 776 CZ PHE A 203 19.146 5.771 -1.712 1.00 62.32 C
ANISOU 776 CZ PHE A 203 9712 5944 8022 408 -361 654 C
ATOM 777 N PHE A 204 14.852 2.395 3.182 1.00 57.52 N
ANISOU 777 N PHE A 204 8551 5727 7578 621 -866 442 N
ATOM 778 CA PHE A 204 13.873 2.361 4.246 1.00 57.43 C
ANISOU 778 CA PHE A 204 8499 5736 7585 662 -897 416 C
ATOM 779 C PHE A 204 14.392 1.606 5.472 1.00 60.12 C
ANISOU 779 C PHE A 204 8760 6107 7976 542 -936 332 C
ATOM 780 O PHE A 204 13.940 1.878 6.597 1.00 58.73 O
ANISOU 780 O PHE A 204 8582 5910 7822 535 -930 298 O
ATOM 781 CB PHE A 204 12.567 1.758 3.699 1.00 54.12 C
ANISOU 781 CB PHE A 204 7993 5464 7106 777 -974 449 C
ATOM 782 CG PHE A 204 11.662 2.763 3.016 1.00 57.73 C
ANISOU 782 CG PHE A 204 8506 5933 7495 958 -933 550 C
ATOM 783 CD1 PHE A 204 12.008 3.334 1.800 1.00 59.23 C
ANISOU 783 CD1 PHE A 204 8782 6091 7631 1025 -882 633 C
ATOM 784 CD2 PHE A 204 10.487 3.183 3.621 1.00 61.23 C
ANISOU 784 CD2 PHE A 204 8922 6424 7919 1083 -929 576 C
ATOM 785 CE1 PHE A 204 11.174 4.255 1.174 1.00 59.09 C
ANISOU 785 CE1 PHE A 204 8824 6096 7531 1234 -832 753 C
ATOM 786 CE2 PHE A 204 9.653 4.120 2.997 1.00 61.78 C
ANISOU 786 CE2 PHE A 204 9039 6527 7909 1302 -876 695 C
ATOM 787 CZ PHE A 204 10.006 4.644 1.759 1.00 60.95 C
ANISOU 787 CZ PHE A 204 9024 6394 7741 1386 -828 791 C
ATOM 788 N TRP A 205 15.328 0.665 5.275 1.00 57.22 N
ANISOU 788 N TRP A 205 8331 5796 7613 468 -966 310 N
ATOM 789 CA TRP A 205 15.970 0.002 6.405 1.00 55.81 C
ANISOU 789 CA TRP A 205 8079 5667 7460 390 -989 259 C
ATOM 790 C TRP A 205 17.086 0.844 7.017 1.00 57.64 C
ANISOU 790 C TRP A 205 8324 5880 7695 276 -932 224 C
ATOM 791 O TRP A 205 17.415 0.651 8.192 1.00 60.08 O
ANISOU 791 O TRP A 205 8572 6252 8004 214 -948 181 O
ATOM 792 CB TRP A 205 16.524 -1.364 5.982 1.00 57.11 C
ANISOU 792 CB TRP A 205 8183 5904 7613 396 -1019 266 C
ATOM 793 CG TRP A 205 15.493 -2.478 6.082 1.00 57.30 C
ANISOU 793 CG TRP A 205 8187 5956 7627 436 -1062 254 C
ATOM 794 CD1 TRP A 205 14.924 -3.189 5.044 1.00 56.27 C
ANISOU 794 CD1 TRP A 205 8073 5849 7460 457 -1072 255 C
ATOM 795 CD2 TRP A 205 14.881 -2.968 7.281 1.00 57.93 C
ANISOU 795 CD2 TRP A 205 8236 6054 7720 429 -1085 227 C
ATOM 796 NE1 TRP A 205 14.001 -4.091 5.532 1.00 54.32 N
ANISOU 796 NE1 TRP A 205 7809 5630 7200 441 -1091 219 N
ATOM 797 CE2 TRP A 205 13.962 -3.979 6.901 1.00 57.59 C
ANISOU 797 CE2 TRP A 205 8197 6034 7650 433 -1098 209 C
ATOM 798 CE3 TRP A 205 15.035 -2.666 8.643 1.00 57.01 C
ANISOU 798 CE3 TRP A 205 8091 5948 7623 402 -1088 208 C
ATOM 799 CZ2 TRP A 205 13.204 -4.682 7.835 1.00 55.86 C
ANISOU 799 CZ2 TRP A 205 7964 5830 7430 410 -1105 179 C
ATOM 800 CZ3 TRP A 205 14.292 -3.368 9.564 1.00 56.19 C
ANISOU 800 CZ3 TRP A 205 7967 5864 7518 404 -1105 190 C
ATOM 801 CH2 TRP A 205 13.382 -4.363 9.154 1.00 56.31 C
ANISOU 801 CH2 TRP A 205 7997 5885 7514 409 -1109 178 C
ATOM 802 N MET A 206 17.711 1.738 6.238 1.00 58.54 N
ANISOU 802 N MET A 206 8515 5931 7796 229 -858 237 N
ATOM 803 CA MET A 206 18.706 2.667 6.794 1.00 62.10 C
ANISOU 803 CA MET A 206 8994 6368 8232 67 -779 178 C
ATOM 804 C MET A 206 18.006 3.778 7.571 1.00 61.63 C
ANISOU 804 C MET A 206 9058 6176 8181 40 -708 140 C
ATOM 805 O MET A 206 18.537 4.284 8.566 1.00 63.70 O
ANISOU 805 O MET A 206 9322 6457 8423 -113 -662 57 O
ATOM 806 CB MET A 206 19.585 3.282 5.674 1.00 63.08 C
ANISOU 806 CB MET A 206 9186 6450 8332 0 -695 198 C
ATOM 807 CG MET A 206 20.881 2.518 5.325 1.00 61.61 C
ANISOU 807 CG MET A 206 8860 6433 8118 -61 -720 194 C
ATOM 808 SD MET A 206 22.072 2.628 6.706 1.00 67.70 S
ANISOU 808 SD MET A 206 9484 7400 8839 -257 -713 99 S
ATOM 809 CE MET A 206 23.605 1.991 5.942 1.00 73.15 C
ANISOU 809 CE MET A 206 10013 8305 9475 -290 -708 123 C
ATOM 810 N PHE A 207 16.836 4.205 7.073 1.00 59.69 N
ANISOU 810 N PHE A 207 8919 5812 7947 192 -685 202 N
ATOM 811 CA PHE A 207 15.943 5.089 7.810 1.00 60.99 C
ANISOU 811 CA PHE A 207 9198 5855 8120 237 -614 187 C
ATOM 812 C PHE A 207 15.453 4.405 9.087 1.00 62.33 C
ANISOU 812 C PHE A 207 9253 6125 8305 231 -699 135 C
ATOM 813 O PHE A 207 15.403 5.032 10.150 1.00 61.21 O
ANISOU 813 O PHE A 207 9168 5929 8159 151 -637 65 O
ATOM 814 CB PHE A 207 14.783 5.492 6.886 1.00 60.12 C
ANISOU 814 CB PHE A 207 9177 5669 7997 458 -588 295 C
ATOM 815 CG PHE A 207 13.682 6.317 7.539 1.00 62.26 C
ANISOU 815 CG PHE A 207 9554 5834 8267 580 -510 310 C
ATOM 816 CD1 PHE A 207 13.746 7.704 7.548 1.00 63.10 C
ANISOU 816 CD1 PHE A 207 9896 5719 8361 588 -323 320 C
ATOM 817 CD2 PHE A 207 12.536 5.703 8.065 1.00 65.64 C
ANISOU 817 CD2 PHE A 207 9862 6379 8699 698 -602 320 C
ATOM 818 CE1 PHE A 207 12.705 8.472 8.116 1.00 66.32 C
ANISOU 818 CE1 PHE A 207 10422 6015 8761 742 -225 347 C
ATOM 819 CE2 PHE A 207 11.489 6.454 8.640 1.00 64.61 C
ANISOU 819 CE2 PHE A 207 9814 6176 8560 839 -523 342 C
ATOM 820 CZ PHE A 207 11.576 7.837 8.665 1.00 67.03 C
ANISOU 820 CZ PHE A 207 10358 6254 8855 877 -333 361 C
ATOM 821 N GLY A 208 15.135 3.104 9.010 1.00 61.61 N
ANISOU 821 N GLY A 208 9015 6172 8222 298 -822 160 N
ATOM 822 CA GLY A 208 14.665 2.399 10.191 1.00 60.82 C
ANISOU 822 CA GLY A 208 8823 6157 8130 293 -888 122 C
ATOM 823 C GLY A 208 15.671 2.444 11.328 1.00 63.85 C
ANISOU 823 C GLY A 208 9161 6606 8492 135 -879 46 C
ATOM 824 O GLY A 208 15.318 2.693 12.490 1.00 61.96 O
ANISOU 824 O GLY A 208 8926 6372 8244 96 -867 -8 O
ATOM 825 N GLU A 209 16.938 2.200 11.011 1.00 62.71 N
ANISOU 825 N GLU A 209 8956 6546 8323 44 -884 40 N
ATOM 826 CA GLU A 209 17.986 2.305 12.017 1.00 64.14 C
ANISOU 826 CA GLU A 209 9059 6862 8451 -113 -879 -31 C
ATOM 827 C GLU A 209 17.994 3.700 12.641 1.00 66.53 C
ANISOU 827 C GLU A 209 9486 7063 8730 -263 -769 -125 C
ATOM 828 O GLU A 209 18.162 3.845 13.859 1.00 69.04 O
ANISOU 828 O GLU A 209 9764 7470 9000 -373 -768 -202 O
ATOM 829 CB GLU A 209 19.328 1.955 11.364 1.00 66.05 C
ANISOU 829 CB GLU A 209 9205 7235 8657 -171 -886 -13 C
ATOM 830 CG GLU A 209 19.619 0.461 11.434 1.00 69.78 C
ANISOU 830 CG GLU A 209 9535 7860 9117 -51 -974 55 C
ATOM 831 CD GLU A 209 20.790 0.096 12.338 1.00 76.49 C
ANISOU 831 CD GLU A 209 10218 8966 9877 -122 -1000 39 C
ATOM 832 OE1 GLU A 209 21.009 0.817 13.344 1.00 79.78 O
ANISOU 832 OE1 GLU A 209 10611 9465 10238 -271 -982 -44 O
ATOM 833 OE2 GLU A 209 21.443 -0.940 12.072 1.00 80.31 O1-
ANISOU 833 OE2 GLU A 209 10597 9583 10334 -15 -1031 112 O1-
ATOM 834 N GLY A 210 17.773 4.736 11.820 1.00 68.14 N
ANISOU 834 N GLY A 210 9864 7071 8957 -263 -659 -118 N
ATOM 835 CA GLY A 210 17.679 6.096 12.323 1.00 68.03 C
ANISOU 835 CA GLY A 210 10034 6893 8920 -390 -508 -204 C
ATOM 836 C GLY A 210 16.459 6.383 13.182 1.00 66.20 C
ANISOU 836 C GLY A 210 9881 6562 8709 -292 -483 -219 C
ATOM 837 O GLY A 210 16.528 7.221 14.082 1.00 66.64 O
ANISOU 837 O GLY A 210 10046 6548 8728 -434 -376 -323 O
ATOM 838 N CYS A 211 15.323 5.738 12.895 1.00 63.70 N
ANISOU 838 N CYS A 211 9517 6246 8440 -64 -565 -124 N
ATOM 839 CA CYS A 211 14.171 5.823 13.795 1.00 66.90 C
ANISOU 839 CA CYS A 211 9945 6620 8856 32 -559 -137 C
ATOM 840 C CYS A 211 14.479 5.200 15.159 1.00 66.09 C
ANISOU 840 C CYS A 211 9712 6682 8718 -91 -632 -217 C
ATOM 841 O CYS A 211 14.144 5.781 16.193 1.00 67.02 O
ANISOU 841 O CYS A 211 9901 6754 8810 -151 -563 -295 O
ATOM 842 CB CYS A 211 12.935 5.160 13.170 1.00 64.87 C
ANISOU 842 CB CYS A 211 9619 6395 8633 268 -640 -30 C
ATOM 843 SG CYS A 211 11.332 5.512 14.014 1.00 71.01 S
ANISOU 843 SG CYS A 211 10432 7135 9414 428 -598 -25 S
ATOM 844 N TYR A 212 15.134 4.030 15.183 1.00 65.70 N
ANISOU 844 N TYR A 212 9484 6824 8653 -117 -758 -192 N
ATOM 845 CA TYR A 212 15.414 3.356 16.451 1.00 67.24 C
ANISOU 845 CA TYR A 212 9554 7199 8797 -190 -827 -235 C
ATOM 846 C TYR A 212 16.326 4.197 17.340 1.00 70.05 C
ANISOU 846 C TYR A 212 9931 7618 9067 -421 -757 -359 C
ATOM 847 O TYR A 212 16.062 4.349 18.544 1.00 72.17 O
ANISOU 847 O TYR A 212 10197 7939 9287 -488 -746 -430 O
ATOM 848 CB TYR A 212 16.025 1.968 16.205 1.00 66.66 C
ANISOU 848 CB TYR A 212 9316 7301 8712 -135 -941 -160 C
ATOM 849 CG TYR A 212 16.615 1.301 17.453 1.00 70.38 C
ANISOU 849 CG TYR A 212 9653 7989 9098 -194 -999 -179 C
ATOM 850 CD1 TYR A 212 15.798 0.704 18.428 1.00 67.82 C
ANISOU 850 CD1 TYR A 212 9306 7697 8766 -127 -1034 -166 C
ATOM 851 CD2 TYR A 212 17.996 1.267 17.649 1.00 70.31 C
ANISOU 851 CD2 TYR A 212 9530 8185 9001 -309 -1014 -200 C
ATOM 852 CE1 TYR A 212 16.356 0.093 19.554 1.00 70.71 C
ANISOU 852 CE1 TYR A 212 9557 8272 9036 -159 -1081 -163 C
ATOM 853 CE2 TYR A 212 18.560 0.657 18.760 1.00 71.23 C
ANISOU 853 CE2 TYR A 212 9502 8548 9012 -331 -1070 -195 C
ATOM 854 CZ TYR A 212 17.746 0.076 19.718 1.00 72.90 C
ANISOU 854 CZ TYR A 212 9714 8771 9215 -249 -1102 -171 C
ATOM 855 OH TYR A 212 18.350 -0.505 20.827 1.00 73.78 O
ANISOU 855 OH TYR A 212 9688 9145 9202 -254 -1152 -149 O
ATOM 856 N LEU A 213 17.379 4.784 16.754 1.00 70.94 N
ANISOU 856 N LEU A 213 10069 7737 9148 -568 -699 -399 N
ATOM 857 CA LEU A 213 18.399 5.512 17.517 1.00 72.25 C
ANISOU 857 CA LEU A 213 10227 8022 9204 -846 -631 -538 C
ATOM 858 C LEU A 213 17.882 6.825 18.091 1.00 71.35 C
ANISOU 858 C LEU A 213 10341 7695 9076 -972 -466 -658 C
ATOM 859 O LEU A 213 18.369 7.283 19.129 1.00 70.82 O
ANISOU 859 O LEU A 213 10266 7741 8901 -1202 -417 -796 O
ATOM 860 CB LEU A 213 19.620 5.791 16.640 1.00 71.19 C
ANISOU 860 CB LEU A 213 10059 7955 9035 -988 -596 -553 C
ATOM 861 CG LEU A 213 20.969 5.734 17.365 1.00 74.37 C
ANISOU 861 CG LEU A 213 10272 8696 9289 -1235 -624 -650 C
ATOM 862 CD1 LEU A 213 21.495 4.300 17.542 1.00 72.74 C
ANISOU 862 CD1 LEU A 213 9791 8805 9042 -1085 -792 -539 C
ATOM 863 CD2 LEU A 213 21.965 6.613 16.645 1.00 74.02 C
ANISOU 863 CD2 LEU A 213 10286 8640 9200 -1470 -506 -730 C
ATOM 864 N HIS A 214 16.984 7.501 17.378 1.00 70.99 N
ANISOU 864 N HIS A 214 10508 7350 9116 -830 -357 -611 N
ATOM 865 CA HIS A 214 16.384 8.711 17.923 1.00 72.68 C
ANISOU 865 CA HIS A 214 10971 7326 9318 -890 -171 -705 C
ATOM 866 C HIS A 214 15.397 8.367 19.041 1.00 74.52 C
ANISOU 866 C HIS A 214 11164 7600 9552 -785 -217 -716 C
ATOM 867 O HIS A 214 15.255 9.134 20.006 1.00 75.30 O
ANISOU 867 O HIS A 214 11395 7625 9592 -924 -93 -843 O
ATOM 868 CB HIS A 214 15.696 9.506 16.805 1.00 72.00 C
ANISOU 868 CB HIS A 214 11123 6927 9309 -708 -30 -616 C
ATOM 869 CG HIS A 214 14.890 10.677 17.291 1.00 76.43 C
ANISOU 869 CG HIS A 214 11966 7209 9865 -674 184 -671 C
ATOM 870 ND1 HIS A 214 13.569 10.562 17.680 1.00 76.75 N
ANISOU 870 ND1 HIS A 214 12020 7194 9947 -422 175 -606 N
ATOM 871 CD2 HIS A 214 15.211 11.987 17.435 1.00 78.37 C
ANISOU 871 CD2 HIS A 214 12507 7208 10064 -856 435 -785 C
ATOM 872 CE1 HIS A 214 13.118 11.742 18.065 1.00 77.18 C
ANISOU 872 CE1 HIS A 214 12359 6986 9982 -420 407 -668 C
ATOM 873 NE2 HIS A 214 14.094 12.624 17.924 1.00 81.61 N
ANISOU 873 NE2 HIS A 214 13115 7404 10491 -685 578 -779 N
ATOM 874 N THR A 215 14.694 7.222 18.914 1.00 72.92 N
ANISOU 874 N THR A 215 10792 7507 9406 -558 -379 -592 N
ATOM 875 CA THR A 215 13.738 6.800 19.937 1.00 73.30 C
ANISOU 875 CA THR A 215 10789 7610 9453 -463 -424 -594 C
ATOM 876 C THR A 215 14.453 6.250 21.168 1.00 73.26 C
ANISOU 876 C THR A 215 10628 7863 9345 -642 -507 -676 C
ATOM 877 O THR A 215 14.103 6.604 22.302 1.00 71.14 O
ANISOU 877 O THR A 215 10407 7603 9018 -718 -453 -768 O
ATOM 878 CB THR A 215 12.760 5.770 19.363 1.00 69.65 C
ANISOU 878 CB THR A 215 10210 7185 9068 -204 -545 -450 C
ATOM 879 OG1 THR A 215 12.030 6.379 18.294 1.00 70.52 O
ANISOU 879 OG1 THR A 215 10448 7104 9240 -29 -464 -374 O
ATOM 880 CG2 THR A 215 11.738 5.347 20.430 1.00 71.54 C
ANISOU 880 CG2 THR A 215 10396 7486 9298 -126 -575 -458 C
ATOM 881 N ALA A 216 15.498 5.442 20.955 1.00 72.67 N
ANISOU 881 N ALA A 216 10371 8010 9229 -703 -626 -640 N
ATOM 882 CA ALA A 216 16.207 4.811 22.061 1.00 72.86 C
ANISOU 882 CA ALA A 216 10217 8334 9133 -820 -717 -679 C
ATOM 883 C ALA A 216 16.860 5.833 22.993 1.00 74.88 C
ANISOU 883 C ALA A 216 10529 8665 9256 -1116 -616 -861 C
ATOM 884 O ALA A 216 17.042 5.555 24.184 1.00 79.24 O
ANISOU 884 O ALA A 216 10977 9439 9693 -1205 -663 -916 O
ATOM 885 CB ALA A 216 17.254 3.841 21.517 1.00 72.79 C
ANISOU 885 CB ALA A 216 10013 8548 9096 -790 -836 -588 C
ATOM 886 N ILE A 217 17.271 6.996 22.470 1.00 74.95 N
ANISOU 886 N ILE A 217 10707 8507 9262 -1290 -468 -961 N
ATOM 887 CA ILE A 217 17.880 8.020 23.330 1.00 77.63 C
ANISOU 887 CA ILE A 217 11135 8901 9462 -1624 -338 -1165 C
ATOM 888 C ILE A 217 16.866 8.966 23.956 1.00 77.76 C
ANISOU 888 C ILE A 217 11413 8637 9496 -1637 -167 -1263 C
ATOM 889 O ILE A 217 17.270 9.928 24.626 1.00 76.07 O
ANISOU 889 O ILE A 217 11334 8401 9167 -1931 -15 -1454 O
ATOM 890 CB ILE A 217 18.902 8.975 22.677 1.00 77.05 C
ANISOU 890 CB ILE A 217 11164 8775 9339 -1898 -204 -1277 C
ATOM 891 CG1 ILE A 217 18.260 9.794 21.570 1.00 75.60 C
ANISOU 891 CG1 ILE A 217 11270 8162 9292 -1775 -40 -1230 C
ATOM 892 CG2 ILE A 217 20.138 8.227 22.208 1.00 78.39 C
ANISOU 892 CG2 ILE A 217 11058 9282 9445 -1956 -344 -1222 C
ATOM 893 CD1 ILE A 217 19.238 10.825 21.027 1.00 76.98 C
ANISOU 893 CD1 ILE A 217 11596 8247 9405 -2078 135 -1355 C
ATOM 894 N VAL A 218 15.575 8.780 23.691 1.00 75.37 N
ANISOU 894 N VAL A 218 11196 8117 9323 -1336 -164 -1146 N
ATOM 895 CA VAL A 218 14.548 9.684 24.198 1.00 75.77 C
ANISOU 895 CA VAL A 218 11495 7899 9394 -1289 16 -1215 C
ATOM 896 C VAL A 218 13.516 8.970 25.069 1.00 75.43 C
ANISOU 896 C VAL A 218 11350 7945 9365 -1106 -76 -1161 C
ATOM 897 O VAL A 218 12.992 9.579 26.010 1.00 77.57 O
ANISOU 897 O VAL A 218 11757 8130 9585 -1164 47 -1270 O
ATOM 898 CB VAL A 218 13.852 10.424 23.036 1.00 75.24 C
ANISOU 898 CB VAL A 218 11665 7472 9450 -1082 164 -1127 C
ATOM 899 CG1 VAL A 218 12.583 11.121 23.527 1.00 77.78 C
ANISOU 899 CG1 VAL A 218 12201 7551 9802 -916 329 -1140 C
ATOM 900 CG2 VAL A 218 14.787 11.431 22.368 1.00 76.05 C
ANISOU 900 CG2 VAL A 218 11963 7412 9519 -1306 334 -1214 C
ATOM 901 N LEU A 219 13.211 7.703 24.791 1.00 76.58 N
ANISOU 901 N LEU A 219 11277 8248 9570 -902 -269 -1006 N
ATOM 902 CA LEU A 219 12.251 6.937 25.569 1.00 74.26 C
ANISOU 902 CA LEU A 219 10885 8045 9284 -750 -349 -952 C
ATOM 903 C LEU A 219 12.955 5.724 26.153 1.00 74.10 C
ANISOU 903 C LEU A 219 10621 8352 9182 -805 -529 -911 C
ATOM 904 O LEU A 219 13.638 4.984 25.431 1.00 73.53 O
ANISOU 904 O LEU A 219 10416 8393 9128 -767 -640 -817 O
ATOM 905 CB LEU A 219 11.037 6.517 24.733 1.00 71.68 C
ANISOU 905 CB LEU A 219 10552 7592 9090 -448 -378 -802 C
ATOM 906 CG LEU A 219 10.330 7.622 23.940 1.00 73.05 C
ANISOU 906 CG LEU A 219 10942 7476 9338 -310 -211 -786 C
ATOM 907 CD1 LEU A 219 9.184 7.080 23.080 1.00 72.07 C
ANISOU 907 CD1 LEU A 219 10742 7332 9309 -16 -273 -630 C
ATOM 908 CD2 LEU A 219 9.841 8.726 24.844 1.00 75.95 C
ANISOU 908 CD2 LEU A 219 11517 7681 9657 -358 -14 -908 C
ATOM 909 N THR A 220 12.789 5.531 27.459 1.00 72.57 N
ANISOU 909 N THR A 220 10380 8307 8886 -877 -543 -972 N
ATOM 910 CA THR A 220 13.409 4.403 28.120 1.00 70.94 C
ANISOU 910 CA THR A 220 9958 8417 8576 -894 -694 -913 C
ATOM 911 C THR A 220 12.824 3.144 27.531 1.00 68.11 C
ANISOU 911 C THR A 220 9506 8048 8323 -644 -800 -732 C
ATOM 912 O THR A 220 11.607 2.978 27.429 1.00 68.82 O
ANISOU 912 O THR A 220 9652 7990 8505 -493 -774 -686 O
ATOM 913 CB THR A 220 13.216 4.422 29.643 1.00 72.02 C
ANISOU 913 CB THR A 220 10075 8715 8574 -996 -681 -1000 C
ATOM 914 OG1 THR A 220 11.867 4.791 29.980 1.00 75.29 O
ANISOU 914 OG1 THR A 220 10628 8919 9060 -891 -583 -1024 O
ATOM 915 CG2 THR A 220 14.197 5.401 30.276 1.00 70.63 C
ANISOU 915 CG2 THR A 220 9931 8671 8235 -1310 -607 -1190 C
ATOM 916 N ASP A 224 10.767 -6.955 23.050 1.00 65.56 N
ANISOU 916 N ASP A 224 9082 7468 8359 316 -1015 183 N
ATOM 917 CA ASP A 224 11.366 -6.503 21.796 1.00 65.91 C
ANISOU 917 CA ASP A 224 9105 7477 8461 326 -1049 172 C
ATOM 918 C ASP A 224 10.655 -7.153 20.567 1.00 65.92 C
ANISOU 918 C ASP A 224 9170 7350 8528 319 -1014 168 C
ATOM 919 O ASP A 224 10.464 -6.503 19.525 1.00 62.20 O
ANISOU 919 O ASP A 224 8676 6844 8112 299 -1042 124 O
ATOM 920 CB ASP A 224 12.878 -6.781 21.783 1.00 64.39 C
ANISOU 920 CB ASP A 224 8872 7385 8209 401 -1067 251 C
ATOM 921 CG ASP A 224 13.686 -5.788 22.635 1.00 64.09 C
ANISOU 921 CG ASP A 224 8730 7525 8096 350 -1118 213 C
ATOM 922 OD1 ASP A 224 14.825 -6.141 23.035 1.00 68.66 O
ANISOU 922 OD1 ASP A 224 9237 8273 8578 413 -1135 287 O
ATOM 923 OD2 ASP A 224 13.224 -4.651 22.903 1.00 63.98 O1-
ANISOU 923 OD2 ASP A 224 8707 7500 8104 246 -1130 108 O1-
ATOM 924 N ARG A 225 10.235 -8.421 20.714 1.00 66.06 N
ANISOU 924 N ARG A 225 9276 7302 8521 323 -940 209 N
ATOM 925 CA ARG A 225 9.641 -9.146 19.591 1.00 64.46 C
ANISOU 925 CA ARG A 225 9144 6995 8350 275 -889 185 C
ATOM 926 C ARG A 225 8.373 -8.462 19.075 1.00 65.20 C
ANISOU 926 C ARG A 225 9169 7122 8481 182 -923 88 C
ATOM 927 O ARG A 225 7.978 -8.692 17.932 1.00 68.33 O
ANISOU 927 O ARG A 225 9574 7496 8894 135 -915 53 O
ATOM 928 CB ARG A 225 9.373 -10.606 19.984 1.00 62.87 C
ANISOU 928 CB ARG A 225 9089 6697 8102 262 -766 230 C
ATOM 929 N LEU A 226 7.713 -7.628 19.889 1.00 66.57 N
ANISOU 929 N LEU A 226 9269 7371 8654 167 -953 46 N
ATOM 930 CA LEU A 226 6.492 -6.962 19.421 1.00 67.43 C
ANISOU 930 CA LEU A 226 9296 7544 8781 127 -974 -24 C
ATOM 931 C LEU A 226 6.779 -5.628 18.712 1.00 65.74 C
ANISOU 931 C LEU A 226 9028 7343 8609 201 -1033 -31 C
ATOM 932 O LEU A 226 6.131 -5.295 17.713 1.00 64.99 O
ANISOU 932 O LEU A 226 8883 7290 8521 212 -1050 -51 O
ATOM 933 CB LEU A 226 5.527 -6.757 20.596 1.00 65.35 C
ANISOU 933 CB LEU A 226 8991 7351 8490 96 -949 -60 C
ATOM 934 CG LEU A 226 4.532 -7.896 20.905 1.00 68.03 C
ANISOU 934 CG LEU A 226 9353 7713 8782 -21 -874 -88 C
ATOM 935 CD1 LEU A 226 3.661 -7.629 22.155 1.00 69.15 C
ANISOU 935 CD1 LEU A 226 9447 7936 8892 -47 -845 -119 C
ATOM 936 CD2 LEU A 226 3.649 -8.228 19.718 1.00 71.46 C
ANISOU 936 CD2 LEU A 226 9734 8215 9203 -109 -867 -143 C
ATOM 937 N ARG A 227 7.723 -4.839 19.223 1.00 65.12 N
ANISOU 937 N ARG A 227 8961 7241 8540 243 -1053 -17 N
ATOM 938 CA ARG A 227 7.963 -3.517 18.658 1.00 66.35 C
ANISOU 938 CA ARG A 227 9108 7374 8729 290 -1071 -32 C
ATOM 939 C ARG A 227 8.569 -3.619 17.274 1.00 66.40 C
ANISOU 939 C ARG A 227 9128 7340 8759 312 -1093 0 C
ATOM 940 O ARG A 227 8.419 -2.705 16.449 1.00 64.85 O
ANISOU 940 O ARG A 227 8933 7124 8584 360 -1096 0 O
ATOM 941 CB ARG A 227 8.890 -2.732 19.576 1.00 65.12 C
ANISOU 941 CB ARG A 227 8976 7210 8558 271 -1066 -50 C
ATOM 942 CG ARG A 227 8.389 -2.690 20.976 1.00 62.62 C
ANISOU 942 CG ARG A 227 8652 6940 8202 242 -1042 -85 C
ATOM 943 CD ARG A 227 8.730 -1.395 21.639 1.00 65.51 C
ANISOU 943 CD ARG A 227 9051 7289 8552 214 -1012 -146 C
ATOM 944 NE ARG A 227 10.122 -1.298 22.059 1.00 66.01 N
ANISOU 944 NE ARG A 227 9111 7405 8566 142 -1032 -153 N
ATOM 945 CZ ARG A 227 10.903 -0.263 21.792 1.00 63.40 C
ANISOU 945 CZ ARG A 227 8817 7041 8232 83 -1009 -199 C
ATOM 946 NH1 ARG A 227 10.482 0.735 21.028 1.00 66.27 N
ANISOU 946 NH1 ARG A 227 9256 7276 8649 116 -955 -223 N
ATOM 947 NH2 ARG A 227 12.132 -0.227 22.310 1.00 60.45 N
ANISOU 947 NH2 ARG A 227 8403 6782 7784 -11 -1030 -219 N
ATOM 948 N ALA A 228 9.191 -4.758 16.977 1.00 65.74 N
ANISOU 948 N ALA A 228 9072 7240 8664 290 -1092 34 N
ATOM 949 CA ALA A 228 9.902 -4.939 15.688 1.00 64.94 C
ANISOU 949 CA ALA A 228 8992 7102 8579 309 -1103 62 C
ATOM 950 C ALA A 228 8.957 -4.926 14.491 1.00 66.04 C
ANISOU 950 C ALA A 228 9111 7264 8718 306 -1111 43 C
ATOM 951 O ALA A 228 9.420 -4.620 13.390 1.00 64.60 O
ANISOU 951 O ALA A 228 8938 7062 8545 334 -1126 61 O
ATOM 952 CB ALA A 228 10.647 -6.240 15.725 1.00 63.63 C
ANISOU 952 CB ALA A 228 8878 6906 8392 311 -1071 106 C
ATOM 953 N TRP A 229 7.690 -5.256 14.694 1.00 69.83 N
ANISOU 953 N TRP A 229 9549 7815 9170 267 -1102 6 N
ATOM 954 CA TRP A 229 6.763 -5.371 13.544 1.00 69.97 C
ANISOU 954 CA TRP A 229 9510 7927 9149 246 -1116 -18 C
ATOM 955 C TRP A 229 6.633 -4.028 12.827 1.00 69.38 C
ANISOU 955 C TRP A 229 9392 7889 9080 362 -1149 14 C
ATOM 956 O TRP A 229 6.514 -4.042 11.605 1.00 69.30 O
ANISOU 956 O TRP A 229 9360 7935 9038 375 -1169 25 O
ATOM 957 CB TRP A 229 5.417 -5.953 13.981 1.00 71.87 C
ANISOU 957 CB TRP A 229 9682 8289 9336 159 -1095 -73 C
ATOM 958 CG TRP A 229 5.515 -7.393 14.377 1.00 76.56 C
ANISOU 958 CG TRP A 229 10364 8816 9909 28 -1030 -103 C
ATOM 959 CD1 TRP A 229 5.520 -7.898 15.643 1.00 79.80 C
ANISOU 959 CD1 TRP A 229 10826 9170 10322 -5 -981 -100 C
ATOM 960 CD2 TRP A 229 5.647 -8.523 13.496 1.00 80.98 C
ANISOU 960 CD2 TRP A 229 11003 9335 10431 -82 -979 -136 C
ATOM 961 NE1 TRP A 229 5.636 -9.261 15.612 1.00 83.23 N
ANISOU 961 NE1 TRP A 229 11380 9516 10725 -112 -893 -115 N
ATOM 962 CE2 TRP A 229 5.716 -9.673 14.309 1.00 82.86 C
ANISOU 962 CE2 TRP A 229 11362 9466 10655 -168 -883 -145 C
ATOM 963 CE3 TRP A 229 5.707 -8.677 12.107 1.00 83.04 C
ANISOU 963 CE3 TRP A 229 11260 9633 10657 -117 -992 -159 C
ATOM 964 CZ2 TRP A 229 5.842 -10.954 13.776 1.00 84.60 C
ANISOU 964 CZ2 TRP A 229 11725 9585 10835 -288 -778 -181 C
ATOM 965 CZ3 TRP A 229 5.833 -9.943 11.581 1.00 81.89 C
ANISOU 965 CZ3 TRP A 229 11236 9409 10468 -253 -903 -209 C
ATOM 966 CH2 TRP A 229 5.899 -11.065 12.406 1.00 82.61 C
ANISOU 966 CH2 TRP A 229 11471 9364 10552 -337 -787 -222 C
ATOM 967 N MET A 230 6.686 -2.921 13.563 1.00 66.76 N
ANISOU 967 N MET A 230 9072 7515 8780 442 -1136 29 N
ATOM 968 CA MET A 230 6.545 -1.580 12.943 1.00 68.11 C
ANISOU 968 CA MET A 230 9252 7674 8951 573 -1126 72 C
ATOM 969 C MET A 230 7.758 -1.345 12.051 1.00 65.19 C
ANISOU 969 C MET A 230 8960 7203 8607 572 -1127 104 C
ATOM 970 O MET A 230 7.587 -0.794 10.964 1.00 61.82 O
ANISOU 970 O MET A 230 8535 6798 8155 657 -1127 150 O
ATOM 971 CB MET A 230 6.477 -0.483 14.007 1.00 68.16 C
ANISOU 971 CB MET A 230 9308 7605 8984 633 -1072 65 C
ATOM 972 CG MET A 230 5.796 0.780 13.527 1.00 73.05 C
ANISOU 972 CG MET A 230 9946 8227 9583 805 -1022 116 C
ATOM 973 SD MET A 230 6.610 2.273 14.139 1.00 79.20 S
ANISOU 973 SD MET A 230 10908 8779 10404 836 -911 107 S
ATOM 974 CE MET A 230 5.527 3.534 13.469 1.00 72.76 C
ANISOU 974 CE MET A 230 10133 7965 9546 1098 -821 199 C
ATOM 975 N PHE A 231 8.934 -1.758 12.509 1.00 62.42 N
ANISOU 975 N PHE A 231 8657 6769 8289 491 -1125 90 N
ATOM 976 CA PHE A 231 10.166 -1.643 11.691 1.00 62.49 C
ANISOU 976 CA PHE A 231 8718 6712 8315 477 -1123 116 C
ATOM 977 C PHE A 231 10.074 -2.545 10.457 1.00 61.59 C
ANISOU 977 C PHE A 231 8583 6646 8171 468 -1148 130 C
ATOM 978 O PHE A 231 10.538 -2.129 9.391 1.00 59.86 O
ANISOU 978 O PHE A 231 8394 6404 7946 500 -1145 163 O
ATOM 979 CB PHE A 231 11.385 -1.946 12.558 1.00 61.46 C
ANISOU 979 CB PHE A 231 8602 6552 8200 406 -1117 102 C
ATOM 980 CG PHE A 231 11.682 -0.895 13.596 1.00 64.26 C
ANISOU 980 CG PHE A 231 8984 6873 8559 375 -1083 68 C
ATOM 981 CD1 PHE A 231 11.200 -1.017 14.888 1.00 66.84 C
ANISOU 981 CD1 PHE A 231 9289 7234 8874 352 -1081 34 C
ATOM 982 CD2 PHE A 231 12.441 0.218 13.278 1.00 61.60 C
ANISOU 982 CD2 PHE A 231 8710 6467 8228 347 -1037 60 C
ATOM 983 CE1 PHE A 231 11.473 -0.050 15.841 1.00 64.33 C
ANISOU 983 CE1 PHE A 231 9008 6888 8545 302 -1039 -16 C
ATOM 984 CE2 PHE A 231 12.713 1.184 14.232 1.00 65.63 C
ANISOU 984 CE2 PHE A 231 9271 6938 8728 277 -982 3 C
ATOM 985 CZ PHE A 231 12.229 1.049 15.511 1.00 65.15 C
ANISOU 985 CZ PHE A 231 9185 6919 8650 254 -985 -38 C
ATOM 986 N ILE A 232 9.519 -3.748 10.610 1.00 63.20 N
ANISOU 986 N ILE A 232 8758 6906 8349 408 -1157 99 N
ATOM 987 CA ILE A 232 9.352 -4.691 9.465 1.00 61.28 C
ANISOU 987 CA ILE A 232 8517 6705 8060 358 -1158 84 C
ATOM 988 C ILE A 232 8.255 -4.139 8.558 1.00 62.23 C
ANISOU 988 C ILE A 232 8562 6965 8118 400 -1191 87 C
ATOM 989 O ILE A 232 8.338 -4.340 7.342 1.00 62.47 O
ANISOU 989 O ILE A 232 8594 7043 8100 390 -1201 91 O
ATOM 990 CB ILE A 232 9.027 -6.113 9.966 1.00 61.39 C
ANISOU 990 CB ILE A 232 8559 6714 8052 254 -1120 36 C
ATOM 991 CG1 ILE A 232 10.202 -6.720 10.735 1.00 59.48 C
ANISOU 991 CG1 ILE A 232 8395 6355 7848 266 -1078 67 C
ATOM 992 CG2 ILE A 232 8.576 -7.021 8.835 1.00 60.99 C
ANISOU 992 CG2 ILE A 232 8524 6716 7932 160 -1099 -14 C
ATOM 993 CD1 ILE A 232 10.204 -8.228 10.745 1.00 63.48 C
ANISOU 993 CD1 ILE A 232 8998 6798 8324 197 -998 46 C
ATOM 994 N CYS A 233 7.298 -3.416 9.136 1.00 62.98 N
ANISOU 994 N CYS A 233 8590 7140 8202 464 -1201 94 N
ATOM 995 CA CYS A 233 6.255 -2.837 8.299 1.00 65.81 C
ANISOU 995 CA CYS A 233 8852 7676 8478 554 -1229 124 C
ATOM 996 C CYS A 233 6.814 -1.700 7.447 1.00 63.56 C
ANISOU 996 C CYS A 233 8627 7324 8197 693 -1218 209 C
ATOM 997 O CYS A 233 6.322 -1.443 6.336 1.00 64.40 O
ANISOU 997 O CYS A 233 8678 7572 8217 768 -1241 253 O
ATOM 998 CB CYS A 233 5.088 -2.389 9.197 1.00 64.76 C
ANISOU 998 CB CYS A 233 8626 7656 8324 617 -1225 121 C
ATOM 999 SG CYS A 233 3.645 -1.632 8.432 1.00 74.86 S
ANISOU 999 SG CYS A 233 9742 9225 9476 786 -1250 181 S
ATOM 1000 N ILE A 234 7.836 -1.013 7.949 1.00 59.43 N
ANISOU 1000 N ILE A 234 8217 6605 7758 715 -1175 230 N
ATOM 1001 CA ILE A 234 8.413 0.097 7.210 1.00 61.91 C
ANISOU 1001 CA ILE A 234 8622 6824 8077 817 -1133 302 C
ATOM 1002 C ILE A 234 9.451 -0.414 6.211 1.00 61.16 C
ANISOU 1002 C ILE A 234 8567 6689 7981 744 -1145 304 C
ATOM 1003 O ILE A 234 9.488 0.023 5.049 1.00 58.44 O
ANISOU 1003 O ILE A 234 8245 6374 7584 818 -1138 364 O
ATOM 1004 CB ILE A 234 9.019 1.121 8.192 1.00 61.89 C
ANISOU 1004 CB ILE A 234 8732 6639 8145 829 -1058 300 C
ATOM 1005 CG1 ILE A 234 7.928 1.737 9.063 1.00 61.90 C
ANISOU 1005 CG1 ILE A 234 8714 6669 8136 931 -1025 305 C
ATOM 1006 CG2 ILE A 234 9.791 2.210 7.427 1.00 61.34 C
ANISOU 1006 CG2 ILE A 234 8796 6431 8079 883 -983 359 C
ATOM 1007 CD1 ILE A 234 8.253 3.139 9.531 1.00 63.94 C
ANISOU 1007 CD1 ILE A 234 9130 6739 8426 998 -908 326 C
ATOM 1008 N GLY A 235 10.298 -1.349 6.664 1.00 59.85 N
ANISOU 1008 N GLY A 235 8413 6467 7862 619 -1152 248 N
ATOM 1009 CA GLY A 235 11.409 -1.806 5.855 1.00 57.64 C
ANISOU 1009 CA GLY A 235 8175 6141 7586 569 -1143 253 C
ATOM 1010 C GLY A 235 10.970 -2.581 4.628 1.00 58.51 C
ANISOU 1010 C GLY A 235 8253 6359 7618 550 -1170 244 C
ATOM 1011 O GLY A 235 11.437 -2.303 3.522 1.00 57.74 O
ANISOU 1011 O GLY A 235 8191 6260 7489 578 -1159 281 O
ATOM 1012 N TRP A 236 10.082 -3.571 4.806 1.00 57.84 N
ANISOU 1012 N TRP A 236 8111 6376 7490 480 -1193 184 N
ATOM 1013 CA TRP A 236 9.625 -4.430 3.716 1.00 57.61 C
ANISOU 1013 CA TRP A 236 8057 6467 7365 405 -1204 141 C
ATOM 1014 C TRP A 236 8.253 -4.060 3.172 1.00 62.66 C
ANISOU 1014 C TRP A 236 8577 7340 7891 441 -1254 146 C
ATOM 1015 O TRP A 236 7.917 -4.449 2.045 1.00 63.06 O
ANISOU 1015 O TRP A 236 8590 7540 7830 391 -1273 122 O
ATOM 1016 CB TRP A 236 9.566 -5.903 4.143 1.00 57.62 C
ANISOU 1016 CB TRP A 236 8095 6436 7363 258 -1164 51 C
ATOM 1017 CG TRP A 236 10.844 -6.467 4.633 1.00 57.56 C
ANISOU 1017 CG TRP A 236 8190 6244 7435 256 -1106 62 C
ATOM 1018 CD1 TRP A 236 11.186 -6.733 5.931 1.00 57.91 C
ANISOU 1018 CD1 TRP A 236 8258 6198 7546 265 -1081 70 C
ATOM 1019 CD2 TRP A 236 11.984 -6.826 3.834 1.00 58.79 C
ANISOU 1019 CD2 TRP A 236 8425 6318 7596 269 -1061 78 C
ATOM 1020 NE1 TRP A 236 12.468 -7.251 5.987 1.00 55.34 N
ANISOU 1020 NE1 TRP A 236 8008 5763 7256 298 -1027 100 N
ATOM 1021 CE2 TRP A 236 12.980 -7.309 4.718 1.00 56.23 C
ANISOU 1021 CE2 TRP A 236 8153 5873 7337 302 -1010 104 C
ATOM 1022 CE3 TRP A 236 12.261 -6.783 2.450 1.00 58.06 C
ANISOU 1022 CE3 TRP A 236 8354 6262 7445 265 -1055 79 C
ATOM 1023 CZ2 TRP A 236 14.227 -7.745 4.272 1.00 55.67 C
ANISOU 1023 CZ2 TRP A 236 8144 5731 7278 346 -951 135 C
ATOM 1024 CZ3 TRP A 236 13.498 -7.206 2.007 1.00 54.70 C
ANISOU 1024 CZ3 TRP A 236 8006 5737 7042 289 -993 98 C
ATOM 1025 CH2 TRP A 236 14.467 -7.685 2.917 1.00 55.95 C
ANISOU 1025 CH2 TRP A 236 8203 5786 7267 336 -939 128 C
ATOM 1026 N GLY A 237 7.446 -3.347 3.952 1.00 63.72 N
ANISOU 1026 N GLY A 237 8640 7538 8034 530 -1272 177 N
ATOM 1027 CA GLY A 237 6.040 -3.194 3.665 1.00 64.32 C
ANISOU 1027 CA GLY A 237 8563 7889 7987 568 -1316 179 C
ATOM 1028 C GLY A 237 5.682 -1.964 2.879 1.00 64.87 C
ANISOU 1028 C GLY A 237 8591 8073 7983 783 -1332 300 C
ATOM 1029 O GLY A 237 4.977 -2.044 1.862 1.00 66.79 O
ANISOU 1029 O GLY A 237 8719 8581 8076 806 -1376 315 O
ATOM 1030 N VAL A 238 6.103 -0.797 3.370 1.00 64.85 N
ANISOU 1030 N VAL A 238 8687 7888 8067 943 -1283 388 N
ATOM 1031 CA VAL A 238 5.819 0.452 2.653 1.00 64.49 C
ANISOU 1031 CA VAL A 238 8658 7893 7953 1180 -1257 525 C
ATOM 1032 C VAL A 238 6.386 0.391 1.235 1.00 64.59 C
ANISOU 1032 C VAL A 238 8710 7938 7894 1178 -1269 566 C
ATOM 1033 O VAL A 238 5.701 0.851 0.289 1.00 65.51 O
ANISOU 1033 O VAL A 238 8749 8275 7865 1335 -1290 660 O
ATOM 1034 CB VAL A 238 6.279 1.659 3.473 1.00 64.03 C
ANISOU 1034 CB VAL A 238 8756 7571 8003 1306 -1161 588 C
ATOM 1035 CG1 VAL A 238 6.201 2.973 2.702 1.00 62.71 C
ANISOU 1035 CG1 VAL A 238 8686 7366 7775 1553 -1085 741 C
ATOM 1036 CG2 VAL A 238 5.453 1.784 4.758 1.00 62.92 C
ANISOU 1036 CG2 VAL A 238 8553 7461 7894 1341 -1149 557 C
ATOM 1037 N PRO A 239 7.590 -0.152 1.002 1.00 63.64 N
ANISOU 1037 N PRO A 239 8694 7637 7848 1027 -1253 509 N
ATOM 1038 CA PRO A 239 8.098 -0.243 -0.379 1.00 65.53 C
ANISOU 1038 CA PRO A 239 8968 7921 8009 1022 -1258 542 C
ATOM 1039 C PRO A 239 7.192 -0.989 -1.357 1.00 65.92 C
ANISOU 1039 C PRO A 239 8866 8300 7881 970 -1332 505 C
ATOM 1040 O PRO A 239 7.175 -0.632 -2.546 1.00 66.48 O
ANISOU 1040 O PRO A 239 8931 8497 7833 1058 -1341 581 O
ATOM 1041 CB PRO A 239 9.428 -0.980 -0.194 1.00 62.80 C
ANISOU 1041 CB PRO A 239 8725 7362 7776 850 -1228 460 C
ATOM 1042 CG PRO A 239 9.845 -0.603 1.173 1.00 61.43 C
ANISOU 1042 CG PRO A 239 8609 6992 7739 844 -1188 446 C
ATOM 1043 CD PRO A 239 8.586 -0.670 1.970 1.00 62.23 C
ANISOU 1043 CD PRO A 239 8602 7229 7815 878 -1224 426 C
ATOM 1044 N PHE A 240 6.488 -2.029 -0.918 1.00 63.23 N
ANISOU 1044 N PHE A 240 8411 8107 7506 807 -1374 384 N
ATOM 1045 CA PHE A 240 5.797 -2.887 -1.877 1.00 66.20 C
ANISOU 1045 CA PHE A 240 8662 8789 7703 673 -1426 305 C
ATOM 1046 C PHE A 240 4.753 -2.118 -2.678 1.00 68.38 C
ANISOU 1046 C PHE A 240 8773 9423 7785 859 -1483 414 C
ATOM 1047 O PHE A 240 4.715 -2.268 -3.913 1.00 70.65 O
ANISOU 1047 O PHE A 240 9019 9908 7918 840 -1514 423 O
ATOM 1048 CB PHE A 240 5.188 -4.086 -1.143 1.00 67.55 C
ANISOU 1048 CB PHE A 240 8765 9033 7869 438 -1430 146 C
ATOM 1049 CG PHE A 240 4.678 -5.160 -2.064 1.00 68.58 C
ANISOU 1049 CG PHE A 240 8817 9419 7822 209 -1448 14 C
ATOM 1050 CD1 PHE A 240 5.535 -6.126 -2.577 1.00 69.00 C
ANISOU 1050 CD1 PHE A 240 9022 9302 7894 25 -1387 -86 C
ATOM 1051 CD2 PHE A 240 3.335 -5.172 -2.455 1.00 69.81 C
ANISOU 1051 CD2 PHE A 240 8741 10012 7771 177 -1516 -12 C
ATOM 1052 CE1 PHE A 240 5.053 -7.110 -3.454 1.00 71.87 C
ANISOU 1052 CE1 PHE A 240 9342 9887 8077 -216 -1378 -230 C
ATOM 1053 CE2 PHE A 240 2.835 -6.144 -3.326 1.00 70.19 C
ANISOU 1053 CE2 PHE A 240 8707 10336 7625 -81 -1526 -159 C
ATOM 1054 CZ PHE A 240 3.691 -7.120 -3.829 1.00 70.79 C
ANISOU 1054 CZ PHE A 240 8971 10201 7726 -293 -1451 -277 C
ATOM 1055 N PRO A 241 3.894 -1.293 -2.067 1.00 70.00 N
ANISOU 1055 N PRO A 241 8878 9745 7973 1060 -1493 508 N
ATOM 1056 CA PRO A 241 2.920 -0.506 -2.855 1.00 68.99 C
ANISOU 1056 CA PRO A 241 8587 9985 7641 1303 -1536 649 C
ATOM 1057 C PRO A 241 3.559 0.570 -3.718 1.00 67.88 C
ANISOU 1057 C PRO A 241 8590 9720 7483 1547 -1487 826 C
ATOM 1058 O PRO A 241 2.929 1.025 -4.684 1.00 68.68 O
ANISOU 1058 O PRO A 241 8573 10144 7380 1732 -1522 946 O
ATOM 1059 CB PRO A 241 2.026 0.123 -1.769 1.00 69.76 C
ANISOU 1059 CB PRO A 241 8591 10147 7767 1482 -1521 710 C
ATOM 1060 CG PRO A 241 2.268 -0.707 -0.555 1.00 67.05 C
ANISOU 1060 CG PRO A 241 8297 9590 7590 1236 -1505 550 C
ATOM 1061 CD PRO A 241 3.708 -1.089 -0.622 1.00 67.27 C
ANISOU 1061 CD PRO A 241 8552 9235 7772 1086 -1461 493 C
ATOM 1062 N ILE A 242 4.748 1.055 -3.336 1.00 66.46 N
ANISOU 1062 N ILE A 242 8654 9100 7497 1563 -1398 855 N
ATOM 1063 CA ILE A 242 5.456 2.048 -4.143 1.00 69.32 C
ANISOU 1063 CA ILE A 242 9186 9303 7848 1748 -1324 1007 C
ATOM 1064 C ILE A 242 5.949 1.422 -5.451 1.00 68.49 C
ANISOU 1064 C ILE A 242 9077 9312 7634 1618 -1364 970 C
ATOM 1065 O ILE A 242 5.743 1.970 -6.539 1.00 67.91 O
ANISOU 1065 O ILE A 242 8989 9418 7397 1792 -1365 1103 O
ATOM 1066 CB ILE A 242 6.618 2.663 -3.330 1.00 68.71 C
ANISOU 1066 CB ILE A 242 9356 8756 7995 1732 -1210 1012 C
ATOM 1067 CG1 ILE A 242 6.101 3.543 -2.180 1.00 66.71 C
ANISOU 1067 CG1 ILE A 242 9144 8384 7817 1902 -1141 1072 C
ATOM 1068 CG2 ILE A 242 7.660 3.349 -4.282 1.00 66.80 C
ANISOU 1068 CG2 ILE A 242 9310 8319 7752 1794 -1124 1111 C
ATOM 1069 CD1 ILE A 242 7.180 3.975 -1.186 1.00 62.83 C
ANISOU 1069 CD1 ILE A 242 8864 7478 7530 1806 -1039 1023 C
ATOM 1070 N ILE A 243 6.582 0.249 -5.363 1.00 68.27 N
ANISOU 1070 N ILE A 243 9069 9189 7682 1324 -1386 794 N
ATOM 1071 CA ILE A 243 7.016 -0.445 -6.566 1.00 68.95 C
ANISOU 1071 CA ILE A 243 9160 9380 7660 1183 -1409 735 C
ATOM 1072 C ILE A 243 5.818 -0.806 -7.422 1.00 70.66 C
ANISOU 1072 C ILE A 243 9153 10082 7612 1178 -1502 723 C
ATOM 1073 O ILE A 243 5.886 -0.754 -8.654 1.00 71.78 O
ANISOU 1073 O ILE A 243 9278 10408 7588 1206 -1521 769 O
ATOM 1074 CB ILE A 243 7.850 -1.685 -6.207 1.00 67.34 C
ANISOU 1074 CB ILE A 243 9035 8970 7582 896 -1386 551 C
ATOM 1075 CG1 ILE A 243 9.198 -1.219 -5.690 1.00 65.35 C
ANISOU 1075 CG1 ILE A 243 8976 8318 7536 923 -1300 589 C
ATOM 1076 CG2 ILE A 243 8.055 -2.576 -7.422 1.00 66.54 C
ANISOU 1076 CG2 ILE A 243 8926 9018 7339 727 -1399 458 C
ATOM 1077 CD1 ILE A 243 9.853 -0.273 -6.629 1.00 65.80 C
ANISOU 1077 CD1 ILE A 243 9142 8302 7555 1066 -1248 724 C
ATOM 1078 N VAL A 244 4.711 -1.201 -6.789 1.00 70.44 N
ANISOU 1078 N VAL A 244 8938 10302 7525 1123 -1561 653 N
ATOM 1079 CA VAL A 244 3.513 -1.571 -7.540 1.00 71.56 C
ANISOU 1079 CA VAL A 244 8823 10979 7388 1083 -1654 623 C
ATOM 1080 C VAL A 244 2.985 -0.378 -8.314 1.00 74.19 C
ANISOU 1080 C VAL A 244 9068 11582 7540 1441 -1676 856 C
ATOM 1081 O VAL A 244 2.555 -0.503 -9.469 1.00 75.85 O
ANISOU 1081 O VAL A 244 9138 12185 7498 1447 -1738 879 O
ATOM 1082 CB VAL A 244 2.424 -2.122 -6.607 1.00 71.42 C
ANISOU 1082 CB VAL A 244 8611 11182 7344 958 -1698 510 C
ATOM 1083 CG1 VAL A 244 1.118 -2.249 -7.373 1.00 72.04 C
ANISOU 1083 CG1 VAL A 244 8379 11891 7104 960 -1795 508 C
ATOM 1084 CG2 VAL A 244 2.838 -3.446 -6.001 1.00 72.17 C
ANISOU 1084 CG2 VAL A 244 8800 11056 7566 591 -1660 280 C
ATOM 1085 N ALA A 245 2.943 0.788 -7.665 1.00 72.19 N
ANISOU 1085 N ALA A 245 8895 11141 7393 1752 -1615 1034 N
ATOM 1086 CA ALA A 245 2.461 1.981 -8.351 1.00 73.43 C
ANISOU 1086 CA ALA A 245 9016 11504 7381 2144 -1598 1286 C
ATOM 1087 C ALA A 245 3.409 2.374 -9.476 1.00 72.54 C
ANISOU 1087 C ALA A 245 9092 11237 7233 2208 -1547 1384 C
ATOM 1088 O ALA A 245 2.971 2.779 -10.559 1.00 75.00 O
ANISOU 1088 O ALA A 245 9309 11886 7300 2405 -1577 1530 O
ATOM 1089 CB ALA A 245 2.280 3.120 -7.347 1.00 71.78 C
ANISOU 1089 CB ALA A 245 8916 11050 7309 2448 -1499 1440 C
ATOM 1090 N TRP A 246 4.715 2.260 -9.230 1.00 72.85 N
ANISOU 1090 N TRP A 246 9385 10794 7500 2048 -1467 1310 N
ATOM 1091 CA TRP A 246 5.701 2.430 -10.286 1.00 72.96 C
ANISOU 1091 CA TRP A 246 9566 10666 7489 2035 -1417 1361 C
ATOM 1092 C TRP A 246 5.405 1.512 -11.462 1.00 75.00 C
ANISOU 1092 C TRP A 246 9660 11325 7512 1862 -1517 1266 C
ATOM 1093 O TRP A 246 5.452 1.934 -12.619 1.00 77.49 O
ANISOU 1093 O TRP A 246 9985 11814 7643 2004 -1515 1395 O
ATOM 1094 CB TRP A 246 7.093 2.147 -9.728 1.00 70.83 C
ANISOU 1094 CB TRP A 246 9523 9902 7488 1820 -1335 1244 C
ATOM 1095 CG TRP A 246 8.208 2.157 -10.766 1.00 76.13 C
ANISOU 1095 CG TRP A 246 10352 10427 8146 1756 -1279 1261 C
ATOM 1096 CD1 TRP A 246 8.806 3.269 -11.329 1.00 74.51 C
ANISOU 1096 CD1 TRP A 246 10338 10039 7934 1954 -1169 1442 C
ATOM 1097 CD2 TRP A 246 8.900 1.005 -11.326 1.00 76.84 C
ANISOU 1097 CD2 TRP A 246 10447 10515 8234 1471 -1304 1088 C
ATOM 1098 NE1 TRP A 246 9.808 2.879 -12.201 1.00 74.17 N
ANISOU 1098 NE1 TRP A 246 10389 9909 7882 1803 -1140 1391 N
ATOM 1099 CE2 TRP A 246 9.892 1.508 -12.217 1.00 75.42 C
ANISOU 1099 CE2 TRP A 246 10437 10174 8044 1521 -1220 1178 C
ATOM 1100 CE3 TRP A 246 8.789 -0.394 -11.149 1.00 73.31 C
ANISOU 1100 CE3 TRP A 246 9903 10162 7790 1182 -1364 867 C
ATOM 1101 CZ2 TRP A 246 10.753 0.664 -12.928 1.00 75.21 C
ANISOU 1101 CZ2 TRP A 246 10462 10104 8011 1309 -1206 1057 C
ATOM 1102 CZ3 TRP A 246 9.642 -1.224 -11.855 1.00 71.69 C
ANISOU 1102 CZ3 TRP A 246 9778 9884 7578 981 -1333 751 C
ATOM 1103 CH2 TRP A 246 10.612 -0.690 -12.738 1.00 74.40 C
ANISOU 1103 CH2 TRP A 246 10268 10090 7912 1054 -1260 847 C
ATOM 1104 N ALA A 247 5.083 0.255 -11.184 1.00 77.07 N
ANISOU 1104 N ALA A 247 9784 11736 7762 1547 -1591 1038 N
ATOM 1105 CA ALA A 247 4.908 -0.720 -12.252 1.00 78.76 C
ANISOU 1105 CA ALA A 247 9883 12279 7761 1310 -1658 900 C
ATOM 1106 C ALA A 247 3.691 -0.394 -13.111 1.00 81.18 C
ANISOU 1106 C ALA A 247 9924 13194 7726 1475 -1756 1008 C
ATOM 1107 O ALA A 247 3.742 -0.501 -14.338 1.00 83.67 O
ANISOU 1107 O ALA A 247 10201 13768 7823 1456 -1786 1028 O
ATOM 1108 CB ALA A 247 4.799 -2.122 -11.657 1.00 77.84 C
ANISOU 1108 CB ALA A 247 9722 12143 7712 926 -1675 625 C
ATOM 1109 N ILE A 248 2.575 -0.025 -12.484 1.00 81.11 N
ANISOU 1109 N ILE A 248 9710 13459 7648 1639 -1807 1079 N
ATOM 1110 CA ILE A 248 1.400 0.332 -13.267 1.00 82.57 C
ANISOU 1110 CA ILE A 248 9604 14283 7484 1839 -1902 1206 C
ATOM 1111 C ILE A 248 1.725 1.524 -14.140 1.00 85.78 C
ANISOU 1111 C ILE A 248 10130 14670 7793 2233 -1850 1494 C
ATOM 1112 O ILE A 248 1.206 1.658 -15.255 1.00 89.64 O
ANISOU 1112 O ILE A 248 10448 15649 7964 2349 -1918 1592 O
ATOM 1113 CB ILE A 248 0.189 0.596 -12.347 1.00 80.64 C
ANISOU 1113 CB ILE A 248 9119 14322 7199 1989 -1947 1251 C
ATOM 1114 CG1 ILE A 248 -0.233 -0.700 -11.642 1.00 80.54 C
ANISOU 1114 CG1 ILE A 248 8970 14406 7227 1552 -1996 951 C
ATOM 1115 CG2 ILE A 248 -0.983 1.170 -13.114 1.00 81.33 C
ANISOU 1115 CG2 ILE A 248 8895 15087 6919 2295 -2032 1441 C
ATOM 1116 CD1 ILE A 248 -1.694 -0.722 -11.229 1.00 80.99 C
ANISOU 1116 CD1 ILE A 248 8664 15022 7087 1608 -2081 951 C
ATOM 1117 N GLY A 249 2.594 2.405 -13.649 1.00 83.84 N
ANISOU 1117 N GLY A 249 10186 13867 7802 2431 -1718 1631 N
ATOM 1118 CA GLY A 249 3.006 3.545 -14.446 1.00 86.78 C
ANISOU 1118 CA GLY A 249 10734 14137 8099 2780 -1628 1899 C
ATOM 1119 C GLY A 249 3.868 3.159 -15.629 1.00 89.73 C
ANISOU 1119 C GLY A 249 11219 14481 8393 2608 -1624 1849 C
ATOM 1120 O GLY A 249 3.761 3.749 -16.707 1.00 93.59 O
ANISOU 1120 O GLY A 249 11706 15202 8652 2845 -1615 2044 O
ATOM 1121 N LYS A 250 4.764 2.194 -15.438 1.00 90.55 N
ANISOU 1121 N LYS A 250 11434 14288 8681 2220 -1614 1604 N
ATOM 1122 CA LYS A 250 5.497 1.660 -16.574 1.00 90.15 C
ANISOU 1122 CA LYS A 250 11458 14260 8532 2028 -1612 1525 C
ATOM 1123 C LYS A 250 4.532 1.028 -17.562 1.00 93.79 C
ANISOU 1123 C LYS A 250 11630 15378 8626 1932 -1746 1460 C
ATOM 1124 O LYS A 250 4.607 1.269 -18.765 1.00 97.66 O
ANISOU 1124 O LYS A 250 12112 16110 8885 2026 -1756 1564 O
ATOM 1125 CB LYS A 250 6.526 0.648 -16.088 1.00 86.59 C
ANISOU 1125 CB LYS A 250 11158 13406 8335 1652 -1568 1270 C
ATOM 1126 CG LYS A 250 7.503 1.220 -15.105 1.00 84.38 C
ANISOU 1126 CG LYS A 250 11124 12549 8388 1714 -1448 1316 C
ATOM 1127 CD LYS A 250 8.285 2.401 -15.645 1.00 87.17 C
ANISOU 1127 CD LYS A 250 11703 12652 8766 1958 -1328 1536 C
ATOM 1128 CE LYS A 250 9.465 1.963 -16.476 1.00 89.27 C
ANISOU 1128 CE LYS A 250 12116 12749 9054 1769 -1271 1457 C
ATOM 1129 NZ LYS A 250 10.384 3.110 -16.707 1.00 90.97 N
ANISOU 1129 NZ LYS A 250 12583 12623 9358 1949 -1124 1642 N
ATOM 1130 N LEU A 251 3.580 0.253 -17.057 1.00 91.48 N
ANISOU 1130 N LEU A 251 11088 15412 8258 1739 -1844 1290 N
ATOM 1131 CA LEU A 251 2.699 -0.511 -17.928 1.00 93.21 C
ANISOU 1131 CA LEU A 251 11020 16273 8121 1542 -1965 1164 C
ATOM 1132 C LEU A 251 1.832 0.399 -18.798 1.00 98.20 C
ANISOU 1132 C LEU A 251 11438 17469 8403 1923 -2036 1432 C
ATOM 1133 O LEU A 251 1.735 0.196 -20.011 1.00 98.35 O
ANISOU 1133 O LEU A 251 11362 17879 8127 1870 -2089 1431 O
ATOM 1134 CB LEU A 251 1.834 -1.446 -17.081 1.00 92.45 C
ANISOU 1134 CB LEU A 251 10710 16390 8024 1248 -2032 930 C
ATOM 1135 CG LEU A 251 1.452 -2.755 -17.765 1.00 93.79 C
ANISOU 1135 CG LEU A 251 10726 16959 7952 789 -2091 637 C
ATOM 1136 CD1 LEU A 251 2.585 -3.778 -17.592 1.00 90.47 C
ANISOU 1136 CD1 LEU A 251 10602 15999 7774 420 -1980 392 C
ATOM 1137 CD2 LEU A 251 0.108 -3.269 -17.238 1.00 93.89 C
ANISOU 1137 CD2 LEU A 251 10402 17476 7794 619 -2184 502 C
ATOM 1138 N TYR A 252 1.162 1.391 -18.198 1.00109.99 N
ANISOU 1138 N TYR A 252 12849 19039 9905 2324 -2032 1668 N
ATOM 1139 CA TYR A 252 0.255 2.240 -18.976 1.00111.94 C
ANISOU 1139 CA TYR A 252 12914 19646 9971 2637 -1992 1867 C
ATOM 1140 C TYR A 252 1.007 3.252 -19.847 1.00112.38 C
ANISOU 1140 C TYR A 252 13227 19451 10023 2945 -1876 2119 C
ATOM 1141 O TYR A 252 0.456 3.715 -20.859 1.00112.22 O
ANISOU 1141 O TYR A 252 13072 19770 9798 3122 -1849 2243 O
ATOM 1142 CB TYR A 252 -0.738 2.966 -18.039 1.00113.54 C
ANISOU 1142 CB TYR A 252 12980 19893 10268 2921 -1939 1989 C
ATOM 1143 CG TYR A 252 -2.222 3.130 -18.472 1.00117.14 C
ANISOU 1143 CG TYR A 252 13047 20973 10486 3038 -1950 2025 C
ATOM 1144 CD1 TYR A 252 -2.591 3.972 -19.542 1.00120.40 C
ANISOU 1144 CD1 TYR A 252 13400 21633 10715 3358 -1876 2240 C
ATOM 1145 CD2 TYR A 252 -3.259 2.547 -17.729 1.00119.06 C
ANISOU 1145 CD2 TYR A 252 12996 21544 10698 2869 -2011 1868 C
ATOM 1146 CE1 TYR A 252 -3.955 4.161 -19.907 1.00124.31 C
ANISOU 1146 CE1 TYR A 252 13524 22733 10977 3503 -1873 2290 C
ATOM 1147 CE2 TYR A 252 -4.621 2.735 -18.082 1.00123.19 C
ANISOU 1147 CE2 TYR A 252 13152 22661 10995 2994 -2003 1912 C
ATOM 1148 CZ TYR A 252 -4.961 3.543 -19.171 1.00126.70 C
ANISOU 1148 CZ TYR A 252 13521 23377 11241 3320 -1935 2127 C
ATOM 1149 OH TYR A 252 -6.294 3.727 -19.513 1.00127.88 O
ANISOU 1149 OH TYR A 252 13292 24150 11145 3462 -1919 2179 O
ATOM 1150 N TYR A 253 2.240 3.635 -19.466 1.00102.40 N
ANISOU 1150 N TYR A 253 12328 17603 8977 3016 -1791 2200 N
ATOM 1151 CA TYR A 253 2.918 4.778 -20.082 1.00 99.77 C
ANISOU 1151 CA TYR A 253 12275 16945 8686 3326 -1633 2453 C
ATOM 1152 C TYR A 253 4.325 4.501 -20.639 1.00 99.47 C
ANISOU 1152 C TYR A 253 12525 16594 8674 3174 -1604 2429 C
ATOM 1153 O TYR A 253 4.706 5.161 -21.606 1.00102.66 O
ANISOU 1153 O TYR A 253 13068 16940 8997 3338 -1506 2591 O
ATOM 1154 CB TYR A 253 3.006 5.962 -19.083 1.00102.73 C
ANISOU 1154 CB TYR A 253 12872 16838 9322 3646 -1465 2637 C
ATOM 1155 CG TYR A 253 1.674 6.556 -18.540 1.00108.48 C
ANISOU 1155 CG TYR A 253 13382 17806 10030 3902 -1430 2721 C
ATOM 1156 CD1 TYR A 253 0.466 5.865 -18.628 1.00111.17 C
ANISOU 1156 CD1 TYR A 253 13315 18748 10175 3790 -1569 2599 C
ATOM 1157 CD2 TYR A 253 1.641 7.814 -17.936 1.00109.15 C
ANISOU 1157 CD2 TYR A 253 13680 17510 10283 4237 -1233 2910 C
ATOM 1158 CE1 TYR A 253 -0.734 6.404 -18.131 1.00112.13 C
ANISOU 1158 CE1 TYR A 253 13232 19109 10265 4035 -1522 2682 C
ATOM 1159 CE2 TYR A 253 0.442 8.360 -17.441 1.00110.09 C
ANISOU 1159 CE2 TYR A 253 13614 17852 10365 4488 -1181 2988 C
ATOM 1160 CZ TYR A 253 -0.741 7.646 -17.543 1.00110.76 C
ANISOU 1160 CZ TYR A 253 13276 18558 10248 4399 -1331 2883 C
ATOM 1161 OH TYR A 253 -1.934 8.163 -17.067 1.00108.84 O
ANISOU 1161 OH TYR A 253 12835 18570 9948 4653 -1271 2964 O
ATOM 1162 N ASP A 254 5.117 3.584 -20.069 1.00 97.39 N
ANISOU 1162 N ASP A 254 12362 15962 8679 2759 -1596 2143 N
ATOM 1163 CA ASP A 254 6.545 3.429 -20.433 1.00 96.79 C
ANISOU 1163 CA ASP A 254 12577 15418 8783 2565 -1485 2066 C
ATOM 1164 C ASP A 254 6.983 1.955 -20.559 1.00 96.98 C
ANISOU 1164 C ASP A 254 12549 15448 8852 2083 -1545 1726 C
ATOM 1165 O ASP A 254 7.968 1.524 -19.950 1.00 96.55 O
ANISOU 1165 O ASP A 254 12673 14923 9089 1863 -1468 1573 O
ATOM 1166 CB ASP A 254 7.448 4.147 -19.426 1.00 96.58 C
ANISOU 1166 CB ASP A 254 12845 14732 9118 2638 -1328 2123 C
ATOM 1167 CG ASP A 254 8.817 4.484 -20.006 1.00100.76 C
ANISOU 1167 CG ASP A 254 13669 14862 9755 2585 -1185 2163 C
ATOM 1168 OD1 ASP A 254 9.377 3.643 -20.748 1.00104.53 O
ANISOU 1168 OD1 ASP A 254 14137 15405 10174 2324 -1214 2006 O
ATOM 1169 OD2 ASP A 254 9.360 5.567 -19.702 1.00101.33 O1-
ANISOU 1169 OD2 ASP A 254 13991 14541 9968 2783 -1028 2336 O1-
ATOM 1170 N ASN A 255 6.250 1.156 -21.337 1.00101.65 N
ANISOU 1170 N ASN A 255 12898 16583 9141 1913 -1668 1602 N
ATOM 1171 CA ASN A 255 6.482 -0.291 -21.410 1.00100.19 C
ANISOU 1171 CA ASN A 255 12675 16420 8971 1447 -1700 1264 C
ATOM 1172 C ASN A 255 7.595 -0.634 -22.412 1.00103.82 C
ANISOU 1172 C ASN A 255 13332 16702 9413 1292 -1618 1198 C
ATOM 1173 O ASN A 255 7.363 -1.239 -23.462 1.00103.99 O
ANISOU 1173 O ASN A 255 13256 17104 9153 1119 -1668 1091 O
ATOM 1174 CB ASN A 255 5.181 -0.988 -21.783 1.00 96.92 C
ANISOU 1174 CB ASN A 255 11924 16679 8222 1287 -1846 1134 C
ATOM 1175 CG ASN A 255 5.134 -2.416 -21.320 1.00 95.20 C
ANISOU 1175 CG ASN A 255 11675 16417 8079 816 -1853 780 C
ATOM 1176 OD1 ASN A 255 5.823 -2.796 -20.362 1.00 95.10 O
ANISOU 1176 OD1 ASN A 255 11846 15888 8400 688 -1769 668 O
ATOM 1177 ND2 ASN A 255 4.345 -3.233 -22.007 1.00 88.93 N
ANISOU 1177 ND2 ASN A 255 10660 16166 6962 545 -1938 596 N
ATOM 1178 N GLU A 256 8.840 -0.288 -22.051 1.00107.07 N
ANISOU 1178 N GLU A 256 14019 16539 10123 1328 -1485 1240 N
ATOM 1179 CA GLU A 256 9.974 -0.489 -22.955 1.00107.14 C
ANISOU 1179 CA GLU A 256 14219 16357 10132 1220 -1390 1204 C
ATOM 1180 C GLU A 256 11.237 -0.823 -22.166 1.00106.53 C
ANISOU 1180 C GLU A 256 14357 15700 10418 1071 -1268 1088 C
ATOM 1181 O GLU A 256 11.307 -0.651 -20.944 1.00105.23 O
ANISOU 1181 O GLU A 256 14220 15255 10506 1103 -1252 1086 O
ATOM 1182 CB GLU A 256 10.263 0.750 -23.815 1.00107.87 C
ANISOU 1182 CB GLU A 256 14422 16464 10099 1543 -1330 1499 C
ATOM 1183 CG GLU A 256 10.346 2.055 -23.016 1.00109.26 C
ANISOU 1183 CG GLU A 256 14723 16327 10463 1871 -1252 1747 C
ATOM 1184 CD GLU A 256 11.252 3.105 -23.643 1.00111.15 C
ANISOU 1184 CD GLU A 256 15217 16295 10720 2071 -1101 1968 C
ATOM 1185 OE1 GLU A 256 11.404 3.118 -24.885 1.00109.88 O
ANISOU 1185 OE1 GLU A 256 15072 16355 10320 2092 -1093 2029 O
ATOM 1186 OE2 GLU A 256 11.815 3.921 -22.876 1.00113.39 O1-
ANISOU 1186 OE2 GLU A 256 15692 16144 11249 2187 -979 2072 O1-
ATOM 1187 N LYS A 257 12.248 -1.288 -22.907 1.00100.59 N
ANISOU 1187 N LYS A 257 13748 14803 9670 919 -1180 999 N
ATOM 1188 CA LYS A 257 13.617 -1.469 -22.409 1.00 98.41 C
ANISOU 1188 CA LYS A 257 13668 14030 9691 828 -1049 935 C
ATOM 1189 C LYS A 257 13.648 -2.224 -21.074 1.00 92.98 C
ANISOU 1189 C LYS A 257 12963 13113 9252 676 -1052 765 C
ATOM 1190 O LYS A 257 14.489 -1.970 -20.206 1.00 91.47 O
ANISOU 1190 O LYS A 257 12878 12546 9329 706 -976 787 O
ATOM 1191 CB LYS A 257 14.348 -0.117 -22.302 1.00 99.61 C
ANISOU 1191 CB LYS A 257 13976 13897 9974 1071 -952 1174 C
ATOM 1192 CG LYS A 257 14.585 0.608 -23.647 1.00101.52 C
ANISOU 1192 CG LYS A 257 14299 14278 9994 1216 -901 1350 C
ATOM 1193 CD LYS A 257 16.077 0.905 -23.971 1.00101.55 C
ANISOU 1193 CD LYS A 257 14515 13932 10140 1175 -738 1378 C
ATOM 1194 CE LYS A 257 16.298 2.260 -24.677 1.00101.41 C
ANISOU 1194 CE LYS A 257 14640 13874 10016 1419 -644 1651 C
ATOM 1195 NZ LYS A 257 17.743 2.619 -24.835 1.00 98.88 N
ANISOU 1195 NZ LYS A 257 14516 13203 9849 1350 -472 1670 N
ATOM 1196 N CYS A 258 12.743 -3.191 -20.929 1.00 92.62 N
ANISOU 1196 N CYS A 258 12781 13313 9097 492 -1132 587 N
ATOM 1197 CA CYS A 258 12.624 -4.014 -19.732 1.00 88.56 C
ANISOU 1197 CA CYS A 258 12253 12619 8775 334 -1130 421 C
ATOM 1198 C CYS A 258 12.396 -3.170 -18.488 1.00 86.39 C
ANISOU 1198 C CYS A 258 11946 12176 8701 523 -1162 556 C
ATOM 1199 O CYS A 258 12.643 -3.630 -17.378 1.00 83.09 O
ANISOU 1199 O CYS A 258 11561 11510 8499 441 -1134 465 O
ATOM 1200 CB CYS A 258 13.859 -4.915 -19.554 1.00 87.99 C
ANISOU 1200 CB CYS A 258 12357 12186 8887 170 -995 273 C
ATOM 1201 SG CYS A 258 13.856 -6.376 -20.621 1.00 76.55 S
ANISOU 1201 SG CYS A 258 10965 10896 7226 -137 -929 15 S
ATOM 1202 N TRP A 259 11.911 -1.943 -18.669 1.00 90.05 N
ANISOU 1202 N TRP A 259 12358 12776 9080 786 -1207 778 N
ATOM 1203 CA TRP A 259 11.686 -0.951 -17.624 1.00 86.83 C
ANISOU 1203 CA TRP A 259 11953 12204 8834 999 -1209 930 C
ATOM 1204 C TRP A 259 12.982 -0.332 -17.109 1.00 86.62 C
ANISOU 1204 C TRP A 259 12127 11720 9064 1054 -1085 1000 C
ATOM 1205 O TRP A 259 12.945 0.492 -16.187 1.00 84.29 O
ANISOU 1205 O TRP A 259 11872 11237 8918 1194 -1060 1102 O
ATOM 1206 CB TRP A 259 10.880 -1.551 -16.472 1.00 85.17 C
ANISOU 1206 CB TRP A 259 11614 12041 8708 898 -1280 805 C
ATOM 1207 CG TRP A 259 9.507 -1.958 -16.907 1.00 84.48 C
ANISOU 1207 CG TRP A 259 11299 12452 8349 851 -1400 753 C
ATOM 1208 CD1 TRP A 259 8.931 -1.705 -18.112 1.00 87.08 C
ANISOU 1208 CD1 TRP A 259 11519 13193 8376 931 -1458 833 C
ATOM 1209 CD2 TRP A 259 8.544 -2.686 -16.143 1.00 83.23 C
ANISOU 1209 CD2 TRP A 259 10978 12470 8176 698 -1472 606 C
ATOM 1210 NE1 TRP A 259 7.666 -2.226 -18.153 1.00 88.27 N
ANISOU 1210 NE1 TRP A 259 11426 13802 8312 830 -1570 739 N
ATOM 1211 CE2 TRP A 259 7.401 -2.836 -16.955 1.00 85.60 C
ANISOU 1211 CE2 TRP A 259 11056 13319 8151 675 -1575 594 C
ATOM 1212 CE3 TRP A 259 8.538 -3.228 -14.849 1.00 81.26 C
ANISOU 1212 CE3 TRP A 259 10745 11987 8144 574 -1455 486 C
ATOM 1213 CZ2 TRP A 259 6.258 -3.502 -16.520 1.00 85.03 C
ANISOU 1213 CZ2 TRP A 259 10770 13573 7964 506 -1656 451 C
ATOM 1214 CZ3 TRP A 259 7.407 -3.888 -14.415 1.00 81.17 C
ANISOU 1214 CZ3 TRP A 259 10550 12260 8031 421 -1527 355 C
ATOM 1215 CH2 TRP A 259 6.279 -4.018 -15.251 1.00 84.71 C
ANISOU 1215 CH2 TRP A 259 10771 13261 8155 376 -1625 332 C
ATOM 1216 N ALA A 260 14.126 -0.681 -17.703 1.00 91.13 N
ANISOU 1216 N ALA A 260 12820 12131 9674 940 -998 944 N
ATOM 1217 CA ALA A 260 15.428 -0.122 -17.350 1.00 91.96 C
ANISOU 1217 CA ALA A 260 13086 11870 9984 959 -875 998 C
ATOM 1218 C ALA A 260 15.877 0.978 -18.294 1.00 96.20 C
ANISOU 1218 C ALA A 260 13747 12379 10425 1110 -791 1186 C
ATOM 1219 O ALA A 260 17.011 1.457 -18.182 1.00 95.66 O
ANISOU 1219 O ALA A 260 13814 12040 10492 1089 -672 1221 O
ATOM 1220 CB ALA A 260 16.493 -1.219 -17.331 1.00 90.12 C
ANISOU 1220 CB ALA A 260 12899 11482 9860 752 -812 824 C
ATOM 1221 N GLY A 261 15.031 1.367 -19.238 1.00 97.17 N
ANISOU 1221 N GLY A 261 13823 12797 10300 1254 -842 1306 N
ATOM 1222 CA GLY A 261 15.397 2.432 -20.143 1.00100.41 C
ANISOU 1222 CA GLY A 261 14375 13176 10601 1424 -746 1508 C
ATOM 1223 C GLY A 261 15.486 3.758 -19.412 1.00103.52 C
ANISOU 1223 C GLY A 261 14910 13299 11126 1611 -647 1683 C
ATOM 1224 O GLY A 261 14.749 4.023 -18.463 1.00103.20 O
ANISOU 1224 O GLY A 261 14810 13244 11155 1705 -692 1706 O
ATOM 1225 N LYS A 262 16.421 4.588 -19.846 1.00105.94 N
ANISOU 1225 N LYS A 262 15418 13375 11460 1646 -491 1796 N
ATOM 1226 CA LYS A 262 16.460 5.984 -19.449 1.00109.59 C
ANISOU 1226 CA LYS A 262 16074 13584 11981 1832 -350 1986 C
ATOM 1227 C LYS A 262 16.029 6.809 -20.655 1.00115.11 C
ANISOU 1227 C LYS A 262 16877 14435 12424 2090 -290 2228 C
ATOM 1228 O LYS A 262 16.539 6.604 -21.762 1.00114.54 O
ANISOU 1228 O LYS A 262 16841 14459 12222 2035 -261 2240 O
ATOM 1229 CB LYS A 262 17.853 6.379 -18.957 1.00106.91 C
ANISOU 1229 CB LYS A 262 15907 12859 11856 1651 -188 1928 C
ATOM 1230 N ARG A 263 15.047 7.690 -20.456 1.00122.95 N
ANISOU 1230 N ARG A 263 17910 15478 13328 2391 -270 2426 N
ATOM 1231 CA ARG A 263 14.518 8.538 -21.518 1.00126.27 C
ANISOU 1231 CA ARG A 263 18431 16063 13484 2708 -204 2698 C
ATOM 1232 C ARG A 263 14.232 9.931 -20.975 1.00130.87 C
ANISOU 1232 C ARG A 263 19256 16359 14109 2993 -21 2922 C
ATOM 1233 O ARG A 263 13.838 10.081 -19.811 1.00127.64 O
ANISOU 1233 O ARG A 263 18824 15818 13856 3015 -30 2875 O
ATOM 1234 CB ARG A 263 13.238 7.950 -22.131 1.00123.95 C
ANISOU 1234 CB ARG A 263 17854 16328 12913 2859 -407 2734 C
ATOM 1235 N PRO A 264 14.414 10.964 -21.796 1.00138.09 N
ANISOU 1235 N PRO A 264 20429 17160 14880 3217 166 3169 N
ATOM 1236 CA PRO A 264 14.209 12.336 -21.314 1.00137.80 C
ANISOU 1236 CA PRO A 264 20688 16786 14885 3483 396 3381 C
ATOM 1237 C PRO A 264 12.735 12.678 -21.154 1.00136.72 C
ANISOU 1237 C PRO A 264 20341 16949 14658 3790 323 3467 C
ATOM 1238 O PRO A 264 11.873 12.179 -21.881 1.00137.56 O
ANISOU 1238 O PRO A 264 20176 17552 14540 3928 147 3514 O
ATOM 1239 CB PRO A 264 14.856 13.197 -22.407 1.00139.51 C
ANISOU 1239 CB PRO A 264 21150 16844 15014 3524 615 3516 C
ATOM 1240 CG PRO A 264 14.742 12.367 -23.643 1.00139.55 C
ANISOU 1240 CG PRO A 264 20972 17289 14762 3539 446 3549 C
ATOM 1241 CD PRO A 264 14.880 10.931 -23.194 1.00138.98 C
ANISOU 1241 CD PRO A 264 20603 17413 14792 3219 204 3257 C
ATOM 1242 N GLY A 265 12.457 13.560 -20.194 1.00130.75 N
ANISOU 1242 N GLY A 265 19712 15900 14066 3883 476 3478 N
ATOM 1243 CA GLY A 265 11.096 13.981 -19.947 1.00125.45 C
ANISOU 1243 CA GLY A 265 18870 15475 13320 4187 448 3563 C
ATOM 1244 C GLY A 265 10.213 12.934 -19.314 1.00122.49 C
ANISOU 1244 C GLY A 265 18142 15474 12926 4166 177 3453 C
ATOM 1245 O GLY A 265 8.991 13.107 -19.295 1.00122.54 O
ANISOU 1245 O GLY A 265 17935 15808 12818 4410 120 3522 O
ATOM 1246 N VAL A 266 10.783 11.850 -18.795 1.00119.25 N
ANISOU 1246 N VAL A 266 17662 15035 12613 3882 21 3282 N
ATOM 1247 CA VAL A 266 10.005 10.764 -18.211 1.00114.08 C
ANISOU 1247 CA VAL A 266 16682 14735 11928 3828 -234 3158 C
ATOM 1248 C VAL A 266 10.122 10.862 -16.697 1.00109.86 C
ANISOU 1248 C VAL A 266 16222 13859 11660 3725 -190 3039 C
ATOM 1249 O VAL A 266 11.222 10.766 -16.137 1.00109.81 O
ANISOU 1249 O VAL A 266 16365 13466 11891 3416 -112 2869 O
ATOM 1250 CB VAL A 266 10.469 9.392 -18.718 1.00114.04 C
ANISOU 1250 CB VAL A 266 16468 14965 11896 3474 -427 2930 C
ATOM 1251 CG1 VAL A 266 9.527 8.316 -18.234 1.00106.37 C
ANISOU 1251 CG1 VAL A 266 15133 14390 10891 3362 -659 2755 C
ATOM 1252 CG2 VAL A 266 10.567 9.386 -20.248 1.00118.07 C
ANISOU 1252 CG2 VAL A 266 16977 15750 12133 3563 -436 3058 C
ATOM 1253 N TYR A 267 8.993 11.058 -16.033 1.00106.96 N
ANISOU 1253 N TYR A 267 15689 13662 11288 3905 -231 3059 N
ATOM 1254 CA TYR A 267 8.983 11.207 -14.592 1.00103.14 C
ANISOU 1254 CA TYR A 267 15273 12886 11031 3840 -184 2961 C
ATOM 1255 C TYR A 267 8.572 9.925 -13.876 1.00101.77 C
ANISOU 1255 C TYR A 267 14778 12969 10920 3611 -426 2735 C
ATOM 1256 O TYR A 267 8.465 9.930 -12.647 1.00101.39 O
ANISOU 1256 O TYR A 267 14733 12734 11055 3535 -412 2629 O
ATOM 1257 CB TYR A 267 8.062 12.372 -14.202 1.00103.53 C
ANISOU 1257 CB TYR A 267 15363 12892 11082 4126 -18 3074 C
ATOM 1258 N THR A 268 8.372 8.819 -14.608 1.00 97.31 N
ANISOU 1258 N THR A 268 13942 12812 10218 3447 -625 2624 N
ATOM 1259 CA THR A 268 7.816 7.617 -13.984 1.00 93.93 C
ANISOU 1259 CA THR A 268 13208 12652 9830 3216 -824 2397 C
ATOM 1260 C THR A 268 8.683 7.132 -12.828 1.00 86.63 C
ANISOU 1260 C THR A 268 12364 11341 9213 2883 -805 2166 C
ATOM 1261 O THR A 268 8.162 6.665 -11.813 1.00 84.22 O
ANISOU 1261 O THR A 268 11915 11084 9002 2800 -883 2045 O
ATOM 1262 CB THR A 268 7.644 6.484 -15.005 1.00 93.93 C
ANISOU 1262 CB THR A 268 12968 13084 9638 3026 -997 2282 C
ATOM 1263 OG1 THR A 268 8.687 6.535 -15.986 1.00 95.78 O
ANISOU 1263 OG1 THR A 268 13375 13168 9849 2932 -926 2300 O
ATOM 1264 CG2 THR A 268 6.282 6.545 -15.686 1.00 92.44 C
ANISOU 1264 CG2 THR A 268 12515 13486 9122 3293 -1109 2427 C
ATOM 1265 N ASP A 269 10.005 7.207 -12.978 1.00 84.60 N
ANISOU 1265 N ASP A 269 12316 10733 9095 2690 -703 2105 N
ATOM 1266 CA ASP A 269 10.951 6.743 -11.968 1.00 81.07 C
ANISOU 1266 CA ASP A 269 11927 9966 8908 2384 -684 1900 C
ATOM 1267 C ASP A 269 10.916 7.578 -10.690 1.00 79.54 C
ANISOU 1267 C ASP A 269 11878 9463 8883 2456 -567 1922 C
ATOM 1268 O ASP A 269 11.515 7.171 -9.688 1.00 76.09 O
ANISOU 1268 O ASP A 269 11443 8828 8640 2220 -573 1752 O
ATOM 1269 CB ASP A 269 12.384 6.744 -12.532 1.00 79.43 C
ANISOU 1269 CB ASP A 269 11892 9515 8773 2190 -588 1854 C
ATOM 1270 CG ASP A 269 12.652 5.613 -13.553 1.00 79.31 C
ANISOU 1270 CG ASP A 269 11734 9751 8648 2020 -703 1750 C
ATOM 1271 OD1 ASP A 269 11.790 4.720 -13.746 1.00 78.01 O
ANISOU 1271 OD1 ASP A 269 11344 9932 8366 1991 -857 1675 O
ATOM 1272 OD2 ASP A 269 13.754 5.625 -14.159 1.00 80.39 O1-
ANISOU 1272 OD2 ASP A 269 11996 9737 8812 1898 -622 1733 O1-
ATOM 1273 N TYR A 270 10.261 8.741 -10.700 1.00 79.89 N
ANISOU 1273 N TYR A 270 12054 9457 8845 2784 -446 2131 N
ATOM 1274 CA TYR A 270 10.155 9.521 -9.483 1.00 77.82 C
ANISOU 1274 CA TYR A 270 11943 8898 8726 2850 -319 2140 C
ATOM 1275 C TYR A 270 9.187 8.878 -8.499 1.00 75.20 C
ANISOU 1275 C TYR A 270 11364 8776 8431 2844 -464 2038 C
ATOM 1276 O TYR A 270 9.297 9.127 -7.291 1.00 73.39 O
ANISOU 1276 O TYR A 270 11211 8310 8363 2772 -402 1956 O
ATOM 1277 CB TYR A 270 9.739 10.959 -9.820 1.00 82.90 C
ANISOU 1277 CB TYR A 270 12844 9393 9262 3230 -107 2405 C
ATOM 1278 CG TYR A 270 10.805 11.730 -10.577 1.00 87.45 C
ANISOU 1278 CG TYR A 270 13735 9660 9833 3196 92 2493 C
ATOM 1279 CD1 TYR A 270 10.548 13.007 -11.096 1.00 91.41 C
ANISOU 1279 CD1 TYR A 270 14482 10019 10231 3490 317 2712 C
ATOM 1280 CD2 TYR A 270 12.075 11.168 -10.802 1.00 87.98 C
ANISOU 1280 CD2 TYR A 270 13817 9607 10004 2832 70 2326 C
ATOM 1281 CE1 TYR A 270 11.542 13.713 -11.811 1.00 91.20 C
ANISOU 1281 CE1 TYR A 270 14734 9716 10203 3403 517 2762 C
ATOM 1282 CE2 TYR A 270 13.072 11.863 -11.522 1.00 88.60 C
ANISOU 1282 CE2 TYR A 270 14170 9426 10068 2775 259 2398 C
ATOM 1283 CZ TYR A 270 12.796 13.135 -12.016 1.00 91.77 C
ANISOU 1283 CZ TYR A 270 14870 9647 10353 3084 488 2645 C
ATOM 1284 OH TYR A 270 13.767 13.823 -12.714 1.00 95.96 O
ANISOU 1284 OH TYR A 270 15684 9910 10865 3003 694 2709 O
ATOM 1285 N ILE A 271 8.285 8.015 -8.973 1.00 75.10 N
ANISOU 1285 N ILE A 271 11056 9214 8266 2879 -652 2021 N
ATOM 1286 CA ILE A 271 7.355 7.355 -8.062 1.00 75.25 C
ANISOU 1286 CA ILE A 271 10834 9451 8308 2839 -781 1912 C
ATOM 1287 C ILE A 271 8.117 6.648 -6.958 1.00 73.36 C
ANISOU 1287 C ILE A 271 10607 8966 8302 2499 -807 1682 C
ATOM 1288 O ILE A 271 7.769 6.742 -5.775 1.00 70.55 O
ANISOU 1288 O ILE A 271 10236 8516 8056 2494 -794 1626 O
ATOM 1289 CB ILE A 271 6.454 6.377 -8.825 1.00 75.33 C
ANISOU 1289 CB ILE A 271 10524 9991 8108 2818 -972 1878 C
ATOM 1290 CG1 ILE A 271 5.622 7.149 -9.842 1.00 78.10 C
ANISOU 1290 CG1 ILE A 271 10829 10651 8196 3200 -951 2130 C
ATOM 1291 CG2 ILE A 271 5.612 5.551 -7.846 1.00 73.54 C
ANISOU 1291 CG2 ILE A 271 10055 9970 7918 2693 -1095 1725 C
ATOM 1292 CD1 ILE A 271 5.340 8.572 -9.433 1.00 80.82 C
ANISOU 1292 CD1 ILE A 271 11388 10764 8555 3576 -763 2352 C
ATOM 1293 N TYR A 272 9.174 5.935 -7.323 1.00 71.49 N
ANISOU 1293 N TYR A 272 10396 8635 8133 2228 -838 1556 N
ATOM 1294 CA TYR A 272 9.978 5.306 -6.291 1.00 69.32 C
ANISOU 1294 CA TYR A 272 10136 8141 8061 1946 -850 1367 C
ATOM 1295 C TYR A 272 11.195 6.142 -5.892 1.00 68.95 C
ANISOU 1295 C TYR A 272 10342 7695 8160 1872 -687 1372 C
ATOM 1296 O TYR A 272 11.650 6.034 -4.754 1.00 66.97 O
ANISOU 1296 O TYR A 272 10118 7267 8063 1718 -668 1257 O
ATOM 1297 CB TYR A 272 10.382 3.889 -6.737 1.00 68.59 C
ANISOU 1297 CB TYR A 272 9904 8198 7959 1693 -969 1210 C
ATOM 1298 CG TYR A 272 11.564 3.755 -7.701 1.00 70.03 C
ANISOU 1298 CG TYR A 272 10194 8277 8136 1582 -921 1202 C
ATOM 1299 CD1 TYR A 272 11.366 3.717 -9.092 1.00 73.25 C
ANISOU 1299 CD1 TYR A 272 10576 8897 8359 1661 -945 1283 C
ATOM 1300 CD2 TYR A 272 12.865 3.604 -7.222 1.00 66.55 C
ANISOU 1300 CD2 TYR A 272 9855 7572 7858 1392 -857 1109 C
ATOM 1301 CE1 TYR A 272 12.434 3.577 -9.974 1.00 71.22 C
ANISOU 1301 CE1 TYR A 272 10415 8551 8092 1557 -894 1272 C
ATOM 1302 CE2 TYR A 272 13.936 3.477 -8.086 1.00 67.38 C
ANISOU 1302 CE2 TYR A 272 10038 7610 7952 1296 -807 1102 C
ATOM 1303 CZ TYR A 272 13.717 3.453 -9.466 1.00 71.35 C
ANISOU 1303 CZ TYR A 272 10534 8293 8284 1377 -822 1181 C
ATOM 1304 OH TYR A 272 14.787 3.314 -10.325 1.00 68.87 O
ANISOU 1304 OH TYR A 272 10298 7913 7956 1280 -764 1170 O
ATOM 1305 N GLN A 273 11.742 6.984 -6.776 1.00 70.05 N
ANISOU 1305 N GLN A 273 10671 7704 8242 1960 -562 1496 N
ATOM 1306 CA GLN A 273 12.926 7.748 -6.381 1.00 70.13 C
ANISOU 1306 CA GLN A 273 10916 7353 8377 1830 -394 1471 C
ATOM 1307 C GLN A 273 12.583 8.869 -5.405 1.00 68.53 C
ANISOU 1307 C GLN A 273 10892 6912 8235 1948 -244 1523 C
ATOM 1308 O GLN A 273 13.380 9.191 -4.523 1.00 63.88 O
ANISOU 1308 O GLN A 273 10420 6075 7775 1755 -150 1418 O
ATOM 1309 CB GLN A 273 13.638 8.311 -7.609 1.00 69.43 C
ANISOU 1309 CB GLN A 273 10997 7178 8205 1858 -279 1579 C
ATOM 1310 CG GLN A 273 14.832 7.509 -8.010 1.00 71.88 C
ANISOU 1310 CG GLN A 273 11250 7494 8566 1592 -322 1453 C
ATOM 1311 CD GLN A 273 15.150 7.703 -9.487 1.00 76.28 C
ANISOU 1311 CD GLN A 273 11884 8113 8985 1660 -275 1566 C
ATOM 1312 OE1 GLN A 273 14.231 7.807 -10.298 1.00 76.40 O
ANISOU 1312 OE1 GLN A 273 11859 8333 8837 1888 -319 1702 O
ATOM 1313 NE2 GLN A 273 16.443 7.731 -9.846 1.00 70.55 N
ANISOU 1313 NE2 GLN A 273 11249 7250 8307 1463 -188 1512 N
ATOM 1314 N GLY A 274 11.430 9.494 -5.561 1.00 68.30 N
ANISOU 1314 N GLY A 274 10888 6966 8098 2264 -208 1684 N
ATOM 1315 CA GLY A 274 11.039 10.590 -4.707 1.00 68.49 C
ANISOU 1315 CA GLY A 274 11112 6748 8164 2417 -35 1747 C
ATOM 1316 C GLY A 274 11.014 10.184 -3.244 1.00 68.19 C
ANISOU 1316 C GLY A 274 10983 6655 8271 2235 -91 1570 C
ATOM 1317 O GLY A 274 11.563 10.879 -2.375 1.00 67.36 O
ANISOU 1317 O GLY A 274 11080 6246 8268 2117 64 1502 O
ATOM 1318 N PRO A 275 10.367 9.044 -2.935 1.00 67.80 N
ANISOU 1318 N PRO A 275 10636 6906 8220 2192 -303 1483 N
ATOM 1319 CA PRO A 275 10.438 8.501 -1.571 1.00 65.09 C
ANISOU 1319 CA PRO A 275 10196 6526 8009 1997 -367 1311 C
ATOM 1320 C PRO A 275 11.852 8.329 -1.038 1.00 64.16 C
ANISOU 1320 C PRO A 275 10158 6197 8023 1673 -330 1158 C
ATOM 1321 O PRO A 275 12.113 8.664 0.124 1.00 64.40 O
ANISOU 1321 O PRO A 275 10264 6059 8147 1559 -261 1066 O
ATOM 1322 CB PRO A 275 9.713 7.154 -1.726 1.00 62.72 C
ANISOU 1322 CB PRO A 275 9584 6588 7657 1963 -588 1250 C
ATOM 1323 CG PRO A 275 8.635 7.466 -2.666 1.00 64.60 C
ANISOU 1323 CG PRO A 275 9753 7070 7720 2258 -606 1419 C
ATOM 1324 CD PRO A 275 9.285 8.387 -3.701 1.00 68.26 C
ANISOU 1324 CD PRO A 275 10449 7362 8126 2365 -462 1559 C
ATOM 1325 N MET A 276 12.780 7.819 -1.846 1.00 64.13 N
ANISOU 1325 N MET A 276 10126 6227 8013 1523 -370 1127 N
ATOM 1326 CA MET A 276 14.107 7.532 -1.308 1.00 63.62 C
ANISOU 1326 CA MET A 276 10076 6043 8054 1229 -352 983 C
ATOM 1327 C MET A 276 14.729 8.814 -0.778 1.00 61.45 C
ANISOU 1327 C MET A 276 10058 5469 7822 1150 -141 973 C
ATOM 1328 O MET A 276 15.344 8.830 0.293 1.00 62.42 O
ANISOU 1328 O MET A 276 10183 5510 8025 942 -116 841 O
ATOM 1329 CB MET A 276 15.022 6.893 -2.373 1.00 64.23 C
ANISOU 1329 CB MET A 276 10098 6204 8102 1115 -398 970 C
ATOM 1330 CG MET A 276 14.369 6.070 -3.511 1.00 64.43 C
ANISOU 1330 CG MET A 276 9980 6480 8021 1238 -528 1031 C
ATOM 1331 SD MET A 276 15.251 4.535 -4.026 1.00 63.00 S
ANISOU 1331 SD MET A 276 9631 6453 7853 1037 -648 913 S
ATOM 1332 CE MET A 276 16.746 5.247 -4.726 1.00 65.90 C
ANISOU 1332 CE MET A 276 10161 6649 8228 920 -500 936 C
ATOM 1333 N ALA A 277 14.554 9.906 -1.515 1.00 63.96 N
ANISOU 1333 N ALA A 277 10606 5626 8068 1312 26 1113 N
ATOM 1334 CA ALA A 277 15.092 11.198 -1.101 1.00 65.38 C
ANISOU 1334 CA ALA A 277 11091 5478 8271 1227 276 1103 C
ATOM 1335 C ALA A 277 14.386 11.723 0.144 1.00 66.80 C
ANISOU 1335 C ALA A 277 11352 5536 8494 1289 349 1066 C
ATOM 1336 O ALA A 277 15.010 12.359 1.003 1.00 64.98 O
ANISOU 1336 O ALA A 277 11284 5091 8313 1077 497 950 O
ATOM 1337 CB ALA A 277 14.966 12.204 -2.250 1.00 62.43 C
ANISOU 1337 CB ALA A 277 10978 4945 7798 1429 462 1288 C
ATOM 1338 N LEU A 278 13.073 11.503 0.232 1.00 66.08 N
ANISOU 1338 N LEU A 278 11148 5595 8365 1572 259 1158 N
ATOM 1339 CA LEU A 278 12.298 12.022 1.346 1.00 64.20 C
ANISOU 1339 CA LEU A 278 10987 5253 8155 1675 340 1141 C
ATOM 1340 C LEU A 278 12.739 11.407 2.676 1.00 65.50 C
ANISOU 1340 C LEU A 278 11012 5454 8420 1390 245 934 C
ATOM 1341 O LEU A 278 12.904 12.133 3.669 1.00 64.85 O
ANISOU 1341 O LEU A 278 11104 5160 8377 1285 397 848 O
ATOM 1342 CB LEU A 278 10.820 11.767 1.086 1.00 63.79 C
ANISOU 1342 CB LEU A 278 10776 5438 8024 2031 237 1283 C
ATOM 1343 CG LEU A 278 9.961 12.419 2.161 1.00 70.37 C
ANISOU 1343 CG LEU A 278 11707 6158 8874 2188 351 1290 C
ATOM 1344 CD1 LEU A 278 9.810 13.937 1.907 1.00 66.11 C
ANISOU 1344 CD1 LEU A 278 11559 5282 8278 2419 664 1437 C
ATOM 1345 CD2 LEU A 278 8.646 11.652 2.343 1.00 70.89 C
ANISOU 1345 CD2 LEU A 278 11469 6574 8892 2395 162 1333 C
ATOM 1346 N VAL A 279 12.943 10.079 2.730 1.00 63.68 N
ANISOU 1346 N VAL A 279 10486 5487 8221 1261 12 853 N
ATOM 1347 CA VAL A 279 13.365 9.503 4.013 1.00 64.12 C
ANISOU 1347 CA VAL A 279 10419 5587 8355 1024 -67 682 C
ATOM 1348 C VAL A 279 14.788 9.936 4.344 1.00 64.83 C
ANISOU 1348 C VAL A 279 10628 5530 8476 716 44 561 C
ATOM 1349 O VAL A 279 15.129 10.107 5.522 1.00 66.12 O
ANISOU 1349 O VAL A 279 10806 5643 8672 532 82 430 O
ATOM 1350 CB VAL A 279 13.205 7.959 4.092 1.00 60.34 C
ANISOU 1350 CB VAL A 279 9632 5399 7897 981 -309 633 C
ATOM 1351 CG1 VAL A 279 11.755 7.558 3.930 1.00 61.18 C
ANISOU 1351 CG1 VAL A 279 9607 5680 7957 1226 -406 717 C
ATOM 1352 CG2 VAL A 279 14.079 7.209 3.091 1.00 61.51 C
ANISOU 1352 CG2 VAL A 279 9686 5653 8033 880 -392 633 C
ATOM 1353 N LEU A 280 15.628 10.150 3.327 1.00 65.03 N
ANISOU 1353 N LEU A 280 10729 5506 8473 641 104 596 N
ATOM 1354 CA LEU A 280 16.967 10.674 3.584 1.00 66.05 C
ANISOU 1354 CA LEU A 280 10968 5520 8608 329 233 478 C
ATOM 1355 C LEU A 280 16.909 12.076 4.187 1.00 65.45 C
ANISOU 1355 C LEU A 280 11212 5138 8518 265 494 440 C
ATOM 1356 O LEU A 280 17.700 12.405 5.079 1.00 66.78 O
ANISOU 1356 O LEU A 280 11423 5259 8692 -34 575 278 O
ATOM 1357 CB LEU A 280 17.792 10.665 2.295 1.00 65.18 C
ANISOU 1357 CB LEU A 280 10885 5419 8461 278 264 535 C
ATOM 1358 CG LEU A 280 19.281 11.035 2.394 1.00 65.64 C
ANISOU 1358 CG LEU A 280 10992 5439 8508 -71 376 410 C
ATOM 1359 CD1 LEU A 280 20.079 10.107 3.289 1.00 66.13 C
ANISOU 1359 CD1 LEU A 280 10777 5752 8596 -292 224 264 C
ATOM 1360 CD2 LEU A 280 19.894 11.028 1.022 1.00 66.17 C
ANISOU 1360 CD2 LEU A 280 11092 5516 8534 -69 411 491 C
ATOM 1361 N LEU A 281 15.998 12.924 3.696 1.00 64.27 N
ANISOU 1361 N LEU A 281 11297 4787 8335 541 643 586 N
ATOM 1362 CA LEU A 281 15.799 14.228 4.313 1.00 66.26 C
ANISOU 1362 CA LEU A 281 11892 4711 8572 526 920 559 C
ATOM 1363 C LEU A 281 15.458 14.080 5.795 1.00 69.09 C
ANISOU 1363 C LEU A 281 12174 5107 8971 434 879 419 C
ATOM 1364 O LEU A 281 15.951 14.843 6.635 1.00 67.23 O
ANISOU 1364 O LEU A 281 12136 4680 8727 185 1065 274 O
ATOM 1365 CB LEU A 281 14.692 14.994 3.591 1.00 63.62 C
ANISOU 1365 CB LEU A 281 11784 4203 8186 936 1067 778 C
ATOM 1366 CG LEU A 281 14.364 16.362 4.211 1.00 67.41 C
ANISOU 1366 CG LEU A 281 12668 4299 8645 985 1395 773 C
ATOM 1367 CD1 LEU A 281 15.392 17.455 3.895 1.00 68.90 C
ANISOU 1367 CD1 LEU A 281 13194 4189 8794 723 1692 711 C
ATOM 1368 CD2 LEU A 281 12.948 16.829 3.864 1.00 68.33 C
ANISOU 1368 CD2 LEU A 281 12846 4410 8706 1468 1459 987 C
ATOM 1369 N ILE A 282 14.625 13.093 6.134 1.00 66.76 N
ANISOU 1369 N ILE A 282 11598 5063 8706 606 646 450 N
ATOM 1370 CA ILE A 282 14.182 12.973 7.509 1.00 67.06 C
ANISOU 1370 CA ILE A 282 11575 5133 8773 555 616 339 C
ATOM 1371 C ILE A 282 15.266 12.364 8.394 1.00 67.44 C
ANISOU 1371 C ILE A 282 11445 5340 8840 184 509 145 C
ATOM 1372 O ILE A 282 15.284 12.609 9.608 1.00 69.26 O
ANISOU 1372 O ILE A 282 11710 5538 9069 33 560 12 O
ATOM 1373 CB ILE A 282 12.861 12.192 7.581 1.00 67.11 C
ANISOU 1373 CB ILE A 282 11358 5350 8791 860 433 441 C
ATOM 1374 CG1 ILE A 282 11.772 12.974 6.827 1.00 65.82 C
ANISOU 1374 CG1 ILE A 282 11372 5062 8576 1247 568 638 C
ATOM 1375 CG2 ILE A 282 12.467 11.968 9.032 1.00 63.55 C
ANISOU 1375 CG2 ILE A 282 10825 4951 8368 785 392 319 C
ATOM 1376 CD1 ILE A 282 10.421 12.338 6.902 1.00 64.93 C
ANISOU 1376 CD1 ILE A 282 11030 5192 8446 1537 411 732 C
ATOM 1377 N ASN A 283 16.179 11.583 7.826 1.00 64.67 N
ANISOU 1377 N ASN A 283 10901 5179 8491 45 369 130 N
ATOM 1378 CA ASN A 283 17.310 11.098 8.608 1.00 65.84 C
ANISOU 1378 CA ASN A 283 10879 5506 8630 -282 292 -33 C
ATOM 1379 C ASN A 283 18.305 12.218 8.903 1.00 68.65 C
ANISOU 1379 C ASN A 283 11459 5693 8932 -609 522 -171 C
ATOM 1380 O ASN A 283 19.122 12.107 9.825 1.00 70.14 O
ANISOU 1380 O ASN A 283 11539 6029 9081 -904 502 -333 O
ATOM 1381 CB ASN A 283 18.001 9.953 7.865 1.00 69.00 C
ANISOU 1381 CB ASN A 283 11020 6159 9038 -298 102 6 C
ATOM 1382 CG ASN A 283 17.842 8.614 8.561 1.00 68.06 C
ANISOU 1382 CG ASN A 283 10606 6310 8944 -262 -124 -15 C
ATOM 1383 OD1 ASN A 283 17.028 8.474 9.474 1.00 66.22 O
ANISOU 1383 OD1 ASN A 283 10347 6086 8728 -186 -164 -36 O
ATOM 1384 ND2 ASN A 283 18.613 7.616 8.123 1.00 64.45 N
ANISOU 1384 ND2 ASN A 283 9942 6062 8483 -304 -256 -3 N
ATOM 1385 N PHE A 284 18.304 13.277 8.100 1.00 67.86 N
ANISOU 1385 N PHE A 284 11666 5306 8811 -578 748 -112 N
ATOM 1386 CA PHE A 284 19.212 14.377 8.390 1.00 70.17 C
ANISOU 1386 CA PHE A 284 12210 5409 9043 -928 1004 -262 C
ATOM 1387 C PHE A 284 18.734 15.183 9.590 1.00 71.18 C
ANISOU 1387 C PHE A 284 12555 5340 9150 -1012 1177 -381 C
ATOM 1388 O PHE A 284 19.532 15.557 10.460 1.00 72.44 O
ANISOU 1388 O PHE A 284 12745 5533 9247 -1393 1269 -587 O
ATOM 1389 CB PHE A 284 19.354 15.252 7.161 1.00 70.59 C
ANISOU 1389 CB PHE A 284 12564 5182 9073 -869 1224 -154 C
ATOM 1390 CG PHE A 284 20.519 14.890 6.324 1.00 71.40 C
ANISOU 1390 CG PHE A 284 12528 5451 9150 -1064 1169 -168 C
ATOM 1391 CD1 PHE A 284 21.791 15.307 6.675 1.00 72.14 C
ANISOU 1391 CD1 PHE A 284 12642 5594 9176 -1511 1289 -358 C
ATOM 1392 CD2 PHE A 284 20.357 14.080 5.207 1.00 70.71 C
ANISOU 1392 CD2 PHE A 284 12264 5510 9092 -816 993 -3 C
ATOM 1393 CE1 PHE A 284 22.894 14.951 5.899 1.00 74.21 C
ANISOU 1393 CE1 PHE A 284 12746 6046 9404 -1685 1240 -369 C
ATOM 1394 CE2 PHE A 284 21.463 13.715 4.408 1.00 70.19 C
ANISOU 1394 CE2 PHE A 284 12066 5604 8998 -986 951 -16 C
ATOM 1395 CZ PHE A 284 22.730 14.150 4.759 1.00 70.28 C
ANISOU 1395 CZ PHE A 284 12090 5665 8948 -1408 1073 -192 C
ATOM 1396 N ILE A 285 17.428 15.440 9.666 1.00 70.11 N
ANISOU 1396 N ILE A 285 12557 5030 9053 -662 1224 -259 N
ATOM 1397 CA ILE A 285 16.857 16.058 10.857 1.00 70.33 C
ANISOU 1397 CA ILE A 285 12760 4897 9067 -693 1368 -364 C
ATOM 1398 C ILE A 285 17.149 15.214 12.095 1.00 71.88 C
ANISOU 1398 C ILE A 285 12644 5413 9254 -901 1157 -520 C
ATOM 1399 O ILE A 285 17.492 15.747 13.161 1.00 72.86 O
ANISOU 1399 O ILE A 285 12877 5487 9319 -1188 1286 -711 O
ATOM 1400 CB ILE A 285 15.348 16.272 10.655 1.00 70.18 C
ANISOU 1400 CB ILE A 285 12858 4724 9085 -219 1409 -174 C
ATOM 1401 CG1 ILE A 285 15.114 17.024 9.334 1.00 70.01 C
ANISOU 1401 CG1 ILE A 285 13114 4439 9048 26 1599 16 C
ATOM 1402 CG2 ILE A 285 14.732 16.984 11.865 1.00 69.77 C
ANISOU 1402 CG2 ILE A 285 13018 4475 9015 -226 1593 -278 C
ATOM 1403 CD1 ILE A 285 13.656 17.060 8.888 1.00 68.38 C
ANISOU 1403 CD1 ILE A 285 12930 4201 8852 550 1587 247 C
ATOM 1404 N PHE A 286 17.026 13.887 11.976 1.00 70.01 N
ANISOU 1404 N PHE A 286 12031 5510 9062 -764 848 -443 N
ATOM 1405 CA PHE A 286 17.314 13.016 13.112 1.00 70.23 C
ANISOU 1405 CA PHE A 286 11768 5847 9071 -922 653 -560 C
ATOM 1406 C PHE A 286 18.776 13.127 13.532 1.00 72.76 C
ANISOU 1406 C PHE A 286 12010 6335 9302 -1357 677 -743 C
ATOM 1407 O PHE A 286 19.085 13.125 14.730 1.00 73.51 O
ANISOU 1407 O PHE A 286 12029 6572 9328 -1586 666 -901 O
ATOM 1408 CB PHE A 286 16.965 11.565 12.778 1.00 68.65 C
ANISOU 1408 CB PHE A 286 11226 5930 8927 -692 357 -431 C
ATOM 1409 CG PHE A 286 15.502 11.257 12.852 1.00 68.10 C
ANISOU 1409 CG PHE A 286 11139 5821 8913 -346 292 -311 C
ATOM 1410 CD1 PHE A 286 14.620 12.127 13.481 1.00 71.52 C
ANISOU 1410 CD1 PHE A 286 11794 6037 9342 -248 461 -331 C
ATOM 1411 CD2 PHE A 286 15.003 10.095 12.291 1.00 66.42 C
ANISOU 1411 CD2 PHE A 286 10689 5801 8745 -127 77 -185 C
ATOM 1412 CE1 PHE A 286 13.256 11.836 13.543 1.00 71.91 C
ANISOU 1412 CE1 PHE A 286 11792 6102 9428 78 401 -215 C
ATOM 1413 CE2 PHE A 286 13.646 9.791 12.352 1.00 68.09 C
ANISOU 1413 CE2 PHE A 286 10855 6028 8988 157 18 -88 C
ATOM 1414 CZ PHE A 286 12.771 10.658 12.979 1.00 69.37 C
ANISOU 1414 CZ PHE A 286 11203 6013 9143 267 171 -98 C
ATOM 1415 N LEU A 287 19.695 13.199 12.561 1.00 74.18 N
ANISOU 1415 N LEU A 287 12181 6542 9464 -1479 705 -725 N
ATOM 1416 CA LEU A 287 21.110 13.307 12.903 1.00 73.91 C
ANISOU 1416 CA LEU A 287 12034 6725 9324 -1900 729 -898 C
ATOM 1417 C LEU A 287 21.376 14.585 13.673 1.00 73.72 C
ANISOU 1417 C LEU A 287 12305 6498 9208 -2245 1007 -1104 C
ATOM 1418 O LEU A 287 22.017 14.565 14.733 1.00 74.87 O
ANISOU 1418 O LEU A 287 12318 6884 9247 -2564 985 -1289 O
ATOM 1419 CB LEU A 287 21.961 13.222 11.633 1.00 73.63 C
ANISOU 1419 CB LEU A 287 11956 6732 9286 -1949 735 -833 C
ATOM 1420 CG LEU A 287 23.486 13.368 11.724 1.00 73.18 C
ANISOU 1420 CG LEU A 287 11766 6930 9110 -2376 774 -993 C
ATOM 1421 CD1 LEU A 287 24.093 12.704 12.945 1.00 73.87 C
ANISOU 1421 CD1 LEU A 287 11521 7444 9101 -2570 609 -1122 C
ATOM 1422 CD2 LEU A 287 24.113 12.763 10.484 1.00 70.39 C
ANISOU 1422 CD2 LEU A 287 11248 6714 8781 -2287 677 -872 C
ATOM 1423 N PHE A 288 20.850 15.706 13.162 1.00 76.20 N
ANISOU 1423 N PHE A 288 13035 6368 9549 -2175 1284 -1070 N
ATOM 1424 CA PHE A 288 21.010 16.993 13.826 1.00 75.68 C
ANISOU 1424 CA PHE A 288 13334 6023 9397 -2491 1606 -1264 C
ATOM 1425 C PHE A 288 20.402 16.964 15.225 1.00 75.03 C
ANISOU 1425 C PHE A 288 13233 5986 9289 -2508 1582 -1376 C
ATOM 1426 O PHE A 288 20.896 17.639 16.131 1.00 77.75 O
ANISOU 1426 O PHE A 288 13708 6314 9517 -2901 1752 -1610 O
ATOM 1427 CB PHE A 288 20.384 18.116 12.979 1.00 75.36 C
ANISOU 1427 CB PHE A 288 13775 5458 9399 -2303 1921 -1154 C
ATOM 1428 CG PHE A 288 20.623 19.525 13.529 1.00 75.61 C
ANISOU 1428 CG PHE A 288 14132 5278 9317 -2569 2271 -1313 C
ATOM 1429 CD1 PHE A 288 21.826 20.199 13.310 1.00 72.75 C
ANISOU 1429 CD1 PHE A 288 13828 4979 8833 -2980 2443 -1455 C
ATOM 1430 CD2 PHE A 288 19.641 20.141 14.317 1.00 75.79 C
ANISOU 1430 CD2 PHE A 288 14344 5120 9334 -2388 2412 -1312 C
ATOM 1431 CE1 PHE A 288 22.028 21.475 13.834 1.00 76.66 C
ANISOU 1431 CE1 PHE A 288 14594 5334 9199 -3205 2762 -1592 C
ATOM 1432 CE2 PHE A 288 19.827 21.408 14.847 1.00 75.89 C
ANISOU 1432 CE2 PHE A 288 14628 4983 9225 -2600 2729 -1442 C
ATOM 1433 CZ PHE A 288 21.027 22.079 14.615 1.00 77.89 C
ANISOU 1433 CZ PHE A 288 14962 5282 9351 -3017 2909 -1586 C
ATOM 1434 N ASN A 289 19.307 16.221 15.420 1.00 74.85 N
ANISOU 1434 N ASN A 289 13061 6019 9360 -2104 1390 -1222 N
ATOM 1435 CA ASN A 289 18.692 16.183 16.752 1.00 77.57 C
ANISOU 1435 CA ASN A 289 13389 6407 9677 -2110 1373 -1321 C
ATOM 1436 C ASN A 289 19.478 15.282 17.707 1.00 78.25 C
ANISOU 1436 C ASN A 289 13081 6976 9675 -2364 1132 -1449 C
ATOM 1437 O ASN A 289 19.607 15.584 18.903 1.00 79.47 O
ANISOU 1437 O ASN A 289 13260 7209 9728 -2618 1194 -1636 O
ATOM 1438 CB ASN A 289 17.224 15.736 16.676 1.00 76.53 C
ANISOU 1438 CB ASN A 289 13232 6188 9660 -1611 1270 -1122 C
ATOM 1439 CG ASN A 289 16.251 16.918 16.503 1.00 79.55 C
ANISOU 1439 CG ASN A 289 14057 6099 10069 -1396 1582 -1067 C
ATOM 1440 OD1 ASN A 289 15.085 16.724 16.147 1.00 78.42 O
ANISOU 1440 OD1 ASN A 289 13916 5876 10004 -965 1538 -877 O
ATOM 1441 ND2 ASN A 289 16.748 18.156 16.729 1.00 79.29 N
ANISOU 1441 ND2 ASN A 289 14408 5763 9957 -1698 1918 -1233 N
ATOM 1442 N ILE A 290 20.019 14.174 17.199 1.00 78.13 N
ANISOU 1442 N ILE A 290 12708 7296 9682 -2290 870 -1345 N
ATOM 1443 CA ILE A 290 20.817 13.283 18.040 1.00 77.46 C
ANISOU 1443 CA ILE A 290 12245 7689 9497 -2478 651 -1429 C
ATOM 1444 C ILE A 290 22.058 14.008 18.527 1.00 79.85 C
ANISOU 1444 C ILE A 290 12569 8146 9626 -2994 792 -1672 C
ATOM 1445 O ILE A 290 22.443 13.908 19.698 1.00 82.21 O
ANISOU 1445 O ILE A 290 12717 8729 9788 -3238 744 -1828 O
ATOM 1446 CB ILE A 290 21.174 12.002 17.262 1.00 77.06 C
ANISOU 1446 CB ILE A 290 11858 7918 9504 -2263 389 -1254 C
ATOM 1447 CG1 ILE A 290 19.899 11.213 16.972 1.00 74.84 C
ANISOU 1447 CG1 ILE A 290 11537 7534 9364 -1813 248 -1053 C
ATOM 1448 CG2 ILE A 290 22.175 11.155 18.020 1.00 77.62 C
ANISOU 1448 CG2 ILE A 290 11554 8491 9449 -2442 200 -1320 C
ATOM 1449 CD1 ILE A 290 20.060 10.156 15.941 1.00 72.31 C
ANISOU 1449 CD1 ILE A 290 11006 7352 9117 -1587 64 -880 C
ATOM 1450 N VAL A 291 22.707 14.743 17.621 1.00 79.61 N
ANISOU 1450 N VAL A 291 12718 7951 9581 -3184 973 -1710 N
ATOM 1451 CA VAL A 291 23.907 15.508 17.953 1.00 81.17 C
ANISOU 1451 CA VAL A 291 12953 8287 9601 -3724 1141 -1958 C
ATOM 1452 C VAL A 291 23.560 16.663 18.881 1.00 80.72 C
ANISOU 1452 C VAL A 291 13256 7953 9461 -3997 1421 -2174 C
ATOM 1453 O VAL A 291 24.289 16.948 19.838 1.00 84.06 O
ANISOU 1453 O VAL A 291 13595 8645 9700 -4433 1467 -2414 O
ATOM 1454 CB VAL A 291 24.591 16.013 16.666 1.00 77.02 C
ANISOU 1454 CB VAL A 291 12565 7607 9090 -3844 1290 -1931 C
ATOM 1455 CG1 VAL A 291 25.828 16.821 17.007 1.00 76.58 C
ANISOU 1455 CG1 VAL A 291 12548 7712 8836 -4449 1482 -2206 C
ATOM 1456 CG2 VAL A 291 24.914 14.855 15.739 1.00 76.57 C
ANISOU 1456 CG2 VAL A 291 12165 7815 9111 -3565 1025 -1722 C
ATOM 1457 N ARG A 292 22.465 17.370 18.580 1.00 79.30 N
ANISOU 1457 N ARG A 292 13487 7243 9399 -3745 1630 -2094 N
ATOM 1458 CA ARG A 292 21.969 18.443 19.440 1.00 81.75 C
ANISOU 1458 CA ARG A 292 14110 7305 9645 -3841 1898 -2219 C
ATOM 1459 C ARG A 292 21.730 17.926 20.862 1.00 83.53 C
ANISOU 1459 C ARG A 292 14140 7806 9793 -3930 1746 -2346 C
ATOM 1460 O ARG A 292 22.186 18.527 21.843 1.00 79.44 O
ANISOU 1460 O ARG A 292 13623 7454 9108 -4250 1868 -2532 O
ATOM 1461 CB ARG A 292 20.684 19.021 18.821 1.00 81.08 C
ANISOU 1461 CB ARG A 292 14386 6709 9710 -3383 2074 -2020 C
ATOM 1462 CG ARG A 292 20.096 20.248 19.504 1.00 81.62 C
ANISOU 1462 CG ARG A 292 14788 6508 9718 -3374 2386 -2080 C
ATOM 1463 CD ARG A 292 18.604 20.441 19.172 1.00 83.64 C
ANISOU 1463 CD ARG A 292 15271 6394 10117 -2835 2459 -1863 C
ATOM 1464 NE ARG A 292 17.751 19.777 20.156 1.00 86.77 N
ANISOU 1464 NE ARG A 292 15542 6875 10553 -2674 2299 -1879 N
ATOM 1465 CZ ARG A 292 16.615 20.275 20.631 1.00 93.14 C
ANISOU 1465 CZ ARG A 292 16549 7451 11388 -2396 2444 -1821 C
ATOM 1466 NH1 ARG A 292 16.235 21.521 20.359 1.00 94.95 N
ANISOU 1466 NH1 ARG A 292 17124 7363 11590 -2278 2771 -1761 N
ATOM 1467 NH2 ARG A 292 15.864 19.530 21.439 1.00 91.46 N
ANISOU 1467 NH2 ARG A 292 16192 7341 11217 -2243 2273 -1829 N
ATOM 1468 N ILE A 293 21.036 16.785 20.981 1.00 82.50 N
ANISOU 1468 N ILE A 293 13752 7826 9766 -3561 1458 -2180 N
ATOM 1469 CA ILE A 293 20.769 16.170 22.286 1.00 83.04 C
ANISOU 1469 CA ILE A 293 13588 8202 9762 -3566 1286 -2244 C
ATOM 1470 C ILE A 293 22.052 15.636 22.917 1.00 83.98 C
ANISOU 1470 C ILE A 293 13320 8900 9690 -3938 1111 -2387 C
ATOM 1471 O ILE A 293 22.289 15.789 24.122 1.00 83.69 O
ANISOU 1471 O ILE A 293 13221 9090 9486 -4222 1124 -2581 O
ATOM 1472 CB ILE A 293 19.732 15.040 22.134 1.00 82.23 C
ANISOU 1472 CB ILE A 293 13274 8152 9818 -3037 1026 -1984 C
ATOM 1473 CG1 ILE A 293 18.452 15.582 21.480 1.00 82.88 C
ANISOU 1473 CG1 ILE A 293 13694 7734 10061 -2657 1191 -1834 C
ATOM 1474 CG2 ILE A 293 19.502 14.341 23.485 1.00 81.05 C
ANISOU 1474 CG2 ILE A 293 12881 8331 9585 -3045 850 -2037 C
ATOM 1475 CD1 ILE A 293 17.277 14.628 21.474 1.00 81.44 C
ANISOU 1475 CD1 ILE A 293 13338 7598 10007 -2188 981 -1621 C
ATOM 1476 N LEU A 294 22.870 14.941 22.125 1.00 84.37 N
ANISOU 1476 N LEU A 294 13079 9230 9746 -3909 935 -2279 N
ATOM 1477 CA LEU A 294 24.056 14.304 22.677 1.00 84.51 C
ANISOU 1477 CA LEU A 294 12676 9856 9576 -4173 746 -2366 C
ATOM 1478 C LEU A 294 25.018 15.324 23.269 1.00 86.02 C
ANISOU 1478 C LEU A 294 12957 10192 9535 -4783 956 -2683 C
ATOM 1479 O LEU A 294 25.829 14.981 24.137 1.00 87.28 O
ANISOU 1479 O LEU A 294 12789 10891 9481 -5052 829 -2810 O
ATOM 1480 CB LEU A 294 24.745 13.491 21.594 1.00 82.84 C
ANISOU 1480 CB LEU A 294 12188 9866 9421 -4013 571 -2190 C
ATOM 1481 CG LEU A 294 24.417 12.001 21.601 1.00 84.10 C
ANISOU 1481 CG LEU A 294 12011 10280 9664 -3574 258 -1948 C
ATOM 1482 CD1 LEU A 294 25.591 11.242 20.966 1.00 84.05 C
ANISOU 1482 CD1 LEU A 294 11651 10688 9596 -3586 102 -1867 C
ATOM 1483 CD2 LEU A 294 24.074 11.497 23.011 1.00 87.05 C
ANISOU 1483 CD2 LEU A 294 12221 10916 9937 -3547 131 -1987 C
ATOM 1484 N MET A 295 24.973 16.568 22.793 1.00 87.47 N
ANISOU 1484 N MET A 295 13541 9948 9745 -4940 1281 -2764 N
ATOM 1485 CA MET A 295 25.954 17.567 23.192 1.00 87.55 C
ANISOU 1485 CA MET A 295 13577 10140 9548 -5361 1505 -2945 C
ATOM 1486 C MET A 295 25.494 18.454 24.339 1.00 89.20 C
ANISOU 1486 C MET A 295 14020 10214 9658 -5493 1723 -3084 C
ATOM 1487 O MET A 295 26.332 19.160 24.922 1.00 91.07 O
ANISOU 1487 O MET A 295 14231 10693 9680 -5885 1886 -3260 O
ATOM 1488 CB MET A 295 26.330 18.460 22.008 1.00 85.33 C
ANISOU 1488 CB MET A 295 13574 9535 9315 -5440 1761 -2921 C
ATOM 1489 CG MET A 295 27.291 17.806 21.048 1.00 89.86 C
ANISOU 1489 CG MET A 295 13856 10401 9884 -5501 1598 -2860 C
ATOM 1490 SD MET A 295 28.432 18.986 20.288 1.00 97.69 S
ANISOU 1490 SD MET A 295 15014 11359 10744 -5879 1916 -2968 S
ATOM 1491 CE MET A 295 29.945 18.011 20.152 1.00 94.55 C
ANISOU 1491 CE MET A 295 14014 11731 10179 -6113 1644 -3004 C
ATOM 1492 N THR A 296 24.196 18.474 24.658 1.00 89.78 N
ANISOU 1492 N THR A 296 14328 9912 9872 -5186 1752 -3014 N
ATOM 1493 CA THR A 296 23.692 19.328 25.730 1.00 90.22 C
ANISOU 1493 CA THR A 296 14622 9816 9842 -5289 1974 -3139 C
ATOM 1494 C THR A 296 23.167 18.507 26.898 1.00 91.72 C
ANISOU 1494 C THR A 296 14592 10263 9994 -5193 1748 -3161 C
ATOM 1495 O THR A 296 23.742 18.557 27.987 1.00 92.84 O
ANISOU 1495 O THR A 296 14545 10807 9925 -5488 1729 -3314 O
ATOM 1496 CB THR A 296 22.593 20.268 25.213 1.00 87.75 C
ANISOU 1496 CB THR A 296 14807 8842 9690 -5012 2265 -3043 C
ATOM 1497 OG1 THR A 296 21.510 19.498 24.676 1.00 81.43 O
ANISOU 1497 OG1 THR A 296 14022 7802 9113 -4534 2092 -2840 O
ATOM 1498 CG2 THR A 296 23.120 21.213 24.154 1.00 87.62 C
ANISOU 1498 CG2 THR A 296 15046 8572 9673 -5123 2530 -3026 C
ATOM 1499 N LYS A 297 22.125 17.694 26.697 1.00 89.38 N
ANISOU 1499 N LYS A 297 14296 9785 9881 -4791 1570 -3010 N
ATOM 1500 CA LYS A 297 21.473 17.053 27.834 1.00 90.37 C
ANISOU 1500 CA LYS A 297 14288 10080 9966 -4688 1410 -3035 C
ATOM 1501 C LYS A 297 22.179 15.763 28.215 1.00 92.84 C
ANISOU 1501 C LYS A 297 14108 11006 10159 -4753 1051 -3025 C
ATOM 1502 O LYS A 297 22.431 15.513 29.401 1.00 94.24 O
ANISOU 1502 O LYS A 297 14072 11581 10154 -4907 960 -3120 O
ATOM 1503 CB LYS A 297 19.997 16.790 27.522 1.00 88.46 C
ANISOU 1503 CB LYS A 297 14275 9388 9948 -4233 1405 -2884 C
ATOM 1504 N LEU A 298 22.531 14.949 27.218 1.00 93.55 N
ANISOU 1504 N LEU A 298 13980 11217 10349 -4562 854 -2849 N
ATOM 1505 CA LEU A 298 23.268 13.714 27.438 1.00 94.57 C
ANISOU 1505 CA LEU A 298 13602 11948 10380 -4485 532 -2735 C
ATOM 1506 C LEU A 298 24.784 13.921 27.383 1.00 97.13 C
ANISOU 1506 C LEU A 298 13694 12731 10479 -4938 528 -2898 C
ATOM 1507 O LEU A 298 25.527 12.985 27.059 1.00 98.71 O
ANISOU 1507 O LEU A 298 13507 13361 10639 -4820 299 -2757 O
ATOM 1508 CB LEU A 298 22.800 12.660 26.432 1.00 94.52 C
ANISOU 1508 CB LEU A 298 13461 11848 10605 -3961 334 -2412 C
ATOM 1509 CG LEU A 298 21.364 12.154 26.682 1.00 93.70 C
ANISOU 1509 CG LEU A 298 13451 11476 10673 -3522 269 -2243 C
ATOM 1510 CD1 LEU A 298 20.948 10.992 25.762 1.00 89.54 C
ANISOU 1510 CD1 LEU A 298 12757 10926 10338 -3055 64 -1948 C
ATOM 1511 CD2 LEU A 298 21.180 11.768 28.150 1.00 96.18 C
ANISOU 1511 CD2 LEU A 298 13613 12098 10834 -3580 173 -2316 C
ATOM 1512 N ARG A 299 25.263 15.122 27.732 1.00 97.20 N
ANISOU 1512 N ARG A 299 13883 12689 10361 -5302 800 -3088 N
ATOM 1513 CA ARG A 299 26.701 15.375 27.750 1.00 99.63 C
ANISOU 1513 CA ARG A 299 13929 13471 10453 -5648 828 -3179 C
ATOM 1514 C ARG A 299 27.427 14.381 28.650 1.00105.54 C
ANISOU 1514 C ARG A 299 14162 14956 10981 -5674 550 -3158 C
ATOM 1515 O ARG A 299 28.406 13.754 28.233 1.00107.86 O
ANISOU 1515 O ARG A 299 14095 15700 11187 -5685 388 -3085 O
ATOM 1516 CB ARG A 299 26.983 16.810 28.201 1.00 97.51 C
ANISOU 1516 CB ARG A 299 13943 13048 10057 -6016 1184 -3377 C
ATOM 1517 N ALA A 300 26.944 14.199 29.881 1.00108.78 N
ANISOU 1517 N ALA A 300 14528 15506 11296 -5646 496 -3198 N
ATOM 1518 CA ALA A 300 27.627 13.391 30.885 1.00110.45 C
ANISOU 1518 CA ALA A 300 14279 16421 11266 -5665 275 -3169 C
ATOM 1519 C ALA A 300 26.982 12.025 31.130 1.00112.37 C
ANISOU 1519 C ALA A 300 14316 16811 11567 -5261 -36 -2978 C
ATOM 1520 O ALA A 300 27.360 11.346 32.094 1.00114.44 O
ANISOU 1520 O ALA A 300 14243 17610 11631 -5211 -204 -2926 O
ATOM 1521 CB ALA A 300 27.718 14.163 32.204 1.00113.78 C
ANISOU 1521 CB ALA A 300 14758 16991 11481 -5965 446 -3354 C
ATOM 1522 N SER A 301 26.029 11.601 30.298 1.00109.07 N
ANISOU 1522 N SER A 301 14095 15943 11404 -4954 -100 -2854 N
ATOM 1523 CA SER A 301 25.378 10.315 30.533 1.00111.21 C
ANISOU 1523 CA SER A 301 14191 16282 11782 -4433 -329 -2569 C
ATOM 1524 C SER A 301 26.351 9.166 30.322 1.00115.23 C
ANISOU 1524 C SER A 301 14242 17355 12185 -4245 -569 -2374 C
ATOM 1525 O SER A 301 27.163 9.175 29.392 1.00114.61 O
ANISOU 1525 O SER A 301 14050 17379 12118 -4303 -572 -2346 O
ATOM 1526 CB SER A 301 24.158 10.111 29.623 1.00106.67 C
ANISOU 1526 CB SER A 301 13901 15072 11556 -4002 -292 -2370 C
ATOM 1527 OG SER A 301 23.333 11.257 29.532 1.00102.97 O
ANISOU 1527 OG SER A 301 13872 14050 11203 -4129 -38 -2520 O
ATOM 1528 N THR A 302 26.250 8.166 31.191 1.00121.10 N
ANISOU 1528 N THR A 302 14737 18454 12820 -3998 -756 -2227 N
ATOM 1529 CA THR A 302 26.976 6.917 31.031 1.00120.52 C
ANISOU 1529 CA THR A 302 14273 18850 12669 -3692 -970 -1981 C
ATOM 1530 C THR A 302 26.036 5.724 30.915 1.00118.80 C
ANISOU 1530 C THR A 302 14097 18385 12658 -3142 -1085 -1684 C
ATOM 1531 O THR A 302 26.502 4.577 30.923 1.00120.31 O
ANISOU 1531 O THR A 302 14010 18919 12783 -2832 -1242 -1456 O
ATOM 1532 CB THR A 302 27.950 6.720 32.194 1.00125.12 C
ANISOU 1532 CB THR A 302 14471 20203 12865 -3898 -1082 -2055 C
ATOM 1533 OG1 THR A 302 28.638 5.476 32.021 1.00127.45 O
ANISOU 1533 OG1 THR A 302 14399 20945 13081 -3533 -1272 -1781 O
ATOM 1534 CG2 THR A 302 27.212 6.745 33.557 1.00124.22 C
ANISOU 1534 CG2 THR A 302 14433 20125 12638 -3925 -1089 -2122 C
ATOM 1535 N THR A 303 24.730 5.963 30.808 1.00113.90 N
ANISOU 1535 N THR A 303 13819 17187 12273 -3013 -994 -1680 N
ATOM 1536 CA THR A 303 23.794 4.876 30.574 1.00112.30 C
ANISOU 1536 CA THR A 303 13672 16725 12273 -2540 -1081 -1422 C
ATOM 1537 C THR A 303 24.183 4.142 29.296 1.00110.57 C
ANISOU 1537 C THR A 303 13365 16446 12199 -2274 -1144 -1223 C
ATOM 1538 O THR A 303 24.738 4.728 28.363 1.00110.67 O
ANISOU 1538 O THR A 303 13409 16381 12259 -2434 -1076 -1296 O
ATOM 1539 CB THR A 303 22.369 5.419 30.473 1.00112.09 C
ANISOU 1539 CB THR A 303 14014 16103 12472 -2485 -953 -1475 C
ATOM 1540 OG1 THR A 303 22.079 5.782 29.121 1.00109.68 O
ANISOU 1540 OG1 THR A 303 13904 15368 12401 -2414 -868 -1445 O
ATOM 1541 CG2 THR A 303 22.230 6.662 31.335 1.00114.88 C
ANISOU 1541 CG2 THR A 303 14534 16418 12698 -2876 -803 -1755 C
ATOM 1542 N SER A 304 23.909 2.836 29.259 1.00111.92 N
ANISOU 1542 N SER A 304 13442 16652 12430 -1872 -1259 -972 N
ATOM 1543 CA SER A 304 24.449 2.018 28.173 1.00112.02 C
ANISOU 1543 CA SER A 304 13342 16693 12529 -1620 -1317 -782 C
ATOM 1544 C SER A 304 23.918 2.450 26.802 1.00108.94 C
ANISOU 1544 C SER A 304 13198 15789 12406 -1596 -1227 -795 C
ATOM 1545 O SER A 304 24.621 2.304 25.793 1.00102.43 O
ANISOU 1545 O SER A 304 12294 15007 11620 -1558 -1233 -738 O
ATOM 1546 CB SER A 304 24.153 0.538 28.435 1.00110.97 C
ANISOU 1546 CB SER A 304 13129 16626 12410 -1199 -1414 -520 C
ATOM 1547 OG SER A 304 24.854 -0.292 27.525 1.00107.45 O
ANISOU 1547 OG SER A 304 12553 16280 11995 -961 -1456 -342 O
ATOM 1548 N GLU A 305 22.686 2.973 26.738 1.00110.11 N
ANISOU 1548 N GLU A 305 13634 15477 12727 -1601 -1140 -859 N
ATOM 1549 CA GLU A 305 22.156 3.444 25.461 1.00108.91 C
ANISOU 1549 CA GLU A 305 13708 14876 12798 -1564 -1052 -862 C
ATOM 1550 C GLU A 305 22.950 4.640 24.932 1.00107.51 C
ANISOU 1550 C GLU A 305 13578 14696 12573 -1898 -940 -1036 C
ATOM 1551 O GLU A 305 23.018 4.842 23.713 1.00105.39 O
ANISOU 1551 O GLU A 305 13405 14201 12438 -1856 -891 -1000 O
ATOM 1552 CB GLU A 305 20.667 3.802 25.591 1.00109.25 C
ANISOU 1552 CB GLU A 305 14021 14489 13000 -1482 -976 -886 C
ATOM 1553 CG GLU A 305 19.750 2.673 26.051 1.00109.24 C
ANISOU 1553 CG GLU A 305 14003 14447 13058 -1187 -1060 -731 C
ATOM 1554 CD GLU A 305 19.693 2.553 27.563 1.00111.70 C
ANISOU 1554 CD GLU A 305 14232 15012 13198 -1261 -1092 -781 C
ATOM 1555 OE1 GLU A 305 20.766 2.583 28.211 1.00117.49 O
ANISOU 1555 OE1 GLU A 305 14766 16156 13720 -1417 -1138 -832 O
ATOM 1556 OE2 GLU A 305 18.574 2.438 28.107 1.00107.37 O1-
ANISOU 1556 OE2 GLU A 305 13803 14282 12711 -1166 -1069 -772 O1-
ATOM 1557 N THR A 306 23.535 5.450 25.830 1.00106.20 N
ANISOU 1557 N THR A 306 13362 14779 12208 -2250 -885 -1236 N
ATOM 1558 CA THR A 306 24.239 6.669 25.419 1.00103.39 C
ANISOU 1558 CA THR A 306 13097 14396 11792 -2630 -739 -1436 C
ATOM 1559 C THR A 306 25.605 6.368 24.799 1.00100.59 C
ANISOU 1559 C THR A 306 12468 14422 11329 -2708 -802 -1402 C
ATOM 1560 O THR A 306 25.985 6.992 23.801 1.00 96.73 O
ANISOU 1560 O THR A 306 12084 13764 10904 -2848 -697 -1456 O
ATOM 1561 CB THR A 306 24.392 7.628 26.610 1.00106.02 C
ANISOU 1561 CB THR A 306 13484 14872 11928 -3026 -638 -1690 C
ATOM 1562 OG1 THR A 306 23.100 8.065 27.062 1.00105.50 O
ANISOU 1562 OG1 THR A 306 13713 14394 11976 -2957 -539 -1733 O
ATOM 1563 CG2 THR A 306 25.238 8.844 26.227 1.00102.67 C
ANISOU 1563 CG2 THR A 306 13152 14450 11407 -3475 -464 -1917 C
ATOM 1564 N ILE A 307 26.374 5.442 25.389 1.00105.20 N
ANISOU 1564 N ILE A 307 12700 15537 11733 -2611 -959 -1306 N
ATOM 1565 CA ILE A 307 27.666 5.064 24.804 1.00102.28 C
ANISOU 1565 CA ILE A 307 12037 15574 11252 -2628 -1020 -1247 C
ATOM 1566 C ILE A 307 27.466 4.461 23.423 1.00 96.31 C
ANISOU 1566 C ILE A 307 11360 14512 10723 -2309 -1033 -1057 C
ATOM 1567 O ILE A 307 28.233 4.733 22.492 1.00 94.90 O
ANISOU 1567 O ILE A 307 11126 14384 10546 -2416 -987 -1077 O
ATOM 1568 CB ILE A 307 28.441 4.096 25.726 1.00102.49 C
ANISOU 1568 CB ILE A 307 11670 16239 11033 -2496 -1182 -1136 C
ATOM 1569 CG1 ILE A 307 28.341 4.500 27.209 1.00103.96 C
ANISOU 1569 CG1 ILE A 307 11801 16697 11003 -2734 -1192 -1291 C
ATOM 1570 CG2 ILE A 307 29.882 3.954 25.258 1.00101.52 C
ANISOU 1570 CG2 ILE A 307 11213 16622 10738 -2586 -1220 -1121 C
ATOM 1571 CD1 ILE A 307 27.258 3.761 27.965 1.00107.34 C
ANISOU 1571 CD1 ILE A 307 12331 16949 11506 -2420 -1258 -1154 C
ATOM 1572 N GLN A 308 26.441 3.623 23.271 1.00 94.85 N
ANISOU 1572 N GLN A 308 11300 14022 10718 -1934 -1088 -880 N
ATOM 1573 CA GLN A 308 26.138 3.073 21.957 1.00 94.97 C
ANISOU 1573 CA GLN A 308 11416 13727 10940 -1659 -1090 -723 C
ATOM 1574 C GLN A 308 25.799 4.189 20.970 1.00 91.92 C
ANISOU 1574 C GLN A 308 11305 12921 10699 -1841 -946 -836 C
ATOM 1575 O GLN A 308 26.309 4.210 19.843 1.00 90.45 O
ANISOU 1575 O GLN A 308 11110 12686 10570 -1826 -916 -795 O
ATOM 1576 CB GLN A 308 25.002 2.049 22.071 1.00 94.39 C
ANISOU 1576 CB GLN A 308 11448 13405 11011 -1292 -1154 -551 C
ATOM 1577 CG GLN A 308 25.454 0.595 22.404 1.00 95.11 C
ANISOU 1577 CG GLN A 308 11309 13814 11014 -977 -1268 -346 C
ATOM 1578 CD GLN A 308 26.343 -0.065 21.334 1.00 97.02 C
ANISOU 1578 CD GLN A 308 11416 14182 11267 -809 -1285 -216 C
ATOM 1579 OE1 GLN A 308 27.575 -0.001 21.405 1.00100.86 O
ANISOU 1579 OE1 GLN A 308 11646 15099 11578 -902 -1307 -228 O
ATOM 1580 NE2 GLN A 308 25.715 -0.665 20.323 1.00 93.87 N
ANISOU 1580 NE2 GLN A 308 11182 13423 11060 -576 -1266 -102 N
ATOM 1581 N ALA A 309 24.991 5.162 21.396 1.00 99.60 N
ANISOU 1581 N ALA A 309 12528 13599 11715 -2012 -838 -978 N
ATOM 1582 CA ALA A 309 24.622 6.255 20.503 1.00 96.13 C
ANISOU 1582 CA ALA A 309 12385 12740 11400 -2145 -673 -1063 C
ATOM 1583 C ALA A 309 25.857 6.985 19.982 1.00 95.13 C
ANISOU 1583 C ALA A 309 12197 12785 11164 -2471 -581 -1186 C
ATOM 1584 O ALA A 309 25.927 7.343 18.798 1.00 90.46 O
ANISOU 1584 O ALA A 309 11744 11949 10678 -2462 -496 -1156 O
ATOM 1585 CB ALA A 309 23.681 7.224 21.223 1.00 94.81 C
ANISOU 1585 CB ALA A 309 12492 12277 11255 -2280 -544 -1203 C
ATOM 1586 N ARG A 310 26.838 7.220 20.856 1.00 91.19 N
ANISOU 1586 N ARG A 310 11481 12731 10436 -2775 -591 -1328 N
ATOM 1587 CA ARG A 310 28.048 7.918 20.440 1.00 89.56 C
ANISOU 1587 CA ARG A 310 11187 12748 10096 -3138 -496 -1468 C
ATOM 1588 C ARG A 310 28.820 7.111 19.398 1.00 88.05 C
ANISOU 1588 C ARG A 310 10771 12753 9931 -2941 -586 -1305 C
ATOM 1589 O ARG A 310 29.341 7.676 18.431 1.00 86.50 O
ANISOU 1589 O ARG A 310 10648 12458 9758 -3104 -475 -1352 O
ATOM 1590 CB ARG A 310 28.922 8.225 21.659 1.00 87.85 C
ANISOU 1590 CB ARG A 310 10729 13056 9593 -3507 -509 -1657 C
ATOM 1591 N LYS A 311 28.906 5.788 19.578 1.00 87.21 N
ANISOU 1591 N LYS A 311 10411 12908 9816 -2586 -767 -1109 N
ATOM 1592 CA LYS A 311 29.630 4.946 18.626 1.00 84.74 C
ANISOU 1592 CA LYS A 311 9898 12776 9522 -2363 -837 -946 C
ATOM 1593 C LYS A 311 28.969 4.971 17.251 1.00 84.15 C
ANISOU 1593 C LYS A 311 10094 12192 9688 -2177 -773 -851 C
ATOM 1594 O LYS A 311 29.661 4.972 16.220 1.00 83.14 O
ANISOU 1594 O LYS A 311 9910 12108 9572 -2192 -736 -818 O
ATOM 1595 CB LYS A 311 29.726 3.512 19.154 1.00 86.86 C
ANISOU 1595 CB LYS A 311 9910 13356 9736 -1985 -1005 -745 C
ATOM 1596 N ALA A 312 27.631 5.007 17.217 1.00 83.64 N
ANISOU 1596 N ALA A 312 10308 11673 9798 -2004 -757 -808 N
ATOM 1597 CA ALA A 312 26.908 5.109 15.952 1.00 82.26 C
ANISOU 1597 CA ALA A 312 10385 11045 9823 -1836 -698 -723 C
ATOM 1598 C ALA A 312 27.223 6.417 15.217 1.00 81.69 C
ANISOU 1598 C ALA A 312 10514 10766 9758 -2135 -517 -854 C
ATOM 1599 O ALA A 312 27.596 6.407 14.033 1.00 81.00 O
ANISOU 1599 O ALA A 312 10452 10600 9725 -2092 -478 -792 O
ATOM 1600 CB ALA A 312 25.412 4.979 16.215 1.00 79.49 C
ANISOU 1600 CB ALA A 312 10255 10331 9618 -1624 -714 -669 C
ATOM 1601 N VAL A 313 27.105 7.553 15.912 1.00 80.20 N
ANISOU 1601 N VAL A 313 10490 10481 9503 -2448 -385 -1037 N
ATOM 1602 CA VAL A 313 27.228 8.859 15.263 1.00 79.77 C
ANISOU 1602 CA VAL A 313 10714 10130 9462 -2722 -166 -1158 C
ATOM 1603 C VAL A 313 28.630 9.057 14.691 1.00 81.05 C
ANISOU 1603 C VAL A 313 10702 10592 9504 -2985 -117 -1224 C
ATOM 1604 O VAL A 313 28.811 9.734 13.667 1.00 78.86 O
ANISOU 1604 O VAL A 313 10618 10070 9274 -3089 33 -1237 O
ATOM 1605 CB VAL A 313 26.840 9.979 16.251 1.00 79.75 C
ANISOU 1605 CB VAL A 313 10943 9964 9395 -3014 -8 -1355 C
ATOM 1606 CG1 VAL A 313 27.562 11.279 15.938 1.00 78.35 C
ANISOU 1606 CG1 VAL A 313 10959 9686 9126 -3453 237 -1546 C
ATOM 1607 CG2 VAL A 313 25.339 10.206 16.225 1.00 79.24 C
ANISOU 1607 CG2 VAL A 313 11188 9424 9497 -2746 41 -1278 C
ATOM 1608 N LYS A 314 29.648 8.512 15.360 1.00 80.41 N
ANISOU 1608 N LYS A 314 10246 11062 9244 -3101 -231 -1265 N
ATOM 1609 CA LYS A 314 30.978 8.519 14.767 1.00 80.78 C
ANISOU 1609 CA LYS A 314 10060 11462 9169 -3294 -209 -1298 C
ATOM 1610 C LYS A 314 31.024 7.644 13.510 1.00 82.64 C
ANISOU 1610 C LYS A 314 10236 11625 9536 -2933 -286 -1085 C
ATOM 1611 O LYS A 314 31.586 8.047 12.483 1.00 81.25 O
ANISOU 1611 O LYS A 314 10111 11391 9369 -3054 -180 -1097 O
ATOM 1612 CB LYS A 314 32.000 8.070 15.809 1.00 79.84 C
ANISOU 1612 CB LYS A 314 9517 12011 8808 -3446 -326 -1366 C
ATOM 1613 N ALA A 315 30.418 6.451 13.568 1.00 81.39 N
ANISOU 1613 N ALA A 315 9995 11454 9476 -2505 -451 -897 N
ATOM 1614 CA ALA A 315 30.437 5.531 12.430 1.00 79.78 C
ANISOU 1614 CA ALA A 315 9746 11185 9383 -2168 -515 -708 C
ATOM 1615 C ALA A 315 29.615 6.071 11.259 1.00 80.59 C
ANISOU 1615 C ALA A 315 10201 10759 9662 -2097 -408 -668 C
ATOM 1616 O ALA A 315 30.073 6.074 10.111 1.00 80.83 O
ANISOU 1616 O ALA A 315 10245 10747 9721 -2078 -356 -618 O
ATOM 1617 CB ALA A 315 29.919 4.160 12.867 1.00 78.14 C
ANISOU 1617 CB ALA A 315 9414 11054 9223 -1766 -682 -539 C
ATOM 1618 N THR A 316 28.394 6.539 11.540 1.00 80.60 N
ANISOU 1618 N THR A 316 10480 10375 9768 -2044 -369 -682 N
ATOM 1619 CA THR A 316 27.544 7.153 10.518 1.00 78.76 C
ANISOU 1619 CA THR A 316 10580 9671 9673 -1959 -259 -635 C
ATOM 1620 C THR A 316 28.222 8.346 9.853 1.00 79.49 C
ANISOU 1620 C THR A 316 10833 9654 9715 -2276 -57 -740 C
ATOM 1621 O THR A 316 27.966 8.627 8.676 1.00 78.46 O
ANISOU 1621 O THR A 316 10894 9251 9665 -2180 24 -660 O
ATOM 1622 CB THR A 316 26.213 7.615 11.144 1.00 78.09 C
ANISOU 1622 CB THR A 316 10742 9261 9669 -1881 -226 -652 C
ATOM 1623 OG1 THR A 316 25.431 6.485 11.584 1.00 72.60 O
ANISOU 1623 OG1 THR A 316 9935 8613 9037 -1572 -398 -540 O
ATOM 1624 CG2 THR A 316 25.394 8.430 10.136 1.00 76.91 C
ANISOU 1624 CG2 THR A 316 10935 8662 9625 -1796 -84 -599 C
ATOM 1625 N LEU A 317 29.048 9.090 10.594 1.00 78.06 N
ANISOU 1625 N LEU A 317 10596 9677 9388 -2671 41 -926 N
ATOM 1626 CA LEU A 317 29.727 10.218 9.977 1.00 78.12 C
ANISOU 1626 CA LEU A 317 10775 9574 9334 -3017 262 -1042 C
ATOM 1627 C LEU A 317 30.774 9.768 8.969 1.00 81.04 C
ANISOU 1627 C LEU A 317 10935 10194 9664 -3022 237 -981 C
ATOM 1628 O LEU A 317 31.127 10.535 8.058 1.00 82.09 O
ANISOU 1628 O LEU A 317 11254 10143 9793 -3196 414 -1010 O
ATOM 1629 CB LEU A 317 30.368 11.106 11.031 1.00 79.51 C
ANISOU 1629 CB LEU A 317 10940 9930 9339 -3492 387 -1284 C
ATOM 1630 CG LEU A 317 29.364 11.863 11.907 1.00 79.97 C
ANISOU 1630 CG LEU A 317 11302 9652 9429 -3551 492 -1376 C
ATOM 1631 CD1 LEU A 317 30.081 12.977 12.679 1.00 77.16 C
ANISOU 1631 CD1 LEU A 317 11029 9395 8893 -4106 695 -1650 C
ATOM 1632 CD2 LEU A 317 28.176 12.386 11.081 1.00 77.27 C
ANISOU 1632 CD2 LEU A 317 11380 8719 9262 -3292 618 -1253 C
ATOM 1633 N VAL A 318 31.291 8.546 9.125 1.00 81.60 N
ANISOU 1633 N VAL A 318 10633 10675 9695 -2827 41 -892 N
ATOM 1634 CA VAL A 318 32.290 8.013 8.199 1.00 83.25 C
ANISOU 1634 CA VAL A 318 10621 11148 9862 -2786 17 -822 C
ATOM 1635 C VAL A 318 31.621 7.350 6.993 1.00 83.23 C
ANISOU 1635 C VAL A 318 10747 10854 10022 -2394 -33 -627 C
ATOM 1636 O VAL A 318 31.987 7.583 5.837 1.00 82.74 O
ANISOU 1636 O VAL A 318 10764 10696 9978 -2419 59 -591 O
ATOM 1637 CB VAL A 318 33.213 7.028 8.943 1.00 82.74 C
ANISOU 1637 CB VAL A 318 10102 11680 9656 -2734 -142 -806 C
ATOM 1638 CG1 VAL A 318 34.213 6.395 7.979 1.00 83.95 C
ANISOU 1638 CG1 VAL A 318 10018 12112 9765 -2632 -160 -715 C
ATOM 1639 CG2 VAL A 318 33.932 7.720 10.097 1.00 79.96 C
ANISOU 1639 CG2 VAL A 318 9590 11689 9104 -3159 -96 -1013 C
ATOM 1640 N LEU A 319 30.625 6.510 7.243 1.00 83.01 N
ANISOU 1640 N LEU A 319 10743 10697 10102 -2047 -174 -509 N
ATOM 1641 CA LEU A 319 29.945 5.815 6.154 1.00 83.64 C
ANISOU 1641 CA LEU A 319 10928 10538 10311 -1704 -226 -345 C
ATOM 1642 C LEU A 319 29.206 6.778 5.216 1.00 82.69 C
ANISOU 1642 C LEU A 319 11168 9975 10276 -1724 -87 -329 C
ATOM 1643 O LEU A 319 29.033 6.482 4.027 1.00 81.77 O
ANISOU 1643 O LEU A 319 11126 9727 10216 -1548 -83 -221 O
ATOM 1644 CB LEU A 319 28.997 4.768 6.754 1.00 78.58 C
ANISOU 1644 CB LEU A 319 10245 9864 9746 -1389 -385 -251 C
ATOM 1645 CG LEU A 319 28.275 3.802 5.815 1.00 81.02 C
ANISOU 1645 CG LEU A 319 10620 9999 10164 -1047 -458 -101 C
ATOM 1646 CD1 LEU A 319 29.172 2.642 5.377 1.00 80.90 C
ANISOU 1646 CD1 LEU A 319 10369 10265 10106 -890 -516 -20 C
ATOM 1647 CD2 LEU A 319 27.029 3.268 6.516 1.00 79.74 C
ANISOU 1647 CD2 LEU A 319 10526 9692 10079 -849 -556 -59 C
ATOM 1648 N LEU A 320 28.730 7.907 5.731 1.00 82.72 N
ANISOU 1648 N LEU A 320 11407 9744 10279 -1913 37 -424 N
ATOM 1649 CA LEU A 320 27.874 8.773 4.921 1.00 81.51 C
ANISOU 1649 CA LEU A 320 11615 9154 10201 -1849 175 -371 C
ATOM 1650 C LEU A 320 28.615 9.358 3.724 1.00 82.51 C
ANISOU 1650 C LEU A 320 11847 9214 10290 -1991 329 -362 C
ATOM 1651 O LEU A 320 28.101 9.260 2.595 1.00 82.68 O
ANISOU 1651 O LEU A 320 12009 9035 10372 -1768 338 -229 O
ATOM 1652 CB LEU A 320 27.257 9.849 5.828 1.00 80.42 C
ANISOU 1652 CB LEU A 320 11722 8776 10059 -2005 304 -475 C
ATOM 1653 CG LEU A 320 26.026 10.685 5.422 1.00 77.92 C
ANISOU 1653 CG LEU A 320 11784 8002 9820 -1842 435 -400 C
ATOM 1654 CD1 LEU A 320 24.882 9.859 4.846 1.00 74.96 C
ANISOU 1654 CD1 LEU A 320 11394 7544 9545 -1420 279 -221 C
ATOM 1655 CD2 LEU A 320 25.507 11.434 6.646 1.00 76.72 C
ANISOU 1655 CD2 LEU A 320 11791 7706 9653 -1972 528 -517 C
ATOM 1656 N PRO A 321 29.797 9.961 3.874 1.00 81.36 N
ANISOU 1656 N PRO A 321 11637 9244 10032 -2362 455 -499 N
ATOM 1657 CA PRO A 321 30.542 10.369 2.668 1.00 84.69 C
ANISOU 1657 CA PRO A 321 12132 9632 10415 -2486 595 -480 C
ATOM 1658 C PRO A 321 30.906 9.193 1.755 1.00 84.59 C
ANISOU 1658 C PRO A 321 11882 9833 10424 -2232 449 -350 C
ATOM 1659 O PRO A 321 30.855 9.327 0.525 1.00 84.81 O
ANISOU 1659 O PRO A 321 12054 9693 10476 -2138 520 -255 O
ATOM 1660 CB PRO A 321 31.781 11.080 3.250 1.00 86.40 C
ANISOU 1660 CB PRO A 321 12247 10096 10484 -2971 734 -682 C
ATOM 1661 CG PRO A 321 31.381 11.486 4.638 1.00 83.54 C
ANISOU 1661 CG PRO A 321 11929 9716 10096 -3120 740 -811 C
ATOM 1662 CD PRO A 321 30.484 10.370 5.110 1.00 82.54 C
ANISOU 1662 CD PRO A 321 11656 9638 10067 -2716 494 -688 C
ATOM 1663 N LEU A 322 31.250 8.032 2.324 1.00 85.75 N
ANISOU 1663 N LEU A 322 11690 10337 10556 -2101 260 -335 N
ATOM 1664 CA LEU A 322 31.590 6.864 1.513 1.00 84.24 C
ANISOU 1664 CA LEU A 322 11301 10325 10381 -1844 148 -215 C
ATOM 1665 C LEU A 322 30.442 6.462 0.600 1.00 85.14 C
ANISOU 1665 C LEU A 322 11617 10124 10609 -1514 97 -71 C
ATOM 1666 O LEU A 322 30.629 6.247 -0.611 1.00 88.83 O
ANISOU 1666 O LEU A 322 12124 10547 11079 -1417 130 8 O
ATOM 1667 CB LEU A 322 31.972 5.693 2.416 1.00 83.75 C
ANISOU 1667 CB LEU A 322 10898 10640 10284 -1709 -23 -204 C
ATOM 1668 CG LEU A 322 33.458 5.371 2.414 1.00 84.32 C
ANISOU 1668 CG LEU A 322 10639 11177 10223 -1843 -12 -244 C
ATOM 1669 CD1 LEU A 322 33.772 4.349 3.449 1.00 83.95 C
ANISOU 1669 CD1 LEU A 322 10281 11497 10119 -1690 -161 -218 C
ATOM 1670 CD2 LEU A 322 33.816 4.842 1.043 1.00 88.03 C
ANISOU 1670 CD2 LEU A 322 11099 11635 10714 -1674 14 -140 C
ATOM 1671 N LEU A 323 29.253 6.317 1.181 1.00 83.64 N
ANISOU 1671 N LEU A 323 11533 9750 10495 -1345 14 -39 N
ATOM 1672 CA LEU A 323 28.071 5.950 0.419 1.00 82.21 C
ANISOU 1672 CA LEU A 323 11514 9324 10397 -1053 -43 84 C
ATOM 1673 C LEU A 323 27.505 7.142 -0.340 1.00 82.17 C
ANISOU 1673 C LEU A 323 11830 8988 10400 -1087 110 120 C
ATOM 1674 O LEU A 323 26.833 6.966 -1.360 1.00 81.30 O
ANISOU 1674 O LEU A 323 11837 8739 10314 -878 95 233 O
ATOM 1675 CB LEU A 323 27.028 5.359 1.364 1.00 81.75 C
ANISOU 1675 CB LEU A 323 11426 9234 10401 -878 -179 98 C
ATOM 1676 CG LEU A 323 27.442 4.151 2.216 1.00 80.53 C
ANISOU 1676 CG LEU A 323 10994 9370 10234 -801 -317 87 C
ATOM 1677 CD1 LEU A 323 26.265 3.660 3.027 1.00 78.73 C
ANISOU 1677 CD1 LEU A 323 10793 9053 10070 -635 -425 108 C
ATOM 1678 CD2 LEU A 323 27.994 3.024 1.371 1.00 78.69 C
ANISOU 1678 CD2 LEU A 323 10619 9290 9990 -639 -365 161 C
ATOM 1679 N GLY A 324 27.748 8.355 0.150 1.00 83.60 N
ANISOU 1679 N GLY A 324 12171 9046 10547 -1344 272 29 N
ATOM 1680 CA GLY A 324 27.138 9.519 -0.467 1.00 82.23 C
ANISOU 1680 CA GLY A 324 12349 8516 10376 -1338 449 82 C
ATOM 1681 C GLY A 324 27.773 9.891 -1.794 1.00 83.52 C
ANISOU 1681 C GLY A 324 12617 8626 10490 -1397 580 137 C
ATOM 1682 O GLY A 324 27.079 10.288 -2.735 1.00 82.64 O
ANISOU 1682 O GLY A 324 12735 8282 10383 -1216 647 264 O
ATOM 1683 N ILE A 325 29.098 9.769 -1.888 1.00 85.32 N
ANISOU 1683 N ILE A 325 12666 9098 10654 -1644 619 50 N
ATOM 1684 CA ILE A 325 29.802 10.129 -3.116 1.00 86.27 C
ANISOU 1684 CA ILE A 325 12872 9190 10718 -1734 756 90 C
ATOM 1685 C ILE A 325 29.164 9.454 -4.321 1.00 85.29 C
ANISOU 1685 C ILE A 325 12776 9007 10622 -1395 662 256 C
ATOM 1686 O ILE A 325 28.718 10.120 -5.259 1.00 84.07 O
ANISOU 1686 O ILE A 325 12888 8607 10448 -1310 783 359 O
ATOM 1687 CB ILE A 325 31.287 9.757 -2.986 1.00 87.03 C
ANISOU 1687 CB ILE A 325 12667 9663 10738 -1991 756 -20 C
ATOM 1688 CG1 ILE A 325 31.915 10.603 -1.888 1.00 88.14 C
ANISOU 1688 CG1 ILE A 325 12802 9875 10812 -2386 880 -201 C
ATOM 1689 CG2 ILE A 325 32.007 10.050 -4.258 1.00 89.59 C
ANISOU 1689 CG2 ILE A 325 13059 9978 11002 -2079 894 22 C
ATOM 1690 CD1 ILE A 325 31.852 12.050 -2.182 1.00 85.49 C
ANISOU 1690 CD1 ILE A 325 12855 9188 10440 -2625 1157 -241 C
ATOM 1691 N THR A 326 29.008 8.135 -4.264 1.00 86.45 N
ANISOU 1691 N THR A 326 12671 9369 10807 -1186 453 287 N
ATOM 1692 CA THR A 326 28.600 7.374 -5.443 1.00 85.77 C
ANISOU 1692 CA THR A 326 12580 9287 10722 -926 372 408 C
ATOM 1693 C THR A 326 27.264 7.898 -5.996 1.00 82.69 C
ANISOU 1693 C THR A 326 12457 8620 10341 -714 392 529 C
ATOM 1694 O THR A 326 26.975 7.749 -7.192 1.00 81.83 O
ANISOU 1694 O THR A 326 12426 8475 10191 -561 395 634 O
ATOM 1695 CB THR A 326 28.546 5.851 -5.090 1.00 84.06 C
ANISOU 1695 CB THR A 326 12090 9305 10544 -751 170 402 C
ATOM 1696 OG1 THR A 326 27.842 5.096 -6.082 1.00 79.34 O
ANISOU 1696 OG1 THR A 326 11526 8674 9947 -504 88 497 O
ATOM 1697 CG2 THR A 326 27.790 5.608 -3.776 1.00 82.60 C
ANISOU 1697 CG2 THR A 326 11853 9110 10422 -693 57 362 C
ATOM 1698 N TYR A 327 26.436 8.513 -5.144 1.00 81.09 N
ANISOU 1698 N TYR A 327 12386 8247 10177 -690 409 521 N
ATOM 1699 CA TYR A 327 25.132 9.007 -5.587 1.00 81.03 C
ANISOU 1699 CA TYR A 327 12602 8022 10164 -448 429 651 C
ATOM 1700 C TYR A 327 25.226 10.360 -6.291 1.00 83.49 C
ANISOU 1700 C TYR A 327 13240 8071 10412 -501 672 727 C
ATOM 1701 O TYR A 327 24.519 10.600 -7.277 1.00 82.67 O
ANISOU 1701 O TYR A 327 13287 7869 10254 -273 700 879 O
ATOM 1702 CB TYR A 327 24.177 9.068 -4.399 1.00 75.36 C
ANISOU 1702 CB TYR A 327 11888 7239 9506 -365 360 623 C
ATOM 1703 CG TYR A 327 23.613 7.714 -4.067 1.00 73.84 C
ANISOU 1703 CG TYR A 327 11448 7251 9358 -204 127 614 C
ATOM 1704 CD1 TYR A 327 24.112 6.971 -3.009 1.00 75.72 C
ANISOU 1704 CD1 TYR A 327 11466 7660 9642 -316 25 500 C
ATOM 1705 CD2 TYR A 327 22.584 7.167 -4.829 1.00 73.40 C
ANISOU 1705 CD2 TYR A 327 11382 7229 9278 53 20 721 C
ATOM 1706 CE1 TYR A 327 23.603 5.716 -2.715 1.00 71.94 C
ANISOU 1706 CE1 TYR A 327 10802 7333 9200 -170 -156 499 C
ATOM 1707 CE2 TYR A 327 22.053 5.900 -4.541 1.00 66.94 C
ANISOU 1707 CE2 TYR A 327 10364 6581 8490 162 -167 695 C
ATOM 1708 CZ TYR A 327 22.569 5.171 -3.492 1.00 70.17 C
ANISOU 1708 CZ TYR A 327 10594 7109 8959 54 -244 588 C
ATOM 1709 OH TYR A 327 22.053 3.890 -3.222 1.00 68.77 O
ANISOU 1709 OH TYR A 327 10258 7065 8805 160 -397 568 O
ATOM 1710 N MET A 328 26.072 11.261 -5.796 1.00 82.35 N
ANISOU 1710 N MET A 328 13216 7818 10256 -802 863 624 N
ATOM 1711 CA MET A 328 26.315 12.499 -6.524 1.00 84.56 C
ANISOU 1711 CA MET A 328 13833 7830 10467 -891 1132 688 C
ATOM 1712 C MET A 328 27.074 12.241 -7.834 1.00 87.27 C
ANISOU 1712 C MET A 328 14136 8279 10743 -919 1163 746 C
ATOM 1713 O MET A 328 26.797 12.892 -8.845 1.00 88.85 O
ANISOU 1713 O MET A 328 14593 8290 10875 -799 1307 888 O
ATOM 1714 CB MET A 328 27.053 13.505 -5.632 1.00 86.08 C
ANISOU 1714 CB MET A 328 14176 7880 10651 -1266 1352 531 C
ATOM 1715 CG MET A 328 26.649 14.980 -5.858 1.00 91.73 C
ANISOU 1715 CG MET A 328 15365 8168 11321 -1272 1663 606 C
ATOM 1716 SD MET A 328 25.462 15.695 -4.688 1.00 98.18 S
ANISOU 1716 SD MET A 328 16416 8702 12185 -1137 1740 605 S
ATOM 1717 CE MET A 328 26.556 16.181 -3.347 1.00 91.47 C
ANISOU 1717 CE MET A 328 15546 7878 11331 -1681 1875 314 C
ATOM 1718 N LEU A 329 28.032 11.300 -7.845 1.00 90.56 N
ANISOU 1718 N LEU A 329 14240 9002 11167 -1055 1042 649 N
ATOM 1719 CA LEU A 329 28.724 10.946 -9.090 1.00 92.17 C
ANISOU 1719 CA LEU A 329 14386 9327 11306 -1058 1063 701 C
ATOM 1720 C LEU A 329 27.767 10.487 -10.178 1.00 92.63 C
ANISOU 1720 C LEU A 329 14497 9368 11332 -708 961 871 C
ATOM 1721 O LEU A 329 28.078 10.602 -11.374 1.00 94.55 O
ANISOU 1721 O LEU A 329 14825 9605 11495 -679 1041 955 O
ATOM 1722 CB LEU A 329 29.762 9.865 -8.816 1.00 90.74 C
ANISOU 1722 CB LEU A 329 13836 9500 11139 -1184 932 584 C
ATOM 1723 CG LEU A 329 31.012 10.282 -8.069 1.00 92.91 C
ANISOU 1723 CG LEU A 329 14000 9912 11390 -1565 1046 420 C
ATOM 1724 CD1 LEU A 329 31.893 11.075 -8.995 1.00 94.83 C
ANISOU 1724 CD1 LEU A 329 14394 10093 11544 -1790 1276 423 C
ATOM 1725 CD2 LEU A 329 30.550 11.118 -6.823 1.00 98.82 C
ANISOU 1725 CD2 LEU A 329 14896 10477 12173 -1700 1114 338 C
ATOM 1726 N ALA A 330 26.605 9.962 -9.792 1.00 88.90 N
ANISOU 1726 N ALA A 330 13964 8912 10904 -457 787 916 N
ATOM 1727 CA ALA A 330 25.635 9.544 -10.793 1.00 89.83 C
ANISOU 1727 CA ALA A 330 14108 9063 10961 -152 686 1062 C
ATOM 1728 C ALA A 330 25.027 10.720 -11.548 1.00 92.79 C
ANISOU 1728 C ALA A 330 14812 9197 11245 -6 861 1232 C
ATOM 1729 O ALA A 330 24.301 10.496 -12.522 1.00 93.56 O
ANISOU 1729 O ALA A 330 14936 9361 11254 242 797 1370 O
ATOM 1730 CB ALA A 330 24.521 8.708 -10.167 1.00 86.25 C
ANISOU 1730 CB ALA A 330 13496 8716 10559 48 470 1055 C
ATOM 1731 N PHE A 331 25.290 11.957 -11.128 1.00 93.93 N
ANISOU 1731 N PHE A 331 15220 9075 11395 -148 1092 1230 N
ATOM 1732 CA PHE A 331 24.829 13.143 -11.842 1.00 94.68 C
ANISOU 1732 CA PHE A 331 15680 8897 11395 -1 1312 1408 C
ATOM 1733 C PHE A 331 25.931 13.871 -12.607 1.00 96.41 C
ANISOU 1733 C PHE A 331 16101 8986 11545 -230 1561 1416 C
ATOM 1734 O PHE A 331 25.656 14.914 -13.205 1.00 97.00 O
ANISOU 1734 O PHE A 331 16523 8798 11533 -124 1787 1571 O
ATOM 1735 CB PHE A 331 24.180 14.147 -10.870 1.00 94.22 C
ANISOU 1735 CB PHE A 331 15869 8553 11376 40 1458 1423 C
ATOM 1736 CG PHE A 331 23.060 13.578 -10.049 1.00 93.23 C
ANISOU 1736 CG PHE A 331 15572 8536 11314 258 1247 1418 C
ATOM 1737 CD1 PHE A 331 23.246 13.275 -8.713 1.00 90.63 C
ANISOU 1737 CD1 PHE A 331 15091 8249 11097 71 1168 1239 C
ATOM 1738 CD2 PHE A 331 21.807 13.371 -10.615 1.00 96.24 C
ANISOU 1738 CD2 PHE A 331 15937 9005 11624 644 1133 1596 C
ATOM 1739 CE1 PHE A 331 22.207 12.751 -7.965 1.00 91.98 C
ANISOU 1739 CE1 PHE A 331 15111 8516 11320 264 985 1237 C
ATOM 1740 CE2 PHE A 331 20.765 12.851 -9.868 1.00 96.42 C
ANISOU 1740 CE2 PHE A 331 15791 9152 11694 823 948 1585 C
ATOM 1741 CZ PHE A 331 20.963 12.540 -8.541 1.00 93.62 C
ANISOU 1741 CZ PHE A 331 15303 8804 11464 632 879 1406 C
ATOM 1742 N VAL A 332 27.169 13.383 -12.594 1.00 99.27 N
ANISOU 1742 N VAL A 332 16264 9522 11931 -533 1545 1262 N
ATOM 1743 CA VAL A 332 28.275 14.261 -12.961 1.00103.39 C
ANISOU 1743 CA VAL A 332 16986 9898 12398 -843 1822 1222 C
ATOM 1744 C VAL A 332 28.242 14.598 -14.450 1.00108.25 C
ANISOU 1744 C VAL A 332 17805 10439 12888 -692 1942 1408 C
ATOM 1745 O VAL A 332 28.257 15.776 -14.832 1.00108.39 O
ANISOU 1745 O VAL A 332 18204 10146 12833 -722 2227 1509 O
ATOM 1746 CB VAL A 332 29.617 13.631 -12.561 1.00106.54 C
ANISOU 1746 CB VAL A 332 17073 10572 12834 -1193 1767 1016 C
ATOM 1747 CG1 VAL A 332 30.729 14.121 -13.503 1.00110.57 C
ANISOU 1747 CG1 VAL A 332 17694 11068 13251 -1436 1987 1014 C
ATOM 1748 CG2 VAL A 332 29.913 13.928 -11.092 1.00100.58 C
ANISOU 1748 CG2 VAL A 332 16263 9800 12154 -1460 1796 833 C
ATOM 1749 N ASN A 333 28.186 13.572 -15.317 1.00111.98 N
ANISOU 1749 N ASN A 333 18046 11181 13319 -524 1746 1458 N
ATOM 1750 CA ASN A 333 28.375 13.761 -16.755 1.00116.26 C
ANISOU 1750 CA ASN A 333 18728 11719 13726 -434 1849 1604 C
ATOM 1751 C ASN A 333 29.757 14.357 -17.031 1.00122.07 C
ANISOU 1751 C ASN A 333 19568 12384 14430 -810 2099 1519 C
ATOM 1752 O ASN A 333 29.857 15.548 -17.356 1.00122.48 O
ANISOU 1752 O ASN A 333 19993 12132 14411 -882 2387 1609 O
ATOM 1753 CB ASN A 333 27.275 14.653 -17.336 1.00109.64 C
ANISOU 1753 CB ASN A 333 18235 10641 12783 -108 1970 1848 C
ATOM 1754 N PRO A 334 30.844 13.579 -16.903 1.00125.61 N
ANISOU 1754 N PRO A 334 19704 13107 14917 -1056 2017 1349 N
ATOM 1755 CA PRO A 334 32.188 14.193 -16.890 1.00128.25 C
ANISOU 1755 CA PRO A 334 20088 13418 15221 -1472 2256 1229 C
ATOM 1756 C PRO A 334 32.670 14.698 -18.245 1.00130.91 C
ANISOU 1756 C PRO A 334 20640 13674 15425 -1511 2466 1346 C
ATOM 1757 O PRO A 334 33.217 15.808 -18.312 1.00133.02 O
ANISOU 1757 O PRO A 334 21196 13705 15640 -1778 2769 1335 O
ATOM 1758 CB PRO A 334 33.079 13.058 -16.365 1.00129.55 C
ANISOU 1758 CB PRO A 334 19798 13974 15451 -1632 2068 1044 C
ATOM 1759 CG PRO A 334 32.386 11.819 -16.815 1.00128.52 C
ANISOU 1759 CG PRO A 334 19458 14038 15336 -1278 1794 1116 C
ATOM 1760 CD PRO A 334 30.909 12.126 -16.654 1.00126.06 C
ANISOU 1760 CD PRO A 334 19349 13509 15039 -973 1724 1252 C
ATOM 1761 N GLY A 335 32.516 13.925 -19.313 1.00128.01 N
ANISOU 1761 N GLY A 335 20154 13491 14991 -1280 2333 1445 N
ATOM 1762 CA GLY A 335 32.933 14.346 -20.640 1.00131.26 C
ANISOU 1762 CA GLY A 335 20762 13848 15263 -1294 2520 1566 C
ATOM 1763 C GLY A 335 33.789 13.301 -21.334 1.00134.62 C
ANISOU 1763 C GLY A 335 20872 14621 15655 -1351 2413 1491 C
ATOM 1764 O GLY A 335 34.170 12.279 -20.767 1.00135.21 O
ANISOU 1764 O GLY A 335 20586 14972 15816 -1393 2221 1344 O
ATOM 1765 N GLU A 336 34.098 13.598 -22.599 1.00142.05 N
ANISOU 1765 N GLU A 336 21979 15535 16460 -1336 2564 1607 N
ATOM 1766 CA GLU A 336 34.810 12.671 -23.473 1.00141.99 C
ANISOU 1766 CA GLU A 336 21729 15829 16393 -1344 2493 1567 C
ATOM 1767 C GLU A 336 36.327 12.797 -23.371 1.00145.10 C
ANISOU 1767 C GLU A 336 21979 16366 16786 -1744 2662 1409 C
ATOM 1768 O GLU A 336 37.039 12.082 -24.084 1.00143.18 O
ANISOU 1768 O GLU A 336 21535 16379 16490 -1763 2637 1373 O
ATOM 1769 CB GLU A 336 34.366 12.870 -24.927 1.00135.94 C
ANISOU 1769 CB GLU A 336 21190 15004 15456 -1119 2560 1771 C
ATOM 1770 N ASP A 337 36.829 13.677 -22.501 1.00148.41 N
ANISOU 1770 N ASP A 337 22489 16649 17250 -2071 2839 1307 N
ATOM 1771 CA ASP A 337 38.261 13.773 -22.228 1.00149.42 C
ANISOU 1771 CA ASP A 337 22418 16987 17366 -2489 2980 1128 C
ATOM 1772 C ASP A 337 38.780 12.409 -21.769 1.00149.55 C
ANISOU 1772 C ASP A 337 21936 17434 17454 -2438 2731 992 C
ATOM 1773 O ASP A 337 38.165 11.752 -20.924 1.00148.61 O
ANISOU 1773 O ASP A 337 21652 17373 17442 -2256 2500 957 O
ATOM 1774 CB ASP A 337 38.485 14.866 -21.164 1.00149.67 C
ANISOU 1774 CB ASP A 337 22619 16814 17435 -2841 3172 1016 C
ATOM 1775 CG ASP A 337 39.886 14.863 -20.551 1.00151.13 C
ANISOU 1775 CG ASP A 337 22506 17310 17608 -3300 3263 789 C
ATOM 1776 OD1 ASP A 337 40.682 13.937 -20.806 1.00152.71 O
ANISOU 1776 OD1 ASP A 337 22322 17910 17788 -3304 3152 721 O
ATOM 1777 OD2 ASP A 337 40.184 15.805 -19.781 1.00149.63 O1-
ANISOU 1777 OD2 ASP A 337 22464 16976 17413 -3660 3456 672 O1-
ATOM 1778 N GLU A 338 39.906 11.971 -22.347 1.00147.69 N
ANISOU 1778 N GLU A 338 21472 17495 17149 -2579 2792 928 N
ATOM 1779 CA GLU A 338 40.382 10.605 -22.121 1.00148.32 C
ANISOU 1779 CA GLU A 338 21113 17970 17273 -2448 2584 841 C
ATOM 1780 C GLU A 338 40.755 10.369 -20.662 1.00147.50 C
ANISOU 1780 C GLU A 338 20714 18068 17259 -2596 2482 685 C
ATOM 1781 O GLU A 338 40.304 9.398 -20.044 1.00144.63 O
ANISOU 1781 O GLU A 338 20145 17820 16986 -2350 2246 669 O
ATOM 1782 CB GLU A 338 41.577 10.300 -23.027 1.00148.56 C
ANISOU 1782 CB GLU A 338 20968 18281 17196 -2572 2711 809 C
ATOM 1783 N VAL A 339 41.598 11.237 -20.098 1.00150.18 N
ANISOU 1783 N VAL A 339 21030 18471 17560 -3015 2667 562 N
ATOM 1784 CA VAL A 339 42.093 11.019 -18.739 1.00148.24 C
ANISOU 1784 CA VAL A 339 20463 18501 17363 -3191 2578 402 C
ATOM 1785 C VAL A 339 40.965 11.177 -17.714 1.00146.09 C
ANISOU 1785 C VAL A 339 20330 17972 17204 -3064 2438 411 C
ATOM 1786 O VAL A 339 40.846 10.384 -16.770 1.00144.76 O
ANISOU 1786 O VAL A 339 19884 18009 17111 -2933 2229 354 O
ATOM 1787 CB VAL A 339 43.276 11.960 -18.443 1.00149.66 C
ANISOU 1787 CB VAL A 339 20582 18843 17438 -3725 2827 249 C
ATOM 1788 CG1 VAL A 339 44.541 11.451 -19.129 1.00150.95 C
ANISOU 1788 CG1 VAL A 339 20420 19438 17494 -3822 2896 208 C
ATOM 1789 CG2 VAL A 339 42.955 13.388 -18.873 1.00149.63 C
ANISOU 1789 CG2 VAL A 339 21085 18380 17386 -3970 3108 288 C
ATOM 1790 N SER A 340 40.127 12.211 -17.877 1.00145.18 N
ANISOU 1790 N SER A 340 20655 17410 17097 -3085 2567 490 N
ATOM 1791 CA SER A 340 39.025 12.434 -16.938 1.00141.67 C
ANISOU 1791 CA SER A 340 20361 16713 16753 -2954 2458 505 C
ATOM 1792 C SER A 340 37.991 11.307 -17.003 1.00135.74 C
ANISOU 1792 C SER A 340 19512 15973 16088 -2480 2169 612 C
ATOM 1793 O SER A 340 37.403 10.933 -15.979 1.00131.18 O
ANISOU 1793 O SER A 340 18831 15406 15605 -2367 1995 573 O
ATOM 1794 CB SER A 340 38.364 13.794 -17.208 1.00141.52 C
ANISOU 1794 CB SER A 340 20858 16206 16706 -3031 2694 593 C
ATOM 1795 OG SER A 340 39.319 14.825 -17.424 1.00142.11 O
ANISOU 1795 OG SER A 340 21092 16225 16679 -3475 3009 508 O
ATOM 1796 N ARG A 341 37.739 10.772 -18.203 1.00138.98 N
ANISOU 1796 N ARG A 341 19966 16383 16456 -2222 2126 738 N
ATOM 1797 CA ARG A 341 36.758 9.699 -18.364 1.00135.69 C
ANISOU 1797 CA ARG A 341 19474 15985 16096 -1819 1877 820 C
ATOM 1798 C ARG A 341 37.218 8.406 -17.690 1.00131.15 C
ANISOU 1798 C ARG A 341 18491 15755 15583 -1739 1685 717 C
ATOM 1799 O ARG A 341 36.426 7.740 -17.015 1.00126.43 O
ANISOU 1799 O ARG A 341 17818 15148 15073 -1529 1490 717 O
ATOM 1800 CB ARG A 341 36.471 9.463 -19.850 1.00135.95 C
ANISOU 1800 CB ARG A 341 19650 15970 16036 -1613 1900 956 C
ATOM 1801 N VAL A 342 38.490 8.021 -17.873 1.00132.89 N
ANISOU 1801 N VAL A 342 18450 16290 15750 -1886 1751 639 N
ATOM 1802 CA VAL A 342 38.960 6.740 -17.338 1.00130.46 C
ANISOU 1802 CA VAL A 342 17769 16318 15481 -1745 1594 575 C
ATOM 1803 C VAL A 342 38.907 6.740 -15.818 1.00129.69 C
ANISOU 1803 C VAL A 342 17508 16307 15460 -1826 1492 484 C
ATOM 1804 O VAL A 342 38.464 5.764 -15.198 1.00127.91 O
ANISOU 1804 O VAL A 342 17135 16158 15308 -1589 1308 486 O
ATOM 1805 CB VAL A 342 40.381 6.411 -17.831 1.00131.09 C
ANISOU 1805 CB VAL A 342 17588 16751 15469 -1869 1708 524 C
ATOM 1806 CG1 VAL A 342 41.384 7.406 -17.269 1.00133.24 C
ANISOU 1806 CG1 VAL A 342 17764 17179 15681 -2293 1872 412 C
ATOM 1807 CG2 VAL A 342 40.757 4.990 -17.420 1.00127.28 C
ANISOU 1807 CG2 VAL A 342 16763 16582 15016 -1624 1562 500 C
ATOM 1808 N VAL A 343 39.380 7.818 -15.190 1.00134.07 N
ANISOU 1808 N VAL A 343 18094 16859 15986 -2179 1624 396 N
ATOM 1809 CA VAL A 343 39.347 7.886 -13.734 1.00130.15 C
ANISOU 1809 CA VAL A 343 17448 16464 15540 -2288 1536 297 C
ATOM 1810 C VAL A 343 37.909 7.885 -13.237 1.00125.97 C
ANISOU 1810 C VAL A 343 17135 15608 15119 -2069 1400 357 C
ATOM 1811 O VAL A 343 37.589 7.228 -12.239 1.00123.08 O
ANISOU 1811 O VAL A 343 16597 15348 14820 -1940 1230 326 O
ATOM 1812 CB VAL A 343 40.128 9.114 -13.239 1.00130.72 C
ANISOU 1812 CB VAL A 343 17546 16586 15536 -2763 1736 167 C
ATOM 1813 CG1 VAL A 343 41.616 8.825 -13.265 1.00131.42 C
ANISOU 1813 CG1 VAL A 343 17254 17167 15512 -2972 1802 73 C
ATOM 1814 CG2 VAL A 343 39.800 10.320 -14.093 1.00135.49 C
ANISOU 1814 CG2 VAL A 343 18583 16792 16105 -2918 1959 220 C
ATOM 1815 N PHE A 344 37.014 8.604 -13.928 1.00119.20 N
ANISOU 1815 N PHE A 344 16650 14372 14268 -2004 1476 455 N
ATOM 1816 CA PHE A 344 35.610 8.624 -13.514 1.00116.13 C
ANISOU 1816 CA PHE A 344 16450 13709 13965 -1776 1352 524 C
ATOM 1817 C PHE A 344 35.017 7.214 -13.485 1.00114.21 C
ANISOU 1817 C PHE A 344 16029 13585 13782 -1429 1116 567 C
ATOM 1818 O PHE A 344 34.283 6.859 -12.554 1.00110.93 O
ANISOU 1818 O PHE A 344 15568 13134 13447 -1309 970 551 O
ATOM 1819 CB PHE A 344 34.781 9.540 -14.431 1.00117.55 C
ANISOU 1819 CB PHE A 344 17034 13522 14110 -1699 1477 656 C
ATOM 1820 CG PHE A 344 33.308 9.640 -14.034 1.00116.43 C
ANISOU 1820 CG PHE A 344 17071 13132 14035 -1448 1363 740 C
ATOM 1821 CD1 PHE A 344 32.908 10.418 -12.948 1.00115.40 C
ANISOU 1821 CD1 PHE A 344 17065 12825 13956 -1564 1409 688 C
ATOM 1822 CD2 PHE A 344 32.322 8.974 -14.768 1.00112.16 C
ANISOU 1822 CD2 PHE A 344 16572 12556 13489 -1111 1221 861 C
ATOM 1823 CE1 PHE A 344 31.559 10.523 -12.599 1.00111.83 C
ANISOU 1823 CE1 PHE A 344 16766 12167 13557 -1318 1315 771 C
ATOM 1824 CE2 PHE A 344 30.972 9.079 -14.423 1.00105.75 C
ANISOU 1824 CE2 PHE A 344 15892 11569 12718 -888 1119 937 C
ATOM 1825 CZ PHE A 344 30.592 9.852 -13.339 1.00106.32 C
ANISOU 1825 CZ PHE A 344 16079 11469 12850 -976 1166 900 C
ATOM 1826 N ILE A 345 35.316 6.397 -14.497 1.00116.67 N
ANISOU 1826 N ILE A 345 16257 14024 14049 -1278 1095 614 N
ATOM 1827 CA ILE A 345 34.693 5.080 -14.605 1.00112.28 C
ANISOU 1827 CA ILE A 345 15599 13529 13535 -970 913 647 C
ATOM 1828 C ILE A 345 35.241 4.106 -13.553 1.00109.95 C
ANISOU 1828 C ILE A 345 14989 13497 13289 -929 807 567 C
ATOM 1829 O ILE A 345 34.498 3.265 -13.037 1.00107.04 O
ANISOU 1829 O ILE A 345 14579 13106 12986 -725 657 574 O
ATOM 1830 CB ILE A 345 34.848 4.549 -16.045 1.00113.37 C
ANISOU 1830 CB ILE A 345 15781 13702 13591 -841 954 709 C
ATOM 1831 CG1 ILE A 345 34.035 5.418 -17.022 1.00112.19 C
ANISOU 1831 CG1 ILE A 345 15952 13296 13380 -809 1023 818 C
ATOM 1832 CG2 ILE A 345 34.448 3.086 -16.137 1.00111.94 C
ANISOU 1832 CG2 ILE A 345 15483 13612 13436 -577 808 706 C
ATOM 1833 CD1 ILE A 345 32.533 5.485 -16.740 1.00107.96 C
ANISOU 1833 CD1 ILE A 345 15572 12565 12885 -622 893 882 C
ATOM 1834 N TYR A 346 36.542 4.174 -13.237 1.00112.18 N
ANISOU 1834 N TYR A 346 15040 14058 13526 -1111 890 497 N
ATOM 1835 CA TYR A 346 37.129 3.218 -12.292 1.00110.83 C
ANISOU 1835 CA TYR A 346 14549 14188 13372 -1026 797 449 C
ATOM 1836 C TYR A 346 36.753 3.531 -10.848 1.00107.94 C
ANISOU 1836 C TYR A 346 14131 13816 13064 -1110 708 393 C
ATOM 1837 O TYR A 346 36.461 2.622 -10.059 1.00106.49 O
ANISOU 1837 O TYR A 346 13815 13716 12930 -919 575 398 O
ATOM 1838 CB TYR A 346 38.651 3.189 -12.422 1.00113.30 C
ANISOU 1838 CB TYR A 346 14587 14874 13588 -1176 910 402 C
ATOM 1839 CG TYR A 346 39.176 2.522 -13.665 1.00116.04 C
ANISOU 1839 CG TYR A 346 14903 15312 13877 -1030 984 453 C
ATOM 1840 CD1 TYR A 346 40.448 1.965 -13.682 1.00117.60 C
ANISOU 1840 CD1 TYR A 346 14785 15901 13994 -1012 1044 434 C
ATOM 1841 CD2 TYR A 346 38.406 2.448 -14.822 1.00116.20 C
ANISOU 1841 CD2 TYR A 346 15195 15054 13902 -902 997 521 C
ATOM 1842 CE1 TYR A 346 40.946 1.360 -14.816 1.00117.94 C
ANISOU 1842 CE1 TYR A 346 14808 16024 13980 -871 1130 477 C
ATOM 1843 CE2 TYR A 346 38.892 1.840 -15.961 1.00117.56 C
ANISOU 1843 CE2 TYR A 346 15349 15312 14009 -783 1074 554 C
ATOM 1844 CZ TYR A 346 40.165 1.297 -15.958 1.00119.19 C
ANISOU 1844 CZ TYR A 346 15263 15875 14151 -767 1147 530 C
ATOM 1845 OH TYR A 346 40.663 0.690 -17.094 1.00119.86 O
ANISOU 1845 OH TYR A 346 15336 16038 14166 -639 1241 561 O
ATOM 1846 N PHE A 347 36.817 4.805 -10.467 1.00105.58 N
ANISOU 1846 N PHE A 347 13945 13423 12749 -1408 802 334 N
ATOM 1847 CA PHE A 347 36.458 5.195 -9.108 1.00105.41 C
ANISOU 1847 CA PHE A 347 13899 13384 12770 -1517 737 265 C
ATOM 1848 C PHE A 347 35.003 4.844 -8.811 1.00101.61 C
ANISOU 1848 C PHE A 347 13593 12620 12392 -1266 596 328 C
ATOM 1849 O PHE A 347 34.687 4.252 -7.766 1.00 98.78 O
ANISOU 1849 O PHE A 347 13105 12346 12083 -1162 465 307 O
ATOM 1850 CB PHE A 347 36.700 6.695 -8.941 1.00106.44 C
ANISOU 1850 CB PHE A 347 14202 13385 12855 -1894 909 185 C
ATOM 1851 CG PHE A 347 36.813 7.155 -7.515 1.00105.03 C
ANISOU 1851 CG PHE A 347 13926 13309 12671 -2114 890 67 C
ATOM 1852 CD1 PHE A 347 37.984 6.970 -6.802 1.00106.37 C
ANISOU 1852 CD1 PHE A 347 13746 13923 12749 -2310 889 -37 C
ATOM 1853 CD2 PHE A 347 35.757 7.814 -6.901 1.00104.07 C
ANISOU 1853 CD2 PHE A 347 14060 12863 12618 -2128 882 58 C
ATOM 1854 CE1 PHE A 347 38.089 7.415 -5.497 1.00108.02 C
ANISOU 1854 CE1 PHE A 347 13861 14256 12927 -2536 872 -157 C
ATOM 1855 CE2 PHE A 347 35.859 8.264 -5.597 1.00103.20 C
ANISOU 1855 CE2 PHE A 347 13880 12840 12492 -2348 878 -64 C
ATOM 1856 CZ PHE A 347 37.025 8.063 -4.891 1.00104.25 C
ANISOU 1856 CZ PHE A 347 13663 13422 12526 -2564 869 -177 C
ATOM 1857 N ASN A 348 34.106 5.178 -9.744 1.00100.60 N
ANISOU 1857 N ASN A 348 13751 12189 12285 -1160 624 410 N
ATOM 1858 CA ASN A 348 32.687 4.898 -9.560 1.00 96.68 C
ANISOU 1858 CA ASN A 348 13405 11466 11863 -932 497 470 C
ATOM 1859 C ASN A 348 32.418 3.390 -9.486 1.00 95.37 C
ANISOU 1859 C ASN A 348 13076 11426 11732 -666 344 492 C
ATOM 1860 O ASN A 348 31.549 2.949 -8.722 1.00 93.41 O
ANISOU 1860 O ASN A 348 12827 11114 11549 -540 220 492 O
ATOM 1861 CB ASN A 348 31.889 5.561 -10.686 1.00 93.00 C
ANISOU 1861 CB ASN A 348 13240 10727 11370 -862 567 568 C
ATOM 1862 CG ASN A 348 30.412 5.711 -10.360 1.00 94.61 C
ANISOU 1862 CG ASN A 348 13611 10711 11628 -689 472 625 C
ATOM 1863 OD1 ASN A 348 30.025 5.974 -9.211 1.00 94.88 O
ANISOU 1863 OD1 ASN A 348 13635 10695 11720 -732 429 577 O
ATOM 1864 ND2 ASN A 348 29.573 5.542 -11.374 1.00 94.26 N
ANISOU 1864 ND2 ASN A 348 13704 10564 11546 -494 441 725 N
ATOM 1865 N ALA A 349 33.153 2.580 -10.266 1.00 97.67 N
ANISOU 1865 N ALA A 349 13248 11884 11976 -582 370 508 N
ATOM 1866 CA ALA A 349 32.954 1.125 -10.238 1.00 95.50 C
ANISOU 1866 CA ALA A 349 12867 11693 11725 -333 272 524 C
ATOM 1867 C ALA A 349 33.484 0.501 -8.947 1.00 95.66 C
ANISOU 1867 C ALA A 349 12644 11932 11771 -300 210 485 C
ATOM 1868 O ALA A 349 32.914 -0.476 -8.439 1.00 90.57 O
ANISOU 1868 O ALA A 349 11977 11263 11173 -109 115 499 O
ATOM 1869 CB ALA A 349 33.610 0.465 -11.450 1.00 93.33 C
ANISOU 1869 CB ALA A 349 12563 11515 11383 -243 349 551 C
ATOM 1870 N PHE A 350 34.584 1.034 -8.409 1.00 97.41 N
ANISOU 1870 N PHE A 350 12677 12390 11945 -489 272 438 N
ATOM 1871 CA PHE A 350 35.063 0.561 -7.118 1.00 96.95 C
ANISOU 1871 CA PHE A 350 12370 12584 11881 -462 206 409 C
ATOM 1872 C PHE A 350 34.111 0.942 -5.977 1.00 94.51 C
ANISOU 1872 C PHE A 350 12142 12127 11642 -508 107 378 C
ATOM 1873 O PHE A 350 33.966 0.192 -5.007 1.00 93.02 O
ANISOU 1873 O PHE A 350 11830 12040 11474 -371 14 386 O
ATOM 1874 CB PHE A 350 36.456 1.106 -6.845 1.00 99.75 C
ANISOU 1874 CB PHE A 350 12477 13288 12136 -690 293 352 C
ATOM 1875 CG PHE A 350 36.928 0.782 -5.486 1.00100.20 C
ANISOU 1875 CG PHE A 350 12265 13651 12156 -686 220 324 C
ATOM 1876 CD1 PHE A 350 37.507 -0.447 -5.219 1.00100.19 C
ANISOU 1876 CD1 PHE A 350 12030 13923 12114 -416 186 390 C
ATOM 1877 CD2 PHE A 350 36.690 1.663 -4.439 1.00100.33 C
ANISOU 1877 CD2 PHE A 350 12287 13661 12174 -924 190 240 C
ATOM 1878 CE1 PHE A 350 37.906 -0.760 -3.942 1.00 99.67 C
ANISOU 1878 CE1 PHE A 350 11713 14163 11995 -379 115 387 C
ATOM 1879 CE2 PHE A 350 37.080 1.358 -3.168 1.00 98.74 C
ANISOU 1879 CE2 PHE A 350 11833 13763 11919 -922 113 214 C
ATOM 1880 CZ PHE A 350 37.688 0.145 -2.912 1.00 98.77 C
ANISOU 1880 CZ PHE A 350 11582 14076 11872 -642 68 295 C
ATOM 1881 N LEU A 351 33.490 2.122 -6.043 1.00 95.51 N
ANISOU 1881 N LEU A 351 12481 12015 11794 -690 143 348 N
ATOM 1882 CA LEU A 351 32.615 2.550 -4.952 1.00 92.15 C
ANISOU 1882 CA LEU A 351 12136 11450 11426 -733 70 314 C
ATOM 1883 C LEU A 351 31.302 1.784 -4.937 1.00 89.55 C
ANISOU 1883 C LEU A 351 11930 10918 11177 -478 -46 373 C
ATOM 1884 O LEU A 351 30.781 1.461 -3.861 1.00 89.39 O
ANISOU 1884 O LEU A 351 11863 10901 11200 -419 -140 357 O
ATOM 1885 CB LEU A 351 32.332 4.046 -5.035 1.00 90.88 C
ANISOU 1885 CB LEU A 351 12197 11070 11261 -976 178 273 C
ATOM 1886 CG LEU A 351 33.372 4.946 -4.401 1.00 93.19 C
ANISOU 1886 CG LEU A 351 12383 11546 11479 -1315 284 162 C
ATOM 1887 CD1 LEU A 351 33.520 4.572 -2.939 1.00 90.58 C
ANISOU 1887 CD1 LEU A 351 11834 11441 11141 -1339 180 98 C
ATOM 1888 CD2 LEU A 351 34.665 4.759 -5.155 1.00 94.27 C
ANISOU 1888 CD2 LEU A 351 12342 11950 11526 -1403 370 155 C
ATOM 1889 N GLU A 352 30.721 1.516 -6.107 1.00 87.15 N
ANISOU 1889 N GLU A 352 11782 10451 10880 -346 -39 433 N
ATOM 1890 CA GLU A 352 29.438 0.825 -6.115 1.00 82.65 C
ANISOU 1890 CA GLU A 352 11317 9724 10362 -150 -143 468 C
ATOM 1891 C GLU A 352 29.572 -0.633 -5.701 1.00 79.96 C
ANISOU 1891 C GLU A 352 10837 9508 10035 29 -208 473 C
ATOM 1892 O GLU A 352 28.696 -1.159 -5.013 1.00 79.40 O
ANISOU 1892 O GLU A 352 10791 9364 10013 126 -295 471 O
ATOM 1893 CB GLU A 352 28.782 0.907 -7.480 1.00 82.28 C
ANISOU 1893 CB GLU A 352 11453 9524 10286 -74 -120 522 C
ATOM 1894 CG GLU A 352 27.332 1.271 -7.377 1.00 83.64 C
ANISOU 1894 CG GLU A 352 11783 9510 10486 -7 -188 551 C
ATOM 1895 CD GLU A 352 26.649 1.199 -8.709 1.00 91.63 C
ANISOU 1895 CD GLU A 352 12932 10446 11437 91 -185 610 C
ATOM 1896 OE1 GLU A 352 27.248 0.582 -9.624 1.00 95.70 O
ANISOU 1896 OE1 GLU A 352 13418 11043 11900 119 -144 612 O
ATOM 1897 OE2 GLU A 352 25.512 1.721 -8.831 1.00 96.71 O1-
ANISOU 1897 OE2 GLU A 352 13701 10975 12070 152 -222 655 O1-
ATOM 1898 N SER A 353 30.643 -1.310 -6.127 1.00 83.10 N
ANISOU 1898 N SER A 353 11105 10085 10386 87 -147 485 N
ATOM 1899 CA SER A 353 30.758 -2.750 -5.912 1.00 80.66 C
ANISOU 1899 CA SER A 353 10721 9847 10078 301 -165 509 C
ATOM 1900 C SER A 353 31.139 -3.090 -4.472 1.00 79.96 C
ANISOU 1900 C SER A 353 10451 9931 9998 343 -213 510 C
ATOM 1901 O SER A 353 30.693 -4.113 -3.944 1.00 77.70 O
ANISOU 1901 O SER A 353 10181 9605 9738 515 -250 534 O
ATOM 1902 CB SER A 353 31.778 -3.375 -6.888 1.00 80.23 C
ANISOU 1902 CB SER A 353 10603 9921 9959 391 -59 536 C
ATOM 1903 OG SER A 353 33.128 -3.034 -6.590 1.00 82.02 O
ANISOU 1903 OG SER A 353 10603 10433 10128 318 -1 537 O
ATOM 1904 N PHE A 354 31.985 -2.282 -3.830 1.00 81.88 N
ANISOU 1904 N PHE A 354 10524 10384 10202 179 -202 480 N
ATOM 1905 CA PHE A 354 32.403 -2.552 -2.458 1.00 83.25 C
ANISOU 1905 CA PHE A 354 10497 10782 10350 208 -253 481 C
ATOM 1906 C PHE A 354 31.429 -1.987 -1.429 1.00 81.11 C
ANISOU 1906 C PHE A 354 10307 10374 10137 107 -342 437 C
ATOM 1907 O PHE A 354 31.688 -2.046 -0.218 1.00 77.66 O
ANISOU 1907 O PHE A 354 9717 10121 9671 93 -391 425 O
ATOM 1908 CB PHE A 354 33.815 -2.021 -2.231 1.00 85.07 C
ANISOU 1908 CB PHE A 354 10470 11374 10478 58 -199 455 C
ATOM 1909 CG PHE A 354 34.847 -2.926 -2.776 1.00 88.08 C
ANISOU 1909 CG PHE A 354 10689 11989 10788 250 -127 523 C
ATOM 1910 CD1 PHE A 354 35.268 -2.789 -4.100 1.00 90.54 C
ANISOU 1910 CD1 PHE A 354 11059 12262 11079 221 -30 526 C
ATOM 1911 CD2 PHE A 354 35.325 -3.985 -2.014 1.00 85.02 C
ANISOU 1911 CD2 PHE A 354 10118 11835 10349 499 -142 600 C
ATOM 1912 CE1 PHE A 354 36.190 -3.649 -4.640 1.00 88.65 C
ANISOU 1912 CE1 PHE A 354 10685 12225 10773 420 53 590 C
ATOM 1913 CE2 PHE A 354 36.254 -4.860 -2.549 1.00 87.39 C
ANISOU 1913 CE2 PHE A 354 10290 12336 10578 727 -51 680 C
ATOM 1914 CZ PHE A 354 36.691 -4.690 -3.869 1.00 87.59 C
ANISOU 1914 CZ PHE A 354 10366 12327 10589 683 48 669 C
ATOM 1915 N GLN A 355 30.304 -1.466 -1.900 1.00 77.08 N
ANISOU 1915 N GLN A 355 10028 9565 9694 56 -360 419 N
ATOM 1916 CA GLN A 355 29.339 -0.842 -1.017 1.00 76.79 C
ANISOU 1916 CA GLN A 355 10082 9387 9709 -27 -424 380 C
ATOM 1917 C GLN A 355 28.840 -1.809 0.060 1.00 74.56 C
ANISOU 1917 C GLN A 355 9744 9133 9453 129 -509 402 C
ATOM 1918 O GLN A 355 28.825 -1.472 1.248 1.00 74.75 O
ANISOU 1918 O GLN A 355 9687 9245 9470 51 -553 367 O
ATOM 1919 CB GLN A 355 28.199 -0.312 -1.869 1.00 74.67 C
ANISOU 1919 CB GLN A 355 10054 8829 9488 -31 -421 389 C
ATOM 1920 CG GLN A 355 27.042 0.121 -1.082 1.00 70.58 C
ANISOU 1920 CG GLN A 355 9638 8156 9024 -45 -483 369 C
ATOM 1921 CD GLN A 355 26.069 0.893 -1.922 1.00 71.77 C
ANISOU 1921 CD GLN A 355 9998 8080 9191 -48 -460 394 C
ATOM 1922 OE1 GLN A 355 24.897 0.522 -2.003 1.00 69.52 O
ANISOU 1922 OE1 GLN A 355 9795 7684 8935 73 -525 418 O
ATOM 1923 NE2 GLN A 355 26.536 1.987 -2.552 1.00 72.69 N
ANISOU 1923 NE2 GLN A 355 10203 8143 9275 -184 -357 393 N
ATOM 1924 N GLY A 356 28.425 -3.021 -0.333 1.00 73.70 N
ANISOU 1924 N GLY A 356 9694 8943 9366 337 -518 452 N
ATOM 1925 CA GLY A 356 27.947 -3.986 0.652 1.00 68.96 C
ANISOU 1925 CA GLY A 356 9076 8340 8784 483 -569 479 C
ATOM 1926 C GLY A 356 29.025 -4.384 1.644 1.00 71.36 C
ANISOU 1926 C GLY A 356 9157 8938 9020 551 -567 516 C
ATOM 1927 O GLY A 356 28.743 -4.665 2.812 1.00 70.20 O
ANISOU 1927 O GLY A 356 8960 8842 8870 597 -620 527 O
ATOM 1928 N PHE A 357 30.273 -4.439 1.185 1.00 73.94 N
ANISOU 1928 N PHE A 357 9331 9489 9273 572 -502 543 N
ATOM 1929 CA PHE A 357 31.387 -4.645 2.099 1.00 73.32 C
ANISOU 1929 CA PHE A 357 8986 9776 9094 623 -504 581 C
ATOM 1930 C PHE A 357 31.468 -3.524 3.134 1.00 74.80 C
ANISOU 1930 C PHE A 357 9060 10112 9248 373 -568 498 C
ATOM 1931 O PHE A 357 31.645 -3.774 4.332 1.00 76.03 O
ANISOU 1931 O PHE A 357 9072 10471 9344 419 -620 518 O
ATOM 1932 CB PHE A 357 32.678 -4.736 1.297 1.00 75.15 C
ANISOU 1932 CB PHE A 357 9059 10250 9244 659 -418 613 C
ATOM 1933 CG PHE A 357 33.897 -4.888 2.140 1.00 74.90 C
ANISOU 1933 CG PHE A 357 8706 10675 9077 713 -419 657 C
ATOM 1934 CD1 PHE A 357 34.396 -6.146 2.435 1.00 72.13 C
ANISOU 1934 CD1 PHE A 357 8252 10491 8662 1051 -380 788 C
ATOM 1935 CD2 PHE A 357 34.553 -3.771 2.645 1.00 76.94 C
ANISOU 1935 CD2 PHE A 357 8766 11216 9253 425 -446 569 C
ATOM 1936 CE1 PHE A 357 35.542 -6.288 3.208 1.00 73.06 C
ANISOU 1936 CE1 PHE A 357 8038 11096 8626 1136 -384 850 C
ATOM 1937 CE2 PHE A 357 35.693 -3.907 3.423 1.00 75.78 C
ANISOU 1937 CE2 PHE A 357 8279 11566 8947 456 -456 602 C
ATOM 1938 CZ PHE A 357 36.189 -5.163 3.708 1.00 73.09 C
ANISOU 1938 CZ PHE A 357 7801 11435 8534 828 -435 752 C
ATOM 1939 N PHE A 358 31.354 -2.276 2.689 1.00 75.56 N
ANISOU 1939 N PHE A 358 9238 10106 9367 104 -547 405 N
ATOM 1940 CA PHE A 358 31.300 -1.171 3.635 1.00 76.55 C
ANISOU 1940 CA PHE A 358 9323 10297 9463 -158 -575 305 C
ATOM 1941 C PHE A 358 30.207 -1.401 4.676 1.00 77.18 C
ANISOU 1941 C PHE A 358 9494 10230 9600 -89 -658 305 C
ATOM 1942 O PHE A 358 30.438 -1.222 5.882 1.00 77.38 O
ANISOU 1942 O PHE A 358 9380 10463 9556 -168 -703 269 O
ATOM 1943 CB PHE A 358 31.055 0.148 2.897 1.00 76.82 C
ANISOU 1943 CB PHE A 358 9539 10114 9536 -414 -503 221 C
ATOM 1944 CG PHE A 358 32.108 0.499 1.881 1.00 80.79 C
ANISOU 1944 CG PHE A 358 9971 10749 9978 -525 -406 210 C
ATOM 1945 CD1 PHE A 358 33.426 0.108 2.057 1.00 82.17 C
ANISOU 1945 CD1 PHE A 358 9850 11338 10033 -522 -389 223 C
ATOM 1946 CD2 PHE A 358 31.777 1.239 0.746 1.00 83.56 C
ANISOU 1946 CD2 PHE A 358 10541 10830 10377 -622 -325 197 C
ATOM 1947 CE1 PHE A 358 34.391 0.441 1.109 1.00 84.16 C
ANISOU 1947 CE1 PHE A 358 10026 11729 10224 -635 -291 209 C
ATOM 1948 CE2 PHE A 358 32.740 1.574 -0.196 1.00 85.54 C
ANISOU 1948 CE2 PHE A 358 10738 11197 10568 -736 -224 188 C
ATOM 1949 CZ PHE A 358 34.045 1.175 -0.017 1.00 85.10 C
ANISOU 1949 CZ PHE A 358 10385 11549 10401 -753 -206 186 C
ATOM 1950 N VAL A 359 29.010 -1.809 4.232 1.00 75.90 N
ANISOU 1950 N VAL A 359 9552 9739 9546 45 -678 339 N
ATOM 1951 CA VAL A 359 27.873 -1.951 5.147 1.00 73.84 C
ANISOU 1951 CA VAL A 359 9388 9327 9340 88 -746 330 C
ATOM 1952 C VAL A 359 28.133 -3.054 6.167 1.00 73.19 C
ANISOU 1952 C VAL A 359 9164 9439 9207 272 -790 399 C
ATOM 1953 O VAL A 359 27.770 -2.926 7.335 1.00 74.89 O
ANISOU 1953 O VAL A 359 9346 9704 9406 234 -844 375 O
ATOM 1954 CB VAL A 359 26.564 -2.198 4.363 1.00 70.68 C
ANISOU 1954 CB VAL A 359 9220 8593 9042 181 -754 349 C
ATOM 1955 CG1 VAL A 359 25.449 -2.617 5.296 1.00 70.09 C
ANISOU 1955 CG1 VAL A 359 9211 8408 9011 254 -818 351 C
ATOM 1956 CG2 VAL A 359 26.132 -0.936 3.602 1.00 71.90 C
ANISOU 1956 CG2 VAL A 359 9526 8560 9232 21 -714 298 C
ATOM 1957 N SER A 360 28.755 -4.158 5.745 1.00 74.55 N
ANISOU 1957 N SER A 360 9268 9715 9343 490 -753 495 N
ATOM 1958 CA SER A 360 28.974 -5.283 6.655 1.00 74.87 C
ANISOU 1958 CA SER A 360 9214 9908 9326 719 -764 592 C
ATOM 1959 C SER A 360 29.935 -4.909 7.785 1.00 75.69 C
ANISOU 1959 C SER A 360 9045 10420 9295 652 -806 589 C
ATOM 1960 O SER A 360 29.772 -5.348 8.928 1.00 75.20 O
ANISOU 1960 O SER A 360 8921 10469 9182 748 -850 634 O
ATOM 1961 CB SER A 360 29.486 -6.501 5.870 1.00 70.67 C
ANISOU 1961 CB SER A 360 8701 9375 8776 987 -676 701 C
ATOM 1962 OG SER A 360 30.806 -6.297 5.352 1.00 71.00 O
ANISOU 1962 OG SER A 360 8546 9703 8730 987 -629 722 O
ATOM 1963 N VAL A 361 30.962 -4.120 7.474 1.00 76.04 N
ANISOU 1963 N VAL A 361 8913 10718 9260 476 -786 534 N
ATOM 1964 CA VAL A 361 31.854 -3.612 8.511 1.00 77.70 C
ANISOU 1964 CA VAL A 361 8847 11361 9317 334 -826 495 C
ATOM 1965 C VAL A 361 31.073 -2.710 9.454 1.00 79.23 C
ANISOU 1965 C VAL A 361 9122 11448 9533 93 -882 376 C
ATOM 1966 O VAL A 361 31.103 -2.876 10.683 1.00 80.91 O
ANISOU 1966 O VAL A 361 9211 11875 9656 112 -942 385 O
ATOM 1967 CB VAL A 361 33.049 -2.876 7.861 1.00 79.45 C
ANISOU 1967 CB VAL A 361 8883 11858 9447 132 -773 432 C
ATOM 1968 CG1 VAL A 361 33.962 -2.238 8.899 1.00 78.47 C
ANISOU 1968 CG1 VAL A 361 8457 12220 9138 -90 -809 354 C
ATOM 1969 CG2 VAL A 361 33.852 -3.827 6.967 1.00 74.22 C
ANISOU 1969 CG2 VAL A 361 8124 11324 8751 405 -707 559 C
ATOM 1970 N PHE A 362 30.306 -1.782 8.876 1.00 78.75 N
ANISOU 1970 N PHE A 362 9290 11042 9588 -108 -853 274 N
ATOM 1971 CA PHE A 362 29.431 -0.911 9.651 1.00 79.15 C
ANISOU 1971 CA PHE A 362 9474 10922 9678 -304 -878 167 C
ATOM 1972 C PHE A 362 28.570 -1.716 10.630 1.00 80.24 C
ANISOU 1972 C PHE A 362 9654 10993 9843 -112 -949 230 C
ATOM 1973 O PHE A 362 28.518 -1.413 11.828 1.00 81.64 O
ANISOU 1973 O PHE A 362 9752 11324 9945 -214 -991 177 O
ATOM 1974 CB PHE A 362 28.571 -0.094 8.668 1.00 79.12 C
ANISOU 1974 CB PHE A 362 9748 10505 9808 -411 -819 111 C
ATOM 1975 CG PHE A 362 27.557 0.803 9.317 1.00 79.75 C
ANISOU 1975 CG PHE A 362 10005 10356 9940 -560 -816 19 C
ATOM 1976 CD1 PHE A 362 27.943 2.023 9.860 1.00 80.64 C
ANISOU 1976 CD1 PHE A 362 10113 10545 9980 -871 -757 -119 C
ATOM 1977 CD2 PHE A 362 26.216 0.446 9.363 1.00 78.83 C
ANISOU 1977 CD2 PHE A 362 10066 9952 9935 -400 -854 62 C
ATOM 1978 CE1 PHE A 362 27.015 2.868 10.472 1.00 78.35 C
ANISOU 1978 CE1 PHE A 362 10012 10023 9734 -992 -726 -204 C
ATOM 1979 CE2 PHE A 362 25.271 1.285 9.973 1.00 78.72 C
ANISOU 1979 CE2 PHE A 362 10204 9743 9961 -509 -840 -14 C
ATOM 1980 CZ PHE A 362 25.677 2.501 10.523 1.00 78.00 C
ANISOU 1980 CZ PHE A 362 10129 9703 9804 -790 -770 -143 C
ATOM 1981 N ALA A 363 27.932 -2.780 10.143 1.00 77.65 N
ANISOU 1981 N ALA A 363 9450 10451 9604 152 -951 338 N
ATOM 1982 CA ALA A 363 27.005 -3.547 10.965 1.00 78.53 C
ANISOU 1982 CA ALA A 363 9643 10446 9749 311 -994 392 C
ATOM 1983 C ALA A 363 27.721 -4.324 12.063 1.00 81.71 C
ANISOU 1983 C ALA A 363 9839 11192 10013 464 -1025 483 C
ATOM 1984 O ALA A 363 27.235 -4.385 13.196 1.00 83.86 O
ANISOU 1984 O ALA A 363 10108 11500 10254 462 -1070 477 O
ATOM 1985 CB ALA A 363 26.198 -4.495 10.085 1.00 78.60 C
ANISOU 1985 CB ALA A 363 9847 10149 9868 508 -961 464 C
ATOM 1986 N CYS A 364 28.855 -4.951 11.751 1.00 79.39 N
ANISOU 1986 N CYS A 364 9373 11167 9625 625 -994 580 N
ATOM 1987 CA CYS A 364 29.532 -5.736 12.778 1.00 82.76 C
ANISOU 1987 CA CYS A 364 9598 11951 9898 830 -1015 700 C
ATOM 1988 C CYS A 364 30.152 -4.840 13.855 1.00 85.27 C
ANISOU 1988 C CYS A 364 9669 12671 10058 598 -1084 610 C
ATOM 1989 O CYS A 364 30.203 -5.222 15.031 1.00 88.50 O
ANISOU 1989 O CYS A 364 9966 13308 10351 695 -1131 669 O
ATOM 1990 CB CYS A 364 30.571 -6.660 12.127 1.00 80.19 C
ANISOU 1990 CB CYS A 364 9151 11818 9500 1107 -945 845 C
ATOM 1991 SG CYS A 364 29.837 -8.276 11.614 1.00 77.62 S
ANISOU 1991 SG CYS A 364 9116 11095 9280 1485 -840 1000 S
ATOM 1992 N PHE A 365 30.604 -3.646 13.471 1.00 86.07 N
ANISOU 1992 N PHE A 365 9702 12858 10141 276 -1078 460 N
ATOM 1993 CA PHE A 365 31.135 -2.676 14.427 1.00 87.92 C
ANISOU 1993 CA PHE A 365 9740 13444 10221 -26 -1119 328 C
ATOM 1994 C PHE A 365 30.085 -2.308 15.478 1.00 87.26 C
ANISOU 1994 C PHE A 365 9800 13184 10172 -135 -1162 251 C
ATOM 1995 O PHE A 365 30.404 -2.165 16.661 1.00 89.24 O
ANISOU 1995 O PHE A 365 9873 13773 10260 -218 -1215 219 O
ATOM 1996 CB PHE A 365 31.618 -1.449 13.634 1.00 87.76 C
ANISOU 1996 CB PHE A 365 9723 13412 10210 -377 -1059 167 C
ATOM 1997 CG PHE A 365 32.354 -0.399 14.443 1.00 89.34 C
ANISOU 1997 CG PHE A 365 9720 13998 10226 -755 -1064 -1 C
ATOM 1998 CD1 PHE A 365 31.648 0.621 15.089 1.00 88.28 C
ANISOU 1998 CD1 PHE A 365 9756 13670 10119 -1052 -1048 -169 C
ATOM 1999 CD2 PHE A 365 33.751 -0.383 14.486 1.00 88.62 C
ANISOU 1999 CD2 PHE A 365 9279 14464 9930 -837 -1066 -5 C
ATOM 2000 CE1 PHE A 365 32.309 1.609 15.804 1.00 86.81 C
ANISOU 2000 CE1 PHE A 365 9418 13811 9753 -1445 -1025 -351 C
ATOM 2001 CE2 PHE A 365 34.424 0.606 15.201 1.00 91.11 C
ANISOU 2001 CE2 PHE A 365 9404 15160 10054 -1243 -1060 -188 C
ATOM 2002 CZ PHE A 365 33.693 1.604 15.865 1.00 91.37 C
ANISOU 2002 CZ PHE A 365 9639 14963 10115 -1562 -1034 -370 C
ATOM 2003 N LEU A 366 28.827 -2.159 15.058 1.00 89.55 N
ANISOU 2003 N LEU A 366 10395 12973 10656 -132 -1139 221 N
ATOM 2004 CA LEU A 366 27.724 -1.836 15.960 1.00 92.50 C
ANISOU 2004 CA LEU A 366 10920 13147 11078 -208 -1165 155 C
ATOM 2005 C LEU A 366 27.361 -2.980 16.894 1.00 95.90 C
ANISOU 2005 C LEU A 366 11318 13654 11464 62 -1216 291 C
ATOM 2006 O LEU A 366 26.607 -2.773 17.854 1.00 96.44 O
ANISOU 2006 O LEU A 366 11458 13656 11530 -1 -1244 242 O
ATOM 2007 CB LEU A 366 26.485 -1.462 15.157 1.00 89.39 C
ANISOU 2007 CB LEU A 366 10830 12245 10888 -229 -1123 113 C
ATOM 2008 CG LEU A 366 26.301 -0.004 14.759 1.00 86.97 C
ANISOU 2008 CG LEU A 366 10658 11758 10629 -532 -1057 -48 C
ATOM 2009 CD1 LEU A 366 27.633 0.621 14.413 1.00 87.28 C
ANISOU 2009 CD1 LEU A 366 10529 12081 10551 -746 -1015 -119 C
ATOM 2010 CD2 LEU A 366 25.327 0.061 13.591 1.00 84.28 C
ANISOU 2010 CD2 LEU A 366 10563 10993 10465 -440 -1016 -18 C
ATOM 2011 N ASN A 367 27.827 -4.190 16.600 1.00 98.68 N
ANISOU 2011 N ASN A 367 11599 14109 11786 372 -1206 465 N
ATOM 2012 CA ASN A 367 27.543 -5.319 17.471 1.00 98.48 C
ANISOU 2012 CA ASN A 367 11575 14139 11705 648 -1221 613 C
ATOM 2013 C ASN A 367 28.229 -5.183 18.823 1.00 99.92 C
ANISOU 2013 C ASN A 367 11500 14802 11664 611 -1286 622 C
ATOM 2014 O ASN A 367 27.814 -5.835 19.789 1.00101.46 O
ANISOU 2014 O ASN A 367 11718 15031 11802 772 -1304 714 O
ATOM 2015 CB ASN A 367 27.962 -6.622 16.791 1.00 98.28 C
ANISOU 2015 CB ASN A 367 11566 14090 11685 1000 -1156 802 C
ATOM 2016 CG ASN A 367 27.223 -7.814 17.338 1.00 99.13 C
ANISOU 2016 CG ASN A 367 11839 14011 11815 1271 -1116 941 C
ATOM 2017 OD1 ASN A 367 26.228 -7.668 18.051 1.00 98.57 O
ANISOU 2017 OD1 ASN A 367 11893 13770 11791 1183 -1143 888 O
ATOM 2018 ND2 ASN A 367 27.701 -9.006 17.011 1.00101.00 N
ANISOU 2018 ND2 ASN A 367 12096 14267 12013 1603 -1031 1121 N
ATOM 2019 N SER A 368 29.257 -4.348 18.916 1.00103.16 N
ANISOU 2019 N SER A 368 11665 15599 11930 384 -1314 523 N
ATOM 2020 CA SER A 368 30.004 -4.174 20.160 1.00105.51 C
ANISOU 2020 CA SER A 368 11675 16438 11975 313 -1381 514 C
ATOM 2021 C SER A 368 29.159 -3.544 21.282 1.00105.48 C
ANISOU 2021 C SER A 368 11767 16354 11956 95 -1418 383 C
ATOM 2022 O SER A 368 28.948 -4.157 22.343 1.00102.63 O
ANISOU 2022 O SER A 368 11360 16147 11488 261 -1459 482 O
ATOM 2023 CB SER A 368 31.260 -3.332 19.885 1.00104.84 C
ANISOU 2023 CB SER A 368 11312 16787 11737 45 -1388 398 C
ATOM 2024 OG SER A 368 31.786 -3.634 18.595 1.00102.74 O
ANISOU 2024 OG SER A 368 11040 16446 11551 170 -1331 467 O
TER 2025 SER A 368
ATOM 2026 N ASN B1000 13.675 0.981 28.893 1.00 72.23 N
ANISOU 2026 N ASN B1000 9734 9062 8648 -566 -999 -565 N
ATOM 2027 CA ASN B1000 12.545 0.468 28.113 1.00 69.41 C
ANISOU 2027 CA ASN B1000 9444 8474 8454 -384 -989 -475 C
ATOM 2028 C ASN B1000 11.229 0.421 28.865 1.00 68.40 C
ANISOU 2028 C ASN B1000 9378 8265 8345 -333 -940 -494 C
ATOM 2029 O ASN B1000 10.176 0.159 28.258 1.00 65.48 O
ANISOU 2029 O ASN B1000 9050 7737 8092 -213 -920 -446 O
ATOM 2030 CB ASN B1000 12.889 -0.906 27.572 1.00 69.64 C
ANISOU 2030 CB ASN B1000 9387 8569 8503 -235 -1069 -314 C
ATOM 2031 CG ASN B1000 14.050 -0.844 26.603 1.00 67.72 C
ANISOU 2031 CG ASN B1000 9087 8378 8267 -252 -1105 -287 C
ATOM 2032 OD1 ASN B1000 13.843 -0.877 25.386 1.00 68.35 O
ANISOU 2032 OD1 ASN B1000 9213 8289 8467 -184 -1098 -252 O
ATOM 2033 ND2 ASN B1000 15.268 -0.706 27.129 1.00 64.94 N
ANISOU 2033 ND2 ASN B1000 8620 8285 7768 -353 -1141 -310 N
ATOM 2034 N ILE B1001 11.305 0.720 30.171 1.00 70.79 N
ANISOU 2034 N ILE B1001 9675 8705 8518 -440 -918 -574 N
ATOM 2035 CA ILE B1001 10.148 0.573 31.050 1.00 70.13 C
ANISOU 2035 CA ILE B1001 9631 8588 8425 -398 -871 -588 C
ATOM 2036 C ILE B1001 8.992 1.412 30.543 1.00 69.15 C
ANISOU 2036 C ILE B1001 9624 8222 8427 -342 -771 -647 C
ATOM 2037 O ILE B1001 7.827 0.992 30.613 1.00 66.75 O
ANISOU 2037 O ILE B1001 9321 7862 8180 -232 -749 -603 O
ATOM 2038 CB ILE B1001 10.508 0.937 32.501 1.00 70.24 C
ANISOU 2038 CB ILE B1001 9631 8795 8262 -544 -853 -686 C
ATOM 2039 CG1 ILE B1001 9.295 0.694 33.407 1.00 72.18 C
ANISOU 2039 CG1 ILE B1001 9916 9011 8498 -489 -800 -689 C
ATOM 2040 CG2 ILE B1001 10.944 2.393 32.600 1.00 69.81 C
ANISOU 2040 CG2 ILE B1001 9670 8691 8164 -738 -763 -868 C
ATOM 2041 CD1 ILE B1001 9.576 0.824 34.883 1.00 70.39 C
ANISOU 2041 CD1 ILE B1001 9666 8999 8079 -613 -791 -763 C
ATOM 2042 N PHE B1002 9.292 2.612 30.029 1.00 69.40 N
ANISOU 2042 N PHE B1002 9756 8122 8490 -413 -696 -742 N
ATOM 2043 CA PHE B1002 8.247 3.418 29.412 1.00 69.48 C
ANISOU 2043 CA PHE B1002 9884 7903 8612 -303 -588 -762 C
ATOM 2044 C PHE B1002 7.672 2.707 28.186 1.00 70.11 C
ANISOU 2044 C PHE B1002 9900 7925 8813 -127 -650 -630 C
ATOM 2045 O PHE B1002 6.449 2.721 27.963 1.00 68.70 O
ANISOU 2045 O PHE B1002 9724 7684 8696 12 -609 -598 O
ATOM 2046 CB PHE B1002 8.796 4.799 29.049 1.00 71.40 C
ANISOU 2046 CB PHE B1002 10287 7989 8854 -408 -469 -874 C
ATOM 2047 CG PHE B1002 7.785 5.694 28.353 1.00 75.46 C
ANISOU 2047 CG PHE B1002 10947 8257 9468 -245 -334 -866 C
ATOM 2048 CD1 PHE B1002 6.900 6.479 29.088 1.00 76.54 C
ANISOU 2048 CD1 PHE B1002 11210 8288 9584 -200 -184 -942 C
ATOM 2049 CD2 PHE B1002 7.714 5.749 26.954 1.00 73.90 C
ANISOU 2049 CD2 PHE B1002 10758 7947 9372 -112 -348 -770 C
ATOM 2050 CE1 PHE B1002 5.967 7.306 28.443 1.00 78.51 C
ANISOU 2050 CE1 PHE B1002 11591 8331 9910 3 -44 -908 C
ATOM 2051 CE2 PHE B1002 6.778 6.577 26.309 1.00 75.05 C
ANISOU 2051 CE2 PHE B1002 11027 7903 9586 78 -221 -737 C
ATOM 2052 CZ PHE B1002 5.905 7.353 27.054 1.00 76.65 C
ANISOU 2052 CZ PHE B1002 11351 8008 9763 151 -67 -798 C
ATOM 2053 N GLU B1003 8.534 2.088 27.366 1.00 67.24 N
ANISOU 2053 N GLU B1003 9469 7606 8473 -134 -744 -557 N
ATOM 2054 CA GLU B1003 8.003 1.313 26.249 1.00 67.86 C
ANISOU 2054 CA GLU B1003 9491 7647 8645 3 -799 -447 C
ATOM 2055 C GLU B1003 7.200 0.116 26.747 1.00 66.25 C
ANISOU 2055 C GLU B1003 9206 7536 8429 53 -838 -386 C
ATOM 2056 O GLU B1003 6.135 -0.199 26.188 1.00 65.59 O
ANISOU 2056 O GLU B1003 9093 7425 8403 145 -830 -348 O
ATOM 2057 CB GLU B1003 9.130 0.863 25.303 1.00 68.02 C
ANISOU 2057 CB GLU B1003 9471 7690 8684 -17 -874 -388 C
ATOM 2058 CG GLU B1003 9.743 1.985 24.477 1.00 67.31 C
ANISOU 2058 CG GLU B1003 9467 7483 8626 -57 -823 -432 C
ATOM 2059 CD GLU B1003 8.732 2.608 23.535 1.00 69.16 C
ANISOU 2059 CD GLU B1003 9773 7557 8947 82 -759 -407 C
ATOM 2060 OE1 GLU B1003 7.720 1.938 23.233 1.00 68.87 O
ANISOU 2060 OE1 GLU B1003 9668 7551 8947 200 -792 -343 O
ATOM 2061 OE2 GLU B1003 8.929 3.777 23.122 1.00 70.31 O1-
ANISOU 2061 OE2 GLU B1003 10046 7561 9108 72 -663 -450 O1-
ATOM 2062 N MET B1004 7.702 -0.558 27.794 1.00 67.42 N
ANISOU 2062 N MET B1004 9318 7812 8485 -14 -872 -376 N
ATOM 2063 CA MET B1004 7.025 -1.728 28.363 1.00 68.65 C
ANISOU 2063 CA MET B1004 9434 8036 8614 17 -882 -314 C
ATOM 2064 C MET B1004 5.580 -1.413 28.736 1.00 68.73 C
ANISOU 2064 C MET B1004 9448 8019 8646 51 -812 -360 C
ATOM 2065 O MET B1004 4.644 -2.114 28.326 1.00 66.29 O
ANISOU 2065 O MET B1004 9098 7711 8377 94 -806 -319 O
ATOM 2066 CB MET B1004 7.777 -2.210 29.603 1.00 67.65 C
ANISOU 2066 CB MET B1004 9287 8060 8357 -40 -905 -296 C
ATOM 2067 CG MET B1004 7.108 -3.392 30.352 1.00 69.05 C
ANISOU 2067 CG MET B1004 9459 8288 8487 -10 -886 -224 C
ATOM 2068 SD MET B1004 8.066 -3.900 31.824 1.00 67.53 S
ANISOU 2068 SD MET B1004 9244 8306 8109 -37 -911 -174 S
ATOM 2069 CE MET B1004 8.309 -5.630 31.579 1.00 64.32 C
ANISOU 2069 CE MET B1004 8864 7890 7685 75 -910 5 C
ATOM 2070 N LEU B1005 5.387 -0.343 29.516 1.00 70.03 N
ANISOU 2070 N LEU B1005 9662 8172 8773 21 -744 -455 N
ATOM 2071 CA LEU B1005 4.068 -0.031 30.039 1.00 71.50 C
ANISOU 2071 CA LEU B1005 9847 8359 8961 71 -663 -495 C
ATOM 2072 C LEU B1005 3.170 0.592 28.985 1.00 71.21 C
ANISOU 2072 C LEU B1005 9802 8242 9014 200 -620 -488 C
ATOM 2073 O LEU B1005 1.949 0.357 29.000 1.00 71.24 O
ANISOU 2073 O LEU B1005 9733 8308 9027 272 -586 -474 O
ATOM 2074 CB LEU B1005 4.193 0.865 31.273 1.00 74.96 C
ANISOU 2074 CB LEU B1005 10360 8807 9313 0 -586 -602 C
ATOM 2075 CG LEU B1005 4.168 0.092 32.622 1.00 73.65 C
ANISOU 2075 CG LEU B1005 10161 8786 9035 -76 -598 -599 C
ATOM 2076 CD1 LEU B1005 2.887 -0.720 32.759 1.00 74.11 C
ANISOU 2076 CD1 LEU B1005 10156 8888 9116 -15 -574 -548 C
ATOM 2077 CD2 LEU B1005 5.409 -0.765 32.880 1.00 71.14 C
ANISOU 2077 CD2 LEU B1005 9809 8584 8637 -145 -695 -532 C
ATOM 2078 N ARG B1006 3.752 1.352 28.045 1.00 72.10 N
ANISOU 2078 N ARG B1006 9975 8243 9178 236 -617 -488 N
ATOM 2079 CA ARG B1006 2.963 1.864 26.925 1.00 70.20 C
ANISOU 2079 CA ARG B1006 9720 7950 9004 392 -583 -449 C
ATOM 2080 C ARG B1006 2.313 0.723 26.149 1.00 68.96 C
ANISOU 2080 C ARG B1006 9421 7908 8871 424 -662 -372 C
ATOM 2081 O ARG B1006 1.158 0.830 25.712 1.00 69.02 O
ANISOU 2081 O ARG B1006 9344 7995 8886 538 -634 -348 O
ATOM 2082 CB ARG B1006 3.839 2.708 26.011 1.00 69.75 C
ANISOU 2082 CB ARG B1006 9766 7749 8987 408 -567 -447 C
ATOM 2083 N ILE B1007 3.027 -0.398 26.019 1.00 68.00 N
ANISOU 2083 N ILE B1007 9274 7816 8746 319 -748 -337 N
ATOM 2084 CA ILE B1007 2.496 -1.577 25.336 1.00 68.95 C
ANISOU 2084 CA ILE B1007 9302 8018 8876 301 -796 -286 C
ATOM 2085 C ILE B1007 1.316 -2.172 26.092 1.00 72.43 C
ANISOU 2085 C ILE B1007 9667 8582 9272 266 -754 -306 C
ATOM 2086 O ILE B1007 0.196 -2.225 25.569 1.00 73.72 O
ANISOU 2086 O ILE B1007 9722 8857 9431 310 -739 -306 O
ATOM 2087 CB ILE B1007 3.595 -2.630 25.137 1.00 67.52 C
ANISOU 2087 CB ILE B1007 9158 7804 8694 214 -857 -241 C
ATOM 2088 CG1 ILE B1007 4.696 -2.025 24.245 1.00 64.76 C
ANISOU 2088 CG1 ILE B1007 8855 7364 8386 245 -895 -224 C
ATOM 2089 CG2 ILE B1007 2.967 -3.948 24.637 1.00 64.29 C
ANISOU 2089 CG2 ILE B1007 8701 7450 8278 158 -862 -211 C
ATOM 2090 CD1 ILE B1007 5.437 -3.024 23.433 1.00 63.83 C
ANISOU 2090 CD1 ILE B1007 8742 7228 8284 216 -947 -166 C
ATOM 2091 N ASP B1008 1.544 -2.674 27.315 1.00 71.90 N
ANISOU 2091 N ASP B1008 9640 8526 9153 181 -734 -319 N
ATOM 2092 CA ASP B1008 0.468 -3.468 27.908 1.00 75.32 C
ANISOU 2092 CA ASP B1008 10010 9069 9539 119 -688 -329 C
ATOM 2093 C ASP B1008 -0.518 -2.631 28.719 1.00 77.28 C
ANISOU 2093 C ASP B1008 10211 9395 9758 178 -614 -385 C
ATOM 2094 O ASP B1008 -1.625 -3.110 28.997 1.00 77.12 O
ANISOU 2094 O ASP B1008 10097 9504 9700 141 -569 -401 O
ATOM 2095 CB ASP B1008 0.980 -4.671 28.760 1.00 72.74 C
ANISOU 2095 CB ASP B1008 9756 8725 9156 9 -679 -292 C
ATOM 2096 CG ASP B1008 2.263 -4.397 29.539 1.00 69.44 C
ANISOU 2096 CG ASP B1008 9424 8258 8700 16 -708 -274 C
ATOM 2097 OD1 ASP B1008 3.167 -5.256 29.540 1.00 65.40 O
ANISOU 2097 OD1 ASP B1008 8970 7717 8163 -4 -735 -203 O
ATOM 2098 OD2 ASP B1008 2.362 -3.322 30.149 1.00 73.21 O1-
ANISOU 2098 OD2 ASP B1008 9912 8744 9159 42 -693 -332 O1-
ATOM 2099 N GLU B1009 -0.198 -1.380 29.041 1.00 81.83 N
ANISOU 2099 N GLU B1009 10852 9898 10343 265 -582 -422 N
ATOM 2100 CA GLU B1009 -1.201 -0.587 29.739 1.00 85.25 C
ANISOU 2100 CA GLU B1009 11256 10390 10746 348 -485 -472 C
ATOM 2101 C GLU B1009 -1.919 0.376 28.799 1.00 84.20 C
ANISOU 2101 C GLU B1009 11069 10273 10650 537 -444 -456 C
ATOM 2102 O GLU B1009 -3.151 0.390 28.788 1.00 86.52 O
ANISOU 2102 O GLU B1009 11230 10728 10915 621 -397 -451 O
ATOM 2103 CB GLU B1009 -0.597 0.169 30.941 1.00 86.80 C
ANISOU 2103 CB GLU B1009 11583 10501 10897 316 -427 -539 C
ATOM 2104 CG GLU B1009 -1.626 0.864 31.854 1.00 88.35 C
ANISOU 2104 CG GLU B1009 11772 10748 11047 390 -304 -600 C
ATOM 2105 CD GLU B1009 -1.536 0.497 33.347 1.00 88.71 C
ANISOU 2105 CD GLU B1009 11857 10847 11002 265 -273 -650 C
ATOM 2106 OE1 GLU B1009 -1.917 1.369 34.162 1.00 89.62 O
ANISOU 2106 OE1 GLU B1009 12034 10944 11074 309 -162 -724 O
ATOM 2107 OE2 GLU B1009 -1.069 -0.608 33.720 1.00 88.03 O1-
ANISOU 2107 OE2 GLU B1009 11760 10812 10877 139 -341 -611 O1-
ATOM 2108 N GLY B1010 -1.190 1.174 28.002 1.00 79.65 N
ANISOU 2108 N GLY B1010 10587 9554 10124 616 -453 -437 N
ATOM 2109 CA GLY B1010 -1.817 2.128 27.079 1.00 78.22 C
ANISOU 2109 CA GLY B1010 10382 9373 9964 834 -398 -394 C
ATOM 2110 C GLY B1010 -1.398 3.590 27.233 1.00 80.11 C
ANISOU 2110 C GLY B1010 10817 9402 10219 951 -276 -422 C
ATOM 2111 O GLY B1010 -0.984 4.008 28.316 1.00 83.15 O
ANISOU 2111 O GLY B1010 11332 9684 10578 865 -205 -505 O
ATOM 2112 N LEU B1011 -1.503 4.394 26.173 1.00 80.33 N
ANISOU 2112 N LEU B1011 10886 9361 10274 1138 -232 -357 N
ATOM 2113 CA LEU B1011 -1.031 5.776 26.194 1.00 82.04 C
ANISOU 2113 CA LEU B1011 11341 9326 10504 1235 -84 -380 C
ATOM 2114 C LEU B1011 -2.028 6.685 25.482 1.00 85.03 C
ANISOU 2114 C LEU B1011 11720 9718 10870 1565 37 -284 C
ATOM 2115 O LEU B1011 -2.333 6.476 24.302 1.00 88.54 O
ANISOU 2115 O LEU B1011 12042 10281 11318 1692 -35 -179 O
ATOM 2116 CB LEU B1011 0.346 5.889 25.534 1.00 81.29 C
ANISOU 2116 CB LEU B1011 11373 9062 10453 1102 -137 -387 C
ATOM 2117 CG LEU B1011 0.694 7.205 24.860 1.00 81.74 C
ANISOU 2117 CG LEU B1011 11648 8880 10530 1237 7 -363 C
ATOM 2118 CD1 LEU B1011 0.730 8.282 25.930 1.00 84.20 C
ANISOU 2118 CD1 LEU B1011 12188 8997 10807 1225 209 -468 C
ATOM 2119 CD2 LEU B1011 2.050 7.089 24.173 1.00 82.45 C
ANISOU 2119 CD2 LEU B1011 11810 8861 10655 1065 -70 -372 C
ATOM 2120 N ARG B1012 -2.518 7.695 26.202 1.00 86.57 N
ANISOU 2120 N ARG B1012 12059 9799 11036 1714 230 -314 N
ATOM 2121 CA ARG B1012 -3.479 8.674 25.709 1.00 88.69 C
ANISOU 2121 CA ARG B1012 12361 10062 11274 2083 391 -209 C
ATOM 2122 C ARG B1012 -2.969 10.075 26.060 1.00 91.01 C
ANISOU 2122 C ARG B1012 13024 9983 11573 2151 635 -260 C
ATOM 2123 O ARG B1012 -2.496 10.301 27.180 1.00 91.56 O
ANISOU 2123 O ARG B1012 13252 9904 11633 1951 713 -403 O
ATOM 2124 CB ARG B1012 -4.866 8.402 26.316 1.00 88.93 C
ANISOU 2124 CB ARG B1012 12176 10373 11242 2236 420 -189 C
ATOM 2125 N LEU B1013 -3.050 11.018 25.109 1.00 96.31 N
ANISOU 2125 N LEU B1013 13848 10498 12245 2420 769 -146 N
ATOM 2126 CA LEU B1013 -2.395 12.321 25.257 1.00 97.51 C
ANISOU 2126 CA LEU B1013 14405 10239 12404 2438 1021 -198 C
ATOM 2127 C LEU B1013 -3.350 13.511 25.420 1.00101.01 C
ANISOU 2127 C LEU B1013 15041 10540 12797 2834 1318 -120 C
ATOM 2128 O LEU B1013 -2.879 14.652 25.476 1.00103.98 O
ANISOU 2128 O LEU B1013 15801 10535 13171 2871 1574 -157 O
ATOM 2129 CB LEU B1013 -1.444 12.577 24.080 1.00 95.68 C
ANISOU 2129 CB LEU B1013 14303 9837 12213 2391 996 -141 C
ATOM 2130 CG LEU B1013 -0.137 11.776 24.001 1.00 92.97 C
ANISOU 2130 CG LEU B1013 13904 9505 11916 1984 791 -243 C
ATOM 2131 CD1 LEU B1013 0.331 11.611 22.562 1.00 91.71 C
ANISOU 2131 CD1 LEU B1013 13703 9356 11789 2033 689 -125 C
ATOM 2132 CD2 LEU B1013 0.954 12.428 24.841 1.00 98.15 C
ANISOU 2132 CD2 LEU B1013 14853 9874 12564 1683 930 -427 C
ATOM 2133 N LYS B1014 -4.665 13.287 25.508 1.00100.06 N
ANISOU 2133 N LYS B1014 14677 10715 12626 3129 1311 -18 N
ATOM 2134 CA LYS B1014 -5.613 14.321 25.930 1.00103.74 C
ANISOU 2134 CA LYS B1014 15302 11081 13032 3508 1601 42 C
ATOM 2135 C LYS B1014 -6.473 13.791 27.076 1.00104.85 C
ANISOU 2135 C LYS B1014 15225 11480 13132 3480 1571 -34 C
ATOM 2136 O LYS B1014 -6.733 12.588 27.157 1.00100.87 O
ANISOU 2136 O LYS B1014 14365 11331 12628 3305 1316 -51 O
ATOM 2137 CB LYS B1014 -6.514 14.787 24.778 1.00102.47 C
ANISOU 2137 CB LYS B1014 15053 11067 12814 4015 1674 292 C
ATOM 2138 N ILE B1015 -6.947 14.711 27.938 1.00106.80 N
ANISOU 2138 N ILE B1015 15705 11537 13337 3662 1857 -76 N
ATOM 2139 CA ILE B1015 -7.581 14.338 29.209 1.00105.51 C
ANISOU 2139 CA ILE B1015 15411 11543 13134 3581 1868 -187 C
ATOM 2140 C ILE B1015 -8.800 13.452 28.971 1.00105.59 C
ANISOU 2140 C ILE B1015 14945 12078 13094 3763 1694 -67 C
ATOM 2141 O ILE B1015 -9.700 13.806 28.198 1.00106.42 O
ANISOU 2141 O ILE B1015 14918 12374 13143 4187 1759 122 O
ATOM 2142 CB ILE B1015 -7.978 15.595 30.009 1.00108.49 C
ANISOU 2142 CB ILE B1015 16141 11618 13462 3818 2245 -230 C
ATOM 2143 CG1 ILE B1015 -6.825 16.101 30.887 1.00110.57 C
ANISOU 2143 CG1 ILE B1015 16803 11464 13744 3430 2380 -464 C
ATOM 2144 CG2 ILE B1015 -9.163 15.307 30.920 1.00108.64 C
ANISOU 2144 CG2 ILE B1015 15928 11935 13414 3966 2281 -238 C
ATOM 2145 CD1 ILE B1015 -6.960 17.568 31.308 1.00115.71 C
ANISOU 2145 CD1 ILE B1015 17932 11682 14351 3653 2811 -504 C
ATOM 2146 N TYR B1016 -8.846 12.303 29.666 1.00104.11 N
ANISOU 2146 N TYR B1016 14503 12145 12910 3438 1487 -176 N
ATOM 2147 CA TYR B1016 -9.999 11.398 29.682 1.00107.98 C
ANISOU 2147 CA TYR B1016 14558 13130 13339 3513 1347 -114 C
ATOM 2148 C TYR B1016 -10.456 11.124 31.121 1.00111.07 C
ANISOU 2148 C TYR B1016 14907 13603 13691 3375 1408 -246 C
ATOM 2149 O TYR B1016 -9.797 11.504 32.097 1.00109.62 O
ANISOU 2149 O TYR B1016 15009 13115 13525 3181 1520 -394 O
ATOM 2150 CB TYR B1016 -9.705 10.080 28.924 1.00106.29 C
ANISOU 2150 CB TYR B1016 14049 13182 13153 3242 1032 -98 C
ATOM 2151 CG TYR B1016 -8.659 9.141 29.515 1.00104.39 C
ANISOU 2151 CG TYR B1016 13854 12835 12975 2757 861 -251 C
ATOM 2152 CD1 TYR B1016 -8.981 7.823 29.843 1.00105.12 C
ANISOU 2152 CD1 TYR B1016 13664 13230 13047 2507 679 -295 C
ATOM 2153 CD2 TYR B1016 -7.343 9.559 29.699 1.00101.33 C
ANISOU 2153 CD2 TYR B1016 13789 12062 12650 2555 892 -342 C
ATOM 2154 CE1 TYR B1016 -8.026 6.958 30.366 1.00102.35 C
ANISOU 2154 CE1 TYR B1016 13369 12782 12738 2117 542 -404 C
ATOM 2155 CE2 TYR B1016 -6.385 8.704 30.215 1.00 99.55 C
ANISOU 2155 CE2 TYR B1016 13575 11792 12458 2156 735 -457 C
ATOM 2156 CZ TYR B1016 -6.727 7.407 30.545 1.00 99.44 C
ANISOU 2156 CZ TYR B1016 13294 12065 12424 1963 562 -476 C
ATOM 2157 OH TYR B1016 -5.755 6.574 31.056 1.00 96.81 O
ANISOU 2157 OH TYR B1016 12994 11678 12110 1617 428 -563 O
ATOM 2158 N LYS B1017 -11.624 10.484 31.245 1.00118.69 N
ANISOU 2158 N LYS B1017 15504 15008 14585 3470 1345 -196 N
ATOM 2159 CA LYS B1017 -12.252 10.185 32.528 1.00118.58 C
ANISOU 2159 CA LYS B1017 15401 15136 14517 3378 1409 -298 C
ATOM 2160 C LYS B1017 -12.374 8.674 32.677 1.00121.10 C
ANISOU 2160 C LYS B1017 15402 15782 14828 3020 1157 -350 C
ATOM 2161 O LYS B1017 -12.790 7.992 31.736 1.00123.37 O
ANISOU 2161 O LYS B1017 15395 16387 15094 3029 998 -263 O
ATOM 2162 CB LYS B1017 -13.630 10.849 32.629 1.00122.04 C
ANISOU 2162 CB LYS B1017 15695 15817 14857 3833 1610 -192 C
ATOM 2163 N ASP B1018 -12.014 8.153 33.849 1.00125.58 N
ANISOU 2163 N ASP B1018 16044 16272 15398 2701 1137 -493 N
ATOM 2164 CA ASP B1018 -11.952 6.710 34.050 1.00124.53 C
ANISOU 2164 CA ASP B1018 15694 16362 15261 2340 929 -541 C
ATOM 2165 C ASP B1018 -13.329 6.130 34.405 1.00126.29 C
ANISOU 2165 C ASP B1018 15576 17023 15387 2384 946 -527 C
ATOM 2166 O ASP B1018 -14.331 6.844 34.496 1.00127.59 O
ANISOU 2166 O ASP B1018 15640 17353 15484 2713 1106 -472 O
ATOM 2167 CB ASP B1018 -10.908 6.386 35.116 1.00125.60 C
ANISOU 2167 CB ASP B1018 16060 16241 15420 1999 900 -677 C
ATOM 2168 CG ASP B1018 -11.191 7.075 36.426 1.00127.86 C
ANISOU 2168 CG ASP B1018 16508 16426 15650 2052 1102 -772 C
ATOM 2169 OD1 ASP B1018 -12.282 7.671 36.555 1.00130.42 O
ANISOU 2169 OD1 ASP B1018 16741 16893 15919 2349 1266 -732 O
ATOM 2170 OD2 ASP B1018 -10.319 7.033 37.317 1.00125.17 O1-
ANISOU 2170 OD2 ASP B1018 16376 15879 15302 1806 1104 -886 O1-
ATOM 2171 N THR B1019 -13.387 4.803 34.599 1.00118.24 N
ANISOU 2171 N THR B1019 14376 16199 14349 2049 795 -573 N
ATOM 2172 CA THR B1019 -14.676 4.163 34.862 1.00115.04 C
ANISOU 2172 CA THR B1019 13635 16233 13843 2028 811 -573 C
ATOM 2173 C THR B1019 -15.380 4.814 36.047 1.00115.57 C
ANISOU 2173 C THR B1019 13734 16333 13844 2188 1015 -618 C
ATOM 2174 O THR B1019 -16.607 4.968 36.033 1.00115.01 O
ANISOU 2174 O THR B1019 13392 16627 13680 2396 1103 -574 O
ATOM 2175 CB THR B1019 -14.522 2.647 35.085 1.00111.07 C
ANISOU 2175 CB THR B1019 13027 15844 13328 1598 667 -636 C
ATOM 2176 OG1 THR B1019 -13.308 2.345 35.792 1.00111.74 O
ANISOU 2176 OG1 THR B1019 13407 15572 13476 1353 625 -704 O
ATOM 2177 CG2 THR B1019 -14.539 1.899 33.759 1.00112.65 C
ANISOU 2177 CG2 THR B1019 13036 16231 13534 1497 506 -584 C
ATOM 2178 N GLU B1020 -14.626 5.220 37.077 1.00116.41 N
ANISOU 2178 N GLU B1020 14157 16091 13981 2097 1099 -709 N
ATOM 2179 CA GLU B1020 -15.219 5.872 38.242 1.00116.20 C
ANISOU 2179 CA GLU B1020 14201 16061 13887 2234 1309 -769 C
ATOM 2180 C GLU B1020 -15.525 7.355 38.031 1.00126.43 C
ANISOU 2180 C GLU B1020 15642 17216 15180 2677 1524 -714 C
ATOM 2181 O GLU B1020 -16.299 7.925 38.811 1.00125.37 O
ANISOU 2181 O GLU B1020 15508 17154 14975 2875 1726 -738 O
ATOM 2182 CB GLU B1020 -14.307 5.715 39.459 1.00112.44 C
ANISOU 2182 CB GLU B1020 14006 15300 13417 1943 1323 -899 C
ATOM 2183 CG GLU B1020 -13.972 4.278 39.778 1.00107.17 C
ANISOU 2183 CG GLU B1020 13244 14736 12739 1546 1148 -932 C
ATOM 2184 CD GLU B1020 -13.636 4.076 41.238 1.00103.97 C
ANISOU 2184 CD GLU B1020 13006 14227 12272 1333 1209 -1039 C
ATOM 2185 OE1 GLU B1020 -13.215 2.954 41.591 1.00100.83 O
ANISOU 2185 OE1 GLU B1020 12594 13861 11857 1029 1087 -1052 O
ATOM 2186 OE2 GLU B1020 -13.812 5.031 42.032 1.00105.00 O1-
ANISOU 2186 OE2 GLU B1020 13290 14247 12358 1478 1392 -1106 O1-
ATOM 2187 N GLY B1021 -14.947 7.996 37.015 1.00159.86 N
ANISOU 2187 N GLY B1021 20020 21238 19483 2849 1510 -638 N
ATOM 2188 CA GLY B1021 -15.331 9.344 36.640 1.00160.94 C
ANISOU 2188 CA GLY B1021 20291 21255 19606 3311 1731 -550 C
ATOM 2189 C GLY B1021 -14.364 10.468 36.967 1.00161.08 C
ANISOU 2189 C GLY B1021 20788 20740 19676 3353 1908 -621 C
ATOM 2190 O GLY B1021 -14.751 11.640 36.863 1.00162.30 O
ANISOU 2190 O GLY B1021 21115 20746 19806 3744 2157 -561 O
ATOM 2191 N TYR B1022 -13.134 10.164 37.361 1.00133.87 N
ANISOU 2191 N TYR B1022 17564 17016 16285 2968 1805 -747 N
ATOM 2192 CA TYR B1022 -12.159 11.208 37.626 1.00127.78 C
ANISOU 2192 CA TYR B1022 17235 15772 15545 2943 1969 -838 C
ATOM 2193 C TYR B1022 -11.344 11.519 36.360 1.00123.63 C
ANISOU 2193 C TYR B1022 16830 15041 15103 2986 1894 -756 C
ATOM 2194 O TYR B1022 -11.444 10.839 35.334 1.00122.39 O
ANISOU 2194 O TYR B1022 16417 15105 14980 3002 1691 -639 O
ATOM 2195 CB TYR B1022 -11.246 10.810 38.793 1.00123.81 C
ANISOU 2195 CB TYR B1022 16895 15125 15022 2506 1914 -1026 C
ATOM 2196 CG TYR B1022 -11.926 10.197 40.021 1.00124.01 C
ANISOU 2196 CG TYR B1022 16766 15393 14961 2382 1926 -1102 C
ATOM 2197 CD1 TYR B1022 -11.963 8.816 40.205 1.00121.31 C
ANISOU 2197 CD1 TYR B1022 16149 15332 14609 2108 1691 -1094 C
ATOM 2198 CD2 TYR B1022 -12.494 10.998 41.003 1.00121.56 C
ANISOU 2198 CD2 TYR B1022 16612 15002 14573 2530 2193 -1185 C
ATOM 2199 CE1 TYR B1022 -12.553 8.261 41.322 1.00115.89 C
ANISOU 2199 CE1 TYR B1022 15346 14849 13839 1984 1718 -1158 C
ATOM 2200 CE2 TYR B1022 -13.083 10.453 42.119 1.00118.55 C
ANISOU 2200 CE2 TYR B1022 16097 14839 14107 2409 2209 -1255 C
ATOM 2201 CZ TYR B1022 -13.111 9.084 42.276 1.00116.40 C
ANISOU 2201 CZ TYR B1022 15547 14852 13826 2133 1969 -1238 C
ATOM 2202 OH TYR B1022 -13.701 8.529 43.390 1.00113.38 O
ANISOU 2202 OH TYR B1022 15047 14679 13352 2006 2000 -1301 O
ATOM 2203 N TYR B1023 -10.528 12.571 36.445 1.00116.60 N
ANISOU 2203 N TYR B1023 16348 13721 14232 2985 2076 -831 N
ATOM 2204 CA TYR B1023 -9.743 13.062 35.314 1.00110.16 C
ANISOU 2204 CA TYR B1023 15710 12660 13487 3038 2064 -762 C
ATOM 2205 C TYR B1023 -8.332 12.476 35.340 1.00108.69 C
ANISOU 2205 C TYR B1023 15600 12348 13349 2576 1857 -875 C
ATOM 2206 O TYR B1023 -7.613 12.615 36.337 1.00107.65 O
ANISOU 2206 O TYR B1023 15672 12049 13182 2281 1908 -1052 O
ATOM 2207 CB TYR B1023 -9.682 14.593 35.333 1.00111.23 C
ANISOU 2207 CB TYR B1023 16275 12381 13606 3302 2422 -775 C
ATOM 2208 N THR B1024 -7.930 11.836 34.236 1.00108.31 N
ANISOU 2208 N THR B1024 15382 12405 13365 2523 1630 -773 N
ATOM 2209 CA THR B1024 -6.641 11.164 34.147 1.00105.36 C
ANISOU 2209 CA THR B1024 15029 11969 13033 2130 1420 -850 C
ATOM 2210 C THR B1024 -5.989 11.487 32.804 1.00103.89 C
ANISOU 2210 C THR B1024 14929 11627 12918 2200 1376 -756 C
ATOM 2211 O THR B1024 -6.604 12.094 31.924 1.00104.93 O
ANISOU 2211 O THR B1024 15069 11738 13060 2555 1481 -616 O
ATOM 2212 CB THR B1024 -6.789 9.647 34.350 1.00105.02 C
ANISOU 2212 CB THR B1024 14645 12270 12987 1913 1151 -836 C
ATOM 2213 OG1 THR B1024 -7.048 8.991 33.108 1.00103.35 O
ANISOU 2213 OG1 THR B1024 14190 12255 12825 2009 977 -692 O
ATOM 2214 CG2 THR B1024 -7.940 9.369 35.302 1.00108.56 C
ANISOU 2214 CG2 THR B1024 14932 12950 13364 1991 1219 -856 C
ATOM 2215 N ILE B1025 -4.717 11.100 32.660 1.00100.67 N
ANISOU 2215 N ILE B1025 14584 11122 12544 1874 1228 -826 N
ATOM 2216 CA ILE B1025 -3.923 11.436 31.473 1.00 97.08 C
ANISOU 2216 CA ILE B1025 14242 10493 12150 1886 1197 -763 C
ATOM 2217 C ILE B1025 -2.724 10.485 31.372 1.00 93.42 C
ANISOU 2217 C ILE B1025 13687 10094 11714 1520 951 -816 C
ATOM 2218 O ILE B1025 -2.169 10.058 32.390 1.00 93.03 O
ANISOU 2218 O ILE B1025 13641 10088 11619 1236 892 -943 O
ATOM 2219 CB ILE B1025 -3.486 12.929 31.512 1.00 97.29 C
ANISOU 2219 CB ILE B1025 14692 10110 12164 1954 1496 -831 C
ATOM 2220 CG1 ILE B1025 -3.575 13.580 30.122 1.00 96.68 C
ANISOU 2220 CG1 ILE B1025 14711 9890 12132 2250 1577 -669 C
ATOM 2221 CG2 ILE B1025 -2.102 13.097 32.151 1.00 96.01 C
ANISOU 2221 CG2 ILE B1025 14742 9762 11975 1529 1500 -1027 C
ATOM 2222 CD1 ILE B1025 -4.961 13.747 29.557 1.00100.65 C
ANISOU 2222 CD1 ILE B1025 15053 10569 12618 2720 1643 -477 C
ATOM 2223 N GLY B1026 -2.331 10.156 30.128 1.00 91.19 N
ANISOU 2223 N GLY B1026 13320 9835 11494 1550 815 -709 N
ATOM 2224 CA GLY B1026 -1.042 9.510 29.880 1.00 89.57 C
ANISOU 2224 CA GLY B1026 13091 9628 11315 1248 634 -752 C
ATOM 2225 C GLY B1026 -1.086 7.993 29.931 1.00 87.26 C
ANISOU 2225 C GLY B1026 12501 9625 11028 1113 385 -713 C
ATOM 2226 O GLY B1026 -1.976 7.357 29.371 1.00 87.22 O
ANISOU 2226 O GLY B1026 12278 9821 11041 1263 300 -606 O
ATOM 2227 N ILE B1027 -0.089 7.408 30.591 1.00 83.12 N
ANISOU 2227 N ILE B1027 11976 9130 10474 822 280 -799 N
ATOM 2228 CA ILE B1027 -0.216 6.032 31.146 1.00 83.60 C
ANISOU 2228 CA ILE B1027 11823 9433 10509 691 113 -784 C
ATOM 2229 C ILE B1027 -0.778 6.183 32.557 1.00 84.79 C
ANISOU 2229 C ILE B1027 12002 9635 10579 654 214 -874 C
ATOM 2230 O ILE B1027 -0.062 6.167 33.565 1.00 85.23 O
ANISOU 2230 O ILE B1027 12136 9688 10559 447 216 -977 O
ATOM 2231 CB ILE B1027 1.110 5.260 31.127 1.00 81.59 C
ANISOU 2231 CB ILE B1027 11540 9215 10244 454 -44 -796 C
ATOM 2232 CG1 ILE B1027 1.729 5.238 29.713 1.00 79.20 C
ANISOU 2232 CG1 ILE B1027 11233 8840 10018 491 -121 -718 C
ATOM 2233 CG2 ILE B1027 0.918 3.878 31.763 1.00 81.09 C
ANISOU 2233 CG2 ILE B1027 11307 9362 10142 357 -170 -763 C
ATOM 2234 CD1 ILE B1027 3.249 5.238 29.702 1.00 75.71 C
ANISOU 2234 CD1 ILE B1027 10862 8351 9555 282 -183 -769 C
ATOM 2235 N GLY B1028 -2.094 6.350 32.627 1.00 87.19 N
ANISOU 2235 N GLY B1028 12229 10016 10882 863 303 -834 N
ATOM 2236 CA GLY B1028 -2.818 6.242 33.883 1.00 90.63 C
ANISOU 2236 CA GLY B1028 12635 10556 11243 844 380 -898 C
ATOM 2237 C GLY B1028 -2.438 7.192 34.997 1.00 91.84 C
ANISOU 2237 C GLY B1028 13021 10553 11322 752 545 -1045 C
ATOM 2238 O GLY B1028 -2.371 6.773 36.160 1.00 91.29 O
ANISOU 2238 O GLY B1028 12934 10585 11169 590 532 -1120 O
ATOM 2239 N HIS B1029 -2.207 8.467 34.680 1.00 92.55 N
ANISOU 2239 N HIS B1029 13346 10392 11427 844 719 -1091 N
ATOM 2240 CA HIS B1029 -1.974 9.484 35.702 1.00 92.62 C
ANISOU 2240 CA HIS B1029 13614 10224 11354 753 926 -1252 C
ATOM 2241 C HIS B1029 -3.299 10.140 36.069 1.00 95.53 C
ANISOU 2241 C HIS B1029 14028 10563 11706 1033 1139 -1242 C
ATOM 2242 O HIS B1029 -3.873 10.876 35.262 1.00 95.88 O
ANISOU 2242 O HIS B1029 14146 10482 11801 1327 1273 -1154 O
ATOM 2243 CB HIS B1029 -0.977 10.543 35.238 1.00 91.08 C
ANISOU 2243 CB HIS B1029 13698 9739 11167 664 1047 -1330 C
ATOM 2244 CG HIS B1029 -0.523 11.441 36.344 1.00 93.62 C
ANISOU 2244 CG HIS B1029 14291 9901 11380 462 1245 -1535 C
ATOM 2245 ND1 HIS B1029 0.697 11.298 36.970 1.00 94.79 N
ANISOU 2245 ND1 HIS B1029 14479 10103 11432 93 1169 -1678 N
ATOM 2246 CD2 HIS B1029 -1.156 12.454 36.985 1.00 96.95 C
ANISOU 2246 CD2 HIS B1029 14947 10140 11751 570 1524 -1629 C
ATOM 2247 CE1 HIS B1029 0.810 12.205 37.927 1.00 96.03 C
ANISOU 2247 CE1 HIS B1029 14885 10121 11479 -50 1388 -1866 C
ATOM 2248 NE2 HIS B1029 -0.303 12.918 37.958 1.00 97.36 N
ANISOU 2248 NE2 HIS B1029 15194 10118 11680 236 1615 -1842 N
ATOM 2249 N LEU B1030 -3.763 9.896 37.297 1.00 99.49 N
ANISOU 2249 N LEU B1030 14490 11188 12122 958 1181 -1322 N
ATOM 2250 CA LEU B1030 -4.949 10.557 37.826 1.00100.36 C
ANISOU 2250 CA LEU B1030 14658 11277 12197 1205 1406 -1335 C
ATOM 2251 C LEU B1030 -4.610 11.995 38.190 1.00102.22 C
ANISOU 2251 C LEU B1030 15281 11168 12389 1214 1696 -1472 C
ATOM 2252 O LEU B1030 -3.675 12.236 38.962 1.00102.92 O
ANISOU 2252 O LEU B1030 15548 11159 12397 900 1727 -1644 O
ATOM 2253 CB LEU B1030 -5.469 9.803 39.040 1.00100.58 C
ANISOU 2253 CB LEU B1030 14533 11544 12140 1090 1361 -1387 C
ATOM 2254 CG LEU B1030 -6.657 10.398 39.800 1.00104.41 C
ANISOU 2254 CG LEU B1030 15061 12044 12567 1307 1594 -1421 C
ATOM 2255 CD1 LEU B1030 -8.007 9.800 39.401 1.00107.90 C
ANISOU 2255 CD1 LEU B1030 15188 12772 13038 1571 1548 -1269 C
ATOM 2256 CD2 LEU B1030 -6.414 10.205 41.273 1.00102.28 C
ANISOU 2256 CD2 LEU B1030 14856 11832 12174 1046 1624 -1577 C
ATOM 2257 N LEU B1031 -5.369 12.948 37.625 1.00103.65 N
ANISOU 2257 N LEU B1031 15599 11177 12606 1574 1921 -1396 N
ATOM 2258 CA LEU B1031 -5.144 14.379 37.860 1.00108.01 C
ANISOU 2258 CA LEU B1031 16577 11342 13121 1627 2255 -1511 C
ATOM 2259 C LEU B1031 -5.847 14.886 39.127 1.00113.17 C
ANISOU 2259 C LEU B1031 17369 11956 13674 1679 2496 -1634 C
ATOM 2260 O LEU B1031 -5.219 15.548 39.964 1.00114.36 O
ANISOU 2260 O LEU B1031 17823 11890 13738 1426 2670 -1841 O
ATOM 2261 CB LEU B1031 -5.596 15.191 36.646 1.00109.69 C
ANISOU 2261 CB LEU B1031 16912 11358 13405 2030 2417 -1347 C
ATOM 2262 CG LEU B1031 -4.816 14.971 35.351 1.00106.66 C
ANISOU 2262 CG LEU B1031 16484 10933 13109 1983 2245 -1244 C
ATOM 2263 CD1 LEU B1031 -5.524 15.645 34.193 1.00109.23 C
ANISOU 2263 CD1 LEU B1031 16867 11153 13483 2451 2390 -1042 C
ATOM 2264 CD2 LEU B1031 -3.398 15.486 35.504 1.00106.32 C
ANISOU 2264 CD2 LEU B1031 16747 10609 13043 1602 2304 -1423 C
ATOM 2265 N THR B1032 -7.152 14.627 39.268 1.00116.86 N
ANISOU 2265 N THR B1032 17620 12641 14139 1995 2526 -1519 N
ATOM 2266 CA THR B1032 -7.896 15.015 40.466 1.00119.27 C
ANISOU 2266 CA THR B1032 18020 12949 14350 2065 2747 -1624 C
ATOM 2267 C THR B1032 -9.190 14.217 40.550 1.00119.52 C
ANISOU 2267 C THR B1032 17658 13376 14380 2307 2644 -1483 C
ATOM 2268 O THR B1032 -9.795 13.869 39.531 1.00117.38 O
ANISOU 2268 O THR B1032 17132 13292 14174 2574 2535 -1289 O
ATOM 2269 CB THR B1032 -8.242 16.519 40.513 1.00125.26 C
ANISOU 2269 CB THR B1032 19197 13318 15079 2351 3169 -1664 C
ATOM 2270 OG1 THR B1032 -8.703 16.968 39.229 1.00131.16 O
ANISOU 2270 OG1 THR B1032 19943 13985 15907 2774 3241 -1450 O
ATOM 2271 CG2 THR B1032 -7.053 17.366 40.985 1.00124.13 C
ANISOU 2271 CG2 THR B1032 19501 12786 14877 1997 3350 -1900 C
ATOM 2272 N LYS B1033 -9.630 13.976 41.785 1.00120.49 N
ANISOU 2272 N LYS B1033 17736 13634 14410 2202 2699 -1591 N
ATOM 2273 CA LYS B1033 -10.925 13.361 42.029 1.00119.25 C
ANISOU 2273 CA LYS B1033 17240 13840 14229 2417 2665 -1488 C
ATOM 2274 C LYS B1033 -12.069 14.362 41.932 1.00122.44 C
ANISOU 2274 C LYS B1033 17727 14184 14609 2908 2981 -1409 C
ATOM 2275 O LYS B1033 -13.236 13.952 41.956 1.00122.53 O
ANISOU 2275 O LYS B1033 17424 14537 14595 3146 2969 -1299 O
ATOM 2276 CB LYS B1033 -10.938 12.673 43.401 1.00113.45 C
ANISOU 2276 CB LYS B1033 16425 13285 13396 2110 2604 -1625 C
ATOM 2277 N SER B1034 -11.754 15.654 41.794 1.00123.14 N
ANISOU 2277 N SER B1034 18236 13856 14697 3067 3276 -1457 N
ATOM 2278 CA SER B1034 -12.771 16.697 41.764 1.00127.99 C
ANISOU 2278 CA SER B1034 18998 14358 15276 3570 3628 -1376 C
ATOM 2279 C SER B1034 -13.551 16.654 40.452 1.00130.66 C
ANISOU 2279 C SER B1034 19068 14910 15667 4027 3571 -1105 C
ATOM 2280 O SER B1034 -12.974 16.393 39.393 1.00131.90 O
ANISOU 2280 O SER B1034 19162 15052 15902 3973 3379 -1012 O
ATOM 2281 CB SER B1034 -12.127 18.076 41.936 1.00132.44 C
ANISOU 2281 CB SER B1034 20142 14361 15818 3586 3986 -1506 C
ATOM 2282 OG SER B1034 -13.025 19.112 41.579 1.00136.48 O
ANISOU 2282 OG SER B1034 20830 14715 16312 4150 4335 -1370 O
ATOM 2283 N PRO B1035 -14.861 16.916 40.487 1.00138.90 N
ANISOU 2283 N PRO B1035 19937 16186 16652 4488 3737 -973 N
ATOM 2284 CA PRO B1035 -15.629 16.945 39.232 1.00140.96 C
ANISOU 2284 CA PRO B1035 19926 16706 16928 4950 3694 -707 C
ATOM 2285 C PRO B1035 -15.181 18.036 38.277 1.00144.45 C
ANISOU 2285 C PRO B1035 20737 16738 17410 5242 3896 -600 C
ATOM 2286 O PRO B1035 -15.246 17.842 37.055 1.00142.84 O
ANISOU 2286 O PRO B1035 20336 16695 17241 5429 3742 -410 O
ATOM 2287 CB PRO B1035 -17.068 17.179 39.711 1.00138.66 C
ANISOU 2287 CB PRO B1035 19428 16724 16533 5384 3896 -618 C
ATOM 2288 CG PRO B1035 -16.913 17.886 41.012 1.00138.15 C
ANISOU 2288 CG PRO B1035 19765 16307 16418 5291 4201 -822 C
ATOM 2289 CD PRO B1035 -15.685 17.294 41.647 1.00136.62 C
ANISOU 2289 CD PRO B1035 19707 15937 16265 4636 3997 -1056 C
ATOM 2290 N SER B1036 -14.734 19.180 38.797 1.00150.30 N
ANISOU 2290 N SER B1036 22022 16951 18135 5274 4252 -721 N
ATOM 2291 CA SER B1036 -14.419 20.317 37.942 1.00150.83 C
ANISOU 2291 CA SER B1036 22428 16645 18235 5466 4418 -583 C
ATOM 2292 C SER B1036 -13.281 19.968 36.994 1.00149.52 C
ANISOU 2292 C SER B1036 22325 16329 18158 5231 4223 -594 C
ATOM 2293 O SER B1036 -12.239 19.459 37.416 1.00150.01 O
ANISOU 2293 O SER B1036 22469 16273 18257 4718 4071 -807 O
ATOM 2294 CB SER B1036 -14.047 21.538 38.793 1.00151.83 C
ANISOU 2294 CB SER B1036 23077 16281 18332 5297 4731 -722 C
ATOM 2295 OG SER B1036 -12.641 21.732 38.873 1.00151.57 O
ANISOU 2295 OG SER B1036 23396 15851 18342 4818 4725 -924 O
ATOM 2296 N LEU B1037 -13.498 20.216 35.700 1.00146.98 N
ANISOU 2296 N LEU B1037 21896 16089 17860 5524 4153 -336 N
ATOM 2297 CA LEU B1037 -12.419 20.056 34.732 1.00143.14 C
ANISOU 2297 CA LEU B1037 21510 15422 17455 5321 3999 -328 C
ATOM 2298 C LEU B1037 -11.328 21.085 34.965 1.00144.33 C
ANISOU 2298 C LEU B1037 22204 15008 17626 4994 4200 -467 C
ATOM 2299 O LEU B1037 -10.146 20.824 34.707 1.00143.48 O
ANISOU 2299 O LEU B1037 22231 14705 17578 4622 4084 -598 O
ATOM 2300 CB LEU B1037 -12.960 20.169 33.309 1.00137.38 C
ANISOU 2300 CB LEU B1037 20551 14929 16717 5713 3898 -13 C
ATOM 2301 CG LEU B1037 -11.942 20.093 32.166 1.00132.41 C
ANISOU 2301 CG LEU B1037 20017 14131 16163 5556 3751 35 C
ATOM 2302 CD1 LEU B1037 -11.030 21.311 32.072 1.00131.93 C
ANISOU 2302 CD1 LEU B1037 20494 13517 16115 5363 3982 -10 C
ATOM 2303 CD2 LEU B1037 -11.103 18.857 32.353 1.00130.14 C
ANISOU 2303 CD2 LEU B1037 19547 13950 15951 5109 3450 -155 C
ATOM 2304 N SER B1038 -11.712 22.267 35.439 1.00146.54 N
ANISOU 2304 N SER B1038 22792 15042 17844 5121 4506 -438 N
ATOM 2305 CA SER B1038 -10.750 23.334 35.670 1.00148.33 C
ANISOU 2305 CA SER B1038 23533 14759 18065 4808 4733 -563 C
ATOM 2306 C SER B1038 -9.581 22.848 36.518 1.00154.04 C
ANISOU 2306 C SER B1038 24383 15336 18811 4211 4646 -901 C
ATOM 2307 O SER B1038 -8.416 22.985 36.129 1.00153.00 O
ANISOU 2307 O SER B1038 24442 14977 18714 3860 4598 -994 O
ATOM 2308 CB SER B1038 -11.456 24.503 36.357 1.00148.22 C
ANISOU 2308 CB SER B1038 23806 14545 17965 5013 5087 -522 C
ATOM 2309 OG SER B1038 -12.142 24.054 37.516 1.00149.55 O
ANISOU 2309 OG SER B1038 23807 14920 18094 5030 5099 -649 O
ATOM 2310 N VAL B1039 -9.878 22.245 37.672 1.00159.29 N
ANISOU 2310 N VAL B1039 24919 16168 19434 4083 4616 -1084 N
ATOM 2311 CA VAL B1039 -8.820 21.809 38.581 1.00159.25 C
ANISOU 2311 CA VAL B1039 25030 16070 19406 3511 4540 -1406 C
ATOM 2312 C VAL B1039 -7.946 20.723 37.942 1.00158.67 C
ANISOU 2312 C VAL B1039 24761 16130 19398 3272 4224 -1453 C
ATOM 2313 O VAL B1039 -6.747 20.623 38.239 1.00158.81 O
ANISOU 2313 O VAL B1039 24934 16006 19401 2772 4152 -1666 O
ATOM 2314 CB VAL B1039 -9.440 21.363 39.924 1.00160.57 C
ANISOU 2314 CB VAL B1039 25085 16433 19492 3466 4581 -1565 C
ATOM 2315 CG1 VAL B1039 -10.291 22.491 40.510 1.00161.65 C
ANISOU 2315 CG1 VAL B1039 25437 16416 19569 3716 4905 -1508 C
ATOM 2316 CG2 VAL B1039 -10.279 20.101 39.745 1.00160.53 C
ANISOU 2316 CG2 VAL B1039 24558 16928 19506 3700 4316 -1439 C
ATOM 2317 N ALA B1040 -8.521 19.897 37.060 1.00146.72 N
ANISOU 2317 N ALA B1040 22815 14984 17948 3542 3955 -1222 N
ATOM 2318 CA ALA B1040 -7.726 18.896 36.353 1.00137.57 C
ANISOU 2318 CA ALA B1040 21362 14045 16864 3241 3553 -1187 C
ATOM 2319 C ALA B1040 -6.686 19.551 35.448 1.00136.71 C
ANISOU 2319 C ALA B1040 21576 13565 16801 3138 3637 -1188 C
ATOM 2320 O ALA B1040 -5.549 19.073 35.345 1.00132.92 O
ANISOU 2320 O ALA B1040 21062 13093 16348 2696 3420 -1300 O
ATOM 2321 CB ALA B1040 -8.642 17.973 35.549 1.00132.84 C
ANISOU 2321 CB ALA B1040 20254 13913 16308 3546 3281 -941 C
ATOM 2322 N LYS B1041 -7.062 20.637 34.765 1.00150.81 N
ANISOU 2322 N LYS B1041 23640 15070 18589 3527 3928 -1038 N
ATOM 2323 CA LYS B1041 -6.103 21.369 33.940 1.00147.90 C
ANISOU 2323 CA LYS B1041 23537 14408 18252 3350 3981 -1003 C
ATOM 2324 C LYS B1041 -5.044 22.069 34.791 1.00151.94 C
ANISOU 2324 C LYS B1041 24417 14606 18708 2826 4144 -1270 C
ATOM 2325 O LYS B1041 -3.864 22.098 34.422 1.00149.22 O
ANISOU 2325 O LYS B1041 24185 14131 18381 2455 4070 -1367 O
ATOM 2326 CB LYS B1041 -6.836 22.378 33.059 1.00141.50 C
ANISOU 2326 CB LYS B1041 22826 13512 17425 3803 4173 -714 C
ATOM 2327 N SER B1042 -5.446 22.650 35.927 1.00148.33 N
ANISOU 2327 N SER B1042 24136 14054 18170 2780 4368 -1389 N
ATOM 2328 CA SER B1042 -4.495 23.355 36.787 1.00147.25 C
ANISOU 2328 CA SER B1042 24331 13664 17955 2272 4534 -1644 C
ATOM 2329 C SER B1042 -3.504 22.392 37.430 1.00145.98 C
ANISOU 2329 C SER B1042 24033 13667 17766 1755 4288 -1913 C
ATOM 2330 O SER B1042 -2.288 22.616 37.389 1.00145.49 O
ANISOU 2330 O SER B1042 24108 13497 17674 1303 4262 -2060 O
ATOM 2331 CB SER B1042 -5.240 24.144 37.868 1.00149.95 C
ANISOU 2331 CB SER B1042 24875 13891 18210 2366 4826 -1701 C
ATOM 2332 OG SER B1042 -6.147 25.073 37.306 1.00150.80 O
ANISOU 2332 OG SER B1042 25125 13852 18320 2848 5068 -1443 O
ATOM 2333 N GLU B1043 -4.005 21.315 38.040 1.00146.52 N
ANISOU 2333 N GLU B1043 23824 14026 17822 1809 4114 -1976 N
ATOM 2334 CA GLU B1043 -3.105 20.298 38.563 1.00142.13 C
ANISOU 2334 CA GLU B1043 23078 13702 17223 1341 3832 -2174 C
ATOM 2335 C GLU B1043 -2.147 19.841 37.472 1.00139.62 C
ANISOU 2335 C GLU B1043 22616 13447 16986 1174 3571 -2091 C
ATOM 2336 O GLU B1043 -0.978 19.548 37.743 1.00138.81 O
ANISOU 2336 O GLU B1043 22490 13421 16832 694 3420 -2259 O
ATOM 2337 CB GLU B1043 -3.909 19.122 39.125 1.00136.36 C
ANISOU 2337 CB GLU B1043 21872 13444 16494 1440 3546 -2086 C
ATOM 2338 N LEU B1044 -2.627 19.800 36.223 1.00144.43 N
ANISOU 2338 N LEU B1044 23123 14046 17708 1578 3524 -1831 N
ATOM 2339 CA LEU B1044 -1.767 19.492 35.083 1.00141.85 C
ANISOU 2339 CA LEU B1044 22706 13732 17457 1462 3324 -1743 C
ATOM 2340 C LEU B1044 -0.727 20.585 34.853 1.00144.65 C
ANISOU 2340 C LEU B1044 23505 13680 17776 1186 3579 -1885 C
ATOM 2341 O LEU B1044 0.446 20.292 34.586 1.00142.10 O
ANISOU 2341 O LEU B1044 23161 13383 17448 802 3428 -1992 O
ATOM 2342 CB LEU B1044 -2.630 19.284 33.835 1.00138.37 C
ANISOU 2342 CB LEU B1044 22066 13390 17118 1977 3245 -1432 C
ATOM 2343 CG LEU B1044 -2.057 18.710 32.532 1.00132.25 C
ANISOU 2343 CG LEU B1044 21084 12733 16432 1961 2978 -1281 C
ATOM 2344 CD1 LEU B1044 -3.139 18.689 31.469 1.00133.69 C
ANISOU 2344 CD1 LEU B1044 21105 13022 16669 2515 2970 -989 C
ATOM 2345 CD2 LEU B1044 -0.846 19.491 32.026 1.00134.10 C
ANISOU 2345 CD2 LEU B1044 21684 12605 16664 1695 3132 -1383 C
ATOM 2346 N ASP B1045 -1.137 21.851 34.949 1.00146.74 N
ANISOU 2346 N ASP B1045 24050 13699 18007 1330 3894 -1823 N
ATOM 2347 CA ASP B1045 -0.218 22.950 34.666 1.00147.71 C
ANISOU 2347 CA ASP B1045 24483 13552 18088 1043 4090 -1873 C
ATOM 2348 C ASP B1045 0.967 22.956 35.625 1.00146.59 C
ANISOU 2348 C ASP B1045 24410 13450 17836 410 4064 -2182 C
ATOM 2349 O ASP B1045 2.115 23.136 35.200 1.00145.45 O
ANISOU 2349 O ASP B1045 24322 13270 17673 57 4024 -2255 O
ATOM 2350 CB ASP B1045 -0.961 24.283 34.727 1.00151.57 C
ANISOU 2350 CB ASP B1045 25290 13764 18535 1320 4465 -1754 C
ATOM 2351 CG ASP B1045 -0.544 25.222 33.622 1.00152.76 C
ANISOU 2351 CG ASP B1045 25683 13664 18696 1375 4637 -1602 C
ATOM 2352 OD1 ASP B1045 -0.320 26.422 33.894 1.00154.30 O
ANISOU 2352 OD1 ASP B1045 26246 13576 18806 1237 4966 -1649 O
ATOM 2353 OD2 ASP B1045 -0.440 24.745 32.473 1.00149.29 O1-
ANISOU 2353 OD2 ASP B1045 25071 13312 18340 1552 4452 -1436 O1-
ATOM 2354 N LYS B1046 0.714 22.758 36.923 1.00139.30 N
ANISOU 2354 N LYS B1046 23461 12642 16824 255 4082 -2362 N
ATOM 2355 CA LYS B1046 1.802 22.733 37.898 1.00136.57 C
ANISOU 2355 CA LYS B1046 23135 12414 16343 -344 4038 -2647 C
ATOM 2356 C LYS B1046 2.781 21.605 37.591 1.00132.56 C
ANISOU 2356 C LYS B1046 22338 12191 15839 -632 3682 -2720 C
ATOM 2357 O LYS B1046 4.000 21.767 37.731 1.00131.35 O
ANISOU 2357 O LYS B1046 22196 12116 15596 -1104 3638 -2875 O
ATOM 2358 CB LYS B1046 1.242 22.600 39.319 1.00136.49 C
ANISOU 2358 CB LYS B1046 23110 12523 16228 -409 4093 -2803 C
ATOM 2359 N ALA B1047 2.262 20.439 37.197 1.00137.46 N
ANISOU 2359 N ALA B1047 22687 12994 16548 -356 3433 -2609 N
ATOM 2360 CA ALA B1047 3.140 19.348 36.790 1.00133.54 C
ANISOU 2360 CA ALA B1047 21867 12804 16069 -582 3067 -2602 C
ATOM 2361 C ALA B1047 3.840 19.659 35.470 1.00134.42 C
ANISOU 2361 C ALA B1047 22080 12728 16264 -590 3077 -2515 C
ATOM 2362 O ALA B1047 5.069 19.584 35.388 1.00134.74 O
ANISOU 2362 O ALA B1047 22086 12868 16242 -1007 2977 -2642 O
ATOM 2363 CB ALA B1047 2.356 18.038 36.694 1.00127.08 C
ANISOU 2363 CB ALA B1047 20568 12376 15341 -283 2720 -2373 C
ATOM 2364 N ILE B1048 3.084 20.039 34.428 1.00133.69 N
ANISOU 2364 N ILE B1048 22084 12412 16299 -130 3192 -2281 N
ATOM 2365 CA ILE B1048 3.705 20.204 33.108 1.00134.49 C
ANISOU 2365 CA ILE B1048 22204 12414 16482 -109 3147 -2147 C
ATOM 2366 C ILE B1048 4.704 21.354 33.104 1.00139.02 C
ANISOU 2366 C ILE B1048 23034 12814 16972 -481 3360 -2256 C
ATOM 2367 O ILE B1048 5.697 21.314 32.364 1.00137.99 O
ANISOU 2367 O ILE B1048 22873 12705 16853 -702 3272 -2258 O
ATOM 2368 CB ILE B1048 2.660 20.392 31.987 1.00135.36 C
ANISOU 2368 CB ILE B1048 22323 12390 16716 476 3210 -1844 C
ATOM 2369 CG1 ILE B1048 3.337 20.200 30.612 1.00131.14 C
ANISOU 2369 CG1 ILE B1048 21726 11838 16262 483 3077 -1710 C
ATOM 2370 CG2 ILE B1048 1.957 21.738 32.126 1.00142.10 C
ANISOU 2370 CG2 ILE B1048 23475 12983 17534 706 3569 -1761 C
ATOM 2371 CD1 ILE B1048 2.466 20.468 29.405 1.00130.92 C
ANISOU 2371 CD1 ILE B1048 21695 11724 16324 1017 3131 -1405 C
ATOM 2372 N GLY B1049 4.459 22.396 33.894 1.00135.98 N
ANISOU 2372 N GLY B1049 22913 12257 16497 -557 3657 -2343 N
ATOM 2373 CA GLY B1049 5.359 23.543 33.892 1.00137.77 C
ANISOU 2373 CA GLY B1049 23415 12302 16628 -913 3904 -2446 C
ATOM 2374 C GLY B1049 5.473 24.187 32.528 1.00138.44 C
ANISOU 2374 C GLY B1049 23664 12153 16786 -710 4032 -2245 C
ATOM 2375 O GLY B1049 6.552 24.657 32.142 1.00139.17 O
ANISOU 2375 O GLY B1049 23858 12196 16823 -1053 4099 -2320 O
ATOM 2376 N ARG B1050 4.372 24.213 31.787 1.00142.56 N
ANISOU 2376 N ARG B1050 24193 12562 17411 -154 4067 -1985 N
ATOM 2377 CA ARG B1050 4.294 24.758 30.443 1.00143.64 C
ANISOU 2377 CA ARG B1050 24456 12515 17605 124 4172 -1753 C
ATOM 2378 C ARG B1050 2.848 25.193 30.235 1.00149.44 C
ANISOU 2378 C ARG B1050 25281 13128 18373 712 4340 -1514 C
ATOM 2379 O ARG B1050 2.091 25.341 31.202 1.00150.50 O
ANISOU 2379 O ARG B1050 25461 13254 18469 818 4449 -1564 O
ATOM 2380 CB ARG B1050 4.774 23.729 29.403 1.00140.64 C
ANISOU 2380 CB ARG B1050 23785 12326 17327 152 3840 -1663 C
ATOM 2381 N ASN B1051 2.468 25.403 28.980 1.00156.25 N
ANISOU 2381 N ASN B1051 26154 13925 19287 1094 4361 -1251 N
ATOM 2382 CA ASN B1051 1.097 25.775 28.672 1.00159.24 C
ANISOU 2382 CA ASN B1051 26564 14266 19674 1680 4495 -994 C
ATOM 2383 C ASN B1051 0.129 24.772 29.291 1.00156.81 C
ANISOU 2383 C ASN B1051 25935 14227 19419 1928 4283 -984 C
ATOM 2384 O ASN B1051 0.288 23.558 29.125 1.00156.12 O
ANISOU 2384 O ASN B1051 25519 14392 19409 1886 3954 -1010 O
ATOM 2385 CB ASN B1051 0.920 25.833 27.154 1.00160.21 C
ANISOU 2385 CB ASN B1051 26633 14403 19838 2028 4447 -716 C
ATOM 2386 CG ASN B1051 -0.451 26.307 26.745 1.00162.64 C
ANISOU 2386 CG ASN B1051 26962 14718 20115 2634 4595 -432 C
ATOM 2387 OD1 ASN B1051 -1.051 27.147 27.413 1.00166.23 O
ANISOU 2387 OD1 ASN B1051 27658 15009 20493 2763 4883 -423 O
ATOM 2388 ND2 ASN B1051 -0.958 25.771 25.642 1.00161.43 N
ANISOU 2388 ND2 ASN B1051 26547 14780 20007 3010 4400 -193 N
ATOM 2389 N SER B1052 -0.868 25.281 30.020 1.00164.10 N
ANISOU 2389 N SER B1052 26966 15093 20291 2181 4490 -948 N
ATOM 2390 CA SER B1052 -1.890 24.435 30.633 1.00161.58 C
ANISOU 2390 CA SER B1052 26354 15035 20003 2446 4335 -930 C
ATOM 2391 C SER B1052 -2.966 24.168 29.592 1.00166.46 C
ANISOU 2391 C SER B1052 26738 15848 20660 3033 4244 -610 C
ATOM 2392 O SER B1052 -3.753 25.058 29.260 1.00166.17 O
ANISOU 2392 O SER B1052 26853 15718 20565 3411 4479 -406 O
ATOM 2393 CB SER B1052 -2.497 25.087 31.873 1.00156.44 C
ANISOU 2393 CB SER B1052 25900 14269 19272 2462 4595 -1032 C
ATOM 2394 OG SER B1052 -3.490 24.252 32.452 1.00153.17 O
ANISOU 2394 OG SER B1052 25188 14129 18879 2719 4452 -1016 O
ATOM 2395 N ASN B1053 -3.010 22.940 29.087 1.00167.08 N
ANISOU 2395 N ASN B1053 26443 16221 20820 3105 3908 -561 N
ATOM 2396 CA ASN B1053 -3.975 22.581 28.061 1.00167.05 C
ANISOU 2396 CA ASN B1053 26159 16479 20835 3616 3784 -268 C
ATOM 2397 C ASN B1053 -4.310 21.098 28.187 1.00166.38 C
ANISOU 2397 C ASN B1053 25643 16760 20813 3666 3452 -295 C
ATOM 2398 O ASN B1053 -3.637 20.343 28.897 1.00166.41 O
ANISOU 2398 O ASN B1053 25599 16776 20852 3295 3311 -526 O
ATOM 2399 CB ASN B1053 -3.463 22.953 26.649 1.00166.86 C
ANISOU 2399 CB ASN B1053 26208 16374 20818 3674 3771 -96 C
ATOM 2400 CG ASN B1053 -2.027 22.499 26.387 1.00165.83 C
ANISOU 2400 CG ASN B1053 26109 16145 20751 3188 3609 -269 C
ATOM 2401 OD1 ASN B1053 -1.214 22.412 27.305 1.00165.60 O
ANISOU 2401 OD1 ASN B1053 26199 15997 20724 2740 3619 -533 O
ATOM 2402 ND2 ASN B1053 -1.710 22.226 25.121 1.00165.73 N
ANISOU 2402 ND2 ASN B1053 25982 16213 20774 3272 3459 -117 N
ATOM 2403 N GLY B1054 -5.403 20.704 27.528 1.00149.17 N
ANISOU 2403 N GLY B1054 23146 14907 18623 4131 3343 -55 N
ATOM 2404 CA GLY B1054 -5.822 19.312 27.571 1.00134.69 C
ANISOU 2404 CA GLY B1054 20888 13456 16832 4210 3048 -57 C
ATOM 2405 C GLY B1054 -4.803 18.376 26.953 1.00128.35 C
ANISOU 2405 C GLY B1054 19878 12790 16098 3813 2703 -104 C
ATOM 2406 O GLY B1054 -4.585 17.270 27.453 1.00123.96 O
ANISOU 2406 O GLY B1054 19007 12526 15568 3478 2410 -217 O
ATOM 2407 N VAL B1055 -4.168 18.807 25.851 1.00133.04 N
ANISOU 2407 N VAL B1055 20656 13174 16717 3856 2748 -8 N
ATOM 2408 CA VAL B1055 -3.156 18.014 25.160 1.00124.72 C
ANISOU 2408 CA VAL B1055 19434 12228 15725 3508 2451 -41 C
ATOM 2409 C VAL B1055 -1.784 18.280 25.768 1.00125.21 C
ANISOU 2409 C VAL B1055 19789 11974 15810 2988 2516 -293 C
ATOM 2410 O VAL B1055 -1.458 19.413 26.150 1.00131.82 O
ANISOU 2410 O VAL B1055 21083 12387 16617 2952 2860 -392 O
ATOM 2411 CB VAL B1055 -3.164 18.325 23.652 1.00121.03 C
ANISOU 2411 CB VAL B1055 18999 11729 15259 3810 2463 190 C
ATOM 2412 CG1 VAL B1055 -2.279 17.333 22.891 1.00115.08 C
ANISOU 2412 CG1 VAL B1055 17996 11167 14564 3487 2124 173 C
ATOM 2413 CG2 VAL B1055 -4.589 18.323 23.118 1.00119.29 C
ANISOU 2413 CG2 VAL B1055 18529 11825 14970 4370 2467 444 C
ATOM 2414 N ILE B1056 -0.960 17.233 25.838 1.00118.68 N
ANISOU 2414 N ILE B1056 18704 11366 15023 2580 2199 -399 N
ATOM 2415 CA ILE B1056 0.388 17.329 26.375 1.00117.13 C
ANISOU 2415 CA ILE B1056 18690 10988 14825 2073 2206 -630 C
ATOM 2416 C ILE B1056 1.351 16.739 25.362 1.00115.01 C
ANISOU 2416 C ILE B1056 18280 10812 14607 1880 1974 -587 C
ATOM 2417 O ILE B1056 0.951 16.128 24.369 1.00111.93 O
ANISOU 2417 O ILE B1056 17632 10643 14254 2101 1785 -401 O
ATOM 2418 CB ILE B1056 0.545 16.604 27.722 1.00116.40 C
ANISOU 2418 CB ILE B1056 18419 11108 14702 1744 2058 -820 C
ATOM 2419 CG1 ILE B1056 0.008 15.175 27.603 1.00112.30 C
ANISOU 2419 CG1 ILE B1056 17408 11044 14215 1801 1704 -716 C
ATOM 2420 CG2 ILE B1056 -0.151 17.392 28.836 1.00119.34 C
ANISOU 2420 CG2 ILE B1056 19026 11308 15008 1848 2346 -920 C
ATOM 2421 CD1 ILE B1056 0.905 14.122 28.199 1.00108.17 C
ANISOU 2421 CD1 ILE B1056 16672 10739 13688 1378 1440 -851 C
ATOM 2422 N THR B1057 2.638 16.918 25.648 1.00114.17 N
ANISOU 2422 N THR B1057 18334 10560 14486 1446 1994 -773 N
ATOM 2423 CA THR B1057 3.696 16.387 24.803 1.00112.98 C
ANISOU 2423 CA THR B1057 18059 10496 14372 1220 1793 -759 C
ATOM 2424 C THR B1057 3.992 14.926 25.155 1.00109.76 C
ANISOU 2424 C THR B1057 17226 10496 13981 1008 1424 -792 C
ATOM 2425 O THR B1057 4.048 14.559 26.334 1.00108.66 O
ANISOU 2425 O THR B1057 17003 10486 13797 806 1370 -932 O
ATOM 2426 CB THR B1057 4.941 17.259 24.966 1.00111.44 C
ANISOU 2426 CB THR B1057 18211 9998 14133 843 1997 -948 C
ATOM 2427 OG1 THR B1057 5.731 16.777 26.051 1.00112.29 O
ANISOU 2427 OG1 THR B1057 18201 10282 14183 409 1873 -1165 O
ATOM 2428 CG2 THR B1057 4.512 18.672 25.323 1.00114.55 C
ANISOU 2428 CG2 THR B1057 19076 9968 14479 974 2422 -1000 C
ATOM 2429 N LYS B1058 4.200 14.092 24.123 1.00104.30 N
ANISOU 2429 N LYS B1058 16288 9997 13344 1058 1188 -660 N
ATOM 2430 CA LYS B1058 4.579 12.698 24.373 1.00101.53 C
ANISOU 2430 CA LYS B1058 15584 9987 13006 862 872 -683 C
ATOM 2431 C LYS B1058 5.792 12.629 25.291 1.00102.09 C
ANISOU 2431 C LYS B1058 15694 10076 13018 437 848 -885 C
ATOM 2432 O LYS B1058 5.906 11.720 26.124 1.00 99.43 O
ANISOU 2432 O LYS B1058 15140 9987 12651 289 676 -942 O
ATOM 2433 CB LYS B1058 4.861 11.949 23.061 1.00 95.02 C
ANISOU 2433 CB LYS B1058 14564 9301 12238 928 671 -541 C
ATOM 2434 CG LYS B1058 5.181 10.466 23.294 1.00 91.74 C
ANISOU 2434 CG LYS B1058 13819 9205 11834 763 380 -550 C
ATOM 2435 CD LYS B1058 5.720 9.681 22.079 1.00 89.86 C
ANISOU 2435 CD LYS B1058 13419 9083 11641 755 196 -449 C
ATOM 2436 CE LYS B1058 4.837 9.797 20.831 1.00 89.77 C
ANISOU 2436 CE LYS B1058 13370 9078 11659 1078 202 -274 C
ATOM 2437 NZ LYS B1058 5.412 9.185 19.580 1.00 87.18 N
ANISOU 2437 NZ LYS B1058 12930 8832 11363 1058 55 -190 N
ATOM 2438 N ASP B1059 6.709 13.586 25.146 1.00 99.83 N
ANISOU 2438 N ASP B1059 15683 9548 12699 232 1029 -992 N
ATOM 2439 CA ASP B1059 7.778 13.760 26.120 1.00 99.38 C
ANISOU 2439 CA ASP B1059 15689 9524 12547 -187 1058 -1212 C
ATOM 2440 C ASP B1059 7.213 14.111 27.490 1.00 98.95 C
ANISOU 2440 C ASP B1059 15734 9445 12419 -235 1188 -1346 C
ATOM 2441 O ASP B1059 7.688 13.606 28.515 1.00 99.25 O
ANISOU 2441 O ASP B1059 15631 9708 12373 -495 1075 -1474 O
ATOM 2442 CB ASP B1059 8.735 14.852 25.635 1.00101.26 C
ANISOU 2442 CB ASP B1059 16237 9485 12752 -405 1277 -1313 C
ATOM 2443 CG ASP B1059 9.108 14.690 24.168 1.00102.57 C
ANISOU 2443 CG ASP B1059 16360 9619 12995 -293 1201 -1159 C
ATOM 2444 OD1 ASP B1059 10.305 14.839 23.833 1.00106.25 O
ANISOU 2444 OD1 ASP B1059 16857 10087 13425 -586 1200 -1244 O
ATOM 2445 OD2 ASP B1059 8.208 14.388 23.352 1.00102.01 O1-
ANISOU 2445 OD2 ASP B1059 16200 9554 13005 78 1137 -957 O1-
ATOM 2446 N GLU B1060 6.196 14.978 27.530 1.00103.66 N
ANISOU 2446 N GLU B1060 16572 9782 13032 33 1433 -1309 N
ATOM 2447 CA GLU B1060 5.571 15.316 28.803 1.00103.53 C
ANISOU 2447 CA GLU B1060 16657 9734 12948 21 1574 -1430 C
ATOM 2448 C GLU B1060 4.989 14.071 29.462 1.00100.12 C
ANISOU 2448 C GLU B1060 15857 9666 12517 86 1312 -1376 C
ATOM 2449 O GLU B1060 5.112 13.886 30.679 1.00 98.85 O
ANISOU 2449 O GLU B1060 15660 9632 12267 -122 1297 -1521 O
ATOM 2450 CB GLU B1060 4.499 16.390 28.591 1.00105.88 C
ANISOU 2450 CB GLU B1060 17258 9702 13268 381 1886 -1356 C
ATOM 2451 N ALA B1061 4.394 13.180 28.664 1.00 98.59 N
ANISOU 2451 N ALA B1061 15395 9654 12413 347 1108 -1176 N
ATOM 2452 CA ALA B1061 3.845 11.937 29.204 1.00 96.02 C
ANISOU 2452 CA ALA B1061 14740 9655 12088 387 878 -1124 C
ATOM 2453 C ALA B1061 4.919 11.099 29.896 1.00 93.44 C
ANISOU 2453 C ALA B1061 14250 9558 11694 39 685 -1226 C
ATOM 2454 O ALA B1061 4.658 10.485 30.940 1.00 92.44 O
ANISOU 2454 O ALA B1061 13991 9625 11509 -32 606 -1271 O
ATOM 2455 CB ALA B1061 3.171 11.132 28.090 1.00 93.40 C
ANISOU 2455 CB ALA B1061 14168 9473 11847 661 706 -915 C
ATOM 2456 N GLU B1062 6.127 11.043 29.323 1.00 90.86 N
ANISOU 2456 N GLU B1062 13920 9237 11364 -162 610 -1250 N
ATOM 2457 CA GLU B1062 7.207 10.284 29.949 1.00 87.97 C
ANISOU 2457 CA GLU B1062 13384 9130 10912 -458 435 -1328 C
ATOM 2458 C GLU B1062 7.701 10.954 31.230 1.00 91.03 C
ANISOU 2458 C GLU B1062 13916 9520 11152 -752 567 -1546 C
ATOM 2459 O GLU B1062 8.190 10.274 32.141 1.00 90.26 O
ANISOU 2459 O GLU B1062 13649 9698 10947 -934 432 -1603 O
ATOM 2460 CB GLU B1062 8.353 10.086 28.958 1.00 84.11 C
ANISOU 2460 CB GLU B1062 12836 8673 10447 -576 334 -1292 C
ATOM 2461 CG GLU B1062 9.452 9.165 29.442 1.00 82.27 C
ANISOU 2461 CG GLU B1062 12378 8757 10122 -807 135 -1324 C
ATOM 2462 CD GLU B1062 10.640 9.159 28.492 1.00 79.30 C
ANISOU 2462 CD GLU B1062 11966 8409 9756 -935 76 -1309 C
ATOM 2463 OE1 GLU B1062 10.405 9.166 27.269 1.00 77.94 O
ANISOU 2463 OE1 GLU B1062 11820 8094 9701 -753 71 -1187 O
ATOM 2464 OE2 GLU B1062 11.800 9.152 28.967 1.00 78.11 O1-
ANISOU 2464 OE2 GLU B1062 11748 8451 9480 -1216 34 -1418 O1-
ATOM 2465 N LYS B1063 7.584 12.275 31.333 1.00 95.41 N
ANISOU 2465 N LYS B1063 14793 9777 11681 -802 844 -1670 N
ATOM 2466 CA LYS B1063 7.985 12.920 32.576 1.00 96.64 C
ANISOU 2466 CA LYS B1063 15103 9934 11680 -1108 990 -1902 C
ATOM 2467 C LYS B1063 6.951 12.691 33.684 1.00 97.66 C
ANISOU 2467 C LYS B1063 15197 10139 11771 -988 1015 -1919 C
ATOM 2468 O LYS B1063 7.321 12.514 34.851 1.00 98.93 O
ANISOU 2468 O LYS B1063 15302 10502 11785 -1232 982 -2058 O
ATOM 2469 CB LYS B1063 8.243 14.409 32.330 1.00 99.99 C
ANISOU 2469 CB LYS B1063 15932 9980 12080 -1236 1317 -2048 C
ATOM 2470 CG LYS B1063 9.469 14.729 31.426 1.00103.35 C
ANISOU 2470 CG LYS B1063 16414 10354 12501 -1465 1321 -2085 C
ATOM 2471 CD LYS B1063 9.671 16.238 31.189 1.00107.67 C
ANISOU 2471 CD LYS B1063 17415 10477 13018 -1604 1691 -2233 C
ATOM 2472 CE LYS B1063 10.899 16.524 30.317 1.00108.26 C
ANISOU 2472 CE LYS B1063 17534 10522 13078 -1864 1700 -2277 C
ATOM 2473 NZ LYS B1063 11.110 17.981 30.048 1.00113.19 N
ANISOU 2473 NZ LYS B1063 18638 10700 13668 -2021 2091 -2420 N
ATOM 2474 N LEU B1064 5.653 12.705 33.344 1.00 93.64 N
ANISOU 2474 N LEU B1064 14706 9498 11374 -616 1076 -1778 N
ATOM 2475 CA LEU B1064 4.624 12.250 34.283 1.00 93.37 C
ANISOU 2475 CA LEU B1064 14564 9598 11314 -478 1056 -1760 C
ATOM 2476 C LEU B1064 4.726 10.755 34.557 1.00 91.36 C
ANISOU 2476 C LEU B1064 13953 9709 11050 -501 753 -1659 C
ATOM 2477 O LEU B1064 4.522 10.314 35.695 1.00 89.51 O
ANISOU 2477 O LEU B1064 13631 9660 10718 -588 711 -1716 O
ATOM 2478 CB LEU B1064 3.232 12.568 33.755 1.00 93.93 C
ANISOU 2478 CB LEU B1064 14691 9504 11494 -66 1181 -1619 C
ATOM 2479 CG LEU B1064 2.902 14.027 33.567 1.00 94.69 C
ANISOU 2479 CG LEU B1064 15168 9216 11594 53 1524 -1681 C
ATOM 2480 CD1 LEU B1064 1.436 14.117 33.212 1.00 95.14 C
ANISOU 2480 CD1 LEU B1064 15188 9232 11727 504 1607 -1512 C
ATOM 2481 CD2 LEU B1064 3.193 14.727 34.879 1.00 95.41 C
ANISOU 2481 CD2 LEU B1064 15488 9220 11542 -224 1721 -1924 C
ATOM 2482 N PHE B1065 4.996 9.951 33.524 1.00 91.65 N
ANISOU 2482 N PHE B1065 13802 9839 11181 -411 559 -1502 N
ATOM 2483 CA PHE B1065 5.207 8.532 33.769 1.00 87.92 C
ANISOU 2483 CA PHE B1065 13043 9674 10691 -445 308 -1409 C
ATOM 2484 C PHE B1065 6.331 8.338 34.773 1.00 88.22 C
ANISOU 2484 C PHE B1065 13036 9920 10564 -759 240 -1536 C
ATOM 2485 O PHE B1065 6.224 7.515 35.692 1.00 87.41 O
ANISOU 2485 O PHE B1065 12786 10049 10375 -796 136 -1519 O
ATOM 2486 CB PHE B1065 5.518 7.799 32.465 1.00 82.86 C
ANISOU 2486 CB PHE B1065 12255 9069 10160 -340 143 -1250 C
ATOM 2487 CG PHE B1065 5.892 6.346 32.655 1.00 81.19 C
ANISOU 2487 CG PHE B1065 11797 9130 9923 -381 -82 -1154 C
ATOM 2488 CD1 PHE B1065 4.914 5.369 32.838 1.00 79.57 C
ANISOU 2488 CD1 PHE B1065 11446 9035 9751 -229 -158 -1048 C
ATOM 2489 CD2 PHE B1065 7.223 5.955 32.663 1.00 79.61 C
ANISOU 2489 CD2 PHE B1065 11517 9082 9651 -568 -199 -1169 C
ATOM 2490 CE1 PHE B1065 5.261 4.044 33.022 1.00 76.37 C
ANISOU 2490 CE1 PHE B1065 10869 8832 9315 -262 -323 -956 C
ATOM 2491 CE2 PHE B1065 7.574 4.618 32.836 1.00 74.69 C
ANISOU 2491 CE2 PHE B1065 10695 8688 8994 -560 -377 -1059 C
ATOM 2492 CZ PHE B1065 6.600 3.676 33.020 1.00 75.08 C
ANISOU 2492 CZ PHE B1065 10651 8793 9084 -408 -427 -953 C
ATOM 2493 N ASN B1066 7.414 9.106 34.626 1.00 87.83 N
ANISOU 2493 N ASN B1066 13110 9813 10449 -995 308 -1664 N
ATOM 2494 CA ASN B1066 8.528 8.968 35.553 1.00 87.70 C
ANISOU 2494 CA ASN B1066 13016 10064 10243 -1310 239 -1792 C
ATOM 2495 C ASN B1066 8.086 9.270 36.980 1.00 88.55 C
ANISOU 2495 C ASN B1066 13197 10240 10209 -1419 342 -1933 C
ATOM 2496 O ASN B1066 8.483 8.580 37.920 1.00 87.68 O
ANISOU 2496 O ASN B1066 12920 10445 9950 -1539 216 -1945 O
ATOM 2497 CB ASN B1066 9.685 9.864 35.109 1.00 88.40 C
ANISOU 2497 CB ASN B1066 13233 10081 10275 -1578 327 -1931 C
ATOM 2498 CG ASN B1066 10.506 9.239 33.977 1.00 89.76 C
ANISOU 2498 CG ASN B1066 13237 10348 10521 -1543 157 -1797 C
ATOM 2499 OD1 ASN B1066 10.630 8.010 33.882 1.00 87.91 O
ANISOU 2499 OD1 ASN B1066 12756 10345 10302 -1421 -54 -1639 O
ATOM 2500 ND2 ASN B1066 11.030 10.080 33.090 1.00 91.16 N
ANISOU 2500 ND2 ASN B1066 13572 10320 10743 -1637 272 -1853 N
ATOM 2501 N GLN B1067 7.233 10.278 37.154 1.00 90.14 N
ANISOU 2501 N GLN B1067 13651 10152 10445 -1351 581 -2026 N
ATOM 2502 CA GLN B1067 6.740 10.636 38.479 1.00 87.63 C
ANISOU 2502 CA GLN B1067 13431 9867 9996 -1443 708 -2170 C
ATOM 2503 C GLN B1067 6.034 9.466 39.147 1.00 88.21 C
ANISOU 2503 C GLN B1067 13276 10182 10057 -1286 550 -2040 C
ATOM 2504 O GLN B1067 6.231 9.202 40.340 1.00 90.15 O
ANISOU 2504 O GLN B1067 13461 10661 10130 -1450 518 -2125 O
ATOM 2505 CB GLN B1067 5.783 11.807 38.347 1.00 87.70 C
ANISOU 2505 CB GLN B1067 13750 9492 10082 -1294 1003 -2238 C
ATOM 2506 CG GLN B1067 6.450 13.130 38.282 1.00 90.55 C
ANISOU 2506 CG GLN B1067 14428 9603 10373 -1544 1247 -2447 C
ATOM 2507 CD GLN B1067 5.438 14.242 38.269 1.00 95.16 C
ANISOU 2507 CD GLN B1067 15348 9791 11016 -1350 1572 -2496 C
ATOM 2508 OE1 GLN B1067 4.360 14.113 37.674 1.00 96.31 O
ANISOU 2508 OE1 GLN B1067 15469 9811 11312 -958 1591 -2314 O
ATOM 2509 NE2 GLN B1067 5.761 15.337 38.941 1.00 98.98 N
ANISOU 2509 NE2 GLN B1067 16149 10094 11367 -1618 1841 -2744 N
ATOM 2510 N ASP B1068 5.168 8.786 38.397 1.00 88.58 N
ANISOU 2510 N ASP B1068 13207 10177 10272 -979 469 -1841 N
ATOM 2511 CA ASP B1068 4.443 7.643 38.929 1.00 88.30 C
ANISOU 2511 CA ASP B1068 12975 10343 10234 -845 343 -1716 C
ATOM 2512 C ASP B1068 5.373 6.479 39.206 1.00 89.07 C
ANISOU 2512 C ASP B1068 12856 10750 10236 -961 117 -1635 C
ATOM 2513 O ASP B1068 5.208 5.777 40.207 1.00 89.81 O
ANISOU 2513 O ASP B1068 12850 11057 10217 -990 56 -1613 O
ATOM 2514 CB ASP B1068 3.355 7.233 37.956 1.00 88.86 C
ANISOU 2514 CB ASP B1068 12970 10303 10489 -536 322 -1543 C
ATOM 2515 CG ASP B1068 2.462 8.372 37.632 1.00 90.51 C
ANISOU 2515 CG ASP B1068 13374 10241 10774 -364 547 -1588 C
ATOM 2516 OD1 ASP B1068 2.651 9.420 38.275 1.00 91.28 O
ANISOU 2516 OD1 ASP B1068 13693 10207 10784 -493 736 -1761 O
ATOM 2517 OD2 ASP B1068 1.582 8.233 36.764 1.00 91.50 O1-
ANISOU 2517 OD2 ASP B1068 13438 10299 11029 -103 548 -1456 O1-
ATOM 2518 N VAL B1069 6.348 6.249 38.322 1.00 90.39 N
ANISOU 2518 N VAL B1069 12952 10949 10441 -1007 2 -1577 N
ATOM 2519 CA VAL B1069 7.344 5.212 38.571 1.00 88.94 C
ANISOU 2519 CA VAL B1069 12572 11072 10150 -1091 -192 -1492 C
ATOM 2520 C VAL B1069 8.064 5.489 39.889 1.00 88.80 C
ANISOU 2520 C VAL B1069 12546 11310 9885 -1347 -182 -1641 C
ATOM 2521 O VAL B1069 8.377 4.564 40.645 1.00 87.88 O
ANISOU 2521 O VAL B1069 12274 11484 9631 -1354 -304 -1560 O
ATOM 2522 CB VAL B1069 8.317 5.107 37.378 1.00 83.61 C
ANISOU 2522 CB VAL B1069 11838 10383 9547 -1103 -286 -1428 C
ATOM 2523 CG1 VAL B1069 9.523 4.246 37.734 1.00 80.47 C
ANISOU 2523 CG1 VAL B1069 11247 10333 8997 -1199 -455 -1363 C
ATOM 2524 CG2 VAL B1069 7.597 4.563 36.158 1.00 81.25 C
ANISOU 2524 CG2 VAL B1069 11508 9902 9459 -848 -327 -1262 C
ATOM 2525 N ASP B1070 8.314 6.768 40.194 1.00 87.72 N
ANISOU 2525 N ASP B1070 12590 11070 9672 -1562 -19 -1861 N
ATOM 2526 CA ASP B1070 8.921 7.144 41.473 1.00 88.49 C
ANISOU 2526 CA ASP B1070 12692 11419 9510 -1847 14 -2041 C
ATOM 2527 C ASP B1070 8.063 6.717 42.663 1.00 89.36 C
ANISOU 2527 C ASP B1070 12784 11638 9530 -1779 32 -2029 C
ATOM 2528 O ASP B1070 8.562 6.102 43.613 1.00 89.46 O
ANISOU 2528 O ASP B1070 12649 12005 9338 -1875 -78 -2013 O
ATOM 2529 CB ASP B1070 9.156 8.657 41.532 1.00 88.00 C
ANISOU 2529 CB ASP B1070 12890 11149 9397 -2102 240 -2302 C
ATOM 2530 CG ASP B1070 10.208 9.127 40.572 1.00 90.81 C
ANISOU 2530 CG ASP B1070 13263 11462 9777 -2257 234 -2350 C
ATOM 2531 OD1 ASP B1070 11.014 9.983 40.984 1.00 94.30 O
ANISOU 2531 OD1 ASP B1070 13802 11982 10047 -2606 337 -2577 O
ATOM 2532 OD2 ASP B1070 10.248 8.652 39.420 1.00 92.37 O1-
ANISOU 2532 OD2 ASP B1070 13381 11561 10153 -2058 135 -2175 O1-
ATOM 2533 N ALA B1071 6.775 7.080 42.647 1.00 90.34 N
ANISOU 2533 N ALA B1071 13055 11480 9788 -1609 182 -2036 N
ATOM 2534 CA ALA B1071 5.882 6.762 43.757 1.00 92.41 C
ANISOU 2534 CA ALA B1071 13313 11827 9971 -1550 226 -2037 C
ATOM 2535 C ALA B1071 5.651 5.261 43.889 1.00 92.85 C
ANISOU 2535 C ALA B1071 13152 12092 10037 -1376 42 -1807 C
ATOM 2536 O ALA B1071 5.446 4.763 45.006 1.00 93.09 O
ANISOU 2536 O ALA B1071 13125 12333 9912 -1406 22 -1797 O
ATOM 2537 CB ALA B1071 4.550 7.492 43.581 1.00 94.79 C
ANISOU 2537 CB ALA B1071 13800 11796 10420 -1375 435 -2080 C
ATOM 2538 N ALA B1072 5.659 4.530 42.770 1.00 89.08 N
ANISOU 2538 N ALA B1072 12574 11544 9730 -1198 -73 -1624 N
ATOM 2539 CA ALA B1072 5.502 3.084 42.849 1.00 87.83 C
ANISOU 2539 CA ALA B1072 12252 11545 9575 -1052 -215 -1412 C
ATOM 2540 C ALA B1072 6.701 2.435 43.535 1.00 86.55 C
ANISOU 2540 C ALA B1072 11956 11736 9191 -1164 -353 -1362 C
ATOM 2541 O ALA B1072 6.549 1.435 44.249 1.00 86.28 O
ANISOU 2541 O ALA B1072 11842 11885 9057 -1091 -412 -1233 O
ATOM 2542 CB ALA B1072 5.287 2.501 41.456 1.00 86.16 C
ANISOU 2542 CB ALA B1072 11986 11169 9581 -866 -285 -1252 C
ATOM 2543 N VAL B1073 7.903 2.974 43.319 1.00 85.70 N
ANISOU 2543 N VAL B1073 11821 11749 8994 -1334 -398 -1452 N
ATOM 2544 CA VAL B1073 9.085 2.401 43.960 1.00 85.93 C
ANISOU 2544 CA VAL B1073 11683 12183 8782 -1426 -534 -1398 C
ATOM 2545 C VAL B1073 9.120 2.748 45.444 1.00 87.30 C
ANISOU 2545 C VAL B1073 11866 12611 8693 -1607 -487 -1536 C
ATOM 2546 O VAL B1073 9.604 1.958 46.268 1.00 86.71 O
ANISOU 2546 O VAL B1073 11651 12889 8405 -1588 -588 -1429 O
ATOM 2547 CB VAL B1073 10.371 2.857 43.251 1.00 85.84 C
ANISOU 2547 CB VAL B1073 11602 12277 8737 -1569 -598 -1458 C
ATOM 2548 CG1 VAL B1073 11.533 1.963 43.671 1.00 83.85 C
ANISOU 2548 CG1 VAL B1073 11122 12476 8263 -1557 -764 -1321 C
ATOM 2549 CG2 VAL B1073 10.179 2.844 41.756 1.00 85.70 C
ANISOU 2549 CG2 VAL B1073 11630 11940 8992 -1423 -600 -1377 C
ATOM 2550 N ARG B1074 8.648 3.947 45.804 1.00 90.93 N
ANISOU 2550 N ARG B1074 12501 12903 9145 -1779 -320 -1772 N
ATOM 2551 CA ARG B1074 8.530 4.296 47.214 1.00 90.71 C
ANISOU 2551 CA ARG B1074 12509 13082 8874 -1954 -250 -1919 C
ATOM 2552 C ARG B1074 7.561 3.353 47.915 1.00 91.86 C
ANISOU 2552 C ARG B1074 12629 13260 9015 -1753 -258 -1762 C
ATOM 2553 O ARG B1074 7.808 2.919 49.049 1.00 91.42 O
ANISOU 2553 O ARG B1074 12490 13534 8711 -1812 -306 -1742 O
ATOM 2554 CB ARG B1074 8.095 5.756 47.355 1.00 92.19 C
ANISOU 2554 CB ARG B1074 12940 13003 9084 -2146 -27 -2198 C
ATOM 2555 N GLY B1075 6.465 2.997 47.236 1.00 89.05 N
ANISOU 2555 N GLY B1075 12331 12589 8914 -1522 -210 -1646 N
ATOM 2556 CA GLY B1075 5.538 2.022 47.791 1.00 90.68 C
ANISOU 2556 CA GLY B1075 12508 12820 9126 -1351 -209 -1493 C
ATOM 2557 C GLY B1075 6.133 0.633 47.924 1.00 87.79 C
ANISOU 2557 C GLY B1075 11990 12704 8663 -1230 -366 -1249 C
ATOM 2558 O GLY B1075 5.930 -0.043 48.936 1.00 89.12 O
ANISOU 2558 O GLY B1075 12128 13068 8666 -1197 -372 -1164 O
ATOM 2559 N ILE B1076 6.866 0.182 46.903 1.00 87.81 N
ANISOU 2559 N ILE B1076 11911 12693 8761 -1145 -478 -1124 N
ATOM 2560 CA ILE B1076 7.490 -1.137 46.958 1.00 86.73 C
ANISOU 2560 CA ILE B1076 11654 12767 8531 -993 -601 -878 C
ATOM 2561 C ILE B1076 8.412 -1.234 48.169 1.00 87.50 C
ANISOU 2561 C ILE B1076 11644 13312 8288 -1091 -669 -878 C
ATOM 2562 O ILE B1076 8.353 -2.190 48.957 1.00 86.85 O
ANISOU 2562 O ILE B1076 11528 13418 8052 -970 -691 -707 O
ATOM 2563 CB ILE B1076 8.247 -1.419 45.646 1.00 84.18 C
ANISOU 2563 CB ILE B1076 11266 12369 8351 -905 -695 -778 C
ATOM 2564 CG1 ILE B1076 7.303 -1.310 44.455 1.00 84.12 C
ANISOU 2564 CG1 ILE B1076 11353 11956 8653 -814 -631 -781 C
ATOM 2565 CG2 ILE B1076 8.928 -2.773 45.676 1.00 83.13 C
ANISOU 2565 CG2 ILE B1076 11034 12435 8118 -715 -794 -515 C
ATOM 2566 CD1 ILE B1076 7.840 -1.966 43.189 1.00 80.46 C
ANISOU 2566 CD1 ILE B1076 10838 11401 8333 -679 -716 -630 C
ATOM 2567 N LEU B1077 9.268 -0.232 48.340 1.00 85.11 N
ANISOU 2567 N LEU B1077 11292 13201 7845 -1322 -693 -1074 N
ATOM 2568 CA LEU B1077 10.289 -0.306 49.374 1.00 86.14 C
ANISOU 2568 CA LEU B1077 11271 13836 7622 -1436 -780 -1081 C
ATOM 2569 C LEU B1077 9.699 -0.220 50.778 1.00 88.26 C
ANISOU 2569 C LEU B1077 11592 14258 7685 -1517 -707 -1152 C
ATOM 2570 O LEU B1077 10.372 -0.588 51.746 1.00 86.39 O
ANISOU 2570 O LEU B1077 11222 14469 7133 -1542 -785 -1090 O
ATOM 2571 CB LEU B1077 11.314 0.802 49.169 1.00 86.92 C
ANISOU 2571 CB LEU B1077 11303 14109 7612 -1724 -805 -1310 C
ATOM 2572 CG LEU B1077 12.388 0.631 48.088 1.00 85.69 C
ANISOU 2572 CG LEU B1077 11009 14033 7515 -1682 -918 -1226 C
ATOM 2573 CD1 LEU B1077 13.450 1.695 48.289 1.00 86.30 C
ANISOU 2573 CD1 LEU B1077 10995 14414 7380 -2034 -932 -1474 C
ATOM 2574 CD2 LEU B1077 13.019 -0.764 48.074 1.00 87.56 C
ANISOU 2574 CD2 LEU B1077 11068 14551 7651 -1393 -1056 -905 C
ATOM 2575 N ARG B1078 8.484 0.315 50.926 1.00 87.85 N
ANISOU 2575 N ARG B1078 11720 13876 7783 -1558 -556 -1286 N
ATOM 2576 CA ARG B1078 7.865 0.348 52.247 1.00 88.51 C
ANISOU 2576 CA ARG B1078 11859 14092 7678 -1622 -475 -1346 C
ATOM 2577 C ARG B1078 7.227 -0.995 52.609 1.00 89.94 C
ANISOU 2577 C ARG B1078 12036 14270 7865 -1363 -483 -1074 C
ATOM 2578 O ARG B1078 6.969 -1.262 53.793 1.00 92.11 O
ANISOU 2578 O ARG B1078 12317 14759 7921 -1381 -451 -1053 O
ATOM 2579 CB ARG B1078 6.840 1.487 52.331 1.00 89.61 C
ANISOU 2579 CB ARG B1078 12193 13904 7950 -1758 -287 -1600 C
ATOM 2580 N ASN B1079 6.967 -1.846 51.617 1.00 87.60 N
ANISOU 2580 N ASN B1079 11748 13732 7804 -1141 -511 -871 N
ATOM 2581 CA ASN B1079 6.324 -3.133 51.858 1.00 87.51 C
ANISOU 2581 CA ASN B1079 11776 13660 7815 -924 -482 -625 C
ATOM 2582 C ASN B1079 7.360 -4.191 52.241 1.00 86.06 C
ANISOU 2582 C ASN B1079 11481 13821 7397 -768 -594 -371 C
ATOM 2583 O ASN B1079 8.376 -4.351 51.566 1.00 85.97 O
ANISOU 2583 O ASN B1079 11363 13920 7382 -705 -703 -292 O
ATOM 2584 CB ASN B1079 5.562 -3.569 50.611 1.00 86.90 C
ANISOU 2584 CB ASN B1079 11771 13173 8075 -787 -438 -542 C
ATOM 2585 CG ASN B1079 4.526 -4.591 50.913 1.00 84.56 C
ANISOU 2585 CG ASN B1079 11563 12741 7827 -661 -342 -386 C
ATOM 2586 OD1 ASN B1079 4.799 -5.576 51.596 1.00 86.19 O
ANISOU 2586 OD1 ASN B1079 11772 13124 7852 -552 -350 -189 O
ATOM 2587 ND2 ASN B1079 3.319 -4.369 50.423 1.00 84.33 N
ANISOU 2587 ND2 ASN B1079 11606 12412 8025 -674 -238 -469 N
ATOM 2588 N ALA B1080 7.093 -4.928 53.315 1.00 86.83 N
ANISOU 2588 N ALA B1080 11608 14091 7292 -682 -554 -230 N
ATOM 2589 CA ALA B1080 8.105 -5.796 53.928 1.00 88.66 C
ANISOU 2589 CA ALA B1080 11734 14726 7228 -519 -644 11 C
ATOM 2590 C ALA B1080 8.182 -7.169 53.270 1.00 84.44 C
ANISOU 2590 C ALA B1080 11262 14020 6802 -219 -630 326 C
ATOM 2591 O ALA B1080 9.162 -7.901 53.477 1.00 82.43 O
ANISOU 2591 O ALA B1080 10919 14062 6339 -21 -702 556 O
ATOM 2592 CB ALA B1080 7.840 -5.951 55.441 1.00 88.35 C
ANISOU 2592 CB ALA B1080 11711 14975 6883 -549 -596 34 C
ATOM 2593 N LYS B1081 7.147 -7.556 52.532 1.00 84.75 N
ANISOU 2593 N LYS B1081 11457 13606 7139 -178 -521 345 N
ATOM 2594 CA LYS B1081 7.272 -8.718 51.677 1.00 83.65 C
ANISOU 2594 CA LYS B1081 11397 13253 7135 53 -494 590 C
ATOM 2595 C LYS B1081 7.845 -8.315 50.323 1.00 82.16 C
ANISOU 2595 C LYS B1081 11130 12933 7156 42 -584 521 C
ATOM 2596 O LYS B1081 8.651 -9.052 49.753 1.00 83.13 O
ANISOU 2596 O LYS B1081 11228 13088 7268 238 -627 718 O
ATOM 2597 CB LYS B1081 5.916 -9.412 51.539 1.00 79.67 C
ANISOU 2597 CB LYS B1081 11091 12365 6816 68 -325 638 C
ATOM 2598 N LEU B1082 7.470 -7.138 49.806 1.00 82.15 N
ANISOU 2598 N LEU B1082 11097 12786 7330 -169 -601 252 N
ATOM 2599 CA LEU B1082 7.949 -6.735 48.482 1.00 86.60 C
ANISOU 2599 CA LEU B1082 11606 13201 8098 -182 -672 189 C
ATOM 2600 C LEU B1082 9.413 -6.330 48.496 1.00 86.40 C
ANISOU 2600 C LEU B1082 11399 13542 7887 -200 -813 183 C
ATOM 2601 O LEU B1082 10.123 -6.589 47.525 1.00 81.23 O
ANISOU 2601 O LEU B1082 10688 12853 7322 -99 -876 268 O
ATOM 2602 CB LEU B1082 7.125 -5.582 47.909 1.00 85.44 C
ANISOU 2602 CB LEU B1082 11497 12786 8180 -373 -629 -74 C
ATOM 2603 CG LEU B1082 5.715 -5.945 47.458 1.00 84.33 C
ANISOU 2603 CG LEU B1082 11485 12284 8272 -345 -508 -72 C
ATOM 2604 CD1 LEU B1082 5.017 -4.729 46.860 1.00 84.87 C
ANISOU 2604 CD1 LEU B1082 11566 12143 8538 -481 -470 -309 C
ATOM 2605 CD2 LEU B1082 5.704 -7.140 46.519 1.00 79.71 C
ANISOU 2605 CD2 LEU B1082 10959 11501 7826 -176 -493 132 C
ATOM 2606 N LYS B1083 9.884 -5.694 49.569 1.00 86.81 N
ANISOU 2606 N LYS B1083 11347 13969 7668 -343 -859 73 N
ATOM 2607 CA LYS B1083 11.217 -5.096 49.518 1.00 87.28 C
ANISOU 2607 CA LYS B1083 11208 14403 7551 -441 -988 1 C
ATOM 2608 C LYS B1083 12.330 -6.119 49.296 1.00 89.23 C
ANISOU 2608 C LYS B1083 11325 14922 7658 -174 -1078 284 C
ATOM 2609 O LYS B1083 13.121 -5.927 48.360 1.00 88.63 O
ANISOU 2609 O LYS B1083 11146 14870 7659 -168 -1152 276 O
ATOM 2610 CB LYS B1083 11.481 -4.255 50.774 1.00 83.92 C
ANISOU 2610 CB LYS B1083 10695 14365 6825 -680 -1008 -188 C
ATOM 2611 CG LYS B1083 12.971 -3.959 50.927 1.00 87.65 C
ANISOU 2611 CG LYS B1083 10920 15363 7022 -759 -1148 -205 C
ATOM 2612 CD LYS B1083 13.334 -3.048 52.086 1.00 89.21 C
ANISOU 2612 CD LYS B1083 11014 15984 6897 -1059 -1170 -434 C
ATOM 2613 CE LYS B1083 14.785 -2.560 51.959 1.00 95.05 C
ANISOU 2613 CE LYS B1083 11493 17215 7406 -1216 -1301 -515 C
ATOM 2614 NZ LYS B1083 14.939 -1.090 52.185 1.00 97.69 N
ANISOU 2614 NZ LYS B1083 11832 17620 7664 -1664 -1261 -904 N
ATOM 2615 N PRO B1084 12.460 -7.202 50.083 1.00 90.76 N
ANISOU 2615 N PRO B1084 11524 15320 7642 69 -1062 549 N
ATOM 2616 CA PRO B1084 13.625 -8.102 49.904 1.00 89.44 C
ANISOU 2616 CA PRO B1084 11222 15455 7306 362 -1136 832 C
ATOM 2617 C PRO B1084 13.691 -8.795 48.543 1.00 90.24 C
ANISOU 2617 C PRO B1084 11415 15190 7683 564 -1102 977 C
ATOM 2618 O PRO B1084 14.785 -9.212 48.126 1.00 89.44 O
ANISOU 2618 O PRO B1084 11172 15327 7484 757 -1173 1141 O
ATOM 2619 CB PRO B1084 13.461 -9.120 51.041 1.00 85.80 C
ANISOU 2619 CB PRO B1084 10827 15178 6596 600 -1073 1092 C
ATOM 2620 CG PRO B1084 12.017 -9.085 51.363 1.00 87.40 C
ANISOU 2620 CG PRO B1084 11262 14979 6966 478 -937 990 C
ATOM 2621 CD PRO B1084 11.571 -7.664 51.160 1.00 85.33 C
ANISOU 2621 CD PRO B1084 10972 14600 6851 110 -961 619 C
ATOM 2622 N VAL B1085 12.552 -8.991 47.867 1.00 86.00 N
ANISOU 2622 N VAL B1085 11103 14111 7463 536 -988 931 N
ATOM 2623 CA VAL B1085 12.584 -9.576 46.528 1.00 86.86 C
ANISOU 2623 CA VAL B1085 11301 13874 7826 682 -952 1032 C
ATOM 2624 C VAL B1085 13.099 -8.563 45.511 1.00 85.61 C
ANISOU 2624 C VAL B1085 11013 13700 7817 504 -1052 827 C
ATOM 2625 O VAL B1085 13.768 -8.930 44.540 1.00 84.74 O
ANISOU 2625 O VAL B1085 10863 13544 7792 643 -1082 929 O
ATOM 2626 CB VAL B1085 11.203 -10.132 46.134 1.00 84.85 C
ANISOU 2626 CB VAL B1085 11307 13103 7829 680 -799 1038 C
ATOM 2627 CG1 VAL B1085 11.280 -10.807 44.750 1.00 83.74 C
ANISOU 2627 CG1 VAL B1085 11265 12632 7921 818 -755 1139 C
ATOM 2628 CG2 VAL B1085 10.725 -11.120 47.171 1.00 82.31 C
ANISOU 2628 CG2 VAL B1085 11133 12796 7346 831 -679 1236 C
ATOM 2629 N TYR B1086 12.805 -7.279 45.725 1.00 86.38 N
ANISOU 2629 N TYR B1086 11060 13822 7939 199 -1085 540 N
ATOM 2630 CA TYR B1086 13.179 -6.234 44.775 1.00 86.23 C
ANISOU 2630 CA TYR B1086 10966 13730 8068 7 -1143 332 C
ATOM 2631 C TYR B1086 14.695 -6.020 44.730 1.00 90.57 C
ANISOU 2631 C TYR B1086 11271 14736 8405 6 -1268 359 C
ATOM 2632 O TYR B1086 15.284 -5.923 43.645 1.00 90.20 O
ANISOU 2632 O TYR B1086 11167 14622 8483 28 -1309 361 O
ATOM 2633 CB TYR B1086 12.449 -4.933 45.127 1.00 85.91 C
ANISOU 2633 CB TYR B1086 10980 13580 8083 -301 -1103 30 C
ATOM 2634 CG TYR B1086 12.832 -3.708 44.310 1.00 86.20 C
ANISOU 2634 CG TYR B1086 10976 13542 8236 -526 -1130 -201 C
ATOM 2635 CD1 TYR B1086 12.112 -3.353 43.157 1.00 82.56 C
ANISOU 2635 CD1 TYR B1086 10645 12636 8087 -543 -1072 -280 C
ATOM 2636 CD2 TYR B1086 13.888 -2.887 44.706 1.00 87.19 C
ANISOU 2636 CD2 TYR B1086 10937 14052 8139 -737 -1202 -347 C
ATOM 2637 CE1 TYR B1086 12.444 -2.227 42.424 1.00 80.06 C
ANISOU 2637 CE1 TYR B1086 10324 12229 7867 -733 -1073 -475 C
ATOM 2638 CE2 TYR B1086 14.231 -1.760 43.976 1.00 84.17 C
ANISOU 2638 CE2 TYR B1086 10554 13573 7856 -968 -1195 -564 C
ATOM 2639 CZ TYR B1086 13.508 -1.431 42.840 1.00 84.12 C
ANISOU 2639 CZ TYR B1086 10705 13089 8168 -952 -1125 -619 C
ATOM 2640 OH TYR B1086 13.870 -0.306 42.118 1.00 86.36 O
ANISOU 2640 OH TYR B1086 11013 13263 8538 -1165 -1099 -818 O
ATOM 2641 N ASP B1087 15.352 -5.925 45.896 1.00103.84 N
ANISOU 2641 N ASP B1087 12788 16921 9746 -32 -1331 373 N
ATOM 2642 CA ASP B1087 16.801 -5.697 45.895 1.00103.20 C
ANISOU 2642 CA ASP B1087 12429 17357 9426 -56 -1455 386 C
ATOM 2643 C ASP B1087 17.565 -6.873 45.291 1.00102.26 C
ANISOU 2643 C ASP B1087 12236 17330 9289 321 -1483 702 C
ATOM 2644 O ASP B1087 18.591 -6.676 44.630 1.00102.32 O
ANISOU 2644 O ASP B1087 12059 17558 9261 320 -1560 701 O
ATOM 2645 CB ASP B1087 17.337 -5.409 47.301 1.00104.80 C
ANISOU 2645 CB ASP B1087 12444 18146 9228 -172 -1521 343 C
ATOM 2646 CG ASP B1087 16.409 -4.558 48.141 1.00106.16 C
ANISOU 2646 CG ASP B1087 12747 18201 9389 -466 -1454 90 C
ATOM 2647 OD1 ASP B1087 16.707 -3.370 48.347 1.00109.15 O
ANISOU 2647 OD1 ASP B1087 13052 18744 9677 -823 -1472 -200 O
ATOM 2648 OD2 ASP B1087 15.352 -5.068 48.577 1.00112.54 O1-
ANISOU 2648 OD2 ASP B1087 13749 18732 10281 -350 -1362 172 O1-
ATOM 2649 N SER B1088 17.099 -8.101 45.527 1.00 93.73 N
ANISOU 2649 N SER B1088 11309 16085 8219 643 -1401 973 N
ATOM 2650 CA SER B1088 17.740 -9.272 44.938 1.00 91.22 C
ANISOU 2650 CA SER B1088 10986 15779 7896 1029 -1380 1282 C
ATOM 2651 C SER B1088 17.510 -9.372 43.436 1.00 89.16 C
ANISOU 2651 C SER B1088 10858 15036 7984 1047 -1333 1252 C
ATOM 2652 O SER B1088 18.248 -10.098 42.764 1.00 87.34 O
ANISOU 2652 O SER B1088 10586 14845 7754 1314 -1328 1452 O
ATOM 2653 CB SER B1088 17.244 -10.559 45.602 1.00 88.39 C
ANISOU 2653 CB SER B1088 10818 15311 7453 1354 -1260 1573 C
ATOM 2654 OG SER B1088 16.107 -11.069 44.931 1.00 87.93 O
ANISOU 2654 OG SER B1088 11069 14627 7713 1376 -1118 1581 O
ATOM 2655 N LEU B1089 16.498 -8.695 42.903 1.00 88.03 N
ANISOU 2655 N LEU B1089 10873 14454 8122 795 -1290 1021 N
ATOM 2656 CA LEU B1089 16.279 -8.729 41.473 1.00 84.48 C
ANISOU 2656 CA LEU B1089 10529 13592 7978 799 -1256 984 C
ATOM 2657 C LEU B1089 17.164 -7.715 40.768 1.00 85.34 C
ANISOU 2657 C LEU B1089 10445 13877 8104 610 -1359 812 C
ATOM 2658 O LEU B1089 17.669 -6.756 41.365 1.00 85.39 O
ANISOU 2658 O LEU B1089 10276 14234 7934 376 -1439 641 O
ATOM 2659 CB LEU B1089 14.829 -8.453 41.110 1.00 82.10 C
ANISOU 2659 CB LEU B1089 10456 12785 7955 639 -1165 831 C
ATOM 2660 CG LEU B1089 13.775 -9.445 41.529 1.00 80.95 C
ANISOU 2660 CG LEU B1089 10533 12370 7856 771 -1035 966 C
ATOM 2661 CD1 LEU B1089 12.415 -8.795 41.366 1.00 79.72 C
ANISOU 2661 CD1 LEU B1089 10507 11870 7915 541 -978 751 C
ATOM 2662 CD2 LEU B1089 13.894 -10.702 40.712 1.00 79.40 C
ANISOU 2662 CD2 LEU B1089 10476 11937 7758 1039 -946 1192 C
ATOM 2663 N ASP B1090 17.331 -7.949 39.464 1.00 79.59 N
ANISOU 2663 N ASP B1090 9766 12889 7586 693 -1342 849 N
ATOM 2664 CA ASP B1090 18.059 -7.098 38.541 1.00 76.31 C
ANISOU 2664 CA ASP B1090 9216 12536 7242 530 -1411 702 C
ATOM 2665 C ASP B1090 17.081 -6.130 37.883 1.00 75.22 C
ANISOU 2665 C ASP B1090 9234 11975 7372 269 -1371 458 C
ATOM 2666 O ASP B1090 15.881 -6.129 38.165 1.00 75.17 O
ANISOU 2666 O ASP B1090 9403 11676 7480 226 -1299 405 O
ATOM 2667 CB ASP B1090 18.746 -7.953 37.488 1.00 74.82 C
ANISOU 2667 CB ASP B1090 9011 12294 7124 796 -1400 897 C
ATOM 2668 CG ASP B1090 17.756 -8.830 36.737 1.00 76.43 C
ANISOU 2668 CG ASP B1090 9492 11968 7582 951 -1282 995 C
ATOM 2669 OD1 ASP B1090 17.667 -10.051 37.040 1.00 75.65 O
ANISOU 2669 OD1 ASP B1090 9504 11820 7420 1232 -1199 1230 O
ATOM 2670 OD2 ASP B1090 17.043 -8.276 35.858 1.00 77.16 O1-
ANISOU 2670 OD2 ASP B1090 9697 11698 7920 780 -1260 832 O1-
ATOM 2671 N ALA B1091 17.580 -5.343 36.935 1.00 77.26 N
ANISOU 2671 N ALA B1091 9431 12196 7730 120 -1404 324 N
ATOM 2672 CA ALA B1091 16.781 -4.256 36.377 1.00 77.34 C
ANISOU 2672 CA ALA B1091 9575 11861 7951 -120 -1358 95 C
ATOM 2673 C ALA B1091 15.601 -4.766 35.547 1.00 76.74 C
ANISOU 2673 C ALA B1091 9710 11301 8146 2 -1282 148 C
ATOM 2674 O ALA B1091 14.475 -4.266 35.690 1.00 76.58 O
ANISOU 2674 O ALA B1091 9825 11032 8242 -104 -1222 27 O
ATOM 2675 CB ALA B1091 17.676 -3.342 35.545 1.00 77.79 C
ANISOU 2675 CB ALA B1091 9529 11998 8028 -298 -1394 -39 C
ATOM 2676 N VAL B1092 15.835 -5.730 34.644 1.00 75.03 N
ANISOU 2676 N VAL B1092 9522 10964 8023 216 -1273 319 N
ATOM 2677 CA VAL B1092 14.732 -6.181 33.785 1.00 74.93 C
ANISOU 2677 CA VAL B1092 9697 10526 8248 282 -1199 341 C
ATOM 2678 C VAL B1092 13.657 -6.839 34.635 1.00 72.30 C
ANISOU 2678 C VAL B1092 9489 10082 7901 338 -1128 398 C
ATOM 2679 O VAL B1092 12.460 -6.760 34.324 1.00 70.35 O
ANISOU 2679 O VAL B1092 9368 9548 7812 281 -1067 327 O
ATOM 2680 CB VAL B1092 15.221 -7.122 32.657 1.00 70.44 C
ANISOU 2680 CB VAL B1092 9154 9846 7764 478 -1184 497 C
ATOM 2681 CG1 VAL B1092 14.039 -7.658 31.848 1.00 68.72 C
ANISOU 2681 CG1 VAL B1092 9126 9230 7755 510 -1101 504 C
ATOM 2682 CG2 VAL B1092 16.144 -6.389 31.746 1.00 71.20 C
ANISOU 2682 CG2 VAL B1092 9135 10023 7893 398 -1244 422 C
ATOM 2683 N ARG B1093 14.064 -7.487 35.716 1.00 70.52 N
ANISOU 2683 N ARG B1093 9218 10106 7469 453 -1130 530 N
ATOM 2684 CA ARG B1093 13.099 -8.120 36.593 1.00 75.26 C
ANISOU 2684 CA ARG B1093 9945 10614 8034 499 -1049 591 C
ATOM 2685 C ARG B1093 12.371 -7.107 37.485 1.00 73.87 C
ANISOU 2685 C ARG B1093 9760 10482 7825 286 -1051 402 C
ATOM 2686 O ARG B1093 11.171 -7.275 37.741 1.00 71.18 O
ANISOU 2686 O ARG B1093 9544 9934 7568 251 -972 369 O
ATOM 2687 CB ARG B1093 13.819 -9.221 37.363 1.00 75.49 C
ANISOU 2687 CB ARG B1093 9953 10881 7847 737 -1031 830 C
ATOM 2688 CG ARG B1093 14.282 -10.283 36.367 1.00 72.93 C
ANISOU 2688 CG ARG B1093 9708 10405 7598 965 -976 1013 C
ATOM 2689 CD ARG B1093 14.771 -11.561 36.996 1.00 72.31 C
ANISOU 2689 CD ARG B1093 9691 10446 7336 1262 -899 1287 C
ATOM 2690 NE ARG B1093 14.675 -12.689 36.072 1.00 73.09 N
ANISOU 2690 NE ARG B1093 9988 10226 7556 1446 -770 1433 N
ATOM 2691 CZ ARG B1093 15.709 -13.363 35.580 1.00 73.28 C
ANISOU 2691 CZ ARG B1093 9992 10334 7516 1702 -745 1615 C
ATOM 2692 NH1 ARG B1093 16.958 -13.027 35.865 1.00 71.63 N
ANISOU 2692 NH1 ARG B1093 9536 10558 7123 1811 -857 1682 N
ATOM 2693 NH2 ARG B1093 15.482 -14.416 34.800 1.00 73.86 N
ANISOU 2693 NH2 ARG B1093 10299 10065 7699 1847 -591 1730 N
ATOM 2694 N ARG B1094 13.038 -6.013 37.877 1.00 73.48 N
ANISOU 2694 N ARG B1094 9575 10681 7662 122 -1125 257 N
ATOM 2695 CA ARG B1094 12.353 -4.942 38.599 1.00 72.17 C
ANISOU 2695 CA ARG B1094 9436 10506 7479 -93 -1099 51 C
ATOM 2696 C ARG B1094 11.235 -4.335 37.769 1.00 72.74 C
ANISOU 2696 C ARG B1094 9633 10203 7802 -172 -1033 -81 C
ATOM 2697 O ARG B1094 10.156 -4.029 38.292 1.00 76.09 O
ANISOU 2697 O ARG B1094 10140 10507 8262 -234 -963 -167 O
ATOM 2698 CB ARG B1094 13.325 -3.840 38.996 1.00 73.36 C
ANISOU 2698 CB ARG B1094 9449 10957 7468 -294 -1162 -107 C
ATOM 2699 CG ARG B1094 14.233 -4.141 40.170 1.00 77.66 C
ANISOU 2699 CG ARG B1094 9836 11970 7701 -278 -1227 -34 C
ATOM 2700 CD ARG B1094 15.539 -3.475 39.881 1.00 80.37 C
ANISOU 2700 CD ARG B1094 9998 12615 7924 -415 -1308 -119 C
ATOM 2701 NE ARG B1094 16.037 -2.609 40.939 1.00 81.47 N
ANISOU 2701 NE ARG B1094 10024 13122 7810 -667 -1336 -293 N
ATOM 2702 CZ ARG B1094 16.834 -3.024 41.916 1.00 84.84 C
ANISOU 2702 CZ ARG B1094 10265 14042 7930 -624 -1410 -200 C
ATOM 2703 NH1 ARG B1094 17.165 -4.303 42.041 1.00 85.59 N
ANISOU 2703 NH1 ARG B1094 10292 14291 7938 -300 -1448 86 N
ATOM 2704 NH2 ARG B1094 17.348 -2.129 42.760 1.00 84.15 N
ANISOU 2704 NH2 ARG B1094 10058 14313 7600 -910 -1435 -398 N
ATOM 2705 N SER B1095 11.480 -4.114 36.481 1.00 73.26 N
ANISOU 2705 N SER B1095 9702 10107 8028 -161 -1052 -96 N
ATOM 2706 CA SER B1095 10.449 -3.507 35.652 1.00 71.75 C
ANISOU 2706 CA SER B1095 9610 9602 8049 -208 -994 -203 C
ATOM 2707 C SER B1095 9.197 -4.359 35.669 1.00 68.46 C
ANISOU 2707 C SER B1095 9283 9004 7723 -114 -928 -127 C
ATOM 2708 O SER B1095 8.076 -3.842 35.773 1.00 65.77 O
ANISOU 2708 O SER B1095 8998 8528 7462 -166 -863 -226 O
ATOM 2709 CB SER B1095 10.981 -3.337 34.233 1.00 70.65 C
ANISOU 2709 CB SER B1095 9456 9344 8043 -183 -1029 -194 C
ATOM 2710 OG SER B1095 12.279 -2.783 34.331 1.00 71.54 O
ANISOU 2710 OG SER B1095 9465 9685 8034 -276 -1088 -241 O
ATOM 2711 N ALA B1096 9.381 -5.679 35.572 1.00 69.57 N
ANISOU 2711 N ALA B1096 9444 9149 7841 26 -925 50 N
ATOM 2712 CA ALA B1096 8.268 -6.612 35.589 1.00 69.92 C
ANISOU 2712 CA ALA B1096 9589 9028 7950 78 -840 119 C
ATOM 2713 C ALA B1096 7.550 -6.631 36.950 1.00 70.36 C
ANISOU 2713 C ALA B1096 9673 9168 7893 30 -783 95 C
ATOM 2714 O ALA B1096 6.345 -6.917 37.002 1.00 67.43 O
ANISOU 2714 O ALA B1096 9365 8662 7592 2 -701 72 O
ATOM 2715 CB ALA B1096 8.788 -7.994 35.183 1.00 65.86 C
ANISOU 2715 CB ALA B1096 9133 8473 7417 231 -817 311 C
ATOM 2716 N LEU B1097 8.263 -6.302 38.037 1.00 70.41 N
ANISOU 2716 N LEU B1097 9618 9423 7711 6 -822 88 N
ATOM 2717 CA LEU B1097 7.646 -6.115 39.345 1.00 71.21 C
ANISOU 2717 CA LEU B1097 9738 9627 7691 -60 -773 38 C
ATOM 2718 C LEU B1097 6.819 -4.831 39.409 1.00 72.32 C
ANISOU 2718 C LEU B1097 9885 9681 7914 -201 -736 -173 C
ATOM 2719 O LEU B1097 5.722 -4.828 39.999 1.00 73.03 O
ANISOU 2719 O LEU B1097 10023 9716 8010 -232 -654 -217 O
ATOM 2720 CB LEU B1097 8.714 -6.106 40.445 1.00 70.88 C
ANISOU 2720 CB LEU B1097 9614 9920 7397 -52 -832 86 C
ATOM 2721 CG LEU B1097 8.030 -6.371 41.800 1.00 73.67 C
ANISOU 2721 CG LEU B1097 10016 10368 7607 -72 -764 100 C
ATOM 2722 CD1 LEU B1097 7.241 -7.663 41.725 1.00 72.07 C
ANISOU 2722 CD1 LEU B1097 9940 9980 7464 45 -665 258 C
ATOM 2723 CD2 LEU B1097 9.009 -6.434 42.966 1.00 74.26 C
ANISOU 2723 CD2 LEU B1097 9998 10821 7395 -56 -822 161 C
ATOM 2724 N ILE B1098 7.356 -3.739 38.837 1.00 69.24 N
ANISOU 2724 N ILE B1098 9457 9278 7573 -280 -778 -298 N
ATOM 2725 CA ILE B1098 6.650 -2.463 38.741 1.00 69.72 C
ANISOU 2725 CA ILE B1098 9562 9210 7720 -378 -714 -483 C
ATOM 2726 C ILE B1098 5.459 -2.575 37.813 1.00 71.36 C
ANISOU 2726 C ILE B1098 9808 9180 8126 -303 -659 -475 C
ATOM 2727 O ILE B1098 4.386 -2.014 38.068 1.00 72.74 O
ANISOU 2727 O ILE B1098 10017 9277 8344 -315 -572 -565 O
ATOM 2728 CB ILE B1098 7.609 -1.373 38.241 1.00 71.46 C
ANISOU 2728 CB ILE B1098 9766 9445 7940 -481 -748 -599 C
ATOM 2729 CG1 ILE B1098 8.939 -1.425 38.979 1.00 72.65 C
ANISOU 2729 CG1 ILE B1098 9827 9904 7874 -566 -826 -593 C
ATOM 2730 CG2 ILE B1098 6.947 0.000 38.262 1.00 71.21 C
ANISOU 2730 CG2 ILE B1098 9830 9257 7970 -570 -642 -786 C
ATOM 2731 CD1 ILE B1098 9.661 -0.101 38.914 1.00 73.91 C
ANISOU 2731 CD1 ILE B1098 9993 10107 7982 -761 -812 -781 C
ATOM 2732 N ASN B1099 5.652 -3.249 36.687 1.00 71.92 N
ANISOU 2732 N ASN B1099 9864 9158 8306 -222 -704 -372 N
ATOM 2733 CA ASN B1099 4.546 -3.525 35.784 1.00 71.39 C
ANISOU 2733 CA ASN B1099 9807 8925 8395 -167 -662 -357 C
ATOM 2734 C ASN B1099 3.376 -4.112 36.561 1.00 69.68 C
ANISOU 2734 C ASN B1099 9603 8728 8143 -174 -581 -343 C
ATOM 2735 O ASN B1099 2.229 -3.672 36.421 1.00 71.08 O
ANISOU 2735 O ASN B1099 9764 8854 8390 -172 -516 -414 O
ATOM 2736 CB ASN B1099 5.019 -4.506 34.701 1.00 68.70 C
ANISOU 2736 CB ASN B1099 9461 8517 8124 -101 -714 -235 C
ATOM 2737 CG ASN B1099 4.106 -4.545 33.505 1.00 68.05 C
ANISOU 2737 CG ASN B1099 9368 8296 8192 -75 -692 -249 C
ATOM 2738 OD1 ASN B1099 2.921 -4.865 33.624 1.00 68.12 O
ANISOU 2738 OD1 ASN B1099 9368 8292 8224 -89 -627 -263 O
ATOM 2739 ND2 ASN B1099 4.667 -4.267 32.319 1.00 71.00 N
ANISOU 2739 ND2 ASN B1099 9729 8595 8652 -42 -745 -243 N
ATOM 2740 N MET B1100 3.668 -5.098 37.411 1.00 69.42 N
ANISOU 2740 N MET B1100 9599 8789 7989 -173 -574 -243 N
ATOM 2741 CA MET B1100 2.629 -5.744 38.220 1.00 73.93 C
ANISOU 2741 CA MET B1100 10200 9380 8510 -199 -481 -221 C
ATOM 2742 C MET B1100 1.965 -4.789 39.208 1.00 72.37 C
ANISOU 2742 C MET B1100 9987 9256 8253 -254 -424 -350 C
ATOM 2743 O MET B1100 0.752 -4.878 39.437 1.00 73.48 O
ANISOU 2743 O MET B1100 10117 9382 8420 -274 -337 -386 O
ATOM 2744 CB MET B1100 3.203 -6.939 38.977 1.00 68.56 C
ANISOU 2744 CB MET B1100 9586 8776 7690 -164 -468 -69 C
ATOM 2745 CG MET B1100 3.144 -8.204 38.152 1.00 65.73 C
ANISOU 2745 CG MET B1100 9299 8279 7398 -121 -431 56 C
ATOM 2746 SD MET B1100 3.953 -9.596 38.936 1.00 67.62 S
ANISOU 2746 SD MET B1100 9660 8565 7467 -16 -382 271 S
ATOM 2747 CE MET B1100 2.468 -10.468 39.451 1.00 70.97 C
ANISOU 2747 CE MET B1100 10193 8889 7884 -118 -210 276 C
ATOM 2748 N VAL B1101 2.749 -3.917 39.852 1.00 72.47 N
ANISOU 2748 N VAL B1101 10001 9367 8168 -291 -458 -425 N
ATOM 2749 CA VAL B1101 2.179 -2.960 40.802 1.00 75.05 C
ANISOU 2749 CA VAL B1101 10345 9744 8427 -353 -381 -564 C
ATOM 2750 C VAL B1101 1.273 -1.959 40.094 1.00 77.61 C
ANISOU 2750 C VAL B1101 10667 9926 8898 -318 -314 -675 C
ATOM 2751 O VAL B1101 0.192 -1.618 40.600 1.00 77.01 O
ANISOU 2751 O VAL B1101 10591 9852 8819 -308 -213 -741 O
ATOM 2752 CB VAL B1101 3.292 -2.239 41.585 1.00 75.88 C
ANISOU 2752 CB VAL B1101 10462 9995 8374 -441 -421 -642 C
ATOM 2753 CG1 VAL B1101 2.716 -1.035 42.350 1.00 75.07 C
ANISOU 2753 CG1 VAL B1101 10413 9885 8224 -519 -315 -824 C
ATOM 2754 CG2 VAL B1101 3.990 -3.206 42.525 1.00 75.14 C
ANISOU 2754 CG2 VAL B1101 10350 10112 8090 -441 -471 -519 C
ATOM 2755 N PHE B1102 1.710 -1.449 38.927 1.00 75.45 N
ANISOU 2755 N PHE B1102 10390 9539 8740 -280 -361 -688 N
ATOM 2756 CA PHE B1102 0.852 -0.555 38.153 1.00 75.53 C
ANISOU 2756 CA PHE B1102 10400 9420 8878 -200 -292 -757 C
ATOM 2757 C PHE B1102 -0.513 -1.192 37.913 1.00 75.66 C
ANISOU 2757 C PHE B1102 10334 9457 8954 -134 -244 -708 C
ATOM 2758 O PHE B1102 -1.539 -0.502 37.872 1.00 75.48 O
ANISOU 2758 O PHE B1102 10288 9422 8970 -57 -151 -767 O
ATOM 2759 CB PHE B1102 1.524 -0.214 36.817 1.00 76.89 C
ANISOU 2759 CB PHE B1102 10577 9478 9161 -158 -358 -735 C
ATOM 2760 CG PHE B1102 2.325 1.045 36.856 1.00 77.36 C
ANISOU 2760 CG PHE B1102 10732 9466 9196 -212 -327 -847 C
ATOM 2761 CD1 PHE B1102 3.379 1.188 37.752 1.00 76.09 C
ANISOU 2761 CD1 PHE B1102 10604 9416 8892 -356 -355 -904 C
ATOM 2762 CD2 PHE B1102 2.018 2.100 36.001 1.00 78.65 C
ANISOU 2762 CD2 PHE B1102 10958 9465 9462 -128 -254 -897 C
ATOM 2763 CE1 PHE B1102 4.121 2.357 37.792 1.00 78.10 C
ANISOU 2763 CE1 PHE B1102 10955 9615 9105 -461 -307 -1036 C
ATOM 2764 CE2 PHE B1102 2.758 3.283 36.032 1.00 78.58 C
ANISOU 2764 CE2 PHE B1102 11081 9352 9425 -206 -189 -1012 C
ATOM 2765 CZ PHE B1102 3.812 3.413 36.927 1.00 80.57 C
ANISOU 2765 CZ PHE B1102 11368 9712 9534 -396 -212 -1095 C
ATOM 2766 N GLN B1103 -0.534 -2.515 37.733 1.00 74.39 N
ANISOU 2766 N GLN B1103 10134 9338 8791 -166 -292 -600 N
ATOM 2767 CA GLN B1103 -1.772 -3.224 37.454 1.00 76.99 C
ANISOU 2767 CA GLN B1103 10383 9710 9160 -163 -240 -569 C
ATOM 2768 C GLN B1103 -2.569 -3.549 38.733 1.00 80.00 C
ANISOU 2768 C GLN B1103 10762 10199 9436 -221 -144 -591 C
ATOM 2769 O GLN B1103 -3.788 -3.353 38.757 1.00 77.62 O
ANISOU 2769 O GLN B1103 10374 9966 9152 -199 -63 -636 O
ATOM 2770 CB GLN B1103 -1.450 -4.483 36.651 1.00 74.83 C
ANISOU 2770 CB GLN B1103 10109 9398 8924 -203 -297 -463 C
ATOM 2771 CG GLN B1103 -2.672 -5.217 36.128 1.00 74.21 C
ANISOU 2771 CG GLN B1103 9945 9369 8882 -250 -242 -456 C
ATOM 2772 CD GLN B1103 -2.296 -6.422 35.277 1.00 74.60 C
ANISOU 2772 CD GLN B1103 10037 9344 8962 -313 -272 -373 C
ATOM 2773 OE1 GLN B1103 -1.108 -6.806 35.160 1.00 71.56 O
ANISOU 2773 OE1 GLN B1103 9749 8870 8571 -290 -329 -299 O
ATOM 2774 NE2 GLN B1103 -3.306 -7.019 34.661 1.00 76.32 N
ANISOU 2774 NE2 GLN B1103 10179 9617 9204 -396 -223 -392 N
ATOM 2775 N MET B1104 -1.923 -4.049 39.807 1.00 79.80 N
ANISOU 2775 N MET B1104 10815 10217 9286 -286 -148 -552 N
ATOM 2776 CA MET B1104 -2.700 -4.492 40.971 1.00 81.14 C
ANISOU 2776 CA MET B1104 10992 10488 9350 -347 -50 -557 C
ATOM 2777 C MET B1104 -2.393 -3.767 42.296 1.00 81.42 C
ANISOU 2777 C MET B1104 11084 10602 9251 -368 -16 -630 C
ATOM 2778 O MET B1104 -3.029 -4.079 43.306 1.00 82.25 O
ANISOU 2778 O MET B1104 11197 10796 9257 -415 70 -637 O
ATOM 2779 CB MET B1104 -2.571 -6.027 41.192 1.00 80.72 C
ANISOU 2779 CB MET B1104 11000 10434 9236 -415 -34 -425 C
ATOM 2780 CG MET B1104 -1.193 -6.695 40.941 1.00 79.21 C
ANISOU 2780 CG MET B1104 10894 10188 9014 -382 -123 -302 C
ATOM 2781 SD MET B1104 -1.126 -8.535 40.953 1.00 80.96 S
ANISOU 2781 SD MET B1104 11242 10337 9184 -416 -52 -127 S
ATOM 2782 CE MET B1104 -2.738 -9.003 40.298 1.00 80.22 C
ANISOU 2782 CE MET B1104 11090 10206 9186 -543 61 -195 C
ATOM 2783 N GLY B1105 -1.476 -2.809 42.338 1.00 81.75 N
ANISOU 2783 N GLY B1105 11167 10623 9272 -358 -66 -699 N
ATOM 2784 CA GLY B1105 -1.096 -2.202 43.598 1.00 75.22 C
ANISOU 2784 CA GLY B1105 10400 9893 8288 -421 -32 -784 C
ATOM 2785 C GLY B1105 -0.111 -3.055 44.388 1.00 77.26 C
ANISOU 2785 C GLY B1105 10686 10289 8379 -474 -102 -681 C
ATOM 2786 O GLY B1105 0.059 -4.253 44.151 1.00 78.08 O
ANISOU 2786 O GLY B1105 10789 10393 8483 -443 -137 -529 O
ATOM 2787 N GLU B1106 0.551 -2.413 45.361 1.00 78.34 N
ANISOU 2787 N GLU B1106 10856 10556 8352 -550 -107 -767 N
ATOM 2788 CA GLU B1106 1.569 -3.099 46.164 1.00 80.07 C
ANISOU 2788 CA GLU B1106 11075 10978 8372 -579 -182 -666 C
ATOM 2789 C GLU B1106 0.954 -4.237 46.966 1.00 78.19 C
ANISOU 2789 C GLU B1106 10862 10807 8039 -551 -120 -536 C
ATOM 2790 O GLU B1106 1.589 -5.272 47.213 1.00 76.60 O
ANISOU 2790 O GLU B1106 10676 10699 7731 -495 -165 -363 O
ATOM 2791 CB GLU B1106 2.238 -2.101 47.110 1.00 82.05 C
ANISOU 2791 CB GLU B1106 11339 11399 8438 -704 -185 -816 C
ATOM 2792 CG GLU B1106 3.145 -1.097 46.392 1.00 84.12 C
ANISOU 2792 CG GLU B1106 11595 11620 8747 -772 -242 -934 C
ATOM 2793 CD GLU B1106 2.461 0.243 46.137 1.00 87.73 C
ANISOU 2793 CD GLU B1106 12137 11881 9316 -816 -119 -1133 C
ATOM 2794 OE1 GLU B1106 1.308 0.440 46.609 1.00 87.64 O
ANISOU 2794 OE1 GLU B1106 12168 11804 9327 -785 5 -1186 O
ATOM 2795 OE2 GLU B1106 3.070 1.084 45.431 1.00 87.34 O1-
ANISOU 2795 OE2 GLU B1106 12118 11737 9329 -868 -132 -1226 O1-
ATOM 2796 N THR B1107 -0.284 -4.030 47.392 1.00 76.53 N
ANISOU 2796 N THR B1107 10668 10554 7858 -578 2 -613 N
ATOM 2797 CA THR B1107 -1.044 -4.996 48.159 1.00 78.27 C
ANISOU 2797 CA THR B1107 10922 10822 7995 -583 93 -517 C
ATOM 2798 C THR B1107 -1.299 -6.293 47.400 1.00 78.12 C
ANISOU 2798 C THR B1107 10925 10682 8075 -534 105 -352 C
ATOM 2799 O THR B1107 -1.189 -7.387 47.979 1.00 76.67 O
ANISOU 2799 O THR B1107 10817 10541 7772 -519 147 -200 O
ATOM 2800 CB THR B1107 -2.343 -4.310 48.509 1.00 83.46 C
ANISOU 2800 CB THR B1107 11561 11454 8697 -621 222 -662 C
ATOM 2801 OG1 THR B1107 -2.683 -3.494 47.356 1.00 80.81 O
ANISOU 2801 OG1 THR B1107 11172 10971 8561 -574 214 -758 O
ATOM 2802 CG2 THR B1107 -2.188 -3.464 49.813 1.00 76.28 C
ANISOU 2802 CG2 THR B1107 10690 10697 7598 -693 269 -792 C
ATOM 2803 N GLY B1108 -1.690 -6.190 46.118 1.00 78.53 N
ANISOU 2803 N GLY B1108 10929 10579 8332 -514 89 -381 N
ATOM 2804 CA GLY B1108 -1.946 -7.385 45.316 1.00 75.52 C
ANISOU 2804 CA GLY B1108 10579 10075 8038 -505 114 -255 C
ATOM 2805 C GLY B1108 -0.701 -8.219 45.063 1.00 73.75 C
ANISOU 2805 C GLY B1108 10432 9828 7764 -428 40 -89 C
ATOM 2806 O GLY B1108 -0.736 -9.446 45.146 1.00 75.71 O
ANISOU 2806 O GLY B1108 10787 10012 7967 -415 113 58 O
ATOM 2807 N VAL B1109 0.422 -7.573 44.760 1.00 73.88 N
ANISOU 2807 N VAL B1109 10403 9893 7774 -372 -87 -106 N
ATOM 2808 CA VAL B1109 1.603 -8.351 44.397 1.00 76.04 C
ANISOU 2808 CA VAL B1109 10720 10167 8004 -270 -157 59 C
ATOM 2809 C VAL B1109 2.109 -9.102 45.621 1.00 73.21 C
ANISOU 2809 C VAL B1109 10436 9968 7414 -208 -124 212 C
ATOM 2810 O VAL B1109 2.639 -10.217 45.499 1.00 71.69 O
ANISOU 2810 O VAL B1109 10337 9733 7167 -93 -97 406 O
ATOM 2811 CB VAL B1109 2.673 -7.438 43.737 1.00 74.91 C
ANISOU 2811 CB VAL B1109 10486 10071 7904 -244 -297 -7 C
ATOM 2812 CG1 VAL B1109 3.694 -8.242 42.966 1.00 68.86 C
ANISOU 2812 CG1 VAL B1109 9742 9267 7153 -127 -358 152 C
ATOM 2813 CG2 VAL B1109 2.015 -6.447 42.791 1.00 70.77 C
ANISOU 2813 CG2 VAL B1109 9904 9411 7576 -301 -303 -173 C
ATOM 2814 N ALA B1110 1.863 -8.546 46.819 1.00 76.61 N
ANISOU 2814 N ALA B1110 10842 10571 7695 -271 -103 134 N
ATOM 2815 CA ALA B1110 2.153 -9.200 48.096 1.00 75.07 C
ANISOU 2815 CA ALA B1110 10712 10555 7256 -218 -59 272 C
ATOM 2816 C ALA B1110 1.364 -10.498 48.310 1.00 75.14 C
ANISOU 2816 C ALA B1110 10879 10414 7256 -196 104 422 C
ATOM 2817 O ALA B1110 1.829 -11.364 49.063 1.00 77.56 O
ANISOU 2817 O ALA B1110 11286 10810 7374 -85 152 616 O
ATOM 2818 CB ALA B1110 1.891 -8.220 49.241 1.00 74.09 C
ANISOU 2818 CB ALA B1110 10530 10630 6990 -326 -57 116 C
ATOM 2819 N GLY B1111 0.209 -10.676 47.656 1.00 74.81 N
ANISOU 2819 N GLY B1111 10865 10162 7398 -299 200 343 N
ATOM 2820 CA GLY B1111 -0.512 -11.941 47.736 1.00 75.26 C
ANISOU 2820 CA GLY B1111 11086 10061 7448 -328 374 464 C
ATOM 2821 C GLY B1111 0.189 -13.127 47.089 1.00 77.43 C
ANISOU 2821 C GLY B1111 11515 10173 7732 -205 416 666 C
ATOM 2822 O GLY B1111 -0.128 -14.276 47.415 1.00 78.19 O
ANISOU 2822 O GLY B1111 11808 10144 7756 -200 588 808 O
ATOM 2823 N PHE B1112 1.119 -12.889 46.169 1.00 77.97 N
ANISOU 2823 N PHE B1112 11519 10222 7884 -106 286 682 N
ATOM 2824 CA PHE B1112 1.757 -13.998 45.453 1.00 78.18 C
ANISOU 2824 CA PHE B1112 11699 10072 7932 24 343 865 C
ATOM 2825 C PHE B1112 2.955 -14.536 46.250 1.00 81.07 C
ANISOU 2825 C PHE B1112 12136 10598 8070 263 331 1101 C
ATOM 2826 O PHE B1112 4.112 -14.490 45.804 1.00 80.47 O
ANISOU 2826 O PHE B1112 11999 10605 7972 428 220 1189 O
ATOM 2827 CB PHE B1112 2.154 -13.544 44.054 1.00 75.89 C
ANISOU 2827 CB PHE B1112 11306 9694 7833 26 223 778 C
ATOM 2828 CG PHE B1112 0.991 -13.462 43.077 1.00 77.23 C
ANISOU 2828 CG PHE B1112 11456 9681 8206 -164 278 617 C
ATOM 2829 CD1 PHE B1112 0.007 -12.478 43.221 1.00 76.58 C
ANISOU 2829 CD1 PHE B1112 11221 9685 8191 -312 248 419 C
ATOM 2830 CD2 PHE B1112 0.884 -14.373 42.013 1.00 74.87 C
ANISOU 2830 CD2 PHE B1112 11288 9148 8013 -189 369 664 C
ATOM 2831 CE1 PHE B1112 -1.068 -12.407 42.321 1.00 77.41 C
ANISOU 2831 CE1 PHE B1112 11270 9689 8453 -462 292 286 C
ATOM 2832 CE2 PHE B1112 -0.185 -14.317 41.111 1.00 73.92 C
ANISOU 2832 CE2 PHE B1112 11120 8920 8045 -382 412 510 C
ATOM 2833 CZ PHE B1112 -1.158 -13.329 41.252 1.00 76.27 C
ANISOU 2833 CZ PHE B1112 11230 9351 8398 -509 364 328 C
ATOM 2834 N THR B1113 2.643 -15.101 47.441 1.00 80.20 N
ANISOU 2834 N THR B1113 12150 10547 7773 290 457 1217 N
ATOM 2835 CA THR B1113 3.674 -15.376 48.458 1.00 82.89 C
ANISOU 2835 CA THR B1113 12504 11147 7845 518 425 1427 C
ATOM 2836 C THR B1113 4.641 -16.487 48.029 1.00 82.21 C
ANISOU 2836 C THR B1113 12578 10961 7696 794 495 1700 C
ATOM 2837 O THR B1113 5.845 -16.413 48.317 1.00 82.35 O
ANISOU 2837 O THR B1113 12494 11251 7545 1020 382 1844 O
ATOM 2838 CB THR B1113 3.048 -15.732 49.834 1.00 84.07 C
ANISOU 2838 CB THR B1113 12765 11381 7798 490 559 1497 C
ATOM 2839 OG1 THR B1113 1.852 -16.498 49.661 1.00 84.85 O
ANISOU 2839 OG1 THR B1113 13071 11167 8002 337 779 1480 O
ATOM 2840 CG2 THR B1113 2.728 -14.471 50.696 1.00 77.97 C
ANISOU 2840 CG2 THR B1113 11784 10892 6951 333 438 1288 C
ATOM 2841 N ASN B1114 4.156 -17.546 47.384 1.00 88.50 N
ANISOU 2841 N ASN B1114 13631 11392 8604 786 697 1780 N
ATOM 2842 CA ASN B1114 5.112 -18.537 46.895 1.00 87.84 C
ANISOU 2842 CA ASN B1114 13717 11186 8471 1068 781 2030 C
ATOM 2843 C ASN B1114 6.016 -17.957 45.808 1.00 87.39 C
ANISOU 2843 C ASN B1114 13464 11202 8537 1138 589 1966 C
ATOM 2844 O ASN B1114 7.246 -18.019 45.927 1.00 88.13 O
ANISOU 2844 O ASN B1114 13474 11525 8487 1409 500 2139 O
ATOM 2845 CB ASN B1114 4.392 -19.787 46.398 1.00 90.57 C
ANISOU 2845 CB ASN B1114 14418 11089 8906 1008 1070 2103 C
ATOM 2846 CG ASN B1114 3.921 -20.681 47.546 1.00 93.88 C
ANISOU 2846 CG ASN B1114 15106 11431 9132 1055 1309 2280 C
ATOM 2847 OD1 ASN B1114 3.951 -20.289 48.717 1.00 94.37 O
ANISOU 2847 OD1 ASN B1114 15066 11780 9011 1097 1244 2319 O
ATOM 2848 ND2 ASN B1114 3.509 -21.900 47.207 1.00 99.47 N
ANISOU 2848 ND2 ASN B1114 16180 11745 9868 1040 1603 2388 N
ATOM 2849 N SER B1115 5.438 -17.345 44.765 1.00 83.20 N
ANISOU 2849 N SER B1115 12836 10522 8255 902 518 1723 N
ATOM 2850 CA SER B1115 6.273 -16.898 43.654 1.00 83.68 C
ANISOU 2850 CA SER B1115 12749 10609 8436 967 367 1677 C
ATOM 2851 C SER B1115 7.390 -15.961 44.115 1.00 84.39 C
ANISOU 2851 C SER B1115 12563 11115 8386 1083 140 1681 C
ATOM 2852 O SER B1115 8.485 -15.979 43.540 1.00 82.44 O
ANISOU 2852 O SER B1115 12233 10967 8124 1259 55 1770 O
ATOM 2853 CB SER B1115 5.429 -16.218 42.568 1.00 81.44 C
ANISOU 2853 CB SER B1115 12374 10157 8414 695 309 1409 C
ATOM 2854 OG SER B1115 4.230 -16.918 42.286 1.00 81.95 O
ANISOU 2854 OG SER B1115 12635 9927 8577 513 502 1354 O
ATOM 2855 N LEU B1116 7.146 -15.138 45.142 1.00 83.44 N
ANISOU 2855 N LEU B1116 12296 11255 8151 970 52 1574 N
ATOM 2856 CA LEU B1116 8.166 -14.177 45.573 1.00 83.05 C
ANISOU 2856 CA LEU B1116 11984 11617 7955 1009 -153 1532 C
ATOM 2857 C LEU B1116 9.381 -14.875 46.182 1.00 84.71 C
ANISOU 2857 C LEU B1116 12181 12113 7892 1329 -159 1818 C
ATOM 2858 O LEU B1116 10.526 -14.473 45.932 1.00 83.64 O
ANISOU 2858 O LEU B1116 11844 12258 7676 1432 -307 1844 O
ATOM 2859 CB LEU B1116 7.570 -13.179 46.569 1.00 82.12 C
ANISOU 2859 CB LEU B1116 11749 11692 7760 797 -213 1339 C
ATOM 2860 CG LEU B1116 6.278 -12.450 46.182 1.00 80.56 C
ANISOU 2860 CG LEU B1116 11555 11264 7791 522 -188 1076 C
ATOM 2861 CD1 LEU B1116 5.922 -11.387 47.238 1.00 78.04 C
ANISOU 2861 CD1 LEU B1116 11116 11176 7358 357 -244 898 C
ATOM 2862 CD2 LEU B1116 6.409 -11.834 44.808 1.00 78.20 C
ANISOU 2862 CD2 LEU B1116 11167 10817 7727 446 -277 933 C
ATOM 2863 N ARG B1117 9.153 -15.907 47.003 1.00 85.04 N
ANISOU 2863 N ARG B1117 12428 12112 7772 1494 8 2042 N
ATOM 2864 CA ARG B1117 10.267 -16.651 47.575 1.00 85.06 C
ANISOU 2864 CA ARG B1117 12435 12387 7496 1857 27 2355 C
ATOM 2865 C ARG B1117 11.036 -17.398 46.490 1.00 85.04 C
ANISOU 2865 C ARG B1117 12517 12219 7575 2107 82 2526 C
ATOM 2866 O ARG B1117 12.252 -17.585 46.614 1.00 86.11 O
ANISOU 2866 O ARG B1117 12520 12683 7516 2396 12 2723 O
ATOM 2867 CB ARG B1117 9.758 -17.598 48.669 1.00 83.38 C
ANISOU 2867 CB ARG B1117 12468 12116 7097 1986 227 2566 C
ATOM 2868 N MET B1118 10.346 -17.828 45.423 1.00 85.73 N
ANISOU 2868 N MET B1118 12813 11827 7932 1998 213 2451 N
ATOM 2869 CA MET B1118 11.011 -18.422 44.258 1.00 84.56 C
ANISOU 2869 CA MET B1118 12749 11489 7892 2187 266 2562 C
ATOM 2870 C MET B1118 11.889 -17.410 43.513 1.00 86.77 C
ANISOU 2870 C MET B1118 12706 12025 8239 2141 24 2421 C
ATOM 2871 O MET B1118 13.027 -17.720 43.137 1.00 87.85 O
ANISOU 2871 O MET B1118 12768 12324 8288 2415 -7 2592 O
ATOM 2872 CB MET B1118 9.976 -19.012 43.293 1.00 82.79 C
ANISOU 2872 CB MET B1118 12807 10720 7929 2007 454 2463 C
ATOM 2873 CG MET B1118 9.059 -20.053 43.844 1.00 81.90 C
ANISOU 2873 CG MET B1118 13044 10299 7775 1991 728 2571 C
ATOM 2874 SD MET B1118 9.908 -21.574 44.319 1.00 92.40 S
ANISOU 2874 SD MET B1118 14694 11554 8860 2480 985 3010 S
ATOM 2875 CE MET B1118 8.802 -22.814 43.628 1.00 88.19 C
ANISOU 2875 CE MET B1118 14656 10352 8499 2319 1354 2996 C
ATOM 2876 N LEU B1119 11.353 -16.208 43.241 1.00 85.61 N
ANISOU 2876 N LEU B1119 12381 11897 8250 1802 -127 2112 N
ATOM 2877 CA LEU B1119 12.121 -15.173 42.545 1.00 83.66 C
ANISOU 2877 CA LEU B1119 11857 11860 8069 1718 -334 1958 C
ATOM 2878 C LEU B1119 13.343 -14.768 43.362 1.00 85.46 C
ANISOU 2878 C LEU B1119 11819 12643 8008 1863 -484 2053 C
ATOM 2879 O LEU B1119 14.452 -14.627 42.821 1.00 84.06 O
ANISOU 2879 O LEU B1119 11469 12686 7786 1993 -581 2108 O
ATOM 2880 CB LEU B1119 11.221 -13.961 42.266 1.00 81.54 C
ANISOU 2880 CB LEU B1119 11494 11491 7996 1348 -427 1628 C
ATOM 2881 CG LEU B1119 9.970 -14.277 41.425 1.00 78.52 C
ANISOU 2881 CG LEU B1119 11317 10640 7878 1186 -299 1518 C
ATOM 2882 CD1 LEU B1119 9.206 -13.042 40.970 1.00 71.09 C
ANISOU 2882 CD1 LEU B1119 10255 9632 7125 889 -396 1221 C
ATOM 2883 CD2 LEU B1119 10.376 -15.121 40.228 1.00 76.31 C
ANISOU 2883 CD2 LEU B1119 11168 10111 7714 1338 -216 1634 C
ATOM 2884 N GLN B1120 13.166 -14.632 44.682 1.00 85.05 N
ANISOU 2884 N GLN B1120 11725 12853 7736 1845 -496 2080 N
ATOM 2885 CA GLN B1120 14.277 -14.287 45.556 1.00 84.90 C
ANISOU 2885 CA GLN B1120 11440 13421 7398 1963 -636 2166 C
ATOM 2886 C GLN B1120 15.316 -15.399 45.672 1.00 84.36 C
ANISOU 2886 C GLN B1120 11385 13558 7112 2411 -573 2531 C
ATOM 2887 O GLN B1120 16.451 -15.110 46.064 1.00 85.10 O
ANISOU 2887 O GLN B1120 11195 14189 6950 2537 -711 2609 O
ATOM 2888 CB GLN B1120 13.768 -13.914 46.946 1.00 85.79 C
ANISOU 2888 CB GLN B1120 11522 13759 7314 1829 -651 2104 C
ATOM 2889 CG GLN B1120 14.893 -13.745 47.941 1.00 87.96 C
ANISOU 2889 CG GLN B1120 11534 14682 7206 1972 -776 2227 C
ATOM 2890 CD GLN B1120 14.409 -13.723 49.365 1.00 92.12 C
ANISOU 2890 CD GLN B1120 12086 15416 7498 1923 -749 2245 C
ATOM 2891 OE1 GLN B1120 13.377 -14.317 49.701 1.00 94.60 O
ANISOU 2891 OE1 GLN B1120 12670 15385 7890 1931 -585 2302 O
ATOM 2892 NE2 GLN B1120 15.175 -13.074 50.230 1.00 95.28 N
ANISOU 2892 NE2 GLN B1120 12203 16410 7589 1865 -902 2199 N
ATOM 2893 N GLN B1121 14.969 -16.654 45.355 1.00 84.48 N
ANISOU 2893 N GLN B1121 11721 13175 7201 2656 -354 2755 N
ATOM 2894 CA GLN B1121 15.945 -17.750 45.335 1.00 86.94 C
ANISOU 2894 CA GLN B1121 12093 13612 7327 3129 -252 3120 C
ATOM 2895 C GLN B1121 16.540 -18.010 43.947 1.00 87.01 C
ANISOU 2895 C GLN B1121 12116 13427 7517 3252 -232 3148 C
ATOM 2896 O GLN B1121 17.206 -19.034 43.754 1.00 87.66 O
ANISOU 2896 O GLN B1121 12322 13489 7495 3662 -93 3451 O
ATOM 2897 CB GLN B1121 15.328 -19.053 45.882 1.00 88.79 C
ANISOU 2897 CB GLN B1121 12723 13520 7494 3366 26 3383 C
ATOM 2898 CG GLN B1121 15.101 -19.066 47.416 1.00 90.74 C
ANISOU 2898 CG GLN B1121 12948 14079 7452 3404 27 3483 C
ATOM 2899 CD GLN B1121 14.292 -20.264 47.926 1.00 92.50 C
ANISOU 2899 CD GLN B1121 13601 13902 7643 3557 325 3698 C
ATOM 2900 OE1 GLN B1121 14.212 -21.313 47.274 1.00 92.47 O
ANISOU 2900 OE1 GLN B1121 13921 13465 7748 3757 560 3867 O
ATOM 2901 NE2 GLN B1121 13.676 -20.097 49.099 1.00 94.03 N
ANISOU 2901 NE2 GLN B1121 13814 14226 7686 3438 334 3676 N
ATOM 2902 N LYS B1122 16.305 -17.122 42.978 1.00 85.32 N
ANISOU 2902 N LYS B1122 11794 13059 7563 2927 -350 2851 N
ATOM 2903 CA LYS B1122 16.727 -17.286 41.590 1.00 82.70 C
ANISOU 2903 CA LYS B1122 11487 12504 7430 2986 -332 2836 C
ATOM 2904 C LYS B1122 16.056 -18.471 40.907 1.00 82.13 C
ANISOU 2904 C LYS B1122 11831 11839 7536 3101 -67 2950 C
ATOM 2905 O LYS B1122 16.462 -18.840 39.798 1.00 79.70 O
ANISOU 2905 O LYS B1122 11593 11332 7357 3213 -8 2987 O
ATOM 2906 CB LYS B1122 18.256 -17.443 41.458 1.00 81.42 C
ANISOU 2906 CB LYS B1122 11079 12799 7056 3326 -411 3044 C
ATOM 2907 CG LYS B1122 19.068 -16.608 42.422 1.00 84.03 C
ANISOU 2907 CG LYS B1122 11014 13819 7093 3293 -626 3018 C
ATOM 2908 CD LYS B1122 18.770 -15.114 42.302 1.00 84.79 C
ANISOU 2908 CD LYS B1122 10891 14015 7311 2802 -824 2632 C
ATOM 2909 CE LYS B1122 20.063 -14.294 42.270 1.00 86.58 C
ANISOU 2909 CE LYS B1122 10701 14844 7350 2764 -1027 2570 C
ATOM 2910 NZ LYS B1122 19.916 -12.947 42.919 1.00 87.73 N
ANISOU 2910 NZ LYS B1122 10627 15283 7421 2344 -1192 2267 N
ATOM 2911 N ARG B1123 15.064 -19.103 41.550 1.00 83.54 N
ANISOU 2911 N ARG B1123 12297 11736 7707 3066 112 3002 N
ATOM 2912 CA ARG B1123 14.391 -20.274 40.981 1.00 82.69 C
ANISOU 2912 CA ARG B1123 12615 11063 7740 3129 398 3095 C
ATOM 2913 C ARG B1123 13.333 -19.804 39.983 1.00 80.93 C
ANISOU 2913 C ARG B1123 12454 10461 7836 2713 384 2775 C
ATOM 2914 O ARG B1123 12.124 -19.931 40.188 1.00 81.77 O
ANISOU 2914 O ARG B1123 12739 10290 8039 2463 488 2653 O
ATOM 2915 CB ARG B1123 13.785 -21.148 42.070 1.00 82.68 C
ANISOU 2915 CB ARG B1123 12902 10928 7584 3240 614 3280 C
ATOM 2916 CG ARG B1123 14.780 -22.051 42.766 1.00 86.29 C
ANISOU 2916 CG ARG B1123 13437 11607 7741 3754 735 3676 C
ATOM 2917 CD ARG B1123 14.094 -23.062 43.693 1.00 90.85 C
ANISOU 2917 CD ARG B1123 14365 11933 8222 3837 1007 3837 C
ATOM 2918 NE ARG B1123 12.880 -23.635 43.114 1.00 92.10 N
ANISOU 2918 NE ARG B1123 14935 11475 8583 3592 1250 3738 N
ATOM 2919 CZ ARG B1123 12.835 -24.739 42.379 1.00 90.99 C
ANISOU 2919 CZ ARG B1123 15117 10876 8578 3673 1524 3783 C
ATOM 2920 NH1 ARG B1123 13.934 -25.421 42.085 1.00 95.02 N
ANISOU 2920 NH1 ARG B1123 15578 11447 9077 4002 1597 3903 N
ATOM 2921 NH2 ARG B1123 11.656 -25.168 41.925 1.00 84.89 N
ANISOU 2921 NH2 ARG B1123 14704 9593 7957 3382 1738 3667 N
ATOM 2922 N TRP B1124 13.824 -19.274 38.861 1.00 79.11 N
ANISOU 2922 N TRP B1124 12061 10244 7754 2653 257 2650 N
ATOM 2923 CA TRP B1124 12.957 -18.581 37.913 1.00 81.04 C
ANISOU 2923 CA TRP B1124 12275 10246 8270 2275 188 2344 C
ATOM 2924 C TRP B1124 12.012 -19.524 37.191 1.00 82.25 C
ANISOU 2924 C TRP B1124 12787 9880 8585 2169 429 2316 C
ATOM 2925 O TRP B1124 10.904 -19.118 36.826 1.00 81.82 O
ANISOU 2925 O TRP B1124 12747 9641 8700 1833 416 2081 O
ATOM 2926 CB TRP B1124 13.794 -17.784 36.915 1.00 79.30 C
ANISOU 2926 CB TRP B1124 11799 10188 8143 2256 1 2238 C
ATOM 2927 CG TRP B1124 14.485 -16.716 37.654 1.00 78.79 C
ANISOU 2927 CG TRP B1124 11388 10620 7928 2233 -227 2189 C
ATOM 2928 CD1 TRP B1124 13.908 -15.724 38.436 1.00 77.09 C
ANISOU 2928 CD1 TRP B1124 11023 10575 7691 1973 -352 2003 C
ATOM 2929 CD2 TRP B1124 15.883 -16.556 37.771 1.00 75.54 C
ANISOU 2929 CD2 TRP B1124 10738 10627 7336 2471 -338 2326 C
ATOM 2930 NE1 TRP B1124 14.889 -14.949 39.009 1.00 75.68 N
ANISOU 2930 NE1 TRP B1124 10545 10883 7328 2008 -531 2000 N
ATOM 2931 CE2 TRP B1124 16.110 -15.440 38.617 1.00 76.54 C
ANISOU 2931 CE2 TRP B1124 10574 11177 7332 2303 -534 2196 C
ATOM 2932 CE3 TRP B1124 16.971 -17.247 37.251 1.00 74.11 C
ANISOU 2932 CE3 TRP B1124 10554 10526 7078 2808 -282 2544 C
ATOM 2933 CZ2 TRP B1124 17.383 -15.000 38.936 1.00 78.34 C
ANISOU 2933 CZ2 TRP B1124 10494 11925 7345 2426 -682 2262 C
ATOM 2934 CZ3 TRP B1124 18.239 -16.811 37.566 1.00 78.44 C
ANISOU 2934 CZ3 TRP B1124 10777 11607 7418 2967 -436 2628 C
ATOM 2935 CH2 TRP B1124 18.439 -15.694 38.399 1.00 80.22 C
ANISOU 2935 CH2 TRP B1124 10700 12274 7507 2758 -639 2481 C
ATOM 2936 N ASP B1125 12.417 -20.764 36.948 1.00 85.93 N
ANISOU 2936 N ASP B1125 13543 10115 8992 2442 663 2543 N
ATOM 2937 CA ASP B1125 11.480 -21.675 36.305 1.00 84.96 C
ANISOU 2937 CA ASP B1125 13788 9491 9002 2285 921 2489 C
ATOM 2938 C ASP B1125 10.340 -22.053 37.256 1.00 85.43 C
ANISOU 2938 C ASP B1125 14042 9407 9011 2109 1070 2470 C
ATOM 2939 O ASP B1125 9.187 -22.196 36.827 1.00 85.48 O
ANISOU 2939 O ASP B1125 14188 9132 9157 1777 1171 2277 O
ATOM 2940 CB ASP B1125 12.228 -22.902 35.752 1.00 85.03 C
ANISOU 2940 CB ASP B1125 14103 9245 8960 2618 1170 2726 C
ATOM 2941 CG ASP B1125 13.034 -22.577 34.481 1.00 88.83 C
ANISOU 2941 CG ASP B1125 14435 9760 9557 2682 1059 2669 C
ATOM 2942 OD1 ASP B1125 12.857 -23.277 33.455 1.00 94.55 O
ANISOU 2942 OD1 ASP B1125 15422 10109 10393 2639 1247 2634 O
ATOM 2943 OD2 ASP B1125 13.846 -21.621 34.494 1.00 92.21 O1-
ANISOU 2943 OD2 ASP B1125 14491 10591 9954 2753 794 2647 O1-
ATOM 2944 N GLU B1126 10.623 -22.191 38.554 1.00 84.62 N
ANISOU 2944 N GLU B1126 13930 9528 8694 2312 1082 2660 N
ATOM 2945 CA GLU B1126 9.552 -22.565 39.477 1.00 83.29 C
ANISOU 2945 CA GLU B1126 13954 9223 8468 2146 1237 2650 C
ATOM 2946 C GLU B1126 8.521 -21.444 39.654 1.00 81.03 C
ANISOU 2946 C GLU B1126 13420 9068 8300 1744 1048 2345 C
ATOM 2947 O GLU B1126 7.323 -21.721 39.814 1.00 79.69 O
ANISOU 2947 O GLU B1126 13410 8680 8188 1472 1189 2226 O
ATOM 2948 CB GLU B1126 10.150 -22.986 40.818 1.00 83.86 C
ANISOU 2948 CB GLU B1126 14077 9525 8262 2488 1297 2946 C
ATOM 2949 N ALA B1127 8.955 -20.181 39.595 1.00 80.18 N
ANISOU 2949 N ALA B1127 12931 9309 8225 1698 750 2212 N
ATOM 2950 CA ALA B1127 8.047 -19.070 39.861 1.00 79.30 C
ANISOU 2950 CA ALA B1127 12600 9330 8202 1374 590 1949 C
ATOM 2951 C ALA B1127 6.989 -18.906 38.770 1.00 81.64 C
ANISOU 2951 C ALA B1127 12927 9358 8733 1053 619 1705 C
ATOM 2952 O ALA B1127 5.856 -18.512 39.062 1.00 81.63 O
ANISOU 2952 O ALA B1127 12884 9345 8789 790 621 1533 O
ATOM 2953 CB ALA B1127 8.840 -17.782 40.048 1.00 78.57 C
ANISOU 2953 CB ALA B1127 12140 9642 8070 1405 303 1870 C
ATOM 2954 N ALA B1128 7.333 -19.215 37.510 1.00 81.87 N
ANISOU 2954 N ALA B1128 13021 9199 8886 1077 647 1690 N
ATOM 2955 CA ALA B1128 6.417 -19.012 36.385 1.00 77.34 C
ANISOU 2955 CA ALA B1128 12441 8433 8513 782 652 1459 C
ATOM 2956 C ALA B1128 5.229 -19.957 36.428 1.00 77.76 C
ANISOU 2956 C ALA B1128 12769 8198 8578 562 906 1413 C
ATOM 2957 O ALA B1128 4.151 -19.618 35.937 1.00 77.16 O
ANISOU 2957 O ALA B1128 12617 8082 8616 260 892 1196 O
ATOM 2958 CB ALA B1128 7.168 -19.174 35.060 1.00 79.90 C
ANISOU 2958 CB ALA B1128 12780 8643 8937 875 629 1469 C
ATOM 2959 N VAL B1129 5.409 -21.162 36.960 1.00 79.76 N
ANISOU 2959 N VAL B1129 13348 8252 8704 705 1157 1616 N
ATOM 2960 CA VAL B1129 4.257 -22.028 37.172 1.00 80.60 C
ANISOU 2960 CA VAL B1129 13731 8098 8797 457 1422 1564 C
ATOM 2961 C VAL B1129 3.364 -21.479 38.279 1.00 81.75 C
ANISOU 2961 C VAL B1129 13737 8438 8887 292 1369 1480 C
ATOM 2962 O VAL B1129 2.132 -21.548 38.183 1.00 83.44 O
ANISOU 2962 O VAL B1129 13971 8577 9155 -38 1459 1301 O
ATOM 2963 CB VAL B1129 4.722 -23.463 37.455 1.00 82.38 C
ANISOU 2963 CB VAL B1129 14391 8018 8892 671 1742 1817 C
ATOM 2964 CG1 VAL B1129 3.607 -24.475 37.150 1.00 87.70 C
ANISOU 2964 CG1 VAL B1129 15410 8323 9588 344 2062 1714 C
ATOM 2965 CG2 VAL B1129 5.966 -23.736 36.640 1.00 80.21 C
ANISOU 2965 CG2 VAL B1129 14167 7676 8633 974 1729 1957 C
ATOM 2966 N ASN B1130 3.956 -20.921 39.342 1.00 78.94 N
ANISOU 2966 N ASN B1130 13225 8360 8407 504 1227 1598 N
ATOM 2967 CA ASN B1130 3.143 -20.376 40.435 1.00 81.52 C
ANISOU 2967 CA ASN B1130 13428 8876 8671 357 1184 1516 C
ATOM 2968 C ASN B1130 2.227 -19.251 39.954 1.00 79.39 C
ANISOU 2968 C ASN B1130 12865 8742 8557 72 1011 1227 C
ATOM 2969 O ASN B1130 1.022 -19.245 40.260 1.00 75.86 O
ANISOU 2969 O ASN B1130 12416 8281 8124 -183 1097 1094 O
ATOM 2970 CB ASN B1130 4.049 -19.899 41.583 1.00 80.59 C
ANISOU 2970 CB ASN B1130 13173 9070 8376 630 1044 1676 C
ATOM 2971 CG ASN B1130 4.763 -21.070 42.308 1.00 80.64 C
ANISOU 2971 CG ASN B1130 13474 8986 8178 938 1248 1996 C
ATOM 2972 OD1 ASN B1130 5.968 -20.989 42.614 1.00 80.41 O
ANISOU 2972 OD1 ASN B1130 13363 9170 8020 1260 1146 2183 O
ATOM 2973 ND2 ASN B1130 4.009 -22.133 42.622 1.00 78.17 N
ANISOU 2973 ND2 ASN B1130 13500 8384 7818 840 1543 2061 N
ATOM 2974 N LEU B1131 2.783 -18.296 39.192 1.00 76.72 N
ANISOU 2974 N LEU B1131 12281 8542 8328 125 781 1137 N
ATOM 2975 CA LEU B1131 2.038 -17.104 38.809 1.00 75.87 C
ANISOU 2975 CA LEU B1131 11895 8583 8348 -73 614 897 C
ATOM 2976 C LEU B1131 1.035 -17.372 37.706 1.00 75.72 C
ANISOU 2976 C LEU B1131 11900 8405 8465 -328 694 734 C
ATOM 2977 O LEU B1131 0.219 -16.496 37.398 1.00 75.53 O
ANISOU 2977 O LEU B1131 11656 8512 8530 -488 592 549 O
ATOM 2978 CB LEU B1131 2.970 -15.982 38.349 1.00 74.58 C
ANISOU 2978 CB LEU B1131 11492 8600 8245 59 368 858 C
ATOM 2979 CG LEU B1131 4.212 -15.571 39.143 1.00 75.53 C
ANISOU 2979 CG LEU B1131 11526 8944 8228 295 243 991 C
ATOM 2980 CD1 LEU B1131 5.514 -16.054 38.459 1.00 74.76 C
ANISOU 2980 CD1 LEU B1131 11485 8802 8119 524 222 1148 C
ATOM 2981 CD2 LEU B1131 4.195 -14.074 39.329 1.00 72.18 C
ANISOU 2981 CD2 LEU B1131 10832 8753 7839 226 44 823 C
ATOM 2982 N ALA B1132 1.096 -18.534 37.076 1.00 77.95 N
ANISOU 2982 N ALA B1132 12439 8425 8754 -363 881 798 N
ATOM 2983 CA ALA B1132 0.097 -18.834 36.061 1.00 77.28 C
ANISOU 2983 CA ALA B1132 12371 8228 8765 -653 969 622 C
ATOM 2984 C ALA B1132 -1.118 -19.550 36.643 1.00 78.04 C
ANISOU 2984 C ALA B1132 12609 8254 8789 -920 1193 562 C
ATOM 2985 O ALA B1132 -2.206 -19.506 36.046 1.00 78.99 O
ANISOU 2985 O ALA B1132 12632 8417 8962 -1211 1227 372 O
ATOM 2986 CB ALA B1132 0.726 -19.657 34.941 1.00 75.80 C
ANISOU 2986 CB ALA B1132 12387 7792 8622 -611 1066 674 C
ATOM 2987 N LYS B1133 -0.947 -20.233 37.779 1.00 79.15 N
ANISOU 2987 N LYS B1133 12973 8306 8794 -829 1354 724 N
ATOM 2988 CA LYS B1133 -2.072 -20.750 38.547 1.00 76.43 C
ANISOU 2988 CA LYS B1133 12739 7935 8365 -1073 1555 673 C
ATOM 2989 C LYS B1133 -2.587 -19.593 39.395 1.00 77.86 C
ANISOU 2989 C LYS B1133 12612 8436 8535 -1079 1378 588 C
ATOM 2990 O LYS B1133 -2.294 -19.465 40.586 1.00 78.29 O
ANISOU 2990 O LYS B1133 12692 8578 8477 -928 1373 708 O
ATOM 2991 CB LYS B1133 -1.645 -21.949 39.383 1.00 74.11 C
ANISOU 2991 CB LYS B1133 12839 7396 7923 -950 1818 900 C
ATOM 2992 N SER B1134 -3.309 -18.692 38.726 1.00 79.09 N
ANISOU 2992 N SER B1134 12469 8780 8801 -1232 1228 382 N
ATOM 2993 CA SER B1134 -3.802 -17.500 39.400 1.00 79.16 C
ANISOU 2993 CA SER B1134 12190 9074 8812 -1216 1072 290 C
ATOM 2994 C SER B1134 -4.878 -16.834 38.554 1.00 79.31 C
ANISOU 2994 C SER B1134 11939 9265 8932 -1417 997 73 C
ATOM 2995 O SER B1134 -4.798 -16.818 37.322 1.00 79.34 O
ANISOU 2995 O SER B1134 11888 9230 9029 -1461 940 7 O
ATOM 2996 CB SER B1134 -2.671 -16.508 39.697 1.00 76.25 C
ANISOU 2996 CB SER B1134 11691 8826 8454 -921 847 367 C
ATOM 2997 OG SER B1134 -2.390 -15.719 38.572 1.00 77.17 O
ANISOU 2997 OG SER B1134 11622 8994 8706 -878 670 276 O
ATOM 2998 N ARG B1135 -5.865 -16.249 39.252 1.00 81.19 N
ANISOU 2998 N ARG B1135 11996 9718 9134 -1512 997 -26 N
ATOM 2999 CA ARG B1135 -6.967 -15.546 38.597 1.00 81.73 C
ANISOU 2999 CA ARG B1135 11772 10014 9267 -1658 933 -212 C
ATOM 3000 C ARG B1135 -6.493 -14.359 37.750 1.00 82.63 C
ANISOU 3000 C ARG B1135 11671 10223 9500 -1467 701 -253 C
ATOM 3001 O ARG B1135 -7.201 -13.945 36.824 1.00 83.04 O
ANISOU 3001 O ARG B1135 11516 10424 9612 -1551 647 -374 O
ATOM 3002 CB ARG B1135 -7.960 -15.063 39.657 1.00 79.22 C
ANISOU 3002 CB ARG B1135 11308 9915 8877 -1723 980 -280 C
ATOM 3003 CG ARG B1135 -8.722 -16.164 40.391 1.00 79.93 C
ANISOU 3003 CG ARG B1135 11566 9958 8845 -1973 1227 -278 C
ATOM 3004 CD ARG B1135 -9.396 -15.625 41.645 1.00 80.94 C
ANISOU 3004 CD ARG B1135 11580 10282 8891 -1967 1259 -306 C
ATOM 3005 NE ARG B1135 -10.472 -16.499 42.087 1.00 79.82 N
ANISOU 3005 NE ARG B1135 11504 10178 8647 -2270 1491 -363 N
ATOM 3006 CZ ARG B1135 -10.301 -17.543 42.880 1.00 80.52 C
ANISOU 3006 CZ ARG B1135 11900 10068 8626 -2354 1692 -253 C
ATOM 3007 NH1 ARG B1135 -9.103 -17.861 43.357 1.00 79.81 N
ANISOU 3007 NH1 ARG B1135 12064 9757 8502 -2128 1682 -63 N
ATOM 3008 NH2 ARG B1135 -11.351 -18.302 43.176 1.00 82.09 N
ANISOU 3008 NH2 ARG B1135 12152 10304 8733 -2673 1918 -328 N
ATOM 3009 N TRP B1136 -5.331 -13.778 38.085 1.00 80.03 N
ANISOU 3009 N TRP B1136 11380 9837 9190 -1216 572 -154 N
ATOM 3010 CA TRP B1136 -4.731 -12.688 37.318 1.00 76.57 C
ANISOU 3010 CA TRP B1136 10790 9447 8858 -1046 377 -183 C
ATOM 3011 C TRP B1136 -4.367 -13.141 35.910 1.00 82.36 C
ANISOU 3011 C TRP B1136 11560 10060 9673 -1078 348 -184 C
ATOM 3012 O TRP B1136 -4.622 -12.442 34.915 1.00 80.99 O
ANISOU 3012 O TRP B1136 11208 9980 9584 -1062 244 -268 O
ATOM 3013 CB TRP B1136 -3.478 -12.212 38.059 1.00 76.38 C
ANISOU 3013 CB TRP B1136 10835 9388 8799 -831 281 -79 C
ATOM 3014 CG TRP B1136 -2.485 -11.383 37.243 1.00 77.95 C
ANISOU 3014 CG TRP B1136 10961 9568 9090 -672 110 -76 C
ATOM 3015 CD1 TRP B1136 -2.716 -10.160 36.683 1.00 76.37 C
ANISOU 3015 CD1 TRP B1136 10578 9463 8976 -618 0 -180 C
ATOM 3016 CD2 TRP B1136 -1.101 -11.707 36.943 1.00 75.60 C
ANISOU 3016 CD2 TRP B1136 10777 9155 8791 -538 48 44 C
ATOM 3017 NE1 TRP B1136 -1.575 -9.711 36.041 1.00 76.68 N
ANISOU 3017 NE1 TRP B1136 10624 9438 9073 -492 -122 -142 N
ATOM 3018 CE2 TRP B1136 -0.570 -10.633 36.197 1.00 74.55 C
ANISOU 3018 CE2 TRP B1136 10515 9060 8750 -445 -103 -10 C
ATOM 3019 CE3 TRP B1136 -0.267 -12.801 37.234 1.00 76.13 C
ANISOU 3019 CE3 TRP B1136 11047 9099 8780 -471 121 203 C
ATOM 3020 CZ2 TRP B1136 0.760 -10.621 35.724 1.00 74.29 C
ANISOU 3020 CZ2 TRP B1136 10525 8968 8734 -318 -193 72 C
ATOM 3021 CZ3 TRP B1136 1.059 -12.785 36.771 1.00 74.82 C
ANISOU 3021 CZ3 TRP B1136 10913 8890 8627 -308 28 298 C
ATOM 3022 CH2 TRP B1136 1.554 -11.703 36.022 1.00 72.03 C
ANISOU 3022 CH2 TRP B1136 10404 8598 8368 -248 -132 224 C
ATOM 3023 N TYR B1137 -3.742 -14.317 35.818 1.00 80.15 N
ANISOU 3023 N TYR B1137 11528 9567 9358 -1104 454 -79 N
ATOM 3024 CA TYR B1137 -3.380 -14.882 34.533 1.00 79.14 C
ANISOU 3024 CA TYR B1137 11478 9299 9294 -1148 461 -81 C
ATOM 3025 C TYR B1137 -4.616 -15.168 33.686 1.00 81.68 C
ANISOU 3025 C TYR B1137 11693 9715 9627 -1417 531 -236 C
ATOM 3026 O TYR B1137 -4.594 -14.985 32.464 1.00 81.30 O
ANISOU 3026 O TYR B1137 11553 9691 9645 -1443 454 -300 O
ATOM 3027 CB TYR B1137 -2.532 -16.131 34.760 1.00 76.90 C
ANISOU 3027 CB TYR B1137 11517 8753 8950 -1102 607 72 C
ATOM 3028 CG TYR B1137 -2.206 -16.875 33.486 1.00 79.56 C
ANISOU 3028 CG TYR B1137 11985 8907 9336 -1167 666 64 C
ATOM 3029 CD1 TYR B1137 -3.185 -17.594 32.800 1.00 79.31 C
ANISOU 3029 CD1 TYR B1137 12001 8839 9293 -1468 811 -64 C
ATOM 3030 CD2 TYR B1137 -0.935 -16.768 32.915 1.00 79.74 C
ANISOU 3030 CD2 TYR B1137 12057 8830 9410 -945 568 165 C
ATOM 3031 CE1 TYR B1137 -2.897 -18.259 31.651 1.00 81.51 C
ANISOU 3031 CE1 TYR B1137 12413 8954 9603 -1548 876 -89 C
ATOM 3032 CE2 TYR B1137 -0.627 -17.413 31.752 1.00 78.25 C
ANISOU 3032 CE2 TYR B1137 11993 8475 9264 -996 627 154 C
ATOM 3033 CZ TYR B1137 -1.605 -18.159 31.115 1.00 82.56 C
ANISOU 3033 CZ TYR B1137 12615 8959 9795 -1298 783 24 C
ATOM 3034 OH TYR B1137 -1.277 -18.805 29.939 1.00 82.97 O
ANISOU 3034 OH TYR B1137 12807 8840 9876 -1364 854 -3 O
ATOM 3035 N ASN B1138 -5.703 -15.616 34.321 1.00 88.33 N
ANISOU 3035 N ASN B1138 12533 10643 10387 -1631 678 -302 N
ATOM 3036 CA ASN B1138 -6.965 -15.866 33.619 1.00 89.51 C
ANISOU 3036 CA ASN B1138 12534 10964 10512 -1921 748 -466 C
ATOM 3037 C ASN B1138 -7.659 -14.583 33.169 1.00 90.16 C
ANISOU 3037 C ASN B1138 12247 11371 10639 -1850 577 -567 C
ATOM 3038 O ASN B1138 -8.495 -14.621 32.257 1.00 90.28 O
ANISOU 3038 O ASN B1138 12084 11582 10638 -2026 576 -688 O
ATOM 3039 CB ASN B1138 -7.922 -16.651 34.513 1.00 90.74 C
ANISOU 3039 CB ASN B1138 12774 11150 10552 -2178 962 -509 C
ATOM 3040 CG ASN B1138 -7.742 -18.134 34.386 1.00 90.25 C
ANISOU 3040 CG ASN B1138 13065 10798 10429 -2390 1199 -481 C
ATOM 3041 OD1 ASN B1138 -6.782 -18.706 34.914 1.00 90.04 O
ANISOU 3041 OD1 ASN B1138 13335 10488 10386 -2237 1278 -320 O
ATOM 3042 ND2 ASN B1138 -8.675 -18.780 33.690 1.00 92.89 N
ANISOU 3042 ND2 ASN B1138 13376 11210 10710 -2747 1332 -638 N
ATOM 3043 N GLN B1139 -7.398 -13.456 33.827 1.00 87.97 N
ANISOU 3043 N GLN B1139 11854 11174 10398 -1602 453 -523 N
ATOM 3044 CA GLN B1139 -8.211 -12.289 33.521 1.00 88.67 C
ANISOU 3044 CA GLN B1139 11627 11555 10510 -1523 347 -610 C
ATOM 3045 C GLN B1139 -7.568 -11.430 32.432 1.00 88.07 C
ANISOU 3045 C GLN B1139 11459 11469 10534 -1323 176 -593 C
ATOM 3046 O GLN B1139 -8.286 -10.887 31.585 1.00 88.49 O
ANISOU 3046 O GLN B1139 11279 11749 10594 -1317 116 -664 O
ATOM 3047 CB GLN B1139 -8.472 -11.503 34.813 1.00 90.08 C
ANISOU 3047 CB GLN B1139 11741 11826 10658 -1391 350 -596 C
ATOM 3048 CG GLN B1139 -9.753 -10.664 34.866 1.00 91.01 C
ANISOU 3048 CG GLN B1139 11558 12276 10746 -1376 347 -693 C
ATOM 3049 CD GLN B1139 -9.441 -9.188 34.937 1.00 94.13 C
ANISOU 3049 CD GLN B1139 11852 12707 11208 -1073 226 -674 C
ATOM 3050 OE1 GLN B1139 -8.497 -8.772 35.624 1.00 96.26 O
ANISOU 3050 OE1 GLN B1139 12274 12798 11504 -929 187 -613 O
ATOM 3051 NE2 GLN B1139 -10.251 -8.379 34.261 1.00 95.94 N
ANISOU 3051 NE2 GLN B1139 11826 13181 11445 -976 182 -726 N
ATOM 3052 N THR B1140 -6.228 -11.304 32.438 1.00 88.50 N
ANISOU 3052 N THR B1140 11686 11289 10651 -1154 101 -494 N
ATOM 3053 CA THR B1140 -5.457 -10.621 31.388 1.00 83.44 C
ANISOU 3053 CA THR B1140 11004 10597 10103 -990 -42 -470 C
ATOM 3054 C THR B1140 -4.300 -11.518 30.960 1.00 81.69 C
ANISOU 3054 C THR B1140 11012 10122 9905 -1000 -31 -389 C
ATOM 3055 O THR B1140 -3.133 -11.279 31.304 1.00 78.66 O
ANISOU 3055 O THR B1140 10740 9598 9548 -835 -90 -297 O
ATOM 3056 CB THR B1140 -4.923 -9.262 31.841 1.00 81.61 C
ANISOU 3056 CB THR B1140 10718 10371 9919 -745 -148 -442 C
ATOM 3057 OG1 THR B1140 -4.128 -9.415 33.019 1.00 81.75 O
ANISOU 3057 OG1 THR B1140 10898 10263 9900 -694 -125 -372 O
ATOM 3058 CG2 THR B1140 -6.049 -8.316 32.119 1.00 82.39 C
ANISOU 3058 CG2 THR B1140 10607 10700 9998 -689 -141 -514 C
ATOM 3059 N PRO B1141 -4.593 -12.564 30.194 1.00 81.39 N
ANISOU 3059 N PRO B1141 11046 10034 9842 -1198 58 -427 N
ATOM 3060 CA PRO B1141 -3.536 -13.513 29.810 1.00 79.40 C
ANISOU 3060 CA PRO B1141 11047 9516 9604 -1195 110 -344 C
ATOM 3061 C PRO B1141 -2.427 -12.930 28.945 1.00 78.25 C
ANISOU 3061 C PRO B1141 10890 9295 9546 -999 -35 -290 C
ATOM 3062 O PRO B1141 -1.265 -13.349 29.086 1.00 76.74 O
ANISOU 3062 O PRO B1141 10881 8913 9365 -881 -25 -179 O
ATOM 3063 CB PRO B1141 -4.319 -14.595 29.055 1.00 79.93 C
ANISOU 3063 CB PRO B1141 11172 9579 9619 -1490 250 -442 C
ATOM 3064 CG PRO B1141 -5.520 -13.886 28.535 1.00 80.66 C
ANISOU 3064 CG PRO B1141 10955 9997 9696 -1586 180 -572 C
ATOM 3065 CD PRO B1141 -5.893 -12.906 29.598 1.00 83.39 C
ANISOU 3065 CD PRO B1141 11150 10494 10041 -1438 122 -555 C
ATOM 3066 N ASN B1142 -2.735 -12.021 28.016 1.00 75.42 N
ANISOU 3066 N ASN B1142 10327 9089 9240 -954 -157 -356 N
ATOM 3067 CA ASN B1142 -1.676 -11.615 27.105 1.00 73.15 C
ANISOU 3067 CA ASN B1142 10059 8707 9028 -804 -267 -307 C
ATOM 3068 C ASN B1142 -0.634 -10.779 27.821 1.00 72.87 C
ANISOU 3068 C ASN B1142 10043 8616 9028 -585 -357 -223 C
ATOM 3069 O ASN B1142 0.572 -10.934 27.573 1.00 72.03 O
ANISOU 3069 O ASN B1142 10044 8376 8948 -480 -392 -142 O
ATOM 3070 CB ASN B1142 -2.248 -10.875 25.907 1.00 76.33 C
ANISOU 3070 CB ASN B1142 10257 9283 9461 -800 -362 -383 C
ATOM 3071 CG ASN B1142 -2.935 -11.809 24.940 1.00 76.90 C
ANISOU 3071 CG ASN B1142 10325 9414 9482 -1033 -288 -468 C
ATOM 3072 OD1 ASN B1142 -2.577 -12.992 24.842 1.00 74.30 O
ANISOU 3072 OD1 ASN B1142 10206 8898 9126 -1167 -171 -460 O
ATOM 3073 ND2 ASN B1142 -3.921 -11.285 24.206 1.00 81.56 N
ANISOU 3073 ND2 ASN B1142 10679 10272 10040 -1080 -343 -550 N
ATOM 3074 N ARG B1143 -1.081 -9.879 28.698 1.00 75.05 N
ANISOU 3074 N ARG B1143 10211 9012 9291 -525 -385 -249 N
ATOM 3075 CA ARG B1143 -0.156 -9.159 29.563 1.00 70.99 C
ANISOU 3075 CA ARG B1143 9731 8465 8778 -377 -444 -194 C
ATOM 3076 C ARG B1143 0.580 -10.108 30.512 1.00 71.45 C
ANISOU 3076 C ARG B1143 9962 8424 8763 -372 -376 -95 C
ATOM 3077 O ARG B1143 1.792 -9.967 30.709 1.00 71.20 O
ANISOU 3077 O ARG B1143 9984 8346 8721 -253 -433 -18 O
ATOM 3078 CB ARG B1143 -0.921 -8.088 30.341 1.00 72.46 C
ANISOU 3078 CB ARG B1143 9794 8788 8948 -339 -450 -260 C
ATOM 3079 CG ARG B1143 -0.084 -7.234 31.295 1.00 70.72 C
ANISOU 3079 CG ARG B1143 9609 8556 8707 -231 -494 -243 C
ATOM 3080 CD ARG B1143 -0.895 -6.014 31.796 1.00 73.56 C
ANISOU 3080 CD ARG B1143 9865 9020 9065 -182 -480 -327 C
ATOM 3081 NE ARG B1143 -0.115 -5.103 32.633 1.00 72.98 N
ANISOU 3081 NE ARG B1143 9840 8930 8961 -118 -505 -344 N
ATOM 3082 CZ ARG B1143 -0.550 -3.923 33.059 1.00 73.45 C
ANISOU 3082 CZ ARG B1143 9864 9025 9018 -61 -474 -420 C
ATOM 3083 NH1 ARG B1143 -1.768 -3.493 32.763 1.00 74.25 N
ANISOU 3083 NH1 ARG B1143 9864 9200 9146 -15 -423 -466 N
ATOM 3084 NH2 ARG B1143 0.267 -3.149 33.778 1.00 71.35 N
ANISOU 3084 NH2 ARG B1143 9667 8735 8709 -49 -484 -455 N
ATOM 3085 N ALA B1144 -0.127 -11.077 31.117 1.00 72.71 N
ANISOU 3085 N ALA B1144 10205 8566 8854 -497 -246 -89 N
ATOM 3086 CA ALA B1144 0.505 -11.933 32.131 1.00 72.11 C
ANISOU 3086 CA ALA B1144 10308 8402 8689 -457 -162 29 C
ATOM 3087 C ALA B1144 1.637 -12.770 31.535 1.00 70.50 C
ANISOU 3087 C ALA B1144 10264 8035 8489 -369 -140 143 C
ATOM 3088 O ALA B1144 2.720 -12.902 32.138 1.00 65.97 O
ANISOU 3088 O ALA B1144 9760 7450 7854 -213 -160 266 O
ATOM 3089 CB ALA B1144 -0.538 -12.842 32.784 1.00 72.28 C
ANISOU 3089 CB ALA B1144 10418 8408 8636 -625 3 12 C
ATOM 3090 N LYS B1145 1.404 -13.343 30.347 1.00 69.66 N
ANISOU 3090 N LYS B1145 10206 7825 8436 -464 -94 104 N
ATOM 3091 CA LYS B1145 2.448 -14.093 29.657 1.00 66.26 C
ANISOU 3091 CA LYS B1145 9932 7228 8015 -370 -59 202 C
ATOM 3092 C LYS B1145 3.673 -13.238 29.343 1.00 64.47 C
ANISOU 3092 C LYS B1145 9603 7062 7830 -177 -220 253 C
ATOM 3093 O LYS B1145 4.800 -13.737 29.409 1.00 62.50 O
ANISOU 3093 O LYS B1145 9459 6746 7542 -22 -202 384 O
ATOM 3094 CB LYS B1145 1.901 -14.681 28.376 1.00 68.43 C
ANISOU 3094 CB LYS B1145 10256 7408 8335 -536 11 114 C
ATOM 3095 CG LYS B1145 0.715 -15.581 28.568 1.00 73.34 C
ANISOU 3095 CG LYS B1145 10981 7985 8901 -783 188 39 C
ATOM 3096 CD LYS B1145 0.872 -16.808 27.679 1.00 75.01 C
ANISOU 3096 CD LYS B1145 11429 7972 9099 -894 354 38 C
ATOM 3097 CE LYS B1145 -0.448 -17.501 27.469 1.00 78.69 C
ANISOU 3097 CE LYS B1145 11941 8444 9513 -1227 511 -106 C
ATOM 3098 NZ LYS B1145 -1.101 -16.999 26.230 1.00 79.52 N
ANISOU 3098 NZ LYS B1145 11831 8725 9656 -1380 409 -264 N
ATOM 3099 N ARG B1146 3.491 -11.963 28.980 1.00 62.82 N
ANISOU 3099 N ARG B1146 9196 6983 7689 -178 -363 156 N
ATOM 3100 CA ARG B1146 4.669 -11.131 28.724 1.00 65.01 C
ANISOU 3100 CA ARG B1146 9395 7313 7994 -34 -493 191 C
ATOM 3101 C ARG B1146 5.486 -10.907 29.994 1.00 63.09 C
ANISOU 3101 C ARG B1146 9147 7172 7654 77 -523 273 C
ATOM 3102 O ARG B1146 6.715 -11.086 29.994 1.00 58.47 O
ANISOU 3102 O ARG B1146 8580 6610 7025 208 -557 375 O
ATOM 3103 CB ARG B1146 4.262 -9.794 28.092 1.00 66.25 C
ANISOU 3103 CB ARG B1146 9385 7554 8235 -60 -602 74 C
ATOM 3104 CG ARG B1146 3.664 -9.974 26.706 1.00 65.83 C
ANISOU 3104 CG ARG B1146 9308 7451 8252 -137 -597 13 C
ATOM 3105 CD ARG B1146 3.633 -8.739 25.879 1.00 64.94 C
ANISOU 3105 CD ARG B1146 9063 7399 8211 -94 -700 -50 C
ATOM 3106 NE ARG B1146 2.630 -7.797 26.345 1.00 69.93 N
ANISOU 3106 NE ARG B1146 9581 8144 8845 -107 -712 -126 N
ATOM 3107 CZ ARG B1146 1.366 -7.783 25.945 1.00 70.59 C
ANISOU 3107 CZ ARG B1146 9574 8318 8930 -179 -685 -193 C
ATOM 3108 NH1 ARG B1146 0.889 -8.715 25.125 1.00 65.22 N
ANISOU 3108 NH1 ARG B1146 8905 7635 8239 -293 -642 -213 N
ATOM 3109 NH2 ARG B1146 0.557 -6.819 26.395 1.00 69.53 N
ANISOU 3109 NH2 ARG B1146 9330 8296 8791 -138 -688 -245 N
ATOM 3110 N VAL B1147 4.808 -10.510 31.086 1.00 67.41 N
ANISOU 3110 N VAL B1147 9652 7813 8148 23 -510 228 N
ATOM 3111 CA VAL B1147 5.461 -10.203 32.366 1.00 64.20 C
ANISOU 3111 CA VAL B1147 9224 7547 7624 97 -543 281 C
ATOM 3112 C VAL B1147 6.168 -11.432 32.906 1.00 63.19 C
ANISOU 3112 C VAL B1147 9234 7393 7382 214 -462 457 C
ATOM 3113 O VAL B1147 7.318 -11.363 33.372 1.00 61.77 O
ANISOU 3113 O VAL B1147 9019 7348 7104 346 -518 553 O
ATOM 3114 CB VAL B1147 4.423 -9.660 33.370 1.00 67.74 C
ANISOU 3114 CB VAL B1147 9625 8078 8037 4 -516 190 C
ATOM 3115 CG1 VAL B1147 5.088 -9.160 34.679 1.00 68.52 C
ANISOU 3115 CG1 VAL B1147 9684 8350 7998 51 -559 214 C
ATOM 3116 CG2 VAL B1147 3.611 -8.539 32.744 1.00 65.73 C
ANISOU 3116 CG2 VAL B1147 9253 7829 7891 -67 -561 41 C
ATOM 3117 N ILE B1148 5.497 -12.585 32.831 1.00 64.31 N
ANISOU 3117 N ILE B1148 9540 7374 7522 169 -313 504 N
ATOM 3118 CA ILE B1148 6.069 -13.830 33.341 1.00 66.49 C
ANISOU 3118 CA ILE B1148 10003 7574 7684 303 -187 689 C
ATOM 3119 C ILE B1148 7.371 -14.183 32.592 1.00 65.97 C
ANISOU 3119 C ILE B1148 9967 7479 7618 488 -213 808 C
ATOM 3120 O ILE B1148 8.404 -14.506 33.208 1.00 66.40 O
ANISOU 3120 O ILE B1148 10037 7648 7545 692 -215 971 O
ATOM 3121 CB ILE B1148 4.990 -14.943 33.287 1.00 63.55 C
ANISOU 3121 CB ILE B1148 9836 6991 7318 167 13 684 C
ATOM 3122 CG1 ILE B1148 3.960 -14.720 34.417 1.00 69.54 C
ANISOU 3122 CG1 ILE B1148 10566 7838 8018 41 53 623 C
ATOM 3123 CG2 ILE B1148 5.587 -16.340 33.433 1.00 63.38 C
ANISOU 3123 CG2 ILE B1148 10082 6794 7206 316 194 879 C
ATOM 3124 CD1 ILE B1148 2.679 -15.630 34.383 1.00 70.48 C
ANISOU 3124 CD1 ILE B1148 10841 7796 8142 -171 248 567 C
ATOM 3125 N ALA B1149 7.370 -14.061 31.259 1.00 66.83 N
ANISOU 3125 N ALA B1149 10058 7478 7855 434 -242 730 N
ATOM 3126 CA ALA B1149 8.570 -14.395 30.478 1.00 65.52 C
ANISOU 3126 CA ALA B1149 9918 7281 7694 605 -255 834 C
ATOM 3127 C ALA B1149 9.763 -13.499 30.824 1.00 64.25 C
ANISOU 3127 C ALA B1149 9556 7386 7470 734 -419 873 C
ATOM 3128 O ALA B1149 10.915 -13.965 30.860 1.00 61.89 O
ANISOU 3128 O ALA B1149 9267 7165 7082 944 -409 1029 O
ATOM 3129 CB ALA B1149 8.262 -14.280 28.995 1.00 62.87 C
ANISOU 3129 CB ALA B1149 9581 6806 7503 492 -268 719 C
ATOM 3130 N THR B1150 9.513 -12.205 31.051 1.00 62.81 N
ANISOU 3130 N THR B1150 9191 7353 7320 609 -554 728 N
ATOM 3131 CA THR B1150 10.574 -11.322 31.524 1.00 65.01 C
ANISOU 3131 CA THR B1150 9290 7898 7511 668 -687 733 C
ATOM 3132 C THR B1150 11.172 -11.806 32.836 1.00 68.78 C
ANISOU 3132 C THR B1150 9766 8577 7788 811 -666 883 C
ATOM 3133 O THR B1150 12.396 -11.742 33.022 1.00 67.51 O
ANISOU 3133 O THR B1150 9494 8648 7510 950 -732 978 O
ATOM 3134 CB THR B1150 10.040 -9.904 31.684 1.00 63.53 C
ANISOU 3134 CB THR B1150 8973 7786 7380 488 -783 542 C
ATOM 3135 OG1 THR B1150 9.063 -9.643 30.666 1.00 62.74 O
ANISOU 3135 OG1 THR B1150 8905 7490 7444 375 -766 427 O
ATOM 3136 CG2 THR B1150 11.174 -8.868 31.693 1.00 65.43 C
ANISOU 3136 CG2 THR B1150 9048 8247 7567 480 -905 495 C
ATOM 3137 N PHE B1151 10.324 -12.259 33.774 1.00 68.67 N
ANISOU 3137 N PHE B1151 9858 8518 7717 779 -576 907 N
ATOM 3138 CA PHE B1151 10.844 -12.800 35.025 1.00 68.93 C
ANISOU 3138 CA PHE B1151 9907 8741 7541 936 -542 1073 C
ATOM 3139 C PHE B1151 11.751 -14.001 34.746 1.00 70.31 C
ANISOU 3139 C PHE B1151 10199 8879 7638 1208 -447 1307 C
ATOM 3140 O PHE B1151 12.888 -14.064 35.233 1.00 70.52 O
ANISOU 3140 O PHE B1151 10112 9187 7494 1404 -501 1448 O
ATOM 3141 CB PHE B1151 9.687 -13.197 35.959 1.00 69.87 C
ANISOU 3141 CB PHE B1151 10158 8766 7622 851 -431 1065 C
ATOM 3142 CG PHE B1151 9.206 -12.099 36.886 1.00 67.55 C
ANISOU 3142 CG PHE B1151 9727 8657 7283 690 -519 915 C
ATOM 3143 CD1 PHE B1151 10.089 -11.440 37.744 1.00 70.14 C
ANISOU 3143 CD1 PHE B1151 9889 9321 7440 729 -632 924 C
ATOM 3144 CD2 PHE B1151 7.851 -11.753 36.917 1.00 66.00 C
ANISOU 3144 CD2 PHE B1151 9565 8315 7195 496 -474 760 C
ATOM 3145 CE1 PHE B1151 9.643 -10.426 38.615 1.00 68.83 C
ANISOU 3145 CE1 PHE B1151 9627 9305 7220 563 -687 768 C
ATOM 3146 CE2 PHE B1151 7.379 -10.744 37.775 1.00 67.62 C
ANISOU 3146 CE2 PHE B1151 9666 8669 7356 368 -528 622 C
ATOM 3147 CZ PHE B1151 8.286 -10.067 38.621 1.00 69.46 C
ANISOU 3147 CZ PHE B1151 9768 9198 7426 395 -629 619 C
ATOM 3148 N ARG B1152 11.283 -14.944 33.916 1.00 74.65 N
ANISOU 3148 N ARG B1152 10970 9097 8298 1224 -296 1345 N
ATOM 3149 CA ARG B1152 12.008 -16.207 33.735 1.00 75.15 C
ANISOU 3149 CA ARG B1152 11218 9058 8280 1500 -144 1578 C
ATOM 3150 C ARG B1152 13.338 -16.025 32.995 1.00 74.67 C
ANISOU 3150 C ARG B1152 11013 9155 8204 1681 -234 1649 C
ATOM 3151 O ARG B1152 14.321 -16.708 33.311 1.00 76.18 O
ANISOU 3151 O ARG B1152 11227 9478 8241 1984 -176 1875 O
ATOM 3152 CB ARG B1152 11.128 -17.223 33.005 1.00 75.25 C
ANISOU 3152 CB ARG B1152 11530 8652 8409 1418 66 1563 C
ATOM 3153 CG ARG B1152 11.744 -18.623 32.896 1.00 78.72 C
ANISOU 3153 CG ARG B1152 12244 8908 8759 1703 288 1806 C
ATOM 3154 CD ARG B1152 10.676 -19.546 32.414 1.00 82.08 C
ANISOU 3154 CD ARG B1152 12988 8923 9275 1531 519 1746 C
ATOM 3155 NE ARG B1152 10.007 -18.900 31.288 1.00 85.48 N
ANISOU 3155 NE ARG B1152 13316 9268 9893 1240 422 1497 N
ATOM 3156 CZ ARG B1152 10.366 -19.037 30.018 1.00 86.82 C
ANISOU 3156 CZ ARG B1152 13518 9309 10162 1244 434 1455 C
ATOM 3157 NH1 ARG B1152 9.765 -18.353 29.054 1.00 83.48 N
ANISOU 3157 NH1 ARG B1152 12972 8862 9886 996 326 1240 N
ATOM 3158 NH2 ARG B1152 11.355 -19.882 29.711 1.00 85.87 N
ANISOU 3158 NH2 ARG B1152 13558 9091 9978 1525 564 1644 N
ATOM 3159 N THR B1153 13.394 -15.135 31.995 1.00 72.00 N
ANISOU 3159 N THR B1153 10527 8815 8014 1518 -363 1472 N
ATOM 3160 CA THR B1153 14.624 -14.956 31.218 1.00 72.69 C
ANISOU 3160 CA THR B1153 10479 9045 8094 1662 -437 1526 C
ATOM 3161 C THR B1153 15.421 -13.717 31.612 1.00 71.59 C
ANISOU 3161 C THR B1153 10024 9305 7871 1602 -641 1449 C
ATOM 3162 O THR B1153 16.648 -13.718 31.455 1.00 69.04 O
ANISOU 3162 O THR B1153 9553 9234 7445 1776 -694 1553 O
ATOM 3163 CB THR B1153 14.325 -14.887 29.706 1.00 69.38 C
ANISOU 3163 CB THR B1153 10128 8356 7877 1539 -420 1401 C
ATOM 3164 OG1 THR B1153 13.938 -13.542 29.338 1.00 69.84 O
ANISOU 3164 OG1 THR B1153 10007 8481 8048 1284 -580 1179 O
ATOM 3165 CG2 THR B1153 13.253 -15.920 29.283 1.00 68.01 C
ANISOU 3165 CG2 THR B1153 10258 7786 7794 1470 -222 1392 C
ATOM 3166 N GLY B1154 14.769 -12.698 32.176 1.00 77.29 N
ANISOU 3166 N GLY B1154 10646 10106 8613 1362 -738 1271 N
ATOM 3167 CA GLY B1154 15.437 -11.443 32.472 1.00 75.76 C
ANISOU 3167 CA GLY B1154 10194 10240 8349 1239 -902 1153 C
ATOM 3168 C GLY B1154 15.848 -10.637 31.248 1.00 75.31 C
ANISOU 3168 C GLY B1154 10040 10147 8429 1123 -980 1022 C
ATOM 3169 O GLY B1154 16.837 -9.893 31.310 1.00 74.51 O
ANISOU 3169 O GLY B1154 9731 10345 8233 1084 -1085 982 O
ATOM 3170 N THR B1155 15.110 -10.754 30.134 1.00 70.18 N
ANISOU 3170 N THR B1155 9528 9156 7980 1052 -928 950 N
ATOM 3171 CA THR B1155 15.368 -9.973 28.924 1.00 70.09 C
ANISOU 3171 CA THR B1155 9448 9081 8102 941 -991 828 C
ATOM 3172 C THR B1155 14.083 -9.288 28.462 1.00 70.21 C
ANISOU 3172 C THR B1155 9538 8852 8287 734 -990 651 C
ATOM 3173 O THR B1155 12.991 -9.487 29.034 1.00 69.91 O
ANISOU 3173 O THR B1155 9594 8702 8267 674 -938 620 O
ATOM 3174 CB THR B1155 15.934 -10.828 27.767 1.00 68.24 C
ANISOU 3174 CB THR B1155 9286 8716 7924 1106 -928 940 C
ATOM 3175 OG1 THR B1155 14.980 -11.808 27.340 1.00 68.60 O
ANISOU 3175 OG1 THR B1155 9564 8434 8066 1131 -797 972 O
ATOM 3176 CG2 THR B1155 17.201 -11.551 28.195 1.00 68.23 C
ANISOU 3176 CG2 THR B1155 9208 8972 7745 1368 -910 1143 C
ATOM 3177 N TRP B1156 14.226 -8.469 27.411 1.00 67.26 N
ANISOU 3177 N TRP B1156 9114 8418 8024 636 -1041 544 N
ATOM 3178 CA TRP B1156 13.101 -7.739 26.831 1.00 68.31 C
ANISOU 3178 CA TRP B1156 9297 8354 8302 484 -1041 397 C
ATOM 3179 C TRP B1156 12.512 -8.447 25.604 1.00 66.64 C
ANISOU 3179 C TRP B1156 9202 7903 8215 511 -982 415 C
ATOM 3180 O TRP B1156 11.580 -7.920 24.981 1.00 66.56 O
ANISOU 3180 O TRP B1156 9212 7767 8310 410 -985 311 O
ATOM 3181 CB TRP B1156 13.514 -6.297 26.470 1.00 66.70 C
ANISOU 3181 CB TRP B1156 8996 8218 8130 355 -1112 267 C
ATOM 3182 CG TRP B1156 13.914 -5.357 27.648 1.00 69.20 C
ANISOU 3182 CG TRP B1156 9217 8753 8323 245 -1152 185 C
ATOM 3183 CD1 TRP B1156 15.181 -4.935 27.972 1.00 68.02 C
ANISOU 3183 CD1 TRP B1156 8933 8866 8046 206 -1205 179 C
ATOM 3184 CD2 TRP B1156 13.030 -4.720 28.602 1.00 69.03 C
ANISOU 3184 CD2 TRP B1156 9226 8721 8282 139 -1131 82 C
ATOM 3185 NE1 TRP B1156 15.141 -4.101 29.070 1.00 68.75 N
ANISOU 3185 NE1 TRP B1156 8982 9108 8033 60 -1216 68 N
ATOM 3186 CE2 TRP B1156 13.837 -3.947 29.471 1.00 69.47 C
ANISOU 3186 CE2 TRP B1156 9184 9018 8194 28 -1168 10 C
ATOM 3187 CE3 TRP B1156 11.642 -4.735 28.802 1.00 67.55 C
ANISOU 3187 CE3 TRP B1156 9128 8367 8171 121 -1079 40 C
ATOM 3188 CZ2 TRP B1156 13.301 -3.199 30.522 1.00 68.20 C
ANISOU 3188 CZ2 TRP B1156 9042 8900 7971 -98 -1144 -106 C
ATOM 3189 CZ3 TRP B1156 11.114 -3.997 29.832 1.00 68.18 C
ANISOU 3189 CZ3 TRP B1156 9212 8497 8197 24 -1059 -61 C
ATOM 3190 CH2 TRP B1156 11.942 -3.234 30.683 1.00 69.22 C
ANISOU 3190 CH2 TRP B1156 9275 8835 8192 -83 -1086 -135 C
ATOM 3191 N ASP B1157 13.003 -9.644 25.276 1.00 66.12 N
ANISOU 3191 N ASP B1157 9219 7783 8122 650 -915 544 N
ATOM 3192 CA ASP B1157 12.602 -10.316 24.045 1.00 66.44 C
ANISOU 3192 CA ASP B1157 9377 7608 8259 651 -848 544 C
ATOM 3193 C ASP B1157 11.097 -10.331 23.809 1.00 64.94 C
ANISOU 3193 C ASP B1157 9258 7269 8148 504 -809 439 C
ATOM 3194 O ASP B1157 10.646 -10.373 22.653 1.00 67.23 O
ANISOU 3194 O ASP B1157 9581 7445 8520 441 -798 379 O
ATOM 3195 CB ASP B1157 13.180 -11.724 24.061 1.00 66.39 C
ANISOU 3195 CB ASP B1157 9505 7533 8187 826 -730 702 C
ATOM 3196 CG ASP B1157 14.695 -11.707 24.218 1.00 69.89 C
ANISOU 3196 CG ASP B1157 9837 8183 8533 1004 -771 820 C
ATOM 3197 OD1 ASP B1157 15.292 -10.586 24.215 1.00 70.81 O
ANISOU 3197 OD1 ASP B1157 9771 8493 8641 941 -893 753 O
ATOM 3198 OD2 ASP B1157 15.303 -12.795 24.327 1.00 71.36 O1-
ANISOU 3198 OD2 ASP B1157 10119 8350 8642 1206 -669 979 O1-
ATOM 3199 N ALA B1158 10.312 -10.269 24.870 1.00 65.48 N
ANISOU 3199 N ALA B1158 9331 7371 8179 446 -792 413 N
ATOM 3200 CA ALA B1158 8.871 -10.454 24.766 1.00 65.61 C
ANISOU 3200 CA ALA B1158 9397 7289 8241 313 -738 327 C
ATOM 3201 C ALA B1158 8.137 -9.195 24.317 1.00 64.52 C
ANISOU 3201 C ALA B1158 9138 7197 8178 220 -820 198 C
ATOM 3202 O ALA B1158 7.024 -9.298 23.776 1.00 64.70 O
ANISOU 3202 O ALA B1158 9163 7178 8243 126 -791 127 O
ATOM 3203 CB ALA B1158 8.318 -10.944 26.117 1.00 61.79 C
ANISOU 3203 CB ALA B1158 8971 6831 7677 297 -668 360 C
ATOM 3204 N TYR B1159 8.716 -8.017 24.514 1.00 64.25 N
ANISOU 3204 N TYR B1159 9006 7258 8149 242 -906 167 N
ATOM 3205 CA TYR B1159 7.897 -6.823 24.366 1.00 67.02 C
ANISOU 3205 CA TYR B1159 9285 7627 8552 183 -941 61 C
ATOM 3206 C TYR B1159 7.984 -6.185 22.953 1.00 65.63 C
ANISOU 3206 C TYR B1159 9079 7402 8455 192 -981 28 C
ATOM 3207 O TYR B1159 9.052 -5.904 22.426 1.00 59.82 O
ANISOU 3207 O TYR B1159 8336 6663 7730 228 -1018 53 O
ATOM 3208 CB TYR B1159 8.239 -5.820 25.492 1.00 65.40 C
ANISOU 3208 CB TYR B1159 9033 7522 8294 172 -969 21 C
ATOM 3209 CG TYR B1159 7.327 -5.999 26.708 1.00 68.33 C
ANISOU 3209 CG TYR B1159 9413 7937 8613 135 -922 -2 C
ATOM 3210 CD1 TYR B1159 6.078 -5.368 26.777 1.00 67.85 C
ANISOU 3210 CD1 TYR B1159 9323 7869 8589 99 -895 -84 C
ATOM 3211 CD2 TYR B1159 7.699 -6.831 27.762 1.00 66.34 C
ANISOU 3211 CD2 TYR B1159 9197 7746 8262 156 -895 73 C
ATOM 3212 CE1 TYR B1159 5.252 -5.555 27.857 1.00 67.53 C
ANISOU 3212 CE1 TYR B1159 9283 7879 8497 63 -844 -106 C
ATOM 3213 CE2 TYR B1159 6.874 -7.029 28.846 1.00 65.86 C
ANISOU 3213 CE2 TYR B1159 9154 7723 8146 116 -843 57 C
ATOM 3214 CZ TYR B1159 5.652 -6.389 28.904 1.00 68.15 C
ANISOU 3214 CZ TYR B1159 9408 8003 8481 58 -819 -41 C
ATOM 3215 OH TYR B1159 4.827 -6.579 30.018 1.00 66.08 O
ANISOU 3215 OH TYR B1159 9155 7793 8158 16 -759 -60 O
TER 3216 TYR B1159
HETATM 3217 C7 CW9 A 401 19.303 6.824 4.527 1.00 64.37 C
ANISOU 3217 C7 CW9 A 401 9902 6099 8458 -85 -308 236 C
HETATM 3218 C CW9 A 401 23.461 8.956 0.999 1.00 74.21 C
ANISOU 3218 C CW9 A 401 11467 7201 9528 -680 185 230 C
HETATM 3219 C5 CW9 A 401 23.023 2.119 0.692 1.00 66.11 C
ANISOU 3219 C5 CW9 A 401 9479 7045 8594 -16 -584 346 C
HETATM 3220 C10 CW9 A 401 23.630 6.728 6.057 1.00 71.33 C
ANISOU 3220 C10 CW9 A 401 10387 7523 9192 -888 -246 -95 C
HETATM 3221 C14 CW9 A 401 22.389 4.597 9.715 1.00 68.38 C
ANISOU 3221 C14 CW9 A 401 9609 7545 8828 -702 -598 -158 C
HETATM 3222 C15 CW9 A 401 21.459 7.272 10.189 1.00 71.31 C
ANISOU 3222 C15 CW9 A 401 10457 7434 9202 -933 -296 -300 C
HETATM 3223 C11 CW9 A 401 24.995 6.779 6.738 1.00 75.04 C
ANISOU 3223 C11 CW9 A 401 10674 8267 9569 -1167 -229 -214 C
HETATM 3224 C6 CW9 A 401 21.241 6.115 3.449 1.00 68.07 C
ANISOU 3224 C6 CW9 A 401 10203 6776 8884 -264 -327 218 C
HETATM 3225 C4 CW9 A 401 21.126 3.505 0.728 1.00 64.12 C
ANISOU 3225 C4 CW9 A 401 9481 6518 8364 81 -548 394 C
HETATM 3226 C1 CW9 A 401 23.946 6.809 1.815 1.00 73.20 C
ANISOU 3226 C1 CW9 A 401 10856 7525 9431 -626 -123 177 C
HETATM 3227 N CW9 A 401 21.841 5.509 2.200 1.00 66.10 N
ANISOU 3227 N CW9 A 401 9885 6616 8613 -222 -355 277 N
HETATM 3228 C3 CW9 A 401 20.879 4.976 1.203 1.00 66.50 C
ANISOU 3228 C3 CW9 A 401 9958 6641 8666 7 -426 382 C
HETATM 3229 C9 CW9 A 401 22.393 7.146 6.567 1.00 69.37 C
ANISOU 3229 C9 CW9 A 401 10297 7071 8990 -776 -228 -83 C
HETATM 3230 C13 CW9 A 401 21.828 6.812 8.949 1.00 70.92 C
ANISOU 3230 C13 CW9 A 401 10360 7413 9174 -838 -330 -206 C
HETATM 3231 C12 CW9 A 401 22.025 7.724 7.940 1.00 71.93 C
ANISOU 3231 C12 CW9 A 401 10684 7348 9300 -892 -182 -188 C
HETATM 3232 C8 CW9 A 401 21.386 6.921 5.598 1.00 67.92 C
ANISOU 3232 C8 CW9 A 401 10203 6745 8857 -512 -261 47 C
HETATM 3233 C2 CW9 A 401 23.302 5.413 1.976 1.00 71.41 C
ANISOU 3233 C2 CW9 A 401 10453 7433 9247 -405 -314 226 C
HETATM 3234 O1 CW9 A 401 22.121 2.852 1.494 1.00 65.45 O
ANISOU 3234 O1 CW9 A 401 9486 6843 8538 -22 -581 328 O
HETATM 3235 O CW9 A 401 23.055 7.606 1.058 1.00 73.38 O
ANISOU 3235 O CW9 A 401 11130 7292 9460 -494 -29 268 O
HETATM 3236 N1 CW9 A 401 19.928 6.324 3.465 1.00 68.28 N
ANISOU 3236 N1 CW9 A 401 10331 6677 8934 -79 -339 280 N
HETATM 3237 N2 CW9 A 401 20.036 7.141 5.609 1.00 65.66 N
ANISOU 3237 N2 CW9 A 401 10040 6300 8610 -308 -263 114 N
HETATM 3238 N3 CW9 A 401 23.380 6.281 4.811 1.00 70.28 N
ANISOU 3238 N3 CW9 A 401 10276 7334 9091 -702 -278 19 N
HETATM 3239 N4 CW9 A 401 21.986 6.418 4.564 1.00 69.04 N
ANISOU 3239 N4 CW9 A 401 10270 6974 8987 -483 -291 101 N
HETATM 3240 O2 CW9 A 401 22.018 5.444 8.658 1.00 70.52 O
ANISOU 3240 O2 CW9 A 401 10091 7564 9138 -684 -489 -127 O
HETATM 3241 C16 CW9 A 401 21.282 8.625 10.387 1.00 76.50 C
ANISOU 3241 C16 CW9 A 401 11373 7852 9841 -1079 -103 -380 C
HETATM 3242 BR CW9 A 401 20.758 9.193 12.188 1.00 67.37 BR
ANISOU 3242 BR CW9 A 401 10289 6665 8642 -1219 -46 -529 BR
HETATM 3243 C17 CW9 A 401 21.473 9.541 9.358 1.00 70.01 C
ANISOU 3243 C17 CW9 A 401 10774 6807 9020 -1124 65 -355 C
HETATM 3244 C18 CW9 A 401 21.837 9.081 8.101 1.00 71.96 C
ANISOU 3244 C18 CW9 A 401 10958 7098 9285 -1023 17 -251 C
HETATM 3245 O3 CW9 A 401 22.055 9.965 7.021 1.00 72.36 O
ANISOU 3245 O3 CW9 A 401 11233 6933 9326 -1059 188 -211 O
HETATM 3246 C19 CW9 A 401 21.385 11.195 7.127 1.00 72.58 C
ANISOU 3246 C19 CW9 A 401 11590 6630 9356 -1051 394 -218 C
HETATM 3247 C20 CW9 A 401 17.786 7.032 4.432 1.00 62.41 C
ANISOU 3247 C20 CW9 A 401 9742 5749 8222 161 -318 324 C
HETATM 3248 H1 CW9 A 401 24.421 9.012 1.126 1.00 90.80 H
HETATM 3249 H2 CW9 A 401 23.013 9.460 1.696 1.00 90.80 H
HETATM 3250 H3 CW9 A 401 23.228 9.327 0.133 1.00 90.80 H
HETATM 3251 H4 CW9 A 401 22.526 1.553 0.081 1.00 80.38 H
HETATM 3252 H5 CW9 A 401 23.584 1.567 1.259 1.00 80.38 H
HETATM 3253 H6 CW9 A 401 23.578 2.733 0.187 1.00 80.38 H
HETATM 3254 H7 CW9 A 401 22.819 3.804 9.359 1.00 80.03 H
HETATM 3255 H8 CW9 A 401 21.599 4.338 10.215 1.00 80.03 H
HETATM 3256 H9 CW9 A 401 23.005 5.063 10.302 1.00 80.03 H
HETATM 3257 H10 CW9 A 401 21.330 6.675 10.891 1.00 86.62 H
HETATM 3258 H11 CW9 A 401 25.690 6.845 6.064 1.00 88.86 H
HETATM 3259 H12 CW9 A 401 25.127 5.973 7.260 1.00 88.86 H
HETATM 3260 H13 CW9 A 401 25.036 7.553 7.321 1.00 88.86 H
HETATM 3261 H14 CW9 A 401 21.407 3.521 -0.200 1.00 78.90 H
HETATM 3262 H15 CW9 A 401 20.296 3.009 0.809 1.00 78.90 H
HETATM 3263 H16 CW9 A 401 24.088 7.209 2.687 1.00 88.92 H
HETATM 3264 H17 CW9 A 401 24.794 6.729 1.350 1.00 88.92 H
HETATM 3265 H18 CW9 A 401 20.912 5.550 0.422 1.00 82.83 H
HETATM 3266 H19 CW9 A 401 19.992 5.017 1.594 1.00 82.83 H
HETATM 3267 H20 CW9 A 401 23.464 4.895 1.172 1.00 87.63 H
HETATM 3268 H21 CW9 A 401 23.708 4.963 2.734 1.00 87.63 H
HETATM 3269 H22 CW9 A 401 21.357 10.451 9.511 1.00 82.83 H
HETATM 3270 H23 CW9 A 401 21.418 11.655 6.273 1.00 88.08 H
HETATM 3271 H24 CW9 A 401 20.460 11.039 7.375 1.00 88.08 H
HETATM 3272 H25 CW9 A 401 21.814 11.740 7.805 1.00 88.08 H
HETATM 3273 H26 CW9 A 401 17.340 6.452 5.070 1.00 75.63 H
HETATM 3274 H27 CW9 A 401 17.573 7.957 4.632 1.00 75.63 H
HETATM 3275 H28 CW9 A 401 17.485 6.817 3.535 1.00 75.63 H
CONECT 647 1201
CONECT 1201 647
CONECT 3217 3236 3237 3247
CONECT 3218 3235 3248 3249 3250
CONECT 3219 3234 3251 3252 3253
CONECT 3220 3223 3229 3238
CONECT 3221 3240 3254 3255 3256
CONECT 3222 3230 3241 3257
CONECT 3223 3220 3258 3259 3260
CONECT 3224 3227 3236 3239
CONECT 3225 3228 3234 3261 3262
CONECT 3226 3233 3235 3263 3264
CONECT 3227 3224 3228 3233
CONECT 3228 3225 3227 3265 3266
CONECT 3229 3220 3231 3232
CONECT 3230 3222 3231 3240
CONECT 3231 3229 3230 3244
CONECT 3232 3229 3237 3239
CONECT 3233 3226 3227 3267 3268
CONECT 3234 3219 3225
CONECT 3235 3218 3226
CONECT 3236 3217 3224
CONECT 3237 3217 3232
CONECT 3238 3220 3239
CONECT 3239 3224 3232 3238
CONECT 3240 3221 3230
CONECT 3241 3222 3242 3243
CONECT 3242 3241
CONECT 3243 3241 3244 3269
CONECT 3244 3231 3243 3245
CONECT 3245 3244 3246
CONECT 3246 3245 3270 3271 3272
CONECT 3247 3217 3273 3274 3275
CONECT 3248 3218
CONECT 3249 3218
CONECT 3250 3218
CONECT 3251 3219
CONECT 3252 3219
CONECT 3253 3219
CONECT 3254 3221
CONECT 3255 3221
CONECT 3256 3221
CONECT 3257 3222
CONECT 3258 3223
CONECT 3259 3223
CONECT 3260 3223
CONECT 3261 3225
CONECT 3262 3225
CONECT 3263 3226
CONECT 3264 3226
CONECT 3265 3228
CONECT 3266 3228
CONECT 3267 3233
CONECT 3268 3233
CONECT 3269 3243
CONECT 3270 3246
CONECT 3271 3246
CONECT 3272 3246
CONECT 3273 3247
CONECT 3274 3247
CONECT 3275 3247
MASTER 309 0 1 21 3 0 0 6 3245 2 61 35
END