HEADER MEMBRANE PROTEIN 18-NOV-21 7SUS
TITLE CRYSTAL STRUCTURE OF APELIN RECEPTOR IN COMPLEX WITH SMALL MOLECULE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APELIN RECEPTOR, WITH RUBREDOXIN INSERTION;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, CLOSTRIDIUM PASTEURIANUM;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 1501;
SOURCE 5 GENE: APLNR, AGTRL1, APJ;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS GPCR, CLASS A GPCR, SMALL MOLECULE, MEMBRANE PROTEIN, APELIN RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR F.XU,Y.YUE,L.E.LIU,G.W.HAN,M.HANSON
REVDAT 1 27-JUL-22 7SUS 0
JRNL AUTH Y.YUE,L.LIU,L.J.WU,Y.WU,L.WANG,F.LI,J.LIU,G.W.HAN,B.CHEN,
JRNL AUTH 2 X.LIN,R.L.BROUILLETTE,E.BREAULT,J.M.LONGPRE,S.SHI,H.LEI,
JRNL AUTH 3 P.SARRET,R.C.STEVENS,M.A.HANSON,F.XU
JRNL TITL STRUCTURAL INSIGHT INTO APELIN RECEPTOR-G PROTEIN
JRNL TITL 2 STOICHIOMETRY.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 29 688 2022
JRNL REFN ESSN 1545-9985
JRNL PMID 35817871
JRNL DOI 10.1038/S41594-022-00797-5
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 13292
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.253
REMARK 3 R VALUE (WORKING SET) : 0.252
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 645
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 7
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.79
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2381
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2100
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2273
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE : 0.2170
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.54
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 108
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2686
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 129.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.44250
REMARK 3 B22 (A**2) : -6.50000
REMARK 3 B33 (A**2) : 6.94250
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -8.16380
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.697
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.335
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.755
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.344
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2819 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3859 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 878 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 39 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 418 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2819 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 368 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3076 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.83
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.42
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.96
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|31 - A|336 A|1102 - A|1103 }
REMARK 3 ORIGIN FOR THE GROUP (A): -39.4374 6.7962 36.7906
REMARK 3 T TENSOR
REMARK 3 T11: 0.1409 T22: 0.0582
REMARK 3 T33: -0.2064 T12: 0.0842
REMARK 3 T13: 0.2099 T23: -0.0888
REMARK 3 L TENSOR
REMARK 3 L11: 0.8595 L22: 1.7378
REMARK 3 L33: 2.4672 L12: 0.3694
REMARK 3 L13: -1.4760 L23: 0.5921
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: -0.3183 S13: 0.1050
REMARK 3 S21: 0.1195 S22: 0.0486 S23: -0.2030
REMARK 3 S31: -0.0751 S32: 0.1427 S33: -0.0442
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|1001 - A|1101 }
REMARK 3 ORIGIN FOR THE GROUP (A): -44.1008 -16.9781 -0.7842
REMARK 3 T TENSOR
REMARK 3 T11: 0.2429 T22: 0.0153
REMARK 3 T33: -0.2337 T12: 0.0515
REMARK 3 T13: 0.1633 T23: -0.1007
REMARK 3 L TENSOR
REMARK 3 L11: 0.4896 L22: 1.4280
REMARK 3 L33: 1.5381 L12: 0.5554
REMARK 3 L13: -0.8793 L23: 1.0361
REMARK 3 S TENSOR
REMARK 3 S11: 0.0120 S12: -0.0196 S13: -0.0167
REMARK 3 S21: 0.0081 S22: -0.0069 S23: 0.0370
REMARK 3 S31: -0.0158 S32: -0.0324 S33: -0.0051
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7SUS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-22.
REMARK 100 THE DEPOSITION ID IS D_1000261106.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUN-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13301
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 42.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5VBL, 1IRO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.1, 26% PEG500 DME, 125
REMARK 280 MM MGCL2, 100 MM NACL, LIPIDIC CUBIC PHASE, TEMPERATURE 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 81.50500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.28000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 81.50500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.28000
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 300 REMARK: THE AUTHORS STATE THAT THE BIOLOGICAL OLIGOMERIC STATE IS
REMARK 300 UNKNOWN.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -17
REMARK 465 LYS A -16
REMARK 465 THR A -15
REMARK 465 ILE A -14
REMARK 465 ILE A -13
REMARK 465 ALA A -12
REMARK 465 LEU A -11
REMARK 465 SER A -10
REMARK 465 TYR A -9
REMARK 465 ILE A -8
REMARK 465 PHE A -7
REMARK 465 CYS A -6
REMARK 465 LEU A -5
REMARK 465 VAL A -4
REMARK 465 PHE A -3
REMARK 465 ALA A -2
REMARK 465 ASP A -1
REMARK 465 TYR A 0
REMARK 465 LYS A 1
REMARK 465 ASP A 2
REMARK 465 ASP A 3
REMARK 465 ASP A 4
REMARK 465 ASP A 5
REMARK 465 LYS A 6
REMARK 465 PHE A 7
REMARK 465 ASP A 8
REMARK 465 ASN A 9
REMARK 465 TYR A 10
REMARK 465 TYR A 11
REMARK 465 GLY A 12
REMARK 465 ALA A 13
REMARK 465 ASP A 14
REMARK 465 ASN A 15
REMARK 465 GLN A 16
REMARK 465 SER A 17
REMARK 465 GLU A 18
REMARK 465 CYS A 19
REMARK 465 GLU A 20
REMARK 465 TYR A 21
REMARK 465 THR A 22
REMARK 465 ASP A 23
REMARK 465 TRP A 24
REMARK 465 LYS A 25
REMARK 465 SER A 26
REMARK 465 SER A 27
REMARK 465 GLY A 28
REMARK 465 ALA A 29
REMARK 465 LEU A 30
REMARK 465 GLY A 337
REMARK 465 PRO A 338
REMARK 465 HIS A 339
REMARK 465 HIS A 340
REMARK 465 HIS A 341
REMARK 465 HIS A 342
REMARK 465 HIS A 343
REMARK 465 HIS A 344
REMARK 465 HIS A 345
REMARK 465 HIS A 346
REMARK 465 HIS A 347
REMARK 465 HIS A 348
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 ILE A 31 CG1 CG2 CD1
REMARK 470 ILE A 34 CG1 CG2 CD1
REMARK 470 ARG A 55 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 59 CG CD OE1 OE2
REMARK 470 LYS A 60 CG CD CE NZ
REMARK 470 LEU A 76 CG CD1 CD2
REMARK 470 ARG A 139 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 141 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 175 CG OD1 ND2
REMARK 470 THR A 176 OG1 CG2
REMARK 470 ASN A 177 CG OD1 ND2
REMARK 470 LYS A 178 CG CD CE NZ
REMARK 470 GLN A 180 CG CD OE1 NE2
REMARK 470 VAL A 191 CG1 CG2
REMARK 470 LEU A 218 CG CD1 CD2
REMARK 470 ARG A 243 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 273 CG CD1 CD2
REMARK 470 MET A 323 CG SD CE
REMARK 470 VAL A 333 CG1 CG2
REMARK 470 GLN A 336 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 92 76.63 59.42
REMARK 500 TYR A 93 74.86 58.93
REMARK 500 ARG A 133 81.47 62.01
REMARK 500 CYS A 174 -35.72 -141.41
REMARK 500 THR A 176 -59.04 67.85
REMARK 500 THR A 190 -146.04 -84.02
REMARK 500 PHE A 210 -55.14 -141.45
REMARK 500 ASP A1019 73.55 -150.79
REMARK 500 ARG A 243 79.18 -69.62
REMARK 500 HIS A 278 78.95 60.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLC A 1103
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1006 SG
REMARK 620 2 CYS A1009 SG 100.2
REMARK 620 3 CYS A1039 SG 126.8 104.1
REMARK 620 4 CYS A1042 SG 108.0 102.9 111.5
REMARK 620 N 1 2 3
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RUBREDOXIN FROM A CLOSTRIDIUM SPECIES IS INSERTED IN THE
REMARK 999 CYTOPLASMIC REGION BETWEEN HELICES 5 AND 6
DBREF 7SUS A 7 229 UNP P35414 APJ_HUMAN 7 229
DBREF 7SUS A 1001 1054 UNP P00268 RUBR_CLOPA 1 54
DBREF 7SUS A 243 330 UNP P35414 APJ_HUMAN 243 330
SEQADV 7SUS MET A -17 UNP P35414 INITIATING METHIONINE
SEQADV 7SUS LYS A -16 UNP P35414 EXPRESSION TAG
SEQADV 7SUS THR A -15 UNP P35414 EXPRESSION TAG
SEQADV 7SUS ILE A -14 UNP P35414 EXPRESSION TAG
SEQADV 7SUS ILE A -13 UNP P35414 EXPRESSION TAG
SEQADV 7SUS ALA A -12 UNP P35414 EXPRESSION TAG
SEQADV 7SUS LEU A -11 UNP P35414 EXPRESSION TAG
SEQADV 7SUS SER A -10 UNP P35414 EXPRESSION TAG
SEQADV 7SUS TYR A -9 UNP P35414 EXPRESSION TAG
SEQADV 7SUS ILE A -8 UNP P35414 EXPRESSION TAG
SEQADV 7SUS PHE A -7 UNP P35414 EXPRESSION TAG
SEQADV 7SUS CYS A -6 UNP P35414 EXPRESSION TAG
SEQADV 7SUS LEU A -5 UNP P35414 EXPRESSION TAG
SEQADV 7SUS VAL A -4 UNP P35414 EXPRESSION TAG
SEQADV 7SUS PHE A -3 UNP P35414 EXPRESSION TAG
SEQADV 7SUS ALA A -2 UNP P35414 EXPRESSION TAG
SEQADV 7SUS ASP A -1 UNP P35414 EXPRESSION TAG
SEQADV 7SUS TYR A 0 UNP P35414 EXPRESSION TAG
SEQADV 7SUS LYS A 1 UNP P35414 EXPRESSION TAG
SEQADV 7SUS ASP A 2 UNP P35414 EXPRESSION TAG
SEQADV 7SUS ASP A 3 UNP P35414 EXPRESSION TAG
SEQADV 7SUS ASP A 4 UNP P35414 EXPRESSION TAG
SEQADV 7SUS ASP A 5 UNP P35414 EXPRESSION TAG
SEQADV 7SUS LYS A 6 UNP P35414 EXPRESSION TAG
SEQADV 7SUS ALA A 117 UNP P35414 VAL 117 ENGINEERED MUTATION
SEQADV 7SUS CYS A 174 UNP P35414 GLU 174 ENGINEERED MUTATION
SEQADV 7SUS ASN A 177 UNP P35414 THR 177 ENGINEERED MUTATION
SEQADV 7SUS CYS A 217 UNP P35414 MET 217 ENGINEERED MUTATION
SEQADV 7SUS CYS A 250 UNP P35414 ILE 250 ENGINEERED MUTATION
SEQADV 7SUS LEU A 325 UNP P35414 CYS 325 ENGINEERED MUTATION
SEQADV 7SUS MET A 326 UNP P35414 CYS 326 ENGINEERED MUTATION
SEQADV 7SUS LEU A 331 UNP P35414 EXPRESSION TAG
SEQADV 7SUS GLU A 332 UNP P35414 EXPRESSION TAG
SEQADV 7SUS VAL A 333 UNP P35414 EXPRESSION TAG
SEQADV 7SUS LEU A 334 UNP P35414 EXPRESSION TAG
SEQADV 7SUS PHE A 335 UNP P35414 EXPRESSION TAG
SEQADV 7SUS GLN A 336 UNP P35414 EXPRESSION TAG
SEQADV 7SUS GLY A 337 UNP P35414 EXPRESSION TAG
SEQADV 7SUS PRO A 338 UNP P35414 EXPRESSION TAG
SEQADV 7SUS HIS A 339 UNP P35414 EXPRESSION TAG
SEQADV 7SUS HIS A 340 UNP P35414 EXPRESSION TAG
SEQADV 7SUS HIS A 341 UNP P35414 EXPRESSION TAG
SEQADV 7SUS HIS A 342 UNP P35414 EXPRESSION TAG
SEQADV 7SUS HIS A 343 UNP P35414 EXPRESSION TAG
SEQADV 7SUS HIS A 344 UNP P35414 EXPRESSION TAG
SEQADV 7SUS HIS A 345 UNP P35414 EXPRESSION TAG
SEQADV 7SUS HIS A 346 UNP P35414 EXPRESSION TAG
SEQADV 7SUS HIS A 347 UNP P35414 EXPRESSION TAG
SEQADV 7SUS HIS A 348 UNP P35414 EXPRESSION TAG
SEQRES 1 A 407 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU
SEQRES 2 A 407 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LYS PHE ASP
SEQRES 3 A 407 ASN TYR TYR GLY ALA ASP ASN GLN SER GLU CYS GLU TYR
SEQRES 4 A 407 THR ASP TRP LYS SER SER GLY ALA LEU ILE PRO ALA ILE
SEQRES 5 A 407 TYR MET LEU VAL PHE LEU LEU GLY THR THR GLY ASN GLY
SEQRES 6 A 407 LEU VAL LEU TRP THR VAL PHE ARG SER SER ARG GLU LYS
SEQRES 7 A 407 ARG ARG SER ALA ASP ILE PHE ILE ALA SER LEU ALA VAL
SEQRES 8 A 407 ALA ASP LEU THR PHE VAL VAL THR LEU PRO LEU TRP ALA
SEQRES 9 A 407 THR TYR THR TYR ARG ASP TYR ASP TRP PRO PHE GLY THR
SEQRES 10 A 407 PHE PHE CYS LYS LEU SER SER TYR LEU ILE PHE VAL ASN
SEQRES 11 A 407 MET TYR ALA SER ALA PHE CYS LEU THR GLY LEU SER PHE
SEQRES 12 A 407 ASP ARG TYR LEU ALA ILE VAL ARG PRO VAL ALA ASN ALA
SEQRES 13 A 407 ARG LEU ARG LEU ARG VAL SER GLY ALA VAL ALA THR ALA
SEQRES 14 A 407 VAL LEU TRP VAL LEU ALA ALA LEU LEU ALA MET PRO VAL
SEQRES 15 A 407 MET VAL LEU ARG THR THR GLY ASP LEU CYS ASN THR ASN
SEQRES 16 A 407 LYS VAL GLN CYS TYR MET ASP TYR SER MET VAL ALA THR
SEQRES 17 A 407 VAL SER SER GLU TRP ALA TRP GLU VAL GLY LEU GLY VAL
SEQRES 18 A 407 SER SER THR THR VAL GLY PHE VAL VAL PRO PHE THR ILE
SEQRES 19 A 407 CYS LEU THR CYS TYR PHE PHE ILE ALA GLN THR ILE ALA
SEQRES 20 A 407 MET LYS LYS TYR THR CYS THR VAL CYS GLY TYR ILE TYR
SEQRES 21 A 407 ASN PRO GLU ASP GLY ASP PRO ASP ASN GLY VAL ASN PRO
SEQRES 22 A 407 GLY THR ASP PHE LYS ASP ILE PRO ASP ASP TRP VAL CYS
SEQRES 23 A 407 PRO LEU CYS GLY VAL GLY LYS ASP GLN PHE GLU GLU VAL
SEQRES 24 A 407 GLU GLU ARG ARG ARG LEU LEU SER ILE CYS VAL VAL LEU
SEQRES 25 A 407 VAL VAL THR PHE ALA LEU CYS TRP MET PRO TYR HIS LEU
SEQRES 26 A 407 VAL LYS THR LEU TYR MET LEU GLY SER LEU LEU HIS TRP
SEQRES 27 A 407 PRO CYS ASP PHE ASP LEU PHE LEU MET ASN ILE PHE PRO
SEQRES 28 A 407 TYR CYS THR CYS ILE SER TYR VAL ASN SER CYS LEU ASN
SEQRES 29 A 407 PRO PHE LEU TYR ALA PHE PHE ASP PRO ARG PHE ARG GLN
SEQRES 30 A 407 ALA CYS THR SER MET LEU LEU MET GLY GLN SER ARG LEU
SEQRES 31 A 407 GLU VAL LEU PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS
SEQRES 32 A 407 HIS HIS HIS HIS
HET ZN A1101 1
HET 8EH A1102 37
HET OLC A1103 13
HETNAM ZN ZINC ION
HETNAM 8EH (1R,2S)-N-[4-(2,6-DIMETHOXYPHENYL)-5-(6-METHYLPYRIDIN-
HETNAM 2 8EH 2-YL)-1,2,4-TRIAZOL-3-YL]-1-(5-METHYLPYRIMIDIN-2-YL)-
HETNAM 3 8EH 1-OXIDANYL-PROPANE-2-SULFONAMIDE
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 ZN ZN 2+
FORMUL 3 8EH C24 H27 N7 O5 S
FORMUL 4 OLC C21 H40 O4
FORMUL 5 HOH *(H2 O)
HELIX 1 AA1 ILE A 31 SER A 56 1 26
HELIX 2 AA2 ALA A 64 THR A 81 1 18
HELIX 3 AA3 THR A 81 ARG A 91 1 11
HELIX 4 AA4 GLY A 98 VAL A 132 1 35
HELIX 5 AA5 ALA A 136 ARG A 141 1 6
HELIX 6 AA6 ARG A 141 ALA A 161 1 21
HELIX 7 AA7 ALA A 161 LEU A 167 1 7
HELIX 8 AA8 TYR A 185 VAL A 188 5 4
HELIX 9 AA9 SER A 193 PHE A 210 1 18
HELIX 10 AB1 PHE A 210 ALA A 229 1 20
HELIX 11 AB2 GLY A 1045 ASP A 1047 5 3
HELIX 12 AB3 ARG A 244 GLY A 274 1 31
HELIX 13 AB4 PRO A 280 ALA A 310 1 31
HELIX 14 AB5 ASP A 313 PHE A 335 1 23
SHEET 1 AA1 2 ARG A 168 GLY A 171 0
SHEET 2 AA1 2 GLN A 180 MET A 183 -1 O TYR A 182 N THR A 169
SHEET 1 AA2 3 ILE A1012 TYR A1013 0
SHEET 2 AA2 3 TYR A1004 CYS A1006 -1 N TYR A1004 O TYR A1013
SHEET 3 AA2 3 PHE A1049 GLU A1051 -1 O GLU A1050 N THR A1005
SSBOND 1 CYS A 102 CYS A 181 1555 1555 2.03
LINK SG CYS A1006 ZN ZN A1101 1555 1555 2.35
LINK SG CYS A1009 ZN ZN A1101 1555 1555 2.52
LINK SG CYS A1039 ZN ZN A1101 1555 1555 2.29
LINK SG CYS A1042 ZN ZN A1101 1555 1555 2.18
CRYST1 163.010 44.560 79.680 90.00 115.62 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 0.006135 0.000000 0.002942 0.00000
SCALE2 0.000000 0.022442 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013919 0.00000
ATOM 1 N ILE A 31 -23.252 0.679 50.283 1.00199.24 N
ANISOU 1 N ILE A 31 24849 28791 22061 2211 -18 -623 N
ATOM 2 CA ILE A 31 -24.571 1.303 50.238 1.00196.45 C
ANISOU 2 CA ILE A 31 24742 28214 21687 2011 121 -683 C
ATOM 3 C ILE A 31 -24.505 2.839 50.029 1.00199.46 C
ANISOU 3 C ILE A 31 25019 28636 22130 1706 150 -929 C
ATOM 4 O ILE A 31 -25.177 3.304 49.106 1.00196.58 O
ANISOU 4 O ILE A 31 24750 28034 21908 1570 328 -983 O
ATOM 5 CB ILE A 31 -25.442 0.914 51.456 1.00199.97 C
ANISOU 5 CB ILE A 31 25439 28652 21888 2075 70 -583 C
ATOM 6 N PRO A 32 -23.743 3.658 50.815 1.00198.02 N
ANISOU 6 N PRO A 32 24656 28738 21844 1588 -6 -1085 N
ATOM 7 CA PRO A 32 -23.740 5.109 50.544 1.00197.10 C
ANISOU 7 CA PRO A 32 24481 28616 21794 1285 69 -1322 C
ATOM 8 C PRO A 32 -22.933 5.519 49.310 1.00200.29 C
ANISOU 8 C PRO A 32 24678 28991 22433 1200 160 -1436 C
ATOM 9 O PRO A 32 -23.286 6.504 48.660 1.00198.27 O
ANISOU 9 O PRO A 32 24475 28578 22281 986 313 -1575 O
ATOM 10 CB PRO A 32 -23.187 5.717 51.833 1.00201.55 C
ANISOU 10 CB PRO A 32 24934 29498 22149 1186 -119 -1447 C
ATOM 11 CG PRO A 32 -22.336 4.661 52.416 1.00208.59 C
ANISOU 11 CG PRO A 32 25679 30636 22939 1447 -324 -1308 C
ATOM 12 CD PRO A 32 -22.874 3.329 51.969 1.00202.81 C
ANISOU 12 CD PRO A 32 25115 29683 22260 1714 -248 -1058 C
ATOM 13 N ALA A 33 -21.866 4.759 48.982 1.00198.18 N
ANISOU 13 N ALA A 33 24188 28863 22248 1375 79 -1373 N
ATOM 14 CA ALA A 33 -20.993 4.999 47.828 1.00197.88 C
ANISOU 14 CA ALA A 33 23940 28810 22438 1315 166 -1473 C
ATOM 15 C ALA A 33 -21.704 4.729 46.497 1.00198.39 C
ANISOU 15 C ALA A 33 24176 28515 22689 1321 390 -1394 C
ATOM 16 O ALA A 33 -21.358 5.348 45.487 1.00197.20 O
ANISOU 16 O ALA A 33 23948 28269 22711 1173 520 -1522 O
ATOM 17 CB ALA A 33 -19.739 4.145 47.935 1.00201.28 C
ANISOU 17 CB ALA A 33 24092 29488 22896 1534 17 -1405 C
ATOM 18 N ILE A 34 -22.694 3.810 46.501 1.00193.10 N
ANISOU 18 N ILE A 34 23746 27650 21973 1480 442 -1193 N
ATOM 19 CA ILE A 34 -23.492 3.438 45.330 1.00190.09 C
ANISOU 19 CA ILE A 34 23547 26946 21734 1490 642 -1106 C
ATOM 20 C ILE A 34 -24.384 4.594 44.869 1.00191.37 C
ANISOU 20 C ILE A 34 23858 26920 21932 1249 782 -1234 C
ATOM 21 O ILE A 34 -24.450 4.858 43.669 1.00189.47 O
ANISOU 21 O ILE A 34 23637 26497 21856 1168 933 -1273 O
ATOM 22 CB ILE A 34 -24.305 2.152 45.597 1.00192.53 C
ANISOU 22 CB ILE A 34 24066 27128 21957 1706 658 -876 C
ATOM 23 N TYR A 35 -25.045 5.291 45.823 1.00187.56 N
ANISOU 23 N TYR A 35 23487 26484 21294 1141 736 -1297 N
ATOM 24 CA TYR A 35 -25.923 6.441 45.568 1.00185.54 C
ANISOU 24 CA TYR A 35 23380 26065 21053 932 864 -1414 C
ATOM 25 C TYR A 35 -25.159 7.627 44.971 1.00189.13 C
ANISOU 25 C TYR A 35 23694 26547 21620 725 931 -1623 C
ATOM 26 O TYR A 35 -25.698 8.329 44.113 1.00187.05 O
ANISOU 26 O TYR A 35 23545 26073 21453 604 1092 -1681 O
ATOM 27 CB TYR A 35 -26.639 6.881 46.856 1.00187.21 C
ANISOU 27 CB TYR A 35 23718 26346 21065 871 797 -1442 C
ATOM 28 CG TYR A 35 -27.862 6.063 47.208 1.00187.76 C
ANISOU 28 CG TYR A 35 24017 26278 21046 998 824 -1273 C
ATOM 29 CD1 TYR A 35 -29.080 6.282 46.569 1.00187.47 C
ANISOU 29 CD1 TYR A 35 24168 25990 21070 947 983 -1249 C
ATOM 30 CD2 TYR A 35 -27.823 5.118 48.228 1.00189.83 C
ANISOU 30 CD2 TYR A 35 24311 26668 21149 1162 693 -1148 C
ATOM 31 CE1 TYR A 35 -30.214 5.544 46.901 1.00187.26 C
ANISOU 31 CE1 TYR A 35 24336 25850 20964 1042 1018 -1117 C
ATOM 32 CE2 TYR A 35 -28.954 4.380 48.576 1.00189.71 C
ANISOU 32 CE2 TYR A 35 24521 26515 21046 1259 741 -1010 C
ATOM 33 CZ TYR A 35 -30.149 4.599 47.911 1.00194.81 C
ANISOU 33 CZ TYR A 35 25332 26919 21767 1188 907 -1004 C
ATOM 34 OH TYR A 35 -31.269 3.880 48.253 1.00194.86 O
ANISOU 34 OH TYR A 35 25544 26803 21690 1264 964 -889 O
ATOM 35 N MET A 36 -23.908 7.842 45.428 1.00187.50 N
ANISOU 35 N MET A 36 23244 26605 21394 687 811 -1737 N
ATOM 36 CA MET A 36 -23.013 8.914 44.975 1.00188.01 C
ANISOU 36 CA MET A 36 23146 26735 21553 477 872 -1959 C
ATOM 37 C MET A 36 -22.610 8.721 43.508 1.00189.96 C
ANISOU 37 C MET A 36 23343 26813 22019 487 1015 -1954 C
ATOM 38 O MET A 36 -22.454 9.705 42.783 1.00189.12 O
ANISOU 38 O MET A 36 23251 26595 22009 296 1161 -2108 O
ATOM 39 CB MET A 36 -21.763 8.992 45.870 1.00193.47 C
ANISOU 39 CB MET A 36 23559 27790 22161 455 689 -2072 C
ATOM 40 CG MET A 36 -22.064 9.411 47.296 1.00198.39 C
ANISOU 40 CG MET A 36 24231 28592 22556 386 560 -2122 C
ATOM 41 SD MET A 36 -20.767 8.925 48.456 1.00206.33 S
ANISOU 41 SD MET A 36 24927 30053 23416 481 278 -2150 S
ATOM 42 CE MET A 36 -21.626 9.145 49.998 1.00203.52 C
ANISOU 42 CE MET A 36 24766 29785 22776 446 166 -2126 C
ATOM 43 N LEU A 37 -22.458 7.452 43.079 1.00185.50 N
ANISOU 43 N LEU A 37 22744 26214 21523 707 988 -1775 N
ATOM 44 CA LEU A 37 -22.101 7.068 41.712 1.00184.10 C
ANISOU 44 CA LEU A 37 22535 25871 21545 738 1124 -1745 C
ATOM 45 C LEU A 37 -23.275 7.289 40.748 1.00184.16 C
ANISOU 45 C LEU A 37 22811 25552 21611 683 1304 -1690 C
ATOM 46 O LEU A 37 -23.046 7.634 39.587 1.00182.99 O
ANISOU 46 O LEU A 37 22673 25248 21608 592 1452 -1752 O
ATOM 47 CB LEU A 37 -21.647 5.597 41.680 1.00184.91 C
ANISOU 47 CB LEU A 37 22540 26035 21680 1000 1047 -1561 C
ATOM 48 CG LEU A 37 -20.797 5.164 40.482 1.00189.87 C
ANISOU 48 CG LEU A 37 23038 26590 22516 1037 1154 -1563 C
ATOM 49 CD1 LEU A 37 -19.314 5.388 40.747 1.00192.88 C
ANISOU 49 CD1 LEU A 37 23083 27252 22951 1014 1059 -1707 C
ATOM 50 CD2 LEU A 37 -21.035 3.705 40.155 1.00191.80 C
ANISOU 50 CD2 LEU A 37 23358 26724 22793 1282 1175 -1334 C
ATOM 51 N VAL A 38 -24.523 7.087 41.231 1.00178.54 N
ANISOU 51 N VAL A 38 22311 24746 20780 739 1292 -1577 N
ATOM 52 CA VAL A 38 -25.763 7.258 40.458 1.00175.55 C
ANISOU 52 CA VAL A 38 22175 24096 20432 705 1436 -1516 C
ATOM 53 C VAL A 38 -25.961 8.735 40.058 1.00177.87 C
ANISOU 53 C VAL A 38 22540 24287 20757 490 1554 -1686 C
ATOM 54 O VAL A 38 -26.355 9.002 38.922 1.00176.02 O
ANISOU 54 O VAL A 38 22421 23841 20619 442 1698 -1681 O
ATOM 55 CB VAL A 38 -27.003 6.638 41.175 1.00178.49 C
ANISOU 55 CB VAL A 38 22725 24424 20668 818 1390 -1368 C
ATOM 56 CG1 VAL A 38 -28.299 6.910 40.413 1.00176.11 C
ANISOU 56 CG1 VAL A 38 22641 23878 20393 773 1528 -1326 C
ATOM 57 CG2 VAL A 38 -26.826 5.136 41.379 1.00178.72 C
ANISOU 57 CG2 VAL A 38 22727 24501 20676 1032 1322 -1192 C
ATOM 58 N PHE A 39 -25.653 9.681 40.975 1.00174.97 N
ANISOU 58 N PHE A 39 22113 24068 20299 359 1501 -1836 N
ATOM 59 CA PHE A 39 -25.760 11.125 40.731 1.00174.37 C
ANISOU 59 CA PHE A 39 22115 23899 20237 149 1629 -2010 C
ATOM 60 C PHE A 39 -24.767 11.594 39.657 1.00177.61 C
ANISOU 60 C PHE A 39 22429 24256 20800 32 1748 -2138 C
ATOM 61 O PHE A 39 -25.111 12.458 38.847 1.00176.33 O
ANISOU 61 O PHE A 39 22412 23890 20694 -82 1914 -2204 O
ATOM 62 CB PHE A 39 -25.582 11.924 42.039 1.00177.81 C
ANISOU 62 CB PHE A 39 22507 24523 20530 26 1551 -2148 C
ATOM 63 CG PHE A 39 -25.653 13.429 41.888 1.00179.71 C
ANISOU 63 CG PHE A 39 22843 24664 20773 -199 1706 -2336 C
ATOM 64 CD1 PHE A 39 -26.876 14.074 41.745 1.00181.40 C
ANISOU 64 CD1 PHE A 39 23302 24665 20959 -223 1826 -2306 C
ATOM 65 CD2 PHE A 39 -24.497 14.201 41.906 1.00183.81 C
ANISOU 65 CD2 PHE A 39 23211 25307 21322 -385 1742 -2548 C
ATOM 66 CE1 PHE A 39 -26.940 15.462 41.592 1.00182.78 C
ANISOU 66 CE1 PHE A 39 23588 24727 21134 -412 1990 -2470 C
ATOM 67 CE2 PHE A 39 -24.563 15.591 41.762 1.00187.08 C
ANISOU 67 CE2 PHE A 39 23741 25608 21732 -600 1915 -2727 C
ATOM 68 CZ PHE A 39 -25.784 16.212 41.610 1.00183.72 C
ANISOU 68 CZ PHE A 39 23581 24949 21277 -605 2042 -2679 C
ATOM 69 N LEU A 40 -23.547 11.021 39.656 1.00174.83 N
ANISOU 69 N LEU A 40 21834 24081 20510 69 1669 -2170 N
ATOM 70 CA LEU A 40 -22.484 11.337 38.699 1.00175.02 C
ANISOU 70 CA LEU A 40 21732 24081 20688 -39 1779 -2301 C
ATOM 71 C LEU A 40 -22.827 10.805 37.300 1.00175.88 C
ANISOU 71 C LEU A 40 21965 23931 20928 34 1912 -2182 C
ATOM 72 O LEU A 40 -22.606 11.508 36.313 1.00175.18 O
ANISOU 72 O LEU A 40 21944 23680 20936 -101 2080 -2284 O
ATOM 73 CB LEU A 40 -21.143 10.762 39.188 1.00177.43 C
ANISOU 73 CB LEU A 40 21719 24676 21020 10 1640 -2354 C
ATOM 74 CG LEU A 40 -19.883 11.434 38.648 1.00183.93 C
ANISOU 74 CG LEU A 40 22353 25568 21964 -172 1735 -2575 C
ATOM 75 CD1 LEU A 40 -18.920 11.760 39.770 1.00186.88 C
ANISOU 75 CD1 LEU A 40 22461 26291 22255 -255 1587 -2738 C
ATOM 76 CD2 LEU A 40 -19.206 10.569 37.601 1.00186.42 C
ANISOU 76 CD2 LEU A 40 22557 25820 22456 -69 1793 -2511 C
ATOM 77 N LEU A 41 -23.371 9.573 37.224 1.00170.39 N
ANISOU 77 N LEU A 41 21317 23196 20225 238 1847 -1972 N
ATOM 78 CA LEU A 41 -23.763 8.917 35.972 1.00168.13 C
ANISOU 78 CA LEU A 41 21155 22685 20043 310 1962 -1847 C
ATOM 79 C LEU A 41 -25.113 9.413 35.438 1.00168.72 C
ANISOU 79 C LEU A 41 21504 22527 20076 273 2063 -1792 C
ATOM 80 O LEU A 41 -25.376 9.291 34.242 1.00167.13 O
ANISOU 80 O LEU A 41 21420 22128 19956 265 2187 -1746 O
ATOM 81 CB LEU A 41 -23.790 7.386 36.142 1.00168.07 C
ANISOU 81 CB LEU A 41 21094 22730 20033 529 1871 -1656 C
ATOM 82 CG LEU A 41 -22.439 6.679 36.294 1.00174.77 C
ANISOU 82 CG LEU A 41 21680 23763 20964 616 1802 -1669 C
ATOM 83 CD1 LEU A 41 -22.596 5.371 37.039 1.00175.30 C
ANISOU 83 CD1 LEU A 41 21716 23934 20955 848 1672 -1484 C
ATOM 84 CD2 LEU A 41 -21.780 6.436 34.942 1.00177.22 C
ANISOU 84 CD2 LEU A 41 21953 23928 21453 584 1956 -1692 C
ATOM 85 N GLY A 42 -25.947 9.951 36.328 1.00164.05 N
ANISOU 85 N GLY A 42 21007 21969 19355 257 2009 -1796 N
ATOM 86 CA GLY A 42 -27.274 10.462 36.001 1.00161.80 C
ANISOU 86 CA GLY A 42 20957 21498 19021 243 2087 -1745 C
ATOM 87 C GLY A 42 -27.262 11.812 35.315 1.00164.45 C
ANISOU 87 C GLY A 42 21406 21682 19396 83 2242 -1879 C
ATOM 88 O GLY A 42 -27.891 11.974 34.267 1.00162.81 O
ANISOU 88 O GLY A 42 21361 21273 19225 88 2351 -1824 O
ATOM 89 N THR A 43 -26.551 12.792 35.911 1.00161.59 N
ANISOU 89 N THR A 43 20966 21417 19012 -63 2258 -2059 N
ATOM 90 CA THR A 43 -26.424 14.162 35.394 1.00161.37 C
ANISOU 90 CA THR A 43 21058 21248 19010 -234 2430 -2212 C
ATOM 91 C THR A 43 -25.700 14.221 34.046 1.00164.03 C
ANISOU 91 C THR A 43 21400 21443 19479 -300 2570 -2261 C
ATOM 92 O THR A 43 -26.100 14.997 33.176 1.00163.09 O
ANISOU 92 O THR A 43 21480 21108 19379 -361 2727 -2282 O
ATOM 93 CB THR A 43 -25.784 15.097 36.434 1.00171.43 C
ANISOU 93 CB THR A 43 22238 22678 20218 -395 2421 -2407 C
ATOM 94 OG1 THR A 43 -24.605 14.489 36.965 1.00172.59 O
ANISOU 94 OG1 THR A 43 22114 23073 20389 -402 2296 -2469 O
ATOM 95 CG2 THR A 43 -26.740 15.467 37.560 1.00169.86 C
ANISOU 95 CG2 THR A 43 22136 22524 19880 -374 2359 -2382 C
ATOM 96 N THR A 44 -24.646 13.400 33.876 1.00160.31 N
ANISOU 96 N THR A 44 20721 21092 19097 -279 2518 -2273 N
ATOM 97 CA THR A 44 -23.857 13.326 32.641 1.00159.86 C
ANISOU 97 CA THR A 44 20646 20915 19178 -342 2653 -2324 C
ATOM 98 C THR A 44 -24.543 12.457 31.581 1.00160.55 C
ANISOU 98 C THR A 44 20870 20825 19307 -214 2686 -2137 C
ATOM 99 O THR A 44 -24.469 12.774 30.392 1.00159.76 O
ANISOU 99 O THR A 44 20901 20526 19274 -282 2841 -2159 O
ATOM 100 CB THR A 44 -22.421 12.854 32.921 1.00170.02 C
ANISOU 100 CB THR A 44 21636 22413 20552 -373 2596 -2428 C
ATOM 101 OG1 THR A 44 -22.456 11.592 33.588 1.00169.61 O
ANISOU 101 OG1 THR A 44 21439 22532 20474 -183 2412 -2278 O
ATOM 102 CG2 THR A 44 -21.613 13.864 33.732 1.00170.74 C
ANISOU 102 CG2 THR A 44 21591 22673 20609 -555 2601 -2657 C
ATOM 103 N GLY A 45 -25.194 11.379 32.025 1.00155.07 N
ANISOU 103 N GLY A 45 20155 20203 18563 -44 2549 -1964 N
ATOM 104 CA GLY A 45 -25.905 10.436 31.169 1.00152.82 C
ANISOU 104 CA GLY A 45 19985 19781 18297 71 2569 -1790 C
ATOM 105 C GLY A 45 -27.150 11.020 30.538 1.00153.94 C
ANISOU 105 C GLY A 45 20381 19731 18377 64 2644 -1730 C
ATOM 106 O GLY A 45 -27.238 11.094 29.310 1.00152.97 O
ANISOU 106 O GLY A 45 20388 19431 18304 28 2764 -1710 O
ATOM 107 N ASN A 46 -28.121 11.446 31.376 1.00149.00 N
ANISOU 107 N ASN A 46 19827 19146 17639 102 2575 -1701 N
ATOM 108 CA ASN A 46 -29.379 12.053 30.923 1.00147.25 C
ANISOU 108 CA ASN A 46 19824 18772 17352 121 2631 -1641 C
ATOM 109 C ASN A 46 -29.175 13.424 30.274 1.00150.29 C
ANISOU 109 C ASN A 46 20350 18998 17754 -4 2787 -1761 C
ATOM 110 O ASN A 46 -29.994 13.838 29.452 1.00149.15 O
ANISOU 110 O ASN A 46 20398 18691 17582 21 2862 -1700 O
ATOM 111 CB ASN A 46 -30.413 12.111 32.047 1.00147.74 C
ANISOU 111 CB ASN A 46 19907 18924 17302 197 2527 -1587 C
ATOM 112 CG ASN A 46 -31.091 10.789 32.300 1.00169.64 C
ANISOU 112 CG ASN A 46 22647 21768 20039 331 2422 -1433 C
ATOM 113 OD1 ASN A 46 -31.901 10.310 31.497 1.00162.67 O
ANISOU 113 OD1 ASN A 46 21867 20789 19151 387 2447 -1326 O
ATOM 114 ND2 ASN A 46 -30.779 10.170 33.428 1.00162.14 N
ANISOU 114 ND2 ASN A 46 21562 20990 19053 379 2306 -1424 N
ATOM 115 N GLY A 47 -28.076 14.093 30.632 1.00147.20 N
ANISOU 115 N GLY A 47 19864 18662 17403 -136 2840 -1931 N
ATOM 116 CA GLY A 47 -27.677 15.377 30.066 1.00147.42 C
ANISOU 116 CA GLY A 47 20024 18537 17452 -281 3018 -2073 C
ATOM 117 C GLY A 47 -27.240 15.225 28.622 1.00149.84 C
ANISOU 117 C GLY A 47 20417 18671 17844 -322 3147 -2066 C
ATOM 118 O GLY A 47 -27.432 16.137 27.815 1.00149.60 O
ANISOU 118 O GLY A 47 20598 18441 17802 -382 3302 -2103 O
ATOM 119 N LEU A 48 -26.665 14.048 28.290 1.00145.11 N
ANISOU 119 N LEU A 48 19671 18139 17327 -281 3093 -2013 N
ATOM 120 CA LEU A 48 -26.217 13.681 26.948 1.00144.27 C
ANISOU 120 CA LEU A 48 19629 17881 17307 -317 3210 -1998 C
ATOM 121 C LEU A 48 -27.423 13.292 26.086 1.00145.41 C
ANISOU 121 C LEU A 48 19974 17886 17391 -212 3206 -1821 C
ATOM 122 O LEU A 48 -27.532 13.770 24.957 1.00144.94 O
ANISOU 122 O LEU A 48 20108 17630 17332 -262 3340 -1823 O
ATOM 123 CB LEU A 48 -25.212 12.518 27.019 1.00144.72 C
ANISOU 123 CB LEU A 48 19447 18068 17470 -296 3155 -1998 C
ATOM 124 CG LEU A 48 -23.884 12.728 26.300 1.00150.74 C
ANISOU 124 CG LEU A 48 20139 18771 18362 -439 3306 -2149 C
ATOM 125 CD1 LEU A 48 -22.824 13.260 27.253 1.00152.68 C
ANISOU 125 CD1 LEU A 48 20163 19202 18644 -544 3286 -2339 C
ATOM 126 CD2 LEU A 48 -23.399 11.436 25.678 1.00152.99 C
ANISOU 126 CD2 LEU A 48 20324 19055 18749 -375 3307 -2066 C
ATOM 127 N VAL A 49 -28.336 12.446 26.633 1.00139.97 N
ANISOU 127 N VAL A 49 19240 17303 16639 -72 3055 -1676 N
ATOM 128 CA VAL A 49 -29.567 11.963 25.980 1.00138.07 C
ANISOU 128 CA VAL A 49 19147 16984 16329 27 3026 -1515 C
ATOM 129 C VAL A 49 -30.449 13.149 25.550 1.00140.92 C
ANISOU 129 C VAL A 49 19732 17206 16607 29 3093 -1510 C
ATOM 130 O VAL A 49 -30.920 13.176 24.411 1.00140.09 O
ANISOU 130 O VAL A 49 19793 16960 16473 40 3154 -1440 O
ATOM 131 CB VAL A 49 -30.340 10.930 26.859 1.00141.06 C
ANISOU 131 CB VAL A 49 19423 17521 16652 155 2867 -1395 C
ATOM 132 CG1 VAL A 49 -31.635 10.470 26.189 1.00139.76 C
ANISOU 132 CG1 VAL A 49 19395 17296 16412 234 2844 -1254 C
ATOM 133 CG2 VAL A 49 -29.467 9.724 27.199 1.00141.08 C
ANISOU 133 CG2 VAL A 49 19235 17638 16730 180 2817 -1381 C
ATOM 134 N LEU A 50 -30.632 14.136 26.451 1.00137.37 N
ANISOU 134 N LEU A 50 19290 16791 16111 19 3088 -1583 N
ATOM 135 CA LEU A 50 -31.415 15.350 26.202 1.00137.16 C
ANISOU 135 CA LEU A 50 19474 16631 16009 37 3167 -1582 C
ATOM 136 C LEU A 50 -30.771 16.231 25.129 1.00141.16 C
ANISOU 136 C LEU A 50 20158 16932 16545 -70 3356 -1667 C
ATOM 137 O LEU A 50 -31.487 16.849 24.341 1.00140.78 O
ANISOU 137 O LEU A 50 20329 16730 16432 -19 3426 -1604 O
ATOM 138 CB LEU A 50 -31.594 16.147 27.502 1.00137.78 C
ANISOU 138 CB LEU A 50 19513 16793 16044 31 3143 -1659 C
ATOM 139 CG LEU A 50 -33.018 16.232 28.037 1.00141.87 C
ANISOU 139 CG LEU A 50 20082 17352 16470 170 3055 -1549 C
ATOM 140 CD1 LEU A 50 -33.036 16.150 29.548 1.00142.18 C
ANISOU 140 CD1 LEU A 50 19972 17565 16484 170 2958 -1596 C
ATOM 141 CD2 LEU A 50 -33.712 17.499 27.560 1.00144.97 C
ANISOU 141 CD2 LEU A 50 20707 17571 16805 207 3175 -1541 C
ATOM 142 N TRP A 51 -29.425 16.273 25.092 1.00137.99 N
ANISOU 142 N TRP A 51 19661 16531 16238 -214 3441 -1811 N
ATOM 143 CA TRP A 51 -28.656 17.058 24.127 1.00138.56 C
ANISOU 143 CA TRP A 51 19889 16408 16349 -347 3643 -1921 C
ATOM 144 C TRP A 51 -28.676 16.436 22.727 1.00140.83 C
ANISOU 144 C TRP A 51 20289 16563 16655 -335 3693 -1831 C
ATOM 145 O TRP A 51 -28.788 17.174 21.750 1.00140.88 O
ANISOU 145 O TRP A 51 20541 16363 16623 -368 3838 -1834 O
ATOM 146 CB TRP A 51 -27.215 17.272 24.626 1.00138.63 C
ANISOU 146 CB TRP A 51 19724 16492 16456 -516 3716 -2124 C
ATOM 147 CG TRP A 51 -26.412 18.275 23.845 1.00141.02 C
ANISOU 147 CG TRP A 51 20191 16598 16794 -683 3953 -2278 C
ATOM 148 CD1 TRP A 51 -26.757 19.567 23.568 1.00144.77 C
ANISOU 148 CD1 TRP A 51 20930 16881 17194 -722 4114 -2325 C
ATOM 149 CD2 TRP A 51 -25.085 18.096 23.334 1.00141.85 C
ANISOU 149 CD2 TRP A 51 20201 16677 17018 -840 4073 -2421 C
ATOM 150 NE1 TRP A 51 -25.748 20.185 22.866 1.00145.61 N
ANISOU 150 NE1 TRP A 51 21137 16830 17358 -902 4336 -2487 N
ATOM 151 CE2 TRP A 51 -24.706 19.308 22.714 1.00147.13 C
ANISOU 151 CE2 TRP A 51 21101 17127 17673 -984 4313 -2556 C
ATOM 152 CE3 TRP A 51 -24.182 17.018 23.320 1.00143.11 C
ANISOU 152 CE3 TRP A 51 20107 16971 17297 -865 4013 -2447 C
ATOM 153 CZ2 TRP A 51 -23.465 19.472 22.086 1.00147.73 C
ANISOU 153 CZ2 TRP A 51 21158 17121 17854 -1170 4496 -2728 C
ATOM 154 CZ3 TRP A 51 -22.953 17.182 22.698 1.00145.89 C
ANISOU 154 CZ3 TRP A 51 20422 17249 17760 -1035 4185 -2612 C
ATOM 155 CH2 TRP A 51 -22.605 18.396 22.090 1.00147.80 C
ANISOU 155 CH2 TRP A 51 20892 17278 17988 -1194 4424 -2756 C
ATOM 156 N THR A 52 -28.580 15.089 22.633 1.00135.71 N
ANISOU 156 N THR A 52 19483 16024 16057 -290 3585 -1748 N
ATOM 157 CA THR A 52 -28.579 14.336 21.368 1.00134.70 C
ANISOU 157 CA THR A 52 19445 15788 15947 -294 3630 -1665 C
ATOM 158 C THR A 52 -29.881 14.485 20.572 1.00137.12 C
ANISOU 158 C THR A 52 19978 15995 16126 -192 3606 -1515 C
ATOM 159 O THR A 52 -29.828 14.606 19.347 1.00136.99 O
ANISOU 159 O THR A 52 20151 15811 16088 -237 3714 -1494 O
ATOM 160 CB THR A 52 -28.222 12.856 21.588 1.00141.93 C
ANISOU 160 CB THR A 52 20143 16846 16940 -261 3532 -1611 C
ATOM 161 OG1 THR A 52 -29.061 12.304 22.603 1.00140.65 O
ANISOU 161 OG1 THR A 52 19862 16860 16720 -133 3354 -1514 O
ATOM 162 CG2 THR A 52 -26.755 12.647 21.939 1.00141.48 C
ANISOU 162 CG2 THR A 52 19880 16855 17022 -363 3588 -1754 C
ATOM 163 N VAL A 53 -31.038 14.473 21.264 1.00132.35 N
ANISOU 163 N VAL A 53 19351 15503 15435 -59 3465 -1418 N
ATOM 164 CA VAL A 53 -32.368 14.614 20.653 1.00131.49 C
ANISOU 164 CA VAL A 53 19410 15350 15201 58 3414 -1278 C
ATOM 165 C VAL A 53 -32.572 16.062 20.162 1.00135.71 C
ANISOU 165 C VAL A 53 20196 15701 15667 64 3541 -1305 C
ATOM 166 O VAL A 53 -33.045 16.265 19.041 1.00135.51 O
ANISOU 166 O VAL A 53 20376 15551 15562 99 3584 -1226 O
ATOM 167 CB VAL A 53 -33.506 14.125 21.602 1.00134.51 C
ANISOU 167 CB VAL A 53 19664 15918 15525 192 3236 -1182 C
ATOM 168 CG1 VAL A 53 -34.886 14.292 20.966 1.00134.19 C
ANISOU 168 CG1 VAL A 53 19767 15860 15359 314 3179 -1049 C
ATOM 169 CG2 VAL A 53 -33.291 12.672 22.019 1.00133.42 C
ANISOU 169 CG2 VAL A 53 19320 15931 15442 187 3138 -1149 C
ATOM 170 N PHE A 54 -32.186 17.052 20.992 1.00132.54 N
ANISOU 170 N PHE A 54 19790 15281 15288 27 3610 -1419 N
ATOM 171 CA PHE A 54 -32.291 18.482 20.684 1.00133.37 C
ANISOU 171 CA PHE A 54 20144 15198 15333 27 3764 -1462 C
ATOM 172 C PHE A 54 -31.343 18.933 19.564 1.00137.57 C
ANISOU 172 C PHE A 54 20866 15512 15892 -110 3967 -1547 C
ATOM 173 O PHE A 54 -31.671 19.878 18.844 1.00138.08 O
ANISOU 173 O PHE A 54 21208 15385 15872 -74 4090 -1519 O
ATOM 174 CB PHE A 54 -32.095 19.328 21.953 1.00135.81 C
ANISOU 174 CB PHE A 54 20388 15555 15659 -4 3798 -1578 C
ATOM 175 CG PHE A 54 -33.373 19.674 22.683 1.00137.15 C
ANISOU 175 CG PHE A 54 20567 15799 15745 162 3697 -1481 C
ATOM 176 CD1 PHE A 54 -33.991 18.748 23.517 1.00139.06 C
ANISOU 176 CD1 PHE A 54 20591 16257 15990 245 3502 -1409 C
ATOM 177 CD2 PHE A 54 -33.947 20.933 22.556 1.00140.44 C
ANISOU 177 CD2 PHE A 54 21218 16060 16084 238 3813 -1466 C
ATOM 178 CE1 PHE A 54 -35.170 19.071 24.197 1.00139.88 C
ANISOU 178 CE1 PHE A 54 20697 16427 16024 389 3424 -1332 C
ATOM 179 CE2 PHE A 54 -35.124 21.256 23.239 1.00143.20 C
ANISOU 179 CE2 PHE A 54 21564 16477 16369 400 3731 -1379 C
ATOM 180 CZ PHE A 54 -35.728 20.323 24.054 1.00140.07 C
ANISOU 180 CZ PHE A 54 20935 16303 15982 468 3536 -1318 C
ATOM 181 N ARG A 55 -30.182 18.258 19.413 1.00133.55 N
ANISOU 181 N ARG A 55 20216 15028 15499 -258 4010 -1647 N
ATOM 182 CA ARG A 55 -29.187 18.560 18.376 1.00134.10 C
ANISOU 182 CA ARG A 55 20438 14900 15614 -411 4214 -1747 C
ATOM 183 C ARG A 55 -29.651 18.129 16.981 1.00137.09 C
ANISOU 183 C ARG A 55 21013 15154 15921 -368 4226 -1615 C
ATOM 184 O ARG A 55 -29.197 18.701 15.988 1.00137.67 O
ANISOU 184 O ARG A 55 21326 15010 15974 -456 4411 -1662 O
ATOM 185 CB ARG A 55 -27.832 17.917 18.708 1.00134.53 C
ANISOU 185 CB ARG A 55 20245 15045 15826 -567 4248 -1895 C
ATOM 186 N SER A 56 -30.545 17.120 16.912 1.00131.95 N
ANISOU 186 N SER A 56 20269 14642 15222 -247 4039 -1458 N
ATOM 187 CA SER A 56 -31.107 16.580 15.670 1.00131.29 C
ANISOU 187 CA SER A 56 20342 14490 15052 -210 4018 -1328 C
ATOM 188 C SER A 56 -31.984 17.607 14.947 1.00135.44 C
ANISOU 188 C SER A 56 21176 14868 15419 -102 4059 -1236 C
ATOM 189 O SER A 56 -32.584 18.469 15.595 1.00135.32 O
ANISOU 189 O SER A 56 21199 14865 15349 8 4035 -1219 O
ATOM 190 CB SER A 56 -31.906 15.312 15.953 1.00133.46 C
ANISOU 190 CB SER A 56 20426 14974 15308 -118 3812 -1204 C
ATOM 191 OG SER A 56 -31.086 14.298 16.511 1.00141.44 O
ANISOU 191 OG SER A 56 21185 16099 16455 -198 3787 -1268 O
ATOM 192 N SER A 57 -32.049 17.509 13.602 1.00132.08 N
ANISOU 192 N SER A 57 20975 14299 14912 -129 4127 -1174 N
ATOM 193 CA SER A 57 -32.821 18.404 12.734 1.00132.84 C
ANISOU 193 CA SER A 57 21388 14247 14838 -17 4166 -1071 C
ATOM 194 C SER A 57 -34.334 18.328 12.985 1.00135.66 C
ANISOU 194 C SER A 57 21702 14773 15069 202 3954 -904 C
ATOM 195 O SER A 57 -34.835 17.301 13.449 1.00133.94 O
ANISOU 195 O SER A 57 21244 14773 14876 236 3779 -853 O
ATOM 196 CB SER A 57 -32.503 18.133 11.266 1.00137.03 C
ANISOU 196 CB SER A 57 22147 14614 15304 -110 4268 -1044 C
ATOM 197 OG SER A 57 -33.107 19.093 10.414 1.00147.23 O
ANISOU 197 OG SER A 57 23775 15743 16424 -3 4326 -951 O
ATOM 198 N ARG A 58 -35.046 19.432 12.678 1.00132.93 N
ANISOU 198 N ARG A 58 21595 14321 14590 354 3985 -825 N
ATOM 199 CA ARG A 58 -36.496 19.599 12.850 1.00132.61 C
ANISOU 199 CA ARG A 58 21538 14422 14425 586 3807 -670 C
ATOM 200 C ARG A 58 -37.320 18.579 12.050 1.00135.11 C
ANISOU 200 C ARG A 58 21808 14891 14637 631 3632 -539 C
ATOM 201 O ARG A 58 -38.338 18.096 12.549 1.00134.06 O
ANISOU 201 O ARG A 58 21483 14982 14472 750 3443 -460 O
ATOM 202 CB ARG A 58 -36.926 21.036 12.491 1.00134.95 C
ANISOU 202 CB ARG A 58 22145 14530 14599 741 3916 -609 C
ATOM 203 CG ARG A 58 -36.225 22.128 13.302 1.00146.59 C
ANISOU 203 CG ARG A 58 23690 15848 16158 692 4110 -743 C
ATOM 204 CD ARG A 58 -37.098 22.695 14.406 1.00157.23 C
ANISOU 204 CD ARG A 58 24936 17302 17501 870 4034 -703 C
ATOM 205 NE ARG A 58 -38.001 23.734 13.908 1.00167.96 N
ANISOU 205 NE ARG A 58 26565 18543 18708 1100 4069 -568 N
ATOM 206 CZ ARG A 58 -38.750 24.515 14.682 1.00182.98 C
ANISOU 206 CZ ARG A 58 28469 20464 20590 1279 4064 -525 C
ATOM 207 NH1 ARG A 58 -39.540 25.432 14.141 1.00172.14 N
ANISOU 207 NH1 ARG A 58 27352 18975 19077 1508 4104 -390 N
ATOM 208 NH2 ARG A 58 -38.711 24.387 16.003 1.00168.86 N
ANISOU 208 NH2 ARG A 58 26435 18808 18917 1236 4025 -614 N
ATOM 209 N GLU A 59 -36.876 18.255 10.820 1.00131.32 N
ANISOU 209 N GLU A 59 21506 14291 14100 521 3706 -529 N
ATOM 210 CA GLU A 59 -37.544 17.305 9.925 1.00130.57 C
ANISOU 210 CA GLU A 59 21402 14320 13888 522 3568 -424 C
ATOM 211 C GLU A 59 -36.936 15.890 9.969 1.00131.75 C
ANISOU 211 C GLU A 59 21345 14561 14152 329 3554 -492 C
ATOM 212 O GLU A 59 -37.492 14.972 9.360 1.00131.13 O
ANISOU 212 O GLU A 59 21229 14605 13989 304 3446 -422 O
ATOM 213 CB GLU A 59 -37.561 17.849 8.486 1.00133.64 C
ANISOU 213 CB GLU A 59 22148 14520 14109 533 3655 -354 C
ATOM 214 N LYS A 60 -35.812 15.713 10.695 1.00126.45 N
ANISOU 214 N LYS A 60 20539 13837 13668 197 3665 -630 N
ATOM 215 CA LYS A 60 -35.114 14.428 10.818 1.00124.54 C
ANISOU 215 CA LYS A 60 20103 13663 13554 36 3675 -695 C
ATOM 216 C LYS A 60 -35.357 13.706 12.162 1.00125.71 C
ANISOU 216 C LYS A 60 19923 14035 13805 77 3540 -711 C
ATOM 217 O LYS A 60 -34.709 12.691 12.434 1.00124.39 O
ANISOU 217 O LYS A 60 19588 13919 13756 -32 3559 -765 O
ATOM 218 CB LYS A 60 -33.611 14.605 10.543 1.00127.38 C
ANISOU 218 CB LYS A 60 20538 13814 14047 -144 3897 -836 C
ATOM 219 N ARG A 61 -36.303 14.208 12.982 1.00121.13 N
ANISOU 219 N ARG A 61 19263 13583 13177 242 3414 -658 N
ATOM 220 CA ARG A 61 -36.642 13.612 14.279 1.00119.24 C
ANISOU 220 CA ARG A 61 18743 13550 13014 290 3289 -668 C
ATOM 221 C ARG A 61 -37.588 12.419 14.139 1.00120.93 C
ANISOU 221 C ARG A 61 18833 13958 13159 309 3141 -582 C
ATOM 222 O ARG A 61 -38.542 12.476 13.360 1.00121.08 O
ANISOU 222 O ARG A 61 18953 14022 13029 376 3065 -488 O
ATOM 223 CB ARG A 61 -37.237 14.656 15.236 1.00119.88 C
ANISOU 223 CB ARG A 61 18800 13672 13078 441 3241 -661 C
ATOM 224 CG ARG A 61 -36.192 15.472 15.980 1.00130.53 C
ANISOU 224 CG ARG A 61 20147 14906 14543 381 3372 -790 C
ATOM 225 CD ARG A 61 -36.807 16.225 17.141 1.00140.80 C
ANISOU 225 CD ARG A 61 21373 16284 15838 509 3315 -791 C
ATOM 226 NE ARG A 61 -35.832 17.081 17.818 1.00150.46 N
ANISOU 226 NE ARG A 61 22614 17401 17154 433 3452 -926 N
ATOM 227 CZ ARG A 61 -35.677 18.380 17.579 1.00166.59 C
ANISOU 227 CZ ARG A 61 24879 19260 19158 453 3595 -960 C
ATOM 228 NH1 ARG A 61 -34.766 19.078 18.243 1.00154.63 N
ANISOU 228 NH1 ARG A 61 23361 17667 17726 352 3728 -1104 N
ATOM 229 NH2 ARG A 61 -36.433 18.992 16.675 1.00154.71 N
ANISOU 229 NH2 ARG A 61 23607 17653 17524 575 3612 -852 N
ATOM 230 N ARG A 62 -37.324 11.346 14.910 1.00115.26 N
ANISOU 230 N ARG A 62 17895 13358 12540 251 3105 -616 N
ATOM 231 CA ARG A 62 -38.127 10.117 14.929 1.00113.87 C
ANISOU 231 CA ARG A 62 17593 13359 12314 243 2997 -558 C
ATOM 232 C ARG A 62 -39.468 10.346 15.639 1.00116.65 C
ANISOU 232 C ARG A 62 17841 13895 12585 394 2842 -499 C
ATOM 233 O ARG A 62 -39.611 11.315 16.390 1.00116.45 O
ANISOU 233 O ARG A 62 17801 13864 12580 501 2825 -513 O
ATOM 234 CB ARG A 62 -37.362 8.972 15.621 1.00112.75 C
ANISOU 234 CB ARG A 62 17273 13260 12305 154 3031 -611 C
ATOM 235 CG ARG A 62 -36.123 8.486 14.874 1.00122.12 C
ANISOU 235 CG ARG A 62 18530 14292 13579 6 3184 -663 C
ATOM 236 CD ARG A 62 -35.417 7.356 15.604 1.00129.66 C
ANISOU 236 CD ARG A 62 19301 15299 14663 -44 3213 -700 C
ATOM 237 NE ARG A 62 -34.756 7.808 16.831 1.00136.39 N
ANISOU 237 NE ARG A 62 20009 16182 15630 8 3201 -767 N
ATOM 238 CZ ARG A 62 -34.027 7.029 17.626 1.00149.35 C
ANISOU 238 CZ ARG A 62 21482 17878 17387 -2 3213 -801 C
ATOM 239 NH1 ARG A 62 -33.465 7.527 18.719 1.00136.54 N
ANISOU 239 NH1 ARG A 62 19732 16301 15844 42 3187 -865 N
ATOM 240 NH2 ARG A 62 -33.852 5.746 17.332 1.00135.54 N
ANISOU 240 NH2 ARG A 62 19698 16136 15664 -56 3257 -769 N
ATOM 241 N SER A 63 -40.442 9.444 15.407 1.00112.14 N
ANISOU 241 N SER A 63 17196 13486 11924 389 2745 -444 N
ATOM 242 CA SER A 63 -41.771 9.497 16.024 1.00111.57 C
ANISOU 242 CA SER A 63 17001 13612 11779 514 2604 -400 C
ATOM 243 C SER A 63 -41.700 9.202 17.526 1.00113.47 C
ANISOU 243 C SER A 63 17050 13937 12125 543 2579 -446 C
ATOM 244 O SER A 63 -42.470 9.771 18.301 1.00113.14 O
ANISOU 244 O SER A 63 16934 13988 12066 667 2503 -434 O
ATOM 245 CB SER A 63 -42.715 8.514 15.340 1.00115.19 C
ANISOU 245 CB SER A 63 17422 14226 12117 460 2529 -356 C
ATOM 246 OG SER A 63 -42.254 7.177 15.454 1.00122.50 O
ANISOU 246 OG SER A 63 18274 15168 13101 312 2588 -393 O
ATOM 247 N ALA A 64 -40.768 8.315 17.924 1.00108.44 N
ANISOU 247 N ALA A 64 16342 13266 11593 435 2647 -496 N
ATOM 248 CA ALA A 64 -40.538 7.902 19.308 1.00107.08 C
ANISOU 248 CA ALA A 64 16006 13168 11512 453 2629 -535 C
ATOM 249 C ALA A 64 -39.703 8.915 20.106 1.00110.09 C
ANISOU 249 C ALA A 64 16381 13462 11986 496 2666 -596 C
ATOM 250 O ALA A 64 -39.737 8.881 21.338 1.00109.24 O
ANISOU 250 O ALA A 64 16149 13435 11922 540 2625 -623 O
ATOM 251 CB ALA A 64 -39.868 6.536 19.332 1.00107.20 C
ANISOU 251 CB ALA A 64 15962 13179 11588 341 2691 -551 C
ATOM 252 N ASP A 65 -38.969 9.816 19.408 1.00106.60 N
ANISOU 252 N ASP A 65 16083 12857 11565 470 2754 -623 N
ATOM 253 CA ASP A 65 -38.098 10.844 19.998 1.00106.39 C
ANISOU 253 CA ASP A 65 16075 12731 11619 475 2820 -702 C
ATOM 254 C ASP A 65 -38.796 11.790 20.983 1.00109.80 C
ANISOU 254 C ASP A 65 16474 13222 12024 594 2763 -706 C
ATOM 255 O ASP A 65 -38.149 12.248 21.926 1.00109.31 O
ANISOU 255 O ASP A 65 16352 13148 12033 580 2793 -783 O
ATOM 256 CB ASP A 65 -37.371 11.653 18.908 1.00108.96 C
ANISOU 256 CB ASP A 65 16596 12858 11945 416 2945 -730 C
ATOM 257 CG ASP A 65 -36.095 11.025 18.370 1.00118.18 C
ANISOU 257 CG ASP A 65 17769 13926 13208 273 3055 -788 C
ATOM 258 OD1 ASP A 65 -35.486 10.198 19.087 1.00117.93 O
ANISOU 258 OD1 ASP A 65 17569 13967 13270 232 3046 -826 O
ATOM 259 OD2 ASP A 65 -35.673 11.404 17.258 1.00124.74 O
ANISOU 259 OD2 ASP A 65 18775 14600 14020 209 3159 -797 O
ATOM 260 N ILE A 66 -40.101 12.074 20.772 1.00106.25 N
ANISOU 260 N ILE A 66 16056 12844 11471 707 2685 -628 N
ATOM 261 CA ILE A 66 -40.907 12.941 21.645 1.00106.23 C
ANISOU 261 CA ILE A 66 16025 12896 11441 836 2640 -622 C
ATOM 262 C ILE A 66 -41.055 12.317 23.052 1.00108.84 C
ANISOU 262 C ILE A 66 16164 13370 11820 834 2576 -658 C
ATOM 263 O ILE A 66 -41.046 13.044 24.048 1.00108.59 O
ANISOU 263 O ILE A 66 16105 13339 11814 877 2587 -703 O
ATOM 264 CB ILE A 66 -42.265 13.349 20.982 1.00110.15 C
ANISOU 264 CB ILE A 66 16586 13447 11819 973 2570 -526 C
ATOM 265 CG1 ILE A 66 -42.968 14.488 21.760 1.00111.27 C
ANISOU 265 CG1 ILE A 66 16737 13595 11946 1122 2565 -521 C
ATOM 266 CG2 ILE A 66 -43.205 12.153 20.740 1.00110.53 C
ANISOU 266 CG2 ILE A 66 16513 13679 11805 966 2459 -472 C
ATOM 267 CD1 ILE A 66 -43.630 15.547 20.887 1.00120.11 C
ANISOU 267 CD1 ILE A 66 18028 14637 12973 1268 2579 -442 C
ATOM 268 N PHE A 67 -41.136 10.973 23.122 1.00104.30 N
ANISOU 268 N PHE A 67 15478 12903 11250 775 2526 -640 N
ATOM 269 CA PHE A 67 -41.243 10.224 24.374 1.00103.29 C
ANISOU 269 CA PHE A 67 15195 12898 11152 770 2476 -663 C
ATOM 270 C PHE A 67 -39.863 9.967 24.982 1.00106.52 C
ANISOU 270 C PHE A 67 15552 13264 11657 689 2522 -731 C
ATOM 271 O PHE A 67 -39.754 9.880 26.203 1.00105.90 O
ANISOU 271 O PHE A 67 15377 13261 11601 705 2489 -767 O
ATOM 272 CB PHE A 67 -42.014 8.909 24.173 1.00104.62 C
ANISOU 272 CB PHE A 67 15291 13191 11270 746 2423 -613 C
ATOM 273 CG PHE A 67 -43.378 9.072 23.542 1.00106.69 C
ANISOU 273 CG PHE A 67 15569 13535 11432 813 2363 -558 C
ATOM 274 CD1 PHE A 67 -44.455 9.545 24.285 1.00110.14 C
ANISOU 274 CD1 PHE A 67 15938 14075 11835 918 2304 -553 C
ATOM 275 CD2 PHE A 67 -43.589 8.744 22.209 1.00109.13 C
ANISOU 275 CD2 PHE A 67 15954 13832 11679 771 2366 -514 C
ATOM 276 CE1 PHE A 67 -45.714 9.705 23.698 1.00111.78 C
ANISOU 276 CE1 PHE A 67 16132 14383 11955 994 2241 -505 C
ATOM 277 CE2 PHE A 67 -44.850 8.897 21.625 1.00112.71 C
ANISOU 277 CE2 PHE A 67 16403 14394 12028 838 2293 -465 C
ATOM 278 CZ PHE A 67 -45.904 9.375 22.373 1.00111.22 C
ANISOU 278 CZ PHE A 67 16124 14319 11813 955 2227 -460 C
ATOM 279 N ILE A 68 -38.814 9.859 24.132 1.00103.01 N
ANISOU 279 N ILE A 68 15168 12706 11263 605 2600 -753 N
ATOM 280 CA ILE A 68 -37.417 9.652 24.540 1.00102.72 C
ANISOU 280 CA ILE A 68 15067 12635 11326 531 2649 -824 C
ATOM 281 C ILE A 68 -36.901 10.909 25.264 1.00106.95 C
ANISOU 281 C ILE A 68 15610 13133 11894 532 2679 -913 C
ATOM 282 O ILE A 68 -36.266 10.790 26.315 1.00106.53 O
ANISOU 282 O ILE A 68 15440 13152 11885 513 2655 -972 O
ATOM 283 CB ILE A 68 -36.527 9.220 23.328 1.00105.92 C
ANISOU 283 CB ILE A 68 15539 12924 11782 437 2742 -829 C
ATOM 284 CG1 ILE A 68 -36.907 7.799 22.843 1.00105.87 C
ANISOU 284 CG1 ILE A 68 15509 12966 11751 415 2728 -755 C
ATOM 285 CG2 ILE A 68 -35.021 9.300 23.653 1.00106.99 C
ANISOU 285 CG2 ILE A 68 15603 13016 12033 366 2808 -922 C
ATOM 286 CD1 ILE A 68 -36.580 7.487 21.362 1.00113.50 C
ANISOU 286 CD1 ILE A 68 16598 13811 12716 330 2818 -735 C
ATOM 287 N ALA A 69 -37.207 12.104 24.712 1.00104.00 N
ANISOU 287 N ALA A 69 15382 12650 11485 555 2736 -922 N
ATOM 288 CA ALA A 69 -36.825 13.400 25.278 1.00104.54 C
ANISOU 288 CA ALA A 69 15498 12654 11568 545 2799 -1011 C
ATOM 289 C ALA A 69 -37.537 13.658 26.609 1.00108.30 C
ANISOU 289 C ALA A 69 15894 13245 12011 616 2727 -1017 C
ATOM 290 O ALA A 69 -36.907 14.151 27.544 1.00108.36 O
ANISOU 290 O ALA A 69 15850 13272 12049 567 2749 -1111 O
ATOM 291 CB ALA A 69 -37.130 14.517 24.291 1.00106.05 C
ANISOU 291 CB ALA A 69 15898 12683 11712 575 2892 -995 C
ATOM 292 N SER A 70 -38.838 13.300 26.698 1.00104.31 N
ANISOU 292 N SER A 70 15370 12824 11439 719 2645 -927 N
ATOM 293 CA SER A 70 -39.660 13.454 27.902 1.00103.98 C
ANISOU 293 CA SER A 70 15257 12888 11364 788 2584 -928 C
ATOM 294 C SER A 70 -39.217 12.499 29.018 1.00107.20 C
ANISOU 294 C SER A 70 15511 13425 11796 743 2517 -957 C
ATOM 295 O SER A 70 -39.312 12.856 30.193 1.00106.99 O
ANISOU 295 O SER A 70 15438 13457 11757 751 2498 -1005 O
ATOM 296 CB SER A 70 -41.135 13.253 27.575 1.00107.34 C
ANISOU 296 CB SER A 70 15689 13376 11720 900 2524 -833 C
ATOM 297 OG SER A 70 -41.594 14.223 26.648 1.00116.76 O
ANISOU 297 OG SER A 70 17025 14462 12874 974 2573 -794 O
ATOM 298 N LEU A 71 -38.723 11.297 28.644 1.00103.22 N
ANISOU 298 N LEU A 71 14942 12957 11319 700 2490 -926 N
ATOM 299 CA LEU A 71 -38.206 10.280 29.567 1.00102.76 C
ANISOU 299 CA LEU A 71 14756 13007 11280 678 2435 -935 C
ATOM 300 C LEU A 71 -36.882 10.770 30.168 1.00107.38 C
ANISOU 300 C LEU A 71 15288 13591 11922 610 2457 -1036 C
ATOM 301 O LEU A 71 -36.615 10.522 31.345 1.00107.15 O
ANISOU 301 O LEU A 71 15166 13669 11879 612 2399 -1067 O
ATOM 302 CB LEU A 71 -38.002 8.944 28.827 1.00102.28 C
ANISOU 302 CB LEU A 71 14670 12952 11238 657 2434 -870 C
ATOM 303 CG LEU A 71 -37.671 7.721 29.679 1.00106.78 C
ANISOU 303 CG LEU A 71 15135 13624 11811 667 2387 -847 C
ATOM 304 CD1 LEU A 71 -38.669 6.608 29.441 1.00106.43 C
ANISOU 304 CD1 LEU A 71 15104 13624 11712 692 2374 -766 C
ATOM 305 CD2 LEU A 71 -36.265 7.232 29.400 1.00109.48 C
ANISOU 305 CD2 LEU A 71 15423 13936 12237 621 2422 -870 C
ATOM 306 N ALA A 72 -36.068 11.475 29.353 1.00104.60 N
ANISOU 306 N ALA A 72 14998 13122 11622 543 2545 -1095 N
ATOM 307 CA ALA A 72 -34.782 12.047 29.753 1.00105.34 C
ANISOU 307 CA ALA A 72 15039 13213 11773 452 2588 -1215 C
ATOM 308 C ALA A 72 -34.975 13.186 30.758 1.00110.10 C
ANISOU 308 C ALA A 72 15663 13837 12335 438 2598 -1298 C
ATOM 309 O ALA A 72 -34.181 13.300 31.690 1.00110.27 O
ANISOU 309 O ALA A 72 15580 13950 12366 378 2572 -1388 O
ATOM 310 CB ALA A 72 -34.024 12.541 28.531 1.00106.47 C
ANISOU 310 CB ALA A 72 15271 13206 11977 373 2706 -1262 C
ATOM 311 N VAL A 73 -36.038 14.007 30.580 1.00106.91 N
ANISOU 311 N VAL A 73 15389 13353 11878 496 2638 -1267 N
ATOM 312 CA VAL A 73 -36.397 15.125 31.465 1.00107.57 C
ANISOU 312 CA VAL A 73 15525 13428 11919 493 2675 -1335 C
ATOM 313 C VAL A 73 -36.844 14.561 32.825 1.00111.66 C
ANISOU 313 C VAL A 73 15931 14106 12389 528 2566 -1322 C
ATOM 314 O VAL A 73 -36.408 15.058 33.867 1.00111.99 O
ANISOU 314 O VAL A 73 15935 14206 12411 464 2568 -1418 O
ATOM 315 CB VAL A 73 -37.462 16.065 30.818 1.00111.69 C
ANISOU 315 CB VAL A 73 16219 13815 12402 579 2753 -1283 C
ATOM 316 CG1 VAL A 73 -38.015 17.081 31.819 1.00112.22 C
ANISOU 316 CG1 VAL A 73 16338 13873 12425 600 2799 -1335 C
ATOM 317 CG2 VAL A 73 -36.896 16.783 29.597 1.00112.05 C
ANISOU 317 CG2 VAL A 73 16410 13685 12477 534 2880 -1310 C
ATOM 318 N ALA A 74 -37.682 13.501 32.801 1.00107.65 N
ANISOU 318 N ALA A 74 15379 13670 11856 616 2481 -1212 N
ATOM 319 CA ALA A 74 -38.190 12.813 33.990 1.00107.38 C
ANISOU 319 CA ALA A 74 15261 13771 11768 654 2390 -1187 C
ATOM 320 C ALA A 74 -37.053 12.162 34.784 1.00111.93 C
ANISOU 320 C ALA A 74 15715 14461 12351 597 2323 -1233 C
ATOM 321 O ALA A 74 -37.012 12.305 36.005 1.00111.99 O
ANISOU 321 O ALA A 74 15684 14561 12307 580 2280 -1280 O
ATOM 322 CB ALA A 74 -39.224 11.770 33.593 1.00107.25 C
ANISOU 322 CB ALA A 74 15234 13789 11727 736 2341 -1073 C
ATOM 323 N ASP A 75 -36.114 11.488 34.092 1.00108.74 N
ANISOU 323 N ASP A 75 15254 14054 12010 572 2318 -1220 N
ATOM 324 CA ASP A 75 -34.966 10.841 34.727 1.00109.31 C
ANISOU 324 CA ASP A 75 15193 14243 12098 543 2253 -1253 C
ATOM 325 C ASP A 75 -33.922 11.839 35.239 1.00115.02 C
ANISOU 325 C ASP A 75 15866 15000 12835 437 2275 -1398 C
ATOM 326 O ASP A 75 -33.251 11.540 36.225 1.00115.31 O
ANISOU 326 O ASP A 75 15788 15182 12842 422 2193 -1439 O
ATOM 327 CB ASP A 75 -34.328 9.793 33.801 1.00110.76 C
ANISOU 327 CB ASP A 75 15328 14404 12353 560 2258 -1192 C
ATOM 328 CG ASP A 75 -35.094 8.486 33.707 1.00119.51 C
ANISOU 328 CG ASP A 75 16446 15533 13428 647 2221 -1064 C
ATOM 329 OD1 ASP A 75 -35.456 7.928 34.768 1.00120.00 O
ANISOU 329 OD1 ASP A 75 16478 15697 13421 700 2149 -1030 O
ATOM 330 OD2 ASP A 75 -35.282 7.990 32.577 1.00124.77 O
ANISOU 330 OD2 ASP A 75 17161 16114 14132 652 2272 -1004 O
ATOM 331 N LEU A 76 -33.794 13.018 34.585 1.00112.51 N
ANISOU 331 N LEU A 76 15643 14555 12552 362 2390 -1478 N
ATOM 332 CA LEU A 76 -32.846 14.068 34.982 1.00113.94 C
ANISOU 332 CA LEU A 76 15798 14749 12743 231 2449 -1638 C
ATOM 333 C LEU A 76 -33.247 14.709 36.310 1.00119.21 C
ANISOU 333 C LEU A 76 16479 15496 13319 202 2423 -1702 C
ATOM 334 O LEU A 76 -32.416 14.782 37.215 1.00119.76 O
ANISOU 334 O LEU A 76 16435 15708 13360 123 2369 -1800 O
ATOM 335 CB LEU A 76 -32.697 15.138 33.891 1.00114.28 C
ANISOU 335 CB LEU A 76 15982 14604 12836 160 2610 -1701 C
ATOM 336 N THR A 77 -34.526 15.133 36.436 1.00116.01 N
ANISOU 336 N THR A 77 16203 15010 12864 269 2459 -1646 N
ATOM 337 CA THR A 77 -35.092 15.745 37.648 1.00116.77 C
ANISOU 337 CA THR A 77 16338 15152 12875 249 2459 -1696 C
ATOM 338 C THR A 77 -35.143 14.755 38.821 1.00121.42 C
ANISOU 338 C THR A 77 16817 15924 13394 287 2311 -1656 C
ATOM 339 O THR A 77 -35.137 15.178 39.979 1.00121.76 O
ANISOU 339 O THR A 77 16857 16049 13359 228 2293 -1732 O
ATOM 340 CB THR A 77 -36.452 16.403 37.362 1.00124.70 C
ANISOU 340 CB THR A 77 17500 16017 13864 331 2547 -1638 C
ATOM 341 OG1 THR A 77 -37.260 15.521 36.580 1.00123.20 O
ANISOU 341 OG1 THR A 77 17312 15802 13696 458 2498 -1494 O
ATOM 342 CG2 THR A 77 -36.317 17.746 36.659 1.00124.17 C
ANISOU 342 CG2 THR A 77 17578 15773 13828 276 2716 -1712 C
ATOM 343 N PHE A 78 -35.171 13.442 38.511 1.00117.92 N
ANISOU 343 N PHE A 78 16300 15535 12969 382 2219 -1540 N
ATOM 344 CA PHE A 78 -35.168 12.338 39.473 1.00118.15 C
ANISOU 344 CA PHE A 78 16246 15716 12930 440 2090 -1479 C
ATOM 345 C PHE A 78 -33.789 12.241 40.144 1.00124.28 C
ANISOU 345 C PHE A 78 16882 16650 13688 371 2009 -1566 C
ATOM 346 O PHE A 78 -33.702 11.868 41.313 1.00124.52 O
ANISOU 346 O PHE A 78 16867 16822 13623 384 1911 -1566 O
ATOM 347 CB PHE A 78 -35.502 11.022 38.751 1.00118.87 C
ANISOU 347 CB PHE A 78 16322 15787 13057 550 2056 -1338 C
ATOM 348 CG PHE A 78 -36.127 9.950 39.611 1.00120.23 C
ANISOU 348 CG PHE A 78 16492 16046 13145 635 1976 -1248 C
ATOM 349 CD1 PHE A 78 -37.505 9.887 39.781 1.00122.69 C
ANISOU 349 CD1 PHE A 78 16895 16309 13413 681 2008 -1197 C
ATOM 350 CD2 PHE A 78 -35.341 8.977 40.217 1.00123.05 C
ANISOU 350 CD2 PHE A 78 16759 16528 13466 677 1879 -1212 C
ATOM 351 CE1 PHE A 78 -38.084 8.885 40.566 1.00123.52 C
ANISOU 351 CE1 PHE A 78 17015 16480 13437 743 1958 -1126 C
ATOM 352 CE2 PHE A 78 -35.921 7.975 41.001 1.00125.83 C
ANISOU 352 CE2 PHE A 78 17142 16938 13729 758 1826 -1125 C
ATOM 353 CZ PHE A 78 -37.288 7.936 41.169 1.00123.20 C
ANISOU 353 CZ PHE A 78 16914 16544 13352 780 1873 -1088 C
ATOM 354 N VAL A 79 -32.721 12.588 39.395 1.00122.18 N
ANISOU 354 N VAL A 79 16548 16365 13509 297 2052 -1642 N
ATOM 355 CA VAL A 79 -31.324 12.593 39.849 1.00123.87 C
ANISOU 355 CA VAL A 79 16599 16740 13726 220 1986 -1746 C
ATOM 356 C VAL A 79 -31.045 13.859 40.698 1.00129.98 C
ANISOU 356 C VAL A 79 17385 17570 14432 64 2023 -1917 C
ATOM 357 O VAL A 79 -30.230 13.806 41.621 1.00130.94 O
ANISOU 357 O VAL A 79 17376 17886 14489 8 1924 -1997 O
ATOM 358 CB VAL A 79 -30.344 12.403 38.647 1.00127.88 C
ANISOU 358 CB VAL A 79 17025 17198 14366 197 2038 -1767 C
ATOM 359 CG1 VAL A 79 -28.887 12.638 39.038 1.00129.50 C
ANISOU 359 CG1 VAL A 79 17043 17572 14589 94 1994 -1910 C
ATOM 360 CG2 VAL A 79 -30.501 11.017 38.029 1.00126.67 C
ANISOU 360 CG2 VAL A 79 16847 17021 14261 342 1993 -1605 C
ATOM 361 N VAL A 80 -31.761 14.972 40.415 1.00127.01 N
ANISOU 361 N VAL A 80 17173 17028 14059 1 2167 -1968 N
ATOM 362 CA VAL A 80 -31.650 16.253 41.136 1.00128.48 C
ANISOU 362 CA VAL A 80 17419 17219 14181 -154 2250 -2129 C
ATOM 363 C VAL A 80 -32.124 16.098 42.605 1.00133.82 C
ANISOU 363 C VAL A 80 18095 18031 14718 -148 2152 -2126 C
ATOM 364 O VAL A 80 -31.631 16.806 43.486 1.00134.92 O
ANISOU 364 O VAL A 80 18213 18274 14779 -293 2158 -2271 O
ATOM 365 CB VAL A 80 -32.374 17.413 40.380 1.00132.02 C
ANISOU 365 CB VAL A 80 18068 17422 14670 -186 2449 -2156 C
ATOM 366 CG1 VAL A 80 -32.240 18.748 41.113 1.00133.32 C
ANISOU 366 CG1 VAL A 80 18318 17568 14769 -354 2569 -2328 C
ATOM 367 CG2 VAL A 80 -31.855 17.552 38.951 1.00131.50 C
ANISOU 367 CG2 VAL A 80 18021 17221 14721 -199 2546 -2161 C
ATOM 368 N THR A 81 -33.050 15.150 42.862 1.00129.99 N
ANISOU 368 N THR A 81 17642 17550 14198 6 2070 -1969 N
ATOM 369 CA THR A 81 -33.590 14.870 44.199 1.00130.55 C
ANISOU 369 CA THR A 81 17738 17730 14135 25 1987 -1949 C
ATOM 370 C THR A 81 -32.678 13.954 45.041 1.00136.43 C
ANISOU 370 C THR A 81 18327 18712 14798 46 1804 -1938 C
ATOM 371 O THR A 81 -32.887 13.851 46.253 1.00136.79 O
ANISOU 371 O THR A 81 18394 18871 14710 31 1730 -1950 O
ATOM 372 CB THR A 81 -35.030 14.329 44.114 1.00136.67 C
ANISOU 372 CB THR A 81 18628 18396 14906 164 2006 -1804 C
ATOM 373 OG1 THR A 81 -35.054 13.155 43.301 1.00134.80 O
ANISOU 373 OG1 THR A 81 18336 18146 14735 294 1949 -1668 O
ATOM 374 CG2 THR A 81 -36.022 15.362 43.587 1.00134.62 C
ANISOU 374 CG2 THR A 81 18517 17938 14694 155 2172 -1823 C
ATOM 375 N LEU A 82 -31.671 13.303 44.408 1.00133.96 N
ANISOU 375 N LEU A 82 17864 18473 14562 87 1736 -1914 N
ATOM 376 CA LEU A 82 -30.724 12.394 45.071 1.00135.41 C
ANISOU 376 CA LEU A 82 17882 18885 14683 143 1562 -1888 C
ATOM 377 C LEU A 82 -29.867 13.054 46.182 1.00142.41 C
ANISOU 377 C LEU A 82 18671 19986 15453 -4 1484 -2050 C
ATOM 378 O LEU A 82 -29.793 12.443 47.248 1.00142.89 O
ANISOU 378 O LEU A 82 18698 20215 15379 56 1341 -2003 O
ATOM 379 CB LEU A 82 -29.822 11.659 44.063 1.00135.35 C
ANISOU 379 CB LEU A 82 17731 18892 14803 218 1535 -1838 C
ATOM 380 CG LEU A 82 -29.602 10.161 44.300 1.00140.18 C
ANISOU 380 CG LEU A 82 18266 19608 15387 406 1399 -1678 C
ATOM 381 CD1 LEU A 82 -29.268 9.462 43.009 1.00139.44 C
ANISOU 381 CD1 LEU A 82 18123 19413 15446 492 1450 -1595 C
ATOM 382 CD2 LEU A 82 -28.494 9.902 45.318 1.00144.93 C
ANISOU 382 CD2 LEU A 82 18690 20486 15890 412 1231 -1727 C
ATOM 383 N PRO A 83 -29.230 14.256 46.019 1.00140.82 N
ANISOU 383 N PRO A 83 18433 19791 15281 -200 1577 -2241 N
ATOM 384 CA PRO A 83 -28.436 14.822 47.134 1.00143.27 C
ANISOU 384 CA PRO A 83 18642 20332 15461 -358 1499 -2406 C
ATOM 385 C PRO A 83 -29.233 15.114 48.407 1.00148.55 C
ANISOU 385 C PRO A 83 19450 21035 15958 -402 1478 -2417 C
ATOM 386 O PRO A 83 -28.645 15.196 49.484 1.00150.02 O
ANISOU 386 O PRO A 83 19550 21451 15998 -486 1358 -2505 O
ATOM 387 CB PRO A 83 -27.844 16.106 46.541 1.00145.72 C
ANISOU 387 CB PRO A 83 18943 20574 15850 -574 1664 -2610 C
ATOM 388 CG PRO A 83 -27.924 15.931 45.076 1.00148.45 C
ANISOU 388 CG PRO A 83 19315 20713 16374 -496 1774 -2537 C
ATOM 389 CD PRO A 83 -29.168 15.143 44.840 1.00141.83 C
ANISOU 389 CD PRO A 83 18618 19724 15548 -296 1763 -2324 C
ATOM 390 N LEU A 84 -30.564 15.262 48.282 1.00144.29 N
ANISOU 390 N LEU A 84 19117 20275 15430 -346 1593 -2332 N
ATOM 391 CA LEU A 84 -31.485 15.503 49.394 1.00144.69 C
ANISOU 391 CA LEU A 84 19321 20314 15340 -374 1606 -2331 C
ATOM 392 C LEU A 84 -31.847 14.174 50.075 1.00149.09 C
ANISOU 392 C LEU A 84 19879 20971 15799 -197 1444 -2163 C
ATOM 393 O LEU A 84 -32.024 14.138 51.293 1.00149.75 O
ANISOU 393 O LEU A 84 20016 21168 15715 -234 1373 -2183 O
ATOM 394 CB LEU A 84 -32.762 16.201 48.888 1.00143.27 C
ANISOU 394 CB LEU A 84 19344 19858 15235 -370 1808 -2310 C
ATOM 395 CG LEU A 84 -32.594 17.596 48.282 1.00148.41 C
ANISOU 395 CG LEU A 84 20060 20365 15964 -531 2005 -2463 C
ATOM 396 CD1 LEU A 84 -33.512 17.784 47.093 1.00146.78 C
ANISOU 396 CD1 LEU A 84 19973 19898 15900 -422 2151 -2367 C
ATOM 397 CD2 LEU A 84 -32.832 18.681 49.316 1.00152.37 C
ANISOU 397 CD2 LEU A 84 20681 20868 16347 -711 2106 -2613 C
ATOM 398 N TRP A 85 -31.951 13.090 49.277 1.00145.01 N
ANISOU 398 N TRP A 85 19321 20398 15378 -12 1401 -2001 N
ATOM 399 CA TRP A 85 -32.293 11.732 49.711 1.00144.86 C
ANISOU 399 CA TRP A 85 19322 20431 15286 172 1283 -1828 C
ATOM 400 C TRP A 85 -31.095 10.971 50.308 1.00151.13 C
ANISOU 400 C TRP A 85 19949 21486 15988 236 1083 -1806 C
ATOM 401 O TRP A 85 -31.265 10.277 51.312 1.00151.46 O
ANISOU 401 O TRP A 85 20041 21633 15874 318 973 -1727 O
ATOM 402 CB TRP A 85 -32.943 10.958 48.543 1.00141.58 C
ANISOU 402 CB TRP A 85 18949 19832 15012 321 1354 -1680 C
ATOM 403 CG TRP A 85 -33.000 9.465 48.704 1.00142.40 C
ANISOU 403 CG TRP A 85 19049 19982 15073 508 1254 -1508 C
ATOM 404 CD1 TRP A 85 -32.179 8.549 48.117 1.00145.45 C
ANISOU 404 CD1 TRP A 85 19312 20426 15527 627 1182 -1422 C
ATOM 405 CD2 TRP A 85 -33.941 8.719 49.487 1.00142.03 C
ANISOU 405 CD2 TRP A 85 19148 19908 14907 595 1242 -1404 C
ATOM 406 NE1 TRP A 85 -32.543 7.277 48.493 1.00144.82 N
ANISOU 406 NE1 TRP A 85 19302 20352 15373 789 1130 -1265 N
ATOM 407 CE2 TRP A 85 -33.621 7.351 49.335 1.00146.00 C
ANISOU 407 CE2 TRP A 85 19620 20451 15404 767 1166 -1255 C
ATOM 408 CE3 TRP A 85 -35.022 9.072 50.312 1.00143.17 C
ANISOU 408 CE3 TRP A 85 19454 19992 14952 540 1304 -1427 C
ATOM 409 CZ2 TRP A 85 -34.343 6.337 49.974 1.00145.27 C
ANISOU 409 CZ2 TRP A 85 19667 20331 15200 879 1157 -1131 C
ATOM 410 CZ3 TRP A 85 -35.734 8.066 50.948 1.00144.57 C
ANISOU 410 CZ3 TRP A 85 19754 20151 15024 646 1287 -1312 C
ATOM 411 CH2 TRP A 85 -35.396 6.717 50.775 1.00145.28 C
ANISOU 411 CH2 TRP A 85 19824 20274 15101 809 1218 -1167 C
ATOM 412 N ALA A 86 -29.903 11.088 49.684 1.00149.03 N
ANISOU 412 N ALA A 86 19487 21322 15816 208 1041 -1872 N
ATOM 413 CA ALA A 86 -28.665 10.422 50.111 1.00151.07 C
ANISOU 413 CA ALA A 86 19543 21845 16013 282 852 -1858 C
ATOM 414 C ALA A 86 -28.159 10.911 51.471 1.00157.94 C
ANISOU 414 C ALA A 86 20362 22967 16682 163 723 -1978 C
ATOM 415 O ALA A 86 -27.655 10.104 52.255 1.00159.04 O
ANISOU 415 O ALA A 86 20425 23315 16688 285 541 -1901 O
ATOM 416 CB ALA A 86 -27.584 10.586 49.055 1.00152.08 C
ANISOU 416 CB ALA A 86 19470 22006 16309 252 872 -1929 C
ATOM 417 N THR A 87 -28.295 12.225 51.747 1.00155.48 N
ANISOU 417 N THR A 87 20104 22632 16339 -72 825 -2165 N
ATOM 418 CA THR A 87 -27.897 12.851 53.016 1.00157.90 C
ANISOU 418 CA THR A 87 20387 23161 16447 -235 736 -2310 C
ATOM 419 C THR A 87 -28.856 12.430 54.133 1.00162.28 C
ANISOU 419 C THR A 87 21143 23699 16818 -171 692 -2209 C
ATOM 420 O THR A 87 -28.433 12.260 55.278 1.00163.93 O
ANISOU 420 O THR A 87 21318 24144 16826 -191 532 -2233 O
ATOM 421 CB THR A 87 -27.831 14.381 52.880 1.00166.72 C
ANISOU 421 CB THR A 87 21536 24212 17597 -515 906 -2540 C
ATOM 422 OG1 THR A 87 -29.025 14.857 52.256 1.00164.15 O
ANISOU 422 OG1 THR A 87 21425 23563 17380 -522 1121 -2506 O
ATOM 423 CG2 THR A 87 -26.612 14.849 52.101 1.00166.40 C
ANISOU 423 CG2 THR A 87 21274 24269 17680 -625 922 -2687 C
ATOM 424 N TYR A 88 -30.146 12.257 53.780 1.00157.04 N
ANISOU 424 N TYR A 88 20684 22762 16222 -97 836 -2102 N
ATOM 425 CA TYR A 88 -31.238 11.833 54.659 1.00156.69 C
ANISOU 425 CA TYR A 88 20851 22643 16040 -36 844 -2006 C
ATOM 426 C TYR A 88 -31.018 10.393 55.150 1.00161.55 C
ANISOU 426 C TYR A 88 21452 23385 16545 187 667 -1824 C
ATOM 427 O TYR A 88 -31.316 10.094 56.307 1.00162.22 O
ANISOU 427 O TYR A 88 21655 23553 16430 201 592 -1790 O
ATOM 428 CB TYR A 88 -32.580 11.973 53.909 1.00155.39 C
ANISOU 428 CB TYR A 88 20857 22167 16016 -2 1048 -1945 C
ATOM 429 CG TYR A 88 -33.814 11.598 54.702 1.00156.68 C
ANISOU 429 CG TYR A 88 21235 22227 16069 45 1096 -1864 C
ATOM 430 CD1 TYR A 88 -34.365 12.477 55.629 1.00159.41 C
ANISOU 430 CD1 TYR A 88 21719 22549 16299 -116 1177 -1980 C
ATOM 431 CD2 TYR A 88 -34.480 10.399 54.466 1.00156.23 C
ANISOU 431 CD2 TYR A 88 21253 22073 16033 237 1093 -1685 C
ATOM 432 CE1 TYR A 88 -35.514 12.147 56.347 1.00159.78 C
ANISOU 432 CE1 TYR A 88 21962 22492 16254 -82 1240 -1917 C
ATOM 433 CE2 TYR A 88 -35.636 10.062 55.168 1.00156.76 C
ANISOU 433 CE2 TYR A 88 21517 22039 16006 264 1159 -1628 C
ATOM 434 CZ TYR A 88 -36.147 10.938 56.112 1.00164.91 C
ANISOU 434 CZ TYR A 88 22675 23058 16927 107 1230 -1744 C
ATOM 435 OH TYR A 88 -37.284 10.609 56.809 1.00165.61 O
ANISOU 435 OH TYR A 88 22955 23041 16928 126 1309 -1698 O
ATOM 436 N THR A 89 -30.479 9.518 54.276 1.00157.88 N
ANISOU 436 N THR A 89 20856 22926 16203 360 613 -1707 N
ATOM 437 CA THR A 89 -30.189 8.111 54.579 1.00158.56 C
ANISOU 437 CA THR A 89 20928 23108 16208 596 470 -1522 C
ATOM 438 C THR A 89 -28.889 7.971 55.395 1.00165.73 C
ANISOU 438 C THR A 89 21652 24354 16964 620 242 -1558 C
ATOM 439 O THR A 89 -28.806 7.088 56.252 1.00166.67 O
ANISOU 439 O THR A 89 21829 24591 16907 774 107 -1433 O
ATOM 440 CB THR A 89 -30.192 7.265 53.288 1.00164.82 C
ANISOU 440 CB THR A 89 21673 23751 17200 763 535 -1388 C
ATOM 441 OG1 THR A 89 -31.264 7.685 52.441 1.00161.89 O
ANISOU 441 OG1 THR A 89 21425 23109 16975 695 735 -1402 O
ATOM 442 CG2 THR A 89 -30.324 5.769 53.562 1.00163.66 C
ANISOU 442 CG2 THR A 89 21608 23601 16975 1010 467 -1177 C
ATOM 443 N TYR A 90 -27.887 8.844 55.129 1.00163.72 N
ANISOU 443 N TYR A 90 21180 24258 16770 466 205 -1732 N
ATOM 444 CA TYR A 90 -26.581 8.881 55.804 1.00166.71 C
ANISOU 444 CA TYR A 90 21330 24991 17019 452 -10 -1808 C
ATOM 445 C TYR A 90 -26.726 9.117 57.314 1.00172.74 C
ANISOU 445 C TYR A 90 22199 25933 17500 368 -127 -1854 C
ATOM 446 O TYR A 90 -26.155 8.366 58.107 1.00174.50 O
ANISOU 446 O TYR A 90 22362 26393 17547 518 -335 -1762 O
ATOM 447 CB TYR A 90 -25.667 9.947 55.151 1.00168.55 C
ANISOU 447 CB TYR A 90 21337 25317 17388 243 33 -2027 C
ATOM 448 CG TYR A 90 -24.393 10.259 55.913 1.00173.72 C
ANISOU 448 CG TYR A 90 21745 26361 17902 153 -169 -2167 C
ATOM 449 CD1 TYR A 90 -23.248 9.487 55.743 1.00177.48 C
ANISOU 449 CD1 TYR A 90 21955 27076 18403 331 -347 -2104 C
ATOM 450 CD2 TYR A 90 -24.320 11.355 56.769 1.00176.06 C
ANISOU 450 CD2 TYR A 90 22062 26792 18043 -117 -171 -2373 C
ATOM 451 CE1 TYR A 90 -22.071 9.776 56.433 1.00181.61 C
ANISOU 451 CE1 TYR A 90 22220 27989 18795 251 -545 -2241 C
ATOM 452 CE2 TYR A 90 -23.150 11.651 57.468 1.00180.25 C
ANISOU 452 CE2 TYR A 90 22351 27706 18430 -220 -361 -2518 C
ATOM 453 CZ TYR A 90 -22.027 10.861 57.294 1.00189.42 C
ANISOU 453 CZ TYR A 90 23230 29126 19617 -33 -556 -2453 C
ATOM 454 OH TYR A 90 -20.870 11.154 57.976 1.00193.80 O
ANISOU 454 OH TYR A 90 23518 30089 20029 -133 -756 -2604 O
ATOM 455 N ARG A 91 -27.495 10.155 57.700 1.00168.79 N
ANISOU 455 N ARG A 91 21867 25314 16952 136 13 -1992 N
ATOM 456 CA ARG A 91 -27.747 10.535 59.095 1.00170.42 C
ANISOU 456 CA ARG A 91 22208 25649 16896 9 -54 -2062 C
ATOM 457 C ARG A 91 -28.847 9.675 59.751 1.00173.44 C
ANISOU 457 C ARG A 91 22868 25881 17150 163 -36 -1879 C
ATOM 458 O ARG A 91 -29.210 9.923 60.905 1.00174.25 O
ANISOU 458 O ARG A 91 23127 26047 17033 64 -66 -1922 O
ATOM 459 CB ARG A 91 -28.093 12.035 59.190 1.00170.63 C
ANISOU 459 CB ARG A 91 22306 25588 16938 -310 123 -2294 C
ATOM 460 CG ARG A 91 -26.940 12.968 58.839 1.00182.84 C
ANISOU 460 CG ARG A 91 23603 27322 18545 -513 105 -2512 C
ATOM 461 CD ARG A 91 -27.343 14.424 58.950 1.00192.90 C
ANISOU 461 CD ARG A 91 24993 28474 19825 -824 314 -2733 C
ATOM 462 NE ARG A 91 -26.327 15.312 58.383 1.00202.62 N
ANISOU 462 NE ARG A 91 26012 29821 21155 -1022 355 -2944 N
ATOM 463 CZ ARG A 91 -26.342 16.638 58.486 1.00217.47 C
ANISOU 463 CZ ARG A 91 27951 31650 23026 -1320 530 -3173 C
ATOM 464 NH1 ARG A 91 -27.318 17.249 59.148 1.00204.64 N
ANISOU 464 NH1 ARG A 91 26586 29865 21303 -1447 675 -3216 N
ATOM 465 NH2 ARG A 91 -25.378 17.363 57.937 1.00205.30 N
ANISOU 465 NH2 ARG A 91 26219 30212 21575 -1498 577 -3365 N
ATOM 466 N ASP A 92 -29.350 8.652 59.015 1.00168.04 N
ANISOU 466 N ASP A 92 22250 25001 16598 392 23 -1685 N
ATOM 467 CA ASP A 92 -30.407 7.711 59.404 1.00166.89 C
ANISOU 467 CA ASP A 92 22361 24678 16370 548 77 -1508 C
ATOM 468 C ASP A 92 -31.723 8.435 59.725 1.00169.03 C
ANISOU 468 C ASP A 92 22871 24723 16630 376 278 -1588 C
ATOM 469 O ASP A 92 -32.076 8.623 60.894 1.00169.91 O
ANISOU 469 O ASP A 92 23142 24888 16528 290 254 -1624 O
ATOM 470 CB ASP A 92 -29.959 6.751 60.526 1.00171.29 C
ANISOU 470 CB ASP A 92 22968 25448 16666 718 -133 -1378 C
ATOM 471 CG ASP A 92 -29.079 5.620 60.036 1.00182.24 C
ANISOU 471 CG ASP A 92 24195 26944 18103 991 -270 -1213 C
ATOM 472 OD1 ASP A 92 -29.629 4.617 59.533 1.00181.27 O
ANISOU 472 OD1 ASP A 92 24193 26620 18061 1182 -180 -1039 O
ATOM 473 OD2 ASP A 92 -27.842 5.733 60.164 1.00190.46 O
ANISOU 473 OD2 ASP A 92 24987 28275 19102 1011 -458 -1262 O
ATOM 474 N TYR A 93 -32.428 8.858 58.651 1.00162.79 N
ANISOU 474 N TYR A 93 22098 23682 16071 328 477 -1616 N
ATOM 475 CA TYR A 93 -33.715 9.567 58.649 1.00160.89 C
ANISOU 475 CA TYR A 93 22045 23200 15884 197 694 -1683 C
ATOM 476 C TYR A 93 -33.646 10.904 59.421 1.00165.44 C
ANISOU 476 C TYR A 93 22655 23847 16356 -64 734 -1888 C
ATOM 477 O TYR A 93 -34.132 11.010 60.552 1.00166.06 O
ANISOU 477 O TYR A 93 22905 23943 16245 -139 741 -1915 O
ATOM 478 CB TYR A 93 -34.876 8.656 59.122 1.00161.43 C
ANISOU 478 CB TYR A 93 22351 23113 15873 315 764 -1544 C
ATOM 479 CG TYR A 93 -34.926 7.311 58.424 1.00162.27 C
ANISOU 479 CG TYR A 93 22446 23148 16060 552 743 -1353 C
ATOM 480 CD1 TYR A 93 -35.538 7.169 57.182 1.00161.89 C
ANISOU 480 CD1 TYR A 93 22379 22894 16238 601 889 -1310 C
ATOM 481 CD2 TYR A 93 -34.369 6.178 59.010 1.00164.62 C
ANISOU 481 CD2 TYR A 93 22767 23583 16198 729 586 -1213 C
ATOM 482 CE1 TYR A 93 -35.579 5.937 56.531 1.00161.87 C
ANISOU 482 CE1 TYR A 93 22377 22822 16303 795 888 -1146 C
ATOM 483 CE2 TYR A 93 -34.405 4.940 58.370 1.00164.74 C
ANISOU 483 CE2 TYR A 93 22794 23514 16287 944 595 -1038 C
ATOM 484 CZ TYR A 93 -35.014 4.823 57.131 1.00169.74 C
ANISOU 484 CZ TYR A 93 23407 23938 17147 964 753 -1013 C
ATOM 485 OH TYR A 93 -35.057 3.605 56.497 1.00170.00 O
ANISOU 485 OH TYR A 93 23463 23883 17246 1153 780 -853 O
ATOM 486 N ASP A 94 -33.008 11.914 58.795 1.00161.54 N
ANISOU 486 N ASP A 94 22006 23389 15984 -209 776 -2038 N
ATOM 487 CA ASP A 94 -32.830 13.267 59.333 1.00162.39 C
ANISOU 487 CA ASP A 94 22132 23548 16020 -477 848 -2253 C
ATOM 488 C ASP A 94 -32.876 14.287 58.188 1.00164.08 C
ANISOU 488 C ASP A 94 22288 23593 16462 -585 1034 -2363 C
ATOM 489 O ASP A 94 -32.065 14.206 57.261 1.00163.34 O
ANISOU 489 O ASP A 94 22006 23551 16504 -542 989 -2365 O
ATOM 490 CB ASP A 94 -31.514 13.374 60.128 1.00167.16 C
ANISOU 490 CB ASP A 94 22578 24498 16435 -571 635 -2351 C
ATOM 491 CG ASP A 94 -31.295 14.721 60.787 1.00178.77 C
ANISOU 491 CG ASP A 94 24079 26043 17801 -875 712 -2588 C
ATOM 492 OD1 ASP A 94 -31.849 14.942 61.884 1.00180.21 O
ANISOU 492 OD1 ASP A 94 24448 26226 17796 -977 740 -2626 O
ATOM 493 OD2 ASP A 94 -30.563 15.551 60.208 1.00185.10 O
ANISOU 493 OD2 ASP A 94 24729 26896 18703 -1024 760 -2742 O
ATOM 494 N TRP A 95 -33.845 15.222 58.242 1.00159.27 N
ANISOU 494 N TRP A 95 21850 22770 15895 -711 1253 -2446 N
ATOM 495 CA TRP A 95 -34.057 16.243 57.212 1.00157.60 C
ANISOU 495 CA TRP A 95 21637 22362 15882 -795 1457 -2536 C
ATOM 496 C TRP A 95 -33.662 17.664 57.682 1.00162.14 C
ANISOU 496 C TRP A 95 22246 22971 16390 -1077 1575 -2769 C
ATOM 497 O TRP A 95 -34.472 18.345 58.319 1.00161.97 O
ANISOU 497 O TRP A 95 22412 22824 16305 -1189 1730 -2838 O
ATOM 498 CB TRP A 95 -35.507 16.189 56.695 1.00154.19 C
ANISOU 498 CB TRP A 95 21364 21639 15582 -682 1636 -2434 C
ATOM 499 CG TRP A 95 -35.741 16.980 55.444 1.00153.83 C
ANISOU 499 CG TRP A 95 21309 21391 15750 -692 1815 -2469 C
ATOM 500 CD1 TRP A 95 -36.140 18.281 55.359 1.00157.00 C
ANISOU 500 CD1 TRP A 95 21821 21634 16198 -836 2029 -2599 C
ATOM 501 CD2 TRP A 95 -35.599 16.514 54.095 1.00152.05 C
ANISOU 501 CD2 TRP A 95 20975 21089 15707 -544 1803 -2367 C
ATOM 502 NE1 TRP A 95 -36.255 18.656 54.041 1.00155.13 N
ANISOU 502 NE1 TRP A 95 21556 21229 16156 -775 2144 -2576 N
ATOM 503 CE2 TRP A 95 -35.925 17.592 53.243 1.00155.33 C
ANISOU 503 CE2 TRP A 95 21447 21306 16266 -605 2004 -2439 C
ATOM 504 CE3 TRP A 95 -35.223 15.287 53.522 1.00152.44 C
ANISOU 504 CE3 TRP A 95 20901 21211 15809 -365 1653 -2220 C
ATOM 505 CZ2 TRP A 95 -35.884 17.482 51.848 1.00153.16 C
ANISOU 505 CZ2 TRP A 95 21108 20914 16173 -499 2045 -2370 C
ATOM 506 CZ3 TRP A 95 -35.187 15.178 52.140 1.00152.39 C
ANISOU 506 CZ3 TRP A 95 20827 21085 15990 -274 1704 -2160 C
ATOM 507 CH2 TRP A 95 -35.520 16.264 51.319 1.00152.41 C
ANISOU 507 CH2 TRP A 95 20887 20900 16122 -343 1892 -2234 C
ATOM 508 N PRO A 96 -32.436 18.142 57.357 1.00159.16 N
ANISOU 508 N PRO A 96 21693 22751 16030 -1204 1525 -2903 N
ATOM 509 CA PRO A 96 -32.026 19.483 57.806 1.00160.49 C
ANISOU 509 CA PRO A 96 21902 22953 16125 -1498 1657 -3143 C
ATOM 510 C PRO A 96 -32.239 20.601 56.771 1.00162.36 C
ANISOU 510 C PRO A 96 22204 22937 16551 -1588 1922 -3238 C
ATOM 511 O PRO A 96 -31.705 21.699 56.947 1.00163.51 O
ANISOU 511 O PRO A 96 22364 23108 16656 -1837 2046 -3448 O
ATOM 512 CB PRO A 96 -30.541 19.284 58.129 1.00164.54 C
ANISOU 512 CB PRO A 96 22174 23816 16528 -1591 1440 -3243 C
ATOM 513 CG PRO A 96 -30.100 18.120 57.238 1.00167.82 C
ANISOU 513 CG PRO A 96 22402 24287 17074 -1335 1275 -3067 C
ATOM 514 CD PRO A 96 -31.330 17.476 56.639 1.00160.69 C
ANISOU 514 CD PRO A 96 21642 23110 16301 -1103 1356 -2858 C
ATOM 515 N PHE A 97 -33.023 20.332 55.704 1.00155.71 N
ANISOU 515 N PHE A 97 21411 21851 15901 -1391 2015 -3089 N
ATOM 516 CA PHE A 97 -33.275 21.291 54.624 1.00154.24 C
ANISOU 516 CA PHE A 97 21300 21413 15891 -1428 2254 -3143 C
ATOM 517 C PHE A 97 -34.435 22.253 54.913 1.00156.83 C
ANISOU 517 C PHE A 97 21875 21489 16223 -1487 2509 -3184 C
ATOM 518 O PHE A 97 -34.228 23.468 54.894 1.00157.59 O
ANISOU 518 O PHE A 97 22064 21491 16320 -1682 2711 -3354 O
ATOM 519 CB PHE A 97 -33.461 20.577 53.271 1.00153.83 C
ANISOU 519 CB PHE A 97 21172 21244 16034 -1195 2223 -2971 C
ATOM 520 CG PHE A 97 -32.327 19.657 52.880 1.00155.56 C
ANISOU 520 CG PHE A 97 21153 21679 16275 -1125 2006 -2928 C
ATOM 521 CD1 PHE A 97 -31.167 20.161 52.303 1.00159.68 C
ANISOU 521 CD1 PHE A 97 21538 22278 16856 -1258 2026 -3067 C
ATOM 522 CD2 PHE A 97 -32.425 18.285 53.077 1.00157.02 C
ANISOU 522 CD2 PHE A 97 21257 21978 16425 -925 1800 -2751 C
ATOM 523 CE1 PHE A 97 -30.119 19.309 51.941 1.00160.90 C
ANISOU 523 CE1 PHE A 97 21458 22634 17044 -1184 1835 -3030 C
ATOM 524 CE2 PHE A 97 -31.377 17.433 52.714 1.00160.16 C
ANISOU 524 CE2 PHE A 97 21440 22565 16851 -841 1615 -2703 C
ATOM 525 CZ PHE A 97 -30.232 17.951 52.148 1.00159.27 C
ANISOU 525 CZ PHE A 97 21173 22537 16806 -967 1629 -2842 C
ATOM 526 N GLY A 98 -35.627 21.711 55.169 1.00151.19 N
ANISOU 526 N GLY A 98 21266 20665 15513 -1323 2512 -3036 N
ATOM 527 CA GLY A 98 -36.817 22.505 55.459 1.00150.43 C
ANISOU 527 CA GLY A 98 21388 20337 15434 -1343 2747 -3055 C
ATOM 528 C GLY A 98 -38.136 21.845 55.110 1.00151.11 C
ANISOU 528 C GLY A 98 21531 20267 15617 -1102 2765 -2867 C
ATOM 529 O GLY A 98 -38.166 20.687 54.683 1.00149.25 O
ANISOU 529 O GLY A 98 21182 20102 15424 -925 2593 -2716 O
ATOM 530 N THR A 99 -39.242 22.592 55.293 1.00146.80 N
ANISOU 530 N THR A 99 21161 19509 15108 -1099 2986 -2883 N
ATOM 531 CA THR A 99 -40.609 22.130 55.027 1.00144.66 C
ANISOU 531 CA THR A 99 20943 19091 14931 -891 3036 -2733 C
ATOM 532 C THR A 99 -40.937 22.151 53.528 1.00145.73 C
ANISOU 532 C THR A 99 21027 19081 15263 -709 3084 -2625 C
ATOM 533 O THR A 99 -41.484 21.171 53.018 1.00143.74 O
ANISOU 533 O THR A 99 20699 18836 15079 -523 2981 -2474 O
ATOM 534 CB THR A 99 -41.629 22.911 55.882 1.00153.81 C
ANISOU 534 CB THR A 99 22292 20101 16049 -957 3252 -2800 C
ATOM 535 OG1 THR A 99 -41.131 23.054 57.214 1.00155.34 O
ANISOU 535 OG1 THR A 99 22546 20432 16044 -1169 3219 -2928 O
ATOM 536 CG2 THR A 99 -43.002 22.243 55.919 1.00151.15 C
ANISOU 536 CG2 THR A 99 21982 19676 15772 -768 3270 -2665 C
ATOM 537 N PHE A 100 -40.611 23.265 52.832 1.00141.85 N
ANISOU 537 N PHE A 100 20591 18454 14851 -770 3251 -2706 N
ATOM 538 CA PHE A 100 -40.857 23.440 51.396 1.00139.99 C
ANISOU 538 CA PHE A 100 20337 18070 14783 -612 3313 -2614 C
ATOM 539 C PHE A 100 -40.029 22.475 50.543 1.00141.20 C
ANISOU 539 C PHE A 100 20313 18354 14984 -541 3107 -2534 C
ATOM 540 O PHE A 100 -40.530 21.983 49.530 1.00139.26 O
ANISOU 540 O PHE A 100 20021 18039 14851 -357 3074 -2397 O
ATOM 541 CB PHE A 100 -40.627 24.901 50.967 1.00143.03 C
ANISOU 541 CB PHE A 100 20862 18268 15215 -711 3560 -2731 C
ATOM 542 CG PHE A 100 -41.021 25.217 49.541 1.00143.75 C
ANISOU 542 CG PHE A 100 20981 18177 15461 -534 3652 -2630 C
ATOM 543 CD1 PHE A 100 -42.352 25.426 49.199 1.00146.43 C
ANISOU 543 CD1 PHE A 100 21400 18352 15884 -339 3763 -2520 C
ATOM 544 CD2 PHE A 100 -40.058 25.329 48.545 1.00145.80 C
ANISOU 544 CD2 PHE A 100 21189 18433 15776 -564 3631 -2650 C
ATOM 545 CE1 PHE A 100 -42.716 25.718 47.881 1.00146.75 C
ANISOU 545 CE1 PHE A 100 21468 18242 16047 -165 3832 -2420 C
ATOM 546 CE2 PHE A 100 -40.422 25.623 47.227 1.00147.94 C
ANISOU 546 CE2 PHE A 100 21509 18532 16171 -403 3716 -2554 C
ATOM 547 CZ PHE A 100 -41.748 25.817 46.904 1.00145.61 C
ANISOU 547 CZ PHE A 100 21295 18088 15944 -200 3808 -2435 C
ATOM 548 N PHE A 101 -38.773 22.204 50.955 1.00137.46 N
ANISOU 548 N PHE A 101 19735 18074 14421 -686 2972 -2622 N
ATOM 549 CA PHE A 101 -37.877 21.278 50.258 1.00135.92 C
ANISOU 549 CA PHE A 101 19362 18016 14267 -627 2782 -2558 C
ATOM 550 C PHE A 101 -38.323 19.825 50.422 1.00137.07 C
ANISOU 550 C PHE A 101 19421 18267 14394 -460 2592 -2395 C
ATOM 551 O PHE A 101 -38.109 19.025 49.515 1.00135.34 O
ANISOU 551 O PHE A 101 19096 18067 14259 -336 2493 -2287 O
ATOM 552 CB PHE A 101 -36.415 21.480 50.682 1.00139.32 C
ANISOU 552 CB PHE A 101 19689 18636 14611 -827 2702 -2710 C
ATOM 553 CG PHE A 101 -35.675 22.492 49.837 1.00141.55 C
ANISOU 553 CG PHE A 101 19987 18821 14974 -945 2852 -2832 C
ATOM 554 CD1 PHE A 101 -35.675 23.840 50.178 1.00146.16 C
ANISOU 554 CD1 PHE A 101 20726 19288 15521 -1127 3076 -2996 C
ATOM 555 CD2 PHE A 101 -34.980 22.098 48.700 1.00142.94 C
ANISOU 555 CD2 PHE A 101 20043 19008 15261 -883 2790 -2788 C
ATOM 556 CE1 PHE A 101 -34.994 24.776 49.393 1.00147.82 C
ANISOU 556 CE1 PHE A 101 20977 19389 15800 -1244 3241 -3115 C
ATOM 557 CE2 PHE A 101 -34.299 23.035 47.916 1.00146.47 C
ANISOU 557 CE2 PHE A 101 20524 19351 15778 -1003 2947 -2909 C
ATOM 558 CZ PHE A 101 -34.310 24.367 48.269 1.00146.08 C
ANISOU 558 CZ PHE A 101 20636 19182 15686 -1183 3173 -3072 C
ATOM 559 N CYS A 102 -38.966 19.497 51.563 1.00132.99 N
ANISOU 559 N CYS A 102 18967 17800 13763 -465 2564 -2383 N
ATOM 560 CA CYS A 102 -39.527 18.173 51.857 1.00131.32 C
ANISOU 560 CA CYS A 102 18719 17661 13515 -322 2426 -2240 C
ATOM 561 C CYS A 102 -40.748 17.949 50.956 1.00132.34 C
ANISOU 561 C CYS A 102 18880 17622 13780 -147 2511 -2118 C
ATOM 562 O CYS A 102 -40.938 16.845 50.446 1.00130.66 O
ANISOU 562 O CYS A 102 18592 17445 13608 -13 2406 -1991 O
ATOM 563 CB CYS A 102 -39.878 18.060 53.341 1.00132.68 C
ANISOU 563 CB CYS A 102 18983 17909 13520 -402 2410 -2284 C
ATOM 564 SG CYS A 102 -41.115 16.793 53.746 1.00135.47 S
ANISOU 564 SG CYS A 102 19384 18244 13842 -239 2363 -2132 S
ATOM 565 N LYS A 103 -41.541 19.018 50.731 1.00128.09 N
ANISOU 565 N LYS A 103 18451 16907 13311 -150 2706 -2160 N
ATOM 566 CA LYS A 103 -42.735 19.013 49.885 1.00126.26 C
ANISOU 566 CA LYS A 103 18241 16528 13203 15 2796 -2059 C
ATOM 567 C LYS A 103 -42.389 18.873 48.400 1.00127.70 C
ANISOU 567 C LYS A 103 18345 16667 13510 111 2764 -1985 C
ATOM 568 O LYS A 103 -42.977 18.030 47.725 1.00126.05 O
ANISOU 568 O LYS A 103 18076 16458 13361 252 2702 -1864 O
ATOM 569 CB LYS A 103 -43.576 20.282 50.116 1.00129.64 C
ANISOU 569 CB LYS A 103 18810 16787 13663 -4 3018 -2127 C
ATOM 570 CG LYS A 103 -44.389 20.264 51.400 1.00144.60 C
ANISOU 570 CG LYS A 103 20788 18685 15467 -48 3078 -2165 C
ATOM 571 CD LYS A 103 -45.321 21.466 51.488 1.00155.39 C
ANISOU 571 CD LYS A 103 22284 19864 16892 -30 3315 -2213 C
ATOM 572 CE LYS A 103 -46.286 21.374 52.646 1.00166.58 C
ANISOU 572 CE LYS A 103 23778 21269 18246 -52 3391 -2241 C
ATOM 573 NZ LYS A 103 -47.386 20.407 52.384 1.00174.36 N
ANISOU 573 NZ LYS A 103 24686 22271 19291 113 3339 -2124 N
ATOM 574 N LEU A 104 -41.439 19.695 47.899 1.00123.77 N
ANISOU 574 N LEU A 104 17856 16129 13041 20 2817 -2067 N
ATOM 575 CA LEU A 104 -41.016 19.718 46.495 1.00122.29 C
ANISOU 575 CA LEU A 104 17623 15878 12963 86 2814 -2016 C
ATOM 576 C LEU A 104 -40.281 18.450 46.044 1.00123.83 C
ANISOU 576 C LEU A 104 17669 16211 13169 127 2625 -1939 C
ATOM 577 O LEU A 104 -40.611 17.923 44.980 1.00122.13 O
ANISOU 577 O LEU A 104 17416 15950 13039 251 2597 -1830 O
ATOM 578 CB LEU A 104 -40.181 20.978 46.194 1.00123.49 C
ANISOU 578 CB LEU A 104 17848 15939 13134 -47 2952 -2147 C
ATOM 579 CG LEU A 104 -40.052 21.384 44.721 1.00127.68 C
ANISOU 579 CG LEU A 104 18408 16327 13778 28 3029 -2103 C
ATOM 580 CD1 LEU A 104 -41.244 22.220 44.269 1.00127.96 C
ANISOU 580 CD1 LEU A 104 18585 16164 13869 154 3199 -2050 C
ATOM 581 CD2 LEU A 104 -38.776 22.160 44.487 1.00131.23 C
ANISOU 581 CD2 LEU A 104 18878 16758 14228 -144 3105 -2244 C
ATOM 582 N SER A 105 -39.293 17.969 46.835 1.00120.08 N
ANISOU 582 N SER A 105 17113 15908 12604 27 2500 -1995 N
ATOM 583 CA SER A 105 -38.505 16.769 46.523 1.00118.82 C
ANISOU 583 CA SER A 105 16813 15884 12450 75 2329 -1923 C
ATOM 584 C SER A 105 -39.376 15.515 46.436 1.00120.34 C
ANISOU 584 C SER A 105 16987 16092 12644 227 2251 -1772 C
ATOM 585 O SER A 105 -39.212 14.735 45.499 1.00118.89 O
ANISOU 585 O SER A 105 16735 15906 12533 316 2195 -1679 O
ATOM 586 CB SER A 105 -37.379 16.573 47.534 1.00123.62 C
ANISOU 586 CB SER A 105 17340 16687 12944 -43 2210 -2010 C
ATOM 587 OG SER A 105 -36.523 15.503 47.169 1.00131.95 O
ANISOU 587 OG SER A 105 18253 17867 14017 19 2059 -1941 O
ATOM 588 N SER A 106 -40.318 15.344 47.388 1.00116.25 N
ANISOU 588 N SER A 106 16541 15580 12048 245 2267 -1758 N
ATOM 589 CA SER A 106 -41.256 14.217 47.437 1.00114.71 C
ANISOU 589 CA SER A 106 16348 15393 11842 363 2226 -1640 C
ATOM 590 C SER A 106 -42.229 14.259 46.253 1.00116.16 C
ANISOU 590 C SER A 106 16538 15450 12147 471 2306 -1566 C
ATOM 591 O SER A 106 -42.590 13.206 45.724 1.00114.76 O
ANISOU 591 O SER A 106 16317 15291 11996 560 2255 -1465 O
ATOM 592 CB SER A 106 -42.024 14.221 48.755 1.00119.01 C
ANISOU 592 CB SER A 106 16983 15958 12277 329 2258 -1671 C
ATOM 593 OG SER A 106 -42.936 13.139 48.844 1.00127.27 O
ANISOU 593 OG SER A 106 18042 17008 13309 425 2239 -1575 O
ATOM 594 N TYR A 107 -42.639 15.478 45.840 1.00111.98 N
ANISOU 594 N TYR A 107 16069 14797 11680 462 2436 -1616 N
ATOM 595 CA TYR A 107 -43.541 15.720 44.713 1.00110.61 C
ANISOU 595 CA TYR A 107 15906 14513 11609 575 2509 -1550 C
ATOM 596 C TYR A 107 -42.857 15.354 43.395 1.00112.80 C
ANISOU 596 C TYR A 107 16120 14779 11961 610 2455 -1492 C
ATOM 597 O TYR A 107 -43.442 14.622 42.599 1.00111.48 O
ANISOU 597 O TYR A 107 15913 14609 11837 704 2424 -1397 O
ATOM 598 CB TYR A 107 -44.022 17.185 44.712 1.00112.56 C
ANISOU 598 CB TYR A 107 16253 14625 11889 568 2670 -1616 C
ATOM 599 CG TYR A 107 -44.951 17.561 43.575 1.00113.79 C
ANISOU 599 CG TYR A 107 16425 14673 12137 707 2742 -1542 C
ATOM 600 CD1 TYR A 107 -46.271 17.120 43.552 1.00115.43 C
ANISOU 600 CD1 TYR A 107 16600 14895 12362 818 2749 -1477 C
ATOM 601 CD2 TYR A 107 -44.531 18.415 42.561 1.00114.70 C
ANISOU 601 CD2 TYR A 107 16592 14676 12314 725 2813 -1546 C
ATOM 602 CE1 TYR A 107 -47.137 17.483 42.521 1.00116.07 C
ANISOU 602 CE1 TYR A 107 16676 14907 12517 956 2798 -1409 C
ATOM 603 CE2 TYR A 107 -45.390 18.790 41.528 1.00115.46 C
ANISOU 603 CE2 TYR A 107 16713 14680 12476 870 2870 -1468 C
ATOM 604 CZ TYR A 107 -46.694 18.322 41.514 1.00122.36 C
ANISOU 604 CZ TYR A 107 17532 15595 13363 990 2852 -1397 C
ATOM 605 OH TYR A 107 -47.544 18.683 40.497 1.00123.21 O
ANISOU 605 OH TYR A 107 17644 15643 13525 1143 2889 -1319 O
ATOM 606 N LEU A 108 -41.605 15.823 43.191 1.00109.03 N
ANISOU 606 N LEU A 108 15632 14302 11494 521 2450 -1559 N
ATOM 607 CA LEU A 108 -40.810 15.552 41.989 1.00107.86 C
ANISOU 607 CA LEU A 108 15430 14132 11418 532 2416 -1524 C
ATOM 608 C LEU A 108 -40.458 14.070 41.827 1.00110.06 C
ANISOU 608 C LEU A 108 15609 14518 11691 574 2285 -1438 C
ATOM 609 O LEU A 108 -40.391 13.594 40.694 1.00108.80 O
ANISOU 609 O LEU A 108 15422 14321 11598 627 2273 -1368 O
ATOM 610 CB LEU A 108 -39.547 16.430 41.936 1.00108.80 C
ANISOU 610 CB LEU A 108 15557 14234 11549 405 2460 -1641 C
ATOM 611 CG LEU A 108 -39.765 17.926 41.675 1.00114.25 C
ANISOU 611 CG LEU A 108 16377 14768 12265 367 2630 -1718 C
ATOM 612 CD1 LEU A 108 -38.610 18.744 42.211 1.00115.73 C
ANISOU 612 CD1 LEU A 108 16574 14979 12419 193 2681 -1875 C
ATOM 613 CD2 LEU A 108 -39.980 18.216 40.194 1.00116.23 C
ANISOU 613 CD2 LEU A 108 16681 14878 12602 451 2698 -1652 C
ATOM 614 N ILE A 109 -40.262 13.340 42.950 1.00106.36 N
ANISOU 614 N ILE A 109 15104 14173 11135 554 2198 -1439 N
ATOM 615 CA ILE A 109 -39.966 11.901 42.954 1.00105.41 C
ANISOU 615 CA ILE A 109 14914 14144 10993 609 2092 -1350 C
ATOM 616 C ILE A 109 -41.159 11.117 42.372 1.00107.53 C
ANISOU 616 C ILE A 109 15205 14366 11286 703 2116 -1248 C
ATOM 617 O ILE A 109 -40.958 10.270 41.499 1.00106.38 O
ANISOU 617 O ILE A 109 15019 14214 11185 747 2089 -1174 O
ATOM 618 CB ILE A 109 -39.506 11.408 44.368 1.00109.43 C
ANISOU 618 CB ILE A 109 15408 14790 11381 578 2001 -1373 C
ATOM 619 CG1 ILE A 109 -38.020 11.769 44.616 1.00110.95 C
ANISOU 619 CG1 ILE A 109 15517 15078 11560 495 1936 -1455 C
ATOM 620 CG2 ILE A 109 -39.739 9.895 44.572 1.00109.70 C
ANISOU 620 CG2 ILE A 109 15432 14881 11367 667 1932 -1260 C
ATOM 621 CD1 ILE A 109 -37.573 11.819 46.107 1.00119.71 C
ANISOU 621 CD1 ILE A 109 16623 16333 12529 431 1856 -1519 C
ATOM 622 N PHE A 110 -42.390 11.443 42.819 1.00103.56 N
ANISOU 622 N PHE A 110 14762 13831 10757 725 2177 -1256 N
ATOM 623 CA PHE A 110 -43.619 10.794 42.359 1.00102.36 C
ANISOU 623 CA PHE A 110 14613 13658 10621 797 2207 -1185 C
ATOM 624 C PHE A 110 -44.089 11.266 40.980 1.00104.95 C
ANISOU 624 C PHE A 110 14932 13905 11040 847 2255 -1154 C
ATOM 625 O PHE A 110 -44.606 10.441 40.226 1.00103.80 O
ANISOU 625 O PHE A 110 14757 13770 10914 890 2244 -1086 O
ATOM 626 CB PHE A 110 -44.741 10.905 43.401 1.00104.58 C
ANISOU 626 CB PHE A 110 14941 13951 10842 799 2257 -1215 C
ATOM 627 CG PHE A 110 -44.858 9.671 44.264 1.00106.19 C
ANISOU 627 CG PHE A 110 15161 14230 10955 795 2215 -1182 C
ATOM 628 CD1 PHE A 110 -44.083 9.526 45.409 1.00110.00 C
ANISOU 628 CD1 PHE A 110 15676 14776 11341 748 2159 -1211 C
ATOM 629 CD2 PHE A 110 -45.722 8.639 43.917 1.00107.86 C
ANISOU 629 CD2 PHE A 110 15366 14452 11166 834 2237 -1123 C
ATOM 630 CE1 PHE A 110 -44.177 8.374 46.196 1.00111.14 C
ANISOU 630 CE1 PHE A 110 15864 14978 11388 761 2126 -1167 C
ATOM 631 CE2 PHE A 110 -45.815 7.488 44.706 1.00110.89 C
ANISOU 631 CE2 PHE A 110 15794 14880 11457 828 2224 -1093 C
ATOM 632 CZ PHE A 110 -45.039 7.362 45.837 1.00109.69 C
ANISOU 632 CZ PHE A 110 15693 14777 11209 802 2169 -1107 C
ATOM 633 N VAL A 111 -43.910 12.569 40.642 1.00101.40 N
ANISOU 633 N VAL A 111 14522 13373 10634 838 2315 -1204 N
ATOM 634 CA VAL A 111 -44.281 13.127 39.328 1.00100.70 C
ANISOU 634 CA VAL A 111 14449 13197 10614 900 2362 -1168 C
ATOM 635 C VAL A 111 -43.504 12.377 38.237 1.00103.07 C
ANISOU 635 C VAL A 111 14712 13498 10954 891 2311 -1114 C
ATOM 636 O VAL A 111 -44.111 11.872 37.292 1.00102.14 O
ANISOU 636 O VAL A 111 14577 13377 10856 943 2302 -1045 O
ATOM 637 CB VAL A 111 -44.102 14.676 39.252 1.00105.45 C
ANISOU 637 CB VAL A 111 15135 13688 11243 891 2459 -1233 C
ATOM 638 CG1 VAL A 111 -44.001 15.177 37.810 1.00105.15 C
ANISOU 638 CG1 VAL A 111 15138 13549 11264 942 2497 -1192 C
ATOM 639 CG2 VAL A 111 -45.231 15.395 39.979 1.00105.96 C
ANISOU 639 CG2 VAL A 111 15244 13726 11290 939 2538 -1259 C
ATOM 640 N ASN A 112 -42.176 12.246 38.422 1.00 99.13 N
ANISOU 640 N ASN A 112 14191 13016 10459 818 2276 -1151 N
ATOM 641 CA ASN A 112 -41.282 11.544 37.504 1.00 98.13 C
ANISOU 641 CA ASN A 112 14024 12885 10377 802 2242 -1112 C
ATOM 642 C ASN A 112 -41.462 10.021 37.542 1.00100.43 C
ANISOU 642 C ASN A 112 14265 13251 10643 830 2183 -1034 C
ATOM 643 O ASN A 112 -41.105 9.354 36.571 1.00 99.46 O
ANISOU 643 O ASN A 112 14125 13105 10560 833 2179 -983 O
ATOM 644 CB ASN A 112 -39.825 11.950 37.745 1.00 99.76 C
ANISOU 644 CB ASN A 112 14202 13100 10604 718 2232 -1190 C
ATOM 645 CG ASN A 112 -39.540 13.432 37.583 1.00124.78 C
ANISOU 645 CG ASN A 112 17440 16174 13798 666 2322 -1280 C
ATOM 646 OD1 ASN A 112 -38.730 14.008 38.316 1.00120.23 O
ANISOU 646 OD1 ASN A 112 16850 15631 13203 578 2330 -1379 O
ATOM 647 ND2 ASN A 112 -40.168 14.085 36.609 1.00116.86 N
ANISOU 647 ND2 ASN A 112 16520 15054 12829 714 2398 -1251 N
ATOM 648 N MET A 113 -42.030 9.475 38.645 1.00 96.47 N
ANISOU 648 N MET A 113 13760 12825 10070 843 2157 -1028 N
ATOM 649 CA MET A 113 -42.309 8.040 38.790 1.00 95.58 C
ANISOU 649 CA MET A 113 13633 12766 9918 868 2131 -959 C
ATOM 650 C MET A 113 -43.443 7.652 37.832 1.00 97.85 C
ANISOU 650 C MET A 113 13927 13028 10222 895 2172 -910 C
ATOM 651 O MET A 113 -43.355 6.617 37.167 1.00 96.89 O
ANISOU 651 O MET A 113 13798 12908 10109 893 2175 -854 O
ATOM 652 CB MET A 113 -42.683 7.690 40.243 1.00 98.43 C
ANISOU 652 CB MET A 113 14017 13196 10186 868 2112 -975 C
ATOM 653 CG MET A 113 -42.569 6.209 40.562 1.00102.03 C
ANISOU 653 CG MET A 113 14483 13696 10588 891 2092 -907 C
ATOM 654 SD MET A 113 -43.383 5.743 42.113 1.00106.81 S
ANISOU 654 SD MET A 113 15158 14355 11070 893 2103 -919 S
ATOM 655 CE MET A 113 -45.055 5.506 41.543 1.00102.96 C
ANISOU 655 CE MET A 113 14681 13840 10600 891 2194 -916 C
ATOM 656 N TYR A 114 -44.490 8.501 37.749 1.00 93.82 N
ANISOU 656 N TYR A 114 13428 12501 9717 922 2207 -935 N
ATOM 657 CA TYR A 114 -45.631 8.295 36.859 1.00 93.03 C
ANISOU 657 CA TYR A 114 13312 12409 9626 955 2232 -900 C
ATOM 658 C TYR A 114 -45.256 8.634 35.417 1.00 95.69 C
ANISOU 658 C TYR A 114 13657 12683 10016 963 2233 -868 C
ATOM 659 O TYR A 114 -45.552 7.845 34.519 1.00 94.90 O
ANISOU 659 O TYR A 114 13543 12602 9914 953 2232 -822 O
ATOM 660 CB TYR A 114 -46.857 9.120 37.307 1.00 94.75 C
ANISOU 660 CB TYR A 114 13524 12644 9835 1003 2267 -936 C
ATOM 661 CG TYR A 114 -47.377 8.800 38.693 1.00 96.80 C
ANISOU 661 CG TYR A 114 13786 12955 10037 984 2285 -975 C
ATOM 662 CD1 TYR A 114 -47.692 7.494 39.059 1.00 98.56 C
ANISOU 662 CD1 TYR A 114 14004 13237 10209 950 2288 -957 C
ATOM 663 CD2 TYR A 114 -47.637 9.813 39.612 1.00 98.18 C
ANISOU 663 CD2 TYR A 114 13990 13109 10205 997 2319 -1033 C
ATOM 664 CE1 TYR A 114 -48.183 7.196 40.328 1.00 99.79 C
ANISOU 664 CE1 TYR A 114 14187 13426 10302 929 2319 -994 C
ATOM 665 CE2 TYR A 114 -48.129 9.527 40.884 1.00 99.48 C
ANISOU 665 CE2 TYR A 114 14173 13313 10311 970 2346 -1073 C
ATOM 666 CZ TYR A 114 -48.405 8.216 41.237 1.00106.67 C
ANISOU 666 CZ TYR A 114 15082 14281 11166 938 2343 -1052 C
ATOM 667 OH TYR A 114 -48.897 7.926 42.485 1.00108.14 O
ANISOU 667 OH TYR A 114 15310 14493 11285 908 2381 -1093 O
ATOM 668 N ALA A 115 -44.589 9.796 35.206 1.00 91.81 N
ANISOU 668 N ALA A 115 13205 12114 9566 969 2248 -899 N
ATOM 669 CA ALA A 115 -44.156 10.306 33.898 1.00 91.21 C
ANISOU 669 CA ALA A 115 13169 11953 9534 974 2266 -877 C
ATOM 670 C ALA A 115 -43.289 9.328 33.103 1.00 93.55 C
ANISOU 670 C ALA A 115 13456 12236 9854 920 2253 -841 C
ATOM 671 O ALA A 115 -43.575 9.107 31.927 1.00 92.90 O
ANISOU 671 O ALA A 115 13394 12128 9775 925 2261 -796 O
ATOM 672 CB ALA A 115 -43.443 11.641 34.055 1.00 92.50 C
ANISOU 672 CB ALA A 115 13393 12024 9727 965 2311 -937 C
ATOM 673 N SER A 116 -42.258 8.726 33.744 1.00 89.36 N
ANISOU 673 N SER A 116 12893 11727 9333 875 2234 -858 N
ATOM 674 CA SER A 116 -41.356 7.752 33.113 1.00 88.56 C
ANISOU 674 CA SER A 116 12775 11608 9265 836 2236 -824 C
ATOM 675 C SER A 116 -42.105 6.493 32.667 1.00 91.30 C
ANISOU 675 C SER A 116 13120 11992 9577 835 2244 -760 C
ATOM 676 O SER A 116 -41.782 5.933 31.619 1.00 90.60 O
ANISOU 676 O SER A 116 13050 11860 9514 802 2273 -724 O
ATOM 677 CB SER A 116 -40.203 7.390 34.044 1.00 92.43 C
ANISOU 677 CB SER A 116 13216 12139 9766 817 2204 -851 C
ATOM 678 OG SER A 116 -40.670 6.853 35.271 1.00101.88 O
ANISOU 678 OG SER A 116 14394 13421 10894 844 2169 -843 O
ATOM 679 N ALA A 117 -43.119 6.073 33.449 1.00 87.42 N
ANISOU 679 N ALA A 117 12613 11577 9024 856 2234 -756 N
ATOM 680 CA ALA A 117 -43.969 4.921 33.146 1.00 86.80 C
ANISOU 680 CA ALA A 117 12535 11544 8901 834 2261 -718 C
ATOM 681 C ALA A 117 -44.923 5.261 31.996 1.00 89.94 C
ANISOU 681 C ALA A 117 12933 11950 9289 832 2268 -708 C
ATOM 682 O ALA A 117 -45.158 4.412 31.135 1.00 89.35 O
ANISOU 682 O ALA A 117 12868 11884 9195 783 2296 -678 O
ATOM 683 CB ALA A 117 -44.756 4.509 34.381 1.00 87.79 C
ANISOU 683 CB ALA A 117 12650 11744 8963 846 2263 -736 C
ATOM 684 N PHE A 118 -45.451 6.509 31.973 1.00 86.29 N
ANISOU 684 N PHE A 118 12465 11487 8834 890 2245 -730 N
ATOM 685 CA PHE A 118 -46.356 6.999 30.929 1.00 86.17 C
ANISOU 685 CA PHE A 118 12448 11492 8802 923 2234 -711 C
ATOM 686 C PHE A 118 -45.633 7.224 29.596 1.00 89.58 C
ANISOU 686 C PHE A 118 12943 11835 9259 901 2243 -679 C
ATOM 687 O PHE A 118 -46.271 7.151 28.543 1.00 89.46 O
ANISOU 687 O PHE A 118 12934 11850 9207 902 2231 -648 O
ATOM 688 CB PHE A 118 -47.085 8.282 31.371 1.00 88.53 C
ANISOU 688 CB PHE A 118 12735 11800 9102 1018 2222 -734 C
ATOM 689 CG PHE A 118 -48.094 8.160 32.494 1.00 90.37 C
ANISOU 689 CG PHE A 118 12904 12126 9307 1043 2225 -770 C
ATOM 690 CD1 PHE A 118 -48.952 7.067 32.569 1.00 93.47 C
ANISOU 690 CD1 PHE A 118 13236 12625 9655 997 2231 -775 C
ATOM 691 CD2 PHE A 118 -48.244 9.179 33.428 1.00 92.88 C
ANISOU 691 CD2 PHE A 118 13231 12417 9641 1101 2240 -807 C
ATOM 692 CE1 PHE A 118 -49.895 6.966 33.597 1.00 94.76 C
ANISOU 692 CE1 PHE A 118 13345 12864 9793 1009 2251 -820 C
ATOM 693 CE2 PHE A 118 -49.190 9.079 34.452 1.00 96.06 C
ANISOU 693 CE2 PHE A 118 13583 12895 10021 1117 2258 -846 C
ATOM 694 CZ PHE A 118 -50.010 7.974 34.529 1.00 94.16 C
ANISOU 694 CZ PHE A 118 13278 12758 9739 1073 2262 -852 C
ATOM 695 N CYS A 119 -44.311 7.504 29.643 1.00 85.56 N
ANISOU 695 N CYS A 119 12476 11225 8806 876 2265 -692 N
ATOM 696 CA CYS A 119 -43.467 7.703 28.460 1.00 85.13 C
ANISOU 696 CA CYS A 119 12492 11068 8787 838 2296 -676 C
ATOM 697 C CYS A 119 -43.310 6.384 27.706 1.00 88.35 C
ANISOU 697 C CYS A 119 12903 11484 9182 760 2321 -640 C
ATOM 698 O CYS A 119 -43.352 6.373 26.474 1.00 87.94 O
ANISOU 698 O CYS A 119 12910 11391 9114 729 2338 -613 O
ATOM 699 CB CYS A 119 -42.113 8.292 28.846 1.00 85.39 C
ANISOU 699 CB CYS A 119 12545 11011 8889 817 2324 -722 C
ATOM 700 SG CYS A 119 -42.141 10.074 29.165 1.00 89.90 S
ANISOU 700 SG CYS A 119 13175 11512 9471 875 2343 -771 S
ATOM 701 N LEU A 120 -43.158 5.272 28.456 1.00 84.45 N
ANISOU 701 N LEU A 120 12364 11039 8686 729 2332 -639 N
ATOM 702 CA LEU A 120 -43.032 3.915 27.919 1.00 83.94 C
ANISOU 702 CA LEU A 120 12314 10971 8607 654 2384 -608 C
ATOM 703 C LEU A 120 -44.370 3.436 27.350 1.00 87.50 C
ANISOU 703 C LEU A 120 12760 11513 8975 619 2383 -597 C
ATOM 704 O LEU A 120 -44.381 2.651 26.399 1.00 87.04 O
ANISOU 704 O LEU A 120 12741 11438 8891 537 2432 -578 O
ATOM 705 CB LEU A 120 -42.517 2.943 28.995 1.00 83.89 C
ANISOU 705 CB LEU A 120 12281 10982 8612 656 2408 -603 C
ATOM 706 CG LEU A 120 -41.098 3.197 29.517 1.00 88.65 C
ANISOU 706 CG LEU A 120 12863 11528 9291 685 2401 -615 C
ATOM 707 CD1 LEU A 120 -40.944 2.693 30.929 1.00 88.97 C
ANISOU 707 CD1 LEU A 120 12867 11630 9309 732 2377 -613 C
ATOM 708 CD2 LEU A 120 -40.047 2.572 28.612 1.00 91.07 C
ANISOU 708 CD2 LEU A 120 13199 11744 9659 638 2470 -591 C
ATOM 709 N THR A 121 -45.495 3.924 27.929 1.00 83.94 N
ANISOU 709 N THR A 121 12252 11162 8480 674 2332 -618 N
ATOM 710 CA THR A 121 -46.866 3.638 27.487 1.00 84.08 C
ANISOU 710 CA THR A 121 12226 11302 8420 650 2316 -626 C
ATOM 711 C THR A 121 -47.072 4.293 26.116 1.00 88.15 C
ANISOU 711 C THR A 121 12775 11808 8909 660 2281 -599 C
ATOM 712 O THR A 121 -47.684 3.690 25.232 1.00 88.17 O
ANISOU 712 O THR A 121 12773 11883 8843 587 2285 -595 O
ATOM 713 CB THR A 121 -47.886 4.131 28.529 1.00 92.76 C
ANISOU 713 CB THR A 121 13244 12501 9500 723 2277 -661 C
ATOM 714 OG1 THR A 121 -47.467 3.732 29.834 1.00 92.62 O
ANISOU 714 OG1 THR A 121 13227 12461 9504 724 2307 -680 O
ATOM 715 CG2 THR A 121 -49.296 3.617 28.263 1.00 91.95 C
ANISOU 715 CG2 THR A 121 13063 12551 9322 683 2272 -688 C
ATOM 716 N GLY A 122 -46.529 5.504 25.962 1.00 84.44 N
ANISOU 716 N GLY A 122 12353 11248 8483 741 2255 -585 N
ATOM 717 CA GLY A 122 -46.560 6.270 24.723 1.00 84.53 C
ANISOU 717 CA GLY A 122 12436 11216 8467 771 2232 -550 C
ATOM 718 C GLY A 122 -45.698 5.633 23.652 1.00 87.57 C
ANISOU 718 C GLY A 122 12909 11507 8855 661 2288 -532 C
ATOM 719 O GLY A 122 -46.103 5.583 22.488 1.00 87.61 O
ANISOU 719 O GLY A 122 12961 11537 8790 630 2273 -505 O
ATOM 720 N LEU A 123 -44.510 5.116 24.053 1.00 83.11 N
ANISOU 720 N LEU A 123 12366 10843 8369 605 2355 -547 N
ATOM 721 CA LEU A 123 -43.550 4.426 23.182 1.00 82.53 C
ANISOU 721 CA LEU A 123 12369 10664 8324 503 2433 -536 C
ATOM 722 C LEU A 123 -44.151 3.139 22.617 1.00 85.88 C
ANISOU 722 C LEU A 123 12793 11160 8676 395 2470 -527 C
ATOM 723 O LEU A 123 -44.008 2.875 21.423 1.00 85.67 O
ANISOU 723 O LEU A 123 12849 11089 8614 312 2509 -511 O
ATOM 724 CB LEU A 123 -42.254 4.098 23.947 1.00 82.11 C
ANISOU 724 CB LEU A 123 12298 10524 8375 493 2488 -555 C
ATOM 725 CG LEU A 123 -41.198 5.196 24.021 1.00 86.91 C
ANISOU 725 CG LEU A 123 12936 11021 9063 530 2498 -583 C
ATOM 726 CD1 LEU A 123 -40.414 5.105 25.312 1.00 86.97 C
ANISOU 726 CD1 LEU A 123 12863 11039 9142 562 2493 -615 C
ATOM 727 CD2 LEU A 123 -40.246 5.124 22.843 1.00 89.37 C
ANISOU 727 CD2 LEU A 123 13341 11199 9417 451 2580 -582 C
ATOM 728 N SER A 124 -44.830 2.351 23.478 1.00 81.98 N
ANISOU 728 N SER A 124 12221 10773 8154 383 2471 -544 N
ATOM 729 CA SER A 124 -45.486 1.092 23.118 1.00 81.87 C
ANISOU 729 CA SER A 124 12207 10835 8065 265 2529 -555 C
ATOM 730 C SER A 124 -46.678 1.321 22.189 1.00 86.02 C
ANISOU 730 C SER A 124 12712 11493 8480 231 2466 -562 C
ATOM 731 O SER A 124 -46.882 0.534 21.263 1.00 86.03 O
ANISOU 731 O SER A 124 12759 11515 8412 101 2519 -569 O
ATOM 732 CB SER A 124 -45.920 0.338 24.370 1.00 85.26 C
ANISOU 732 CB SER A 124 12573 11333 8488 269 2557 -580 C
ATOM 733 OG SER A 124 -44.792 -0.031 25.145 1.00 93.48 O
ANISOU 733 OG SER A 124 13639 12266 9612 301 2611 -563 O
ATOM 734 N PHE A 125 -47.451 2.404 22.425 1.00 82.49 N
ANISOU 734 N PHE A 125 12195 11136 8010 350 2357 -561 N
ATOM 735 CA PHE A 125 -48.601 2.764 21.595 1.00 83.09 C
ANISOU 735 CA PHE A 125 12229 11362 7980 359 2272 -558 C
ATOM 736 C PHE A 125 -48.147 3.322 20.241 1.00 87.10 C
ANISOU 736 C PHE A 125 12855 11788 8452 355 2254 -512 C
ATOM 737 O PHE A 125 -48.835 3.116 19.240 1.00 87.56 O
ANISOU 737 O PHE A 125 12917 11955 8398 294 2214 -508 O
ATOM 738 CB PHE A 125 -49.537 3.740 22.327 1.00 85.28 C
ANISOU 738 CB PHE A 125 12395 11751 8255 513 2175 -564 C
ATOM 739 CG PHE A 125 -50.913 3.879 21.713 1.00 88.03 C
ANISOU 739 CG PHE A 125 12645 12309 8494 532 2085 -572 C
ATOM 740 CD1 PHE A 125 -51.806 2.811 21.714 1.00 91.53 C
ANISOU 740 CD1 PHE A 125 12990 12922 8863 403 2104 -635 C
ATOM 741 CD2 PHE A 125 -51.332 5.088 21.172 1.00 90.99 C
ANISOU 741 CD2 PHE A 125 13021 12719 8834 683 1985 -521 C
ATOM 742 CE1 PHE A 125 -53.079 2.942 21.151 1.00 93.82 C
ANISOU 742 CE1 PHE A 125 13160 13438 9050 415 2011 -656 C
ATOM 743 CE2 PHE A 125 -52.612 5.221 20.623 1.00 95.23 C
ANISOU 743 CE2 PHE A 125 13444 13474 9264 723 1886 -524 C
ATOM 744 CZ PHE A 125 -53.474 4.146 20.611 1.00 93.82 C
ANISOU 744 CZ PHE A 125 13143 13488 9017 584 1892 -596 C
ATOM 745 N ASP A 126 -46.972 3.995 20.211 1.00 82.84 N
ANISOU 745 N ASP A 126 12417 11061 8000 405 2289 -485 N
ATOM 746 CA ASP A 126 -46.353 4.542 18.998 1.00 82.87 C
ANISOU 746 CA ASP A 126 12563 10942 7982 392 2303 -447 C
ATOM 747 C ASP A 126 -45.943 3.391 18.074 1.00 86.15 C
ANISOU 747 C ASP A 126 13057 11315 8362 211 2394 -456 C
ATOM 748 O ASP A 126 -46.129 3.487 16.859 1.00 86.47 O
ANISOU 748 O ASP A 126 13188 11360 8307 158 2379 -433 O
ATOM 749 CB ASP A 126 -45.134 5.418 19.358 1.00 84.20 C
ANISOU 749 CB ASP A 126 12806 10918 8266 459 2350 -445 C
ATOM 750 CG ASP A 126 -44.230 5.777 18.193 1.00 94.28 C
ANISOU 750 CG ASP A 126 14248 12028 9544 407 2414 -426 C
ATOM 751 OD1 ASP A 126 -44.687 6.509 17.289 1.00 95.76 O
ANISOU 751 OD1 ASP A 126 14525 12221 9640 457 2365 -385 O
ATOM 752 OD2 ASP A 126 -43.061 5.335 18.194 1.00 99.28 O
ANISOU 752 OD2 ASP A 126 14925 12527 10270 324 2516 -450 O
ATOM 753 N ARG A 127 -45.405 2.300 18.660 1.00 81.53 N
ANISOU 753 N ARG A 127 12447 10686 7844 121 2493 -486 N
ATOM 754 CA ARG A 127 -44.997 1.098 17.932 1.00 81.09 C
ANISOU 754 CA ARG A 127 12470 10574 7769 -51 2613 -497 C
ATOM 755 C ARG A 127 -46.222 0.302 17.476 1.00 85.10 C
ANISOU 755 C ARG A 127 12936 11262 8136 -165 2596 -525 C
ATOM 756 O ARG A 127 -46.148 -0.384 16.457 1.00 85.27 O
ANISOU 756 O ARG A 127 13048 11262 8088 -318 2670 -534 O
ATOM 757 CB ARG A 127 -44.057 0.214 18.779 1.00 80.51 C
ANISOU 757 CB ARG A 127 12385 10394 7811 -77 2731 -509 C
ATOM 758 CG ARG A 127 -42.689 0.821 19.112 1.00 89.72 C
ANISOU 758 CG ARG A 127 13579 11393 9115 0 2762 -498 C
ATOM 759 CD ARG A 127 -41.724 0.858 17.938 1.00 98.75 C
ANISOU 759 CD ARG A 127 14854 12375 10290 -83 2854 -490 C
ATOM 760 NE ARG A 127 -41.665 2.192 17.340 1.00107.01 N
ANISOU 760 NE ARG A 127 15965 13377 11318 -22 2788 -480 N
ATOM 761 CZ ARG A 127 -42.125 2.502 16.132 1.00120.55 C
ANISOU 761 CZ ARG A 127 17784 15096 12921 -73 2767 -462 C
ATOM 762 NH1 ARG A 127 -42.671 1.568 15.361 1.00107.30 N
ANISOU 762 NH1 ARG A 127 16147 13481 11141 -207 2802 -463 N
ATOM 763 NH2 ARG A 127 -42.031 3.744 15.679 1.00107.25 N
ANISOU 763 NH2 ARG A 127 16180 13352 11217 4 2719 -444 N
ATOM 764 N TYR A 128 -47.345 0.401 18.222 1.00 81.33 N
ANISOU 764 N TYR A 128 12320 10967 7615 -105 2509 -550 N
ATOM 765 CA TYR A 128 -48.605 -0.276 17.904 1.00 81.88 C
ANISOU 765 CA TYR A 128 12313 11244 7552 -214 2486 -598 C
ATOM 766 C TYR A 128 -49.246 0.315 16.645 1.00 86.57 C
ANISOU 766 C TYR A 128 12927 11953 8015 -220 2377 -579 C
ATOM 767 O TYR A 128 -49.574 -0.436 15.728 1.00 86.92 O
ANISOU 767 O TYR A 128 13010 12068 7947 -391 2415 -609 O
ATOM 768 CB TYR A 128 -49.579 -0.240 19.105 1.00 83.08 C
ANISOU 768 CB TYR A 128 12303 11554 7710 -138 2430 -639 C
ATOM 769 CG TYR A 128 -50.990 -0.685 18.775 1.00 86.03 C
ANISOU 769 CG TYR A 128 12561 12176 7949 -233 2384 -703 C
ATOM 770 CD1 TYR A 128 -51.317 -2.036 18.698 1.00 88.32 C
ANISOU 770 CD1 TYR A 128 12857 12522 8178 -438 2509 -776 C
ATOM 771 CD2 TYR A 128 -52.001 0.245 18.545 1.00 87.86 C
ANISOU 771 CD2 TYR A 128 12675 12594 8114 -117 2225 -696 C
ATOM 772 CE1 TYR A 128 -52.609 -2.451 18.377 1.00 90.45 C
ANISOU 772 CE1 TYR A 128 13009 13040 8319 -551 2474 -857 C
ATOM 773 CE2 TYR A 128 -53.296 -0.158 18.222 1.00 90.19 C
ANISOU 773 CE2 TYR A 128 12834 13148 8285 -204 2172 -765 C
ATOM 774 CZ TYR A 128 -53.597 -1.508 18.143 1.00 97.85 C
ANISOU 774 CZ TYR A 128 13801 14184 9193 -434 2296 -854 C
ATOM 775 OH TYR A 128 -54.874 -1.911 17.834 1.00100.32 O
ANISOU 775 OH TYR A 128 13966 14769 9380 -544 2252 -944 O
ATOM 776 N LEU A 129 -49.425 1.654 16.606 1.00 83.22 N
ANISOU 776 N LEU A 129 12484 11542 7593 -34 2248 -526 N
ATOM 777 CA LEU A 129 -50.035 2.377 15.482 1.00 84.29 C
ANISOU 777 CA LEU A 129 12647 11782 7596 14 2127 -486 C
ATOM 778 C LEU A 129 -49.231 2.253 14.184 1.00 88.19 C
ANISOU 778 C LEU A 129 13337 12133 8038 -98 2189 -455 C
ATOM 779 O LEU A 129 -49.820 2.286 13.103 1.00 89.05 O
ANISOU 779 O LEU A 129 13480 12363 7993 -150 2118 -443 O
ATOM 780 CB LEU A 129 -50.234 3.868 15.818 1.00 84.58 C
ANISOU 780 CB LEU A 129 12661 11810 7665 261 2013 -424 C
ATOM 781 CG LEU A 129 -51.124 4.236 17.009 1.00 89.23 C
ANISOU 781 CG LEU A 129 13064 12542 8297 399 1943 -447 C
ATOM 782 CD1 LEU A 129 -50.799 5.628 17.501 1.00 89.18 C
ANISOU 782 CD1 LEU A 129 13099 12414 8372 616 1907 -390 C
ATOM 783 CD2 LEU A 129 -52.604 4.139 16.660 1.00 93.19 C
ANISOU 783 CD2 LEU A 129 13406 13338 8665 412 1821 -470 C
ATOM 784 N ALA A 130 -47.895 2.122 14.294 1.00 83.53 N
ANISOU 784 N ALA A 130 12872 11295 7572 -136 2321 -447 N
ATOM 785 CA ALA A 130 -46.981 2.016 13.157 1.00 83.46 C
ANISOU 785 CA ALA A 130 13055 11110 7543 -245 2412 -427 C
ATOM 786 C ALA A 130 -46.877 0.605 12.570 1.00 87.51 C
ANISOU 786 C ALA A 130 13621 11624 8004 -487 2540 -476 C
ATOM 787 O ALA A 130 -46.955 0.455 11.350 1.00 87.96 O
ANISOU 787 O ALA A 130 13796 11689 7937 -605 2549 -471 O
ATOM 788 CB ALA A 130 -45.602 2.532 13.544 1.00 83.07 C
ANISOU 788 CB ALA A 130 13095 10809 7660 -180 2504 -410 C
ATOM 789 N ILE A 131 -46.696 -0.422 13.423 1.00 83.40 N
ANISOU 789 N ILE A 131 13031 11088 7568 -561 2649 -522 N
ATOM 790 CA ILE A 131 -46.533 -1.811 12.980 1.00 83.52 C
ANISOU 790 CA ILE A 131 13115 11071 7547 -785 2811 -570 C
ATOM 791 C ILE A 131 -47.888 -2.486 12.678 1.00 89.07 C
ANISOU 791 C ILE A 131 13733 12029 8080 -923 2767 -632 C
ATOM 792 O ILE A 131 -48.051 -3.040 11.588 1.00 89.60 O
ANISOU 792 O ILE A 131 13896 12127 8022 -1109 2821 -660 O
ATOM 793 CB ILE A 131 -45.643 -2.629 13.970 1.00 85.43 C
ANISOU 793 CB ILE A 131 13352 11158 7950 -791 2969 -582 C
ATOM 794 CG1 ILE A 131 -44.225 -2.007 14.077 1.00 84.87 C
ANISOU 794 CG1 ILE A 131 13356 10854 8037 -687 3016 -537 C
ATOM 795 CG2 ILE A 131 -45.559 -4.117 13.576 1.00 86.61 C
ANISOU 795 CG2 ILE A 131 13585 11265 8059 -1013 3162 -628 C
ATOM 796 CD1 ILE A 131 -43.476 -2.263 15.393 1.00 90.72 C
ANISOU 796 CD1 ILE A 131 14024 11506 8941 -584 3074 -531 C
ATOM 797 N VAL A 132 -48.845 -2.439 13.627 1.00 86.07 N
ANISOU 797 N VAL A 132 13175 11834 7693 -845 2679 -663 N
ATOM 798 CA VAL A 132 -50.161 -3.079 13.477 1.00 87.38 C
ANISOU 798 CA VAL A 132 13227 12263 7710 -980 2645 -743 C
ATOM 799 C VAL A 132 -51.056 -2.334 12.468 1.00 93.58 C
ANISOU 799 C VAL A 132 13968 13261 8328 -956 2460 -731 C
ATOM 800 O VAL A 132 -51.569 -2.969 11.542 1.00 94.59 O
ANISOU 800 O VAL A 132 14120 13520 8299 -1154 2477 -785 O
ATOM 801 CB VAL A 132 -50.880 -3.320 14.837 1.00 90.88 C
ANISOU 801 CB VAL A 132 13497 12827 8205 -918 2635 -794 C
ATOM 802 CG1 VAL A 132 -52.139 -4.166 14.663 1.00 92.10 C
ANISOU 802 CG1 VAL A 132 13543 13237 8214 -1105 2649 -903 C
ATOM 803 CG2 VAL A 132 -49.943 -3.968 15.852 1.00 89.27 C
ANISOU 803 CG2 VAL A 132 13355 12411 8154 -907 2800 -786 C
ATOM 804 N ARG A 133 -51.228 -1.001 12.646 1.00 90.56 N
ANISOU 804 N ARG A 133 13528 12910 7970 -713 2290 -658 N
ATOM 805 CA ARG A 133 -52.065 -0.113 11.818 1.00 92.18 C
ANISOU 805 CA ARG A 133 13689 13310 8026 -617 2096 -619 C
ATOM 806 C ARG A 133 -53.556 -0.531 11.874 1.00 98.37 C
ANISOU 806 C ARG A 133 14255 14444 8677 -684 1997 -702 C
ATOM 807 O ARG A 133 -54.024 -1.246 10.981 1.00 99.16 O
ANISOU 807 O ARG A 133 14364 14695 8618 -892 2005 -763 O
ATOM 808 CB ARG A 133 -51.548 0.012 10.362 1.00 92.79 C
ANISOU 808 CB ARG A 133 13972 13298 7988 -708 2104 -574 C
ATOM 809 CG ARG A 133 -50.137 0.570 10.235 1.00100.44 C
ANISOU 809 CG ARG A 133 15142 13936 9083 -634 2196 -501 C
ATOM 810 CD ARG A 133 -49.613 0.452 8.818 1.00109.32 C
ANISOU 810 CD ARG A 133 16485 14958 10096 -776 2249 -479 C
ATOM 811 NE ARG A 133 -48.230 -0.027 8.792 1.00114.86 N
ANISOU 811 NE ARG A 133 17348 15356 10935 -881 2457 -486 N
ATOM 812 CZ ARG A 133 -47.876 -1.296 8.607 1.00127.89 C
ANISOU 812 CZ ARG A 133 19054 16943 12595 -1111 2633 -550 C
ATOM 813 NH1 ARG A 133 -48.800 -2.230 8.418 1.00115.83 N
ANISOU 813 NH1 ARG A 133 17447 15627 10938 -1287 2638 -624 N
ATOM 814 NH2 ARG A 133 -46.595 -1.639 8.602 1.00113.34 N
ANISOU 814 NH2 ARG A 133 17347 14825 10893 -1169 2817 -546 N
ATOM 815 N PRO A 134 -54.309 -0.132 12.932 1.00 95.62 N
ANISOU 815 N PRO A 134 13708 14232 8392 -530 1916 -721 N
ATOM 816 CA PRO A 134 -55.725 -0.542 13.017 1.00 97.37 C
ANISOU 816 CA PRO A 134 13702 14794 8499 -603 1835 -818 C
ATOM 817 C PRO A 134 -56.658 0.173 12.036 1.00104.24 C
ANISOU 817 C PRO A 134 14478 15933 9194 -512 1620 -785 C
ATOM 818 O PRO A 134 -57.629 -0.430 11.576 1.00105.63 O
ANISOU 818 O PRO A 134 14515 16398 9222 -669 1571 -879 O
ATOM 819 CB PRO A 134 -56.092 -0.265 14.476 1.00 98.29 C
ANISOU 819 CB PRO A 134 13661 14929 8757 -453 1834 -840 C
ATOM 820 CG PRO A 134 -55.172 0.815 14.903 1.00101.26 C
ANISOU 820 CG PRO A 134 14148 15054 9271 -220 1816 -725 C
ATOM 821 CD PRO A 134 -53.912 0.696 14.092 1.00 95.88 C
ANISOU 821 CD PRO A 134 13712 14120 8597 -301 1906 -666 C
ATOM 822 N VAL A 135 -56.363 1.448 11.720 1.00101.33 N
ANISOU 822 N VAL A 135 14189 15475 8836 -261 1500 -654 N
ATOM 823 CA VAL A 135 -57.144 2.281 10.795 1.00103.52 C
ANISOU 823 CA VAL A 135 14412 15975 8948 -114 1290 -588 C
ATOM 824 C VAL A 135 -56.325 2.644 9.536 1.00107.93 C
ANISOU 824 C VAL A 135 15239 16363 9407 -128 1283 -492 C
ATOM 825 O VAL A 135 -55.216 2.131 9.363 1.00106.01 O
ANISOU 825 O VAL A 135 15198 15852 9228 -284 1451 -499 O
ATOM 826 CB VAL A 135 -57.777 3.527 11.487 1.00108.03 C
ANISOU 826 CB VAL A 135 14833 16628 9584 223 1148 -516 C
ATOM 827 CG1 VAL A 135 -58.902 3.124 12.437 1.00108.41 C
ANISOU 827 CG1 VAL A 135 14583 16938 9671 211 1123 -628 C
ATOM 828 CG2 VAL A 135 -56.729 4.380 12.205 1.00105.87 C
ANISOU 828 CG2 VAL A 135 14718 16011 9496 406 1232 -427 C
ATOM 829 N ALA A 136 -56.882 3.508 8.656 1.00106.78 N
ANISOU 829 N ALA A 136 15098 16372 9101 39 1095 -404 N
ATOM 830 CA ALA A 136 -56.234 3.971 7.424 1.00107.29 C
ANISOU 830 CA ALA A 136 15429 16290 9044 50 1074 -305 C
ATOM 831 C ALA A 136 -55.005 4.831 7.741 1.00109.55 C
ANISOU 831 C ALA A 136 15944 16185 9494 205 1182 -209 C
ATOM 832 O ALA A 136 -54.990 5.520 8.764 1.00108.29 O
ANISOU 832 O ALA A 136 15709 15949 9489 410 1184 -180 O
ATOM 833 CB ALA A 136 -57.222 4.761 6.580 1.00110.90 C
ANISOU 833 CB ALA A 136 15822 17024 9291 239 835 -223 C
ATOM 834 N ASN A 137 -53.978 4.777 6.865 1.00105.73 N
ANISOU 834 N ASN A 137 15740 15459 8975 90 1284 -174 N
ATOM 835 CA ASN A 137 -52.707 5.502 7.001 1.00104.04 C
ANISOU 835 CA ASN A 137 15760 14869 8903 184 1412 -106 C
ATOM 836 C ASN A 137 -52.864 7.017 7.178 1.00108.48 C
ANISOU 836 C ASN A 137 16368 15372 9477 520 1313 13 C
ATOM 837 O ASN A 137 -52.168 7.605 8.009 1.00106.54 O
ANISOU 837 O ASN A 137 16169 14898 9413 632 1409 28 O
ATOM 838 CB ASN A 137 -51.770 5.184 5.834 1.00105.23 C
ANISOU 838 CB ASN A 137 16192 14817 8975 -7 1525 -96 C
ATOM 839 CG ASN A 137 -51.331 3.741 5.777 1.00128.08 C
ANISOU 839 CG ASN A 137 19086 17674 11905 -330 1686 -209 C
ATOM 840 OD1 ASN A 137 -51.783 2.964 4.930 1.00124.03 O
ANISOU 840 OD1 ASN A 137 18581 17326 11219 -534 1665 -256 O
ATOM 841 ND2 ASN A 137 -50.436 3.351 6.674 1.00117.88 N
ANISOU 841 ND2 ASN A 137 17793 16165 10832 -382 1857 -254 N
ATOM 842 N ALA A 138 -53.783 7.636 6.414 1.00107.30 N
ANISOU 842 N ALA A 138 16206 15434 9130 680 1126 95 N
ATOM 843 CA ALA A 138 -54.063 9.072 6.484 1.00108.18 C
ANISOU 843 CA ALA A 138 16374 15505 9225 1022 1033 221 C
ATOM 844 C ALA A 138 -54.856 9.432 7.746 1.00111.45 C
ANISOU 844 C ALA A 138 16517 16066 9765 1217 969 206 C
ATOM 845 O ALA A 138 -54.690 10.532 8.275 1.00110.92 O
ANISOU 845 O ALA A 138 16511 15843 9789 1461 991 279 O
ATOM 846 CB ALA A 138 -54.819 9.518 5.243 1.00111.89 C
ANISOU 846 CB ALA A 138 16912 16172 9427 1139 849 321 C
ATOM 847 N ARG A 139 -55.711 8.503 8.223 1.00107.80 N
ANISOU 847 N ARG A 139 15765 15891 9304 1096 910 102 N
ATOM 848 CA ARG A 139 -56.556 8.676 9.409 1.00107.44 C
ANISOU 848 CA ARG A 139 15441 16012 9369 1240 858 65 C
ATOM 849 C ARG A 139 -55.845 8.359 10.736 1.00108.14 C
ANISOU 849 C ARG A 139 15499 15892 9697 1159 1031 -14 C
ATOM 850 O ARG A 139 -56.376 8.696 11.798 1.00107.42 O
ANISOU 850 O ARG A 139 15230 15869 9716 1301 1015 -33 O
ATOM 851 CB ARG A 139 -57.847 7.852 9.271 1.00109.44 C
ANISOU 851 CB ARG A 139 15399 16682 9500 1140 721 -22 C
ATOM 852 N LEU A 140 -54.654 7.721 10.677 1.00102.53 N
ANISOU 852 N LEU A 140 14959 14934 9064 940 1196 -58 N
ATOM 853 CA LEU A 140 -53.857 7.349 11.852 1.00 99.76 C
ANISOU 853 CA LEU A 140 14595 14386 8922 856 1355 -126 C
ATOM 854 C LEU A 140 -53.343 8.558 12.638 1.00102.51 C
ANISOU 854 C LEU A 140 15021 14515 9411 1081 1401 -67 C
ATOM 855 O LEU A 140 -53.521 8.600 13.857 1.00101.13 O
ANISOU 855 O LEU A 140 14705 14353 9368 1136 1430 -111 O
ATOM 856 CB LEU A 140 -52.687 6.422 11.466 1.00 98.29 C
ANISOU 856 CB LEU A 140 14576 13996 8774 594 1514 -175 C
ATOM 857 CG LEU A 140 -52.973 4.919 11.453 1.00102.64 C
ANISOU 857 CG LEU A 140 15016 14694 9290 322 1566 -283 C
ATOM 858 CD1 LEU A 140 -52.026 4.197 10.522 1.00102.36 C
ANISOU 858 CD1 LEU A 140 15185 14491 9215 95 1690 -298 C
ATOM 859 CD2 LEU A 140 -52.876 4.320 12.847 1.00103.35 C
ANISOU 859 CD2 LEU A 140 14966 14758 9544 276 1662 -362 C
ATOM 860 N ARG A 141 -52.717 9.537 11.937 1.00 99.40 N
ANISOU 860 N ARG A 141 14866 13920 8981 1197 1420 26 N
ATOM 861 CA ARG A 141 -52.135 10.770 12.487 1.00 98.70 C
ANISOU 861 CA ARG A 141 14905 13594 9003 1389 1490 79 C
ATOM 862 C ARG A 141 -51.156 10.482 13.641 1.00 99.98 C
ANISOU 862 C ARG A 141 15053 13567 9367 1283 1640 -3 C
ATOM 863 O ARG A 141 -51.411 10.845 14.791 1.00 98.96 O
ANISOU 863 O ARG A 141 14802 13453 9346 1389 1648 -27 O
ATOM 864 CB ARG A 141 -53.226 11.791 12.871 1.00100.60 C
ANISOU 864 CB ARG A 141 15034 13975 9214 1682 1376 147 C
ATOM 865 N LEU A 142 -50.047 9.792 13.312 1.00 95.23 N
ANISOU 865 N LEU A 142 14572 12799 8811 1073 1758 -48 N
ATOM 866 CA LEU A 142 -48.991 9.379 14.243 1.00 93.00 C
ANISOU 866 CA LEU A 142 14282 12350 8705 957 1895 -122 C
ATOM 867 C LEU A 142 -48.284 10.562 14.921 1.00 96.28 C
ANISOU 867 C LEU A 142 14792 12553 9236 1092 1971 -111 C
ATOM 868 O LEU A 142 -48.009 10.495 16.120 1.00 94.63 O
ANISOU 868 O LEU A 142 14480 12319 9157 1091 2016 -166 O
ATOM 869 CB LEU A 142 -47.978 8.472 13.515 1.00 92.28 C
ANISOU 869 CB LEU A 142 14315 12128 8621 728 2004 -157 C
ATOM 870 CG LEU A 142 -46.969 7.705 14.375 1.00 95.21 C
ANISOU 870 CG LEU A 142 14640 12380 9157 592 2131 -234 C
ATOM 871 CD1 LEU A 142 -47.593 6.461 14.993 1.00 94.90 C
ANISOU 871 CD1 LEU A 142 14409 12525 9121 487 2112 -289 C
ATOM 872 CD2 LEU A 142 -45.771 7.302 13.554 1.00 97.13 C
ANISOU 872 CD2 LEU A 142 15055 12423 9426 431 2261 -249 C
ATOM 873 N ARG A 143 -47.993 11.633 14.156 1.00 93.89 N
ANISOU 873 N ARG A 143 14700 12100 8875 1200 1995 -45 N
ATOM 874 CA ARG A 143 -47.329 12.843 14.656 1.00 93.66 C
ANISOU 874 CA ARG A 143 14798 11854 8934 1313 2093 -41 C
ATOM 875 C ARG A 143 -48.256 13.645 15.577 1.00 98.14 C
ANISOU 875 C ARG A 143 15249 12518 9520 1528 2030 -15 C
ATOM 876 O ARG A 143 -47.792 14.211 16.569 1.00 97.00 O
ANISOU 876 O ARG A 143 15104 12259 9495 1563 2114 -59 O
ATOM 877 CB ARG A 143 -46.828 13.724 13.492 1.00 95.21 C
ANISOU 877 CB ARG A 143 15281 11852 9043 1360 2157 22 C
ATOM 878 CG ARG A 143 -45.809 13.055 12.560 1.00105.06 C
ANISOU 878 CG ARG A 143 16673 12964 10283 1144 2250 -11 C
ATOM 879 CD ARG A 143 -44.385 13.112 13.088 1.00113.08 C
ANISOU 879 CD ARG A 143 17744 13756 11466 1017 2420 -104 C
ATOM 880 NE ARG A 143 -43.449 12.423 12.197 1.00119.97 N
ANISOU 880 NE ARG A 143 18734 14507 12342 815 2517 -139 N
ATOM 881 CZ ARG A 143 -42.155 12.251 12.450 1.00132.53 C
ANISOU 881 CZ ARG A 143 20356 15925 14075 677 2663 -225 C
ATOM 882 NH1 ARG A 143 -41.383 11.613 11.582 1.00119.79 N
ANISOU 882 NH1 ARG A 143 18847 14205 12464 503 2757 -254 N
ATOM 883 NH2 ARG A 143 -41.623 12.716 13.574 1.00118.26 N
ANISOU 883 NH2 ARG A 143 18469 14058 12405 708 2719 -289 N
ATOM 884 N VAL A 144 -49.566 13.675 15.250 1.00 96.11 N
ANISOU 884 N VAL A 144 14888 12483 9145 1665 1887 50 N
ATOM 885 CA VAL A 144 -50.607 14.377 16.012 1.00 96.79 C
ANISOU 885 CA VAL A 144 14844 12690 9242 1884 1821 82 C
ATOM 886 C VAL A 144 -50.879 13.641 17.335 1.00 99.19 C
ANISOU 886 C VAL A 144 14907 13121 9662 1804 1816 -11 C
ATOM 887 O VAL A 144 -50.885 14.281 18.388 1.00 98.57 O
ANISOU 887 O VAL A 144 14794 12979 9679 1897 1869 -34 O
ATOM 888 CB VAL A 144 -51.902 14.605 15.175 1.00102.89 C
ANISOU 888 CB VAL A 144 15561 13683 9850 2061 1661 179 C
ATOM 889 CG1 VAL A 144 -52.941 15.407 15.958 1.00103.85 C
ANISOU 889 CG1 VAL A 144 15549 13913 9998 2310 1611 214 C
ATOM 890 CG2 VAL A 144 -51.593 15.294 13.847 1.00104.18 C
ANISOU 890 CG2 VAL A 144 15994 13711 9877 2140 1667 280 C
ATOM 891 N SER A 145 -51.077 12.300 17.277 1.00 94.83 N
ANISOU 891 N SER A 145 14209 12731 9093 1622 1769 -67 N
ATOM 892 CA SER A 145 -51.340 11.439 18.439 1.00 93.39 C
ANISOU 892 CA SER A 145 13821 12665 8998 1525 1775 -155 C
ATOM 893 C SER A 145 -50.211 11.483 19.474 1.00 95.46 C
ANISOU 893 C SER A 145 14131 12733 9407 1449 1899 -216 C
ATOM 894 O SER A 145 -50.487 11.448 20.672 1.00 94.48 O
ANISOU 894 O SER A 145 13883 12656 9358 1473 1910 -264 O
ATOM 895 CB SER A 145 -51.601 10.001 18.000 1.00 96.59 C
ANISOU 895 CB SER A 145 14125 13232 9342 1326 1739 -201 C
ATOM 896 OG SER A 145 -52.018 9.192 19.088 1.00104.79 O
ANISOU 896 OG SER A 145 14979 14392 10445 1249 1750 -281 O
ATOM 897 N GLY A 146 -48.968 11.571 18.997 1.00 91.44 N
ANISOU 897 N GLY A 146 13796 12017 8929 1356 1989 -219 N
ATOM 898 CA GLY A 146 -47.777 11.664 19.834 1.00 90.01 C
ANISOU 898 CA GLY A 146 13660 11662 8878 1280 2100 -280 C
ATOM 899 C GLY A 146 -47.694 12.982 20.578 1.00 94.40 C
ANISOU 899 C GLY A 146 14270 12108 9488 1426 2147 -281 C
ATOM 900 O GLY A 146 -47.285 13.012 21.741 1.00 93.16 O
ANISOU 900 O GLY A 146 14052 11918 9426 1395 2194 -344 O
ATOM 901 N ALA A 147 -48.105 14.080 19.908 1.00 92.49 N
ANISOU 901 N ALA A 147 14156 11810 9177 1588 2140 -208 N
ATOM 902 CA ALA A 147 -48.132 15.438 20.459 1.00 93.15 C
ANISOU 902 CA ALA A 147 14328 11770 9294 1744 2209 -197 C
ATOM 903 C ALA A 147 -49.242 15.592 21.506 1.00 97.50 C
ANISOU 903 C ALA A 147 14703 12475 9868 1869 2154 -203 C
ATOM 904 O ALA A 147 -49.093 16.381 22.441 1.00 97.17 O
ANISOU 904 O ALA A 147 14686 12340 9894 1929 2233 -237 O
ATOM 905 CB ALA A 147 -48.323 16.452 19.342 1.00 95.57 C
ANISOU 905 CB ALA A 147 14839 11971 9501 1895 2224 -102 C
ATOM 906 N VAL A 148 -50.351 14.842 21.342 1.00 94.47 N
ANISOU 906 N VAL A 148 14143 12327 9425 1895 2030 -180 N
ATOM 907 CA VAL A 148 -51.492 14.844 22.263 1.00 94.71 C
ANISOU 907 CA VAL A 148 13981 12529 9476 1998 1979 -196 C
ATOM 908 C VAL A 148 -51.123 14.045 23.524 1.00 96.90 C
ANISOU 908 C VAL A 148 14141 12829 9847 1842 2018 -297 C
ATOM 909 O VAL A 148 -51.290 14.555 24.632 1.00 96.43 O
ANISOU 909 O VAL A 148 14043 12743 9852 1900 2067 -335 O
ATOM 910 CB VAL A 148 -52.802 14.345 21.578 1.00 99.84 C
ANISOU 910 CB VAL A 148 14474 13437 10022 2069 1838 -151 C
ATOM 911 CG1 VAL A 148 -53.915 14.084 22.593 1.00 99.93 C
ANISOU 911 CG1 VAL A 148 14255 13643 10072 2120 1799 -200 C
ATOM 912 CG2 VAL A 148 -53.276 15.331 20.514 1.00101.64 C
ANISOU 912 CG2 VAL A 148 14815 13653 10150 2280 1789 -37 C
ATOM 913 N ALA A 149 -50.593 12.813 23.343 1.00 92.27 N
ANISOU 913 N ALA A 149 13517 12281 9262 1649 2006 -337 N
ATOM 914 CA ALA A 149 -50.184 11.904 24.418 1.00 90.74 C
ANISOU 914 CA ALA A 149 13232 12108 9136 1505 2040 -417 C
ATOM 915 C ALA A 149 -49.126 12.488 25.356 1.00 94.01 C
ANISOU 915 C ALA A 149 13729 12350 9642 1480 2132 -464 C
ATOM 916 O ALA A 149 -49.213 12.260 26.564 1.00 93.08 O
ANISOU 916 O ALA A 149 13526 12271 9569 1454 2149 -519 O
ATOM 917 CB ALA A 149 -49.701 10.583 23.840 1.00 90.59 C
ANISOU 917 CB ALA A 149 13205 12122 9095 1325 2034 -432 C
ATOM 918 N THR A 150 -48.144 13.246 24.813 1.00 90.80 N
ANISOU 918 N THR A 150 13489 11760 9252 1480 2197 -450 N
ATOM 919 CA THR A 150 -47.076 13.866 25.609 1.00 90.27 C
ANISOU 919 CA THR A 150 13497 11540 9262 1437 2290 -511 C
ATOM 920 C THR A 150 -47.624 15.004 26.497 1.00 94.94 C
ANISOU 920 C THR A 150 14099 12101 9871 1567 2332 -525 C
ATOM 921 O THR A 150 -47.123 15.201 27.605 1.00 94.05 O
ANISOU 921 O THR A 150 13972 11948 9813 1513 2384 -597 O
ATOM 922 CB THR A 150 -45.863 14.273 24.741 1.00 98.81 C
ANISOU 922 CB THR A 150 14745 12439 10357 1370 2365 -514 C
ATOM 923 OG1 THR A 150 -44.762 14.590 25.595 1.00 98.07 O
ANISOU 923 OG1 THR A 150 14675 12244 10342 1284 2445 -598 O
ATOM 924 CG2 THR A 150 -46.148 15.443 23.795 1.00 99.00 C
ANISOU 924 CG2 THR A 150 14938 12352 10326 1502 2403 -449 C
ATOM 925 N ALA A 151 -48.664 15.718 26.024 1.00 92.79 N
ANISOU 925 N ALA A 151 13848 11859 9550 1740 2310 -457 N
ATOM 926 CA ALA A 151 -49.305 16.805 26.764 1.00 93.64 C
ANISOU 926 CA ALA A 151 13971 11932 9675 1887 2365 -458 C
ATOM 927 C ALA A 151 -50.188 16.252 27.884 1.00 97.24 C
ANISOU 927 C ALA A 151 14240 12553 10155 1891 2321 -499 C
ATOM 928 O ALA A 151 -50.205 16.817 28.977 1.00 96.96 O
ANISOU 928 O ALA A 151 14209 12469 10163 1907 2393 -551 O
ATOM 929 CB ALA A 151 -50.130 17.667 25.820 1.00 96.06 C
ANISOU 929 CB ALA A 151 14356 12224 9917 2095 2353 -357 C
ATOM 930 N VAL A 152 -50.902 15.140 27.613 1.00 93.52 N
ANISOU 930 N VAL A 152 13615 12271 9648 1857 2219 -486 N
ATOM 931 CA VAL A 152 -51.804 14.472 28.556 1.00 93.19 C
ANISOU 931 CA VAL A 152 13396 12393 9618 1841 2186 -532 C
ATOM 932 C VAL A 152 -51.016 13.783 29.693 1.00 95.96 C
ANISOU 932 C VAL A 152 13730 12717 10013 1676 2223 -614 C
ATOM 933 O VAL A 152 -51.440 13.877 30.847 1.00 95.61 O
ANISOU 933 O VAL A 152 13628 12706 9996 1684 2256 -665 O
ATOM 934 CB VAL A 152 -52.805 13.522 27.826 1.00 97.38 C
ANISOU 934 CB VAL A 152 13778 13135 10087 1839 2081 -506 C
ATOM 935 CG1 VAL A 152 -53.629 12.686 28.805 1.00 96.96 C
ANISOU 935 CG1 VAL A 152 13552 13242 10046 1779 2071 -576 C
ATOM 936 CG2 VAL A 152 -53.732 14.307 26.901 1.00 98.92 C
ANISOU 936 CG2 VAL A 152 13962 13393 10229 2036 2028 -425 C
ATOM 937 N LEU A 153 -49.867 13.132 29.380 1.00 91.74 N
ANISOU 937 N LEU A 153 13253 12121 9485 1537 2222 -624 N
ATOM 938 CA LEU A 153 -49.061 12.437 30.392 1.00 90.69 C
ANISOU 938 CA LEU A 153 13101 11974 9382 1403 2244 -687 C
ATOM 939 C LEU A 153 -48.425 13.393 31.420 1.00 95.23 C
ANISOU 939 C LEU A 153 13747 12436 9998 1405 2316 -742 C
ATOM 940 O LEU A 153 -48.417 13.061 32.604 1.00 94.56 O
ANISOU 940 O LEU A 153 13615 12394 9920 1353 2325 -795 O
ATOM 941 CB LEU A 153 -48.018 11.465 29.788 1.00 89.80 C
ANISOU 941 CB LEU A 153 13015 11833 9271 1274 2229 -679 C
ATOM 942 CG LEU A 153 -46.808 11.996 29.002 1.00 94.44 C
ANISOU 942 CG LEU A 153 13727 12270 9886 1242 2268 -670 C
ATOM 943 CD1 LEU A 153 -45.601 12.192 29.913 1.00 94.22 C
ANISOU 943 CD1 LEU A 153 13727 12162 9910 1164 2314 -736 C
ATOM 944 CD2 LEU A 153 -46.396 11.000 27.935 1.00 96.28 C
ANISOU 944 CD2 LEU A 153 13969 12512 10103 1156 2246 -635 C
ATOM 945 N TRP A 154 -47.920 14.569 30.982 1.00 92.76 N
ANISOU 945 N TRP A 154 13561 11982 9703 1455 2377 -736 N
ATOM 946 CA TRP A 154 -47.314 15.556 31.884 1.00 93.11 C
ANISOU 946 CA TRP A 154 13686 11915 9777 1436 2466 -803 C
ATOM 947 C TRP A 154 -48.358 16.272 32.746 1.00 98.33 C
ANISOU 947 C TRP A 154 14329 12594 10439 1539 2511 -818 C
ATOM 948 O TRP A 154 -48.045 16.682 33.865 1.00 98.16 O
ANISOU 948 O TRP A 154 14331 12535 10429 1486 2571 -891 O
ATOM 949 CB TRP A 154 -46.422 16.554 31.130 1.00 92.34 C
ANISOU 949 CB TRP A 154 13747 11645 9694 1433 2547 -806 C
ATOM 950 CG TRP A 154 -45.071 16.007 30.765 1.00 92.50 C
ANISOU 950 CG TRP A 154 13783 11625 9736 1290 2540 -838 C
ATOM 951 CD1 TRP A 154 -44.635 15.667 29.519 1.00 95.15 C
ANISOU 951 CD1 TRP A 154 14165 11919 10069 1267 2525 -793 C
ATOM 952 CD2 TRP A 154 -43.980 15.738 31.659 1.00 91.88 C
ANISOU 952 CD2 TRP A 154 13670 11554 9687 1155 2549 -925 C
ATOM 953 NE1 TRP A 154 -43.343 15.199 29.579 1.00 93.98 N
ANISOU 953 NE1 TRP A 154 14006 11743 9960 1128 2535 -849 N
ATOM 954 CE2 TRP A 154 -42.915 15.232 30.881 1.00 95.26 C
ANISOU 954 CE2 TRP A 154 14109 11945 10142 1065 2542 -928 C
ATOM 955 CE3 TRP A 154 -43.799 15.874 33.047 1.00 93.26 C
ANISOU 955 CE3 TRP A 154 13802 11770 9861 1102 2560 -1002 C
ATOM 956 CZ2 TRP A 154 -41.686 14.864 31.441 1.00 94.25 C
ANISOU 956 CZ2 TRP A 154 13930 11833 10047 940 2539 -1003 C
ATOM 957 CZ3 TRP A 154 -42.582 15.505 33.602 1.00 94.43 C
ANISOU 957 CZ3 TRP A 154 13909 11943 10026 974 2545 -1073 C
ATOM 958 CH2 TRP A 154 -41.542 15.008 32.803 1.00 94.64 C
ANISOU 958 CH2 TRP A 154 13927 11945 10087 902 2532 -1072 C
ATOM 959 N VAL A 155 -49.599 16.402 32.231 1.00 95.83 N
ANISOU 959 N VAL A 155 13961 12345 10105 1684 2483 -754 N
ATOM 960 CA VAL A 155 -50.729 17.010 32.941 1.00 96.74 C
ANISOU 960 CA VAL A 155 14033 12492 10231 1805 2529 -761 C
ATOM 961 C VAL A 155 -51.232 16.030 34.017 1.00100.29 C
ANISOU 961 C VAL A 155 14345 13082 10680 1724 2492 -816 C
ATOM 962 O VAL A 155 -51.454 16.444 35.158 1.00100.19 O
ANISOU 962 O VAL A 155 14339 13046 10683 1718 2562 -875 O
ATOM 963 CB VAL A 155 -51.834 17.499 31.955 1.00101.88 C
ANISOU 963 CB VAL A 155 14661 13184 10864 2004 2503 -671 C
ATOM 964 CG1 VAL A 155 -53.207 17.602 32.619 1.00102.62 C
ANISOU 964 CG1 VAL A 155 14624 13393 10974 2119 2511 -679 C
ATOM 965 CG2 VAL A 155 -51.446 18.833 31.324 1.00102.74 C
ANISOU 965 CG2 VAL A 155 14958 13106 10972 2115 2596 -626 C
ATOM 966 N LEU A 156 -51.362 14.729 33.660 1.00 96.32 N
ANISOU 966 N LEU A 156 13739 12708 10151 1650 2401 -802 N
ATOM 967 CA LEU A 156 -51.798 13.666 34.570 1.00 95.80 C
ANISOU 967 CA LEU A 156 13567 12762 10070 1563 2380 -852 C
ATOM 968 C LEU A 156 -50.797 13.419 35.697 1.00 99.39 C
ANISOU 968 C LEU A 156 14081 13161 10523 1434 2408 -913 C
ATOM 969 O LEU A 156 -51.208 13.370 36.854 1.00 99.13 O
ANISOU 969 O LEU A 156 14026 13156 10483 1411 2447 -968 O
ATOM 970 CB LEU A 156 -52.090 12.353 33.819 1.00 95.29 C
ANISOU 970 CB LEU A 156 13410 12827 9971 1502 2301 -824 C
ATOM 971 CG LEU A 156 -53.472 12.203 33.178 1.00100.94 C
ANISOU 971 CG LEU A 156 13997 13689 10667 1592 2262 -801 C
ATOM 972 CD1 LEU A 156 -53.492 11.028 32.224 1.00100.63 C
ANISOU 972 CD1 LEU A 156 13904 13750 10581 1504 2195 -778 C
ATOM 973 CD2 LEU A 156 -54.564 12.014 34.228 1.00103.97 C
ANISOU 973 CD2 LEU A 156 14271 14174 11060 1602 2301 -865 C
ATOM 974 N ALA A 157 -49.488 13.297 35.367 1.00 95.72 N
ANISOU 974 N ALA A 157 13687 12622 10060 1354 2390 -908 N
ATOM 975 CA ALA A 157 -48.402 13.065 36.332 1.00 95.29 C
ANISOU 975 CA ALA A 157 13672 12538 9997 1241 2396 -963 C
ATOM 976 C ALA A 157 -48.330 14.131 37.431 1.00100.42 C
ANISOU 976 C ALA A 157 14385 13122 10649 1240 2472 -1031 C
ATOM 977 O ALA A 157 -47.951 13.812 38.557 1.00 99.93 O
ANISOU 977 O ALA A 157 14325 13089 10554 1157 2470 -1084 O
ATOM 978 CB ALA A 157 -47.066 12.963 35.614 1.00 95.50 C
ANISOU 978 CB ALA A 157 13747 12499 10041 1178 2373 -950 C
ATOM 979 N ALA A 158 -48.705 15.383 37.104 1.00 98.22 N
ANISOU 979 N ALA A 158 14169 12752 10398 1333 2547 -1028 N
ATOM 980 CA ALA A 158 -48.725 16.506 38.042 1.00 99.10 C
ANISOU 980 CA ALA A 158 14361 12779 10513 1333 2652 -1095 C
ATOM 981 C ALA A 158 -49.983 16.477 38.919 1.00103.87 C
ANISOU 981 C ALA A 158 14910 13444 11112 1387 2690 -1115 C
ATOM 982 O ALA A 158 -49.893 16.765 40.113 1.00103.81 O
ANISOU 982 O ALA A 158 14943 13417 11083 1320 2749 -1188 O
ATOM 983 CB ALA A 158 -48.639 17.822 37.284 1.00100.72 C
ANISOU 983 CB ALA A 158 14680 12841 10749 1422 2744 -1076 C
ATOM 984 N LEU A 159 -51.148 16.126 38.327 1.00100.96 N
ANISOU 984 N LEU A 159 14445 13157 10760 1498 2659 -1059 N
ATOM 985 CA LEU A 159 -52.439 16.049 39.020 1.00101.65 C
ANISOU 985 CA LEU A 159 14451 13316 10855 1556 2700 -1083 C
ATOM 986 C LEU A 159 -52.548 14.836 39.946 1.00105.44 C
ANISOU 986 C LEU A 159 14872 13899 11292 1435 2665 -1129 C
ATOM 987 O LEU A 159 -53.102 14.956 41.039 1.00105.59 O
ANISOU 987 O LEU A 159 14893 13924 11302 1414 2735 -1189 O
ATOM 988 CB LEU A 159 -53.608 16.046 38.017 1.00102.33 C
ANISOU 988 CB LEU A 159 14428 13485 10969 1709 2668 -1017 C
ATOM 989 CG LEU A 159 -53.995 17.386 37.388 1.00108.36 C
ANISOU 989 CG LEU A 159 15248 14154 11770 1888 2734 -967 C
ATOM 990 CD1 LEU A 159 -54.753 17.172 36.097 1.00109.02 C
ANISOU 990 CD1 LEU A 159 15230 14342 11853 2023 2648 -881 C
ATOM 991 CD2 LEU A 159 -54.836 18.229 38.340 1.00112.14 C
ANISOU 991 CD2 LEU A 159 15733 14589 12286 1971 2861 -1011 C
ATOM 992 N LEU A 160 -52.049 13.669 39.498 1.00101.41 N
ANISOU 992 N LEU A 160 14324 13458 10751 1359 2572 -1099 N
ATOM 993 CA LEU A 160 -52.093 12.419 40.260 1.00100.94 C
ANISOU 993 CA LEU A 160 14234 13480 10638 1254 2547 -1128 C
ATOM 994 C LEU A 160 -51.126 12.409 41.443 1.00105.21 C
ANISOU 994 C LEU A 160 14870 13974 11130 1151 2558 -1177 C
ATOM 995 O LEU A 160 -51.445 11.816 42.471 1.00104.98 O
ANISOU 995 O LEU A 160 14851 13986 11051 1092 2581 -1217 O
ATOM 996 CB LEU A 160 -51.874 11.199 39.350 1.00100.15 C
ANISOU 996 CB LEU A 160 14081 13451 10519 1215 2468 -1076 C
ATOM 997 CG LEU A 160 -53.045 10.843 38.429 1.00105.24 C
ANISOU 997 CG LEU A 160 14610 14198 11181 1275 2453 -1051 C
ATOM 998 CD1 LEU A 160 -52.557 10.368 37.078 1.00104.83 C
ANISOU 998 CD1 LEU A 160 14546 14159 11126 1268 2381 -986 C
ATOM 999 CD2 LEU A 160 -53.959 9.808 39.065 1.00107.97 C
ANISOU 999 CD2 LEU A 160 14887 14647 11490 1210 2487 -1101 C
ATOM 1000 N ALA A 161 -49.960 13.071 41.308 1.00102.06 N
ANISOU 1000 N ALA A 161 14543 13497 10737 1125 2544 -1179 N
ATOM 1001 CA ALA A 161 -48.959 13.157 42.375 1.00102.21 C
ANISOU 1001 CA ALA A 161 14634 13498 10702 1024 2538 -1234 C
ATOM 1002 C ALA A 161 -49.128 14.418 43.244 1.00107.78 C
ANISOU 1002 C ALA A 161 15418 14130 11405 1013 2640 -1309 C
ATOM 1003 O ALA A 161 -48.335 14.638 44.162 1.00107.71 O
ANISOU 1003 O ALA A 161 15472 14114 11339 916 2641 -1369 O
ATOM 1004 CB ALA A 161 -47.556 13.087 41.792 1.00102.43 C
ANISOU 1004 CB ALA A 161 14676 13506 10736 979 2471 -1215 C
ATOM 1005 N MET A 162 -50.182 15.221 42.971 1.00105.55 N
ANISOU 1005 N MET A 162 15129 13797 11178 1113 2729 -1308 N
ATOM 1006 CA MET A 162 -50.520 16.442 43.711 1.00106.79 C
ANISOU 1006 CA MET A 162 15368 13863 11344 1122 2859 -1373 C
ATOM 1007 C MET A 162 -50.841 16.182 45.207 1.00111.49 C
ANISOU 1007 C MET A 162 15998 14489 11872 1032 2904 -1447 C
ATOM 1008 O MET A 162 -50.327 16.947 46.028 1.00111.78 O
ANISOU 1008 O MET A 162 16136 14464 11870 949 2971 -1520 O
ATOM 1009 CB MET A 162 -51.646 17.231 43.011 1.00109.96 C
ANISOU 1009 CB MET A 162 15741 14214 11825 1284 2941 -1335 C
ATOM 1010 CG MET A 162 -51.824 18.659 43.521 1.00115.02 C
ANISOU 1010 CG MET A 162 16494 14719 12489 1315 3100 -1389 C
ATOM 1011 SD MET A 162 -50.441 19.776 43.161 1.00119.60 S
ANISOU 1011 SD MET A 162 17224 15154 13062 1251 3157 -1419 S
ATOM 1012 CE MET A 162 -50.759 20.149 41.442 1.00116.34 C
ANISOU 1012 CE MET A 162 16794 14692 12719 1438 3141 -1305 C
ATOM 1013 N PRO A 163 -51.614 15.128 45.616 1.00108.04 N
ANISOU 1013 N PRO A 163 15499 14142 11408 1026 2879 -1440 N
ATOM 1014 CA PRO A 163 -51.862 14.922 47.057 1.00108.52 C
ANISOU 1014 CA PRO A 163 15625 14215 11393 932 2935 -1513 C
ATOM 1015 C PRO A 163 -50.613 14.600 47.880 1.00112.55 C
ANISOU 1015 C PRO A 163 16219 14750 11794 801 2863 -1543 C
ATOM 1016 O PRO A 163 -50.631 14.802 49.093 1.00112.91 O
ANISOU 1016 O PRO A 163 16354 14785 11763 715 2919 -1613 O
ATOM 1017 CB PRO A 163 -52.864 13.760 47.090 1.00109.99 C
ANISOU 1017 CB PRO A 163 15729 14488 11573 951 2925 -1494 C
ATOM 1018 CG PRO A 163 -53.439 13.696 45.721 1.00114.03 C
ANISOU 1018 CG PRO A 163 16118 15033 12175 1070 2894 -1429 C
ATOM 1019 CD PRO A 163 -52.324 14.104 44.821 1.00108.96 C
ANISOU 1019 CD PRO A 163 15498 14350 11553 1088 2818 -1379 C
ATOM 1020 N VAL A 164 -49.531 14.122 47.225 1.00108.56 N
ANISOU 1020 N VAL A 164 15684 14286 11279 788 2742 -1493 N
ATOM 1021 CA VAL A 164 -48.251 13.783 47.862 1.00108.56 C
ANISOU 1021 CA VAL A 164 15728 14337 11182 687 2651 -1512 C
ATOM 1022 C VAL A 164 -47.595 15.043 48.459 1.00113.94 C
ANISOU 1022 C VAL A 164 16490 14967 11836 599 2710 -1604 C
ATOM 1023 O VAL A 164 -47.187 15.011 49.618 1.00114.23 O
ANISOU 1023 O VAL A 164 16594 15046 11762 498 2697 -1664 O
ATOM 1024 CB VAL A 164 -47.291 12.995 46.922 1.00111.43 C
ANISOU 1024 CB VAL A 164 16021 14754 11565 709 2524 -1437 C
ATOM 1025 CG1 VAL A 164 -46.071 12.475 47.680 1.00111.49 C
ANISOU 1025 CG1 VAL A 164 16050 14844 11467 629 2420 -1449 C
ATOM 1026 CG2 VAL A 164 -48.011 11.841 46.227 1.00110.40 C
ANISOU 1026 CG2 VAL A 164 15824 14660 11465 781 2497 -1356 C
ATOM 1027 N MET A 165 -47.539 16.151 47.686 1.00111.16 N
ANISOU 1027 N MET A 165 16146 14518 11571 634 2786 -1620 N
ATOM 1028 CA MET A 165 -46.965 17.437 48.109 1.00112.28 C
ANISOU 1028 CA MET A 165 16381 14586 11696 543 2880 -1718 C
ATOM 1029 C MET A 165 -47.760 18.073 49.260 1.00117.74 C
ANISOU 1029 C MET A 165 17170 15221 12345 496 3019 -1796 C
ATOM 1030 O MET A 165 -47.162 18.685 50.148 1.00118.44 O
ANISOU 1030 O MET A 165 17347 15304 12352 360 3064 -1895 O
ATOM 1031 CB MET A 165 -46.886 18.410 46.919 1.00114.66 C
ANISOU 1031 CB MET A 165 16694 14770 12102 614 2958 -1702 C
ATOM 1032 CG MET A 165 -45.958 19.589 47.150 1.00119.40 C
ANISOU 1032 CG MET A 165 17391 15296 12679 493 3049 -1808 C
ATOM 1033 SD MET A 165 -46.106 20.855 45.869 1.00124.02 S
ANISOU 1033 SD MET A 165 18050 15696 13375 592 3198 -1788 S
ATOM 1034 CE MET A 165 -44.935 22.046 46.467 1.00122.13 C
ANISOU 1034 CE MET A 165 17937 15390 13077 389 3319 -1947 C
ATOM 1035 N VAL A 166 -49.099 17.931 49.234 1.00114.46 N
ANISOU 1035 N VAL A 166 16734 14772 11983 601 3093 -1761 N
ATOM 1036 CA VAL A 166 -50.015 18.483 50.240 1.00115.44 C
ANISOU 1036 CA VAL A 166 16940 14831 12090 576 3245 -1830 C
ATOM 1037 C VAL A 166 -49.863 17.758 51.591 1.00119.86 C
ANISOU 1037 C VAL A 166 17556 15474 12511 447 3202 -1880 C
ATOM 1038 O VAL A 166 -49.755 18.417 52.626 1.00120.63 O
ANISOU 1038 O VAL A 166 17769 15531 12534 331 3297 -1975 O
ATOM 1039 CB VAL A 166 -51.492 18.501 49.739 1.00119.33 C
ANISOU 1039 CB VAL A 166 17363 15284 12693 737 3331 -1780 C
ATOM 1040 CG1 VAL A 166 -52.412 19.215 50.728 1.00120.47 C
ANISOU 1040 CG1 VAL A 166 17590 15343 12841 720 3517 -1859 C
ATOM 1041 CG2 VAL A 166 -51.605 19.142 48.356 1.00118.95 C
ANISOU 1041 CG2 VAL A 166 17266 15171 12760 883 3349 -1713 C
ATOM 1042 N LEU A 167 -49.839 16.412 51.569 1.00115.71 N
ANISOU 1042 N LEU A 167 16966 15058 11941 465 3068 -1815 N
ATOM 1043 CA LEU A 167 -49.746 15.569 52.765 1.00116.03 C
ANISOU 1043 CA LEU A 167 17074 15174 11839 372 3021 -1838 C
ATOM 1044 C LEU A 167 -48.357 15.512 53.412 1.00121.02 C
ANISOU 1044 C LEU A 167 17758 15889 12335 250 2906 -1872 C
ATOM 1045 O LEU A 167 -48.271 15.271 54.618 1.00121.43 O
ANISOU 1045 O LEU A 167 17909 15982 12247 153 2902 -1919 O
ATOM 1046 CB LEU A 167 -50.259 14.150 52.472 1.00115.15 C
ANISOU 1046 CB LEU A 167 16895 15131 11727 443 2948 -1755 C
ATOM 1047 CG LEU A 167 -51.754 14.023 52.170 1.00119.77 C
ANISOU 1047 CG LEU A 167 17424 15674 12409 527 3063 -1749 C
ATOM 1048 CD1 LEU A 167 -52.048 12.747 51.428 1.00118.93 C
ANISOU 1048 CD1 LEU A 167 17223 15638 12326 593 2984 -1668 C
ATOM 1049 CD2 LEU A 167 -52.588 14.104 53.432 1.00123.39 C
ANISOU 1049 CD2 LEU A 167 17984 16094 12805 455 3197 -1830 C
ATOM 1050 N ARG A 168 -47.281 15.721 52.629 1.00117.78 N
ANISOU 1050 N ARG A 168 17279 15512 11958 253 2812 -1853 N
ATOM 1051 CA ARG A 168 -45.906 15.688 53.136 1.00118.52 C
ANISOU 1051 CA ARG A 168 17382 15713 11935 144 2692 -1893 C
ATOM 1052 C ARG A 168 -45.560 16.924 53.961 1.00124.82 C
ANISOU 1052 C ARG A 168 18280 16478 12665 -8 2790 -2029 C
ATOM 1053 O ARG A 168 -45.753 18.048 53.495 1.00124.60 O
ANISOU 1053 O ARG A 168 18279 16333 12731 -16 2928 -2080 O
ATOM 1054 CB ARG A 168 -44.894 15.491 51.997 1.00117.66 C
ANISOU 1054 CB ARG A 168 17155 15651 11899 190 2577 -1841 C
ATOM 1055 CG ARG A 168 -44.702 14.036 51.602 1.00126.06 C
ANISOU 1055 CG ARG A 168 18141 16803 12954 284 2435 -1723 C
ATOM 1056 CD ARG A 168 -43.450 13.445 52.212 1.00135.29 C
ANISOU 1056 CD ARG A 168 19287 18121 13995 232 2276 -1722 C
ATOM 1057 NE ARG A 168 -43.348 12.010 51.948 1.00142.08 N
ANISOU 1057 NE ARG A 168 20103 19044 14838 336 2168 -1602 N
ATOM 1058 CZ ARG A 168 -42.311 11.255 52.292 1.00156.29 C
ANISOU 1058 CZ ARG A 168 21867 20974 16543 347 2021 -1562 C
ATOM 1059 NH1 ARG A 168 -42.307 9.959 52.016 1.00142.85 N
ANISOU 1059 NH1 ARG A 168 20148 19299 14831 454 1956 -1446 N
ATOM 1060 NH2 ARG A 168 -41.267 11.791 52.912 1.00144.11 N
ANISOU 1060 NH2 ARG A 168 20304 19541 14912 252 1943 -1640 N
ATOM 1061 N THR A 169 -45.056 16.703 55.193 1.00123.30 N
ANISOU 1061 N THR A 169 18158 16390 12300 -130 2726 -2085 N
ATOM 1062 CA THR A 169 -44.647 17.742 56.150 1.00125.15 C
ANISOU 1062 CA THR A 169 18497 16625 12428 -311 2806 -2227 C
ATOM 1063 C THR A 169 -43.536 17.246 57.078 1.00131.13 C
ANISOU 1063 C THR A 169 19255 17579 12991 -421 2631 -2260 C
ATOM 1064 O THR A 169 -43.512 16.066 57.434 1.00130.46 O
ANISOU 1064 O THR A 169 19159 17591 12820 -352 2496 -2171 O
ATOM 1065 CB THR A 169 -45.842 18.267 56.976 1.00133.53 C
ANISOU 1065 CB THR A 169 19704 17560 13471 -354 3001 -2287 C
ATOM 1066 OG1 THR A 169 -46.830 17.245 57.127 1.00132.26 O
ANISOU 1066 OG1 THR A 169 19548 17388 13317 -245 2992 -2198 O
ATOM 1067 CG2 THR A 169 -46.462 19.521 56.383 1.00132.12 C
ANISOU 1067 CG2 THR A 169 19560 17197 13441 -331 3216 -2335 C
ATOM 1068 N THR A 170 -42.629 18.157 57.478 1.00129.91 N
ANISOU 1068 N THR A 170 19117 17484 12760 -593 2640 -2392 N
ATOM 1069 CA THR A 170 -41.520 17.863 58.393 1.00131.62 C
ANISOU 1069 CA THR A 170 19317 17916 12778 -714 2470 -2446 C
ATOM 1070 C THR A 170 -41.962 17.964 59.852 1.00137.99 C
ANISOU 1070 C THR A 170 20293 18741 13396 -839 2520 -2515 C
ATOM 1071 O THR A 170 -42.867 18.737 60.175 1.00137.87 O
ANISOU 1071 O THR A 170 20410 18562 13412 -902 2731 -2583 O
ATOM 1072 CB THR A 170 -40.305 18.763 58.115 1.00140.70 C
ANISOU 1072 CB THR A 170 20385 19148 13926 -862 2455 -2573 C
ATOM 1073 OG1 THR A 170 -40.737 20.087 57.797 1.00140.54 O
ANISOU 1073 OG1 THR A 170 20454 18938 14006 -949 2696 -2677 O
ATOM 1074 CG2 THR A 170 -39.415 18.217 57.018 1.00138.33 C
ANISOU 1074 CG2 THR A 170 19895 18936 13727 -756 2306 -2499 C
ATOM 1075 N GLY A 171 -41.310 17.186 60.713 1.00136.39 N
ANISOU 1075 N GLY A 171 20091 18736 12997 -867 2330 -2493 N
ATOM 1076 CA GLY A 171 -41.591 17.153 62.143 1.00138.21 C
ANISOU 1076 CA GLY A 171 20491 19010 13011 -988 2344 -2550 C
ATOM 1077 C GLY A 171 -41.025 15.943 62.855 1.00143.79 C
ANISOU 1077 C GLY A 171 21196 19919 13518 -926 2109 -2458 C
ATOM 1078 O GLY A 171 -40.615 14.970 62.214 1.00142.37 O
ANISOU 1078 O GLY A 171 20890 19814 13389 -754 1955 -2326 O
ATOM 1079 N ASP A 172 -41.006 16.001 64.197 1.00143.03 N
ANISOU 1079 N ASP A 172 21254 19905 13187 -1061 2091 -2525 N
ATOM 1080 CA ASP A 172 -40.505 14.927 65.054 1.00144.47 C
ANISOU 1080 CA ASP A 172 21478 20278 13137 -1006 1876 -2439 C
ATOM 1081 C ASP A 172 -41.513 13.784 65.170 1.00147.96 C
ANISOU 1081 C ASP A 172 22043 20595 13580 -837 1914 -2291 C
ATOM 1082 O ASP A 172 -42.708 14.029 65.353 1.00146.93 O
ANISOU 1082 O ASP A 172 22052 20264 13511 -868 2125 -2319 O
ATOM 1083 CB ASP A 172 -40.111 15.468 66.443 1.00149.01 C
ANISOU 1083 CB ASP A 172 22186 20990 13440 -1228 1845 -2573 C
ATOM 1084 CG ASP A 172 -41.224 16.179 67.191 1.00159.87 C
ANISOU 1084 CG ASP A 172 23792 22169 14782 -1381 2098 -2676 C
ATOM 1085 OD1 ASP A 172 -41.634 17.274 66.746 1.00159.91 O
ANISOU 1085 OD1 ASP A 172 23796 22014 14949 -1479 2310 -2785 O
ATOM 1086 OD2 ASP A 172 -41.664 15.655 68.237 1.00166.85 O
ANISOU 1086 OD2 ASP A 172 24867 23056 15473 -1402 2094 -2649 O
ATOM 1087 N LEU A 173 -41.027 12.536 65.048 1.00144.98 N
ANISOU 1087 N LEU A 173 21613 20333 13139 -659 1723 -2138 N
ATOM 1088 CA LEU A 173 -41.855 11.332 65.138 1.00144.29 C
ANISOU 1088 CA LEU A 173 21650 20138 13036 -500 1757 -1995 C
ATOM 1089 C LEU A 173 -41.676 10.648 66.495 1.00150.86 C
ANISOU 1089 C LEU A 173 22678 21079 13562 -512 1652 -1955 C
ATOM 1090 O LEU A 173 -42.654 10.490 67.228 1.00150.73 O
ANISOU 1090 O LEU A 173 22880 20929 13463 -561 1798 -1969 O
ATOM 1091 CB LEU A 173 -41.549 10.357 63.982 1.00142.79 C
ANISOU 1091 CB LEU A 173 21302 19956 12996 -282 1661 -1842 C
ATOM 1092 CG LEU A 173 -42.001 10.787 62.585 1.00145.28 C
ANISOU 1092 CG LEU A 173 21467 20124 13607 -239 1785 -1851 C
ATOM 1093 CD1 LEU A 173 -41.032 10.300 61.528 1.00144.69 C
ANISOU 1093 CD1 LEU A 173 21183 20149 13641 -103 1632 -1761 C
ATOM 1094 CD2 LEU A 173 -43.410 10.298 62.282 1.00146.34 C
ANISOU 1094 CD2 LEU A 173 21699 20050 13854 -168 1970 -1799 C
ATOM 1095 N CYS A 174 -40.427 10.264 66.832 1.00149.52 N
ANISOU 1095 N CYS A 174 22430 21158 13222 -465 1402 -1908 N
ATOM 1096 CA CYS A 174 -40.061 9.601 68.088 1.00151.93 C
ANISOU 1096 CA CYS A 174 22906 21610 13211 -449 1257 -1852 C
ATOM 1097 C CYS A 174 -38.715 10.100 68.625 1.00158.34 C
ANISOU 1097 C CYS A 174 23597 22725 13841 -545 1029 -1928 C
ATOM 1098 O CYS A 174 -38.543 10.197 69.842 1.00160.18 O
ANISOU 1098 O CYS A 174 23987 23077 13798 -653 960 -1973 O
ATOM 1099 CB CYS A 174 -40.063 8.083 67.922 1.00152.04 C
ANISOU 1099 CB CYS A 174 22976 21611 13183 -193 1172 -1644 C
ATOM 1100 SG CYS A 174 -41.714 7.340 67.840 1.00154.29 S
ANISOU 1100 SG CYS A 174 23492 21575 13555 -133 1443 -1578 S
ATOM 1101 N ASN A 175 -37.764 10.400 67.714 1.00154.60 N
ANISOU 1101 N ASN A 175 22844 22383 13514 -512 914 -1948 N
ATOM 1102 CA ASN A 175 -36.407 10.866 68.021 1.00156.65 C
ANISOU 1102 CA ASN A 175 22925 22953 13641 -601 696 -2034 C
ATOM 1103 C ASN A 175 -36.340 12.227 68.724 1.00162.04 C
ANISOU 1103 C ASN A 175 23655 23693 14222 -913 775 -2261 C
ATOM 1104 O ASN A 175 -35.394 12.463 69.478 1.00164.23 O
ANISOU 1104 O ASN A 175 23875 24249 14274 -1018 590 -2336 O
ATOM 1105 CB ASN A 175 -35.546 10.875 66.759 1.00156.46 C
ANISOU 1105 CB ASN A 175 22596 23011 13841 -502 608 -2014 C
ATOM 1106 N THR A 176 -37.331 13.118 68.463 1.00157.12 N
ANISOU 1106 N THR A 176 23129 22810 13760 -1059 1053 -2371 N
ATOM 1107 CA THR A 176 -37.488 14.483 69.002 1.00157.97 C
ANISOU 1107 CA THR A 176 23317 22887 13817 -1357 1209 -2589 C
ATOM 1108 C THR A 176 -36.401 15.447 68.489 1.00162.32 C
ANISOU 1108 C THR A 176 23633 23604 14437 -1507 1155 -2743 C
ATOM 1109 O THR A 176 -36.741 16.455 67.868 1.00160.76 O
ANISOU 1109 O THR A 176 23416 23233 14432 -1627 1369 -2860 O
ATOM 1110 CB THR A 176 -37.622 14.501 70.536 1.00168.75 C
ANISOU 1110 CB THR A 176 24920 24344 14853 -1506 1179 -2645 C
ATOM 1111 N ASN A 177 -35.111 15.142 68.747 1.00160.69 N
ANISOU 1111 N ASN A 177 23252 23730 14073 -1497 881 -2746 N
ATOM 1112 CA ASN A 177 -33.965 15.950 68.318 1.00161.43 C
ANISOU 1112 CA ASN A 177 23101 24023 14211 -1647 810 -2904 C
ATOM 1113 C ASN A 177 -33.748 15.894 66.801 1.00162.58 C
ANISOU 1113 C ASN A 177 23034 24066 14674 -1503 849 -2849 C
ATOM 1114 O ASN A 177 -33.266 16.868 66.220 1.00162.15 O
ANISOU 1114 O ASN A 177 22850 24017 14741 -1664 938 -3007 O
ATOM 1115 CB ASN A 177 -32.698 15.519 69.054 1.00165.30 C
ANISOU 1115 CB ASN A 177 23448 24921 14438 -1651 490 -2911 C
ATOM 1116 N LYS A 178 -34.103 14.757 66.167 1.00156.96 N
ANISOU 1116 N LYS A 178 22302 23251 14084 -1213 797 -2633 N
ATOM 1117 CA LYS A 178 -33.967 14.546 64.726 1.00154.35 C
ANISOU 1117 CA LYS A 178 21791 22813 14041 -1058 830 -2559 C
ATOM 1118 C LYS A 178 -35.325 14.626 64.021 1.00154.91 C
ANISOU 1118 C LYS A 178 22005 22526 14330 -988 1083 -2496 C
ATOM 1119 O LYS A 178 -36.228 13.843 64.327 1.00153.67 O
ANISOU 1119 O LYS A 178 22011 22240 14137 -857 1120 -2365 O
ATOM 1120 CB LYS A 178 -33.273 13.204 64.437 1.00157.03 C
ANISOU 1120 CB LYS A 178 21982 23316 14364 -788 588 -2369 C
ATOM 1121 N VAL A 179 -35.467 15.590 63.091 1.00149.79 N
ANISOU 1121 N VAL A 179 21296 21721 13898 -1078 1263 -2596 N
ATOM 1122 CA VAL A 179 -36.694 15.809 62.311 1.00146.98 C
ANISOU 1122 CA VAL A 179 21040 21047 13759 -1009 1498 -2549 C
ATOM 1123 C VAL A 179 -36.679 15.000 61.011 1.00148.10 C
ANISOU 1123 C VAL A 179 21042 21118 14111 -777 1454 -2393 C
ATOM 1124 O VAL A 179 -35.627 14.871 60.384 1.00147.84 O
ANISOU 1124 O VAL A 179 20811 21224 14137 -743 1327 -2393 O
ATOM 1125 CB VAL A 179 -37.033 17.307 62.069 1.00150.87 C
ANISOU 1125 CB VAL A 179 21594 21374 14355 -1211 1746 -2725 C
ATOM 1126 CG1 VAL A 179 -37.563 17.965 63.339 1.00152.29 C
ANISOU 1126 CG1 VAL A 179 21987 21523 14355 -1409 1866 -2846 C
ATOM 1127 CG2 VAL A 179 -35.844 18.084 61.501 1.00151.52 C
ANISOU 1127 CG2 VAL A 179 21498 21579 14493 -1343 1717 -2862 C
ATOM 1128 N GLN A 180 -37.843 14.455 60.613 1.00142.30 N
ANISOU 1128 N GLN A 180 20408 20172 13487 -631 1565 -2270 N
ATOM 1129 CA GLN A 180 -37.965 13.639 59.404 1.00139.86 C
ANISOU 1129 CA GLN A 180 19994 19783 13364 -425 1541 -2123 C
ATOM 1130 C GLN A 180 -39.115 14.062 58.492 1.00141.02 C
ANISOU 1130 C GLN A 180 20190 19670 13723 -386 1756 -2110 C
ATOM 1131 O GLN A 180 -40.184 14.442 58.973 1.00140.45 O
ANISOU 1131 O GLN A 180 20271 19457 13636 -437 1913 -2145 O
ATOM 1132 CB GLN A 180 -38.091 12.153 59.768 1.00141.19 C
ANISOU 1132 CB GLN A 180 20207 20009 13429 -242 1411 -1952 C
ATOM 1133 N CYS A 181 -38.884 13.979 57.169 1.00135.63 N
ANISOU 1133 N CYS A 181 19371 18930 13232 -291 1759 -2058 N
ATOM 1134 CA CYS A 181 -39.856 14.295 56.121 1.00133.35 C
ANISOU 1134 CA CYS A 181 19097 18423 13144 -224 1928 -2027 C
ATOM 1135 C CYS A 181 -40.722 13.045 55.905 1.00135.03 C
ANISOU 1135 C CYS A 181 19349 18572 13386 -52 1917 -1872 C
ATOM 1136 O CYS A 181 -40.201 11.998 55.509 1.00134.18 O
ANISOU 1136 O CYS A 181 19158 18542 13281 68 1788 -1762 O
ATOM 1137 CB CYS A 181 -39.134 14.724 54.842 1.00132.94 C
ANISOU 1137 CB CYS A 181 18900 18355 13257 -211 1927 -2044 C
ATOM 1138 SG CYS A 181 -40.216 14.999 53.413 1.00134.74 S
ANISOU 1138 SG CYS A 181 19136 18343 13717 -98 2096 -1980 S
ATOM 1139 N TYR A 182 -42.031 13.142 56.220 1.00130.45 N
ANISOU 1139 N TYR A 182 18896 17851 12817 -49 2066 -1872 N
ATOM 1140 CA TYR A 182 -42.976 12.023 56.113 1.00128.95 C
ANISOU 1140 CA TYR A 182 18756 17596 12643 78 2090 -1756 C
ATOM 1141 C TYR A 182 -44.366 12.433 55.598 1.00130.97 C
ANISOU 1141 C TYR A 182 19045 17676 13042 107 2277 -1767 C
ATOM 1142 O TYR A 182 -44.691 13.622 55.577 1.00130.68 O
ANISOU 1142 O TYR A 182 19031 17555 13066 32 2402 -1862 O
ATOM 1143 CB TYR A 182 -43.081 11.274 57.463 1.00131.38 C
ANISOU 1143 CB TYR A 182 19204 17975 12738 59 2037 -1734 C
ATOM 1144 CG TYR A 182 -43.797 12.038 58.560 1.00134.15 C
ANISOU 1144 CG TYR A 182 19710 18266 12996 -76 2168 -1845 C
ATOM 1145 CD1 TYR A 182 -43.117 12.956 59.356 1.00137.68 C
ANISOU 1145 CD1 TYR A 182 20192 18795 13324 -232 2145 -1964 C
ATOM 1146 CD2 TYR A 182 -45.142 11.809 58.834 1.00134.52 C
ANISOU 1146 CD2 TYR A 182 19869 18179 13064 -60 2323 -1839 C
ATOM 1147 CE1 TYR A 182 -43.769 13.658 60.370 1.00139.53 C
ANISOU 1147 CE1 TYR A 182 20584 18963 13468 -368 2282 -2070 C
ATOM 1148 CE2 TYR A 182 -45.805 12.505 59.843 1.00136.49 C
ANISOU 1148 CE2 TYR A 182 20264 18362 13236 -185 2461 -1944 C
ATOM 1149 CZ TYR A 182 -45.113 13.427 60.612 1.00145.43 C
ANISOU 1149 CZ TYR A 182 21444 19561 14250 -338 2443 -2056 C
ATOM 1150 OH TYR A 182 -45.760 14.110 61.614 1.00147.66 O
ANISOU 1150 OH TYR A 182 21885 19768 14452 -473 2594 -2163 O
ATOM 1151 N MET A 183 -45.187 11.434 55.210 1.00126.11 N
ANISOU 1151 N MET A 183 18432 17010 12474 216 2304 -1673 N
ATOM 1152 CA MET A 183 -46.558 11.623 54.732 1.00124.94 C
ANISOU 1152 CA MET A 183 18287 16732 12451 257 2462 -1677 C
ATOM 1153 C MET A 183 -47.512 11.704 55.930 1.00129.38 C
ANISOU 1153 C MET A 183 18995 17244 12919 187 2584 -1740 C
ATOM 1154 O MET A 183 -47.751 10.694 56.600 1.00129.24 O
ANISOU 1154 O MET A 183 19067 17251 12785 195 2566 -1699 O
ATOM 1155 CB MET A 183 -46.969 10.477 53.786 1.00125.98 C
ANISOU 1155 CB MET A 183 18348 16855 12664 377 2439 -1567 C
ATOM 1156 CG MET A 183 -46.520 10.673 52.352 1.00128.45 C
ANISOU 1156 CG MET A 183 18520 17161 13126 446 2392 -1523 C
ATOM 1157 SD MET A 183 -47.635 11.714 51.376 1.00131.92 S
ANISOU 1157 SD MET A 183 18896 17482 13746 487 2537 -1558 S
ATOM 1158 CE MET A 183 -48.905 10.532 50.954 1.00127.85 C
ANISOU 1158 CE MET A 183 18352 16955 13271 564 2589 -1494 C
ATOM 1159 N ASP A 184 -48.030 12.912 56.216 1.00126.28 N
ANISOU 1159 N ASP A 184 18642 16767 12571 117 2723 -1840 N
ATOM 1160 CA ASP A 184 -48.956 13.149 57.326 1.00126.98 C
ANISOU 1160 CA ASP A 184 18870 16790 12589 39 2868 -1916 C
ATOM 1161 C ASP A 184 -50.404 13.104 56.824 1.00129.96 C
ANISOU 1161 C ASP A 184 19203 17065 13112 118 3021 -1912 C
ATOM 1162 O ASP A 184 -50.913 14.094 56.292 1.00129.42 O
ANISOU 1162 O ASP A 184 19078 16915 13180 149 3131 -1950 O
ATOM 1163 CB ASP A 184 -48.629 14.473 58.046 1.00130.07 C
ANISOU 1163 CB ASP A 184 19344 17148 12928 -96 2947 -2037 C
ATOM 1164 CG ASP A 184 -49.494 14.748 59.260 1.00140.91 C
ANISOU 1164 CG ASP A 184 20877 18446 14215 -194 3105 -2124 C
ATOM 1165 OD1 ASP A 184 -49.247 14.128 60.318 1.00142.19 O
ANISOU 1165 OD1 ASP A 184 21162 18672 14189 -269 3049 -2129 O
ATOM 1166 OD2 ASP A 184 -50.410 15.590 59.156 1.00146.92 O
ANISOU 1166 OD2 ASP A 184 21648 19084 15093 -191 3291 -2183 O
ATOM 1167 N TYR A 185 -51.056 11.938 56.993 1.00126.11 N
ANISOU 1167 N TYR A 185 18740 16589 12588 152 3032 -1867 N
ATOM 1168 CA TYR A 185 -52.433 11.668 56.561 1.00125.47 C
ANISOU 1168 CA TYR A 185 18596 16448 12627 213 3165 -1872 C
ATOM 1169 C TYR A 185 -53.510 12.355 57.417 1.00130.20 C
ANISOU 1169 C TYR A 185 19276 16955 13238 149 3364 -1979 C
ATOM 1170 O TYR A 185 -54.668 12.410 56.997 1.00129.65 O
ANISOU 1170 O TYR A 185 19119 16844 13296 207 3484 -2001 O
ATOM 1171 CB TYR A 185 -52.690 10.149 56.482 1.00126.20 C
ANISOU 1171 CB TYR A 185 18703 16584 12665 244 3127 -1804 C
ATOM 1172 CG TYR A 185 -51.764 9.413 55.537 1.00126.88 C
ANISOU 1172 CG TYR A 185 18703 16744 12762 321 2961 -1695 C
ATOM 1173 CD1 TYR A 185 -52.040 9.338 54.175 1.00127.73 C
ANISOU 1173 CD1 TYR A 185 18648 16859 13024 411 2944 -1648 C
ATOM 1174 CD2 TYR A 185 -50.624 8.769 56.008 1.00127.92 C
ANISOU 1174 CD2 TYR A 185 18917 16941 12745 309 2824 -1636 C
ATOM 1175 CE1 TYR A 185 -51.191 8.660 53.301 1.00127.58 C
ANISOU 1175 CE1 TYR A 185 18562 16895 13019 472 2810 -1553 C
ATOM 1176 CE2 TYR A 185 -49.767 8.087 55.145 1.00127.96 C
ANISOU 1176 CE2 TYR A 185 18841 17008 12772 388 2687 -1537 C
ATOM 1177 CZ TYR A 185 -50.056 8.034 53.790 1.00134.02 C
ANISOU 1177 CZ TYR A 185 19457 17764 13701 461 2689 -1499 C
ATOM 1178 OH TYR A 185 -49.217 7.362 52.934 1.00133.89 O
ANISOU 1178 OH TYR A 185 19370 17794 13707 528 2573 -1406 O
ATOM 1179 N SER A 186 -53.125 12.893 58.597 1.00127.81 N
ANISOU 1179 N SER A 186 19131 16628 12802 27 3401 -2051 N
ATOM 1180 CA SER A 186 -53.995 13.577 59.566 1.00128.85 C
ANISOU 1180 CA SER A 186 19376 16661 12922 -60 3600 -2162 C
ATOM 1181 C SER A 186 -54.801 14.757 58.999 1.00132.58 C
ANISOU 1181 C SER A 186 19749 17037 13586 5 3757 -2211 C
ATOM 1182 O SER A 186 -55.855 15.091 59.546 1.00133.08 O
ANISOU 1182 O SER A 186 19855 17016 13692 -21 3947 -2288 O
ATOM 1183 CB SER A 186 -53.183 14.035 60.774 1.00133.72 C
ANISOU 1183 CB SER A 186 20173 17285 13350 -211 3583 -2226 C
ATOM 1184 OG SER A 186 -52.546 12.942 61.414 1.00142.80 O
ANISOU 1184 OG SER A 186 21427 18524 14305 -251 3446 -2175 O
ATOM 1185 N MET A 187 -54.303 15.380 57.913 1.00128.14 N
ANISOU 1185 N MET A 187 19067 16484 13137 94 3688 -2164 N
ATOM 1186 CA MET A 187 -54.923 16.523 57.235 1.00128.06 C
ANISOU 1186 CA MET A 187 18973 16382 13302 188 3819 -2184 C
ATOM 1187 C MET A 187 -56.267 16.180 56.581 1.00131.13 C
ANISOU 1187 C MET A 187 19213 16769 13841 322 3897 -2161 C
ATOM 1188 O MET A 187 -57.200 16.982 56.660 1.00131.60 O
ANISOU 1188 O MET A 187 19251 16743 14007 374 4072 -2213 O
ATOM 1189 CB MET A 187 -53.968 17.108 56.176 1.00129.68 C
ANISOU 1189 CB MET A 187 19105 16599 13568 251 3711 -2128 C
ATOM 1190 CG MET A 187 -52.737 17.770 56.756 1.00133.97 C
ANISOU 1190 CG MET A 187 19771 17140 13993 112 3676 -2183 C
ATOM 1191 SD MET A 187 -51.578 18.296 55.472 1.00137.34 S
ANISOU 1191 SD MET A 187 20108 17587 14490 169 3555 -2128 S
ATOM 1192 CE MET A 187 -50.272 18.945 56.478 1.00135.22 C
ANISOU 1192 CE MET A 187 19982 17344 14053 -43 3536 -2234 C
ATOM 1193 N VAL A 188 -56.362 15.004 55.931 1.00126.22 N
ANISOU 1193 N VAL A 188 18484 16248 13226 377 3775 -2088 N
ATOM 1194 CA VAL A 188 -57.567 14.576 55.210 1.00125.71 C
ANISOU 1194 CA VAL A 188 18253 16219 13290 488 3825 -2074 C
ATOM 1195 C VAL A 188 -58.353 13.455 55.918 1.00129.47 C
ANISOU 1195 C VAL A 188 18761 16728 13703 411 3893 -2122 C
ATOM 1196 O VAL A 188 -59.575 13.394 55.768 1.00129.64 O
ANISOU 1196 O VAL A 188 18673 16759 13828 458 4013 -2168 O
ATOM 1197 CB VAL A 188 -57.277 14.211 53.727 1.00128.36 C
ANISOU 1197 CB VAL A 188 18426 16638 13707 609 3672 -1970 C
ATOM 1198 CG1 VAL A 188 -56.950 15.457 52.907 1.00128.18 C
ANISOU 1198 CG1 VAL A 188 18356 16560 13787 716 3668 -1935 C
ATOM 1199 CG2 VAL A 188 -56.173 13.163 53.596 1.00127.07 C
ANISOU 1199 CG2 VAL A 188 18306 16546 13427 553 3496 -1901 C
ATOM 1200 N ALA A 189 -57.662 12.572 56.664 1.00125.46 N
ANISOU 1200 N ALA A 189 18403 16241 13025 298 3822 -2112 N
ATOM 1201 CA ALA A 189 -58.277 11.443 57.371 1.00125.51 C
ANISOU 1201 CA ALA A 189 18487 16258 12942 216 3895 -2151 C
ATOM 1202 C ALA A 189 -58.957 11.842 58.685 1.00130.41 C
ANISOU 1202 C ALA A 189 19253 16786 13512 108 4089 -2268 C
ATOM 1203 O ALA A 189 -58.673 12.913 59.227 1.00130.67 O
ANISOU 1203 O ALA A 189 19370 16748 13532 72 4143 -2311 O
ATOM 1204 CB ALA A 189 -57.234 10.366 57.633 1.00125.67 C
ANISOU 1204 CB ALA A 189 18632 16326 12792 164 3747 -2078 C
ATOM 1205 N THR A 190 -59.840 10.957 59.205 1.00127.20 N
ANISOU 1205 N THR A 190 18890 16372 13067 42 4210 -2327 N
ATOM 1206 CA THR A 190 -60.545 11.149 60.480 1.00128.31 C
ANISOU 1206 CA THR A 190 19186 16417 13148 -77 4413 -2445 C
ATOM 1207 C THR A 190 -59.642 10.682 61.644 1.00132.26 C
ANISOU 1207 C THR A 190 19962 16887 13404 -205 4360 -2433 C
ATOM 1208 O THR A 190 -58.420 10.832 61.566 1.00131.25 O
ANISOU 1208 O THR A 190 19883 16799 13185 -193 4182 -2355 O
ATOM 1209 CB THR A 190 -61.936 10.467 60.470 1.00136.26 C
ANISOU 1209 CB THR A 190 20107 17432 14235 -98 4585 -2530 C
ATOM 1210 OG1 THR A 190 -61.788 9.064 60.254 1.00134.88 O
ANISOU 1210 OG1 THR A 190 19967 17314 13966 -128 4518 -2485 O
ATOM 1211 CG2 THR A 190 -62.898 11.076 59.456 1.00134.68 C
ANISOU 1211 CG2 THR A 190 19623 17281 14267 34 4641 -2555 C
ATOM 1212 N VAL A 191 -60.238 10.122 62.714 1.00129.72 N
ANISOU 1212 N VAL A 191 19818 16499 12970 -325 4514 -2513 N
ATOM 1213 CA VAL A 191 -59.508 9.635 63.885 1.00130.10 C
ANISOU 1213 CA VAL A 191 20149 16519 12766 -439 4476 -2501 C
ATOM 1214 C VAL A 191 -58.985 8.204 63.707 1.00132.92 C
ANISOU 1214 C VAL A 191 20580 16934 12990 -416 4350 -2400 C
ATOM 1215 O VAL A 191 -57.968 7.854 64.309 1.00132.75 O
ANISOU 1215 O VAL A 191 20737 16935 12767 -442 4220 -2332 O
ATOM 1216 CB VAL A 191 -60.349 9.777 65.170 1.00135.74 C
ANISOU 1216 CB VAL A 191 21058 17114 13404 -584 4715 -2633 C
ATOM 1217 N SER A 192 -59.672 7.383 62.890 1.00128.52 N
ANISOU 1217 N SER A 192 19886 16406 12539 -364 4394 -2391 N
ATOM 1218 CA SER A 192 -59.292 5.987 62.660 1.00127.76 C
ANISOU 1218 CA SER A 192 19869 16343 12331 -344 4319 -2302 C
ATOM 1219 C SER A 192 -58.984 5.644 61.201 1.00129.53 C
ANISOU 1219 C SER A 192 19865 16664 12686 -221 4175 -2208 C
ATOM 1220 O SER A 192 -58.309 4.645 60.950 1.00128.61 O
ANISOU 1220 O SER A 192 19818 16577 12471 -184 4071 -2107 O
ATOM 1221 CB SER A 192 -60.366 5.049 63.202 1.00132.47 C
ANISOU 1221 CB SER A 192 20591 16866 12877 -445 4542 -2391 C
ATOM 1222 OG SER A 192 -61.601 5.239 62.533 1.00141.40 O
ANISOU 1222 OG SER A 192 21493 18015 14218 -444 4687 -2492 O
ATOM 1223 N SER A 193 -59.464 6.464 60.244 1.00124.99 N
ANISOU 1223 N SER A 193 19031 16133 12325 -151 4174 -2236 N
ATOM 1224 CA SER A 193 -59.276 6.237 58.807 1.00123.17 C
ANISOU 1224 CA SER A 193 18580 15994 12224 -42 4049 -2158 C
ATOM 1225 C SER A 193 -57.867 6.595 58.275 1.00125.25 C
ANISOU 1225 C SER A 193 18814 16306 12467 45 3819 -2036 C
ATOM 1226 O SER A 193 -57.701 6.763 57.063 1.00123.72 O
ANISOU 1226 O SER A 193 18430 16176 12403 138 3722 -1981 O
ATOM 1227 CB SER A 193 -60.362 6.955 58.009 1.00126.70 C
ANISOU 1227 CB SER A 193 18774 16478 12888 11 4133 -2230 C
ATOM 1228 OG SER A 193 -60.243 8.364 58.119 1.00135.66 O
ANISOU 1228 OG SER A 193 19859 17583 14104 55 4127 -2250 O
ATOM 1229 N GLU A 194 -56.855 6.671 59.169 1.00121.73 N
ANISOU 1229 N GLU A 194 18555 15842 11853 10 3733 -1997 N
ATOM 1230 CA GLU A 194 -55.465 6.979 58.810 1.00120.58 C
ANISOU 1230 CA GLU A 194 18384 15756 11673 73 3522 -1900 C
ATOM 1231 C GLU A 194 -54.823 5.862 57.982 1.00122.79 C
ANISOU 1231 C GLU A 194 18624 16094 11935 150 3396 -1782 C
ATOM 1232 O GLU A 194 -54.087 6.156 57.038 1.00121.25 O
ANISOU 1232 O GLU A 194 18291 15955 11824 229 3257 -1715 O
ATOM 1233 CB GLU A 194 -54.621 7.306 60.052 1.00123.02 C
ANISOU 1233 CB GLU A 194 18892 16059 11793 2 3466 -1906 C
ATOM 1234 CG GLU A 194 -54.928 8.672 60.644 1.00134.34 C
ANISOU 1234 CG GLU A 194 20340 17441 13261 -71 3560 -2014 C
ATOM 1235 CD GLU A 194 -53.883 9.220 61.596 1.00155.30 C
ANISOU 1235 CD GLU A 194 23139 20123 15747 -145 3466 -2023 C
ATOM 1236 OE1 GLU A 194 -53.356 10.322 61.322 1.00149.19 O
ANISOU 1236 OE1 GLU A 194 22283 19366 15038 -149 3417 -2048 O
ATOM 1237 OE2 GLU A 194 -53.599 8.559 62.622 1.00150.28 O
ANISOU 1237 OE2 GLU A 194 22705 19492 14904 -205 3448 -2010 O
ATOM 1238 N TRP A 195 -55.120 4.589 58.322 1.00119.28 N
ANISOU 1238 N TRP A 195 18315 15623 11384 124 3467 -1761 N
ATOM 1239 CA TRP A 195 -54.623 3.421 57.587 1.00118.13 C
ANISOU 1239 CA TRP A 195 18161 15506 11216 191 3392 -1654 C
ATOM 1240 C TRP A 195 -55.351 3.286 56.247 1.00119.79 C
ANISOU 1240 C TRP A 195 18156 15746 11612 221 3436 -1669 C
ATOM 1241 O TRP A 195 -54.739 2.872 55.263 1.00118.32 O
ANISOU 1241 O TRP A 195 17880 15603 11472 292 3329 -1581 O
ATOM 1242 CB TRP A 195 -54.751 2.126 58.417 1.00118.01 C
ANISOU 1242 CB TRP A 195 18391 15430 11016 152 3487 -1630 C
ATOM 1243 CG TRP A 195 -56.154 1.770 58.819 1.00119.83 C
ANISOU 1243 CG TRP A 195 18686 15588 11256 46 3723 -1748 C
ATOM 1244 CD1 TRP A 195 -56.787 2.121 59.974 1.00124.01 C
ANISOU 1244 CD1 TRP A 195 19358 16050 11708 -52 3859 -1849 C
ATOM 1245 CD2 TRP A 195 -57.089 0.974 58.074 1.00119.46 C
ANISOU 1245 CD2 TRP A 195 18561 15534 11296 13 3860 -1791 C
ATOM 1246 NE1 TRP A 195 -58.067 1.615 59.987 1.00124.03 N
ANISOU 1246 NE1 TRP A 195 19365 16003 11757 -140 4077 -1955 N
ATOM 1247 CE2 TRP A 195 -58.279 0.907 58.832 1.00124.58 C
ANISOU 1247 CE2 TRP A 195 19293 16117 11924 -107 4079 -1926 C
ATOM 1248 CE3 TRP A 195 -57.042 0.321 56.829 1.00119.75 C
ANISOU 1248 CE3 TRP A 195 18461 15617 11422 58 3827 -1739 C
ATOM 1249 CZ2 TRP A 195 -59.410 0.207 58.391 1.00124.17 C
ANISOU 1249 CZ2 TRP A 195 19179 16059 11941 -185 4261 -2018 C
ATOM 1250 CZ3 TRP A 195 -58.165 -0.364 56.390 1.00121.50 C
ANISOU 1250 CZ3 TRP A 195 18629 15833 11701 -24 4003 -1827 C
ATOM 1251 CH2 TRP A 195 -59.330 -0.420 57.168 1.00123.37 C
ANISOU 1251 CH2 TRP A 195 18937 16019 11918 -145 4216 -1969 C
ATOM 1252 N ALA A 196 -56.659 3.643 56.222 1.00115.89 N
ANISOU 1252 N ALA A 196 17577 15237 11219 165 3593 -1785 N
ATOM 1253 CA ALA A 196 -57.542 3.590 55.052 1.00114.72 C
ANISOU 1253 CA ALA A 196 17210 15142 11236 183 3643 -1822 C
ATOM 1254 C ALA A 196 -57.061 4.497 53.923 1.00116.38 C
ANISOU 1254 C ALA A 196 17217 15413 11588 286 3495 -1768 C
ATOM 1255 O ALA A 196 -57.201 4.134 52.755 1.00115.10 O
ANISOU 1255 O ALA A 196 16911 15310 11512 326 3456 -1735 O
ATOM 1256 CB ALA A 196 -58.964 3.955 55.451 1.00116.45 C
ANISOU 1256 CB ALA A 196 17372 15347 11527 114 3831 -1964 C
ATOM 1257 N TRP A 197 -56.493 5.667 54.271 1.00112.25 N
ANISOU 1257 N TRP A 197 16699 14872 11078 318 3424 -1764 N
ATOM 1258 CA TRP A 197 -55.953 6.619 53.304 1.00110.85 C
ANISOU 1258 CA TRP A 197 16370 14728 11020 408 3303 -1718 C
ATOM 1259 C TRP A 197 -54.573 6.196 52.818 1.00112.84 C
ANISOU 1259 C TRP A 197 16645 15008 11221 452 3134 -1605 C
ATOM 1260 O TRP A 197 -54.269 6.387 51.642 1.00111.42 O
ANISOU 1260 O TRP A 197 16329 14864 11142 520 3050 -1553 O
ATOM 1261 CB TRP A 197 -55.935 8.040 53.872 1.00110.18 C
ANISOU 1261 CB TRP A 197 16298 14597 10968 407 3332 -1774 C
ATOM 1262 CG TRP A 197 -57.244 8.748 53.706 1.00111.73 C
ANISOU 1262 CG TRP A 197 16374 14782 11296 431 3471 -1859 C
ATOM 1263 CD1 TRP A 197 -58.253 8.831 54.619 1.00115.78 C
ANISOU 1263 CD1 TRP A 197 16939 15253 11799 365 3640 -1962 C
ATOM 1264 CD2 TRP A 197 -57.712 9.417 52.528 1.00111.24 C
ANISOU 1264 CD2 TRP A 197 16112 14757 11395 539 3454 -1845 C
ATOM 1265 NE1 TRP A 197 -59.305 9.545 54.098 1.00115.66 N
ANISOU 1265 NE1 TRP A 197 16753 15253 11941 433 3729 -2014 N
ATOM 1266 CE2 TRP A 197 -59.004 9.913 52.813 1.00116.21 C
ANISOU 1266 CE2 TRP A 197 16669 15376 12111 548 3611 -1938 C
ATOM 1267 CE3 TRP A 197 -57.160 9.660 51.258 1.00111.53 C
ANISOU 1267 CE3 TRP A 197 16032 14834 11508 634 3325 -1760 C
ATOM 1268 CZ2 TRP A 197 -59.750 10.640 51.879 1.00115.76 C
ANISOU 1268 CZ2 TRP A 197 16417 15359 12207 669 3628 -1939 C
ATOM 1269 CZ3 TRP A 197 -57.902 10.377 50.332 1.00113.17 C
ANISOU 1269 CZ3 TRP A 197 16071 15072 11857 741 3346 -1762 C
ATOM 1270 CH2 TRP A 197 -59.181 10.858 50.645 1.00114.98 C
ANISOU 1270 CH2 TRP A 197 16221 15301 12164 768 3489 -1845 C
ATOM 1271 N GLU A 198 -53.749 5.601 53.712 1.00109.19 N
ANISOU 1271 N GLU A 198 16355 14532 10599 419 3086 -1566 N
ATOM 1272 CA GLU A 198 -52.411 5.097 53.383 1.00108.16 C
ANISOU 1272 CA GLU A 198 16246 14438 10412 471 2931 -1459 C
ATOM 1273 C GLU A 198 -52.525 3.938 52.380 1.00110.48 C
ANISOU 1273 C GLU A 198 16488 14746 10743 506 2934 -1393 C
ATOM 1274 O GLU A 198 -51.729 3.865 51.444 1.00109.14 O
ANISOU 1274 O GLU A 198 16231 14607 10630 567 2825 -1319 O
ATOM 1275 CB GLU A 198 -51.653 4.665 54.654 1.00110.54 C
ANISOU 1275 CB GLU A 198 16743 14737 10520 443 2886 -1431 C
ATOM 1276 CG GLU A 198 -50.162 4.445 54.433 1.00120.79 C
ANISOU 1276 CG GLU A 198 18032 16096 11767 510 2707 -1332 C
ATOM 1277 CD GLU A 198 -49.339 4.121 55.666 1.00141.99 C
ANISOU 1277 CD GLU A 198 20886 18813 14252 503 2631 -1299 C
ATOM 1278 OE1 GLU A 198 -49.666 3.133 56.363 1.00136.75 O
ANISOU 1278 OE1 GLU A 198 20391 18111 13456 497 2701 -1272 O
ATOM 1279 OE2 GLU A 198 -48.329 4.822 55.900 1.00136.23 O
ANISOU 1279 OE2 GLU A 198 20120 18151 13490 505 2500 -1298 O
ATOM 1280 N VAL A 199 -53.540 3.064 52.561 1.00106.89 N
ANISOU 1280 N VAL A 199 16090 14265 10258 454 3077 -1433 N
ATOM 1281 CA VAL A 199 -53.811 1.936 51.668 1.00105.96 C
ANISOU 1281 CA VAL A 199 15940 14156 10165 454 3121 -1396 C
ATOM 1282 C VAL A 199 -54.600 2.409 50.421 1.00108.54 C
ANISOU 1282 C VAL A 199 16046 14537 10658 463 3135 -1438 C
ATOM 1283 O VAL A 199 -54.393 1.870 49.336 1.00107.47 O
ANISOU 1283 O VAL A 199 15834 14429 10570 485 3098 -1386 O
ATOM 1284 CB VAL A 199 -54.451 0.717 52.403 1.00110.79 C
ANISOU 1284 CB VAL A 199 16730 14712 10653 378 3282 -1425 C
ATOM 1285 CG1 VAL A 199 -55.920 0.948 52.758 1.00111.31 C
ANISOU 1285 CG1 VAL A 199 16761 14773 10760 285 3453 -1564 C
ATOM 1286 CG2 VAL A 199 -54.276 -0.574 51.609 1.00110.29 C
ANISOU 1286 CG2 VAL A 199 16695 14638 10572 382 3315 -1360 C
ATOM 1287 N GLY A 200 -55.448 3.429 50.588 1.00104.96 N
ANISOU 1287 N GLY A 200 15498 14098 10285 454 3186 -1526 N
ATOM 1288 CA GLY A 200 -56.247 4.013 49.514 1.00104.28 C
ANISOU 1288 CA GLY A 200 15201 14074 10345 489 3191 -1562 C
ATOM 1289 C GLY A 200 -55.398 4.715 48.475 1.00106.72 C
ANISOU 1289 C GLY A 200 15408 14403 10737 581 3043 -1483 C
ATOM 1290 O GLY A 200 -55.581 4.500 47.273 1.00105.79 O
ANISOU 1290 O GLY A 200 15166 14339 10690 608 3008 -1455 O
ATOM 1291 N LEU A 201 -54.446 5.546 48.939 1.00102.79 N
ANISOU 1291 N LEU A 201 14970 13863 10220 614 2962 -1454 N
ATOM 1292 CA LEU A 201 -53.511 6.270 48.076 1.00101.63 C
ANISOU 1292 CA LEU A 201 14753 13719 10142 685 2838 -1391 C
ATOM 1293 C LEU A 201 -52.395 5.338 47.585 1.00104.47 C
ANISOU 1293 C LEU A 201 15151 14086 10457 693 2743 -1299 C
ATOM 1294 O LEU A 201 -51.902 5.513 46.471 1.00103.42 O
ANISOU 1294 O LEU A 201 14932 13965 10396 739 2668 -1248 O
ATOM 1295 CB LEU A 201 -52.912 7.492 48.798 1.00102.04 C
ANISOU 1295 CB LEU A 201 14859 13726 10184 691 2811 -1418 C
ATOM 1296 CG LEU A 201 -53.863 8.658 49.098 1.00107.49 C
ANISOU 1296 CG LEU A 201 15508 14387 10945 706 2910 -1498 C
ATOM 1297 CD1 LEU A 201 -53.423 9.410 50.330 1.00108.41 C
ANISOU 1297 CD1 LEU A 201 15749 14450 10990 653 2936 -1549 C
ATOM 1298 CD2 LEU A 201 -53.973 9.612 47.920 1.00109.64 C
ANISOU 1298 CD2 LEU A 201 15655 14658 11347 801 2881 -1474 C
ATOM 1299 N GLY A 202 -52.028 4.361 48.418 1.00101.00 N
ANISOU 1299 N GLY A 202 14848 13631 9896 656 2758 -1276 N
ATOM 1300 CA GLY A 202 -50.986 3.376 48.139 1.00100.24 C
ANISOU 1300 CA GLY A 202 14807 13534 9745 680 2688 -1183 C
ATOM 1301 C GLY A 202 -51.304 2.403 47.021 1.00102.98 C
ANISOU 1301 C GLY A 202 15104 13890 10135 675 2727 -1147 C
ATOM 1302 O GLY A 202 -50.462 2.182 46.146 1.00101.84 O
ANISOU 1302 O GLY A 202 14917 13747 10030 715 2651 -1075 O
ATOM 1303 N VAL A 203 -52.513 1.798 47.052 1.00 99.64 N
ANISOU 1303 N VAL A 203 14686 13475 9700 611 2856 -1205 N
ATOM 1304 CA VAL A 203 -52.983 0.837 46.040 1.00 99.05 C
ANISOU 1304 CA VAL A 203 14566 13420 9649 572 2919 -1198 C
ATOM 1305 C VAL A 203 -53.182 1.541 44.686 1.00101.71 C
ANISOU 1305 C VAL A 203 14720 13813 10111 604 2852 -1197 C
ATOM 1306 O VAL A 203 -52.759 1.009 43.656 1.00100.70 O
ANISOU 1306 O VAL A 203 14563 13691 10008 605 2823 -1142 O
ATOM 1307 CB VAL A 203 -54.235 0.034 46.514 1.00103.84 C
ANISOU 1307 CB VAL A 203 15225 14031 10200 472 3090 -1285 C
ATOM 1308 CG1 VAL A 203 -54.887 -0.747 45.372 1.00103.55 C
ANISOU 1308 CG1 VAL A 203 15103 14043 10197 405 3160 -1310 C
ATOM 1309 CG2 VAL A 203 -53.880 -0.909 47.661 1.00104.38 C
ANISOU 1309 CG2 VAL A 203 15518 14019 10123 448 3166 -1259 C
ATOM 1310 N SER A 204 -53.782 2.751 44.704 1.00 98.04 N
ANISOU 1310 N SER A 204 14149 13383 9719 636 2833 -1252 N
ATOM 1311 CA SER A 204 -54.025 3.568 43.511 1.00 97.30 C
ANISOU 1311 CA SER A 204 13899 13337 9731 691 2769 -1245 C
ATOM 1312 C SER A 204 -52.725 4.010 42.830 1.00 99.84 C
ANISOU 1312 C SER A 204 14226 13618 10090 753 2651 -1160 C
ATOM 1313 O SER A 204 -52.699 4.116 41.606 1.00 98.98 O
ANISOU 1313 O SER A 204 14034 13535 10039 776 2607 -1128 O
ATOM 1314 CB SER A 204 -54.892 4.776 43.848 1.00101.45 C
ANISOU 1314 CB SER A 204 14341 13886 10317 736 2793 -1311 C
ATOM 1315 OG SER A 204 -54.283 5.590 44.835 1.00110.30 O
ANISOU 1315 OG SER A 204 15552 14939 11420 762 2776 -1315 O
ATOM 1316 N SER A 205 -51.649 4.241 43.619 1.00 95.91 N
ANISOU 1316 N SER A 205 13825 13065 9553 770 2602 -1131 N
ATOM 1317 CA SER A 205 -50.320 4.625 43.124 1.00 94.90 C
ANISOU 1317 CA SER A 205 13698 12903 9456 812 2500 -1069 C
ATOM 1318 C SER A 205 -49.706 3.491 42.297 1.00 97.70 C
ANISOU 1318 C SER A 205 14067 13252 9804 800 2485 -998 C
ATOM 1319 O SER A 205 -49.089 3.755 41.265 1.00 96.73 O
ANISOU 1319 O SER A 205 13893 13116 9745 825 2429 -958 O
ATOM 1320 CB SER A 205 -49.397 4.981 44.286 1.00 98.67 C
ANISOU 1320 CB SER A 205 14261 13356 9873 814 2456 -1072 C
ATOM 1321 OG SER A 205 -48.089 5.299 43.840 1.00106.55 O
ANISOU 1321 OG SER A 205 15242 14339 10902 842 2364 -1028 O
ATOM 1322 N THR A 206 -49.886 2.235 42.756 1.00 94.19 N
ANISOU 1322 N THR A 206 13706 12803 9279 759 2553 -985 N
ATOM 1323 CA THR A 206 -49.407 1.020 42.090 1.00 93.59 C
ANISOU 1323 CA THR A 206 13672 12703 9185 743 2578 -920 C
ATOM 1324 C THR A 206 -50.234 0.787 40.816 1.00 96.66 C
ANISOU 1324 C THR A 206 13973 13128 9625 695 2622 -941 C
ATOM 1325 O THR A 206 -49.684 0.355 39.803 1.00 95.64 O
ANISOU 1325 O THR A 206 13833 12979 9528 689 2609 -889 O
ATOM 1326 CB THR A 206 -49.460 -0.175 43.066 1.00102.66 C
ANISOU 1326 CB THR A 206 14967 13820 10219 718 2666 -905 C
ATOM 1327 OG1 THR A 206 -48.840 0.193 44.301 1.00103.24 O
ANISOU 1327 OG1 THR A 206 15114 13885 10230 764 2610 -895 O
ATOM 1328 CG2 THR A 206 -48.788 -1.431 42.510 1.00100.85 C
ANISOU 1328 CG2 THR A 206 14811 13541 9966 722 2708 -825 C
ATOM 1329 N THR A 207 -51.547 1.098 40.872 1.00 93.38 N
ANISOU 1329 N THR A 207 13487 12775 9217 658 2674 -1020 N
ATOM 1330 CA THR A 207 -52.487 0.957 39.757 1.00 93.14 C
ANISOU 1330 CA THR A 207 13349 12820 9220 611 2702 -1055 C
ATOM 1331 C THR A 207 -52.162 1.966 38.643 1.00 96.28 C
ANISOU 1331 C THR A 207 13649 13231 9701 678 2596 -1019 C
ATOM 1332 O THR A 207 -51.930 1.560 37.505 1.00 95.43 O
ANISOU 1332 O THR A 207 13521 13131 9607 651 2582 -984 O
ATOM 1333 CB THR A 207 -53.945 1.049 40.262 1.00101.80 C
ANISOU 1333 CB THR A 207 14380 13998 10303 566 2782 -1156 C
ATOM 1334 OG1 THR A 207 -54.106 0.220 41.414 1.00101.70 O
ANISOU 1334 OG1 THR A 207 14492 13943 10205 506 2889 -1188 O
ATOM 1335 CG2 THR A 207 -54.965 0.649 39.200 1.00100.83 C
ANISOU 1335 CG2 THR A 207 14135 13986 10190 496 2819 -1206 C
ATOM 1336 N VAL A 208 -52.119 3.267 38.989 1.00 92.81 N
ANISOU 1336 N VAL A 208 13172 12782 9308 759 2537 -1029 N
ATOM 1337 CA VAL A 208 -51.843 4.387 38.082 1.00 92.30 C
ANISOU 1337 CA VAL A 208 13046 12708 9315 835 2457 -999 C
ATOM 1338 C VAL A 208 -50.398 4.361 37.537 1.00 95.17 C
ANISOU 1338 C VAL A 208 13470 12989 9701 845 2401 -930 C
ATOM 1339 O VAL A 208 -50.195 4.597 36.345 1.00 94.42 O
ANISOU 1339 O VAL A 208 13344 12888 9643 859 2364 -896 O
ATOM 1340 CB VAL A 208 -52.211 5.743 38.762 1.00 96.71 C
ANISOU 1340 CB VAL A 208 13580 13255 9909 912 2449 -1036 C
ATOM 1341 CG1 VAL A 208 -51.586 6.941 38.051 1.00 96.36 C
ANISOU 1341 CG1 VAL A 208 13533 13153 9926 992 2387 -998 C
ATOM 1342 CG2 VAL A 208 -53.724 5.913 38.875 1.00 97.36 C
ANISOU 1342 CG2 VAL A 208 13561 13433 9999 925 2499 -1099 C
ATOM 1343 N GLY A 209 -49.432 4.075 38.408 1.00 91.47 N
ANISOU 1343 N GLY A 209 13081 12467 9206 839 2394 -914 N
ATOM 1344 CA GLY A 209 -48.013 4.069 38.068 1.00 90.79 C
ANISOU 1344 CA GLY A 209 13030 12317 9147 852 2344 -862 C
ATOM 1345 C GLY A 209 -47.394 2.791 37.537 1.00 94.23 C
ANISOU 1345 C GLY A 209 13506 12729 9567 815 2369 -807 C
ATOM 1346 O GLY A 209 -46.285 2.846 36.998 1.00 93.42 O
ANISOU 1346 O GLY A 209 13409 12578 9509 829 2333 -767 O
ATOM 1347 N PHE A 210 -48.067 1.631 37.694 1.00 90.94 N
ANISOU 1347 N PHE A 210 13125 12336 9091 763 2448 -809 N
ATOM 1348 CA PHE A 210 -47.492 0.368 37.225 1.00 90.57 C
ANISOU 1348 CA PHE A 210 13141 12246 9025 728 2502 -755 C
ATOM 1349 C PHE A 210 -48.501 -0.604 36.599 1.00 94.41 C
ANISOU 1349 C PHE A 210 13635 12764 9471 635 2603 -778 C
ATOM 1350 O PHE A 210 -48.273 -1.028 35.469 1.00 93.59 O
ANISOU 1350 O PHE A 210 13530 12640 9390 593 2626 -751 O
ATOM 1351 CB PHE A 210 -46.689 -0.325 38.345 1.00 92.77 C
ANISOU 1351 CB PHE A 210 13513 12486 9249 767 2514 -714 C
ATOM 1352 CG PHE A 210 -45.794 -1.446 37.871 1.00 94.40 C
ANISOU 1352 CG PHE A 210 13785 12628 9455 773 2563 -640 C
ATOM 1353 CD1 PHE A 210 -44.532 -1.179 37.351 1.00 97.27 C
ANISOU 1353 CD1 PHE A 210 14114 12955 9890 821 2500 -594 C
ATOM 1354 CD2 PHE A 210 -46.207 -2.770 37.954 1.00 97.03 C
ANISOU 1354 CD2 PHE A 210 14219 12929 9720 727 2690 -622 C
ATOM 1355 CE1 PHE A 210 -43.708 -2.217 36.907 1.00 98.36 C
ANISOU 1355 CE1 PHE A 210 14305 13028 10039 838 2558 -524 C
ATOM 1356 CE2 PHE A 210 -45.383 -3.806 37.509 1.00100.03 C
ANISOU 1356 CE2 PHE A 210 14673 13231 10102 742 2757 -548 C
ATOM 1357 CZ PHE A 210 -44.137 -3.524 36.993 1.00 97.87 C
ANISOU 1357 CZ PHE A 210 14352 12925 9909 805 2687 -496 C
ATOM 1358 N VAL A 211 -49.588 -0.969 37.318 1.00 91.51 N
ANISOU 1358 N VAL A 211 13281 12446 9042 589 2675 -837 N
ATOM 1359 CA VAL A 211 -50.602 -1.937 36.860 1.00 91.71 C
ANISOU 1359 CA VAL A 211 13311 12516 9018 474 2791 -886 C
ATOM 1360 C VAL A 211 -51.229 -1.529 35.507 1.00 95.36 C
ANISOU 1360 C VAL A 211 13653 13062 9517 431 2753 -914 C
ATOM 1361 O VAL A 211 -51.192 -2.330 34.572 1.00 94.82 O
ANISOU 1361 O VAL A 211 13608 12988 9429 347 2812 -905 O
ATOM 1362 CB VAL A 211 -51.675 -2.255 37.943 1.00 96.34 C
ANISOU 1362 CB VAL A 211 13923 13145 9538 425 2882 -965 C
ATOM 1363 CG1 VAL A 211 -52.689 -3.286 37.447 1.00 96.77 C
ANISOU 1363 CG1 VAL A 211 13978 13253 9538 282 3019 -1035 C
ATOM 1364 CG2 VAL A 211 -51.026 -2.736 39.239 1.00 96.42 C
ANISOU 1364 CG2 VAL A 211 14080 13067 9486 470 2920 -925 C
ATOM 1365 N VAL A 212 -51.768 -0.297 35.398 1.00 92.08 N
ANISOU 1365 N VAL A 212 13121 12718 9145 494 2661 -943 N
ATOM 1366 CA VAL A 212 -52.382 0.212 34.162 1.00 92.11 C
ANISOU 1366 CA VAL A 212 13012 12814 9171 486 2605 -957 C
ATOM 1367 C VAL A 212 -51.310 0.404 33.042 1.00 95.51 C
ANISOU 1367 C VAL A 212 13478 13169 9641 508 2547 -880 C
ATOM 1368 O VAL A 212 -51.521 -0.166 31.970 1.00 95.24 O
ANISOU 1368 O VAL A 212 13436 13170 9579 424 2573 -881 O
ATOM 1369 CB VAL A 212 -53.286 1.465 34.383 1.00 96.49 C
ANISOU 1369 CB VAL A 212 13443 13458 9760 574 2535 -997 C
ATOM 1370 CG1 VAL A 212 -53.809 2.028 33.062 1.00 96.63 C
ANISOU 1370 CG1 VAL A 212 13357 13570 9790 600 2460 -989 C
ATOM 1371 CG2 VAL A 212 -54.451 1.144 35.317 1.00 97.12 C
ANISOU 1371 CG2 VAL A 212 13475 13623 9805 528 2614 -1089 C
ATOM 1372 N PRO A 213 -50.157 1.113 33.242 1.00 91.58 N
ANISOU 1372 N PRO A 213 13025 12569 9201 597 2486 -825 N
ATOM 1373 CA PRO A 213 -49.180 1.246 32.141 1.00 90.93 C
ANISOU 1373 CA PRO A 213 12977 12412 9159 599 2454 -767 C
ATOM 1374 C PRO A 213 -48.586 -0.066 31.619 1.00 94.56 C
ANISOU 1374 C PRO A 213 13517 12813 9598 508 2540 -737 C
ATOM 1375 O PRO A 213 -48.471 -0.218 30.403 1.00 94.06 O
ANISOU 1375 O PRO A 213 13462 12740 9536 456 2546 -719 O
ATOM 1376 CB PRO A 213 -48.098 2.160 32.728 1.00 92.29 C
ANISOU 1376 CB PRO A 213 13175 12499 9392 691 2396 -741 C
ATOM 1377 CG PRO A 213 -48.759 2.873 33.839 1.00 97.04 C
ANISOU 1377 CG PRO A 213 13738 13148 9985 747 2374 -785 C
ATOM 1378 CD PRO A 213 -49.706 1.878 34.423 1.00 92.99 C
ANISOU 1378 CD PRO A 213 13221 12704 9407 682 2447 -825 C
ATOM 1379 N PHE A 214 -48.232 -1.012 32.521 1.00 91.22 N
ANISOU 1379 N PHE A 214 13167 12343 9148 493 2616 -727 N
ATOM 1380 CA PHE A 214 -47.650 -2.312 32.155 1.00 91.10 C
ANISOU 1380 CA PHE A 214 13249 12251 9113 425 2725 -690 C
ATOM 1381 C PHE A 214 -48.624 -3.215 31.387 1.00 95.27 C
ANISOU 1381 C PHE A 214 13788 12835 9575 283 2827 -735 C
ATOM 1382 O PHE A 214 -48.176 -4.003 30.552 1.00 94.72 O
ANISOU 1382 O PHE A 214 13787 12702 9501 210 2909 -709 O
ATOM 1383 CB PHE A 214 -47.061 -3.033 33.380 1.00 93.17 C
ANISOU 1383 CB PHE A 214 13599 12448 9351 475 2781 -656 C
ATOM 1384 CG PHE A 214 -46.188 -4.228 33.075 1.00 94.97 C
ANISOU 1384 CG PHE A 214 13936 12569 9578 456 2889 -594 C
ATOM 1385 CD1 PHE A 214 -44.876 -4.061 32.645 1.00 97.83 C
ANISOU 1385 CD1 PHE A 214 14299 12854 10018 520 2852 -532 C
ATOM 1386 CD2 PHE A 214 -46.666 -5.521 33.252 1.00 97.79 C
ANISOU 1386 CD2 PHE A 214 14400 12897 9859 377 3046 -602 C
ATOM 1387 CE1 PHE A 214 -44.067 -5.168 32.370 1.00 99.07 C
ANISOU 1387 CE1 PHE A 214 14550 12907 10184 520 2964 -470 C
ATOM 1388 CE2 PHE A 214 -45.855 -6.627 32.980 1.00100.98 C
ANISOU 1388 CE2 PHE A 214 14922 13184 10263 375 3169 -536 C
ATOM 1389 CZ PHE A 214 -44.561 -6.443 32.541 1.00 98.78 C
ANISOU 1389 CZ PHE A 214 14631 12832 10070 455 3123 -467 C
ATOM 1390 N THR A 215 -49.944 -3.098 31.658 1.00 92.33 N
ANISOU 1390 N THR A 215 13343 12587 9151 236 2831 -813 N
ATOM 1391 CA THR A 215 -50.972 -3.870 30.948 1.00 92.82 C
ANISOU 1391 CA THR A 215 13385 12742 9142 82 2920 -882 C
ATOM 1392 C THR A 215 -51.114 -3.379 29.508 1.00 96.48 C
ANISOU 1392 C THR A 215 13778 13268 9610 48 2843 -878 C
ATOM 1393 O THR A 215 -51.278 -4.201 28.608 1.00 96.46 O
ANISOU 1393 O THR A 215 13815 13280 9556 -89 2927 -900 O
ATOM 1394 CB THR A 215 -52.303 -3.928 31.709 1.00102.26 C
ANISOU 1394 CB THR A 215 14507 14063 10285 37 2954 -979 C
ATOM 1395 OG1 THR A 215 -52.612 -2.644 32.252 1.00102.30 O
ANISOU 1395 OG1 THR A 215 14405 14126 10338 165 2826 -984 O
ATOM 1396 CG2 THR A 215 -52.302 -4.981 32.807 1.00101.46 C
ANISOU 1396 CG2 THR A 215 14533 13886 10133 -9 3105 -997 C
ATOM 1397 N ILE A 216 -51.007 -2.045 29.290 1.00 92.48 N
ANISOU 1397 N ILE A 216 13193 12789 9158 170 2696 -849 N
ATOM 1398 CA ILE A 216 -51.049 -1.418 27.960 1.00 92.27 C
ANISOU 1398 CA ILE A 216 13125 12804 9130 171 2612 -828 C
ATOM 1399 C ILE A 216 -49.765 -1.819 27.213 1.00 95.37 C
ANISOU 1399 C ILE A 216 13637 13043 9555 138 2658 -764 C
ATOM 1400 O ILE A 216 -49.828 -2.149 26.028 1.00 95.23 O
ANISOU 1400 O ILE A 216 13646 13042 9497 41 2679 -764 O
ATOM 1401 CB ILE A 216 -51.251 0.130 28.033 1.00 95.33 C
ANISOU 1401 CB ILE A 216 13428 13230 9563 327 2470 -808 C
ATOM 1402 CG1 ILE A 216 -52.534 0.495 28.819 1.00 96.50 C
ANISOU 1402 CG1 ILE A 216 13451 13525 9690 367 2442 -874 C
ATOM 1403 CG2 ILE A 216 -51.281 0.760 26.626 1.00 96.25 C
ANISOU 1403 CG2 ILE A 216 13533 13377 9660 341 2389 -774 C
ATOM 1404 CD1 ILE A 216 -52.546 1.900 29.447 1.00103.82 C
ANISOU 1404 CD1 ILE A 216 14334 14435 10679 536 2353 -853 C
ATOM 1405 N CYS A 217 -48.620 -1.838 27.935 1.00 91.16 N
ANISOU 1405 N CYS A 217 13174 12372 9093 214 2678 -714 N
ATOM 1406 CA CYS A 217 -47.300 -2.243 27.441 1.00 90.54 C
ANISOU 1406 CA CYS A 217 13192 12144 9067 203 2733 -657 C
ATOM 1407 C CYS A 217 -47.334 -3.696 26.947 1.00 94.69 C
ANISOU 1407 C CYS A 217 13807 12632 9540 59 2889 -665 C
ATOM 1408 O CYS A 217 -46.770 -3.997 25.894 1.00 94.27 O
ANISOU 1408 O CYS A 217 13817 12505 9498 -8 2939 -641 O
ATOM 1409 CB CYS A 217 -46.240 -2.078 28.532 1.00 30.00 C
ATOM 1410 SG CYS A 217 -45.947 -0.367 29.035 1.00 30.00 S
ATOM 1411 N LEU A 218 -48.011 -4.584 27.707 1.00 91.62 N
ANISOU 1411 N LEU A 218 13439 12284 9090 3 2983 -705 N
ATOM 1412 CA LEU A 218 -48.168 -6.004 27.392 1.00 91.94 C
ANISOU 1412 CA LEU A 218 13584 12282 9067 -145 3165 -726 C
ATOM 1413 C LEU A 218 -49.119 -6.215 26.212 1.00 96.08 C
ANISOU 1413 C LEU A 218 14075 12923 9509 -312 3187 -795 C
ATOM 1414 O LEU A 218 -48.836 -7.056 25.357 1.00 95.85 O
ANISOU 1414 O LEU A 218 14142 12827 9450 -440 3311 -795 O
ATOM 1415 CB LEU A 218 -48.662 -6.777 28.622 1.00 92.49 C
ANISOU 1415 CB LEU A 218 13700 12356 9085 -154 3267 -757 C
ATOM 1416 N THR A 219 -50.238 -5.453 26.165 1.00 92.83 N
ANISOU 1416 N THR A 219 13523 12691 9057 -310 3068 -855 N
ATOM 1417 CA THR A 219 -51.243 -5.521 25.096 1.00 93.46 C
ANISOU 1417 CA THR A 219 13532 12931 9045 -451 3050 -925 C
ATOM 1418 C THR A 219 -50.641 -5.060 23.762 1.00 97.04 C
ANISOU 1418 C THR A 219 14020 13344 9509 -458 2985 -873 C
ATOM 1419 O THR A 219 -50.866 -5.713 22.743 1.00 97.30 O
ANISOU 1419 O THR A 219 14098 13410 9463 -624 3058 -908 O
ATOM 1420 CB THR A 219 -52.532 -4.771 25.495 1.00101.75 C
ANISOU 1420 CB THR A 219 14406 14190 10064 -406 2931 -992 C
ATOM 1421 OG1 THR A 219 -52.977 -5.251 26.765 1.00101.49 O
ANISOU 1421 OG1 THR A 219 14370 14163 10027 -411 3017 -1043 O
ATOM 1422 CG2 THR A 219 -53.659 -4.942 24.478 1.00101.44 C
ANISOU 1422 CG2 THR A 219 14267 14360 9917 -553 2907 -1077 C
ATOM 1423 N CYS A 220 -49.849 -3.964 23.782 1.00 92.68 N
ANISOU 1423 N CYS A 220 13460 12709 9044 -292 2866 -796 N
ATOM 1424 CA CYS A 220 -49.175 -3.421 22.600 1.00 92.25 C
ANISOU 1424 CA CYS A 220 13460 12586 9006 -285 2815 -745 C
ATOM 1425 C CYS A 220 -48.211 -4.448 22.003 1.00 95.77 C
ANISOU 1425 C CYS A 220 14054 12868 9468 -402 2975 -722 C
ATOM 1426 O CYS A 220 -48.332 -4.762 20.820 1.00 95.94 O
ANISOU 1426 O CYS A 220 14129 12905 9420 -535 3012 -737 O
ATOM 1427 CB CYS A 220 -48.472 -2.104 22.918 1.00 91.82 C
ANISOU 1427 CB CYS A 220 13386 12455 9048 -97 2694 -684 C
ATOM 1428 SG CYS A 220 -49.583 -0.676 23.031 1.00 96.20 S
ANISOU 1428 SG CYS A 220 13799 13181 9573 40 2511 -695 S
ATOM 1429 N TYR A 221 -47.314 -5.020 22.840 1.00 91.60 N
ANISOU 1429 N TYR A 221 13592 12193 9019 -352 3075 -686 N
ATOM 1430 CA TYR A 221 -46.328 -6.040 22.458 1.00 91.35 C
ANISOU 1430 CA TYR A 221 13697 11990 9022 -426 3246 -654 C
ATOM 1431 C TYR A 221 -46.983 -7.310 21.890 1.00 95.65 C
ANISOU 1431 C TYR A 221 14322 12563 9459 -638 3415 -714 C
ATOM 1432 O TYR A 221 -46.429 -7.918 20.973 1.00 95.32 O
ANISOU 1432 O TYR A 221 14394 12411 9414 -749 3539 -703 O
ATOM 1433 CB TYR A 221 -45.406 -6.374 23.649 1.00 92.20 C
ANISOU 1433 CB TYR A 221 13834 11975 9222 -296 3299 -601 C
ATOM 1434 CG TYR A 221 -44.332 -7.401 23.350 1.00 94.26 C
ANISOU 1434 CG TYR A 221 14225 12056 9533 -330 3477 -555 C
ATOM 1435 CD1 TYR A 221 -43.186 -7.054 22.640 1.00 95.96 C
ANISOU 1435 CD1 TYR A 221 14469 12149 9842 -297 3479 -511 C
ATOM 1436 CD2 TYR A 221 -44.445 -8.710 23.808 1.00 95.63 C
ANISOU 1436 CD2 TYR A 221 14500 12170 9666 -388 3660 -556 C
ATOM 1437 CE1 TYR A 221 -42.193 -7.994 22.365 1.00 97.13 C
ANISOU 1437 CE1 TYR A 221 14725 12131 10050 -316 3652 -468 C
ATOM 1438 CE2 TYR A 221 -43.458 -9.658 23.542 1.00 96.89 C
ANISOU 1438 CE2 TYR A 221 14785 12152 9876 -398 3838 -503 C
ATOM 1439 CZ TYR A 221 -42.332 -9.295 22.822 1.00104.23 C
ANISOU 1439 CZ TYR A 221 15721 12972 10908 -357 3830 -459 C
ATOM 1440 OH TYR A 221 -41.354 -10.224 22.559 1.00105.93 O
ANISOU 1440 OH TYR A 221 16050 13014 11186 -354 4015 -407 O
ATOM 1441 N PHE A 222 -48.158 -7.695 22.431 1.00 92.65 N
ANISOU 1441 N PHE A 222 13885 12326 8991 -708 3433 -788 N
ATOM 1442 CA PHE A 222 -48.930 -8.864 22.000 1.00 93.40 C
ANISOU 1442 CA PHE A 222 14044 12475 8971 -933 3601 -872 C
ATOM 1443 C PHE A 222 -49.495 -8.670 20.586 1.00 97.52 C
ANISOU 1443 C PHE A 222 14537 13120 9394 -1089 3551 -923 C
ATOM 1444 O PHE A 222 -49.373 -9.574 19.758 1.00 97.78 O
ANISOU 1444 O PHE A 222 14690 13095 9367 -1276 3713 -954 O
ATOM 1445 CB PHE A 222 -50.043 -9.185 23.020 1.00 95.77 C
ANISOU 1445 CB PHE A 222 14273 12907 9210 -962 3626 -953 C
ATOM 1446 CG PHE A 222 -51.022 -10.264 22.614 1.00 98.72 C
ANISOU 1446 CG PHE A 222 14682 13375 9451 -1216 3793 -1072 C
ATOM 1447 CD1 PHE A 222 -50.676 -11.608 22.695 1.00102.39 C
ANISOU 1447 CD1 PHE A 222 15333 13683 9888 -1342 4055 -1084 C
ATOM 1448 CD2 PHE A 222 -52.301 -9.936 22.179 1.00101.83 C
ANISOU 1448 CD2 PHE A 222 14924 14021 9746 -1327 3696 -1177 C
ATOM 1449 CE1 PHE A 222 -51.584 -12.604 22.323 1.00104.69 C
ANISOU 1449 CE1 PHE A 222 15671 14057 10051 -1602 4233 -1211 C
ATOM 1450 CE2 PHE A 222 -53.208 -10.933 21.808 1.00106.09 C
ANISOU 1450 CE2 PHE A 222 15482 14670 10158 -1585 3854 -1308 C
ATOM 1451 CZ PHE A 222 -52.845 -12.260 21.884 1.00104.65 C
ANISOU 1451 CZ PHE A 222 15499 14318 9945 -1733 4130 -1331 C
ATOM 1452 N PHE A 223 -50.102 -7.495 20.315 1.00 93.71 N
ANISOU 1452 N PHE A 223 13909 12805 8890 -1008 3334 -928 N
ATOM 1453 CA PHE A 223 -50.672 -7.156 19.007 1.00 94.21 C
ANISOU 1453 CA PHE A 223 13936 13013 8847 -1118 3246 -962 C
ATOM 1454 C PHE A 223 -49.595 -6.947 17.944 1.00 97.28 C
ANISOU 1454 C PHE A 223 14457 13238 9268 -1126 3263 -891 C
ATOM 1455 O PHE A 223 -49.829 -7.261 16.775 1.00 97.76 O
ANISOU 1455 O PHE A 223 14573 13348 9222 -1296 3295 -926 O
ATOM 1456 CB PHE A 223 -51.600 -5.936 19.106 1.00 96.33 C
ANISOU 1456 CB PHE A 223 14019 13496 9087 -986 3014 -970 C
ATOM 1457 CG PHE A 223 -53.009 -6.277 19.528 1.00 99.02 C
ANISOU 1457 CG PHE A 223 14211 14076 9335 -1076 3005 -1083 C
ATOM 1458 CD1 PHE A 223 -53.970 -6.624 18.585 1.00103.63 C
ANISOU 1458 CD1 PHE A 223 14730 14875 9770 -1263 2990 -1173 C
ATOM 1459 CD2 PHE A 223 -53.377 -6.252 20.867 1.00100.87 C
ANISOU 1459 CD2 PHE A 223 14367 14331 9627 -985 3016 -1108 C
ATOM 1460 CE1 PHE A 223 -55.271 -6.947 18.977 1.00105.79 C
ANISOU 1460 CE1 PHE A 223 14843 15387 9964 -1358 2989 -1296 C
ATOM 1461 CE2 PHE A 223 -54.679 -6.574 21.258 1.00104.83 C
ANISOU 1461 CE2 PHE A 223 14729 15050 10052 -1079 3027 -1226 C
ATOM 1462 CZ PHE A 223 -55.617 -6.920 20.311 1.00104.48 C
ANISOU 1462 CZ PHE A 223 14602 15225 9870 -1266 3015 -1324 C
ATOM 1463 N ILE A 224 -48.417 -6.428 18.354 1.00 92.29 N
ANISOU 1463 N ILE A 224 13872 12415 8777 -955 3246 -801 N
ATOM 1464 CA ILE A 224 -47.258 -6.199 17.486 1.00 91.51 C
ANISOU 1464 CA ILE A 224 13896 12136 8739 -950 3282 -740 C
ATOM 1465 C ILE A 224 -46.697 -7.552 17.013 1.00 95.61 C
ANISOU 1465 C ILE A 224 14572 12505 9250 -1129 3525 -755 C
ATOM 1466 O ILE A 224 -46.464 -7.726 15.815 1.00 95.79 O
ANISOU 1466 O ILE A 224 14698 12479 9219 -1265 3583 -762 O
ATOM 1467 CB ILE A 224 -46.210 -5.279 18.186 1.00 93.38 C
ANISOU 1467 CB ILE A 224 14111 12239 9131 -728 3205 -663 C
ATOM 1468 CG1 ILE A 224 -46.647 -3.799 18.108 1.00 93.72 C
ANISOU 1468 CG1 ILE A 224 14057 12391 9162 -587 2990 -644 C
ATOM 1469 CG2 ILE A 224 -44.795 -5.458 17.617 1.00 93.64 C
ANISOU 1469 CG2 ILE A 224 14272 12044 9262 -739 3319 -615 C
ATOM 1470 CD1 ILE A 224 -46.097 -2.899 19.221 1.00100.12 C
ANISOU 1470 CD1 ILE A 224 14800 13144 10097 -380 2905 -604 C
ATOM 1471 N ALA A 225 -46.534 -8.514 17.949 1.00 91.83 N
ANISOU 1471 N ALA A 225 14128 11951 8814 -1131 3675 -761 N
ATOM 1472 CA ALA A 225 -46.042 -9.867 17.668 1.00 92.06 C
ANISOU 1472 CA ALA A 225 14319 11821 8839 -1278 3936 -770 C
ATOM 1473 C ALA A 225 -47.035 -10.675 16.823 1.00 97.08 C
ANISOU 1473 C ALA A 225 15007 12570 9307 -1550 4045 -872 C
ATOM 1474 O ALA A 225 -46.611 -11.538 16.052 1.00 97.13 O
ANISOU 1474 O ALA A 225 15170 12447 9288 -1714 4245 -885 O
ATOM 1475 CB ALA A 225 -45.746 -10.598 18.967 1.00 92.57 C
ANISOU 1475 CB ALA A 225 14410 11793 8971 -1181 4054 -743 C
ATOM 1476 N GLN A 226 -48.349 -10.382 16.966 1.00 94.19 N
ANISOU 1476 N GLN A 226 14506 12454 8828 -1603 3919 -950 N
ATOM 1477 CA GLN A 226 -49.450 -11.027 16.243 1.00 95.47 C
ANISOU 1477 CA GLN A 226 14668 12791 8816 -1866 3986 -1070 C
ATOM 1478 C GLN A 226 -49.349 -10.805 14.724 1.00 99.99 C
ANISOU 1478 C GLN A 226 15304 13389 9300 -2006 3953 -1077 C
ATOM 1479 O GLN A 226 -49.554 -11.750 13.960 1.00100.57 O
ANISOU 1479 O GLN A 226 15492 13457 9265 -2259 4129 -1152 O
ATOM 1480 CB GLN A 226 -50.805 -10.528 16.778 1.00 97.33 C
ANISOU 1480 CB GLN A 226 14697 13309 8974 -1843 3816 -1145 C
ATOM 1481 CG GLN A 226 -52.001 -11.389 16.361 1.00114.13 C
ANISOU 1481 CG GLN A 226 16798 15637 10930 -2124 3917 -1296 C
ATOM 1482 CD GLN A 226 -53.331 -10.665 16.398 1.00133.84 C
ANISOU 1482 CD GLN A 226 19058 18461 13335 -2112 3700 -1371 C
ATOM 1483 OE1 GLN A 226 -53.432 -9.473 16.718 1.00128.99 O
ANISOU 1483 OE1 GLN A 226 18305 17924 12782 -1882 3471 -1305 O
ATOM 1484 NE2 GLN A 226 -54.390 -11.376 16.046 1.00127.05 N
ANISOU 1484 NE2 GLN A 226 18144 17805 12324 -2364 3777 -1519 N
ATOM 1485 N THR A 227 -49.038 -9.564 14.296 1.00 96.14 N
ANISOU 1485 N THR A 227 14761 12921 8848 -1849 3741 -1004 N
ATOM 1486 CA THR A 227 -48.892 -9.201 12.880 1.00 96.70 C
ANISOU 1486 CA THR A 227 14909 13003 8830 -1950 3690 -996 C
ATOM 1487 C THR A 227 -47.557 -9.694 12.315 1.00 99.98 C
ANISOU 1487 C THR A 227 15531 13126 9333 -2005 3888 -946 C
ATOM 1488 O THR A 227 -47.505 -10.119 11.160 1.00100.39 O
ANISOU 1488 O THR A 227 15710 13151 9281 -2210 3984 -981 O
ATOM 1489 CB THR A 227 -49.082 -7.690 12.664 1.00105.67 C
ANISOU 1489 CB THR A 227 15935 14251 9964 -1752 3412 -934 C
ATOM 1490 OG1 THR A 227 -48.169 -6.970 13.494 1.00104.69 O
ANISOU 1490 OG1 THR A 227 15796 13961 10022 -1506 3364 -843 O
ATOM 1491 CG2 THR A 227 -50.514 -7.230 12.925 1.00105.24 C
ANISOU 1491 CG2 THR A 227 15676 14514 9797 -1722 3221 -991 C
ATOM 1492 N ILE A 228 -46.486 -9.635 13.134 1.00 95.30 N
ANISOU 1492 N ILE A 228 14962 12322 8925 -1823 3948 -868 N
ATOM 1493 CA ILE A 228 -45.125 -10.063 12.788 1.00 94.73 C
ANISOU 1493 CA ILE A 228 15050 11969 8973 -1829 4135 -815 C
ATOM 1494 C ILE A 228 -45.042 -11.597 12.621 1.00 99.70 C
ANISOU 1494 C ILE A 228 15831 12482 9566 -2037 4435 -864 C
ATOM 1495 O ILE A 228 -44.305 -12.066 11.750 1.00 99.62 O
ANISOU 1495 O ILE A 228 15982 12296 9573 -2156 4609 -857 O
ATOM 1496 CB ILE A 228 -44.095 -9.478 13.809 1.00 96.44 C
ANISOU 1496 CB ILE A 228 15204 12048 9390 -1558 4079 -726 C
ATOM 1497 CG1 ILE A 228 -43.907 -7.960 13.572 1.00 96.22 C
ANISOU 1497 CG1 ILE A 228 15099 12065 9397 -1403 3847 -683 C
ATOM 1498 CG2 ILE A 228 -42.737 -10.213 13.785 1.00 96.98 C
ANISOU 1498 CG2 ILE A 228 15401 11845 9601 -1545 4306 -679 C
ATOM 1499 CD1 ILE A 228 -43.267 -7.182 14.711 1.00102.13 C
ANISOU 1499 CD1 ILE A 228 15737 12765 10301 -1151 3739 -625 C
ATOM 1500 N ALA A 229 -45.831 -12.358 13.423 1.00 96.98 N
ANISOU 1500 N ALA A 229 15450 12232 9167 -2092 4511 -920 N
ATOM 1501 CA ALA A 229 -45.914 -13.830 13.443 1.00 97.83 C
ANISOU 1501 CA ALA A 229 15709 12236 9225 -2286 4814 -976 C
ATOM 1502 C ALA A 229 -45.742 -14.499 12.073 1.00102.84 C
ANISOU 1502 C ALA A 229 16525 12783 9766 -2557 5007 -1028 C
ATOM 1503 O ALA A 229 -44.936 -15.423 11.949 1.00102.66 O
ANISOU 1503 O ALA A 229 16676 12519 9810 -2611 5278 -1004 O
ATOM 1504 CB ALA A 229 -47.215 -14.278 14.095 1.00 99.29 C
ANISOU 1504 CB ALA A 229 15811 12626 9289 -2386 4816 -1075 C
ATOM 1505 N MET A1001 -46.470 -14.010 11.048 1.00 93.76 N
ANISOU 1505 N MET A1001 14453 11890 9283 113 1904 -1082 N
ATOM 1506 CA MET A1001 -46.372 -14.515 9.679 1.00 93.30 C
ANISOU 1506 CA MET A1001 14347 11843 9262 197 1857 -1066 C
ATOM 1507 C MET A1001 -45.360 -13.661 8.904 1.00 96.81 C
ANISOU 1507 C MET A1001 14744 12328 9710 241 1831 -1053 C
ATOM 1508 O MET A1001 -45.704 -12.594 8.384 1.00 96.28 O
ANISOU 1508 O MET A1001 14644 12255 9685 250 1869 -1070 O
ATOM 1509 CB MET A1001 -47.751 -14.551 8.993 1.00 95.62 C
ANISOU 1509 CB MET A1001 14597 12108 9626 210 1892 -1102 C
ATOM 1510 CG MET A1001 -48.617 -15.714 9.435 1.00 99.60 C
ANISOU 1510 CG MET A1001 15144 12576 10123 170 1918 -1130 C
ATOM 1511 SD MET A1001 -50.031 -16.013 8.344 1.00103.85 S
ANISOU 1511 SD MET A1001 15604 13114 10740 198 1938 -1186 S
ATOM 1512 CE MET A1001 -51.172 -14.772 8.940 1.00100.90 C
ANISOU 1512 CE MET A1001 15182 12720 10434 153 2011 -1253 C
ATOM 1513 N LYS A1002 -44.095 -14.116 8.882 1.00 93.22 N
ANISOU 1513 N LYS A1002 14295 11911 9212 267 1772 -1030 N
ATOM 1514 CA LYS A1002 -42.981 -13.427 8.227 1.00 92.82 C
ANISOU 1514 CA LYS A1002 14205 11903 9160 292 1757 -1038 C
ATOM 1515 C LYS A1002 -43.031 -13.510 6.704 1.00 96.16 C
ANISOU 1515 C LYS A1002 14594 12312 9628 350 1743 -1036 C
ATOM 1516 O LYS A1002 -43.503 -14.506 6.152 1.00 95.65 O
ANISOU 1516 O LYS A1002 14530 12227 9585 383 1716 -1019 O
ATOM 1517 CB LYS A1002 -41.630 -13.949 8.751 1.00 95.70 C
ANISOU 1517 CB LYS A1002 14570 12322 9470 302 1695 -1032 C
ATOM 1518 CG LYS A1002 -41.232 -13.409 10.123 1.00110.85 C
ANISOU 1518 CG LYS A1002 16512 14279 11327 236 1706 -1045 C
ATOM 1519 CD LYS A1002 -40.489 -12.077 10.033 1.00121.37 C
ANISOU 1519 CD LYS A1002 17803 15660 12650 197 1752 -1093 C
ATOM 1520 CE LYS A1002 -40.093 -11.559 11.392 1.00133.16 C
ANISOU 1520 CE LYS A1002 19315 17204 14076 119 1769 -1114 C
ATOM 1521 NZ LYS A1002 -39.481 -10.207 11.308 1.00142.39 N
ANISOU 1521 NZ LYS A1002 20450 18416 15235 63 1842 -1172 N
ATOM 1522 N LYS A1003 -42.529 -12.456 6.031 1.00 92.39 N
ANISOU 1522 N LYS A1003 14102 11845 9159 353 1771 -1057 N
ATOM 1523 CA LYS A1003 -42.462 -12.363 4.572 1.00 91.86 C
ANISOU 1523 CA LYS A1003 14025 11760 9120 396 1763 -1058 C
ATOM 1524 C LYS A1003 -41.298 -13.189 4.024 1.00 95.44 C
ANISOU 1524 C LYS A1003 14458 12239 9567 417 1715 -1063 C
ATOM 1525 O LYS A1003 -40.311 -13.411 4.729 1.00 95.24 O
ANISOU 1525 O LYS A1003 14417 12257 9514 405 1693 -1078 O
ATOM 1526 CB LYS A1003 -42.322 -10.899 4.123 1.00 94.44 C
ANISOU 1526 CB LYS A1003 14371 12069 9443 384 1826 -1082 C
ATOM 1527 CG LYS A1003 -43.636 -10.136 4.074 1.00108.88 C
ANISOU 1527 CG LYS A1003 16217 13853 11301 399 1866 -1071 C
ATOM 1528 CD LYS A1003 -43.442 -8.746 3.490 1.00118.95 C
ANISOU 1528 CD LYS A1003 17536 15093 12566 404 1930 -1086 C
ATOM 1529 CE LYS A1003 -44.734 -7.974 3.422 1.00130.40 C
ANISOU 1529 CE LYS A1003 19000 16494 14052 440 1963 -1073 C
ATOM 1530 NZ LYS A1003 -44.538 -6.625 2.830 1.00140.27 N
ANISOU 1530 NZ LYS A1003 20319 17694 15284 456 2031 -1079 N
ATOM 1531 N TYR A1004 -41.420 -13.641 2.766 1.00 91.67 N
ANISOU 1531 N TYR A1004 13978 11738 9115 450 1699 -1056 N
ATOM 1532 CA TYR A1004 -40.397 -14.429 2.080 1.00 91.45 C
ANISOU 1532 CA TYR A1004 13929 11721 9095 465 1667 -1068 C
ATOM 1533 C TYR A1004 -40.137 -13.870 0.684 1.00 95.00 C
ANISOU 1533 C TYR A1004 14395 12145 9554 461 1693 -1092 C
ATOM 1534 O TYR A1004 -41.079 -13.688 -0.090 1.00 94.39 O
ANISOU 1534 O TYR A1004 14345 12035 9484 476 1698 -1071 O
ATOM 1535 CB TYR A1004 -40.788 -15.917 2.033 1.00 92.60 C
ANISOU 1535 CB TYR A1004 14071 11855 9259 494 1628 -1034 C
ATOM 1536 CG TYR A1004 -40.362 -16.698 3.258 1.00 94.60 C
ANISOU 1536 CG TYR A1004 14325 12128 9490 505 1594 -1018 C
ATOM 1537 CD1 TYR A1004 -41.119 -16.671 4.426 1.00 96.67 C
ANISOU 1537 CD1 TYR A1004 14620 12386 9725 486 1602 -999 C
ATOM 1538 CD2 TYR A1004 -39.212 -17.482 3.244 1.00 95.65 C
ANISOU 1538 CD2 TYR A1004 14435 12280 9629 537 1554 -1025 C
ATOM 1539 CE1 TYR A1004 -40.736 -17.394 5.554 1.00 97.90 C
ANISOU 1539 CE1 TYR A1004 14803 12551 9843 495 1567 -978 C
ATOM 1540 CE2 TYR A1004 -38.820 -18.211 4.366 1.00 97.03 C
ANISOU 1540 CE2 TYR A1004 14624 12469 9773 565 1510 -1001 C
ATOM 1541 CZ TYR A1004 -39.585 -18.164 5.520 1.00104.63 C
ANISOU 1541 CZ TYR A1004 15638 13423 10692 543 1514 -974 C
ATOM 1542 OH TYR A1004 -39.202 -18.880 6.628 1.00106.31 O
ANISOU 1542 OH TYR A1004 15891 13644 10859 569 1467 -946 O
ATOM 1543 N THR A1005 -38.863 -13.568 0.377 1.00 91.67 N
ANISOU 1543 N THR A1005 13963 11741 9128 438 1711 -1144 N
ATOM 1544 CA THR A1005 -38.471 -12.996 -0.915 1.00 91.49 C
ANISOU 1544 CA THR A1005 13978 11682 9103 416 1752 -1180 C
ATOM 1545 C THR A1005 -37.706 -13.965 -1.798 1.00 95.12 C
ANISOU 1545 C THR A1005 14413 12135 9593 413 1735 -1206 C
ATOM 1546 O THR A1005 -36.857 -14.718 -1.314 1.00 94.93 O
ANISOU 1546 O THR A1005 14328 12148 9592 423 1706 -1228 O
ATOM 1547 CB THR A1005 -37.706 -11.680 -0.745 1.00100.26 C
ANISOU 1547 CB THR A1005 15115 12800 10181 368 1821 -1243 C
ATOM 1548 OG1 THR A1005 -36.638 -11.856 0.189 1.00100.43 O
ANISOU 1548 OG1 THR A1005 15069 12889 10202 349 1812 -1293 O
ATOM 1549 CG2 THR A1005 -38.605 -10.539 -0.319 1.00 98.95 C
ANISOU 1549 CG2 THR A1005 15001 12608 9987 368 1864 -1216 C
ATOM 1550 N CYS A1006 -38.008 -13.927 -3.106 1.00 91.36 N
ANISOU 1550 N CYS A1006 13988 11611 9116 401 1752 -1203 N
ATOM 1551 CA CYS A1006 -37.375 -14.753 -4.129 1.00 91.12 C
ANISOU 1551 CA CYS A1006 13948 11559 9114 380 1754 -1232 C
ATOM 1552 C CYS A1006 -35.962 -14.240 -4.406 1.00 95.16 C
ANISOU 1552 C CYS A1006 14454 12073 9631 327 1808 -1328 C
ATOM 1553 O CYS A1006 -35.778 -13.054 -4.686 1.00 94.84 O
ANISOU 1553 O CYS A1006 14477 12007 9549 287 1867 -1368 O
ATOM 1554 CB CYS A1006 -38.224 -14.776 -5.398 1.00 91.30 C
ANISOU 1554 CB CYS A1006 14038 11533 9118 371 1756 -1201 C
ATOM 1555 SG CYS A1006 -37.489 -15.703 -6.770 1.00 95.29 S
ANISOU 1555 SG CYS A1006 14550 12002 9654 319 1779 -1243 S
ATOM 1556 N THR A1007 -34.967 -15.136 -4.322 1.00 91.96 N
ANISOU 1556 N THR A1007 13972 11693 9277 327 1794 -1374 N
ATOM 1557 CA THR A1007 -33.560 -14.800 -4.565 1.00 92.30 C
ANISOU 1557 CA THR A1007 13980 11749 9340 275 1845 -1490 C
ATOM 1558 C THR A1007 -33.217 -14.784 -6.066 1.00 96.50 C
ANISOU 1558 C THR A1007 14573 12212 9881 205 1909 -1544 C
ATOM 1559 O THR A1007 -32.110 -14.382 -6.435 1.00 96.49 O
ANISOU 1559 O THR A1007 14561 12207 9894 141 1974 -1659 O
ATOM 1560 CB THR A1007 -32.627 -15.713 -3.748 1.00100.32 C
ANISOU 1560 CB THR A1007 14876 12829 10412 320 1793 -1523 C
ATOM 1561 OG1 THR A1007 -32.922 -17.081 -4.036 1.00 99.70 O
ANISOU 1561 OG1 THR A1007 14776 12724 10380 366 1751 -1466 O
ATOM 1562 CG2 THR A1007 -32.713 -15.457 -2.247 1.00 98.82 C
ANISOU 1562 CG2 THR A1007 14643 12711 10192 365 1742 -1494 C
ATOM 1563 N VAL A1008 -34.173 -15.199 -6.926 1.00 92.94 N
ANISOU 1563 N VAL A1008 14188 11708 9417 208 1896 -1473 N
ATOM 1564 CA VAL A1008 -34.002 -15.261 -8.380 1.00 93.01 C
ANISOU 1564 CA VAL A1008 14273 11648 9420 136 1949 -1511 C
ATOM 1565 C VAL A1008 -34.574 -14.008 -9.073 1.00 97.38 C
ANISOU 1565 C VAL A1008 14970 12145 9887 101 1990 -1498 C
ATOM 1566 O VAL A1008 -33.822 -13.312 -9.759 1.00 97.39 O
ANISOU 1566 O VAL A1008 15046 12097 9862 21 2072 -1584 O
ATOM 1567 CB VAL A1008 -34.542 -16.589 -8.991 1.00 96.65 C
ANISOU 1567 CB VAL A1008 14716 12091 9917 147 1916 -1456 C
ATOM 1568 CG1 VAL A1008 -34.227 -16.685 -10.482 1.00 96.72 C
ANISOU 1568 CG1 VAL A1008 14801 12029 9919 54 1978 -1507 C
ATOM 1569 CG2 VAL A1008 -33.987 -17.807 -8.255 1.00 96.51 C
ANISOU 1569 CG2 VAL A1008 14578 12113 9980 197 1883 -1460 C
ATOM 1570 N CYS A1009 -35.886 -13.726 -8.902 1.00 93.96 N
ANISOU 1570 N CYS A1009 14579 11713 9409 161 1937 -1397 N
ATOM 1571 CA CYS A1009 -36.534 -12.570 -9.535 1.00 94.19 C
ANISOU 1571 CA CYS A1009 14747 11685 9355 156 1959 -1370 C
ATOM 1572 C CYS A1009 -36.727 -11.383 -8.582 1.00 98.57 C
ANISOU 1572 C CYS A1009 15323 12251 9877 191 1979 -1361 C
ATOM 1573 O CYS A1009 -36.472 -10.243 -8.975 1.00 98.64 O
ANISOU 1573 O CYS A1009 15450 12203 9827 155 2052 -1396 O
ATOM 1574 CB CYS A1009 -37.841 -12.965 -10.222 1.00 94.42 C
ANISOU 1574 CB CYS A1009 14815 11705 9357 198 1890 -1281 C
ATOM 1575 SG CYS A1009 -39.210 -13.329 -9.090 1.00 97.88 S
ANISOU 1575 SG CYS A1009 15157 12215 9819 302 1801 -1189 S
ATOM 1576 N GLY A1010 -37.173 -11.661 -7.357 1.00 95.07 N
ANISOU 1576 N GLY A1010 14780 11874 9468 252 1928 -1317 N
ATOM 1577 CA GLY A1010 -37.410 -10.649 -6.334 1.00 95.06 C
ANISOU 1577 CA GLY A1010 14786 11890 9445 277 1950 -1308 C
ATOM 1578 C GLY A1010 -38.857 -10.516 -5.902 1.00 99.12 C
ANISOU 1578 C GLY A1010 15296 12410 9953 354 1891 -1216 C
ATOM 1579 O GLY A1010 -39.271 -9.435 -5.470 1.00 98.91 O
ANISOU 1579 O GLY A1010 15319 12363 9897 375 1924 -1202 O
ATOM 1580 N TYR A1011 -39.636 -11.615 -6.003 1.00 95.62 N
ANISOU 1580 N TYR A1011 14793 11995 9542 393 1816 -1164 N
ATOM 1581 CA TYR A1011 -41.048 -11.650 -5.615 1.00 95.47 C
ANISOU 1581 CA TYR A1011 14751 11993 9529 459 1761 -1098 C
ATOM 1582 C TYR A1011 -41.185 -11.623 -4.095 1.00 99.33 C
ANISOU 1582 C TYR A1011 15168 12526 10046 473 1761 -1093 C
ATOM 1583 O TYR A1011 -40.741 -12.552 -3.416 1.00 98.60 O
ANISOU 1583 O TYR A1011 15004 12475 9985 461 1743 -1102 O
ATOM 1584 CB TYR A1011 -41.765 -12.871 -6.234 1.00 96.55 C
ANISOU 1584 CB TYR A1011 14846 12151 9686 474 1700 -1068 C
ATOM 1585 CG TYR A1011 -43.184 -13.089 -5.747 1.00 98.26 C
ANISOU 1585 CG TYR A1011 15013 12401 9920 530 1650 -1026 C
ATOM 1586 CD1 TYR A1011 -44.234 -12.308 -6.222 1.00100.64 C
ANISOU 1586 CD1 TYR A1011 15355 12689 10197 583 1622 -998 C
ATOM 1587 CD2 TYR A1011 -43.483 -14.102 -4.840 1.00 98.77 C
ANISOU 1587 CD2 TYR A1011 14996 12509 10025 530 1633 -1022 C
ATOM 1588 CE1 TYR A1011 -45.542 -12.509 -5.783 1.00101.66 C
ANISOU 1588 CE1 TYR A1011 15418 12856 10352 631 1580 -981 C
ATOM 1589 CE2 TYR A1011 -44.787 -14.312 -4.394 1.00 99.82 C
ANISOU 1589 CE2 TYR A1011 15083 12669 10174 564 1605 -1005 C
ATOM 1590 CZ TYR A1011 -45.814 -13.512 -4.867 1.00107.85 C
ANISOU 1590 CZ TYR A1011 16117 13682 11178 612 1578 -992 C
ATOM 1591 OH TYR A1011 -47.102 -13.718 -4.434 1.00109.04 O
ANISOU 1591 OH TYR A1011 16205 13868 11357 643 1553 -996 O
ATOM 1592 N ILE A1012 -41.789 -10.545 -3.571 1.00 96.37 N
ANISOU 1592 N ILE A1012 14824 12136 9657 499 1786 -1078 N
ATOM 1593 CA ILE A1012 -42.008 -10.349 -2.137 1.00 96.17 C
ANISOU 1593 CA ILE A1012 14748 12143 9650 498 1800 -1076 C
ATOM 1594 C ILE A1012 -43.339 -11.001 -1.749 1.00100.26 C
ANISOU 1594 C ILE A1012 15211 12681 10203 540 1747 -1037 C
ATOM 1595 O ILE A1012 -44.402 -10.415 -1.978 1.00100.14 O
ANISOU 1595 O ILE A1012 15212 12645 10193 586 1739 -1016 O
ATOM 1596 CB ILE A1012 -41.937 -8.841 -1.733 1.00 99.61 C
ANISOU 1596 CB ILE A1012 15244 12544 10058 488 1877 -1091 C
ATOM 1597 CG1 ILE A1012 -40.711 -8.131 -2.354 1.00100.33 C
ANISOU 1597 CG1 ILE A1012 15410 12604 10105 436 1948 -1146 C
ATOM 1598 CG2 ILE A1012 -41.967 -8.672 -0.206 1.00100.24 C
ANISOU 1598 CG2 ILE A1012 15273 12663 10152 461 1902 -1100 C
ATOM 1599 CD1 ILE A1012 -40.947 -6.674 -2.765 1.00108.53 C
ANISOU 1599 CD1 ILE A1012 16569 13567 11099 447 2026 -1146 C
ATOM 1600 N TYR A1013 -43.282 -12.224 -1.186 1.00 96.77 N
ANISOU 1600 N TYR A1013 14707 12277 9783 526 1714 -1035 N
ATOM 1601 CA TYR A1013 -44.491 -12.924 -0.761 1.00 96.69 C
ANISOU 1601 CA TYR A1013 14654 12284 9801 546 1685 -1018 C
ATOM 1602 C TYR A1013 -44.986 -12.370 0.571 1.00100.97 C
ANISOU 1602 C TYR A1013 15182 12828 10353 534 1716 -1022 C
ATOM 1603 O TYR A1013 -44.272 -12.434 1.575 1.00100.42 O
ANISOU 1603 O TYR A1013 15111 12774 10269 497 1735 -1031 O
ATOM 1604 CB TYR A1013 -44.301 -14.458 -0.707 1.00 97.66 C
ANISOU 1604 CB TYR A1013 14744 12428 9935 531 1657 -1015 C
ATOM 1605 CG TYR A1013 -45.499 -15.186 -0.129 1.00 99.40 C
ANISOU 1605 CG TYR A1013 14933 12660 10175 532 1651 -1015 C
ATOM 1606 CD1 TYR A1013 -46.651 -15.385 -0.886 1.00101.55 C
ANISOU 1606 CD1 TYR A1013 15180 12942 10462 551 1633 -1023 C
ATOM 1607 CD2 TYR A1013 -45.497 -15.638 1.188 1.00100.14 C
ANISOU 1607 CD2 TYR A1013 15026 12757 10266 506 1667 -1016 C
ATOM 1608 CE1 TYR A1013 -47.769 -16.020 -0.348 1.00102.50 C
ANISOU 1608 CE1 TYR A1013 15264 13077 10603 539 1643 -1047 C
ATOM 1609 CE2 TYR A1013 -46.611 -16.269 1.738 1.00101.19 C
ANISOU 1609 CE2 TYR A1013 15145 12889 10412 490 1681 -1032 C
ATOM 1610 CZ TYR A1013 -47.749 -16.449 0.969 1.00108.63 C
ANISOU 1610 CZ TYR A1013 16052 13844 11378 503 1675 -1054 C
ATOM 1611 OH TYR A1013 -48.843 -17.090 1.499 1.00109.63 O
ANISOU 1611 OH TYR A1013 16159 13976 11521 475 1702 -1092 O
ATOM 1612 N ASN A1014 -46.213 -11.831 0.567 1.00 98.12 N
ANISOU 1612 N ASN A1014 14810 12454 10017 565 1721 -1022 N
ATOM 1613 CA ASN A1014 -46.869 -11.280 1.749 1.00 98.22 C
ANISOU 1613 CA ASN A1014 14808 12460 10052 548 1762 -1036 C
ATOM 1614 C ASN A1014 -47.953 -12.268 2.209 1.00102.38 C
ANISOU 1614 C ASN A1014 15285 13005 10612 538 1748 -1055 C
ATOM 1615 O ASN A1014 -48.847 -12.584 1.417 1.00102.17 O
ANISOU 1615 O ASN A1014 15222 12990 10608 576 1715 -1065 O
ATOM 1616 CB ASN A1014 -47.458 -9.891 1.445 1.00 99.49 C
ANISOU 1616 CB ASN A1014 14989 12584 10227 594 1792 -1034 C
ATOM 1617 CG ASN A1014 -48.176 -9.218 2.596 1.00123.72 C
ANISOU 1617 CG ASN A1014 18040 15635 13332 574 1849 -1055 C
ATOM 1618 OD1 ASN A1014 -47.818 -9.358 3.772 1.00118.45 O
ANISOU 1618 OD1 ASN A1014 17373 14977 12655 504 1889 -1069 O
ATOM 1619 ND2 ASN A1014 -49.190 -8.433 2.271 1.00116.42 N
ANISOU 1619 ND2 ASN A1014 17103 14683 12448 636 1855 -1060 N
ATOM 1620 N PRO A1015 -47.884 -12.790 3.462 1.00 99.06 N
ANISOU 1620 N PRO A1015 14867 12587 10184 480 1775 -1067 N
ATOM 1621 CA PRO A1015 -48.904 -13.756 3.917 1.00 99.10 C
ANISOU 1621 CA PRO A1015 14846 12596 10212 454 1782 -1098 C
ATOM 1622 C PRO A1015 -50.322 -13.188 4.003 1.00103.66 C
ANISOU 1622 C PRO A1015 15372 13168 10847 467 1808 -1145 C
ATOM 1623 O PRO A1015 -51.281 -13.955 3.914 1.00103.38 O
ANISOU 1623 O PRO A1015 15296 13147 10837 456 1809 -1189 O
ATOM 1624 CB PRO A1015 -48.386 -14.210 5.287 1.00100.78 C
ANISOU 1624 CB PRO A1015 15106 12799 10389 388 1811 -1096 C
ATOM 1625 CG PRO A1015 -46.945 -13.801 5.324 1.00104.96 C
ANISOU 1625 CG PRO A1015 15664 13340 10876 393 1793 -1061 C
ATOM 1626 CD PRO A1015 -46.881 -12.548 4.517 1.00100.49 C
ANISOU 1626 CD PRO A1015 15085 12770 10328 431 1802 -1059 C
ATOM 1627 N GLU A1016 -50.450 -11.851 4.155 1.00100.78 N
ANISOU 1627 N GLU A1016 15006 12781 10506 489 1836 -1143 N
ATOM 1628 CA GLU A1016 -51.722 -11.126 4.224 1.00101.34 C
ANISOU 1628 CA GLU A1016 15021 12839 10643 520 1860 -1187 C
ATOM 1629 C GLU A1016 -52.466 -11.217 2.880 1.00105.80 C
ANISOU 1629 C GLU A1016 15531 13435 11234 608 1791 -1194 C
ATOM 1630 O GLU A1016 -53.659 -11.528 2.866 1.00105.86 O
ANISOU 1630 O GLU A1016 15462 13467 11294 618 1787 -1256 O
ATOM 1631 CB GLU A1016 -51.475 -9.656 4.622 1.00102.90 C
ANISOU 1631 CB GLU A1016 15250 12995 10852 530 1914 -1172 C
ATOM 1632 CG GLU A1016 -52.737 -8.838 4.852 1.00114.40 C
ANISOU 1632 CG GLU A1016 16650 14426 12390 565 1951 -1219 C
ATOM 1633 CD GLU A1016 -52.541 -7.334 4.830 1.00135.36 C
ANISOU 1633 CD GLU A1016 19346 17030 15056 607 2000 -1194 C
ATOM 1634 OE1 GLU A1016 -52.108 -6.802 3.782 1.00129.72 O
ANISOU 1634 OE1 GLU A1016 18675 16304 14311 686 1962 -1147 O
ATOM 1635 OE2 GLU A1016 -52.859 -6.681 5.850 1.00129.81 O
ANISOU 1635 OE2 GLU A1016 18641 16290 14392 557 2086 -1227 O
ATOM 1636 N ASP A1017 -51.756 -10.957 1.762 1.00102.42 N
ANISOU 1636 N ASP A1017 15143 13008 10764 664 1740 -1140 N
ATOM 1637 CA ASP A1017 -52.315 -11.008 0.409 1.00102.77 C
ANISOU 1637 CA ASP A1017 15157 13082 10810 744 1665 -1136 C
ATOM 1638 C ASP A1017 -52.367 -12.439 -0.130 1.00106.72 C
ANISOU 1638 C ASP A1017 15626 13633 11289 711 1628 -1152 C
ATOM 1639 O ASP A1017 -53.377 -12.835 -0.714 1.00106.76 O
ANISOU 1639 O ASP A1017 15559 13686 11317 741 1587 -1194 O
ATOM 1640 CB ASP A1017 -51.520 -10.103 -0.555 1.00104.62 C
ANISOU 1640 CB ASP A1017 15473 13281 10995 803 1641 -1075 C
ATOM 1641 CG ASP A1017 -51.438 -8.633 -0.174 1.00114.83 C
ANISOU 1641 CG ASP A1017 16817 14513 12299 839 1693 -1057 C
ATOM 1642 OD1 ASP A1017 -52.371 -8.136 0.498 1.00115.81 O
ANISOU 1642 OD1 ASP A1017 16890 14627 12487 859 1723 -1091 O
ATOM 1643 OD2 ASP A1017 -50.462 -7.970 -0.583 1.00120.52 O
ANISOU 1643 OD2 ASP A1017 17631 15192 12967 842 1715 -1019 O
ATOM 1644 N GLY A1018 -51.279 -13.187 0.065 1.00102.94 N
ANISOU 1644 N GLY A1018 15199 13146 10768 652 1644 -1125 N
ATOM 1645 CA GLY A1018 -51.142 -14.563 -0.400 1.00102.69 C
ANISOU 1645 CA GLY A1018 15158 13145 10715 615 1628 -1134 C
ATOM 1646 C GLY A1018 -50.965 -14.648 -1.902 1.00107.04 C
ANISOU 1646 C GLY A1018 15718 13718 11237 655 1569 -1110 C
ATOM 1647 O GLY A1018 -50.271 -13.816 -2.495 1.00106.57 O
ANISOU 1647 O GLY A1018 15714 13629 11150 690 1550 -1067 O
ATOM 1648 N ASP A1019 -51.596 -15.659 -2.526 1.00104.10 N
ANISOU 1648 N ASP A1019 15297 13393 10863 637 1549 -1145 N
ATOM 1649 CA ASP A1019 -51.564 -15.887 -3.975 1.00104.21 C
ANISOU 1649 CA ASP A1019 15315 13436 10842 657 1494 -1131 C
ATOM 1650 C ASP A1019 -52.875 -16.584 -4.419 1.00108.90 C
ANISOU 1650 C ASP A1019 15818 14108 11451 651 1471 -1200 C
ATOM 1651 O ASP A1019 -52.866 -17.793 -4.676 1.00108.32 O
ANISOU 1651 O ASP A1019 15733 14060 11362 587 1499 -1227 O
ATOM 1652 CB ASP A1019 -50.303 -16.691 -4.373 1.00105.42 C
ANISOU 1652 CB ASP A1019 15530 13563 10962 605 1515 -1098 C
ATOM 1653 CG ASP A1019 -50.001 -16.765 -5.862 1.00115.43 C
ANISOU 1653 CG ASP A1019 16829 14840 12188 609 1473 -1079 C
ATOM 1654 OD1 ASP A1019 -50.584 -15.968 -6.633 1.00116.51 O
ANISOU 1654 OD1 ASP A1019 16968 14995 12306 666 1414 -1072 O
ATOM 1655 OD2 ASP A1019 -49.149 -17.590 -6.251 1.00120.83 O
ANISOU 1655 OD2 ASP A1019 17545 15507 12857 556 1499 -1070 O
ATOM 1656 N PRO A1020 -54.027 -15.858 -4.460 1.00106.41 N
ANISOU 1656 N PRO A1020 15430 13831 11168 716 1429 -1238 N
ATOM 1657 CA PRO A1020 -55.297 -16.516 -4.833 1.00107.04 C
ANISOU 1657 CA PRO A1020 15402 14004 11266 706 1408 -1327 C
ATOM 1658 C PRO A1020 -55.418 -16.926 -6.301 1.00111.47 C
ANISOU 1658 C PRO A1020 15953 14627 11773 713 1339 -1324 C
ATOM 1659 O PRO A1020 -56.284 -17.738 -6.632 1.00111.52 O
ANISOU 1659 O PRO A1020 15872 14718 11780 675 1338 -1405 O
ATOM 1660 CB PRO A1020 -56.360 -15.493 -4.429 1.00109.60 C
ANISOU 1660 CB PRO A1020 15646 14346 11649 787 1376 -1369 C
ATOM 1661 CG PRO A1020 -55.674 -14.186 -4.520 1.00113.86 C
ANISOU 1661 CG PRO A1020 16273 14814 12176 867 1347 -1279 C
ATOM 1662 CD PRO A1020 -54.235 -14.424 -4.161 1.00108.29 C
ANISOU 1662 CD PRO A1020 15677 14034 11432 801 1405 -1213 C
ATOM 1663 N ASP A1021 -54.552 -16.370 -7.171 1.00108.02 N
ANISOU 1663 N ASP A1021 15611 14149 11284 750 1292 -1240 N
ATOM 1664 CA ASP A1021 -54.507 -16.659 -8.607 1.00108.32 C
ANISOU 1664 CA ASP A1021 15671 14230 11257 747 1229 -1226 C
ATOM 1665 C ASP A1021 -54.054 -18.102 -8.859 1.00111.65 C
ANISOU 1665 C ASP A1021 16097 14666 11658 629 1296 -1250 C
ATOM 1666 O ASP A1021 -54.536 -18.739 -9.798 1.00111.72 O
ANISOU 1666 O ASP A1021 16069 14751 11631 594 1268 -1288 O
ATOM 1667 CB ASP A1021 -53.574 -15.669 -9.327 1.00110.12 C
ANISOU 1667 CB ASP A1021 16027 14383 11432 796 1189 -1136 C
ATOM 1668 CG ASP A1021 -53.888 -14.210 -9.053 1.00120.90 C
ANISOU 1668 CG ASP A1021 17416 15708 12811 913 1146 -1103 C
ATOM 1669 OD1 ASP A1021 -54.883 -13.701 -9.614 1.00122.58 O
ANISOU 1669 OD1 ASP A1021 17585 15975 13015 1004 1055 -1116 O
ATOM 1670 OD2 ASP A1021 -53.137 -13.578 -8.281 1.00126.13 O
ANISOU 1670 OD2 ASP A1021 18143 16289 13493 915 1204 -1066 O
ATOM 1671 N ASN A1022 -53.139 -18.613 -8.009 1.00107.26 N
ANISOU 1671 N ASN A1022 15589 14040 11123 571 1384 -1230 N
ATOM 1672 CA ASN A1022 -52.604 -19.973 -8.081 1.00106.56 C
ANISOU 1672 CA ASN A1022 15521 13942 11025 473 1460 -1245 C
ATOM 1673 C ASN A1022 -53.391 -20.950 -7.199 1.00110.17 C
ANISOU 1673 C ASN A1022 15915 14432 11514 416 1535 -1324 C
ATOM 1674 O ASN A1022 -53.617 -22.090 -7.610 1.00109.89 O
ANISOU 1674 O ASN A1022 15863 14431 11461 339 1587 -1371 O
ATOM 1675 CB ASN A1022 -51.114 -19.992 -7.726 1.00106.77 C
ANISOU 1675 CB ASN A1022 15639 13874 11054 457 1504 -1180 C
ATOM 1676 CG ASN A1022 -50.229 -19.321 -8.750 1.00129.83 C
ANISOU 1676 CG ASN A1022 18635 16757 13937 474 1462 -1127 C
ATOM 1677 OD1 ASN A1022 -50.323 -18.114 -9.004 1.00124.23 O
ANISOU 1677 OD1 ASN A1022 17955 16037 13211 542 1404 -1098 O
ATOM 1678 ND2 ASN A1022 -49.318 -20.085 -9.333 1.00121.50 N
ANISOU 1678 ND2 ASN A1022 17625 15670 12868 410 1504 -1117 N
ATOM 1679 N GLY A1023 -53.797 -20.498 -6.011 1.00106.46 N
ANISOU 1679 N GLY A1023 15421 13944 11086 443 1554 -1343 N
ATOM 1680 CA GLY A1023 -54.565 -21.302 -5.065 1.00106.39 C
ANISOU 1680 CA GLY A1023 15371 13949 11102 382 1636 -1427 C
ATOM 1681 C GLY A1023 -54.346 -20.984 -3.598 1.00109.60 C
ANISOU 1681 C GLY A1023 15817 14286 11540 385 1683 -1414 C
ATOM 1682 O GLY A1023 -55.119 -21.444 -2.752 1.00109.53 O
ANISOU 1682 O GLY A1023 15782 14282 11551 334 1752 -1493 O
ATOM 1683 N VAL A1024 -53.292 -20.203 -3.281 1.00105.31 N
ANISOU 1683 N VAL A1024 15341 13679 10995 432 1655 -1326 N
ATOM 1684 CA VAL A1024 -52.935 -19.812 -1.910 1.00104.68 C
ANISOU 1684 CA VAL A1024 15305 13537 10932 430 1692 -1305 C
ATOM 1685 C VAL A1024 -53.948 -18.789 -1.364 1.00108.74 C
ANISOU 1685 C VAL A1024 15753 14071 11493 465 1680 -1352 C
ATOM 1686 O VAL A1024 -54.040 -17.674 -1.877 1.00108.46 O
ANISOU 1686 O VAL A1024 15693 14048 11471 540 1615 -1324 O
ATOM 1687 CB VAL A1024 -51.458 -19.324 -1.806 1.00107.90 C
ANISOU 1687 CB VAL A1024 15791 13886 11320 460 1670 -1213 C
ATOM 1688 CG1 VAL A1024 -51.115 -18.866 -0.390 1.00107.46 C
ANISOU 1688 CG1 VAL A1024 15775 13783 11272 453 1702 -1196 C
ATOM 1689 CG2 VAL A1024 -50.484 -20.407 -2.265 1.00107.40 C
ANISOU 1689 CG2 VAL A1024 15780 13801 11228 428 1690 -1181 C
ATOM 1690 N ASN A1025 -54.708 -19.183 -0.329 1.00105.42 N
ANISOU 1690 N ASN A1025 15314 13643 11097 408 1750 -1426 N
ATOM 1691 CA ASN A1025 -55.727 -18.342 0.305 1.00105.68 C
ANISOU 1691 CA ASN A1025 15277 13688 11188 423 1760 -1491 C
ATOM 1692 C ASN A1025 -55.112 -17.158 1.078 1.00108.69 C
ANISOU 1692 C ASN A1025 15706 14008 11582 459 1755 -1427 C
ATOM 1693 O ASN A1025 -54.058 -17.336 1.695 1.00107.55 O
ANISOU 1693 O ASN A1025 15654 13810 11400 429 1779 -1365 O
ATOM 1694 CB ASN A1025 -56.618 -19.182 1.222 1.00107.41 C
ANISOU 1694 CB ASN A1025 15482 13904 11424 327 1859 -1602 C
ATOM 1695 CG ASN A1025 -57.474 -20.175 0.478 1.00133.16 C
ANISOU 1695 CG ASN A1025 18673 17240 14681 284 1879 -1698 C
ATOM 1696 OD1 ASN A1025 -58.521 -19.835 -0.083 1.00128.87 O
ANISOU 1696 OD1 ASN A1025 18006 16779 14181 316 1842 -1781 O
ATOM 1697 ND2 ASN A1025 -57.045 -21.428 0.455 1.00125.28 N
ANISOU 1697 ND2 ASN A1025 17752 16218 13630 213 1941 -1695 N
ATOM 1698 N PRO A1026 -55.739 -15.950 1.064 1.00105.43 N
ANISOU 1698 N PRO A1026 15232 13605 11223 524 1726 -1444 N
ATOM 1699 CA PRO A1026 -55.161 -14.812 1.806 1.00104.83 C
ANISOU 1699 CA PRO A1026 15207 13467 11156 544 1743 -1389 C
ATOM 1700 C PRO A1026 -55.206 -15.022 3.321 1.00108.12 C
ANISOU 1700 C PRO A1026 15662 13835 11581 451 1834 -1426 C
ATOM 1701 O PRO A1026 -56.272 -14.962 3.940 1.00108.24 O
ANISOU 1701 O PRO A1026 15620 13852 11653 414 1886 -1518 O
ATOM 1702 CB PRO A1026 -56.001 -13.609 1.344 1.00107.35 C
ANISOU 1702 CB PRO A1026 15450 13804 11534 641 1700 -1409 C
ATOM 1703 CG PRO A1026 -56.779 -14.091 0.153 1.00112.43 C
ANISOU 1703 CG PRO A1026 16009 14528 12181 688 1628 -1452 C
ATOM 1704 CD PRO A1026 -56.984 -15.551 0.380 1.00107.87 C
ANISOU 1704 CD PRO A1026 15420 13980 11584 586 1678 -1515 C
ATOM 1705 N GLY A1027 -54.037 -15.311 3.884 1.00103.71 N
ANISOU 1705 N GLY A1027 15204 13237 10965 410 1852 -1360 N
ATOM 1706 CA GLY A1027 -53.850 -15.586 5.305 1.00103.30 C
ANISOU 1706 CA GLY A1027 15220 13136 10892 320 1925 -1374 C
ATOM 1707 C GLY A1027 -53.030 -16.834 5.567 1.00106.30 C
ANISOU 1707 C GLY A1027 15690 13499 11201 276 1931 -1338 C
ATOM 1708 O GLY A1027 -52.808 -17.198 6.726 1.00105.81 O
ANISOU 1708 O GLY A1027 15707 13393 11103 206 1981 -1340 O
ATOM 1709 N THR A1028 -52.570 -17.496 4.486 1.00102.30 N
ANISOU 1709 N THR A1028 15178 13020 10670 317 1881 -1302 N
ATOM 1710 CA THR A1028 -51.770 -18.720 4.543 1.00101.68 C
ANISOU 1710 CA THR A1028 15177 12921 10534 294 1885 -1265 C
ATOM 1711 C THR A1028 -50.295 -18.392 4.778 1.00104.62 C
ANISOU 1711 C THR A1028 15606 13278 10868 324 1843 -1179 C
ATOM 1712 O THR A1028 -49.721 -17.570 4.059 1.00103.79 O
ANISOU 1712 O THR A1028 15469 13194 10774 377 1795 -1143 O
ATOM 1713 CB THR A1028 -51.992 -19.572 3.275 1.00109.28 C
ANISOU 1713 CB THR A1028 16103 13921 11499 312 1867 -1279 C
ATOM 1714 OG1 THR A1028 -53.389 -19.648 2.985 1.00109.24 O
ANISOU 1714 OG1 THR A1028 16017 13955 11534 289 1895 -1373 O
ATOM 1715 CG2 THR A1028 -51.416 -20.980 3.398 1.00107.84 C
ANISOU 1715 CG2 THR A1028 16004 13705 11267 280 1898 -1258 C
ATOM 1716 N ASP A1029 -49.689 -19.045 5.787 1.00101.02 N
ANISOU 1716 N ASP A1029 15240 12784 10360 290 1862 -1154 N
ATOM 1717 CA ASP A1029 -48.276 -18.901 6.145 1.00100.46 C
ANISOU 1717 CA ASP A1029 15213 12710 10247 318 1816 -1087 C
ATOM 1718 C ASP A1029 -47.423 -19.573 5.064 1.00103.54 C
ANISOU 1718 C ASP A1029 15592 13114 10635 371 1772 -1051 C
ATOM 1719 O ASP A1029 -47.892 -20.518 4.422 1.00103.16 O
ANISOU 1719 O ASP A1029 15543 13059 10595 366 1792 -1068 O
ATOM 1720 CB ASP A1029 -48.012 -19.540 7.521 1.00102.72 C
ANISOU 1720 CB ASP A1029 15604 12954 10471 274 1839 -1074 C
ATOM 1721 CG ASP A1029 -46.631 -19.273 8.086 1.00112.95 C
ANISOU 1721 CG ASP A1029 16931 14263 11720 303 1783 -1018 C
ATOM 1722 OD1 ASP A1029 -46.404 -18.156 8.596 1.00113.41 O
ANISOU 1722 OD1 ASP A1029 16969 14344 11777 283 1781 -1021 O
ATOM 1723 OD2 ASP A1029 -45.784 -20.190 8.040 1.00119.20 O
ANISOU 1723 OD2 ASP A1029 17767 15046 12478 344 1744 -977 O
ATOM 1724 N PHE A1030 -46.184 -19.082 4.854 1.00 99.54 N
ANISOU 1724 N PHE A1030 15074 12627 10120 410 1723 -1012 N
ATOM 1725 CA PHE A1030 -45.262 -19.614 3.844 1.00 99.02 C
ANISOU 1725 CA PHE A1030 14993 12569 10062 453 1688 -988 C
ATOM 1726 C PHE A1030 -44.927 -21.098 4.044 1.00102.60 C
ANISOU 1726 C PHE A1030 15503 12988 10492 463 1693 -968 C
ATOM 1727 O PHE A1030 -44.777 -21.821 3.059 1.00102.05 O
ANISOU 1727 O PHE A1030 15420 12912 10441 478 1697 -967 O
ATOM 1728 CB PHE A1030 -43.986 -18.762 3.737 1.00100.70 C
ANISOU 1728 CB PHE A1030 15180 12809 10271 479 1649 -975 C
ATOM 1729 CG PHE A1030 -43.098 -19.128 2.569 1.00102.15 C
ANISOU 1729 CG PHE A1030 15338 12998 10476 510 1626 -971 C
ATOM 1730 CD1 PHE A1030 -43.400 -18.696 1.282 1.00104.99 C
ANISOU 1730 CD1 PHE A1030 15667 13362 10862 509 1632 -986 C
ATOM 1731 CD2 PHE A1030 -41.969 -19.917 2.754 1.00104.59 C
ANISOU 1731 CD2 PHE A1030 15656 13305 10779 540 1597 -956 C
ATOM 1732 CE1 PHE A1030 -42.589 -19.050 0.201 1.00105.83 C
ANISOU 1732 CE1 PHE A1030 15761 13465 10986 519 1623 -990 C
ATOM 1733 CE2 PHE A1030 -41.158 -20.270 1.671 1.00107.37 C
ANISOU 1733 CE2 PHE A1030 15977 13655 11162 560 1588 -965 C
ATOM 1734 CZ PHE A1030 -41.476 -19.837 0.403 1.00105.13 C
ANISOU 1734 CZ PHE A1030 15671 13370 10902 539 1607 -984 C
ATOM 1735 N LYS A1031 -44.824 -21.546 5.306 1.00 99.16 N
ANISOU 1735 N LYS A1031 15143 12524 10009 453 1698 -951 N
ATOM 1736 CA LYS A1031 -44.537 -22.942 5.644 1.00 99.30 C
ANISOU 1736 CA LYS A1031 15246 12492 9992 473 1708 -923 C
ATOM 1737 C LYS A1031 -45.764 -23.837 5.408 1.00102.92 C
ANISOU 1737 C LYS A1031 15745 12910 10449 423 1790 -960 C
ATOM 1738 O LYS A1031 -45.606 -25.031 5.146 1.00102.73 O
ANISOU 1738 O LYS A1031 15777 12842 10412 437 1819 -946 O
ATOM 1739 CB LYS A1031 -44.032 -23.060 7.092 1.00102.44 C
ANISOU 1739 CB LYS A1031 15731 12868 10322 481 1680 -890 C
ATOM 1740 CG LYS A1031 -42.633 -22.487 7.294 1.00117.40 C
ANISOU 1740 CG LYS A1031 17581 14815 12211 537 1596 -863 C
ATOM 1741 CD LYS A1031 -42.247 -22.427 8.762 1.00128.78 C
ANISOU 1741 CD LYS A1031 19101 16255 13576 536 1558 -836 C
ATOM 1742 CE LYS A1031 -40.895 -21.786 8.953 1.00140.57 C
ANISOU 1742 CE LYS A1031 20528 17821 15063 582 1475 -830 C
ATOM 1743 NZ LYS A1031 -40.543 -21.661 10.391 1.00151.01 N
ANISOU 1743 NZ LYS A1031 21921 19157 16299 574 1431 -808 N
ATOM 1744 N ASP A1032 -46.978 -23.249 5.481 1.00 99.16 N
ANISOU 1744 N ASP A1032 15235 12449 9991 364 1833 -1015 N
ATOM 1745 CA ASP A1032 -48.263 -23.928 5.280 1.00 99.12 C
ANISOU 1745 CA ASP A1032 15244 12426 9991 302 1916 -1079 C
ATOM 1746 C ASP A1032 -48.632 -24.101 3.795 1.00102.42 C
ANISOU 1746 C ASP A1032 15573 12887 10454 307 1920 -1109 C
ATOM 1747 O ASP A1032 -49.555 -24.858 3.483 1.00102.25 O
ANISOU 1747 O ASP A1032 15556 12861 10432 256 1991 -1168 O
ATOM 1748 CB ASP A1032 -49.382 -23.189 6.041 1.00101.09 C
ANISOU 1748 CB ASP A1032 15479 12680 10250 239 1958 -1141 C
ATOM 1749 CG ASP A1032 -49.266 -23.208 7.558 1.00110.86 C
ANISOU 1749 CG ASP A1032 16828 13863 11429 201 1981 -1129 C
ATOM 1750 OD1 ASP A1032 -48.132 -23.364 8.070 1.00111.24 O
ANISOU 1750 OD1 ASP A1032 16941 13894 11430 246 1927 -1057 O
ATOM 1751 OD2 ASP A1032 -50.300 -23.026 8.233 1.00117.08 O
ANISOU 1751 OD2 ASP A1032 17636 14632 12219 124 2049 -1197 O
ATOM 1752 N ILE A1033 -47.911 -23.402 2.891 1.00 98.36 N
ANISOU 1752 N ILE A1033 14986 12415 9973 358 1852 -1076 N
ATOM 1753 CA ILE A1033 -48.095 -23.446 1.433 1.00 97.91 C
ANISOU 1753 CA ILE A1033 14858 12397 9947 363 1841 -1093 C
ATOM 1754 C ILE A1033 -47.803 -24.865 0.888 1.00101.77 C
ANISOU 1754 C ILE A1033 15390 12854 10423 349 1889 -1089 C
ATOM 1755 O ILE A1033 -46.816 -25.467 1.318 1.00101.49 O
ANISOU 1755 O ILE A1033 15420 12771 10372 382 1885 -1041 O
ATOM 1756 CB ILE A1033 -47.214 -22.341 0.761 1.00100.58 C
ANISOU 1756 CB ILE A1033 15145 12765 10307 413 1768 -1056 C
ATOM 1757 CG1 ILE A1033 -47.890 -20.956 0.851 1.00100.91 C
ANISOU 1757 CG1 ILE A1033 15134 12840 10366 420 1743 -1077 C
ATOM 1758 CG2 ILE A1033 -46.812 -22.675 -0.689 1.00101.14 C
ANISOU 1758 CG2 ILE A1033 15186 12849 10392 418 1756 -1053 C
ATOM 1759 CD1 ILE A1033 -46.993 -19.780 0.474 1.00107.67 C
ANISOU 1759 CD1 ILE A1033 15974 13706 11228 460 1693 -1044 C
ATOM 1760 N PRO A1034 -48.627 -25.413 -0.051 1.00 98.25 N
ANISOU 1760 N PRO A1034 14908 12436 9985 303 1934 -1141 N
ATOM 1761 CA PRO A1034 -48.334 -26.755 -0.594 1.00 98.19 C
ANISOU 1761 CA PRO A1034 14948 12394 9968 279 1998 -1141 C
ATOM 1762 C PRO A1034 -46.971 -26.827 -1.286 1.00101.57 C
ANISOU 1762 C PRO A1034 15373 12803 10418 327 1956 -1083 C
ATOM 1763 O PRO A1034 -46.522 -25.842 -1.872 1.00100.72 O
ANISOU 1763 O PRO A1034 15205 12731 10332 355 1886 -1067 O
ATOM 1764 CB PRO A1034 -49.486 -27.006 -1.575 1.00100.14 C
ANISOU 1764 CB PRO A1034 15130 12702 10219 214 2040 -1218 C
ATOM 1765 CG PRO A1034 -50.559 -26.057 -1.170 1.00104.70 C
ANISOU 1765 CG PRO A1034 15643 13332 10806 206 2013 -1269 C
ATOM 1766 CD PRO A1034 -49.840 -24.845 -0.672 1.00 99.84 C
ANISOU 1766 CD PRO A1034 15021 12708 10206 275 1928 -1207 C
ATOM 1767 N ASP A1035 -46.311 -27.991 -1.192 1.00 98.30 N
ANISOU 1767 N ASP A1035 15029 12324 9997 336 2006 -1057 N
ATOM 1768 CA ASP A1035 -44.971 -28.244 -1.732 1.00 97.92 C
ANISOU 1768 CA ASP A1035 14977 12246 9981 383 1980 -1015 C
ATOM 1769 C ASP A1035 -44.870 -28.176 -3.267 1.00100.93 C
ANISOU 1769 C ASP A1035 15294 12661 10394 343 1986 -1040 C
ATOM 1770 O ASP A1035 -43.772 -27.964 -3.786 1.00100.27 O
ANISOU 1770 O ASP A1035 15187 12567 10346 372 1952 -1020 O
ATOM 1771 CB ASP A1035 -44.426 -29.579 -1.205 1.00100.41 C
ANISOU 1771 CB ASP A1035 15391 12476 10285 413 2040 -984 C
ATOM 1772 CG ASP A1035 -44.385 -29.646 0.310 1.00111.26 C
ANISOU 1772 CG ASP A1035 16852 13808 11613 458 2022 -951 C
ATOM 1773 OD1 ASP A1035 -43.505 -28.991 0.910 1.00111.80 O
ANISOU 1773 OD1 ASP A1035 16904 13888 11686 526 1932 -911 O
ATOM 1774 OD2 ASP A1035 -45.231 -30.355 0.895 1.00117.81 O
ANISOU 1774 OD2 ASP A1035 17771 14595 12395 415 2103 -971 O
ATOM 1775 N ASP A1036 -46.001 -28.331 -3.984 1.00 97.20 N
ANISOU 1775 N ASP A1036 14792 12233 9905 270 2029 -1091 N
ATOM 1776 CA ASP A1036 -46.044 -28.270 -5.449 1.00 96.77 C
ANISOU 1776 CA ASP A1036 14689 12217 9863 220 2032 -1117 C
ATOM 1777 C ASP A1036 -46.045 -26.827 -5.995 1.00 99.87 C
ANISOU 1777 C ASP A1036 15024 12666 10257 241 1936 -1112 C
ATOM 1778 O ASP A1036 -45.800 -26.626 -7.187 1.00 99.41 O
ANISOU 1778 O ASP A1036 14946 12624 10201 209 1923 -1120 O
ATOM 1779 CB ASP A1036 -47.231 -29.081 -6.000 1.00 98.99 C
ANISOU 1779 CB ASP A1036 14962 12534 10115 131 2115 -1181 C
ATOM 1780 CG ASP A1036 -48.592 -28.572 -5.572 1.00109.02 C
ANISOU 1780 CG ASP A1036 16190 13873 11360 114 2099 -1233 C
ATOM 1781 OD1 ASP A1036 -48.977 -28.816 -4.409 1.00109.83 O
ANISOU 1781 OD1 ASP A1036 16334 13946 11450 121 2134 -1243 O
ATOM 1782 OD2 ASP A1036 -49.283 -27.953 -6.409 1.00114.70 O
ANISOU 1782 OD2 ASP A1036 16837 14674 12070 92 2051 -1268 O
ATOM 1783 N TRP A1037 -46.310 -25.834 -5.120 1.00 95.90 N
ANISOU 1783 N TRP A1037 14507 12182 9747 289 1877 -1099 N
ATOM 1784 CA TRP A1037 -46.355 -24.408 -5.457 1.00 95.29 C
ANISOU 1784 CA TRP A1037 14394 12143 9668 319 1797 -1091 C
ATOM 1785 C TRP A1037 -44.971 -23.851 -5.797 1.00 98.38 C
ANISOU 1785 C TRP A1037 14800 12503 10078 346 1766 -1061 C
ATOM 1786 O TRP A1037 -43.989 -24.157 -5.116 1.00 97.83 O
ANISOU 1786 O TRP A1037 14750 12393 10029 375 1774 -1040 O
ATOM 1787 CB TRP A1037 -46.997 -23.611 -4.304 1.00 94.01 C
ANISOU 1787 CB TRP A1037 14220 11998 9501 356 1768 -1091 C
ATOM 1788 CG TRP A1037 -47.081 -22.124 -4.510 1.00 94.81 C
ANISOU 1788 CG TRP A1037 14297 12125 9601 395 1701 -1080 C
ATOM 1789 CD1 TRP A1037 -48.121 -21.431 -5.056 1.00 97.98 C
ANISOU 1789 CD1 TRP A1037 14658 12577 9994 403 1665 -1104 C
ATOM 1790 CD2 TRP A1037 -46.115 -21.144 -4.102 1.00 94.34 C
ANISOU 1790 CD2 TRP A1037 14257 12042 9547 434 1669 -1048 C
ATOM 1791 NE1 TRP A1037 -47.850 -20.082 -5.044 1.00 97.32 N
ANISOU 1791 NE1 TRP A1037 14583 12486 9908 451 1617 -1078 N
ATOM 1792 CE2 TRP A1037 -46.624 -19.877 -4.466 1.00 98.33 C
ANISOU 1792 CE2 TRP A1037 14748 12570 10042 461 1627 -1049 C
ATOM 1793 CE3 TRP A1037 -44.852 -21.214 -3.489 1.00 95.37 C
ANISOU 1793 CE3 TRP A1037 14413 12138 9687 450 1673 -1025 C
ATOM 1794 CZ2 TRP A1037 -45.918 -18.690 -4.232 1.00 97.44 C
ANISOU 1794 CZ2 TRP A1037 14659 12437 9926 491 1609 -1029 C
ATOM 1795 CZ3 TRP A1037 -44.154 -20.038 -3.256 1.00 96.66 C
ANISOU 1795 CZ3 TRP A1037 14581 12299 9848 475 1646 -1016 C
ATOM 1796 CH2 TRP A1037 -44.686 -18.795 -3.626 1.00 97.31 C
ANISOU 1796 CH2 TRP A1037 14662 12395 9917 488 1624 -1018 C
ATOM 1797 N VAL A1038 -44.914 -23.016 -6.848 1.00 94.56 N
ANISOU 1797 N VAL A1038 14311 12037 9582 335 1731 -1066 N
ATOM 1798 CA VAL A1038 -43.705 -22.333 -7.324 1.00 94.02 C
ANISOU 1798 CA VAL A1038 14264 11937 9523 341 1715 -1059 C
ATOM 1799 C VAL A1038 -43.945 -20.814 -7.416 1.00 97.30 C
ANISOU 1799 C VAL A1038 14691 12368 9910 372 1664 -1052 C
ATOM 1800 O VAL A1038 -45.090 -20.372 -7.281 1.00 97.01 O
ANISOU 1800 O VAL A1038 14638 12368 9853 394 1633 -1049 O
ATOM 1801 CB VAL A1038 -43.117 -22.929 -8.637 1.00 98.08 C
ANISOU 1801 CB VAL A1038 14796 12425 10045 278 1752 -1080 C
ATOM 1802 CG1 VAL A1038 -42.455 -24.281 -8.390 1.00 97.98 C
ANISOU 1802 CG1 VAL A1038 14778 12374 10076 264 1813 -1084 C
ATOM 1803 CG2 VAL A1038 -44.163 -23.018 -9.748 1.00 98.17 C
ANISOU 1803 CG2 VAL A1038 14811 12476 10014 229 1745 -1094 C
ATOM 1804 N CYS A1039 -42.869 -20.026 -7.634 1.00 93.34 N
ANISOU 1804 N CYS A1039 14220 11835 9410 372 1663 -1057 N
ATOM 1805 CA CYS A1039 -42.919 -18.564 -7.754 1.00 93.03 C
ANISOU 1805 CA CYS A1039 14219 11791 9338 397 1637 -1052 C
ATOM 1806 C CYS A1039 -43.850 -18.124 -8.904 1.00 96.62 C
ANISOU 1806 C CYS A1039 14709 12257 9745 393 1604 -1044 C
ATOM 1807 O CYS A1039 -43.714 -18.640 -10.016 1.00 96.32 O
ANISOU 1807 O CYS A1039 14697 12210 9691 341 1615 -1056 O
ATOM 1808 CB CYS A1039 -41.513 -17.989 -7.915 1.00 93.32 C
ANISOU 1808 CB CYS A1039 14289 11788 9381 374 1667 -1080 C
ATOM 1809 SG CYS A1039 -41.445 -16.178 -7.947 1.00 97.37 S
ANISOU 1809 SG CYS A1039 14873 12278 9846 394 1667 -1082 S
ATOM 1810 N PRO A1040 -44.806 -17.190 -8.671 1.00 92.87 N
ANISOU 1810 N PRO A1040 14237 11802 9246 449 1562 -1025 N
ATOM 1811 CA PRO A1040 -45.711 -16.787 -9.764 1.00 93.01 C
ANISOU 1811 CA PRO A1040 14286 11839 9215 465 1511 -1015 C
ATOM 1812 C PRO A1040 -45.095 -15.852 -10.816 1.00 96.45 C
ANISOU 1812 C PRO A1040 14836 12217 9593 454 1510 -1007 C
ATOM 1813 O PRO A1040 -45.801 -15.429 -11.735 1.00 96.52 O
ANISOU 1813 O PRO A1040 14892 12235 9547 478 1458 -990 O
ATOM 1814 CB PRO A1040 -46.890 -16.147 -9.026 1.00 95.03 C
ANISOU 1814 CB PRO A1040 14495 12131 9480 541 1469 -1004 C
ATOM 1815 CG PRO A1040 -46.304 -15.615 -7.776 1.00 99.08 C
ANISOU 1815 CG PRO A1040 15006 12615 10025 557 1507 -1000 C
ATOM 1816 CD PRO A1040 -45.131 -16.485 -7.412 1.00 94.17 C
ANISOU 1816 CD PRO A1040 14376 11976 9430 501 1557 -1014 C
ATOM 1817 N LEU A1041 -43.783 -15.551 -10.702 1.00 92.23 N
ANISOU 1817 N LEU A1041 14351 11626 9068 414 1569 -1027 N
ATOM 1818 CA LEU A1041 -43.075 -14.671 -11.636 1.00 92.14 C
ANISOU 1818 CA LEU A1041 14464 11545 8999 382 1596 -1038 C
ATOM 1819 C LEU A1041 -41.933 -15.352 -12.401 1.00 95.42 C
ANISOU 1819 C LEU A1041 14909 11922 9423 283 1656 -1085 C
ATOM 1820 O LEU A1041 -41.680 -14.976 -13.547 1.00 95.46 O
ANISOU 1820 O LEU A1041 15026 11876 9368 234 1670 -1096 O
ATOM 1821 CB LEU A1041 -42.567 -13.392 -10.938 1.00 92.15 C
ANISOU 1821 CB LEU A1041 14517 11505 8991 412 1634 -1043 C
ATOM 1822 CG LEU A1041 -43.600 -12.488 -10.240 1.00 96.98 C
ANISOU 1822 CG LEU A1041 15120 12132 9595 507 1594 -1002 C
ATOM 1823 CD1 LEU A1041 -42.916 -11.338 -9.539 1.00 97.12 C
ANISOU 1823 CD1 LEU A1041 15190 12105 9607 511 1659 -1018 C
ATOM 1824 CD2 LEU A1041 -44.634 -11.939 -11.218 1.00100.13 C
ANISOU 1824 CD2 LEU A1041 15593 12522 9930 566 1528 -961 C
ATOM 1825 N CYS A1042 -41.240 -16.332 -11.778 1.00 91.15 N
ANISOU 1825 N CYS A1042 14278 11399 8956 253 1692 -1114 N
ATOM 1826 CA CYS A1042 -40.118 -17.036 -12.411 1.00 90.77 C
ANISOU 1826 CA CYS A1042 14237 11313 8939 166 1754 -1168 C
ATOM 1827 C CYS A1042 -40.202 -18.576 -12.314 1.00 94.13 C
ANISOU 1827 C CYS A1042 14573 11769 9424 146 1762 -1169 C
ATOM 1828 O CYS A1042 -39.425 -19.268 -12.974 1.00 93.92 O
ANISOU 1828 O CYS A1042 14550 11708 9428 73 1816 -1212 O
ATOM 1829 CB CYS A1042 -38.784 -16.513 -11.888 1.00 90.96 C
ANISOU 1829 CB CYS A1042 14259 11305 8996 147 1812 -1228 C
ATOM 1830 SG CYS A1042 -38.518 -16.793 -10.120 1.00 94.40 S
ANISOU 1830 SG CYS A1042 14570 11798 9498 219 1793 -1220 S
ATOM 1831 N GLY A1043 -41.138 -19.086 -11.516 1.00 90.19 N
ANISOU 1831 N GLY A1043 14003 11325 8940 204 1722 -1129 N
ATOM 1832 CA GLY A1043 -41.368 -20.519 -11.353 1.00 89.80 C
ANISOU 1832 CA GLY A1043 13889 11297 8933 187 1742 -1127 C
ATOM 1833 C GLY A1043 -40.293 -21.294 -10.617 1.00 93.30 C
ANISOU 1833 C GLY A1043 14282 11718 9450 194 1784 -1148 C
ATOM 1834 O GLY A1043 -39.946 -22.404 -11.031 1.00 92.91 O
ANISOU 1834 O GLY A1043 14216 11647 9439 151 1832 -1166 O
ATOM 1835 N VAL A1044 -39.774 -20.732 -9.510 1.00 89.60 N
ANISOU 1835 N VAL A1044 13788 11257 9001 251 1765 -1147 N
ATOM 1836 CA VAL A1044 -38.757 -21.395 -8.681 1.00 89.37 C
ANISOU 1836 CA VAL A1044 13705 11218 9033 280 1782 -1164 C
ATOM 1837 C VAL A1044 -39.392 -22.021 -7.432 1.00 92.91 C
ANISOU 1837 C VAL A1044 14122 11695 9486 343 1754 -1117 C
ATOM 1838 O VAL A1044 -40.424 -21.537 -6.958 1.00 92.27 O
ANISOU 1838 O VAL A1044 14048 11644 9365 366 1723 -1087 O
ATOM 1839 CB VAL A1044 -37.523 -20.510 -8.340 1.00 93.38 C
ANISOU 1839 CB VAL A1044 14200 11721 9558 286 1786 -1213 C
ATOM 1840 CG1 VAL A1044 -36.788 -20.068 -9.601 1.00 93.39 C
ANISOU 1840 CG1 VAL A1044 14246 11679 9558 204 1837 -1278 C
ATOM 1841 CG2 VAL A1044 -37.897 -19.311 -7.471 1.00 93.06 C
ANISOU 1841 CG2 VAL A1044 14171 11714 9473 326 1750 -1193 C
ATOM 1842 N GLY A1045 -38.760 -23.073 -6.912 1.00 89.58 N
ANISOU 1842 N GLY A1045 13671 11255 9110 371 1770 -1116 N
ATOM 1843 CA GLY A1045 -39.216 -23.789 -5.725 1.00 89.46 C
ANISOU 1843 CA GLY A1045 13653 11247 9090 427 1755 -1074 C
ATOM 1844 C GLY A1045 -39.182 -22.975 -4.445 1.00 93.11 C
ANISOU 1844 C GLY A1045 14107 11742 9527 479 1703 -1056 C
ATOM 1845 O GLY A1045 -38.581 -21.896 -4.402 1.00 92.68 O
ANISOU 1845 O GLY A1045 14037 11708 9468 478 1683 -1083 O
ATOM 1846 N LYS A1046 -39.829 -23.501 -3.387 1.00 89.50 N
ANISOU 1846 N LYS A1046 13671 11286 9047 513 1694 -1018 N
ATOM 1847 CA LYS A1046 -39.909 -22.875 -2.060 1.00 89.22 C
ANISOU 1847 CA LYS A1046 13640 11277 8980 550 1652 -999 C
ATOM 1848 C LYS A1046 -38.540 -22.749 -1.381 1.00 93.22 C
ANISOU 1848 C LYS A1046 14117 11799 9503 599 1612 -1010 C
ATOM 1849 O LYS A1046 -38.342 -21.839 -0.573 1.00 92.81 O
ANISOU 1849 O LYS A1046 14054 11784 9425 608 1580 -1014 O
ATOM 1850 CB LYS A1046 -40.883 -23.646 -1.159 1.00 91.88 C
ANISOU 1850 CB LYS A1046 14026 11597 9286 559 1667 -965 C
ATOM 1851 CG LYS A1046 -42.356 -23.349 -1.438 1.00105.29 C
ANISOU 1851 CG LYS A1046 15732 13311 10963 513 1693 -975 C
ATOM 1852 CD LYS A1046 -43.291 -24.291 -0.676 1.00115.36 C
ANISOU 1852 CD LYS A1046 17059 14562 12212 501 1734 -967 C
ATOM 1853 CE LYS A1046 -43.475 -23.911 0.776 1.00125.74 C
ANISOU 1853 CE LYS A1046 18408 15876 13492 517 1714 -951 C
ATOM 1854 NZ LYS A1046 -44.059 -25.024 1.567 1.00134.88 N
ANISOU 1854 NZ LYS A1046 19646 16985 14615 505 1764 -944 N
ATOM 1855 N ASP A1047 -37.599 -23.652 -1.725 1.00 90.04 N
ANISOU 1855 N ASP A1047 13694 11371 9147 628 1617 -1022 N
ATOM 1856 CA ASP A1047 -36.228 -23.695 -1.206 1.00 90.42 C
ANISOU 1856 CA ASP A1047 13691 11440 9223 686 1572 -1047 C
ATOM 1857 C ASP A1047 -35.365 -22.501 -1.654 1.00 94.01 C
ANISOU 1857 C ASP A1047 14085 11939 9696 650 1569 -1120 C
ATOM 1858 O ASP A1047 -34.322 -22.245 -1.047 1.00 93.99 O
ANISOU 1858 O ASP A1047 14027 11981 9705 688 1527 -1157 O
ATOM 1859 CB ASP A1047 -35.550 -25.029 -1.573 1.00 92.86 C
ANISOU 1859 CB ASP A1047 13992 11701 9591 732 1588 -1047 C
ATOM 1860 CG ASP A1047 -35.626 -25.382 -3.045 1.00103.04 C
ANISOU 1860 CG ASP A1047 15275 12949 10927 665 1661 -1079 C
ATOM 1861 OD1 ASP A1047 -34.800 -24.859 -3.825 1.00103.74 O
ANISOU 1861 OD1 ASP A1047 15310 13047 11059 629 1675 -1146 O
ATOM 1862 OD2 ASP A1047 -36.507 -26.185 -3.417 1.00108.68 O
ANISOU 1862 OD2 ASP A1047 16043 13620 11631 638 1712 -1046 O
ATOM 1863 N GLN A1048 -35.802 -21.775 -2.704 1.00 90.06 N
ANISOU 1863 N GLN A1048 13601 11426 9190 576 1615 -1145 N
ATOM 1864 CA GLN A1048 -35.096 -20.612 -3.253 1.00 89.81 C
ANISOU 1864 CA GLN A1048 13546 11416 9163 526 1637 -1218 C
ATOM 1865 C GLN A1048 -35.593 -19.271 -2.672 1.00 93.46 C
ANISOU 1865 C GLN A1048 14034 11912 9565 508 1632 -1212 C
ATOM 1866 O GLN A1048 -35.265 -18.207 -3.206 1.00 93.02 O
ANISOU 1866 O GLN A1048 13991 11858 9496 457 1669 -1265 O
ATOM 1867 CB GLN A1048 -35.138 -20.618 -4.798 1.00 90.92 C
ANISOU 1867 CB GLN A1048 13714 11508 9325 456 1697 -1252 C
ATOM 1868 CG GLN A1048 -34.462 -21.829 -5.459 1.00105.02 C
ANISOU 1868 CG GLN A1048 15468 13255 11181 455 1725 -1279 C
ATOM 1869 CD GLN A1048 -32.998 -21.988 -5.111 1.00123.83 C
ANISOU 1869 CD GLN A1048 17766 15660 13625 489 1712 -1353 C
ATOM 1870 OE1 GLN A1048 -32.191 -21.059 -5.231 1.00119.13 O
ANISOU 1870 OE1 GLN A1048 17138 15093 13034 452 1728 -1437 O
ATOM 1871 NE2 GLN A1048 -32.621 -23.184 -4.685 1.00116.34 N
ANISOU 1871 NE2 GLN A1048 16780 14699 12725 563 1687 -1331 N
ATOM 1872 N PHE A1049 -36.357 -19.327 -1.563 1.00 89.93 N
ANISOU 1872 N PHE A1049 13605 11483 9082 543 1597 -1152 N
ATOM 1873 CA PHE A1049 -36.898 -18.155 -0.871 1.00 89.53 C
ANISOU 1873 CA PHE A1049 13577 11459 8982 526 1599 -1143 C
ATOM 1874 C PHE A1049 -36.224 -17.951 0.486 1.00 93.74 C
ANISOU 1874 C PHE A1049 14076 12048 9494 551 1560 -1154 C
ATOM 1875 O PHE A1049 -35.992 -18.922 1.212 1.00 93.56 O
ANISOU 1875 O PHE A1049 14042 12033 9473 603 1512 -1124 O
ATOM 1876 CB PHE A1049 -38.416 -18.292 -0.681 1.00 90.99 C
ANISOU 1876 CB PHE A1049 13808 11621 9143 529 1600 -1081 C
ATOM 1877 CG PHE A1049 -39.259 -17.988 -1.897 1.00 92.22 C
ANISOU 1877 CG PHE A1049 13996 11745 9299 500 1629 -1077 C
ATOM 1878 CD1 PHE A1049 -39.499 -18.963 -2.859 1.00 95.28 C
ANISOU 1878 CD1 PHE A1049 14388 12106 9709 492 1637 -1070 C
ATOM 1879 CD2 PHE A1049 -39.854 -16.743 -2.056 1.00 94.22 C
ANISOU 1879 CD2 PHE A1049 14279 11996 9525 485 1646 -1079 C
ATOM 1880 CE1 PHE A1049 -40.294 -18.685 -3.975 1.00 96.08 C
ANISOU 1880 CE1 PHE A1049 14519 12190 9798 465 1651 -1067 C
ATOM 1881 CE2 PHE A1049 -40.651 -16.467 -3.171 1.00 96.95 C
ANISOU 1881 CE2 PHE A1049 14659 12317 9862 475 1654 -1069 C
ATOM 1882 CZ PHE A1049 -40.865 -17.439 -4.123 1.00 95.08 C
ANISOU 1882 CZ PHE A1049 14421 12065 9639 464 1651 -1064 C
ATOM 1883 N GLU A1050 -35.925 -16.685 0.829 1.00 90.44 N
ANISOU 1883 N GLU A1050 13651 11666 9046 513 1584 -1197 N
ATOM 1884 CA GLU A1050 -35.293 -16.308 2.098 1.00 90.79 C
ANISOU 1884 CA GLU A1050 13661 11778 9057 518 1554 -1219 C
ATOM 1885 C GLU A1050 -36.251 -15.534 3.013 1.00 94.52 C
ANISOU 1885 C GLU A1050 14180 12254 9481 491 1572 -1181 C
ATOM 1886 O GLU A1050 -37.065 -14.747 2.524 1.00 93.68 O
ANISOU 1886 O GLU A1050 14116 12110 9370 459 1625 -1173 O
ATOM 1887 CB GLU A1050 -33.971 -15.539 1.874 1.00 92.62 C
ANISOU 1887 CB GLU A1050 13832 12063 9296 481 1581 -1324 C
ATOM 1888 CG GLU A1050 -34.099 -14.216 1.128 1.00103.26 C
ANISOU 1888 CG GLU A1050 15224 13385 10627 407 1673 -1373 C
ATOM 1889 CD GLU A1050 -32.884 -13.307 1.161 1.00124.66 C
ANISOU 1889 CD GLU A1050 17889 16151 13325 349 1724 -1492 C
ATOM 1890 OE1 GLU A1050 -32.260 -13.173 2.239 1.00120.27 O
ANISOU 1890 OE1 GLU A1050 17272 15681 12746 349 1692 -1527 O
ATOM 1891 OE2 GLU A1050 -32.591 -12.681 0.117 1.00118.58 O
ANISOU 1891 OE2 GLU A1050 17155 15340 12560 294 1802 -1554 O
ATOM 1892 N GLU A1051 -36.153 -15.766 4.337 1.00 91.49 N
ANISOU 1892 N GLU A1051 13792 11911 9058 505 1526 -1159 N
ATOM 1893 CA GLU A1051 -36.988 -15.105 5.343 1.00 91.21 C
ANISOU 1893 CA GLU A1051 13801 11878 8978 466 1549 -1132 C
ATOM 1894 C GLU A1051 -36.579 -13.639 5.502 1.00 95.12 C
ANISOU 1894 C GLU A1051 14281 12412 9448 401 1612 -1195 C
ATOM 1895 O GLU A1051 -35.388 -13.342 5.633 1.00 95.12 O
ANISOU 1895 O GLU A1051 14225 12479 9437 386 1605 -1263 O
ATOM 1896 CB GLU A1051 -36.902 -15.842 6.692 1.00 93.15 C
ANISOU 1896 CB GLU A1051 14065 12150 9177 491 1484 -1094 C
ATOM 1897 CG GLU A1051 -38.061 -15.543 7.630 1.00103.49 C
ANISOU 1897 CG GLU A1051 15442 13430 10449 446 1515 -1056 C
ATOM 1898 CD GLU A1051 -37.841 -15.919 9.083 1.00123.79 C
ANISOU 1898 CD GLU A1051 18050 16033 12950 442 1464 -1033 C
ATOM 1899 OE1 GLU A1051 -37.952 -15.020 9.947 1.00117.79 O
ANISOU 1899 OE1 GLU A1051 17303 15305 12148 374 1496 -1052 O
ATOM 1900 OE2 GLU A1051 -37.571 -17.110 9.361 1.00117.86 O
ANISOU 1900 OE2 GLU A1051 17327 15271 12182 505 1396 -993 O
ATOM 1901 N VAL A1052 -37.568 -12.728 5.480 1.00 91.35 N
ANISOU 1901 N VAL A1052 13850 11892 8966 361 1680 -1181 N
ATOM 1902 CA VAL A1052 -37.332 -11.289 5.619 1.00 91.26 C
ANISOU 1902 CA VAL A1052 13848 11898 8930 297 1763 -1235 C
ATOM 1903 C VAL A1052 -37.197 -10.930 7.104 1.00 95.65 C
ANISOU 1903 C VAL A1052 14400 12510 9433 247 1766 -1244 C
ATOM 1904 O VAL A1052 -38.202 -10.797 7.810 1.00 95.09 O
ANISOU 1904 O VAL A1052 14369 12406 9353 227 1785 -1202 O
ATOM 1905 CB VAL A1052 -38.379 -10.414 4.866 1.00 94.75 C
ANISOU 1905 CB VAL A1052 14348 12261 9391 290 1837 -1216 C
ATOM 1906 CG1 VAL A1052 -38.014 -8.932 4.933 1.00 94.76 C
ANISOU 1906 CG1 VAL A1052 14377 12264 9362 226 1940 -1274 C
ATOM 1907 CG2 VAL A1052 -38.525 -10.853 3.413 1.00 94.29 C
ANISOU 1907 CG2 VAL A1052 14303 12154 9369 335 1820 -1203 C
ATOM 1908 N GLU A1053 -35.944 -10.806 7.574 1.00 92.92 N
ANISOU 1908 N GLU A1053 13999 12254 9054 222 1745 -1308 N
ATOM 1909 CA GLU A1053 -35.626 -10.450 8.957 1.00 93.36 C
ANISOU 1909 CA GLU A1053 14044 12384 9045 167 1741 -1329 C
ATOM 1910 C GLU A1053 -35.545 -8.924 9.062 1.00 97.10 C
ANISOU 1910 C GLU A1053 14532 12868 9494 71 1867 -1395 C
ATOM 1911 O GLU A1053 -34.454 -8.346 9.014 1.00 97.06 O
ANISOU 1911 O GLU A1053 14479 12938 9464 24 1903 -1488 O
ATOM 1912 CB GLU A1053 -34.328 -11.138 9.425 1.00 95.59 C
ANISOU 1912 CB GLU A1053 14249 12772 9299 199 1641 -1369 C
ATOM 1913 CG GLU A1053 -34.478 -12.627 9.683 1.00106.88 C
ANISOU 1913 CG GLU A1053 15691 14183 10734 293 1522 -1290 C
ATOM 1914 CD GLU A1053 -33.213 -13.305 10.169 1.00129.60 C
ANISOU 1914 CD GLU A1053 18495 17161 13585 348 1411 -1324 C
ATOM 1915 OE1 GLU A1053 -32.908 -13.198 11.379 1.00125.83 O
ANISOU 1915 OE1 GLU A1053 18017 16759 13033 323 1364 -1328 O
ATOM 1916 OE2 GLU A1053 -32.528 -13.948 9.342 1.00124.01 O
ANISOU 1916 OE2 GLU A1053 17728 16458 12932 416 1368 -1349 O
ATOM 1917 N GLU A1054 -36.724 -8.278 9.161 1.00 93.23 N
ANISOU 1917 N GLU A1054 14109 12298 9015 43 1945 -1354 N
ATOM 1918 CA GLU A1054 -36.885 -6.824 9.237 1.00 93.12 C
ANISOU 1918 CA GLU A1054 14133 12263 8986 -38 2083 -1400 C
ATOM 1919 C GLU A1054 -36.194 -6.217 10.458 1.00 97.98 C
ANISOU 1919 C GLU A1054 14725 12974 9531 -139 2123 -1464 C
ATOM 1920 O GLU A1054 -36.553 -6.533 11.597 1.00 97.75 O
ANISOU 1920 O GLU A1054 14703 12969 9469 -168 2087 -1430 O
ATOM 1921 CB GLU A1054 -38.371 -6.428 9.167 1.00 94.01 C
ANISOU 1921 CB GLU A1054 14311 12269 9139 -26 2139 -1338 C
ATOM 1922 CG GLU A1054 -38.969 -6.579 7.778 1.00103.31 C
ANISOU 1922 CG GLU A1054 15516 13363 10374 57 2130 -1301 C
ATOM 1923 CD GLU A1054 -40.483 -6.565 7.715 1.00121.34 C
ANISOU 1923 CD GLU A1054 17834 15564 12707 97 2139 -1239 C
ATOM 1924 OE1 GLU A1054 -41.108 -7.536 8.200 1.00114.63 O
ANISOU 1924 OE1 GLU A1054 16967 14714 11873 119 2069 -1197 O
ATOM 1925 OE2 GLU A1054 -41.044 -5.606 7.138 1.00114.39 O
ANISOU 1925 OE2 GLU A1054 16999 14614 11848 111 2217 -1238 O
ATOM 1926 N ARG A 243 -35.176 -5.369 10.208 1.00 92.87 N
ANISOU 1926 N ARG A 243 15140 10281 9865 -1221 4403 -568 N
ATOM 1927 CA ARG A 243 -34.382 -4.699 11.240 1.00 92.22 C
ANISOU 1927 CA ARG A 243 14893 10197 9947 -1027 4323 -562 C
ATOM 1928 C ARG A 243 -35.210 -3.638 11.979 1.00 95.65 C
ANISOU 1928 C ARG A 243 15220 10815 10309 -898 4074 -552 C
ATOM 1929 O ARG A 243 -35.110 -2.442 11.688 1.00 95.32 O
ANISOU 1929 O ARG A 243 15199 10761 10256 -865 3982 -568 O
ATOM 1930 CB ARG A 243 -33.087 -4.116 10.643 1.00 92.73 C
ANISOU 1930 CB ARG A 243 15002 10078 10153 -1043 4428 -600 C
ATOM 1931 N ARG A 244 -36.047 -4.098 12.925 1.00 91.74 N
ANISOU 1931 N ARG A 244 14623 10475 9758 -831 3986 -527 N
ATOM 1932 CA ARG A 244 -36.927 -3.244 13.722 1.00 91.00 C
ANISOU 1932 CA ARG A 244 14419 10560 9597 -710 3769 -518 C
ATOM 1933 C ARG A 244 -36.162 -2.679 14.922 1.00 94.44 C
ANISOU 1933 C ARG A 244 14703 11000 10179 -534 3700 -517 C
ATOM 1934 O ARG A 244 -36.273 -3.187 16.043 1.00 93.71 O
ANISOU 1934 O ARG A 244 14501 10985 10118 -440 3671 -496 O
ATOM 1935 CB ARG A 244 -38.209 -3.996 14.138 1.00 91.00 C
ANISOU 1935 CB ARG A 244 14385 10725 9465 -743 3723 -507 C
ATOM 1936 CG ARG A 244 -39.039 -4.495 12.959 1.00100.69 C
ANISOU 1936 CG ARG A 244 15743 11987 10526 -936 3775 -525 C
ATOM 1937 CD ARG A 244 -40.286 -5.225 13.411 1.00108.16 C
ANISOU 1937 CD ARG A 244 16637 13110 11348 -984 3741 -538 C
ATOM 1938 NE ARG A 244 -40.887 -6.007 12.328 1.00114.73 N
ANISOU 1938 NE ARG A 244 17594 13964 12034 -1204 3842 -572 N
ATOM 1939 CZ ARG A 244 -41.798 -5.544 11.476 1.00127.96 C
ANISOU 1939 CZ ARG A 244 19303 15773 13543 -1292 3732 -592 C
ATOM 1940 NH1 ARG A 244 -42.287 -6.332 10.528 1.00115.94 N
ANISOU 1940 NH1 ARG A 244 17890 14280 11881 -1510 3832 -632 N
ATOM 1941 NH2 ARG A 244 -42.223 -4.290 11.563 1.00113.88 N
ANISOU 1941 NH2 ARG A 244 17449 14096 11725 -1159 3525 -570 N
ATOM 1942 N ARG A 245 -35.355 -1.636 14.658 1.00 91.05 N
ANISOU 1942 N ARG A 245 14281 10484 9830 -502 3686 -545 N
ATOM 1943 CA ARG A 245 -34.522 -0.955 15.650 1.00 90.62 C
ANISOU 1943 CA ARG A 245 14088 10433 9909 -366 3628 -568 C
ATOM 1944 C ARG A 245 -35.334 -0.226 16.721 1.00 93.82 C
ANISOU 1944 C ARG A 245 14387 11002 10258 -242 3440 -559 C
ATOM 1945 O ARG A 245 -34.989 -0.323 17.898 1.00 93.13 O
ANISOU 1945 O ARG A 245 14164 10977 10244 -134 3393 -558 O
ATOM 1946 CB ARG A 245 -33.517 -0.014 14.970 1.00 91.35 C
ANISOU 1946 CB ARG A 245 14237 10385 10088 -403 3688 -622 C
ATOM 1947 CG ARG A 245 -32.258 -0.731 14.490 1.00102.89 C
ANISOU 1947 CG ARG A 245 15712 11690 11690 -469 3881 -647 C
ATOM 1948 CD ARG A 245 -31.775 -0.243 13.135 1.00114.09 C
ANISOU 1948 CD ARG A 245 17299 12939 13110 -603 4001 -691 C
ATOM 1949 NE ARG A 245 -31.208 1.106 13.194 1.00123.50 N
ANISOU 1949 NE ARG A 245 18480 14089 14357 -572 3964 -754 N
ATOM 1950 CZ ARG A 245 -30.378 1.613 12.287 1.00138.86 C
ANISOU 1950 CZ ARG A 245 20534 15865 16360 -669 4096 -817 C
ATOM 1951 NH1 ARG A 245 -29.996 0.887 11.244 1.00126.73 N
ANISOU 1951 NH1 ARG A 245 19124 14186 14840 -801 4269 -821 N
ATOM 1952 NH2 ARG A 245 -29.914 2.848 12.424 1.00126.40 N
ANISOU 1952 NH2 ARG A 245 18953 14250 14823 -647 4075 -884 N
ATOM 1953 N LEU A 246 -36.417 0.476 16.320 1.00 90.22 N
ANISOU 1953 N LEU A 246 13993 10620 9667 -252 3336 -549 N
ATOM 1954 CA LEU A 246 -37.296 1.223 17.229 1.00 89.66 C
ANISOU 1954 CA LEU A 246 13834 10696 9537 -136 3171 -542 C
ATOM 1955 C LEU A 246 -38.021 0.330 18.239 1.00 93.24 C
ANISOU 1955 C LEU A 246 14184 11286 9956 -93 3128 -518 C
ATOM 1956 O LEU A 246 -38.219 0.748 19.382 1.00 92.40 O
ANISOU 1956 O LEU A 246 13971 11270 9869 18 3030 -522 O
ATOM 1957 CB LEU A 246 -38.292 2.100 16.453 1.00 90.03 C
ANISOU 1957 CB LEU A 246 13973 10787 9447 -141 3083 -527 C
ATOM 1958 CG LEU A 246 -37.725 3.385 15.845 1.00 95.06 C
ANISOU 1958 CG LEU A 246 14711 11302 10105 -126 3094 -549 C
ATOM 1959 CD1 LEU A 246 -38.502 3.792 14.617 1.00 95.94 C
ANISOU 1959 CD1 LEU A 246 14975 11412 10067 -170 3065 -516 C
ATOM 1960 CD2 LEU A 246 -37.705 4.522 16.856 1.00 97.21 C
ANISOU 1960 CD2 LEU A 246 14903 11612 10420 7 3003 -569 C
ATOM 1961 N LEU A 247 -38.397 -0.898 17.825 1.00 90.16 N
ANISOU 1961 N LEU A 247 13843 10903 9511 -192 3216 -500 N
ATOM 1962 CA LEU A 247 -39.052 -1.881 18.692 1.00 89.87 C
ANISOU 1962 CA LEU A 247 13743 10969 9434 -177 3218 -485 C
ATOM 1963 C LEU A 247 -38.033 -2.446 19.690 1.00 93.81 C
ANISOU 1963 C LEU A 247 14171 11414 10058 -91 3277 -470 C
ATOM 1964 O LEU A 247 -38.384 -2.685 20.847 1.00 93.12 O
ANISOU 1964 O LEU A 247 14004 11419 9960 -5 3221 -458 O
ATOM 1965 CB LEU A 247 -39.694 -3.010 17.859 1.00 90.34 C
ANISOU 1965 CB LEU A 247 13899 11035 9392 -334 3327 -484 C
ATOM 1966 CG LEU A 247 -40.576 -4.023 18.610 1.00 95.08 C
ANISOU 1966 CG LEU A 247 14463 11743 9921 -354 3352 -485 C
ATOM 1967 CD1 LEU A 247 -41.920 -3.419 18.996 1.00 95.24 C
ANISOU 1967 CD1 LEU A 247 14402 11952 9833 -321 3196 -505 C
ATOM 1968 CD2 LEU A 247 -40.796 -5.267 17.779 1.00 98.12 C
ANISOU 1968 CD2 LEU A 247 14964 12079 10237 -531 3523 -496 C
ATOM 1969 N SER A 248 -36.768 -2.627 19.243 1.00 90.86 N
ANISOU 1969 N SER A 248 13825 10898 9801 -107 3388 -471 N
ATOM 1970 CA SER A 248 -35.653 -3.120 20.058 1.00 90.93 C
ANISOU 1970 CA SER A 248 13752 10861 9937 -9 3441 -454 C
ATOM 1971 C SER A 248 -35.327 -2.141 21.193 1.00 94.47 C
ANISOU 1971 C SER A 248 14064 11396 10436 126 3293 -474 C
ATOM 1972 O SER A 248 -35.003 -2.584 22.292 1.00 94.12 O
ANISOU 1972 O SER A 248 13932 11403 10425 231 3269 -450 O
ATOM 1973 CB SER A 248 -34.421 -3.373 19.194 1.00 95.14 C
ANISOU 1973 CB SER A 248 14329 11232 10587 -63 3589 -465 C
ATOM 1974 OG SER A 248 -33.385 -3.999 19.933 1.00104.63 O
ANISOU 1974 OG SER A 248 15439 12405 11908 44 3646 -441 O
ATOM 1975 N ILE A 249 -35.443 -0.819 20.932 1.00 90.86 N
ANISOU 1975 N ILE A 249 13603 10952 9969 120 3202 -518 N
ATOM 1976 CA ILE A 249 -35.223 0.239 21.928 1.00 90.61 C
ANISOU 1976 CA ILE A 249 13464 10995 9969 220 3077 -553 C
ATOM 1977 C ILE A 249 -36.390 0.206 22.934 1.00 94.30 C
ANISOU 1977 C ILE A 249 13889 11604 10336 285 2966 -530 C
ATOM 1978 O ILE A 249 -36.157 0.299 24.140 1.00 93.94 O
ANISOU 1978 O ILE A 249 13746 11634 10314 379 2897 -534 O
ATOM 1979 CB ILE A 249 -35.042 1.642 21.261 1.00 93.76 C
ANISOU 1979 CB ILE A 249 13911 11336 10379 184 3052 -607 C
ATOM 1980 CG1 ILE A 249 -33.846 1.655 20.281 1.00 94.64 C
ANISOU 1980 CG1 ILE A 249 14070 11294 10593 105 3183 -643 C
ATOM 1981 CG2 ILE A 249 -34.889 2.759 22.310 1.00 94.46 C
ANISOU 1981 CG2 ILE A 249 13905 11496 10488 269 2944 -654 C
ATOM 1982 CD1 ILE A 249 -33.987 2.635 19.104 1.00101.90 C
ANISOU 1982 CD1 ILE A 249 15132 12113 11473 24 3213 -674 C
ATOM 1983 N CYS A 250 -37.631 0.033 22.427 1.00 90.80 N
ANISOU 1983 N CYS A 250 13515 11205 9778 229 2954 -513 N
ATOM 1984 CA CYS A 250 -38.864 -0.032 23.216 1.00 90.49 C
ANISOU 1984 CA CYS A 250 13439 11301 9643 270 2869 -503 C
ATOM 1985 C CYS A 250 -38.894 -1.228 24.175 1.00 94.38 C
ANISOU 1985 C CYS A 250 13901 11832 10128 304 2911 -473 C
ATOM 1986 O CYS A 250 -39.129 -1.029 25.366 1.00 93.70 O
ANISOU 1986 O CYS A 250 13746 11829 10028 389 2833 -476 O
ATOM 1987 CB CYS A 250 -40.093 -0.005 22.309 1.00 90.93 C
ANISOU 1987 CB CYS A 250 13559 11408 9584 190 2855 -502 C
ATOM 1988 SG CYS A 250 -41.676 -0.051 23.193 1.00 94.82 S
ANISOU 1988 SG CYS A 250 13982 12080 9966 228 2762 -509 S
ATOM 1989 N VAL A 251 -38.647 -2.455 23.661 1.00 91.35 N
ANISOU 1989 N VAL A 251 13587 11376 9748 236 3047 -444 N
ATOM 1990 CA VAL A 251 -38.653 -3.705 24.437 1.00 91.48 C
ANISOU 1990 CA VAL A 251 13617 11395 9747 268 3126 -405 C
ATOM 1991 C VAL A 251 -37.597 -3.678 25.560 1.00 95.77 C
ANISOU 1991 C VAL A 251 14076 11938 10374 411 3086 -381 C
ATOM 1992 O VAL A 251 -37.951 -3.921 26.716 1.00 95.33 O
ANISOU 1992 O VAL A 251 13993 11958 10271 489 3039 -364 O
ATOM 1993 CB VAL A 251 -38.548 -4.966 23.526 1.00 95.74 C
ANISOU 1993 CB VAL A 251 14272 11829 10274 158 3310 -382 C
ATOM 1994 CG1 VAL A 251 -38.292 -6.237 24.336 1.00 96.06 C
ANISOU 1994 CG1 VAL A 251 14350 11833 10315 218 3421 -330 C
ATOM 1995 CG2 VAL A 251 -39.801 -5.129 22.671 1.00 95.55 C
ANISOU 1995 CG2 VAL A 251 14317 11857 10130 8 3334 -415 C
ATOM 1996 N VAL A 252 -36.328 -3.348 25.224 1.00 92.79 N
ANISOU 1996 N VAL A 252 13656 11488 10113 440 3102 -386 N
ATOM 1997 CA VAL A 252 -35.203 -3.273 26.169 1.00 93.22 C
ANISOU 1997 CA VAL A 252 13602 11566 10251 570 3055 -374 C
ATOM 1998 C VAL A 252 -35.501 -2.289 27.320 1.00 97.17 C
ANISOU 1998 C VAL A 252 14012 12194 10713 642 2890 -408 C
ATOM 1999 O VAL A 252 -35.311 -2.655 28.482 1.00 97.22 O
ANISOU 1999 O VAL A 252 13972 12268 10698 746 2843 -377 O
ATOM 2000 CB VAL A 252 -33.851 -2.994 25.447 1.00 97.55 C
ANISOU 2000 CB VAL A 252 14104 12025 10936 560 3109 -399 C
ATOM 2001 CG1 VAL A 252 -32.767 -2.513 26.410 1.00 97.97 C
ANISOU 2001 CG1 VAL A 252 14003 12153 11068 676 3016 -420 C
ATOM 2002 CG2 VAL A 252 -33.375 -4.231 24.691 1.00 97.90 C
ANISOU 2002 CG2 VAL A 252 14227 11943 11029 530 3289 -349 C
ATOM 2003 N LEU A 253 -36.014 -1.080 27.000 1.00 93.38 N
ANISOU 2003 N LEU A 253 13527 11740 10213 590 2814 -466 N
ATOM 2004 CA LEU A 253 -36.365 -0.063 27.999 1.00 93.19 C
ANISOU 2004 CA LEU A 253 13437 11818 10152 642 2683 -506 C
ATOM 2005 C LEU A 253 -37.509 -0.497 28.923 1.00 97.21 C
ANISOU 2005 C LEU A 253 13967 12414 10553 676 2646 -481 C
ATOM 2006 O LEU A 253 -37.478 -0.170 30.108 1.00 96.89 O
ANISOU 2006 O LEU A 253 13870 12455 10488 747 2562 -492 O
ATOM 2007 CB LEU A 253 -36.686 1.291 27.346 1.00 92.90 C
ANISOU 2007 CB LEU A 253 13418 11761 10118 588 2643 -564 C
ATOM 2008 CG LEU A 253 -35.496 2.163 26.936 1.00 97.90 C
ANISOU 2008 CG LEU A 253 14014 12332 10852 567 2654 -623 C
ATOM 2009 CD1 LEU A 253 -35.926 3.220 25.947 1.00 97.85 C
ANISOU 2009 CD1 LEU A 253 14090 12258 10829 503 2665 -657 C
ATOM 2010 CD2 LEU A 253 -34.845 2.832 28.142 1.00100.82 C
ANISOU 2010 CD2 LEU A 253 14273 12785 11248 627 2569 -674 C
ATOM 2011 N VAL A 254 -38.500 -1.239 28.385 1.00 93.92 N
ANISOU 2011 N VAL A 254 13633 11985 10068 611 2716 -456 N
ATOM 2012 CA VAL A 254 -39.656 -1.750 29.134 1.00 93.88 C
ANISOU 2012 CA VAL A 254 13655 12056 9961 615 2712 -447 C
ATOM 2013 C VAL A 254 -39.232 -2.897 30.071 1.00 98.93 C
ANISOU 2013 C VAL A 254 14320 12687 10581 687 2765 -393 C
ATOM 2014 O VAL A 254 -39.585 -2.871 31.253 1.00 98.67 O
ANISOU 2014 O VAL A 254 14274 12725 10491 748 2710 -393 O
ATOM 2015 CB VAL A 254 -40.847 -2.111 28.194 1.00 97.54 C
ANISOU 2015 CB VAL A 254 14181 12527 10353 502 2773 -460 C
ATOM 2016 CG1 VAL A 254 -41.894 -2.980 28.891 1.00 97.56 C
ANISOU 2016 CG1 VAL A 254 14220 12591 10258 481 2820 -459 C
ATOM 2017 CG2 VAL A 254 -41.495 -0.851 27.628 1.00 97.05 C
ANISOU 2017 CG2 VAL A 254 14085 12510 10278 480 2684 -502 C
ATOM 2018 N VAL A 255 -38.460 -3.878 29.547 1.00 96.47 N
ANISOU 2018 N VAL A 255 14057 12282 10316 686 2879 -343 N
ATOM 2019 CA VAL A 255 -37.944 -5.040 30.291 1.00 97.34 C
ANISOU 2019 CA VAL A 255 14213 12361 10413 778 2952 -272 C
ATOM 2020 C VAL A 255 -37.084 -4.587 31.488 1.00102.18 C
ANISOU 2020 C VAL A 255 14729 13047 11049 921 2827 -258 C
ATOM 2021 O VAL A 255 -37.293 -5.076 32.600 1.00102.18 O
ANISOU 2021 O VAL A 255 14763 13090 10970 1002 2812 -220 O
ATOM 2022 CB VAL A 255 -37.225 -6.062 29.356 1.00101.77 C
ANISOU 2022 CB VAL A 255 14843 12790 11035 756 3114 -223 C
ATOM 2023 CG1 VAL A 255 -36.419 -7.097 30.142 1.00102.67 C
ANISOU 2023 CG1 VAL A 255 14987 12865 11156 900 3178 -135 C
ATOM 2024 CG2 VAL A 255 -38.223 -6.758 28.434 1.00101.38 C
ANISOU 2024 CG2 VAL A 255 14916 12685 10920 603 3253 -238 C
ATOM 2025 N THR A 256 -36.163 -3.623 31.262 1.00 99.24 N
ANISOU 2025 N THR A 256 14242 12695 10770 937 2742 -298 N
ATOM 2026 CA THR A 256 -35.290 -3.058 32.302 1.00 99.98 C
ANISOU 2026 CA THR A 256 14219 12883 10885 1043 2615 -309 C
ATOM 2027 C THR A 256 -36.084 -2.271 33.347 1.00104.25 C
ANISOU 2027 C THR A 256 14747 13529 11335 1045 2499 -354 C
ATOM 2028 O THR A 256 -35.729 -2.308 34.526 1.00104.59 O
ANISOU 2028 O THR A 256 14752 13657 11331 1139 2418 -337 O
ATOM 2029 CB THR A 256 -34.157 -2.223 31.698 1.00108.53 C
ANISOU 2029 CB THR A 256 15187 13958 12091 1023 2581 -366 C
ATOM 2030 OG1 THR A 256 -34.702 -1.284 30.770 1.00107.52 O
ANISOU 2030 OG1 THR A 256 15084 13787 11983 902 2588 -433 O
ATOM 2031 CG2 THR A 256 -33.087 -3.079 31.031 1.00107.98 C
ANISOU 2031 CG2 THR A 256 15100 13807 12121 1063 2685 -317 C
ATOM 2032 N PHE A 257 -37.162 -1.574 32.916 1.00100.39 N
ANISOU 2032 N PHE A 257 14290 13036 10817 949 2495 -407 N
ATOM 2033 CA PHE A 257 -38.053 -0.815 33.799 1.00100.20 C
ANISOU 2033 CA PHE A 257 14260 13094 10716 944 2412 -453 C
ATOM 2034 C PHE A 257 -38.810 -1.778 34.711 1.00104.92 C
ANISOU 2034 C PHE A 257 14941 13717 11206 981 2448 -408 C
ATOM 2035 O PHE A 257 -38.881 -1.535 35.912 1.00104.90 O
ANISOU 2035 O PHE A 257 14929 13788 11140 1034 2375 -417 O
ATOM 2036 CB PHE A 257 -39.031 0.061 32.988 1.00101.22 C
ANISOU 2036 CB PHE A 257 14402 13208 10847 855 2415 -507 C
ATOM 2037 CG PHE A 257 -40.179 0.667 33.766 1.00102.64 C
ANISOU 2037 CG PHE A 257 14587 13459 10951 852 2365 -547 C
ATOM 2038 CD1 PHE A 257 -39.992 1.805 34.542 1.00105.91 C
ANISOU 2038 CD1 PHE A 257 14950 13924 11367 878 2279 -601 C
ATOM 2039 CD2 PHE A 257 -41.457 0.125 33.685 1.00104.60 C
ANISOU 2039 CD2 PHE A 257 14890 13723 11131 811 2420 -543 C
ATOM 2040 CE1 PHE A 257 -41.057 2.370 35.251 1.00106.79 C
ANISOU 2040 CE1 PHE A 257 15072 14086 11416 876 2252 -640 C
ATOM 2041 CE2 PHE A 257 -42.521 0.690 34.396 1.00107.40 C
ANISOU 2041 CE2 PHE A 257 15236 14144 11428 811 2385 -587 C
ATOM 2042 CZ PHE A 257 -42.313 1.809 35.173 1.00105.64 C
ANISOU 2042 CZ PHE A 257 14970 13957 11213 850 2304 -630 C
ATOM 2043 N ALA A 258 -39.350 -2.876 34.137 1.00101.93 N
ANISOU 2043 N ALA A 258 14657 13272 10799 939 2573 -367 N
ATOM 2044 CA ALA A 258 -40.087 -3.916 34.858 1.00102.45 C
ANISOU 2044 CA ALA A 258 14831 13335 10760 952 2652 -332 C
ATOM 2045 C ALA A 258 -39.212 -4.613 35.901 1.00108.30 C
ANISOU 2045 C ALA A 258 15604 14080 11466 1087 2640 -257 C
ATOM 2046 O ALA A 258 -39.713 -4.953 36.966 1.00108.37 O
ANISOU 2046 O ALA A 258 15685 14119 11372 1124 2642 -243 O
ATOM 2047 CB ALA A 258 -40.653 -4.933 33.882 1.00103.05 C
ANISOU 2047 CB ALA A 258 15002 13330 10822 859 2810 -315 C
ATOM 2048 N LEU A 259 -37.909 -4.796 35.611 1.00106.19 N
ANISOU 2048 N LEU A 259 15280 13788 11280 1166 2626 -209 N
ATOM 2049 CA LEU A 259 -36.956 -5.421 36.534 1.00107.71 C
ANISOU 2049 CA LEU A 259 15476 14005 11443 1323 2595 -128 C
ATOM 2050 C LEU A 259 -36.574 -4.486 37.692 1.00113.08 C
ANISOU 2050 C LEU A 259 16058 14821 12085 1386 2418 -164 C
ATOM 2051 O LEU A 259 -36.201 -4.969 38.763 1.00113.74 O
ANISOU 2051 O LEU A 259 16174 14955 12085 1508 2374 -103 O
ATOM 2052 CB LEU A 259 -35.692 -5.885 35.787 1.00108.32 C
ANISOU 2052 CB LEU A 259 15497 14026 11634 1391 2640 -75 C
ATOM 2053 CG LEU A 259 -35.819 -7.152 34.937 1.00113.19 C
ANISOU 2053 CG LEU A 259 16246 14496 12266 1371 2841 -10 C
ATOM 2054 CD1 LEU A 259 -34.823 -7.140 33.796 1.00113.37 C
ANISOU 2054 CD1 LEU A 259 16190 14453 12433 1361 2890 -8 C
ATOM 2055 CD2 LEU A 259 -35.638 -8.411 35.778 1.00117.00 C
ANISOU 2055 CD2 LEU A 259 16857 14937 12661 1518 2924 103 C
ATOM 2056 N CYS A 260 -36.668 -3.157 37.474 1.00109.80 N
ANISOU 2056 N CYS A 260 15538 14461 11719 1300 2326 -262 N
ATOM 2057 CA CYS A 260 -36.323 -2.127 38.460 1.00110.49 C
ANISOU 2057 CA CYS A 260 15535 14672 11775 1320 2177 -321 C
ATOM 2058 C CYS A 260 -37.539 -1.528 39.194 1.00114.98 C
ANISOU 2058 C CYS A 260 16163 15275 12250 1257 2153 -378 C
ATOM 2059 O CYS A 260 -37.354 -0.840 40.201 1.00115.12 O
ANISOU 2059 O CYS A 260 16140 15387 12211 1272 2048 -420 O
ATOM 2060 CB CYS A 260 -35.467 -1.038 37.818 1.00110.61 C
ANISOU 2060 CB CYS A 260 15405 14714 11907 1270 2115 -399 C
ATOM 2061 SG CYS A 260 -33.858 -1.614 37.214 1.00115.42 S
ANISOU 2061 SG CYS A 260 15905 15316 12633 1355 2126 -352 S
ATOM 2062 N TRP A 261 -38.769 -1.781 38.700 1.00111.53 N
ANISOU 2062 N TRP A 261 15813 14769 11794 1179 2253 -388 N
ATOM 2063 CA TRP A 261 -39.996 -1.257 39.310 1.00111.40 C
ANISOU 2063 CA TRP A 261 15840 14783 11705 1120 2250 -447 C
ATOM 2064 C TRP A 261 -40.860 -2.334 39.980 1.00116.27 C
ANISOU 2064 C TRP A 261 16595 15373 12207 1131 2342 -407 C
ATOM 2065 O TRP A 261 -41.661 -1.995 40.854 1.00115.97 O
ANISOU 2065 O TRP A 261 16597 15374 12093 1106 2331 -451 O
ATOM 2066 CB TRP A 261 -40.810 -0.428 38.305 1.00109.20 C
ANISOU 2066 CB TRP A 261 15521 14478 11493 1022 2275 -514 C
ATOM 2067 CG TRP A 261 -40.839 1.041 38.615 1.00110.11 C
ANISOU 2067 CG TRP A 261 15564 14641 11631 998 2189 -594 C
ATOM 2068 CD1 TRP A 261 -41.903 1.759 39.073 1.00112.90 C
ANISOU 2068 CD1 TRP A 261 15931 15021 11947 963 2188 -653 C
ATOM 2069 CD2 TRP A 261 -39.745 1.964 38.514 1.00110.15 C
ANISOU 2069 CD2 TRP A 261 15482 14669 11702 1004 2112 -632 C
ATOM 2070 NE1 TRP A 261 -41.545 3.074 39.257 1.00112.48 N
ANISOU 2070 NE1 TRP A 261 15819 14989 11928 951 2124 -717 N
ATOM 2071 CE2 TRP A 261 -40.226 3.229 38.921 1.00114.09 C
ANISOU 2071 CE2 TRP A 261 15964 15193 12192 965 2078 -712 C
ATOM 2072 CE3 TRP A 261 -38.403 1.848 38.113 1.00111.75 C
ANISOU 2072 CE3 TRP A 261 15616 14870 11974 1032 2083 -614 C
ATOM 2073 CZ2 TRP A 261 -39.413 4.369 38.939 1.00113.70 C
ANISOU 2073 CZ2 TRP A 261 15849 15161 12191 940 2026 -779 C
ATOM 2074 CZ3 TRP A 261 -37.600 2.978 38.133 1.00113.53 C
ANISOU 2074 CZ3 TRP A 261 15757 15129 12252 1003 2021 -688 C
ATOM 2075 CH2 TRP A 261 -38.104 4.220 38.541 1.00114.13 C
ANISOU 2075 CH2 TRP A 261 15834 15222 12308 951 1998 -772 C
ATOM 2076 N MET A 262 -40.694 -3.619 39.590 1.00113.66 N
ANISOU 2076 N MET A 262 16352 14968 11866 1161 2451 -330 N
ATOM 2077 CA MET A 262 -41.425 -4.746 40.184 1.00114.35 C
ANISOU 2077 CA MET A 262 16601 15008 11839 1165 2572 -292 C
ATOM 2078 C MET A 262 -41.052 -4.958 41.668 1.00119.84 C
ANISOU 2078 C MET A 262 17369 15749 12418 1275 2511 -247 C
ATOM 2079 O MET A 262 -41.986 -5.065 42.461 1.00119.68 O
ANISOU 2079 O MET A 262 17447 15730 12297 1236 2557 -279 O
ATOM 2080 CB MET A 262 -41.246 -6.045 39.375 1.00116.98 C
ANISOU 2080 CB MET A 262 17028 15232 12187 1168 2727 -221 C
ATOM 2081 CG MET A 262 -42.308 -7.095 39.647 1.00121.14 C
ANISOU 2081 CG MET A 262 17727 15692 12609 1106 2900 -222 C
ATOM 2082 SD MET A 262 -43.835 -6.844 38.708 1.00124.42 S
ANISOU 2082 SD MET A 262 18109 16121 13045 904 2988 -340 S
ATOM 2083 CE MET A 262 -43.348 -7.494 37.108 1.00120.76 C
ANISOU 2083 CE MET A 262 17643 15570 12669 850 3091 -305 C
ATOM 2084 N PRO A 263 -39.752 -4.991 42.097 1.00117.66 N
ANISOU 2084 N PRO A 263 17044 15519 12141 1407 2406 -180 N
ATOM 2085 CA PRO A 263 -39.465 -5.186 43.533 1.00118.96 C
ANISOU 2085 CA PRO A 263 17285 15745 12168 1512 2334 -136 C
ATOM 2086 C PRO A 263 -39.988 -4.061 44.427 1.00123.04 C
ANISOU 2086 C PRO A 263 17769 16353 12628 1445 2235 -231 C
ATOM 2087 O PRO A 263 -40.419 -4.336 45.544 1.00123.31 O
ANISOU 2087 O PRO A 263 17932 16397 12524 1467 2245 -219 O
ATOM 2088 CB PRO A 263 -37.935 -5.291 43.586 1.00121.70 C
ANISOU 2088 CB PRO A 263 17531 16158 12552 1658 2221 -61 C
ATOM 2089 CG PRO A 263 -37.517 -5.614 42.194 1.00125.39 C
ANISOU 2089 CG PRO A 263 17933 16546 13164 1642 2301 -41 C
ATOM 2090 CD PRO A 263 -38.492 -4.884 41.332 1.00119.28 C
ANISOU 2090 CD PRO A 263 17121 15736 12465 1468 2349 -146 C
ATOM 2091 N TYR A 264 -39.978 -2.808 43.925 1.00119.10 N
ANISOU 2091 N TYR A 264 17118 15902 12231 1359 2159 -325 N
ATOM 2092 CA TYR A 264 -40.474 -1.630 44.643 1.00118.98 C
ANISOU 2092 CA TYR A 264 17071 15955 12182 1286 2088 -424 C
ATOM 2093 C TYR A 264 -41.996 -1.685 44.822 1.00122.93 C
ANISOU 2093 C TYR A 264 17670 16401 12639 1194 2204 -477 C
ATOM 2094 O TYR A 264 -42.486 -1.389 45.913 1.00123.08 O
ANISOU 2094 O TYR A 264 17757 16450 12557 1174 2192 -516 O
ATOM 2095 CB TYR A 264 -40.034 -0.329 43.933 1.00119.40 C
ANISOU 2095 CB TYR A 264 16958 16046 12361 1225 2010 -505 C
ATOM 2096 CG TYR A 264 -40.795 0.915 44.348 1.00120.71 C
ANISOU 2096 CG TYR A 264 17107 16239 12520 1133 1993 -612 C
ATOM 2097 CD1 TYR A 264 -40.526 1.551 45.556 1.00123.58 C
ANISOU 2097 CD1 TYR A 264 17476 16685 12792 1128 1908 -658 C
ATOM 2098 CD2 TYR A 264 -41.765 1.471 43.519 1.00120.39 C
ANISOU 2098 CD2 TYR A 264 17042 16142 12561 1056 2065 -667 C
ATOM 2099 CE1 TYR A 264 -41.223 2.695 45.943 1.00124.12 C
ANISOU 2099 CE1 TYR A 264 17542 16760 12858 1042 1917 -758 C
ATOM 2100 CE2 TYR A 264 -42.470 2.614 43.895 1.00121.15 C
ANISOU 2100 CE2 TYR A 264 17125 16251 12657 994 2064 -757 C
ATOM 2101 CZ TYR A 264 -42.193 3.225 45.107 1.00129.30 C
ANISOU 2101 CZ TYR A 264 18176 17345 13606 984 2000 -803 C
ATOM 2102 OH TYR A 264 -42.882 4.354 45.480 1.00130.05 O
ANISOU 2102 OH TYR A 264 18271 17436 13705 921 2023 -893 O
ATOM 2103 N HIS A 265 -42.735 -2.052 43.756 1.00119.09 N
ANISOU 2103 N HIS A 265 17183 15842 12223 1131 2317 -486 N
ATOM 2104 CA HIS A 265 -44.196 -2.132 43.779 1.00118.82 C
ANISOU 2104 CA HIS A 265 17207 15778 12163 1037 2430 -549 C
ATOM 2105 C HIS A 265 -44.735 -3.388 44.464 1.00124.26 C
ANISOU 2105 C HIS A 265 18076 16411 12727 1042 2558 -511 C
ATOM 2106 O HIS A 265 -45.807 -3.317 45.064 1.00123.97 O
ANISOU 2106 O HIS A 265 18100 16372 12630 974 2630 -578 O
ATOM 2107 CB HIS A 265 -44.791 -1.971 42.374 1.00118.51 C
ANISOU 2107 CB HIS A 265 17081 15714 12232 960 2486 -585 C
ATOM 2108 CG HIS A 265 -44.865 -0.547 41.919 1.00121.16 C
ANISOU 2108 CG HIS A 265 17282 16093 12661 933 2399 -651 C
ATOM 2109 ND1 HIS A 265 -45.791 0.334 42.450 1.00122.90 N
ANISOU 2109 ND1 HIS A 265 17480 16347 12869 893 2397 -732 N
ATOM 2110 CD2 HIS A 265 -44.129 0.102 40.989 1.00122.30 C
ANISOU 2110 CD2 HIS A 265 17326 16235 12907 944 2333 -647 C
ATOM 2111 CE1 HIS A 265 -45.585 1.486 41.834 1.00121.78 C
ANISOU 2111 CE1 HIS A 265 17234 16219 12817 892 2332 -766 C
ATOM 2112 NE2 HIS A 265 -44.596 1.396 40.946 1.00121.74 N
ANISOU 2112 NE2 HIS A 265 17185 16192 12880 916 2292 -719 N
ATOM 2113 N LEU A 266 -44.008 -4.525 44.386 1.00122.18 N
ANISOU 2113 N LEU A 266 17906 16092 12425 1124 2604 -408 N
ATOM 2114 CA LEU A 266 -44.426 -5.780 45.022 1.00123.38 C
ANISOU 2114 CA LEU A 266 18266 16166 12449 1140 2750 -361 C
ATOM 2115 C LEU A 266 -44.315 -5.693 46.547 1.00129.58 C
ANISOU 2115 C LEU A 266 19164 16982 13089 1204 2695 -345 C
ATOM 2116 O LEU A 266 -45.263 -6.067 47.236 1.00129.64 O
ANISOU 2116 O LEU A 266 19314 16947 12997 1143 2812 -385 O
ATOM 2117 CB LEU A 266 -43.634 -6.985 44.479 1.00123.92 C
ANISOU 2117 CB LEU A 266 18416 16149 12519 1228 2829 -246 C
ATOM 2118 CG LEU A 266 -44.237 -8.371 44.726 1.00129.50 C
ANISOU 2118 CG LEU A 266 19354 16735 13116 1210 3045 -210 C
ATOM 2119 CD1 LEU A 266 -45.260 -8.731 43.656 1.00128.90 C
ANISOU 2119 CD1 LEU A 266 19270 16609 13097 1043 3209 -290 C
ATOM 2120 CD2 LEU A 266 -43.155 -9.428 44.769 1.00133.04 C
ANISOU 2120 CD2 LEU A 266 19918 17106 13524 1372 3085 -63 C
ATOM 2121 N VAL A 267 -43.175 -5.178 47.064 1.00127.64 N
ANISOU 2121 N VAL A 267 18850 16819 12827 1313 2520 -298 N
ATOM 2122 CA VAL A 267 -42.910 -4.996 48.500 1.00129.20 C
ANISOU 2122 CA VAL A 267 19139 17075 12875 1375 2434 -281 C
ATOM 2123 C VAL A 267 -43.912 -3.997 49.109 1.00133.90 C
ANISOU 2123 C VAL A 267 19722 17704 13449 1248 2434 -409 C
ATOM 2124 O VAL A 267 -44.420 -4.242 50.206 1.00134.44 O
ANISOU 2124 O VAL A 267 19953 17752 13376 1235 2486 -419 O
ATOM 2125 CB VAL A 267 -41.416 -4.644 48.780 1.00133.90 C
ANISOU 2125 CB VAL A 267 19625 17785 13465 1505 2237 -217 C
ATOM 2126 CG1 VAL A 267 -41.200 -4.097 50.192 1.00134.93 C
ANISOU 2126 CG1 VAL A 267 19804 18016 13448 1527 2115 -236 C
ATOM 2127 CG2 VAL A 267 -40.515 -5.852 48.538 1.00134.69 C
ANISOU 2127 CG2 VAL A 267 19790 17843 13544 1667 2261 -72 C
ATOM 2128 N LYS A 268 -44.230 -2.909 48.371 1.00130.16 N
ANISOU 2128 N LYS A 268 19073 17267 13116 1158 2396 -502 N
ATOM 2129 CA LYS A 268 -45.188 -1.888 48.800 1.00130.14 C
ANISOU 2129 CA LYS A 268 19040 17286 13122 1051 2411 -621 C
ATOM 2130 C LYS A 268 -46.607 -2.446 48.922 1.00135.24 C
ANISOU 2130 C LYS A 268 19794 17858 13732 962 2593 -676 C
ATOM 2131 O LYS A 268 -47.242 -2.240 49.956 1.00135.45 O
ANISOU 2131 O LYS A 268 19919 17880 13666 915 2637 -732 O
ATOM 2132 CB LYS A 268 -45.162 -0.666 47.871 1.00131.50 C
ANISOU 2132 CB LYS A 268 19014 17497 13452 1003 2344 -690 C
ATOM 2133 CG LYS A 268 -44.819 0.619 48.605 1.00146.20 C
ANISOU 2133 CG LYS A 268 20821 19429 15298 982 2236 -756 C
ATOM 2134 CD LYS A 268 -45.306 1.851 47.864 1.00155.22 C
ANISOU 2134 CD LYS A 268 21828 20571 16576 917 2240 -843 C
ATOM 2135 CE LYS A 268 -44.765 3.102 48.505 1.00166.39 C
ANISOU 2135 CE LYS A 268 23199 22042 17978 892 2148 -908 C
ATOM 2136 NZ LYS A 268 -45.815 4.139 48.677 1.00175.33 N
ANISOU 2136 NZ LYS A 268 24319 23148 19151 820 2221 -1007 N
ATOM 2137 N THR A 269 -47.089 -3.172 47.885 1.00132.20 N
ANISOU 2137 N THR A 269 19396 17421 13415 925 2706 -668 N
ATOM 2138 CA THR A 269 -48.424 -3.787 47.854 1.00132.65 C
ANISOU 2138 CA THR A 269 19532 17424 13445 820 2891 -736 C
ATOM 2139 C THR A 269 -48.558 -4.868 48.936 1.00139.05 C
ANISOU 2139 C THR A 269 20590 18158 14085 836 3009 -697 C
ATOM 2140 O THR A 269 -49.606 -4.953 49.575 1.00139.13 O
ANISOU 2140 O THR A 269 20688 18141 14034 745 3132 -782 O
ATOM 2141 CB THR A 269 -48.780 -4.278 46.436 1.00140.02 C
ANISOU 2141 CB THR A 269 20382 18339 14479 765 2970 -743 C
ATOM 2142 OG1 THR A 269 -48.484 -3.246 45.494 1.00138.58 O
ANISOU 2142 OG1 THR A 269 19999 18219 14435 774 2846 -759 O
ATOM 2143 CG2 THR A 269 -50.249 -4.671 46.294 1.00138.84 C
ANISOU 2143 CG2 THR A 269 20253 18179 14322 628 3145 -849 C
ATOM 2144 N LEU A 270 -47.487 -5.662 49.162 1.00137.35 N
ANISOU 2144 N LEU A 270 20490 17907 13792 959 2975 -568 N
ATOM 2145 CA LEU A 270 -47.444 -6.711 50.186 1.00139.22 C
ANISOU 2145 CA LEU A 270 20989 18060 13849 1012 3078 -502 C
ATOM 2146 C LEU A 270 -47.508 -6.125 51.601 1.00145.30 C
ANISOU 2146 C LEU A 270 21849 18869 14492 1021 3010 -531 C
ATOM 2147 O LEU A 270 -48.105 -6.740 52.486 1.00145.98 O
ANISOU 2147 O LEU A 270 22153 18877 14435 989 3147 -543 O
ATOM 2148 CB LEU A 270 -46.195 -7.593 50.013 1.00139.98 C
ANISOU 2148 CB LEU A 270 21160 18121 13904 1178 3037 -343 C
ATOM 2149 CG LEU A 270 -46.416 -8.998 49.434 1.00145.10 C
ANISOU 2149 CG LEU A 270 21968 18634 14530 1174 3250 -289 C
ATOM 2150 CD1 LEU A 270 -46.837 -8.952 47.965 1.00143.84 C
ANISOU 2150 CD1 LEU A 270 21646 18474 14535 1060 3313 -353 C
ATOM 2151 CD2 LEU A 270 -45.164 -9.832 49.564 1.00148.68 C
ANISOU 2151 CD2 LEU A 270 22528 19045 14918 1373 3214 -119 C
ATOM 2152 N TYR A 271 -46.918 -4.926 51.799 1.00142.55 N
ANISOU 2152 N TYR A 271 21342 18632 14189 1047 2814 -551 N
ATOM 2153 CA TYR A 271 -46.927 -4.193 53.068 1.00143.72 C
ANISOU 2153 CA TYR A 271 21551 18832 14226 1032 2738 -595 C
ATOM 2154 C TYR A 271 -48.323 -3.612 53.329 1.00148.52 C
ANISOU 2154 C TYR A 271 22155 19411 14865 877 2864 -742 C
ATOM 2155 O TYR A 271 -48.776 -3.613 54.475 1.00149.14 O
ANISOU 2155 O TYR A 271 22398 19461 14809 834 2925 -781 O
ATOM 2156 CB TYR A 271 -45.852 -3.086 53.064 1.00144.67 C
ANISOU 2156 CB TYR A 271 21491 19081 14396 1083 2513 -589 C
ATOM 2157 CG TYR A 271 -45.841 -2.210 54.300 1.00147.34 C
ANISOU 2157 CG TYR A 271 21876 19482 14623 1040 2435 -651 C
ATOM 2158 CD1 TYR A 271 -45.310 -2.671 55.502 1.00151.07 C
ANISOU 2158 CD1 TYR A 271 22531 19979 14888 1114 2379 -582 C
ATOM 2159 CD2 TYR A 271 -46.325 -0.906 54.258 1.00147.37 C
ANISOU 2159 CD2 TYR A 271 21751 19522 14721 931 2419 -776 C
ATOM 2160 CE1 TYR A 271 -45.290 -1.866 56.640 1.00152.81 C
ANISOU 2160 CE1 TYR A 271 22805 20265 14992 1057 2308 -646 C
ATOM 2161 CE2 TYR A 271 -46.310 -0.091 55.390 1.00149.20 C
ANISOU 2161 CE2 TYR A 271 22038 19802 14849 876 2367 -841 C
ATOM 2162 CZ TYR A 271 -45.789 -0.575 56.579 1.00158.34 C
ANISOU 2162 CZ TYR A 271 23377 20991 15794 928 2309 -781 C
ATOM 2163 OH TYR A 271 -45.768 0.225 57.696 1.00160.36 O
ANISOU 2163 OH TYR A 271 23697 21300 15933 856 2260 -852 O
ATOM 2164 N MET A 272 -48.995 -3.119 52.265 1.00144.84 N
ANISOU 2164 N MET A 272 21503 18957 14571 799 2905 -821 N
ATOM 2165 CA MET A 272 -50.348 -2.554 52.331 1.00144.94 C
ANISOU 2165 CA MET A 272 21465 18961 14643 670 3023 -960 C
ATOM 2166 C MET A 272 -51.381 -3.659 52.575 1.00150.88 C
ANISOU 2166 C MET A 272 22383 19624 15321 588 3246 -1002 C
ATOM 2167 O MET A 272 -52.366 -3.428 53.277 1.00151.06 O
ANISOU 2167 O MET A 272 22464 19624 15309 493 3361 -1107 O
ATOM 2168 CB MET A 272 -50.690 -1.767 51.051 1.00145.90 C
ANISOU 2168 CB MET A 272 21338 19137 14960 641 2985 -1014 C
ATOM 2169 CG MET A 272 -49.879 -0.491 50.867 1.00148.97 C
ANISOU 2169 CG MET A 272 21577 19597 15428 692 2806 -1008 C
ATOM 2170 SD MET A 272 -50.210 0.799 52.091 1.00153.85 S
ANISOU 2170 SD MET A 272 22217 20235 16002 640 2788 -1106 S
ATOM 2171 CE MET A 272 -48.921 1.954 51.684 1.00149.98 C
ANISOU 2171 CE MET A 272 21581 19818 15588 699 2591 -1077 C
ATOM 2172 N LEU A 273 -51.143 -4.858 52.002 1.00148.63 N
ANISOU 2172 N LEU A 273 22181 19281 15011 616 3324 -926 N
ATOM 2173 CA LEU A 273 -52.002 -6.034 52.159 1.00149.85 C
ANISOU 2173 CA LEU A 273 22517 19336 15084 529 3559 -964 C
ATOM 2174 C LEU A 273 -51.688 -6.789 53.460 1.00156.73 C
ANISOU 2174 C LEU A 273 23693 20113 15743 581 3626 -896 C
ATOM 2175 O LEU A 273 -52.514 -7.577 53.923 1.00157.32 O
ANISOU 2175 O LEU A 273 23959 20091 15723 490 3842 -953 O
ATOM 2176 CB LEU A 273 -51.865 -6.972 50.952 1.00149.44 C
ANISOU 2176 CB LEU A 273 22439 19250 15090 526 3634 -917 C
ATOM 2177 N GLY A 274 -50.508 -6.528 54.030 1.00154.77 N
ANISOU 2177 N GLY A 274 23487 19901 15416 724 3443 -782 N
ATOM 2178 CA GLY A 274 -50.035 -7.136 55.271 1.00156.83 C
ANISOU 2178 CA GLY A 274 24026 20100 15461 809 3455 -694 C
ATOM 2179 C GLY A 274 -50.820 -6.740 56.508 1.00162.96 C
ANISOU 2179 C GLY A 274 24945 20849 16122 710 3534 -793 C
ATOM 2180 O GLY A 274 -50.858 -7.497 57.482 1.00164.11 O
ANISOU 2180 O GLY A 274 25380 20902 16074 734 3636 -749 O
ATOM 2181 N SER A 275 -51.446 -5.548 56.478 1.00159.69 N
ANISOU 2181 N SER A 275 24344 20508 15825 605 3497 -925 N
ATOM 2182 CA SER A 275 -52.257 -5.015 57.574 1.00160.82 C
ANISOU 2182 CA SER A 275 24589 20624 15891 495 3583 -1039 C
ATOM 2183 C SER A 275 -53.706 -5.510 57.515 1.00166.08 C
ANISOU 2183 C SER A 275 25315 21202 16585 337 3853 -1175 C
ATOM 2184 O SER A 275 -54.331 -5.680 58.563 1.00166.92 O
ANISOU 2184 O SER A 275 25627 21229 16565 256 3998 -1242 O
ATOM 2185 CB SER A 275 -52.219 -3.490 57.575 1.00163.58 C
ANISOU 2185 CB SER A 275 24716 21081 16356 466 3437 -1115 C
ATOM 2186 OG SER A 275 -52.698 -2.953 56.353 1.00170.82 O
ANISOU 2186 OG SER A 275 25361 22050 17492 427 3434 -1181 O
ATOM 2187 N LEU A 276 -54.236 -5.735 56.294 1.00162.48 N
ANISOU 2187 N LEU A 276 24678 20767 16289 285 3923 -1223 N
ATOM 2188 CA LEU A 276 -55.610 -6.195 56.066 1.00163.05 C
ANISOU 2188 CA LEU A 276 24751 20793 16408 122 4170 -1369 C
ATOM 2189 C LEU A 276 -55.760 -7.719 56.134 1.00168.95 C
ANISOU 2189 C LEU A 276 25761 21409 17024 88 4384 -1338 C
ATOM 2190 O LEU A 276 -56.654 -8.206 56.828 1.00169.80 O
ANISOU 2190 O LEU A 276 26051 21425 17041 -37 4610 -1440 O
ATOM 2191 CB LEU A 276 -56.163 -5.649 54.736 1.00161.77 C
ANISOU 2191 CB LEU A 276 24258 20741 16465 73 4135 -1448 C
ATOM 2192 CG LEU A 276 -56.521 -4.161 54.709 1.00165.86 C
ANISOU 2192 CG LEU A 276 24538 21361 17120 67 4022 -1529 C
ATOM 2193 CD1 LEU A 276 -56.254 -3.562 53.345 1.00164.56 C
ANISOU 2193 CD1 LEU A 276 24086 21305 17133 125 3869 -1501 C
ATOM 2194 CD2 LEU A 276 -57.970 -3.930 55.118 1.00169.21 C
ANISOU 2194 CD2 LEU A 276 24926 21783 17583 -79 4215 -1709 C
ATOM 2195 N LEU A 277 -54.894 -8.467 55.418 1.00165.89 N
ANISOU 2195 N LEU A 277 25402 20999 16628 192 4333 -1202 N
ATOM 2196 CA LEU A 277 -54.916 -9.935 55.380 1.00167.15 C
ANISOU 2196 CA LEU A 277 25825 21018 16668 178 4547 -1154 C
ATOM 2197 C LEU A 277 -54.256 -10.566 56.621 1.00173.42 C
ANISOU 2197 C LEU A 277 26976 21690 17227 294 4573 -1029 C
ATOM 2198 O LEU A 277 -54.479 -11.749 56.894 1.00174.33 O
ANISOU 2198 O LEU A 277 27377 21652 17207 266 4803 -1009 O
ATOM 2199 CB LEU A 277 -54.252 -10.445 54.085 1.00166.32 C
ANISOU 2199 CB LEU A 277 25607 20930 16655 248 4494 -1059 C
ATOM 2200 CG LEU A 277 -54.730 -11.799 53.548 1.00171.85 C
ANISOU 2200 CG LEU A 277 26470 21511 17314 146 4769 -1087 C
ATOM 2201 CD1 LEU A 277 -55.953 -11.641 52.655 1.00171.44 C
ANISOU 2201 CD1 LEU A 277 26195 21540 17404 -65 4889 -1277 C
ATOM 2202 CD2 LEU A 277 -53.628 -12.490 52.773 1.00174.06 C
ANISOU 2202 CD2 LEU A 277 26784 21748 17601 288 4715 -921 C
ATOM 2203 N HIS A 278 -53.464 -9.765 57.374 1.00170.66 N
ANISOU 2203 N HIS A 278 26615 21410 16819 418 4345 -950 N
ATOM 2204 CA HIS A 278 -52.729 -10.138 58.591 1.00172.46 C
ANISOU 2204 CA HIS A 278 27140 21571 16816 550 4301 -822 C
ATOM 2205 C HIS A 278 -51.715 -11.268 58.339 1.00177.67 C
ANISOU 2205 C HIS A 278 27971 22156 17379 736 4296 -628 C
ATOM 2206 O HIS A 278 -51.980 -12.437 58.635 1.00178.66 O
ANISOU 2206 O HIS A 278 28402 22116 17364 732 4530 -593 O
ATOM 2207 CB HIS A 278 -53.672 -10.445 59.775 1.00174.90 C
ANISOU 2207 CB HIS A 278 27741 21755 16958 423 4528 -920 C
ATOM 2208 CG HIS A 278 -54.480 -9.267 60.222 1.00177.84 C
ANISOU 2208 CG HIS A 278 27964 22200 17406 279 4510 -1087 C
ATOM 2209 ND1 HIS A 278 -55.715 -8.987 59.667 1.00178.85 N
ANISOU 2209 ND1 HIS A 278 27912 22343 17698 92 4667 -1273 N
ATOM 2210 CD2 HIS A 278 -54.201 -8.334 61.162 1.00179.93 C
ANISOU 2210 CD2 HIS A 278 28238 22526 17600 300 4361 -1092 C
ATOM 2211 CE1 HIS A 278 -56.146 -7.898 60.282 1.00178.16 C
ANISOU 2211 CE1 HIS A 278 27734 22314 17645 22 4617 -1377 C
ATOM 2212 NE2 HIS A 278 -55.269 -7.469 61.189 1.00179.10 N
ANISOU 2212 NE2 HIS A 278 27971 22455 17625 131 4442 -1277 N
ATOM 2213 N TRP A 279 -50.558 -10.898 57.763 1.00173.86 N
ANISOU 2213 N TRP A 279 27289 21791 16980 896 4045 -508 N
ATOM 2214 CA TRP A 279 -49.452 -11.804 57.446 1.00174.61 C
ANISOU 2214 CA TRP A 279 27483 21844 17017 1102 4002 -316 C
ATOM 2215 C TRP A 279 -48.597 -12.081 58.703 1.00180.71 C
ANISOU 2215 C TRP A 279 28505 22608 17547 1293 3894 -164 C
ATOM 2216 O TRP A 279 -48.611 -11.249 59.616 1.00180.61 O
ANISOU 2216 O TRP A 279 28486 22681 17456 1267 3764 -209 O
ATOM 2217 CB TRP A 279 -48.591 -11.210 56.317 1.00171.76 C
ANISOU 2217 CB TRP A 279 26782 21623 16856 1182 3779 -270 C
ATOM 2218 CG TRP A 279 -49.180 -11.391 54.949 1.00171.26 C
ANISOU 2218 CG TRP A 279 26549 21536 16985 1053 3905 -355 C
ATOM 2219 CD1 TRP A 279 -50.125 -10.609 54.353 1.00172.69 C
ANISOU 2219 CD1 TRP A 279 26504 21785 17326 869 3927 -523 C
ATOM 2220 CD2 TRP A 279 -48.853 -12.417 54.002 1.00171.14 C
ANISOU 2220 CD2 TRP A 279 26579 21431 17014 1104 4025 -273 C
ATOM 2221 NE1 TRP A 279 -50.409 -11.084 53.094 1.00171.27 N
ANISOU 2221 NE1 TRP A 279 26221 21578 17275 796 4037 -553 N
ATOM 2222 CE2 TRP A 279 -49.643 -12.195 52.852 1.00173.53 C
ANISOU 2222 CE2 TRP A 279 26677 21761 17495 926 4107 -407 C
ATOM 2223 CE3 TRP A 279 -47.967 -13.509 54.013 1.00173.72 C
ANISOU 2223 CE3 TRP A 279 27107 21655 17244 1291 4077 -97 C
ATOM 2224 CZ2 TRP A 279 -49.575 -13.022 51.725 1.00172.54 C
ANISOU 2224 CZ2 TRP A 279 26546 21565 17445 903 4241 -381 C
ATOM 2225 CZ3 TRP A 279 -47.900 -14.327 52.895 1.00174.86 C
ANISOU 2225 CZ3 TRP A 279 27250 21711 17477 1276 4226 -68 C
ATOM 2226 CH2 TRP A 279 -48.697 -14.082 51.768 1.00173.91 C
ANISOU 2226 CH2 TRP A 279 26929 21621 17526 1072 4308 -214 C
ATOM 2227 N PRO A 280 -47.845 -13.216 58.785 1.00178.95 N
ANISOU 2227 N PRO A 280 28507 22289 17197 1491 3944 17 N
ATOM 2228 CA PRO A 280 -47.040 -13.484 59.997 1.00181.07 C
ANISOU 2228 CA PRO A 280 29013 22567 17217 1694 3827 173 C
ATOM 2229 C PRO A 280 -45.956 -12.446 60.303 1.00184.85 C
ANISOU 2229 C PRO A 280 29250 23281 17703 1817 3462 227 C
ATOM 2230 O PRO A 280 -45.537 -11.705 59.411 1.00182.62 O
ANISOU 2230 O PRO A 280 28623 23135 17630 1801 3299 190 O
ATOM 2231 CB PRO A 280 -46.437 -14.869 59.729 1.00184.32 C
ANISOU 2231 CB PRO A 280 29654 22834 17543 1898 3957 359 C
ATOM 2232 CG PRO A 280 -47.297 -15.473 58.675 1.00187.60 C
ANISOU 2232 CG PRO A 280 30070 23105 18105 1729 4241 259 C
ATOM 2233 CD PRO A 280 -47.718 -14.325 57.817 1.00180.52 C
ANISOU 2233 CD PRO A 280 28773 22358 17457 1542 4124 91 C
ATOM 2234 N CYS A 281 -45.517 -12.400 61.579 1.00183.54 N
ANISOU 2234 N CYS A 281 29276 23163 17297 1928 3344 308 N
ATOM 2235 CA CYS A 281 -44.505 -11.478 62.110 1.00183.87 C
ANISOU 2235 CA CYS A 281 29137 23439 17287 2029 3008 350 C
ATOM 2236 C CYS A 281 -43.166 -11.534 61.365 1.00187.62 C
ANISOU 2236 C CYS A 281 29366 24054 17865 2242 2791 484 C
ATOM 2237 O CYS A 281 -42.561 -10.486 61.134 1.00186.23 O
ANISOU 2237 O CYS A 281 28879 24080 17801 2220 2552 432 O
ATOM 2238 CB CYS A 281 -44.317 -11.686 63.610 1.00186.85 C
ANISOU 2238 CB CYS A 281 29824 23822 17348 2120 2956 428 C
ATOM 2239 SG CYS A 281 -45.812 -11.405 64.594 1.00190.94 S
ANISOU 2239 SG CYS A 281 30607 24197 17746 1850 3189 247 S
ATOM 2240 N ASP A 282 -42.713 -12.748 60.993 1.00185.25 N
ANISOU 2240 N ASP A 282 29215 23640 17531 2439 2895 649 N
ATOM 2241 CA ASP A 282 -41.455 -12.976 60.276 1.00185.24 C
ANISOU 2241 CA ASP A 282 29010 23745 17629 2660 2730 789 C
ATOM 2242 C ASP A 282 -41.500 -12.460 58.832 1.00186.13 C
ANISOU 2242 C ASP A 282 28779 23889 18054 2534 2730 685 C
ATOM 2243 O ASP A 282 -40.483 -11.976 58.333 1.00185.31 O
ANISOU 2243 O ASP A 282 28389 23953 18067 2630 2512 720 O
ATOM 2244 CB ASP A 282 -41.077 -14.466 60.307 1.00189.20 C
ANISOU 2244 CB ASP A 282 29805 24078 18003 2905 2890 993 C
ATOM 2245 CG ASP A 282 -39.660 -14.746 59.851 1.00200.43 C
ANISOU 2245 CG ASP A 282 31048 25626 19481 3185 2701 1163 C
ATOM 2246 OD1 ASP A 282 -38.735 -14.622 60.681 1.00203.12 O
ANISOU 2246 OD1 ASP A 282 31379 26140 19658 3389 2461 1278 O
ATOM 2247 OD2 ASP A 282 -39.477 -15.090 58.664 1.00205.12 O
ANISOU 2247 OD2 ASP A 282 31505 26152 20280 3196 2795 1176 O
ATOM 2248 N PHE A 283 -42.672 -12.567 58.171 1.00180.79 N
ANISOU 2248 N PHE A 283 28132 23057 17501 2316 2974 554 N
ATOM 2249 CA PHE A 283 -42.890 -12.130 56.787 1.00177.99 C
ANISOU 2249 CA PHE A 283 27491 22717 17421 2179 3000 451 C
ATOM 2250 C PHE A 283 -42.796 -10.607 56.630 1.00179.70 C
ANISOU 2250 C PHE A 283 27378 23127 17773 2053 2777 315 C
ATOM 2251 O PHE A 283 -42.250 -10.134 55.631 1.00177.87 O
ANISOU 2251 O PHE A 283 26868 22981 17734 2056 2669 300 O
ATOM 2252 CB PHE A 283 -44.239 -12.651 56.262 1.00178.85 C
ANISOU 2252 CB PHE A 283 27731 22635 17589 1975 3312 338 C
ATOM 2253 CG PHE A 283 -44.308 -12.818 54.762 1.00178.73 C
ANISOU 2253 CG PHE A 283 27526 22582 17799 1906 3397 303 C
ATOM 2254 CD1 PHE A 283 -43.924 -14.011 54.161 1.00182.59 C
ANISOU 2254 CD1 PHE A 283 28149 22935 18292 2023 3554 425 C
ATOM 2255 CD2 PHE A 283 -44.776 -11.791 53.952 1.00178.70 C
ANISOU 2255 CD2 PHE A 283 27231 22672 17996 1725 3332 151 C
ATOM 2256 CE1 PHE A 283 -43.993 -14.168 52.773 1.00182.00 C
ANISOU 2256 CE1 PHE A 283 27913 22824 18413 1941 3639 386 C
ATOM 2257 CE2 PHE A 283 -44.846 -11.949 52.565 1.00180.07 C
ANISOU 2257 CE2 PHE A 283 27246 22815 18358 1659 3405 121 C
ATOM 2258 CZ PHE A 283 -44.454 -13.136 51.985 1.00178.87 C
ANISOU 2258 CZ PHE A 283 27225 22533 18203 1757 3557 234 C
ATOM 2259 N ASP A 284 -43.320 -9.849 57.614 1.00176.15 N
ANISOU 2259 N ASP A 284 26978 22732 17219 1939 2727 217 N
ATOM 2260 CA ASP A 284 -43.295 -8.383 57.623 1.00174.53 C
ANISOU 2260 CA ASP A 284 26510 22689 17116 1812 2548 83 C
ATOM 2261 C ASP A 284 -41.899 -7.817 57.909 1.00178.59 C
ANISOU 2261 C ASP A 284 26847 23412 17597 1955 2254 153 C
ATOM 2262 O ASP A 284 -41.605 -6.695 57.489 1.00176.89 O
ANISOU 2262 O ASP A 284 26361 23326 17523 1871 2112 58 O
ATOM 2263 CB ASP A 284 -44.328 -7.821 58.613 1.00176.63 C
ANISOU 2263 CB ASP A 284 26910 22927 17275 1640 2622 -46 C
ATOM 2264 CG ASP A 284 -45.702 -7.606 58.011 1.00185.12 C
ANISOU 2264 CG ASP A 284 27948 23892 18498 1429 2833 -201 C
ATOM 2265 OD1 ASP A 284 -46.381 -8.611 57.706 1.00185.76 O
ANISOU 2265 OD1 ASP A 284 28195 23816 18570 1401 3063 -191 O
ATOM 2266 OD2 ASP A 284 -46.108 -6.434 57.865 1.00189.81 O
ANISOU 2266 OD2 ASP A 284 28349 24560 19209 1291 2777 -336 O
ATOM 2267 N LEU A 285 -41.047 -8.588 58.621 1.00176.94 N
ANISOU 2267 N LEU A 285 26792 23241 17198 2172 2170 316 N
ATOM 2268 CA LEU A 285 -39.674 -8.203 58.966 1.00177.86 C
ANISOU 2268 CA LEU A 285 26741 23581 17257 2330 1886 392 C
ATOM 2269 C LEU A 285 -38.769 -8.127 57.736 1.00179.99 C
ANISOU 2269 C LEU A 285 26718 23923 17747 2410 1797 425 C
ATOM 2270 O LEU A 285 -37.880 -7.275 57.691 1.00179.62 O
ANISOU 2270 O LEU A 285 26415 24078 17753 2419 1576 386 O
ATOM 2271 CB LEU A 285 -39.074 -9.162 60.009 1.00180.91 C
ANISOU 2271 CB LEU A 285 27379 23984 17373 2568 1831 573 C
ATOM 2272 CG LEU A 285 -39.483 -8.938 61.467 1.00187.30 C
ANISOU 2272 CG LEU A 285 28426 24821 17918 2516 1800 547 C
ATOM 2273 CD1 LEU A 285 -39.344 -10.214 62.269 1.00190.11 C
ANISOU 2273 CD1 LEU A 285 29138 25076 18018 2734 1875 733 C
ATOM 2274 CD2 LEU A 285 -38.662 -7.826 62.114 1.00190.67 C
ANISOU 2274 CD2 LEU A 285 28649 25524 18273 2494 1505 489 C
ATOM 2275 N PHE A 286 -38.996 -9.015 56.745 1.00175.18 N
ANISOU 2275 N PHE A 286 26154 23146 17261 2453 1983 485 N
ATOM 2276 CA PHE A 286 -38.236 -9.067 55.493 1.00173.76 C
ANISOU 2276 CA PHE A 286 25732 22994 17294 2518 1946 516 C
ATOM 2277 C PHE A 286 -38.515 -7.839 54.622 1.00174.32 C
ANISOU 2277 C PHE A 286 25528 23120 17585 2306 1905 344 C
ATOM 2278 O PHE A 286 -37.571 -7.172 54.200 1.00173.66 O
ANISOU 2278 O PHE A 286 25184 23188 17611 2333 1731 323 O
ATOM 2279 CB PHE A 286 -38.543 -10.360 54.714 1.00175.43 C
ANISOU 2279 CB PHE A 286 26108 22988 17559 2588 2191 613 C
ATOM 2280 CG PHE A 286 -37.701 -11.555 55.096 1.00179.50 C
ANISOU 2280 CG PHE A 286 26791 23471 17939 2876 2198 821 C
ATOM 2281 CD1 PHE A 286 -36.488 -11.802 54.464 1.00183.22 C
ANISOU 2281 CD1 PHE A 286 27077 24023 18517 3062 2093 924 C
ATOM 2282 CD2 PHE A 286 -38.138 -12.454 56.061 1.00183.54 C
ANISOU 2282 CD2 PHE A 286 27659 23859 18219 2966 2327 916 C
ATOM 2283 CE1 PHE A 286 -35.714 -12.914 54.809 1.00186.63 C
ANISOU 2283 CE1 PHE A 286 27659 24423 18829 3355 2106 1127 C
ATOM 2284 CE2 PHE A 286 -37.364 -13.566 56.406 1.00188.86 C
ANISOU 2284 CE2 PHE A 286 28507 24490 18760 3257 2343 1124 C
ATOM 2285 CZ PHE A 286 -36.158 -13.789 55.777 1.00187.58 C
ANISOU 2285 CZ PHE A 286 28143 24417 18710 3458 2230 1232 C
ATOM 2286 N LEU A 287 -39.812 -7.528 54.389 1.00168.56 N
ANISOU 2286 N LEU A 287 24860 22273 16912 2099 2068 220 N
ATOM 2287 CA LEU A 287 -40.296 -6.405 53.573 1.00165.83 C
ANISOU 2287 CA LEU A 287 24297 21951 16760 1905 2062 63 C
ATOM 2288 C LEU A 287 -39.758 -5.040 54.020 1.00168.80 C
ANISOU 2288 C LEU A 287 24481 22512 17142 1845 1850 -31 C
ATOM 2289 O LEU A 287 -39.472 -4.196 53.170 1.00167.04 O
ANISOU 2289 O LEU A 287 24030 22345 17094 1771 1788 -108 O
ATOM 2290 CB LEU A 287 -41.836 -6.381 53.526 1.00164.78 C
ANISOU 2290 CB LEU A 287 24288 21680 16640 1723 2267 -44 C
ATOM 2291 CG LEU A 287 -42.537 -7.604 52.919 1.00169.29 C
ANISOU 2291 CG LEU A 287 25025 22070 17229 1716 2509 0 C
ATOM 2292 CD1 LEU A 287 -43.929 -7.771 53.491 1.00169.51 C
ANISOU 2292 CD1 LEU A 287 25244 21993 17171 1571 2696 -90 C
ATOM 2293 CD2 LEU A 287 -42.596 -7.521 51.400 1.00170.07 C
ANISOU 2293 CD2 LEU A 287 24938 22136 17545 1652 2560 -35 C
ATOM 2294 N MET A 288 -39.612 -4.835 55.345 1.00166.28 N
ANISOU 2294 N MET A 288 24272 22283 16623 1867 1751 -27 N
ATOM 2295 CA MET A 288 -39.104 -3.596 55.943 1.00166.16 C
ANISOU 2295 CA MET A 288 24111 22449 16574 1793 1563 -123 C
ATOM 2296 C MET A 288 -37.608 -3.385 55.666 1.00169.80 C
ANISOU 2296 C MET A 288 24344 23095 17080 1911 1355 -78 C
ATOM 2297 O MET A 288 -37.162 -2.238 55.599 1.00169.02 O
ANISOU 2297 O MET A 288 24048 23127 17045 1809 1235 -192 O
ATOM 2298 CB MET A 288 -39.380 -3.579 57.455 1.00170.29 C
ANISOU 2298 CB MET A 288 24844 23012 16845 1781 1529 -126 C
ATOM 2299 CG MET A 288 -39.607 -2.191 58.017 1.00173.76 C
ANISOU 2299 CG MET A 288 25206 23546 17269 1597 1459 -286 C
ATOM 2300 SD MET A 288 -41.257 -1.541 57.654 1.00175.83 S
ANISOU 2300 SD MET A 288 25512 23630 17664 1376 1685 -439 S
ATOM 2301 CE MET A 288 -41.190 -0.003 58.534 1.00173.07 C
ANISOU 2301 CE MET A 288 25100 23407 17251 1210 1583 -595 C
ATOM 2302 N ASN A 289 -36.841 -4.485 55.513 1.00166.80 N
ANISOU 2302 N ASN A 289 23992 22721 16665 2125 1328 81 N
ATOM 2303 CA ASN A 289 -35.400 -4.457 55.242 1.00167.37 C
ANISOU 2303 CA ASN A 289 23840 22970 16783 2266 1143 136 C
ATOM 2304 C ASN A 289 -35.059 -4.500 53.745 1.00168.58 C
ANISOU 2304 C ASN A 289 23803 23059 17190 2266 1205 131 C
ATOM 2305 O ASN A 289 -33.980 -4.046 53.359 1.00168.53 O
ANISOU 2305 O ASN A 289 23554 23203 17277 2300 1064 107 O
ATOM 2306 CB ASN A 289 -34.682 -5.574 55.998 1.00171.01 C
ANISOU 2306 CB ASN A 289 24429 23492 17055 2525 1065 319 C
ATOM 2307 CG ASN A 289 -34.549 -5.307 57.475 1.00197.06 C
ANISOU 2307 CG ASN A 289 27836 26945 20094 2542 915 318 C
ATOM 2308 OD1 ASN A 289 -35.420 -5.657 58.277 1.00192.02 O
ANISOU 2308 OD1 ASN A 289 27474 26196 19288 2513 1017 338 O
ATOM 2309 ND2 ASN A 289 -33.451 -4.679 57.868 1.00190.67 N
ANISOU 2309 ND2 ASN A 289 26811 26398 19238 2576 676 286 N
ATOM 2310 N ILE A 290 -35.972 -5.037 52.910 1.00162.65 N
ANISOU 2310 N ILE A 290 23161 22092 16544 2214 1419 143 N
ATOM 2311 CA ILE A 290 -35.796 -5.137 51.455 1.00160.48 C
ANISOU 2311 CA ILE A 290 22746 21733 16496 2195 1503 137 C
ATOM 2312 C ILE A 290 -36.177 -3.802 50.766 1.00161.35 C
ANISOU 2312 C ILE A 290 22685 21857 16765 1980 1497 -33 C
ATOM 2313 O ILE A 290 -35.545 -3.437 49.771 1.00160.17 O
ANISOU 2313 O ILE A 290 22343 21730 16784 1964 1469 -64 O
ATOM 2314 CB ILE A 290 -36.527 -6.397 50.875 1.00163.03 C
ANISOU 2314 CB ILE A 290 23271 21835 16837 2237 1735 230 C
ATOM 2315 CG1 ILE A 290 -35.885 -7.703 51.412 1.00165.67 C
ANISOU 2315 CG1 ILE A 290 23761 22151 17035 2485 1745 414 C
ATOM 2316 CG2 ILE A 290 -36.544 -6.415 49.335 1.00162.00 C
ANISOU 2316 CG2 ILE A 290 23015 21607 16930 2170 1840 201 C
ATOM 2317 CD1 ILE A 290 -36.800 -8.956 51.409 1.00173.06 C
ANISOU 2317 CD1 ILE A 290 25000 22863 17892 2511 1995 497 C
ATOM 2318 N PHE A 291 -37.169 -3.062 51.325 1.00156.45 N
ANISOU 2318 N PHE A 291 22141 21217 16086 1826 1529 -140 N
ATOM 2319 CA PHE A 291 -37.656 -1.774 50.804 1.00154.25 C
ANISOU 2319 CA PHE A 291 21738 20934 15935 1640 1541 -292 C
ATOM 2320 C PHE A 291 -36.558 -0.684 50.639 1.00157.50 C
ANISOU 2320 C PHE A 291 21917 21504 16421 1602 1382 -375 C
ATOM 2321 O PHE A 291 -36.555 -0.069 49.571 1.00155.67 O
ANISOU 2321 O PHE A 291 21558 21227 16361 1519 1421 -442 O
ATOM 2322 CB PHE A 291 -38.845 -1.235 51.620 1.00155.76 C
ANISOU 2322 CB PHE A 291 22063 21084 16033 1511 1607 -381 C
ATOM 2323 CG PHE A 291 -39.588 -0.095 50.960 1.00155.59 C
ANISOU 2323 CG PHE A 291 21950 21013 16153 1348 1669 -514 C
ATOM 2324 CD1 PHE A 291 -40.476 -0.332 49.916 1.00157.08 C
ANISOU 2324 CD1 PHE A 291 22145 21069 16467 1301 1815 -521 C
ATOM 2325 CD2 PHE A 291 -39.409 1.215 51.389 1.00157.89 C
ANISOU 2325 CD2 PHE A 291 22155 21394 16442 1244 1589 -631 C
ATOM 2326 CE1 PHE A 291 -41.161 0.723 49.305 1.00156.68 C
ANISOU 2326 CE1 PHE A 291 22010 20983 16538 1179 1863 -630 C
ATOM 2327 CE2 PHE A 291 -40.096 2.269 50.779 1.00159.36 C
ANISOU 2327 CE2 PHE A 291 22275 21519 16755 1118 1661 -741 C
ATOM 2328 CZ PHE A 291 -40.968 2.015 49.742 1.00155.96 C
ANISOU 2328 CZ PHE A 291 21846 20962 16447 1100 1790 -732 C
ATOM 2329 N PRO A 292 -35.616 -0.418 51.597 1.00155.22 N
ANISOU 2329 N PRO A 292 21565 21401 16009 1651 1209 -380 N
ATOM 2330 CA PRO A 292 -34.585 0.612 51.338 1.00155.08 C
ANISOU 2330 CA PRO A 292 21314 21534 16074 1586 1083 -482 C
ATOM 2331 C PRO A 292 -33.671 0.272 50.156 1.00157.61 C
ANISOU 2331 C PRO A 292 21464 21854 16566 1665 1078 -440 C
ATOM 2332 O PRO A 292 -33.109 1.178 49.540 1.00156.73 O
ANISOU 2332 O PRO A 292 21177 21793 16580 1569 1047 -546 O
ATOM 2333 CB PRO A 292 -33.803 0.681 52.656 1.00159.31 C
ANISOU 2333 CB PRO A 292 21832 22285 16413 1640 901 -478 C
ATOM 2334 CG PRO A 292 -34.696 0.062 53.674 1.00164.39 C
ANISOU 2334 CG PRO A 292 22730 22863 16868 1678 950 -409 C
ATOM 2335 CD PRO A 292 -35.429 -1.009 52.937 1.00158.74 C
ANISOU 2335 CD PRO A 292 22148 21938 16226 1758 1122 -301 C
ATOM 2336 N TYR A 293 -33.545 -1.033 49.835 1.00153.68 N
ANISOU 2336 N TYR A 293 21036 21281 16073 1833 1130 -289 N
ATOM 2337 CA TYR A 293 -32.769 -1.544 48.705 1.00152.87 C
ANISOU 2337 CA TYR A 293 20806 21144 16132 1921 1160 -232 C
ATOM 2338 C TYR A 293 -33.606 -1.510 47.418 1.00153.37 C
ANISOU 2338 C TYR A 293 20912 21004 16357 1816 1339 -258 C
ATOM 2339 O TYR A 293 -33.038 -1.459 46.326 1.00152.30 O
ANISOU 2339 O TYR A 293 20649 20835 16382 1810 1370 -269 O
ATOM 2340 CB TYR A 293 -32.243 -2.960 48.994 1.00155.66 C
ANISOU 2340 CB TYR A 293 21234 21503 16407 2157 1152 -53 C
ATOM 2341 CG TYR A 293 -31.145 -2.993 50.035 1.00160.01 C
ANISOU 2341 CG TYR A 293 21682 22291 16823 2293 946 -17 C
ATOM 2342 CD1 TYR A 293 -29.809 -2.844 49.673 1.00163.16 C
ANISOU 2342 CD1 TYR A 293 21828 22849 17317 2368 829 -30 C
ATOM 2343 CD2 TYR A 293 -31.439 -3.178 51.383 1.00162.22 C
ANISOU 2343 CD2 TYR A 293 22114 22647 16874 2345 868 25 C
ATOM 2344 CE1 TYR A 293 -28.793 -2.870 50.628 1.00166.58 C
ANISOU 2344 CE1 TYR A 293 22139 23534 17619 2496 624 -3 C
ATOM 2345 CE2 TYR A 293 -30.432 -3.205 52.347 1.00165.73 C
ANISOU 2345 CE2 TYR A 293 22462 23333 17173 2474 661 60 C
ATOM 2346 CZ TYR A 293 -29.109 -3.052 51.964 1.00174.35 C
ANISOU 2346 CZ TYR A 293 23279 24604 18363 2552 533 46 C
ATOM 2347 OH TYR A 293 -28.112 -3.081 52.909 1.00178.17 O
ANISOU 2347 OH TYR A 293 23641 25358 18698 2682 315 76 O
ATOM 2348 N CYS A 294 -34.954 -1.522 47.553 1.00147.98 N
ANISOU 2348 N CYS A 294 20403 20196 15627 1729 1454 -276 N
ATOM 2349 CA CYS A 294 -35.897 -1.435 46.433 1.00145.42 C
ANISOU 2349 CA CYS A 294 20116 19707 15428 1622 1609 -310 C
ATOM 2350 C CYS A 294 -35.909 -0.015 45.867 1.00147.41 C
ANISOU 2350 C CYS A 294 20234 19980 15795 1473 1583 -450 C
ATOM 2351 O CYS A 294 -36.108 0.165 44.664 1.00145.67 O
ANISOU 2351 O CYS A 294 19971 19664 15713 1414 1665 -472 O
ATOM 2352 CB CYS A 294 -37.294 -1.885 46.849 1.00145.12 C
ANISOU 2352 CB CYS A 294 20280 19562 15296 1580 1731 -296 C
ATOM 2353 SG CYS A 294 -37.479 -3.679 47.007 1.00149.78 S
ANISOU 2353 SG CYS A 294 21072 20045 15793 1725 1854 -137 S
ATOM 2354 N THR A 295 -35.686 0.989 46.739 1.00144.05 N
ANISOU 2354 N THR A 295 19757 19675 15301 1409 1478 -543 N
ATOM 2355 CA THR A 295 -35.605 2.404 46.365 1.00142.94 C
ANISOU 2355 CA THR A 295 19511 19552 15248 1268 1464 -681 C
ATOM 2356 C THR A 295 -34.254 2.687 45.699 1.00146.42 C
ANISOU 2356 C THR A 295 19765 20068 15800 1277 1399 -712 C
ATOM 2357 O THR A 295 -34.149 3.623 44.907 1.00145.20 O
ANISOU 2357 O THR A 295 19536 19870 15761 1172 1438 -805 O
ATOM 2358 CB THR A 295 -35.857 3.322 47.573 1.00151.93 C
ANISOU 2358 CB THR A 295 20683 20780 16264 1182 1404 -776 C
ATOM 2359 OG1 THR A 295 -35.001 2.944 48.652 1.00153.62 O
ANISOU 2359 OG1 THR A 295 20872 21158 16339 1260 1266 -743 O
ATOM 2360 CG2 THR A 295 -37.313 3.319 48.024 1.00149.72 C
ANISOU 2360 CG2 THR A 295 20571 20399 15916 1137 1503 -781 C
ATOM 2361 N CYS A 296 -33.228 1.867 46.017 1.00143.78 N
ANISOU 2361 N CYS A 296 19359 19841 15429 1411 1308 -632 N
ATOM 2362 CA CYS A 296 -31.878 1.968 45.460 1.00144.11 C
ANISOU 2362 CA CYS A 296 19204 19973 15576 1439 1246 -657 C
ATOM 2363 C CYS A 296 -31.862 1.530 43.993 1.00145.87 C
ANISOU 2363 C CYS A 296 19415 20041 15970 1451 1371 -614 C
ATOM 2364 O CYS A 296 -31.354 2.270 43.151 1.00144.97 O
ANISOU 2364 O CYS A 296 19187 19910 15984 1359 1395 -704 O
ATOM 2365 CB CYS A 296 -30.882 1.168 46.297 1.00146.55 C
ANISOU 2365 CB CYS A 296 19440 20455 15787 1605 1110 -572 C
ATOM 2366 SG CYS A 296 -29.154 1.362 45.787 1.00151.90 S
ANISOU 2366 SG CYS A 296 19831 21295 16591 1641 1015 -625 S
ATOM 2367 N ILE A 297 -32.441 0.344 43.689 1.00141.33 N
ANISOU 2367 N ILE A 297 18972 19343 15384 1547 1464 -484 N
ATOM 2368 CA ILE A 297 -32.515 -0.226 42.335 1.00139.75 C
ANISOU 2368 CA ILE A 297 18790 18989 15322 1552 1597 -434 C
ATOM 2369 C ILE A 297 -33.439 0.589 41.409 1.00141.12 C
ANISOU 2369 C ILE A 297 19010 19035 15574 1395 1695 -516 C
ATOM 2370 O ILE A 297 -33.243 0.561 40.192 1.00139.92 O
ANISOU 2370 O ILE A 297 18827 18786 15548 1358 1776 -521 O
ATOM 2371 CB ILE A 297 -32.852 -1.746 42.318 1.00143.05 C
ANISOU 2371 CB ILE A 297 19350 19311 15691 1686 1688 -282 C
ATOM 2372 CG1 ILE A 297 -34.118 -2.087 43.127 1.00143.19 C
ANISOU 2372 CG1 ILE A 297 19561 19283 15562 1676 1730 -250 C
ATOM 2373 CG2 ILE A 297 -31.658 -2.584 42.771 1.00145.69 C
ANISOU 2373 CG2 ILE A 297 19609 19744 16002 1873 1615 -184 C
ATOM 2374 CD1 ILE A 297 -35.284 -2.485 42.293 1.00149.11 C
ANISOU 2374 CD1 ILE A 297 20441 19868 16348 1596 1893 -239 C
ATOM 2375 N SER A 298 -34.421 1.322 41.980 1.00136.67 N
ANISOU 2375 N SER A 298 18522 18472 14934 1311 1688 -578 N
ATOM 2376 CA SER A 298 -35.325 2.188 41.216 1.00134.82 C
ANISOU 2376 CA SER A 298 18326 18137 14763 1188 1767 -651 C
ATOM 2377 C SER A 298 -34.562 3.434 40.746 1.00138.13 C
ANISOU 2377 C SER A 298 18626 18581 15275 1098 1738 -765 C
ATOM 2378 O SER A 298 -34.821 3.934 39.650 1.00136.66 O
ANISOU 2378 O SER A 298 18449 18291 15183 1030 1816 -799 O
ATOM 2379 CB SER A 298 -36.545 2.577 42.046 1.00138.09 C
ANISOU 2379 CB SER A 298 18845 18550 15073 1145 1776 -682 C
ATOM 2380 OG SER A 298 -36.207 3.415 43.139 1.00147.82 O
ANISOU 2380 OG SER A 298 20040 19895 16229 1112 1682 -759 O
ATOM 2381 N TYR A 299 -33.604 3.910 41.573 1.00135.59 N
ANISOU 2381 N TYR A 299 18199 18403 14916 1094 1632 -828 N
ATOM 2382 CA TYR A 299 -32.736 5.049 41.267 1.00135.64 C
ANISOU 2382 CA TYR A 299 18087 18452 14999 993 1614 -956 C
ATOM 2383 C TYR A 299 -31.689 4.656 40.219 1.00139.16 C
ANISOU 2383 C TYR A 299 18424 18874 15578 1018 1643 -942 C
ATOM 2384 O TYR A 299 -31.248 5.514 39.453 1.00138.52 O
ANISOU 2384 O TYR A 299 18290 18746 15594 916 1694 -1038 O
ATOM 2385 CB TYR A 299 -32.044 5.577 42.536 1.00138.42 C
ANISOU 2385 CB TYR A 299 18350 18990 15251 967 1491 -1037 C
ATOM 2386 CG TYR A 299 -32.707 6.792 43.152 1.00140.00 C
ANISOU 2386 CG TYR A 299 18620 19187 15385 844 1507 -1147 C
ATOM 2387 CD1 TYR A 299 -32.624 8.041 42.543 1.00141.66 C
ANISOU 2387 CD1 TYR A 299 18821 19327 15674 712 1585 -1269 C
ATOM 2388 CD2 TYR A 299 -33.364 6.706 44.375 1.00141.15 C
ANISOU 2388 CD2 TYR A 299 18854 19393 15384 860 1457 -1131 C
ATOM 2389 CE1 TYR A 299 -33.211 9.167 43.117 1.00142.51 C
ANISOU 2389 CE1 TYR A 299 19007 19417 15723 607 1622 -1368 C
ATOM 2390 CE2 TYR A 299 -33.956 7.825 44.959 1.00142.09 C
ANISOU 2390 CE2 TYR A 299 19042 19500 15446 745 1490 -1235 C
ATOM 2391 CZ TYR A 299 -33.879 9.054 44.325 1.00149.03 C
ANISOU 2391 CZ TYR A 299 19910 20303 16411 623 1575 -1351 C
ATOM 2392 OH TYR A 299 -34.461 10.161 44.894 1.00150.02 O
ANISOU 2392 OH TYR A 299 20117 20399 16483 518 1630 -1450 O
ATOM 2393 N VAL A 300 -31.297 3.357 40.191 1.00135.82 N
ANISOU 2393 N VAL A 300 17979 18469 15158 1152 1628 -823 N
ATOM 2394 CA VAL A 300 -30.333 2.779 39.243 1.00135.77 C
ANISOU 2394 CA VAL A 300 17876 18429 15279 1198 1672 -791 C
ATOM 2395 C VAL A 300 -30.878 2.913 37.810 1.00137.66 C
ANISOU 2395 C VAL A 300 18205 18475 15624 1118 1815 -792 C
ATOM 2396 O VAL A 300 -30.135 3.323 36.920 1.00137.30 O
ANISOU 2396 O VAL A 300 18083 18388 15697 1054 1865 -856 O
ATOM 2397 CB VAL A 300 -29.944 1.315 39.622 1.00140.60 C
ANISOU 2397 CB VAL A 300 18482 19084 15855 1380 1644 -647 C
ATOM 2398 CG1 VAL A 300 -29.211 0.598 38.487 1.00140.46 C
ANISOU 2398 CG1 VAL A 300 18409 18979 15981 1429 1737 -597 C
ATOM 2399 CG2 VAL A 300 -29.106 1.281 40.896 1.00142.40 C
ANISOU 2399 CG2 VAL A 300 18586 19531 15989 1469 1484 -653 C
ATOM 2400 N ASN A 301 -32.189 2.633 37.618 1.00132.62 N
ANISOU 2400 N ASN A 301 17725 17730 14933 1110 1878 -733 N
ATOM 2401 CA ASN A 301 -32.915 2.721 36.343 1.00130.89 C
ANISOU 2401 CA ASN A 301 17603 17352 14778 1039 1995 -724 C
ATOM 2402 C ASN A 301 -32.783 4.098 35.671 1.00134.09 C
ANISOU 2402 C ASN A 301 17991 17707 15252 918 2024 -841 C
ATOM 2403 O ASN A 301 -32.746 4.169 34.442 1.00133.07 O
ANISOU 2403 O ASN A 301 17896 17459 15204 867 2114 -843 O
ATOM 2404 CB ASN A 301 -34.388 2.366 36.552 1.00130.59 C
ANISOU 2404 CB ASN A 301 17705 17266 14646 1045 2027 -669 C
ATOM 2405 CG ASN A 301 -35.196 2.258 35.283 1.00151.45 C
ANISOU 2405 CG ASN A 301 20437 19777 17330 985 2132 -648 C
ATOM 2406 OD1 ASN A 301 -35.138 1.258 34.561 1.00145.80 O
ANISOU 2406 OD1 ASN A 301 19759 18990 16646 1003 2210 -578 O
ATOM 2407 ND2 ASN A 301 -35.983 3.284 34.993 1.00142.16 N
ANISOU 2407 ND2 ASN A 301 19300 18568 16146 915 2140 -706 N
ATOM 2408 N SER A 302 -32.705 5.176 36.478 1.00130.94 N
ANISOU 2408 N SER A 302 17555 17388 14809 867 1962 -938 N
ATOM 2409 CA SER A 302 -32.555 6.557 36.010 1.00130.64 C
ANISOU 2409 CA SER A 302 17522 17296 14818 751 2007 -1056 C
ATOM 2410 C SER A 302 -31.205 6.784 35.313 1.00134.95 C
ANISOU 2410 C SER A 302 17960 17835 15479 697 2044 -1129 C
ATOM 2411 O SER A 302 -31.150 7.527 34.331 1.00134.12 O
ANISOU 2411 O SER A 302 17908 17610 15441 611 2138 -1187 O
ATOM 2412 CB SER A 302 -32.731 7.535 37.167 1.00134.86 C
ANISOU 2412 CB SER A 302 18050 17921 15269 705 1949 -1146 C
ATOM 2413 OG SER A 302 -32.823 8.874 36.711 1.00143.57 O
ANISOU 2413 OG SER A 302 19206 18939 16406 599 2025 -1250 O
ATOM 2414 N CYS A 303 -30.129 6.135 35.809 1.00132.52 N
ANISOU 2414 N CYS A 303 17504 17655 15193 753 1975 -1125 N
ATOM 2415 CA CYS A 303 -28.782 6.238 35.237 1.00133.24 C
ANISOU 2415 CA CYS A 303 17457 17766 15401 710 2007 -1200 C
ATOM 2416 C CYS A 303 -28.415 5.034 34.347 1.00136.70 C
ANISOU 2416 C CYS A 303 17882 18127 15929 790 2070 -1097 C
ATOM 2417 O CYS A 303 -27.392 5.076 33.659 1.00136.91 O
ANISOU 2417 O CYS A 303 17812 18135 16073 750 2129 -1155 O
ATOM 2418 CB CYS A 303 -27.736 6.488 36.322 1.00135.34 C
ANISOU 2418 CB CYS A 303 17536 18247 15641 708 1893 -1289 C
ATOM 2419 SG CYS A 303 -27.307 5.026 37.305 1.00140.33 S
ANISOU 2419 SG CYS A 303 18057 19051 16211 908 1757 -1155 S
ATOM 2420 N LEU A 304 -29.255 3.977 34.351 1.00132.30 N
ANISOU 2420 N LEU A 304 17430 17519 15318 889 2077 -955 N
ATOM 2421 CA LEU A 304 -29.056 2.768 33.547 1.00131.86 C
ANISOU 2421 CA LEU A 304 17397 17372 15330 959 2160 -851 C
ATOM 2422 C LEU A 304 -29.575 2.957 32.119 1.00134.37 C
ANISOU 2422 C LEU A 304 17847 17500 15705 861 2294 -853 C
ATOM 2423 O LEU A 304 -29.036 2.340 31.200 1.00133.99 O
ANISOU 2423 O LEU A 304 17796 17363 15751 861 2391 -824 O
ATOM 2424 CB LEU A 304 -29.727 1.550 34.208 1.00131.78 C
ANISOU 2424 CB LEU A 304 17462 17385 15223 1090 2132 -711 C
ATOM 2425 CG LEU A 304 -29.166 0.171 33.844 1.00137.08 C
ANISOU 2425 CG LEU A 304 18121 18013 15951 1204 2200 -602 C
ATOM 2426 CD1 LEU A 304 -27.975 -0.192 34.722 1.00139.11 C
ANISOU 2426 CD1 LEU A 304 18202 18433 16220 1336 2102 -589 C
ATOM 2427 CD2 LEU A 304 -30.232 -0.895 33.978 1.00138.92 C
ANISOU 2427 CD2 LEU A 304 18520 18174 16090 1266 2253 -478 C
ATOM 2428 N ASN A 305 -30.617 3.802 31.938 1.00129.91 N
ANISOU 2428 N ASN A 305 17402 16878 15080 785 2302 -883 N
ATOM 2429 CA ASN A 305 -31.224 4.111 30.639 1.00128.74 C
ANISOU 2429 CA ASN A 305 17388 16571 14957 702 2406 -882 C
ATOM 2430 C ASN A 305 -30.220 4.685 29.609 1.00133.30 C
ANISOU 2430 C ASN A 305 17940 17056 15652 607 2499 -968 C
ATOM 2431 O ASN A 305 -30.189 4.139 28.505 1.00132.47 O
ANISOU 2431 O ASN A 305 17906 16831 15596 580 2599 -926 O
ATOM 2432 CB ASN A 305 -32.460 5.012 30.783 1.00128.27 C
ANISOU 2432 CB ASN A 305 17436 16494 14808 668 2380 -899 C
ATOM 2433 CG ASN A 305 -33.692 4.333 31.344 1.00148.77 C
ANISOU 2433 CG ASN A 305 20095 19131 17299 733 2338 -811 C
ATOM 2434 OD1 ASN A 305 -33.804 3.101 31.405 1.00142.42 O
ANISOU 2434 OD1 ASN A 305 19300 18334 16478 789 2354 -725 O
ATOM 2435 ND2 ASN A 305 -34.665 5.135 31.747 1.00140.21 N
ANISOU 2435 ND2 ASN A 305 19064 18065 16143 724 2302 -835 N
ATOM 2436 N PRO A 306 -29.352 5.697 29.922 1.00131.01 N
ANISOU 2436 N PRO A 306 17554 16815 15406 544 2485 -1096 N
ATOM 2437 CA PRO A 306 -28.390 6.179 28.907 1.00131.45 C
ANISOU 2437 CA PRO A 306 17597 16772 15577 441 2600 -1188 C
ATOM 2438 C PRO A 306 -27.408 5.113 28.414 1.00136.19 C
ANISOU 2438 C PRO A 306 18100 17358 16289 476 2659 -1156 C
ATOM 2439 O PRO A 306 -26.948 5.201 27.275 1.00135.76 O
ANISOU 2439 O PRO A 306 18094 17168 16320 395 2786 -1192 O
ATOM 2440 CB PRO A 306 -27.665 7.328 29.616 1.00134.29 C
ANISOU 2440 CB PRO A 306 17850 17226 15949 367 2567 -1340 C
ATOM 2441 CG PRO A 306 -28.579 7.741 30.708 1.00138.35 C
ANISOU 2441 CG PRO A 306 18398 17831 16338 407 2460 -1323 C
ATOM 2442 CD PRO A 306 -29.216 6.476 31.170 1.00133.27 C
ANISOU 2442 CD PRO A 306 17755 17245 15637 541 2383 -1176 C
ATOM 2443 N PHE A 307 -27.105 4.105 29.261 1.00133.68 N
ANISOU 2443 N PHE A 307 17659 17170 15964 604 2577 -1083 N
ATOM 2444 CA PHE A 307 -26.235 2.977 28.919 1.00134.47 C
ANISOU 2444 CA PHE A 307 17668 17261 16164 677 2635 -1029 C
ATOM 2445 C PHE A 307 -26.937 2.068 27.906 1.00137.85 C
ANISOU 2445 C PHE A 307 18269 17520 16588 679 2749 -916 C
ATOM 2446 O PHE A 307 -26.283 1.553 26.999 1.00137.78 O
ANISOU 2446 O PHE A 307 18258 17408 16685 656 2874 -912 O
ATOM 2447 CB PHE A 307 -25.853 2.175 30.174 1.00137.32 C
ANISOU 2447 CB PHE A 307 17881 17804 16490 840 2511 -962 C
ATOM 2448 CG PHE A 307 -24.699 2.738 30.969 1.00140.57 C
ANISOU 2448 CG PHE A 307 18062 18403 16944 846 2417 -1076 C
ATOM 2449 CD1 PHE A 307 -24.916 3.669 31.977 1.00143.91 C
ANISOU 2449 CD1 PHE A 307 18444 18964 17271 806 2294 -1155 C
ATOM 2450 CD2 PHE A 307 -23.398 2.311 30.732 1.00144.24 C
ANISOU 2450 CD2 PHE A 307 18343 18920 17541 889 2454 -1108 C
ATOM 2451 CE1 PHE A 307 -23.847 4.182 32.720 1.00146.58 C
ANISOU 2451 CE1 PHE A 307 18563 19497 17633 790 2205 -1275 C
ATOM 2452 CE2 PHE A 307 -22.330 2.823 31.475 1.00148.88 C
ANISOU 2452 CE2 PHE A 307 18691 19715 18162 887 2357 -1227 C
ATOM 2453 CZ PHE A 307 -22.562 3.754 32.464 1.00147.21 C
ANISOU 2453 CZ PHE A 307 18444 19648 17842 830 2230 -1312 C
ATOM 2454 N LEU A 308 -28.270 1.893 28.053 1.00133.72 N
ANISOU 2454 N LEU A 308 17892 16973 15940 693 2716 -837 N
ATOM 2455 CA LEU A 308 -29.104 1.074 27.165 1.00132.85 C
ANISOU 2455 CA LEU A 308 17949 16732 15797 673 2814 -744 C
ATOM 2456 C LEU A 308 -29.225 1.703 25.774 1.00136.83 C
ANISOU 2456 C LEU A 308 18575 17080 16334 532 2923 -796 C
ATOM 2457 O LEU A 308 -29.317 0.974 24.785 1.00136.11 O
ANISOU 2457 O LEU A 308 18583 16869 16266 490 3041 -748 O
ATOM 2458 CB LEU A 308 -30.498 0.818 27.771 1.00132.03 C
ANISOU 2458 CB LEU A 308 17942 16675 15549 712 2743 -671 C
ATOM 2459 CG LEU A 308 -30.549 0.123 29.140 1.00137.24 C
ANISOU 2459 CG LEU A 308 18532 17467 16147 848 2649 -607 C
ATOM 2460 CD1 LEU A 308 -31.871 0.377 29.826 1.00136.62 C
ANISOU 2460 CD1 LEU A 308 18531 17444 15933 852 2570 -587 C
ATOM 2461 CD2 LEU A 308 -30.276 -1.373 29.031 1.00140.22 C
ANISOU 2461 CD2 LEU A 308 18935 17797 16546 935 2739 -501 C
ATOM 2462 N TYR A 309 -29.202 3.054 25.700 1.00133.97 N
ANISOU 2462 N TYR A 309 18220 16714 15967 456 2894 -896 N
ATOM 2463 CA TYR A 309 -29.243 3.809 24.443 1.00133.85 C
ANISOU 2463 CA TYR A 309 18338 16548 15973 332 2996 -949 C
ATOM 2464 C TYR A 309 -27.901 3.683 23.706 1.00139.46 C
ANISOU 2464 C TYR A 309 18991 17171 16828 269 3124 -1017 C
ATOM 2465 O TYR A 309 -27.863 3.797 22.483 1.00138.83 O
ANISOU 2465 O TYR A 309 19043 16935 16770 171 3246 -1031 O
ATOM 2466 CB TYR A 309 -29.567 5.295 24.694 1.00134.95 C
ANISOU 2466 CB TYR A 309 18517 16697 16061 287 2947 -1034 C
ATOM 2467 CG TYR A 309 -31.028 5.594 24.961 1.00135.74 C
ANISOU 2467 CG TYR A 309 18721 16827 16026 327 2865 -972 C
ATOM 2468 CD1 TYR A 309 -31.960 5.600 23.926 1.00137.07 C
ANISOU 2468 CD1 TYR A 309 19056 16897 16126 292 2907 -916 C
ATOM 2469 CD2 TYR A 309 -31.464 5.955 26.232 1.00136.45 C
ANISOU 2469 CD2 TYR A 309 18741 17050 16055 393 2748 -979 C
ATOM 2470 CE1 TYR A 309 -33.302 5.898 24.162 1.00137.25 C
ANISOU 2470 CE1 TYR A 309 19148 16968 16032 338 2829 -866 C
ATOM 2471 CE2 TYR A 309 -32.803 6.255 26.481 1.00136.67 C
ANISOU 2471 CE2 TYR A 309 18853 17104 15972 431 2685 -931 C
ATOM 2472 CZ TYR A 309 -33.719 6.228 25.442 1.00143.40 C
ANISOU 2472 CZ TYR A 309 19847 17871 16767 409 2724 -875 C
ATOM 2473 OH TYR A 309 -35.038 6.529 25.683 1.00143.64 O
ANISOU 2473 OH TYR A 309 19934 17948 16696 456 2659 -833 O
ATOM 2474 N ALA A 310 -26.806 3.454 24.458 1.00137.89 N
ANISOU 2474 N ALA A 310 18591 17081 16721 325 3094 -1062 N
ATOM 2475 CA ALA A 310 -25.452 3.294 23.927 1.00139.25 C
ANISOU 2475 CA ALA A 310 18657 17206 17047 281 3209 -1137 C
ATOM 2476 C ALA A 310 -25.141 1.835 23.540 1.00144.35 C
ANISOU 2476 C ALA A 310 19288 17799 17758 353 3295 -1036 C
ATOM 2477 O ALA A 310 -24.088 1.573 22.953 1.00144.85 O
ANISOU 2477 O ALA A 310 19280 17798 17958 321 3417 -1085 O
ATOM 2478 CB ALA A 310 -24.435 3.801 24.941 1.00141.30 C
ANISOU 2478 CB ALA A 310 18682 17637 17369 309 3125 -1244 C
ATOM 2479 N PHE A 311 -26.054 0.894 23.860 1.00141.02 N
ANISOU 2479 N PHE A 311 18943 17396 17242 444 3253 -902 N
ATOM 2480 CA PHE A 311 -25.891 -0.533 23.565 1.00141.57 C
ANISOU 2480 CA PHE A 311 19035 17403 17353 514 3354 -798 C
ATOM 2481 C PHE A 311 -26.841 -1.071 22.490 1.00145.55 C
ANISOU 2481 C PHE A 311 19768 17748 17785 424 3468 -731 C
ATOM 2482 O PHE A 311 -26.454 -1.978 21.750 1.00145.47 O
ANISOU 2482 O PHE A 311 19810 17619 17843 407 3623 -692 O
ATOM 2483 CB PHE A 311 -26.011 -1.377 24.845 1.00143.78 C
ANISOU 2483 CB PHE A 311 19220 17828 17582 694 3247 -700 C
ATOM 2484 CG PHE A 311 -24.701 -1.690 25.531 1.00147.02 C
ANISOU 2484 CG PHE A 311 19401 18354 18106 824 3216 -715 C
ATOM 2485 CD1 PHE A 311 -23.902 -2.741 25.095 1.00151.17 C
ANISOU 2485 CD1 PHE A 311 19886 18804 18746 897 3352 -661 C
ATOM 2486 CD2 PHE A 311 -24.285 -0.960 26.637 1.00149.87 C
ANISOU 2486 CD2 PHE A 311 19584 18908 18451 878 3051 -781 C
ATOM 2487 CE1 PHE A 311 -22.695 -3.036 25.737 1.00153.88 C
ANISOU 2487 CE1 PHE A 311 19997 19275 19195 1042 3313 -668 C
ATOM 2488 CE2 PHE A 311 -23.079 -1.257 27.280 1.00154.49 C
ANISOU 2488 CE2 PHE A 311 19937 19635 19129 1003 3003 -797 C
ATOM 2489 CZ PHE A 311 -22.293 -2.293 26.826 1.00153.68 C
ANISOU 2489 CZ PHE A 311 19779 19466 19145 1095 3128 -737 C
ATOM 2490 N PHE A 312 -28.079 -0.541 22.415 1.00141.95 N
ANISOU 2490 N PHE A 312 19443 17301 17192 367 3395 -719 N
ATOM 2491 CA PHE A 312 -29.087 -1.008 21.458 1.00141.47 C
ANISOU 2491 CA PHE A 312 19581 17133 17038 277 3475 -663 C
ATOM 2492 C PHE A 312 -29.506 0.031 20.409 1.00146.11 C
ANISOU 2492 C PHE A 312 20306 17631 17579 139 3496 -722 C
ATOM 2493 O PHE A 312 -29.843 -0.360 19.290 1.00145.47 O
ANISOU 2493 O PHE A 312 20378 17432 17462 37 3606 -699 O
ATOM 2494 CB PHE A 312 -30.318 -1.566 22.191 1.00142.61 C
ANISOU 2494 CB PHE A 312 19767 17373 17044 339 3387 -580 C
ATOM 2495 CG PHE A 312 -30.060 -2.849 22.947 1.00144.71 C
ANISOU 2495 CG PHE A 312 19979 17675 17329 460 3420 -498 C
ATOM 2496 CD1 PHE A 312 -30.206 -4.084 22.324 1.00147.99 C
ANISOU 2496 CD1 PHE A 312 20510 17981 17738 428 3579 -432 C
ATOM 2497 CD2 PHE A 312 -29.683 -2.825 24.285 1.00147.35 C
ANISOU 2497 CD2 PHE A 312 20165 18147 17673 606 3300 -484 C
ATOM 2498 CE1 PHE A 312 -29.969 -5.271 23.024 1.00149.59 C
ANISOU 2498 CE1 PHE A 312 20690 18196 17952 554 3631 -348 C
ATOM 2499 CE2 PHE A 312 -29.445 -4.013 24.984 1.00150.87 C
ANISOU 2499 CE2 PHE A 312 20585 18619 18122 739 3333 -394 C
ATOM 2500 CZ PHE A 312 -29.590 -5.228 24.349 1.00149.17 C
ANISOU 2500 CZ PHE A 312 20495 18277 17906 719 3505 -323 C
ATOM 2501 N ASP A 313 -29.500 1.333 20.759 1.00143.71 N
ANISOU 2501 N ASP A 313 19964 17377 17262 137 3400 -794 N
ATOM 2502 CA ASP A 313 -29.879 2.408 19.836 1.00143.87 C
ANISOU 2502 CA ASP A 313 20132 17303 17228 33 3423 -841 C
ATOM 2503 C ASP A 313 -28.674 2.872 18.989 1.00149.99 C
ANISOU 2503 C ASP A 313 20925 17938 18124 -66 3564 -935 C
ATOM 2504 O ASP A 313 -27.721 3.427 19.542 1.00150.18 O
ANISOU 2504 O ASP A 313 20811 18002 18248 -52 3557 -1024 O
ATOM 2505 CB ASP A 313 -30.557 3.578 20.588 1.00145.33 C
ANISOU 2505 CB ASP A 313 20303 17585 17332 81 3281 -868 C
ATOM 2506 CG ASP A 313 -30.964 4.783 19.748 1.00154.83 C
ANISOU 2506 CG ASP A 313 21668 18690 18470 9 3303 -906 C
ATOM 2507 OD1 ASP A 313 -31.300 4.597 18.556 1.00155.19 O
ANISOU 2507 OD1 ASP A 313 21872 18625 18466 -67 3380 -874 O
ATOM 2508 OD2 ASP A 313 -30.998 5.903 20.299 1.00160.70 O
ANISOU 2508 OD2 ASP A 313 22392 19467 19199 34 3244 -962 O
ATOM 2509 N PRO A 314 -28.694 2.651 17.650 1.00147.86 N
ANISOU 2509 N PRO A 314 20826 17510 17844 -179 3699 -928 N
ATOM 2510 CA PRO A 314 -27.553 3.070 16.816 1.00149.02 C
ANISOU 2510 CA PRO A 314 21007 17507 18107 -285 3856 -1025 C
ATOM 2511 C PRO A 314 -27.476 4.577 16.566 1.00154.61 C
ANISOU 2511 C PRO A 314 21802 18156 18787 -346 3856 -1116 C
ATOM 2512 O PRO A 314 -26.398 5.074 16.237 1.00155.01 O
ANISOU 2512 O PRO A 314 21831 18116 18950 -426 3975 -1227 O
ATOM 2513 CB PRO A 314 -27.750 2.286 15.509 1.00150.71 C
ANISOU 2513 CB PRO A 314 21402 17570 18289 -390 3999 -977 C
ATOM 2514 CG PRO A 314 -28.912 1.353 15.754 1.00154.21 C
ANISOU 2514 CG PRO A 314 21877 18105 18611 -337 3918 -861 C
ATOM 2515 CD PRO A 314 -29.724 1.991 16.828 1.00149.04 C
ANISOU 2515 CD PRO A 314 21144 17613 17870 -230 3724 -842 C
ATOM 2516 N ARG A 315 -28.609 5.299 16.712 1.00151.80 N
ANISOU 2516 N ARG A 315 21547 17845 18285 -308 3740 -1074 N
ATOM 2517 CA ARG A 315 -28.690 6.751 16.520 1.00152.57 C
ANISOU 2517 CA ARG A 315 21759 17875 18334 -342 3746 -1142 C
ATOM 2518 C ARG A 315 -27.943 7.498 17.635 1.00158.43 C
ANISOU 2518 C ARG A 315 22328 18705 19164 -314 3710 -1249 C
ATOM 2519 O ARG A 315 -27.282 8.500 17.355 1.00158.73 O
ANISOU 2519 O ARG A 315 22424 18644 19244 -398 3810 -1362 O
ATOM 2520 CB ARG A 315 -30.156 7.208 16.416 1.00152.28 C
ANISOU 2520 CB ARG A 315 21862 17878 18120 -278 3629 -1051 C
ATOM 2521 CG ARG A 315 -30.329 8.628 15.883 1.00163.38 C
ANISOU 2521 CG ARG A 315 23458 19164 19456 -306 3673 -1093 C
ATOM 2522 CD ARG A 315 -31.756 8.903 15.458 1.00173.40 C
ANISOU 2522 CD ARG A 315 24880 20457 20547 -236 3575 -984 C
ATOM 2523 NE ARG A 315 -32.060 10.335 15.469 1.00182.78 N
ANISOU 2523 NE ARG A 315 26200 21581 21666 -193 3576 -1008 N
ATOM 2524 CZ ARG A 315 -32.845 10.946 14.587 1.00197.50 C
ANISOU 2524 CZ ARG A 315 28285 23366 23391 -164 3575 -943 C
ATOM 2525 NH1 ARG A 315 -33.408 10.260 13.600 1.00184.97 N
ANISOU 2525 NH1 ARG A 315 26800 21770 21708 -192 3560 -859 N
ATOM 2526 NH2 ARG A 315 -33.066 12.250 14.680 1.00184.85 N
ANISOU 2526 NH2 ARG A 315 26808 21693 21735 -106 3594 -961 N
ATOM 2527 N PHE A 316 -28.038 6.999 18.886 1.00155.99 N
ANISOU 2527 N PHE A 316 21817 18580 18873 -209 3578 -1220 N
ATOM 2528 CA PHE A 316 -27.360 7.575 20.052 1.00157.06 C
ANISOU 2528 CA PHE A 316 21766 18836 19073 -183 3521 -1319 C
ATOM 2529 C PHE A 316 -25.848 7.334 19.985 1.00163.73 C
ANISOU 2529 C PHE A 316 22456 19670 20085 -250 3628 -1429 C
ATOM 2530 O PHE A 316 -25.077 8.189 20.423 1.00164.19 O
ANISOU 2530 O PHE A 316 22422 19761 20202 -306 3652 -1565 O
ATOM 2531 CB PHE A 316 -27.954 7.025 21.362 1.00158.28 C
ANISOU 2531 CB PHE A 316 21773 19189 19179 -49 3347 -1244 C
ATOM 2532 CG PHE A 316 -27.417 7.667 22.622 1.00160.48 C
ANISOU 2532 CG PHE A 316 21878 19611 19488 -25 3266 -1338 C
ATOM 2533 CD1 PHE A 316 -27.842 8.932 23.014 1.00163.66 C
ANISOU 2533 CD1 PHE A 316 22350 20015 19819 -47 3238 -1398 C
ATOM 2534 CD2 PHE A 316 -26.502 6.999 23.427 1.00163.31 C
ANISOU 2534 CD2 PHE A 316 22008 20108 19936 23 3221 -1365 C
ATOM 2535 CE1 PHE A 316 -27.342 9.526 24.176 1.00165.30 C
ANISOU 2535 CE1 PHE A 316 22407 20357 20043 -49 3175 -1498 C
ATOM 2536 CE2 PHE A 316 -26.008 7.591 24.593 1.00166.92 C
ANISOU 2536 CE2 PHE A 316 22301 20720 20402 33 3135 -1458 C
ATOM 2537 CZ PHE A 316 -26.432 8.850 24.960 1.00165.05 C
ANISOU 2537 CZ PHE A 316 22140 20480 20090 -16 3115 -1530 C
ATOM 2538 N ARG A 317 -25.432 6.175 19.431 1.00161.78 N
ANISOU 2538 N ARG A 317 22178 19378 19915 -248 3703 -1378 N
ATOM 2539 CA ARG A 317 -24.026 5.800 19.253 1.00163.50 C
ANISOU 2539 CA ARG A 317 22241 19578 20303 -295 3819 -1470 C
ATOM 2540 C ARG A 317 -23.361 6.677 18.188 1.00170.04 C
ANISOU 2540 C ARG A 317 23198 20220 21188 -463 4004 -1600 C
ATOM 2541 O ARG A 317 -22.181 7.007 18.317 1.00170.83 O
ANISOU 2541 O ARG A 317 23149 20338 21419 -530 4085 -1742 O
ATOM 2542 CB ARG A 317 -23.901 4.317 18.873 1.00163.56 C
ANISOU 2542 CB ARG A 317 22222 19556 20366 -240 3874 -1365 C
ATOM 2543 CG ARG A 317 -23.943 3.374 20.067 1.00173.47 C
ANISOU 2543 CG ARG A 317 23282 21001 21629 -72 3738 -1278 C
ATOM 2544 CD ARG A 317 -23.703 1.931 19.662 1.00182.74 C
ANISOU 2544 CD ARG A 317 24447 22118 22868 -18 3833 -1182 C
ATOM 2545 NE ARG A 317 -24.906 1.307 19.109 1.00189.30 N
ANISOU 2545 NE ARG A 317 25489 22866 23571 -28 3845 -1060 N
ATOM 2546 CZ ARG A 317 -25.031 0.009 18.853 1.00202.85 C
ANISOU 2546 CZ ARG A 317 27242 24534 25297 15 3923 -960 C
ATOM 2547 NH1 ARG A 317 -24.027 -0.824 19.104 1.00191.01 N
ANISOU 2547 NH1 ARG A 317 25590 23050 23935 98 3995 -950 N
ATOM 2548 NH2 ARG A 317 -26.160 -0.469 18.349 1.00188.46 N
ANISOU 2548 NH2 ARG A 317 25608 22653 23345 -24 3935 -872 N
ATOM 2549 N GLN A 318 -24.128 7.053 17.145 1.00167.61 N
ANISOU 2549 N GLN A 318 23169 19741 20774 -531 4071 -1556 N
ATOM 2550 CA GLN A 318 -23.687 7.896 16.033 1.00168.94 C
ANISOU 2550 CA GLN A 318 23532 19700 20958 -687 4255 -1657 C
ATOM 2551 C GLN A 318 -23.507 9.355 16.475 1.00175.33 C
ANISOU 2551 C GLN A 318 24365 20511 21743 -740 4262 -1785 C
ATOM 2552 O GLN A 318 -22.575 10.018 16.016 1.00176.06 O
ANISOU 2552 O GLN A 318 24489 20488 21917 -877 4429 -1935 O
ATOM 2553 CB GLN A 318 -24.682 7.794 14.866 1.00169.60 C
ANISOU 2553 CB GLN A 318 23912 19627 20901 -716 4294 -1546 C
ATOM 2554 CG GLN A 318 -24.049 8.014 13.493 1.00186.29 C
ANISOU 2554 CG GLN A 318 26224 21505 23055 -877 4518 -1618 C
ATOM 2555 CD GLN A 318 -24.937 7.616 12.331 1.00205.52 C
ANISOU 2555 CD GLN A 318 28924 23813 25351 -908 4548 -1499 C
ATOM 2556 OE1 GLN A 318 -26.148 7.388 12.464 1.00200.29 O
ANISOU 2556 OE1 GLN A 318 28322 23236 24543 -816 4399 -1370 O
ATOM 2557 NE2 GLN A 318 -24.348 7.540 11.148 1.00198.37 N
ANISOU 2557 NE2 GLN A 318 28182 22707 24484 -1049 4747 -1550 N
ATOM 2558 N ALA A 319 -24.392 9.844 17.369 1.00172.79 N
ANISOU 2558 N ALA A 319 24034 20310 21309 -641 4099 -1733 N
ATOM 2559 CA ALA A 319 -24.352 11.203 17.915 1.00173.99 C
ANISOU 2559 CA ALA A 319 24218 20468 21422 -681 4105 -1843 C
ATOM 2560 C ALA A 319 -23.259 11.344 18.984 1.00180.75 C
ANISOU 2560 C ALA A 319 24787 21491 22399 -714 4084 -1991 C
ATOM 2561 O ALA A 319 -22.778 12.455 19.222 1.00181.32 O
ANISOU 2561 O ALA A 319 24873 21538 22481 -817 4165 -2144 O
ATOM 2562 CB ALA A 319 -25.708 11.577 18.490 1.00173.76 C
ANISOU 2562 CB ALA A 319 24274 20510 21238 -557 3947 -1729 C
ATOM 2563 N CYS A 320 -22.866 10.216 19.616 1.00178.75 N
ANISOU 2563 N CYS A 320 24278 21411 22228 -627 3981 -1948 N
ATOM 2564 CA CYS A 320 -21.807 10.155 20.626 1.00180.50 C
ANISOU 2564 CA CYS A 320 24194 21829 22558 -632 3932 -2069 C
ATOM 2565 C CYS A 320 -20.450 10.405 19.960 1.00187.73 C
ANISOU 2565 C CYS A 320 25043 22660 23627 -790 4130 -2246 C
ATOM 2566 O CYS A 320 -19.653 11.186 20.481 1.00188.65 O
ANISOU 2566 O CYS A 320 25024 22860 23795 -890 4166 -2425 O
ATOM 2567 CB CYS A 320 -21.834 8.818 21.363 1.00180.41 C
ANISOU 2567 CB CYS A 320 23968 22002 22576 -467 3778 -1945 C
ATOM 2568 SG CYS A 320 -20.713 8.728 22.784 1.00185.86 S
ANISOU 2568 SG CYS A 320 24277 22986 23355 -426 3658 -2061 S
ATOM 2569 N THR A 321 -20.208 9.767 18.791 1.00185.67 N
ANISOU 2569 N THR A 321 24883 22228 23433 -829 4271 -2208 N
ATOM 2570 CA THR A 321 -18.983 9.922 17.992 1.00187.66 C
ANISOU 2570 CA THR A 321 25103 22364 23836 -986 4489 -2369 C
ATOM 2571 C THR A 321 -18.901 11.329 17.394 1.00193.90 C
ANISOU 2571 C THR A 321 26127 22968 24580 -1166 4659 -2514 C
ATOM 2572 O THR A 321 -17.804 11.872 17.253 1.00195.07 O
ANISOU 2572 O THR A 321 26186 23092 24841 -1321 4815 -2716 O
ATOM 2573 CB THR A 321 -18.885 8.844 16.901 1.00195.58 C
ANISOU 2573 CB THR A 321 26190 23215 24905 -979 4602 -2274 C
ATOM 2574 OG1 THR A 321 -20.102 8.807 16.152 1.00193.91 O
ANISOU 2574 OG1 THR A 321 26292 22845 24539 -958 4595 -2124 O
ATOM 2575 CG2 THR A 321 -18.565 7.464 17.463 1.00194.17 C
ANISOU 2575 CG2 THR A 321 25752 23203 24820 -822 4501 -2177 C
ATOM 2576 N SER A 322 -20.070 11.914 17.054 1.00190.78 N
ANISOU 2576 N SER A 322 26030 22443 24015 -1141 4636 -2412 N
ATOM 2577 CA SER A 322 -20.210 13.264 16.503 1.00191.88 C
ANISOU 2577 CA SER A 322 26449 22384 24073 -1271 4791 -2508 C
ATOM 2578 C SER A 322 -19.914 14.318 17.577 1.00198.35 C
ANISOU 2578 C SER A 322 27155 23328 24881 -1326 4767 -2661 C
ATOM 2579 O SER A 322 -19.470 15.419 17.244 1.00199.12 O
ANISOU 2579 O SER A 322 27399 23282 24975 -1486 4956 -2823 O
ATOM 2580 CB SER A 322 -21.612 13.464 15.938 1.00194.15 C
ANISOU 2580 CB SER A 322 27053 22539 24176 -1179 4738 -2326 C
ATOM 2581 OG SER A 322 -21.708 14.682 15.217 1.00203.71 O
ANISOU 2581 OG SER A 322 28573 23522 25306 -1286 4913 -2398 O
ATOM 2582 N MET A 323 -20.160 13.972 18.862 1.00195.82 N
ANISOU 2582 N MET A 323 26591 23266 24545 -1202 4548 -2614 N
ATOM 2583 CA MET A 323 -19.896 14.826 20.022 1.00197.23 C
ANISOU 2583 CA MET A 323 26630 23603 24704 -1251 4497 -2753 C
ATOM 2584 C MET A 323 -18.387 14.970 20.243 1.00204.76 C
ANISOU 2584 C MET A 323 27326 24660 25815 -1413 4605 -2990 C
ATOM 2585 O MET A 323 -17.936 16.034 20.670 1.00205.64 O
ANISOU 2585 O MET A 323 27426 24793 25915 -1560 4695 -3181 O
ATOM 2586 CB MET A 323 -20.580 14.270 21.280 1.00198.55 C
ANISOU 2586 CB MET A 323 26617 24017 24805 -1072 4230 -2625 C
ATOM 2587 N LEU A 324 -17.611 13.903 19.944 1.00203.11 N
ANISOU 2587 N LEU A 324 26907 24515 25749 -1388 4609 -2984 N
ATOM 2588 CA LEU A 324 -16.149 13.919 20.045 1.00205.72 C
ANISOU 2588 CA LEU A 324 26962 24954 26247 -1525 4713 -3204 C
ATOM 2589 C LEU A 324 -15.532 14.639 18.845 1.00212.77 C
ANISOU 2589 C LEU A 324 28061 25579 27202 -1746 5018 -3370 C
ATOM 2590 O LEU A 324 -14.437 15.190 18.963 1.00214.27 O
ANISOU 2590 O LEU A 324 28094 25825 27493 -1926 5154 -3613 O
ATOM 2591 CB LEU A 324 -15.561 12.502 20.203 1.00205.88 C
ANISOU 2591 CB LEU A 324 26680 25142 26404 -1389 4610 -3126 C
ATOM 2592 CG LEU A 324 -15.416 11.916 21.628 1.00210.83 C
ANISOU 2592 CG LEU A 324 26962 26114 27030 -1232 4351 -3084 C
ATOM 2593 CD1 LEU A 324 -14.951 12.956 22.655 1.00212.50 C
ANISOU 2593 CD1 LEU A 324 27012 26522 27205 -1355 4309 -3289 C
ATOM 2594 CD2 LEU A 324 -16.675 11.203 22.078 1.00211.16 C
ANISOU 2594 CD2 LEU A 324 27098 26192 26940 -1013 4144 -2824 C
ATOM 2595 N LEU A 325 -16.249 14.646 17.697 1.00209.98 N
ANISOU 2595 N LEU A 325 28064 24942 26778 -1738 5127 -3243 N
ATOM 2596 CA LEU A 325 -15.853 15.345 16.471 1.00211.81 C
ANISOU 2596 CA LEU A 325 28572 24877 27029 -1932 5420 -3366 C
ATOM 2597 C LEU A 325 -16.042 16.850 16.703 1.00219.48 C
ANISOU 2597 C LEU A 325 29752 25753 27889 -2063 5532 -3502 C
ATOM 2598 O LEU A 325 -15.252 17.653 16.205 1.00220.76 O
ANISOU 2598 O LEU A 325 30009 25768 28102 -2280 5786 -3716 O
ATOM 2599 CB LEU A 325 -16.700 14.856 15.278 1.00210.45 C
ANISOU 2599 CB LEU A 325 28725 24462 26776 -1857 5460 -3162 C
ATOM 2600 CG LEU A 325 -16.253 15.268 13.865 1.00216.16 C
ANISOU 2600 CG LEU A 325 29739 24868 27523 -2039 5758 -3256 C
ATOM 2601 CD1 LEU A 325 -14.952 14.577 13.459 1.00217.46 C
ANISOU 2601 CD1 LEU A 325 29675 25047 27904 -2148 5905 -3394 C
ATOM 2602 CD2 LEU A 325 -17.324 14.936 12.846 1.00216.81 C
ANISOU 2602 CD2 LEU A 325 30166 24745 27466 -1949 5748 -3036 C
ATOM 2603 N MET A 326 -17.078 17.214 17.493 1.00217.01 N
ANISOU 2603 N MET A 326 29507 25521 27427 -1934 5354 -3383 N
ATOM 2604 CA MET A 326 -17.403 18.579 17.915 1.00218.70 C
ANISOU 2604 CA MET A 326 29905 25667 27522 -2018 5434 -3482 C
ATOM 2605 C MET A 326 -16.260 19.100 18.813 1.00229.81 C
ANISOU 2605 C MET A 326 31023 27271 29024 -2199 5489 -3758 C
ATOM 2606 O MET A 326 -15.839 20.248 18.666 1.00231.07 O
ANISOU 2606 O MET A 326 31318 27322 29154 -2363 5656 -3925 O
ATOM 2607 CB MET A 326 -18.781 18.594 18.622 1.00218.99 C
ANISOU 2607 CB MET A 326 30022 25783 27402 -1807 5204 -3271 C
ATOM 2608 CG MET A 326 -19.041 19.796 19.510 1.00223.00 C
ANISOU 2608 CG MET A 326 30596 26323 27812 -1864 5227 -3375 C
ATOM 2609 SD MET A 326 -18.862 19.355 21.255 1.00226.85 S
ANISOU 2609 SD MET A 326 30653 27216 28324 -1798 4955 -3408 S
ATOM 2610 CE MET A 326 -18.884 20.959 21.992 1.00224.93 C
ANISOU 2610 CE MET A 326 30547 26936 27980 -1958 5094 -3601 C
ATOM 2611 N GLY A 327 -15.748 18.223 19.682 1.00230.44 N
ANISOU 2611 N GLY A 327 30694 27664 29201 -2128 5291 -3766 N
ATOM 2612 CA GLY A 327 -14.626 18.503 20.574 1.00233.46 C
ANISOU 2612 CA GLY A 327 30732 28299 29674 -2276 5293 -4015 C
ATOM 2613 C GLY A 327 -13.292 18.516 19.851 1.00238.53 C
ANISOU 2613 C GLY A 327 31172 29093 30365 -2087 4942 -3833 C
ATOM 2614 O GLY A 327 -12.318 19.079 20.358 1.00239.40 O
ANISOU 2614 O GLY A 327 31081 29379 30503 -2163 4885 -3961 O
ATOM 2615 N GLN A 328 -13.243 17.887 18.656 1.00237.11 N
ANISOU 2615 N GLN A 328 31127 28695 30271 -2116 5120 -3805 N
ATOM 2616 CA GLN A 328 -12.064 17.823 17.790 1.00237.99 C
ANISOU 2616 CA GLN A 328 31141 28800 30483 -2136 5109 -3819 C
ATOM 2617 C GLN A 328 -11.948 19.098 16.961 1.00240.94 C
ANISOU 2617 C GLN A 328 31744 29095 30708 -2005 4852 -3636 C
ATOM 2618 O GLN A 328 -10.835 19.539 16.672 1.00240.87 O
ANISOU 2618 O GLN A 328 31626 29150 30743 -2035 4792 -3680 O
ATOM 2619 CB GLN A 328 -12.124 16.593 16.876 1.00238.41 C
ANISOU 2619 CB GLN A 328 31208 28755 30623 -2041 5128 -3677 C
ATOM 2620 CG GLN A 328 -10.853 15.754 16.912 1.00248.83 C
ANISOU 2620 CG GLN A 328 32087 30551 31906 -1549 4336 -3206 C
ATOM 2621 CD GLN A 328 -10.877 14.668 17.965 1.00260.62 C
ANISOU 2621 CD GLN A 328 33259 32551 33215 -950 3483 -2606 C
ATOM 2622 OE1 GLN A 328 -11.329 14.852 19.104 1.00258.64 O
ANISOU 2622 OE1 GLN A 328 32949 32352 32968 -1044 3611 -2760 O
ATOM 2623 NE2 GLN A 328 -10.315 13.521 17.628 1.00256.49 N
ANISOU 2623 NE2 GLN A 328 32594 31960 32902 -1100 3831 -2792 N
ATOM 2624 N SER A 329 -13.101 19.682 16.576 1.00238.34 N
ANISOU 2624 N SER A 329 31800 28484 30275 -2082 5068 -3658 N
ATOM 2625 CA SER A 329 -13.177 20.940 15.832 1.00237.79 C
ANISOU 2625 CA SER A 329 32012 28233 30107 -2097 5081 -3646 C
ATOM 2626 C SER A 329 -12.971 22.100 16.811 1.00241.75 C
ANISOU 2626 C SER A 329 32377 28978 30501 -1952 4731 -3578 C
ATOM 2627 O SER A 329 -12.521 23.170 16.403 1.00241.18 O
ANISOU 2627 O SER A 329 32415 28831 30393 -1987 4731 -3623 O
ATOM 2628 CB SER A 329 -14.525 21.068 15.130 1.00239.07 C
ANISOU 2628 CB SER A 329 32500 28202 30135 -1954 5025 -3442 C
ATOM 2629 OG SER A 329 -14.542 22.178 14.248 1.00242.92 O
ANISOU 2629 OG SER A 329 33093 28689 30518 -1745 4676 -3249 O
ATOM 2630 N ARG A 330 -13.287 21.869 18.107 1.00240.82 N
ANISOU 2630 N ARG A 330 32123 28998 30380 -2020 4796 -3682 N
ATOM 2631 CA ARG A 330 -13.130 22.820 19.211 1.00241.56 C
ANISOU 2631 CA ARG A 330 32130 29253 30400 -2027 4684 -3744 C
ATOM 2632 C ARG A 330 -11.641 23.031 19.517 1.00245.70 C
ANISOU 2632 C ARG A 330 32325 30071 30959 -1889 4310 -3641 C
ATOM 2633 O ARG A 330 -11.224 24.166 19.751 1.00245.46 O
ANISOU 2633 O ARG A 330 32337 30051 30874 -1925 4275 -3695 O
ATOM 2634 CB ARG A 330 -13.879 22.321 20.459 1.00242.32 C
ANISOU 2634 CB ARG A 330 32107 29506 30458 -1996 4636 -3740 C
ATOM 2635 CG ARG A 330 -14.234 23.429 21.445 1.00249.20 C
ANISOU 2635 CG ARG A 330 32921 30614 31149 -1649 4078 -3445 C
ATOM 2636 CD ARG A 330 -15.637 23.285 22.018 1.00254.49 C
ANISOU 2636 CD ARG A 330 33618 31387 31690 -1325 3721 -3143 C
ATOM 2637 NE ARG A 330 -16.686 23.523 21.020 1.00257.59 N
ANISOU 2637 NE ARG A 330 34196 31666 32010 -1083 3517 -2901 N
ATOM 2638 CZ ARG A 330 -17.183 24.719 20.714 1.00264.79 C
ANISOU 2638 CZ ARG A 330 35079 32713 32815 -673 2942 -2578 C
ATOM 2639 NH1 ARG A 330 -16.724 25.811 21.314 1.00257.94 N
ANISOU 2639 NH1 ARG A 330 34400 31666 31939 -1034 3430 -2935 N
ATOM 2640 NH2 ARG A 330 -18.136 24.833 19.799 1.00256.21 N
ANISOU 2640 NH2 ARG A 330 34454 31168 31726 -1023 3628 -2846 N
ATOM 2641 N LEU A 331 -10.849 21.935 19.507 1.00244.59 N
ANISOU 2641 N LEU A 331 31932 30040 30960 -1965 4387 -3717 N
ATOM 2642 CA LEU A 331 -9.400 21.946 19.732 1.00245.49 C
ANISOU 2642 CA LEU A 331 31767 30360 31147 -1964 4250 -3728 C
ATOM 2643 C LEU A 331 -8.670 22.489 18.500 1.00247.59 C
ANISOU 2643 C LEU A 331 32147 30522 31404 -1865 4110 -3588 C
ATOM 2644 O LEU A 331 -7.577 23.042 18.633 1.00247.73 O
ANISOU 2644 O LEU A 331 32045 30640 31440 -1892 4031 -3612 O
ATOM 2645 CB LEU A 331 -8.893 20.521 20.054 1.00246.48 C
ANISOU 2645 CB LEU A 331 31570 30690 31392 -1900 4182 -3681 C
ATOM 2646 CG LEU A 331 -8.560 20.143 21.519 1.00251.20 C
ANISOU 2646 CG LEU A 331 31860 31647 31938 -1682 3799 -3476 C
ATOM 2647 CD1 LEU A 331 -7.279 20.806 22.015 1.00252.23 C
ANISOU 2647 CD1 LEU A 331 31819 31948 32068 -1681 3641 -3448 C
ATOM 2648 CD2 LEU A 331 -9.742 20.344 22.464 1.00252.96 C
ANISOU 2648 CD2 LEU A 331 32175 31908 32031 -1586 3677 -3396 C
ATOM 2649 N GLU A 332 -9.273 22.322 17.303 1.00244.01 N
ANISOU 2649 N GLU A 332 31963 29767 30983 -1980 4396 -3675 N
ATOM 2650 CA GLU A 332 -8.712 22.788 16.035 1.00243.27 C
ANISOU 2650 CA GLU A 332 32025 29494 30913 -2025 4462 -3688 C
ATOM 2651 C GLU A 332 -8.969 24.296 15.823 1.00245.52 C
ANISOU 2651 C GLU A 332 32523 29709 31054 -1909 4271 -3590 C
ATOM 2652 O GLU A 332 -8.146 24.961 15.194 1.00244.99 O
ANISOU 2652 O GLU A 332 32496 29588 31003 -1946 4266 -3626 O
ATOM 2653 CB GLU A 332 -9.185 21.900 14.857 1.00243.44 C
ANISOU 2653 CB GLU A 332 32183 29340 30972 -1975 4519 -3586 C
ATOM 2654 CG GLU A 332 -10.214 22.490 13.900 1.00247.95 C
ANISOU 2654 CG GLU A 332 33014 29810 31386 -1694 4174 -3284 C
ATOM 2655 CD GLU A 332 -9.672 23.132 12.635 1.00257.80 C
ANISOU 2655 CD GLU A 332 34164 31256 32530 -1208 3358 -2820 C
ATOM 2656 OE1 GLU A 332 -10.477 23.746 11.899 1.00253.78 O
ANISOU 2656 OE1 GLU A 332 33977 30451 31996 -1358 3656 -2956 O
ATOM 2657 OE2 GLU A 332 -8.453 23.016 12.368 1.00254.70 O
ANISOU 2657 OE2 GLU A 332 33715 30818 32240 -1397 3582 -2983 O
ATOM 2658 N VAL A 333 -10.087 24.830 16.368 1.00243.12 N
ANISOU 2658 N VAL A 333 32417 29290 30666 -1988 4450 -3687 N
ATOM 2659 CA VAL A 333 -10.450 26.251 16.279 1.00242.67 C
ANISOU 2659 CA VAL A 333 32596 29106 30502 -1984 4465 -3713 C
ATOM 2660 C VAL A 333 -9.709 27.089 17.330 1.00246.62 C
ANISOU 2660 C VAL A 333 32876 29880 30948 -1844 4120 -3627 C
ATOM 2661 O VAL A 333 -9.505 28.286 17.124 1.00246.00 O
ANISOU 2661 O VAL A 333 32936 29715 30819 -1865 4136 -3678 O
ATOM 2662 CB VAL A 333 -11.977 26.467 16.358 1.00244.69 C
ANISOU 2662 CB VAL A 333 33042 29291 30638 -1809 4357 -3552 C
ATOM 2663 N LEU A 334 -9.321 26.458 18.456 1.00245.98 N
ANISOU 2663 N LEU A 334 32545 29998 30916 -1936 4151 -3714 N
ATOM 2664 CA LEU A 334 -8.585 27.089 19.554 1.00246.94 C
ANISOU 2664 CA LEU A 334 32490 30324 31010 -1940 4008 -3735 C
ATOM 2665 C LEU A 334 -7.106 27.311 19.178 1.00250.20 C
ANISOU 2665 C LEU A 334 32736 30863 31464 -1819 3737 -3588 C
ATOM 2666 O LEU A 334 -6.490 28.263 19.665 1.00250.21 O
ANISOU 2666 O LEU A 334 32714 30922 31431 -1848 3678 -3624 O
ATOM 2667 CB LEU A 334 -8.771 26.264 20.857 1.00247.98 C
ANISOU 2667 CB LEU A 334 32380 30690 31149 -1915 3915 -3710 C
ATOM 2668 CG LEU A 334 -7.558 25.901 21.730 1.00252.60 C
ANISOU 2668 CG LEU A 334 32624 31594 31758 -1735 3532 -3492 C
ATOM 2669 CD1 LEU A 334 -7.335 26.930 22.823 1.00254.97 C
ANISOU 2669 CD1 LEU A 334 32901 32015 31962 -1640 3300 -3394 C
ATOM 2670 CD2 LEU A 334 -7.731 24.534 22.346 1.00253.45 C
ANISOU 2670 CD2 LEU A 334 32509 31871 31920 -1686 3481 -3434 C
ATOM 2671 N PHE A 335 -6.558 26.456 18.285 1.00248.05 N
ANISOU 2671 N PHE A 335 32409 30527 31311 -1934 3913 -3671 N
ATOM 2672 CA PHE A 335 -5.168 26.529 17.824 1.00248.32 C
ANISOU 2672 CA PHE A 335 32310 30623 31418 -1957 3854 -3660 C
ATOM 2673 C PHE A 335 -5.007 27.044 16.374 1.00249.38 C
ANISOU 2673 C PHE A 335 32651 30566 31534 -1874 3796 -3576 C
ATOM 2674 O PHE A 335 -3.878 27.117 15.878 1.00249.24 O
ANISOU 2674 O PHE A 335 32551 30572 31579 -1913 3782 -3585 O
ATOM 2675 CB PHE A 335 -4.452 25.178 18.022 1.00250.55 C
ANISOU 2675 CB PHE A 335 32286 31120 31792 -1855 3701 -3512 C
ATOM 2676 CG PHE A 335 -4.130 24.839 19.461 1.00253.08 C
ANISOU 2676 CG PHE A 335 32339 31721 32098 -1758 3486 -3389 C
ATOM 2677 CD1 PHE A 335 -3.299 25.659 20.218 1.00256.14 C
ANISOU 2677 CD1 PHE A 335 32641 32252 32430 -1655 3226 -3237 C
ATOM 2678 CD2 PHE A 335 -4.619 23.676 20.044 1.00255.29 C
ANISOU 2678 CD2 PHE A 335 32472 32139 32388 -1625 3371 -3251 C
ATOM 2679 CE1 PHE A 335 -2.997 25.342 21.546 1.00257.91 C
ANISOU 2679 CE1 PHE A 335 32646 32701 32648 -1582 3049 -3115 C
ATOM 2680 CE2 PHE A 335 -4.308 23.356 21.370 1.00258.48 C
ANISOU 2680 CE2 PHE A 335 32655 32792 32765 -1482 3117 -3063 C
ATOM 2681 CZ PHE A 335 -3.500 24.191 22.112 1.00257.77 C
ANISOU 2681 CZ PHE A 335 32477 32797 32666 -1560 3071 -3106 C
ATOM 2682 N GLN A 336 -6.122 27.425 15.711 1.00245.76 N
ANISOU 2682 N GLN A 336 32513 29821 31043 -2002 4091 -3730 N
ATOM 2683 CA GLN A 336 -6.117 27.969 14.348 1.00260.06 C
ANISOU 2683 CA GLN A 336 34289 31824 32697 -1195 2987 -2966 C
ATOM 2684 C GLN A 336 -7.273 28.943 14.122 1.00274.36 C
ANISOU 2684 C GLN A 336 36001 33927 34315 -392 1892 -2308 C
ATOM 2685 O GLN A 336 -8.424 28.624 14.412 1.00252.77 O
ANISOU 2685 O GLN A 336 33816 30523 31703 -1466 3567 -3289 O
ATOM 2686 CB GLN A 336 -6.125 26.852 13.291 1.00260.58 C
ANISOU 2686 CB GLN A 336 34345 31836 32826 -1174 2989 -2896 C
TER 2687 GLN A 336
HETATM 2688 ZN ZN A1101 -39.232 -15.737 -8.352 1.00 99.86 ZN2+
ANISOU 2688 ZN ZN A1101 15226 12541 10174 317 1749 -1171 ZN2+
HETATM 2689 C10 8EH A1102 -40.140 8.169 50.249 1.00146.25 C
ANISOU 2689 C10 8EH A1102 20337 19860 15371 645 1724 -1255 C
HETATM 2690 C12 8EH A1102 -42.286 6.678 50.025 1.00144.87 C
ANISOU 2690 C12 8EH A1102 20321 19521 15202 744 1887 -1132 C
HETATM 2691 C17 8EH A1102 -43.366 4.465 52.644 1.00146.40 C
ANISOU 2691 C17 8EH A1102 20881 19729 15015 800 1932 -1028 C
HETATM 2692 C18 8EH A1102 -42.409 4.749 53.831 1.00148.02 C
ANISOU 2692 C18 8EH A1102 21124 20061 15057 782 1802 -1047 C
HETATM 2693 C19 8EH A1102 -44.455 3.316 52.972 1.00146.33 C
ANISOU 2693 C19 8EH A1102 21030 19631 14936 825 2059 -978 C
HETATM 2694 C21 8EH A1102 -43.847 1.851 53.109 1.00146.91 C
ANISOU 2694 C21 8EH A1102 21192 19719 14908 943 2018 -844 C
HETATM 2695 C23 8EH A1102 -42.797 0.208 54.543 1.00149.46 C
ANISOU 2695 C23 8EH A1102 21745 20112 14931 1112 1914 -674 C
HETATM 2696 C24 8EH A1102 -42.736 -0.727 53.451 1.00148.55 C
ANISOU 2696 C24 8EH A1102 21597 19927 14920 1192 1975 -587 C
HETATM 2697 C25 8EH A1102 -42.143 -2.103 53.639 1.00149.63 C
ANISOU 2697 C25 8EH A1102 21857 20047 14950 1346 1969 -439 C
HETATM 2698 C26 8EH A1102 -43.267 -0.281 52.191 1.00146.80 C
ANISOU 2698 C26 8EH A1102 21234 19646 14896 1124 2048 -644 C
HETATM 2699 C30 8EH A1102 -40.682 6.486 48.305 1.00144.31 C
ANISOU 2699 C30 8EH A1102 20050 19483 15298 810 1788 -1073 C
HETATM 2700 C31 8EH A1102 -39.478 6.549 47.293 1.00144.36 C
ANISOU 2700 C31 8EH A1102 19921 19519 15411 832 1726 -1060 C
HETATM 2701 C32 8EH A1102 -38.169 7.011 47.729 1.00145.72 C
ANISOU 2701 C32 8EH A1102 20002 19816 15548 799 1616 -1116 C
HETATM 2702 C01 8EH A1102 -39.090 5.613 52.124 1.00148.54 C
ANISOU 2702 C01 8EH A1102 20742 20371 15326 838 1497 -1054 C
HETATM 2703 C03 8EH A1102 -39.655 7.982 51.626 1.00147.83 C
ANISOU 2703 C03 8EH A1102 20592 20188 15389 622 1629 -1271 C
HETATM 2704 C04 8EH A1102 -38.874 8.976 52.308 1.00149.19 C
ANISOU 2704 C04 8EH A1102 20725 20469 15491 507 1568 -1387 C
HETATM 2705 C05 8EH A1102 -38.552 10.196 51.626 1.00148.93 C
ANISOU 2705 C05 8EH A1102 20611 20399 15575 409 1623 -1495 C
HETATM 2706 C06 8EH A1102 -39.008 10.444 50.285 1.00147.37 C
ANISOU 2706 C06 8EH A1102 20379 20058 15558 443 1725 -1475 C
HETATM 2707 C07 8EH A1102 -39.803 9.454 49.612 1.00146.07 C
ANISOU 2707 C07 8EH A1102 20240 19804 15455 560 1764 -1355 C
HETATM 2708 C09 8EH A1102 -41.550 10.233 48.009 1.00144.02 C
ANISOU 2708 C09 8EH A1102 20011 19301 15411 585 1978 -1353 C
HETATM 2709 C33 8EH A1102 -37.090 7.043 46.759 1.00145.73 C
ANISOU 2709 C33 8EH A1102 19870 19840 15661 812 1579 -1115 C
HETATM 2710 C34 8EH A1102 -37.299 6.616 45.427 1.00144.51 C
ANISOU 2710 C34 8EH A1102 19696 19575 15637 857 1647 -1053 C
HETATM 2711 C35 8EH A1102 -38.619 6.152 45.049 1.00143.33 C
ANISOU 2711 C35 8EH A1102 19646 19311 15502 887 1744 -994 C
HETATM 2712 C36 8EH A1102 -38.909 5.668 43.600 1.00142.17 C
ANISOU 2712 C36 8EH A1102 19484 19059 15476 919 1816 -932 C
HETATM 2713 N11 8EH A1102 -40.993 7.147 49.560 1.00145.12 N
ANISOU 2713 N11 8EH A1102 20231 19622 15285 736 1791 -1152 N
HETATM 2714 N13 8EH A1102 -43.058 7.006 51.221 1.00145.52 N
ANISOU 2714 N13 8EH A1102 20523 19594 15173 681 1944 -1192 N
HETATM 2715 N22 8EH A1102 -43.347 1.477 54.369 1.00148.62 N
ANISOU 2715 N22 8EH A1102 21542 20000 14926 981 1944 -805 N
HETATM 2716 N27 8EH A1102 -43.797 0.981 52.056 1.00146.04 N
ANISOU 2716 N27 8EH A1102 21044 19558 14888 1011 2059 -765 N
HETATM 2717 N28 8EH A1102 -42.720 5.756 49.082 1.00143.88 N
ANISOU 2717 N28 8EH A1102 20183 19332 15152 813 1935 -1049 N
HETATM 2718 N29 8EH A1102 -41.780 5.645 48.070 1.00143.50 N
ANISOU 2718 N29 8EH A1102 20024 19300 15199 853 1876 -1011 N
HETATM 2719 N37 8EH A1102 -39.632 6.136 45.989 1.00143.30 N
ANISOU 2719 N37 8EH A1102 19749 19300 15400 874 1778 -1003 N
HETATM 2720 O02 8EH A1102 -39.972 6.759 52.287 1.00148.16 O
ANISOU 2720 O02 8EH A1102 20739 20245 15310 710 1604 -1170 O
HETATM 2721 O08 8EH A1102 -40.237 9.707 48.282 1.00144.77 O
ANISOU 2721 O08 8EH A1102 20039 19519 15449 588 1849 -1336 O
HETATM 2722 O15 8EH A1102 -45.286 5.752 51.139 1.00144.48 O
ANISOU 2722 O15 8EH A1102 20527 19321 15049 716 2149 -1143 O
HETATM 2723 O16 8EH A1102 -44.726 6.717 53.194 1.00146.67 O
ANISOU 2723 O16 8EH A1102 20929 19684 15114 608 2086 -1245 O
HETATM 2724 O20 8EH A1102 -45.146 3.690 54.189 1.00147.28 O
ANISOU 2724 O20 8EH A1102 21286 19737 14938 745 2121 -1051 O
HETATM 2725 S14 8EH A1102 -44.184 6.032 52.050 1.00145.65 S
ANISOU 2725 S14 8EH A1102 20699 19563 15078 697 2032 -1156 S
HETATM 2726 C24 OLC A1103 -47.679 8.069 48.237 1.00174.63 C
ANISOU 2726 C24 OLC A1103 24088 22964 19301 720 2378 -1255 C
HETATM 2727 C6 OLC A1103 -55.757 11.703 42.906 1.00176.07 C
ANISOU 2727 C6 OLC A1103 23587 23175 20137 1235 2783 -1320 C
HETATM 2728 C5 OLC A1103 -55.025 10.380 42.716 1.00175.02 C
ANISOU 2728 C5 OLC A1103 23484 23079 19937 1130 2709 -1290 C
HETATM 2729 C4 OLC A1103 -54.042 10.127 43.853 1.00174.73 C
ANISOU 2729 C4 OLC A1103 23587 22979 19825 1033 2711 -1310 C
HETATM 2730 C3 OLC A1103 -53.082 8.998 43.496 1.00173.80 C
ANISOU 2730 C3 OLC A1103 23505 22879 19653 971 2630 -1255 C
HETATM 2731 C2 OLC A1103 -52.417 8.438 44.751 1.00173.88 C
ANISOU 2731 C2 OLC A1103 23635 22865 19566 888 2635 -1273 C
HETATM 2732 C21 OLC A1103 -49.767 8.349 46.914 1.00174.13 C
ANISOU 2732 C21 OLC A1103 23908 22854 19401 778 2520 -1272 C
HETATM 2733 C1 OLC A1103 -50.931 8.741 44.840 1.00173.53 C
ANISOU 2733 C1 OLC A1103 23656 22779 19498 876 2551 -1240 C
HETATM 2734 C22 OLC A1103 -48.792 7.333 47.502 1.00174.12 C
ANISOU 2734 C22 OLC A1103 23981 22885 19291 752 2448 -1226 C
HETATM 2735 O19 OLC A1103 -50.420 9.679 44.243 1.00173.45 O
ANISOU 2735 O19 OLC A1103 23626 22731 19547 914 2522 -1230 O
HETATM 2736 O25 OLC A1103 -46.715 7.120 48.705 1.00174.84 O
ANISOU 2736 O25 OLC A1103 24162 23043 19227 724 2291 -1199 O
HETATM 2737 O23 OLC A1103 -49.475 6.479 48.427 1.00174.65 O
ANISOU 2737 O23 OLC A1103 24139 22959 19262 718 2514 -1239 O
HETATM 2738 O20 OLC A1103 -50.146 7.965 45.590 1.00173.46 O
ANISOU 2738 O20 OLC A1103 23728 22782 19397 825 2513 -1224 O
HETATM 2739 O HOH A1201 -40.117 17.325 36.030 1.00 51.23 O
CONECT 564 1138
CONECT 1138 564
CONECT 1555 2688
CONECT 1575 2688
CONECT 1809 2688
CONECT 1830 2688
CONECT 2688 1555 1575 1809 1830
CONECT 2689 2703 2707 2713
CONECT 2690 2713 2714 2717
CONECT 2691 2692 2693 2725
CONECT 2692 2691
CONECT 2693 2691 2694 2724
CONECT 2694 2693 2715 2716
CONECT 2695 2696 2715
CONECT 2696 2695 2697 2698
CONECT 2697 2696
CONECT 2698 2696 2716
CONECT 2699 2700 2713 2718
CONECT 2700 2699 2701 2719
CONECT 2701 2700 2709
CONECT 2702 2720
CONECT 2703 2689 2704 2720
CONECT 2704 2703 2705
CONECT 2705 2704 2706
CONECT 2706 2705 2707
CONECT 2707 2689 2706 2721
CONECT 2708 2721
CONECT 2709 2701 2710
CONECT 2710 2709 2711
CONECT 2711 2710 2712 2719
CONECT 2712 2711
CONECT 2713 2689 2690 2699
CONECT 2714 2690 2725
CONECT 2715 2694 2695
CONECT 2716 2694 2698
CONECT 2717 2690 2718
CONECT 2718 2699 2717
CONECT 2719 2700 2711
CONECT 2720 2702 2703
CONECT 2721 2707 2708
CONECT 2722 2725
CONECT 2723 2725
CONECT 2724 2693
CONECT 2725 2691 2714 2722 2723
CONECT 2726 2734 2736
CONECT 2727 2728
CONECT 2728 2727 2729
CONECT 2729 2728 2730
CONECT 2730 2729 2731
CONECT 2731 2730 2733
CONECT 2732 2734 2738
CONECT 2733 2731 2735 2738
CONECT 2734 2726 2732 2737
CONECT 2735 2733
CONECT 2736 2726
CONECT 2737 2734
CONECT 2738 2732 2733
MASTER 389 0 3 14 5 0 0 6 2738 1 57 32
END