HEADER MEMBRANE PROTEIN 04-MAR-20 6W25
TITLE CRYSTAL STRUCTURE OF THE MELANOCORTIN-4 RECEPTOR (MC4R) IN COMPLEX
TITLE 2 WITH SHU9119
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MELANOCORTIN RECEPTOR 4,GLGA GLYCOGEN SYNTHASE,MELANOCORTIN
COMPND 3 RECEPTOR 4;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: MC4-R,GLYCOGEN SYNTHASE,MC4-R;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SHU9119;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 272844;
SOURCE 5 STRAIN: GE5 / ORSAY;
SOURCE 6 GENE: MC4R, PAB2292;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 12 ORGANISM_TAXID: 32630
KEYWDS MELANOCORTIN-4 RECEPTOR, CA++ COFACTOR, SHU9119, GPCR, PGS FUSION,
KEYWDS 2 MEMBRANE PROTEIN, LCP
EXPDTA X-RAY DIFFRACTION
AUTHOR J.YU,L.E.GIMENEZ,C.C.HERNANDEZ,Y.WU,A.H.WEIN,G.W.HAN,K.MCCLARY,
AUTHOR 2 S.R.MITTAL,K.BURDSALL,B.STAUCH,L.WU,S.N.STEVENS,A.PEISLEY,
AUTHOR 3 S.Y.WILLIAMS,V.CHEN,G.L.MILLHAUSER,S.ZHAO,R.D.CONE,R.C.STEVENS
REVDAT 3 09-SEP-20 6W25 1 REMARK DBREF LINK SITE
REVDAT 3 2 1 ATOM
REVDAT 2 06-MAY-20 6W25 1 JRNL REMARK
REVDAT 1 29-APR-20 6W25 0
JRNL AUTH J.YU,L.E.GIMENEZ,C.C.HERNANDEZ,Y.WU,A.H.WEIN,G.W.HAN,
JRNL AUTH 2 K.MCCLARY,S.R.MITTAL,K.BURDSALL,B.STAUCH,L.WU,S.N.STEVENS,
JRNL AUTH 3 A.PEISLEY,S.Y.WILLIAMS,V.CHEN,G.L.MILLHAUSER,S.ZHAO,
JRNL AUTH 4 R.D.CONE,R.C.STEVENS
JRNL TITL DETERMINATION OF THE MELANOCORTIN-4 RECEPTOR STRUCTURE
JRNL TITL 2 IDENTIFIES CA2+AS A COFACTOR FOR LIGAND BINDING.
JRNL REF SCIENCE V. 368 428 2020
JRNL REFN ESSN 1095-9203
JRNL PMID 32327598
JRNL DOI 10.1126/SCIENCE.AAZ8995
REMARK 2
REMARK 2 RESOLUTION. 2.75 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) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 16759
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 815
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.94
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3004
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2790
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2854
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.99
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 150
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 : 3697
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 94
REMARK 3 SOLVENT ATOMS : 21
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 18.02050
REMARK 3 B22 (A**2) : -20.49250
REMARK 3 B33 (A**2) : 2.47200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.64380
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.000
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.916
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.330
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 1.027
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.339
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 : 0.908
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3868 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5208 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1786 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 64 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 567 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3868 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 519 ; 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 : 4965 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.98
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.10
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|43 - A|320, A|2000 - A|2008 }
REMARK 3 ORIGIN FOR THE GROUP (A): 152.6549 4.8245 108.6687
REMARK 3 T TENSOR
REMARK 3 T11: -0.1602 T22: -0.0653
REMARK 3 T33: -0.1144 T12: -0.0360
REMARK 3 T13: -0.0081 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.9152 L22: 1.1073
REMARK 3 L33: 1.8296 L12: 0.4890
REMARK 3 L13: 0.3209 L23: -0.2403
REMARK 3 S TENSOR
REMARK 3 S11: -0.0798 S12: 0.4999 S13: -0.0887
REMARK 3 S21: -0.0928 S22: 0.0892 S23: -0.0107
REMARK 3 S31: 0.1084 S32: 0.0938 S33: -0.0093
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|1001 - A|1196 }
REMARK 3 ORIGIN FOR THE GROUP (A): 181.2486 -3.9922 144.6664
REMARK 3 T TENSOR
REMARK 3 T11: -0.2210 T22: -0.1028
REMARK 3 T33: -0.0549 T12: 0.0266
REMARK 3 T13: 0.0028 T23: 0.0570
REMARK 3 L TENSOR
REMARK 3 L11: 4.8909 L22: 2.0427
REMARK 3 L33: 2.2195 L12: -0.4961
REMARK 3 L13: -0.3546 L23: -0.2423
REMARK 3 S TENSOR
REMARK 3 S11: -0.0389 S12: -0.3879 S13: -0.3374
REMARK 3 S21: 0.1698 S22: 0.1061 S23: -0.0427
REMARK 3 S31: 0.1467 S32: 0.2669 S33: -0.0672
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6W25 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-20.
REMARK 100 THE DEPOSITION ID IS D_1000247500.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL45XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16761
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 43.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 15.00
REMARK 200 R MERGE (I) : 0.23400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 3.30200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.960
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB 3EML
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG 400, 100 MM BIS-TRIS PROPANE
REMARK 280 BUFFER, AND 50 MM CACL2 2H2O, PH 7.9, LIPIDIC CUBIC PHASE,
REMARK 280 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 81.95500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.24500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 81.95500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.24500
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: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -11
REMARK 465 LYS A -10
REMARK 465 THR A -9
REMARK 465 ILE A -8
REMARK 465 ILE A -7
REMARK 465 ALA A -6
REMARK 465 LEU A -5
REMARK 465 SER A -4
REMARK 465 TYR A -3
REMARK 465 ILE A -2
REMARK 465 PHE A -1
REMARK 465 CYS A 0
REMARK 465 LEU A 1
REMARK 465 VAL A 2
REMARK 465 PHE A 3
REMARK 465 ALA A 4
REMARK 465 ASP A 5
REMARK 465 TYR A 6
REMARK 465 LYS A 7
REMARK 465 ASP A 8
REMARK 465 ASP A 9
REMARK 465 ASP A 10
REMARK 465 ASP A 11
REMARK 465 ALA A 12
REMARK 465 GLY A 13
REMARK 465 ARG A 14
REMARK 465 ALA A 15
REMARK 465 TRP A 16
REMARK 465 ASN A 17
REMARK 465 ARG A 18
REMARK 465 SER A 19
REMARK 465 SER A 20
REMARK 465 TYR A 21
REMARK 465 ARG A 22
REMARK 465 LEU A 23
REMARK 465 HIS A 24
REMARK 465 SER A 25
REMARK 465 ASN A 26
REMARK 465 ALA A 27
REMARK 465 SER A 28
REMARK 465 GLU A 29
REMARK 465 SER A 30
REMARK 465 LEU A 31
REMARK 465 GLY A 32
REMARK 465 LYS A 33
REMARK 465 GLY A 34
REMARK 465 TYR A 35
REMARK 465 SER A 36
REMARK 465 ASP A 37
REMARK 465 GLY A 38
REMARK 465 GLY A 39
REMARK 465 CYS A 40
REMARK 465 TYR A 41
REMARK 465 GLU A 42
REMARK 465 ASP A 111
REMARK 465 THR A 112
REMARK 465 PRO A 2009
REMARK 465 HIS A 2010
REMARK 465 HIS A 2011
REMARK 465 HIS A 2012
REMARK 465 HIS A 2013
REMARK 465 HIS A 2014
REMARK 465 HIS A 2015
REMARK 465 HIS A 2016
REMARK 465 HIS A 2017
REMARK 465 HIS A 2018
REMARK 465 HIS A 2019
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 LEU A 44 CG CD1 CD2
REMARK 470 LYS A 71 CG CD CE NZ
REMARK 470 LYS A 73 CG CD CE NZ
REMARK 470 GLN A 115 CG CD OE1 NE2
REMARK 470 LYS A1062 CG CD CE NZ
REMARK 470 LYS A1159 NZ
REMARK 470 ARG A 236 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 237 CG CD OE1 NE2
REMARK 470 TYR A 320 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A2000 CG CD OE1 OE2
REMARK 470 PHE A2001 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A2003 CG CD OE1 OE2
REMARK 470 VAL A2004 CG1 CG2
REMARK 470 LEU A2005 CG CD1 CD2
REMARK 470 ASP B 2 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CG ASP B 2 NZ LYS B 7 1.34
REMARK 500 OD1 ASP B 2 NZ LYS B 7 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 HIS A 76 59.98 -90.16
REMARK 500 GLN A 115 -138.76 54.62
REMARK 500 TYR A 153 55.70 -118.30
REMARK 500 TYR A 187 40.46 -103.82
REMARK 500 GLN A1045 -73.02 -126.00
REMARK 500 PRO A1118 37.80 -89.91
REMARK 500 CYS A 271 52.03 -145.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLA A 2102
REMARK 610 OLA A 2103
REMARK 610 OLA A 2104
REMARK 610 OLA A 2105
REMARK 610 OLA A 2106
REMARK 610 OLA A 2107
REMARK 610 OLA A 2108
REMARK 610 OLA A 2109
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 CA A2101 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 100 OE2
REMARK 620 2 ASP A 122 OD1 94.2
REMARK 620 3 ASP A 126 OD1 75.7 108.8
REMARK 620 4 ASP A 126 OD2 115.4 79.2 48.3
REMARK 620 5 ASP B 2 O 85.6 94.1 151.2 158.2
REMARK 620 6 4J2 B 4 O 107.0 158.7 75.7 89.7 89.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 2101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE B 1 and NLE B 2
DBREF 6W25 A 16 222 UNP P32245 MC4R_HUMAN 16 222
DBREF 6W25 A 1001 1196 UNP Q9V2J8 Q9V2J8_PYRAB 218 413
DBREF 6W25 A 236 320 UNP P32245 MC4R_HUMAN 236 320
DBREF 6W25 B 0 8 PDB 6W25 6W25 0 8
SEQADV 6W25 MET A -11 UNP P32245 INITIATING METHIONINE
SEQADV 6W25 LYS A -10 UNP P32245 EXPRESSION TAG
SEQADV 6W25 THR A -9 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ILE A -8 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ILE A -7 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ALA A -6 UNP P32245 EXPRESSION TAG
SEQADV 6W25 LEU A -5 UNP P32245 EXPRESSION TAG
SEQADV 6W25 SER A -4 UNP P32245 EXPRESSION TAG
SEQADV 6W25 TYR A -3 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ILE A -2 UNP P32245 EXPRESSION TAG
SEQADV 6W25 PHE A -1 UNP P32245 EXPRESSION TAG
SEQADV 6W25 CYS A 0 UNP P32245 EXPRESSION TAG
SEQADV 6W25 LEU A 1 UNP P32245 EXPRESSION TAG
SEQADV 6W25 VAL A 2 UNP P32245 EXPRESSION TAG
SEQADV 6W25 PHE A 3 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ALA A 4 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ASP A 5 UNP P32245 EXPRESSION TAG
SEQADV 6W25 TYR A 6 UNP P32245 EXPRESSION TAG
SEQADV 6W25 LYS A 7 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ASP A 8 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ASP A 9 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ASP A 10 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ASP A 11 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ALA A 12 UNP P32245 EXPRESSION TAG
SEQADV 6W25 GLY A 13 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ARG A 14 UNP P32245 EXPRESSION TAG
SEQADV 6W25 ALA A 15 UNP P32245 EXPRESSION TAG
SEQADV 6W25 VAL A 49 UNP P32245 GLU 49 ENGINEERED MUTATION
SEQADV 6W25 LEU A 97 UNP P32245 ASN 97 ENGINEERED MUTATION
SEQADV 6W25 PHE A 99 UNP P32245 SER 99 ENGINEERED MUTATION
SEQADV 6W25 ALA A 131 UNP P32245 SER 131 ENGINEERED MUTATION
SEQADV 6W25 ASN A 298 UNP P32245 ASP 298 ENGINEERED MUTATION
SEQADV 6W25 GLU A 2000 UNP P32245 EXPRESSION TAG
SEQADV 6W25 PHE A 2001 UNP P32245 EXPRESSION TAG
SEQADV 6W25 LEU A 2002 UNP P32245 EXPRESSION TAG
SEQADV 6W25 GLU A 2003 UNP P32245 EXPRESSION TAG
SEQADV 6W25 VAL A 2004 UNP P32245 EXPRESSION TAG
SEQADV 6W25 LEU A 2005 UNP P32245 EXPRESSION TAG
SEQADV 6W25 PHE A 2006 UNP P32245 EXPRESSION TAG
SEQADV 6W25 GLN A 2007 UNP P32245 EXPRESSION TAG
SEQADV 6W25 GLY A 2008 UNP P32245 EXPRESSION TAG
SEQADV 6W25 PRO A 2009 UNP P32245 EXPRESSION TAG
SEQADV 6W25 HIS A 2010 UNP P32245 EXPRESSION TAG
SEQADV 6W25 HIS A 2011 UNP P32245 EXPRESSION TAG
SEQADV 6W25 HIS A 2012 UNP P32245 EXPRESSION TAG
SEQADV 6W25 HIS A 2013 UNP P32245 EXPRESSION TAG
SEQADV 6W25 HIS A 2014 UNP P32245 EXPRESSION TAG
SEQADV 6W25 HIS A 2015 UNP P32245 EXPRESSION TAG
SEQADV 6W25 HIS A 2016 UNP P32245 EXPRESSION TAG
SEQADV 6W25 HIS A 2017 UNP P32245 EXPRESSION TAG
SEQADV 6W25 HIS A 2018 UNP P32245 EXPRESSION TAG
SEQADV 6W25 HIS A 2019 UNP P32245 EXPRESSION TAG
SEQRES 1 A 535 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU
SEQRES 2 A 535 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA GLY ARG
SEQRES 3 A 535 ALA TRP ASN ARG SER SER TYR ARG LEU HIS SER ASN ALA
SEQRES 4 A 535 SER GLU SER LEU GLY LYS GLY TYR SER ASP GLY GLY CYS
SEQRES 5 A 535 TYR GLU GLN LEU PHE VAL SER PRO VAL VAL PHE VAL THR
SEQRES 6 A 535 LEU GLY VAL ILE SER LEU LEU GLU ASN ILE LEU VAL ILE
SEQRES 7 A 535 VAL ALA ILE ALA LYS ASN LYS ASN LEU HIS SER PRO MET
SEQRES 8 A 535 TYR PHE PHE ILE CYS SER LEU ALA VAL ALA ASP MET LEU
SEQRES 9 A 535 VAL SER VAL SER LEU GLY PHE GLU THR ILE VAL ILE THR
SEQRES 10 A 535 LEU LEU ASN SER THR ASP THR ASP ALA GLN SER PHE THR
SEQRES 11 A 535 VAL ASN ILE ASP ASN VAL ILE ASP SER VAL ILE CYS ALA
SEQRES 12 A 535 SER LEU LEU ALA SER ILE CYS SER LEU LEU SER ILE ALA
SEQRES 13 A 535 VAL ASP ARG TYR PHE THR ILE PHE TYR ALA LEU GLN TYR
SEQRES 14 A 535 HIS ASN ILE MET THR VAL LYS ARG VAL GLY ILE ILE ILE
SEQRES 15 A 535 SER CYS ILE TRP ALA ALA CYS THR VAL SER GLY ILE LEU
SEQRES 16 A 535 PHE ILE ILE TYR SER ASP SER SER ALA VAL ILE ILE CYS
SEQRES 17 A 535 LEU ILE THR MET PHE PHE THR MET LEU ALA LEU MET ALA
SEQRES 18 A 535 SER LEU TYR VAL HIS MET PHE LEU MET ALA ARG LEU HIS
SEQRES 19 A 535 GLY ILE ASP YCM SER PHE TRP ASN GLU SER TYR LEU THR
SEQRES 20 A 535 GLY SER ARG ASP GLU ARG LYS LYS SER LEU LEU SER LYS
SEQRES 21 A 535 PHE GLY MET ASP GLU GLY VAL THR PHE MET PHE ILE GLY
SEQRES 22 A 535 ARG PHE ASP ARG GLY GLN LYS GLY VAL ASP VAL LEU LEU
SEQRES 23 A 535 LYS ALA ILE GLU ILE LEU SER SER LYS LYS GLU PHE GLN
SEQRES 24 A 535 GLU MET ARG PHE ILE ILE ILE GLY LYS GLY ASP PRO GLU
SEQRES 25 A 535 LEU GLU GLY TRP ALA ARG SER LEU GLU GLU LYS HIS GLY
SEQRES 26 A 535 ASN VAL LYS VAL ILE THR GLU MET LEU SER ARG GLU PHE
SEQRES 27 A 535 VAL ARG GLU LEU TYR GLY SER VAL ASP PHE VAL ILE ILE
SEQRES 28 A 535 PRO SER TYR PHE GLU PRO PHE GLY LEU VAL ALA LEU GLU
SEQRES 29 A 535 ALA MET CYS LEU GLY ALA ILE PRO ILE ALA SER ALA VAL
SEQRES 30 A 535 GLY GLY LEU ARG ASP ILE ILE THR ASN GLU THR GLY ILE
SEQRES 31 A 535 LEU VAL LYS ALA GLY ASP PRO GLY GLU LEU ALA ASN ALA
SEQRES 32 A 535 ILE LEU LYS ALA LEU GLU LEU SER ARG SER ASP LEU SER
SEQRES 33 A 535 LYS PHE ARG GLU ASN CYS LYS LYS ARG ALA MET SER PHE
SEQRES 34 A 535 SER ARG GLN GLY ALA ASN MET LYS GLY ALA ILE THR LEU
SEQRES 35 A 535 THR ILE LEU ILE GLY VAL PHE VAL VAL CYS TRP ALA PRO
SEQRES 36 A 535 PHE PHE LEU HIS LEU ILE PHE TYR ILE SER CYS PRO GLN
SEQRES 37 A 535 ASN PRO TYR CYS VAL CYS PHE MET SER HIS PHE ASN LEU
SEQRES 38 A 535 TYR LEU ILE LEU ILE MET CYS ASN SER ILE ILE ASN PRO
SEQRES 39 A 535 LEU ILE TYR ALA LEU ARG SER GLN GLU LEU ARG LYS THR
SEQRES 40 A 535 PHE LYS GLU ILE ILE CYS CYS TYR GLU PHE LEU GLU VAL
SEQRES 41 A 535 LEU PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 42 A 535 HIS HIS
SEQRES 1 B 9 ACE NLE ASP HIS 4J2 ARG TRP LYS NH2
MODRES 6W25 YCM A 1004 CYS MODIFIED RESIDUE
HET YCM A1004 10
HET ACE B 0 3
HET NLE B 1 8
HET 4J2 B 4 15
HET NH2 B 8 1
HET CA A2101 1
HET OLA A2102 6
HET OLA A2103 10
HET OLA A2104 7
HET OLA A2105 18
HET OLA A2106 12
HET OLA A2107 17
HET OLA A2108 8
HET OLA A2109 15
HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE
HETNAM ACE ACETYL GROUP
HETNAM NLE NORLEUCINE
HETNAM 4J2 (2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC ACID
HETNAM NH2 AMINO GROUP
HETNAM CA CALCIUM ION
HETNAM OLA OLEIC ACID
HETSYN YCM CYSTEINE-S-ACETAMIDE
FORMUL 1 YCM C5 H10 N2 O3 S
FORMUL 2 ACE C2 H4 O
FORMUL 2 NLE C6 H13 N O2
FORMUL 2 4J2 C13 H13 N O2
FORMUL 2 NH2 H2 N
FORMUL 3 CA CA 2+
FORMUL 4 OLA 8(C18 H34 O2)
FORMUL 12 HOH *21(H2 O)
HELIX 1 AA1 SER A 47 ASN A 72 1 26
HELIX 2 AA2 LYS A 73 HIS A 76 5 4
HELIX 3 AA3 SER A 77 THR A 110 1 34
HELIX 4 AA4 GLN A 115 TYR A 153 1 39
HELIX 5 AA5 TYR A 153 MET A 161 1 9
HELIX 6 AA6 THR A 162 TYR A 187 1 26
HELIX 7 AA7 SER A 190 PHE A 216 1 27
HELIX 8 AA8 MET A 218 GLY A 1001 1 6
HELIX 9 AA9 ASN A 1008 LEU A 1012 5 5
HELIX 10 AB1 SER A 1015 PHE A 1027 1 13
HELIX 11 AB2 GLY A 1047 SER A 1060 1 14
HELIX 12 AB3 LYS A 1061 GLN A 1065 5 5
HELIX 13 AB4 ASP A 1076 GLY A 1091 1 16
HELIX 14 AB5 SER A 1101 GLY A 1110 1 10
HELIX 15 AB6 GLY A 1125 LEU A 1134 1 10
HELIX 16 AB7 VAL A 1143 ILE A 1150 1 8
HELIX 17 AB8 ASP A 1162 SER A 1177 1 16
HELIX 18 AB9 LEU A 1181 PHE A 1195 1 15
HELIX 19 AC1 GLY A 238 CYS A 271 1 34
HELIX 20 AC2 ASN A 274 SER A 282 1 9
HELIX 21 AC3 HIS A 283 SER A 306 1 24
HELIX 22 AC4 SER A 306 GLY A 2008 1 24
SHEET 1 AA1 6 VAL A1093 ILE A1096 0
SHEET 2 AA1 6 MET A1067 ILE A1072 1 N PHE A1069 O LYS A1094
SHEET 3 AA1 6 VAL A1033 ILE A1038 1 N PHE A1035 O ARG A1068
SHEET 4 AA1 6 PHE A1114 ILE A1117 1 O ILE A1116 N MET A1036
SHEET 5 AA1 6 ILE A1137 SER A1141 1 O ILE A1139 N VAL A1115
SHEET 6 AA1 6 ILE A1156 VAL A1158 1 O ILE A1156 N PRO A1138
SSBOND 1 CYS A 271 CYS A 277 1555 1555 2.03
LINK C ASP A1003 N YCM A1004 1555 1555 1.35
LINK C YCM A1004 N SER A1005 1555 1555 1.35
LINK C ACE B 0 N NLE B 1 1555 1555 1.35
LINK C NLE B 1 N ASP B 2 1555 1555 1.34
LINK C HIS B 3 N 4J2 B 4 1555 1555 1.34
LINK C 4J2 B 4 N ARG B 5 1555 1555 1.33
LINK C LYS B 7 N NH2 B 8 1555 1555 1.33
LINK OE2 GLU A 100 CA CA A2101 1555 1555 2.21
LINK OD1 ASP A 122 CA CA A2101 1555 1555 2.27
LINK OD1 ASP A 126 CA CA A2101 1555 1555 2.64
LINK OD2 ASP A 126 CA CA A2101 1555 1555 2.73
LINK CA CA A2101 O ASP B 2 1555 1555 2.57
LINK CA CA A2101 O 4J2 B 4 1555 1555 2.26
SITE 1 AC1 5 GLU A 100 ASP A 122 ASP A 126 ASP B 2
SITE 2 AC1 5 4J2 B 4
SITE 1 AC2 2 ILE A 245 ARG A 305
SITE 1 AC3 3 HIS A 214 PHE A1124 OLA A2104
SITE 1 AC4 4 PRO A1123 ASP A1148 OLA A2103 OLA A2105
SITE 1 AC5 8 ALA A 144 PHE A 152 HIS A 222 GLY A1125
SITE 2 AC5 8 LEU A1129 ILE A1149 PHE A1195 OLA A2104
SITE 1 AC6 2 TYR A 212 PHE A 216
SITE 1 AC7 2 PHE A 81 TRP A 174
SITE 1 AC8 1 ALA A 192
SITE 1 AC9 1 ASP A1148
SITE 1 AD1 2 ASP A 122 ASP B 2
CRYST1 163.910 44.490 88.050 90.00 97.47 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 0.006101 0.000000 0.000800 0.00000
SCALE2 0.000000 0.022477 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011454 0.00000
ATOM 1 N GLN A 43 128.270 14.938 106.409 1.00101.36 N
ANISOU 1 N GLN A 43 10610 14145 13756 251 -735 1528 N
ATOM 2 CA GLN A 43 129.723 14.780 106.403 1.00 99.47 C
ANISOU 2 CA GLN A 43 10571 13789 13433 181 -709 1450 C
ATOM 3 C GLN A 43 130.435 16.122 106.216 1.00103.47 C
ANISOU 3 C GLN A 43 11163 14149 14002 286 -741 1540 C
ATOM 4 O GLN A 43 130.048 16.908 105.348 1.00104.53 O
ANISOU 4 O GLN A 43 11220 14331 14166 329 -845 1696 O
ATOM 5 CB GLN A 43 130.162 13.796 105.305 1.00100.31 C
ANISOU 5 CB GLN A 43 10709 14034 13370 -8 -780 1431 C
ATOM 6 CG GLN A 43 130.265 12.342 105.771 1.00110.33 C
ANISOU 6 CG GLN A 43 12021 15337 14563 -135 -714 1274 C
ATOM 7 CD GLN A 43 131.569 12.006 106.465 1.00121.45 C
ANISOU 7 CD GLN A 43 13614 16591 15941 -154 -626 1146 C
ATOM 8 OE1 GLN A 43 132.658 12.444 106.072 1.00114.72 O
ANISOU 8 OE1 GLN A 43 12871 15671 15046 -157 -643 1157 O
ATOM 9 NE2 GLN A 43 131.489 11.167 107.488 1.00110.94 N
ANISOU 9 NE2 GLN A 43 12313 15215 14625 -178 -536 1028 N
ATOM 10 N LEU A 44 131.484 16.369 107.029 1.00 98.66 N
ANISOU 10 N LEU A 44 10713 13360 13411 317 -659 1449 N
ATOM 11 CA LEU A 44 132.312 17.579 107.001 1.00 98.50 C
ANISOU 11 CA LEU A 44 10802 13175 13450 394 -679 1512 C
ATOM 12 C LEU A 44 133.077 17.662 105.682 1.00101.79 C
ANISOU 12 C LEU A 44 11264 13663 13750 279 -782 1608 C
ATOM 13 O LEU A 44 133.763 16.705 105.304 1.00100.42 O
ANISOU 13 O LEU A 44 11148 13569 13437 138 -774 1531 O
ATOM 14 CB LEU A 44 133.285 17.600 108.188 1.00 97.17 C
ANISOU 14 CB LEU A 44 10791 12829 13301 417 -570 1374 C
ATOM 15 N PHE A 45 132.929 18.793 104.968 1.00 98.89 N
ANISOU 15 N PHE A 45 10866 13270 13439 341 -877 1778 N
ATOM 16 CA PHE A 45 133.559 18.989 103.668 1.00 98.55 C
ANISOU 16 CA PHE A 45 10851 13313 13280 231 -981 1896 C
ATOM 17 C PHE A 45 134.955 19.585 103.771 1.00100.40 C
ANISOU 17 C PHE A 45 11249 13400 13500 205 -962 1893 C
ATOM 18 O PHE A 45 135.192 20.570 104.475 1.00100.18 O
ANISOU 18 O PHE A 45 11288 13172 13603 316 -936 1910 O
ATOM 19 CB PHE A 45 132.688 19.859 102.738 1.00102.43 C
ANISOU 19 CB PHE A 45 11220 13874 13824 288 -1112 2110 C
ATOM 20 CG PHE A 45 133.291 20.141 101.376 1.00104.58 C
ANISOU 20 CG PHE A 45 11520 14250 13967 169 -1224 2254 C
ATOM 21 CD1 PHE A 45 133.293 19.168 100.381 1.00107.58 C
ANISOU 21 CD1 PHE A 45 11855 14862 14159 7 -1272 2243 C
ATOM 22 CD2 PHE A 45 133.857 21.378 101.090 1.00107.50 C
ANISOU 22 CD2 PHE A 45 11961 14486 14397 212 -1282 2400 C
ATOM 23 CE1 PHE A 45 133.860 19.426 99.128 1.00109.18 C
ANISOU 23 CE1 PHE A 45 12081 15180 14222 -109 -1367 2371 C
ATOM 24 CE2 PHE A 45 134.423 21.635 99.837 1.00111.00 C
ANISOU 24 CE2 PHE A 45 12427 15042 14708 89 -1383 2545 C
ATOM 25 CZ PHE A 45 134.419 20.659 98.864 1.00109.00 C
ANISOU 25 CZ PHE A 45 12123 15037 14254 -70 -1421 2528 C
ATOM 26 N VAL A 46 135.861 18.973 103.006 1.00 95.18 N
ANISOU 26 N VAL A 46 10643 12848 12672 53 -978 1870 N
ATOM 27 CA VAL A 46 137.252 19.347 102.770 1.00 93.82 C
ANISOU 27 CA VAL A 46 10599 12611 12438 -18 -974 1882 C
ATOM 28 C VAL A 46 137.469 19.144 101.273 1.00 96.45 C
ANISOU 28 C VAL A 46 10894 13150 12603 -155 -1067 1989 C
ATOM 29 O VAL A 46 137.111 18.082 100.750 1.00 95.83 O
ANISOU 29 O VAL A 46 10753 13254 12405 -242 -1074 1924 O
ATOM 30 CB VAL A 46 138.286 18.604 103.656 1.00 96.08 C
ANISOU 30 CB VAL A 46 10997 12823 12685 -59 -860 1691 C
ATOM 31 CG1 VAL A 46 138.319 19.183 105.068 1.00 95.61 C
ANISOU 31 CG1 VAL A 46 11004 12541 12781 67 -785 1623 C
ATOM 32 CG2 VAL A 46 138.044 17.099 103.685 1.00 94.93 C
ANISOU 32 CG2 VAL A 46 10814 12815 12439 -134 -812 1542 C
ATOM 33 N SER A 47 137.957 20.187 100.570 1.00 92.62 N
ANISOU 33 N SER A 47 10441 12640 12110 -176 -1145 2159 N
ATOM 34 CA SER A 47 138.134 20.162 99.116 1.00 92.70 C
ANISOU 34 CA SER A 47 10412 12855 11954 -307 -1240 2290 C
ATOM 35 C SER A 47 138.989 18.968 98.656 1.00 93.59 C
ANISOU 35 C SER A 47 10561 13133 11868 -456 -1184 2143 C
ATOM 36 O SER A 47 140.022 18.689 99.270 1.00 91.78 O
ANISOU 36 O SER A 47 10426 12816 11631 -473 -1093 2015 O
ATOM 37 CB SER A 47 138.717 21.476 98.605 1.00 97.43 C
ANISOU 37 CB SER A 47 11064 13373 12580 -317 -1317 2491 C
ATOM 38 OG SER A 47 139.963 21.795 99.197 1.00105.08 O
ANISOU 38 OG SER A 47 12159 14194 13571 -335 -1246 2428 O
ATOM 39 N PRO A 48 138.537 18.232 97.604 1.00 89.44 N
ANISOU 39 N PRO A 48 9956 12844 11182 -559 -1239 2152 N
ATOM 40 CA PRO A 48 139.287 17.053 97.128 1.00 87.82 C
ANISOU 40 CA PRO A 48 9785 12794 10789 -691 -1183 1994 C
ATOM 41 C PRO A 48 140.753 17.318 96.771 1.00 89.79 C
ANISOU 41 C PRO A 48 10124 13055 10939 -771 -1148 1998 C
ATOM 42 O PRO A 48 141.563 16.394 96.845 1.00 88.00 O
ANISOU 42 O PRO A 48 9944 12875 10617 -830 -1064 1827 O
ATOM 43 CB PRO A 48 138.509 16.635 95.878 1.00 91.07 C
ANISOU 43 CB PRO A 48 10098 13456 11048 -791 -1281 2061 C
ATOM 44 CG PRO A 48 137.131 17.094 96.132 1.00 96.63 C
ANISOU 44 CG PRO A 48 10700 14122 11892 -689 -1353 2172 C
ATOM 45 CD PRO A 48 137.302 18.418 96.813 1.00 92.48 C
ANISOU 45 CD PRO A 48 10216 13371 11553 -559 -1356 2298 C
ATOM 46 N VAL A 49 141.090 18.573 96.403 1.00 86.52 N
ANISOU 46 N VAL A 49 9728 12592 10553 -772 -1212 2198 N
ATOM 47 CA VAL A 49 142.440 19.018 96.044 1.00 85.88 C
ANISOU 47 CA VAL A 49 9719 12525 10388 -857 -1190 2242 C
ATOM 48 C VAL A 49 143.392 18.894 97.265 1.00 87.39 C
ANISOU 48 C VAL A 49 10002 12524 10678 -803 -1076 2091 C
ATOM 49 O VAL A 49 144.575 18.624 97.060 1.00 86.77 O
ANISOU 49 O VAL A 49 9967 12508 10495 -885 -1019 2028 O
ATOM 50 CB VAL A 49 142.439 20.448 95.414 1.00 91.32 C
ANISOU 50 CB VAL A 49 10406 13187 11105 -873 -1301 2515 C
ATOM 51 CG1 VAL A 49 141.942 21.519 96.388 1.00 91.21 C
ANISOU 51 CG1 VAL A 49 10421 12896 11339 -723 -1328 2603 C
ATOM 52 CG2 VAL A 49 143.800 20.819 94.827 1.00 91.46 C
ANISOU 52 CG2 VAL A 49 10479 13277 10996 -1000 -1285 2578 C
ATOM 53 N VAL A 50 142.874 19.038 98.515 1.00 82.22 N
ANISOU 53 N VAL A 50 9370 11657 10213 -669 -1041 2027 N
ATOM 54 CA VAL A 50 143.661 18.913 99.756 1.00 80.09 C
ANISOU 54 CA VAL A 50 9187 11208 10037 -617 -942 1885 C
ATOM 55 C VAL A 50 144.209 17.472 99.855 1.00 81.93 C
ANISOU 55 C VAL A 50 9428 11546 10157 -670 -852 1673 C
ATOM 56 O VAL A 50 145.405 17.304 100.092 1.00 80.63 O
ANISOU 56 O VAL A 50 9319 11362 9953 -710 -791 1599 O
ATOM 57 CB VAL A 50 142.871 19.343 101.029 1.00 83.40 C
ANISOU 57 CB VAL A 50 9623 11404 10662 -466 -923 1858 C
ATOM 58 CG1 VAL A 50 143.668 19.084 102.307 1.00 81.58 C
ANISOU 58 CG1 VAL A 50 9481 11016 10500 -427 -823 1700 C
ATOM 59 CG2 VAL A 50 142.476 20.812 100.955 1.00 84.59 C
ANISOU 59 CG2 VAL A 50 9779 11422 10940 -401 -1007 2055 C
ATOM 60 N PHE A 51 143.350 16.454 99.608 1.00 77.81 N
ANISOU 60 N PHE A 51 8846 11137 9582 -677 -852 1584 N
ATOM 61 CA PHE A 51 143.728 15.035 99.611 1.00 76.46 C
ANISOU 61 CA PHE A 51 8684 11057 9311 -727 -780 1385 C
ATOM 62 C PHE A 51 144.777 14.721 98.543 1.00 80.47 C
ANISOU 62 C PHE A 51 9197 11744 9633 -844 -768 1366 C
ATOM 63 O PHE A 51 145.665 13.906 98.782 1.00 79.10 O
ANISOU 63 O PHE A 51 9062 11579 9412 -862 -688 1212 O
ATOM 64 CB PHE A 51 142.503 14.139 99.366 1.00 78.47 C
ANISOU 64 CB PHE A 51 8870 11407 9539 -734 -806 1324 C
ATOM 65 CG PHE A 51 141.530 13.967 100.505 1.00 79.29 C
ANISOU 65 CG PHE A 51 8958 11368 9799 -633 -783 1276 C
ATOM 66 CD1 PHE A 51 141.845 13.166 101.596 1.00 80.97 C
ANISOU 66 CD1 PHE A 51 9227 11466 10071 -595 -693 1111 C
ATOM 67 CD2 PHE A 51 140.260 14.526 100.443 1.00 82.37 C
ANISOU 67 CD2 PHE A 51 9268 11762 10269 -579 -852 1396 C
ATOM 68 CE1 PHE A 51 140.930 12.982 102.635 1.00 81.49 C
ANISOU 68 CE1 PHE A 51 9275 11424 10264 -514 -667 1071 C
ATOM 69 CE2 PHE A 51 139.342 14.335 101.480 1.00 84.74 C
ANISOU 69 CE2 PHE A 51 9538 11956 10702 -488 -820 1346 C
ATOM 70 CZ PHE A 51 139.684 13.565 102.570 1.00 81.45 C
ANISOU 70 CZ PHE A 51 9184 11432 10333 -462 -725 1184 C
ATOM 71 N VAL A 52 144.659 15.353 97.361 1.00 78.63 N
ANISOU 71 N VAL A 52 8920 11663 9292 -921 -848 1526 N
ATOM 72 CA VAL A 52 145.565 15.145 96.228 1.00 79.33 C
ANISOU 72 CA VAL A 52 9001 11959 9181 -1043 -839 1527 C
ATOM 73 C VAL A 52 146.916 15.825 96.509 1.00 82.78 C
ANISOU 73 C VAL A 52 9490 12327 9635 -1057 -793 1569 C
ATOM 74 O VAL A 52 147.946 15.171 96.356 1.00 82.00 O
ANISOU 74 O VAL A 52 9405 12313 9440 -1103 -716 1443 O
ATOM 75 CB VAL A 52 144.934 15.607 94.885 1.00 85.12 C
ANISOU 75 CB VAL A 52 9668 12892 9780 -1131 -946 1700 C
ATOM 76 CG1 VAL A 52 145.876 15.362 93.707 1.00 85.93 C
ANISOU 76 CG1 VAL A 52 9762 13234 9655 -1265 -926 1691 C
ATOM 77 CG2 VAL A 52 143.598 14.909 94.646 1.00 85.28 C
ANISOU 77 CG2 VAL A 52 9629 12988 9787 -1125 -997 1655 C
ATOM 78 N THR A 53 146.909 17.108 96.945 1.00 79.54 N
ANISOU 78 N THR A 53 9108 11759 9356 -1017 -841 1736 N
ATOM 79 CA THR A 53 148.127 17.876 97.248 1.00 79.21 C
ANISOU 79 CA THR A 53 9115 11636 9343 -1044 -813 1795 C
ATOM 80 C THR A 53 148.903 17.256 98.419 1.00 80.73 C
ANISOU 80 C THR A 53 9359 11699 9615 -986 -712 1607 C
ATOM 81 O THR A 53 150.118 17.110 98.294 1.00 80.41 O
ANISOU 81 O THR A 53 9326 11725 9500 -1045 -657 1564 O
ATOM 82 CB THR A 53 147.836 19.365 97.496 1.00 89.00 C
ANISOU 82 CB THR A 53 10387 12707 10724 -1012 -896 2007 C
ATOM 83 OG1 THR A 53 146.771 19.502 98.438 1.00 89.04 O
ANISOU 83 OG1 THR A 53 10404 12521 10906 -878 -912 1982 O
ATOM 84 CG2 THR A 53 147.510 20.122 96.211 1.00 89.61 C
ANISOU 84 CG2 THR A 53 10420 12928 10700 -1101 -1000 2232 C
ATOM 85 N LEU A 54 148.217 16.848 99.521 1.00 75.33 N
ANISOU 85 N LEU A 54 8702 10851 9071 -875 -687 1500 N
ATOM 86 CA LEU A 54 148.873 16.202 100.672 1.00 73.30 C
ANISOU 86 CA LEU A 54 8493 10474 8883 -820 -600 1330 C
ATOM 87 C LEU A 54 149.478 14.857 100.267 1.00 76.30 C
ANISOU 87 C LEU A 54 8850 11009 9133 -861 -531 1159 C
ATOM 88 O LEU A 54 150.549 14.503 100.756 1.00 75.28 O
ANISOU 88 O LEU A 54 8746 10852 9006 -858 -466 1065 O
ATOM 89 CB LEU A 54 147.926 16.010 101.871 1.00 72.31 C
ANISOU 89 CB LEU A 54 8395 10167 8913 -705 -588 1260 C
ATOM 90 CG LEU A 54 147.476 17.260 102.641 1.00 77.10 C
ANISOU 90 CG LEU A 54 9042 10573 9680 -630 -627 1373 C
ATOM 91 CD1 LEU A 54 146.479 16.891 103.719 1.00 76.49 C
ANISOU 91 CD1 LEU A 54 8972 10367 9722 -522 -600 1283 C
ATOM 92 CD2 LEU A 54 148.650 18.013 103.260 1.00 79.01 C
ANISOU 92 CD2 LEU A 54 9354 10693 9974 -646 -609 1396 C
ATOM 93 N GLY A 55 148.805 14.152 99.356 1.00 73.14 N
ANISOU 93 N GLY A 55 8401 10768 8620 -900 -550 1123 N
ATOM 94 CA GLY A 55 149.260 12.884 98.797 1.00 72.86 C
ANISOU 94 CA GLY A 55 8347 10885 8453 -942 -492 956 C
ATOM 95 C GLY A 55 150.496 13.059 97.938 1.00 77.54 C
ANISOU 95 C GLY A 55 8916 11645 8901 -1028 -460 977 C
ATOM 96 O GLY A 55 151.348 12.171 97.903 1.00 77.07 O
ANISOU 96 O GLY A 55 8853 11648 8780 -1029 -383 823 O
ATOM 97 N VAL A 56 150.605 14.223 97.254 1.00 75.07 N
ANISOU 97 N VAL A 56 8581 11403 8538 -1098 -519 1175 N
ATOM 98 CA VAL A 56 151.739 14.606 96.405 1.00 75.86 C
ANISOU 98 CA VAL A 56 8650 11676 8497 -1198 -497 1239 C
ATOM 99 C VAL A 56 152.924 14.975 97.318 1.00 78.74 C
ANISOU 99 C VAL A 56 9044 11917 8958 -1173 -444 1227 C
ATOM 100 O VAL A 56 154.025 14.463 97.101 1.00 78.51 O
ANISOU 100 O VAL A 56 8985 12003 8842 -1203 -369 1131 O
ATOM 101 CB VAL A 56 151.361 15.742 95.406 1.00 81.29 C
ANISOU 101 CB VAL A 56 9311 12471 9106 -1291 -591 1479 C
ATOM 102 CG1 VAL A 56 152.593 16.465 94.855 1.00 82.05 C
ANISOU 102 CG1 VAL A 56 9386 12684 9105 -1397 -574 1593 C
ATOM 103 CG2 VAL A 56 150.505 15.202 94.264 1.00 82.21 C
ANISOU 103 CG2 VAL A 56 9381 12793 9064 -1349 -633 1471 C
ATOM 104 N ILE A 57 152.686 15.834 98.345 1.00 74.42 N
ANISOU 104 N ILE A 57 8552 11138 8588 -1115 -484 1315 N
ATOM 105 CA ILE A 57 153.689 16.272 99.334 1.00 73.42 C
ANISOU 105 CA ILE A 57 8462 10870 8565 -1096 -451 1309 C
ATOM 106 C ILE A 57 154.270 15.029 100.034 1.00 76.00 C
ANISOU 106 C ILE A 57 8790 11178 8908 -1030 -362 1092 C
ATOM 107 O ILE A 57 155.490 14.930 100.169 1.00 75.31 O
ANISOU 107 O ILE A 57 8681 11139 8794 -1056 -311 1052 O
ATOM 108 CB ILE A 57 153.104 17.310 100.349 1.00 76.01 C
ANISOU 108 CB ILE A 57 8860 10940 9079 -1034 -510 1410 C
ATOM 109 CG1 ILE A 57 152.670 18.616 99.640 1.00 77.64 C
ANISOU 109 CG1 ILE A 57 9069 11146 9285 -1096 -605 1641 C
ATOM 110 CG2 ILE A 57 154.095 17.624 101.487 1.00 76.03 C
ANISOU 110 CG2 ILE A 57 8911 10792 9185 -1016 -477 1373 C
ATOM 111 CD1 ILE A 57 151.542 19.408 100.353 1.00 83.20 C
ANISOU 111 CD1 ILE A 57 9826 11623 10162 -1003 -671 1720 C
ATOM 112 N SER A 58 153.396 14.070 100.420 1.00 72.10 N
ANISOU 112 N SER A 58 8313 10626 8456 -950 -349 961 N
ATOM 113 CA SER A 58 153.776 12.804 101.056 1.00 71.18 C
ANISOU 113 CA SER A 58 8206 10475 8363 -883 -277 762 C
ATOM 114 C SER A 58 154.578 11.917 100.095 1.00 76.06 C
ANISOU 114 C SER A 58 8765 11306 8827 -925 -215 651 C
ATOM 115 O SER A 58 155.545 11.288 100.525 1.00 75.62 O
ANISOU 115 O SER A 58 8701 11246 8787 -888 -152 536 O
ATOM 116 CB SER A 58 152.540 12.057 101.546 1.00 74.06 C
ANISOU 116 CB SER A 58 8601 10739 8798 -812 -289 675 C
ATOM 117 OG SER A 58 152.775 10.663 101.651 1.00 82.85 O
ANISOU 117 OG SER A 58 9715 11878 9886 -777 -230 489 O
ATOM 118 N LEU A 59 154.166 11.857 98.809 1.00 73.33 N
ANISOU 118 N LEU A 59 8379 11151 8334 -998 -234 681 N
ATOM 119 CA LEU A 59 154.842 11.077 97.770 1.00 73.89 C
ANISOU 119 CA LEU A 59 8394 11446 8234 -1044 -171 570 C
ATOM 120 C LEU A 59 156.256 11.624 97.564 1.00 78.12 C
ANISOU 120 C LEU A 59 8880 12088 8715 -1095 -126 625 C
ATOM 121 O LEU A 59 157.207 10.848 97.576 1.00 77.88 O
ANISOU 121 O LEU A 59 8813 12127 8650 -1064 -45 484 O
ATOM 122 CB LEU A 59 154.024 11.107 96.459 1.00 75.12 C
ANISOU 122 CB LEU A 59 8521 11790 8232 -1130 -216 620 C
ATOM 123 CG LEU A 59 154.595 10.412 95.215 1.00 81.13 C
ANISOU 123 CG LEU A 59 9227 12816 8782 -1196 -156 511 C
ATOM 124 CD1 LEU A 59 154.557 8.898 95.346 1.00 80.99 C
ANISOU 124 CD1 LEU A 59 9229 12781 8764 -1125 -93 257 C
ATOM 125 CD2 LEU A 59 153.825 10.819 93.983 1.00 84.76 C
ANISOU 125 CD2 LEU A 59 9661 13462 9083 -1303 -222 623 C
ATOM 126 N LEU A 60 156.387 12.960 97.441 1.00 74.93 N
ANISOU 126 N LEU A 60 8471 11680 8317 -1169 -181 834 N
ATOM 127 CA LEU A 60 157.656 13.666 97.256 1.00 75.43 C
ANISOU 127 CA LEU A 60 8487 11838 8335 -1244 -154 925 C
ATOM 128 C LEU A 60 158.585 13.471 98.457 1.00 78.05 C
ANISOU 128 C LEU A 60 8827 12032 8798 -1173 -110 847 C
ATOM 129 O LEU A 60 159.769 13.191 98.266 1.00 78.32 O
ANISOU 129 O LEU A 60 8791 12197 8769 -1193 -41 791 O
ATOM 130 CB LEU A 60 157.400 15.175 97.023 1.00 76.19 C
ANISOU 130 CB LEU A 60 8602 11899 8448 -1336 -244 1178 C
ATOM 131 CG LEU A 60 157.428 15.730 95.577 1.00 82.77 C
ANISOU 131 CG LEU A 60 9382 12977 9091 -1473 -270 1326 C
ATOM 132 CD1 LEU A 60 158.823 15.659 94.955 1.00 84.10 C
ANISOU 132 CD1 LEU A 60 9462 13375 9116 -1561 -188 1312 C
ATOM 133 CD2 LEU A 60 156.358 15.105 94.685 1.00 85.68 C
ANISOU 133 CD2 LEU A 60 9742 13468 9343 -1476 -292 1277 C
ATOM 134 N GLU A 61 158.036 13.591 99.686 1.00 72.87 N
ANISOU 134 N GLU A 61 8249 11123 8316 -1091 -149 840 N
ATOM 135 CA GLU A 61 158.772 13.442 100.944 1.00 71.39 C
ANISOU 135 CA GLU A 61 8083 10787 8257 -1026 -124 776 C
ATOM 136 C GLU A 61 159.264 12.017 101.176 1.00 74.30 C
ANISOU 136 C GLU A 61 8421 11192 8618 -938 -47 569 C
ATOM 137 O GLU A 61 160.440 11.834 101.484 1.00 74.07 O
ANISOU 137 O GLU A 61 8341 11205 8597 -928 -2 526 O
ATOM 138 CB GLU A 61 157.903 13.865 102.136 1.00 71.50 C
ANISOU 138 CB GLU A 61 8192 10540 8435 -962 -182 809 C
ATOM 139 CG GLU A 61 157.987 15.337 102.475 1.00 81.76 C
ANISOU 139 CG GLU A 61 9532 11730 9805 -1023 -247 987 C
ATOM 140 CD GLU A 61 157.244 15.678 103.748 1.00 98.32 C
ANISOU 140 CD GLU A 61 11722 13573 12061 -945 -286 985 C
ATOM 141 OE1 GLU A 61 156.009 15.866 103.681 1.00 92.21 O
ANISOU 141 OE1 GLU A 61 10984 12727 11324 -909 -325 1021 O
ATOM 142 OE2 GLU A 61 157.889 15.720 104.820 1.00 90.65 O
ANISOU 142 OE2 GLU A 61 10781 12488 11173 -919 -275 943 O
ATOM 143 N ASN A 62 158.370 11.016 101.052 1.00 70.08 N
ANISOU 143 N ASN A 62 7916 10633 8078 -875 -37 444 N
ATOM 144 CA ASN A 62 158.706 9.619 101.313 1.00 69.59 C
ANISOU 144 CA ASN A 62 7844 10565 8031 -785 26 247 C
ATOM 145 C ASN A 62 159.586 9.001 100.225 1.00 74.62 C
ANISOU 145 C ASN A 62 8392 11437 8522 -805 102 148 C
ATOM 146 O ASN A 62 160.384 8.128 100.563 1.00 74.16 O
ANISOU 146 O ASN A 62 8304 11378 8496 -727 161 13 O
ATOM 147 CB ASN A 62 157.464 8.782 101.555 1.00 69.72 C
ANISOU 147 CB ASN A 62 7928 10468 8096 -727 6 153 C
ATOM 148 CG ASN A 62 156.837 9.072 102.897 1.00 88.91 C
ANISOU 148 CG ASN A 62 10435 12663 10685 -675 -40 198 C
ATOM 149 OD1 ASN A 62 157.362 8.703 103.956 1.00 82.66 O
ANISOU 149 OD1 ASN A 62 9666 11749 9991 -610 -24 144 O
ATOM 150 ND2 ASN A 62 155.714 9.769 102.886 1.00 79.71 N
ANISOU 150 ND2 ASN A 62 9306 11438 9543 -702 -99 303 N
ATOM 151 N ILE A 63 159.491 9.461 98.950 1.00 72.50 N
ANISOU 151 N ILE A 63 8078 11376 8094 -906 104 217 N
ATOM 152 CA ILE A 63 160.381 8.968 97.884 1.00 73.85 C
ANISOU 152 CA ILE A 63 8157 11799 8106 -934 188 125 C
ATOM 153 C ILE A 63 161.803 9.401 98.258 1.00 77.75 C
ANISOU 153 C ILE A 63 8571 12344 8624 -940 229 171 C
ATOM 154 O ILE A 63 162.698 8.561 98.289 1.00 77.69 O
ANISOU 154 O ILE A 63 8502 12405 8611 -868 308 26 O
ATOM 155 CB ILE A 63 159.956 9.414 96.448 1.00 78.33 C
ANISOU 155 CB ILE A 63 8693 12594 8477 -1056 176 203 C
ATOM 156 CG1 ILE A 63 158.812 8.517 95.920 1.00 78.76 C
ANISOU 156 CG1 ILE A 63 8796 12655 8473 -1037 162 78 C
ATOM 157 CG2 ILE A 63 161.152 9.422 95.463 1.00 80.78 C
ANISOU 157 CG2 ILE A 63 8889 13189 8615 -1119 264 180 C
ATOM 158 CD1 ILE A 63 158.128 9.004 94.634 1.00 86.27 C
ANISOU 158 CD1 ILE A 63 9732 13803 9243 -1161 120 177 C
ATOM 159 N LEU A 64 161.966 10.689 98.644 1.00 74.20 N
ANISOU 159 N LEU A 64 8130 11838 8224 -1018 170 369 N
ATOM 160 CA LEU A 64 163.216 11.309 99.097 1.00 74.41 C
ANISOU 160 CA LEU A 64 8092 11893 8288 -1053 185 448 C
ATOM 161 C LEU A 64 163.844 10.500 100.248 1.00 77.27 C
ANISOU 161 C LEU A 64 8450 12123 8787 -927 215 316 C
ATOM 162 O LEU A 64 165.057 10.313 100.250 1.00 77.55 O
ANISOU 162 O LEU A 64 8383 12277 8804 -917 272 280 O
ATOM 163 CB LEU A 64 162.936 12.768 99.528 1.00 74.16 C
ANISOU 163 CB LEU A 64 8117 11735 8325 -1147 92 667 C
ATOM 164 CG LEU A 64 164.038 13.555 100.248 1.00 79.08 C
ANISOU 164 CG LEU A 64 8705 12320 9022 -1197 78 765 C
ATOM 165 CD1 LEU A 64 165.018 14.159 99.267 1.00 80.88 C
ANISOU 165 CD1 LEU A 64 8821 12803 9109 -1332 114 871 C
ATOM 166 CD2 LEU A 64 163.440 14.654 101.105 1.00 80.88 C
ANISOU 166 CD2 LEU A 64 9042 12309 9380 -1229 -21 908 C
ATOM 167 N VAL A 65 163.010 9.991 101.187 1.00 72.37 N
ANISOU 167 N VAL A 65 7930 11271 8297 -832 176 249 N
ATOM 168 CA VAL A 65 163.423 9.169 102.335 1.00 71.28 C
ANISOU 168 CA VAL A 65 7806 10985 8290 -711 188 137 C
ATOM 169 C VAL A 65 163.976 7.814 101.834 1.00 75.75 C
ANISOU 169 C VAL A 65 8304 11668 8809 -618 275 -57 C
ATOM 170 O VAL A 65 165.087 7.441 102.217 1.00 75.71 O
ANISOU 170 O VAL A 65 8221 11700 8844 -559 315 -110 O
ATOM 171 CB VAL A 65 162.261 8.983 103.359 1.00 73.61 C
ANISOU 171 CB VAL A 65 8230 11024 8714 -652 126 127 C
ATOM 172 CG1 VAL A 65 162.604 7.947 104.429 1.00 72.72 C
ANISOU 172 CG1 VAL A 65 8136 10775 8718 -530 140 5 C
ATOM 173 CG2 VAL A 65 161.883 10.308 104.010 1.00 72.72 C
ANISOU 173 CG2 VAL A 65 8180 10782 8667 -720 50 296 C
ATOM 174 N ILE A 66 163.205 7.102 100.977 1.00 72.59 N
ANISOU 174 N ILE A 66 7931 11325 8326 -604 301 -164 N
ATOM 175 CA ILE A 66 163.566 5.794 100.407 1.00 73.42 C
ANISOU 175 CA ILE A 66 7992 11523 8381 -515 383 -369 C
ATOM 176 C ILE A 66 164.853 5.921 99.564 1.00 79.22 C
ANISOU 176 C ILE A 66 8582 12524 8995 -542 469 -389 C
ATOM 177 O ILE A 66 165.759 5.096 99.710 1.00 79.69 O
ANISOU 177 O ILE A 66 8570 12618 9089 -436 534 -520 O
ATOM 178 CB ILE A 66 162.384 5.175 99.593 1.00 76.66 C
ANISOU 178 CB ILE A 66 8471 11948 8709 -529 380 -466 C
ATOM 179 CG1 ILE A 66 161.161 4.903 100.501 1.00 75.44 C
ANISOU 179 CG1 ILE A 66 8442 11537 8685 -494 304 -460 C
ATOM 180 CG2 ILE A 66 162.806 3.886 98.862 1.00 78.71 C
ANISOU 180 CG2 ILE A 66 8690 12317 8900 -450 469 -693 C
ATOM 181 CD1 ILE A 66 159.806 4.979 99.793 1.00 82.70 C
ANISOU 181 CD1 ILE A 66 9421 12476 9525 -567 261 -443 C
ATOM 182 N VAL A 67 164.935 6.968 98.720 1.00 76.37 N
ANISOU 182 N VAL A 67 8173 12347 8498 -681 467 -248 N
ATOM 183 CA VAL A 67 166.083 7.244 97.851 1.00 77.86 C
ANISOU 183 CA VAL A 67 8218 12818 8549 -739 548 -236 C
ATOM 184 C VAL A 67 167.327 7.529 98.716 1.00 82.12 C
ANISOU 184 C VAL A 67 8669 13342 9192 -708 558 -183 C
ATOM 185 O VAL A 67 168.375 6.944 98.454 1.00 83.19 O
ANISOU 185 O VAL A 67 8681 13631 9296 -643 647 -291 O
ATOM 186 CB VAL A 67 165.775 8.389 96.838 1.00 82.14 C
ANISOU 186 CB VAL A 67 8745 13538 8927 -915 524 -60 C
ATOM 187 CG1 VAL A 67 167.041 8.925 96.172 1.00 83.51 C
ANISOU 187 CG1 VAL A 67 8767 13988 8976 -1003 595 9 C
ATOM 188 CG2 VAL A 67 164.775 7.928 95.780 1.00 82.48 C
ANISOU 188 CG2 VAL A 67 8839 13671 8830 -943 532 -141 C
ATOM 189 N ALA A 68 167.192 8.372 99.763 1.00 77.40 N
ANISOU 189 N ALA A 68 8131 12558 8720 -747 467 -30 N
ATOM 190 CA ALA A 68 168.286 8.750 100.665 1.00 77.27 C
ANISOU 190 CA ALA A 68 8043 12514 8802 -741 454 37 C
ATOM 191 C ALA A 68 168.896 7.558 101.411 1.00 80.98 C
ANISOU 191 C ALA A 68 8474 12907 9387 -570 490 -125 C
ATOM 192 O ALA A 68 170.120 7.486 101.511 1.00 81.57 O
ANISOU 192 O ALA A 68 8413 13110 9469 -546 535 -134 O
ATOM 193 CB ALA A 68 167.813 9.785 101.667 1.00 76.64 C
ANISOU 193 CB ALA A 68 8068 12218 8832 -809 344 202 C
ATOM 194 N ILE A 69 168.060 6.638 101.936 1.00 76.41 N
ANISOU 194 N ILE A 69 8009 12124 8901 -456 467 -242 N
ATOM 195 CA ILE A 69 168.531 5.455 102.666 1.00 76.28 C
ANISOU 195 CA ILE A 69 7975 12003 9005 -290 488 -385 C
ATOM 196 C ILE A 69 169.224 4.493 101.677 1.00 82.92 C
ANISOU 196 C ILE A 69 8699 13044 9764 -202 603 -561 C
ATOM 197 O ILE A 69 170.268 3.937 102.013 1.00 83.57 O
ANISOU 197 O ILE A 69 8674 13166 9911 -96 642 -629 O
ATOM 198 CB ILE A 69 167.385 4.778 103.480 1.00 77.68 C
ANISOU 198 CB ILE A 69 8313 11904 9299 -213 427 -443 C
ATOM 199 CG1 ILE A 69 166.868 5.734 104.587 1.00 76.34 C
ANISOU 199 CG1 ILE A 69 8239 11549 9216 -284 326 -281 C
ATOM 200 CG2 ILE A 69 167.831 3.434 104.094 1.00 78.50 C
ANISOU 200 CG2 ILE A 69 8405 11899 9522 -41 448 -594 C
ATOM 201 CD1 ILE A 69 165.445 5.482 105.077 1.00 81.57 C
ANISOU 201 CD1 ILE A 69 9059 11996 9939 -269 270 -293 C
ATOM 202 N ALA A 70 168.679 4.352 100.453 1.00 80.75 N
ANISOU 202 N ALA A 70 8436 12906 9339 -249 655 -631 N
ATOM 203 CA ALA A 70 169.238 3.484 99.413 1.00 82.55 C
ANISOU 203 CA ALA A 70 8566 13337 9463 -176 772 -815 C
ATOM 204 C ALA A 70 170.555 4.033 98.836 1.00 88.43 C
ANISOU 204 C ALA A 70 9120 14375 10106 -227 852 -764 C
ATOM 205 O ALA A 70 171.466 3.246 98.572 1.00 89.80 O
ANISOU 205 O ALA A 70 9172 14669 10277 -108 946 -912 O
ATOM 206 CB ALA A 70 168.226 3.291 98.297 1.00 83.65 C
ANISOU 206 CB ALA A 70 8781 13550 9453 -239 793 -890 C
ATOM 207 N LYS A 71 170.653 5.367 98.643 1.00 84.74 N
ANISOU 207 N LYS A 71 8622 14017 9558 -401 816 -556 N
ATOM 208 CA LYS A 71 171.825 6.041 98.070 1.00 86.06 C
ANISOU 208 CA LYS A 71 8612 14472 9616 -491 882 -471 C
ATOM 209 C LYS A 71 172.978 6.205 99.071 1.00 89.63 C
ANISOU 209 C LYS A 71 8952 14901 10203 -445 865 -409 C
ATOM 210 O LYS A 71 174.122 6.384 98.646 1.00 90.92 O
ANISOU 210 O LYS A 71 8934 15315 10297 -469 942 -396 O
ATOM 211 CB LYS A 71 171.437 7.419 97.510 1.00 88.45 C
ANISOU 211 CB LYS A 71 8940 14875 9793 -708 834 -255 C
ATOM 212 N ASN A 72 172.687 6.152 100.383 1.00 84.37 N
ANISOU 212 N ASN A 72 8385 13953 9717 -387 765 -369 N
ATOM 213 CA ASN A 72 173.698 6.320 101.427 1.00 84.18 C
ANISOU 213 CA ASN A 72 8270 13892 9821 -352 728 -301 C
ATOM 214 C ASN A 72 173.970 4.996 102.155 1.00 88.09 C
ANISOU 214 C ASN A 72 8758 14246 10466 -134 738 -465 C
ATOM 215 O ASN A 72 173.074 4.440 102.798 1.00 86.36 O
ANISOU 215 O ASN A 72 8696 13772 10347 -58 679 -518 O
ATOM 216 CB ASN A 72 173.262 7.412 102.414 1.00 82.67 C
ANISOU 216 CB ASN A 72 8195 13506 9711 -474 598 -108 C
ATOM 217 CG ASN A 72 174.318 7.958 103.351 1.00102.01 C
ANISOU 217 CG ASN A 72 10549 15961 12249 -510 546 6 C
ATOM 218 OD1 ASN A 72 173.995 8.633 104.331 1.00 90.61 O
ANISOU 218 OD1 ASN A 72 9210 14326 10891 -576 440 121 O
ATOM 219 ND2 ASN A 72 175.596 7.739 103.062 1.00 98.04 N
ANISOU 219 ND2 ASN A 72 9843 15688 11721 -480 617 -21 N
ATOM 220 N LYS A 73 175.223 4.503 102.049 1.00 86.14 N
ANISOU 220 N LYS A 73 8322 14173 10235 -36 813 -536 N
ATOM 221 CA LYS A 73 175.698 3.262 102.672 1.00 86.23 C
ANISOU 221 CA LYS A 73 8292 14078 10394 182 827 -681 C
ATOM 222 C LYS A 73 175.772 3.394 104.201 1.00 88.00 C
ANISOU 222 C LYS A 73 8576 14070 10790 206 699 -572 C
ATOM 223 O LYS A 73 175.767 2.381 104.903 1.00 87.42 O
ANISOU 223 O LYS A 73 8540 13823 10855 373 673 -665 O
ATOM 224 CB LYS A 73 177.071 2.868 102.105 1.00 91.32 C
ANISOU 224 CB LYS A 73 8692 15001 11005 273 942 -764 C
ATOM 225 N ASN A 74 175.829 4.642 104.709 1.00 83.14 N
ANISOU 225 N ASN A 74 7978 13451 10162 33 618 -376 N
ATOM 226 CA ASN A 74 175.875 4.973 106.135 1.00 81.39 C
ANISOU 226 CA ASN A 74 7821 13032 10072 16 493 -261 C
ATOM 227 C ASN A 74 174.531 4.729 106.817 1.00 82.58 C
ANISOU 227 C ASN A 74 8204 12883 10291 37 416 -275 C
ATOM 228 O ASN A 74 174.481 4.601 108.042 1.00 81.32 O
ANISOU 228 O ASN A 74 8112 12537 10248 75 326 -230 O
ATOM 229 CB ASN A 74 176.288 6.425 106.320 1.00 81.44 C
ANISOU 229 CB ASN A 74 7787 13129 10026 -190 438 -66 C
ATOM 230 CG ASN A 74 177.772 6.617 106.354 1.00101.30 C
ANISOU 230 CG ASN A 74 10073 15871 12544 -203 462 -16 C
ATOM 231 OD1 ASN A 74 178.422 6.378 107.373 1.00 94.69 O
ANISOU 231 OD1 ASN A 74 9181 14976 11822 -139 398 11 O
ATOM 232 ND2 ASN A 74 178.339 7.056 105.243 1.00 94.51 N
ANISOU 232 ND2 ASN A 74 9067 15289 11552 -291 553 4 N
ATOM 233 N LEU A 75 173.447 4.686 106.026 1.00 78.16 N
ANISOU 233 N LEU A 75 7758 12291 9649 4 450 -329 N
ATOM 234 CA LEU A 75 172.087 4.444 106.506 1.00 76.06 C
ANISOU 234 CA LEU A 75 7696 11770 9432 16 391 -347 C
ATOM 235 C LEU A 75 171.657 2.994 106.197 1.00 80.43 C
ANISOU 235 C LEU A 75 8295 12241 10025 180 441 -539 C
ATOM 236 O LEU A 75 170.469 2.673 106.270 1.00 78.91 O
ANISOU 236 O LEU A 75 8256 11880 9846 183 414 -578 O
ATOM 237 CB LEU A 75 171.104 5.460 105.882 1.00 75.11 C
ANISOU 237 CB LEU A 75 7673 11662 9203 -144 377 -259 C
ATOM 238 CG LEU A 75 171.430 6.947 106.057 1.00 79.34 C
ANISOU 238 CG LEU A 75 8186 12261 9700 -318 325 -70 C
ATOM 239 CD1 LEU A 75 170.699 7.778 105.041 1.00 79.35 C
ANISOU 239 CD1 LEU A 75 8233 12342 9574 -453 339 -2 C
ATOM 240 CD2 LEU A 75 171.111 7.433 107.458 1.00 80.21 C
ANISOU 240 CD2 LEU A 75 8410 12146 9922 -346 217 25 C
ATOM 241 N HIS A 76 172.629 2.109 105.886 1.00 78.67 N
ANISOU 241 N HIS A 76 7934 12128 9829 319 512 -660 N
ATOM 242 CA HIS A 76 172.349 0.705 105.586 1.00 79.14 C
ANISOU 242 CA HIS A 76 8032 12098 9939 484 561 -854 C
ATOM 243 C HIS A 76 172.396 -0.149 106.868 1.00 82.86 C
ANISOU 243 C HIS A 76 8565 12326 10593 619 484 -865 C
ATOM 244 O HIS A 76 173.182 -1.095 106.985 1.00 83.79 O
ANISOU 244 O HIS A 76 8593 12442 10800 784 514 -964 O
ATOM 245 CB HIS A 76 173.286 0.159 104.494 1.00 82.05 C
ANISOU 245 CB HIS A 76 8231 12706 10239 576 687 -999 C
ATOM 246 CG HIS A 76 172.969 0.653 103.114 1.00 85.87 C
ANISOU 246 CG HIS A 76 8693 13404 10529 460 770 -1032 C
ATOM 247 ND1 HIS A 76 173.790 0.361 102.040 1.00 89.80 N
ANISOU 247 ND1 HIS A 76 9032 14163 10924 509 895 -1150 N
ATOM 248 CD2 HIS A 76 171.931 1.403 102.675 1.00 86.22 C
ANISOU 248 CD2 HIS A 76 8852 13444 10465 303 742 -955 C
ATOM 249 CE1 HIS A 76 173.229 0.940 100.991 1.00 89.14 C
ANISOU 249 CE1 HIS A 76 8977 14228 10663 369 935 -1137 C
ATOM 250 NE2 HIS A 76 172.110 1.581 101.326 1.00 87.42 N
ANISOU 250 NE2 HIS A 76 8920 13854 10440 244 841 -1016 N
ATOM 251 N SER A 77 171.519 0.201 107.823 1.00 77.77 N
ANISOU 251 N SER A 77 8073 11476 9999 548 386 -761 N
ATOM 252 CA SER A 77 171.348 -0.483 109.102 1.00 77.00 C
ANISOU 252 CA SER A 77 8064 11141 10053 638 301 -742 C
ATOM 253 C SER A 77 169.887 -0.954 109.221 1.00 79.75 C
ANISOU 253 C SER A 77 8606 11277 10416 622 272 -788 C
ATOM 254 O SER A 77 169.017 -0.310 108.626 1.00 78.30 O
ANISOU 254 O SER A 77 8489 11131 10130 502 286 -767 O
ATOM 255 CB SER A 77 171.737 0.435 110.260 1.00 79.71 C
ANISOU 255 CB SER A 77 8397 11457 10431 554 209 -564 C
ATOM 256 OG SER A 77 170.697 1.328 110.625 1.00 86.95 O
ANISOU 256 OG SER A 77 9454 12280 11304 410 156 -464 O
ATOM 257 N PRO A 78 169.587 -2.046 109.976 1.00 76.63 N
ANISOU 257 N PRO A 78 8300 10666 10149 733 226 -837 N
ATOM 258 CA PRO A 78 168.191 -2.520 110.078 1.00 75.61 C
ANISOU 258 CA PRO A 78 8347 10348 10034 703 200 -876 C
ATOM 259 C PRO A 78 167.157 -1.436 110.412 1.00 78.07 C
ANISOU 259 C PRO A 78 8758 10625 10279 541 154 -751 C
ATOM 260 O PRO A 78 166.104 -1.424 109.778 1.00 77.24 O
ANISOU 260 O PRO A 78 8733 10503 10111 479 174 -795 O
ATOM 261 CB PRO A 78 168.256 -3.558 111.197 1.00 77.55 C
ANISOU 261 CB PRO A 78 8656 10374 10435 817 133 -876 C
ATOM 262 CG PRO A 78 169.633 -4.082 111.129 1.00 83.63 C
ANISOU 262 CG PRO A 78 9278 11226 11272 962 159 -926 C
ATOM 263 CD PRO A 78 170.503 -2.933 110.726 1.00 79.30 C
ANISOU 263 CD PRO A 78 8578 10927 10627 889 195 -855 C
ATOM 264 N MET A 79 167.465 -0.515 111.360 1.00 74.15 N
ANISOU 264 N MET A 79 8252 10126 9795 474 94 -601 N
ATOM 265 CA MET A 79 166.575 0.573 111.790 1.00 72.62 C
ANISOU 265 CA MET A 79 8151 9889 9553 336 50 -484 C
ATOM 266 C MET A 79 166.101 1.426 110.609 1.00 76.28 C
ANISOU 266 C MET A 79 8598 10494 9891 231 99 -481 C
ATOM 267 O MET A 79 164.893 1.630 110.465 1.00 75.13 O
ANISOU 267 O MET A 79 8553 10278 9714 169 89 -472 O
ATOM 268 CB MET A 79 167.252 1.469 112.840 1.00 74.67 C
ANISOU 268 CB MET A 79 8381 10157 9834 283 -12 -347 C
ATOM 269 CG MET A 79 166.263 2.236 113.696 1.00 77.00 C
ANISOU 269 CG MET A 79 8805 10329 10123 184 -69 -252 C
ATOM 270 SD MET A 79 166.828 3.904 114.087 1.00 81.01 S
ANISOU 270 SD MET A 79 9275 10927 10579 51 -108 -111 S
ATOM 271 CE MET A 79 165.423 4.512 114.984 1.00 76.07 C
ANISOU 271 CE MET A 79 8819 10128 9957 -25 -154 -50 C
ATOM 272 N TYR A 80 167.041 1.896 109.757 1.00 73.55 N
ANISOU 272 N TYR A 80 8119 10356 9472 211 151 -482 N
ATOM 273 CA TYR A 80 166.718 2.711 108.582 1.00 73.19 C
ANISOU 273 CA TYR A 80 8047 10468 9296 105 195 -463 C
ATOM 274 C TYR A 80 166.007 1.884 107.507 1.00 76.07 C
ANISOU 274 C TYR A 80 8443 10856 9603 138 251 -603 C
ATOM 275 O TYR A 80 165.224 2.448 106.741 1.00 75.47 O
ANISOU 275 O TYR A 80 8401 10843 9430 43 260 -578 O
ATOM 276 CB TYR A 80 167.962 3.395 108.006 1.00 75.71 C
ANISOU 276 CB TYR A 80 8209 11013 9545 63 235 -417 C
ATOM 277 CG TYR A 80 168.582 4.419 108.933 1.00 77.46 C
ANISOU 277 CG TYR A 80 8404 11226 9801 -11 172 -267 C
ATOM 278 CD1 TYR A 80 167.962 5.646 109.166 1.00 78.46 C
ANISOU 278 CD1 TYR A 80 8608 11306 9896 -144 121 -140 C
ATOM 279 CD2 TYR A 80 169.804 4.179 109.550 1.00 79.20 C
ANISOU 279 CD2 TYR A 80 8517 11488 10086 50 159 -256 C
ATOM 280 CE1 TYR A 80 168.528 6.592 110.019 1.00 79.25 C
ANISOU 280 CE1 TYR A 80 8697 11386 10027 -221 60 -17 C
ATOM 281 CE2 TYR A 80 170.382 5.118 110.404 1.00 80.01 C
ANISOU 281 CE2 TYR A 80 8598 11589 10213 -33 92 -123 C
ATOM 282 CZ TYR A 80 169.740 6.324 110.635 1.00 87.44 C
ANISOU 282 CZ TYR A 80 9633 12472 11119 -173 44 -9 C
ATOM 283 OH TYR A 80 170.310 7.257 111.468 1.00 89.84 O
ANISOU 283 OH TYR A 80 9927 12764 11446 -264 -24 108 O
ATOM 284 N PHE A 81 166.247 0.557 107.468 1.00 72.18 N
ANISOU 284 N PHE A 81 7946 10305 9175 270 281 -749 N
ATOM 285 CA PHE A 81 165.567 -0.347 106.540 1.00 72.04 C
ANISOU 285 CA PHE A 81 7976 10283 9114 303 328 -903 C
ATOM 286 C PHE A 81 164.105 -0.529 106.970 1.00 73.62 C
ANISOU 286 C PHE A 81 8330 10295 9347 255 270 -885 C
ATOM 287 O PHE A 81 163.231 -0.667 106.114 1.00 73.24 O
ANISOU 287 O PHE A 81 8327 10281 9219 202 288 -946 O
ATOM 288 CB PHE A 81 166.289 -1.699 106.437 1.00 75.27 C
ANISOU 288 CB PHE A 81 8343 10658 9599 464 372 -1067 C
ATOM 289 CG PHE A 81 167.614 -1.675 105.704 1.00 78.43 C
ANISOU 289 CG PHE A 81 8574 11280 9944 522 455 -1128 C
ATOM 290 CD1 PHE A 81 167.759 -0.973 104.511 1.00 82.13 C
ANISOU 290 CD1 PHE A 81 8964 11992 10249 430 522 -1131 C
ATOM 291 CD2 PHE A 81 168.700 -2.403 106.176 1.00 81.60 C
ANISOU 291 CD2 PHE A 81 8891 11656 10457 672 468 -1183 C
ATOM 292 CE1 PHE A 81 168.976 -0.968 103.827 1.00 84.65 C
ANISOU 292 CE1 PHE A 81 9117 12538 10508 478 608 -1188 C
ATOM 293 CE2 PHE A 81 169.915 -2.401 105.488 1.00 86.10 C
ANISOU 293 CE2 PHE A 81 9287 12448 10978 734 553 -1244 C
ATOM 294 CZ PHE A 81 170.041 -1.693 104.312 1.00 84.83 C
ANISOU 294 CZ PHE A 81 9047 12539 10646 634 628 -1252 C
ATOM 295 N PHE A 82 163.838 -0.492 108.294 1.00 68.45 N
ANISOU 295 N PHE A 82 7747 9459 8800 264 199 -795 N
ATOM 296 CA PHE A 82 162.482 -0.572 108.840 1.00 66.89 C
ANISOU 296 CA PHE A 82 7681 9098 8637 213 148 -759 C
ATOM 297 C PHE A 82 161.794 0.796 108.711 1.00 70.68 C
ANISOU 297 C PHE A 82 8177 9641 9038 85 126 -630 C
ATOM 298 O PHE A 82 160.567 0.848 108.622 1.00 69.76 O
ANISOU 298 O PHE A 82 8139 9463 8905 30 105 -619 O
ATOM 299 CB PHE A 82 162.475 -1.076 110.294 1.00 67.78 C
ANISOU 299 CB PHE A 82 7863 9011 8881 269 88 -713 C
ATOM 300 CG PHE A 82 162.883 -2.522 110.473 1.00 70.03 C
ANISOU 300 CG PHE A 82 8161 9184 9264 395 92 -829 C
ATOM 301 CD1 PHE A 82 162.263 -3.534 109.746 1.00 73.54 C
ANISOU 301 CD1 PHE A 82 8659 9574 9708 420 118 -969 C
ATOM 302 CD2 PHE A 82 163.858 -2.877 111.396 1.00 72.24 C
ANISOU 302 CD2 PHE A 82 8406 9400 9642 486 61 -795 C
ATOM 303 CE1 PHE A 82 162.637 -4.870 109.917 1.00 75.55 C
ANISOU 303 CE1 PHE A 82 8939 9699 10069 541 117 -1079 C
ATOM 304 CE2 PHE A 82 164.241 -4.211 111.557 1.00 76.11 C
ANISOU 304 CE2 PHE A 82 8910 9772 10238 614 58 -893 C
ATOM 305 CZ PHE A 82 163.623 -5.200 110.821 1.00 74.97 C
ANISOU 305 CZ PHE A 82 8827 9557 10102 643 87 -1037 C
ATOM 306 N ILE A 83 162.591 1.896 108.668 1.00 67.69 N
ANISOU 306 N ILE A 83 7719 9384 8615 38 129 -531 N
ATOM 307 CA ILE A 83 162.130 3.275 108.444 1.00 66.92 C
ANISOU 307 CA ILE A 83 7628 9351 8449 -78 108 -404 C
ATOM 308 C ILE A 83 161.719 3.377 106.962 1.00 72.98 C
ANISOU 308 C ILE A 83 8362 10275 9091 -132 150 -447 C
ATOM 309 O ILE A 83 160.746 4.063 106.642 1.00 72.25 O
ANISOU 309 O ILE A 83 8312 10187 8952 -212 125 -377 O
ATOM 310 CB ILE A 83 163.223 4.313 108.866 1.00 69.66 C
ANISOU 310 CB ILE A 83 7904 9768 8796 -117 93 -292 C
ATOM 311 CG1 ILE A 83 163.206 4.532 110.394 1.00 68.81 C
ANISOU 311 CG1 ILE A 83 7863 9494 8789 -105 30 -220 C
ATOM 312 CG2 ILE A 83 163.096 5.660 108.119 1.00 70.17 C
ANISOU 312 CG2 ILE A 83 7940 9956 8765 -238 90 -181 C
ATOM 313 CD1 ILE A 83 164.544 4.997 111.018 1.00 74.04 C
ANISOU 313 CD1 ILE A 83 8448 10205 9479 -108 10 -157 C
ATOM 314 N CYS A 84 162.441 2.647 106.079 1.00 71.71 N
ANISOU 314 N CYS A 84 8124 10244 8877 -82 214 -568 N
ATOM 315 CA CYS A 84 162.201 2.572 104.639 1.00 72.68 C
ANISOU 315 CA CYS A 84 8211 10541 8863 -129 263 -636 C
ATOM 316 C CYS A 84 160.865 1.891 104.345 1.00 76.24 C
ANISOU 316 C CYS A 84 8758 10903 9306 -139 244 -714 C
ATOM 317 O CYS A 84 160.114 2.390 103.510 1.00 76.01 O
ANISOU 317 O CYS A 84 8737 10970 9173 -229 235 -677 O
ATOM 318 CB CYS A 84 163.348 1.858 103.935 1.00 74.71 C
ANISOU 318 CB CYS A 84 8366 10947 9075 -54 344 -769 C
ATOM 319 SG CYS A 84 164.080 2.800 102.575 1.00 79.98 S
ANISOU 319 SG CYS A 84 8902 11928 9558 -154 406 -718 S
ATOM 320 N SER A 85 160.567 0.761 105.025 1.00 72.50 N
ANISOU 320 N SER A 85 8355 10251 8941 -56 231 -810 N
ATOM 321 CA SER A 85 159.301 0.044 104.855 1.00 72.23 C
ANISOU 321 CA SER A 85 8413 10118 8913 -76 206 -882 C
ATOM 322 C SER A 85 158.148 0.896 105.397 1.00 74.80 C
ANISOU 322 C SER A 85 8797 10366 9257 -158 143 -737 C
ATOM 323 O SER A 85 157.068 0.909 104.804 1.00 74.56 O
ANISOU 323 O SER A 85 8798 10364 9169 -225 124 -742 O
ATOM 324 CB SER A 85 159.346 -1.317 105.541 1.00 76.05 C
ANISOU 324 CB SER A 85 8959 10415 9520 24 201 -998 C
ATOM 325 OG SER A 85 159.577 -1.189 106.934 1.00 84.34 O
ANISOU 325 OG SER A 85 10038 11314 10693 65 160 -903 O
ATOM 326 N LEU A 86 158.406 1.647 106.492 1.00 70.07 N
ANISOU 326 N LEU A 86 8205 9686 8734 -152 112 -611 N
ATOM 327 CA LEU A 86 157.454 2.569 107.113 1.00 68.69 C
ANISOU 327 CA LEU A 86 8078 9436 8586 -212 61 -477 C
ATOM 328 C LEU A 86 157.185 3.738 106.158 1.00 72.99 C
ANISOU 328 C LEU A 86 8578 10132 9022 -301 55 -383 C
ATOM 329 O LEU A 86 156.043 4.185 106.061 1.00 72.53 O
ANISOU 329 O LEU A 86 8553 10053 8954 -352 20 -319 O
ATOM 330 CB LEU A 86 157.990 3.059 108.480 1.00 67.85 C
ANISOU 330 CB LEU A 86 7990 9215 8573 -182 35 -389 C
ATOM 331 CG LEU A 86 157.132 4.031 109.320 1.00 71.36 C
ANISOU 331 CG LEU A 86 8489 9566 9057 -226 -8 -266 C
ATOM 332 CD1 LEU A 86 155.808 3.414 109.739 1.00 71.08 C
ANISOU 332 CD1 LEU A 86 8526 9415 9066 -226 -27 -292 C
ATOM 333 CD2 LEU A 86 157.882 4.470 110.560 1.00 72.83 C
ANISOU 333 CD2 LEU A 86 8690 9670 9313 -202 -29 -203 C
ATOM 334 N ALA A 87 158.224 4.192 105.422 1.00 70.21 N
ANISOU 334 N ALA A 87 8145 9942 8590 -320 89 -370 N
ATOM 335 CA ALA A 87 158.113 5.261 104.429 1.00 70.46 C
ANISOU 335 CA ALA A 87 8130 10133 8509 -414 83 -269 C
ATOM 336 C ALA A 87 157.273 4.793 103.240 1.00 74.93 C
ANISOU 336 C ALA A 87 8696 10806 8967 -456 89 -338 C
ATOM 337 O ALA A 87 156.458 5.571 102.748 1.00 74.38 O
ANISOU 337 O ALA A 87 8630 10787 8844 -530 49 -235 O
ATOM 338 CB ALA A 87 159.491 5.708 103.967 1.00 72.00 C
ANISOU 338 CB ALA A 87 8231 10485 8639 -431 125 -245 C
ATOM 339 N VAL A 88 157.443 3.511 102.812 1.00 72.26 N
ANISOU 339 N VAL A 88 8359 10493 8605 -408 133 -512 N
ATOM 340 CA VAL A 88 156.672 2.885 101.723 1.00 72.89 C
ANISOU 340 CA VAL A 88 8449 10666 8580 -452 137 -610 C
ATOM 341 C VAL A 88 155.201 2.840 102.152 1.00 75.81 C
ANISOU 341 C VAL A 88 8891 10906 9009 -481 72 -567 C
ATOM 342 O VAL A 88 154.340 3.288 101.399 1.00 75.66 O
ANISOU 342 O VAL A 88 8862 10981 8903 -561 36 -508 O
ATOM 343 CB VAL A 88 157.207 1.477 101.323 1.00 77.75 C
ANISOU 343 CB VAL A 88 9065 11295 9179 -382 197 -826 C
ATOM 344 CG1 VAL A 88 156.258 0.767 100.358 1.00 78.37 C
ANISOU 344 CG1 VAL A 88 9179 11433 9163 -437 189 -939 C
ATOM 345 CG2 VAL A 88 158.604 1.561 100.719 1.00 78.69 C
ANISOU 345 CG2 VAL A 88 9091 11588 9220 -354 272 -873 C
ATOM 346 N ALA A 89 154.939 2.343 103.384 1.00 71.40 N
ANISOU 346 N ALA A 89 8394 10142 8594 -420 55 -582 N
ATOM 347 CA ALA A 89 153.620 2.230 104.010 1.00 70.45 C
ANISOU 347 CA ALA A 89 8332 9888 8546 -440 4 -543 C
ATOM 348 C ALA A 89 152.922 3.594 104.115 1.00 74.06 C
ANISOU 348 C ALA A 89 8773 10368 8999 -491 -42 -366 C
ATOM 349 O ALA A 89 151.736 3.683 103.806 1.00 73.64 O
ANISOU 349 O ALA A 89 8725 10330 8926 -541 -81 -331 O
ATOM 350 CB ALA A 89 153.753 1.602 105.387 1.00 70.34 C
ANISOU 350 CB ALA A 89 8378 9673 8676 -366 3 -569 C
ATOM 351 N ASP A 90 153.664 4.654 104.515 1.00 70.56 N
ANISOU 351 N ASP A 90 8307 9927 8577 -481 -39 -255 N
ATOM 352 CA ASP A 90 153.158 6.029 104.624 1.00 69.92 C
ANISOU 352 CA ASP A 90 8217 9846 8504 -520 -82 -88 C
ATOM 353 C ASP A 90 152.773 6.584 103.245 1.00 74.14 C
ANISOU 353 C ASP A 90 8701 10561 8910 -600 -106 -26 C
ATOM 354 O ASP A 90 151.677 7.120 103.084 1.00 73.74 O
ANISOU 354 O ASP A 90 8649 10507 8862 -631 -156 64 O
ATOM 355 CB ASP A 90 154.208 6.944 105.281 1.00 71.42 C
ANISOU 355 CB ASP A 90 8400 9998 8739 -504 -75 -3 C
ATOM 356 CG ASP A 90 154.347 6.826 106.786 1.00 81.47 C
ANISOU 356 CG ASP A 90 9727 11089 10138 -441 -76 -9 C
ATOM 357 OD1 ASP A 90 153.358 6.436 107.450 1.00 81.60 O
ANISOU 357 OD1 ASP A 90 9791 10993 10219 -418 -90 -27 O
ATOM 358 OD2 ASP A 90 155.428 7.172 107.307 1.00 88.27 O
ANISOU 358 OD2 ASP A 90 10581 11931 11027 -425 -65 13 O
ATOM 359 N MET A 91 153.679 6.433 102.260 1.00 71.28 N
ANISOU 359 N MET A 91 8290 10364 8430 -631 -69 -72 N
ATOM 360 CA MET A 91 153.533 6.860 100.868 1.00 72.17 C
ANISOU 360 CA MET A 91 8351 10682 8389 -718 -83 -22 C
ATOM 361 C MET A 91 152.327 6.173 100.226 1.00 75.43 C
ANISOU 361 C MET A 91 8774 11140 8744 -754 -115 -86 C
ATOM 362 O MET A 91 151.456 6.862 99.708 1.00 75.30 O
ANISOU 362 O MET A 91 8739 11187 8685 -812 -174 32 O
ATOM 363 CB MET A 91 154.829 6.539 100.105 1.00 75.75 C
ANISOU 363 CB MET A 91 8751 11301 8730 -730 -15 -104 C
ATOM 364 CG MET A 91 154.782 6.779 98.618 1.00 81.24 C
ANISOU 364 CG MET A 91 9392 12236 9238 -825 -16 -80 C
ATOM 365 SD MET A 91 156.304 6.159 97.861 1.00 87.23 S
ANISOU 365 SD MET A 91 10083 13187 9872 -817 88 -222 S
ATOM 366 CE MET A 91 155.994 4.382 97.888 1.00 84.28 C
ANISOU 366 CE MET A 91 9760 12743 9521 -741 128 -486 C
ATOM 367 N LEU A 92 152.263 4.829 100.309 1.00 71.24 N
ANISOU 367 N LEU A 92 8276 10567 8226 -720 -83 -266 N
ATOM 368 CA LEU A 92 151.202 3.977 99.764 1.00 71.31 C
ANISOU 368 CA LEU A 92 8303 10604 8186 -763 -111 -357 C
ATOM 369 C LEU A 92 149.820 4.319 100.333 1.00 74.12 C
ANISOU 369 C LEU A 92 8674 10857 8630 -776 -180 -255 C
ATOM 370 O LEU A 92 148.839 4.214 99.604 1.00 74.50 O
ANISOU 370 O LEU A 92 8703 10997 8605 -845 -229 -244 O
ATOM 371 CB LEU A 92 151.531 2.505 100.055 1.00 71.34 C
ANISOU 371 CB LEU A 92 8357 10517 8234 -710 -64 -564 C
ATOM 372 CG LEU A 92 151.883 1.578 98.884 1.00 77.36 C
ANISOU 372 CG LEU A 92 9114 11423 8857 -741 -25 -741 C
ATOM 373 CD1 LEU A 92 152.863 2.217 97.906 1.00 80.70 C
ANISOU 373 CD1 LEU A 92 9467 12064 9131 -771 18 -713 C
ATOM 374 CD2 LEU A 92 152.489 0.297 99.403 1.00 77.46 C
ANISOU 374 CD2 LEU A 92 9177 11298 8955 -654 26 -925 C
ATOM 375 N VAL A 93 149.744 4.730 101.617 1.00 69.08 N
ANISOU 375 N VAL A 93 8063 10042 8140 -711 -182 -182 N
ATOM 376 CA VAL A 93 148.498 5.117 102.285 1.00 68.21 C
ANISOU 376 CA VAL A 93 7959 9837 8123 -707 -231 -88 C
ATOM 377 C VAL A 93 147.991 6.444 101.678 1.00 73.07 C
ANISOU 377 C VAL A 93 8520 10550 8693 -746 -287 88 C
ATOM 378 O VAL A 93 146.832 6.507 101.268 1.00 73.21 O
ANISOU 378 O VAL A 93 8506 10621 8691 -786 -342 136 O
ATOM 379 CB VAL A 93 148.674 5.180 103.832 1.00 70.61 C
ANISOU 379 CB VAL A 93 8311 9940 8580 -626 -207 -75 C
ATOM 380 CG1 VAL A 93 147.786 6.234 104.481 1.00 69.83 C
ANISOU 380 CG1 VAL A 93 8200 9770 8564 -607 -244 69 C
ATOM 381 CG2 VAL A 93 148.422 3.820 104.463 1.00 70.20 C
ANISOU 381 CG2 VAL A 93 8309 9775 8590 -606 -187 -209 C
ATOM 382 N SER A 94 148.864 7.474 101.592 1.00 69.96 N
ANISOU 382 N SER A 94 8113 10183 8284 -740 -280 188 N
ATOM 383 CA SER A 94 148.523 8.796 101.056 1.00 70.42 C
ANISOU 383 CA SER A 94 8132 10310 8314 -775 -337 371 C
ATOM 384 C SER A 94 148.311 8.776 99.547 1.00 75.52 C
ANISOU 384 C SER A 94 8727 11177 8791 -868 -373 396 C
ATOM 385 O SER A 94 147.488 9.550 99.053 1.00 75.78 O
ANISOU 385 O SER A 94 8722 11268 8805 -901 -444 539 O
ATOM 386 CB SER A 94 149.598 9.816 101.404 1.00 74.07 C
ANISOU 386 CB SER A 94 8606 10728 8809 -759 -320 464 C
ATOM 387 OG SER A 94 149.459 10.287 102.734 1.00 82.91 O
ANISOU 387 OG SER A 94 9769 11650 10083 -685 -317 499 O
ATOM 388 N VAL A 95 149.061 7.922 98.816 1.00 72.48 N
ANISOU 388 N VAL A 95 8339 10920 8281 -907 -325 260 N
ATOM 389 CA VAL A 95 148.939 7.769 97.363 1.00 73.61 C
ANISOU 389 CA VAL A 95 8439 11294 8236 -1004 -348 254 C
ATOM 390 C VAL A 95 147.584 7.131 97.072 1.00 77.22 C
ANISOU 390 C VAL A 95 8888 11775 8675 -1040 -405 212 C
ATOM 391 O VAL A 95 146.872 7.623 96.198 1.00 78.04 O
ANISOU 391 O VAL A 95 8947 12019 8687 -1111 -477 321 O
ATOM 392 CB VAL A 95 150.123 6.982 96.731 1.00 78.34 C
ANISOU 392 CB VAL A 95 9036 12019 8709 -1024 -267 93 C
ATOM 393 CG1 VAL A 95 149.769 6.400 95.360 1.00 79.78 C
ANISOU 393 CG1 VAL A 95 9194 12423 8697 -1120 -282 14 C
ATOM 394 CG2 VAL A 95 151.358 7.864 96.628 1.00 78.26 C
ANISOU 394 CG2 VAL A 95 9000 12070 8667 -1030 -230 187 C
ATOM 395 N SER A 96 147.213 6.075 97.831 1.00 72.26 N
ANISOU 395 N SER A 96 8303 11011 8142 -996 -380 68 N
ATOM 396 CA SER A 96 145.930 5.386 97.681 1.00 72.07 C
ANISOU 396 CA SER A 96 8272 10995 8118 -1039 -432 22 C
ATOM 397 C SER A 96 144.771 6.297 98.069 1.00 74.97 C
ANISOU 397 C SER A 96 8594 11316 8577 -1025 -506 201 C
ATOM 398 O SER A 96 143.775 6.316 97.350 1.00 75.87 O
ANISOU 398 O SER A 96 8655 11548 8622 -1093 -578 252 O
ATOM 399 CB SER A 96 145.890 4.105 98.504 1.00 74.63 C
ANISOU 399 CB SER A 96 8658 11163 8537 -1000 -388 -154 C
ATOM 400 OG SER A 96 146.824 3.149 98.036 1.00 83.45 O
ANISOU 400 OG SER A 96 9813 12323 9571 -1007 -327 -336 O
ATOM 401 N LEU A 97 144.907 7.074 99.168 1.00 69.58 N
ANISOU 401 N LEU A 97 7925 10471 8043 -935 -489 295 N
ATOM 402 CA LEU A 97 143.878 8.020 99.614 1.00 68.92 C
ANISOU 402 CA LEU A 97 7798 10328 8063 -898 -546 457 C
ATOM 403 C LEU A 97 143.737 9.186 98.637 1.00 73.47 C
ANISOU 403 C LEU A 97 8317 11038 8560 -937 -617 639 C
ATOM 404 O LEU A 97 142.624 9.664 98.427 1.00 74.23 O
ANISOU 404 O LEU A 97 8352 11170 8682 -940 -691 756 O
ATOM 405 CB LEU A 97 144.166 8.551 101.020 1.00 67.63 C
ANISOU 405 CB LEU A 97 7675 9957 8064 -793 -502 489 C
ATOM 406 CG LEU A 97 143.749 7.663 102.188 1.00 71.35 C
ANISOU 406 CG LEU A 97 8182 10282 8646 -748 -459 378 C
ATOM 407 CD1 LEU A 97 144.553 7.992 103.417 1.00 70.21 C
ANISOU 407 CD1 LEU A 97 8100 9968 8610 -665 -401 370 C
ATOM 408 CD2 LEU A 97 142.267 7.806 102.494 1.00 73.96 C
ANISOU 408 CD2 LEU A 97 8453 10599 9050 -736 -504 446 C
ATOM 409 N GLY A 98 144.854 9.610 98.043 1.00 69.55 N
ANISOU 409 N GLY A 98 7836 10622 7969 -969 -597 667 N
ATOM 410 CA GLY A 98 144.892 10.673 97.043 1.00 70.14 C
ANISOU 410 CA GLY A 98 7866 10835 7950 -1026 -663 846 C
ATOM 411 C GLY A 98 144.270 10.226 95.734 1.00 74.51 C
ANISOU 411 C GLY A 98 8368 11615 8329 -1133 -724 843 C
ATOM 412 O GLY A 98 143.439 10.940 95.168 1.00 75.08 O
ANISOU 412 O GLY A 98 8380 11768 8378 -1162 -818 1008 O
ATOM 413 N PHE A 99 144.650 9.017 95.269 1.00 70.74 N
ANISOU 413 N PHE A 99 7912 11234 7732 -1189 -675 649 N
ATOM 414 CA PHE A 99 144.145 8.382 94.048 1.00 71.91 C
ANISOU 414 CA PHE A 99 8027 11601 7696 -1302 -722 594 C
ATOM 415 C PHE A 99 142.648 8.099 94.168 1.00 76.44 C
ANISOU 415 C PHE A 99 8555 12162 8326 -1314 -803 619 C
ATOM 416 O PHE A 99 141.921 8.304 93.198 1.00 77.62 O
ANISOU 416 O PHE A 99 8644 12489 8359 -1399 -893 710 O
ATOM 417 CB PHE A 99 144.922 7.085 93.752 1.00 73.74 C
ANISOU 417 CB PHE A 99 8309 11886 7824 -1334 -638 346 C
ATOM 418 CG PHE A 99 144.459 6.283 92.558 1.00 76.80 C
ANISOU 418 CG PHE A 99 8680 12482 8017 -1453 -675 242 C
ATOM 419 CD1 PHE A 99 144.720 6.718 91.263 1.00 81.46 C
ANISOU 419 CD1 PHE A 99 9233 13322 8395 -1555 -708 313 C
ATOM 420 CD2 PHE A 99 143.813 5.066 92.727 1.00 78.87 C
ANISOU 420 CD2 PHE A 99 8971 12695 8299 -1475 -677 65 C
ATOM 421 CE1 PHE A 99 144.303 5.968 90.159 1.00 83.96 C
ANISOU 421 CE1 PHE A 99 9542 13844 8516 -1673 -743 204 C
ATOM 422 CE2 PHE A 99 143.399 4.315 91.623 1.00 83.29 C
ANISOU 422 CE2 PHE A 99 9526 13444 8675 -1595 -716 -46 C
ATOM 423 CZ PHE A 99 143.648 4.770 90.347 1.00 82.96 C
ANISOU 423 CZ PHE A 99 9448 13657 8417 -1692 -747 18 C
ATOM 424 N GLU A 100 142.194 7.652 95.360 1.00 71.91 N
ANISOU 424 N GLU A 100 8003 11392 7927 -1234 -772 550 N
ATOM 425 CA GLU A 100 140.790 7.360 95.670 1.00 72.03 C
ANISOU 425 CA GLU A 100 7967 11381 8021 -1238 -833 571 C
ATOM 426 C GLU A 100 139.940 8.615 95.507 1.00 77.08 C
ANISOU 426 C GLU A 100 8519 12058 8710 -1211 -926 809 C
ATOM 427 O GLU A 100 138.850 8.540 94.947 1.00 77.80 O
ANISOU 427 O GLU A 100 8532 12272 8758 -1269 -1015 870 O
ATOM 428 CB GLU A 100 140.666 6.823 97.102 1.00 71.88 C
ANISOU 428 CB GLU A 100 7991 11137 8182 -1150 -766 476 C
ATOM 429 CG GLU A 100 139.355 6.128 97.423 1.00 80.45 C
ANISOU 429 CG GLU A 100 9031 12208 9327 -1180 -807 441 C
ATOM 430 CD GLU A 100 139.242 5.660 98.861 1.00 94.79 C
ANISOU 430 CD GLU A 100 10889 13814 11312 -1101 -738 368 C
ATOM 431 OE1 GLU A 100 139.745 6.370 99.763 1.00 86.64 O
ANISOU 431 OE1 GLU A 100 9885 12641 10392 -996 -688 425 O
ATOM 432 OE2 GLU A 100 138.639 4.587 99.088 1.00 86.75 O
ANISOU 432 OE2 GLU A 100 9878 12774 10311 -1155 -739 257 O
ATOM 433 N THR A 101 140.461 9.766 95.974 1.00 73.54 N
ANISOU 433 N THR A 101 8085 11503 8355 -1124 -911 943 N
ATOM 434 CA THR A 101 139.807 11.070 95.882 1.00 74.28 C
ANISOU 434 CA THR A 101 8110 11592 8520 -1077 -994 1172 C
ATOM 435 C THR A 101 139.664 11.465 94.402 1.00 80.88 C
ANISOU 435 C THR A 101 8891 12665 9173 -1186 -1093 1301 C
ATOM 436 O THR A 101 138.608 11.962 94.019 1.00 81.61 O
ANISOU 436 O THR A 101 8895 12830 9281 -1188 -1195 1452 O
ATOM 437 CB THR A 101 140.582 12.098 96.708 1.00 80.66 C
ANISOU 437 CB THR A 101 8973 12215 9460 -974 -948 1252 C
ATOM 438 OG1 THR A 101 140.760 11.582 98.026 1.00 78.50 O
ANISOU 438 OG1 THR A 101 8755 11752 9321 -893 -857 1114 O
ATOM 439 CG2 THR A 101 139.868 13.421 96.799 1.00 79.87 C
ANISOU 439 CG2 THR A 101 8816 12057 9473 -901 -1027 1471 C
ATOM 440 N ILE A 102 140.702 11.198 93.575 1.00 78.66 N
ANISOU 440 N ILE A 102 8656 12517 8715 -1276 -1060 1240 N
ATOM 441 CA ILE A 102 140.701 11.459 92.129 1.00 80.67 C
ANISOU 441 CA ILE A 102 8868 13025 8758 -1400 -1141 1342 C
ATOM 442 C ILE A 102 139.633 10.564 91.469 1.00 86.12 C
ANISOU 442 C ILE A 102 9500 13879 9341 -1492 -1210 1271 C
ATOM 443 O ILE A 102 138.848 11.063 90.663 1.00 87.44 O
ANISOU 443 O ILE A 102 9588 14201 9434 -1549 -1328 1436 O
ATOM 444 CB ILE A 102 142.125 11.262 91.515 1.00 84.10 C
ANISOU 444 CB ILE A 102 9363 13567 9026 -1471 -1063 1257 C
ATOM 445 CG1 ILE A 102 143.068 12.406 91.940 1.00 83.98 C
ANISOU 445 CG1 ILE A 102 9381 13433 9096 -1412 -1031 1394 C
ATOM 446 CG2 ILE A 102 142.091 11.135 89.981 1.00 87.09 C
ANISOU 446 CG2 ILE A 102 9704 14247 9140 -1623 -1126 1293 C
ATOM 447 CD1 ILE A 102 144.542 12.012 92.122 1.00 91.71 C
ANISOU 447 CD1 ILE A 102 10425 14396 10026 -1416 -908 1247 C
ATOM 448 N VAL A 103 139.577 9.267 91.859 1.00 82.27 N
ANISOU 448 N VAL A 103 9053 13348 8859 -1507 -1145 1035 N
ATOM 449 CA VAL A 103 138.617 8.276 91.350 1.00 83.30 C
ANISOU 449 CA VAL A 103 9144 13607 8900 -1606 -1204 934 C
ATOM 450 C VAL A 103 137.172 8.708 91.705 1.00 88.33 C
ANISOU 450 C VAL A 103 9675 14217 9669 -1567 -1302 1086 C
ATOM 451 O VAL A 103 136.325 8.716 90.814 1.00 89.53 O
ANISOU 451 O VAL A 103 9746 14562 9710 -1661 -1415 1168 O
ATOM 452 CB VAL A 103 138.943 6.830 91.841 1.00 86.26 C
ANISOU 452 CB VAL A 103 9600 13888 9287 -1619 -1109 653 C
ATOM 453 CG1 VAL A 103 137.813 5.853 91.520 1.00 87.13 C
ANISOU 453 CG1 VAL A 103 9672 14084 9348 -1720 -1176 559 C
ATOM 454 CG2 VAL A 103 140.252 6.326 91.241 1.00 86.24 C
ANISOU 454 CG2 VAL A 103 9679 13963 9125 -1665 -1024 495 C
ATOM 455 N ILE A 104 136.912 9.102 92.976 1.00 84.30 N
ANISOU 455 N ILE A 104 9158 13484 9387 -1428 -1261 1128 N
ATOM 456 CA ILE A 104 135.593 9.543 93.460 1.00 84.82 C
ANISOU 456 CA ILE A 104 9116 13511 9602 -1364 -1332 1261 C
ATOM 457 C ILE A 104 135.140 10.816 92.704 1.00 91.96 C
ANISOU 457 C ILE A 104 9929 14529 10482 -1353 -1452 1525 C
ATOM 458 O ILE A 104 134.006 10.843 92.216 1.00 92.92 O
ANISOU 458 O ILE A 104 9936 14787 10581 -1395 -1562 1622 O
ATOM 459 CB ILE A 104 135.584 9.726 95.009 1.00 86.05 C
ANISOU 459 CB ILE A 104 9299 13406 9991 -1214 -1241 1231 C
ATOM 460 CG1 ILE A 104 135.620 8.351 95.715 1.00 85.38 C
ANISOU 460 CG1 ILE A 104 9273 13234 9933 -1243 -1156 1001 C
ATOM 461 CG2 ILE A 104 134.370 10.548 95.494 1.00 87.21 C
ANISOU 461 CG2 ILE A 104 9325 13511 10300 -1113 -1303 1403 C
ATOM 462 CD1 ILE A 104 136.263 8.345 97.099 1.00 90.53 C
ANISOU 462 CD1 ILE A 104 10008 13644 10744 -1125 -1038 922 C
ATOM 463 N THR A 105 136.030 11.833 92.573 1.00 89.72 N
ANISOU 463 N THR A 105 9694 14196 10199 -1306 -1440 1645 N
ATOM 464 CA THR A 105 135.752 13.096 91.863 1.00 91.66 C
ANISOU 464 CA THR A 105 9873 14523 10429 -1296 -1555 1910 C
ATOM 465 C THR A 105 135.409 12.814 90.380 1.00 98.85 C
ANISOU 465 C THR A 105 10727 15734 11098 -1460 -1667 1967 C
ATOM 466 O THR A 105 134.494 13.444 89.843 1.00100.02 O
ANISOU 466 O THR A 105 10767 15988 11247 -1464 -1799 2169 O
ATOM 467 CB THR A 105 136.930 14.082 92.015 1.00 99.35 C
ANISOU 467 CB THR A 105 10932 15380 11436 -1244 -1509 2000 C
ATOM 468 OG1 THR A 105 137.256 14.210 93.400 1.00 97.57 O
ANISOU 468 OG1 THR A 105 10767 14891 11414 -1109 -1404 1917 O
ATOM 469 CG2 THR A 105 136.622 15.469 91.453 1.00 99.45 C
ANISOU 469 CG2 THR A 105 10890 15421 11476 -1217 -1629 2291 C
ATOM 470 N LEU A 106 136.113 11.844 89.748 1.00 96.41 N
ANISOU 470 N LEU A 106 10486 15561 10586 -1591 -1616 1783 N
ATOM 471 CA LEU A 106 135.887 11.419 88.361 1.00 98.62 C
ANISOU 471 CA LEU A 106 10730 16135 10606 -1762 -1705 1787 C
ATOM 472 C LEU A 106 134.487 10.822 88.176 1.00104.57 C
ANISOU 472 C LEU A 106 11379 16996 11357 -1817 -1805 1777 C
ATOM 473 O LEU A 106 133.867 11.043 87.135 1.00106.12 O
ANISOU 473 O LEU A 106 11494 17421 11408 -1919 -1938 1912 O
ATOM 474 CB LEU A 106 136.947 10.391 87.922 1.00 98.41 C
ANISOU 474 CB LEU A 106 10807 16194 10390 -1865 -1603 1541 C
ATOM 475 CG LEU A 106 138.207 10.941 87.259 1.00103.50 C
ANISOU 475 CG LEU A 106 11510 16929 10885 -1909 -1560 1594 C
ATOM 476 CD1 LEU A 106 139.377 9.998 87.455 1.00102.58 C
ANISOU 476 CD1 LEU A 106 11498 16773 10704 -1922 -1409 1325 C
ATOM 477 CD2 LEU A 106 137.989 11.184 85.772 1.00108.66 C
ANISOU 477 CD2 LEU A 106 12114 17897 11277 -2066 -1675 1720 C
ATOM 478 N LEU A 107 133.995 10.074 89.186 1.00100.85 N
ANISOU 478 N LEU A 107 10907 16371 11042 -1759 -1745 1626 N
ATOM 479 CA LEU A 107 132.672 9.437 89.170 1.00102.02 C
ANISOU 479 CA LEU A 107 10950 16602 11209 -1814 -1826 1603 C
ATOM 480 C LEU A 107 131.561 10.462 89.384 1.00107.84 C
ANISOU 480 C LEU A 107 11540 17333 12101 -1715 -1934 1857 C
ATOM 481 O LEU A 107 130.479 10.311 88.812 1.00109.18 O
ANISOU 481 O LEU A 107 11588 17681 12216 -1793 -2058 1937 O
ATOM 482 CB LEU A 107 132.574 8.320 90.223 1.00100.55 C
ANISOU 482 CB LEU A 107 10815 16246 11143 -1791 -1721 1371 C
ATOM 483 CG LEU A 107 133.617 7.203 90.137 1.00104.43 C
ANISOU 483 CG LEU A 107 11452 16709 11519 -1866 -1612 1103 C
ATOM 484 CD1 LEU A 107 133.592 6.337 91.378 1.00103.02 C
ANISOU 484 CD1 LEU A 107 11327 16308 11506 -1807 -1508 925 C
ATOM 485 CD2 LEU A 107 133.486 6.396 88.851 1.00108.43 C
ANISOU 485 CD2 LEU A 107 11965 17465 11770 -2058 -1682 998 C
ATOM 486 N ASN A 108 131.832 11.506 90.196 1.00104.24 N
ANISOU 486 N ASN A 108 11093 16674 11839 -1543 -1889 1981 N
ATOM 487 CA ASN A 108 130.898 12.603 90.462 1.00105.33 C
ANISOU 487 CA ASN A 108 11102 16769 12148 -1415 -1977 2220 C
ATOM 488 C ASN A 108 130.799 13.515 89.231 1.00112.12 C
ANISOU 488 C ASN A 108 11904 17816 12880 -1469 -2125 2467 C
ATOM 489 O ASN A 108 129.795 14.209 89.059 1.00113.26 O
ANISOU 489 O ASN A 108 11911 18014 13110 -1409 -2245 2674 O
ATOM 490 CB ASN A 108 131.325 13.403 91.701 1.00105.20 C
ANISOU 490 CB ASN A 108 11139 16464 12367 -1220 -1876 2247 C
ATOM 491 CG ASN A 108 131.423 12.608 92.989 1.00129.19 C
ANISOU 491 CG ASN A 108 14234 19318 15536 -1159 -1734 2029 C
ATOM 492 OD1 ASN A 108 132.325 12.825 93.803 1.00123.31 O
ANISOU 492 OD1 ASN A 108 13600 18372 14880 -1074 -1621 1957 O
ATOM 493 ND2 ASN A 108 130.496 11.682 93.222 1.00121.50 N
ANISOU 493 ND2 ASN A 108 13182 18407 14575 -1209 -1742 1931 N
ATOM 494 N SER A 109 131.842 13.494 88.374 1.00109.47 N
ANISOU 494 N SER A 109 11668 17587 12337 -1583 -2115 2448 N
ATOM 495 CA SER A 109 131.927 14.247 87.122 1.00111.56 C
ANISOU 495 CA SER A 109 11901 18055 12433 -1670 -2245 2670 C
ATOM 496 C SER A 109 131.211 13.492 85.990 1.00117.67 C
ANISOU 496 C SER A 109 12595 19139 12974 -1855 -2363 2652 C
ATOM 497 O SER A 109 130.515 14.117 85.188 1.00119.49 O
ANISOU 497 O SER A 109 12717 19540 13144 -1892 -2522 2884 O
ATOM 498 CB SER A 109 133.385 14.500 86.749 1.00114.76 C
ANISOU 498 CB SER A 109 12442 18455 12706 -1722 -2167 2644 C
ATOM 499 OG SER A 109 134.078 15.182 87.781 1.00122.03 O
ANISOU 499 OG SER A 109 13438 19095 13831 -1570 -2065 2656 O
ATOM 500 N THR A 110 131.380 12.151 85.936 1.00113.63 N
ANISOU 500 N THR A 110 12141 18694 12339 -1971 -2291 2376 N
ATOM 501 CA THR A 110 130.767 11.274 84.932 1.00143.59 C
ANISOU 501 CA THR A 110 15884 22766 15907 -2162 -2388 2303 C
ATOM 502 C THR A 110 129.411 10.776 85.431 1.00162.99 C
ANISOU 502 C THR A 110 18213 25217 18497 -2146 -2448 2283 C
ATOM 503 O THR A 110 128.540 10.443 84.630 1.00123.87 O
ANISOU 503 O THR A 110 13159 20498 13409 -2279 -2584 2329 O
ATOM 504 CB THR A 110 131.697 10.094 84.585 1.00151.23 C
ANISOU 504 CB THR A 110 16991 23795 16674 -2295 -2278 2005 C
ATOM 505 OG1 THR A 110 132.031 9.379 85.775 1.00148.60 O
ANISOU 505 OG1 THR A 110 16737 23210 16512 -2204 -2127 1780 O
ATOM 506 CG2 THR A 110 132.964 10.531 83.854 1.00150.01 C
ANISOU 506 CG2 THR A 110 16935 23727 16335 -2345 -2232 2032 C
ATOM 507 N ASP A 113 127.340 5.016 87.896 1.00141.28 N
ANISOU 507 N ASP A 113 15524 22214 15942 -2459 -2231 1253 N
ATOM 508 CA ASP A 113 127.881 4.130 88.925 1.00139.14 C
ANISOU 508 CA ASP A 113 15382 21699 15787 -2420 -2079 1026 C
ATOM 509 C ASP A 113 129.010 3.237 88.372 1.00142.54 C
ANISOU 509 C ASP A 113 15997 22126 16036 -2522 -2007 778 C
ATOM 510 O ASP A 113 129.820 2.744 89.158 1.00140.46 O
ANISOU 510 O ASP A 113 15862 21645 15863 -2451 -1870 616 O
ATOM 511 CB ASP A 113 126.760 3.264 89.534 1.00141.36 C
ANISOU 511 CB ASP A 113 15582 21954 16175 -2492 -2104 959 C
ATOM 512 CG ASP A 113 127.172 2.473 90.763 1.00148.87 C
ANISOU 512 CG ASP A 113 16645 22638 17281 -2436 -1957 776 C
ATOM 513 OD1 ASP A 113 127.422 3.099 91.817 1.00147.50 O
ANISOU 513 OD1 ASP A 113 16470 22278 17294 -2254 -1862 846 O
ATOM 514 OD2 ASP A 113 127.239 1.229 90.672 1.00154.99 O
ANISOU 514 OD2 ASP A 113 17513 23387 17991 -2576 -1941 562 O
ATOM 515 N ALA A 114 129.047 3.025 87.029 1.00140.61 N
ANISOU 515 N ALA A 114 15761 22128 15535 -2685 -2100 749 N
ATOM 516 CA ALA A 114 130.016 2.210 86.268 1.00140.61 C
ANISOU 516 CA ALA A 114 15917 22184 15322 -2797 -2047 513 C
ATOM 517 C ALA A 114 130.082 0.732 86.755 1.00143.16 C
ANISOU 517 C ALA A 114 16355 22353 15687 -2871 -1974 220 C
ATOM 518 O ALA A 114 131.093 0.052 86.543 1.00142.49 O
ANISOU 518 O ALA A 114 16421 22208 15510 -2891 -1879 -1 O
ATOM 519 CB ALA A 114 131.403 2.851 86.295 1.00140.05 C
ANISOU 519 CB ALA A 114 15946 22036 15232 -2674 -1932 521 C
ATOM 520 N GLN A 115 128.970 0.241 87.357 1.00139.10 N
ANISOU 520 N GLN A 115 15760 21785 15306 -2917 -2025 228 N
ATOM 521 CA GLN A 115 128.744 -1.115 87.881 1.00138.32 C
ANISOU 521 CA GLN A 115 15743 21539 15273 -3006 -1987 0 C
ATOM 522 C GLN A 115 129.831 -1.560 88.900 1.00138.47 C
ANISOU 522 C GLN A 115 15918 21257 15437 -2871 -1815 -159 C
ATOM 523 O GLN A 115 130.226 -0.766 89.758 1.00136.12 O
ANISOU 523 O GLN A 115 15603 20819 15297 -2689 -1736 -37 O
ATOM 524 CB GLN A 115 128.603 -2.133 86.729 1.00141.99 C
ANISOU 524 CB GLN A 115 16275 22174 15503 -3234 -2066 -199 C
ATOM 525 N SER A 116 130.278 -2.833 88.813 1.00134.19 N
ANISOU 525 N SER A 116 15525 20616 14845 -2962 -1767 -430 N
ATOM 526 CA SER A 116 131.255 -3.478 89.694 1.00131.72 C
ANISOU 526 CA SER A 116 15364 20024 14658 -2858 -1622 -604 C
ATOM 527 C SER A 116 132.668 -2.877 89.614 1.00132.70 C
ANISOU 527 C SER A 116 15568 20108 14745 -2708 -1511 -617 C
ATOM 528 O SER A 116 133.430 -3.041 90.569 1.00130.50 O
ANISOU 528 O SER A 116 15371 19597 14616 -2575 -1394 -678 O
ATOM 529 CB SER A 116 131.335 -4.970 89.384 1.00136.54 C
ANISOU 529 CB SER A 116 16111 20565 15202 -3006 -1622 -887 C
ATOM 530 OG SER A 116 131.739 -5.205 88.045 1.00147.02 O
ANISOU 530 OG SER A 116 17495 22088 16277 -3116 -1656 -1022 O
ATOM 531 N PHE A 117 133.023 -2.207 88.490 1.00129.01 N
ANISOU 531 N PHE A 117 15072 19871 14075 -2738 -1549 -557 N
ATOM 532 CA PHE A 117 134.344 -1.603 88.258 1.00127.45 C
ANISOU 532 CA PHE A 117 14934 19681 13812 -2625 -1452 -558 C
ATOM 533 C PHE A 117 134.776 -0.686 89.413 1.00126.88 C
ANISOU 533 C PHE A 117 14835 19422 13950 -2425 -1372 -396 C
ATOM 534 O PHE A 117 135.902 -0.813 89.891 1.00125.15 O
ANISOU 534 O PHE A 117 14712 19052 13789 -2317 -1251 -494 O
ATOM 535 CB PHE A 117 134.371 -0.824 86.926 1.00131.03 C
ANISOU 535 CB PHE A 117 15322 20440 14023 -2705 -1532 -442 C
ATOM 536 CG PHE A 117 135.723 -0.265 86.534 1.00132.40 C
ANISOU 536 CG PHE A 117 15552 20660 14094 -2624 -1436 -449 C
ATOM 537 CD1 PHE A 117 136.647 -1.048 85.852 1.00136.65 C
ANISOU 537 CD1 PHE A 117 16203 21254 14462 -2675 -1360 -697 C
ATOM 538 CD2 PHE A 117 136.062 1.052 86.828 1.00133.60 C
ANISOU 538 CD2 PHE A 117 15639 20805 14318 -2500 -1422 -208 C
ATOM 539 CE1 PHE A 117 137.895 -0.530 85.487 1.00137.39 C
ANISOU 539 CE1 PHE A 117 16331 21414 14458 -2605 -1266 -698 C
ATOM 540 CE2 PHE A 117 137.312 1.567 86.467 1.00136.25 C
ANISOU 540 CE2 PHE A 117 16020 21192 14558 -2443 -1336 -206 C
ATOM 541 CZ PHE A 117 138.218 0.774 85.796 1.00135.29 C
ANISOU 541 CZ PHE A 117 15995 21145 14263 -2497 -1257 -447 C
ATOM 542 N THR A 118 133.882 0.215 89.860 1.00121.34 N
ANISOU 542 N THR A 118 14003 18734 13366 -2377 -1439 -156 N
ATOM 543 CA THR A 118 134.141 1.174 90.940 1.00118.29 C
ANISOU 543 CA THR A 118 13585 18181 13177 -2195 -1376 5 C
ATOM 544 C THR A 118 134.314 0.474 92.286 1.00118.20 C
ANISOU 544 C THR A 118 13647 17897 13368 -2113 -1278 -110 C
ATOM 545 O THR A 118 135.180 0.876 93.062 1.00116.01 O
ANISOU 545 O THR A 118 13422 17458 13198 -1973 -1180 -96 O
ATOM 546 CB THR A 118 133.030 2.220 91.012 1.00126.66 C
ANISOU 546 CB THR A 118 14484 19332 14308 -2167 -1478 268 C
ATOM 547 OG1 THR A 118 131.779 1.576 91.260 1.00126.92 O
ANISOU 547 OG1 THR A 118 14442 19381 14401 -2255 -1548 254 O
ATOM 548 CG2 THR A 118 132.949 3.048 89.754 1.00126.77 C
ANISOU 548 CG2 THR A 118 14428 19601 14138 -2229 -1579 420 C
ATOM 549 N VAL A 119 133.502 -0.571 92.552 1.00113.65 N
ANISOU 549 N VAL A 119 13074 17272 12835 -2213 -1310 -217 N
ATOM 550 CA VAL A 119 133.551 -1.373 93.780 1.00111.48 C
ANISOU 550 CA VAL A 119 12871 16750 12738 -2167 -1232 -323 C
ATOM 551 C VAL A 119 134.886 -2.146 93.807 1.00112.73 C
ANISOU 551 C VAL A 119 13192 16772 12866 -2131 -1130 -540 C
ATOM 552 O VAL A 119 135.548 -2.174 94.846 1.00110.65 O
ANISOU 552 O VAL A 119 12991 16304 12746 -2007 -1035 -560 O
ATOM 553 CB VAL A 119 132.313 -2.310 93.914 1.00116.60 C
ANISOU 553 CB VAL A 119 13478 17405 13421 -2313 -1306 -372 C
ATOM 554 CG1 VAL A 119 132.367 -3.137 95.199 1.00115.26 C
ANISOU 554 CG1 VAL A 119 13385 16978 13430 -2276 -1228 -462 C
ATOM 555 CG2 VAL A 119 131.009 -1.515 93.853 1.00117.15 C
ANISOU 555 CG2 VAL A 119 13362 17630 13520 -2337 -1407 -152 C
ATOM 556 N ASN A 120 135.294 -2.719 92.650 1.00109.06 N
ANISOU 556 N ASN A 120 12791 16436 12212 -2235 -1149 -698 N
ATOM 557 CA ASN A 120 136.548 -3.462 92.484 1.00107.89 C
ANISOU 557 CA ASN A 120 12785 16194 12017 -2200 -1054 -918 C
ATOM 558 C ASN A 120 137.758 -2.558 92.721 1.00107.59 C
ANISOU 558 C ASN A 120 12757 16127 11997 -2042 -961 -846 C
ATOM 559 O ASN A 120 138.684 -2.969 93.418 1.00106.11 O
ANISOU 559 O ASN A 120 12657 15752 11907 -1939 -863 -951 O
ATOM 560 CB ASN A 120 136.630 -4.102 91.093 1.00111.61 C
ANISOU 560 CB ASN A 120 13300 16851 12256 -2345 -1097 -1092 C
ATOM 561 CG ASN A 120 135.800 -5.351 90.929 1.00138.57 C
ANISOU 561 CG ASN A 120 16762 20226 15661 -2502 -1162 -1253 C
ATOM 562 OD1 ASN A 120 135.977 -6.350 91.638 1.00133.77 O
ANISOU 562 OD1 ASN A 120 16256 19390 15181 -2487 -1115 -1402 O
ATOM 563 ND2 ASN A 120 134.912 -5.345 89.946 1.00132.53 N
ANISOU 563 ND2 ASN A 120 15931 19687 14736 -2666 -1278 -1229 N
ATOM 564 N ILE A 121 137.736 -1.327 92.165 1.00102.18 N
ANISOU 564 N ILE A 121 11978 15621 11223 -2026 -999 -657 N
ATOM 565 CA ILE A 121 138.802 -0.332 92.313 1.00 99.93 C
ANISOU 565 CA ILE A 121 11691 15328 10947 -1900 -928 -558 C
ATOM 566 C ILE A 121 138.824 0.163 93.777 1.00 99.48 C
ANISOU 566 C ILE A 121 11625 15047 11126 -1757 -879 -443 C
ATOM 567 O ILE A 121 139.911 0.321 94.335 1.00 97.86 O
ANISOU 567 O ILE A 121 11477 14721 10986 -1646 -787 -474 O
ATOM 568 CB ILE A 121 138.651 0.812 91.255 1.00104.04 C
ANISOU 568 CB ILE A 121 12120 16103 11307 -1948 -1001 -373 C
ATOM 569 CG1 ILE A 121 138.964 0.319 89.806 1.00106.65 C
ANISOU 569 CG1 ILE A 121 12480 16669 11374 -2081 -1021 -512 C
ATOM 570 CG2 ILE A 121 139.445 2.084 91.594 1.00103.39 C
ANISOU 570 CG2 ILE A 121 12013 15990 11280 -1824 -954 -199 C
ATOM 571 CD1 ILE A 121 140.416 -0.281 89.498 1.00114.28 C
ANISOU 571 CD1 ILE A 121 13551 17621 12249 -2045 -897 -731 C
ATOM 572 N ASP A 122 137.636 0.333 94.409 1.00 93.95 N
ANISOU 572 N ASP A 122 10853 14298 10547 -1764 -938 -326 N
ATOM 573 CA ASP A 122 137.509 0.751 95.813 1.00 91.19 C
ANISOU 573 CA ASP A 122 10491 13751 10407 -1640 -892 -230 C
ATOM 574 C ASP A 122 138.113 -0.302 96.746 1.00 91.95 C
ANISOU 574 C ASP A 122 10700 13626 10611 -1597 -805 -401 C
ATOM 575 O ASP A 122 138.883 0.059 97.630 1.00 90.19 O
ANISOU 575 O ASP A 122 10516 13258 10493 -1475 -729 -376 O
ATOM 576 CB ASP A 122 136.037 1.016 96.188 1.00 93.42 C
ANISOU 576 CB ASP A 122 10659 14060 10776 -1670 -969 -92 C
ATOM 577 CG ASP A 122 135.811 1.464 97.622 1.00101.95 C
ANISOU 577 CG ASP A 122 11719 14959 12058 -1546 -916 1 C
ATOM 578 OD1 ASP A 122 136.321 2.543 97.996 1.00101.66 O
ANISOU 578 OD1 ASP A 122 11671 14877 12077 -1427 -881 117 O
ATOM 579 OD2 ASP A 122 135.073 0.767 98.351 1.00107.30 O
ANISOU 579 OD2 ASP A 122 12388 15550 12831 -1578 -914 -38 O
ATOM 580 N ASN A 123 137.787 -1.596 96.527 1.00 87.83 N
ANISOU 580 N ASN A 123 10235 13077 10060 -1701 -823 -571 N
ATOM 581 CA ASN A 123 138.291 -2.720 97.320 1.00 86.32 C
ANISOU 581 CA ASN A 123 10158 12669 9971 -1674 -757 -735 C
ATOM 582 C ASN A 123 139.808 -2.854 97.202 1.00 88.14 C
ANISOU 582 C ASN A 123 10478 12842 10169 -1583 -669 -852 C
ATOM 583 O ASN A 123 140.454 -3.153 98.203 1.00 86.78 O
ANISOU 583 O ASN A 123 10370 12477 10125 -1486 -601 -889 O
ATOM 584 CB ASN A 123 137.617 -4.032 96.913 1.00 88.02 C
ANISOU 584 CB ASN A 123 10420 12877 10148 -1822 -809 -893 C
ATOM 585 CG ASN A 123 136.145 -4.112 97.233 1.00106.54 C
ANISOU 585 CG ASN A 123 12678 15250 12552 -1918 -888 -792 C
ATOM 586 OD1 ASN A 123 135.688 -3.774 98.333 1.00 97.31 O
ANISOU 586 OD1 ASN A 123 11463 13982 11529 -1858 -869 -671 O
ATOM 587 ND2 ASN A 123 135.370 -4.594 96.277 1.00100.74 N
ANISOU 587 ND2 ASN A 123 11916 14662 11700 -2077 -976 -849 N
ATOM 588 N VAL A 124 140.374 -2.611 95.997 1.00 84.33 N
ANISOU 588 N VAL A 124 9990 12541 9511 -1614 -670 -900 N
ATOM 589 CA VAL A 124 141.819 -2.676 95.739 1.00 83.27 C
ANISOU 589 CA VAL A 124 9915 12399 9325 -1533 -583 -1008 C
ATOM 590 C VAL A 124 142.509 -1.505 96.467 1.00 83.71 C
ANISOU 590 C VAL A 124 9934 12407 9466 -1403 -533 -843 C
ATOM 591 O VAL A 124 143.480 -1.750 97.182 1.00 82.45 O
ANISOU 591 O VAL A 124 9831 12099 9397 -1300 -456 -905 O
ATOM 592 CB VAL A 124 142.153 -2.729 94.218 1.00 88.86 C
ANISOU 592 CB VAL A 124 10617 13343 9802 -1618 -594 -1103 C
ATOM 593 CG1 VAL A 124 143.632 -2.450 93.946 1.00 88.48 C
ANISOU 593 CG1 VAL A 124 10590 13336 9692 -1527 -498 -1159 C
ATOM 594 CG2 VAL A 124 141.754 -4.076 93.620 1.00 90.38 C
ANISOU 594 CG2 VAL A 124 10882 13536 9922 -1731 -622 -1326 C
ATOM 595 N ILE A 125 141.984 -0.260 96.324 1.00 78.59 N
ANISOU 595 N ILE A 125 9192 11869 8798 -1407 -584 -633 N
ATOM 596 CA ILE A 125 142.519 0.941 96.988 1.00 76.46 C
ANISOU 596 CA ILE A 125 8891 11547 8613 -1297 -551 -468 C
ATOM 597 C ILE A 125 142.529 0.723 98.514 1.00 78.03 C
ANISOU 597 C ILE A 125 9132 11506 9012 -1203 -507 -463 C
ATOM 598 O ILE A 125 143.581 0.878 99.141 1.00 76.51 O
ANISOU 598 O ILE A 125 8980 11207 8882 -1109 -438 -479 O
ATOM 599 CB ILE A 125 141.735 2.235 96.595 1.00 79.69 C
ANISOU 599 CB ILE A 125 9199 12090 8989 -1321 -629 -244 C
ATOM 600 CG1 ILE A 125 141.999 2.645 95.133 1.00 81.49 C
ANISOU 600 CG1 ILE A 125 9391 12564 9009 -1404 -666 -216 C
ATOM 601 CG2 ILE A 125 142.064 3.399 97.538 1.00 78.86 C
ANISOU 601 CG2 ILE A 125 9076 11871 9017 -1204 -601 -83 C
ATOM 602 CD1 ILE A 125 140.968 3.647 94.561 1.00 89.59 C
ANISOU 602 CD1 ILE A 125 10315 13738 9988 -1455 -772 -6 C
ATOM 603 N ASP A 126 141.369 0.326 99.090 1.00 73.99 N
ANISOU 603 N ASP A 126 8604 10922 8589 -1239 -548 -443 N
ATOM 604 CA ASP A 126 141.195 0.078 100.524 1.00 72.31 C
ANISOU 604 CA ASP A 126 8423 10505 8548 -1171 -512 -429 C
ATOM 605 C ASP A 126 142.084 -1.066 101.025 1.00 75.54 C
ANISOU 605 C ASP A 126 8940 10755 9007 -1138 -450 -598 C
ATOM 606 O ASP A 126 142.502 -1.030 102.184 1.00 74.05 O
ANISOU 606 O ASP A 126 8788 10407 8940 -1052 -404 -575 O
ATOM 607 CB ASP A 126 139.722 -0.201 100.861 1.00 74.35 C
ANISOU 607 CB ASP A 126 8628 10759 8863 -1241 -568 -378 C
ATOM 608 CG ASP A 126 138.786 0.969 100.601 1.00 83.88 C
ANISOU 608 CG ASP A 126 9715 12095 10061 -1243 -628 -193 C
ATOM 609 OD1 ASP A 126 139.245 2.132 100.684 1.00 83.51 O
ANISOU 609 OD1 ASP A 126 9642 12062 10026 -1158 -613 -75 O
ATOM 610 OD2 ASP A 126 137.598 0.722 100.310 1.00 90.80 O
ANISOU 610 OD2 ASP A 126 10522 13055 10923 -1331 -694 -163 O
ATOM 611 N SER A 127 142.388 -2.059 100.157 1.00 72.77 N
ANISOU 611 N SER A 127 8640 10446 8563 -1201 -452 -770 N
ATOM 612 CA SER A 127 143.272 -3.178 100.494 1.00 72.41 C
ANISOU 612 CA SER A 127 8696 10248 8567 -1157 -398 -941 C
ATOM 613 C SER A 127 144.716 -2.702 100.626 1.00 74.54 C
ANISOU 613 C SER A 127 8979 10507 8837 -1041 -326 -947 C
ATOM 614 O SER A 127 145.413 -3.160 101.527 1.00 73.40 O
ANISOU 614 O SER A 127 8892 10194 8802 -957 -281 -992 O
ATOM 615 CB SER A 127 143.172 -4.295 99.461 1.00 77.67 C
ANISOU 615 CB SER A 127 9412 10966 9131 -1251 -419 -1133 C
ATOM 616 OG SER A 127 141.939 -4.986 99.575 1.00 86.13 O
ANISOU 616 OG SER A 127 10492 11996 10237 -1363 -484 -1149 O
ATOM 617 N VAL A 128 145.151 -1.766 99.752 1.00 70.67 N
ANISOU 617 N VAL A 128 8429 10199 8224 -1042 -321 -886 N
ATOM 618 CA VAL A 128 146.500 -1.188 99.773 1.00 69.80 C
ANISOU 618 CA VAL A 128 8310 10113 8097 -952 -257 -871 C
ATOM 619 C VAL A 128 146.645 -0.335 101.045 1.00 72.19 C
ANISOU 619 C VAL A 128 8602 10291 8537 -868 -245 -718 C
ATOM 620 O VAL A 128 147.667 -0.449 101.719 1.00 71.34 O
ANISOU 620 O VAL A 128 8526 10080 8499 -781 -193 -749 O
ATOM 621 CB VAL A 128 146.852 -0.395 98.479 1.00 74.50 C
ANISOU 621 CB VAL A 128 8843 10950 8515 -999 -261 -830 C
ATOM 622 CG1 VAL A 128 148.256 0.201 98.552 1.00 73.83 C
ANISOU 622 CG1 VAL A 128 8740 10893 8419 -918 -193 -805 C
ATOM 623 CG2 VAL A 128 146.732 -1.279 97.241 1.00 75.98 C
ANISOU 623 CG2 VAL A 128 9049 11271 8550 -1086 -268 -1001 C
ATOM 624 N ILE A 129 145.610 0.467 101.397 1.00 68.33 N
ANISOU 624 N ILE A 129 8067 9808 8089 -892 -294 -562 N
ATOM 625 CA ILE A 129 145.596 1.302 102.610 1.00 66.66 C
ANISOU 625 CA ILE A 129 7849 9478 8002 -818 -283 -428 C
ATOM 626 C ILE A 129 145.644 0.393 103.848 1.00 70.36 C
ANISOU 626 C ILE A 129 8387 9747 8600 -774 -255 -497 C
ATOM 627 O ILE A 129 146.434 0.658 104.756 1.00 69.11 O
ANISOU 627 O ILE A 129 8257 9485 8518 -694 -217 -471 O
ATOM 628 CB ILE A 129 144.384 2.284 102.660 1.00 69.44 C
ANISOU 628 CB ILE A 129 8131 9881 8371 -844 -339 -265 C
ATOM 629 CG1 ILE A 129 144.379 3.216 101.441 1.00 70.35 C
ANISOU 629 CG1 ILE A 129 8182 10187 8362 -887 -378 -174 C
ATOM 630 CG2 ILE A 129 144.399 3.118 103.955 1.00 68.95 C
ANISOU 630 CG2 ILE A 129 8073 9687 8437 -759 -317 -154 C
ATOM 631 CD1 ILE A 129 143.060 3.799 101.071 1.00 76.60 C
ANISOU 631 CD1 ILE A 129 8897 11068 9141 -935 -452 -50 C
ATOM 632 N CYS A 130 144.830 -0.688 103.863 1.00 67.82 N
ANISOU 632 N CYS A 130 8094 9377 8298 -836 -279 -581 N
ATOM 633 CA CYS A 130 144.790 -1.642 104.973 1.00 67.40 C
ANISOU 633 CA CYS A 130 8112 9137 8362 -813 -262 -636 C
ATOM 634 C CYS A 130 146.130 -2.335 105.127 1.00 71.58 C
ANISOU 634 C CYS A 130 8707 9574 8914 -741 -216 -752 C
ATOM 635 O CYS A 130 146.662 -2.350 106.233 1.00 70.56 O
ANISOU 635 O CYS A 130 8613 9314 8881 -669 -190 -721 O
ATOM 636 CB CYS A 130 143.664 -2.655 104.807 1.00 68.63 C
ANISOU 636 CB CYS A 130 8283 9268 8525 -915 -305 -698 C
ATOM 637 SG CYS A 130 143.261 -3.550 106.328 1.00 72.09 S
ANISOU 637 SG CYS A 130 8790 9489 9113 -913 -297 -694 S
ATOM 638 N ALA A 131 146.689 -2.870 104.016 1.00 69.37 N
ANISOU 638 N ALA A 131 8438 9376 8543 -757 -206 -886 N
ATOM 639 CA ALA A 131 147.985 -3.553 103.982 1.00 69.55 C
ANISOU 639 CA ALA A 131 8508 9337 8582 -677 -157 -1014 C
ATOM 640 C ALA A 131 149.097 -2.645 104.492 1.00 72.34 C
ANISOU 640 C ALA A 131 8828 9699 8959 -582 -116 -928 C
ATOM 641 O ALA A 131 149.897 -3.080 105.318 1.00 71.70 O
ANISOU 641 O ALA A 131 8786 9486 8970 -500 -91 -956 O
ATOM 642 CB ALA A 131 148.303 -4.019 102.569 1.00 71.75 C
ANISOU 642 CB ALA A 131 8782 9750 8730 -714 -145 -1163 C
ATOM 643 N SER A 132 149.112 -1.376 104.035 1.00 68.28 N
ANISOU 643 N SER A 132 8243 9334 8367 -600 -120 -813 N
ATOM 644 CA SER A 132 150.101 -0.376 104.427 1.00 67.19 C
ANISOU 644 CA SER A 132 8071 9218 8242 -535 -90 -719 C
ATOM 645 C SER A 132 149.904 0.077 105.878 1.00 69.95 C
ANISOU 645 C SER A 132 8443 9420 8714 -493 -100 -606 C
ATOM 646 O SER A 132 150.895 0.387 106.532 1.00 69.04 O
ANISOU 646 O SER A 132 8331 9255 8645 -427 -74 -578 O
ATOM 647 CB SER A 132 150.065 0.818 103.483 1.00 70.45 C
ANISOU 647 CB SER A 132 8411 9818 8538 -583 -101 -620 C
ATOM 648 OG SER A 132 150.225 0.400 102.138 1.00 79.02 O
ANISOU 648 OG SER A 132 9475 11060 9488 -633 -91 -724 O
ATOM 649 N LEU A 133 148.650 0.101 106.391 1.00 66.23 N
ANISOU 649 N LEU A 133 7984 8890 8290 -535 -134 -546 N
ATOM 650 CA LEU A 133 148.392 0.450 107.793 1.00 64.92 C
ANISOU 650 CA LEU A 133 7843 8594 8228 -498 -134 -456 C
ATOM 651 C LEU A 133 148.951 -0.663 108.683 1.00 69.03 C
ANISOU 651 C LEU A 133 8434 8960 8834 -453 -118 -533 C
ATOM 652 O LEU A 133 149.621 -0.366 109.669 1.00 67.90 O
ANISOU 652 O LEU A 133 8311 8739 8749 -395 -103 -486 O
ATOM 653 CB LEU A 133 146.892 0.702 108.075 1.00 64.74 C
ANISOU 653 CB LEU A 133 7800 8569 8229 -552 -164 -380 C
ATOM 654 CG LEU A 133 146.411 0.614 109.544 1.00 68.74 C
ANISOU 654 CG LEU A 133 8342 8939 8836 -530 -155 -327 C
ATOM 655 CD1 LEU A 133 147.015 1.715 110.425 1.00 67.95 C
ANISOU 655 CD1 LEU A 133 8245 8800 8772 -464 -134 -238 C
ATOM 656 CD2 LEU A 133 144.910 0.645 109.627 1.00 71.37 C
ANISOU 656 CD2 LEU A 133 8637 9297 9181 -590 -178 -277 C
ATOM 657 N LEU A 134 148.701 -1.937 108.311 1.00 66.80 N
ANISOU 657 N LEU A 134 8191 8632 8557 -482 -126 -650 N
ATOM 658 CA LEU A 134 149.213 -3.103 109.034 1.00 67.04 C
ANISOU 658 CA LEU A 134 8295 8502 8676 -438 -121 -725 C
ATOM 659 C LEU A 134 150.741 -3.135 108.945 1.00 71.10 C
ANISOU 659 C LEU A 134 8803 9020 9194 -344 -89 -776 C
ATOM 660 O LEU A 134 151.397 -3.419 109.947 1.00 70.53 O
ANISOU 660 O LEU A 134 8764 8831 9204 -280 -86 -756 O
ATOM 661 CB LEU A 134 148.617 -4.421 108.494 1.00 68.26 C
ANISOU 661 CB LEU A 134 8499 8602 8836 -497 -143 -848 C
ATOM 662 CG LEU A 134 147.097 -4.576 108.475 1.00 73.03 C
ANISOU 662 CG LEU A 134 9100 9213 9435 -607 -180 -811 C
ATOM 663 CD1 LEU A 134 146.683 -5.672 107.528 1.00 74.53 C
ANISOU 663 CD1 LEU A 134 9325 9400 9591 -679 -205 -951 C
ATOM 664 CD2 LEU A 134 146.541 -4.836 109.849 1.00 75.00 C
ANISOU 664 CD2 LEU A 134 9388 9326 9781 -619 -190 -727 C
ATOM 665 N ALA A 135 151.300 -2.810 107.753 1.00 68.13 N
ANISOU 665 N ALA A 135 8373 8794 8721 -340 -65 -833 N
ATOM 666 CA ALA A 135 152.743 -2.765 107.499 1.00 68.31 C
ANISOU 666 CA ALA A 135 8363 8863 8730 -258 -26 -883 C
ATOM 667 C ALA A 135 153.413 -1.641 108.277 1.00 71.88 C
ANISOU 667 C ALA A 135 8778 9330 9205 -221 -21 -751 C
ATOM 668 O ALA A 135 154.549 -1.821 108.708 1.00 71.96 O
ANISOU 668 O ALA A 135 8778 9306 9259 -144 -3 -768 O
ATOM 669 CB ALA A 135 153.022 -2.606 106.016 1.00 69.91 C
ANISOU 669 CB ALA A 135 8510 9250 8802 -285 2 -963 C
ATOM 670 N SER A 136 152.720 -0.494 108.463 1.00 67.77 N
ANISOU 670 N SER A 136 8237 8856 8658 -274 -40 -624 N
ATOM 671 CA SER A 136 153.248 0.641 109.225 1.00 66.72 C
ANISOU 671 CA SER A 136 8082 8721 8547 -253 -41 -503 C
ATOM 672 C SER A 136 153.310 0.282 110.712 1.00 70.19 C
ANISOU 672 C SER A 136 8581 8998 9091 -212 -55 -471 C
ATOM 673 O SER A 136 154.291 0.631 111.370 1.00 69.95 O
ANISOU 673 O SER A 136 8542 8945 9090 -167 -52 -433 O
ATOM 674 CB SER A 136 152.431 1.911 108.988 1.00 69.53 C
ANISOU 674 CB SER A 136 8410 9151 8858 -311 -59 -388 C
ATOM 675 OG SER A 136 151.129 1.863 109.544 1.00 77.41 O
ANISOU 675 OG SER A 136 9441 10075 9898 -342 -82 -348 O
ATOM 676 N ILE A 137 152.295 -0.463 111.221 1.00 66.16 N
ANISOU 676 N ILE A 137 8127 8383 8629 -237 -72 -485 N
ATOM 677 CA ILE A 137 152.238 -0.955 112.606 1.00 65.31 C
ANISOU 677 CA ILE A 137 8080 8127 8607 -214 -87 -452 C
ATOM 678 C ILE A 137 153.412 -1.925 112.807 1.00 68.81 C
ANISOU 678 C ILE A 137 8543 8499 9103 -139 -86 -523 C
ATOM 679 O ILE A 137 154.180 -1.765 113.755 1.00 67.95 O
ANISOU 679 O ILE A 137 8443 8338 9037 -94 -96 -472 O
ATOM 680 CB ILE A 137 150.855 -1.607 112.938 1.00 68.43 C
ANISOU 680 CB ILE A 137 8521 8448 9032 -275 -103 -450 C
ATOM 681 CG1 ILE A 137 149.732 -0.552 112.960 1.00 68.19 C
ANISOU 681 CG1 ILE A 137 8456 8486 8966 -329 -102 -363 C
ATOM 682 CG2 ILE A 137 150.892 -2.384 114.268 1.00 69.10 C
ANISOU 682 CG2 ILE A 137 8676 8382 9198 -260 -118 -425 C
ATOM 683 CD1 ILE A 137 148.314 -1.085 112.752 1.00 75.16 C
ANISOU 683 CD1 ILE A 137 9341 9365 9849 -403 -115 -373 C
ATOM 684 N CYS A 138 153.571 -2.881 111.870 1.00 65.95 N
ANISOU 684 N CYS A 138 8181 8143 8734 -124 -77 -645 N
ATOM 685 CA CYS A 138 154.626 -3.894 111.860 1.00 66.51 C
ANISOU 685 CA CYS A 138 8264 8145 8862 -37 -72 -736 C
ATOM 686 C CYS A 138 156.010 -3.253 111.780 1.00 70.17 C
ANISOU 686 C CYS A 138 8652 8702 9307 32 -49 -719 C
ATOM 687 O CYS A 138 156.911 -3.710 112.476 1.00 69.87 O
ANISOU 687 O CYS A 138 8618 8588 9343 110 -62 -716 O
ATOM 688 CB CYS A 138 154.410 -4.883 110.721 1.00 67.86 C
ANISOU 688 CB CYS A 138 8449 8321 9013 -40 -58 -887 C
ATOM 689 SG CYS A 138 153.090 -6.083 111.023 1.00 72.22 S
ANISOU 689 SG CYS A 138 9104 8707 9629 -111 -99 -924 S
ATOM 690 N SER A 139 156.169 -2.189 110.957 1.00 66.65 N
ANISOU 690 N SER A 139 8136 8424 8766 -3 -23 -695 N
ATOM 691 CA SER A 139 157.425 -1.448 110.793 1.00 66.53 C
ANISOU 691 CA SER A 139 8038 8522 8720 36 -1 -665 C
ATOM 692 C SER A 139 157.817 -0.745 112.090 1.00 69.44 C
ANISOU 692 C SER A 139 8416 8834 9137 41 -32 -541 C
ATOM 693 O SER A 139 158.970 -0.850 112.499 1.00 69.62 O
ANISOU 693 O SER A 139 8398 8858 9196 105 -35 -536 O
ATOM 694 CB SER A 139 157.317 -0.433 109.660 1.00 70.07 C
ANISOU 694 CB SER A 139 8421 9151 9050 -30 25 -643 C
ATOM 695 OG SER A 139 157.134 -1.075 108.410 1.00 79.14 O
ANISOU 695 OG SER A 139 9555 10381 10133 -36 56 -766 O
ATOM 696 N LEU A 140 156.858 -0.057 112.749 1.00 64.74 N
ANISOU 696 N LEU A 140 7868 8192 8540 -22 -56 -449 N
ATOM 697 CA LEU A 140 157.076 0.638 114.022 1.00 63.70 C
ANISOU 697 CA LEU A 140 7760 8003 8440 -28 -85 -345 C
ATOM 698 C LEU A 140 157.405 -0.370 115.131 1.00 67.23 C
ANISOU 698 C LEU A 140 8258 8315 8972 26 -114 -349 C
ATOM 699 O LEU A 140 158.259 -0.089 115.973 1.00 67.07 O
ANISOU 699 O LEU A 140 8228 8281 8976 51 -138 -294 O
ATOM 700 CB LEU A 140 155.855 1.490 114.405 1.00 62.98 C
ANISOU 700 CB LEU A 140 7711 7891 8329 -97 -92 -270 C
ATOM 701 CG LEU A 140 155.621 2.768 113.593 1.00 67.35 C
ANISOU 701 CG LEU A 140 8218 8558 8814 -147 -81 -221 C
ATOM 702 CD1 LEU A 140 154.169 3.176 113.637 1.00 67.08 C
ANISOU 702 CD1 LEU A 140 8214 8500 8772 -194 -84 -183 C
ATOM 703 CD2 LEU A 140 156.487 3.903 114.086 1.00 69.40 C
ANISOU 703 CD2 LEU A 140 8458 8844 9068 -156 -93 -143 C
ATOM 704 N LEU A 141 156.752 -1.556 115.099 1.00 63.34 N
ANISOU 704 N LEU A 141 7820 7725 8523 37 -119 -411 N
ATOM 705 CA LEU A 141 157.002 -2.660 116.028 1.00 63.09 C
ANISOU 705 CA LEU A 141 7843 7550 8577 86 -153 -411 C
ATOM 706 C LEU A 141 158.377 -3.264 115.755 1.00 67.01 C
ANISOU 706 C LEU A 141 8286 8055 9118 188 -154 -469 C
ATOM 707 O LEU A 141 159.027 -3.735 116.684 1.00 67.11 O
ANISOU 707 O LEU A 141 8315 7986 9199 241 -193 -428 O
ATOM 708 CB LEU A 141 155.918 -3.749 115.916 1.00 63.48 C
ANISOU 708 CB LEU A 141 7965 7490 8663 56 -160 -462 C
ATOM 709 CG LEU A 141 154.553 -3.470 116.551 1.00 67.38 C
ANISOU 709 CG LEU A 141 8515 7948 9141 -35 -166 -392 C
ATOM 710 CD1 LEU A 141 153.523 -4.455 116.048 1.00 68.02 C
ANISOU 710 CD1 LEU A 141 8639 7963 9241 -81 -168 -457 C
ATOM 711 CD2 LEU A 141 154.612 -3.539 118.070 1.00 69.87 C
ANISOU 711 CD2 LEU A 141 8883 8172 9492 -39 -199 -293 C
ATOM 712 N SER A 142 158.817 -3.246 114.480 1.00 63.29 N
ANISOU 712 N SER A 142 7745 7695 8607 215 -111 -562 N
ATOM 713 CA SER A 142 160.124 -3.751 114.062 1.00 63.81 C
ANISOU 713 CA SER A 142 7737 7801 8706 320 -94 -633 C
ATOM 714 C SER A 142 161.225 -2.789 114.488 1.00 67.35 C
ANISOU 714 C SER A 142 8102 8353 9135 332 -102 -547 C
ATOM 715 O SER A 142 162.316 -3.246 114.826 1.00 67.81 O
ANISOU 715 O SER A 142 8108 8400 9255 423 -118 -553 O
ATOM 716 CB SER A 142 160.165 -3.986 112.560 1.00 67.53 C
ANISOU 716 CB SER A 142 8160 8381 9118 333 -35 -766 C
ATOM 717 OG SER A 142 159.287 -5.041 112.208 1.00 75.94 O
ANISOU 717 OG SER A 142 9306 9334 10213 327 -37 -862 O
ATOM 718 N ILE A 143 160.932 -1.463 114.502 1.00 62.74 N
ANISOU 718 N ILE A 143 7503 7861 8473 240 -98 -464 N
ATOM 719 CA ILE A 143 161.868 -0.436 114.981 1.00 62.23 C
ANISOU 719 CA ILE A 143 7375 7882 8388 223 -116 -373 C
ATOM 720 C ILE A 143 161.941 -0.585 116.516 1.00 66.38 C
ANISOU 720 C ILE A 143 7963 8285 8975 230 -179 -288 C
ATOM 721 O ILE A 143 163.016 -0.420 117.088 1.00 66.37 O
ANISOU 721 O ILE A 143 7907 8313 8996 261 -211 -241 O
ATOM 722 CB ILE A 143 161.503 1.017 114.522 1.00 64.34 C
ANISOU 722 CB ILE A 143 7625 8258 8564 120 -99 -311 C
ATOM 723 CG1 ILE A 143 161.376 1.125 112.987 1.00 65.00 C
ANISOU 723 CG1 ILE A 143 7651 8475 8572 102 -43 -381 C
ATOM 724 CG2 ILE A 143 162.535 2.039 115.030 1.00 64.81 C
ANISOU 724 CG2 ILE A 143 7624 8391 8608 90 -124 -221 C
ATOM 725 CD1 ILE A 143 160.432 2.235 112.469 1.00 68.89 C
ANISOU 725 CD1 ILE A 143 8165 9022 8988 1 -36 -323 C
ATOM 726 N ALA A 144 160.807 -0.958 117.162 1.00 62.67 N
ANISOU 726 N ALA A 144 7600 7687 8525 196 -199 -269 N
ATOM 727 CA ALA A 144 160.720 -1.199 118.607 1.00 62.50 C
ANISOU 727 CA ALA A 144 7648 7555 8544 191 -254 -190 C
ATOM 728 C ALA A 144 161.552 -2.421 118.990 1.00 67.87 C
ANISOU 728 C ALA A 144 8316 8156 9314 292 -292 -206 C
ATOM 729 O ALA A 144 162.280 -2.371 119.982 1.00 68.14 O
ANISOU 729 O ALA A 144 8343 8176 9373 310 -346 -129 O
ATOM 730 CB ALA A 144 159.269 -1.379 119.032 1.00 62.66 C
ANISOU 730 CB ALA A 144 7770 7482 8557 128 -251 -174 C
ATOM 731 N VAL A 145 161.480 -3.494 118.169 1.00 64.94 N
ANISOU 731 N VAL A 145 7943 7738 8994 360 -268 -308 N
ATOM 732 CA VAL A 145 162.261 -4.724 118.329 1.00 65.92 C
ANISOU 732 CA VAL A 145 8052 7771 9221 478 -298 -343 C
ATOM 733 C VAL A 145 163.737 -4.358 118.112 1.00 70.51 C
ANISOU 733 C VAL A 145 8501 8480 9808 552 -296 -342 C
ATOM 734 O VAL A 145 164.577 -4.715 118.935 1.00 71.09 O
ANISOU 734 O VAL A 145 8549 8516 9947 616 -354 -280 O
ATOM 735 CB VAL A 145 161.765 -5.853 117.372 1.00 70.50 C
ANISOU 735 CB VAL A 145 8669 8270 9849 525 -264 -476 C
ATOM 736 CG1 VAL A 145 162.799 -6.969 117.213 1.00 71.88 C
ANISOU 736 CG1 VAL A 145 8801 8377 10133 673 -278 -544 C
ATOM 737 CG2 VAL A 145 160.429 -6.426 117.839 1.00 69.93 C
ANISOU 737 CG2 VAL A 145 8725 8049 9795 451 -287 -455 C
ATOM 738 N ASP A 146 164.026 -3.588 117.040 1.00 66.75 N
ANISOU 738 N ASP A 146 7938 8167 9257 530 -234 -394 N
ATOM 739 CA ASP A 146 165.366 -3.120 116.681 1.00 67.23 C
ANISOU 739 CA ASP A 146 7856 8383 9305 578 -218 -393 C
ATOM 740 C ASP A 146 166.010 -2.355 117.831 1.00 71.01 C
ANISOU 740 C ASP A 146 8310 8893 9779 536 -284 -260 C
ATOM 741 O ASP A 146 167.136 -2.675 118.208 1.00 71.64 O
ANISOU 741 O ASP A 146 8303 9000 9915 617 -320 -234 O
ATOM 742 CB ASP A 146 165.314 -2.234 115.419 1.00 68.67 C
ANISOU 742 CB ASP A 146 7971 8738 9382 516 -144 -442 C
ATOM 743 CG ASP A 146 166.656 -1.677 114.989 1.00 78.98 C
ANISOU 743 CG ASP A 146 9122 10227 10660 541 -120 -432 C
ATOM 744 OD1 ASP A 146 167.031 -0.591 115.478 1.00 79.14 O
ANISOU 744 OD1 ASP A 146 9110 10322 10639 459 -151 -327 O
ATOM 745 OD2 ASP A 146 167.323 -2.318 114.156 1.00 86.01 O
ANISOU 745 OD2 ASP A 146 9921 11189 11569 638 -69 -535 O
ATOM 746 N ARG A 147 165.288 -1.360 118.388 1.00 66.42 N
ANISOU 746 N ARG A 147 7802 8306 9129 413 -302 -181 N
ATOM 747 CA ARG A 147 165.767 -0.502 119.466 1.00 65.84 C
ANISOU 747 CA ARG A 147 7725 8261 9030 350 -363 -67 C
ATOM 748 C ARG A 147 165.998 -1.276 120.751 1.00 70.74 C
ANISOU 748 C ARG A 147 8393 8768 9718 395 -443 -2 C
ATOM 749 O ARG A 147 167.064 -1.113 121.337 1.00 71.15 O
ANISOU 749 O ARG A 147 8371 8876 9785 414 -498 61 O
ATOM 750 CB ARG A 147 164.832 0.696 119.703 1.00 64.25 C
ANISOU 750 CB ARG A 147 7604 8062 8746 220 -354 -22 C
ATOM 751 CG ARG A 147 164.901 1.767 118.606 1.00 71.77 C
ANISOU 751 CG ARG A 147 8493 9148 9628 158 -301 -40 C
ATOM 752 CD ARG A 147 166.280 2.388 118.458 1.00 79.69 C
ANISOU 752 CD ARG A 147 9369 10292 10616 148 -316 -2 C
ATOM 753 NE ARG A 147 167.077 1.760 117.403 1.00 85.49 N
ANISOU 753 NE ARG A 147 9980 11131 11371 235 -268 -76 N
ATOM 754 CZ ARG A 147 168.403 1.820 117.332 1.00 97.69 C
ANISOU 754 CZ ARG A 147 11390 12797 12931 270 -278 -57 C
ATOM 755 NH1 ARG A 147 169.097 2.467 118.260 1.00 85.15 N
ANISOU 755 NH1 ARG A 147 9776 11238 11341 214 -346 38 N
ATOM 756 NH2 ARG A 147 169.047 1.220 116.340 1.00 84.36 N
ANISOU 756 NH2 ARG A 147 9587 11210 11256 358 -220 -138 N
ATOM 757 N TYR A 148 165.053 -2.154 121.158 1.00 67.44 N
ANISOU 757 N TYR A 148 8087 8197 9338 409 -454 -10 N
ATOM 758 CA TYR A 148 165.198 -2.975 122.365 1.00 68.05 C
ANISOU 758 CA TYR A 148 8221 8159 9477 445 -534 66 C
ATOM 759 C TYR A 148 166.453 -3.853 122.287 1.00 72.95 C
ANISOU 759 C TYR A 148 8741 8781 10197 583 -572 60 C
ATOM 760 O TYR A 148 167.214 -3.922 123.252 1.00 73.42 O
ANISOU 760 O TYR A 148 8773 8845 10280 602 -652 155 O
ATOM 761 CB TYR A 148 163.953 -3.857 122.601 1.00 69.35 C
ANISOU 761 CB TYR A 148 8515 8164 9671 431 -530 53 C
ATOM 762 CG TYR A 148 164.088 -4.793 123.786 1.00 72.42 C
ANISOU 762 CG TYR A 148 8966 8427 10124 464 -615 144 C
ATOM 763 CD1 TYR A 148 163.757 -4.375 125.072 1.00 74.19 C
ANISOU 763 CD1 TYR A 148 9264 8640 10286 373 -666 254 C
ATOM 764 CD2 TYR A 148 164.565 -6.092 123.625 1.00 74.69 C
ANISOU 764 CD2 TYR A 148 9239 8607 10532 587 -647 121 C
ATOM 765 CE1 TYR A 148 163.895 -5.226 126.168 1.00 76.35 C
ANISOU 765 CE1 TYR A 148 9594 8811 10604 391 -749 353 C
ATOM 766 CE2 TYR A 148 164.726 -6.944 124.716 1.00 76.75 C
ANISOU 766 CE2 TYR A 148 9558 8748 10858 617 -737 224 C
ATOM 767 CZ TYR A 148 164.385 -6.509 125.986 1.00 84.46 C
ANISOU 767 CZ TYR A 148 10605 9727 11759 513 -790 348 C
ATOM 768 OH TYR A 148 164.530 -7.351 127.063 1.00 87.10 O
ANISOU 768 OH TYR A 148 10997 9953 12142 530 -883 464 O
ATOM 769 N PHE A 149 166.652 -4.528 121.148 1.00 69.52 N
ANISOU 769 N PHE A 149 8249 8346 9818 682 -515 -55 N
ATOM 770 CA PHE A 149 167.778 -5.423 120.960 1.00 70.71 C
ANISOU 770 CA PHE A 149 8299 8491 10076 836 -537 -84 C
ATOM 771 C PHE A 149 169.089 -4.673 120.709 1.00 74.92 C
ANISOU 771 C PHE A 149 8663 9219 10584 859 -532 -66 C
ATOM 772 O PHE A 149 170.121 -5.195 121.100 1.00 75.68 O
ANISOU 772 O PHE A 149 8669 9323 10763 966 -586 -28 O
ATOM 773 CB PHE A 149 167.493 -6.434 119.853 1.00 73.25 C
ANISOU 773 CB PHE A 149 8630 8737 10463 935 -472 -233 C
ATOM 774 CG PHE A 149 166.614 -7.583 120.293 1.00 75.07 C
ANISOU 774 CG PHE A 149 9005 8743 10774 955 -510 -234 C
ATOM 775 CD1 PHE A 149 167.167 -8.726 120.859 1.00 79.78 C
ANISOU 775 CD1 PHE A 149 9608 9199 11506 1080 -580 -202 C
ATOM 776 CD2 PHE A 149 165.235 -7.524 120.141 1.00 75.93 C
ANISOU 776 CD2 PHE A 149 9238 8783 10829 845 -480 -259 C
ATOM 777 CE1 PHE A 149 166.352 -9.785 121.273 1.00 81.12 C
ANISOU 777 CE1 PHE A 149 9918 9151 11752 1083 -622 -190 C
ATOM 778 CE2 PHE A 149 164.422 -8.584 120.553 1.00 79.17 C
ANISOU 778 CE2 PHE A 149 9777 8992 11312 844 -517 -251 C
ATOM 779 CZ PHE A 149 164.986 -9.708 121.115 1.00 78.84 C
ANISOU 779 CZ PHE A 149 9752 8802 11402 958 -588 -216 C
ATOM 780 N THR A 150 169.075 -3.459 120.112 1.00 70.73 N
ANISOU 780 N THR A 150 8083 8844 9945 757 -477 -79 N
ATOM 781 CA THR A 150 170.331 -2.704 119.937 1.00 71.19 C
ANISOU 781 CA THR A 150 7979 9093 9976 754 -479 -44 C
ATOM 782 C THR A 150 170.764 -2.068 121.269 1.00 74.13 C
ANISOU 782 C THR A 150 8358 9482 10325 675 -581 99 C
ATOM 783 O THR A 150 171.958 -1.849 121.477 1.00 74.81 O
ANISOU 783 O THR A 150 8307 9689 10429 702 -621 149 O
ATOM 784 CB THR A 150 170.256 -1.641 118.828 1.00 81.13 C
ANISOU 784 CB THR A 150 9181 10512 11132 664 -394 -93 C
ATOM 785 OG1 THR A 150 169.059 -0.880 118.961 1.00 82.61 O
ANISOU 785 OG1 THR A 150 9503 10646 11240 530 -385 -69 O
ATOM 786 CG2 THR A 150 170.363 -2.230 117.434 1.00 80.54 C
ANISOU 786 CG2 THR A 150 9035 10497 11068 757 -297 -233 C
ATOM 787 N ILE A 151 169.799 -1.782 122.170 1.00 68.80 N
ANISOU 787 N ILE A 151 7836 8699 9605 574 -621 159 N
ATOM 788 CA ILE A 151 170.074 -1.188 123.480 1.00 68.24 C
ANISOU 788 CA ILE A 151 7796 8639 9492 486 -714 280 C
ATOM 789 C ILE A 151 170.684 -2.252 124.414 1.00 74.00 C
ANISOU 789 C ILE A 151 8511 9295 10313 587 -810 354 C
ATOM 790 O ILE A 151 171.704 -1.974 125.048 1.00 74.66 O
ANISOU 790 O ILE A 151 8503 9469 10395 580 -888 438 O
ATOM 791 CB ILE A 151 168.798 -0.506 124.076 1.00 69.53 C
ANISOU 791 CB ILE A 151 8126 8725 9568 351 -709 304 C
ATOM 792 CG1 ILE A 151 168.572 0.878 123.425 1.00 68.78 C
ANISOU 792 CG1 ILE A 151 8020 8731 9384 238 -650 276 C
ATOM 793 CG2 ILE A 151 168.846 -0.379 125.611 1.00 70.04 C
ANISOU 793 CG2 ILE A 151 8265 8749 9599 287 -808 414 C
ATOM 794 CD1 ILE A 151 167.144 1.418 123.471 1.00 74.10 C
ANISOU 794 CD1 ILE A 151 8834 9324 9995 149 -606 253 C
ATOM 795 N PHE A 152 170.090 -3.466 124.469 1.00 70.98 N
ANISOU 795 N PHE A 152 8210 8749 10011 676 -812 329 N
ATOM 796 CA PHE A 152 170.539 -4.521 125.378 1.00 72.20 C
ANISOU 796 CA PHE A 152 8371 8805 10258 769 -911 414 C
ATOM 797 C PHE A 152 171.476 -5.571 124.749 1.00 78.69 C
ANISOU 797 C PHE A 152 9065 9613 11220 961 -911 364 C
ATOM 798 O PHE A 152 172.484 -5.905 125.369 1.00 79.54 O
ANISOU 798 O PHE A 152 9080 9750 11390 1037 -1000 452 O
ATOM 799 CB PHE A 152 169.333 -5.218 126.022 1.00 73.39 C
ANISOU 799 CB PHE A 152 8701 8768 10416 735 -931 445 C
ATOM 800 CG PHE A 152 168.509 -4.303 126.900 1.00 73.44 C
ANISOU 800 CG PHE A 152 8824 8789 10291 565 -944 509 C
ATOM 801 CD1 PHE A 152 169.008 -3.838 128.113 1.00 76.73 C
ANISOU 801 CD1 PHE A 152 9243 9264 10647 494 -1039 629 C
ATOM 802 CD2 PHE A 152 167.238 -3.901 126.513 1.00 73.86 C
ANISOU 802 CD2 PHE A 152 8980 8804 10280 478 -862 443 C
ATOM 803 CE1 PHE A 152 168.249 -2.985 128.919 1.00 76.56 C
ANISOU 803 CE1 PHE A 152 9333 9258 10498 343 -1041 668 C
ATOM 804 CE2 PHE A 152 166.478 -3.051 127.323 1.00 75.62 C
ANISOU 804 CE2 PHE A 152 9302 9041 10388 337 -865 490 C
ATOM 805 CZ PHE A 152 166.985 -2.609 128.524 1.00 74.17 C
ANISOU 805 CZ PHE A 152 9128 8910 10142 273 -950 595 C
ATOM 806 N TYR A 153 171.153 -6.107 123.564 1.00 76.19 N
ANISOU 806 N TYR A 153 8742 9253 10954 1044 -815 224 N
ATOM 807 CA TYR A 153 171.982 -7.147 122.936 1.00 78.22 C
ANISOU 807 CA TYR A 153 8888 9485 11348 1240 -803 150 C
ATOM 808 C TYR A 153 172.519 -6.629 121.589 1.00 82.90 C
ANISOU 808 C TYR A 153 9336 10260 11904 1272 -690 23 C
ATOM 809 O TYR A 153 172.283 -7.237 120.543 1.00 82.90 O
ANISOU 809 O TYR A 153 9335 10220 11944 1358 -605 -121 O
ATOM 810 CB TYR A 153 171.174 -8.462 122.780 1.00 80.05 C
ANISOU 810 CB TYR A 153 9252 9480 11683 1325 -797 86 C
ATOM 811 CG TYR A 153 170.265 -8.769 123.954 1.00 81.53 C
ANISOU 811 CG TYR A 153 9613 9504 11862 1233 -880 206 C
ATOM 812 CD1 TYR A 153 170.739 -9.448 125.072 1.00 84.95 C
ANISOU 812 CD1 TYR A 153 10059 9841 12377 1292 -1003 344 C
ATOM 813 CD2 TYR A 153 168.933 -8.360 123.955 1.00 80.65 C
ANISOU 813 CD2 TYR A 153 9644 9346 11652 1084 -836 189 C
ATOM 814 CE1 TYR A 153 169.912 -9.712 126.165 1.00 85.79 C
ANISOU 814 CE1 TYR A 153 10322 9817 12457 1193 -1075 464 C
ATOM 815 CE2 TYR A 153 168.099 -8.611 125.043 1.00 81.31 C
ANISOU 815 CE2 TYR A 153 9874 9304 11715 992 -901 299 C
ATOM 816 CZ TYR A 153 168.592 -9.290 126.145 1.00 90.95 C
ANISOU 816 CZ TYR A 153 11112 10439 13008 1042 -1019 437 C
ATOM 817 OH TYR A 153 167.768 -9.541 127.217 1.00 92.44 O
ANISOU 817 OH TYR A 153 11444 10520 13160 940 -1079 553 O
ATOM 818 N ALA A 154 173.212 -5.468 121.635 1.00 79.72 N
ANISOU 818 N ALA A 154 8818 10061 11413 1183 -692 79 N
ATOM 819 CA ALA A 154 173.776 -4.719 120.504 1.00 79.91 C
ANISOU 819 CA ALA A 154 8696 10293 11372 1167 -596 0 C
ATOM 820 C ALA A 154 174.585 -5.586 119.529 1.00 86.50 C
ANISOU 820 C ALA A 154 9384 11180 12302 1358 -529 -122 C
ATOM 821 O ALA A 154 174.254 -5.627 118.342 1.00 85.90 O
ANISOU 821 O ALA A 154 9301 11148 12188 1372 -417 -260 O
ATOM 822 CB ALA A 154 174.651 -3.585 121.020 1.00 80.64 C
ANISOU 822 CB ALA A 154 8675 10569 11396 1062 -649 115 C
ATOM 823 N LEU A 155 175.639 -6.264 120.031 1.00 85.53 N
ANISOU 823 N LEU A 155 9140 11058 12298 1506 -596 -74 N
ATOM 824 CA LEU A 155 176.539 -7.113 119.248 1.00 87.55 C
ANISOU 824 CA LEU A 155 9238 11365 12663 1714 -538 -185 C
ATOM 825 C LEU A 155 175.819 -8.360 118.722 1.00 92.55 C
ANISOU 825 C LEU A 155 9993 11782 13390 1843 -492 -327 C
ATOM 826 O LEU A 155 176.062 -8.760 117.582 1.00 93.22 O
ANISOU 826 O LEU A 155 10001 11925 13493 1951 -383 -491 O
ATOM 827 CB LEU A 155 177.763 -7.508 120.107 1.00 89.38 C
ANISOU 827 CB LEU A 155 9320 11631 13010 1837 -645 -69 C
ATOM 828 CG LEU A 155 179.043 -8.043 119.422 1.00 96.37 C
ANISOU 828 CG LEU A 155 9966 12654 13998 2045 -592 -151 C
ATOM 829 CD1 LEU A 155 179.073 -9.558 119.382 1.00 98.34 C
ANISOU 829 CD1 LEU A 155 10248 12686 14430 2280 -604 -232 C
ATOM 830 CD2 LEU A 155 179.314 -7.397 118.059 1.00 98.61 C
ANISOU 830 CD2 LEU A 155 10122 13171 14176 2011 -439 -283 C
ATOM 831 N GLN A 156 174.935 -8.959 119.545 1.00 88.96 N
ANISOU 831 N GLN A 156 9729 11085 12986 1820 -572 -267 N
ATOM 832 CA GLN A 156 174.164 -10.158 119.201 1.00 89.52 C
ANISOU 832 CA GLN A 156 9942 10920 13154 1914 -551 -381 C
ATOM 833 C GLN A 156 173.170 -9.875 118.063 1.00 92.32 C
ANISOU 833 C GLN A 156 10383 11297 13399 1819 -432 -532 C
ATOM 834 O GLN A 156 173.139 -10.631 117.093 1.00 93.21 O
ANISOU 834 O GLN A 156 10489 11362 13562 1935 -352 -704 O
ATOM 835 CB GLN A 156 173.430 -10.714 120.435 1.00 90.55 C
ANISOU 835 CB GLN A 156 10252 10812 13343 1870 -672 -248 C
ATOM 836 CG GLN A 156 174.349 -11.335 121.483 1.00107.72 C
ANISOU 836 CG GLN A 156 12360 12918 15651 1997 -799 -109 C
ATOM 837 CD GLN A 156 173.570 -11.868 122.657 1.00127.84 C
ANISOU 837 CD GLN A 156 15093 15244 18237 1934 -914 29 C
ATOM 838 OE1 GLN A 156 173.072 -12.998 122.643 1.00124.52 O
ANISOU 838 OE1 GLN A 156 14791 14588 17934 2015 -935 -11 O
ATOM 839 NE2 GLN A 156 173.446 -11.063 123.701 1.00119.30 N
ANISOU 839 NE2 GLN A 156 14044 14233 17052 1779 -992 193 N
ATOM 840 N TYR A 157 172.391 -8.776 118.171 1.00 86.65 N
ANISOU 840 N TYR A 157 9739 10653 12530 1615 -421 -471 N
ATOM 841 CA TYR A 157 171.395 -8.345 117.182 1.00 85.17 C
ANISOU 841 CA TYR A 157 9629 10505 12227 1503 -325 -580 C
ATOM 842 C TYR A 157 172.052 -7.991 115.838 1.00 90.28 C
ANISOU 842 C TYR A 157 10121 11372 12809 1546 -207 -713 C
ATOM 843 O TYR A 157 171.505 -8.348 114.794 1.00 90.02 O
ANISOU 843 O TYR A 157 10132 11327 12743 1558 -123 -867 O
ATOM 844 CB TYR A 157 170.591 -7.144 117.724 1.00 83.89 C
ANISOU 844 CB TYR A 157 9553 10387 11933 1292 -352 -461 C
ATOM 845 CG TYR A 157 169.553 -6.582 116.776 1.00 83.95 C
ANISOU 845 CG TYR A 157 9631 10445 11820 1171 -268 -544 C
ATOM 846 CD1 TYR A 157 168.277 -7.132 116.700 1.00 85.28 C
ANISOU 846 CD1 TYR A 157 9962 10446 11995 1128 -265 -593 C
ATOM 847 CD2 TYR A 157 169.835 -5.476 115.979 1.00 84.04 C
ANISOU 847 CD2 TYR A 157 9544 10677 11712 1091 -200 -560 C
ATOM 848 CE1 TYR A 157 167.299 -6.582 115.875 1.00 84.75 C
ANISOU 848 CE1 TYR A 157 9950 10434 11817 1013 -200 -653 C
ATOM 849 CE2 TYR A 157 168.880 -4.946 115.115 1.00 83.80 C
ANISOU 849 CE2 TYR A 157 9575 10695 11572 981 -134 -619 C
ATOM 850 CZ TYR A 157 167.610 -5.497 115.071 1.00 90.43 C
ANISOU 850 CZ TYR A 157 10569 11370 12419 946 -136 -666 C
ATOM 851 OH TYR A 157 166.672 -4.996 114.204 1.00 90.41 O
ANISOU 851 OH TYR A 157 10615 11426 12311 841 -80 -718 O
ATOM 852 N HIS A 158 173.205 -7.284 115.869 1.00 87.76 N
ANISOU 852 N HIS A 158 9621 11263 12461 1556 -203 -652 N
ATOM 853 CA HIS A 158 173.951 -6.851 114.682 1.00 88.58 C
ANISOU 853 CA HIS A 158 9553 11612 12492 1581 -91 -751 C
ATOM 854 C HIS A 158 174.421 -8.046 113.834 1.00 94.71 C
ANISOU 854 C HIS A 158 10261 12362 13362 1789 -15 -937 C
ATOM 855 O HIS A 158 174.361 -7.970 112.605 1.00 95.09 O
ANISOU 855 O HIS A 158 10265 12540 13324 1790 101 -1082 O
ATOM 856 CB HIS A 158 175.150 -5.977 115.087 1.00 89.83 C
ANISOU 856 CB HIS A 158 9525 11980 12624 1551 -122 -626 C
ATOM 857 CG HIS A 158 175.979 -5.511 113.929 1.00 94.36 C
ANISOU 857 CG HIS A 158 9908 12826 13119 1565 -9 -707 C
ATOM 858 ND1 HIS A 158 177.157 -6.148 113.584 1.00 98.42 N
ANISOU 858 ND1 HIS A 158 10230 13445 13718 1750 34 -780 N
ATOM 859 CD2 HIS A 158 175.758 -4.500 113.057 1.00 95.28 C
ANISOU 859 CD2 HIS A 158 9997 13125 13079 1417 70 -722 C
ATOM 860 CE1 HIS A 158 177.620 -5.501 112.528 1.00 98.30 C
ANISOU 860 CE1 HIS A 158 10076 13689 13586 1701 143 -839 C
ATOM 861 NE2 HIS A 158 176.812 -4.502 112.173 1.00 96.82 N
ANISOU 861 NE2 HIS A 158 9984 13553 13250 1497 164 -800 N
ATOM 862 N ASN A 159 174.877 -9.136 114.486 1.00 92.26 N
ANISOU 862 N ASN A 159 9947 11884 13225 1965 -81 -934 N
ATOM 863 CA ASN A 159 175.347 -10.350 113.813 1.00 94.15 C
ANISOU 863 CA ASN A 159 10132 12056 13584 2188 -19 -1113 C
ATOM 864 C ASN A 159 174.190 -11.113 113.161 1.00 97.24 C
ANISOU 864 C ASN A 159 10712 12259 13976 2183 26 -1274 C
ATOM 865 O ASN A 159 174.361 -11.646 112.064 1.00 98.27 O
ANISOU 865 O ASN A 159 10800 12434 14103 2287 132 -1474 O
ATOM 866 CB ASN A 159 176.098 -11.259 114.790 1.00 96.44 C
ANISOU 866 CB ASN A 159 10377 12193 14072 2372 -122 -1038 C
ATOM 867 CG ASN A 159 177.386 -10.678 115.331 1.00117.06 C
ANISOU 867 CG ASN A 159 12773 15005 16701 2408 -166 -902 C
ATOM 868 OD1 ASN A 159 178.138 -9.977 114.641 1.00110.39 O
ANISOU 868 OD1 ASN A 159 11741 14434 15766 2392 -80 -936 O
ATOM 869 ND2 ASN A 159 177.685 -10.995 116.578 1.00108.73 N
ANISOU 869 ND2 ASN A 159 11731 13824 15759 2452 -305 -740 N
ATOM 870 N ILE A 160 173.017 -11.152 113.828 1.00 91.86 N
ANISOU 870 N ILE A 160 10234 11381 13290 2055 -53 -1190 N
ATOM 871 CA ILE A 160 171.807 -11.823 113.338 1.00 91.29 C
ANISOU 871 CA ILE A 160 10349 11124 13214 2016 -30 -1314 C
ATOM 872 C ILE A 160 171.205 -11.018 112.176 1.00 93.64 C
ANISOU 872 C ILE A 160 10648 11610 13321 1872 75 -1410 C
ATOM 873 O ILE A 160 171.051 -11.553 111.077 1.00 94.44 O
ANISOU 873 O ILE A 160 10760 11726 13399 1927 164 -1607 O
ATOM 874 CB ILE A 160 170.762 -12.046 114.483 1.00 93.03 C
ANISOU 874 CB ILE A 160 10764 11103 13481 1910 -147 -1171 C
ATOM 875 CG1 ILE A 160 171.307 -12.986 115.584 1.00 94.93 C
ANISOU 875 CG1 ILE A 160 11019 11138 13912 2054 -258 -1075 C
ATOM 876 CG2 ILE A 160 169.418 -12.566 113.934 1.00 93.12 C
ANISOU 876 CG2 ILE A 160 10957 10959 13464 1827 -122 -1286 C
ATOM 877 CD1 ILE A 160 170.617 -12.851 116.965 1.00100.73 C
ANISOU 877 CD1 ILE A 160 11888 11727 14658 1929 -382 -868 C
ATOM 878 N MET A 161 170.873 -9.739 112.429 1.00 87.62 N
ANISOU 878 N MET A 161 9879 10988 12424 1688 61 -1269 N
ATOM 879 CA MET A 161 170.217 -8.850 111.474 1.00 86.01 C
ANISOU 879 CA MET A 161 9687 10951 12041 1532 136 -1312 C
ATOM 880 C MET A 161 171.160 -8.331 110.389 1.00 90.62 C
ANISOU 880 C MET A 161 10086 11820 12526 1563 245 -1396 C
ATOM 881 O MET A 161 171.712 -7.229 110.483 1.00 89.38 O
ANISOU 881 O MET A 161 9814 11859 12286 1480 250 -1279 O
ATOM 882 CB MET A 161 169.529 -7.691 112.199 1.00 86.05 C
ANISOU 882 CB MET A 161 9758 10977 11960 1340 74 -1127 C
ATOM 883 CG MET A 161 168.432 -8.151 113.107 1.00 88.85 C
ANISOU 883 CG MET A 161 10296 11084 12378 1286 -11 -1061 C
ATOM 884 SD MET A 161 166.902 -8.592 112.263 1.00 92.44 S
ANISOU 884 SD MET A 161 10911 11438 12774 1197 28 -1189 S
ATOM 885 CE MET A 161 166.040 -9.393 113.597 1.00 88.79 C
ANISOU 885 CE MET A 161 10623 10677 12437 1180 -84 -1091 C
ATOM 886 N THR A 162 171.315 -9.147 109.342 1.00 88.97 N
ANISOU 886 N THR A 162 9853 11632 12320 1676 336 -1604 N
ATOM 887 CA THR A 162 172.096 -8.835 108.147 1.00 90.08 C
ANISOU 887 CA THR A 162 9828 12047 12350 1710 460 -1722 C
ATOM 888 C THR A 162 171.147 -8.185 107.144 1.00 93.09 C
ANISOU 888 C THR A 162 10277 12550 12542 1536 517 -1768 C
ATOM 889 O THR A 162 169.934 -8.219 107.362 1.00 91.29 O
ANISOU 889 O THR A 162 10219 12165 12301 1429 462 -1739 O
ATOM 890 CB THR A 162 172.764 -10.105 107.589 1.00 99.64 C
ANISOU 890 CB THR A 162 10982 13211 13666 1936 530 -1937 C
ATOM 891 OG1 THR A 162 171.782 -11.133 107.441 1.00 98.18 O
ANISOU 891 OG1 THR A 162 10987 12773 13542 1962 510 -2068 O
ATOM 892 CG2 THR A 162 173.917 -10.593 108.456 1.00 99.79 C
ANISOU 892 CG2 THR A 162 10880 13171 13863 2122 481 -1878 C
ATOM 893 N VAL A 163 171.681 -7.612 106.045 1.00 90.52 N
ANISOU 893 N VAL A 163 9815 12511 12068 1503 624 -1832 N
ATOM 894 CA VAL A 163 170.886 -6.972 104.985 1.00 89.62 C
ANISOU 894 CA VAL A 163 9746 12547 11760 1340 679 -1868 C
ATOM 895 C VAL A 163 169.925 -8.026 104.373 1.00 93.59 C
ANISOU 895 C VAL A 163 10403 12892 12264 1368 698 -2064 C
ATOM 896 O VAL A 163 168.780 -7.691 104.050 1.00 91.97 O
ANISOU 896 O VAL A 163 10317 12666 11962 1218 675 -2044 O
ATOM 897 CB VAL A 163 171.778 -6.274 103.915 1.00 94.95 C
ANISOU 897 CB VAL A 163 10231 13569 12274 1311 794 -1902 C
ATOM 898 CG1 VAL A 163 170.937 -5.553 102.861 1.00 94.12 C
ANISOU 898 CG1 VAL A 163 10177 13622 11962 1129 835 -1909 C
ATOM 899 CG2 VAL A 163 172.754 -5.295 104.566 1.00 94.35 C
ANISOU 899 CG2 VAL A 163 10004 13633 12212 1274 765 -1708 C
ATOM 900 N LYS A 164 170.377 -9.305 104.292 1.00 91.41 N
ANISOU 900 N LYS A 164 10127 12489 12114 1562 730 -2245 N
ATOM 901 CA LYS A 164 169.596 -10.441 103.791 1.00 91.79 C
ANISOU 901 CA LYS A 164 10326 12357 12194 1606 742 -2447 C
ATOM 902 C LYS A 164 168.441 -10.769 104.752 1.00 93.07 C
ANISOU 902 C LYS A 164 10682 12217 12461 1533 616 -2348 C
ATOM 903 O LYS A 164 167.298 -10.840 104.299 1.00 91.98 O
ANISOU 903 O LYS A 164 10675 12031 12244 1409 603 -2396 O
ATOM 904 CB LYS A 164 170.493 -11.681 103.561 1.00 96.93 C
ANISOU 904 CB LYS A 164 10922 12930 12977 1849 803 -2657 C
ATOM 905 CG LYS A 164 169.715 -12.974 103.283 1.00109.82 C
ANISOU 905 CG LYS A 164 12735 14301 14691 1906 790 -2858 C
ATOM 906 CD LYS A 164 170.494 -13.990 102.470 1.00121.33 C
ANISOU 906 CD LYS A 164 14132 15775 16191 2111 897 -3133 C
ATOM 907 CE LYS A 164 169.667 -15.229 102.230 1.00131.03 C
ANISOU 907 CE LYS A 164 15561 16722 17504 2146 872 -3328 C
ATOM 908 NZ LYS A 164 170.259 -16.094 101.178 1.00142.05 N
ANISOU 908 NZ LYS A 164 16915 18168 18890 2313 995 -3636 N
ATOM 909 N ARG A 165 168.736 -10.967 106.059 1.00 88.43 N
ANISOU 909 N ARG A 165 10109 11448 12044 1602 524 -2205 N
ATOM 910 CA ARG A 165 167.733 -11.315 107.072 1.00 86.64 C
ANISOU 910 CA ARG A 165 10055 10945 11920 1538 408 -2098 C
ATOM 911 C ARG A 165 166.693 -10.209 107.265 1.00 87.42 C
ANISOU 911 C ARG A 165 10216 11107 11892 1319 365 -1937 C
ATOM 912 O ARG A 165 165.508 -10.528 107.366 1.00 86.37 O
ANISOU 912 O ARG A 165 10233 10820 11762 1225 319 -1943 O
ATOM 913 CB ARG A 165 168.379 -11.674 108.416 1.00 87.07 C
ANISOU 913 CB ARG A 165 10093 10831 12159 1653 321 -1965 C
ATOM 914 CG ARG A 165 167.922 -13.036 108.929 1.00 98.87 C
ANISOU 914 CG ARG A 165 11740 11996 13829 1741 253 -2028 C
ATOM 915 CD ARG A 165 168.393 -13.324 110.340 1.00109.39 C
ANISOU 915 CD ARG A 165 13075 13159 15328 1823 147 -1858 C
ATOM 916 NE ARG A 165 168.435 -14.761 110.620 1.00120.07 N
ANISOU 916 NE ARG A 165 14524 14226 16873 1974 102 -1949 N
ATOM 917 CZ ARG A 165 169.487 -15.401 111.126 1.00135.20 C
ANISOU 917 CZ ARG A 165 16363 16054 18952 2172 72 -1938 C
ATOM 918 NH1 ARG A 165 170.596 -14.736 111.426 1.00122.00 N
ANISOU 918 NH1 ARG A 165 14508 14574 17271 2237 81 -1840 N
ATOM 919 NH2 ARG A 165 169.434 -16.708 111.344 1.00123.16 N
ANISOU 919 NH2 ARG A 165 14943 14246 17609 2303 25 -2018 N
ATOM 920 N VAL A 166 167.116 -8.920 107.278 1.00 82.17 N
ANISOU 920 N VAL A 166 9436 10664 11120 1236 382 -1800 N
ATOM 921 CA VAL A 166 166.183 -7.791 107.432 1.00 79.49 C
ANISOU 921 CA VAL A 166 9148 10385 10669 1043 345 -1650 C
ATOM 922 C VAL A 166 165.323 -7.651 106.165 1.00 82.64 C
ANISOU 922 C VAL A 166 9590 10895 10913 936 399 -1760 C
ATOM 923 O VAL A 166 164.157 -7.274 106.269 1.00 81.01 O
ANISOU 923 O VAL A 166 9482 10638 10659 801 354 -1689 O
ATOM 924 CB VAL A 166 166.829 -6.438 107.844 1.00 82.17 C
ANISOU 924 CB VAL A 166 9372 10900 10949 975 335 -1468 C
ATOM 925 CG1 VAL A 166 167.535 -6.553 109.185 1.00 81.72 C
ANISOU 925 CG1 VAL A 166 9289 10728 11033 1055 262 -1346 C
ATOM 926 CG2 VAL A 166 167.766 -5.882 106.776 1.00 83.06 C
ANISOU 926 CG2 VAL A 166 9321 11298 10941 983 432 -1524 C
ATOM 927 N GLY A 167 165.901 -7.988 105.008 1.00 80.15 N
ANISOU 927 N GLY A 167 9196 10736 10523 1000 495 -1934 N
ATOM 928 CA GLY A 167 165.224 -7.977 103.717 1.00 80.04 C
ANISOU 928 CA GLY A 167 9213 10849 10348 909 551 -2062 C
ATOM 929 C GLY A 167 164.123 -9.017 103.670 1.00 83.28 C
ANISOU 929 C GLY A 167 9790 11038 10814 894 510 -2179 C
ATOM 930 O GLY A 167 163.046 -8.749 103.136 1.00 82.09 O
ANISOU 930 O GLY A 167 9712 10926 10555 752 494 -2180 O
ATOM 931 N ILE A 168 164.381 -10.198 104.276 1.00 80.51 N
ANISOU 931 N ILE A 168 9500 10449 10642 1034 482 -2262 N
ATOM 932 CA ILE A 168 163.441 -11.317 104.385 1.00 80.83 C
ANISOU 932 CA ILE A 168 9706 10237 10770 1027 432 -2366 C
ATOM 933 C ILE A 168 162.305 -10.932 105.347 1.00 82.81 C
ANISOU 933 C ILE A 168 10059 10349 11055 889 330 -2174 C
ATOM 934 O ILE A 168 161.143 -11.121 104.996 1.00 82.56 O
ANISOU 934 O ILE A 168 10129 10267 10971 768 302 -2210 O
ATOM 935 CB ILE A 168 164.171 -12.632 104.815 1.00 85.79 C
ANISOU 935 CB ILE A 168 10362 10641 11595 1227 427 -2487 C
ATOM 936 CG1 ILE A 168 165.087 -13.199 103.685 1.00 88.80 C
ANISOU 936 CG1 ILE A 168 10660 11144 11937 1368 541 -2734 C
ATOM 937 CG2 ILE A 168 163.212 -13.710 105.362 1.00 86.56 C
ANISOU 937 CG2 ILE A 168 10643 10418 11827 1205 341 -2517 C
ATOM 938 CD1 ILE A 168 164.418 -13.582 102.289 1.00 98.03 C
ANISOU 938 CD1 ILE A 168 11895 12397 12955 1292 603 -2963 C
ATOM 939 N ILE A 169 162.642 -10.380 106.536 1.00 77.73 N
ANISOU 939 N ILE A 169 9384 9660 10491 902 277 -1976 N
ATOM 940 CA ILE A 169 161.686 -9.961 107.571 1.00 75.54 C
ANISOU 940 CA ILE A 169 9190 9266 10246 786 191 -1791 C
ATOM 941 C ILE A 169 160.725 -8.888 107.006 1.00 77.84 C
ANISOU 941 C ILE A 169 9478 9723 10373 613 198 -1723 C
ATOM 942 O ILE A 169 159.514 -9.048 107.156 1.00 76.86 O
ANISOU 942 O ILE A 169 9454 9502 10246 507 152 -1697 O
ATOM 943 CB ILE A 169 162.428 -9.502 108.866 1.00 77.71 C
ANISOU 943 CB ILE A 169 9414 9501 10613 842 144 -1611 C
ATOM 944 CG1 ILE A 169 163.014 -10.728 109.603 1.00 79.54 C
ANISOU 944 CG1 ILE A 169 9686 9507 11029 994 104 -1649 C
ATOM 945 CG2 ILE A 169 161.517 -8.698 109.811 1.00 76.15 C
ANISOU 945 CG2 ILE A 169 9274 9263 10396 707 79 -1417 C
ATOM 946 CD1 ILE A 169 164.233 -10.463 110.448 1.00 86.58 C
ANISOU 946 CD1 ILE A 169 10475 10423 11998 1102 82 -1539 C
ATOM 947 N ILE A 170 161.254 -7.845 106.323 1.00 73.91 N
ANISOU 947 N ILE A 170 8863 9474 9743 584 254 -1694 N
ATOM 948 CA ILE A 170 160.449 -6.779 105.704 1.00 72.65 C
ANISOU 948 CA ILE A 170 8691 9481 9431 432 257 -1620 C
ATOM 949 C ILE A 170 159.521 -7.395 104.632 1.00 78.17 C
ANISOU 949 C ILE A 170 9458 10195 10047 363 271 -1772 C
ATOM 950 O ILE A 170 158.333 -7.062 104.603 1.00 77.02 O
ANISOU 950 O ILE A 170 9370 10040 9856 238 226 -1705 O
ATOM 951 CB ILE A 170 161.347 -5.634 105.143 1.00 75.44 C
ANISOU 951 CB ILE A 170 8905 10091 9667 419 313 -1559 C
ATOM 952 CG1 ILE A 170 161.910 -4.774 106.297 1.00 74.36 C
ANISOU 952 CG1 ILE A 170 8722 9935 9597 428 274 -1371 C
ATOM 953 CG2 ILE A 170 160.593 -4.751 104.129 1.00 75.57 C
ANISOU 953 CG2 ILE A 170 8907 10296 9511 275 326 -1526 C
ATOM 954 CD1 ILE A 170 163.200 -4.025 105.989 1.00 82.08 C
ANISOU 954 CD1 ILE A 170 9554 11115 10517 459 326 -1333 C
ATOM 955 N SER A 171 160.055 -8.317 103.793 1.00 76.92 N
ANISOU 955 N SER A 171 9292 10057 9875 447 329 -1980 N
ATOM 956 CA SER A 171 159.292 -9.018 102.753 1.00 77.97 C
ANISOU 956 CA SER A 171 9497 10200 9926 387 342 -2156 C
ATOM 957 C SER A 171 158.180 -9.867 103.366 1.00 81.90 C
ANISOU 957 C SER A 171 10138 10444 10535 337 263 -2162 C
ATOM 958 O SER A 171 157.078 -9.882 102.826 1.00 81.38 O
ANISOU 958 O SER A 171 10128 10407 10387 207 234 -2187 O
ATOM 959 CB SER A 171 160.206 -9.894 101.903 1.00 83.63 C
ANISOU 959 CB SER A 171 10184 10962 10629 511 425 -2391 C
ATOM 960 OG SER A 171 161.167 -9.111 101.214 1.00 92.65 O
ANISOU 960 OG SER A 171 11184 12373 11645 536 508 -2389 O
ATOM 961 N CYS A 172 158.461 -10.542 104.505 1.00 78.67 N
ANISOU 961 N CYS A 172 9782 9799 10309 431 221 -2125 N
ATOM 962 CA CYS A 172 157.505 -11.373 105.241 1.00 78.48 C
ANISOU 962 CA CYS A 172 9891 9522 10405 383 143 -2106 C
ATOM 963 C CYS A 172 156.444 -10.499 105.901 1.00 80.01 C
ANISOU 963 C CYS A 172 10098 9733 10569 243 86 -1903 C
ATOM 964 O CYS A 172 155.286 -10.909 105.965 1.00 79.61 O
ANISOU 964 O CYS A 172 10134 9586 10530 135 36 -1902 O
ATOM 965 CB CYS A 172 158.214 -12.254 106.265 1.00 79.55 C
ANISOU 965 CB CYS A 172 10069 9422 10735 525 114 -2101 C
ATOM 966 SG CYS A 172 159.123 -13.645 105.543 1.00 86.33 S
ANISOU 966 SG CYS A 172 10955 10172 11677 695 165 -2372 S
ATOM 967 N ILE A 173 156.837 -9.297 106.380 1.00 74.81 N
ANISOU 967 N ILE A 173 9351 9198 9875 243 94 -1736 N
ATOM 968 CA ILE A 173 155.936 -8.313 106.986 1.00 72.77 C
ANISOU 968 CA ILE A 173 9092 8973 9584 130 51 -1548 C
ATOM 969 C ILE A 173 154.942 -7.869 105.913 1.00 76.91 C
ANISOU 969 C ILE A 173 9606 9652 9964 0 55 -1576 C
ATOM 970 O ILE A 173 153.742 -8.000 106.121 1.00 76.19 O
ANISOU 970 O ILE A 173 9571 9496 9881 -102 7 -1533 O
ATOM 971 CB ILE A 173 156.723 -7.118 107.618 1.00 74.51 C
ANISOU 971 CB ILE A 173 9224 9293 9796 166 63 -1391 C
ATOM 972 CG1 ILE A 173 157.194 -7.456 109.044 1.00 74.45 C
ANISOU 972 CG1 ILE A 173 9250 9107 9933 243 24 -1302 C
ATOM 973 CG2 ILE A 173 155.924 -5.796 107.599 1.00 73.64 C
ANISOU 973 CG2 ILE A 173 9080 9310 9590 50 49 -1245 C
ATOM 974 CD1 ILE A 173 158.396 -6.652 109.515 1.00 79.72 C
ANISOU 974 CD1 ILE A 173 9824 9862 10605 315 40 -1212 C
ATOM 975 N TRP A 174 155.452 -7.417 104.749 1.00 74.42 N
ANISOU 975 N TRP A 174 9214 9546 9516 1 109 -1649 N
ATOM 976 CA TRP A 174 154.651 -6.938 103.630 1.00 74.64 C
ANISOU 976 CA TRP A 174 9220 9751 9388 -120 110 -1668 C
ATOM 977 C TRP A 174 153.826 -8.052 102.989 1.00 79.59 C
ANISOU 977 C TRP A 174 9933 10309 9999 -182 87 -1830 C
ATOM 978 O TRP A 174 152.713 -7.773 102.557 1.00 78.95 O
ANISOU 978 O TRP A 174 9860 10298 9838 -309 48 -1794 O
ATOM 979 CB TRP A 174 155.531 -6.242 102.593 1.00 74.20 C
ANISOU 979 CB TRP A 174 9063 9941 9190 -102 176 -1701 C
ATOM 980 CG TRP A 174 155.813 -4.816 102.961 1.00 73.98 C
ANISOU 980 CG TRP A 174 8954 10025 9130 -122 174 -1502 C
ATOM 981 CD1 TRP A 174 156.905 -4.339 103.624 1.00 76.34 C
ANISOU 981 CD1 TRP A 174 9196 10323 9488 -38 198 -1426 C
ATOM 982 CD2 TRP A 174 154.939 -3.695 102.768 1.00 72.98 C
ANISOU 982 CD2 TRP A 174 8802 10004 8922 -235 136 -1351 C
ATOM 983 NE1 TRP A 174 156.785 -2.983 103.821 1.00 74.61 N
ANISOU 983 NE1 TRP A 174 8925 10200 9222 -100 179 -1245 N
ATOM 984 CE2 TRP A 174 155.588 -2.560 103.303 1.00 75.82 C
ANISOU 984 CE2 TRP A 174 9099 10414 9295 -213 142 -1196 C
ATOM 985 CE3 TRP A 174 153.673 -3.535 102.175 1.00 74.34 C
ANISOU 985 CE3 TRP A 174 8995 10237 9014 -353 92 -1330 C
ATOM 986 CZ2 TRP A 174 155.022 -1.280 103.251 1.00 74.24 C
ANISOU 986 CZ2 TRP A 174 8866 10303 9039 -296 109 -1028 C
ATOM 987 CZ3 TRP A 174 153.110 -2.269 102.132 1.00 74.89 C
ANISOU 987 CZ3 TRP A 174 9019 10407 9029 -426 58 -1154 C
ATOM 988 CH2 TRP A 174 153.781 -1.159 102.663 1.00 74.56 C
ANISOU 988 CH2 TRP A 174 8924 10394 9010 -394 68 -1008 C
ATOM 989 N ALA A 175 154.330 -9.304 102.964 1.00 77.55 N
ANISOU 989 N ALA A 175 9738 9902 9824 -96 105 -2004 N
ATOM 990 CA ALA A 175 153.589 -10.444 102.414 1.00 78.76 C
ANISOU 990 CA ALA A 175 9991 9955 9979 -158 78 -2173 C
ATOM 991 C ALA A 175 152.401 -10.786 103.308 1.00 81.80 C
ANISOU 991 C ALA A 175 10458 10157 10466 -251 -4 -2071 C
ATOM 992 O ALA A 175 151.298 -10.969 102.796 1.00 81.82 O
ANISOU 992 O ALA A 175 10494 10189 10403 -386 -46 -2101 O
ATOM 993 CB ALA A 175 154.497 -11.654 102.258 1.00 81.31 C
ANISOU 993 CB ALA A 175 10367 10138 10390 -24 118 -2378 C
ATOM 994 N ALA A 176 152.617 -10.835 104.640 1.00 77.44 N
ANISOU 994 N ALA A 176 9927 9435 10062 -189 -28 -1944 N
ATOM 995 CA ALA A 176 151.569 -11.127 105.617 1.00 76.77 C
ANISOU 995 CA ALA A 176 9911 9188 10072 -274 -97 -1830 C
ATOM 996 C ALA A 176 150.563 -9.981 105.706 1.00 79.93 C
ANISOU 996 C ALA A 176 10248 9737 10386 -392 -120 -1663 C
ATOM 997 O ALA A 176 149.375 -10.240 105.877 1.00 79.51 O
ANISOU 997 O ALA A 176 10232 9635 10343 -510 -170 -1625 O
ATOM 998 CB ALA A 176 152.177 -11.394 106.983 1.00 76.91 C
ANISOU 998 CB ALA A 176 9958 9018 10245 -174 -111 -1732 C
ATOM 999 N CYS A 177 151.033 -8.724 105.564 1.00 76.03 N
ANISOU 999 N CYS A 177 9655 9423 9809 -359 -84 -1565 N
ATOM 1000 CA CYS A 177 150.188 -7.532 105.635 1.00 74.81 C
ANISOU 1000 CA CYS A 177 9436 9404 9585 -446 -104 -1404 C
ATOM 1001 C CYS A 177 149.348 -7.352 104.375 1.00 79.62 C
ANISOU 1001 C CYS A 177 10016 10181 10055 -561 -121 -1457 C
ATOM 1002 O CYS A 177 148.232 -6.851 104.489 1.00 78.72 O
ANISOU 1002 O CYS A 177 9876 10117 9918 -655 -162 -1348 O
ATOM 1003 CB CYS A 177 151.014 -6.288 105.935 1.00 73.98 C
ANISOU 1003 CB CYS A 177 9250 9405 9453 -376 -70 -1283 C
ATOM 1004 SG CYS A 177 151.667 -6.239 107.622 1.00 76.79 S
ANISOU 1004 SG CYS A 177 9632 9586 9958 -280 -73 -1168 S
ATOM 1005 N THR A 178 149.860 -7.749 103.188 1.00 77.59 N
ANISOU 1005 N THR A 178 9757 10022 9700 -553 -90 -1621 N
ATOM 1006 CA THR A 178 149.086 -7.657 101.942 1.00 78.32 C
ANISOU 1006 CA THR A 178 9828 10288 9644 -672 -113 -1681 C
ATOM 1007 C THR A 178 147.992 -8.715 101.957 1.00 83.01 C
ANISOU 1007 C THR A 178 10503 10756 10280 -777 -173 -1759 C
ATOM 1008 O THR A 178 146.855 -8.411 101.601 1.00 82.53 O
ANISOU 1008 O THR A 178 10412 10792 10153 -902 -225 -1698 O
ATOM 1009 CB THR A 178 149.962 -7.769 100.693 1.00 87.96 C
ANISOU 1009 CB THR A 178 11024 11665 10730 -641 -57 -1840 C
ATOM 1010 OG1 THR A 178 150.888 -8.842 100.854 1.00 90.44 O
ANISOU 1010 OG1 THR A 178 11402 11830 11131 -531 -14 -2008 O
ATOM 1011 CG2 THR A 178 150.692 -6.480 100.378 1.00 85.26 C
ANISOU 1011 CG2 THR A 178 10579 11523 10294 -603 -14 -1727 C
ATOM 1012 N VAL A 179 148.329 -9.940 102.418 1.00 80.45 N
ANISOU 1012 N VAL A 179 10278 10212 10078 -728 -171 -1881 N
ATOM 1013 CA VAL A 179 147.401 -11.065 102.548 1.00 81.34 C
ANISOU 1013 CA VAL A 179 10485 10164 10257 -829 -231 -1957 C
ATOM 1014 C VAL A 179 146.313 -10.680 103.570 1.00 84.23 C
ANISOU 1014 C VAL A 179 10830 10479 10694 -909 -282 -1758 C
ATOM 1015 O VAL A 179 145.131 -10.755 103.234 1.00 84.59 O
ANISOU 1015 O VAL A 179 10865 10581 10692 -1052 -336 -1739 O
ATOM 1016 CB VAL A 179 148.142 -12.389 102.907 1.00 86.30 C
ANISOU 1016 CB VAL A 179 11227 10543 11020 -737 -218 -2111 C
ATOM 1017 CG1 VAL A 179 147.192 -13.448 103.464 1.00 86.82 C
ANISOU 1017 CG1 VAL A 179 11397 10392 11200 -842 -288 -2122 C
ATOM 1018 CG2 VAL A 179 148.899 -12.937 101.700 1.00 87.87 C
ANISOU 1018 CG2 VAL A 179 11451 10802 11133 -688 -171 -2349 C
ATOM 1019 N SER A 180 146.714 -10.203 104.773 1.00 79.10 N
ANISOU 1019 N SER A 180 10163 9747 10144 -821 -262 -1612 N
ATOM 1020 CA SER A 180 145.792 -9.780 105.834 1.00 77.62 C
ANISOU 1020 CA SER A 180 9952 9521 10020 -878 -293 -1429 C
ATOM 1021 C SER A 180 144.943 -8.581 105.403 1.00 80.51 C
ANISOU 1021 C SER A 180 10208 10103 10278 -950 -306 -1309 C
ATOM 1022 O SER A 180 143.743 -8.586 105.648 1.00 80.22 O
ANISOU 1022 O SER A 180 10149 10078 10252 -1058 -348 -1233 O
ATOM 1023 CB SER A 180 146.546 -9.447 107.118 1.00 79.71 C
ANISOU 1023 CB SER A 180 10221 9678 10386 -762 -263 -1315 C
ATOM 1024 OG SER A 180 147.275 -10.565 107.595 1.00 88.67 O
ANISOU 1024 OG SER A 180 11452 10604 11634 -692 -264 -1401 O
ATOM 1025 N GLY A 181 145.564 -7.600 104.744 1.00 76.37 N
ANISOU 1025 N GLY A 181 9613 9749 9655 -893 -272 -1291 N
ATOM 1026 CA GLY A 181 144.910 -6.393 104.244 1.00 75.54 C
ANISOU 1026 CA GLY A 181 9405 9846 9451 -943 -288 -1172 C
ATOM 1027 C GLY A 181 143.789 -6.665 103.262 1.00 80.52 C
ANISOU 1027 C GLY A 181 10012 10594 9989 -1084 -346 -1216 C
ATOM 1028 O GLY A 181 142.722 -6.055 103.367 1.00 79.71 O
ANISOU 1028 O GLY A 181 9837 10575 9874 -1152 -384 -1089 O
ATOM 1029 N ILE A 182 144.019 -7.600 102.310 1.00 78.63 N
ANISOU 1029 N ILE A 182 9830 10361 9684 -1128 -353 -1402 N
ATOM 1030 CA ILE A 182 143.035 -8.015 101.302 1.00 79.77 C
ANISOU 1030 CA ILE A 182 9967 10615 9727 -1277 -415 -1475 C
ATOM 1031 C ILE A 182 141.876 -8.731 102.020 1.00 83.85 C
ANISOU 1031 C ILE A 182 10513 11000 10345 -1382 -470 -1440 C
ATOM 1032 O ILE A 182 140.719 -8.384 101.782 1.00 83.65 O
ANISOU 1032 O ILE A 182 10414 11095 10276 -1493 -526 -1352 O
ATOM 1033 CB ILE A 182 143.692 -8.881 100.180 1.00 84.53 C
ANISOU 1033 CB ILE A 182 10640 11242 10235 -1289 -398 -1708 C
ATOM 1034 CG1 ILE A 182 144.582 -8.006 99.264 1.00 84.81 C
ANISOU 1034 CG1 ILE A 182 10612 11486 10126 -1226 -349 -1716 C
ATOM 1035 CG2 ILE A 182 142.639 -9.636 99.346 1.00 87.05 C
ANISOU 1035 CG2 ILE A 182 10987 11613 10477 -1461 -472 -1814 C
ATOM 1036 CD1 ILE A 182 145.664 -8.766 98.448 1.00 93.11 C
ANISOU 1036 CD1 ILE A 182 11728 12543 11109 -1173 -292 -1947 C
ATOM 1037 N LEU A 183 142.202 -9.682 102.932 1.00 80.42 N
ANISOU 1037 N LEU A 183 10178 10328 10049 -1346 -456 -1491 N
ATOM 1038 CA LEU A 183 141.247 -10.457 103.737 1.00 80.53 C
ANISOU 1038 CA LEU A 183 10233 10194 10172 -1446 -502 -1452 C
ATOM 1039 C LEU A 183 140.383 -9.553 104.620 1.00 83.33 C
ANISOU 1039 C LEU A 183 10487 10610 10564 -1463 -507 -1237 C
ATOM 1040 O LEU A 183 139.188 -9.806 104.764 1.00 83.71 O
ANISOU 1040 O LEU A 183 10501 10679 10627 -1593 -557 -1183 O
ATOM 1041 CB LEU A 183 141.980 -11.485 104.623 1.00 80.71 C
ANISOU 1041 CB LEU A 183 10380 9949 10338 -1376 -480 -1517 C
ATOM 1042 CG LEU A 183 142.580 -12.717 103.937 1.00 87.16 C
ANISOU 1042 CG LEU A 183 11318 10637 11163 -1374 -487 -1745 C
ATOM 1043 CD1 LEU A 183 143.616 -13.371 104.824 1.00 87.19 C
ANISOU 1043 CD1 LEU A 183 11415 10402 11309 -1242 -453 -1776 C
ATOM 1044 CD2 LEU A 183 141.508 -13.732 103.560 1.00 91.44 C
ANISOU 1044 CD2 LEU A 183 11919 11114 11708 -1558 -562 -1830 C
ATOM 1045 N PHE A 184 140.989 -8.498 105.197 1.00 78.22 N
ANISOU 1045 N PHE A 184 9789 9997 9933 -1333 -454 -1122 N
ATOM 1046 CA PHE A 184 140.332 -7.523 106.069 1.00 76.77 C
ANISOU 1046 CA PHE A 184 9516 9866 9787 -1317 -444 -934 C
ATOM 1047 C PHE A 184 139.298 -6.686 105.314 1.00 81.48 C
ANISOU 1047 C PHE A 184 9987 10679 10291 -1391 -485 -852 C
ATOM 1048 O PHE A 184 138.285 -6.319 105.899 1.00 81.00 O
ANISOU 1048 O PHE A 184 9851 10656 10270 -1434 -498 -729 O
ATOM 1049 CB PHE A 184 141.376 -6.601 106.722 1.00 76.87 C
ANISOU 1049 CB PHE A 184 9520 9859 9827 -1161 -382 -859 C
ATOM 1050 CG PHE A 184 141.998 -7.049 108.031 1.00 77.67 C
ANISOU 1050 CG PHE A 184 9701 9765 10046 -1089 -348 -838 C
ATOM 1051 CD1 PHE A 184 142.119 -8.401 108.343 1.00 81.60 C
ANISOU 1051 CD1 PHE A 184 10303 10084 10618 -1127 -366 -929 C
ATOM 1052 CD2 PHE A 184 142.503 -6.119 108.932 1.00 78.46 C
ANISOU 1052 CD2 PHE A 184 9775 9856 10180 -985 -305 -728 C
ATOM 1053 CE1 PHE A 184 142.711 -8.810 109.541 1.00 82.11 C
ANISOU 1053 CE1 PHE A 184 10439 9973 10787 -1061 -345 -892 C
ATOM 1054 CE2 PHE A 184 143.096 -6.531 110.131 1.00 80.79 C
ANISOU 1054 CE2 PHE A 184 10141 9987 10568 -925 -282 -703 C
ATOM 1055 CZ PHE A 184 143.197 -7.872 110.425 1.00 79.78 C
ANISOU 1055 CZ PHE A 184 10110 9692 10510 -962 -304 -778 C
ATOM 1056 N ILE A 185 139.550 -6.387 104.027 1.00 78.97 N
ANISOU 1056 N ILE A 185 9642 10512 9849 -1406 -505 -917 N
ATOM 1057 CA ILE A 185 138.646 -5.596 103.184 1.00 79.24 C
ANISOU 1057 CA ILE A 185 9559 10762 9785 -1475 -556 -834 C
ATOM 1058 C ILE A 185 137.503 -6.497 102.674 1.00 85.05 C
ANISOU 1058 C ILE A 185 10286 11539 10491 -1647 -632 -893 C
ATOM 1059 O ILE A 185 136.388 -6.002 102.479 1.00 85.12 O
ANISOU 1059 O ILE A 185 10181 11687 10474 -1719 -683 -784 O
ATOM 1060 CB ILE A 185 139.443 -4.875 102.055 1.00 82.27 C
ANISOU 1060 CB ILE A 185 9920 11300 10037 -1426 -548 -861 C
ATOM 1061 CG1 ILE A 185 140.417 -3.812 102.638 1.00 80.85 C
ANISOU 1061 CG1 ILE A 185 9729 11095 9897 -1274 -483 -766 C
ATOM 1062 CG2 ILE A 185 138.560 -4.283 100.942 1.00 83.97 C
ANISOU 1062 CG2 ILE A 185 10031 11747 10128 -1520 -620 -798 C
ATOM 1063 CD1 ILE A 185 139.868 -2.775 103.675 1.00 85.02 C
ANISOU 1063 CD1 ILE A 185 10183 11605 10516 -1213 -472 -580 C
ATOM 1064 N ILE A 186 137.763 -7.815 102.513 1.00 82.84 N
ANISOU 1064 N ILE A 186 10123 11127 10226 -1712 -642 -1061 N
ATOM 1065 CA ILE A 186 136.747 -8.801 102.113 1.00 84.38 C
ANISOU 1065 CA ILE A 186 10333 11323 10405 -1892 -717 -1134 C
ATOM 1066 C ILE A 186 135.699 -8.878 103.240 1.00 88.41 C
ANISOU 1066 C ILE A 186 10788 11774 11030 -1950 -730 -996 C
ATOM 1067 O ILE A 186 134.499 -8.779 102.970 1.00 88.86 O
ANISOU 1067 O ILE A 186 10743 11962 11056 -2073 -792 -927 O
ATOM 1068 CB ILE A 186 137.382 -10.190 101.783 1.00 88.61 C
ANISOU 1068 CB ILE A 186 11027 11689 10953 -1930 -720 -1354 C
ATOM 1069 CG1 ILE A 186 138.209 -10.131 100.482 1.00 89.66 C
ANISOU 1069 CG1 ILE A 186 11191 11935 10940 -1900 -709 -1506 C
ATOM 1070 CG2 ILE A 186 136.316 -11.301 101.698 1.00 91.01 C
ANISOU 1070 CG2 ILE A 186 11367 11932 11282 -2125 -798 -1415 C
ATOM 1071 CD1 ILE A 186 139.324 -11.177 100.379 1.00 97.63 C
ANISOU 1071 CD1 ILE A 186 12351 12758 11985 -1837 -666 -1714 C
ATOM 1072 N TYR A 187 136.171 -8.996 104.499 1.00 84.10 N
ANISOU 1072 N TYR A 187 10297 11049 10607 -1857 -669 -947 N
ATOM 1073 CA TYR A 187 135.327 -9.072 105.690 1.00 83.65 C
ANISOU 1073 CA TYR A 187 10197 10934 10654 -1900 -662 -818 C
ATOM 1074 C TYR A 187 135.328 -7.729 106.454 1.00 85.49 C
ANISOU 1074 C TYR A 187 10329 11241 10912 -1768 -604 -653 C
ATOM 1075 O TYR A 187 135.335 -7.718 107.687 1.00 84.32 O
ANISOU 1075 O TYR A 187 10195 10987 10854 -1723 -557 -575 O
ATOM 1076 CB TYR A 187 135.775 -10.236 106.601 1.00 85.27 C
ANISOU 1076 CB TYR A 187 10543 10884 10970 -1912 -644 -877 C
ATOM 1077 CG TYR A 187 135.892 -11.571 105.897 1.00 89.07 C
ANISOU 1077 CG TYR A 187 11147 11250 11446 -2023 -698 -1055 C
ATOM 1078 CD1 TYR A 187 134.759 -12.323 105.591 1.00 92.76 C
ANISOU 1078 CD1 TYR A 187 11601 11736 11907 -2221 -773 -1076 C
ATOM 1079 CD2 TYR A 187 137.135 -12.103 105.568 1.00 90.05 C
ANISOU 1079 CD2 TYR A 187 11400 11238 11578 -1930 -675 -1208 C
ATOM 1080 CE1 TYR A 187 134.861 -13.557 104.948 1.00 95.37 C
ANISOU 1080 CE1 TYR A 187 12057 11943 12236 -2330 -827 -1252 C
ATOM 1081 CE2 TYR A 187 137.250 -13.335 104.927 1.00 92.81 C
ANISOU 1081 CE2 TYR A 187 11870 11465 11930 -2020 -720 -1389 C
ATOM 1082 CZ TYR A 187 136.110 -14.061 104.622 1.00101.90 C
ANISOU 1082 CZ TYR A 187 13021 12623 13074 -2223 -798 -1414 C
ATOM 1083 OH TYR A 187 136.220 -15.279 103.995 1.00105.02 O
ANISOU 1083 OH TYR A 187 13547 12880 13475 -2318 -847 -1605 O
ATOM 1084 N SER A 188 135.281 -6.599 105.714 1.00 81.54 N
ANISOU 1084 N SER A 188 9729 10923 10329 -1712 -612 -597 N
ATOM 1085 CA SER A 188 135.246 -5.250 106.291 1.00 80.14 C
ANISOU 1085 CA SER A 188 9458 10815 10176 -1587 -566 -450 C
ATOM 1086 C SER A 188 133.963 -5.025 107.092 1.00 85.27 C
ANISOU 1086 C SER A 188 9996 11516 10889 -1634 -565 -322 C
ATOM 1087 O SER A 188 134.010 -4.378 108.134 1.00 83.72 O
ANISOU 1087 O SER A 188 9774 11279 10756 -1537 -503 -231 O
ATOM 1088 CB SER A 188 135.386 -4.191 105.204 1.00 83.24 C
ANISOU 1088 CB SER A 188 9774 11384 10470 -1540 -592 -414 C
ATOM 1089 OG SER A 188 134.302 -4.214 104.291 1.00 93.58 O
ANISOU 1089 OG SER A 188 10983 12865 11709 -1661 -672 -391 O
ATOM 1090 N ASP A 189 132.835 -5.597 106.629 1.00 84.32 N
ANISOU 1090 N ASP A 189 9806 11486 10745 -1790 -632 -323 N
ATOM 1091 CA ASP A 189 131.534 -5.514 107.293 1.00 85.09 C
ANISOU 1091 CA ASP A 189 9778 11657 10896 -1858 -634 -208 C
ATOM 1092 C ASP A 189 131.509 -6.327 108.598 1.00 89.04 C
ANISOU 1092 C ASP A 189 10351 11991 11488 -1894 -584 -203 C
ATOM 1093 O ASP A 189 130.665 -6.061 109.455 1.00 88.88 O
ANISOU 1093 O ASP A 189 10232 12019 11517 -1905 -550 -96 O
ATOM 1094 CB ASP A 189 130.414 -5.993 106.350 1.00 88.88 C
ANISOU 1094 CB ASP A 189 10165 12286 11318 -2033 -731 -218 C
ATOM 1095 CG ASP A 189 129.755 -4.907 105.512 1.00100.80 C
ANISOU 1095 CG ASP A 189 11512 14024 12766 -2006 -780 -122 C
ATOM 1096 OD1 ASP A 189 130.139 -3.721 105.656 1.00100.54 O
ANISOU 1096 OD1 ASP A 189 11436 14023 12741 -1845 -737 -43 O
ATOM 1097 OD2 ASP A 189 128.842 -5.239 104.725 1.00108.20 O
ANISOU 1097 OD2 ASP A 189 12361 15102 13647 -2150 -867 -120 O
ATOM 1098 N SER A 190 132.427 -7.303 108.749 1.00 85.49 N
ANISOU 1098 N SER A 190 10071 11352 11061 -1908 -579 -315 N
ATOM 1099 CA SER A 190 132.522 -8.154 109.935 1.00 85.37 C
ANISOU 1099 CA SER A 190 10146 11162 11131 -1946 -544 -305 C
ATOM 1100 C SER A 190 133.197 -7.425 111.094 1.00 86.94 C
ANISOU 1100 C SER A 190 10365 11293 11374 -1787 -456 -232 C
ATOM 1101 O SER A 190 134.176 -6.700 110.890 1.00 85.60 O
ANISOU 1101 O SER A 190 10229 11113 11183 -1644 -428 -255 O
ATOM 1102 CB SER A 190 133.267 -9.446 109.618 1.00 90.39 C
ANISOU 1102 CB SER A 190 10952 11609 11784 -2008 -581 -448 C
ATOM 1103 OG SER A 190 132.539 -10.229 108.684 1.00103.17 O
ANISOU 1103 OG SER A 190 12563 13274 13364 -2181 -664 -522 O
ATOM 1104 N SER A 191 132.660 -7.626 112.311 1.00 82.89 N
ANISOU 1104 N SER A 191 9833 10744 10917 -1825 -414 -142 N
ATOM 1105 CA SER A 191 133.138 -7.020 113.556 1.00 81.20 C
ANISOU 1105 CA SER A 191 9639 10477 10737 -1701 -331 -70 C
ATOM 1106 C SER A 191 134.560 -7.453 113.902 1.00 83.45 C
ANISOU 1106 C SER A 191 10090 10569 11049 -1619 -319 -137 C
ATOM 1107 O SER A 191 135.340 -6.620 114.353 1.00 81.99 O
ANISOU 1107 O SER A 191 9921 10370 10861 -1476 -269 -115 O
ATOM 1108 CB SER A 191 132.205 -7.367 114.711 1.00 85.32 C
ANISOU 1108 CB SER A 191 10111 11012 11295 -1794 -294 29 C
ATOM 1109 OG SER A 191 130.930 -6.774 114.532 1.00 94.36 O
ANISOU 1109 OG SER A 191 11075 12354 12422 -1837 -289 103 O
ATOM 1110 N ALA A 192 134.897 -8.740 113.665 1.00 80.03 N
ANISOU 1110 N ALA A 192 9776 9986 10645 -1707 -369 -219 N
ATOM 1111 CA ALA A 192 136.202 -9.350 113.943 1.00 79.10 C
ANISOU 1111 CA ALA A 192 9813 9673 10568 -1634 -368 -287 C
ATOM 1112 C ALA A 192 137.376 -8.566 113.338 1.00 80.81 C
ANISOU 1112 C ALA A 192 10046 9910 10748 -1473 -350 -352 C
ATOM 1113 O ALA A 192 138.395 -8.412 114.008 1.00 79.62 O
ANISOU 1113 O ALA A 192 9962 9664 10625 -1363 -317 -343 O
ATOM 1114 CB ALA A 192 136.227 -10.782 113.432 1.00 81.28 C
ANISOU 1114 CB ALA A 192 10196 9805 10882 -1752 -436 -388 C
ATOM 1115 N VAL A 193 137.224 -8.063 112.094 1.00 76.66 N
ANISOU 1115 N VAL A 193 9453 9520 10154 -1470 -374 -407 N
ATOM 1116 CA VAL A 193 138.244 -7.298 111.367 1.00 75.21 C
ANISOU 1116 CA VAL A 193 9271 9386 9920 -1342 -359 -461 C
ATOM 1117 C VAL A 193 138.426 -5.909 112.011 1.00 77.30 C
ANISOU 1117 C VAL A 193 9466 9727 10177 -1223 -303 -352 C
ATOM 1118 O VAL A 193 139.563 -5.516 112.284 1.00 75.85 O
ANISOU 1118 O VAL A 193 9333 9486 10001 -1107 -272 -364 O
ATOM 1119 CB VAL A 193 137.902 -7.214 109.851 1.00 79.65 C
ANISOU 1119 CB VAL A 193 9780 10086 10397 -1400 -408 -537 C
ATOM 1120 CG1 VAL A 193 138.576 -6.023 109.166 1.00 78.44 C
ANISOU 1120 CG1 VAL A 193 9577 10054 10174 -1285 -388 -530 C
ATOM 1121 CG2 VAL A 193 138.260 -8.516 109.142 1.00 80.65 C
ANISOU 1121 CG2 VAL A 193 10014 10106 10523 -1471 -452 -691 C
ATOM 1122 N ILE A 194 137.310 -5.186 112.256 1.00 73.78 N
ANISOU 1122 N ILE A 194 8904 9407 9723 -1250 -291 -252 N
ATOM 1123 CA ILE A 194 137.300 -3.842 112.850 1.00 72.38 C
ANISOU 1123 CA ILE A 194 8658 9298 9546 -1141 -239 -157 C
ATOM 1124 C ILE A 194 137.863 -3.912 114.283 1.00 75.01 C
ANISOU 1124 C ILE A 194 9065 9507 9927 -1085 -186 -120 C
ATOM 1125 O ILE A 194 138.682 -3.066 114.639 1.00 73.82 O
ANISOU 1125 O ILE A 194 8935 9340 9774 -971 -152 -103 O
ATOM 1126 CB ILE A 194 135.886 -3.189 112.781 1.00 76.05 C
ANISOU 1126 CB ILE A 194 8974 9919 10003 -1180 -239 -69 C
ATOM 1127 CG1 ILE A 194 135.337 -3.219 111.331 1.00 77.32 C
ANISOU 1127 CG1 ILE A 194 9062 10211 10107 -1251 -309 -99 C
ATOM 1128 CG2 ILE A 194 135.909 -1.749 113.315 1.00 75.81 C
ANISOU 1128 CG2 ILE A 194 8880 9943 9981 -1050 -186 13 C
ATOM 1129 CD1 ILE A 194 133.837 -3.097 111.187 1.00 85.04 C
ANISOU 1129 CD1 ILE A 194 9895 11332 11084 -1336 -333 -26 C
ATOM 1130 N ILE A 195 137.483 -4.952 115.065 1.00 71.60 N
ANISOU 1130 N ILE A 195 8681 8987 9535 -1175 -186 -108 N
ATOM 1131 CA ILE A 195 137.971 -5.180 116.433 1.00 70.79 C
ANISOU 1131 CA ILE A 195 8657 8771 9468 -1146 -147 -64 C
ATOM 1132 C ILE A 195 139.487 -5.479 116.390 1.00 74.09 C
ANISOU 1132 C ILE A 195 9191 9058 9903 -1060 -160 -129 C
ATOM 1133 O ILE A 195 140.213 -4.971 117.242 1.00 73.02 O
ANISOU 1133 O ILE A 195 9090 8883 9771 -974 -126 -93 O
ATOM 1134 CB ILE A 195 137.152 -6.293 117.164 1.00 74.89 C
ANISOU 1134 CB ILE A 195 9198 9235 10021 -1284 -154 -21 C
ATOM 1135 CG1 ILE A 195 135.746 -5.768 117.544 1.00 75.65 C
ANISOU 1135 CG1 ILE A 195 9158 9484 10099 -1342 -116 65 C
ATOM 1136 CG2 ILE A 195 137.878 -6.838 118.413 1.00 75.43 C
ANISOU 1136 CG2 ILE A 195 9379 9158 10121 -1268 -138 16 C
ATOM 1137 CD1 ILE A 195 134.649 -6.825 117.641 1.00 83.88 C
ANISOU 1137 CD1 ILE A 195 10174 10535 11160 -1518 -143 95 C
ATOM 1138 N CYS A 196 139.959 -6.242 115.378 1.00 71.28 N
ANISOU 1138 N CYS A 196 8885 8647 9550 -1081 -209 -230 N
ATOM 1139 CA CYS A 196 141.375 -6.591 115.207 1.00 70.96 C
ANISOU 1139 CA CYS A 196 8937 8497 9530 -993 -219 -305 C
ATOM 1140 C CYS A 196 142.234 -5.342 114.958 1.00 72.97 C
ANISOU 1140 C CYS A 196 9152 8829 9742 -868 -189 -300 C
ATOM 1141 O CYS A 196 143.317 -5.230 115.538 1.00 72.00 O
ANISOU 1141 O CYS A 196 9082 8634 9641 -783 -175 -296 O
ATOM 1142 CB CYS A 196 141.562 -7.615 114.092 1.00 72.52 C
ANISOU 1142 CB CYS A 196 9182 8638 9732 -1041 -267 -430 C
ATOM 1143 SG CYS A 196 143.243 -8.280 113.978 1.00 76.63 S
ANISOU 1143 SG CYS A 196 9811 9007 10298 -927 -275 -531 S
ATOM 1144 N LEU A 197 141.753 -4.411 114.111 1.00 68.51 N
ANISOU 1144 N LEU A 197 8495 8414 9122 -865 -186 -292 N
ATOM 1145 CA LEU A 197 142.459 -3.167 113.797 1.00 67.06 C
ANISOU 1145 CA LEU A 197 8273 8307 8899 -765 -164 -274 C
ATOM 1146 C LEU A 197 142.482 -2.235 115.010 1.00 69.63 C
ANISOU 1146 C LEU A 197 8588 8625 9243 -706 -121 -180 C
ATOM 1147 O LEU A 197 143.507 -1.606 115.270 1.00 68.87 O
ANISOU 1147 O LEU A 197 8517 8509 9143 -623 -105 -173 O
ATOM 1148 CB LEU A 197 141.830 -2.459 112.585 1.00 67.23 C
ANISOU 1148 CB LEU A 197 8201 8483 8859 -789 -183 -271 C
ATOM 1149 CG LEU A 197 141.990 -3.158 111.233 1.00 72.40 C
ANISOU 1149 CG LEU A 197 8866 9177 9466 -839 -223 -377 C
ATOM 1150 CD1 LEU A 197 140.841 -2.826 110.316 1.00 73.16 C
ANISOU 1150 CD1 LEU A 197 8868 9421 9508 -915 -258 -352 C
ATOM 1151 CD2 LEU A 197 143.319 -2.811 110.575 1.00 73.91 C
ANISOU 1151 CD2 LEU A 197 9078 9387 9616 -759 -212 -433 C
ATOM 1152 N ILE A 198 141.367 -2.177 115.765 1.00 65.97 N
ANISOU 1152 N ILE A 198 8088 8184 8795 -755 -100 -114 N
ATOM 1153 CA ILE A 198 141.219 -1.367 116.979 1.00 65.27 C
ANISOU 1153 CA ILE A 198 7990 8095 8714 -708 -51 -40 C
ATOM 1154 C ILE A 198 142.173 -1.913 118.070 1.00 68.99 C
ANISOU 1154 C ILE A 198 8564 8441 9207 -685 -43 -38 C
ATOM 1155 O ILE A 198 142.842 -1.117 118.737 1.00 68.19 O
ANISOU 1155 O ILE A 198 8485 8327 9097 -613 -18 -13 O
ATOM 1156 CB ILE A 198 139.723 -1.318 117.416 1.00 68.94 C
ANISOU 1156 CB ILE A 198 8376 8635 9184 -772 -25 19 C
ATOM 1157 CG1 ILE A 198 138.935 -0.339 116.515 1.00 69.45 C
ANISOU 1157 CG1 ILE A 198 8323 8834 9231 -751 -29 42 C
ATOM 1158 CG2 ILE A 198 139.555 -0.947 118.891 1.00 69.56 C
ANISOU 1158 CG2 ILE A 198 8470 8694 9266 -748 35 76 C
ATOM 1159 CD1 ILE A 198 137.439 -0.539 116.489 1.00 77.21 C
ANISOU 1159 CD1 ILE A 198 9202 9913 10220 -829 -25 83 C
ATOM 1160 N THR A 199 142.267 -3.262 118.205 1.00 65.80 N
ANISOU 1160 N THR A 199 8226 7940 8834 -749 -73 -64 N
ATOM 1161 CA THR A 199 143.168 -3.950 119.145 1.00 65.33 C
ANISOU 1161 CA THR A 199 8264 7752 8805 -731 -84 -53 C
ATOM 1162 C THR A 199 144.623 -3.624 118.778 1.00 68.29 C
ANISOU 1162 C THR A 199 8669 8096 9180 -629 -99 -100 C
ATOM 1163 O THR A 199 145.419 -3.338 119.671 1.00 67.74 O
ANISOU 1163 O THR A 199 8640 7985 9112 -577 -92 -64 O
ATOM 1164 CB THR A 199 142.896 -5.468 119.146 1.00 72.32 C
ANISOU 1164 CB THR A 199 9211 8530 9738 -820 -125 -72 C
ATOM 1165 OG1 THR A 199 141.530 -5.694 119.491 1.00 71.08 O
ANISOU 1165 OG1 THR A 199 9011 8423 9574 -928 -109 -17 O
ATOM 1166 CG2 THR A 199 143.797 -6.237 120.114 1.00 70.67 C
ANISOU 1166 CG2 THR A 199 9103 8178 9570 -799 -147 -43 C
ATOM 1167 N MET A 200 144.946 -3.628 117.465 1.00 64.27 N
ANISOU 1167 N MET A 200 8133 7624 8661 -609 -118 -177 N
ATOM 1168 CA MET A 200 146.270 -3.302 116.933 1.00 63.56 C
ANISOU 1168 CA MET A 200 8050 7536 8563 -521 -124 -226 C
ATOM 1169 C MET A 200 146.636 -1.848 117.211 1.00 66.58 C
ANISOU 1169 C MET A 200 8393 7996 8910 -463 -97 -173 C
ATOM 1170 O MET A 200 147.812 -1.554 117.420 1.00 65.91 O
ANISOU 1170 O MET A 200 8327 7889 8827 -398 -100 -176 O
ATOM 1171 CB MET A 200 146.336 -3.580 115.434 1.00 66.30 C
ANISOU 1171 CB MET A 200 8367 7938 8886 -530 -141 -319 C
ATOM 1172 CG MET A 200 146.658 -5.007 115.119 1.00 70.98 C
ANISOU 1172 CG MET A 200 9024 8421 9524 -546 -171 -407 C
ATOM 1173 SD MET A 200 146.425 -5.333 113.369 1.00 76.10 S
ANISOU 1173 SD MET A 200 9640 9155 10121 -583 -185 -529 S
ATOM 1174 CE MET A 200 146.756 -7.078 113.326 1.00 74.24 C
ANISOU 1174 CE MET A 200 9505 8741 9962 -597 -218 -637 C
ATOM 1175 N PHE A 201 145.635 -0.944 117.223 1.00 62.71 N
ANISOU 1175 N PHE A 201 7845 7589 8393 -485 -73 -124 N
ATOM 1176 CA PHE A 201 145.846 0.467 117.543 1.00 61.76 C
ANISOU 1176 CA PHE A 201 7698 7519 8251 -431 -48 -76 C
ATOM 1177 C PHE A 201 146.043 0.620 119.052 1.00 65.97 C
ANISOU 1177 C PHE A 201 8283 7989 8793 -417 -27 -29 C
ATOM 1178 O PHE A 201 146.900 1.396 119.480 1.00 65.37 O
ANISOU 1178 O PHE A 201 8228 7904 8706 -368 -23 -14 O
ATOM 1179 CB PHE A 201 144.682 1.347 117.045 1.00 63.43 C
ANISOU 1179 CB PHE A 201 7829 7827 8445 -445 -33 -41 C
ATOM 1180 CG PHE A 201 144.765 2.781 117.520 1.00 64.24 C
ANISOU 1180 CG PHE A 201 7916 7951 8542 -387 -7 9 C
ATOM 1181 CD1 PHE A 201 145.689 3.662 116.965 1.00 66.70 C
ANISOU 1181 CD1 PHE A 201 8224 8281 8838 -342 -22 12 C
ATOM 1182 CD2 PHE A 201 143.956 3.237 118.554 1.00 66.16 C
ANISOU 1182 CD2 PHE A 201 8153 8191 8795 -381 33 48 C
ATOM 1183 CE1 PHE A 201 145.783 4.977 117.422 1.00 67.26 C
ANISOU 1183 CE1 PHE A 201 8296 8348 8914 -297 -5 55 C
ATOM 1184 CE2 PHE A 201 144.056 4.552 119.013 1.00 68.64 C
ANISOU 1184 CE2 PHE A 201 8465 8505 9109 -323 58 76 C
ATOM 1185 CZ PHE A 201 144.978 5.407 118.453 1.00 66.33 C
ANISOU 1185 CZ PHE A 201 8181 8211 8811 -283 34 80 C
ATOM 1186 N PHE A 202 145.242 -0.117 119.853 1.00 62.92 N
ANISOU 1186 N PHE A 202 7919 7569 8418 -473 -14 -4 N
ATOM 1187 CA PHE A 202 145.324 -0.103 121.313 1.00 62.68 C
ANISOU 1187 CA PHE A 202 7940 7496 8378 -477 7 44 C
ATOM 1188 C PHE A 202 146.648 -0.693 121.780 1.00 66.56 C
ANISOU 1188 C PHE A 202 8505 7900 8884 -450 -31 40 C
ATOM 1189 O PHE A 202 147.147 -0.292 122.829 1.00 66.33 O
ANISOU 1189 O PHE A 202 8517 7854 8832 -432 -25 75 O
ATOM 1190 CB PHE A 202 144.137 -0.841 121.949 1.00 65.20 C
ANISOU 1190 CB PHE A 202 8257 7816 8698 -559 29 80 C
ATOM 1191 CG PHE A 202 142.862 -0.034 122.079 1.00 66.94 C
ANISOU 1191 CG PHE A 202 8399 8136 8898 -570 83 105 C
ATOM 1192 CD1 PHE A 202 142.904 1.328 122.370 1.00 69.63 C
ANISOU 1192 CD1 PHE A 202 8717 8522 9217 -501 121 110 C
ATOM 1193 CD2 PHE A 202 141.619 -0.646 121.978 1.00 69.96 C
ANISOU 1193 CD2 PHE A 202 8732 8562 9289 -650 96 124 C
ATOM 1194 CE1 PHE A 202 141.727 2.069 122.504 1.00 70.88 C
ANISOU 1194 CE1 PHE A 202 8799 8765 9369 -493 174 127 C
ATOM 1195 CE2 PHE A 202 140.442 0.093 122.134 1.00 73.16 C
ANISOU 1195 CE2 PHE A 202 9047 9070 9680 -650 150 150 C
ATOM 1196 CZ PHE A 202 140.505 1.446 122.389 1.00 70.83 C
ANISOU 1196 CZ PHE A 202 8726 8816 9371 -562 190 148 C
ATOM 1197 N THR A 203 147.230 -1.614 120.981 1.00 63.20 N
ANISOU 1197 N THR A 203 8093 7424 8495 -443 -71 -8 N
ATOM 1198 CA THR A 203 148.539 -2.223 121.220 1.00 63.01 C
ANISOU 1198 CA THR A 203 8119 7319 8501 -397 -112 -18 C
ATOM 1199 C THR A 203 149.602 -1.132 121.023 1.00 66.59 C
ANISOU 1199 C THR A 203 8545 7824 8930 -328 -110 -27 C
ATOM 1200 O THR A 203 150.494 -0.998 121.859 1.00 66.57 O
ANISOU 1200 O THR A 203 8576 7793 8925 -299 -129 6 O
ATOM 1201 CB THR A 203 148.733 -3.444 120.298 1.00 69.64 C
ANISOU 1201 CB THR A 203 8972 8095 9392 -398 -144 -86 C
ATOM 1202 OG1 THR A 203 147.726 -4.411 120.599 1.00 68.18 O
ANISOU 1202 OG1 THR A 203 8821 7851 9233 -480 -152 -67 O
ATOM 1203 CG2 THR A 203 150.108 -4.089 120.442 1.00 69.00 C
ANISOU 1203 CG2 THR A 203 8929 7931 9358 -328 -184 -105 C
ATOM 1204 N MET A 204 149.468 -0.330 119.943 1.00 62.70 N
ANISOU 1204 N MET A 204 7992 7416 8416 -314 -93 -60 N
ATOM 1205 CA MET A 204 150.362 0.784 119.611 1.00 62.16 C
ANISOU 1205 CA MET A 204 7891 7404 8322 -269 -93 -59 C
ATOM 1206 C MET A 204 150.239 1.909 120.639 1.00 66.88 C
ANISOU 1206 C MET A 204 8508 8011 8892 -270 -74 -4 C
ATOM 1207 O MET A 204 151.236 2.568 120.943 1.00 66.43 O
ANISOU 1207 O MET A 204 8458 7959 8823 -244 -89 9 O
ATOM 1208 CB MET A 204 150.080 1.324 118.199 1.00 64.27 C
ANISOU 1208 CB MET A 204 8094 7760 8567 -270 -83 -90 C
ATOM 1209 CG MET A 204 150.462 0.363 117.074 1.00 68.28 C
ANISOU 1209 CG MET A 204 8583 8277 9082 -263 -97 -165 C
ATOM 1210 SD MET A 204 152.180 -0.219 117.068 1.00 72.66 S
ANISOU 1210 SD MET A 204 9146 8797 9663 -195 -118 -207 S
ATOM 1211 CE MET A 204 153.044 1.314 116.813 1.00 68.83 C
ANISOU 1211 CE MET A 204 8609 8411 9133 -176 -111 -165 C
ATOM 1212 N LEU A 205 149.019 2.122 121.175 1.00 64.35 N
ANISOU 1212 N LEU A 205 8192 7698 8561 -303 -41 21 N
ATOM 1213 CA LEU A 205 148.737 3.119 122.208 1.00 64.35 C
ANISOU 1213 CA LEU A 205 8214 7704 8532 -300 -12 53 C
ATOM 1214 C LEU A 205 149.401 2.678 123.520 1.00 68.77 C
ANISOU 1214 C LEU A 205 8843 8211 9073 -311 -29 79 C
ATOM 1215 O LEU A 205 150.072 3.490 124.156 1.00 68.21 O
ANISOU 1215 O LEU A 205 8801 8140 8975 -297 -35 89 O
ATOM 1216 CB LEU A 205 147.213 3.318 122.369 1.00 64.74 C
ANISOU 1216 CB LEU A 205 8233 7790 8576 -325 37 65 C
ATOM 1217 CG LEU A 205 146.720 4.222 123.510 1.00 69.77 C
ANISOU 1217 CG LEU A 205 8892 8436 9182 -316 84 81 C
ATOM 1218 CD1 LEU A 205 147.013 5.686 123.241 1.00 69.55 C
ANISOU 1218 CD1 LEU A 205 8854 8418 9155 -267 89 72 C
ATOM 1219 CD2 LEU A 205 145.235 4.036 123.736 1.00 73.33 C
ANISOU 1219 CD2 LEU A 205 9299 8932 9631 -343 135 92 C
ATOM 1220 N ALA A 206 149.258 1.379 123.884 1.00 66.21 N
ANISOU 1220 N ALA A 206 8549 7840 8766 -342 -46 94 N
ATOM 1221 CA ALA A 206 149.872 0.773 125.074 1.00 66.52 C
ANISOU 1221 CA ALA A 206 8654 7828 8791 -357 -76 136 C
ATOM 1222 C ALA A 206 151.396 0.794 124.958 1.00 70.88 C
ANISOU 1222 C ALA A 206 9212 8359 9360 -310 -130 132 C
ATOM 1223 O ALA A 206 152.083 0.959 125.968 1.00 71.12 O
ANISOU 1223 O ALA A 206 9282 8380 9358 -313 -157 170 O
ATOM 1224 CB ALA A 206 149.381 -0.654 125.257 1.00 67.81 C
ANISOU 1224 CB ALA A 206 8846 7932 8986 -401 -92 161 C
ATOM 1225 N LEU A 207 151.916 0.646 123.719 1.00 67.09 N
ANISOU 1225 N LEU A 207 8682 7887 8921 -269 -145 86 N
ATOM 1226 CA LEU A 207 153.343 0.698 123.415 1.00 66.82 C
ANISOU 1226 CA LEU A 207 8626 7857 8905 -219 -186 76 C
ATOM 1227 C LEU A 207 153.846 2.131 123.598 1.00 70.65 C
ANISOU 1227 C LEU A 207 9096 8400 9346 -219 -181 86 C
ATOM 1228 O LEU A 207 154.906 2.319 124.187 1.00 70.24 O
ANISOU 1228 O LEU A 207 9053 8350 9284 -209 -220 112 O
ATOM 1229 CB LEU A 207 153.614 0.184 121.985 1.00 66.82 C
ANISOU 1229 CB LEU A 207 8571 7871 8946 -182 -186 12 C
ATOM 1230 CG LEU A 207 155.076 -0.029 121.559 1.00 71.67 C
ANISOU 1230 CG LEU A 207 9145 8498 9587 -120 -219 -10 C
ATOM 1231 CD1 LEU A 207 155.749 -1.134 122.369 1.00 72.57 C
ANISOU 1231 CD1 LEU A 207 9296 8528 9751 -87 -269 19 C
ATOM 1232 CD2 LEU A 207 155.151 -0.388 120.098 1.00 73.82 C
ANISOU 1232 CD2 LEU A 207 9363 8808 9877 -91 -200 -87 C
ATOM 1233 N MET A 208 153.067 3.132 123.131 1.00 67.48 N
ANISOU 1233 N MET A 208 8674 8041 8923 -233 -139 72 N
ATOM 1234 CA MET A 208 153.390 4.556 123.262 1.00 67.42 C
ANISOU 1234 CA MET A 208 8665 8066 8886 -239 -135 80 C
ATOM 1235 C MET A 208 153.384 4.962 124.731 1.00 71.29 C
ANISOU 1235 C MET A 208 9223 8530 9332 -265 -137 105 C
ATOM 1236 O MET A 208 154.297 5.661 125.169 1.00 71.06 O
ANISOU 1236 O MET A 208 9211 8508 9281 -275 -168 115 O
ATOM 1237 CB MET A 208 152.397 5.424 122.470 1.00 69.79 C
ANISOU 1237 CB MET A 208 8933 8396 9186 -239 -94 68 C
ATOM 1238 CG MET A 208 152.825 6.879 122.350 1.00 73.82 C
ANISOU 1238 CG MET A 208 9443 8922 9685 -241 -99 80 C
ATOM 1239 SD MET A 208 151.432 8.031 122.225 1.00 78.67 S
ANISOU 1239 SD MET A 208 10055 9531 10305 -233 -52 81 S
ATOM 1240 CE MET A 208 150.853 8.052 123.941 1.00 75.82 C
ANISOU 1240 CE MET A 208 9771 9128 9910 -243 -18 69 C
ATOM 1241 N ALA A 209 152.357 4.516 125.483 1.00 67.84 N
ANISOU 1241 N ALA A 209 8824 8075 8876 -287 -104 113 N
ATOM 1242 CA ALA A 209 152.188 4.794 126.907 1.00 67.86 C
ANISOU 1242 CA ALA A 209 8893 8071 8818 -320 -94 130 C
ATOM 1243 C ALA A 209 153.368 4.255 127.709 1.00 71.62 C
ANISOU 1243 C ALA A 209 9406 8533 9275 -333 -160 168 C
ATOM 1244 O ALA A 209 153.911 4.989 128.530 1.00 71.30 O
ANISOU 1244 O ALA A 209 9405 8505 9181 -356 -179 171 O
ATOM 1245 CB ALA A 209 150.886 4.190 127.409 1.00 68.91 C
ANISOU 1245 CB ALA A 209 9042 8207 8935 -347 -44 140 C
ATOM 1246 N SER A 210 153.795 3.001 127.433 1.00 68.23 N
ANISOU 1246 N SER A 210 8960 8074 8891 -317 -200 194 N
ATOM 1247 CA SER A 210 154.926 2.361 128.108 1.00 68.49 C
ANISOU 1247 CA SER A 210 9012 8088 8921 -314 -272 242 C
ATOM 1248 C SER A 210 156.255 3.007 127.702 1.00 71.93 C
ANISOU 1248 C SER A 210 9402 8557 9370 -287 -317 233 C
ATOM 1249 O SER A 210 157.139 3.133 128.549 1.00 72.16 O
ANISOU 1249 O SER A 210 9452 8602 9365 -305 -373 271 O
ATOM 1250 CB SER A 210 154.955 0.861 127.829 1.00 72.49 C
ANISOU 1250 CB SER A 210 9513 8535 9495 -288 -301 267 C
ATOM 1251 OG SER A 210 155.111 0.574 126.449 1.00 81.08 O
ANISOU 1251 OG SER A 210 10539 9616 10652 -238 -292 214 O
ATOM 1252 N LEU A 211 156.388 3.439 126.426 1.00 67.67 N
ANISOU 1252 N LEU A 211 8798 8043 8870 -256 -295 189 N
ATOM 1253 CA LEU A 211 157.603 4.094 125.933 1.00 67.38 C
ANISOU 1253 CA LEU A 211 8706 8054 8843 -243 -329 185 C
ATOM 1254 C LEU A 211 157.736 5.502 126.494 1.00 71.47 C
ANISOU 1254 C LEU A 211 9258 8594 9304 -296 -331 186 C
ATOM 1255 O LEU A 211 158.844 5.898 126.837 1.00 71.46 O
ANISOU 1255 O LEU A 211 9242 8623 9286 -316 -384 208 O
ATOM 1256 CB LEU A 211 157.672 4.122 124.400 1.00 67.04 C
ANISOU 1256 CB LEU A 211 8585 8044 8843 -207 -301 145 C
ATOM 1257 CG LEU A 211 158.247 2.864 123.751 1.00 72.01 C
ANISOU 1257 CG LEU A 211 9162 8667 9530 -145 -319 128 C
ATOM 1258 CD1 LEU A 211 157.753 2.711 122.338 1.00 71.87 C
ANISOU 1258 CD1 LEU A 211 9097 8676 9534 -123 -272 72 C
ATOM 1259 CD2 LEU A 211 159.768 2.862 123.785 1.00 75.04 C
ANISOU 1259 CD2 LEU A 211 9483 9099 9929 -117 -370 149 C
ATOM 1260 N TYR A 212 156.620 6.246 126.616 1.00 68.17 N
ANISOU 1260 N TYR A 212 8883 8158 8859 -317 -276 159 N
ATOM 1261 CA TYR A 212 156.619 7.593 127.193 1.00 68.46 C
ANISOU 1261 CA TYR A 212 8970 8191 8850 -359 -272 144 C
ATOM 1262 C TYR A 212 156.934 7.517 128.695 1.00 72.08 C
ANISOU 1262 C TYR A 212 9501 8648 9239 -404 -306 161 C
ATOM 1263 O TYR A 212 157.638 8.384 129.218 1.00 72.05 O
ANISOU 1263 O TYR A 212 9527 8653 9196 -449 -344 156 O
ATOM 1264 CB TYR A 212 155.277 8.309 126.938 1.00 70.01 C
ANISOU 1264 CB TYR A 212 9187 8363 9050 -349 -201 107 C
ATOM 1265 CG TYR A 212 155.105 9.601 127.710 1.00 73.04 C
ANISOU 1265 CG TYR A 212 9641 8719 9392 -380 -188 76 C
ATOM 1266 CD1 TYR A 212 155.819 10.745 127.364 1.00 75.22 C
ANISOU 1266 CD1 TYR A 212 9919 8982 9680 -405 -220 71 C
ATOM 1267 CD2 TYR A 212 154.226 9.680 128.786 1.00 74.53 C
ANISOU 1267 CD2 TYR A 212 9895 8894 9527 -389 -142 46 C
ATOM 1268 CE1 TYR A 212 155.680 11.930 128.084 1.00 76.83 C
ANISOU 1268 CE1 TYR A 212 10200 9138 9853 -435 -213 30 C
ATOM 1269 CE2 TYR A 212 154.068 10.863 129.505 1.00 76.21 C
ANISOU 1269 CE2 TYR A 212 10179 9076 9700 -410 -125 -4 C
ATOM 1270 CZ TYR A 212 154.801 11.985 129.153 1.00 84.78 C
ANISOU 1270 CZ TYR A 212 11277 10128 10808 -431 -164 -15 C
ATOM 1271 OH TYR A 212 154.649 13.155 129.857 1.00 88.11 O
ANISOU 1271 OH TYR A 212 11781 10498 11198 -453 -150 -76 O
ATOM 1272 N VAL A 213 156.422 6.469 129.373 1.00 68.21 N
ANISOU 1272 N VAL A 213 9040 8149 8728 -401 -298 185 N
ATOM 1273 CA VAL A 213 156.642 6.210 130.795 1.00 68.38 C
ANISOU 1273 CA VAL A 213 9129 8182 8669 -449 -333 216 C
ATOM 1274 C VAL A 213 158.130 5.891 131.013 1.00 72.35 C
ANISOU 1274 C VAL A 213 9603 8711 9176 -457 -430 267 C
ATOM 1275 O VAL A 213 158.708 6.397 131.962 1.00 72.57 O
ANISOU 1275 O VAL A 213 9674 8767 9131 -512 -476 278 O
ATOM 1276 CB VAL A 213 155.680 5.101 131.322 1.00 72.32 C
ANISOU 1276 CB VAL A 213 9659 8668 9151 -452 -300 247 C
ATOM 1277 CG1 VAL A 213 156.269 4.306 132.488 1.00 72.97 C
ANISOU 1277 CG1 VAL A 213 9784 8764 9176 -490 -368 321 C
ATOM 1278 CG2 VAL A 213 154.329 5.695 131.707 1.00 72.10 C
ANISOU 1278 CG2 VAL A 213 9673 8648 9074 -470 -210 199 C
ATOM 1279 N HIS A 214 158.756 5.119 130.113 1.00 68.85 N
ANISOU 1279 N HIS A 214 9080 8265 8816 -401 -459 291 N
ATOM 1280 CA HIS A 214 160.168 4.761 130.231 1.00 69.48 C
ANISOU 1280 CA HIS A 214 9106 8378 8914 -390 -547 341 C
ATOM 1281 C HIS A 214 161.115 5.898 129.816 1.00 72.35 C
ANISOU 1281 C HIS A 214 9422 8793 9276 -419 -574 322 C
ATOM 1282 O HIS A 214 161.965 6.290 130.614 1.00 72.71 O
ANISOU 1282 O HIS A 214 9478 8878 9271 -472 -642 353 O
ATOM 1283 CB HIS A 214 160.485 3.501 129.409 1.00 70.72 C
ANISOU 1283 CB HIS A 214 9191 8512 9168 -307 -559 359 C
ATOM 1284 CG HIS A 214 160.297 2.229 130.169 1.00 75.16 C
ANISOU 1284 CG HIS A 214 9794 9026 9739 -291 -595 420 C
ATOM 1285 ND1 HIS A 214 161.268 1.759 131.035 1.00 78.10 N
ANISOU 1285 ND1 HIS A 214 10161 9413 10098 -293 -687 498 N
ATOM 1286 CD2 HIS A 214 159.255 1.366 130.166 1.00 77.13 C
ANISOU 1286 CD2 HIS A 214 10086 9210 10009 -282 -556 424 C
ATOM 1287 CE1 HIS A 214 160.785 0.631 131.532 1.00 78.13 C
ANISOU 1287 CE1 HIS A 214 10214 9355 10119 -281 -702 551 C
ATOM 1288 NE2 HIS A 214 159.577 0.354 131.040 1.00 77.88 N
ANISOU 1288 NE2 HIS A 214 10213 9271 10108 -280 -624 508 N
ATOM 1289 N MET A 215 160.984 6.405 128.574 1.00 67.47 N
ANISOU 1289 N MET A 215 8750 8180 8706 -395 -527 281 N
ATOM 1290 CA MET A 215 161.871 7.421 127.996 1.00 67.04 C
ANISOU 1290 CA MET A 215 8639 8175 8658 -429 -550 277 C
ATOM 1291 C MET A 215 161.772 8.805 128.624 1.00 71.15 C
ANISOU 1291 C MET A 215 9235 8680 9117 -515 -557 255 C
ATOM 1292 O MET A 215 162.776 9.520 128.628 1.00 71.36 O
ANISOU 1292 O MET A 215 9231 8749 9134 -571 -610 272 O
ATOM 1293 CB MET A 215 161.634 7.581 126.479 1.00 68.62 C
ANISOU 1293 CB MET A 215 8769 8388 8914 -389 -495 248 C
ATOM 1294 CG MET A 215 161.903 6.336 125.652 1.00 71.93 C
ANISOU 1294 CG MET A 215 9106 8830 9395 -306 -485 248 C
ATOM 1295 SD MET A 215 163.504 5.563 125.955 1.00 76.71 S
ANISOU 1295 SD MET A 215 9620 9498 10029 -271 -567 296 S
ATOM 1296 CE MET A 215 162.968 4.034 126.557 1.00 73.60 C
ANISOU 1296 CE MET A 215 9272 9024 9667 -204 -576 309 C
ATOM 1297 N PHE A 216 160.583 9.215 129.093 1.00 67.49 N
ANISOU 1297 N PHE A 216 8866 8159 8619 -525 -502 213 N
ATOM 1298 CA PHE A 216 160.413 10.577 129.593 1.00 67.62 C
ANISOU 1298 CA PHE A 216 8961 8143 8590 -592 -498 171 C
ATOM 1299 C PHE A 216 160.103 10.651 131.088 1.00 72.15 C
ANISOU 1299 C PHE A 216 9638 8704 9069 -638 -507 149 C
ATOM 1300 O PHE A 216 160.743 11.442 131.784 1.00 72.91 O
ANISOU 1300 O PHE A 216 9783 8808 9111 -715 -559 134 O
ATOM 1301 CB PHE A 216 159.340 11.310 128.772 1.00 68.87 C
ANISOU 1301 CB PHE A 216 9133 8245 8789 -561 -422 128 C
ATOM 1302 CG PHE A 216 159.699 11.397 127.304 1.00 69.98 C
ANISOU 1302 CG PHE A 216 9178 8412 9000 -536 -419 155 C
ATOM 1303 CD1 PHE A 216 160.557 12.387 126.838 1.00 73.62 C
ANISOU 1303 CD1 PHE A 216 9613 8884 9473 -593 -459 173 C
ATOM 1304 CD2 PHE A 216 159.218 10.460 126.396 1.00 71.44 C
ANISOU 1304 CD2 PHE A 216 9298 8618 9230 -466 -379 163 C
ATOM 1305 CE1 PHE A 216 160.913 12.448 125.487 1.00 74.31 C
ANISOU 1305 CE1 PHE A 216 9608 9018 9609 -581 -453 205 C
ATOM 1306 CE2 PHE A 216 159.573 10.524 125.046 1.00 74.07 C
ANISOU 1306 CE2 PHE A 216 9542 8993 9606 -450 -373 181 C
ATOM 1307 CZ PHE A 216 160.417 11.518 124.600 1.00 72.63 C
ANISOU 1307 CZ PHE A 216 9332 8837 9428 -506 -407 206 C
ATOM 1308 N LEU A 217 159.147 9.848 131.585 1.00 68.06 N
ANISOU 1308 N LEU A 217 9156 8178 8525 -603 -459 146 N
ATOM 1309 CA LEU A 217 158.768 9.851 133.000 1.00 68.27 C
ANISOU 1309 CA LEU A 217 9279 8214 8446 -651 -456 127 C
ATOM 1310 C LEU A 217 159.856 9.207 133.874 1.00 72.18 C
ANISOU 1310 C LEU A 217 9772 8769 8883 -699 -555 195 C
ATOM 1311 O LEU A 217 160.270 9.809 134.865 1.00 72.82 O
ANISOU 1311 O LEU A 217 9920 8877 8872 -776 -598 176 O
ATOM 1312 CB LEU A 217 157.416 9.142 133.198 1.00 67.99 C
ANISOU 1312 CB LEU A 217 9266 8168 8400 -609 -372 119 C
ATOM 1313 CG LEU A 217 156.258 9.999 133.706 1.00 72.96 C
ANISOU 1313 CG LEU A 217 9970 8774 8978 -615 -284 35 C
ATOM 1314 CD1 LEU A 217 155.800 11.008 132.658 1.00 72.53 C
ANISOU 1314 CD1 LEU A 217 9891 8661 9007 -569 -236 -18 C
ATOM 1315 CD2 LEU A 217 155.088 9.128 134.112 1.00 75.55 C
ANISOU 1315 CD2 LEU A 217 10306 9123 9275 -594 -213 47 C
ATOM 1316 N MET A 218 160.336 8.011 133.482 1.00 67.98 N
ANISOU 1316 N MET A 218 9163 8257 8411 -650 -595 271 N
ATOM 1317 CA MET A 218 161.372 7.238 134.177 1.00 68.44 C
ANISOU 1317 CA MET A 218 9198 8366 8441 -671 -696 355 C
ATOM 1318 C MET A 218 162.775 7.525 133.616 1.00 72.25 C
ANISOU 1318 C MET A 218 9585 8891 8974 -675 -775 384 C
ATOM 1319 O MET A 218 163.698 6.741 133.856 1.00 72.73 O
ANISOU 1319 O MET A 218 9586 8996 9052 -658 -858 461 O
ATOM 1320 CB MET A 218 161.082 5.731 134.063 1.00 70.68 C
ANISOU 1320 CB MET A 218 9451 8627 8776 -603 -697 423 C
ATOM 1321 CG MET A 218 159.897 5.264 134.854 1.00 74.52 C
ANISOU 1321 CG MET A 218 10023 9096 9196 -624 -643 428 C
ATOM 1322 SD MET A 218 159.666 3.499 134.583 1.00 78.84 S
ANISOU 1322 SD MET A 218 10535 9593 9828 -556 -658 514 S
ATOM 1323 CE MET A 218 158.721 3.083 136.024 1.00 76.58 C
ANISOU 1323 CE MET A 218 10358 9327 9413 -633 -638 561 C
ATOM 1324 N ALA A 219 162.933 8.644 132.876 1.00 67.84 N
ANISOU 1324 N ALA A 219 9007 8325 8444 -697 -751 330 N
ATOM 1325 CA ALA A 219 164.180 9.066 132.234 1.00 67.53 C
ANISOU 1325 CA ALA A 219 8870 8337 8450 -717 -811 355 C
ATOM 1326 C ALA A 219 165.363 9.070 133.202 1.00 72.52 C
ANISOU 1326 C ALA A 219 9487 9045 9021 -789 -927 411 C
ATOM 1327 O ALA A 219 166.401 8.479 132.898 1.00 72.36 O
ANISOU 1327 O ALA A 219 9352 9089 9052 -756 -990 476 O
ATOM 1328 CB ALA A 219 164.009 10.449 131.624 1.00 67.89 C
ANISOU 1328 CB ALA A 219 8939 8350 8507 -765 -774 294 C
ATOM 1329 N ARG A 220 165.185 9.690 134.380 1.00 69.84 N
ANISOU 1329 N ARG A 220 9259 8705 8570 -882 -954 383 N
ATOM 1330 CA ARG A 220 166.225 9.829 135.398 1.00 70.85 C
ANISOU 1330 CA ARG A 220 9390 8914 8617 -974 -1071 430 C
ATOM 1331 C ARG A 220 166.270 8.625 136.360 1.00 75.21 C
ANISOU 1331 C ARG A 220 9952 9504 9118 -951 -1126 512 C
ATOM 1332 O ARG A 220 167.055 8.643 137.312 1.00 75.75 O
ANISOU 1332 O ARG A 220 10027 9649 9104 -1028 -1231 562 O
ATOM 1333 CB ARG A 220 166.035 11.147 136.174 1.00 72.02 C
ANISOU 1333 CB ARG A 220 9663 9043 8660 -1096 -1077 346 C
ATOM 1334 CG ARG A 220 166.096 12.387 135.274 1.00 83.43 C
ANISOU 1334 CG ARG A 220 11103 10434 10163 -1130 -1043 283 C
ATOM 1335 CD ARG A 220 166.102 13.703 136.030 1.00 96.99 C
ANISOU 1335 CD ARG A 220 12944 12116 11792 -1256 -1067 198 C
ATOM 1336 NE ARG A 220 164.861 13.938 136.773 1.00108.67 N
ANISOU 1336 NE ARG A 220 14566 13530 13195 -1246 -986 106 N
ATOM 1337 CZ ARG A 220 164.542 15.088 137.361 1.00125.42 C
ANISOU 1337 CZ ARG A 220 16814 15591 15248 -1324 -972 -1 C
ATOM 1338 NH1 ARG A 220 163.396 15.208 138.018 1.00113.38 N
ANISOU 1338 NH1 ARG A 220 15402 14024 13654 -1298 -886 -88 N
ATOM 1339 NH2 ARG A 220 165.365 16.128 137.293 1.00113.17 N
ANISOU 1339 NH2 ARG A 220 15277 14022 13699 -1431 -1043 -25 N
ATOM 1340 N LEU A 221 165.473 7.567 136.091 1.00 71.48 N
ANISOU 1340 N LEU A 221 9481 8983 8697 -853 -1065 534 N
ATOM 1341 CA LEU A 221 165.455 6.362 136.926 1.00 72.23 C
ANISOU 1341 CA LEU A 221 9591 9095 8759 -830 -1117 628 C
ATOM 1342 C LEU A 221 166.433 5.313 136.404 1.00 77.57 C
ANISOU 1342 C LEU A 221 10132 9792 9548 -739 -1190 722 C
ATOM 1343 O LEU A 221 167.112 4.674 137.209 1.00 78.25 O
ANISOU 1343 O LEU A 221 10200 9929 9604 -749 -1295 822 O
ATOM 1344 CB LEU A 221 164.046 5.744 137.054 1.00 71.56 C
ANISOU 1344 CB LEU A 221 9587 8941 8663 -791 -1021 610 C
ATOM 1345 CG LEU A 221 162.899 6.597 137.623 1.00 75.93 C
ANISOU 1345 CG LEU A 221 10265 9477 9108 -858 -931 515 C
ATOM 1346 CD1 LEU A 221 161.754 5.718 138.070 1.00 76.01 C
ANISOU 1346 CD1 LEU A 221 10335 9461 9086 -838 -869 542 C
ATOM 1347 CD2 LEU A 221 163.338 7.453 138.795 1.00 79.07 C
ANISOU 1347 CD2 LEU A 221 10742 9944 9358 -978 -991 492 C
ATOM 1348 N HIS A 222 166.503 5.127 135.071 1.00 74.40 N
ANISOU 1348 N HIS A 222 9637 9356 9274 -645 -1134 691 N
ATOM 1349 CA HIS A 222 167.408 4.147 134.464 1.00 75.22 C
ANISOU 1349 CA HIS A 222 9607 9477 9495 -540 -1185 756 C
ATOM 1350 C HIS A 222 168.464 4.788 133.538 1.00 78.39 C
ANISOU 1350 C HIS A 222 9875 9953 9956 -533 -1198 735 C
ATOM 1351 O HIS A 222 169.359 4.087 133.056 1.00 78.39 O
ANISOU 1351 O HIS A 222 9745 9992 10047 -445 -1239 781 O
ATOM 1352 CB HIS A 222 166.638 3.039 133.717 1.00 75.75 C
ANISOU 1352 CB HIS A 222 9672 9448 9664 -422 -1112 744 C
ATOM 1353 CG HIS A 222 165.525 3.495 132.825 1.00 78.08 C
ANISOU 1353 CG HIS A 222 10007 9683 9975 -415 -987 643 C
ATOM 1354 ND1 HIS A 222 165.735 4.419 131.817 1.00 79.40 N
ANISOU 1354 ND1 HIS A 222 10117 9883 10170 -422 -939 575 N
ATOM 1355 CD2 HIS A 222 164.247 3.056 132.758 1.00 79.44 C
ANISOU 1355 CD2 HIS A 222 10260 9774 10149 -397 -910 614 C
ATOM 1356 CE1 HIS A 222 164.570 4.548 131.202 1.00 78.03 C
ANISOU 1356 CE1 HIS A 222 9994 9645 10008 -405 -839 508 C
ATOM 1357 NE2 HIS A 222 163.645 3.747 131.734 1.00 78.32 N
ANISOU 1357 NE2 HIS A 222 10110 9616 10032 -390 -817 525 N
ATOM 1358 N GLY A1001 168.365 6.099 133.328 1.00 70.66 N
ANISOU 1358 N GLY A1001 7624 9292 9931 268 14 1356 N
ATOM 1359 CA GLY A1001 169.302 6.846 132.498 1.00 70.91 C
ANISOU 1359 CA GLY A1001 7691 9353 9900 282 44 1472 C
ATOM 1360 C GLY A1001 170.576 7.190 133.240 1.00 72.91 C
ANISOU 1360 C GLY A1001 8041 9441 10218 235 142 1396 C
ATOM 1361 O GLY A1001 170.523 7.850 134.283 1.00 72.23 O
ANISOU 1361 O GLY A1001 7983 9168 10295 249 220 1367 O
ATOM 1362 N ILE A1002 171.730 6.734 132.709 1.00 68.31 N
ANISOU 1362 N ILE A1002 7501 8946 9507 181 138 1344 N
ATOM 1363 CA ILE A1002 173.050 6.972 133.303 1.00 66.99 C
ANISOU 1363 CA ILE A1002 7401 8663 9389 126 215 1269 C
ATOM 1364 C ILE A1002 173.504 8.418 133.028 1.00 71.78 C
ANISOU 1364 C ILE A1002 8000 9157 10116 139 301 1443 C
ATOM 1365 O ILE A1002 173.390 8.907 131.902 1.00 72.80 O
ANISOU 1365 O ILE A1002 8085 9389 10188 176 299 1640 O
ATOM 1366 CB ILE A1002 174.121 5.906 132.866 1.00 69.19 C
ANISOU 1366 CB ILE A1002 7706 9075 9507 75 187 1148 C
ATOM 1367 CG1 ILE A1002 175.509 6.149 133.495 1.00 68.79 C
ANISOU 1367 CG1 ILE A1002 7696 8927 9515 21 258 1078 C
ATOM 1368 CG2 ILE A1002 174.240 5.748 131.356 1.00 70.93 C
ANISOU 1368 CG2 ILE A1002 7886 9521 9544 96 152 1240 C
ATOM 1369 CD1 ILE A1002 175.636 5.785 134.927 1.00 74.32 C
ANISOU 1369 CD1 ILE A1002 8437 9503 10299 -3 263 923 C
ATOM 1370 N ASP A1003 174.001 9.091 134.082 1.00 67.85 N
ANISOU 1370 N ASP A1003 7539 8450 9789 106 373 1369 N
ATOM 1371 CA ASP A1003 174.516 10.457 134.021 1.00 68.86 C
ANISOU 1371 CA ASP A1003 7661 8405 10099 93 462 1491 C
ATOM 1372 C ASP A1003 176.021 10.413 133.725 1.00 72.51 C
ANISOU 1372 C ASP A1003 8128 8904 10520 2 498 1472 C
ATOM 1373 O ASP A1003 176.827 10.189 134.632 1.00 71.24 O
ANISOU 1373 O ASP A1003 7996 8680 10394 -65 507 1288 O
ATOM 1374 CB ASP A1003 174.212 11.209 135.334 1.00 70.77 C
ANISOU 1374 CB ASP A1003 7929 8402 10559 101 516 1371 C
ATOM 1375 CG ASP A1003 174.494 12.704 135.324 1.00 81.93 C
ANISOU 1375 CG ASP A1003 9329 9572 12230 95 608 1478 C
ATOM 1376 OD1 ASP A1003 174.656 13.273 134.223 1.00 83.75 O
ANISOU 1376 OD1 ASP A1003 9518 9814 12490 107 637 1723 O
ATOM 1377 OD2 ASP A1003 174.498 13.313 136.415 1.00 87.99 O
ANISOU 1377 OD2 ASP A1003 10122 10138 13174 84 654 1320 O
HETATM 1378 N YCM A1004 176.391 10.590 132.441 1.00 70.17 N
ANISOU 1378 N YCM A1004 7790 8745 10129 6 517 1670 N
HETATM 1379 CA YCM A1004 177.787 10.576 131.994 1.00 70.39 C
ANISOU 1379 CA YCM A1004 7795 8842 10108 -71 570 1690 C
HETATM 1380 CB YCM A1004 177.973 10.335 130.492 1.00 74.13 C
ANISOU 1380 CB YCM A1004 8221 9580 10364 -38 576 1879 C
HETATM 1381 SG YCM A1004 177.619 8.647 129.930 1.00 74.79 S
ANISOU 1381 SG YCM A1004 8319 9972 10125 11 463 1710 S
HETATM 1382 CD YCM A1004 178.603 7.599 131.036 1.00 73.70 C
ANISOU 1382 CD YCM A1004 8223 9776 10002 -55 448 1401 C
HETATM 1383 CE YCM A1004 180.091 7.587 130.753 1.00 75.02 C
ANISOU 1383 CE YCM A1004 8351 10013 10141 -110 521 1394 C
HETATM 1384 OZ1 YCM A1004 180.849 8.412 131.270 1.00 75.35 O
ANISOU 1384 OZ1 YCM A1004 8368 9903 10358 -181 589 1427 O
HETATM 1385 NZ2 YCM A1004 180.509 6.633 129.934 1.00 75.69 N
ANISOU 1385 NZ2 YCM A1004 8417 10330 10011 -79 509 1330 N
HETATM 1386 C YCM A1004 178.556 11.831 132.424 1.00 74.03 C
ANISOU 1386 C YCM A1004 8235 9057 10835 -150 667 1747 C
HETATM 1387 O YCM A1004 179.785 11.791 132.509 1.00 73.73 O
ANISOU 1387 O YCM A1004 8170 9032 10813 -241 706 1689 O
ATOM 1388 N SER A1005 177.833 12.935 132.712 1.00 70.67 N
ANISOU 1388 N SER A1005 7810 8399 10641 -117 706 1848 N
ATOM 1389 CA SER A1005 178.423 14.193 133.174 1.00 71.58 C
ANISOU 1389 CA SER A1005 7906 8223 11068 -196 796 1874 C
ATOM 1390 C SER A1005 178.973 14.042 134.598 1.00 73.12 C
ANISOU 1390 C SER A1005 8136 8295 11351 -277 773 1544 C
ATOM 1391 O SER A1005 179.938 14.721 134.948 1.00 73.84 O
ANISOU 1391 O SER A1005 8193 8231 11632 -390 824 1489 O
ATOM 1392 CB SER A1005 177.407 15.331 133.107 1.00 77.08 C
ANISOU 1392 CB SER A1005 8595 8688 12002 -113 843 2049 C
ATOM 1393 OG SER A1005 176.466 15.297 134.168 1.00 85.99 O
ANISOU 1393 OG SER A1005 9770 9698 13203 -49 807 1848 O
ATOM 1394 N PHE A1006 178.361 13.152 135.409 1.00 66.68 N
ANISOU 1394 N PHE A1006 7375 7565 10395 -225 695 1336 N
ATOM 1395 CA PHE A1006 178.791 12.885 136.778 1.00 64.98 C
ANISOU 1395 CA PHE A1006 7190 7300 10198 -279 662 1041 C
ATOM 1396 C PHE A1006 179.643 11.614 136.841 1.00 67.34 C
ANISOU 1396 C PHE A1006 7486 7832 10270 -316 599 931 C
ATOM 1397 O PHE A1006 180.783 11.679 137.295 1.00 67.23 O
ANISOU 1397 O PHE A1006 7439 7809 10297 -409 598 813 O
ATOM 1398 CB PHE A1006 177.589 12.781 137.738 1.00 65.70 C
ANISOU 1398 CB PHE A1006 7334 7337 10294 -190 638 907 C
ATOM 1399 CG PHE A1006 177.989 12.728 139.196 1.00 66.53 C
ANISOU 1399 CG PHE A1006 7466 7399 10415 -235 618 617 C
ATOM 1400 CD1 PHE A1006 178.156 13.895 139.930 1.00 70.91 C
ANISOU 1400 CD1 PHE A1006 8018 7720 11205 -278 667 481 C
ATOM 1401 CD2 PHE A1006 178.218 11.511 139.829 1.00 66.52 C
ANISOU 1401 CD2 PHE A1006 7487 7595 10194 -233 547 480 C
ATOM 1402 CE1 PHE A1006 178.539 13.846 141.272 1.00 71.70 C
ANISOU 1402 CE1 PHE A1006 8137 7829 11278 -317 636 191 C
ATOM 1403 CE2 PHE A1006 178.618 11.465 141.165 1.00 69.17 C
ANISOU 1403 CE2 PHE A1006 7838 7938 10506 -265 521 239 C
ATOM 1404 CZ PHE A1006 178.777 12.633 141.876 1.00 68.95 C
ANISOU 1404 CZ PHE A1006 7805 7719 10671 -308 561 85 C
ATOM 1405 N TRP A1007 179.090 10.464 136.404 1.00 62.58 N
ANISOU 1405 N TRP A1007 6905 7423 9448 -242 544 960 N
ATOM 1406 CA TRP A1007 179.775 9.170 136.438 1.00 61.19 C
ANISOU 1406 CA TRP A1007 6729 7438 9083 -252 488 857 C
ATOM 1407 C TRP A1007 180.758 9.069 135.271 1.00 65.33 C
ANISOU 1407 C TRP A1007 7195 8090 9539 -287 523 976 C
ATOM 1408 O TRP A1007 180.515 8.376 134.278 1.00 64.40 O
ANISOU 1408 O TRP A1007 7074 8141 9255 -234 507 1056 O
ATOM 1409 CB TRP A1007 178.761 8.015 136.450 1.00 58.84 C
ANISOU 1409 CB TRP A1007 6472 7255 8631 -170 422 825 C
ATOM 1410 CG TRP A1007 177.741 8.143 137.542 1.00 59.59 C
ANISOU 1410 CG TRP A1007 6605 7249 8787 -130 411 741 C
ATOM 1411 CD1 TRP A1007 176.462 8.595 137.415 1.00 62.90 C
ANISOU 1411 CD1 TRP A1007 7027 7606 9267 -67 424 825 C
ATOM 1412 CD2 TRP A1007 177.950 7.915 138.943 1.00 59.09 C
ANISOU 1412 CD2 TRP A1007 6569 7158 8727 -143 395 564 C
ATOM 1413 NE1 TRP A1007 175.842 8.612 138.643 1.00 62.17 N
ANISOU 1413 NE1 TRP A1007 6961 7447 9214 -38 430 703 N
ATOM 1414 CE2 TRP A1007 176.735 8.206 139.600 1.00 63.05 C
ANISOU 1414 CE2 TRP A1007 7092 7587 9277 -85 413 543 C
ATOM 1415 CE3 TRP A1007 179.041 7.465 139.707 1.00 60.14 C
ANISOU 1415 CE3 TRP A1007 6695 7347 8808 -188 365 430 C
ATOM 1416 CZ2 TRP A1007 176.574 8.046 140.982 1.00 62.21 C
ANISOU 1416 CZ2 TRP A1007 7011 7481 9145 -72 412 391 C
ATOM 1417 CZ3 TRP A1007 178.880 7.312 141.075 1.00 61.51 C
ANISOU 1417 CZ3 TRP A1007 6893 7524 8953 -174 347 290 C
ATOM 1418 CH2 TRP A1007 177.660 7.601 141.699 1.00 62.22 C
ANISOU 1418 CH2 TRP A1007 7014 7558 9070 -117 376 270 C
ATOM 1419 N ASN A1008 181.875 9.792 135.411 1.00 63.16 N
ANISOU 1419 N ASN A1008 6863 7741 9394 -381 574 974 N
ATOM 1420 CA ASN A1008 182.949 9.881 134.430 1.00 64.02 C
ANISOU 1420 CA ASN A1008 6890 7961 9473 -431 636 1096 C
ATOM 1421 C ASN A1008 184.288 9.587 135.090 1.00 67.98 C
ANISOU 1421 C ASN A1008 7328 8499 10002 -510 623 939 C
ATOM 1422 O ASN A1008 184.543 10.058 136.203 1.00 67.46 O
ANISOU 1422 O ASN A1008 7257 8296 10077 -574 595 793 O
ATOM 1423 CB ASN A1008 182.960 11.275 133.795 1.00 66.07 C
ANISOU 1423 CB ASN A1008 7105 8074 9923 -482 733 1320 C
ATOM 1424 CG ASN A1008 183.353 11.281 132.344 1.00 88.68 C
ANISOU 1424 CG ASN A1008 9906 11120 12668 -469 807 1559 C
ATOM 1425 OD1 ASN A1008 184.523 11.111 131.990 1.00 84.89 O
ANISOU 1425 OD1 ASN A1008 9343 10756 12154 -529 858 1572 O
ATOM 1426 ND2 ASN A1008 182.383 11.496 131.471 1.00 80.53 N
ANISOU 1426 ND2 ASN A1008 8898 10141 11558 -384 818 1760 N
ATOM 1427 N GLU A1009 185.152 8.825 134.392 1.00 64.94 N
ANISOU 1427 N GLU A1009 6881 8316 9477 -498 642 959 N
ATOM 1428 CA GLU A1009 186.485 8.459 134.879 1.00 65.08 C
ANISOU 1428 CA GLU A1009 6808 8408 9512 -554 630 835 C
ATOM 1429 C GLU A1009 187.442 9.679 134.890 1.00 71.06 C
ANISOU 1429 C GLU A1009 7450 9056 10491 -699 703 901 C
ATOM 1430 O GLU A1009 188.529 9.591 135.463 1.00 71.57 O
ANISOU 1430 O GLU A1009 7418 9159 10617 -769 680 785 O
ATOM 1431 CB GLU A1009 187.077 7.285 134.071 1.00 66.34 C
ANISOU 1431 CB GLU A1009 6925 8808 9473 -478 644 834 C
ATOM 1432 CG GLU A1009 187.344 7.567 132.596 1.00 80.16 C
ANISOU 1432 CG GLU A1009 8616 10697 11145 -473 756 1034 C
ATOM 1433 CD GLU A1009 188.176 6.538 131.852 1.00105.52 C
ANISOU 1433 CD GLU A1009 11758 14155 14180 -405 793 994 C
ATOM 1434 OE1 GLU A1009 188.914 5.764 132.505 1.00104.61 O
ANISOU 1434 OE1 GLU A1009 11600 14080 14068 -385 747 833 O
ATOM 1435 OE2 GLU A1009 188.115 6.532 130.601 1.00101.21 O
ANISOU 1435 OE2 GLU A1009 11191 13777 13488 -363 873 1130 O
ATOM 1436 N SER A1010 187.016 10.815 134.287 1.00 68.54 N
ANISOU 1436 N SER A1010 7132 8594 10315 -743 786 1095 N
ATOM 1437 CA SER A1010 187.757 12.081 134.235 1.00 70.33 C
ANISOU 1437 CA SER A1010 7253 8655 10812 -892 870 1190 C
ATOM 1438 C SER A1010 187.876 12.718 135.630 1.00 73.95 C
ANISOU 1438 C SER A1010 7714 8892 11492 -990 802 959 C
ATOM 1439 O SER A1010 188.809 13.485 135.875 1.00 75.15 O
ANISOU 1439 O SER A1010 7750 8937 11868 -1139 834 930 O
ATOM 1440 CB SER A1010 187.081 13.052 133.273 1.00 75.18 C
ANISOU 1440 CB SER A1010 7885 9150 11529 -884 972 1480 C
ATOM 1441 OG SER A1010 187.024 12.518 131.961 1.00 83.63 O
ANISOU 1441 OG SER A1010 8942 10474 12362 -797 1031 1687 O
ATOM 1442 N TYR A1011 186.936 12.385 136.542 1.00 68.79 N
ANISOU 1442 N TYR A1011 7180 8187 10769 -909 711 787 N
ATOM 1443 CA TYR A1011 186.915 12.854 137.929 1.00 68.77 C
ANISOU 1443 CA TYR A1011 7196 8032 10902 -970 639 531 C
ATOM 1444 C TYR A1011 187.963 12.109 138.764 1.00 72.37 C
ANISOU 1444 C TYR A1011 7576 8667 11255 -1008 543 322 C
ATOM 1445 O TYR A1011 188.348 12.590 139.833 1.00 72.92 O
ANISOU 1445 O TYR A1011 7608 8660 11437 -1096 481 104 O
ATOM 1446 CB TYR A1011 185.516 12.680 138.538 1.00 68.44 C
ANISOU 1446 CB TYR A1011 7296 7926 10781 -851 595 450 C
ATOM 1447 CG TYR A1011 184.487 13.635 137.976 1.00 70.79 C
ANISOU 1447 CG TYR A1011 7647 8009 11241 -817 676 621 C
ATOM 1448 CD1 TYR A1011 183.721 13.291 136.866 1.00 71.85 C
ANISOU 1448 CD1 TYR A1011 7821 8231 11249 -710 713 862 C
ATOM 1449 CD2 TYR A1011 184.268 14.879 138.560 1.00 73.41 C
ANISOU 1449 CD2 TYR A1011 7981 8053 11858 -881 709 532 C
ATOM 1450 CE1 TYR A1011 182.775 14.168 136.341 1.00 73.56 C
ANISOU 1450 CE1 TYR A1011 8068 8271 11611 -662 778 1048 C
ATOM 1451 CE2 TYR A1011 183.306 15.753 138.061 1.00 75.41 C
ANISOU 1451 CE2 TYR A1011 8274 8090 12286 -826 787 705 C
ATOM 1452 CZ TYR A1011 182.565 15.396 136.946 1.00 82.66 C
ANISOU 1452 CZ TYR A1011 9223 9119 13067 -712 819 982 C
ATOM 1453 OH TYR A1011 181.637 16.269 136.432 1.00 86.49 O
ANISOU 1453 OH TYR A1011 9728 9409 13724 -645 888 1184 O
ATOM 1454 N LEU A1012 188.424 10.942 138.267 1.00 67.94 N
ANISOU 1454 N LEU A1012 6984 8349 10483 -933 529 381 N
ATOM 1455 CA LEU A1012 189.456 10.122 138.906 1.00 67.92 C
ANISOU 1455 CA LEU A1012 6891 8536 10380 -938 444 235 C
ATOM 1456 C LEU A1012 190.847 10.563 138.458 1.00 73.95 C
ANISOU 1456 C LEU A1012 7467 9345 11283 -1068 495 283 C
ATOM 1457 O LEU A1012 191.046 10.853 137.275 1.00 74.08 O
ANISOU 1457 O LEU A1012 7436 9366 11345 -1091 613 492 O
ATOM 1458 CB LEU A1012 189.279 8.623 138.586 1.00 66.19 C
ANISOU 1458 CB LEU A1012 6720 8521 9907 -780 415 270 C
ATOM 1459 CG LEU A1012 187.888 7.992 138.656 1.00 69.13 C
ANISOU 1459 CG LEU A1012 7255 8872 10139 -651 389 284 C
ATOM 1460 CD1 LEU A1012 187.887 6.662 137.933 1.00 68.41 C
ANISOU 1460 CD1 LEU A1012 7180 8946 9865 -530 391 344 C
ATOM 1461 CD2 LEU A1012 187.414 7.816 140.095 1.00 70.17 C
ANISOU 1461 CD2 LEU A1012 7452 8979 10231 -624 292 112 C
ATOM 1462 N THR A1013 191.813 10.581 139.391 1.00 71.81 N
ANISOU 1462 N THR A1013 7077 9141 11066 -1151 405 99 N
ATOM 1463 CA THR A1013 193.200 10.957 139.099 1.00 73.71 C
ANISOU 1463 CA THR A1013 7106 9445 11457 -1287 439 122 C
ATOM 1464 C THR A1013 194.138 9.788 139.400 1.00 76.90 C
ANISOU 1464 C THR A1013 7397 10125 11696 -1210 360 52 C
ATOM 1465 O THR A1013 193.927 9.051 140.365 1.00 75.34 O
ANISOU 1465 O THR A1013 7258 10023 11346 -1115 235 -91 O
ATOM 1466 CB THR A1013 193.613 12.228 139.854 1.00 85.12 C
ANISOU 1466 CB THR A1013 8461 10701 13181 -1488 402 -36 C
ATOM 1467 OG1 THR A1013 193.228 12.125 141.226 1.00 85.62 O
ANISOU 1467 OG1 THR A1013 8597 10767 13166 -1463 257 -300 O
ATOM 1468 CG2 THR A1013 193.022 13.489 139.239 1.00 85.36 C
ANISOU 1468 CG2 THR A1013 8541 10430 13463 -1582 525 101 C
ATOM 1469 N GLY A1014 195.156 9.635 138.557 1.00 74.54 N
ANISOU 1469 N GLY A1014 6932 9957 11433 -1240 444 174 N
ATOM 1470 CA GLY A1014 196.154 8.576 138.663 1.00 74.44 C
ANISOU 1470 CA GLY A1014 6779 10201 11302 -1154 397 136 C
ATOM 1471 C GLY A1014 195.686 7.258 138.081 1.00 76.15 C
ANISOU 1471 C GLY A1014 7108 10543 11282 -938 425 210 C
ATOM 1472 O GLY A1014 194.648 7.203 137.414 1.00 74.53 O
ANISOU 1472 O GLY A1014 7069 10253 10998 -871 492 307 O
ATOM 1473 N SER A1015 196.461 6.188 138.312 1.00 72.49 N
ANISOU 1473 N SER A1015 6541 10278 10723 -825 372 160 N
ATOM 1474 CA SER A1015 196.121 4.849 137.836 1.00 70.80 C
ANISOU 1474 CA SER A1015 6418 10159 10325 -616 393 194 C
ATOM 1475 C SER A1015 195.154 4.178 138.813 1.00 72.76 C
ANISOU 1475 C SER A1015 6843 10341 10461 -511 267 108 C
ATOM 1476 O SER A1015 195.031 4.629 139.956 1.00 72.92 O
ANISOU 1476 O SER A1015 6875 10318 10515 -580 156 8 O
ATOM 1477 CB SER A1015 197.379 4.004 137.659 1.00 75.68 C
ANISOU 1477 CB SER A1015 6838 10990 10929 -525 404 187 C
ATOM 1478 OG SER A1015 197.991 3.696 138.901 1.00 86.02 O
ANISOU 1478 OG SER A1015 8044 12381 12257 -510 250 78 O
ATOM 1479 N ARG A1016 194.476 3.101 138.372 1.00 67.12 N
ANISOU 1479 N ARG A1016 6257 9627 9617 -350 289 138 N
ATOM 1480 CA ARG A1016 193.545 2.345 139.212 1.00 65.00 C
ANISOU 1480 CA ARG A1016 6144 9296 9259 -248 191 92 C
ATOM 1481 C ARG A1016 194.289 1.659 140.365 1.00 70.26 C
ANISOU 1481 C ARG A1016 6711 10078 9906 -175 68 33 C
ATOM 1482 O ARG A1016 193.743 1.569 141.466 1.00 69.46 O
ANISOU 1482 O ARG A1016 6689 9951 9752 -160 -33 -7 O
ATOM 1483 CB ARG A1016 192.780 1.313 138.382 1.00 62.55 C
ANISOU 1483 CB ARG A1016 5959 8952 8856 -110 246 131 C
ATOM 1484 CG ARG A1016 191.603 0.726 139.131 1.00 66.98 C
ANISOU 1484 CG ARG A1016 6685 9407 9359 -42 170 114 C
ATOM 1485 CD ARG A1016 190.817 -0.224 138.276 1.00 66.01 C
ANISOU 1485 CD ARG A1016 6671 9231 9178 63 217 129 C
ATOM 1486 NE ARG A1016 189.458 -0.373 138.788 1.00 65.54 N
ANISOU 1486 NE ARG A1016 6767 9046 9090 69 171 138 N
ATOM 1487 CZ ARG A1016 188.442 0.410 138.444 1.00 74.11 C
ANISOU 1487 CZ ARG A1016 7946 10048 10165 -5 201 168 C
ATOM 1488 NH1 ARG A1016 188.620 1.397 137.574 1.00 62.35 N
ANISOU 1488 NH1 ARG A1016 6421 8576 8692 -89 274 211 N
ATOM 1489 NH2 ARG A1016 187.241 0.213 138.966 1.00 55.70 N
ANISOU 1489 NH2 ARG A1016 5730 7618 7815 9 163 177 N
ATOM 1490 N ASP A1017 195.533 1.192 140.106 1.00 68.63 N
ANISOU 1490 N ASP A1017 6319 10022 9735 -121 80 40 N
ATOM 1491 CA ASP A1017 196.412 0.548 141.084 1.00 69.81 C
ANISOU 1491 CA ASP A1017 6330 10317 9877 -37 -38 13 C
ATOM 1492 C ASP A1017 196.651 1.476 142.282 1.00 74.50 C
ANISOU 1492 C ASP A1017 6858 10964 10484 -175 -165 -72 C
ATOM 1493 O ASP A1017 196.490 1.040 143.426 1.00 73.94 O
ANISOU 1493 O ASP A1017 6813 10959 10323 -105 -291 -94 O
ATOM 1494 CB ASP A1017 197.765 0.160 140.437 1.00 73.58 C
ANISOU 1494 CB ASP A1017 6582 10951 10423 22 20 35 C
ATOM 1495 CG ASP A1017 197.717 -0.785 139.247 1.00 85.35 C
ANISOU 1495 CG ASP A1017 8107 12426 11895 173 150 73 C
ATOM 1496 OD1 ASP A1017 196.613 -0.995 138.691 1.00 84.41 O
ANISOU 1496 OD1 ASP A1017 8186 12171 11716 198 206 81 O
ATOM 1497 OD2 ASP A1017 198.793 -1.277 138.841 1.00 94.23 O
ANISOU 1497 OD2 ASP A1017 9048 13688 13066 263 198 79 O
ATOM 1498 N AGLU A1018 197.014 2.749 142.026 0.50 72.10 N
ANISOU 1498 N AGLU A1018 6469 10633 10293 -369 -129 -122 N
ATOM 1499 N BGLU A1018 197.014 2.748 141.999 0.50 71.86 N
ANISOU 1499 N BGLU A1018 6438 10601 10263 -369 -126 -120 N
ATOM 1500 CA AGLU A1018 197.286 3.723 143.084 0.50 73.24 C
ANISOU 1500 CA AGLU A1018 6538 10810 10480 -524 -248 -254 C
ATOM 1501 CA BGLU A1018 197.274 3.811 142.973 0.50 72.95 C
ANISOU 1501 CA BGLU A1018 6502 10758 10456 -537 -233 -250 C
ATOM 1502 C AGLU A1018 195.993 4.193 143.759 0.50 76.01 C
ANISOU 1502 C AGLU A1018 7103 11015 10761 -558 -284 -322 C
ATOM 1503 C BGLU A1018 196.005 4.175 143.732 0.50 75.85 C
ANISOU 1503 C BGLU A1018 7081 10995 10742 -556 -281 -319 C
ATOM 1504 O AGLU A1018 196.010 4.432 144.967 0.50 76.71 O
ANISOU 1504 O AGLU A1018 7176 11187 10783 -588 -416 -447 O
ATOM 1505 O BGLU A1018 196.051 4.353 144.950 0.50 76.55 O
ANISOU 1505 O BGLU A1018 7150 11177 10759 -577 -417 -439 O
ATOM 1506 CB AGLU A1018 198.109 4.916 142.565 0.50 76.36 C
ANISOU 1506 CB AGLU A1018 6759 11182 11071 -733 -188 -286 C
ATOM 1507 CB BGLU A1018 197.820 5.067 142.268 0.50 75.52 C
ANISOU 1507 CB BGLU A1018 6706 11010 10979 -746 -142 -261 C
ATOM 1508 CG AGLU A1018 199.532 4.556 142.150 0.50 88.53 C
ANISOU 1508 CG AGLU A1018 8034 12918 12686 -718 -170 -242 C
ATOM 1509 CG BGLU A1018 199.244 4.957 141.749 0.50 86.53 C
ANISOU 1509 CG BGLU A1018 7830 12571 12475 -773 -105 -218 C
ATOM 1510 CD AGLU A1018 200.371 3.829 143.186 0.50108.51 C
ANISOU 1510 CD AGLU A1018 10401 15686 15143 -621 -339 -301 C
ATOM 1511 CD BGLU A1018 199.638 6.021 140.740 0.50103.36 C
ANISOU 1511 CD BGLU A1018 9860 14613 14800 -955 43 -149 C
ATOM 1512 OE1AGLU A1018 200.838 4.484 144.146 0.50103.47 O
ANISOU 1512 OE1AGLU A1018 9640 15136 14538 -750 -481 -441 O
ATOM 1513 OE1BGLU A1018 199.250 7.198 140.919 0.50 93.38 O
ANISOU 1513 OE1BGLU A1018 8642 13171 13667 -1135 48 -204 O
ATOM 1514 OE2AGLU A1018 200.557 2.599 143.039 0.50100.27 O
ANISOU 1514 OE2AGLU A1018 9348 14740 14012 -410 -334 -211 O
ATOM 1515 OE2BGLU A1018 200.355 5.675 139.773 0.50 96.56 O
ANISOU 1515 OE2BGLU A1018 8864 13859 13967 -912 164 -34 O
ATOM 1516 N ARG A1019 194.875 4.292 143.000 1.00 70.50 N
ANISOU 1516 N ARG A1019 6594 10129 10063 -541 -169 -246 N
ATOM 1517 CA ARG A1019 193.553 4.662 143.532 1.00 68.87 C
ANISOU 1517 CA ARG A1019 6584 9782 9800 -548 -181 -290 C
ATOM 1518 C ARG A1019 193.045 3.599 144.504 1.00 72.17 C
ANISOU 1518 C ARG A1019 7090 10295 10038 -392 -273 -283 C
ATOM 1519 O ARG A1019 192.459 3.950 145.526 1.00 72.49 O
ANISOU 1519 O ARG A1019 7202 10340 10000 -411 -339 -375 O
ATOM 1520 CB ARG A1019 192.535 4.867 142.404 1.00 66.64 C
ANISOU 1520 CB ARG A1019 6450 9314 9555 -543 -45 -181 C
ATOM 1521 CG ARG A1019 192.654 6.206 141.688 1.00 74.40 C
ANISOU 1521 CG ARG A1019 7393 10158 10719 -708 47 -166 C
ATOM 1522 CD ARG A1019 191.381 6.581 140.943 1.00 75.72 C
ANISOU 1522 CD ARG A1019 7726 10144 10899 -694 144 -68 C
ATOM 1523 NE ARG A1019 190.935 5.534 140.019 1.00 77.22 N
ANISOU 1523 NE ARG A1019 7989 10384 10968 -558 200 56 N
ATOM 1524 CZ ARG A1019 191.317 5.431 138.750 1.00 89.55 C
ANISOU 1524 CZ ARG A1019 9497 11991 12536 -549 301 172 C
ATOM 1525 NH1 ARG A1019 192.155 6.316 138.227 1.00 76.40 N
ANISOU 1525 NH1 ARG A1019 7700 10327 11003 -672 373 225 N
ATOM 1526 NH2 ARG A1019 190.861 4.443 137.992 1.00 76.23 N
ANISOU 1526 NH2 ARG A1019 7881 10357 10724 -423 336 232 N
ATOM 1527 N LYS A1020 193.298 2.309 144.195 1.00 67.61 N
ANISOU 1527 N LYS A1020 6494 9793 9402 -237 -267 -170 N
ATOM 1528 CA LYS A1020 192.944 1.168 145.038 1.00 66.90 C
ANISOU 1528 CA LYS A1020 6463 9779 9179 -79 -341 -110 C
ATOM 1529 C LYS A1020 193.881 1.119 146.248 1.00 73.88 C
ANISOU 1529 C LYS A1020 7195 10891 9983 -65 -489 -167 C
ATOM 1530 O LYS A1020 193.411 0.910 147.365 1.00 73.74 O
ANISOU 1530 O LYS A1020 7236 10959 9823 -13 -570 -172 O
ATOM 1531 CB LYS A1020 193.019 -0.138 144.233 1.00 67.90 C
ANISOU 1531 CB LYS A1020 6600 9872 9327 76 -281 14 C
ATOM 1532 CG LYS A1020 192.417 -1.352 144.939 1.00 71.62 C
ANISOU 1532 CG LYS A1020 7159 10339 9715 233 -326 115 C
ATOM 1533 CD LYS A1020 192.330 -2.559 144.018 1.00 74.26 C
ANISOU 1533 CD LYS A1020 7525 10569 10122 366 -252 198 C
ATOM 1534 CE LYS A1020 193.602 -3.371 143.934 1.00 79.34 C
ANISOU 1534 CE LYS A1020 8001 11324 10821 491 -277 236 C
ATOM 1535 NZ LYS A1020 193.621 -4.229 142.720 1.00 84.13 N
ANISOU 1535 NZ LYS A1020 8627 11816 11524 587 -174 243 N
ATOM 1536 N LYS A1021 195.201 1.331 146.018 1.00 73.00 N
ANISOU 1536 N LYS A1021 6877 10905 9956 -112 -521 -205 N
ATOM 1537 CA LYS A1021 196.254 1.341 147.038 1.00 75.43 C
ANISOU 1537 CA LYS A1021 6993 11464 10203 -111 -677 -267 C
ATOM 1538 C LYS A1021 195.964 2.402 148.099 1.00 81.09 C
ANISOU 1538 C LYS A1021 7731 12239 10841 -248 -774 -450 C
ATOM 1539 O LYS A1021 195.989 2.080 149.287 1.00 82.12 O
ANISOU 1539 O LYS A1021 7841 12570 10792 -176 -905 -471 O
ATOM 1540 CB LYS A1021 197.633 1.585 146.392 1.00 79.57 C
ANISOU 1540 CB LYS A1021 7278 12080 10876 -175 -667 -288 C
ATOM 1541 CG LYS A1021 198.824 1.318 147.306 1.00 97.27 C
ANISOU 1541 CG LYS A1021 9281 14611 13064 -135 -834 -317 C
ATOM 1542 CD LYS A1021 200.135 1.392 146.536 1.00108.45 C
ANISOU 1542 CD LYS A1021 10448 16114 14647 -173 -797 -305 C
ATOM 1543 CE LYS A1021 201.314 0.967 147.375 1.00120.38 C
ANISOU 1543 CE LYS A1021 11700 17928 16110 -99 -967 -305 C
ATOM 1544 NZ LYS A1021 202.565 0.915 146.574 1.00129.58 N
ANISOU 1544 NZ LYS A1021 12605 19184 17447 -110 -912 -273 N
ATOM 1545 N SER A1022 195.663 3.649 147.668 1.00 77.79 N
ANISOU 1545 N SER A1022 7355 11647 10555 -433 -705 -579 N
ATOM 1546 CA SER A1022 195.348 4.773 148.553 1.00 79.03 C
ANISOU 1546 CA SER A1022 7538 11802 10687 -573 -776 -798 C
ATOM 1547 C SER A1022 194.057 4.512 149.325 1.00 82.37 C
ANISOU 1547 C SER A1022 8166 12210 10921 -475 -777 -795 C
ATOM 1548 O SER A1022 194.016 4.770 150.528 1.00 83.61 O
ANISOU 1548 O SER A1022 8309 12542 10917 -482 -893 -943 O
ATOM 1549 CB SER A1022 195.237 6.073 147.762 1.00 82.94 C
ANISOU 1549 CB SER A1022 8044 12048 11421 -770 -671 -889 C
ATOM 1550 OG SER A1022 195.192 7.197 148.626 1.00 94.81 O
ANISOU 1550 OG SER A1022 9528 13541 12954 -918 -750 -1144 O
ATOM 1551 N LEU A1023 193.025 3.965 148.638 1.00 76.72 N
ANISOU 1551 N LEU A1023 7624 11314 10213 -381 -650 -631 N
ATOM 1552 CA LEU A1023 191.712 3.620 149.194 1.00 75.39 C
ANISOU 1552 CA LEU A1023 7639 11108 9897 -286 -621 -585 C
ATOM 1553 C LEU A1023 191.840 2.573 150.303 1.00 80.17 C
ANISOU 1553 C LEU A1023 8219 11970 10274 -132 -727 -496 C
ATOM 1554 O LEU A1023 191.269 2.759 151.378 1.00 80.58 O
ANISOU 1554 O LEU A1023 8330 12142 10146 -110 -773 -570 O
ATOM 1555 CB LEU A1023 190.791 3.097 148.079 1.00 73.01 C
ANISOU 1555 CB LEU A1023 7479 10584 9680 -224 -480 -413 C
ATOM 1556 CG LEU A1023 189.292 3.135 148.345 1.00 76.37 C
ANISOU 1556 CG LEU A1023 8083 10895 10037 -184 -413 -388 C
ATOM 1557 CD1 LEU A1023 188.681 4.424 147.819 1.00 76.18 C
ANISOU 1557 CD1 LEU A1023 8125 10663 10158 -310 -329 -496 C
ATOM 1558 CD2 LEU A1023 188.613 1.950 147.701 1.00 76.59 C
ANISOU 1558 CD2 LEU A1023 8199 10832 10068 -64 -344 -186 C
ATOM 1559 N LEU A1024 192.601 1.489 150.045 1.00 76.88 N
ANISOU 1559 N LEU A1024 7706 11643 9864 -17 -759 -331 N
ATOM 1560 CA LEU A1024 192.828 0.411 151.010 1.00 77.92 C
ANISOU 1560 CA LEU A1024 7792 12004 9811 150 -856 -188 C
ATOM 1561 C LEU A1024 193.677 0.901 152.190 1.00 85.29 C
ANISOU 1561 C LEU A1024 8572 13256 10580 112 -1028 -335 C
ATOM 1562 O LEU A1024 193.421 0.486 153.318 1.00 85.94 O
ANISOU 1562 O LEU A1024 8669 13558 10427 213 -1107 -277 O
ATOM 1563 CB LEU A1024 193.473 -0.818 150.344 1.00 77.54 C
ANISOU 1563 CB LEU A1024 7668 11929 9866 290 -837 15 C
ATOM 1564 CG LEU A1024 192.601 -1.588 149.341 1.00 79.59 C
ANISOU 1564 CG LEU A1024 8077 11915 10249 360 -692 158 C
ATOM 1565 CD1 LEU A1024 193.439 -2.489 148.471 1.00 79.55 C
ANISOU 1565 CD1 LEU A1024 7973 11863 10390 462 -662 259 C
ATOM 1566 CD2 LEU A1024 191.507 -2.379 150.033 1.00 81.73 C
ANISOU 1566 CD2 LEU A1024 8484 12163 10407 471 -673 315 C
ATOM 1567 N SER A1025 194.643 1.818 151.939 1.00 83.87 N
ANISOU 1567 N SER A1025 8239 13112 10517 -41 -1085 -528 N
ATOM 1568 CA SER A1025 195.499 2.419 152.971 1.00 87.00 C
ANISOU 1568 CA SER A1025 8464 13805 10785 -116 -1264 -726 C
ATOM 1569 C SER A1025 194.687 3.341 153.897 1.00 92.91 C
ANISOU 1569 C SER A1025 9324 14601 11379 -200 -1291 -958 C
ATOM 1570 O SER A1025 195.012 3.447 155.081 1.00 95.17 O
ANISOU 1570 O SER A1025 9526 15207 11429 -183 -1445 -1078 O
ATOM 1571 CB SER A1025 196.648 3.196 152.337 1.00 91.43 C
ANISOU 1571 CB SER A1025 8831 14337 11571 -287 -1294 -875 C
ATOM 1572 OG SER A1025 197.547 3.691 153.316 1.00103.40 O
ANISOU 1572 OG SER A1025 10152 16156 12979 -365 -1487 -1076 O
ATOM 1573 N LYS A1026 193.631 3.995 153.353 1.00 88.25 N
ANISOU 1573 N LYS A1026 8912 13708 10911 -278 -1142 -1023 N
ATOM 1574 CA LYS A1026 192.721 4.884 154.087 1.00 88.99 C
ANISOU 1574 CA LYS A1026 9126 13785 10900 -340 -1127 -1244 C
ATOM 1575 C LYS A1026 191.892 4.097 155.104 1.00 93.52 C
ANISOU 1575 C LYS A1026 9804 14570 11161 -165 -1137 -1119 C
ATOM 1576 O LYS A1026 191.546 4.633 156.158 1.00 94.97 O
ANISOU 1576 O LYS A1026 10011 14938 11136 -177 -1191 -1321 O
ATOM 1577 CB LYS A1026 191.784 5.624 153.116 1.00 89.61 C
ANISOU 1577 CB LYS A1026 9357 13473 11219 -429 -951 -1274 C
ATOM 1578 CG LYS A1026 192.391 6.879 152.492 1.00107.60 C
ANISOU 1578 CG LYS A1026 11548 15555 13781 -640 -939 -1480 C
ATOM 1579 CD LYS A1026 191.760 7.207 151.132 1.00117.28 C
ANISOU 1579 CD LYS A1026 12882 16410 15268 -684 -760 -1352 C
ATOM 1580 CE LYS A1026 190.597 8.172 151.203 1.00129.16 C
ANISOU 1580 CE LYS A1026 14539 17687 16850 -731 -662 -1486 C
ATOM 1581 NZ LYS A1026 191.052 9.582 151.319 1.00140.61 N
ANISOU 1581 NZ LYS A1026 15911 19003 18511 -926 -686 -1770 N
ATOM 1582 N PHE A1027 191.578 2.827 154.780 1.00 88.80 N
ANISOU 1582 N PHE A1027 9261 13942 10539 -5 -1075 -791 N
ATOM 1583 CA PHE A1027 190.798 1.924 155.625 1.00 89.03 C
ANISOU 1583 CA PHE A1027 9376 14137 10316 164 -1060 -591 C
ATOM 1584 C PHE A1027 191.702 0.966 156.434 1.00 95.16 C
ANISOU 1584 C PHE A1027 10006 15265 10884 305 -1210 -419 C
ATOM 1585 O PHE A1027 191.189 0.082 157.127 1.00 95.43 O
ANISOU 1585 O PHE A1027 10089 15450 10720 461 -1198 -187 O
ATOM 1586 CB PHE A1027 189.791 1.128 154.768 1.00 88.15 C
ANISOU 1586 CB PHE A1027 9412 13732 10349 241 -894 -334 C
ATOM 1587 CG PHE A1027 188.811 1.948 153.955 1.00 87.75 C
ANISOU 1587 CG PHE A1027 9496 13360 10484 133 -751 -448 C
ATOM 1588 CD1 PHE A1027 188.131 3.020 154.526 1.00 91.62 C
ANISOU 1588 CD1 PHE A1027 10052 13860 10898 61 -724 -682 C
ATOM 1589 CD2 PHE A1027 188.520 1.609 152.640 1.00 87.54 C
ANISOU 1589 CD2 PHE A1027 9527 13036 10697 123 -643 -317 C
ATOM 1590 CE1 PHE A1027 187.215 3.767 153.779 1.00 90.91 C
ANISOU 1590 CE1 PHE A1027 10074 13470 10998 -16 -592 -758 C
ATOM 1591 CE2 PHE A1027 187.606 2.359 151.893 1.00 88.80 C
ANISOU 1591 CE2 PHE A1027 9797 12931 11010 38 -524 -393 C
ATOM 1592 CZ PHE A1027 186.956 3.429 152.469 1.00 87.63 C
ANISOU 1592 CZ PHE A1027 9705 12780 10810 -26 -499 -597 C
ATOM 1593 N GLY A1028 193.020 1.176 156.359 1.00 93.20 N
ANISOU 1593 N GLY A1028 9569 15153 10692 251 -1346 -519 N
ATOM 1594 CA GLY A1028 194.026 0.381 157.060 1.00 95.46 C
ANISOU 1594 CA GLY A1028 9677 15786 10808 382 -1509 -369 C
ATOM 1595 C GLY A1028 194.063 -1.062 156.605 1.00 98.28 C
ANISOU 1595 C GLY A1028 10041 16044 11258 570 -1449 16 C
ATOM 1596 O GLY A1028 193.890 -1.976 157.416 1.00 99.33 O
ANISOU 1596 O GLY A1028 10173 16380 11187 745 -1487 266 O
ATOM 1597 N MET A1029 194.265 -1.266 155.290 1.00 92.48 N
ANISOU 1597 N MET A1029 9315 14988 10835 538 -1345 64 N
ATOM 1598 CA MET A1029 194.288 -2.576 154.637 1.00 91.03 C
ANISOU 1598 CA MET A1029 9147 14634 10808 700 -1267 366 C
ATOM 1599 C MET A1029 195.417 -2.706 153.617 1.00 93.64 C
ANISOU 1599 C MET A1029 9324 14872 11383 687 -1270 347 C
ATOM 1600 O MET A1029 195.856 -1.716 153.028 1.00 92.54 O
ANISOU 1600 O MET A1029 9125 14671 11365 516 -1263 120 O
ATOM 1601 CB MET A1029 192.952 -2.844 153.925 1.00 90.65 C
ANISOU 1601 CB MET A1029 9321 14236 10886 694 -1080 449 C
ATOM 1602 CG MET A1029 191.829 -3.242 154.848 1.00 94.74 C
ANISOU 1602 CG MET A1029 9969 14824 11203 775 -1044 597 C
ATOM 1603 SD MET A1029 190.423 -3.909 153.933 1.00 96.34 S
ANISOU 1603 SD MET A1029 10376 14619 11610 792 -843 754 S
ATOM 1604 CE MET A1029 189.652 -2.402 153.355 1.00 91.05 C
ANISOU 1604 CE MET A1029 9820 13780 10996 582 -760 442 C
ATOM 1605 N ASP A1030 195.842 -3.953 153.384 1.00 90.18 N
ANISOU 1605 N ASP A1030 8823 14404 11036 875 -1261 599 N
ATOM 1606 CA ASP A1030 196.875 -4.328 152.423 1.00 89.75 C
ANISOU 1606 CA ASP A1030 8621 14270 11212 918 -1240 619 C
ATOM 1607 C ASP A1030 196.274 -4.373 151.010 1.00 89.76 C
ANISOU 1607 C ASP A1030 8767 13896 11443 861 -1051 580 C
ATOM 1608 O ASP A1030 195.049 -4.384 150.873 1.00 87.39 O
ANISOU 1608 O ASP A1030 8672 13402 11131 829 -954 598 O
ATOM 1609 CB ASP A1030 197.455 -5.699 152.819 1.00 93.65 C
ANISOU 1609 CB ASP A1030 9001 14864 11715 1172 -1298 907 C
ATOM 1610 CG ASP A1030 198.945 -5.873 152.608 1.00108.20 C
ANISOU 1610 CG ASP A1030 10573 16878 13659 1240 -1388 908 C
ATOM 1611 OD1 ASP A1030 199.601 -4.909 152.153 1.00109.37 O
ANISOU 1611 OD1 ASP A1030 10604 17083 13869 1072 -1407 680 O
ATOM 1612 OD2 ASP A1030 199.459 -6.971 152.908 1.00116.60 O
ANISOU 1612 OD2 ASP A1030 11530 18015 14758 1465 -1434 1149 O
ATOM 1613 N GLU A1031 197.127 -4.392 149.963 1.00 85.52 N
ANISOU 1613 N GLU A1031 8109 13285 11099 851 -999 527 N
ATOM 1614 CA GLU A1031 196.677 -4.451 148.569 1.00 82.72 C
ANISOU 1614 CA GLU A1031 7868 12633 10928 809 -826 484 C
ATOM 1615 C GLU A1031 196.155 -5.848 148.225 1.00 84.62 C
ANISOU 1615 C GLU A1031 8213 12673 11267 998 -745 667 C
ATOM 1616 O GLU A1031 196.899 -6.831 148.272 1.00 85.88 O
ANISOU 1616 O GLU A1031 8250 12870 11509 1179 -770 798 O
ATOM 1617 CB GLU A1031 197.791 -4.043 147.593 1.00 84.66 C
ANISOU 1617 CB GLU A1031 7937 12909 11321 749 -784 378 C
ATOM 1618 CG GLU A1031 197.929 -2.546 147.391 1.00 95.50 C
ANISOU 1618 CG GLU A1031 9274 14315 12695 505 -783 180 C
ATOM 1619 CD GLU A1031 199.047 -2.165 146.440 1.00117.58 C
ANISOU 1619 CD GLU A1031 11876 17154 15647 439 -725 116 C
ATOM 1620 OE1 GLU A1031 200.230 -2.247 146.845 1.00108.92 O
ANISOU 1620 OE1 GLU A1031 10536 16282 14567 474 -826 118 O
ATOM 1621 OE2 GLU A1031 198.739 -1.773 145.292 1.00113.04 O
ANISOU 1621 OE2 GLU A1031 11374 16407 15168 355 -577 75 O
ATOM 1622 N GLY A1032 194.872 -5.909 147.903 1.00 78.02 N
ANISOU 1622 N GLY A1032 7590 11615 10440 952 -651 670 N
ATOM 1623 CA GLY A1032 194.185 -7.138 147.536 1.00 76.90 C
ANISOU 1623 CA GLY A1032 7564 11238 10418 1086 -568 807 C
ATOM 1624 C GLY A1032 193.029 -6.876 146.597 1.00 77.46 C
ANISOU 1624 C GLY A1032 7818 11068 10546 975 -448 711 C
ATOM 1625 O GLY A1032 192.727 -5.719 146.288 1.00 75.67 O
ANISOU 1625 O GLY A1032 7635 10859 10258 808 -426 568 O
ATOM 1626 N VAL A1033 192.376 -7.959 146.139 1.00 73.15 N
ANISOU 1626 N VAL A1033 7370 10291 10134 1069 -375 790 N
ATOM 1627 CA VAL A1033 191.228 -7.908 145.228 1.00 70.86 C
ANISOU 1627 CA VAL A1033 7239 9781 9904 981 -277 707 C
ATOM 1628 C VAL A1033 190.064 -7.284 146.002 1.00 73.02 C
ANISOU 1628 C VAL A1033 7632 10067 10044 873 -292 742 C
ATOM 1629 O VAL A1033 189.479 -7.930 146.870 1.00 73.47 O
ANISOU 1629 O VAL A1033 7735 10097 10082 938 -310 905 O
ATOM 1630 CB VAL A1033 190.892 -9.301 144.633 1.00 75.26 C
ANISOU 1630 CB VAL A1033 7846 10089 10660 1105 -213 758 C
ATOM 1631 CG1 VAL A1033 189.904 -9.181 143.477 1.00 73.46 C
ANISOU 1631 CG1 VAL A1033 7745 9682 10483 1006 -128 617 C
ATOM 1632 CG2 VAL A1033 192.160 -10.013 144.175 1.00 76.71 C
ANISOU 1632 CG2 VAL A1033 7888 10286 10973 1258 -204 742 C
ATOM 1633 N THR A1034 189.794 -5.997 145.732 1.00 67.47 N
ANISOU 1633 N THR A1034 6963 9418 9253 718 -279 601 N
ATOM 1634 CA THR A1034 188.801 -5.200 146.444 1.00 66.17 C
ANISOU 1634 CA THR A1034 6892 9286 8963 619 -286 592 C
ATOM 1635 C THR A1034 187.393 -5.342 145.842 1.00 68.10 C
ANISOU 1635 C THR A1034 7279 9327 9271 570 -204 595 C
ATOM 1636 O THR A1034 187.169 -5.068 144.661 1.00 67.03 O
ANISOU 1636 O THR A1034 7178 9085 9208 510 -146 497 O
ATOM 1637 CB THR A1034 189.250 -3.734 146.505 1.00 72.63 C
ANISOU 1637 CB THR A1034 7661 10235 9699 485 -315 435 C
ATOM 1638 OG1 THR A1034 190.630 -3.686 146.869 1.00 72.89 O
ANISOU 1638 OG1 THR A1034 7533 10452 9709 519 -396 416 O
ATOM 1639 CG2 THR A1034 188.464 -2.932 147.507 1.00 71.44 C
ANISOU 1639 CG2 THR A1034 7578 10157 9409 415 -338 402 C
ATOM 1640 N PHE A1035 186.453 -5.753 146.703 1.00 64.14 N
ANISOU 1640 N PHE A1035 6844 8802 8725 597 -200 719 N
ATOM 1641 CA PHE A1035 185.028 -5.952 146.441 1.00 62.76 C
ANISOU 1641 CA PHE A1035 6778 8465 8605 552 -133 754 C
ATOM 1642 C PHE A1035 184.246 -4.908 147.221 1.00 65.87 C
ANISOU 1642 C PHE A1035 7218 8958 8851 475 -125 725 C
ATOM 1643 O PHE A1035 184.522 -4.692 148.403 1.00 66.34 O
ANISOU 1643 O PHE A1035 7244 9200 8760 507 -170 770 O
ATOM 1644 CB PHE A1035 184.598 -7.373 146.833 1.00 65.56 C
ANISOU 1644 CB PHE A1035 7147 8698 9065 650 -117 944 C
ATOM 1645 CG PHE A1035 185.291 -8.474 146.069 1.00 67.75 C
ANISOU 1645 CG PHE A1035 7383 8832 9528 742 -115 951 C
ATOM 1646 CD1 PHE A1035 184.758 -8.961 144.883 1.00 70.21 C
ANISOU 1646 CD1 PHE A1035 7743 8934 10001 711 -65 856 C
ATOM 1647 CD2 PHE A1035 186.470 -9.036 146.543 1.00 71.26 C
ANISOU 1647 CD2 PHE A1035 7730 9361 9983 868 -165 1039 C
ATOM 1648 CE1 PHE A1035 185.405 -9.973 144.172 1.00 72.13 C
ANISOU 1648 CE1 PHE A1035 7948 9042 10417 805 -55 819 C
ATOM 1649 CE2 PHE A1035 187.119 -10.045 145.829 1.00 75.09 C
ANISOU 1649 CE2 PHE A1035 8170 9700 10660 972 -150 1030 C
ATOM 1650 CZ PHE A1035 186.586 -10.502 144.644 1.00 72.74 C
ANISOU 1650 CZ PHE A1035 7932 9181 10524 940 -90 905 C
ATOM 1651 N MET A1036 183.289 -4.242 146.565 1.00 60.99 N
ANISOU 1651 N MET A1036 6668 8239 8267 384 -70 642 N
ATOM 1652 CA MET A1036 182.548 -3.156 147.189 1.00 60.51 C
ANISOU 1652 CA MET A1036 6645 8248 8097 322 -48 587 C
ATOM 1653 C MET A1036 181.035 -3.341 147.116 1.00 64.11 C
ANISOU 1653 C MET A1036 7166 8594 8599 301 21 654 C
ATOM 1654 O MET A1036 180.498 -3.659 146.060 1.00 63.15 O
ANISOU 1654 O MET A1036 7068 8321 8605 271 48 648 O
ATOM 1655 CB MET A1036 182.948 -1.835 146.507 1.00 62.08 C
ANISOU 1655 CB MET A1036 6835 8445 8309 229 -48 416 C
ATOM 1656 CG MET A1036 182.311 -0.591 147.082 1.00 65.82 C
ANISOU 1656 CG MET A1036 7342 8955 8713 169 -23 321 C
ATOM 1657 SD MET A1036 182.135 0.638 145.773 1.00 69.18 S
ANISOU 1657 SD MET A1036 7786 9237 9263 69 23 214 S
ATOM 1658 CE MET A1036 180.935 1.713 146.498 1.00 66.17 C
ANISOU 1658 CE MET A1036 7457 8834 8849 45 76 149 C
ATOM 1659 N PHE A1037 180.356 -3.089 148.243 1.00 61.10 N
ANISOU 1659 N PHE A1037 6800 8316 8101 315 49 705 N
ATOM 1660 CA PHE A1037 178.904 -3.089 148.346 1.00 60.70 C
ANISOU 1660 CA PHE A1037 6785 8200 8078 294 126 767 C
ATOM 1661 C PHE A1037 178.447 -1.691 148.714 1.00 65.32 C
ANISOU 1661 C PHE A1037 7389 8857 8572 256 160 629 C
ATOM 1662 O PHE A1037 179.032 -1.055 149.595 1.00 66.00 O
ANISOU 1662 O PHE A1037 7462 9104 8511 270 132 541 O
ATOM 1663 CB PHE A1037 178.383 -4.119 149.366 1.00 63.54 C
ANISOU 1663 CB PHE A1037 7131 8616 8395 359 162 977 C
ATOM 1664 CG PHE A1037 176.887 -4.068 149.618 1.00 64.87 C
ANISOU 1664 CG PHE A1037 7310 8754 8585 334 255 1051 C
ATOM 1665 CD1 PHE A1037 176.008 -4.810 148.840 1.00 67.33 C
ANISOU 1665 CD1 PHE A1037 7615 8875 9091 293 287 1130 C
ATOM 1666 CD2 PHE A1037 176.361 -3.269 150.628 1.00 67.53 C
ANISOU 1666 CD2 PHE A1037 7647 9262 8749 352 310 1022 C
ATOM 1667 CE1 PHE A1037 174.627 -4.756 149.071 1.00 68.26 C
ANISOU 1667 CE1 PHE A1037 7715 8979 9244 264 372 1203 C
ATOM 1668 CE2 PHE A1037 174.980 -3.207 150.848 1.00 70.38 C
ANISOU 1668 CE2 PHE A1037 7997 9608 9136 340 410 1091 C
ATOM 1669 CZ PHE A1037 174.124 -3.952 150.070 1.00 67.83 C
ANISOU 1669 CZ PHE A1037 7654 9099 9019 293 439 1194 C
ATOM 1670 N ILE A1038 177.380 -1.235 148.055 1.00 61.24 N
ANISOU 1670 N ILE A1038 6895 8223 8151 213 215 603 N
ATOM 1671 CA ILE A1038 176.754 0.057 148.293 1.00 61.10 C
ANISOU 1671 CA ILE A1038 6892 8222 8103 193 265 486 C
ATOM 1672 C ILE A1038 175.232 -0.141 148.191 1.00 64.53 C
ANISOU 1672 C ILE A1038 7320 8593 8604 198 344 581 C
ATOM 1673 O ILE A1038 174.735 -0.744 147.233 1.00 63.31 O
ANISOU 1673 O ILE A1038 7156 8317 8584 169 337 654 O
ATOM 1674 CB ILE A1038 177.323 1.168 147.361 1.00 63.73 C
ANISOU 1674 CB ILE A1038 7233 8462 8518 134 239 341 C
ATOM 1675 CG1 ILE A1038 176.711 2.547 147.666 1.00 64.74 C
ANISOU 1675 CG1 ILE A1038 7375 8567 8657 124 296 217 C
ATOM 1676 CG2 ILE A1038 177.233 0.822 145.869 1.00 63.72 C
ANISOU 1676 CG2 ILE A1038 7232 8324 8655 100 223 391 C
ATOM 1677 CD1 ILE A1038 177.591 3.410 148.495 1.00 74.07 C
ANISOU 1677 CD1 ILE A1038 8551 9838 9752 109 268 43 C
ATOM 1678 N GLY A1039 174.532 0.311 149.223 1.00 61.69 N
ANISOU 1678 N GLY A1039 6954 8342 8145 237 417 569 N
ATOM 1679 CA GLY A1039 173.086 0.195 149.325 1.00 61.66 C
ANISOU 1679 CA GLY A1039 6918 8318 8193 251 508 661 C
ATOM 1680 C GLY A1039 172.615 -0.087 150.733 1.00 66.96 C
ANISOU 1680 C GLY A1039 7565 9176 8700 313 590 742 C
ATOM 1681 O GLY A1039 173.424 -0.369 151.619 1.00 67.88 O
ANISOU 1681 O GLY A1039 7692 9450 8648 350 562 754 O
ATOM 1682 N ARG A1040 171.289 -0.029 150.928 1.00 63.37 N
ANISOU 1682 N ARG A1040 7062 8730 8285 330 693 812 N
ATOM 1683 CA ARG A1040 170.595 -0.235 152.196 1.00 64.60 C
ANISOU 1683 CA ARG A1040 7176 9080 8288 394 808 909 C
ATOM 1684 C ARG A1040 170.827 -1.629 152.786 1.00 69.18 C
ANISOU 1684 C ARG A1040 7734 9742 8810 402 810 1153 C
ATOM 1685 O ARG A1040 171.011 -2.609 152.057 1.00 67.70 O
ANISOU 1685 O ARG A1040 7540 9393 8789 349 751 1276 O
ATOM 1686 CB ARG A1040 169.087 -0.011 152.003 1.00 64.67 C
ANISOU 1686 CB ARG A1040 7111 9046 8416 398 918 962 C
ATOM 1687 CG ARG A1040 168.323 0.313 153.286 1.00 75.65 C
ANISOU 1687 CG ARG A1040 8453 10661 9629 483 1067 977 C
ATOM 1688 CD ARG A1040 166.833 0.081 153.150 1.00 85.81 C
ANISOU 1688 CD ARG A1040 9627 11923 11052 480 1183 1117 C
ATOM 1689 NE ARG A1040 166.214 1.055 152.253 1.00 91.79 N
ANISOU 1689 NE ARG A1040 10361 12531 11983 481 1178 981 N
ATOM 1690 CZ ARG A1040 165.831 0.805 151.005 1.00 99.30 C
ANISOU 1690 CZ ARG A1040 11276 13294 13161 408 1103 1035 C
ATOM 1691 NH1 ARG A1040 165.290 1.761 150.270 1.00 88.78 N
ANISOU 1691 NH1 ARG A1040 9915 11861 11957 430 1099 936 N
ATOM 1692 NH2 ARG A1040 165.982 -0.408 150.486 1.00 77.01 N
ANISOU 1692 NH2 ARG A1040 8438 10385 10437 319 1031 1187 N
ATOM 1693 N PHE A1041 170.801 -1.691 154.124 1.00 67.92 N
ANISOU 1693 N PHE A1041 7559 9838 8412 478 884 1219 N
ATOM 1694 CA PHE A1041 170.938 -2.907 154.908 1.00 69.31 C
ANISOU 1694 CA PHE A1041 7701 10134 8498 511 913 1496 C
ATOM 1695 C PHE A1041 169.530 -3.406 155.227 1.00 74.18 C
ANISOU 1695 C PHE A1041 8229 10771 9184 505 1066 1710 C
ATOM 1696 O PHE A1041 168.883 -2.908 156.153 1.00 75.15 O
ANISOU 1696 O PHE A1041 8314 11119 9119 571 1191 1704 O
ATOM 1697 CB PHE A1041 171.782 -2.643 156.173 1.00 72.95 C
ANISOU 1697 CB PHE A1041 8184 10914 8620 602 896 1456 C
ATOM 1698 CG PHE A1041 173.289 -2.650 156.008 1.00 74.02 C
ANISOU 1698 CG PHE A1041 8367 11055 8702 603 735 1356 C
ATOM 1699 CD1 PHE A1041 173.888 -2.117 154.869 1.00 75.11 C
ANISOU 1699 CD1 PHE A1041 8547 10972 9018 534 632 1151 C
ATOM 1700 CD2 PHE A1041 174.111 -3.133 157.017 1.00 78.14 C
ANISOU 1700 CD2 PHE A1041 8875 11833 8980 681 690 1475 C
ATOM 1701 CE1 PHE A1041 175.279 -2.116 154.726 1.00 75.59 C
ANISOU 1701 CE1 PHE A1041 8628 11054 9039 533 497 1064 C
ATOM 1702 CE2 PHE A1041 175.501 -3.112 156.880 1.00 80.54 C
ANISOU 1702 CE2 PHE A1041 9196 12163 9242 687 537 1379 C
ATOM 1703 CZ PHE A1041 176.075 -2.601 155.739 1.00 76.35 C
ANISOU 1703 CZ PHE A1041 8699 11399 8910 608 447 1169 C
ATOM 1704 N ASP A1042 169.030 -4.338 154.396 1.00 70.22 N
ANISOU 1704 N ASP A1042 7683 10028 8968 421 1058 1871 N
ATOM 1705 CA ASP A1042 167.682 -4.896 154.507 1.00 71.32 C
ANISOU 1705 CA ASP A1042 7712 10137 9248 381 1189 2078 C
ATOM 1706 C ASP A1042 167.638 -6.395 154.184 1.00 75.90 C
ANISOU 1706 C ASP A1042 8249 10518 10072 306 1172 2343 C
ATOM 1707 O ASP A1042 168.482 -6.900 153.437 1.00 74.30 O
ANISOU 1707 O ASP A1042 8103 10123 10003 272 1044 2299 O
ATOM 1708 CB ASP A1042 166.701 -4.137 153.589 1.00 71.99 C
ANISOU 1708 CB ASP A1042 7751 10093 9507 329 1201 1915 C
ATOM 1709 CG ASP A1042 167.195 -3.861 152.177 1.00 80.56 C
ANISOU 1709 CG ASP A1042 8897 10944 10766 265 1046 1722 C
ATOM 1710 OD1 ASP A1042 167.820 -4.763 151.573 1.00 80.65 O
ANISOU 1710 OD1 ASP A1042 8939 10793 10911 209 949 1777 O
ATOM 1711 OD2 ASP A1042 166.897 -2.775 151.651 1.00 86.12 O
ANISOU 1711 OD2 ASP A1042 9610 11626 11487 275 1033 1529 O
ATOM 1712 N ARG A1043 166.636 -7.093 154.749 1.00 74.66 N
ANISOU 1712 N ARG A1043 7980 10399 9990 281 1312 2614 N
ATOM 1713 CA ARG A1043 166.414 -8.521 154.545 1.00 75.63 C
ANISOU 1713 CA ARG A1043 8039 10305 10394 197 1324 2885 C
ATOM 1714 C ARG A1043 165.341 -8.745 153.469 1.00 78.82 C
ANISOU 1714 C ARG A1043 8348 10465 11134 57 1314 2832 C
ATOM 1715 O ARG A1043 164.142 -8.719 153.767 1.00 80.16 O
ANISOU 1715 O ARG A1043 8390 10702 11366 18 1443 2949 O
ATOM 1716 CB ARG A1043 166.023 -9.214 155.867 1.00 79.09 C
ANISOU 1716 CB ARG A1043 8395 10933 10723 244 1491 3258 C
ATOM 1717 CG ARG A1043 167.192 -9.483 156.802 1.00 90.49 C
ANISOU 1717 CG ARG A1043 9912 12568 11901 368 1465 3395 C
ATOM 1718 CD ARG A1043 166.832 -10.501 157.869 1.00101.80 C
ANISOU 1718 CD ARG A1043 11253 14111 13315 396 1616 3845 C
ATOM 1719 NE ARG A1043 167.958 -10.792 158.760 1.00110.15 N
ANISOU 1719 NE ARG A1043 12369 15379 14103 530 1577 4006 N
ATOM 1720 CZ ARG A1043 168.854 -11.756 158.558 1.00123.38 C
ANISOU 1720 CZ ARG A1043 14077 16858 15943 546 1482 4166 C
ATOM 1721 NH1 ARG A1043 168.773 -12.534 157.485 1.00108.46 N
ANISOU 1721 NH1 ARG A1043 12180 14540 14488 433 1421 4154 N
ATOM 1722 NH2 ARG A1043 169.839 -11.945 159.425 1.00111.55 N
ANISOU 1722 NH2 ARG A1043 12611 15599 14174 685 1444 4325 N
ATOM 1723 N GLY A1044 165.787 -8.937 152.229 1.00 73.07 N
ANISOU 1723 N GLY A1044 7674 9488 10603 -12 1160 2646 N
ATOM 1724 CA GLY A1044 164.906 -9.214 151.100 1.00 72.47 C
ANISOU 1724 CA GLY A1044 7510 9195 10828 -147 1111 2561 C
ATOM 1725 C GLY A1044 164.818 -8.187 149.987 1.00 74.28 C
ANISOU 1725 C GLY A1044 7773 9410 11041 -159 1001 2254 C
ATOM 1726 O GLY A1044 163.942 -8.316 149.130 1.00 73.99 O
ANISOU 1726 O GLY A1044 7640 9261 11213 -261 961 2194 O
ATOM 1727 N GLN A1045 165.715 -7.179 149.960 1.00 69.58 N
ANISOU 1727 N GLN A1045 7299 8927 10212 -63 945 2068 N
ATOM 1728 CA GLN A1045 165.687 -6.155 148.910 1.00 67.88 C
ANISOU 1728 CA GLN A1045 7115 8692 9985 -66 852 1817 C
ATOM 1729 C GLN A1045 167.028 -5.999 148.182 1.00 70.53 C
ANISOU 1729 C GLN A1045 7580 8952 10266 -46 719 1643 C
ATOM 1730 O GLN A1045 167.120 -6.380 147.018 1.00 69.59 O
ANISOU 1730 O GLN A1045 7462 8680 10297 -114 614 1543 O
ATOM 1731 CB GLN A1045 165.256 -4.795 149.467 1.00 69.27 C
ANISOU 1731 CB GLN A1045 7283 9064 9973 24 937 1740 C
ATOM 1732 CG GLN A1045 163.763 -4.604 149.652 1.00 87.57 C
ANISOU 1732 CG GLN A1045 9446 11444 12380 6 1046 1826 C
ATOM 1733 CD GLN A1045 163.500 -3.302 150.363 1.00106.88 C
ANISOU 1733 CD GLN A1045 11899 14080 14631 126 1148 1736 C
ATOM 1734 OE1 GLN A1045 163.785 -2.213 149.847 1.00102.48 O
ANISOU 1734 OE1 GLN A1045 11403 13508 14028 175 1092 1541 O
ATOM 1735 NE2 GLN A1045 163.005 -3.389 151.587 1.00 98.17 N
ANISOU 1735 NE2 GLN A1045 10733 13158 13409 181 1308 1875 N
ATOM 1736 N LYS A1046 168.044 -5.397 148.836 1.00 66.79 N
ANISOU 1736 N LYS A1046 7202 8606 9571 47 722 1590 N
ATOM 1737 CA LYS A1046 169.350 -5.148 148.214 1.00 65.25 C
ANISOU 1737 CA LYS A1046 7107 8364 9319 66 609 1432 C
ATOM 1738 C LYS A1046 170.350 -6.289 148.481 1.00 70.48 C
ANISOU 1738 C LYS A1046 7805 8962 10011 83 571 1534 C
ATOM 1739 O LYS A1046 171.459 -6.273 147.943 1.00 69.41 O
ANISOU 1739 O LYS A1046 7733 8784 9857 101 483 1420 O
ATOM 1740 CB LYS A1046 169.927 -3.781 148.644 1.00 66.65 C
ANISOU 1740 CB LYS A1046 7348 8694 9282 139 616 1286 C
ATOM 1741 CG LYS A1046 169.086 -2.566 148.203 1.00 72.90 C
ANISOU 1741 CG LYS A1046 8113 9498 10088 140 645 1168 C
ATOM 1742 CD LYS A1046 168.887 -2.460 146.679 1.00 76.56 C
ANISOU 1742 CD LYS A1046 8564 9820 10703 78 554 1084 C
ATOM 1743 CE LYS A1046 167.582 -1.783 146.330 1.00 81.28 C
ANISOU 1743 CE LYS A1046 9078 10426 11378 76 595 1082 C
ATOM 1744 NZ LYS A1046 167.001 -2.308 145.065 1.00 85.23 N
ANISOU 1744 NZ LYS A1046 9515 10828 12040 -1 511 1085 N
ATOM 1745 N GLY A1047 169.918 -7.281 149.256 1.00 69.15 N
ANISOU 1745 N GLY A1047 7583 8778 9913 80 644 1764 N
ATOM 1746 CA GLY A1047 170.671 -8.489 149.565 1.00 70.06 C
ANISOU 1746 CA GLY A1047 7711 8799 10111 105 626 1921 C
ATOM 1747 C GLY A1047 172.007 -8.347 150.262 1.00 73.64 C
ANISOU 1747 C GLY A1047 8227 9396 10357 213 589 1935 C
ATOM 1748 O GLY A1047 172.940 -9.075 149.922 1.00 73.05 O
ANISOU 1748 O GLY A1047 8177 9201 10376 240 519 1945 O
ATOM 1749 N VAL A1048 172.102 -7.468 151.281 1.00 70.76 N
ANISOU 1749 N VAL A1048 7874 9297 9716 282 634 1933 N
ATOM 1750 CA VAL A1048 173.338 -7.315 152.063 1.00 71.10 C
ANISOU 1750 CA VAL A1048 7955 9526 9536 380 585 1943 C
ATOM 1751 C VAL A1048 173.582 -8.627 152.840 1.00 77.52 C
ANISOU 1751 C VAL A1048 8729 10334 10389 440 616 2262 C
ATOM 1752 O VAL A1048 174.729 -9.055 152.955 1.00 77.93 O
ANISOU 1752 O VAL A1048 8797 10399 10414 510 538 2301 O
ATOM 1753 CB VAL A1048 173.344 -6.054 152.978 1.00 75.22 C
ANISOU 1753 CB VAL A1048 8492 10341 9748 431 618 1822 C
ATOM 1754 CG1 VAL A1048 172.342 -6.165 154.125 1.00 77.05 C
ANISOU 1754 CG1 VAL A1048 8669 10759 9846 467 757 2015 C
ATOM 1755 CG2 VAL A1048 174.748 -5.749 153.501 1.00 75.29 C
ANISOU 1755 CG2 VAL A1048 8530 10530 9548 505 522 1743 C
ATOM 1756 N ASP A1049 172.486 -9.287 153.289 1.00 75.38 N
ANISOU 1756 N ASP A1049 8396 10026 10219 410 733 2503 N
ATOM 1757 CA ASP A1049 172.472 -10.564 154.006 1.00 77.46 C
ANISOU 1757 CA ASP A1049 8608 10246 10576 452 794 2864 C
ATOM 1758 C ASP A1049 173.147 -11.668 153.182 1.00 80.46 C
ANISOU 1758 C ASP A1049 9000 10304 11268 442 713 2896 C
ATOM 1759 O ASP A1049 173.900 -12.458 153.747 1.00 81.62 O
ANISOU 1759 O ASP A1049 9135 10456 11420 538 700 3120 O
ATOM 1760 CB ASP A1049 171.030 -10.968 154.379 1.00 80.94 C
ANISOU 1760 CB ASP A1049 8963 10656 11135 382 944 3083 C
ATOM 1761 CG ASP A1049 170.028 -10.971 153.234 1.00 90.34 C
ANISOU 1761 CG ASP A1049 10119 11590 12618 237 946 2931 C
ATOM 1762 OD1 ASP A1049 169.855 -9.911 152.589 1.00 88.52 O
ANISOU 1762 OD1 ASP A1049 9921 11401 12312 207 898 2640 O
ATOM 1763 OD2 ASP A1049 169.371 -12.013 153.026 1.00 98.52 O
ANISOU 1763 OD2 ASP A1049 11082 12393 13958 154 997 3115 O
ATOM 1764 N VAL A1050 172.914 -11.681 151.846 1.00 74.74 N
ANISOU 1764 N VAL A1050 8293 9321 10784 341 656 2661 N
ATOM 1765 CA VAL A1050 173.493 -12.628 150.882 1.00 74.20 C
ANISOU 1765 CA VAL A1050 8238 8942 11013 326 582 2600 C
ATOM 1766 C VAL A1050 175.020 -12.470 150.886 1.00 77.15 C
ANISOU 1766 C VAL A1050 8659 9406 11246 446 484 2515 C
ATOM 1767 O VAL A1050 175.736 -13.469 150.972 1.00 78.40 O
ANISOU 1767 O VAL A1050 8805 9424 11560 523 463 2659 O
ATOM 1768 CB VAL A1050 172.905 -12.445 149.452 1.00 76.44 C
ANISOU 1768 CB VAL A1050 8529 9025 11490 198 533 2315 C
ATOM 1769 CG1 VAL A1050 173.397 -13.533 148.502 1.00 76.90 C
ANISOU 1769 CG1 VAL A1050 8594 8766 11860 184 471 2235 C
ATOM 1770 CG2 VAL A1050 171.382 -12.415 149.475 1.00 76.81 C
ANISOU 1770 CG2 VAL A1050 8503 9037 11643 79 615 2380 C
ATOM 1771 N LEU A1051 175.501 -11.211 150.827 1.00 71.08 N
ANISOU 1771 N LEU A1051 7932 8868 10208 462 430 2291 N
ATOM 1772 CA LEU A1051 176.918 -10.854 150.842 1.00 69.89 C
ANISOU 1772 CA LEU A1051 7804 8846 9907 553 336 2183 C
ATOM 1773 C LEU A1051 177.555 -11.179 152.200 1.00 74.77 C
ANISOU 1773 C LEU A1051 8387 9686 10338 682 338 2443 C
ATOM 1774 O LEU A1051 178.665 -11.714 152.231 1.00 75.44 O
ANISOU 1774 O LEU A1051 8451 9755 10457 780 270 2500 O
ATOM 1775 CB LEU A1051 177.092 -9.361 150.502 1.00 67.86 C
ANISOU 1775 CB LEU A1051 7585 8760 9440 509 295 1895 C
ATOM 1776 CG LEU A1051 178.489 -8.769 150.693 1.00 72.24 C
ANISOU 1776 CG LEU A1051 8140 9498 9811 579 204 1778 C
ATOM 1777 CD1 LEU A1051 179.390 -9.068 149.516 1.00 71.53 C
ANISOU 1777 CD1 LEU A1051 8052 9240 9886 582 137 1629 C
ATOM 1778 CD2 LEU A1051 178.416 -7.301 150.947 1.00 73.48 C
ANISOU 1778 CD2 LEU A1051 8320 9861 9739 538 196 1582 C
ATOM 1779 N LEU A1052 176.854 -10.863 153.310 1.00 71.23 N
ANISOU 1779 N LEU A1052 7920 9464 9680 693 415 2601 N
ATOM 1780 CA LEU A1052 177.334 -11.121 154.671 1.00 72.78 C
ANISOU 1780 CA LEU A1052 8076 9939 9637 819 421 2864 C
ATOM 1781 C LEU A1052 177.470 -12.628 154.916 1.00 77.82 C
ANISOU 1781 C LEU A1052 8668 10387 10512 893 453 3226 C
ATOM 1782 O LEU A1052 178.437 -13.046 155.553 1.00 78.65 O
ANISOU 1782 O LEU A1052 8738 10630 10516 1027 395 3403 O
ATOM 1783 CB LEU A1052 176.428 -10.457 155.725 1.00 73.62 C
ANISOU 1783 CB LEU A1052 8172 10341 9460 814 519 2934 C
ATOM 1784 CG LEU A1052 176.414 -8.916 155.727 1.00 76.31 C
ANISOU 1784 CG LEU A1052 8553 10895 9548 774 489 2585 C
ATOM 1785 CD1 LEU A1052 175.326 -8.376 156.625 1.00 77.50 C
ANISOU 1785 CD1 LEU A1052 8687 11275 9484 771 615 2637 C
ATOM 1786 CD2 LEU A1052 177.766 -8.334 156.105 1.00 78.51 C
ANISOU 1786 CD2 LEU A1052 8830 11414 9585 847 357 2436 C
ATOM 1787 N LYS A1053 176.539 -13.437 154.355 1.00 74.40 N
ANISOU 1787 N LYS A1053 8226 9622 10422 804 535 3324 N
ATOM 1788 CA LYS A1053 176.576 -14.902 154.414 1.00 76.44 C
ANISOU 1788 CA LYS A1053 8442 9597 11006 848 576 3639 C
ATOM 1789 C LYS A1053 177.723 -15.421 153.546 1.00 79.24 C
ANISOU 1789 C LYS A1053 8810 9721 11575 912 470 3499 C
ATOM 1790 O LYS A1053 178.414 -16.349 153.959 1.00 81.03 O
ANISOU 1790 O LYS A1053 8997 9874 11919 1041 459 3759 O
ATOM 1791 CB LYS A1053 175.245 -15.520 153.950 1.00 79.60 C
ANISOU 1791 CB LYS A1053 8816 9686 11742 703 681 3710 C
ATOM 1792 CG LYS A1053 174.147 -15.579 155.008 1.00 97.95 C
ANISOU 1792 CG LYS A1053 11080 12174 13961 674 827 4023 C
ATOM 1793 CD LYS A1053 172.825 -16.154 154.461 1.00107.78 C
ANISOU 1793 CD LYS A1053 12275 13105 15574 506 923 4067 C
ATOM 1794 CE LYS A1053 171.922 -15.126 153.807 1.00112.10 C
ANISOU 1794 CE LYS A1053 12832 13712 16048 374 923 3742 C
ATOM 1795 NZ LYS A1053 170.789 -15.755 153.078 1.00118.94 N
ANISOU 1795 NZ LYS A1053 13632 14252 17307 206 973 3733 N
ATOM 1796 N ALA A1054 177.932 -14.803 152.353 1.00 72.66 N
ANISOU 1796 N ALA A1054 8026 8795 10785 834 400 3101 N
ATOM 1797 CA ALA A1054 178.987 -15.146 151.391 1.00 71.61 C
ANISOU 1797 CA ALA A1054 7904 8479 10825 888 314 2907 C
ATOM 1798 C ALA A1054 180.381 -14.885 151.963 1.00 75.45 C
ANISOU 1798 C ALA A1054 8357 9225 11083 1043 227 2948 C
ATOM 1799 O ALA A1054 181.259 -15.726 151.782 1.00 76.59 O
ANISOU 1799 O ALA A1054 8466 9222 11415 1160 192 3028 O
ATOM 1800 CB ALA A1054 178.802 -14.372 150.096 1.00 69.59 C
ANISOU 1800 CB ALA A1054 7699 8158 10584 768 275 2504 C
ATOM 1801 N ILE A1055 180.580 -13.747 152.678 1.00 70.59 N
ANISOU 1801 N ILE A1055 7743 8994 10082 1047 190 2889 N
ATOM 1802 CA ILE A1055 181.854 -13.401 153.333 1.00 70.74 C
ANISOU 1802 CA ILE A1055 7711 9314 9852 1175 90 2913 C
ATOM 1803 C ILE A1055 182.156 -14.472 154.405 1.00 77.55 C
ANISOU 1803 C ILE A1055 8504 10231 10730 1335 102 3344 C
ATOM 1804 O ILE A1055 183.305 -14.897 154.523 1.00 78.45 O
ANISOU 1804 O ILE A1055 8553 10388 10867 1475 22 3425 O
ATOM 1805 CB ILE A1055 181.844 -11.947 153.903 1.00 72.49 C
ANISOU 1805 CB ILE A1055 7947 9915 9680 1122 51 2727 C
ATOM 1806 CG1 ILE A1055 181.851 -10.909 152.754 1.00 69.93 C
ANISOU 1806 CG1 ILE A1055 7675 9514 9381 992 25 2328 C
ATOM 1807 CG2 ILE A1055 183.024 -11.694 154.865 1.00 74.54 C
ANISOU 1807 CG2 ILE A1055 8130 10537 9656 1249 -58 2799 C
ATOM 1808 CD1 ILE A1055 181.318 -9.512 153.117 1.00 76.29 C
ANISOU 1808 CD1 ILE A1055 8518 10551 9919 899 36 2134 C
ATOM 1809 N GLU A1056 181.112 -14.942 155.129 1.00 75.36 N
ANISOU 1809 N GLU A1056 8228 9939 10465 1317 211 3640 N
ATOM 1810 CA GLU A1056 181.217 -15.996 156.143 1.00 78.48 C
ANISOU 1810 CA GLU A1056 8557 10367 10895 1460 251 4113 C
ATOM 1811 C GLU A1056 181.589 -17.343 155.500 1.00 83.64 C
ANISOU 1811 C GLU A1056 9186 10576 12020 1532 263 4256 C
ATOM 1812 O GLU A1056 182.341 -18.105 156.108 1.00 86.25 O
ANISOU 1812 O GLU A1056 9444 10939 12388 1708 234 4571 O
ATOM 1813 CB GLU A1056 179.919 -16.125 156.956 1.00 81.19 C
ANISOU 1813 CB GLU A1056 8902 10786 11160 1400 391 4386 C
ATOM 1814 CG GLU A1056 179.734 -15.021 157.986 1.00 91.10 C
ANISOU 1814 CG GLU A1056 10156 12552 11907 1407 386 4350 C
ATOM 1815 CD GLU A1056 178.660 -15.246 159.035 1.00113.57 C
ANISOU 1815 CD GLU A1056 12974 15571 14609 1405 534 4696 C
ATOM 1816 OE1 GLU A1056 177.597 -15.819 158.702 1.00107.15 O
ANISOU 1816 OE1 GLU A1056 12162 14455 14096 1301 663 4822 O
ATOM 1817 OE2 GLU A1056 178.871 -14.812 160.190 1.00110.02 O
ANISOU 1817 OE2 GLU A1056 12489 15583 13729 1501 521 4823 O
ATOM 1818 N ILE A1057 181.082 -17.623 154.272 1.00 78.36 N
ANISOU 1818 N ILE A1057 8568 9502 11703 1406 301 4015 N
ATOM 1819 CA ILE A1057 181.398 -18.840 153.504 1.00 79.55 C
ANISOU 1819 CA ILE A1057 8703 9195 12326 1459 315 4047 C
ATOM 1820 C ILE A1057 182.882 -18.775 153.099 1.00 83.75 C
ANISOU 1820 C ILE A1057 9200 9790 12833 1605 201 3883 C
ATOM 1821 O ILE A1057 183.611 -19.757 153.262 1.00 85.99 O
ANISOU 1821 O ILE A1057 9420 9912 13341 1773 191 4105 O
ATOM 1822 CB ILE A1057 180.459 -19.025 152.257 1.00 81.06 C
ANISOU 1822 CB ILE A1057 8955 9002 12844 1272 366 3756 C
ATOM 1823 CG1 ILE A1057 178.944 -19.094 152.628 1.00 81.97 C
ANISOU 1823 CG1 ILE A1057 9075 9057 13013 1116 479 3917 C
ATOM 1824 CG2 ILE A1057 180.866 -20.220 151.375 1.00 83.20 C
ANISOU 1824 CG2 ILE A1057 9213 8805 13595 1327 370 3695 C
ATOM 1825 CD1 ILE A1057 178.459 -20.197 153.636 1.00 94.99 C
ANISOU 1825 CD1 ILE A1057 10660 10571 14863 1167 590 4440 C
ATOM 1826 N LEU A1058 183.319 -17.598 152.609 1.00 77.93 N
ANISOU 1826 N LEU A1058 8489 9292 11831 1544 123 3516 N
ATOM 1827 CA LEU A1058 184.685 -17.327 152.158 1.00 77.48 C
ANISOU 1827 CA LEU A1058 8381 9339 11718 1648 22 3319 C
ATOM 1828 C LEU A1058 185.692 -17.283 153.316 1.00 84.00 C
ANISOU 1828 C LEU A1058 9106 10521 12292 1826 -64 3578 C
ATOM 1829 O LEU A1058 186.852 -17.617 153.094 1.00 84.57 O
ANISOU 1829 O LEU A1058 9096 10588 12451 1970 -131 3565 O
ATOM 1830 CB LEU A1058 184.749 -16.002 151.376 1.00 74.15 C
ANISOU 1830 CB LEU A1058 8008 9080 11085 1507 -22 2892 C
ATOM 1831 CG LEU A1058 183.980 -15.922 150.052 1.00 76.74 C
ANISOU 1831 CG LEU A1058 8419 9122 11617 1350 32 2589 C
ATOM 1832 CD1 LEU A1058 183.606 -14.494 149.735 1.00 74.01 C
ANISOU 1832 CD1 LEU A1058 8127 8996 10998 1198 13 2315 C
ATOM 1833 CD2 LEU A1058 184.768 -16.517 148.914 1.00 79.33 C
ANISOU 1833 CD2 LEU A1058 8726 9209 12208 1418 20 2389 C
ATOM 1834 N SER A1059 185.253 -16.890 154.539 1.00 82.09 N
ANISOU 1834 N SER A1059 8856 10605 11730 1824 -63 3809 N
ATOM 1835 CA SER A1059 186.076 -16.767 155.756 1.00 84.39 C
ANISOU 1835 CA SER A1059 9047 11314 11704 1981 -157 4056 C
ATOM 1836 C SER A1059 186.981 -17.980 155.994 1.00 92.49 C
ANISOU 1836 C SER A1059 9966 12214 12962 2210 -189 4385 C
ATOM 1837 O SER A1059 188.165 -17.801 156.287 1.00 93.28 O
ANISOU 1837 O SER A1059 9957 12577 12909 2344 -312 4388 O
ATOM 1838 CB SER A1059 185.197 -16.556 156.985 1.00 89.22 C
ANISOU 1838 CB SER A1059 9675 12208 12017 1960 -104 4325 C
ATOM 1839 OG SER A1059 184.512 -15.316 156.937 1.00 96.13 O
ANISOU 1839 OG SER A1059 10626 13269 12629 1785 -89 4019 O
ATOM 1840 N SER A1060 186.424 -19.202 155.857 1.00 91.39 N
ANISOU 1840 N SER A1060 9846 11662 13217 2252 -78 4656 N
ATOM 1841 CA SER A1060 187.133 -20.471 156.044 1.00 94.87 C
ANISOU 1841 CA SER A1060 10192 11887 13967 2476 -80 5001 C
ATOM 1842 C SER A1060 188.156 -20.742 154.927 1.00 98.51 C
ANISOU 1842 C SER A1060 10612 12107 14712 2557 -128 4714 C
ATOM 1843 O SER A1060 189.176 -21.386 155.190 1.00100.90 O
ANISOU 1843 O SER A1060 10794 12416 15125 2781 -185 4925 O
ATOM 1844 CB SER A1060 186.141 -21.628 156.129 1.00100.69 C
ANISOU 1844 CB SER A1060 10967 12193 15096 2461 67 5330 C
ATOM 1845 OG SER A1060 185.254 -21.647 155.022 1.00107.45 O
ANISOU 1845 OG SER A1060 11930 12660 16238 2260 153 5004 O
ATOM 1846 N LYS A1061 187.887 -20.255 153.694 1.00 91.81 N
ANISOU 1846 N LYS A1061 9850 11068 13968 2389 -101 4248 N
ATOM 1847 CA LYS A1061 188.757 -20.442 152.526 1.00 91.03 C
ANISOU 1847 CA LYS A1061 9718 10761 14107 2448 -122 3932 C
ATOM 1848 C LYS A1061 190.060 -19.636 152.641 1.00 94.75 C
ANISOU 1848 C LYS A1061 10075 11642 14283 2533 -252 3791 C
ATOM 1849 O LYS A1061 190.068 -18.547 153.221 1.00 92.81 O
ANISOU 1849 O LYS A1061 9826 11811 13629 2443 -326 3730 O
ATOM 1850 CB LYS A1061 188.027 -20.065 151.224 1.00 90.38 C
ANISOU 1850 CB LYS A1061 9757 10435 14147 2237 -58 3495 C
ATOM 1851 CG LYS A1061 186.937 -21.046 150.813 1.00104.87 C
ANISOU 1851 CG LYS A1061 11673 11790 16384 2162 57 3552 C
ATOM 1852 CD LYS A1061 187.132 -21.522 149.384 1.00115.37 C
ANISOU 1852 CD LYS A1061 13030 12753 18054 2152 93 3185 C
ATOM 1853 CE LYS A1061 186.080 -22.522 148.976 1.00128.52 C
ANISOU 1853 CE LYS A1061 14759 13931 20142 2066 190 3205 C
ATOM 1854 NZ LYS A1061 186.343 -23.075 147.622 1.00138.06 N
ANISOU 1854 NZ LYS A1061 15985 14794 21677 2080 218 2824 N
ATOM 1855 N LYS A1062 191.154 -20.179 152.070 1.00 92.95 N
ANISOU 1855 N LYS A1062 9744 11286 14286 2703 -274 3723 N
ATOM 1856 CA LYS A1062 192.482 -19.555 152.053 1.00 92.78 C
ANISOU 1856 CA LYS A1062 9578 11610 14063 2793 -388 3589 C
ATOM 1857 C LYS A1062 192.542 -18.403 151.039 1.00 93.23 C
ANISOU 1857 C LYS A1062 9685 11768 13971 2595 -389 3109 C
ATOM 1858 O LYS A1062 193.390 -17.516 151.163 1.00 92.24 O
ANISOU 1858 O LYS A1062 9457 11998 13591 2582 -486 2977 O
ATOM 1859 CB LYS A1062 193.561 -20.600 151.732 1.00 98.17 C
ANISOU 1859 CB LYS A1062 10122 12093 15086 3054 -386 3688 C
ATOM 1860 N GLU A1063 191.636 -18.424 150.044 1.00 87.91 N
ANISOU 1860 N GLU A1063 9156 10784 13462 2440 -285 2864 N
ATOM 1861 CA GLU A1063 191.503 -17.428 148.976 1.00 84.63 C
ANISOU 1861 CA GLU A1063 8805 10415 12935 2253 -265 2446 C
ATOM 1862 C GLU A1063 190.993 -16.072 149.498 1.00 85.94 C
ANISOU 1862 C GLU A1063 9026 10911 12714 2060 -316 2374 C
ATOM 1863 O GLU A1063 191.211 -15.050 148.845 1.00 83.43 O
ANISOU 1863 O GLU A1063 8715 10731 12252 1932 -328 2082 O
ATOM 1864 CB GLU A1063 190.542 -17.949 147.896 1.00 85.14 C
ANISOU 1864 CB GLU A1063 9004 10072 13274 2155 -152 2255 C
ATOM 1865 CG GLU A1063 191.131 -18.997 146.964 1.00 97.00 C
ANISOU 1865 CG GLU A1063 10461 11254 15142 2307 -92 2134 C
ATOM 1866 CD GLU A1063 191.188 -20.419 147.488 1.00120.85 C
ANISOU 1866 CD GLU A1063 13441 13964 18513 2502 -61 2446 C
ATOM 1867 OE1 GLU A1063 192.154 -21.135 147.139 1.00119.51 O
ANISOU 1867 OE1 GLU A1063 13167 13666 18576 2705 -46 2427 O
ATOM 1868 OE2 GLU A1063 190.268 -20.825 148.235 1.00115.29 O
ANISOU 1868 OE2 GLU A1063 12801 13136 17868 2458 -40 2718 O
ATOM 1869 N PHE A1064 190.301 -16.076 150.658 1.00 82.87 N
ANISOU 1869 N PHE A1064 8676 10641 12172 2044 -334 2643 N
ATOM 1870 CA PHE A1064 189.719 -14.908 151.332 1.00 80.92 C
ANISOU 1870 CA PHE A1064 8482 10696 11569 1889 -370 2598 C
ATOM 1871 C PHE A1064 190.776 -13.891 151.772 1.00 83.93 C
ANISOU 1871 C PHE A1064 8746 11489 11654 1891 -495 2486 C
ATOM 1872 O PHE A1064 190.478 -12.700 151.844 1.00 81.94 O
ANISOU 1872 O PHE A1064 8539 11427 11168 1729 -518 2284 O
ATOM 1873 CB PHE A1064 188.922 -15.378 152.559 1.00 84.62 C
ANISOU 1873 CB PHE A1064 8981 11221 11949 1929 -350 2959 C
ATOM 1874 CG PHE A1064 188.203 -14.325 153.372 1.00 85.37 C
ANISOU 1874 CG PHE A1064 9132 11621 11682 1798 -366 2934 C
ATOM 1875 CD1 PHE A1064 187.092 -13.662 152.859 1.00 86.07 C
ANISOU 1875 CD1 PHE A1064 9346 11602 11755 1607 -289 2725 C
ATOM 1876 CD2 PHE A1064 188.591 -14.046 154.676 1.00 89.70 C
ANISOU 1876 CD2 PHE A1064 9601 12572 11908 1880 -455 3126 C
ATOM 1877 CE1 PHE A1064 186.410 -12.710 153.623 1.00 86.38 C
ANISOU 1877 CE1 PHE A1064 9431 11906 11483 1506 -289 2694 C
ATOM 1878 CE2 PHE A1064 187.906 -13.097 155.441 1.00 91.94 C
ANISOU 1878 CE2 PHE A1064 9938 13141 11856 1771 -458 3071 C
ATOM 1879 CZ PHE A1064 186.824 -12.431 154.907 1.00 87.46 C
ANISOU 1879 CZ PHE A1064 9496 12435 11301 1588 -368 2851 C
ATOM 1880 N GLN A1065 191.994 -14.361 152.069 1.00 81.93 N
ANISOU 1880 N GLN A1065 8333 11363 11435 2072 -577 2612 N
ATOM 1881 CA GLN A1065 193.118 -13.542 152.528 1.00 82.03 C
ANISOU 1881 CA GLN A1065 8191 11773 11202 2086 -714 2525 C
ATOM 1882 C GLN A1065 193.607 -12.577 151.436 1.00 83.30 C
ANISOU 1882 C GLN A1065 8333 11940 11379 1941 -705 2143 C
ATOM 1883 O GLN A1065 194.157 -11.524 151.762 1.00 82.77 O
ANISOU 1883 O GLN A1065 8183 12179 11088 1850 -800 1994 O
ATOM 1884 CB GLN A1065 194.272 -14.439 153.015 1.00 86.46 C
ANISOU 1884 CB GLN A1065 8564 12437 11848 2336 -798 2783 C
ATOM 1885 CG GLN A1065 193.836 -15.583 153.945 1.00101.25 C
ANISOU 1885 CG GLN A1065 10450 14238 13781 2509 -782 3221 C
ATOM 1886 CD GLN A1065 193.085 -15.114 155.169 1.00120.11 C
ANISOU 1886 CD GLN A1065 12897 16921 15819 2444 -822 3382 C
ATOM 1887 OE1 GLN A1065 193.620 -14.403 156.027 1.00117.15 O
ANISOU 1887 OE1 GLN A1065 12421 16987 15103 2445 -958 3372 O
ATOM 1888 NE2 GLN A1065 191.821 -15.502 155.271 1.00110.22 N
ANISOU 1888 NE2 GLN A1065 11798 15441 14641 2383 -701 3517 N
ATOM 1889 N GLU A1066 193.394 -12.933 150.153 1.00 77.99 N
ANISOU 1889 N GLU A1066 7729 10937 10967 1916 -590 1988 N
ATOM 1890 CA GLU A1066 193.766 -12.124 148.986 1.00 75.62 C
ANISOU 1890 CA GLU A1066 7418 10622 10693 1789 -552 1664 C
ATOM 1891 C GLU A1066 192.623 -11.162 148.600 1.00 76.21 C
ANISOU 1891 C GLU A1066 7662 10635 10659 1563 -493 1480 C
ATOM 1892 O GLU A1066 192.805 -10.309 147.727 1.00 74.12 O
ANISOU 1892 O GLU A1066 7399 10386 10377 1436 -462 1241 O
ATOM 1893 CB GLU A1066 194.128 -13.027 147.788 1.00 77.42 C
ANISOU 1893 CB GLU A1066 7627 10566 11222 1898 -455 1584 C
ATOM 1894 CG GLU A1066 195.255 -14.016 148.035 1.00 90.93 C
ANISOU 1894 CG GLU A1066 9164 12291 13095 2145 -492 1752 C
ATOM 1895 CD GLU A1066 194.893 -15.472 147.803 1.00113.95 C
ANISOU 1895 CD GLU A1066 12134 14836 16326 2310 -410 1898 C
ATOM 1896 OE1 GLU A1066 195.201 -16.307 148.684 1.00112.50 O
ANISOU 1896 OE1 GLU A1066 11871 14653 16221 2496 -459 2201 O
ATOM 1897 OE2 GLU A1066 194.307 -15.780 146.740 1.00105.27 O
ANISOU 1897 OE2 GLU A1066 11149 13447 15403 2255 -300 1711 O
ATOM 1898 N MET A1067 191.449 -11.313 149.255 1.00 72.15 N
ANISOU 1898 N MET A1067 7276 10057 10081 1522 -472 1615 N
ATOM 1899 CA MET A1067 190.236 -10.512 149.041 1.00 69.47 C
ANISOU 1899 CA MET A1067 7087 9657 9651 1337 -415 1486 C
ATOM 1900 C MET A1067 190.118 -9.372 150.044 1.00 72.73 C
ANISOU 1900 C MET A1067 7494 10369 9770 1242 -488 1452 C
ATOM 1901 O MET A1067 190.533 -9.510 151.193 1.00 74.13 O
ANISOU 1901 O MET A1067 7592 10784 9790 1331 -574 1612 O
ATOM 1902 CB MET A1067 188.973 -11.386 149.165 1.00 71.84 C
ANISOU 1902 CB MET A1067 7509 9708 10078 1349 -335 1651 C
ATOM 1903 CG MET A1067 188.830 -12.436 148.101 1.00 75.69 C
ANISOU 1903 CG MET A1067 8029 9855 10876 1403 -257 1620 C
ATOM 1904 SD MET A1067 187.509 -13.598 148.506 1.00 80.93 S
ANISOU 1904 SD MET A1067 8789 10230 11731 1421 -183 1865 S
ATOM 1905 CE MET A1067 187.750 -14.802 147.223 1.00 78.57 C
ANISOU 1905 CE MET A1067 8489 9547 11817 1503 -120 1750 C
ATOM 1906 N ARG A1068 189.502 -8.263 149.613 1.00 67.01 N
ANISOU 1906 N ARG A1068 6854 9632 8974 1069 -450 1243 N
ATOM 1907 CA ARG A1068 189.212 -7.080 150.427 1.00 66.41 C
ANISOU 1907 CA ARG A1068 6796 9778 8658 961 -496 1147 C
ATOM 1908 C ARG A1068 187.743 -6.723 150.230 1.00 69.04 C
ANISOU 1908 C ARG A1068 7282 9956 8992 856 -400 1109 C
ATOM 1909 O ARG A1068 187.255 -6.802 149.104 1.00 67.05 O
ANISOU 1909 O ARG A1068 7099 9471 8907 800 -322 1031 O
ATOM 1910 CB ARG A1068 190.130 -5.891 150.066 1.00 65.17 C
ANISOU 1910 CB ARG A1068 6552 9755 8455 852 -551 905 C
ATOM 1911 CG ARG A1068 191.639 -6.147 150.178 1.00 71.74 C
ANISOU 1911 CG ARG A1068 7198 10760 9301 940 -648 921 C
ATOM 1912 CD ARG A1068 192.142 -6.319 151.605 1.00 77.81 C
ANISOU 1912 CD ARG A1068 7864 11840 9861 1034 -779 1048 C
ATOM 1913 NE ARG A1068 193.570 -6.644 151.641 1.00 83.72 N
ANISOU 1913 NE ARG A1068 8412 12751 10648 1132 -877 1081 N
ATOM 1914 CZ ARG A1068 194.068 -7.872 151.521 1.00 98.49 C
ANISOU 1914 CZ ARG A1068 10210 14555 12656 1319 -875 1287 C
ATOM 1915 NH1 ARG A1068 195.378 -8.069 151.561 1.00 87.85 N
ANISOU 1915 NH1 ARG A1068 8659 13376 11343 1412 -965 1306 N
ATOM 1916 NH2 ARG A1068 193.261 -8.910 151.351 1.00 85.41 N
ANISOU 1916 NH2 ARG A1068 8671 12650 11129 1415 -782 1472 N
ATOM 1917 N PHE A1069 187.026 -6.373 151.309 1.00 66.52 N
ANISOU 1917 N PHE A1069 7007 9787 8480 841 -403 1165 N
ATOM 1918 CA PHE A1069 185.602 -6.053 151.218 1.00 65.07 C
ANISOU 1918 CA PHE A1069 6945 9479 8298 758 -305 1146 C
ATOM 1919 C PHE A1069 185.271 -4.717 151.863 1.00 69.12 C
ANISOU 1919 C PHE A1069 7482 10175 8607 667 -317 971 C
ATOM 1920 O PHE A1069 185.636 -4.482 153.012 1.00 70.40 O
ANISOU 1920 O PHE A1069 7593 10611 8546 709 -386 985 O
ATOM 1921 CB PHE A1069 184.752 -7.162 151.860 1.00 67.97 C
ANISOU 1921 CB PHE A1069 7348 9795 8683 845 -248 1425 C
ATOM 1922 CG PHE A1069 184.787 -8.485 151.134 1.00 69.73 C
ANISOU 1922 CG PHE A1069 7571 9748 9177 915 -212 1573 C
ATOM 1923 CD1 PHE A1069 185.732 -9.451 151.459 1.00 74.40 C
ANISOU 1923 CD1 PHE A1069 8075 10368 9825 1060 -265 1752 C
ATOM 1924 CD2 PHE A1069 183.855 -8.777 150.144 1.00 70.54 C
ANISOU 1924 CD2 PHE A1069 7749 9567 9486 841 -128 1526 C
ATOM 1925 CE1 PHE A1069 185.760 -10.676 150.790 1.00 75.84 C
ANISOU 1925 CE1 PHE A1069 8257 10264 10294 1132 -223 1863 C
ATOM 1926 CE2 PHE A1069 183.886 -10.004 149.473 1.00 73.88 C
ANISOU 1926 CE2 PHE A1069 8169 9728 10174 899 -100 1614 C
ATOM 1927 CZ PHE A1069 184.837 -10.945 149.802 1.00 73.78 C
ANISOU 1927 CZ PHE A1069 8080 9713 10240 1045 -141 1776 C
ATOM 1928 N ILE A1070 184.577 -3.844 151.118 1.00 64.38 N
ANISOU 1928 N ILE A1070 6953 9425 8082 550 -253 801 N
ATOM 1929 CA ILE A1070 184.112 -2.538 151.594 1.00 64.17 C
ANISOU 1929 CA ILE A1070 6961 9497 7925 466 -240 615 C
ATOM 1930 C ILE A1070 182.585 -2.558 151.501 1.00 67.60 C
ANISOU 1930 C ILE A1070 7488 9797 8398 447 -126 675 C
ATOM 1931 O ILE A1070 182.047 -2.584 150.397 1.00 65.65 O
ANISOU 1931 O ILE A1070 7286 9324 8333 396 -70 661 O
ATOM 1932 CB ILE A1070 184.761 -1.354 150.821 1.00 66.29 C
ANISOU 1932 CB ILE A1070 7205 9705 8279 350 -267 373 C
ATOM 1933 CG1 ILE A1070 186.291 -1.351 150.997 1.00 67.76 C
ANISOU 1933 CG1 ILE A1070 7265 10050 8431 361 -381 319 C
ATOM 1934 CG2 ILE A1070 184.158 -0.011 151.258 1.00 67.08 C
ANISOU 1934 CG2 ILE A1070 7347 9836 8304 267 -238 175 C
ATOM 1935 CD1 ILE A1070 187.040 -0.637 149.924 1.00 73.26 C
ANISOU 1935 CD1 ILE A1070 7913 10636 9286 260 -384 173 C
ATOM 1936 N ILE A1071 181.896 -2.598 152.652 1.00 65.96 N
ANISOU 1936 N ILE A1071 7296 9756 8009 494 -91 752 N
ATOM 1937 CA ILE A1071 180.431 -2.665 152.704 1.00 65.70 C
ANISOU 1937 CA ILE A1071 7324 9633 8006 485 27 831 C
ATOM 1938 C ILE A1071 179.885 -1.327 153.222 1.00 70.74 C
ANISOU 1938 C ILE A1071 7990 10373 8515 443 67 618 C
ATOM 1939 O ILE A1071 180.159 -0.949 154.361 1.00 72.19 O
ANISOU 1939 O ILE A1071 8149 10818 8461 482 37 549 O
ATOM 1940 CB ILE A1071 179.953 -3.882 153.551 1.00 70.29 C
ANISOU 1940 CB ILE A1071 7889 10302 8514 580 71 1129 C
ATOM 1941 CG1 ILE A1071 180.627 -5.188 153.090 1.00 70.95 C
ANISOU 1941 CG1 ILE A1071 7939 10256 8761 636 27 1324 C
ATOM 1942 CG2 ILE A1071 178.442 -4.034 153.504 1.00 70.68 C
ANISOU 1942 CG2 ILE A1071 7975 10244 8638 556 200 1227 C
ATOM 1943 CD1 ILE A1071 181.532 -5.787 154.086 1.00 80.72 C
ANISOU 1943 CD1 ILE A1071 9110 11723 9835 749 -46 1487 C
ATOM 1944 N ILE A1072 179.129 -0.606 152.369 1.00 66.30 N
ANISOU 1944 N ILE A1072 7471 9609 8111 371 130 506 N
ATOM 1945 CA ILE A1072 178.560 0.708 152.700 1.00 66.69 C
ANISOU 1945 CA ILE A1072 7546 9686 8107 340 182 296 C
ATOM 1946 C ILE A1072 177.025 0.644 152.719 1.00 70.89 C
ANISOU 1946 C ILE A1072 8102 10150 8682 361 309 388 C
ATOM 1947 O ILE A1072 176.416 0.010 151.853 1.00 69.39 O
ANISOU 1947 O ILE A1072 7917 9781 8667 341 342 531 O
ATOM 1948 CB ILE A1072 179.069 1.816 151.725 1.00 68.77 C
ANISOU 1948 CB ILE A1072 7818 9774 8537 246 149 88 C
ATOM 1949 CG1 ILE A1072 180.610 1.824 151.621 1.00 69.48 C
ANISOU 1949 CG1 ILE A1072 7856 9930 8614 212 30 14 C
ATOM 1950 CG2 ILE A1072 178.551 3.208 152.124 1.00 70.29 C
ANISOU 1950 CG2 ILE A1072 8033 9959 8716 222 203 -139 C
ATOM 1951 CD1 ILE A1072 181.115 1.899 150.233 1.00 75.65 C
ANISOU 1951 CD1 ILE A1072 8629 10508 9605 146 13 17 C
ATOM 1952 N GLY A1073 176.430 1.324 153.699 1.00 69.08 N
ANISOU 1952 N GLY A1073 7875 10077 8294 400 378 283 N
ATOM 1953 CA GLY A1073 174.985 1.417 153.852 1.00 69.07 C
ANISOU 1953 CA GLY A1073 7874 10050 8319 431 512 347 C
ATOM 1954 C GLY A1073 174.476 1.356 155.274 1.00 74.98 C
ANISOU 1954 C GLY A1073 8601 11087 8801 519 595 374 C
ATOM 1955 O GLY A1073 175.169 0.874 156.176 1.00 76.00 O
ANISOU 1955 O GLY A1073 8714 11460 8704 566 545 433 O
ATOM 1956 N LYS A1074 173.245 1.849 155.466 1.00 72.03 N
ANISOU 1956 N LYS A1074 8216 10708 8445 550 728 342 N
ATOM 1957 CA LYS A1074 172.529 1.873 156.741 1.00 74.28 C
ANISOU 1957 CA LYS A1074 8469 11273 8482 642 849 364 C
ATOM 1958 C LYS A1074 171.195 1.131 156.609 1.00 78.49 C
ANISOU 1958 C LYS A1074 8947 11757 9118 658 984 631 C
ATOM 1959 O LYS A1074 170.776 0.813 155.494 1.00 76.03 O
ANISOU 1959 O LYS A1074 8625 11183 9080 593 971 731 O
ATOM 1960 CB LYS A1074 172.297 3.322 157.203 1.00 78.09 C
ANISOU 1960 CB LYS A1074 8968 11811 8889 677 902 17 C
ATOM 1961 CG LYS A1074 173.503 3.939 157.894 1.00 95.06 C
ANISOU 1961 CG LYS A1074 11145 14141 10835 675 791 -251 C
ATOM 1962 CD LYS A1074 173.116 5.041 158.885 1.00108.01 C
ANISOU 1962 CD LYS A1074 12786 15966 12288 746 876 -568 C
ATOM 1963 CE LYS A1074 172.944 4.548 160.307 1.00119.15 C
ANISOU 1963 CE LYS A1074 14162 17817 13293 852 938 -502 C
ATOM 1964 NZ LYS A1074 174.247 4.239 160.955 1.00127.57 N
ANISOU 1964 NZ LYS A1074 15224 19147 14101 845 778 -543 N
ATOM 1965 N GLY A1075 170.546 0.861 157.740 1.00 77.80 N
ANISOU 1965 N GLY A1075 8811 11942 8805 741 1111 742 N
ATOM 1966 CA GLY A1075 169.258 0.182 157.760 1.00 78.24 C
ANISOU 1966 CA GLY A1075 8788 11985 8954 750 1257 1005 C
ATOM 1967 C GLY A1075 169.004 -0.641 159.001 1.00 84.95 C
ANISOU 1967 C GLY A1075 9582 13157 9539 825 1363 1263 C
ATOM 1968 O GLY A1075 168.918 -0.095 160.105 1.00 87.16 O
ANISOU 1968 O GLY A1075 9853 13754 9508 920 1444 1144 O
ATOM 1969 N ASP A1076 168.860 -1.965 158.806 1.00 81.26 N
ANISOU 1969 N ASP A1076 9070 12603 9200 782 1370 1619 N
ATOM 1970 CA ASP A1076 168.578 -2.960 159.842 1.00 83.58 C
ANISOU 1970 CA ASP A1076 9298 13146 9314 839 1480 1967 C
ATOM 1971 C ASP A1076 169.732 -3.021 160.859 1.00 89.13 C
ANISOU 1971 C ASP A1076 10041 14172 9651 928 1400 1964 C
ATOM 1972 O ASP A1076 170.860 -3.328 160.462 1.00 87.53 O
ANISOU 1972 O ASP A1076 9891 13863 9504 902 1233 1949 O
ATOM 1973 CB ASP A1076 168.345 -4.337 159.182 1.00 84.76 C
ANISOU 1973 CB ASP A1076 9401 13024 9779 751 1471 2315 C
ATOM 1974 CG ASP A1076 167.647 -5.408 160.006 1.00 98.61 C
ANISOU 1974 CG ASP A1076 11054 14924 11491 775 1629 2736 C
ATOM 1975 OD1 ASP A1076 167.320 -5.142 161.185 1.00102.39 O
ANISOU 1975 OD1 ASP A1076 11491 15775 11639 875 1763 2799 O
ATOM 1976 OD2 ASP A1076 167.417 -6.512 159.467 1.00104.01 O
ANISOU 1976 OD2 ASP A1076 11693 15348 12478 690 1627 2999 O
ATOM 1977 N PRO A1077 169.481 -2.715 162.163 1.00 88.77 N
ANISOU 1977 N PRO A1077 9963 14549 9218 1040 1513 1967 N
ATOM 1978 CA PRO A1077 170.568 -2.768 163.164 1.00 90.71 C
ANISOU 1978 CA PRO A1077 10231 15158 9075 1130 1420 1959 C
ATOM 1979 C PRO A1077 171.151 -4.176 163.337 1.00 95.34 C
ANISOU 1979 C PRO A1077 10789 15754 9681 1146 1365 2397 C
ATOM 1980 O PRO A1077 172.299 -4.318 163.765 1.00 95.81 O
ANISOU 1980 O PRO A1077 10869 16000 9534 1200 1221 2395 O
ATOM 1981 CB PRO A1077 169.888 -2.293 164.455 1.00 95.89 C
ANISOU 1981 CB PRO A1077 10838 16271 9326 1249 1592 1919 C
ATOM 1982 CG PRO A1077 168.650 -1.584 164.011 1.00 99.38 C
ANISOU 1982 CG PRO A1077 11253 16543 9965 1221 1744 1752 C
ATOM 1983 CD PRO A1077 168.205 -2.318 162.793 1.00 92.26 C
ANISOU 1983 CD PRO A1077 10329 15188 9536 1099 1733 1973 C
ATOM 1984 N GLU A1078 170.351 -5.205 162.987 1.00 91.59 N
ANISOU 1984 N GLU A1078 10255 15062 9484 1096 1477 2767 N
ATOM 1985 CA GLU A1078 170.694 -6.627 163.008 1.00 92.09 C
ANISOU 1985 CA GLU A1078 10282 15021 9687 1098 1456 3213 C
ATOM 1986 C GLU A1078 171.785 -6.915 161.966 1.00 92.13 C
ANISOU 1986 C GLU A1078 10353 14687 9966 1038 1250 3110 C
ATOM 1987 O GLU A1078 172.745 -7.626 162.268 1.00 92.65 O
ANISOU 1987 O GLU A1078 10417 14819 9967 1102 1151 3309 O
ATOM 1988 CB GLU A1078 169.425 -7.455 162.724 1.00 94.04 C
ANISOU 1988 CB GLU A1078 10443 15045 10243 1023 1633 3539 C
ATOM 1989 CG GLU A1078 169.591 -8.963 162.799 1.00107.35 C
ANISOU 1989 CG GLU A1078 12077 16580 12130 1016 1650 4028 C
ATOM 1990 CD GLU A1078 168.320 -9.728 162.488 1.00131.85 C
ANISOU 1990 CD GLU A1078 15079 19437 15580 912 1820 4314 C
ATOM 1991 OE1 GLU A1078 167.842 -9.649 161.332 1.00125.45 O
ANISOU 1991 OE1 GLU A1078 14273 18250 15142 782 1785 4133 O
ATOM 1992 OE2 GLU A1078 167.799 -10.408 163.401 1.00129.87 O
ANISOU 1992 OE2 GLU A1078 14734 19384 15226 957 1986 4727 O
ATOM 1993 N LEU A1079 171.633 -6.348 160.749 1.00 84.78 N
ANISOU 1993 N LEU A1079 9471 13414 9328 929 1191 2810 N
ATOM 1994 CA LEU A1079 172.571 -6.500 159.635 1.00 81.59 C
ANISOU 1994 CA LEU A1079 9124 12694 9182 867 1017 2672 C
ATOM 1995 C LEU A1079 173.739 -5.525 159.763 1.00 84.35 C
ANISOU 1995 C LEU A1079 9529 13214 9306 902 866 2336 C
ATOM 1996 O LEU A1079 174.847 -5.858 159.341 1.00 83.03 O
ANISOU 1996 O LEU A1079 9380 12947 9220 904 721 2322 O
ATOM 1997 CB LEU A1079 171.863 -6.311 158.287 1.00 78.85 C
ANISOU 1997 CB LEU A1079 8792 11957 9210 740 1027 2519 C
ATOM 1998 CG LEU A1079 170.857 -7.394 157.895 1.00 83.75 C
ANISOU 1998 CG LEU A1079 9345 12331 10144 669 1131 2814 C
ATOM 1999 CD1 LEU A1079 169.859 -6.860 156.925 1.00 82.07 C
ANISOU 1999 CD1 LEU A1079 9118 11901 10164 565 1167 2626 C
ATOM 2000 CD2 LEU A1079 171.544 -8.610 157.301 1.00 85.69 C
ANISOU 2000 CD2 LEU A1079 9597 12300 10661 644 1040 2996 C
ATOM 2001 N GLU A1080 173.492 -4.327 160.345 1.00 81.24 N
ANISOU 2001 N GLU A1080 9149 13069 8649 929 903 2055 N
ATOM 2002 CA GLU A1080 174.517 -3.310 160.609 1.00 80.81 C
ANISOU 2002 CA GLU A1080 9131 13195 8376 948 768 1705 C
ATOM 2003 C GLU A1080 175.520 -3.858 161.624 1.00 87.26 C
ANISOU 2003 C GLU A1080 9911 14361 8882 1051 674 1871 C
ATOM 2004 O GLU A1080 176.728 -3.741 161.416 1.00 86.46 O
ANISOU 2004 O GLU A1080 9814 14265 8771 1045 505 1745 O
ATOM 2005 CB GLU A1080 173.886 -2.002 161.120 1.00 82.90 C
ANISOU 2005 CB GLU A1080 9410 13640 8447 963 853 1378 C
ATOM 2006 CG GLU A1080 173.403 -1.064 160.029 1.00 89.11 C
ANISOU 2006 CG GLU A1080 10240 14089 9527 870 869 1096 C
ATOM 2007 CD GLU A1080 172.993 0.313 160.520 1.00107.76 C
ANISOU 2007 CD GLU A1080 12618 16592 11733 898 934 732 C
ATOM 2008 OE1 GLU A1080 173.843 1.014 161.116 1.00100.43 O
ANISOU 2008 OE1 GLU A1080 11707 15873 10578 920 838 462 O
ATOM 2009 OE2 GLU A1080 171.826 0.702 160.287 1.00102.16 O
ANISOU 2009 OE2 GLU A1080 11896 15772 11150 899 1076 701 O
ATOM 2010 N GLY A1081 174.996 -4.490 162.679 1.00 86.44 N
ANISOU 2010 N GLY A1081 9755 14549 8538 1147 789 2183 N
ATOM 2011 CA GLY A1081 175.772 -5.120 163.741 1.00 89.05 C
ANISOU 2011 CA GLY A1081 10035 15258 8542 1269 723 2430 C
ATOM 2012 C GLY A1081 176.525 -6.352 163.279 1.00 91.96 C
ANISOU 2012 C GLY A1081 10378 15410 9150 1286 629 2761 C
ATOM 2013 O GLY A1081 177.600 -6.644 163.806 1.00 93.06 O
ANISOU 2013 O GLY A1081 10478 15787 9092 1375 493 2849 O
ATOM 2014 N TRP A1082 175.963 -7.083 162.289 1.00 86.45 N
ANISOU 2014 N TRP A1082 9694 14265 8887 1207 699 2932 N
ATOM 2015 CA TRP A1082 176.557 -8.284 161.690 1.00 85.85 C
ANISOU 2015 CA TRP A1082 9602 13897 9122 1216 632 3209 C
ATOM 2016 C TRP A1082 177.776 -7.888 160.858 1.00 87.25 C
ANISOU 2016 C TRP A1082 9808 13924 9419 1182 443 2912 C
ATOM 2017 O TRP A1082 178.835 -8.505 160.991 1.00 87.68 O
ANISOU 2017 O TRP A1082 9821 14028 9465 1265 327 3060 O
ATOM 2018 CB TRP A1082 175.513 -9.033 160.829 1.00 83.39 C
ANISOU 2018 CB TRP A1082 9293 13150 9240 1118 759 3384 C
ATOM 2019 CG TRP A1082 175.956 -10.333 160.201 1.00 84.41 C
ANISOU 2019 CG TRP A1082 9405 12931 9736 1124 717 3651 C
ATOM 2020 CD1 TRP A1082 177.135 -10.995 160.398 1.00 88.50 C
ANISOU 2020 CD1 TRP A1082 9896 13487 10244 1231 599 3816 C
ATOM 2021 CD2 TRP A1082 175.190 -11.146 159.301 1.00 83.45 C
ANISOU 2021 CD2 TRP A1082 9280 12369 10057 1024 797 3774 C
ATOM 2022 NE1 TRP A1082 177.166 -12.145 159.647 1.00 87.84 N
ANISOU 2022 NE1 TRP A1082 9802 12986 10587 1211 610 4017 N
ATOM 2023 CE2 TRP A1082 175.980 -12.270 158.973 1.00 88.08 C
ANISOU 2023 CE2 TRP A1082 9850 12719 10899 1077 727 3985 C
ATOM 2024 CE3 TRP A1082 173.906 -11.034 158.739 1.00 83.68 C
ANISOU 2024 CE3 TRP A1082 9306 12186 10302 895 915 3714 C
ATOM 2025 CZ2 TRP A1082 175.532 -13.270 158.101 1.00 87.15 C
ANISOU 2025 CZ2 TRP A1082 9724 12144 11246 997 772 4103 C
ATOM 2026 CZ3 TRP A1082 173.466 -12.021 157.871 1.00 84.82 C
ANISOU 2026 CZ3 TRP A1082 9432 11905 10892 806 944 3839 C
ATOM 2027 CH2 TRP A1082 174.272 -13.125 157.564 1.00 86.29 C
ANISOU 2027 CH2 TRP A1082 9613 11847 11326 853 875 4017 C
ATOM 2028 N ALA A1083 177.625 -6.848 160.016 1.00 80.96 N
ANISOU 2028 N ALA A1083 9069 12958 8735 1069 421 2513 N
ATOM 2029 CA ALA A1083 178.684 -6.320 159.162 1.00 78.64 C
ANISOU 2029 CA ALA A1083 8796 12524 8560 1017 269 2217 C
ATOM 2030 C ALA A1083 179.850 -5.782 160.003 1.00 84.28 C
ANISOU 2030 C ALA A1083 9466 13620 8939 1086 123 2077 C
ATOM 2031 O ALA A1083 181.006 -6.094 159.709 1.00 83.87 O
ANISOU 2031 O ALA A1083 9371 13541 8954 1114 -12 2082 O
ATOM 2032 CB ALA A1083 178.126 -5.231 158.262 1.00 76.76 C
ANISOU 2032 CB ALA A1083 8620 12075 8471 890 302 1868 C
ATOM 2033 N ARG A1084 179.538 -5.028 161.080 1.00 82.54 N
ANISOU 2033 N ARG A1084 9239 13772 8352 1120 152 1955 N
ATOM 2034 CA ARG A1084 180.521 -4.459 162.006 1.00 84.32 C
ANISOU 2034 CA ARG A1084 9410 14416 8211 1178 9 1785 C
ATOM 2035 C ARG A1084 181.226 -5.561 162.820 1.00 90.14 C
ANISOU 2035 C ARG A1084 10060 15426 8762 1327 -66 2171 C
ATOM 2036 O ARG A1084 182.380 -5.369 163.210 1.00 91.08 O
ANISOU 2036 O ARG A1084 10110 15801 8697 1371 -239 2073 O
ATOM 2037 CB ARG A1084 179.866 -3.428 162.942 1.00 86.35 C
ANISOU 2037 CB ARG A1084 9687 14999 8125 1184 79 1537 C
ATOM 2038 CG ARG A1084 179.544 -2.098 162.254 1.00 95.60 C
ANISOU 2038 CG ARG A1084 10922 15947 9453 1055 100 1084 C
ATOM 2039 CD ARG A1084 178.756 -1.138 163.132 1.00111.00 C
ANISOU 2039 CD ARG A1084 12894 18164 11117 1077 200 837 C
ATOM 2040 NE ARG A1084 177.416 -1.638 163.457 1.00124.60 N
ANISOU 2040 NE ARG A1084 14627 19908 12808 1134 408 1104 N
ATOM 2041 CZ ARG A1084 176.442 -0.902 163.986 1.00142.24 C
ANISOU 2041 CZ ARG A1084 16878 22283 14883 1156 551 929 C
ATOM 2042 NH1 ARG A1084 176.636 0.387 164.241 1.00131.73 N
ANISOU 2042 NH1 ARG A1084 15570 21053 13428 1129 509 463 N
ATOM 2043 NH2 ARG A1084 175.263 -1.447 164.256 1.00129.89 N
ANISOU 2043 NH2 ARG A1084 15299 20746 13309 1206 745 1210 N
ATOM 2044 N SER A1085 180.547 -6.711 163.056 1.00 87.08 N
ANISOU 2044 N SER A1085 9665 14975 8446 1402 61 2621 N
ATOM 2045 CA SER A1085 181.127 -7.842 163.787 1.00 89.58 C
ANISOU 2045 CA SER A1085 9897 15502 8636 1557 12 3061 C
ATOM 2046 C SER A1085 182.138 -8.587 162.910 1.00 91.88 C
ANISOU 2046 C SER A1085 10156 15484 9272 1574 -105 3158 C
ATOM 2047 O SER A1085 183.166 -9.020 163.424 1.00 93.82 O
ANISOU 2047 O SER A1085 10310 15965 9372 1696 -240 3321 O
ATOM 2048 CB SER A1085 180.049 -8.795 164.301 1.00 94.70 C
ANISOU 2048 CB SER A1085 10540 16147 9294 1619 204 3524 C
ATOM 2049 OG SER A1085 179.586 -9.702 163.314 1.00101.51 O
ANISOU 2049 OG SER A1085 11431 16491 10647 1560 293 3731 O
ATOM 2050 N LEU A1086 181.857 -8.725 161.595 1.00 84.73 N
ANISOU 2050 N LEU A1086 9313 14076 8806 1462 -56 3051 N
ATOM 2051 CA LEU A1086 182.765 -9.384 160.646 1.00 83.11 C
ANISOU 2051 CA LEU A1086 9080 13558 8940 1477 -145 3088 C
ATOM 2052 C LEU A1086 183.950 -8.468 160.311 1.00 85.71 C
ANISOU 2052 C LEU A1086 9372 13999 9196 1436 -317 2711 C
ATOM 2053 O LEU A1086 185.017 -8.960 159.939 1.00 85.30 O
ANISOU 2053 O LEU A1086 9248 13879 9284 1499 -424 2766 O
ATOM 2054 CB LEU A1086 182.040 -9.810 159.353 1.00 80.41 C
ANISOU 2054 CB LEU A1086 8813 12686 9052 1370 -36 3067 C
ATOM 2055 CG LEU A1086 180.875 -10.808 159.464 1.00 86.05 C
ANISOU 2055 CG LEU A1086 9547 13195 9952 1375 131 3423 C
ATOM 2056 CD1 LEU A1086 180.209 -10.998 158.120 1.00 83.53 C
ANISOU 2056 CD1 LEU A1086 9292 12398 10049 1243 202 3287 C
ATOM 2057 CD2 LEU A1086 181.326 -12.163 160.001 1.00 91.53 C
ANISOU 2057 CD2 LEU A1086 10168 13882 10728 1531 126 3890 C
ATOM 2058 N GLU A1087 183.751 -7.138 160.450 1.00 81.52 N
ANISOU 2058 N GLU A1087 8877 13628 8468 1330 -333 2331 N
ATOM 2059 CA GLU A1087 184.747 -6.088 160.221 1.00 80.69 C
ANISOU 2059 CA GLU A1087 8731 13633 8294 1257 -481 1943 C
ATOM 2060 C GLU A1087 185.885 -6.207 161.251 1.00 88.44 C
ANISOU 2060 C GLU A1087 9581 15063 8961 1375 -653 2015 C
ATOM 2061 O GLU A1087 187.056 -6.197 160.866 1.00 88.08 O
ANISOU 2061 O GLU A1087 9443 15015 9008 1380 -792 1927 O
ATOM 2062 CB GLU A1087 184.074 -4.698 160.295 1.00 80.89 C
ANISOU 2062 CB GLU A1087 8828 13709 8197 1128 -431 1559 C
ATOM 2063 CG GLU A1087 184.990 -3.517 159.997 1.00 88.21 C
ANISOU 2063 CG GLU A1087 9717 14684 9115 1020 -563 1141 C
ATOM 2064 CD GLU A1087 184.467 -2.126 160.312 1.00104.28 C
ANISOU 2064 CD GLU A1087 11805 16809 11007 918 -532 758 C
ATOM 2065 OE1 GLU A1087 183.319 -2.001 160.798 1.00 99.96 O
ANISOU 2065 OE1 GLU A1087 11327 16317 10335 940 -398 793 O
ATOM 2066 OE2 GLU A1087 185.219 -1.154 160.074 1.00 94.48 O
ANISOU 2066 OE2 GLU A1087 10524 15574 9799 815 -636 421 O
ATOM 2067 N GLU A1088 185.530 -6.341 162.548 1.00 88.56 N
ANISOU 2067 N GLU A1088 9572 15482 8594 1478 -643 2188 N
ATOM 2068 CA GLU A1088 186.468 -6.468 163.671 1.00 92.35 C
ANISOU 2068 CA GLU A1088 9920 16469 8700 1606 -810 2284 C
ATOM 2069 C GLU A1088 187.023 -7.905 163.807 1.00 98.50 C
ANISOU 2069 C GLU A1088 10611 17238 9579 1786 -846 2786 C
ATOM 2070 O GLU A1088 187.993 -8.114 164.539 1.00101.03 O
ANISOU 2070 O GLU A1088 10795 17937 9654 1908 -1011 2897 O
ATOM 2071 CB GLU A1088 185.802 -6.018 164.994 1.00 96.60 C
ANISOU 2071 CB GLU A1088 10471 17479 8754 1654 -770 2266 C
ATOM 2072 CG GLU A1088 184.668 -6.912 165.482 1.00108.89 C
ANISOU 2072 CG GLU A1088 12079 19039 10257 1752 -577 2708 C
ATOM 2073 CD GLU A1088 183.953 -6.482 166.749 1.00133.46 C
ANISOU 2073 CD GLU A1088 15197 22634 12878 1808 -505 2700 C
ATOM 2074 OE1 GLU A1088 182.703 -6.561 166.772 1.00126.89 O
ANISOU 2074 OE1 GLU A1088 14446 21677 12088 1784 -296 2806 O
ATOM 2075 OE2 GLU A1088 184.634 -6.100 167.727 1.00131.02 O
ANISOU 2075 OE2 GLU A1088 14800 22847 12134 1881 -656 2591 O
ATOM 2076 N LYS A1089 186.402 -8.878 163.106 1.00 93.91 N
ANISOU 2076 N LYS A1089 10096 16218 9367 1803 -696 3077 N
ATOM 2077 CA LYS A1089 186.760 -10.300 163.132 1.00 95.55 C
ANISOU 2077 CA LYS A1089 10237 16302 9764 1969 -692 3560 C
ATOM 2078 C LYS A1089 187.780 -10.688 162.052 1.00 98.54 C
ANISOU 2078 C LYS A1089 10561 16357 10524 1979 -777 3492 C
ATOM 2079 O LYS A1089 188.621 -11.552 162.308 1.00100.59 O
ANISOU 2079 O LYS A1089 10704 16688 10828 2148 -864 3789 O
ATOM 2080 CB LYS A1089 185.495 -11.156 162.949 1.00 97.58 C
ANISOU 2080 CB LYS A1089 10589 16227 10258 1966 -476 3884 C
ATOM 2081 CG LYS A1089 185.614 -12.604 163.418 1.00114.51 C
ANISOU 2081 CG LYS A1089 12664 18333 12511 2153 -440 4463 C
ATOM 2082 CD LYS A1089 184.382 -13.431 163.043 1.00124.01 C
ANISOU 2082 CD LYS A1089 13952 19116 14051 2106 -226 4733 C
ATOM 2083 CE LYS A1089 183.343 -13.517 164.143 1.00137.07 C
ANISOU 2083 CE LYS A1089 15616 21058 15407 2135 -86 5026 C
ATOM 2084 NZ LYS A1089 182.523 -12.280 164.252 1.00143.64 N
ANISOU 2084 NZ LYS A1089 16527 22063 15988 1988 -24 4640 N
ATOM 2085 N HIS A1090 187.689 -10.094 160.847 1.00 91.84 N
ANISOU 2085 N HIS A1090 9787 15159 9951 1815 -743 3128 N
ATOM 2086 CA HIS A1090 188.551 -10.486 159.734 1.00 90.44 C
ANISOU 2086 CA HIS A1090 9562 14666 10135 1825 -788 3058 C
ATOM 2087 C HIS A1090 189.685 -9.486 159.435 1.00 93.52 C
ANISOU 2087 C HIS A1090 9859 15228 10447 1750 -944 2680 C
ATOM 2088 O HIS A1090 190.839 -9.913 159.338 1.00 94.81 O
ANISOU 2088 O HIS A1090 9882 15455 10685 1858 -1059 2756 O
ATOM 2089 CB HIS A1090 187.706 -10.759 158.488 1.00 88.31 C
ANISOU 2089 CB HIS A1090 9422 13871 10260 1715 -631 2984 C
ATOM 2090 CG HIS A1090 186.711 -11.858 158.705 1.00 92.86 C
ANISOU 2090 CG HIS A1090 10058 14237 10988 1778 -489 3363 C
ATOM 2091 ND1 HIS A1090 185.370 -11.587 158.908 1.00 93.88 N
ANISOU 2091 ND1 HIS A1090 10291 14324 11054 1677 -354 3368 N
ATOM 2092 CD2 HIS A1090 186.909 -13.193 158.821 1.00 96.78 C
ANISOU 2092 CD2 HIS A1090 10504 14568 11700 1934 -462 3755 C
ATOM 2093 CE1 HIS A1090 184.792 -12.762 159.102 1.00 94.91 C
ANISOU 2093 CE1 HIS A1090 10429 14261 11372 1754 -248 3759 C
ATOM 2094 NE2 HIS A1090 185.678 -13.757 159.059 1.00 97.08 N
ANISOU 2094 NE2 HIS A1090 10619 14439 11829 1909 -308 4004 N
ATOM 2095 N GLY A1091 189.370 -8.197 159.309 1.00 87.60 N
ANISOU 2095 N GLY A1091 9169 14542 9572 1574 -945 2295 N
ATOM 2096 CA GLY A1091 190.386 -7.180 159.046 1.00 86.75 C
ANISOU 2096 CA GLY A1091 8967 14573 9420 1474 -1081 1934 C
ATOM 2097 C GLY A1091 190.491 -6.755 157.596 1.00 86.63 C
ANISOU 2097 C GLY A1091 8998 14171 9744 1334 -1018 1682 C
ATOM 2098 O GLY A1091 190.870 -5.614 157.313 1.00 85.52 O
ANISOU 2098 O GLY A1091 8833 14080 9581 1187 -1071 1341 O
ATOM 2099 N ASN A1092 190.171 -7.676 156.665 1.00 80.74 N
ANISOU 2099 N ASN A1092 8314 13045 9319 1378 -904 1848 N
ATOM 2100 CA ASN A1092 190.136 -7.409 155.224 1.00 77.17 C
ANISOU 2100 CA ASN A1092 7918 12235 9168 1263 -825 1642 C
ATOM 2101 C ASN A1092 188.714 -6.951 154.850 1.00 78.67 C
ANISOU 2101 C ASN A1092 8282 12210 9399 1135 -685 1544 C
ATOM 2102 O ASN A1092 188.439 -6.613 153.699 1.00 76.08 O
ANISOU 2102 O ASN A1092 8021 11612 9276 1029 -612 1376 O
ATOM 2103 CB ASN A1092 190.576 -8.641 154.417 1.00 75.66 C
ANISOU 2103 CB ASN A1092 7690 11775 9283 1387 -786 1826 C
ATOM 2104 CG ASN A1092 189.706 -9.862 154.587 1.00 90.29 C
ANISOU 2104 CG ASN A1092 9624 13420 11263 1492 -685 2144 C
ATOM 2105 OD1 ASN A1092 189.138 -10.113 155.650 1.00 86.48 O
ANISOU 2105 OD1 ASN A1092 9162 13102 10593 1548 -679 2362 O
ATOM 2106 ND2 ASN A1092 189.606 -10.667 153.548 1.00 78.57 N
ANISOU 2106 ND2 ASN A1092 8176 11574 10105 1521 -601 2176 N
ATOM 2107 N VAL A1093 187.825 -6.930 155.857 1.00 75.94 N
ANISOU 2107 N VAL A1093 7996 12020 8838 1155 -649 1661 N
ATOM 2108 CA VAL A1093 186.434 -6.500 155.779 1.00 74.14 C
ANISOU 2108 CA VAL A1093 7904 11663 8602 1059 -520 1600 C
ATOM 2109 C VAL A1093 186.338 -5.130 156.467 1.00 78.52 C
ANISOU 2109 C VAL A1093 8464 12485 8885 968 -564 1323 C
ATOM 2110 O VAL A1093 186.734 -4.994 157.626 1.00 80.50 O
ANISOU 2110 O VAL A1093 8646 13101 8841 1033 -653 1350 O
ATOM 2111 CB VAL A1093 185.484 -7.558 156.414 1.00 79.14 C
ANISOU 2111 CB VAL A1093 8581 12270 9219 1157 -423 1954 C
ATOM 2112 CG1 VAL A1093 184.051 -7.048 156.512 1.00 77.92 C
ANISOU 2112 CG1 VAL A1093 8534 12055 9018 1064 -293 1894 C
ATOM 2113 CG2 VAL A1093 185.531 -8.877 155.646 1.00 78.73 C
ANISOU 2113 CG2 VAL A1093 8527 11884 9501 1228 -375 2183 C
ATOM 2114 N LYS A1094 185.859 -4.120 155.725 1.00 73.17 N
ANISOU 2114 N LYS A1094 7861 11625 8316 822 -506 1051 N
ATOM 2115 CA LYS A1094 185.651 -2.742 156.175 1.00 73.36 C
ANISOU 2115 CA LYS A1094 7906 11796 8172 722 -521 748 C
ATOM 2116 C LYS A1094 184.179 -2.393 155.987 1.00 76.82 C
ANISOU 2116 C LYS A1094 8467 12063 8659 671 -369 722 C
ATOM 2117 O LYS A1094 183.597 -2.732 154.955 1.00 74.33 O
ANISOU 2117 O LYS A1094 8211 11438 8592 636 -282 791 O
ATOM 2118 CB LYS A1094 186.570 -1.761 155.412 1.00 74.73 C
ANISOU 2118 CB LYS A1094 8027 11885 8481 596 -594 456 C
ATOM 2119 CG LYS A1094 186.350 -0.267 155.708 1.00 87.89 C
ANISOU 2119 CG LYS A1094 9719 13608 10066 472 -598 115 C
ATOM 2120 CD LYS A1094 186.926 0.182 157.050 1.00100.87 C
ANISOU 2120 CD LYS A1094 11278 15652 11396 494 -726 -33 C
ATOM 2121 CE LYS A1094 186.459 1.565 157.429 1.00111.59 C
ANISOU 2121 CE LYS A1094 12682 17032 12684 388 -703 -380 C
ATOM 2122 NZ LYS A1094 187.254 2.122 158.553 1.00124.28 N
ANISOU 2122 NZ LYS A1094 14185 19015 14020 376 -857 -612 N
ATOM 2123 N VAL A1095 183.569 -1.752 156.996 1.00 75.60 N
ANISOU 2123 N VAL A1095 8338 12132 8257 677 -339 618 N
ATOM 2124 CA VAL A1095 182.155 -1.385 156.955 1.00 75.03 C
ANISOU 2124 CA VAL A1095 8357 11939 8211 648 -189 594 C
ATOM 2125 C VAL A1095 181.991 0.105 157.281 1.00 81.38 C
ANISOU 2125 C VAL A1095 9183 12819 8917 570 -188 226 C
ATOM 2126 O VAL A1095 182.523 0.591 158.283 1.00 83.33 O
ANISOU 2126 O VAL A1095 9382 13377 8902 590 -272 62 O
ATOM 2127 CB VAL A1095 181.291 -2.291 157.882 1.00 80.12 C
ANISOU 2127 CB VAL A1095 9010 12753 8679 761 -97 896 C
ATOM 2128 CG1 VAL A1095 179.831 -1.842 157.913 1.00 79.34 C
ANISOU 2128 CG1 VAL A1095 8978 12569 8597 733 63 857 C
ATOM 2129 CG2 VAL A1095 181.381 -3.751 157.453 1.00 79.46 C
ANISOU 2129 CG2 VAL A1095 8908 12506 8776 824 -85 1255 C
ATOM 2130 N ILE A1096 181.250 0.817 156.413 1.00 77.47 N
ANISOU 2130 N ILE A1096 8755 12035 8646 487 -96 95 N
ATOM 2131 CA ILE A1096 180.918 2.232 156.564 1.00 78.39 C
ANISOU 2131 CA ILE A1096 8902 12126 8758 419 -64 -235 C
ATOM 2132 C ILE A1096 179.388 2.310 156.725 1.00 83.92 C
ANISOU 2132 C ILE A1096 9664 12769 9455 463 101 -173 C
ATOM 2133 O ILE A1096 178.651 2.220 155.739 1.00 81.47 O
ANISOU 2133 O ILE A1096 9392 12178 9387 432 182 -78 O
ATOM 2134 CB ILE A1096 181.485 3.099 155.393 1.00 79.83 C
ANISOU 2134 CB ILE A1096 9084 12019 9227 292 -101 -424 C
ATOM 2135 CG1 ILE A1096 183.026 3.060 155.366 1.00 80.80 C
ANISOU 2135 CG1 ILE A1096 9116 12247 9338 246 -257 -495 C
ATOM 2136 CG2 ILE A1096 180.998 4.554 155.465 1.00 81.16 C
ANISOU 2136 CG2 ILE A1096 9289 12084 9465 228 -45 -733 C
ATOM 2137 CD1 ILE A1096 183.600 2.269 154.250 1.00 86.36 C
ANISOU 2137 CD1 ILE A1096 9795 12775 10244 235 -281 -300 C
ATOM 2138 N THR A1097 178.921 2.423 157.986 1.00 84.33 N
ANISOU 2138 N THR A1097 9709 13121 9213 544 149 -215 N
ATOM 2139 CA THR A1097 177.497 2.504 158.334 1.00 85.25 C
ANISOU 2139 CA THR A1097 9857 13251 9284 602 318 -160 C
ATOM 2140 C THR A1097 177.049 3.977 158.296 1.00 91.20 C
ANISOU 2140 C THR A1097 10642 13897 10112 564 376 -522 C
ATOM 2141 O THR A1097 176.484 4.499 159.261 1.00 93.01 O
ANISOU 2141 O THR A1097 10872 14338 10130 631 456 -682 O
ATOM 2142 CB THR A1097 177.210 1.812 159.685 1.00 96.62 C
ANISOU 2142 CB THR A1097 11262 15088 10360 722 364 15 C
ATOM 2143 OG1 THR A1097 178.202 2.180 160.647 1.00 99.29 O
ANISOU 2143 OG1 THR A1097 11563 15764 10397 747 239 -183 O
ATOM 2144 CG2 THR A1097 177.132 0.297 159.560 1.00 94.64 C
ANISOU 2144 CG2 THR A1097 10986 14826 10145 768 379 454 C
ATOM 2145 N GLU A1098 177.313 4.632 157.154 1.00 87.36 N
ANISOU 2145 N GLU A1098 10179 13076 9937 465 343 -641 N
ATOM 2146 CA GLU A1098 176.999 6.028 156.846 1.00 88.15 C
ANISOU 2146 CA GLU A1098 10307 12972 10213 417 391 -943 C
ATOM 2147 C GLU A1098 176.659 6.167 155.367 1.00 90.98 C
ANISOU 2147 C GLU A1098 10689 12950 10929 353 422 -828 C
ATOM 2148 O GLU A1098 177.240 5.461 154.537 1.00 88.63 O
ANISOU 2148 O GLU A1098 10383 12554 10739 305 350 -645 O
ATOM 2149 CB GLU A1098 178.189 6.948 157.190 1.00 91.15 C
ANISOU 2149 CB GLU A1098 10665 13405 10563 339 265 -1280 C
ATOM 2150 CG GLU A1098 178.385 7.223 158.674 1.00106.02 C
ANISOU 2150 CG GLU A1098 12524 15669 12090 398 236 -1517 C
ATOM 2151 CD GLU A1098 179.724 6.826 159.275 1.00130.86 C
ANISOU 2151 CD GLU A1098 15603 19104 15012 372 57 -1557 C
ATOM 2152 OE1 GLU A1098 180.530 6.161 158.583 1.00125.36 O
ANISOU 2152 OE1 GLU A1098 14875 18326 14431 324 -38 -1357 O
ATOM 2153 OE2 GLU A1098 179.960 7.174 160.455 1.00128.16 O
ANISOU 2153 OE2 GLU A1098 15233 19096 14366 411 10 -1796 O
ATOM 2154 N MET A1099 175.733 7.082 155.031 1.00 88.95 N
ANISOU 2154 N MET A1099 10455 12495 10848 365 529 -937 N
ATOM 2155 CA MET A1099 175.365 7.341 153.639 1.00 87.30 C
ANISOU 2155 CA MET A1099 10259 11957 10955 316 555 -828 C
ATOM 2156 C MET A1099 176.412 8.279 153.036 1.00 90.40 C
ANISOU 2156 C MET A1099 10653 12160 11533 208 473 -1009 C
ATOM 2157 O MET A1099 176.425 9.478 153.336 1.00 91.75 O
ANISOU 2157 O MET A1099 10832 12235 11795 192 501 -1275 O
ATOM 2158 CB MET A1099 173.937 7.909 153.520 1.00 90.40 C
ANISOU 2158 CB MET A1099 10654 12227 11468 389 699 -831 C
ATOM 2159 CG MET A1099 172.841 6.872 153.745 1.00 94.25 C
ANISOU 2159 CG MET A1099 11114 12845 11854 466 784 -579 C
ATOM 2160 SD MET A1099 172.793 5.537 152.514 1.00 96.43 S
ANISOU 2160 SD MET A1099 11375 13005 12257 410 725 -231 S
ATOM 2161 CE MET A1099 172.012 6.383 151.133 1.00 92.10 C
ANISOU 2161 CE MET A1099 10819 12148 12027 393 762 -215 C
ATOM 2162 N LEU A1100 177.339 7.704 152.247 1.00 84.34 N
ANISOU 2162 N LEU A1100 9871 11347 10828 135 377 -872 N
ATOM 2163 CA LEU A1100 178.440 8.437 151.620 1.00 83.50 C
ANISOU 2163 CA LEU A1100 9743 11088 10895 21 305 -991 C
ATOM 2164 C LEU A1100 177.970 9.231 150.407 1.00 85.33 C
ANISOU 2164 C LEU A1100 9991 11006 11424 -14 371 -935 C
ATOM 2165 O LEU A1100 177.007 8.839 149.741 1.00 83.52 O
ANISOU 2165 O LEU A1100 9780 10700 11254 40 433 -737 O
ATOM 2166 CB LEU A1100 179.587 7.487 151.213 1.00 82.30 C
ANISOU 2166 CB LEU A1100 9551 11029 10690 -25 196 -851 C
ATOM 2167 CG LEU A1100 180.330 6.746 152.334 1.00 87.92 C
ANISOU 2167 CG LEU A1100 10224 12053 11128 8 103 -882 C
ATOM 2168 CD1 LEU A1100 181.231 5.676 151.762 1.00 86.81 C
ANISOU 2168 CD1 LEU A1100 10041 11959 10983 -2 22 -687 C
ATOM 2169 CD2 LEU A1100 181.147 7.700 153.206 1.00 92.47 C
ANISOU 2169 CD2 LEU A1100 10756 12737 11639 -54 29 -1200 C
ATOM 2170 N SER A1101 178.663 10.352 150.131 1.00 82.06 N
ANISOU 2170 N SER A1101 9559 10417 11205 -109 354 -1102 N
ATOM 2171 CA SER A1101 178.392 11.245 149.005 1.00 81.23 C
ANISOU 2171 CA SER A1101 9458 10009 11399 -147 416 -1032 C
ATOM 2172 C SER A1101 178.687 10.546 147.682 1.00 81.80 C
ANISOU 2172 C SER A1101 9515 10045 11519 -177 391 -755 C
ATOM 2173 O SER A1101 179.662 9.796 147.596 1.00 80.56 O
ANISOU 2173 O SER A1101 9326 10026 11256 -222 311 -712 O
ATOM 2174 CB SER A1101 179.227 12.518 149.123 1.00 86.87 C
ANISOU 2174 CB SER A1101 10141 10548 12319 -259 401 -1267 C
ATOM 2175 OG SER A1101 180.617 12.236 149.129 1.00 95.18 O
ANISOU 2175 OG SER A1101 11132 11708 13323 -370 294 -1310 O
ATOM 2176 N ARG A1102 177.853 10.809 146.653 1.00 76.81 N
ANISOU 2176 N ARG A1102 8898 9246 11040 -141 459 -577 N
ATOM 2177 CA ARG A1102 177.973 10.247 145.300 1.00 74.58 C
ANISOU 2177 CA ARG A1102 8603 8944 10790 -157 444 -330 C
ATOM 2178 C ARG A1102 179.373 10.452 144.705 1.00 78.24 C
ANISOU 2178 C ARG A1102 9019 9381 11326 -271 400 -325 C
ATOM 2179 O ARG A1102 179.843 9.591 143.961 1.00 76.55 O
ANISOU 2179 O ARG A1102 8787 9266 11032 -281 364 -185 O
ATOM 2180 CB ARG A1102 176.934 10.867 144.364 1.00 74.25 C
ANISOU 2180 CB ARG A1102 8566 8728 10917 -107 516 -175 C
ATOM 2181 CG ARG A1102 175.512 10.349 144.529 1.00 83.32 C
ANISOU 2181 CG ARG A1102 9729 9937 11991 5 551 -94 C
ATOM 2182 CD ARG A1102 174.758 10.365 143.205 1.00 91.86 C
ANISOU 2182 CD ARG A1102 10790 10952 13161 43 567 139 C
ATOM 2183 NE ARG A1102 174.859 11.653 142.510 1.00 99.11 N
ANISOU 2183 NE ARG A1102 11692 11656 14309 28 614 197 N
ATOM 2184 CZ ARG A1102 174.625 11.831 141.213 1.00111.07 C
ANISOU 2184 CZ ARG A1102 13180 13129 15894 41 617 421 C
ATOM 2185 NH1 ARG A1102 174.748 13.034 140.670 1.00 97.57 N
ANISOU 2185 NH1 ARG A1102 11451 11215 14407 32 671 504 N
ATOM 2186 NH2 ARG A1102 174.269 10.805 140.448 1.00 96.83 N
ANISOU 2186 NH2 ARG A1102 11362 11489 13938 62 564 564 N
ATOM 2187 N GLU A1103 180.031 11.585 145.045 1.00 76.21 N
ANISOU 2187 N GLU A1103 8733 8989 11234 -359 409 -491 N
ATOM 2188 CA GLU A1103 181.384 11.950 144.612 1.00 76.50 C
ANISOU 2188 CA GLU A1103 8698 8988 11380 -488 378 -506 C
ATOM 2189 C GLU A1103 182.426 10.969 145.172 1.00 79.48 C
ANISOU 2189 C GLU A1103 9031 9615 11554 -515 277 -580 C
ATOM 2190 O GLU A1103 183.397 10.651 144.479 1.00 78.78 O
ANISOU 2190 O GLU A1103 8877 9579 11479 -575 253 -486 O
ATOM 2191 CB GLU A1103 181.727 13.389 145.044 1.00 80.33 C
ANISOU 2191 CB GLU A1103 9154 9250 12117 -585 406 -705 C
ATOM 2192 CG GLU A1103 181.012 14.480 144.256 1.00 90.98 C
ANISOU 2192 CG GLU A1103 10521 10302 13747 -573 512 -580 C
ATOM 2193 CD GLU A1103 179.572 14.805 144.620 1.00108.56 C
ANISOU 2193 CD GLU A1103 12815 12431 16001 -440 577 -605 C
ATOM 2194 OE1 GLU A1103 179.025 14.190 145.564 1.00102.08 O
ANISOU 2194 OE1 GLU A1103 12033 11784 14967 -357 552 -733 O
ATOM 2195 OE2 GLU A1103 178.992 15.695 143.957 1.00100.35 O
ANISOU 2195 OE2 GLU A1103 11778 11146 15206 -412 660 -479 O
ATOM 2196 N PHE A1104 182.221 10.492 146.419 1.00 75.84 N
ANISOU 2196 N PHE A1104 8594 9322 10900 -459 225 -732 N
ATOM 2197 CA PHE A1104 183.115 9.530 147.066 1.00 75.33 C
ANISOU 2197 CA PHE A1104 8481 9511 10630 -456 124 -775 C
ATOM 2198 C PHE A1104 182.806 8.108 146.588 1.00 75.38 C
ANISOU 2198 C PHE A1104 8516 9639 10487 -358 118 -552 C
ATOM 2199 O PHE A1104 183.731 7.306 146.460 1.00 74.73 O
ANISOU 2199 O PHE A1104 8377 9691 10328 -361 56 -498 O
ATOM 2200 CB PHE A1104 183.040 9.630 148.600 1.00 78.99 C
ANISOU 2200 CB PHE A1104 8951 10134 10927 -428 71 -1007 C
ATOM 2201 CG PHE A1104 184.027 8.772 149.367 1.00 81.49 C
ANISOU 2201 CG PHE A1104 9199 10733 11028 -419 -48 -1047 C
ATOM 2202 CD1 PHE A1104 185.362 8.693 148.975 1.00 85.19 C
ANISOU 2202 CD1 PHE A1104 9561 11249 11560 -507 -121 -1044 C
ATOM 2203 CD2 PHE A1104 183.637 8.094 150.513 1.00 84.34 C
ANISOU 2203 CD2 PHE A1104 9588 11330 11127 -318 -84 -1077 C
ATOM 2204 CE1 PHE A1104 186.271 7.904 149.688 1.00 86.87 C
ANISOU 2204 CE1 PHE A1104 9693 11733 11583 -481 -238 -1065 C
ATOM 2205 CE2 PHE A1104 184.550 7.313 151.232 1.00 88.05 C
ANISOU 2205 CE2 PHE A1104 9985 12074 11396 -293 -199 -1079 C
ATOM 2206 CZ PHE A1104 185.860 7.224 150.814 1.00 86.46 C
ANISOU 2206 CZ PHE A1104 9674 11909 11268 -371 -282 -1077 C
ATOM 2207 N VAL A1105 181.518 7.810 146.297 1.00 69.33 N
ANISOU 2207 N VAL A1105 7824 8814 9706 -274 183 -432 N
ATOM 2208 CA VAL A1105 181.043 6.519 145.766 1.00 66.70 C
ANISOU 2208 CA VAL A1105 7517 8548 9278 -197 183 -240 C
ATOM 2209 C VAL A1105 181.660 6.325 144.366 1.00 68.39 C
ANISOU 2209 C VAL A1105 7697 8709 9579 -237 187 -116 C
ATOM 2210 O VAL A1105 182.067 5.215 144.017 1.00 67.20 O
ANISOU 2210 O VAL A1105 7530 8653 9352 -202 153 -34 O
ATOM 2211 CB VAL A1105 179.486 6.434 145.746 1.00 69.61 C
ANISOU 2211 CB VAL A1105 7946 8855 9648 -122 250 -161 C
ATOM 2212 CG1 VAL A1105 179.000 5.108 145.172 1.00 67.91 C
ANISOU 2212 CG1 VAL A1105 7743 8688 9371 -68 241 11 C
ATOM 2213 CG2 VAL A1105 178.903 6.646 147.139 1.00 70.43 C
ANISOU 2213 CG2 VAL A1105 8071 9041 9646 -73 269 -285 C
ATOM 2214 N ARG A1106 181.751 7.430 143.596 1.00 64.34 N
ANISOU 2214 N ARG A1106 7168 8047 9231 -304 236 -104 N
ATOM 2215 CA ARG A1106 182.353 7.518 142.267 1.00 63.50 C
ANISOU 2215 CA ARG A1106 7018 7907 9201 -348 262 19 C
ATOM 2216 C ARG A1106 183.851 7.176 142.354 1.00 68.05 C
ANISOU 2216 C ARG A1106 7506 8600 9749 -402 213 -33 C
ATOM 2217 O ARG A1106 184.350 6.424 141.516 1.00 67.00 O
ANISOU 2217 O ARG A1106 7340 8549 9568 -380 215 62 O
ATOM 2218 CB ARG A1106 182.128 8.933 141.704 1.00 63.12 C
ANISOU 2218 CB ARG A1106 6964 7666 9354 -409 334 57 C
ATOM 2219 CG ARG A1106 182.792 9.232 140.368 1.00 67.19 C
ANISOU 2219 CG ARG A1106 7420 8159 9947 -463 381 212 C
ATOM 2220 CD ARG A1106 182.479 10.630 139.892 1.00 68.25 C
ANISOU 2220 CD ARG A1106 7548 8082 10302 -512 459 293 C
ATOM 2221 NE ARG A1106 183.040 11.649 140.778 1.00 71.32 N
ANISOU 2221 NE ARG A1106 7901 8328 10869 -611 460 117 N
ATOM 2222 CZ ARG A1106 182.614 12.905 140.840 1.00 82.58 C
ANISOU 2222 CZ ARG A1106 9336 9512 12528 -643 521 108 C
ATOM 2223 NH1 ARG A1106 181.625 13.318 140.057 1.00 64.18 N
ANISOU 2223 NH1 ARG A1106 7043 7069 10275 -572 587 300 N
ATOM 2224 NH2 ARG A1106 183.184 13.763 141.674 1.00 72.99 N
ANISOU 2224 NH2 ARG A1106 8084 8165 11485 -744 512 -100 N
ATOM 2225 N GLU A1107 184.548 7.708 143.385 1.00 66.09 N
ANISOU 2225 N GLU A1107 7210 8376 9527 -466 166 -201 N
ATOM 2226 CA GLU A1107 185.967 7.445 143.635 1.00 66.81 C
ANISOU 2226 CA GLU A1107 7189 8599 9597 -519 102 -266 C
ATOM 2227 C GLU A1107 186.167 5.991 144.047 1.00 69.47 C
ANISOU 2227 C GLU A1107 7524 9123 9747 -411 36 -229 C
ATOM 2228 O GLU A1107 187.163 5.383 143.657 1.00 69.14 O
ANISOU 2228 O GLU A1107 7397 9185 9690 -404 12 -187 O
ATOM 2229 CB GLU A1107 186.534 8.392 144.706 1.00 70.24 C
ANISOU 2229 CB GLU A1107 7564 9027 10096 -618 48 -483 C
ATOM 2230 CG GLU A1107 187.654 9.295 144.203 1.00 83.90 C
ANISOU 2230 CG GLU A1107 9170 10682 12027 -767 63 -516 C
ATOM 2231 CD GLU A1107 188.899 8.619 143.653 1.00108.77 C
ANISOU 2231 CD GLU A1107 12191 13986 15149 -782 40 -433 C
ATOM 2232 OE1 GLU A1107 189.377 7.639 144.271 1.00106.30 O
ANISOU 2232 OE1 GLU A1107 11838 13876 14673 -709 -49 -466 O
ATOM 2233 OE2 GLU A1107 189.413 9.091 142.613 1.00105.11 O
ANISOU 2233 OE2 GLU A1107 11657 13446 14834 -861 117 -324 O
ATOM 2234 N LEU A1108 185.209 5.435 144.818 1.00 65.20 N
ANISOU 2234 N LEU A1108 7070 8619 9085 -322 19 -230 N
ATOM 2235 CA LEU A1108 185.217 4.039 145.254 1.00 64.28 C
ANISOU 2235 CA LEU A1108 6962 8641 8823 -214 -29 -155 C
ATOM 2236 C LEU A1108 185.036 3.125 144.043 1.00 66.22 C
ANISOU 2236 C LEU A1108 7227 8838 9095 -160 12 -12 C
ATOM 2237 O LEU A1108 185.795 2.172 143.900 1.00 65.98 O
ANISOU 2237 O LEU A1108 7143 8893 9033 -105 -21 31 O
ATOM 2238 CB LEU A1108 184.127 3.775 146.308 1.00 64.32 C
ANISOU 2238 CB LEU A1108 7047 8682 8711 -145 -31 -161 C
ATOM 2239 CG LEU A1108 184.407 4.260 147.729 1.00 70.62 C
ANISOU 2239 CG LEU A1108 7817 9621 9394 -157 -91 -315 C
ATOM 2240 CD1 LEU A1108 183.119 4.639 148.434 1.00 70.87 C
ANISOU 2240 CD1 LEU A1108 7933 9628 9365 -121 -37 -359 C
ATOM 2241 CD2 LEU A1108 185.150 3.208 148.537 1.00 73.96 C
ANISOU 2241 CD2 LEU A1108 8180 10262 9658 -80 -181 -264 C
ATOM 2242 N TYR A1109 184.086 3.460 143.136 1.00 61.44 N
ANISOU 2242 N TYR A1109 6687 8105 8553 -171 81 49 N
ATOM 2243 CA TYR A1109 183.819 2.719 141.895 1.00 60.29 C
ANISOU 2243 CA TYR A1109 6559 7932 8415 -131 114 149 C
ATOM 2244 C TYR A1109 185.049 2.673 140.984 1.00 64.08 C
ANISOU 2244 C TYR A1109 6952 8470 8924 -154 130 157 C
ATOM 2245 O TYR A1109 185.254 1.683 140.287 1.00 63.36 O
ANISOU 2245 O TYR A1109 6852 8419 8802 -92 135 191 O
ATOM 2246 CB TYR A1109 182.653 3.346 141.108 1.00 60.97 C
ANISOU 2246 CB TYR A1109 6705 7909 8551 -149 171 208 C
ATOM 2247 CG TYR A1109 181.250 3.133 141.642 1.00 62.22 C
ANISOU 2247 CG TYR A1109 6934 8019 8688 -105 173 231 C
ATOM 2248 CD1 TYR A1109 180.933 2.018 142.413 1.00 63.91 C
ANISOU 2248 CD1 TYR A1109 7169 8280 8836 -45 141 243 C
ATOM 2249 CD2 TYR A1109 180.214 3.991 141.286 1.00 63.08 C
ANISOU 2249 CD2 TYR A1109 7074 8034 8858 -118 218 269 C
ATOM 2250 CE1 TYR A1109 179.635 1.799 142.873 1.00 64.21 C
ANISOU 2250 CE1 TYR A1109 7251 8283 8865 -13 159 284 C
ATOM 2251 CE2 TYR A1109 178.910 3.776 141.728 1.00 63.76 C
ANISOU 2251 CE2 TYR A1109 7200 8091 8934 -75 228 296 C
ATOM 2252 CZ TYR A1109 178.624 2.680 142.522 1.00 70.55 C
ANISOU 2252 CZ TYR A1109 8074 9009 9724 -30 203 300 C
ATOM 2253 OH TYR A1109 177.338 2.474 142.957 1.00 71.46 O
ANISOU 2253 OH TYR A1109 8208 9103 9839 4 228 343 O
ATOM 2254 N GLY A1110 185.832 3.752 140.993 1.00 61.25 N
ANISOU 2254 N GLY A1110 6523 8108 8639 -247 144 118 N
ATOM 2255 CA GLY A1110 187.046 3.888 140.198 1.00 61.75 C
ANISOU 2255 CA GLY A1110 6477 8239 8745 -287 177 138 C
ATOM 2256 C GLY A1110 188.294 3.321 140.841 1.00 66.51 C
ANISOU 2256 C GLY A1110 6970 8975 9326 -267 114 75 C
ATOM 2257 O GLY A1110 189.341 3.248 140.192 1.00 66.97 O
ANISOU 2257 O GLY A1110 6916 9113 9415 -282 145 94 O
ATOM 2258 N SER A1111 188.197 2.915 142.121 1.00 63.11 N
ANISOU 2258 N SER A1111 6556 8592 8831 -225 28 15 N
ATOM 2259 CA SER A1111 189.314 2.346 142.875 1.00 63.79 C
ANISOU 2259 CA SER A1111 6529 8831 8877 -186 -53 -24 C
ATOM 2260 C SER A1111 189.160 0.834 143.063 1.00 66.14 C
ANISOU 2260 C SER A1111 6858 9174 9100 -34 -83 49 C
ATOM 2261 O SER A1111 190.111 0.094 142.813 1.00 66.59 O
ANISOU 2261 O SER A1111 6815 9314 9170 36 -95 73 O
ATOM 2262 CB SER A1111 189.449 3.030 144.231 1.00 68.91 C
ANISOU 2262 CB SER A1111 7150 9542 9489 -245 -139 -140 C
ATOM 2263 OG SER A1111 189.670 4.424 144.088 1.00 80.11 O
ANISOU 2263 OG SER A1111 8529 10883 11027 -395 -113 -232 O
ATOM 2264 N VAL A1112 187.963 0.378 143.482 1.00 60.97 N
ANISOU 2264 N VAL A1112 6328 8447 8392 19 -84 93 N
ATOM 2265 CA VAL A1112 187.661 -1.039 143.726 1.00 60.17 C
ANISOU 2265 CA VAL A1112 6262 8338 8260 149 -103 182 C
ATOM 2266 C VAL A1112 187.709 -1.835 142.414 1.00 63.17 C
ANISOU 2266 C VAL A1112 6648 8642 8711 203 -43 207 C
ATOM 2267 O VAL A1112 187.515 -1.271 141.334 1.00 62.27 O
ANISOU 2267 O VAL A1112 6552 8483 8623 142 20 178 O
ATOM 2268 CB VAL A1112 186.313 -1.264 144.476 1.00 63.20 C
ANISOU 2268 CB VAL A1112 6761 8662 8590 172 -102 235 C
ATOM 2269 CG1 VAL A1112 186.274 -0.492 145.794 1.00 63.68 C
ANISOU 2269 CG1 VAL A1112 6815 8835 8547 135 -153 180 C
ATOM 2270 CG2 VAL A1112 185.103 -0.932 143.603 1.00 61.68 C
ANISOU 2270 CG2 VAL A1112 6665 8325 8446 124 -31 237 C
ATOM 2271 N ASP A1113 187.978 -3.139 142.516 1.00 60.08 N
ANISOU 2271 N ASP A1113 6239 8240 8350 325 -61 259 N
ATOM 2272 CA ASP A1113 188.043 -4.012 141.351 1.00 59.92 C
ANISOU 2272 CA ASP A1113 6223 8143 8401 391 -8 238 C
ATOM 2273 C ASP A1113 186.652 -4.453 140.947 1.00 62.57 C
ANISOU 2273 C ASP A1113 6682 8331 8762 382 18 248 C
ATOM 2274 O ASP A1113 186.300 -4.359 139.771 1.00 61.98 O
ANISOU 2274 O ASP A1113 6637 8222 8691 353 66 186 O
ATOM 2275 CB ASP A1113 188.935 -5.233 141.623 1.00 63.09 C
ANISOU 2275 CB ASP A1113 6543 8559 8870 535 -34 276 C
ATOM 2276 CG ASP A1113 190.333 -4.893 142.073 1.00 72.90 C
ANISOU 2276 CG ASP A1113 7632 9973 10093 555 -76 275 C
ATOM 2277 OD1 ASP A1113 191.054 -4.215 141.309 1.00 74.01 O
ANISOU 2277 OD1 ASP A1113 7692 10195 10234 498 -33 203 O
ATOM 2278 OD2 ASP A1113 190.713 -5.314 143.178 1.00 78.86 O
ANISOU 2278 OD2 ASP A1113 8335 10797 10831 628 -152 358 O
ATOM 2279 N PHE A1114 185.853 -4.911 141.925 1.00 58.89 N
ANISOU 2279 N PHE A1114 6273 7800 8302 404 -13 334 N
ATOM 2280 CA PHE A1114 184.500 -5.406 141.694 1.00 58.15 C
ANISOU 2280 CA PHE A1114 6271 7565 8258 387 7 358 C
ATOM 2281 C PHE A1114 183.482 -4.752 142.613 1.00 61.44 C
ANISOU 2281 C PHE A1114 6743 7992 8612 326 2 423 C
ATOM 2282 O PHE A1114 183.814 -4.383 143.738 1.00 61.56 O
ANISOU 2282 O PHE A1114 6734 8109 8548 336 -27 469 O
ATOM 2283 CB PHE A1114 184.454 -6.932 141.884 1.00 60.99 C
ANISOU 2283 CB PHE A1114 6632 7797 8747 488 -1 418 C
ATOM 2284 CG PHE A1114 185.403 -7.711 141.004 1.00 63.51 C
ANISOU 2284 CG PHE A1114 6896 8082 9154 574 15 330 C
ATOM 2285 CD1 PHE A1114 185.009 -8.151 139.748 1.00 66.71 C
ANISOU 2285 CD1 PHE A1114 7333 8396 9619 565 48 199 C
ATOM 2286 CD2 PHE A1114 186.687 -8.021 141.439 1.00 66.51 C
ANISOU 2286 CD2 PHE A1114 7181 8541 9549 674 -5 367 C
ATOM 2287 CE1 PHE A1114 185.895 -8.849 138.922 1.00 68.80 C
ANISOU 2287 CE1 PHE A1114 7544 8646 9950 658 76 85 C
ATOM 2288 CE2 PHE A1114 187.572 -8.722 140.615 1.00 70.50 C
ANISOU 2288 CE2 PHE A1114 7622 9020 10143 771 25 276 C
ATOM 2289 CZ PHE A1114 187.170 -9.127 139.361 1.00 68.80 C
ANISOU 2289 CZ PHE A1114 7449 8711 9981 764 72 127 C
ATOM 2290 N VAL A1115 182.236 -4.618 142.129 1.00 57.38 N
ANISOU 2290 N VAL A1115 6289 7390 8123 270 29 415 N
ATOM 2291 CA VAL A1115 181.115 -4.070 142.892 1.00 56.72 C
ANISOU 2291 CA VAL A1115 6247 7305 7997 226 44 473 C
ATOM 2292 C VAL A1115 180.062 -5.164 142.989 1.00 60.54 C
ANISOU 2292 C VAL A1115 6756 7665 8580 239 55 554 C
ATOM 2293 O VAL A1115 179.573 -5.637 141.967 1.00 60.18 O
ANISOU 2293 O VAL A1115 6721 7524 8622 215 56 500 O
ATOM 2294 CB VAL A1115 180.556 -2.737 142.322 1.00 59.87 C
ANISOU 2294 CB VAL A1115 6669 7720 8359 146 69 411 C
ATOM 2295 CG1 VAL A1115 179.222 -2.364 142.967 1.00 59.38 C
ANISOU 2295 CG1 VAL A1115 6641 7634 8287 122 97 464 C
ATOM 2296 CG2 VAL A1115 181.558 -1.610 142.517 1.00 59.85 C
ANISOU 2296 CG2 VAL A1115 6633 7810 8296 116 64 350 C
ATOM 2297 N ILE A1116 179.745 -5.587 144.216 1.00 57.41 N
ANISOU 2297 N ILE A1116 6358 7284 8169 273 64 685 N
ATOM 2298 CA ILE A1116 178.767 -6.638 144.460 1.00 57.71 C
ANISOU 2298 CA ILE A1116 6402 7197 8329 275 89 801 C
ATOM 2299 C ILE A1116 177.389 -6.016 144.702 1.00 60.88 C
ANISOU 2299 C ILE A1116 6817 7612 8703 210 132 830 C
ATOM 2300 O ILE A1116 177.193 -5.269 145.665 1.00 60.80 O
ANISOU 2300 O ILE A1116 6810 7727 8564 218 160 870 O
ATOM 2301 CB ILE A1116 179.211 -7.581 145.609 1.00 62.09 C
ANISOU 2301 CB ILE A1116 6932 7762 8898 362 90 979 C
ATOM 2302 CG1 ILE A1116 180.537 -8.285 145.243 1.00 62.92 C
ANISOU 2302 CG1 ILE A1116 7006 7830 9072 445 48 951 C
ATOM 2303 CG2 ILE A1116 178.113 -8.610 145.924 1.00 63.87 C
ANISOU 2303 CG2 ILE A1116 7152 7838 9277 346 135 1136 C
ATOM 2304 CD1 ILE A1116 181.340 -8.749 146.388 1.00 70.43 C
ANISOU 2304 CD1 ILE A1116 7914 8877 9968 549 26 1113 C
ATOM 2305 N ILE A1117 176.445 -6.328 143.800 1.00 56.53 N
ANISOU 2305 N ILE A1117 6263 6943 8274 150 134 791 N
ATOM 2306 CA ILE A1117 175.050 -5.885 143.845 1.00 55.64 C
ANISOU 2306 CA ILE A1117 6135 6830 8176 91 170 823 C
ATOM 2307 C ILE A1117 174.199 -7.171 144.013 1.00 60.20 C
ANISOU 2307 C ILE A1117 6674 7265 8935 60 189 935 C
ATOM 2308 O ILE A1117 173.713 -7.715 143.022 1.00 59.57 O
ANISOU 2308 O ILE A1117 6573 7068 8992 3 154 855 O
ATOM 2309 CB ILE A1117 174.674 -5.032 142.589 1.00 57.54 C
ANISOU 2309 CB ILE A1117 6377 7084 8402 41 142 689 C
ATOM 2310 CG1 ILE A1117 175.773 -4.000 142.240 1.00 56.88 C
ANISOU 2310 CG1 ILE A1117 6323 7092 8197 63 126 595 C
ATOM 2311 CG2 ILE A1117 173.319 -4.343 142.767 1.00 57.89 C
ANISOU 2311 CG2 ILE A1117 6390 7158 8447 6 179 733 C
ATOM 2312 CD1 ILE A1117 176.075 -3.879 140.777 1.00 61.01 C
ANISOU 2312 CD1 ILE A1117 6846 7611 8724 42 87 487 C
ATOM 2313 N PRO A1118 174.059 -7.718 145.249 1.00 58.04 N
ANISOU 2313 N PRO A1118 6383 7002 8668 95 243 1122 N
ATOM 2314 CA PRO A1118 173.322 -8.984 145.413 1.00 59.61 C
ANISOU 2314 CA PRO A1118 6534 7033 9081 56 273 1260 C
ATOM 2315 C PRO A1118 171.823 -8.774 145.661 1.00 64.96 C
ANISOU 2315 C PRO A1118 7149 7725 9806 -19 334 1340 C
ATOM 2316 O PRO A1118 171.193 -9.525 146.413 1.00 66.15 O
ANISOU 2316 O PRO A1118 7247 7822 10066 -38 402 1537 O
ATOM 2317 CB PRO A1118 174.020 -9.633 146.615 1.00 62.44 C
ANISOU 2317 CB PRO A1118 6895 7420 9408 145 309 1465 C
ATOM 2318 CG PRO A1118 174.669 -8.491 147.361 1.00 65.86 C
ANISOU 2318 CG PRO A1118 7361 8103 9560 212 310 1440 C
ATOM 2319 CD PRO A1118 174.575 -7.239 146.545 1.00 59.61 C
ANISOU 2319 CD PRO A1118 6595 7375 8677 168 279 1222 C
ATOM 2320 N SER A1119 171.253 -7.772 144.976 1.00 61.11 N
ANISOU 2320 N SER A1119 6654 7310 9253 -58 312 1202 N
ATOM 2321 CA SER A1119 169.860 -7.353 145.066 1.00 61.54 C
ANISOU 2321 CA SER A1119 6634 7407 9341 -113 361 1247 C
ATOM 2322 C SER A1119 168.874 -8.456 144.711 1.00 67.93 C
ANISOU 2322 C SER A1119 7350 8054 10404 -215 357 1307 C
ATOM 2323 O SER A1119 169.066 -9.177 143.733 1.00 68.21 O
ANISOU 2323 O SER A1119 7386 7943 10587 -268 275 1187 O
ATOM 2324 CB SER A1119 169.614 -6.157 144.156 1.00 63.32 C
ANISOU 2324 CB SER A1119 6865 7711 9481 -120 314 1086 C
ATOM 2325 OG SER A1119 170.506 -5.094 144.446 1.00 70.03 O
ANISOU 2325 OG SER A1119 7791 8676 10142 -45 321 1022 O
ATOM 2326 N TYR A1120 167.823 -8.585 145.533 1.00 65.81 N
ANISOU 2326 N TYR A1120 6994 7820 10191 -245 453 1482 N
ATOM 2327 CA TYR A1120 166.705 -9.506 145.342 1.00 67.30 C
ANISOU 2327 CA TYR A1120 7061 7870 10641 -363 468 1563 C
ATOM 2328 C TYR A1120 165.768 -8.929 144.288 1.00 69.86 C
ANISOU 2328 C TYR A1120 7307 8232 11006 -433 396 1408 C
ATOM 2329 O TYR A1120 165.060 -9.674 143.607 1.00 70.86 O
ANISOU 2329 O TYR A1120 7338 8232 11355 -550 339 1361 O
ATOM 2330 CB TYR A1120 165.947 -9.700 146.663 1.00 70.33 C
ANISOU 2330 CB TYR A1120 7362 8327 11035 -359 617 1832 C
ATOM 2331 CG TYR A1120 166.602 -10.643 147.646 1.00 73.85 C
ANISOU 2331 CG TYR A1120 7840 8708 11513 -315 685 2053 C
ATOM 2332 CD1 TYR A1120 166.310 -12.004 147.634 1.00 78.05 C
ANISOU 2332 CD1 TYR A1120 8303 9000 12352 -406 702 2196 C
ATOM 2333 CD2 TYR A1120 167.446 -10.165 148.644 1.00 74.37 C
ANISOU 2333 CD2 TYR A1120 7989 8957 11311 -184 734 2137 C
ATOM 2334 CE1 TYR A1120 166.866 -12.871 148.572 1.00 80.45 C
ANISOU 2334 CE1 TYR A1120 8625 9238 12703 -351 775 2453 C
ATOM 2335 CE2 TYR A1120 168.005 -11.023 149.590 1.00 76.99 C
ANISOU 2335 CE2 TYR A1120 8334 9270 11650 -128 792 2380 C
ATOM 2336 CZ TYR A1120 167.722 -12.379 149.543 1.00 86.55 C
ANISOU 2336 CZ TYR A1120 9480 10230 13176 -205 816 2556 C
ATOM 2337 OH TYR A1120 168.274 -13.235 150.465 1.00 89.70 O
ANISOU 2337 OH TYR A1120 9885 10596 13600 -136 877 2837 O
ATOM 2338 N PHE A1121 165.761 -7.583 144.180 1.00 64.02 N
ANISOU 2338 N PHE A1121 6598 7667 10058 -359 397 1333 N
ATOM 2339 CA PHE A1121 164.949 -6.802 143.258 1.00 62.96 C
ANISOU 2339 CA PHE A1121 6392 7609 9919 -384 334 1224 C
ATOM 2340 C PHE A1121 165.682 -5.508 142.870 1.00 64.59 C
ANISOU 2340 C PHE A1121 6702 7927 9913 -286 303 1108 C
ATOM 2341 O PHE A1121 166.072 -4.727 143.742 1.00 63.00 O
ANISOU 2341 O PHE A1121 6561 7812 9565 -197 386 1151 O
ATOM 2342 CB PHE A1121 163.582 -6.499 143.902 1.00 65.75 C
ANISOU 2342 CB PHE A1121 6601 8049 10331 -400 433 1363 C
ATOM 2343 CG PHE A1121 162.568 -5.823 143.013 1.00 67.21 C
ANISOU 2343 CG PHE A1121 6669 8314 10553 -422 367 1291 C
ATOM 2344 CD1 PHE A1121 161.855 -6.548 142.066 1.00 71.26 C
ANISOU 2344 CD1 PHE A1121 7062 8765 11250 -547 257 1226 C
ATOM 2345 CD2 PHE A1121 162.292 -4.469 143.153 1.00 68.45 C
ANISOU 2345 CD2 PHE A1121 6824 8610 10575 -315 413 1288 C
ATOM 2346 CE1 PHE A1121 160.910 -5.923 141.250 1.00 72.57 C
ANISOU 2346 CE1 PHE A1121 7100 9042 11430 -558 180 1175 C
ATOM 2347 CE2 PHE A1121 161.341 -3.847 142.342 1.00 71.62 C
ANISOU 2347 CE2 PHE A1121 7104 9089 11021 -315 351 1257 C
ATOM 2348 CZ PHE A1121 160.658 -4.577 141.394 1.00 70.82 C
ANISOU 2348 CZ PHE A1121 6876 8961 11071 -434 230 1210 C
ATOM 2349 N GLU A1122 165.896 -5.317 141.554 1.00 61.14 N
ANISOU 2349 N GLU A1122 6280 7490 9461 -307 183 959 N
ATOM 2350 CA GLU A1122 166.536 -4.148 140.936 1.00 59.99 C
ANISOU 2350 CA GLU A1122 6210 7432 9151 -234 147 872 C
ATOM 2351 C GLU A1122 165.993 -3.985 139.511 1.00 64.27 C
ANISOU 2351 C GLU A1122 6684 8027 9706 -273 30 781 C
ATOM 2352 O GLU A1122 166.522 -4.610 138.587 1.00 64.17 O
ANISOU 2352 O GLU A1122 6702 7990 9690 -312 -62 659 O
ATOM 2353 CB GLU A1122 168.077 -4.257 140.932 1.00 60.53 C
ANISOU 2353 CB GLU A1122 6412 7467 9119 -193 135 802 C
ATOM 2354 CG GLU A1122 168.789 -3.470 142.026 1.00 72.17 C
ANISOU 2354 CG GLU A1122 7962 8991 10467 -113 222 849 C
ATOM 2355 CD GLU A1122 168.699 -1.954 142.023 1.00 98.40 C
ANISOU 2355 CD GLU A1122 11299 12392 13695 -52 255 830 C
ATOM 2356 OE1 GLU A1122 168.799 -1.359 143.120 1.00 99.17 O
ANISOU 2356 OE1 GLU A1122 11422 12531 13727 1 340 859 O
ATOM 2357 OE2 GLU A1122 168.563 -1.357 140.931 1.00 94.25 O
ANISOU 2357 OE2 GLU A1122 10760 11889 13162 -53 197 786 O
ATOM 2358 N PRO A1123 164.913 -3.195 139.307 1.00 61.13 N
ANISOU 2358 N PRO A1123 6184 7722 9320 -254 28 837 N
ATOM 2359 CA PRO A1123 164.355 -3.062 137.948 1.00 61.80 C
ANISOU 2359 CA PRO A1123 6186 7900 9396 -283 -100 772 C
ATOM 2360 C PRO A1123 165.237 -2.253 137.004 1.00 65.20 C
ANISOU 2360 C PRO A1123 6707 8410 9658 -218 -151 718 C
ATOM 2361 O PRO A1123 165.161 -2.458 135.792 1.00 65.75 O
ANISOU 2361 O PRO A1123 6740 8572 9671 -247 -268 635 O
ATOM 2362 CB PRO A1123 163.008 -2.360 138.160 1.00 64.32 C
ANISOU 2362 CB PRO A1123 6359 8301 9780 -253 -72 885 C
ATOM 2363 CG PRO A1123 162.838 -2.202 139.613 1.00 68.34 C
ANISOU 2363 CG PRO A1123 6877 8757 10334 -214 83 988 C
ATOM 2364 CD PRO A1123 164.146 -2.401 140.285 1.00 62.74 C
ANISOU 2364 CD PRO A1123 6331 7967 9541 -192 143 958 C
ATOM 2365 N PHE A1124 166.054 -1.337 137.546 1.00 60.81 N
ANISOU 2365 N PHE A1124 6255 7830 9020 -137 -62 763 N
ATOM 2366 CA PHE A1124 166.932 -0.490 136.744 1.00 60.25 C
ANISOU 2366 CA PHE A1124 6259 7817 8817 -84 -85 747 C
ATOM 2367 C PHE A1124 168.394 -0.851 136.987 1.00 64.18 C
ANISOU 2367 C PHE A1124 6881 8252 9252 -89 -55 670 C
ATOM 2368 O PHE A1124 168.847 -0.880 138.132 1.00 62.94 O
ANISOU 2368 O PHE A1124 6778 8017 9118 -74 25 686 O
ATOM 2369 CB PHE A1124 166.675 1.000 137.039 1.00 61.75 C
ANISOU 2369 CB PHE A1124 6444 8011 9006 6 -12 859 C
ATOM 2370 CG PHE A1124 165.218 1.400 137.096 1.00 64.21 C
ANISOU 2370 CG PHE A1124 6619 8368 9409 38 -12 952 C
ATOM 2371 CD1 PHE A1124 164.432 1.400 135.948 1.00 68.40 C
ANISOU 2371 CD1 PHE A1124 7037 9026 9924 34 -125 986 C
ATOM 2372 CD2 PHE A1124 164.633 1.785 138.296 1.00 66.34 C
ANISOU 2372 CD2 PHE A1124 6859 8580 9767 82 101 1002 C
ATOM 2373 CE1 PHE A1124 163.090 1.781 135.998 1.00 70.43 C
ANISOU 2373 CE1 PHE A1124 7144 9339 10276 73 -131 1083 C
ATOM 2374 CE2 PHE A1124 163.289 2.164 138.346 1.00 70.30 C
ANISOU 2374 CE2 PHE A1124 7215 9132 10364 126 113 1090 C
ATOM 2375 CZ PHE A1124 162.527 2.162 137.197 1.00 69.55 C
ANISOU 2375 CZ PHE A1124 6999 9151 10276 121 -5 1137 C
ATOM 2376 N GLY A1125 169.118 -1.110 135.902 1.00 61.93 N
ANISOU 2376 N GLY A1125 6627 8031 8872 -99 -121 588 N
ATOM 2377 CA GLY A1125 170.530 -1.475 135.947 1.00 61.42 C
ANISOU 2377 CA GLY A1125 6655 7931 8750 -94 -98 510 C
ATOM 2378 C GLY A1125 171.475 -0.337 136.275 1.00 65.44 C
ANISOU 2378 C GLY A1125 7228 8436 9200 -46 -25 566 C
ATOM 2379 O GLY A1125 172.694 -0.523 136.216 1.00 64.82 O
ANISOU 2379 O GLY A1125 7204 8356 9070 -42 -9 510 O
ATOM 2380 N LEU A1126 170.919 0.840 136.651 1.00 62.38 N
ANISOU 2380 N LEU A1126 6822 8036 8844 -11 24 668 N
ATOM 2381 CA LEU A1126 171.639 2.070 136.993 1.00 61.79 C
ANISOU 2381 CA LEU A1126 6794 7921 8763 22 94 711 C
ATOM 2382 C LEU A1126 172.738 1.840 138.044 1.00 64.84 C
ANISOU 2382 C LEU A1126 7244 8247 9145 11 140 640 C
ATOM 2383 O LEU A1126 173.819 2.397 137.883 1.00 64.43 O
ANISOU 2383 O LEU A1126 7225 8195 9062 6 162 625 O
ATOM 2384 CB LEU A1126 170.662 3.161 137.469 1.00 62.24 C
ANISOU 2384 CB LEU A1126 6813 7929 8906 69 146 799 C
ATOM 2385 CG LEU A1126 171.207 4.595 137.495 1.00 67.24 C
ANISOU 2385 CG LEU A1126 7476 8492 9579 101 210 847 C
ATOM 2386 CD1 LEU A1126 171.405 5.140 136.099 1.00 68.10 C
ANISOU 2386 CD1 LEU A1126 7562 8668 9646 113 179 952 C
ATOM 2387 CD2 LEU A1126 170.295 5.508 138.267 1.00 70.37 C
ANISOU 2387 CD2 LEU A1126 7844 8802 10090 160 278 882 C
ATOM 2388 N VAL A1127 172.481 1.009 139.083 1.00 61.14 N
ANISOU 2388 N VAL A1127 6781 7745 8706 5 152 614 N
ATOM 2389 CA VAL A1127 173.463 0.673 140.131 1.00 60.46 C
ANISOU 2389 CA VAL A1127 6741 7640 8592 8 179 569 C
ATOM 2390 C VAL A1127 174.728 0.078 139.499 1.00 63.39 C
ANISOU 2390 C VAL A1127 7133 8034 8917 -4 140 510 C
ATOM 2391 O VAL A1127 175.833 0.490 139.852 1.00 63.10 O
ANISOU 2391 O VAL A1127 7118 8010 8846 0 157 477 O
ATOM 2392 CB VAL A1127 172.912 -0.256 141.247 1.00 64.84 C
ANISOU 2392 CB VAL A1127 7285 8178 9174 13 199 600 C
ATOM 2393 CG1 VAL A1127 172.202 0.542 142.324 1.00 65.08 C
ANISOU 2393 CG1 VAL A1127 7304 8221 9202 45 273 630 C
ATOM 2394 CG2 VAL A1127 172.004 -1.353 140.696 1.00 65.09 C
ANISOU 2394 CG2 VAL A1127 7267 8183 9282 -21 158 628 C
ATOM 2395 N ALA A1128 174.555 -0.856 138.540 1.00 59.29 N
ANISOU 2395 N ALA A1128 6596 7528 8402 -18 88 480 N
ATOM 2396 CA ALA A1128 175.638 -1.502 137.805 1.00 58.69 C
ANISOU 2396 CA ALA A1128 6531 7484 8286 -12 61 402 C
ATOM 2397 C ALA A1128 176.258 -0.530 136.810 1.00 61.23 C
ANISOU 2397 C ALA A1128 6847 7891 8526 -11 75 407 C
ATOM 2398 O ALA A1128 177.483 -0.458 136.731 1.00 60.87 O
ANISOU 2398 O ALA A1128 6806 7877 8445 -3 96 375 O
ATOM 2399 CB ALA A1128 175.118 -2.736 137.084 1.00 60.17 C
ANISOU 2399 CB ALA A1128 6697 7652 8513 -27 5 332 C
ATOM 2400 N LEU A1129 175.409 0.234 136.074 1.00 56.95 N
ANISOU 2400 N LEU A1129 6282 7394 7961 -17 67 472 N
ATOM 2401 CA LEU A1129 175.803 1.234 135.074 1.00 56.45 C
ANISOU 2401 CA LEU A1129 6204 7417 7827 -13 88 537 C
ATOM 2402 C LEU A1129 176.745 2.276 135.662 1.00 59.63 C
ANISOU 2402 C LEU A1129 6621 7764 8271 -25 156 577 C
ATOM 2403 O LEU A1129 177.778 2.552 135.057 1.00 59.67 O
ANISOU 2403 O LEU A1129 6611 7831 8228 -35 186 586 O
ATOM 2404 CB LEU A1129 174.571 1.935 134.473 1.00 56.91 C
ANISOU 2404 CB LEU A1129 6225 7514 7883 0 66 644 C
ATOM 2405 CG LEU A1129 173.702 1.133 133.508 1.00 61.99 C
ANISOU 2405 CG LEU A1129 6826 8272 8456 1 -20 603 C
ATOM 2406 CD1 LEU A1129 172.456 1.908 133.140 1.00 62.64 C
ANISOU 2406 CD1 LEU A1129 6851 8397 8553 24 -48 731 C
ATOM 2407 CD2 LEU A1129 174.461 0.760 132.257 1.00 65.11 C
ANISOU 2407 CD2 LEU A1129 7215 8827 8696 9 -41 543 C
ATOM 2408 N GLU A1130 176.405 2.822 136.853 1.00 55.71 N
ANISOU 2408 N GLU A1130 6142 7162 7864 -28 183 584 N
ATOM 2409 CA GLU A1130 177.195 3.816 137.590 1.00 55.61 C
ANISOU 2409 CA GLU A1130 6139 7081 7912 -53 234 574 C
ATOM 2410 C GLU A1130 178.599 3.289 137.901 1.00 60.12 C
ANISOU 2410 C GLU A1130 6703 7693 8446 -73 228 492 C
ATOM 2411 O GLU A1130 179.575 4.007 137.699 1.00 60.24 O
ANISOU 2411 O GLU A1130 6691 7711 8486 -110 260 498 O
ATOM 2412 CB GLU A1130 176.484 4.219 138.891 1.00 56.79 C
ANISOU 2412 CB GLU A1130 6307 7143 8127 -39 255 542 C
ATOM 2413 CG GLU A1130 175.263 5.103 138.689 1.00 66.67 C
ANISOU 2413 CG GLU A1130 7545 8330 9455 -8 284 625 C
ATOM 2414 CD GLU A1130 174.415 5.363 139.922 1.00 85.13 C
ANISOU 2414 CD GLU A1130 9891 10609 11844 25 319 580 C
ATOM 2415 OE1 GLU A1130 173.613 6.324 139.889 1.00 81.17 O
ANISOU 2415 OE1 GLU A1130 9372 10032 11438 62 362 629 O
ATOM 2416 OE2 GLU A1130 174.545 4.612 140.916 1.00 77.00 O
ANISOU 2416 OE2 GLU A1130 8879 9619 10758 26 312 508 O
ATOM 2417 N ALA A1131 178.690 2.024 138.357 1.00 56.98 N
ANISOU 2417 N ALA A1131 6316 7323 8010 -46 188 432 N
ATOM 2418 CA ALA A1131 179.934 1.336 138.702 1.00 56.99 C
ANISOU 2418 CA ALA A1131 6299 7369 7985 -37 173 369 C
ATOM 2419 C ALA A1131 180.763 1.016 137.455 1.00 61.85 C
ANISOU 2419 C ALA A1131 6879 8067 8555 -31 183 357 C
ATOM 2420 O ALA A1131 181.965 1.284 137.442 1.00 61.92 O
ANISOU 2420 O ALA A1131 6841 8123 8562 -46 204 338 O
ATOM 2421 CB ALA A1131 179.623 0.056 139.467 1.00 57.44 C
ANISOU 2421 CB ALA A1131 6375 7408 8043 6 137 349 C
ATOM 2422 N MET A1132 180.112 0.476 136.402 1.00 58.86 N
ANISOU 2422 N MET A1132 6509 7726 8131 -10 168 358 N
ATOM 2423 CA MET A1132 180.727 0.084 135.130 1.00 59.46 C
ANISOU 2423 CA MET A1132 6554 7916 8123 11 182 323 C
ATOM 2424 C MET A1132 181.404 1.253 134.409 1.00 64.55 C
ANISOU 2424 C MET A1132 7155 8642 8729 -21 246 410 C
ATOM 2425 O MET A1132 182.426 1.037 133.761 1.00 65.22 O
ANISOU 2425 O MET A1132 7192 8834 8756 -6 285 383 O
ATOM 2426 CB MET A1132 179.687 -0.557 134.214 1.00 62.18 C
ANISOU 2426 CB MET A1132 6912 8302 8410 29 139 287 C
ATOM 2427 CG MET A1132 179.381 -1.982 134.587 1.00 65.92 C
ANISOU 2427 CG MET A1132 7405 8697 8944 56 89 177 C
ATOM 2428 SD MET A1132 177.766 -2.568 134.035 1.00 70.61 S
ANISOU 2428 SD MET A1132 8005 9277 9545 35 16 137 S
ATOM 2429 CE MET A1132 178.115 -2.891 132.342 1.00 68.66 C
ANISOU 2429 CE MET A1132 7731 9219 9139 61 3 20 C
ATOM 2430 N CYS A1133 180.850 2.479 134.541 1.00 61.38 N
ANISOU 2430 N CYS A1133 6762 8180 8379 -62 269 521 N
ATOM 2431 CA CYS A1133 181.363 3.731 133.966 1.00 62.02 C
ANISOU 2431 CA CYS A1133 6801 8284 8481 -105 339 646 C
ATOM 2432 C CYS A1133 182.783 4.014 134.425 1.00 65.42 C
ANISOU 2432 C CYS A1133 7173 8708 8973 -151 381 613 C
ATOM 2433 O CYS A1133 183.581 4.556 133.660 1.00 65.90 O
ANISOU 2433 O CYS A1133 7170 8846 9023 -182 450 696 O
ATOM 2434 CB CYS A1133 180.452 4.894 134.342 1.00 62.61 C
ANISOU 2434 CB CYS A1133 6899 8224 8666 -128 351 747 C
ATOM 2435 SG CYS A1133 178.983 5.054 133.306 1.00 67.25 S
ANISOU 2435 SG CYS A1133 7497 8874 9180 -75 323 875 S
ATOM 2436 N LEU A1134 183.070 3.695 135.696 1.00 61.05 N
ANISOU 2436 N LEU A1134 6631 8081 8484 -159 339 506 N
ATOM 2437 CA LEU A1134 184.345 3.970 136.344 1.00 61.07 C
ANISOU 2437 CA LEU A1134 6564 8088 8552 -208 349 454 C
ATOM 2438 C LEU A1134 185.238 2.716 136.443 1.00 63.96 C
ANISOU 2438 C LEU A1134 6887 8558 8855 -148 321 366 C
ATOM 2439 O LEU A1134 186.217 2.716 137.187 1.00 63.68 O
ANISOU 2439 O LEU A1134 6785 8546 8864 -168 301 311 O
ATOM 2440 CB LEU A1134 184.078 4.599 137.721 1.00 60.85 C
ANISOU 2440 CB LEU A1134 6563 7939 8618 -250 313 392 C
ATOM 2441 CG LEU A1134 183.325 5.931 137.638 1.00 65.82 C
ANISOU 2441 CG LEU A1134 7221 8433 9355 -300 356 464 C
ATOM 2442 CD1 LEU A1134 182.165 5.968 138.571 1.00 65.35 C
ANISOU 2442 CD1 LEU A1134 7237 8285 9308 -265 323 413 C
ATOM 2443 CD2 LEU A1134 184.242 7.103 137.833 1.00 69.57 C
ANISOU 2443 CD2 LEU A1134 7624 8833 9975 -404 396 457 C
ATOM 2444 N GLY A1135 184.929 1.705 135.631 1.00 59.99 N
ANISOU 2444 N GLY A1135 6410 8123 8262 -72 319 346 N
ATOM 2445 CA GLY A1135 185.710 0.477 135.520 1.00 59.96 C
ANISOU 2445 CA GLY A1135 6365 8192 8224 6 309 258 C
ATOM 2446 C GLY A1135 185.384 -0.663 136.460 1.00 62.74 C
ANISOU 2446 C GLY A1135 6762 8467 8610 72 238 193 C
ATOM 2447 O GLY A1135 185.922 -1.758 136.288 1.00 62.92 O
ANISOU 2447 O GLY A1135 6756 8516 8634 154 233 127 O
ATOM 2448 N ALA A1136 184.528 -0.431 137.468 1.00 58.14 N
ANISOU 2448 N ALA A1136 6242 7787 8062 46 193 219 N
ATOM 2449 CA ALA A1136 184.161 -1.474 138.426 1.00 57.44 C
ANISOU 2449 CA ALA A1136 6188 7632 8003 105 139 204 C
ATOM 2450 C ALA A1136 183.369 -2.595 137.742 1.00 60.85 C
ANISOU 2450 C ALA A1136 6667 8007 8446 154 130 170 C
ATOM 2451 O ALA A1136 182.361 -2.328 137.082 1.00 59.87 O
ANISOU 2451 O ALA A1136 6584 7867 8297 119 133 177 O
ATOM 2452 CB ALA A1136 183.363 -0.881 139.569 1.00 57.59 C
ANISOU 2452 CB ALA A1136 6255 7595 8031 66 116 244 C
ATOM 2453 N ILE A1137 183.874 -3.838 137.851 1.00 57.78 N
ANISOU 2453 N ILE A1137 6259 7587 8110 235 115 127 N
ATOM 2454 CA ILE A1137 183.245 -5.021 137.258 1.00 57.76 C
ANISOU 2454 CA ILE A1137 6289 7493 8162 277 103 57 C
ATOM 2455 C ILE A1137 182.143 -5.489 138.216 1.00 61.95 C
ANISOU 2455 C ILE A1137 6871 7893 8774 261 67 132 C
ATOM 2456 O ILE A1137 182.448 -5.893 139.337 1.00 62.25 O
ANISOU 2456 O ILE A1137 6900 7893 8861 302 53 211 O
ATOM 2457 CB ILE A1137 184.278 -6.135 136.941 1.00 61.66 C
ANISOU 2457 CB ILE A1137 6735 7974 8721 381 116 -29 C
ATOM 2458 CG1 ILE A1137 185.385 -5.644 135.985 1.00 62.23 C
ANISOU 2458 CG1 ILE A1137 6735 8209 8700 400 172 -93 C
ATOM 2459 CG2 ILE A1137 183.592 -7.396 136.415 1.00 62.87 C
ANISOU 2459 CG2 ILE A1137 6924 7988 8975 416 100 -132 C
ATOM 2460 CD1 ILE A1137 186.771 -6.026 136.423 1.00 66.37 C
ANISOU 2460 CD1 ILE A1137 7167 8776 9276 487 187 -91 C
ATOM 2461 N PRO A1138 180.857 -5.429 137.819 1.00 58.08 N
ANISOU 2461 N PRO A1138 6420 7356 8290 204 54 125 N
ATOM 2462 CA PRO A1138 179.798 -5.812 138.760 1.00 57.58 C
ANISOU 2462 CA PRO A1138 6384 7185 8310 181 39 215 C
ATOM 2463 C PRO A1138 179.587 -7.319 138.902 1.00 62.23 C
ANISOU 2463 C PRO A1138 6971 7613 9060 217 23 202 C
ATOM 2464 O PRO A1138 179.688 -8.072 137.932 1.00 62.73 O
ANISOU 2464 O PRO A1138 7028 7623 9184 233 11 67 O
ATOM 2465 CB PRO A1138 178.552 -5.134 138.190 1.00 58.80 C
ANISOU 2465 CB PRO A1138 6552 7362 8426 108 30 213 C
ATOM 2466 CG PRO A1138 178.825 -4.977 136.755 1.00 63.45 C
ANISOU 2466 CG PRO A1138 7129 8039 8940 105 23 101 C
ATOM 2467 CD PRO A1138 180.300 -4.947 136.540 1.00 59.32 C
ANISOU 2467 CD PRO A1138 6583 7587 8369 160 53 58 C
ATOM 2468 N ILE A1139 179.302 -7.739 140.146 1.00 58.57 N
ANISOU 2468 N ILE A1139 6510 7076 8667 233 31 346 N
ATOM 2469 CA ILE A1139 178.942 -9.100 140.546 1.00 59.41 C
ANISOU 2469 CA ILE A1139 6609 6997 8965 257 31 407 C
ATOM 2470 C ILE A1139 177.523 -8.957 141.076 1.00 63.27 C
ANISOU 2470 C ILE A1139 7102 7451 9487 176 44 512 C
ATOM 2471 O ILE A1139 177.318 -8.719 142.270 1.00 62.97 O
ANISOU 2471 O ILE A1139 7062 7460 9403 189 74 677 O
ATOM 2472 CB ILE A1139 179.930 -9.775 141.549 1.00 63.07 C
ANISOU 2472 CB ILE A1139 7052 7430 9482 363 40 537 C
ATOM 2473 CG1 ILE A1139 181.384 -9.735 141.044 1.00 63.20 C
ANISOU 2473 CG1 ILE A1139 7038 7522 9453 448 31 434 C
ATOM 2474 CG2 ILE A1139 179.494 -11.218 141.855 1.00 65.41 C
ANISOU 2474 CG2 ILE A1139 7338 7490 10024 387 51 626 C
ATOM 2475 CD1 ILE A1139 182.388 -9.905 142.122 1.00 69.56 C
ANISOU 2475 CD1 ILE A1139 7802 8394 10234 547 23 575 C
ATOM 2476 N ALA A1140 176.549 -8.995 140.161 1.00 59.59 N
ANISOU 2476 N ALA A1140 6628 6942 9073 96 20 409 N
ATOM 2477 CA ALA A1140 175.156 -8.775 140.511 1.00 59.05 C
ANISOU 2477 CA ALA A1140 6536 6861 9040 16 32 495 C
ATOM 2478 C ALA A1140 174.272 -9.991 140.295 1.00 63.54 C
ANISOU 2478 C ALA A1140 7064 7235 9844 -49 17 484 C
ATOM 2479 O ALA A1140 174.698 -10.982 139.704 1.00 64.22 O
ANISOU 2479 O ALA A1140 7150 7178 10072 -36 -11 366 O
ATOM 2480 CB ALA A1140 174.611 -7.604 139.717 1.00 58.83 C
ANISOU 2480 CB ALA A1140 6505 6974 8876 -30 9 415 C
ATOM 2481 N SER A1141 173.029 -9.904 140.799 1.00 59.71 N
ANISOU 2481 N SER A1141 6532 6736 9419 -121 41 600 N
ATOM 2482 CA SER A1141 172.013 -10.935 140.657 1.00 60.72 C
ANISOU 2482 CA SER A1141 6594 6684 9793 -215 30 607 C
ATOM 2483 C SER A1141 171.396 -10.850 139.274 1.00 64.45 C
ANISOU 2483 C SER A1141 7030 7183 10276 -296 -59 383 C
ATOM 2484 O SER A1141 171.271 -9.751 138.731 1.00 62.88 O
ANISOU 2484 O SER A1141 6838 7176 9879 -287 -87 325 O
ATOM 2485 CB SER A1141 170.930 -10.772 141.717 1.00 63.91 C
ANISOU 2485 CB SER A1141 6939 7109 10237 -261 101 827 C
ATOM 2486 OG SER A1141 171.462 -10.621 143.022 1.00 71.24 O
ANISOU 2486 OG SER A1141 7899 8097 11070 -176 181 1032 O
ATOM 2487 N ALA A1142 170.984 -11.996 138.709 1.00 62.49 N
ANISOU 2487 N ALA A1142 6735 6746 10263 -373 -106 258 N
ATOM 2488 CA ALA A1142 170.340 -12.038 137.399 1.00 63.07 C
ANISOU 2488 CA ALA A1142 6757 6867 10340 -458 -210 19 C
ATOM 2489 C ALA A1142 168.856 -11.626 137.536 1.00 67.44 C
ANISOU 2489 C ALA A1142 7203 7493 10930 -563 -228 109 C
ATOM 2490 O ALA A1142 167.948 -12.396 137.204 1.00 69.21 O
ANISOU 2490 O ALA A1142 7329 7597 11369 -685 -282 28 O
ATOM 2491 CB ALA A1142 170.481 -13.429 136.792 1.00 66.14 C
ANISOU 2491 CB ALA A1142 7129 7018 10983 -506 -259 -188 C
ATOM 2492 N VAL A1143 168.626 -10.395 138.047 1.00 62.16 N
ANISOU 2492 N VAL A1143 6539 7012 10066 -514 -179 268 N
ATOM 2493 CA VAL A1143 167.301 -9.813 138.293 1.00 62.03 C
ANISOU 2493 CA VAL A1143 6416 7091 10059 -575 -172 380 C
ATOM 2494 C VAL A1143 167.171 -8.458 137.585 1.00 66.02 C
ANISOU 2494 C VAL A1143 6926 7838 10322 -523 -217 338 C
ATOM 2495 O VAL A1143 168.139 -7.693 137.525 1.00 64.50 O
ANISOU 2495 O VAL A1143 6833 7735 9940 -427 -192 336 O
ATOM 2496 CB VAL A1143 166.945 -9.689 139.807 1.00 65.24 C
ANISOU 2496 CB VAL A1143 6803 7469 10514 -554 -39 648 C
ATOM 2497 CG1 VAL A1143 166.854 -11.057 140.476 1.00 66.74 C
ANISOU 2497 CG1 VAL A1143 6960 7423 10976 -617 10 748 C
ATOM 2498 CG2 VAL A1143 167.909 -8.773 140.564 1.00 63.09 C
ANISOU 2498 CG2 VAL A1143 6643 7309 10019 -424 38 744 C
ATOM 2499 N GLY A1144 165.970 -8.194 137.069 1.00 64.03 N
ANISOU 2499 N GLY A1144 6550 7679 10098 -589 -282 321 N
ATOM 2500 CA GLY A1144 165.588 -6.966 136.378 1.00 63.58 C
ANISOU 2500 CA GLY A1144 6462 7841 9855 -540 -330 325 C
ATOM 2501 C GLY A1144 166.643 -6.329 135.496 1.00 67.21 C
ANISOU 2501 C GLY A1144 7026 8422 10090 -457 -367 229 C
ATOM 2502 O GLY A1144 167.165 -6.973 134.582 1.00 67.77 O
ANISOU 2502 O GLY A1144 7124 8499 10128 -479 -444 43 O
ATOM 2503 N GLY A1145 166.957 -5.070 135.805 1.00 62.48 N
ANISOU 2503 N GLY A1145 6479 7913 9348 -363 -300 354 N
ATOM 2504 CA GLY A1145 167.924 -4.247 135.086 1.00 61.41 C
ANISOU 2504 CA GLY A1145 6426 7893 9015 -287 -307 325 C
ATOM 2505 C GLY A1145 169.355 -4.738 135.128 1.00 64.88 C
ANISOU 2505 C GLY A1145 6978 8264 9412 -259 -274 236 C
ATOM 2506 O GLY A1145 170.117 -4.467 134.200 1.00 64.79 O
ANISOU 2506 O GLY A1145 7005 8359 9252 -223 -302 158 O
ATOM 2507 N LEU A1146 169.742 -5.441 136.211 1.00 60.86 N
ANISOU 2507 N LEU A1146 6508 7593 9024 -265 -209 269 N
ATOM 2508 CA LEU A1146 171.090 -5.999 136.377 1.00 59.94 C
ANISOU 2508 CA LEU A1146 6477 7403 8896 -225 -178 204 C
ATOM 2509 C LEU A1146 171.325 -7.112 135.359 1.00 64.54 C
ANISOU 2509 C LEU A1146 7050 7947 9526 -256 -254 1 C
ATOM 2510 O LEU A1146 172.395 -7.176 134.755 1.00 64.06 O
ANISOU 2510 O LEU A1146 7039 7935 9365 -204 -255 -105 O
ATOM 2511 CB LEU A1146 171.302 -6.537 137.807 1.00 59.69 C
ANISOU 2511 CB LEU A1146 6469 7227 8985 -213 -101 322 C
ATOM 2512 CG LEU A1146 171.187 -5.554 138.973 1.00 63.22 C
ANISOU 2512 CG LEU A1146 6931 7722 9366 -172 -18 484 C
ATOM 2513 CD1 LEU A1146 171.078 -6.299 140.290 1.00 63.80 C
ANISOU 2513 CD1 LEU A1146 7001 7695 9547 -171 47 610 C
ATOM 2514 CD2 LEU A1146 172.368 -4.601 139.013 1.00 64.43 C
ANISOU 2514 CD2 LEU A1146 7156 7960 9367 -105 10 473 C
ATOM 2515 N ARG A1147 170.300 -7.967 135.159 1.00 61.99 N
ANISOU 2515 N ARG A1147 6649 7541 9364 -345 -316 -68 N
ATOM 2516 CA ARG A1147 170.276 -9.092 134.224 1.00 63.50 C
ANISOU 2516 CA ARG A1147 6814 7670 9643 -397 -400 -306 C
ATOM 2517 C ARG A1147 170.384 -8.597 132.779 1.00 68.23 C
ANISOU 2517 C ARG A1147 7403 8510 10012 -378 -484 -467 C
ATOM 2518 O ARG A1147 171.041 -9.236 131.957 1.00 69.06 O
ANISOU 2518 O ARG A1147 7533 8630 10075 -358 -518 -684 O
ATOM 2519 CB ARG A1147 168.965 -9.870 134.418 1.00 64.90 C
ANISOU 2519 CB ARG A1147 6882 7720 10055 -522 -450 -318 C
ATOM 2520 CG ARG A1147 168.964 -11.305 133.902 1.00 77.37 C
ANISOU 2520 CG ARG A1147 8436 9113 11848 -595 -514 -555 C
ATOM 2521 CD ARG A1147 167.551 -11.800 133.618 1.00 91.46 C
ANISOU 2521 CD ARG A1147 10079 10859 13811 -744 -607 -628 C
ATOM 2522 NE ARG A1147 166.668 -11.705 134.786 1.00101.59 N
ANISOU 2522 NE ARG A1147 11291 12049 15262 -800 -534 -366 N
ATOM 2523 CZ ARG A1147 165.339 -11.729 134.731 1.00117.73 C
ANISOU 2523 CZ ARG A1147 13187 14125 17422 -915 -590 -340 C
ATOM 2524 NH1 ARG A1147 164.716 -11.846 133.563 1.00108.19 N
ANISOU 2524 NH1 ARG A1147 11883 13046 16179 -994 -741 -567 N
ATOM 2525 NH2 ARG A1147 164.621 -11.630 135.843 1.00103.21 N
ANISOU 2525 NH2 ARG A1147 11279 12217 15719 -950 -496 -88 N
ATOM 2526 N ASP A1148 169.740 -7.454 132.486 1.00 64.60 N
ANISOU 2526 N ASP A1148 6899 8246 9398 -370 -509 -350 N
ATOM 2527 CA ASP A1148 169.684 -6.824 131.168 1.00 65.23 C
ANISOU 2527 CA ASP A1148 6953 8596 9237 -343 -587 -425 C
ATOM 2528 C ASP A1148 170.978 -6.087 130.797 1.00 68.10 C
ANISOU 2528 C ASP A1148 7402 9082 9390 -242 -516 -387 C
ATOM 2529 O ASP A1148 171.408 -6.167 129.647 1.00 68.72 O
ANISOU 2529 O ASP A1148 7482 9343 9286 -213 -559 -531 O
ATOM 2530 CB ASP A1148 168.505 -5.835 131.109 1.00 67.04 C
ANISOU 2530 CB ASP A1148 7091 8965 9417 -353 -628 -257 C
ATOM 2531 CG ASP A1148 167.125 -6.441 131.287 1.00 79.25 C
ANISOU 2531 CG ASP A1148 8509 10453 11149 -458 -710 -288 C
ATOM 2532 OD1 ASP A1148 166.848 -7.492 130.663 1.00 81.74 O
ANISOU 2532 OD1 ASP A1148 8772 10751 11532 -540 -811 -518 O
ATOM 2533 OD2 ASP A1148 166.294 -5.824 131.984 1.00 85.52 O
ANISOU 2533 OD2 ASP A1148 9242 11232 12021 -460 -675 -97 O
ATOM 2534 N ILE A1149 171.577 -5.361 131.759 1.00 62.97 N
ANISOU 2534 N ILE A1149 6814 8351 8762 -194 -407 -202 N
ATOM 2535 CA ILE A1149 172.773 -4.540 131.564 1.00 61.85 C
ANISOU 2535 CA ILE A1149 6733 8302 8466 -119 -330 -135 C
ATOM 2536 C ILE A1149 174.058 -5.386 131.628 1.00 66.20 C
ANISOU 2536 C ILE A1149 7338 8773 9041 -83 -284 -271 C
ATOM 2537 O ILE A1149 174.950 -5.167 130.812 1.00 66.36 O
ANISOU 2537 O ILE A1149 7373 8941 8902 -33 -259 -329 O
ATOM 2538 CB ILE A1149 172.760 -3.354 132.590 1.00 63.22 C
ANISOU 2538 CB ILE A1149 6929 8416 8676 -97 -249 92 C
ATOM 2539 CG1 ILE A1149 172.099 -2.101 131.984 1.00 63.91 C
ANISOU 2539 CG1 ILE A1149 6972 8656 8655 -77 -266 235 C
ATOM 2540 CG2 ILE A1149 174.136 -2.996 133.166 1.00 62.96 C
ANISOU 2540 CG2 ILE A1149 6962 8333 8628 -54 -156 133 C
ATOM 2541 CD1 ILE A1149 170.601 -2.108 131.896 1.00 72.94 C
ANISOU 2541 CD1 ILE A1149 8028 9829 9857 -110 -343 271 C
ATOM 2542 N ILE A1150 174.164 -6.329 132.575 1.00 62.82 N
ANISOU 2542 N ILE A1150 6929 8125 8813 -97 -265 -301 N
ATOM 2543 CA ILE A1150 175.381 -7.130 132.710 1.00 62.97 C
ANISOU 2543 CA ILE A1150 6988 8055 8885 -42 -220 -403 C
ATOM 2544 C ILE A1150 175.351 -8.312 131.737 1.00 69.50 C
ANISOU 2544 C ILE A1150 7796 8865 9746 -47 -279 -669 C
ATOM 2545 O ILE A1150 174.351 -9.028 131.632 1.00 70.59 O
ANISOU 2545 O ILE A1150 7896 8907 10016 -121 -352 -764 O
ATOM 2546 CB ILE A1150 175.625 -7.571 134.181 1.00 65.24 C
ANISOU 2546 CB ILE A1150 7300 8129 9360 -31 -169 -281 C
ATOM 2547 CG1 ILE A1150 175.866 -6.341 135.072 1.00 63.91 C
ANISOU 2547 CG1 ILE A1150 7151 8016 9115 -14 -111 -79 C
ATOM 2548 CG2 ILE A1150 176.797 -8.554 134.304 1.00 66.69 C
ANISOU 2548 CG2 ILE A1150 7503 8203 9632 42 -136 -378 C
ATOM 2549 CD1 ILE A1150 175.317 -6.446 136.432 1.00 70.26 C
ANISOU 2549 CD1 ILE A1150 7957 8695 10042 -34 -85 66 C
ATOM 2550 N THR A1151 176.468 -8.479 131.016 1.00 66.75 N
ANISOU 2550 N THR A1151 7463 8616 9282 29 -243 -803 N
ATOM 2551 CA THR A1151 176.725 -9.559 130.067 1.00 68.76 C
ANISOU 2551 CA THR A1151 7707 8872 9546 55 -275 -1098 C
ATOM 2552 C THR A1151 177.937 -10.347 130.585 1.00 73.30 C
ANISOU 2552 C THR A1151 8307 9273 10271 147 -197 -1147 C
ATOM 2553 O THR A1151 178.514 -9.964 131.606 1.00 71.47 O
ANISOU 2553 O THR A1151 8091 8970 10093 180 -136 -940 O
ATOM 2554 CB THR A1151 176.932 -8.992 128.647 1.00 76.41 C
ANISOU 2554 CB THR A1151 8655 10174 10204 87 -289 -1211 C
ATOM 2555 OG1 THR A1151 178.029 -8.077 128.649 1.00 73.57 O
ANISOU 2555 OG1 THR A1151 8306 9957 9688 158 -188 -1058 O
ATOM 2556 CG2 THR A1151 175.680 -8.320 128.087 1.00 74.86 C
ANISOU 2556 CG2 THR A1151 8417 10158 9869 12 -385 -1156 C
ATOM 2557 N ASN A1152 178.322 -11.437 129.895 1.00 72.25 N
ANISOU 2557 N ASN A1152 8168 9078 10207 196 -203 -1428 N
ATOM 2558 CA ASN A1152 179.477 -12.269 130.258 1.00 72.86 C
ANISOU 2558 CA ASN A1152 8252 8987 10446 308 -128 -1493 C
ATOM 2559 C ASN A1152 180.777 -11.443 130.208 1.00 75.47 C
ANISOU 2559 C ASN A1152 8571 9522 10583 406 -35 -1381 C
ATOM 2560 O ASN A1152 181.669 -11.641 131.037 1.00 74.58 O
ANISOU 2560 O ASN A1152 8451 9294 10594 482 23 -1268 O
ATOM 2561 CB ASN A1152 179.565 -13.485 129.313 1.00 77.37 C
ANISOU 2561 CB ASN A1152 8812 9478 11108 348 -150 -1866 C
ATOM 2562 CG ASN A1152 180.775 -14.381 129.496 1.00106.43 C
ANISOU 2562 CG ASN A1152 12487 12989 14962 493 -66 -1969 C
ATOM 2563 OD1 ASN A1152 181.233 -14.651 130.615 1.00101.48 O
ANISOU 2563 OD1 ASN A1152 11863 12153 14542 542 -24 -1767 O
ATOM 2564 ND2 ASN A1152 181.301 -14.891 128.390 1.00101.53 N
ANISOU 2564 ND2 ASN A1152 11850 12471 14257 576 -40 -2293 N
ATOM 2565 N GLU A1153 180.843 -10.499 129.252 1.00 71.50 N
ANISOU 2565 N GLU A1153 8053 9332 9782 397 -24 -1391 N
ATOM 2566 CA GLU A1153 181.961 -9.597 128.970 1.00 70.49 C
ANISOU 2566 CA GLU A1153 7895 9436 9454 460 70 -1285 C
ATOM 2567 C GLU A1153 182.038 -8.407 129.930 1.00 70.90 C
ANISOU 2567 C GLU A1153 7950 9493 9495 409 91 -970 C
ATOM 2568 O GLU A1153 183.110 -7.816 130.077 1.00 69.98 O
ANISOU 2568 O GLU A1153 7796 9475 9317 452 169 -866 O
ATOM 2569 CB GLU A1153 181.834 -9.044 127.533 1.00 73.15 C
ANISOU 2569 CB GLU A1153 8209 10109 9477 460 75 -1385 C
ATOM 2570 CG GLU A1153 181.931 -10.078 126.422 1.00 86.38 C
ANISOU 2570 CG GLU A1153 9870 11865 11085 525 67 -1743 C
ATOM 2571 CD GLU A1153 180.700 -10.930 126.176 1.00106.67 C
ANISOU 2571 CD GLU A1153 12463 14306 13762 452 -60 -1963 C
ATOM 2572 OE1 GLU A1153 179.596 -10.361 126.009 1.00 98.93 O
ANISOU 2572 OE1 GLU A1153 11483 13420 12687 352 -150 -1873 O
ATOM 2573 OE2 GLU A1153 180.844 -12.173 126.138 1.00102.61 O
ANISOU 2573 OE2 GLU A1153 11953 13587 13447 495 -68 -2228 O
ATOM 2574 N THR A1154 180.902 -8.026 130.541 1.00 65.60 N
ANISOU 2574 N THR A1154 7311 8727 8885 314 24 -836 N
ATOM 2575 CA THR A1154 180.814 -6.837 131.390 1.00 62.99 C
ANISOU 2575 CA THR A1154 6988 8406 8538 264 41 -578 C
ATOM 2576 C THR A1154 180.500 -7.125 132.873 1.00 65.05 C
ANISOU 2576 C THR A1154 7275 8438 9004 242 21 -455 C
ATOM 2577 O THR A1154 180.152 -6.200 133.605 1.00 63.40 O
ANISOU 2577 O THR A1154 7078 8230 8783 194 24 -282 O
ATOM 2578 CB THR A1154 179.765 -5.881 130.816 1.00 69.01 C
ANISOU 2578 CB THR A1154 7754 9307 9159 193 1 -495 C
ATOM 2579 OG1 THR A1154 178.483 -6.505 130.875 1.00 67.37 O
ANISOU 2579 OG1 THR A1154 7557 8993 9047 138 -87 -564 O
ATOM 2580 CG2 THR A1154 180.081 -5.451 129.392 1.00 69.62 C
ANISOU 2580 CG2 THR A1154 7799 9660 8992 221 26 -555 C
ATOM 2581 N GLY A1155 180.644 -8.371 133.309 1.00 61.99 N
ANISOU 2581 N GLY A1155 6892 7862 8799 285 10 -538 N
ATOM 2582 CA GLY A1155 180.411 -8.727 134.703 1.00 60.95 C
ANISOU 2582 CA GLY A1155 6776 7541 8842 279 2 -390 C
ATOM 2583 C GLY A1155 180.057 -10.174 134.954 1.00 66.04 C
ANISOU 2583 C GLY A1155 7424 7945 9722 297 -21 -466 C
ATOM 2584 O GLY A1155 180.012 -10.984 134.022 1.00 67.32 O
ANISOU 2584 O GLY A1155 7580 8060 9938 313 -38 -683 O
ATOM 2585 N ILE A1156 179.815 -10.503 136.235 1.00 62.05 N
ANISOU 2585 N ILE A1156 6926 7288 9362 295 -18 -287 N
ATOM 2586 CA ILE A1156 179.459 -11.851 136.681 1.00 63.16 C
ANISOU 2586 CA ILE A1156 7063 7164 9770 307 -25 -283 C
ATOM 2587 C ILE A1156 178.038 -11.824 137.252 1.00 66.76 C
ANISOU 2587 C ILE A1156 7521 7536 10307 194 -48 -159 C
ATOM 2588 O ILE A1156 177.764 -11.065 138.181 1.00 64.94 O
ANISOU 2588 O ILE A1156 7296 7388 9989 173 -29 38 O
ATOM 2589 CB ILE A1156 180.496 -12.422 137.701 1.00 66.55 C
ANISOU 2589 CB ILE A1156 7476 7495 10313 426 12 -135 C
ATOM 2590 CG1 ILE A1156 181.934 -12.406 137.126 1.00 67.09 C
ANISOU 2590 CG1 ILE A1156 7514 7668 10307 545 40 -256 C
ATOM 2591 CG2 ILE A1156 180.110 -13.839 138.153 1.00 69.23 C
ANISOU 2591 CG2 ILE A1156 7809 7527 10967 444 16 -90 C
ATOM 2592 CD1 ILE A1156 183.037 -12.171 138.147 1.00 71.26 C
ANISOU 2592 CD1 ILE A1156 8004 8271 10800 642 59 -72 C
ATOM 2593 N LEU A1157 177.141 -12.648 136.687 1.00 65.08 N
ANISOU 2593 N LEU A1157 7293 7170 10266 119 -87 -293 N
ATOM 2594 CA LEU A1157 175.754 -12.757 137.141 1.00 65.13 C
ANISOU 2594 CA LEU A1157 7271 7088 10389 1 -105 -188 C
ATOM 2595 C LEU A1157 175.561 -14.008 137.992 1.00 71.55 C
ANISOU 2595 C LEU A1157 8064 7605 11517 0 -74 -63 C
ATOM 2596 O LEU A1157 176.072 -15.077 137.648 1.00 73.08 O
ANISOU 2596 O LEU A1157 8257 7596 11914 48 -74 -192 O
ATOM 2597 CB LEU A1157 174.766 -12.759 135.963 1.00 65.84 C
ANISOU 2597 CB LEU A1157 7326 7224 10465 -106 -183 -405 C
ATOM 2598 CG LEU A1157 174.506 -11.423 135.272 1.00 68.85 C
ANISOU 2598 CG LEU A1157 7708 7899 10552 -126 -215 -432 C
ATOM 2599 CD1 LEU A1157 173.851 -11.635 133.927 1.00 70.32 C
ANISOU 2599 CD1 LEU A1157 7855 8165 10700 -195 -307 -684 C
ATOM 2600 CD2 LEU A1157 173.649 -10.500 136.133 1.00 70.08 C
ANISOU 2600 CD2 LEU A1157 7845 8130 10651 -174 -193 -198 C
ATOM 2601 N VAL A1158 174.826 -13.869 139.106 1.00 68.39 N
ANISOU 2601 N VAL A1158 7641 7179 11163 -47 -35 196 N
ATOM 2602 CA VAL A1158 174.548 -14.971 140.032 1.00 70.34 C
ANISOU 2602 CA VAL A1158 7858 7168 11700 -54 13 392 C
ATOM 2603 C VAL A1158 173.064 -15.050 140.368 1.00 76.02 C
ANISOU 2603 C VAL A1158 8511 7830 12542 -199 23 504 C
ATOM 2604 O VAL A1158 172.325 -14.098 140.126 1.00 74.33 O
ANISOU 2604 O VAL A1158 8278 7812 12152 -265 -1 474 O
ATOM 2605 CB VAL A1158 175.395 -14.919 141.331 1.00 73.71 C
ANISOU 2605 CB VAL A1158 8306 7639 12061 71 78 675 C
ATOM 2606 CG1 VAL A1158 176.766 -15.527 141.106 1.00 74.37 C
ANISOU 2606 CG1 VAL A1158 8412 7635 12210 212 75 601 C
ATOM 2607 CG2 VAL A1158 175.494 -13.507 141.908 1.00 71.09 C
ANISOU 2607 CG2 VAL A1158 7998 7620 11393 93 92 777 C
ATOM 2608 N LYS A1159 172.634 -16.193 140.930 1.00 75.72 N
ANISOU 2608 N LYS A1159 8426 7515 12830 -243 65 650 N
ATOM 2609 CA LYS A1159 171.257 -16.408 141.361 1.00 77.05 C
ANISOU 2609 CA LYS A1159 8506 7608 13163 -386 95 797 C
ATOM 2610 C LYS A1159 171.012 -15.577 142.621 1.00 80.54 C
ANISOU 2610 C LYS A1159 8944 8272 13387 -345 181 1108 C
ATOM 2611 O LYS A1159 171.839 -15.600 143.539 1.00 80.14 O
ANISOU 2611 O LYS A1159 8937 8265 13249 -221 238 1311 O
ATOM 2612 CB LYS A1159 170.991 -17.907 141.608 1.00 82.78 C
ANISOU 2612 CB LYS A1159 9175 7945 14332 -446 131 885 C
ATOM 2613 CG LYS A1159 169.515 -18.291 141.573 1.00 96.69 C
ANISOU 2613 CG LYS A1159 10816 9582 16340 -641 133 918 C
ATOM 2614 CD LYS A1159 169.066 -18.922 142.882 1.00107.28 C
ANISOU 2614 CD LYS A1159 12091 10770 17899 -666 260 1328 C
ATOM 2615 CE LYS A1159 167.609 -19.306 142.847 1.00119.02 C
ANISOU 2615 CE LYS A1159 13432 12135 19654 -872 273 1372 C
ATOM 2616 N ALA A1160 169.909 -14.802 142.634 1.00 76.75 N
ANISOU 2616 N ALA A1160 8406 7956 12802 -436 185 1126 N
ATOM 2617 CA ALA A1160 169.523 -13.938 143.752 1.00 75.61 C
ANISOU 2617 CA ALA A1160 8248 8036 12445 -399 274 1368 C
ATOM 2618 C ALA A1160 169.163 -14.765 144.986 1.00 81.79 C
ANISOU 2618 C ALA A1160 8972 8701 13403 -407 390 1708 C
ATOM 2619 O ALA A1160 168.464 -15.779 144.877 1.00 83.60 O
ANISOU 2619 O ALA A1160 9116 8684 13966 -521 407 1766 O
ATOM 2620 CB ALA A1160 168.352 -13.055 143.352 1.00 75.54 C
ANISOU 2620 CB ALA A1160 8167 8187 12346 -489 255 1290 C
ATOM 2621 N GLY A1161 169.678 -14.338 146.136 1.00 78.01 N
ANISOU 2621 N GLY A1161 8534 8406 12699 -289 465 1929 N
ATOM 2622 CA GLY A1161 169.456 -15.004 147.414 1.00 80.02 C
ANISOU 2622 CA GLY A1161 8739 8628 13037 -264 586 2297 C
ATOM 2623 C GLY A1161 170.288 -16.252 147.627 1.00 85.99 C
ANISOU 2623 C GLY A1161 9515 9129 14029 -201 591 2440 C
ATOM 2624 O GLY A1161 170.024 -17.017 148.559 1.00 88.20 O
ANISOU 2624 O GLY A1161 9737 9320 14455 -195 692 2778 O
ATOM 2625 N ASP A1162 171.302 -16.463 146.768 1.00 81.72 N
ANISOU 2625 N ASP A1162 9046 8473 13533 -143 492 2201 N
ATOM 2626 CA ASP A1162 172.200 -17.609 146.844 1.00 83.41 C
ANISOU 2626 CA ASP A1162 9277 8427 13987 -56 490 2293 C
ATOM 2627 C ASP A1162 173.589 -17.141 147.311 1.00 85.69 C
ANISOU 2627 C ASP A1162 9639 8931 13989 131 462 2332 C
ATOM 2628 O ASP A1162 174.360 -16.607 146.505 1.00 83.55 O
ANISOU 2628 O ASP A1162 9424 8739 13580 176 378 2047 O
ATOM 2629 CB ASP A1162 172.273 -18.344 145.492 1.00 86.00 C
ANISOU 2629 CB ASP A1162 9610 8443 14624 -126 409 1970 C
ATOM 2630 CG ASP A1162 172.607 -19.817 145.605 1.00 98.72 C
ANISOU 2630 CG ASP A1162 11195 9657 16658 -96 442 2099 C
ATOM 2631 OD1 ASP A1162 173.696 -20.143 146.122 1.00 99.81 O
ANISOU 2631 OD1 ASP A1162 11369 9782 16774 74 457 2255 O
ATOM 2632 OD2 ASP A1162 171.791 -20.645 145.148 1.00106.97 O
ANISOU 2632 OD2 ASP A1162 12174 10393 18075 -241 447 2035 O
ATOM 2633 N PRO A1163 173.912 -17.297 148.620 1.00 82.94 N
ANISOU 2633 N PRO A1163 9274 8710 13529 240 530 2688 N
ATOM 2634 CA PRO A1163 175.225 -16.851 149.114 1.00 81.80 C
ANISOU 2634 CA PRO A1163 9174 8801 13105 411 485 2721 C
ATOM 2635 C PRO A1163 176.369 -17.750 148.649 1.00 86.58 C
ANISOU 2635 C PRO A1163 9790 9174 13933 526 434 2675 C
ATOM 2636 O PRO A1163 177.486 -17.265 148.486 1.00 84.81 O
ANISOU 2636 O PRO A1163 9596 9114 13515 634 365 2541 O
ATOM 2637 CB PRO A1163 175.070 -16.904 150.638 1.00 85.20 C
ANISOU 2637 CB PRO A1163 9565 9439 13367 485 571 3130 C
ATOM 2638 CG PRO A1163 173.602 -17.111 150.896 1.00 90.67 C
ANISOU 2638 CG PRO A1163 10198 10057 14197 343 676 3281 C
ATOM 2639 CD PRO A1163 173.109 -17.868 149.716 1.00 86.80 C
ANISOU 2639 CD PRO A1163 9690 9170 14120 212 650 3086 C
ATOM 2640 N GLY A1164 176.075 -19.036 148.447 1.00 85.74 N
ANISOU 2640 N GLY A1164 9648 8682 14248 501 474 2781 N
ATOM 2641 CA GLY A1164 177.030 -20.036 147.983 1.00 87.33 C
ANISOU 2641 CA GLY A1164 9849 8592 14739 616 445 2734 C
ATOM 2642 C GLY A1164 177.480 -19.798 146.557 1.00 89.71 C
ANISOU 2642 C GLY A1164 10195 8827 15064 594 363 2268 C
ATOM 2643 O GLY A1164 178.655 -19.997 146.239 1.00 89.64 O
ANISOU 2643 O GLY A1164 10195 8799 15064 738 324 2166 O
ATOM 2644 N GLU A1165 176.543 -19.362 145.690 1.00 84.90 N
ANISOU 2644 N GLU A1165 9600 8209 14449 420 340 1994 N
ATOM 2645 CA GLU A1165 176.811 -19.045 144.286 1.00 83.38 C
ANISOU 2645 CA GLU A1165 9445 8011 14224 385 265 1556 C
ATOM 2646 C GLU A1165 177.549 -17.706 144.192 1.00 83.80 C
ANISOU 2646 C GLU A1165 9540 8456 13845 447 219 1439 C
ATOM 2647 O GLU A1165 178.414 -17.548 143.326 1.00 82.65 O
ANISOU 2647 O GLU A1165 9415 8346 13640 511 175 1183 O
ATOM 2648 CB GLU A1165 175.509 -19.015 143.469 1.00 84.78 C
ANISOU 2648 CB GLU A1165 9605 8090 14519 183 244 1343 C
ATOM 2649 CG GLU A1165 175.718 -19.287 141.988 1.00 96.59 C
ANISOU 2649 CG GLU A1165 11120 9459 16120 153 173 914 C
ATOM 2650 CD GLU A1165 174.459 -19.264 141.145 1.00117.97 C
ANISOU 2650 CD GLU A1165 13793 12107 18921 -44 126 687 C
ATOM 2651 OE1 GLU A1165 173.609 -20.169 141.314 1.00115.74 O
ANISOU 2651 OE1 GLU A1165 13451 11536 18990 -157 150 762 O
ATOM 2652 OE2 GLU A1165 174.339 -18.361 140.286 1.00109.99 O
ANISOU 2652 OE2 GLU A1165 12806 11341 17646 -85 61 439 O
ATOM 2653 N LEU A1166 177.211 -16.753 145.096 1.00 78.46 N
ANISOU 2653 N LEU A1166 8866 8066 12881 427 239 1623 N
ATOM 2654 CA LEU A1166 177.845 -15.436 145.189 1.00 75.62 C
ANISOU 2654 CA LEU A1166 8537 8056 12141 470 202 1537 C
ATOM 2655 C LEU A1166 179.285 -15.586 145.689 1.00 79.61 C
ANISOU 2655 C LEU A1166 9028 8651 12569 643 181 1633 C
ATOM 2656 O LEU A1166 180.174 -14.930 145.150 1.00 77.93 O
ANISOU 2656 O LEU A1166 8825 8592 12193 687 135 1440 O
ATOM 2657 CB LEU A1166 177.040 -14.486 146.101 1.00 74.59 C
ANISOU 2657 CB LEU A1166 8405 8169 11766 408 237 1691 C
ATOM 2658 CG LEU A1166 177.594 -13.062 146.300 1.00 77.15 C
ANISOU 2658 CG LEU A1166 8759 8826 11730 436 204 1595 C
ATOM 2659 CD1 LEU A1166 177.499 -12.235 145.023 1.00 75.48 C
ANISOU 2659 CD1 LEU A1166 8577 8653 11448 358 160 1286 C
ATOM 2660 CD2 LEU A1166 176.870 -12.354 147.413 1.00 79.32 C
ANISOU 2660 CD2 LEU A1166 9025 9310 11801 410 255 1766 C
ATOM 2661 N ALA A1167 179.515 -16.468 146.692 1.00 78.00 N
ANISOU 2661 N ALA A1167 8786 8355 12494 744 215 1948 N
ATOM 2662 CA ALA A1167 180.848 -16.759 147.232 1.00 78.70 C
ANISOU 2662 CA ALA A1167 8837 8525 12540 927 186 2082 C
ATOM 2663 C ALA A1167 181.746 -17.316 146.127 1.00 82.61 C
ANISOU 2663 C ALA A1167 9323 8830 13234 1005 159 1840 C
ATOM 2664 O ALA A1167 182.903 -16.908 146.025 1.00 81.82 O
ANISOU 2664 O ALA A1167 9194 8909 12984 1109 114 1758 O
ATOM 2665 CB ALA A1167 180.754 -17.745 148.388 1.00 82.24 C
ANISOU 2665 CB ALA A1167 9239 8869 13139 1019 236 2494 C
ATOM 2666 N ASN A1168 181.184 -18.199 145.267 1.00 79.70 N
ANISOU 2666 N ASN A1168 8970 8115 13197 945 186 1696 N
ATOM 2667 CA ASN A1168 181.864 -18.795 144.115 1.00 80.07 C
ANISOU 2667 CA ASN A1168 9014 7964 13446 1010 174 1411 C
ATOM 2668 C ASN A1168 182.160 -17.734 143.053 1.00 80.90 C
ANISOU 2668 C ASN A1168 9148 8304 13288 954 135 1065 C
ATOM 2669 O ASN A1168 183.194 -17.819 142.394 1.00 80.87 O
ANISOU 2669 O ASN A1168 9120 8324 13285 1061 126 884 O
ATOM 2670 CB ASN A1168 181.030 -19.929 143.509 1.00 82.52 C
ANISOU 2670 CB ASN A1168 9333 7858 14162 932 207 1309 C
ATOM 2671 CG ASN A1168 180.985 -21.203 144.321 1.00107.23 C
ANISOU 2671 CG ASN A1168 12422 10662 17661 1015 261 1630 C
ATOM 2672 OD1 ASN A1168 181.771 -21.426 145.252 1.00102.17 O
ANISOU 2672 OD1 ASN A1168 11739 10087 16994 1179 271 1931 O
ATOM 2673 ND2 ASN A1168 180.069 -22.087 143.960 1.00101.54 N
ANISOU 2673 ND2 ASN A1168 11700 9575 17306 903 293 1576 N
ATOM 2674 N ALA A1169 181.259 -16.740 142.895 1.00 74.75 N
ANISOU 2674 N ALA A1169 8409 7700 12294 796 120 993 N
ATOM 2675 CA ALA A1169 181.418 -15.633 141.948 1.00 72.06 C
ANISOU 2675 CA ALA A1169 8093 7588 11697 734 89 725 C
ATOM 2676 C ALA A1169 182.530 -14.691 142.398 1.00 74.07 C
ANISOU 2676 C ALA A1169 8321 8141 11680 816 70 781 C
ATOM 2677 O ALA A1169 183.237 -14.146 141.553 1.00 72.73 O
ANISOU 2677 O ALA A1169 8141 8105 11388 832 60 578 O
ATOM 2678 CB ALA A1169 180.120 -14.871 141.805 1.00 71.17 C
ANISOU 2678 CB ALA A1169 8016 7559 11466 565 81 692 C
ATOM 2679 N ILE A1170 182.683 -14.511 143.729 1.00 70.41 N
ANISOU 2679 N ILE A1170 7835 7796 11121 862 65 1057 N
ATOM 2680 CA ILE A1170 183.734 -13.696 144.346 1.00 69.29 C
ANISOU 2680 CA ILE A1170 7648 7940 10738 934 29 1119 C
ATOM 2681 C ILE A1170 185.069 -14.451 144.164 1.00 74.35 C
ANISOU 2681 C ILE A1170 8214 8527 11509 1104 19 1112 C
ATOM 2682 O ILE A1170 186.089 -13.819 143.883 1.00 73.45 O
ANISOU 2682 O ILE A1170 8047 8608 11253 1145 -6 1003 O
ATOM 2683 CB ILE A1170 183.395 -13.364 145.833 1.00 72.47 C
ANISOU 2683 CB ILE A1170 8045 8506 10983 935 21 1393 C
ATOM 2684 CG1 ILE A1170 182.160 -12.440 145.925 1.00 70.93 C
ANISOU 2684 CG1 ILE A1170 7911 8396 10642 779 42 1355 C
ATOM 2685 CG2 ILE A1170 184.581 -12.725 146.560 1.00 73.32 C
ANISOU 2685 CG2 ILE A1170 8085 8903 10869 1021 -38 1449 C
ATOM 2686 CD1 ILE A1170 181.389 -12.501 147.257 1.00 79.30 C
ANISOU 2686 CD1 ILE A1170 8973 9532 11626 773 73 1624 C
ATOM 2687 N LEU A1171 185.038 -15.802 144.263 1.00 72.87 N
ANISOU 2687 N LEU A1171 8011 8056 11620 1201 47 1222 N
ATOM 2688 CA LEU A1171 186.196 -16.679 144.046 1.00 74.73 C
ANISOU 2688 CA LEU A1171 8171 8179 12045 1386 51 1217 C
ATOM 2689 C LEU A1171 186.611 -16.649 142.575 1.00 78.64 C
ANISOU 2689 C LEU A1171 8667 8627 12586 1385 76 859 C
ATOM 2690 O LEU A1171 187.807 -16.657 142.277 1.00 79.14 O
ANISOU 2690 O LEU A1171 8648 8788 12633 1512 76 783 O
ATOM 2691 CB LEU A1171 185.888 -18.129 144.471 1.00 77.57 C
ANISOU 2691 CB LEU A1171 8523 8187 12764 1479 88 1423 C
ATOM 2692 CG LEU A1171 185.859 -18.435 145.965 1.00 83.38 C
ANISOU 2692 CG LEU A1171 9220 8979 13480 1558 76 1843 C
ATOM 2693 CD1 LEU A1171 184.988 -19.633 146.254 1.00 85.75 C
ANISOU 2693 CD1 LEU A1171 9544 8906 14130 1552 137 2044 C
ATOM 2694 CD2 LEU A1171 187.244 -18.668 146.508 1.00 87.42 C
ANISOU 2694 CD2 LEU A1171 9619 9628 13967 1770 34 1999 C
ATOM 2695 N LYS A1172 185.610 -16.614 141.663 1.00 74.41 N
ANISOU 2695 N LYS A1172 8211 7970 12092 1244 96 645 N
ATOM 2696 CA LYS A1172 185.783 -16.541 140.208 1.00 73.89 C
ANISOU 2696 CA LYS A1172 8157 7900 12017 1223 119 294 C
ATOM 2697 C LYS A1172 186.412 -15.198 139.853 1.00 75.13 C
ANISOU 2697 C LYS A1172 8289 8410 11848 1184 107 206 C
ATOM 2698 O LYS A1172 187.342 -15.156 139.049 1.00 75.23 O
ANISOU 2698 O LYS A1172 8247 8513 11826 1265 138 30 O
ATOM 2699 CB LYS A1172 184.431 -16.731 139.486 1.00 76.11 C
ANISOU 2699 CB LYS A1172 8518 8021 12379 1065 118 125 C
ATOM 2700 CG LYS A1172 184.535 -16.976 137.981 1.00 92.90 C
ANISOU 2700 CG LYS A1172 10654 10114 14529 1064 136 -250 C
ATOM 2701 CD LYS A1172 184.142 -15.743 137.166 1.00102.07 C
ANISOU 2701 CD LYS A1172 11848 11561 15373 933 117 -401 C
ATOM 2702 CE LYS A1172 184.321 -15.955 135.682 1.00114.08 C
ANISOU 2702 CE LYS A1172 13369 13119 16857 949 136 -755 C
ATOM 2703 NZ LYS A1172 184.057 -14.712 134.909 1.00120.56 N
ANISOU 2703 NZ LYS A1172 14209 14249 17350 845 124 -842 N
ATOM 2704 N ALA A1173 185.914 -14.114 140.484 1.00 69.19 N
ANISOU 2704 N ALA A1173 7567 7848 10874 1065 74 334 N
ATOM 2705 CA ALA A1173 186.386 -12.742 140.316 1.00 67.09 C
ANISOU 2705 CA ALA A1173 7278 7880 10334 1003 63 286 C
ATOM 2706 C ALA A1173 187.820 -12.587 140.827 1.00 71.92 C
ANISOU 2706 C ALA A1173 7776 8655 10894 1124 48 367 C
ATOM 2707 O ALA A1173 188.603 -11.851 140.223 1.00 71.11 O
ANISOU 2707 O ALA A1173 7616 8740 10664 1115 65 250 O
ATOM 2708 CB ALA A1173 185.464 -11.788 141.050 1.00 66.04 C
ANISOU 2708 CB ALA A1173 7201 7849 10042 868 34 409 C
ATOM 2709 N LEU A1174 188.164 -13.294 141.927 1.00 69.81 N
ANISOU 2709 N LEU A1174 7463 8329 10732 1239 18 584 N
ATOM 2710 CA LEU A1174 189.504 -13.293 142.517 1.00 70.68 C
ANISOU 2710 CA LEU A1174 7442 8601 10811 1374 -16 686 C
ATOM 2711 C LEU A1174 190.499 -13.933 141.541 1.00 75.92 C
ANISOU 2711 C LEU A1174 8022 9205 11620 1511 36 523 C
ATOM 2712 O LEU A1174 191.592 -13.402 141.347 1.00 75.57 O
ANISOU 2712 O LEU A1174 7862 9373 11478 1551 34 470 O
ATOM 2713 CB LEU A1174 189.495 -14.032 143.867 1.00 72.31 C
ANISOU 2713 CB LEU A1174 7622 8754 11099 1481 -61 984 C
ATOM 2714 CG LEU A1174 190.854 -14.352 144.479 1.00 78.95 C
ANISOU 2714 CG LEU A1174 8308 9732 11957 1662 -108 1120 C
ATOM 2715 CD1 LEU A1174 191.267 -13.308 145.475 1.00 78.42 C
ANISOU 2715 CD1 LEU A1174 8177 10003 11616 1611 -197 1221 C
ATOM 2716 CD2 LEU A1174 190.836 -15.698 145.122 1.00 84.32 C
ANISOU 2716 CD2 LEU A1174 8968 10193 12878 1830 -105 1362 C
ATOM 2717 N GLU A1175 190.105 -15.056 140.914 1.00 73.84 N
ANISOU 2717 N GLU A1175 7807 8653 11598 1576 88 426 N
ATOM 2718 CA GLU A1175 190.925 -15.757 139.928 1.00 75.37 C
ANISOU 2718 CA GLU A1175 7931 8762 11944 1719 153 226 C
ATOM 2719 C GLU A1175 191.034 -14.919 138.655 1.00 78.17 C
ANISOU 2719 C GLU A1175 8294 9300 12107 1623 204 -43 C
ATOM 2720 O GLU A1175 192.106 -14.847 138.066 1.00 78.48 O
ANISOU 2720 O GLU A1175 8224 9476 12120 1720 254 -156 O
ATOM 2721 CB GLU A1175 190.358 -17.155 139.630 1.00 78.77 C
ANISOU 2721 CB GLU A1175 8422 8807 12702 1796 192 162 C
ATOM 2722 CG GLU A1175 190.511 -18.144 140.778 1.00 91.06 C
ANISOU 2722 CG GLU A1175 9938 10160 14502 1940 167 459 C
ATOM 2723 CD GLU A1175 191.924 -18.338 141.296 1.00111.46 C
ANISOU 2723 CD GLU A1175 12360 12874 17114 2149 153 604 C
ATOM 2724 OE1 GLU A1175 192.200 -17.902 142.437 1.00105.51 O
ANISOU 2724 OE1 GLU A1175 11552 12319 16218 2159 78 878 O
ATOM 2725 OE2 GLU A1175 192.765 -18.893 140.552 1.00104.83 O
ANISOU 2725 OE2 GLU A1175 11439 11967 16425 2305 213 430 O
ATOM 2726 N LEU A1176 189.938 -14.235 138.277 1.00 73.37 N
ANISOU 2726 N LEU A1176 7800 8720 11356 1437 194 -114 N
ATOM 2727 CA LEU A1176 189.845 -13.343 137.118 1.00 72.16 C
ANISOU 2727 CA LEU A1176 7667 8754 10996 1332 235 -313 C
ATOM 2728 C LEU A1176 190.836 -12.171 137.230 1.00 76.11 C
ANISOU 2728 C LEU A1176 8063 9559 11298 1305 241 -250 C
ATOM 2729 O LEU A1176 191.447 -11.792 136.228 1.00 76.17 O
ANISOU 2729 O LEU A1176 8011 9727 11205 1314 311 -395 O
ATOM 2730 CB LEU A1176 188.405 -12.810 137.026 1.00 70.24 C
ANISOU 2730 CB LEU A1176 7553 8477 10659 1149 199 -314 C
ATOM 2731 CG LEU A1176 187.848 -12.447 135.659 1.00 74.41 C
ANISOU 2731 CG LEU A1176 8132 9084 11055 1062 231 -540 C
ATOM 2732 CD1 LEU A1176 187.632 -13.688 134.795 1.00 76.68 C
ANISOU 2732 CD1 LEU A1176 8443 9179 11514 1140 260 -781 C
ATOM 2733 CD2 LEU A1176 186.533 -11.711 135.813 1.00 74.45 C
ANISOU 2733 CD2 LEU A1176 8231 9100 10956 891 182 -471 C
ATOM 2734 N SER A1177 191.021 -11.638 138.459 1.00 72.13 N
ANISOU 2734 N SER A1177 7526 9138 10744 1272 171 -37 N
ATOM 2735 CA SER A1177 191.903 -10.508 138.771 1.00 71.26 C
ANISOU 2735 CA SER A1177 7307 9288 10479 1220 154 24 C
ATOM 2736 C SER A1177 193.399 -10.835 138.640 1.00 76.73 C
ANISOU 2736 C SER A1177 7818 10100 11234 1369 185 6 C
ATOM 2737 O SER A1177 194.204 -9.901 138.572 1.00 76.60 O
ANISOU 2737 O SER A1177 7688 10308 11110 1311 192 9 O
ATOM 2738 CB SER A1177 191.622 -9.987 140.176 1.00 73.96 C
ANISOU 2738 CB SER A1177 7664 9683 10754 1153 59 214 C
ATOM 2739 OG SER A1177 192.241 -10.803 141.155 1.00 84.13 O
ANISOU 2739 OG SER A1177 8868 10950 12146 1303 5 364 O
ATOM 2740 N ARG A1178 193.772 -12.136 138.627 1.00 74.47 N
ANISOU 2740 N ARG A1178 7492 9656 11148 1560 205 -5 N
ATOM 2741 CA ARG A1178 195.170 -12.582 138.498 1.00 76.03 C
ANISOU 2741 CA ARG A1178 7501 9949 11438 1739 242 -20 C
ATOM 2742 C ARG A1178 195.719 -12.213 137.114 1.00 81.12 C
ANISOU 2742 C ARG A1178 8081 10741 11999 1732 362 -232 C
ATOM 2743 O ARG A1178 196.903 -11.895 136.984 1.00 82.06 O
ANISOU 2743 O ARG A1178 8018 11065 12096 1789 398 -229 O
ATOM 2744 CB ARG A1178 195.312 -14.088 138.770 1.00 76.15 C
ANISOU 2744 CB ARG A1178 7502 9711 11721 1956 247 19 C
ATOM 2745 CG ARG A1178 194.743 -14.500 140.117 1.00 78.73 C
ANISOU 2745 CG ARG A1178 7888 9904 12124 1969 144 274 C
ATOM 2746 CD ARG A1178 195.324 -15.791 140.639 1.00 81.10 C
ANISOU 2746 CD ARG A1178 8099 10028 12687 2212 137 410 C
ATOM 2747 NE ARG A1178 194.565 -16.287 141.787 1.00 81.99 N
ANISOU 2747 NE ARG A1178 8294 9981 12877 2216 64 669 N
ATOM 2748 CZ ARG A1178 194.748 -15.892 143.044 1.00 91.57 C
ANISOU 2748 CZ ARG A1178 9453 11381 13959 2210 -40 926 C
ATOM 2749 NH1 ARG A1178 195.669 -14.980 143.336 1.00 73.33 N
ANISOU 2749 NH1 ARG A1178 7002 9405 11454 2185 -99 936 N
ATOM 2750 NH2 ARG A1178 194.007 -16.400 144.019 1.00 79.49 N
ANISOU 2750 NH2 ARG A1178 7998 9717 12487 2222 -84 1170 N
ATOM 2751 N SER A1179 194.837 -12.222 136.097 1.00 77.26 N
ANISOU 2751 N SER A1179 7730 10175 11450 1657 423 -406 N
ATOM 2752 CA SER A1179 195.116 -11.795 134.728 1.00 77.47 C
ANISOU 2752 CA SER A1179 7723 10374 11336 1632 539 -594 C
ATOM 2753 C SER A1179 194.850 -10.285 134.628 1.00 79.13 C
ANISOU 2753 C SER A1179 7954 10785 11326 1417 529 -512 C
ATOM 2754 O SER A1179 194.421 -9.683 135.616 1.00 77.35 O
ANISOU 2754 O SER A1179 7775 10535 11079 1302 432 -354 O
ATOM 2755 CB SER A1179 194.243 -12.572 133.748 1.00 81.78 C
ANISOU 2755 CB SER A1179 8404 10759 11910 1659 585 -821 C
ATOM 2756 OG SER A1179 192.861 -12.340 133.969 1.00 88.75 O
ANISOU 2756 OG SER A1179 9458 11512 12751 1505 508 -784 O
ATOM 2757 N ASP A1180 195.087 -9.667 133.458 1.00 75.62 N
ANISOU 2757 N ASP A1180 7472 10537 10722 1367 635 -611 N
ATOM 2758 CA ASP A1180 194.827 -8.236 133.319 1.00 73.66 C
ANISOU 2758 CA ASP A1180 7239 10443 10305 1170 638 -508 C
ATOM 2759 C ASP A1180 193.332 -7.997 133.091 1.00 74.93 C
ANISOU 2759 C ASP A1180 7598 10490 10383 1052 590 -525 C
ATOM 2760 O ASP A1180 192.763 -8.504 132.119 1.00 75.70 O
ANISOU 2760 O ASP A1180 7772 10569 10420 1088 632 -682 O
ATOM 2761 CB ASP A1180 195.671 -7.613 132.195 1.00 76.98 C
ANISOU 2761 CB ASP A1180 7527 11129 10592 1160 780 -546 C
ATOM 2762 CG ASP A1180 195.726 -6.093 132.197 1.00 88.44 C
ANISOU 2762 CG ASP A1180 8941 12723 11939 964 793 -389 C
ATOM 2763 OD1 ASP A1180 195.339 -5.480 133.220 1.00 88.30 O
ANISOU 2763 OD1 ASP A1180 8971 12608 11969 846 684 -270 O
ATOM 2764 OD2 ASP A1180 196.170 -5.513 131.183 1.00 95.07 O
ANISOU 2764 OD2 ASP A1180 9698 13768 12656 932 919 -385 O
ATOM 2765 N LEU A1181 192.693 -7.258 134.015 1.00 67.96 N
ANISOU 2765 N LEU A1181 6786 9539 9498 918 497 -379 N
ATOM 2766 CA LEU A1181 191.268 -6.930 133.935 1.00 65.44 C
ANISOU 2766 CA LEU A1181 6631 9119 9116 806 449 -367 C
ATOM 2767 C LEU A1181 191.024 -5.647 133.134 1.00 68.11 C
ANISOU 2767 C LEU A1181 6975 9615 9288 674 504 -318 C
ATOM 2768 O LEU A1181 189.868 -5.253 132.979 1.00 66.53 O
ANISOU 2768 O LEU A1181 6891 9359 9028 588 468 -294 O
ATOM 2769 CB LEU A1181 190.656 -6.774 135.342 1.00 63.78 C
ANISOU 2769 CB LEU A1181 6487 8765 8981 745 340 -235 C
ATOM 2770 CG LEU A1181 190.446 -8.025 136.189 1.00 68.23 C
ANISOU 2770 CG LEU A1181 7085 9138 9703 855 277 -223 C
ATOM 2771 CD1 LEU A1181 190.054 -7.639 137.589 1.00 67.07 C
ANISOU 2771 CD1 LEU A1181 6971 8943 9570 793 189 -64 C
ATOM 2772 CD2 LEU A1181 189.376 -8.936 135.600 1.00 70.13 C
ANISOU 2772 CD2 LEU A1181 7441 9205 10001 877 278 -339 C
ATOM 2773 N SER A1182 192.103 -5.002 132.627 1.00 65.38 N
ANISOU 2773 N SER A1182 6492 9464 8884 663 595 -283 N
ATOM 2774 CA SER A1182 192.074 -3.747 131.865 1.00 65.08 C
ANISOU 2774 CA SER A1182 6431 9578 8719 543 669 -188 C
ATOM 2775 C SER A1182 191.015 -3.747 130.751 1.00 67.87 C
ANISOU 2775 C SER A1182 6897 9978 8914 533 693 -237 C
ATOM 2776 O SER A1182 190.262 -2.777 130.653 1.00 66.84 O
ANISOU 2776 O SER A1182 6829 9841 8728 420 677 -117 O
ATOM 2777 CB SER A1182 193.448 -3.434 131.278 1.00 71.18 C
ANISOU 2777 CB SER A1182 7018 10563 9463 567 792 -164 C
ATOM 2778 OG SER A1182 193.838 -4.390 130.305 1.00 84.33 O
ANISOU 2778 OG SER A1182 8645 12346 11052 716 880 -319 O
ATOM 2779 N LYS A1183 190.927 -4.833 129.949 1.00 64.56 N
ANISOU 2779 N LYS A1183 6499 9600 8430 654 721 -423 N
ATOM 2780 CA LYS A1183 189.937 -4.930 128.872 1.00 64.43 C
ANISOU 2780 CA LYS A1183 6574 9665 8241 650 722 -508 C
ATOM 2781 C LYS A1183 188.533 -5.181 129.409 1.00 67.10 C
ANISOU 2781 C LYS A1183 7054 9794 8647 594 592 -522 C
ATOM 2782 O LYS A1183 187.578 -4.640 128.852 1.00 66.55 O
ANISOU 2782 O LYS A1183 7047 9787 8452 526 566 -476 O
ATOM 2783 CB LYS A1183 190.299 -6.012 127.855 1.00 68.43 C
ANISOU 2783 CB LYS A1183 7051 10292 8657 792 789 -752 C
ATOM 2784 CG LYS A1183 190.005 -5.573 126.429 1.00 75.49 C
ANISOU 2784 CG LYS A1183 7945 11473 9267 785 860 -778 C
ATOM 2785 CD LYS A1183 188.623 -5.960 125.917 1.00 78.15 C
ANISOU 2785 CD LYS A1183 8406 11785 9504 763 759 -908 C
ATOM 2786 CE LYS A1183 188.326 -5.336 124.573 1.00 80.80 C
ANISOU 2786 CE LYS A1183 8728 12453 9521 751 815 -876 C
ATOM 2787 NZ LYS A1183 188.209 -3.856 124.652 1.00 82.61 N
ANISOU 2787 NZ LYS A1183 8937 12757 9695 636 842 -542 N
ATOM 2788 N PHE A1184 188.405 -5.996 130.478 1.00 63.12 N
ANISOU 2788 N PHE A1184 6586 9056 8342 629 516 -563 N
ATOM 2789 CA PHE A1184 187.126 -6.299 131.115 1.00 61.88 C
ANISOU 2789 CA PHE A1184 6542 8694 8276 575 408 -554 C
ATOM 2790 C PHE A1184 186.448 -5.007 131.562 1.00 65.17 C
ANISOU 2790 C PHE A1184 6996 9112 8652 446 376 -359 C
ATOM 2791 O PHE A1184 185.253 -4.837 131.322 1.00 64.59 O
ANISOU 2791 O PHE A1184 6997 9009 8536 389 324 -351 O
ATOM 2792 CB PHE A1184 187.313 -7.246 132.313 1.00 63.40 C
ANISOU 2792 CB PHE A1184 6741 8660 8688 636 356 -557 C
ATOM 2793 CG PHE A1184 186.156 -8.187 132.559 1.00 64.98 C
ANISOU 2793 CG PHE A1184 7033 8647 9008 630 280 -634 C
ATOM 2794 CD1 PHE A1184 184.906 -7.702 132.927 1.00 66.49 C
ANISOU 2794 CD1 PHE A1184 7299 8774 9190 520 215 -540 C
ATOM 2795 CD2 PHE A1184 186.322 -9.561 132.449 1.00 68.86 C
ANISOU 2795 CD2 PHE A1184 7523 8987 9653 735 279 -796 C
ATOM 2796 CE1 PHE A1184 183.839 -8.572 133.145 1.00 67.61 C
ANISOU 2796 CE1 PHE A1184 7502 8726 9462 500 152 -600 C
ATOM 2797 CE2 PHE A1184 185.252 -10.431 132.674 1.00 71.94 C
ANISOU 2797 CE2 PHE A1184 7985 9155 10196 708 213 -859 C
ATOM 2798 CZ PHE A1184 184.021 -9.931 133.032 1.00 68.48 C
ANISOU 2798 CZ PHE A1184 7608 8675 9737 584 150 -754 C
ATOM 2799 N ARG A1185 187.227 -4.086 132.173 1.00 61.40 N
ANISOU 2799 N ARG A1185 6456 8671 8201 401 407 -217 N
ATOM 2800 CA ARG A1185 186.773 -2.773 132.645 1.00 59.97 C
ANISOU 2800 CA ARG A1185 6298 8470 8018 284 392 -53 C
ATOM 2801 C ARG A1185 186.395 -1.888 131.467 1.00 64.87 C
ANISOU 2801 C ARG A1185 6920 9239 8490 236 446 19 C
ATOM 2802 O ARG A1185 185.435 -1.125 131.573 1.00 63.89 O
ANISOU 2802 O ARG A1185 6853 9062 8362 167 414 121 O
ATOM 2803 CB ARG A1185 187.852 -2.083 133.494 1.00 59.55 C
ANISOU 2803 CB ARG A1185 6156 8425 8045 244 411 31 C
ATOM 2804 CG ARG A1185 188.368 -2.939 134.631 1.00 67.04 C
ANISOU 2804 CG ARG A1185 7079 9285 9108 311 354 -12 C
ATOM 2805 CD ARG A1185 189.234 -2.155 135.584 1.00 73.30 C
ANISOU 2805 CD ARG A1185 7785 10105 9961 252 338 59 C
ATOM 2806 NE ARG A1185 189.910 -3.033 136.541 1.00 78.43 N
ANISOU 2806 NE ARG A1185 8379 10732 10687 341 282 34 N
ATOM 2807 CZ ARG A1185 189.365 -3.489 137.665 1.00 88.99 C
ANISOU 2807 CZ ARG A1185 9780 11962 12068 365 199 61 C
ATOM 2808 NH1 ARG A1185 188.121 -3.160 137.990 1.00 74.61 N
ANISOU 2808 NH1 ARG A1185 8077 10044 10228 303 169 94 N
ATOM 2809 NH2 ARG A1185 190.059 -4.279 138.471 1.00 75.94 N
ANISOU 2809 NH2 ARG A1185 8062 10315 10475 461 151 75 N
ATOM 2810 N GLU A1186 187.140 -2.000 130.340 1.00 63.21 N
ANISOU 2810 N GLU A1186 6638 9228 8152 285 534 -21 N
ATOM 2811 CA GLU A1186 186.874 -1.246 129.112 1.00 64.04 C
ANISOU 2811 CA GLU A1186 6728 9527 8075 260 597 74 C
ATOM 2812 C GLU A1186 185.555 -1.697 128.490 1.00 67.46 C
ANISOU 2812 C GLU A1186 7251 9984 8397 280 521 -6 C
ATOM 2813 O GLU A1186 184.851 -0.867 127.919 1.00 67.21 O
ANISOU 2813 O GLU A1186 7236 10040 8262 237 519 132 O
ATOM 2814 CB GLU A1186 188.030 -1.360 128.102 1.00 67.44 C
ANISOU 2814 CB GLU A1186 7050 10203 8372 322 723 46 C
ATOM 2815 CG GLU A1186 189.252 -0.517 128.449 1.00 79.72 C
ANISOU 2815 CG GLU A1186 8482 11789 10020 264 814 191 C
ATOM 2816 CD GLU A1186 189.010 0.925 128.865 1.00103.41 C
ANISOU 2816 CD GLU A1186 11481 14694 13115 129 819 418 C
ATOM 2817 OE1 GLU A1186 188.363 1.674 128.096 1.00100.36 O
ANISOU 2817 OE1 GLU A1186 11122 14387 12623 96 849 567 O
ATOM 2818 OE2 GLU A1186 189.474 1.307 129.964 1.00 97.30 O
ANISOU 2818 OE2 GLU A1186 10674 13770 12527 63 789 443 O
ATOM 2819 N ASN A1187 185.201 -2.994 128.647 1.00 63.72 N
ANISOU 2819 N ASN A1187 6823 9416 7970 340 452 -219 N
ATOM 2820 CA ASN A1187 183.931 -3.559 128.179 1.00 63.60 C
ANISOU 2820 CA ASN A1187 6875 9395 7894 340 359 -334 C
ATOM 2821 C ASN A1187 182.785 -3.006 129.018 1.00 65.93 C
ANISOU 2821 C ASN A1187 7230 9519 8302 257 277 -198 C
ATOM 2822 O ASN A1187 181.742 -2.664 128.463 1.00 66.29 O
ANISOU 2822 O ASN A1187 7296 9640 8253 228 225 -156 O
ATOM 2823 CB ASN A1187 183.942 -5.087 128.245 1.00 63.41 C
ANISOU 2823 CB ASN A1187 6873 9258 7962 411 317 -596 C
ATOM 2824 CG ASN A1187 184.944 -5.765 127.352 1.00 77.71 C
ANISOU 2824 CG ASN A1187 8627 11232 9668 516 399 -785 C
ATOM 2825 OD1 ASN A1187 185.319 -5.267 126.284 1.00 70.84 O
ANISOU 2825 OD1 ASN A1187 7708 10641 8568 540 474 -767 O
ATOM 2826 ND2 ASN A1187 185.360 -6.953 127.759 1.00 68.44 N
ANISOU 2826 ND2 ASN A1187 7452 9889 8661 593 393 -964 N
ATOM 2827 N CYS A1188 182.999 -2.903 130.355 1.00 60.44 N
ANISOU 2827 N CYS A1188 6549 8618 7795 230 268 -129 N
ATOM 2828 CA CYS A1188 182.059 -2.353 131.336 1.00 58.48 C
ANISOU 2828 CA CYS A1188 6349 8212 7660 164 214 -9 C
ATOM 2829 C CYS A1188 181.792 -0.884 131.021 1.00 62.03 C
ANISOU 2829 C CYS A1188 6786 8738 8047 111 249 181 C
ATOM 2830 O CYS A1188 180.633 -0.479 130.965 1.00 61.57 O
ANISOU 2830 O CYS A1188 6755 8654 7985 84 201 251 O
ATOM 2831 CB CYS A1188 182.596 -2.524 132.756 1.00 57.64 C
ANISOU 2831 CB CYS A1188 6245 7941 7713 162 212 13 C
ATOM 2832 SG CYS A1188 182.735 -4.244 133.302 1.00 61.79 S
ANISOU 2832 SG CYS A1188 6787 8323 8366 235 169 -142 S
ATOM 2833 N LYS A1189 182.873 -0.098 130.795 1.00 58.80 N
ANISOU 2833 N LYS A1189 6320 8412 7610 98 336 275 N
ATOM 2834 CA LYS A1189 182.833 1.325 130.451 1.00 58.77 C
ANISOU 2834 CA LYS A1189 6290 8452 7589 46 392 478 C
ATOM 2835 C LYS A1189 182.044 1.547 129.161 1.00 64.13 C
ANISOU 2835 C LYS A1189 6967 9309 8089 71 384 552 C
ATOM 2836 O LYS A1189 181.142 2.381 129.158 1.00 64.03 O
ANISOU 2836 O LYS A1189 6972 9251 8105 47 362 700 O
ATOM 2837 CB LYS A1189 184.254 1.897 130.309 1.00 61.70 C
ANISOU 2837 CB LYS A1189 6576 8893 7975 20 496 548 C
ATOM 2838 CG LYS A1189 184.958 2.180 131.629 1.00 68.86 C
ANISOU 2838 CG LYS A1189 7461 9637 9066 -32 493 530 C
ATOM 2839 CD LYS A1189 186.454 2.366 131.420 1.00 76.28 C
ANISOU 2839 CD LYS A1189 8287 10678 10018 -49 580 546 C
ATOM 2840 CE LYS A1189 187.202 2.528 132.719 1.00 84.03 C
ANISOU 2840 CE LYS A1189 9226 11539 11161 -98 551 498 C
ATOM 2841 NZ LYS A1189 188.667 2.340 132.541 1.00 92.88 N
ANISOU 2841 NZ LYS A1189 10214 12783 12292 -92 614 473 N
ATOM 2842 N LYS A1190 182.355 0.773 128.091 1.00 61.93 N
ANISOU 2842 N LYS A1190 6663 9246 7622 131 397 438 N
ATOM 2843 CA LYS A1190 181.703 0.842 126.775 1.00 63.38 C
ANISOU 2843 CA LYS A1190 6833 9674 7574 168 377 474 C
ATOM 2844 C LYS A1190 180.225 0.465 126.850 1.00 66.78 C
ANISOU 2844 C LYS A1190 7310 10052 8012 164 245 412 C
ATOM 2845 O LYS A1190 179.407 1.109 126.190 1.00 67.37 O
ANISOU 2845 O LYS A1190 7368 10254 7977 170 212 558 O
ATOM 2846 CB LYS A1190 182.418 -0.056 125.753 1.00 67.68 C
ANISOU 2846 CB LYS A1190 7340 10463 7911 240 417 293 C
ATOM 2847 CG LYS A1190 183.629 0.608 125.117 1.00 87.55 C
ANISOU 2847 CG LYS A1190 9775 13169 10320 253 566 438 C
ATOM 2848 CD LYS A1190 184.656 -0.411 124.649 1.00100.74 C
ANISOU 2848 CD LYS A1190 11402 14988 11888 331 632 212 C
ATOM 2849 CE LYS A1190 186.058 0.128 124.794 1.00111.63 C
ANISOU 2849 CE LYS A1190 12687 16397 13329 316 776 335 C
ATOM 2850 NZ LYS A1190 187.074 -0.954 124.742 1.00121.32 N
ANISOU 2850 NZ LYS A1190 13866 17679 14551 401 830 98 N
ATOM 2851 N ARG A1191 179.885 -0.566 127.651 1.00 62.18 N
ANISOU 2851 N ARG A1191 6770 9286 7569 156 172 218 N
ATOM 2852 CA ARG A1191 178.510 -1.031 127.838 1.00 61.74 C
ANISOU 2852 CA ARG A1191 6738 9156 7563 134 54 149 C
ATOM 2853 C ARG A1191 177.683 0.026 128.569 1.00 65.91 C
ANISOU 2853 C ARG A1191 7274 9549 8219 96 42 360 C
ATOM 2854 O ARG A1191 176.601 0.367 128.099 1.00 66.51 O
ANISOU 2854 O ARG A1191 7326 9709 8236 97 -23 438 O
ATOM 2855 CB ARG A1191 178.480 -2.363 128.598 1.00 59.65 C
ANISOU 2855 CB ARG A1191 6507 8700 7459 129 7 -69 C
ATOM 2856 CG ARG A1191 177.091 -2.953 128.780 1.00 64.75 C
ANISOU 2856 CG ARG A1191 7156 9260 8185 89 -107 -146 C
ATOM 2857 CD ARG A1191 176.838 -4.128 127.868 1.00 70.20 C
ANISOU 2857 CD ARG A1191 7829 10050 8793 99 -181 -408 C
ATOM 2858 NE ARG A1191 175.553 -4.743 128.185 1.00 69.95 N
ANISOU 2858 NE ARG A1191 7783 9898 8897 37 -289 -484 N
ATOM 2859 CZ ARG A1191 174.426 -4.523 127.520 1.00 82.15 C
ANISOU 2859 CZ ARG A1191 9275 11592 10347 6 -388 -479 C
ATOM 2860 NH1 ARG A1191 173.301 -5.106 127.903 1.00 68.52 N
ANISOU 2860 NH1 ARG A1191 7515 9740 8779 -64 -479 -543 N
ATOM 2861 NH2 ARG A1191 174.418 -3.730 126.455 1.00 71.24 N
ANISOU 2861 NH2 ARG A1191 7859 10499 8709 45 -398 -394 N
ATOM 2862 N ALA A1192 178.200 0.557 129.694 1.00 61.89 N
ANISOU 2862 N ALA A1192 6789 8847 7880 69 104 440 N
ATOM 2863 CA ALA A1192 177.535 1.586 130.492 1.00 61.35 C
ANISOU 2863 CA ALA A1192 6732 8630 7949 42 112 601 C
ATOM 2864 C ALA A1192 177.360 2.894 129.714 1.00 67.81 C
ANISOU 2864 C ALA A1192 7514 9547 8705 54 154 827 C
ATOM 2865 O ALA A1192 176.368 3.593 129.919 1.00 67.46 O
ANISOU 2865 O ALA A1192 7461 9434 8735 61 131 951 O
ATOM 2866 CB ALA A1192 178.314 1.842 131.764 1.00 60.86 C
ANISOU 2866 CB ALA A1192 6695 8386 8043 13 168 593 C
ATOM 2867 N MET A1193 178.309 3.205 128.815 1.00 66.74 N
ANISOU 2867 N MET A1193 7346 9573 8440 66 223 897 N
ATOM 2868 CA MET A1193 178.302 4.397 127.970 1.00 68.76 C
ANISOU 2868 CA MET A1193 7558 9938 8630 80 281 1154 C
ATOM 2869 C MET A1193 177.155 4.354 126.948 1.00 74.77 C
ANISOU 2869 C MET A1193 8287 10907 9215 135 196 1229 C
ATOM 2870 O MET A1193 176.546 5.393 126.687 1.00 75.62 O
ANISOU 2870 O MET A1193 8365 11011 9356 160 205 1469 O
ATOM 2871 CB MET A1193 179.649 4.524 127.248 1.00 72.51 C
ANISOU 2871 CB MET A1193 7990 10572 8989 78 387 1201 C
ATOM 2872 CG MET A1193 179.891 5.872 126.622 1.00 78.26 C
ANISOU 2872 CG MET A1193 8666 11348 9720 72 483 1512 C
ATOM 2873 SD MET A1193 181.447 5.878 125.710 1.00 84.56 S
ANISOU 2873 SD MET A1193 9389 12379 10359 66 622 1571 S
ATOM 2874 CE MET A1193 182.590 6.316 127.020 1.00 80.08 C
ANISOU 2874 CE MET A1193 8812 11515 10101 -35 698 1525 C
ATOM 2875 N SER A1194 176.857 3.159 126.384 1.00 71.82 N
ANISOU 2875 N SER A1194 7911 10709 8670 157 107 1017 N
ATOM 2876 CA SER A1194 175.811 2.965 125.373 1.00 73.28 C
ANISOU 2876 CA SER A1194 8049 11139 8655 200 -2 1032 C
ATOM 2877 C SER A1194 174.386 3.167 125.933 1.00 77.25 C
ANISOU 2877 C SER A1194 8535 11511 9304 195 -99 1082 C
ATOM 2878 O SER A1194 173.454 3.365 125.150 1.00 78.31 O
ANISOU 2878 O SER A1194 8606 11843 9305 236 -188 1175 O
ATOM 2879 CB SER A1194 175.933 1.587 124.725 1.00 77.02 C
ANISOU 2879 CB SER A1194 8521 11799 8943 209 -74 729 C
ATOM 2880 OG SER A1194 175.566 0.527 125.592 1.00 82.80 O
ANISOU 2880 OG SER A1194 9290 12320 9849 164 -142 485 O
ATOM 2881 N PHE A1195 174.224 3.140 127.270 1.00 72.73 N
ANISOU 2881 N PHE A1195 8007 10638 8990 153 -80 1030 N
ATOM 2882 CA PHE A1195 172.930 3.317 127.934 1.00 72.49 C
ANISOU 2882 CA PHE A1195 7952 10476 9114 153 -143 1070 C
ATOM 2883 C PHE A1195 172.635 4.794 128.286 1.00 77.75 C
ANISOU 2883 C PHE A1195 8603 11010 9926 190 -72 1339 C
ATOM 2884 O PHE A1195 171.621 5.072 128.935 1.00 77.26 O
ANISOU 2884 O PHE A1195 8516 10823 10015 205 -98 1380 O
ATOM 2885 CB PHE A1195 172.845 2.434 129.190 1.00 72.38 C
ANISOU 2885 CB PHE A1195 7985 10239 9279 98 -150 874 C
ATOM 2886 CG PHE A1195 172.595 0.975 128.889 1.00 74.21 C
ANISOU 2886 CG PHE A1195 8206 10545 9447 64 -246 630 C
ATOM 2887 CD1 PHE A1195 171.307 0.503 128.674 1.00 78.05 C
ANISOU 2887 CD1 PHE A1195 8622 11090 9943 46 -361 577 C
ATOM 2888 CD2 PHE A1195 173.647 0.074 128.814 1.00 76.05 C
ANISOU 2888 CD2 PHE A1195 8486 10775 9635 50 -220 446 C
ATOM 2889 CE1 PHE A1195 171.077 -0.846 128.399 1.00 79.62 C
ANISOU 2889 CE1 PHE A1195 8804 11323 10126 -3 -451 330 C
ATOM 2890 CE2 PHE A1195 173.416 -1.275 128.538 1.00 79.51 C
ANISOU 2890 CE2 PHE A1195 8914 11237 10058 22 -302 204 C
ATOM 2891 CZ PHE A1195 172.133 -1.725 128.328 1.00 78.48 C
ANISOU 2891 CZ PHE A1195 8721 11145 9954 -13 -419 141 C
ATOM 2892 N SER A1196 173.492 5.734 127.838 1.00 75.68 N
ANISOU 2892 N SER A1196 8346 10770 9638 207 25 1523 N
ATOM 2893 CA SER A1196 173.302 7.165 128.087 1.00 76.32 C
ANISOU 2893 CA SER A1196 8413 10691 9896 241 102 1778 C
ATOM 2894 C SER A1196 172.277 7.752 127.129 1.00 82.73 C
ANISOU 2894 C SER A1196 9139 11675 10619 329 42 2018 C
ATOM 2895 O SER A1196 172.219 7.334 125.969 1.00 83.92 O
ANISOU 2895 O SER A1196 9245 12136 10505 358 -25 2046 O
ATOM 2896 CB SER A1196 174.623 7.918 127.967 1.00 80.28 C
ANISOU 2896 CB SER A1196 8934 11127 10441 207 231 1895 C
ATOM 2897 OG SER A1196 175.166 7.833 126.660 1.00 90.68 O
ANISOU 2897 OG SER A1196 10213 12731 11511 229 246 2005 O
ATOM 2898 N ARG A 236 171.496 8.747 127.608 1.00 76.38 N
ANISOU 2898 N ARG A 236 9066 10058 9897 -644 -1022 593 N
ATOM 2899 CA ARG A 236 170.458 9.451 126.843 1.00 75.17 C
ANISOU 2899 CA ARG A 236 8998 9827 9735 -668 -931 534 C
ATOM 2900 C ARG A 236 171.020 10.138 125.583 1.00 79.27 C
ANISOU 2900 C ARG A 236 9405 10440 10273 -710 -894 542 C
ATOM 2901 O ARG A 236 170.317 10.220 124.573 1.00 78.41 O
ANISOU 2901 O ARG A 236 9309 10304 10181 -674 -809 504 O
ATOM 2902 CB ARG A 236 169.749 10.485 127.727 1.00 75.11 C
ANISOU 2902 CB ARG A 236 9158 9722 9658 -780 -950 511 C
ATOM 2903 N GLN A 237 172.290 10.603 125.642 1.00 76.40 N
ANISOU 2903 N GLN A 237 8926 10200 9901 -792 -960 598 N
ATOM 2904 CA GLN A 237 172.989 11.263 124.535 1.00 76.44 C
ANISOU 2904 CA GLN A 237 8806 10322 9914 -853 -933 624 C
ATOM 2905 C GLN A 237 173.559 10.245 123.516 1.00 80.19 C
ANISOU 2905 C GLN A 237 9105 10923 10441 -723 -876 618 C
ATOM 2906 O GLN A 237 174.059 10.648 122.462 1.00 80.27 O
ANISOU 2906 O GLN A 237 9001 11049 10449 -759 -832 634 O
ATOM 2907 CB GLN A 237 174.112 12.163 125.076 1.00 78.98 C
ANISOU 2907 CB GLN A 237 9071 10732 10204 -1008 -1030 690 C
ATOM 2908 N GLY A 238 173.466 8.954 123.837 1.00 76.23 N
ANISOU 2908 N GLY A 238 8587 10394 9983 -578 -874 595 N
ATOM 2909 CA GLY A 238 173.935 7.868 122.982 1.00 76.33 C
ANISOU 2909 CA GLY A 238 8451 10495 10054 -431 -820 567 C
ATOM 2910 C GLY A 238 173.004 7.580 121.822 1.00 78.94 C
ANISOU 2910 C GLY A 238 8819 10783 10392 -363 -707 491 C
ATOM 2911 O GLY A 238 171.814 7.901 121.887 1.00 77.48 O
ANISOU 2911 O GLY A 238 8787 10469 10181 -392 -679 461 O
ATOM 2912 N ALA A 239 173.541 6.953 120.757 1.00 75.83 N
ANISOU 2912 N ALA A 239 8277 10506 10028 -268 -642 454 N
ATOM 2913 CA ALA A 239 172.813 6.596 119.534 1.00 75.08 C
ANISOU 2913 CA ALA A 239 8193 10406 9928 -203 -536 374 C
ATOM 2914 C ALA A 239 171.693 5.573 119.783 1.00 78.50 C
ANISOU 2914 C ALA A 239 8755 10671 10400 -94 -515 307 C
ATOM 2915 O ALA A 239 170.689 5.591 119.068 1.00 77.47 O
ANISOU 2915 O ALA A 239 8701 10488 10247 -92 -449 254 O
ATOM 2916 CB ALA A 239 173.779 6.051 118.495 1.00 77.01 C
ANISOU 2916 CB ALA A 239 8244 10827 10192 -119 -475 338 C
ATOM 2917 N ASN A 240 171.873 4.685 120.783 1.00 75.34 N
ANISOU 2917 N ASN A 240 8375 10193 10057 -12 -577 321 N
ATOM 2918 CA ASN A 240 170.910 3.646 121.154 1.00 74.35 C
ANISOU 2918 CA ASN A 240 8369 9905 9975 80 -570 276 C
ATOM 2919 C ASN A 240 169.664 4.243 121.820 1.00 77.05 C
ANISOU 2919 C ASN A 240 8892 10117 10268 -14 -582 292 C
ATOM 2920 O ASN A 240 168.546 3.854 121.469 1.00 76.26 O
ANISOU 2920 O ASN A 240 8882 9922 10170 15 -530 237 O
ATOM 2921 CB ASN A 240 171.562 2.613 122.082 1.00 75.01 C
ANISOU 2921 CB ASN A 240 8418 9951 10133 180 -646 313 C
ATOM 2922 CG ASN A 240 172.502 1.633 121.411 1.00 94.83 C
ANISOU 2922 CG ASN A 240 10769 12540 12723 330 -621 270 C
ATOM 2923 OD1 ASN A 240 172.677 1.613 120.185 1.00 89.20 O
ANISOU 2923 OD1 ASN A 240 9968 11920 12004 367 -535 195 O
ATOM 2924 ND2 ASN A 240 173.116 0.773 122.211 1.00 85.54 N
ANISOU 2924 ND2 ASN A 240 9553 11325 11622 426 -697 314 N
ATOM 2925 N MET A 241 169.851 5.182 122.769 1.00 72.93 N
ANISOU 2925 N MET A 241 8417 9594 9699 -127 -648 360 N
ATOM 2926 CA MET A 241 168.740 5.815 123.480 1.00 71.54 C
ANISOU 2926 CA MET A 241 8405 9302 9473 -210 -655 365 C
ATOM 2927 C MET A 241 168.052 6.873 122.621 1.00 73.48 C
ANISOU 2927 C MET A 241 8689 9552 9678 -285 -592 339 C
ATOM 2928 O MET A 241 166.827 6.963 122.668 1.00 72.18 O
ANISOU 2928 O MET A 241 8638 9286 9499 -290 -555 309 O
ATOM 2929 CB MET A 241 169.193 6.417 124.815 1.00 74.51 C
ANISOU 2929 CB MET A 241 8828 9676 9808 -302 -747 430 C
ATOM 2930 CG MET A 241 169.560 5.373 125.856 1.00 79.16 C
ANISOU 2930 CG MET A 241 9418 10234 10425 -237 -819 471 C
ATOM 2931 SD MET A 241 168.173 4.355 126.417 1.00 82.94 S
ANISOU 2931 SD MET A 241 10046 10553 10916 -173 -793 447 S
ATOM 2932 CE MET A 241 169.043 3.183 127.416 1.00 80.99 C
ANISOU 2932 CE MET A 241 9754 10304 10714 -98 -895 524 C
ATOM 2933 N LYS A 242 168.822 7.658 121.827 1.00 69.75 N
ANISOU 2933 N LYS A 242 8116 9199 9188 -344 -582 360 N
ATOM 2934 CA LYS A 242 168.280 8.685 120.923 1.00 68.52 C
ANISOU 2934 CA LYS A 242 7985 9053 8996 -420 -532 356 C
ATOM 2935 C LYS A 242 167.347 8.053 119.889 1.00 70.70 C
ANISOU 2935 C LYS A 242 8272 9309 9281 -341 -451 293 C
ATOM 2936 O LYS A 242 166.346 8.664 119.513 1.00 69.68 O
ANISOU 2936 O LYS A 242 8222 9124 9130 -380 -418 286 O
ATOM 2937 CB LYS A 242 169.400 9.467 120.225 1.00 71.69 C
ANISOU 2937 CB LYS A 242 8259 9604 9376 -499 -539 404 C
ATOM 2938 CG LYS A 242 169.920 10.635 121.047 1.00 84.64 C
ANISOU 2938 CG LYS A 242 9934 11236 10990 -637 -616 468 C
ATOM 2939 CD LYS A 242 171.083 11.331 120.355 1.00 94.71 C
ANISOU 2939 CD LYS A 242 11070 12668 12247 -728 -627 526 C
ATOM 2940 CE LYS A 242 171.576 12.525 121.134 1.00103.49 C
ANISOU 2940 CE LYS A 242 12226 13760 13335 -882 -710 587 C
ATOM 2941 NZ LYS A 242 172.893 12.998 120.634 1.00112.35 N
ANISOU 2941 NZ LYS A 242 13188 15055 14445 -975 -734 654 N
ATOM 2942 N GLY A 243 167.668 6.825 119.480 1.00 66.71 N
ANISOU 2942 N GLY A 243 7691 8843 8814 -229 -424 245 N
ATOM 2943 CA GLY A 243 166.865 6.037 118.555 1.00 65.83 C
ANISOU 2943 CA GLY A 243 7590 8711 8712 -152 -354 170 C
ATOM 2944 C GLY A 243 165.565 5.572 119.187 1.00 68.04 C
ANISOU 2944 C GLY A 243 8009 8835 9009 -128 -355 145 C
ATOM 2945 O GLY A 243 164.560 5.421 118.488 1.00 67.10 O
ANISOU 2945 O GLY A 243 7931 8685 8878 -118 -305 102 O
ATOM 2946 N ALA A 244 165.585 5.311 120.517 1.00 64.05 N
ANISOU 2946 N ALA A 244 7569 8244 8525 -124 -413 178 N
ATOM 2947 CA ALA A 244 164.408 4.894 121.288 1.00 62.81 C
ANISOU 2947 CA ALA A 244 7538 7952 8374 -116 -415 169 C
ATOM 2948 C ALA A 244 163.473 6.081 121.496 1.00 65.64 C
ANISOU 2948 C ALA A 244 7987 8268 8685 -204 -401 185 C
ATOM 2949 O ALA A 244 162.259 5.894 121.584 1.00 64.57 O
ANISOU 2949 O ALA A 244 7932 8055 8548 -197 -369 161 O
ATOM 2950 CB ALA A 244 164.824 4.305 122.624 1.00 63.87 C
ANISOU 2950 CB ALA A 244 7706 8032 8529 -95 -483 211 C
ATOM 2951 N ILE A 245 164.043 7.304 121.554 1.00 62.30 N
ANISOU 2951 N ILE A 245 7547 7894 8229 -285 -425 226 N
ATOM 2952 CA ILE A 245 163.298 8.560 121.668 1.00 61.69 C
ANISOU 2952 CA ILE A 245 7551 7770 8121 -363 -416 240 C
ATOM 2953 C ILE A 245 162.641 8.824 120.303 1.00 65.37 C
ANISOU 2953 C ILE A 245 7988 8266 8583 -357 -358 223 C
ATOM 2954 O ILE A 245 161.468 9.191 120.259 1.00 64.84 O
ANISOU 2954 O ILE A 245 7992 8131 8512 -362 -330 212 O
ATOM 2955 CB ILE A 245 164.198 9.733 122.154 1.00 65.32 C
ANISOU 2955 CB ILE A 245 8007 8258 8555 -460 -471 289 C
ATOM 2956 CG1 ILE A 245 164.761 9.458 123.570 1.00 66.17 C
ANISOU 2956 CG1 ILE A 245 8149 8342 8649 -475 -537 306 C
ATOM 2957 CG2 ILE A 245 163.440 11.066 122.125 1.00 65.80 C
ANISOU 2957 CG2 ILE A 245 8154 8250 8598 -530 -460 296 C
ATOM 2958 CD1 ILE A 245 166.147 10.078 123.860 1.00 75.24 C
ANISOU 2958 CD1 ILE A 245 9231 9573 9782 -553 -607 355 C
ATOM 2959 N THR A 246 163.387 8.573 119.197 1.00 62.05 N
ANISOU 2959 N THR A 246 7456 7960 8161 -341 -338 219 N
ATOM 2960 CA THR A 246 162.931 8.683 117.802 1.00 61.55 C
ANISOU 2960 CA THR A 246 7351 7960 8078 -338 -287 203 C
ATOM 2961 C THR A 246 161.716 7.770 117.604 1.00 64.53 C
ANISOU 2961 C THR A 246 7777 8272 8469 -274 -249 144 C
ATOM 2962 O THR A 246 160.714 8.189 117.023 1.00 63.93 O
ANISOU 2962 O THR A 246 7731 8182 8377 -293 -224 146 O
ATOM 2963 CB THR A 246 164.086 8.309 116.851 1.00 70.08 C
ANISOU 2963 CB THR A 246 8296 9189 9143 -321 -268 193 C
ATOM 2964 OG1 THR A 246 165.197 9.173 117.087 1.00 70.44 O
ANISOU 2964 OG1 THR A 246 8288 9301 9175 -396 -307 258 O
ATOM 2965 CG2 THR A 246 163.685 8.335 115.376 1.00 68.38 C
ANISOU 2965 CG2 THR A 246 8033 9063 8885 -325 -213 172 C
ATOM 2966 N LEU A 247 161.817 6.531 118.123 1.00 60.70 N
ANISOU 2966 N LEU A 247 7297 7746 8019 -203 -254 101 N
ATOM 2967 CA LEU A 247 160.784 5.503 118.103 1.00 60.08 C
ANISOU 2967 CA LEU A 247 7269 7595 7964 -152 -229 48 C
ATOM 2968 C LEU A 247 159.524 5.979 118.846 1.00 63.19 C
ANISOU 2968 C LEU A 247 7764 7892 8354 -187 -228 70 C
ATOM 2969 O LEU A 247 158.421 5.777 118.342 1.00 62.62 O
ANISOU 2969 O LEU A 247 7713 7800 8279 -183 -197 44 O
ATOM 2970 CB LEU A 247 161.349 4.218 118.740 1.00 60.56 C
ANISOU 2970 CB LEU A 247 7325 7610 8074 -80 -252 21 C
ATOM 2971 CG LEU A 247 160.365 3.094 119.049 1.00 64.98 C
ANISOU 2971 CG LEU A 247 7956 8066 8670 -41 -244 -17 C
ATOM 2972 CD1 LEU A 247 160.031 2.300 117.806 1.00 65.29 C
ANISOU 2972 CD1 LEU A 247 7960 8131 8716 -2 -202 -98 C
ATOM 2973 CD2 LEU A 247 160.892 2.206 120.147 1.00 67.80 C
ANISOU 2973 CD2 LEU A 247 8338 8349 9074 3 -291 4 C
ATOM 2974 N THR A 248 159.693 6.616 120.027 1.00 59.65 N
ANISOU 2974 N THR A 248 7371 7393 7900 -222 -262 112 N
ATOM 2975 CA THR A 248 158.591 7.141 120.845 1.00 59.07 C
ANISOU 2975 CA THR A 248 7389 7238 7817 -249 -253 122 C
ATOM 2976 C THR A 248 157.903 8.297 120.101 1.00 62.83 C
ANISOU 2976 C THR A 248 7866 7725 8280 -281 -228 137 C
ATOM 2977 O THR A 248 156.678 8.412 120.170 1.00 62.40 O
ANISOU 2977 O THR A 248 7853 7628 8231 -274 -199 128 O
ATOM 2978 CB THR A 248 159.083 7.563 122.247 1.00 68.06 C
ANISOU 2978 CB THR A 248 8585 8336 8938 -283 -295 151 C
ATOM 2979 OG1 THR A 248 159.927 6.547 122.794 1.00 67.59 O
ANISOU 2979 OG1 THR A 248 8506 8283 8892 -252 -333 157 O
ATOM 2980 CG2 THR A 248 157.934 7.829 123.214 1.00 67.11 C
ANISOU 2980 CG2 THR A 248 8560 8140 8800 -297 -274 143 C
ATOM 2981 N ILE A 249 158.686 9.134 119.380 1.00 59.51 N
ANISOU 2981 N ILE A 249 7395 7369 7846 -318 -243 169 N
ATOM 2982 CA ILE A 249 158.151 10.249 118.588 1.00 59.27 C
ANISOU 2982 CA ILE A 249 7363 7349 7810 -352 -231 202 C
ATOM 2983 C ILE A 249 157.348 9.663 117.416 1.00 62.95 C
ANISOU 2983 C ILE A 249 7784 7865 8268 -321 -196 181 C
ATOM 2984 O ILE A 249 156.206 10.069 117.215 1.00 62.95 O
ANISOU 2984 O ILE A 249 7810 7831 8276 -317 -180 191 O
ATOM 2985 CB ILE A 249 159.250 11.255 118.115 1.00 62.76 C
ANISOU 2985 CB ILE A 249 7762 7848 8235 -417 -262 257 C
ATOM 2986 CG1 ILE A 249 159.938 11.942 119.318 1.00 63.30 C
ANISOU 2986 CG1 ILE A 249 7885 7858 8308 -465 -307 275 C
ATOM 2987 CG2 ILE A 249 158.669 12.316 117.156 1.00 63.38 C
ANISOU 2987 CG2 ILE A 249 7838 7934 8310 -452 -257 309 C
ATOM 2988 CD1 ILE A 249 161.386 12.392 119.065 1.00 70.73 C
ANISOU 2988 CD1 ILE A 249 8759 8881 9233 -530 -345 319 C
ATOM 2989 N LEU A 250 157.926 8.682 116.690 1.00 58.80 N
ANISOU 2989 N LEU A 250 7191 7420 7729 -296 -184 144 N
ATOM 2990 CA LEU A 250 157.289 8.029 115.544 1.00 58.25 C
ANISOU 2990 CA LEU A 250 7082 7411 7640 -277 -154 107 C
ATOM 2991 C LEU A 250 155.989 7.307 115.926 1.00 61.89 C
ANISOU 2991 C LEU A 250 7593 7797 8125 -248 -138 70 C
ATOM 2992 O LEU A 250 155.008 7.415 115.187 1.00 61.79 O
ANISOU 2992 O LEU A 250 7569 7809 8098 -257 -124 72 O
ATOM 2993 CB LEU A 250 158.253 7.049 114.856 1.00 58.55 C
ANISOU 2993 CB LEU A 250 7047 7537 7662 -246 -139 52 C
ATOM 2994 CG LEU A 250 159.360 7.647 113.983 1.00 63.28 C
ANISOU 2994 CG LEU A 250 7562 8266 8216 -281 -136 82 C
ATOM 2995 CD1 LEU A 250 160.229 6.554 113.406 1.00 63.73 C
ANISOU 2995 CD1 LEU A 250 7543 8408 8262 -230 -110 6 C
ATOM 2996 CD2 LEU A 250 158.792 8.515 112.864 1.00 65.57 C
ANISOU 2996 CD2 LEU A 250 7831 8628 8454 -336 -128 131 C
ATOM 2997 N ILE A 251 155.970 6.597 117.071 1.00 58.30 N
ANISOU 2997 N ILE A 251 7188 7259 7702 -222 -144 48 N
ATOM 2998 CA ILE A 251 154.771 5.895 117.541 1.00 58.10 C
ANISOU 2998 CA ILE A 251 7208 7168 7697 -210 -128 24 C
ATOM 2999 C ILE A 251 153.766 6.939 118.046 1.00 62.37 C
ANISOU 2999 C ILE A 251 7788 7669 8240 -229 -118 65 C
ATOM 3000 O ILE A 251 152.583 6.835 117.728 1.00 62.25 O
ANISOU 3000 O ILE A 251 7766 7655 8229 -230 -98 61 O
ATOM 3001 CB ILE A 251 155.094 4.787 118.583 1.00 61.21 C
ANISOU 3001 CB ILE A 251 7645 7491 8121 -184 -141 2 C
ATOM 3002 CG1 ILE A 251 155.866 3.639 117.897 1.00 62.19 C
ANISOU 3002 CG1 ILE A 251 7726 7641 8261 -145 -146 -52 C
ATOM 3003 CG2 ILE A 251 153.815 4.242 119.249 1.00 61.66 C
ANISOU 3003 CG2 ILE A 251 7754 7482 8193 -194 -125 -1 C
ATOM 3004 CD1 ILE A 251 156.551 2.698 118.805 1.00 70.37 C
ANISOU 3004 CD1 ILE A 251 8789 8611 9337 -109 -174 -56 C
ATOM 3005 N GLY A 252 154.260 7.953 118.760 1.00 59.10 N
ANISOU 3005 N GLY A 252 7406 7224 7824 -243 -133 100 N
ATOM 3006 CA GLY A 252 153.456 9.061 119.265 1.00 58.80 C
ANISOU 3006 CA GLY A 252 7410 7137 7795 -250 -122 126 C
ATOM 3007 C GLY A 252 152.720 9.795 118.161 1.00 62.63 C
ANISOU 3007 C GLY A 252 7854 7657 8285 -250 -115 157 C
ATOM 3008 O GLY A 252 151.531 10.083 118.298 1.00 62.48 O
ANISOU 3008 O GLY A 252 7842 7612 8285 -231 -93 162 O
ATOM 3009 N VAL A 253 153.416 10.045 117.033 1.00 59.15 N
ANISOU 3009 N VAL A 253 7360 7289 7824 -272 -134 182 N
ATOM 3010 CA VAL A 253 152.886 10.713 115.840 1.00 59.08 C
ANISOU 3010 CA VAL A 253 7306 7334 7807 -284 -141 230 C
ATOM 3011 C VAL A 253 151.858 9.790 115.164 1.00 63.06 C
ANISOU 3011 C VAL A 253 7770 7890 8300 -270 -123 200 C
ATOM 3012 O VAL A 253 150.795 10.273 114.777 1.00 63.06 O
ANISOU 3012 O VAL A 253 7752 7897 8313 -262 -123 235 O
ATOM 3013 CB VAL A 253 154.034 11.167 114.894 1.00 63.03 C
ANISOU 3013 CB VAL A 253 7760 7917 8270 -328 -164 270 C
ATOM 3014 CG1 VAL A 253 153.572 11.328 113.447 1.00 63.13 C
ANISOU 3014 CG1 VAL A 253 7713 8029 8246 -348 -169 309 C
ATOM 3015 CG2 VAL A 253 154.656 12.462 115.405 1.00 63.03 C
ANISOU 3015 CG2 VAL A 253 7802 7855 8293 -360 -192 326 C
ATOM 3016 N PHE A 254 152.146 8.469 115.081 1.00 59.27 N
ANISOU 3016 N PHE A 254 7279 7438 7804 -265 -112 135 N
ATOM 3017 CA PHE A 254 151.234 7.467 114.517 1.00 58.86 C
ANISOU 3017 CA PHE A 254 7201 7422 7742 -266 -100 92 C
ATOM 3018 C PHE A 254 149.918 7.453 115.306 1.00 62.46 C
ANISOU 3018 C PHE A 254 7680 7817 8235 -254 -84 100 C
ATOM 3019 O PHE A 254 148.855 7.635 114.714 1.00 62.40 O
ANISOU 3019 O PHE A 254 7632 7850 8225 -261 -85 122 O
ATOM 3020 CB PHE A 254 151.883 6.062 114.510 1.00 60.64 C
ANISOU 3020 CB PHE A 254 7431 7648 7963 -257 -94 14 C
ATOM 3021 CG PHE A 254 150.930 4.921 114.221 1.00 62.36 C
ANISOU 3021 CG PHE A 254 7647 7864 8184 -267 -87 -40 C
ATOM 3022 CD1 PHE A 254 150.631 4.556 112.914 1.00 65.77 C
ANISOU 3022 CD1 PHE A 254 8032 8386 8571 -293 -91 -74 C
ATOM 3023 CD2 PHE A 254 150.325 4.218 115.259 1.00 64.41 C
ANISOU 3023 CD2 PHE A 254 7952 8036 8483 -265 -79 -53 C
ATOM 3024 CE1 PHE A 254 149.730 3.520 112.649 1.00 66.97 C
ANISOU 3024 CE1 PHE A 254 8187 8532 8725 -318 -93 -127 C
ATOM 3025 CE2 PHE A 254 149.416 3.191 114.992 1.00 67.46 C
ANISOU 3025 CE2 PHE A 254 8337 8416 8876 -292 -78 -95 C
ATOM 3026 CZ PHE A 254 149.126 2.848 113.690 1.00 65.91 C
ANISOU 3026 CZ PHE A 254 8099 8302 8644 -319 -87 -135 C
ATOM 3027 N VAL A 255 150.006 7.249 116.641 1.00 58.65 N
ANISOU 3027 N VAL A 255 7255 7251 7779 -239 -70 87 N
ATOM 3028 CA VAL A 255 148.879 7.183 117.573 1.00 58.27 C
ANISOU 3028 CA VAL A 255 7228 7156 7754 -230 -42 89 C
ATOM 3029 C VAL A 255 148.028 8.456 117.449 1.00 62.60 C
ANISOU 3029 C VAL A 255 7754 7709 8322 -208 -33 137 C
ATOM 3030 O VAL A 255 146.836 8.329 117.212 1.00 62.74 O
ANISOU 3030 O VAL A 255 7728 7758 8352 -204 -19 146 O
ATOM 3031 CB VAL A 255 149.342 6.915 119.035 1.00 61.82 C
ANISOU 3031 CB VAL A 255 7749 7531 8208 -226 -31 75 C
ATOM 3032 CG1 VAL A 255 148.223 7.170 120.042 1.00 61.73 C
ANISOU 3032 CG1 VAL A 255 7758 7491 8207 -218 9 82 C
ATOM 3033 CG2 VAL A 255 149.874 5.493 119.187 1.00 61.58 C
ANISOU 3033 CG2 VAL A 255 7737 7485 8177 -239 -44 40 C
ATOM 3034 N VAL A 256 148.637 9.659 117.547 1.00 58.91 N
ANISOU 3034 N VAL A 256 7311 7210 7863 -194 -46 169 N
ATOM 3035 CA VAL A 256 147.931 10.946 117.442 1.00 58.98 C
ANISOU 3035 CA VAL A 256 7308 7194 7907 -161 -45 216 C
ATOM 3036 C VAL A 256 147.214 11.066 116.073 1.00 63.93 C
ANISOU 3036 C VAL A 256 7854 7903 8533 -164 -68 263 C
ATOM 3037 O VAL A 256 146.036 11.427 116.042 1.00 64.46 O
ANISOU 3037 O VAL A 256 7882 7975 8634 -129 -57 288 O
ATOM 3038 CB VAL A 256 148.883 12.151 117.711 1.00 62.64 C
ANISOU 3038 CB VAL A 256 7825 7593 8383 -162 -67 242 C
ATOM 3039 CG1 VAL A 256 148.284 13.476 117.236 1.00 62.96 C
ANISOU 3039 CG1 VAL A 256 7851 7601 8469 -130 -83 303 C
ATOM 3040 CG2 VAL A 256 149.252 12.237 119.189 1.00 62.33 C
ANISOU 3040 CG2 VAL A 256 7865 7474 8343 -157 -45 195 C
ATOM 3041 N CYS A 257 147.908 10.735 114.968 1.00 60.27 N
ANISOU 3041 N CYS A 257 7360 7514 8025 -205 -100 274 N
ATOM 3042 CA CYS A 257 147.367 10.844 113.609 1.00 60.27 C
ANISOU 3042 CA CYS A 257 7288 7611 8000 -223 -129 321 C
ATOM 3043 C CYS A 257 146.271 9.812 113.303 1.00 64.03 C
ANISOU 3043 C CYS A 257 7715 8150 8465 -236 -121 288 C
ATOM 3044 O CYS A 257 145.420 10.094 112.462 1.00 64.25 O
ANISOU 3044 O CYS A 257 7679 8247 8488 -240 -147 338 O
ATOM 3045 CB CYS A 257 148.484 10.772 112.575 1.00 60.40 C
ANISOU 3045 CB CYS A 257 7288 7705 7954 -270 -156 331 C
ATOM 3046 SG CYS A 257 149.529 12.251 112.511 1.00 64.42 S
ANISOU 3046 SG CYS A 257 7829 8175 8475 -283 -184 413 S
ATOM 3047 N TRP A 258 146.288 8.638 113.960 1.00 60.16 N
ANISOU 3047 N TRP A 258 7252 7634 7972 -248 -94 214 N
ATOM 3048 CA TRP A 258 145.307 7.576 113.715 1.00 60.14 C
ANISOU 3048 CA TRP A 258 7210 7679 7961 -279 -90 180 C
ATOM 3049 C TRP A 258 144.224 7.464 114.807 1.00 62.88 C
ANISOU 3049 C TRP A 258 7554 7982 8354 -260 -53 181 C
ATOM 3050 O TRP A 258 143.224 6.782 114.577 1.00 63.15 O
ANISOU 3050 O TRP A 258 7539 8066 8388 -293 -54 173 O
ATOM 3051 CB TRP A 258 146.012 6.224 113.548 1.00 58.98 C
ANISOU 3051 CB TRP A 258 7095 7533 7782 -317 -90 99 C
ATOM 3052 CG TRP A 258 146.665 6.044 112.209 1.00 60.36 C
ANISOU 3052 CG TRP A 258 7242 7795 7895 -347 -118 78 C
ATOM 3053 CD1 TRP A 258 147.926 6.418 111.855 1.00 63.14 C
ANISOU 3053 CD1 TRP A 258 7606 8165 8217 -338 -122 78 C
ATOM 3054 CD2 TRP A 258 146.083 5.436 111.047 1.00 60.89 C
ANISOU 3054 CD2 TRP A 258 7262 7961 7912 -397 -142 51 C
ATOM 3055 NE1 TRP A 258 148.173 6.075 110.546 1.00 63.16 N
ANISOU 3055 NE1 TRP A 258 7570 8277 8150 -375 -138 50 N
ATOM 3056 CE2 TRP A 258 147.057 5.472 110.024 1.00 65.07 C
ANISOU 3056 CE2 TRP A 258 7781 8569 8375 -412 -153 28 C
ATOM 3057 CE3 TRP A 258 144.822 4.880 110.762 1.00 62.73 C
ANISOU 3057 CE3 TRP A 258 7454 8236 8144 -439 -156 43 C
ATOM 3058 CZ2 TRP A 258 146.819 4.953 108.745 1.00 65.18 C
ANISOU 3058 CZ2 TRP A 258 7755 8697 8311 -465 -175 -12 C
ATOM 3059 CZ3 TRP A 258 144.586 4.368 109.494 1.00 64.91 C
ANISOU 3059 CZ3 TRP A 258 7693 8619 8350 -497 -188 7 C
ATOM 3060 CH2 TRP A 258 145.572 4.417 108.499 1.00 65.80 C
ANISOU 3060 CH2 TRP A 258 7805 8807 8388 -509 -196 -24 C
ATOM 3061 N ALA A 259 144.402 8.134 115.968 1.00 58.09 N
ANISOU 3061 N ALA A 259 6996 7294 7781 -214 -20 188 N
ATOM 3062 CA ALA A 259 143.450 8.116 117.087 1.00 57.64 C
ANISOU 3062 CA ALA A 259 6937 7210 7755 -192 28 183 C
ATOM 3063 C ALA A 259 142.040 8.571 116.678 1.00 61.27 C
ANISOU 3063 C ALA A 259 7300 7734 8245 -168 33 227 C
ATOM 3064 O ALA A 259 141.101 7.842 117.010 1.00 61.02 O
ANISOU 3064 O ALA A 259 7226 7741 8216 -196 59 216 O
ATOM 3065 CB ALA A 259 143.953 8.960 118.251 1.00 58.21 C
ANISOU 3065 CB ALA A 259 7080 7196 7843 -146 59 175 C
ATOM 3066 N PRO A 260 141.832 9.703 115.944 1.00 57.61 N
ANISOU 3066 N PRO A 260 6793 7290 7807 -122 4 286 N
ATOM 3067 CA PRO A 260 140.457 10.083 115.589 1.00 58.12 C
ANISOU 3067 CA PRO A 260 6752 7421 7909 -89 3 335 C
ATOM 3068 C PRO A 260 139.795 9.061 114.669 1.00 61.77 C
ANISOU 3068 C PRO A 260 7138 7996 8336 -164 -32 340 C
ATOM 3069 O PRO A 260 138.613 8.786 114.849 1.00 62.45 O
ANISOU 3069 O PRO A 260 7142 8141 8444 -167 -14 352 O
ATOM 3070 CB PRO A 260 140.632 11.443 114.911 1.00 60.22 C
ANISOU 3070 CB PRO A 260 7006 7667 8210 -30 -39 408 C
ATOM 3071 CG PRO A 260 141.938 11.945 115.391 1.00 63.92 C
ANISOU 3071 CG PRO A 260 7582 8034 8672 -23 -34 384 C
ATOM 3072 CD PRO A 260 142.781 10.721 115.451 1.00 58.71 C
ANISOU 3072 CD PRO A 260 6970 7389 7948 -99 -32 322 C
ATOM 3073 N PHE A 261 140.563 8.455 113.739 1.00 57.37 N
ANISOU 3073 N PHE A 261 6605 7472 7721 -229 -77 320 N
ATOM 3074 CA PHE A 261 140.064 7.424 112.828 1.00 57.34 C
ANISOU 3074 CA PHE A 261 6548 7567 7671 -312 -114 302 C
ATOM 3075 C PHE A 261 139.655 6.170 113.597 1.00 61.07 C
ANISOU 3075 C PHE A 261 7039 8019 8147 -367 -80 241 C
ATOM 3076 O PHE A 261 138.608 5.596 113.301 1.00 61.48 O
ANISOU 3076 O PHE A 261 7017 8147 8197 -422 -94 248 O
ATOM 3077 CB PHE A 261 141.112 7.067 111.756 1.00 58.80 C
ANISOU 3077 CB PHE A 261 6771 7785 7786 -361 -157 272 C
ATOM 3078 CG PHE A 261 140.738 5.895 110.876 1.00 60.77 C
ANISOU 3078 CG PHE A 261 6990 8120 7979 -452 -191 223 C
ATOM 3079 CD1 PHE A 261 139.900 6.065 109.781 1.00 64.75 C
ANISOU 3079 CD1 PHE A 261 7403 8750 8448 -490 -245 271 C
ATOM 3080 CD2 PHE A 261 141.219 4.619 111.148 1.00 62.64 C
ANISOU 3080 CD2 PHE A 261 7293 8307 8201 -501 -175 127 C
ATOM 3081 CE1 PHE A 261 139.541 4.978 108.980 1.00 66.30 C
ANISOU 3081 CE1 PHE A 261 7579 9027 8585 -587 -280 213 C
ATOM 3082 CE2 PHE A 261 140.857 3.532 110.348 1.00 66.11 C
ANISOU 3082 CE2 PHE A 261 7718 8808 8595 -589 -208 68 C
ATOM 3083 CZ PHE A 261 140.019 3.720 109.272 1.00 65.14 C
ANISOU 3083 CZ PHE A 261 7507 8815 8427 -636 -260 105 C
ATOM 3084 N PHE A 262 140.490 5.726 114.556 1.00 56.67 N
ANISOU 3084 N PHE A 262 6577 7362 7593 -364 -43 191 N
ATOM 3085 CA PHE A 262 140.193 4.525 115.326 1.00 56.25 C
ANISOU 3085 CA PHE A 262 6554 7276 7544 -422 -17 148 C
ATOM 3086 C PHE A 262 139.080 4.769 116.346 1.00 60.51 C
ANISOU 3086 C PHE A 262 7042 7830 8118 -405 36 182 C
ATOM 3087 O PHE A 262 138.335 3.832 116.625 1.00 60.63 O
ANISOU 3087 O PHE A 262 7032 7871 8134 -477 46 175 O
ATOM 3088 CB PHE A 262 141.448 3.937 115.971 1.00 57.19 C
ANISOU 3088 CB PHE A 262 6784 7291 7654 -423 -7 98 C
ATOM 3089 CG PHE A 262 142.219 3.091 114.986 1.00 58.47 C
ANISOU 3089 CG PHE A 262 6977 7454 7784 -465 -50 41 C
ATOM 3090 CD1 PHE A 262 141.757 1.835 114.611 1.00 61.98 C
ANISOU 3090 CD1 PHE A 262 7421 7906 8222 -546 -72 -4 C
ATOM 3091 CD2 PHE A 262 143.378 3.570 114.393 1.00 60.25 C
ANISOU 3091 CD2 PHE A 262 7229 7679 7985 -427 -68 27 C
ATOM 3092 CE1 PHE A 262 142.452 1.067 113.674 1.00 63.04 C
ANISOU 3092 CE1 PHE A 262 7587 8038 8326 -575 -107 -76 C
ATOM 3093 CE2 PHE A 262 144.088 2.791 113.477 1.00 63.19 C
ANISOU 3093 CE2 PHE A 262 7622 8067 8322 -457 -96 -38 C
ATOM 3094 CZ PHE A 262 143.616 1.549 113.117 1.00 61.84 C
ANISOU 3094 CZ PHE A 262 7455 7896 8145 -525 -113 -96 C
ATOM 3095 N LEU A 263 138.907 6.022 116.838 1.00 57.14 N
ANISOU 3095 N LEU A 263 6595 7393 7722 -314 71 217 N
ATOM 3096 CA LEU A 263 137.789 6.358 117.731 1.00 57.58 C
ANISOU 3096 CA LEU A 263 6587 7483 7809 -282 132 239 C
ATOM 3097 C LEU A 263 136.508 6.343 116.899 1.00 63.13 C
ANISOU 3097 C LEU A 263 7150 8306 8530 -302 106 285 C
ATOM 3098 O LEU A 263 135.467 5.905 117.383 1.00 64.01 O
ANISOU 3098 O LEU A 263 7187 8481 8652 -336 143 296 O
ATOM 3099 CB LEU A 263 137.983 7.707 118.453 1.00 57.47 C
ANISOU 3099 CB LEU A 263 6597 7412 7826 -170 177 245 C
ATOM 3100 CG LEU A 263 136.942 8.069 119.539 1.00 62.63 C
ANISOU 3100 CG LEU A 263 7195 8098 8505 -122 260 244 C
ATOM 3101 CD1 LEU A 263 136.975 7.091 120.708 1.00 62.60 C
ANISOU 3101 CD1 LEU A 263 7246 8083 8458 -191 313 210 C
ATOM 3102 CD2 LEU A 263 137.159 9.472 120.056 1.00 64.89 C
ANISOU 3102 CD2 LEU A 263 7512 8316 8828 -4 295 234 C
ATOM 3103 N HIS A 264 136.617 6.764 115.621 1.00 59.72 N
ANISOU 3103 N HIS A 264 6679 7918 8094 -293 38 317 N
ATOM 3104 CA HIS A 264 135.554 6.736 114.620 1.00 60.29 C
ANISOU 3104 CA HIS A 264 6621 8116 8169 -324 -12 369 C
ATOM 3105 C HIS A 264 135.166 5.275 114.347 1.00 64.66 C
ANISOU 3105 C HIS A 264 7163 8722 8685 -459 -36 333 C
ATOM 3106 O HIS A 264 133.981 4.978 114.192 1.00 65.32 O
ANISOU 3106 O HIS A 264 7131 8908 8779 -505 -44 366 O
ATOM 3107 CB HIS A 264 136.032 7.440 113.334 1.00 60.87 C
ANISOU 3107 CB HIS A 264 6687 8216 8223 -301 -86 411 C
ATOM 3108 CG HIS A 264 135.115 7.290 112.164 1.00 65.02 C
ANISOU 3108 CG HIS A 264 7093 8881 8729 -352 -156 464 C
ATOM 3109 ND1 HIS A 264 134.298 8.320 111.762 1.00 67.58 N
ANISOU 3109 ND1 HIS A 264 7304 9273 9100 -277 -184 556 N
ATOM 3110 CD2 HIS A 264 134.933 6.237 111.333 1.00 66.79 C
ANISOU 3110 CD2 HIS A 264 7299 9186 8891 -472 -209 434 C
ATOM 3111 CE1 HIS A 264 133.621 7.857 110.725 1.00 67.68 C
ANISOU 3111 CE1 HIS A 264 7225 9418 9071 -358 -256 589 C
ATOM 3112 NE2 HIS A 264 133.971 6.610 110.433 1.00 67.59 N
ANISOU 3112 NE2 HIS A 264 7271 9420 8991 -482 -271 511 N
ATOM 3113 N LEU A 265 136.172 4.374 114.289 1.00 60.82 N
ANISOU 3113 N LEU A 265 6792 8160 8158 -521 -50 266 N
ATOM 3114 CA LEU A 265 135.997 2.937 114.071 1.00 61.11 C
ANISOU 3114 CA LEU A 265 6849 8203 8166 -647 -76 216 C
ATOM 3115 C LEU A 265 135.348 2.285 115.281 1.00 65.56 C
ANISOU 3115 C LEU A 265 7408 8744 8756 -693 -20 220 C
ATOM 3116 O LEU A 265 134.488 1.421 115.108 1.00 66.16 O
ANISOU 3116 O LEU A 265 7430 8878 8829 -800 -40 222 O
ATOM 3117 CB LEU A 265 137.337 2.263 113.751 1.00 60.49 C
ANISOU 3117 CB LEU A 265 6898 8031 8053 -670 -99 140 C
ATOM 3118 CG LEU A 265 137.432 1.603 112.377 1.00 65.89 C
ANISOU 3118 CG LEU A 265 7577 8773 8685 -750 -168 93 C
ATOM 3119 CD1 LEU A 265 137.219 2.614 111.256 1.00 66.44 C
ANISOU 3119 CD1 LEU A 265 7564 8959 8721 -716 -212 146 C
ATOM 3120 CD2 LEU A 265 138.766 0.902 112.203 1.00 67.80 C
ANISOU 3120 CD2 LEU A 265 7939 8918 8902 -754 -174 5 C
ATOM 3121 N ILE A 266 135.746 2.713 116.505 1.00 61.28 N
ANISOU 3121 N ILE A 266 6923 8128 8233 -623 49 223 N
ATOM 3122 CA ILE A 266 135.169 2.248 117.770 1.00 61.14 C
ANISOU 3122 CA ILE A 266 6902 8103 8225 -661 113 236 C
ATOM 3123 C ILE A 266 133.691 2.623 117.749 1.00 65.81 C
ANISOU 3123 C ILE A 266 7333 8833 8840 -663 138 290 C
ATOM 3124 O ILE A 266 132.844 1.765 117.974 1.00 66.70 O
ANISOU 3124 O ILE A 266 7391 9003 8950 -769 145 307 O
ATOM 3125 CB ILE A 266 135.932 2.836 118.999 1.00 63.47 C
ANISOU 3125 CB ILE A 266 7287 8312 8518 -576 177 225 C
ATOM 3126 CG1 ILE A 266 137.272 2.107 119.219 1.00 62.88 C
ANISOU 3126 CG1 ILE A 266 7358 8111 8423 -603 151 182 C
ATOM 3127 CG2 ILE A 266 135.078 2.808 120.286 1.00 64.84 C
ANISOU 3127 CG2 ILE A 266 7418 8529 8689 -588 262 251 C
ATOM 3128 CD1 ILE A 266 138.351 2.953 119.879 1.00 69.59 C
ANISOU 3128 CD1 ILE A 266 8293 8884 9265 -508 176 167 C
ATOM 3129 N PHE A 267 133.397 3.885 117.388 1.00 62.04 N
ANISOU 3129 N PHE A 267 6775 8408 8390 -550 143 323 N
ATOM 3130 CA PHE A 267 132.047 4.434 117.292 1.00 62.92 C
ANISOU 3130 CA PHE A 267 6718 8653 8537 -517 163 379 C
ATOM 3131 C PHE A 267 131.214 3.729 116.214 1.00 67.03 C
ANISOU 3131 C PHE A 267 7132 9288 9047 -630 86 408 C
ATOM 3132 O PHE A 267 130.035 3.481 116.447 1.00 67.50 O
ANISOU 3132 O PHE A 267 7061 9463 9124 -677 109 447 O
ATOM 3133 CB PHE A 267 132.096 5.952 117.030 1.00 64.71 C
ANISOU 3133 CB PHE A 267 6903 8876 8807 -360 166 409 C
ATOM 3134 CG PHE A 267 132.520 6.835 118.189 1.00 65.93 C
ANISOU 3134 CG PHE A 267 7123 8943 8983 -243 251 381 C
ATOM 3135 CD1 PHE A 267 132.843 6.288 119.429 1.00 68.76 C
ANISOU 3135 CD1 PHE A 267 7568 9249 9307 -280 322 336 C
ATOM 3136 CD2 PHE A 267 132.590 8.213 118.041 1.00 68.19 C
ANISOU 3136 CD2 PHE A 267 7392 9197 9321 -101 255 400 C
ATOM 3137 CE1 PHE A 267 133.227 7.105 120.495 1.00 69.54 C
ANISOU 3137 CE1 PHE A 267 7732 9279 9411 -182 397 301 C
ATOM 3138 CE2 PHE A 267 132.976 9.030 119.109 1.00 70.86 C
ANISOU 3138 CE2 PHE A 267 7801 9446 9678 -1 331 359 C
ATOM 3139 CZ PHE A 267 133.290 8.470 120.328 1.00 68.72 C
ANISOU 3139 CZ PHE A 267 7614 9139 9359 -44 403 304 C
ATOM 3140 N TYR A 268 131.833 3.381 115.063 1.00 63.27 N
ANISOU 3140 N TYR A 268 6711 8794 8537 -681 -1 385 N
ATOM 3141 CA TYR A 268 131.201 2.688 113.932 1.00 63.92 C
ANISOU 3141 CA TYR A 268 6717 8980 8591 -800 -86 395 C
ATOM 3142 C TYR A 268 130.570 1.353 114.367 1.00 68.92 C
ANISOU 3142 C TYR A 268 7340 9630 9215 -955 -79 377 C
ATOM 3143 O TYR A 268 129.457 1.055 113.951 1.00 70.26 O
ANISOU 3143 O TYR A 268 7378 9931 9388 -1040 -114 417 O
ATOM 3144 CB TYR A 268 132.227 2.455 112.798 1.00 64.48 C
ANISOU 3144 CB TYR A 268 6887 9006 8607 -828 -161 344 C
ATOM 3145 CG TYR A 268 131.652 1.856 111.530 1.00 67.08 C
ANISOU 3145 CG TYR A 268 7148 9450 8889 -948 -254 342 C
ATOM 3146 CD1 TYR A 268 131.133 2.667 110.526 1.00 69.80 C
ANISOU 3146 CD1 TYR A 268 7377 9923 9219 -915 -316 411 C
ATOM 3147 CD2 TYR A 268 131.677 0.482 111.310 1.00 68.14 C
ANISOU 3147 CD2 TYR A 268 7344 9556 8990 -1096 -287 270 C
ATOM 3148 CE1 TYR A 268 130.599 2.122 109.357 1.00 71.84 C
ANISOU 3148 CE1 TYR A 268 7574 10304 9419 -1036 -408 408 C
ATOM 3149 CE2 TYR A 268 131.154 -0.074 110.142 1.00 69.98 C
ANISOU 3149 CE2 TYR A 268 7525 9895 9171 -1217 -376 253 C
ATOM 3150 CZ TYR A 268 130.616 0.749 109.168 1.00 77.86 C
ANISOU 3150 CZ TYR A 268 8400 11042 10141 -1190 -436 322 C
ATOM 3151 OH TYR A 268 130.100 0.202 108.016 1.00 79.10 O
ANISOU 3151 OH TYR A 268 8506 11318 10231 -1319 -530 305 O
ATOM 3152 N ILE A 269 131.261 0.568 115.210 1.00 64.81 N
ANISOU 3152 N ILE A 269 6954 8981 8688 -998 -41 327 N
ATOM 3153 CA ILE A 269 130.762 -0.736 115.668 1.00 65.30 C
ANISOU 3153 CA ILE A 269 7031 9033 8749 -1153 -40 320 C
ATOM 3154 C ILE A 269 130.029 -0.660 117.014 1.00 68.99 C
ANISOU 3154 C ILE A 269 7434 9542 9237 -1153 53 373 C
ATOM 3155 O ILE A 269 129.182 -1.515 117.282 1.00 69.73 O
ANISOU 3155 O ILE A 269 7471 9692 9332 -1291 53 402 O
ATOM 3156 CB ILE A 269 131.890 -1.809 115.740 1.00 67.98 C
ANISOU 3156 CB ILE A 269 7554 9204 9073 -1216 -67 245 C
ATOM 3157 CG1 ILE A 269 133.141 -1.307 116.515 1.00 67.24 C
ANISOU 3157 CG1 ILE A 269 7585 8981 8982 -1090 -16 222 C
ATOM 3158 CG2 ILE A 269 132.238 -2.318 114.346 1.00 69.11 C
ANISOU 3158 CG2 ILE A 269 7733 9341 9185 -1277 -160 179 C
ATOM 3159 CD1 ILE A 269 134.157 -2.380 116.937 1.00 74.46 C
ANISOU 3159 CD1 ILE A 269 8663 9731 9897 -1138 -28 170 C
ATOM 3160 N SER A 270 130.360 0.331 117.861 1.00 64.48 N
ANISOU 3160 N SER A 270 6877 8946 8677 -1011 133 383 N
ATOM 3161 CA SER A 270 129.799 0.435 119.210 1.00 64.66 C
ANISOU 3161 CA SER A 270 6856 9009 8701 -1003 235 416 C
ATOM 3162 C SER A 270 128.577 1.347 119.339 1.00 69.30 C
ANISOU 3162 C SER A 270 7249 9762 9318 -928 290 468 C
ATOM 3163 O SER A 270 127.685 1.023 120.127 1.00 70.22 O
ANISOU 3163 O SER A 270 7275 9975 9429 -989 357 504 O
ATOM 3164 CB SER A 270 130.863 0.910 120.193 1.00 66.70 C
ANISOU 3164 CB SER A 270 7252 9147 8944 -901 295 383 C
ATOM 3165 OG SER A 270 132.065 0.172 120.050 1.00 73.02 O
ANISOU 3165 OG SER A 270 8219 9797 9727 -944 242 340 O
ATOM 3166 N CYS A 271 128.548 2.493 118.628 1.00 65.40 N
ANISOU 3166 N CYS A 271 6690 9302 8857 -791 268 475 N
ATOM 3167 CA CYS A 271 127.452 3.460 118.748 1.00 66.28 C
ANISOU 3167 CA CYS A 271 6616 9552 9014 -687 318 523 C
ATOM 3168 C CYS A 271 127.118 4.185 117.404 1.00 69.69 C
ANISOU 3168 C CYS A 271 6941 10052 9484 -621 229 564 C
ATOM 3169 O CYS A 271 126.996 5.412 117.414 1.00 69.38 O
ANISOU 3169 O CYS A 271 6846 10021 9495 -457 255 583 O
ATOM 3170 CB CYS A 271 127.780 4.466 119.850 1.00 66.59 C
ANISOU 3170 CB CYS A 271 6698 9535 9067 -531 425 492 C
ATOM 3171 SG CYS A 271 129.394 5.275 119.663 1.00 68.87 S
ANISOU 3171 SG CYS A 271 7183 9629 9354 -412 394 437 S
ATOM 3172 N PRO A 272 126.879 3.489 116.261 1.00 66.04 N
ANISOU 3172 N PRO A 272 6443 9651 9000 -746 122 584 N
ATOM 3173 CA PRO A 272 126.550 4.222 115.021 1.00 66.15 C
ANISOU 3173 CA PRO A 272 6353 9746 9036 -686 34 636 C
ATOM 3174 C PRO A 272 125.203 4.962 115.051 1.00 71.11 C
ANISOU 3174 C PRO A 272 6750 10539 9727 -603 56 716 C
ATOM 3175 O PRO A 272 124.971 5.827 114.209 1.00 71.52 O
ANISOU 3175 O PRO A 272 6718 10643 9814 -509 -7 774 O
ATOM 3176 CB PRO A 272 126.523 3.122 113.962 1.00 68.16 C
ANISOU 3176 CB PRO A 272 6623 10042 9233 -867 -75 624 C
ATOM 3177 CG PRO A 272 126.227 1.879 114.707 1.00 73.05 C
ANISOU 3177 CG PRO A 272 7269 10655 9832 -1022 -37 596 C
ATOM 3178 CD PRO A 272 126.937 2.033 116.013 1.00 67.66 C
ANISOU 3178 CD PRO A 272 6710 9842 9157 -946 70 557 C
ATOM 3179 N GLN A 273 124.324 4.612 116.002 1.00 67.79 N
ANISOU 3179 N GLN A 273 6224 10209 9322 -639 143 727 N
ATOM 3180 CA GLN A 273 122.993 5.199 116.184 1.00 69.02 C
ANISOU 3180 CA GLN A 273 6143 10540 9542 -561 184 796 C
ATOM 3181 C GLN A 273 123.031 6.438 117.106 1.00 72.94 C
ANISOU 3181 C GLN A 273 6627 10988 10101 -341 300 776 C
ATOM 3182 O GLN A 273 122.125 7.272 117.043 1.00 73.89 O
ANISOU 3182 O GLN A 273 6562 11217 10295 -211 321 829 O
ATOM 3183 CB GLN A 273 122.021 4.137 116.750 1.00 71.30 C
ANISOU 3183 CB GLN A 273 6316 10967 9806 -728 227 815 C
ATOM 3184 CG GLN A 273 122.200 3.779 118.243 1.00 77.84 C
ANISOU 3184 CG GLN A 273 7222 11746 10608 -746 365 767 C
ATOM 3185 CD GLN A 273 123.532 3.150 118.617 1.00 87.23 C
ANISOU 3185 CD GLN A 273 8671 12735 11737 -813 364 695 C
ATOM 3186 OE1 GLN A 273 124.078 2.293 117.910 1.00 78.32 O
ANISOU 3186 OE1 GLN A 273 7652 11532 10572 -946 267 677 O
ATOM 3187 NE2 GLN A 273 124.066 3.542 119.765 1.00 78.81 N
ANISOU 3187 NE2 GLN A 273 7704 11581 10659 -721 472 648 N
ATOM 3188 N ASN A 274 124.066 6.534 117.969 1.00 67.96 N
ANISOU 3188 N ASN A 274 6188 10192 9440 -300 371 698 N
ATOM 3189 CA ASN A 274 124.256 7.600 118.951 1.00 67.64 C
ANISOU 3189 CA ASN A 274 6178 10082 9440 -115 484 653 C
ATOM 3190 C ASN A 274 124.558 8.936 118.261 1.00 72.26 C
ANISOU 3190 C ASN A 274 6766 10588 10101 67 432 675 C
ATOM 3191 O ASN A 274 125.522 9.004 117.494 1.00 70.65 O
ANISOU 3191 O ASN A 274 6696 10272 9876 47 341 676 O
ATOM 3192 CB ASN A 274 125.390 7.218 119.910 1.00 64.16 C
ANISOU 3192 CB ASN A 274 5958 9489 8932 -157 543 570 C
ATOM 3193 CG ASN A 274 125.402 7.908 121.253 1.00 72.34 C
ANISOU 3193 CG ASN A 274 7021 10495 9972 -33 683 508 C
ATOM 3194 OD1 ASN A 274 125.099 9.095 121.388 1.00 67.73 O
ANISOU 3194 OD1 ASN A 274 6371 9905 9458 149 728 497 O
ATOM 3195 ND2 ASN A 274 125.836 7.188 122.274 1.00 57.29 N
ANISOU 3195 ND2 ASN A 274 5228 8554 7987 -128 750 463 N
ATOM 3196 N PRO A 275 123.760 10.008 118.526 1.00 71.02 N
ANISOU 3196 N PRO A 275 6463 10486 10034 248 489 696 N
ATOM 3197 CA PRO A 275 124.017 11.309 117.874 1.00 71.28 C
ANISOU 3197 CA PRO A 275 6505 10426 10155 424 431 730 C
ATOM 3198 C PRO A 275 125.387 11.904 118.207 1.00 74.60 C
ANISOU 3198 C PRO A 275 7159 10625 10562 487 443 660 C
ATOM 3199 O PRO A 275 125.959 12.605 117.370 1.00 73.93 O
ANISOU 3199 O PRO A 275 7134 10443 10511 546 352 702 O
ATOM 3200 CB PRO A 275 122.893 12.203 118.404 1.00 75.06 C
ANISOU 3200 CB PRO A 275 6792 10990 10736 609 520 741 C
ATOM 3201 CG PRO A 275 122.427 11.547 119.653 1.00 79.93 C
ANISOU 3201 CG PRO A 275 7370 11700 11300 551 661 673 C
ATOM 3202 CD PRO A 275 122.573 10.082 119.402 1.00 74.51 C
ANISOU 3202 CD PRO A 275 6721 11080 10509 303 609 691 C
ATOM 3203 N TYR A 276 125.918 11.607 119.413 1.00 70.87 N
ANISOU 3203 N TYR A 276 6812 10082 10032 461 548 563 N
ATOM 3204 CA TYR A 276 127.230 12.074 119.867 1.00 69.46 C
ANISOU 3204 CA TYR A 276 6853 9708 9829 499 562 490 C
ATOM 3205 C TYR A 276 128.347 11.354 119.105 1.00 71.30 C
ANISOU 3205 C TYR A 276 7232 9869 9992 356 457 503 C
ATOM 3206 O TYR A 276 129.417 11.929 118.905 1.00 69.79 O
ANISOU 3206 O TYR A 276 7184 9531 9802 396 419 485 O
ATOM 3207 CB TYR A 276 127.386 11.895 121.387 1.00 70.87 C
ANISOU 3207 CB TYR A 276 7108 9865 9954 500 699 389 C
ATOM 3208 CG TYR A 276 126.339 12.637 122.191 1.00 75.20 C
ANISOU 3208 CG TYR A 276 7519 10490 10562 651 820 355 C
ATOM 3209 CD1 TYR A 276 126.384 14.024 122.322 1.00 78.26 C
ANISOU 3209 CD1 TYR A 276 7922 10769 11044 850 846 319 C
ATOM 3210 CD2 TYR A 276 125.300 11.957 122.818 1.00 77.21 C
ANISOU 3210 CD2 TYR A 276 7626 10926 10784 595 911 355 C
ATOM 3211 CE1 TYR A 276 125.412 14.714 123.046 1.00 81.50 C
ANISOU 3211 CE1 TYR A 276 8202 11247 11518 1007 964 272 C
ATOM 3212 CE2 TYR A 276 124.332 12.635 123.557 1.00 80.13 C
ANISOU 3212 CE2 TYR A 276 7855 11387 11205 741 1035 315 C
ATOM 3213 CZ TYR A 276 124.393 14.014 123.671 1.00 89.57 C
ANISOU 3213 CZ TYR A 276 9067 12468 12497 955 1064 267 C
ATOM 3214 OH TYR A 276 123.434 14.686 124.393 1.00 93.75 O
ANISOU 3214 OH TYR A 276 9455 13082 13083 1116 1192 212 O
ATOM 3215 N CYS A 277 128.083 10.112 118.659 1.00 67.67 N
ANISOU 3215 N CYS A 277 6729 9510 9471 191 412 531 N
ATOM 3216 CA CYS A 277 129.021 9.322 117.870 1.00 66.09 C
ANISOU 3216 CA CYS A 277 6648 9259 9206 57 317 532 C
ATOM 3217 C CYS A 277 128.899 9.713 116.411 1.00 70.90 C
ANISOU 3217 C CYS A 277 7190 9909 9841 69 198 611 C
ATOM 3218 O CYS A 277 129.920 9.801 115.737 1.00 69.67 O
ANISOU 3218 O CYS A 277 7151 9667 9653 46 130 609 O
ATOM 3219 CB CYS A 277 128.797 7.828 118.069 1.00 66.07 C
ANISOU 3219 CB CYS A 277 6644 9326 9134 -123 321 517 C
ATOM 3220 SG CYS A 277 129.014 7.269 119.777 1.00 69.62 S
ANISOU 3220 SG CYS A 277 7185 9733 9534 -162 448 446 S
ATOM 3221 N VAL A 278 127.657 9.962 115.930 1.00 69.34 N
ANISOU 3221 N VAL A 278 6796 9855 9696 104 174 686 N
ATOM 3222 CA VAL A 278 127.344 10.388 114.558 1.00 70.03 C
ANISOU 3222 CA VAL A 278 6791 10012 9807 119 54 782 C
ATOM 3223 C VAL A 278 128.049 11.727 114.267 1.00 75.34 C
ANISOU 3223 C VAL A 278 7542 10549 10534 266 25 810 C
ATOM 3224 O VAL A 278 128.685 11.859 113.217 1.00 74.58 O
ANISOU 3224 O VAL A 278 7503 10430 10403 226 -74 855 O
ATOM 3225 CB VAL A 278 125.804 10.470 114.316 1.00 75.34 C
ANISOU 3225 CB VAL A 278 7220 10869 10536 146 43 861 C
ATOM 3226 CG1 VAL A 278 125.458 11.288 113.071 1.00 76.01 C
ANISOU 3226 CG1 VAL A 278 7203 11010 10668 216 -75 977 C
ATOM 3227 CG2 VAL A 278 125.191 9.081 114.217 1.00 75.33 C
ANISOU 3227 CG2 VAL A 278 7145 11009 10467 -45 29 854 C
ATOM 3228 N CYS A 279 127.959 12.696 115.211 1.00 73.58 N
ANISOU 3228 N CYS A 279 7328 10236 10392 426 114 780 N
ATOM 3229 CA CYS A 279 128.577 14.019 115.090 1.00 73.95 C
ANISOU 3229 CA CYS A 279 7458 10131 10508 567 93 800 C
ATOM 3230 C CYS A 279 130.091 13.895 114.935 1.00 75.33 C
ANISOU 3230 C CYS A 279 7840 10171 10611 491 61 758 C
ATOM 3231 O CYS A 279 130.664 14.596 114.104 1.00 74.89 O
ANISOU 3231 O CYS A 279 7833 10050 10570 518 -21 822 O
ATOM 3232 CB CYS A 279 128.210 14.914 116.270 1.00 75.70 C
ANISOU 3232 CB CYS A 279 7669 10274 10820 737 207 742 C
ATOM 3233 SG CYS A 279 128.710 16.643 116.065 1.00 80.56 S
ANISOU 3233 SG CYS A 279 8364 10694 11553 923 170 778 S
ATOM 3234 N PHE A 280 130.727 12.984 115.702 1.00 69.94 N
ANISOU 3234 N PHE A 280 7269 9456 9849 392 122 662 N
ATOM 3235 CA PHE A 280 132.163 12.715 115.607 1.00 67.68 C
ANISOU 3235 CA PHE A 280 7161 9061 9493 315 96 618 C
ATOM 3236 C PHE A 280 132.461 12.025 114.275 1.00 70.56 C
ANISOU 3236 C PHE A 280 7518 9504 9788 192 -9 666 C
ATOM 3237 O PHE A 280 133.377 12.436 113.576 1.00 70.14 O
ANISOU 3237 O PHE A 280 7545 9391 9712 184 -70 693 O
ATOM 3238 CB PHE A 280 132.646 11.857 116.794 1.00 68.45 C
ANISOU 3238 CB PHE A 280 7360 9117 9530 247 182 515 C
ATOM 3239 CG PHE A 280 134.128 11.544 116.797 1.00 68.47 C
ANISOU 3239 CG PHE A 280 7534 9014 9469 179 158 469 C
ATOM 3240 CD1 PHE A 280 134.617 10.402 116.170 1.00 70.70 C
ANISOU 3240 CD1 PHE A 280 7851 9335 9676 46 106 459 C
ATOM 3241 CD2 PHE A 280 135.032 12.381 117.441 1.00 69.94 C
ANISOU 3241 CD2 PHE A 280 7842 9060 9672 248 186 430 C
ATOM 3242 CE1 PHE A 280 135.984 10.115 116.171 1.00 70.34 C
ANISOU 3242 CE1 PHE A 280 7946 9200 9580 -2 88 415 C
ATOM 3243 CE2 PHE A 280 136.400 12.096 117.436 1.00 71.38 C
ANISOU 3243 CE2 PHE A 280 8163 9160 9798 183 161 395 C
ATOM 3244 CZ PHE A 280 136.868 10.970 116.793 1.00 68.75 C
ANISOU 3244 CZ PHE A 280 7849 8877 9396 66 114 390 C
ATOM 3245 N MET A 281 131.660 11.008 113.911 1.00 66.69 N
ANISOU 3245 N MET A 281 6925 9154 9259 92 -29 676 N
ATOM 3246 CA MET A 281 131.803 10.223 112.685 1.00 65.87 C
ANISOU 3246 CA MET A 281 6809 9141 9079 -38 -124 700 C
ATOM 3247 C MET A 281 131.611 11.047 111.401 1.00 70.30 C
ANISOU 3247 C MET A 281 7298 9763 9652 -1 -226 810 C
ATOM 3248 O MET A 281 132.089 10.630 110.345 1.00 69.25 O
ANISOU 3248 O MET A 281 7195 9681 9437 -98 -303 823 O
ATOM 3249 CB MET A 281 130.831 9.036 112.687 1.00 68.67 C
ANISOU 3249 CB MET A 281 7062 9626 9403 -154 -123 686 C
ATOM 3250 CG MET A 281 131.352 7.838 113.457 1.00 71.24 C
ANISOU 3250 CG MET A 281 7497 9894 9676 -258 -68 588 C
ATOM 3251 SD MET A 281 130.204 6.443 113.519 1.00 76.27 S
ANISOU 3251 SD MET A 281 8027 10666 10287 -413 -70 579 S
ATOM 3252 CE MET A 281 130.199 5.933 111.806 1.00 73.27 C
ANISOU 3252 CE MET A 281 7616 10386 9836 -531 -204 603 C
ATOM 3253 N SER A 282 130.936 12.211 111.491 1.00 68.49 N
ANISOU 3253 N SER A 282 6977 9526 9521 139 -227 889 N
ATOM 3254 CA SER A 282 130.697 13.088 110.342 1.00 69.47 C
ANISOU 3254 CA SER A 282 7028 9697 9669 187 -331 1016 C
ATOM 3255 C SER A 282 131.976 13.847 109.930 1.00 72.48 C
ANISOU 3255 C SER A 282 7553 9954 10033 206 -367 1039 C
ATOM 3256 O SER A 282 132.056 14.323 108.800 1.00 72.99 O
ANISOU 3256 O SER A 282 7588 10069 10074 193 -466 1145 O
ATOM 3257 CB SER A 282 129.558 14.065 110.627 1.00 74.92 C
ANISOU 3257 CB SER A 282 7572 10405 10489 345 -320 1094 C
ATOM 3258 OG SER A 282 129.925 15.084 111.542 1.00 84.79 O
ANISOU 3258 OG SER A 282 8902 11484 11832 491 -248 1063 O
ATOM 3259 N HIS A 283 132.981 13.928 110.827 1.00 67.22 N
ANISOU 3259 N HIS A 283 7035 9138 9368 224 -293 948 N
ATOM 3260 CA HIS A 283 134.253 14.602 110.553 1.00 66.03 C
ANISOU 3260 CA HIS A 283 7018 8871 9199 229 -320 963 C
ATOM 3261 C HIS A 283 135.314 13.591 110.060 1.00 67.69 C
ANISOU 3261 C HIS A 283 7320 9116 9281 84 -336 901 C
ATOM 3262 O HIS A 283 136.512 13.824 110.232 1.00 66.43 O
ANISOU 3262 O HIS A 283 7285 8859 9099 72 -323 868 O
ATOM 3263 CB HIS A 283 134.749 15.362 111.803 1.00 66.53 C
ANISOU 3263 CB HIS A 283 7184 8753 9340 332 -238 901 C
ATOM 3264 CG HIS A 283 133.764 16.347 112.363 1.00 71.36 C
ANISOU 3264 CG HIS A 283 7717 9315 10081 489 -207 935 C
ATOM 3265 ND1 HIS A 283 133.382 17.474 111.654 1.00 74.47 N
ANISOU 3265 ND1 HIS A 283 8054 9683 10559 581 -282 1060 N
ATOM 3266 CD2 HIS A 283 133.139 16.355 113.562 1.00 73.42 C
ANISOU 3266 CD2 HIS A 283 7951 9546 10399 570 -107 856 C
ATOM 3267 CE1 HIS A 283 132.521 18.112 112.431 1.00 74.99 C
ANISOU 3267 CE1 HIS A 283 8055 9697 10739 727 -224 1046 C
ATOM 3268 NE2 HIS A 283 132.343 17.477 113.589 1.00 74.76 N
ANISOU 3268 NE2 HIS A 283 8039 9673 10693 724 -113 920 N
ATOM 3269 N PHE A 284 134.864 12.491 109.411 1.00 63.83 N
ANISOU 3269 N PHE A 284 6766 8772 8713 -25 -369 883 N
ATOM 3270 CA PHE A 284 135.698 11.403 108.882 1.00 62.74 C
ANISOU 3270 CA PHE A 284 6701 8679 8459 -156 -383 808 C
ATOM 3271 C PHE A 284 136.769 11.892 107.905 1.00 67.43 C
ANISOU 3271 C PHE A 284 7358 9276 8985 -188 -439 854 C
ATOM 3272 O PHE A 284 137.885 11.376 107.928 1.00 66.01 O
ANISOU 3272 O PHE A 284 7278 9060 8742 -242 -414 775 O
ATOM 3273 CB PHE A 284 134.832 10.329 108.200 1.00 64.89 C
ANISOU 3273 CB PHE A 284 6880 9109 8668 -263 -426 795 C
ATOM 3274 CG PHE A 284 135.582 9.091 107.759 1.00 65.46 C
ANISOU 3274 CG PHE A 284 7029 9210 8631 -390 -431 691 C
ATOM 3275 CD1 PHE A 284 136.145 8.228 108.691 1.00 67.27 C
ANISOU 3275 CD1 PHE A 284 7354 9342 8863 -413 -359 576 C
ATOM 3276 CD2 PHE A 284 135.735 8.793 106.412 1.00 67.90 C
ANISOU 3276 CD2 PHE A 284 7321 9645 8835 -481 -508 707 C
ATOM 3277 CE1 PHE A 284 136.811 7.071 108.288 1.00 67.69 C
ANISOU 3277 CE1 PHE A 284 7477 9407 8834 -514 -365 477 C
ATOM 3278 CE2 PHE A 284 136.408 7.635 106.008 1.00 70.20 C
ANISOU 3278 CE2 PHE A 284 7685 9957 9030 -587 -505 592 C
ATOM 3279 CZ PHE A 284 136.948 6.786 106.949 1.00 67.31 C
ANISOU 3279 CZ PHE A 284 7411 9477 8688 -595 -433 477 C
ATOM 3280 N ASN A 285 136.426 12.878 107.057 1.00 66.02 N
ANISOU 3280 N ASN A 285 7116 9148 8821 -153 -515 988 N
ATOM 3281 CA ASN A 285 137.317 13.469 106.061 1.00 66.38 C
ANISOU 3281 CA ASN A 285 7207 9217 8800 -191 -575 1063 C
ATOM 3282 C ASN A 285 138.529 14.160 106.723 1.00 70.18 C
ANISOU 3282 C ASN A 285 7811 9535 9319 -146 -529 1043 C
ATOM 3283 O ASN A 285 139.636 14.086 106.181 1.00 69.49 O
ANISOU 3283 O ASN A 285 7789 9468 9147 -214 -540 1034 O
ATOM 3284 CB ASN A 285 136.538 14.442 105.182 1.00 68.97 C
ANISOU 3284 CB ASN A 285 7434 9616 9155 -153 -670 1232 C
ATOM 3285 CG ASN A 285 135.787 13.807 104.025 1.00 96.31 C
ANISOU 3285 CG ASN A 285 10791 13284 12517 -249 -750 1274 C
ATOM 3286 OD1 ASN A 285 135.762 12.581 103.838 1.00 88.86 O
ANISOU 3286 OD1 ASN A 285 9848 12431 11484 -350 -735 1165 O
ATOM 3287 ND2 ASN A 285 135.162 14.641 103.206 1.00 91.35 N
ANISOU 3287 ND2 ASN A 285 10074 12731 11904 -222 -845 1436 N
ATOM 3288 N LEU A 286 138.327 14.780 107.911 1.00 66.69 N
ANISOU 3288 N LEU A 286 7398 8944 8998 -37 -474 1026 N
ATOM 3289 CA LEU A 286 139.389 15.421 108.698 1.00 65.83 C
ANISOU 3289 CA LEU A 286 7407 8673 8930 1 -431 994 C
ATOM 3290 C LEU A 286 140.318 14.366 109.296 1.00 67.97 C
ANISOU 3290 C LEU A 286 7762 8926 9137 -64 -367 856 C
ATOM 3291 O LEU A 286 141.516 14.613 109.448 1.00 67.08 O
ANISOU 3291 O LEU A 286 7738 8746 9002 -87 -356 836 O
ATOM 3292 CB LEU A 286 138.796 16.286 109.825 1.00 66.43 C
ANISOU 3292 CB LEU A 286 7490 8608 9143 133 -387 992 C
ATOM 3293 CG LEU A 286 138.279 17.667 109.432 1.00 72.79 C
ANISOU 3293 CG LEU A 286 8257 9353 10047 226 -448 1128 C
ATOM 3294 CD1 LEU A 286 137.025 18.018 110.208 1.00 73.93 C
ANISOU 3294 CD1 LEU A 286 8324 9456 10310 357 -407 1118 C
ATOM 3295 CD2 LEU A 286 139.344 18.732 109.643 1.00 75.27 C
ANISOU 3295 CD2 LEU A 286 8690 9508 10402 243 -459 1159 C
ATOM 3296 N TYR A 287 139.753 13.189 109.635 1.00 63.75 N
ANISOU 3296 N TYR A 287 7193 8451 8577 -95 -330 769 N
ATOM 3297 CA TYR A 287 140.474 12.056 110.220 1.00 62.13 C
ANISOU 3297 CA TYR A 287 7059 8224 8323 -150 -276 645 C
ATOM 3298 C TYR A 287 141.335 11.403 109.154 1.00 66.62 C
ANISOU 3298 C TYR A 287 7646 8884 8782 -245 -311 622 C
ATOM 3299 O TYR A 287 142.432 10.946 109.460 1.00 65.82 O
ANISOU 3299 O TYR A 287 7622 8739 8648 -271 -280 549 O
ATOM 3300 CB TYR A 287 139.510 11.042 110.873 1.00 62.71 C
ANISOU 3300 CB TYR A 287 7089 8326 8412 -162 -234 578 C
ATOM 3301 CG TYR A 287 138.494 11.651 111.824 1.00 64.27 C
ANISOU 3301 CG TYR A 287 7241 8474 8706 -68 -192 600 C
ATOM 3302 CD1 TYR A 287 138.757 12.849 112.487 1.00 66.07 C
ANISOU 3302 CD1 TYR A 287 7516 8582 9006 27 -168 624 C
ATOM 3303 CD2 TYR A 287 137.280 11.020 112.076 1.00 65.37 C
ANISOU 3303 CD2 TYR A 287 7289 8687 8862 -79 -172 588 C
ATOM 3304 CE1 TYR A 287 137.829 13.415 113.354 1.00 67.01 C
ANISOU 3304 CE1 TYR A 287 7591 8658 9211 125 -120 627 C
ATOM 3305 CE2 TYR A 287 136.341 11.581 112.939 1.00 66.72 C
ANISOU 3305 CE2 TYR A 287 7401 8832 9116 14 -122 603 C
ATOM 3306 CZ TYR A 287 136.622 12.778 113.578 1.00 73.15 C
ANISOU 3306 CZ TYR A 287 8265 9527 10001 122 -92 616 C
ATOM 3307 OH TYR A 287 135.722 13.351 114.439 1.00 73.80 O
ANISOU 3307 OH TYR A 287 8293 9583 10164 225 -33 612 O
ATOM 3308 N LEU A 288 140.862 11.406 107.892 1.00 64.28 N
ANISOU 3308 N LEU A 288 7276 8723 8427 -293 -375 686 N
ATOM 3309 CA LEU A 288 141.626 10.893 106.756 1.00 64.31 C
ANISOU 3309 CA LEU A 288 7289 8836 8309 -383 -406 664 C
ATOM 3310 C LEU A 288 142.772 11.847 106.445 1.00 69.17 C
ANISOU 3310 C LEU A 288 7954 9422 8906 -379 -418 727 C
ATOM 3311 O LEU A 288 143.850 11.392 106.071 1.00 68.56 O
ANISOU 3311 O LEU A 288 7917 9383 8750 -431 -402 670 O
ATOM 3312 CB LEU A 288 140.748 10.705 105.514 1.00 65.28 C
ANISOU 3312 CB LEU A 288 7320 9125 8360 -444 -477 720 C
ATOM 3313 CG LEU A 288 139.605 9.709 105.593 1.00 69.89 C
ANISOU 3313 CG LEU A 288 7842 9768 8945 -480 -481 664 C
ATOM 3314 CD1 LEU A 288 138.663 9.931 104.461 1.00 71.25 C
ANISOU 3314 CD1 LEU A 288 7909 10096 9065 -524 -566 759 C
ATOM 3315 CD2 LEU A 288 140.105 8.270 105.601 1.00 71.41 C
ANISOU 3315 CD2 LEU A 288 8091 9970 9072 -555 -446 513 C
ATOM 3316 N ILE A 289 142.539 13.171 106.626 1.00 66.73 N
ANISOU 3316 N ILE A 289 7639 9039 8676 -315 -445 845 N
ATOM 3317 CA ILE A 289 143.529 14.234 106.433 1.00 66.79 C
ANISOU 3317 CA ILE A 289 7697 8994 8686 -317 -464 925 C
ATOM 3318 C ILE A 289 144.648 14.065 107.474 1.00 69.76 C
ANISOU 3318 C ILE A 289 8164 9252 9087 -305 -400 830 C
ATOM 3319 O ILE A 289 145.819 14.217 107.128 1.00 69.07 O
ANISOU 3319 O ILE A 289 8113 9187 8944 -356 -401 836 O
ATOM 3320 CB ILE A 289 142.858 15.637 106.461 1.00 70.87 C
ANISOU 3320 CB ILE A 289 8192 9431 9304 -243 -514 1067 C
ATOM 3321 CG1 ILE A 289 142.340 15.980 105.049 1.00 72.58 C
ANISOU 3321 CG1 ILE A 289 8328 9793 9456 -289 -602 1203 C
ATOM 3322 CG2 ILE A 289 143.794 16.742 107.012 1.00 71.47 C
ANISOU 3322 CG2 ILE A 289 8356 9353 9445 -217 -508 1109 C
ATOM 3323 CD1 ILE A 289 141.547 17.233 104.931 1.00 82.41 C
ANISOU 3323 CD1 ILE A 289 9536 10972 10804 -211 -665 1355 C
ATOM 3324 N LEU A 290 144.290 13.693 108.722 1.00 65.93 N
ANISOU 3324 N LEU A 290 7710 8664 8675 -247 -346 745 N
ATOM 3325 CA LEU A 290 145.260 13.450 109.789 1.00 64.99 C
ANISOU 3325 CA LEU A 290 7675 8443 8575 -238 -292 658 C
ATOM 3326 C LEU A 290 146.111 12.211 109.474 1.00 68.27 C
ANISOU 3326 C LEU A 290 8101 8938 8902 -302 -271 563 C
ATOM 3327 O LEU A 290 147.284 12.180 109.837 1.00 67.61 O
ANISOU 3327 O LEU A 290 8069 8816 8806 -316 -251 527 O
ATOM 3328 CB LEU A 290 144.565 13.314 111.150 1.00 64.83 C
ANISOU 3328 CB LEU A 290 7678 8317 8636 -170 -242 598 C
ATOM 3329 CG LEU A 290 145.201 14.118 112.291 1.00 69.52 C
ANISOU 3329 CG LEU A 290 8358 8764 9291 -127 -215 583 C
ATOM 3330 CD1 LEU A 290 144.846 15.604 112.201 1.00 70.55 C
ANISOU 3330 CD1 LEU A 290 8493 8813 9498 -72 -249 680 C
ATOM 3331 CD2 LEU A 290 144.768 13.581 113.632 1.00 71.87 C
ANISOU 3331 CD2 LEU A 290 8686 8996 9624 -86 -153 494 C
ATOM 3332 N ILE A 291 145.534 11.224 108.753 1.00 64.95 N
ANISOU 3332 N ILE A 291 7628 8628 8422 -342 -279 522 N
ATOM 3333 CA ILE A 291 146.219 10.011 108.290 1.00 64.46 C
ANISOU 3333 CA ILE A 291 7573 8640 8278 -395 -261 422 C
ATOM 3334 C ILE A 291 147.240 10.425 107.196 1.00 68.64 C
ANISOU 3334 C ILE A 291 8089 9271 8719 -445 -282 462 C
ATOM 3335 O ILE A 291 148.348 9.880 107.171 1.00 67.73 O
ANISOU 3335 O ILE A 291 7998 9174 8563 -462 -252 390 O
ATOM 3336 CB ILE A 291 145.186 8.942 107.814 1.00 67.93 C
ANISOU 3336 CB ILE A 291 7967 9159 8684 -431 -272 367 C
ATOM 3337 CG1 ILE A 291 144.440 8.314 109.010 1.00 68.13 C
ANISOU 3337 CG1 ILE A 291 8012 9087 8788 -399 -237 313 C
ATOM 3338 CG2 ILE A 291 145.823 7.856 106.956 1.00 68.66 C
ANISOU 3338 CG2 ILE A 291 8062 9346 8678 -492 -267 269 C
ATOM 3339 CD1 ILE A 291 143.081 7.672 108.653 1.00 77.94 C
ANISOU 3339 CD1 ILE A 291 9190 10400 10023 -436 -259 305 C
ATOM 3340 N MET A 292 146.877 11.418 106.329 1.00 66.05 N
ANISOU 3340 N MET A 292 7718 9012 8364 -467 -334 587 N
ATOM 3341 CA MET A 292 147.769 11.973 105.290 1.00 66.42 C
ANISOU 3341 CA MET A 292 7748 9167 8322 -527 -358 656 C
ATOM 3342 C MET A 292 148.975 12.628 105.945 1.00 69.34 C
ANISOU 3342 C MET A 292 8169 9445 8731 -516 -335 674 C
ATOM 3343 O MET A 292 150.084 12.537 105.424 1.00 69.18 O
ANISOU 3343 O MET A 292 8141 9510 8634 -566 -320 662 O
ATOM 3344 CB MET A 292 147.082 13.039 104.396 1.00 69.88 C
ANISOU 3344 CB MET A 292 8139 9669 8742 -549 -429 816 C
ATOM 3345 CG MET A 292 145.699 12.701 103.881 1.00 74.07 C
ANISOU 3345 CG MET A 292 8607 10277 9258 -551 -471 836 C
ATOM 3346 SD MET A 292 145.605 11.499 102.544 1.00 78.98 S
ANISOU 3346 SD MET A 292 9180 11117 9712 -648 -481 754 S
ATOM 3347 CE MET A 292 146.566 12.291 101.315 1.00 76.62 C
ANISOU 3347 CE MET A 292 8864 10963 9285 -728 -512 864 C
ATOM 3348 N CYS A 293 148.729 13.320 107.082 1.00 65.07 N
ANISOU 3348 N CYS A 293 7677 8741 8308 -455 -333 702 N
ATOM 3349 CA CYS A 293 149.716 14.047 107.876 1.00 64.29 C
ANISOU 3349 CA CYS A 293 7636 8532 8261 -448 -323 720 C
ATOM 3350 C CYS A 293 150.741 13.105 108.493 1.00 66.97 C
ANISOU 3350 C CYS A 293 8000 8864 8581 -450 -272 600 C
ATOM 3351 O CYS A 293 151.898 13.491 108.592 1.00 66.43 O
ANISOU 3351 O CYS A 293 7946 8794 8500 -482 -269 617 O
ATOM 3352 CB CYS A 293 149.034 14.900 108.939 1.00 64.35 C
ANISOU 3352 CB CYS A 293 7692 8370 8389 -378 -329 754 C
ATOM 3353 SG CYS A 293 148.059 16.269 108.268 1.00 69.33 S
ANISOU 3353 SG CYS A 293 8296 8975 9070 -359 -398 916 S
ATOM 3354 N ASN A 294 150.345 11.867 108.862 1.00 63.12 N
ANISOU 3354 N ASN A 294 7513 8377 8094 -421 -238 488 N
ATOM 3355 CA ASN A 294 151.255 10.852 109.415 1.00 62.60 C
ANISOU 3355 CA ASN A 294 7468 8298 8019 -411 -198 378 C
ATOM 3356 C ASN A 294 152.377 10.534 108.415 1.00 67.14 C
ANISOU 3356 C ASN A 294 7998 9010 8501 -459 -188 358 C
ATOM 3357 O ASN A 294 153.503 10.259 108.824 1.00 66.59 O
ANISOU 3357 O ASN A 294 7935 8933 8433 -453 -166 314 O
ATOM 3358 CB ASN A 294 150.485 9.571 109.769 1.00 63.33 C
ANISOU 3358 CB ASN A 294 7568 8369 8126 -383 -175 279 C
ATOM 3359 CG ASN A 294 151.218 8.549 110.617 1.00 85.71 C
ANISOU 3359 CG ASN A 294 10439 11143 10983 -357 -143 181 C
ATOM 3360 OD1 ASN A 294 150.790 7.397 110.726 1.00 81.11 O
ANISOU 3360 OD1 ASN A 294 9864 10549 10404 -348 -129 101 O
ATOM 3361 ND2 ASN A 294 152.306 8.934 111.274 1.00 77.49 N
ANISOU 3361 ND2 ASN A 294 9424 10056 9963 -348 -138 191 N
ATOM 3362 N SER A 295 152.059 10.613 107.110 1.00 64.46 N
ANISOU 3362 N SER A 295 7607 8809 8077 -506 -206 394 N
ATOM 3363 CA SER A 295 152.959 10.377 105.982 1.00 65.01 C
ANISOU 3363 CA SER A 295 7623 9043 8033 -558 -190 377 C
ATOM 3364 C SER A 295 153.823 11.614 105.650 1.00 69.36 C
ANISOU 3364 C SER A 295 8156 9639 8559 -613 -209 500 C
ATOM 3365 O SER A 295 154.783 11.497 104.886 1.00 69.45 O
ANISOU 3365 O SER A 295 8117 9790 8479 -659 -186 491 O
ATOM 3366 CB SER A 295 152.150 9.978 104.752 1.00 69.33 C
ANISOU 3366 CB SER A 295 8128 9728 8485 -599 -206 367 C
ATOM 3367 OG SER A 295 151.200 8.963 105.037 1.00 79.42 O
ANISOU 3367 OG SER A 295 9424 10958 9794 -567 -201 273 O
ATOM 3368 N ILE A 296 153.468 12.790 106.205 1.00 65.74 N
ANISOU 3368 N ILE A 296 7737 9061 8180 -610 -250 613 N
ATOM 3369 CA ILE A 296 154.159 14.064 105.985 1.00 66.13 C
ANISOU 3369 CA ILE A 296 7786 9114 8226 -671 -282 744 C
ATOM 3370 C ILE A 296 155.049 14.396 107.203 1.00 70.49 C
ANISOU 3370 C ILE A 296 8386 9537 8859 -656 -273 726 C
ATOM 3371 O ILE A 296 156.179 14.848 107.014 1.00 70.92 O
ANISOU 3371 O ILE A 296 8417 9647 8881 -719 -273 772 O
ATOM 3372 CB ILE A 296 153.117 15.179 105.658 1.00 69.57 C
ANISOU 3372 CB ILE A 296 8238 9496 8700 -679 -345 885 C
ATOM 3373 CG1 ILE A 296 152.641 15.055 104.194 1.00 70.82 C
ANISOU 3373 CG1 ILE A 296 8332 9836 8742 -733 -369 942 C
ATOM 3374 CG2 ILE A 296 153.632 16.605 105.950 1.00 70.36 C
ANISOU 3374 CG2 ILE A 296 8380 9495 8861 -719 -388 1015 C
ATOM 3375 CD1 ILE A 296 151.185 15.366 103.969 1.00 76.63 C
ANISOU 3375 CD1 ILE A 296 9063 10536 9516 -699 -420 1010 C
ATOM 3376 N ILE A 297 154.552 14.143 108.433 1.00 66.25 N
ANISOU 3376 N ILE A 297 7909 8846 8415 -584 -264 660 N
ATOM 3377 CA ILE A 297 155.256 14.404 109.696 1.00 65.46 C
ANISOU 3377 CA ILE A 297 7864 8624 8385 -570 -261 634 C
ATOM 3378 C ILE A 297 156.415 13.396 109.878 1.00 68.92 C
ANISOU 3378 C ILE A 297 8264 9137 8784 -568 -223 542 C
ATOM 3379 O ILE A 297 157.493 13.814 110.303 1.00 68.96 O
ANISOU 3379 O ILE A 297 8269 9134 8799 -605 -232 564 O
ATOM 3380 CB ILE A 297 154.278 14.421 110.917 1.00 67.84 C
ANISOU 3380 CB ILE A 297 8239 8760 8779 -496 -258 592 C
ATOM 3381 CG1 ILE A 297 153.181 15.500 110.739 1.00 68.51 C
ANISOU 3381 CG1 ILE A 297 8349 8767 8916 -480 -294 684 C
ATOM 3382 CG2 ILE A 297 155.028 14.654 112.242 1.00 68.38 C
ANISOU 3382 CG2 ILE A 297 8368 8714 8897 -491 -258 558 C
ATOM 3383 CD1 ILE A 297 151.880 15.241 111.502 1.00 74.95 C
ANISOU 3383 CD1 ILE A 297 9194 9488 9796 -398 -276 635 C
ATOM 3384 N ASN A 298 156.208 12.095 109.546 1.00 64.75 N
ANISOU 3384 N ASN A 298 7703 8680 8219 -527 -186 440 N
ATOM 3385 CA ASN A 298 157.239 11.051 109.671 1.00 64.28 C
ANISOU 3385 CA ASN A 298 7605 8682 8138 -503 -150 345 C
ATOM 3386 C ASN A 298 158.537 11.423 108.906 1.00 68.97 C
ANISOU 3386 C ASN A 298 8120 9422 8662 -565 -141 386 C
ATOM 3387 O ASN A 298 159.573 11.458 109.573 1.00 68.43 O
ANISOU 3387 O ASN A 298 8039 9339 8622 -566 -141 380 O
ATOM 3388 CB ASN A 298 156.724 9.670 109.249 1.00 64.27 C
ANISOU 3388 CB ASN A 298 7587 8723 8109 -454 -117 232 C
ATOM 3389 CG ASN A 298 155.983 8.908 110.329 1.00 83.06 C
ANISOU 3389 CG ASN A 298 10031 10962 10565 -392 -115 166 C
ATOM 3390 OD1 ASN A 298 155.630 9.435 111.393 1.00 76.26 O
ANISOU 3390 OD1 ASN A 298 9229 9978 9769 -380 -134 204 O
ATOM 3391 ND2 ASN A 298 155.720 7.639 110.070 1.00 74.85 N
ANISOU 3391 ND2 ASN A 298 8985 9940 9514 -357 -91 65 N
ATOM 3392 N PRO A 299 158.531 11.799 107.587 1.00 66.51 N
ANISOU 3392 N PRO A 299 7753 9259 8260 -627 -137 442 N
ATOM 3393 CA PRO A 299 159.791 12.205 106.929 1.00 67.13 C
ANISOU 3393 CA PRO A 299 7751 9490 8267 -698 -122 491 C
ATOM 3394 C PRO A 299 160.491 13.376 107.625 1.00 70.83 C
ANISOU 3394 C PRO A 299 8240 9884 8788 -760 -164 597 C
ATOM 3395 O PRO A 299 161.722 13.410 107.646 1.00 71.07 O
ANISOU 3395 O PRO A 299 8205 10002 8796 -796 -149 603 O
ATOM 3396 CB PRO A 299 159.338 12.597 105.521 1.00 69.74 C
ANISOU 3396 CB PRO A 299 8043 9965 8491 -766 -125 561 C
ATOM 3397 CG PRO A 299 158.122 11.799 105.296 1.00 73.84 C
ANISOU 3397 CG PRO A 299 8593 10458 9006 -709 -120 483 C
ATOM 3398 CD PRO A 299 157.420 11.827 106.616 1.00 68.35 C
ANISOU 3398 CD PRO A 299 7984 9549 8438 -644 -147 467 C
ATOM 3399 N LEU A 300 159.709 14.305 108.227 1.00 66.73 N
ANISOU 3399 N LEU A 300 7811 9201 8343 -769 -215 672 N
ATOM 3400 CA LEU A 300 160.230 15.454 108.974 1.00 66.59 C
ANISOU 3400 CA LEU A 300 7840 9076 8386 -829 -262 759 C
ATOM 3401 C LEU A 300 160.899 14.998 110.277 1.00 69.46 C
ANISOU 3401 C LEU A 300 8225 9358 8809 -788 -259 678 C
ATOM 3402 O LEU A 300 161.861 15.634 110.699 1.00 69.53 O
ANISOU 3402 O LEU A 300 8226 9359 8832 -856 -286 727 O
ATOM 3403 CB LEU A 300 159.132 16.495 109.274 1.00 66.58 C
ANISOU 3403 CB LEU A 300 7935 8908 8456 -828 -312 837 C
ATOM 3404 CG LEU A 300 158.402 17.121 108.075 1.00 72.15 C
ANISOU 3404 CG LEU A 300 8625 9671 9119 -869 -337 947 C
ATOM 3405 CD1 LEU A 300 157.119 17.798 108.516 1.00 72.16 C
ANISOU 3405 CD1 LEU A 300 8711 9495 9210 -816 -376 986 C
ATOM 3406 CD2 LEU A 300 159.290 18.104 107.309 1.00 75.57 C
ANISOU 3406 CD2 LEU A 300 9020 10193 9501 -996 -368 1085 C
ATOM 3407 N ILE A 301 160.406 13.896 110.899 1.00 64.95 N
ANISOU 3407 N ILE A 301 7678 8732 8267 -688 -231 565 N
ATOM 3408 CA ILE A 301 160.973 13.321 112.128 1.00 64.20 C
ANISOU 3408 CA ILE A 301 7603 8568 8220 -643 -233 494 C
ATOM 3409 C ILE A 301 162.298 12.636 111.794 1.00 68.40 C
ANISOU 3409 C ILE A 301 8027 9250 8711 -645 -207 460 C
ATOM 3410 O ILE A 301 163.286 12.894 112.481 1.00 68.44 O
ANISOU 3410 O ILE A 301 8013 9252 8738 -678 -232 479 O
ATOM 3411 CB ILE A 301 160.002 12.344 112.859 1.00 66.52 C
ANISOU 3411 CB ILE A 301 7958 8759 8557 -546 -215 402 C
ATOM 3412 CG1 ILE A 301 158.724 13.053 113.330 1.00 66.54 C
ANISOU 3412 CG1 ILE A 301 8055 8621 8607 -536 -234 431 C
ATOM 3413 CG2 ILE A 301 160.692 11.618 114.035 1.00 67.00 C
ANISOU 3413 CG2 ILE A 301 8030 8772 8654 -504 -221 341 C
ATOM 3414 CD1 ILE A 301 157.542 12.146 113.334 1.00 74.18 C
ANISOU 3414 CD1 ILE A 301 9042 9558 9583 -465 -205 366 C
ATOM 3415 N TYR A 302 162.319 11.767 110.749 1.00 65.09 N
ANISOU 3415 N TYR A 302 7532 8967 8233 -610 -156 403 N
ATOM 3416 CA TYR A 302 163.523 11.038 110.330 1.00 65.58 C
ANISOU 3416 CA TYR A 302 7479 9183 8257 -590 -117 352 C
ATOM 3417 C TYR A 302 164.702 11.994 110.132 1.00 70.61 C
ANISOU 3417 C TYR A 302 8041 9925 8863 -693 -134 448 C
ATOM 3418 O TYR A 302 165.795 11.719 110.624 1.00 70.74 O
ANISOU 3418 O TYR A 302 7991 9989 8900 -682 -136 432 O
ATOM 3419 CB TYR A 302 163.313 10.228 109.034 1.00 67.15 C
ANISOU 3419 CB TYR A 302 7614 9525 8376 -558 -56 279 C
ATOM 3420 CG TYR A 302 162.077 9.364 108.909 1.00 68.21 C
ANISOU 3420 CG TYR A 302 7813 9582 8520 -488 -42 193 C
ATOM 3421 CD1 TYR A 302 161.637 8.578 109.970 1.00 69.31 C
ANISOU 3421 CD1 TYR A 302 8022 9567 8743 -407 -55 126 C
ATOM 3422 CD2 TYR A 302 161.442 9.208 107.681 1.00 69.38 C
ANISOU 3422 CD2 TYR A 302 7943 9834 8585 -508 -15 174 C
ATOM 3423 CE1 TYR A 302 160.528 7.743 109.840 1.00 69.69 C
ANISOU 3423 CE1 TYR A 302 8124 9553 8802 -357 -43 51 C
ATOM 3424 CE2 TYR A 302 160.332 8.381 107.539 1.00 69.87 C
ANISOU 3424 CE2 TYR A 302 8057 9836 8654 -458 -7 93 C
ATOM 3425 CZ TYR A 302 159.877 7.650 108.620 1.00 76.37 C
ANISOU 3425 CZ TYR A 302 8950 10496 9570 -384 -20 32 C
ATOM 3426 OH TYR A 302 158.783 6.840 108.464 1.00 77.47 O
ANISOU 3426 OH TYR A 302 9138 10582 9717 -351 -16 -41 O
ATOM 3427 N ALA A 303 164.464 13.123 109.433 1.00 67.48 N
ANISOU 3427 N ALA A 303 7655 9563 8423 -797 -153 559 N
ATOM 3428 CA ALA A 303 165.462 14.159 109.177 1.00 68.29 C
ANISOU 3428 CA ALA A 303 7697 9755 8495 -922 -177 672 C
ATOM 3429 C ALA A 303 165.895 14.833 110.483 1.00 71.90 C
ANISOU 3429 C ALA A 303 8215 10071 9034 -963 -242 713 C
ATOM 3430 O ALA A 303 167.092 14.995 110.716 1.00 72.53 O
ANISOU 3430 O ALA A 303 8213 10235 9109 -1019 -253 741 O
ATOM 3431 CB ALA A 303 164.900 15.191 108.213 1.00 69.57 C
ANISOU 3431 CB ALA A 303 7884 9945 8605 -1019 -196 791 C
ATOM 3432 N LEU A 304 164.920 15.176 111.350 1.00 67.05 N
ANISOU 3432 N LEU A 304 7736 9250 8489 -933 -282 707 N
ATOM 3433 CA LEU A 304 165.135 15.831 112.643 1.00 66.55 C
ANISOU 3433 CA LEU A 304 7756 9036 8495 -969 -343 726 C
ATOM 3434 C LEU A 304 165.943 14.964 113.614 1.00 69.14 C
ANISOU 3434 C LEU A 304 8045 9379 8847 -915 -346 651 C
ATOM 3435 O LEU A 304 166.707 15.505 114.416 1.00 69.56 O
ANISOU 3435 O LEU A 304 8107 9401 8923 -984 -398 684 O
ATOM 3436 CB LEU A 304 163.775 16.168 113.275 1.00 65.96 C
ANISOU 3436 CB LEU A 304 7825 8759 8477 -920 -362 707 C
ATOM 3437 CG LEU A 304 163.712 17.393 114.181 1.00 71.29 C
ANISOU 3437 CG LEU A 304 8610 9268 9209 -990 -425 755 C
ATOM 3438 CD1 LEU A 304 163.461 18.664 113.372 1.00 72.34 C
ANISOU 3438 CD1 LEU A 304 8771 9372 9345 -1083 -456 874 C
ATOM 3439 CD2 LEU A 304 162.614 17.233 115.215 1.00 73.25 C
ANISOU 3439 CD2 LEU A 304 8976 9344 9511 -902 -424 681 C
ATOM 3440 N ARG A 305 165.776 13.629 113.536 1.00 63.83 N
ANISOU 3440 N ARG A 305 7332 8749 8170 -796 -298 554 N
ATOM 3441 CA ARG A 305 166.422 12.664 114.427 1.00 62.75 C
ANISOU 3441 CA ARG A 305 7162 8614 8067 -722 -304 487 C
ATOM 3442 C ARG A 305 167.691 12.022 113.843 1.00 67.12 C
ANISOU 3442 C ARG A 305 7551 9360 8590 -704 -272 471 C
ATOM 3443 O ARG A 305 168.499 11.499 114.614 1.00 67.06 O
ANISOU 3443 O ARG A 305 7496 9366 8617 -666 -297 449 O
ATOM 3444 CB ARG A 305 165.427 11.564 114.829 1.00 60.42 C
ANISOU 3444 CB ARG A 305 6936 8217 7803 -600 -280 394 C
ATOM 3445 CG ARG A 305 164.197 12.049 115.617 1.00 64.72 C
ANISOU 3445 CG ARG A 305 7628 8581 8382 -601 -304 397 C
ATOM 3446 CD ARG A 305 164.512 12.752 116.932 1.00 66.42 C
ANISOU 3446 CD ARG A 305 7917 8693 8625 -655 -365 426 C
ATOM 3447 NE ARG A 305 165.180 11.878 117.898 1.00 67.23 N
ANISOU 3447 NE ARG A 305 7999 8799 8747 -606 -388 388 N
ATOM 3448 CZ ARG A 305 165.599 12.273 119.095 1.00 81.11 C
ANISOU 3448 CZ ARG A 305 9808 10495 10514 -651 -447 405 C
ATOM 3449 NH1 ARG A 305 165.416 13.526 119.491 1.00 69.81 N
ANISOU 3449 NH1 ARG A 305 8460 8984 9081 -744 -482 443 N
ATOM 3450 NH2 ARG A 305 166.206 11.418 119.905 1.00 68.59 N
ANISOU 3450 NH2 ARG A 305 8195 8926 8942 -605 -475 384 N
ATOM 3451 N SER A 306 167.869 12.048 112.507 1.00 63.95 N
ANISOU 3451 N SER A 306 7059 9115 8124 -727 -218 482 N
ATOM 3452 CA SER A 306 169.059 11.483 111.866 1.00 64.64 C
ANISOU 3452 CA SER A 306 6980 9407 8176 -706 -172 458 C
ATOM 3453 C SER A 306 169.823 12.569 111.111 1.00 70.14 C
ANISOU 3453 C SER A 306 7587 10257 8807 -852 -172 568 C
ATOM 3454 O SER A 306 169.341 13.096 110.106 1.00 70.20 O
ANISOU 3454 O SER A 306 7605 10320 8750 -915 -146 614 O
ATOM 3455 CB SER A 306 168.696 10.322 110.944 1.00 67.44 C
ANISOU 3455 CB SER A 306 7290 9837 8496 -593 -92 347 C
ATOM 3456 OG SER A 306 169.821 9.833 110.232 1.00 75.12 O
ANISOU 3456 OG SER A 306 8096 11019 9427 -566 -34 312 O
ATOM 3457 N GLN A 307 171.018 12.901 111.622 1.00 67.70 N
ANISOU 3457 N GLN A 307 7188 10020 8514 -913 -208 620 N
ATOM 3458 CA GLN A 307 171.944 13.896 111.077 1.00 68.72 C
ANISOU 3458 CA GLN A 307 7217 10304 8590 -1069 -217 734 C
ATOM 3459 C GLN A 307 172.470 13.445 109.705 1.00 73.91 C
ANISOU 3459 C GLN A 307 7714 11214 9156 -1055 -122 712 C
ATOM 3460 O GLN A 307 172.649 14.276 108.810 1.00 74.12 O
ANISOU 3460 O GLN A 307 7697 11361 9105 -1186 -107 808 O
ATOM 3461 CB GLN A 307 173.104 14.095 112.068 1.00 70.58 C
ANISOU 3461 CB GLN A 307 7381 10565 8871 -1118 -281 773 C
ATOM 3462 CG GLN A 307 174.001 15.289 111.787 1.00 82.56 C
ANISOU 3462 CG GLN A 307 8821 12196 10350 -1311 -316 906 C
ATOM 3463 CD GLN A 307 175.337 15.102 112.456 1.00100.05 C
ANISOU 3463 CD GLN A 307 10895 14526 12593 -1333 -353 922 C
ATOM 3464 OE1 GLN A 307 176.255 14.489 111.901 1.00 94.65 O
ANISOU 3464 OE1 GLN A 307 10020 14062 11879 -1288 -293 901 O
ATOM 3465 NE2 GLN A 307 175.459 15.582 113.684 1.00 92.78 N
ANISOU 3465 NE2 GLN A 307 10061 13463 11729 -1392 -452 952 N
ATOM 3466 N GLU A 308 172.708 12.129 109.553 1.00 71.02 N
ANISOU 3466 N GLU A 308 7264 10922 8797 -898 -57 584 N
ATOM 3467 CA GLU A 308 173.201 11.502 108.330 1.00 72.22 C
ANISOU 3467 CA GLU A 308 7266 11310 8864 -852 46 522 C
ATOM 3468 C GLU A 308 172.147 11.574 107.222 1.00 76.78 C
ANISOU 3468 C GLU A 308 7916 11902 9354 -869 94 504 C
ATOM 3469 O GLU A 308 172.504 11.846 106.076 1.00 77.81 O
ANISOU 3469 O GLU A 308 7947 12243 9373 -943 155 537 O
ATOM 3470 CB GLU A 308 173.613 10.048 108.610 1.00 73.74 C
ANISOU 3470 CB GLU A 308 7382 11521 9115 -660 91 375 C
ATOM 3471 CG GLU A 308 174.486 9.410 107.541 1.00 85.63 C
ANISOU 3471 CG GLU A 308 8696 13291 10548 -602 200 299 C
ATOM 3472 CD GLU A 308 175.857 10.007 107.275 1.00107.54 C
ANISOU 3472 CD GLU A 308 11275 16307 13278 -703 218 389 C
ATOM 3473 OE1 GLU A 308 176.456 10.600 108.203 1.00101.09 O
ANISOU 3473 OE1 GLU A 308 10438 15448 12522 -779 134 487 O
ATOM 3474 OE2 GLU A 308 176.350 9.843 106.136 1.00104.03 O
ANISOU 3474 OE2 GLU A 308 10691 16105 12732 -709 317 355 O
ATOM 3475 N LEU A 309 170.855 11.362 107.564 1.00 72.64 N
ANISOU 3475 N LEU A 309 7559 11168 8874 -812 63 463 N
ATOM 3476 CA LEU A 309 169.743 11.433 106.611 1.00 72.45 C
ANISOU 3476 CA LEU A 309 7609 11143 8775 -829 91 454 C
ATOM 3477 C LEU A 309 169.532 12.880 106.135 1.00 77.37 C
ANISOU 3477 C LEU A 309 8267 11788 9342 -1003 49 622 C
ATOM 3478 O LEU A 309 169.200 13.085 104.969 1.00 77.69 O
ANISOU 3478 O LEU A 309 8286 11958 9274 -1058 86 652 O
ATOM 3479 CB LEU A 309 168.454 10.858 107.219 1.00 71.01 C
ANISOU 3479 CB LEU A 309 7582 10732 8666 -728 62 377 C
ATOM 3480 CG LEU A 309 167.269 10.659 106.263 1.00 75.47 C
ANISOU 3480 CG LEU A 309 8210 11304 9160 -721 90 341 C
ATOM 3481 CD1 LEU A 309 167.410 9.397 105.435 1.00 76.30 C
ANISOU 3481 CD1 LEU A 309 8241 11543 9205 -622 177 187 C
ATOM 3482 CD2 LEU A 309 165.997 10.591 107.015 1.00 76.37 C
ANISOU 3482 CD2 LEU A 309 8477 11186 9355 -677 39 328 C
ATOM 3483 N ARG A 310 169.755 13.871 107.027 1.00 74.33 N
ANISOU 3483 N ARG A 310 7936 11278 9026 -1093 -33 731 N
ATOM 3484 CA ARG A 310 169.669 15.307 106.729 1.00 75.09 C
ANISOU 3484 CA ARG A 310 8075 11358 9096 -1262 -88 899 C
ATOM 3485 C ARG A 310 170.731 15.706 105.706 1.00 82.09 C
ANISOU 3485 C ARG A 310 8805 12513 9873 -1385 -44 984 C
ATOM 3486 O ARG A 310 170.457 16.502 104.805 1.00 82.58 O
ANISOU 3486 O ARG A 310 8877 12643 9857 -1503 -50 1101 O
ATOM 3487 CB ARG A 310 169.866 16.125 108.011 1.00 74.87 C
ANISOU 3487 CB ARG A 310 8133 11140 9174 -1322 -180 965 C
ATOM 3488 CG ARG A 310 168.615 16.812 108.529 1.00 83.39 C
ANISOU 3488 CG ARG A 310 9397 11966 10320 -1324 -245 1001 C
ATOM 3489 CD ARG A 310 168.919 17.675 109.744 1.00 92.56 C
ANISOU 3489 CD ARG A 310 10641 12958 11571 -1397 -331 1053 C
ATOM 3490 NE ARG A 310 169.612 16.926 110.798 1.00101.06 N
ANISOU 3490 NE ARG A 310 11677 14026 12694 -1326 -336 963 N
ATOM 3491 CZ ARG A 310 169.481 17.158 112.099 1.00117.47 C
ANISOU 3491 CZ ARG A 310 13859 15923 14850 -1317 -399 941 C
ATOM 3492 NH1 ARG A 310 168.671 18.116 112.533 1.00105.76 N
ANISOU 3492 NH1 ARG A 310 12529 14242 13414 -1364 -453 984 N
ATOM 3493 NH2 ARG A 310 170.152 16.427 112.979 1.00105.58 N
ANISOU 3493 NH2 ARG A 310 12306 14435 13375 -1257 -408 873 N
ATOM 3494 N LYS A 311 171.949 15.146 105.866 1.00 80.30 N
ANISOU 3494 N LYS A 311 8425 12443 9641 -1357 -1 932 N
ATOM 3495 CA LYS A 311 173.108 15.351 104.999 1.00 82.37 C
ANISOU 3495 CA LYS A 311 8504 12993 9801 -1456 57 992 C
ATOM 3496 C LYS A 311 172.818 14.789 103.607 1.00 87.98 C
ANISOU 3496 C LYS A 311 9151 13904 10374 -1423 157 932 C
ATOM 3497 O LYS A 311 173.127 15.445 102.612 1.00 89.01 O
ANISOU 3497 O LYS A 311 9210 14225 10386 -1564 184 1043 O
ATOM 3498 CB LYS A 311 174.349 14.679 105.613 1.00 85.42 C
ANISOU 3498 CB LYS A 311 8739 13484 10235 -1386 82 921 C
ATOM 3499 CG LYS A 311 175.666 15.060 104.947 1.00100.73 C
ANISOU 3499 CG LYS A 311 10473 15715 12086 -1510 130 1004 C
ATOM 3500 CD LYS A 311 176.776 14.051 105.230 1.00111.96 C
ANISOU 3500 CD LYS A 311 11710 17292 13538 -1384 189 894 C
ATOM 3501 CE LYS A 311 176.650 12.787 104.409 1.00123.27 C
ANISOU 3501 CE LYS A 311 13069 18858 14910 -1212 310 721 C
ATOM 3502 NZ LYS A 311 177.971 12.163 104.150 1.00133.44 N
ANISOU 3502 NZ LYS A 311 14117 20408 16174 -1149 395 661 N
ATOM 3503 N THR A 312 172.203 13.588 103.546 1.00 84.57 N
ANISOU 3503 N THR A 312 8753 13427 9953 -1248 208 760 N
ATOM 3504 CA THR A 312 171.836 12.914 102.299 1.00 85.55 C
ANISOU 3504 CA THR A 312 8835 13723 9948 -1203 300 668 C
ATOM 3505 C THR A 312 170.706 13.692 101.611 1.00 90.89 C
ANISOU 3505 C THR A 312 9631 14350 10554 -1306 258 776 C
ATOM 3506 O THR A 312 170.704 13.783 100.385 1.00 91.73 O
ANISOU 3506 O THR A 312 9676 14668 10508 -1376 313 801 O
ATOM 3507 CB THR A 312 171.472 11.441 102.550 1.00 91.19 C
ANISOU 3507 CB THR A 312 9572 14362 10715 -998 348 456 C
ATOM 3508 OG1 THR A 312 172.400 10.874 103.478 1.00 90.35 O
ANISOU 3508 OG1 THR A 312 9386 14229 10714 -900 350 392 O
ATOM 3509 CG2 THR A 312 171.480 10.616 101.271 1.00 89.82 C
ANISOU 3509 CG2 THR A 312 9316 14409 10401 -945 460 327 C
ATOM 3510 N PHE A 313 169.775 14.275 102.399 1.00 87.40 N
ANISOU 3510 N PHE A 313 9351 13638 10218 -1315 160 843 N
ATOM 3511 CA PHE A 313 168.671 15.103 101.902 1.00 87.60 C
ANISOU 3511 CA PHE A 313 9491 13582 10209 -1399 103 961 C
ATOM 3512 C PHE A 313 169.217 16.382 101.268 1.00 94.78 C
ANISOU 3512 C PHE A 313 10353 14617 11042 -1596 74 1165 C
ATOM 3513 O PHE A 313 168.707 16.824 100.237 1.00 95.21 O
ANISOU 3513 O PHE A 313 10419 14767 10987 -1680 71 1258 O
ATOM 3514 CB PHE A 313 167.700 15.460 103.044 1.00 87.76 C
ANISOU 3514 CB PHE A 313 9679 13284 10381 -1351 11 979 C
ATOM 3515 CG PHE A 313 166.673 14.433 103.474 1.00 87.89 C
ANISOU 3515 CG PHE A 313 9782 13154 10457 -1191 20 826 C
ATOM 3516 CD1 PHE A 313 166.651 13.160 102.910 1.00 91.23 C
ANISOU 3516 CD1 PHE A 313 10147 13701 10817 -1089 101 666 C
ATOM 3517 CD2 PHE A 313 165.729 14.738 104.446 1.00 88.65 C
ANISOU 3517 CD2 PHE A 313 10020 12989 10674 -1149 -50 840 C
ATOM 3518 CE1 PHE A 313 165.700 12.218 103.311 1.00 91.05 C
ANISOU 3518 CE1 PHE A 313 10207 13533 10853 -960 102 535 C
ATOM 3519 CE2 PHE A 313 164.777 13.795 104.842 1.00 90.41 C
ANISOU 3519 CE2 PHE A 313 10314 13091 10948 -1018 -41 712 C
ATOM 3520 CZ PHE A 313 164.767 12.545 104.269 1.00 88.73 C
ANISOU 3520 CZ PHE A 313 10045 12995 10675 -931 31 566 C
ATOM 3521 N LYS A 314 170.273 16.958 101.887 1.00 93.16 N
ANISOU 3521 N LYS A 314 10090 14415 10891 -1678 48 1240 N
ATOM 3522 CA LYS A 314 170.968 18.170 101.446 1.00 95.06 C
ANISOU 3522 CA LYS A 314 10278 14762 11077 -1882 14 1439 C
ATOM 3523 C LYS A 314 171.726 17.928 100.137 1.00102.40 C
ANISOU 3523 C LYS A 314 11035 16048 11823 -1957 114 1455 C
ATOM 3524 O LYS A 314 171.945 18.870 99.377 1.00103.38 O
ANISOU 3524 O LYS A 314 11131 16292 11855 -2134 95 1633 O
ATOM 3525 CB LYS A 314 171.922 18.670 102.540 1.00 97.58 C
ANISOU 3525 CB LYS A 314 10574 14996 11505 -1941 -38 1484 C
ATOM 3526 CG LYS A 314 171.501 20.008 103.134 1.00110.54 C
ANISOU 3526 CG LYS A 314 12366 16390 13244 -2062 -161 1641 C
ATOM 3527 CD LYS A 314 172.025 20.211 104.555 1.00118.68 C
ANISOU 3527 CD LYS A 314 13435 17246 14412 -2056 -224 1614 C
ATOM 3528 CE LYS A 314 170.992 19.875 105.608 1.00124.84 C
ANISOU 3528 CE LYS A 314 14377 17742 15314 -1906 -266 1503 C
ATOM 3529 NZ LYS A 314 171.463 20.214 106.976 1.00131.68 N
ANISOU 3529 NZ LYS A 314 15296 18441 16295 -1925 -338 1491 N
ATOM 3530 N GLU A 315 172.118 16.668 99.877 1.00100.49 N
ANISOU 3530 N GLU A 315 10682 15973 11528 -1821 221 1270 N
ATOM 3531 CA GLU A 315 172.795 16.267 98.644 1.00102.68 C
ANISOU 3531 CA GLU A 315 10793 16599 11624 -1860 337 1239 C
ATOM 3532 C GLU A 315 171.779 16.135 97.508 1.00108.89 C
ANISOU 3532 C GLU A 315 11640 17463 12272 -1871 359 1235 C
ATOM 3533 O GLU A 315 172.129 16.405 96.360 1.00110.22 O
ANISOU 3533 O GLU A 315 11713 17902 12263 -1990 415 1309 O
ATOM 3534 CB GLU A 315 173.560 14.951 98.839 1.00104.23 C
ANISOU 3534 CB GLU A 315 10854 16917 11831 -1691 441 1025 C
ATOM 3535 CG GLU A 315 174.904 15.119 99.528 1.00114.19 C
ANISOU 3535 CG GLU A 315 11975 18251 13162 -1721 444 1058 C
ATOM 3536 CD GLU A 315 175.479 13.858 100.143 1.00131.70 C
ANISOU 3536 CD GLU A 315 14103 20473 15463 -1518 504 858 C
ATOM 3537 OE1 GLU A 315 175.356 12.774 99.526 1.00125.03 O
ANISOU 3537 OE1 GLU A 315 13212 19741 14554 -1379 604 682 O
ATOM 3538 OE2 GLU A 315 176.073 13.958 101.241 1.00124.71 O
ANISOU 3538 OE2 GLU A 315 13196 19479 14710 -1499 447 878 O
ATOM 3539 N ILE A 316 170.523 15.738 97.827 1.00105.36 N
ANISOU 3539 N ILE A 316 11346 16790 11898 -1756 312 1155 N
ATOM 3540 CA ILE A 316 169.447 15.574 96.842 1.00106.12 C
ANISOU 3540 CA ILE A 316 11507 16939 11876 -1760 316 1146 C
ATOM 3541 C ILE A 316 168.924 16.954 96.397 1.00112.97 C
ANISOU 3541 C ILE A 316 12450 17768 12707 -1936 220 1398 C
ATOM 3542 O ILE A 316 168.648 17.111 95.213 1.00113.83 O
ANISOU 3542 O ILE A 316 12532 18074 12646 -2024 240 1463 O
ATOM 3543 CB ILE A 316 168.290 14.637 97.325 1.00107.38 C
ANISOU 3543 CB ILE A 316 11789 16885 12126 -1585 299 977 C
ATOM 3544 CG1 ILE A 316 168.796 13.278 97.898 1.00107.25 C
ANISOU 3544 CG1 ILE A 316 11716 16856 12176 -1406 378 741 C
ATOM 3545 CG2 ILE A 316 167.226 14.411 96.234 1.00108.48 C
ANISOU 3545 CG2 ILE A 316 11977 17113 12129 -1601 302 963 C
ATOM 3546 CD1 ILE A 316 169.724 12.361 96.982 1.00116.10 C
ANISOU 3546 CD1 ILE A 316 12673 18289 13150 -1365 517 590 C
ATOM 3547 N ILE A 317 168.814 17.949 97.315 1.00110.83 N
ANISOU 3547 N ILE A 317 12272 17250 12589 -1989 114 1537 N
ATOM 3548 CA ILE A 317 168.340 19.305 96.976 1.00112.34 C
ANISOU 3548 CA ILE A 317 12545 17362 12777 -2146 12 1781 C
ATOM 3549 C ILE A 317 169.375 20.026 96.058 1.00121.00 C
ANISOU 3549 C ILE A 317 13516 18734 13723 -2351 40 1953 C
ATOM 3550 O ILE A 317 168.980 20.848 95.227 1.00121.78 O
ANISOU 3550 O ILE A 317 13647 18890 13733 -2487 -12 2141 O
ATOM 3551 CB ILE A 317 167.952 20.144 98.240 1.00114.27 C
ANISOU 3551 CB ILE A 317 12932 17253 13233 -2136 -103 1858 C
ATOM 3552 CG1 ILE A 317 167.017 21.326 97.878 1.00115.19 C
ANISOU 3552 CG1 ILE A 317 13168 17227 13372 -2232 -213 2068 C
ATOM 3553 CG2 ILE A 317 169.167 20.602 99.065 1.00115.39 C
ANISOU 3553 CG2 ILE A 317 13022 17363 13457 -2210 -115 1897 C
ATOM 3554 CD1 ILE A 317 166.088 21.823 99.020 1.00121.14 C
ANISOU 3554 CD1 ILE A 317 14088 17608 14330 -2145 -311 2073 C
ATOM 3555 N CYS A 318 170.675 19.680 96.191 1.00120.12 N
ANISOU 3555 N CYS A 318 13256 18804 13581 -2371 122 1891 N
ATOM 3556 CA CYS A 318 171.765 20.224 95.377 1.00123.06 C
ANISOU 3556 CA CYS A 318 13480 19470 13805 -2560 168 2032 C
ATOM 3557 C CYS A 318 171.822 19.506 94.022 1.00129.99 C
ANISOU 3557 C CYS A 318 14245 20696 14449 -2562 286 1957 C
ATOM 3558 O CYS A 318 172.120 20.144 93.010 1.00131.53 O
ANISOU 3558 O CYS A 318 14376 21120 14479 -2743 298 2125 O
ATOM 3559 CB CYS A 318 173.097 20.127 96.116 1.00123.81 C
ANISOU 3559 CB CYS A 318 13448 19623 13969 -2572 207 1991 C
ATOM 3560 SG CYS A 318 173.256 21.266 97.516 1.00126.90 S
ANISOU 3560 SG CYS A 318 13959 19671 14587 -2652 61 2128 S
ATOM 3561 N CYS A 319 171.537 18.182 94.008 1.00126.92 N
ANISOU 3561 N CYS A 319 13838 20343 14043 -2368 371 1703 N
ATOM 3562 CA CYS A 319 171.523 17.358 92.795 1.00128.59 C
ANISOU 3562 CA CYS A 319 13960 20862 14038 -2345 487 1581 C
ATOM 3563 C CYS A 319 170.258 17.621 91.969 1.00133.32 C
ANISOU 3563 C CYS A 319 14675 21446 14535 -2393 426 1663 C
ATOM 3564 O CYS A 319 170.314 17.502 90.746 1.00134.65 O
ANISOU 3564 O CYS A 319 14773 21911 14479 -2479 491 1678 O
ATOM 3565 CB CYS A 319 171.671 15.876 93.128 1.00128.23 C
ANISOU 3565 CB CYS A 319 13867 20823 14031 -2122 588 1280 C
ATOM 3566 SG CYS A 319 173.377 15.357 93.455 1.00133.30 S
ANISOU 3566 SG CYS A 319 14290 21673 14686 -2076 710 1172 S
ATOM 3567 N TYR A 320 169.128 17.980 92.633 1.00128.64 N
ANISOU 3567 N TYR A 320 14253 20523 14099 -2340 303 1716 N
ATOM 3568 CA TYR A 320 167.852 18.318 91.985 1.00128.65 C
ANISOU 3568 CA TYR A 320 14365 20476 14038 -2377 222 1814 C
ATOM 3569 C TYR A 320 167.967 19.682 91.305 1.00134.71 C
ANISOU 3569 C TYR A 320 15134 21329 14719 -2600 147 2119 C
ATOM 3570 O TYR A 320 167.292 19.926 90.302 1.00135.52 O
ANISOU 3570 O TYR A 320 15262 21556 14675 -2681 113 2224 O
ATOM 3571 CB TYR A 320 166.686 18.310 92.984 1.00127.54 C
ANISOU 3571 CB TYR A 320 14387 19963 14109 -2244 121 1779 C
ATOM 3572 N GLU A2000 168.839 20.561 91.851 1.00131.69 N
ANISOU 3572 N GLU A2000 14725 20884 14429 -2707 114 2265 N
ATOM 3573 CA GLU A2000 169.151 21.882 91.303 1.00133.31 C
ANISOU 3573 CA GLU A2000 14924 21157 14570 -2936 43 2563 C
ATOM 3574 C GLU A2000 169.969 21.712 90.018 1.00139.35 C
ANISOU 3574 C GLU A2000 15525 22359 15061 -3078 154 2600 C
ATOM 3575 O GLU A2000 169.839 22.518 89.096 1.00140.64 O
ANISOU 3575 O GLU A2000 15690 22660 15086 -3259 106 2829 O
ATOM 3576 CB GLU A2000 169.913 22.729 92.332 1.00134.48 C
ANISOU 3576 CB GLU A2000 15087 21109 14899 -3007 -16 2671 C
ATOM 3577 N PHE A2001 170.796 20.642 89.963 1.00135.97 N
ANISOU 3577 N PHE A2001 14954 22151 14556 -2989 302 2372 N
ATOM 3578 CA PHE A2001 171.622 20.261 88.815 1.00137.97 C
ANISOU 3578 CA PHE A2001 15034 22841 14548 -3082 440 2341 C
ATOM 3579 C PHE A2001 170.793 19.459 87.800 1.00141.82 C
ANISOU 3579 C PHE A2001 15541 23502 14844 -3021 490 2212 C
ATOM 3580 O PHE A2001 171.081 19.517 86.603 1.00143.59 O
ANISOU 3580 O PHE A2001 15673 24073 14813 -3156 557 2274 O
ATOM 3581 CB PHE A2001 172.844 19.451 89.272 1.00139.91 C
ANISOU 3581 CB PHE A2001 15118 23223 14820 -2986 575 2139 C
ATOM 3582 N LEU A2002 169.768 18.714 88.286 1.00135.98 N
ANISOU 3582 N LEU A2002 14920 22527 14220 -2830 456 2032 N
ATOM 3583 CA LEU A2002 168.837 17.917 87.476 1.00135.73 C
ANISOU 3583 CA LEU A2002 14930 22601 14039 -2763 480 1894 C
ATOM 3584 C LEU A2002 167.979 18.850 86.620 1.00140.17 C
ANISOU 3584 C LEU A2002 15570 23206 14483 -2927 365 2153 C
ATOM 3585 O LEU A2002 167.837 18.608 85.422 1.00141.48 O
ANISOU 3585 O LEU A2002 15688 23674 14394 -3010 413 2150 O
ATOM 3586 CB LEU A2002 167.953 17.021 88.378 1.00133.25 C
ANISOU 3586 CB LEU A2002 14730 21982 13917 -2536 451 1674 C
ATOM 3587 CG LEU A2002 166.798 16.252 87.715 1.00137.75 C
ANISOU 3587 CG LEU A2002 15371 22590 14378 -2469 444 1541 C
ATOM 3588 CD1 LEU A2002 167.267 14.919 87.152 1.00138.77 C
ANISOU 3588 CD1 LEU A2002 15405 22966 14354 -2377 601 1247 C
ATOM 3589 CD2 LEU A2002 165.669 16.025 88.698 1.00137.79 C
ANISOU 3589 CD2 LEU A2002 15523 22221 14611 -2321 343 1480 C
ATOM 3590 N GLU A2003 167.436 19.925 87.236 1.00135.37 N
ANISOU 3590 N GLU A2003 15079 22299 14057 -2972 213 2377 N
ATOM 3591 CA GLU A2003 166.629 20.951 86.574 1.00135.93 C
ANISOU 3591 CA GLU A2003 15230 22351 14064 -3117 80 2658 C
ATOM 3592 C GLU A2003 167.494 21.777 85.613 1.00141.77 C
ANISOU 3592 C GLU A2003 15870 23397 14600 -3362 101 2896 C
ATOM 3593 O GLU A2003 166.986 22.257 84.600 1.00142.92 O
ANISOU 3593 O GLU A2003 16034 23696 14573 -3497 40 3082 O
ATOM 3594 CB GLU A2003 165.952 21.862 87.608 1.00135.71 C
ANISOU 3594 CB GLU A2003 15347 21901 14316 -3077 -75 2810 C
ATOM 3595 N VAL A2004 168.801 21.925 85.931 1.00138.43 N
ANISOU 3595 N VAL A2004 15334 23072 14191 -3425 184 2896 N
ATOM 3596 CA VAL A2004 169.786 22.644 85.117 1.00140.69 C
ANISOU 3596 CA VAL A2004 15501 23665 14289 -3665 223 3108 C
ATOM 3597 C VAL A2004 170.116 21.837 83.856 1.00145.90 C
ANISOU 3597 C VAL A2004 16028 24784 14624 -3708 371 2982 C
ATOM 3598 O VAL A2004 170.258 22.421 82.780 1.00147.88 O
ANISOU 3598 O VAL A2004 16232 25310 14647 -3915 365 3192 O
ATOM 3599 CB VAL A2004 171.064 22.962 85.923 1.00144.65 C
ANISOU 3599 CB VAL A2004 15911 24132 14918 -3708 268 3123 C
ATOM 3600 N LEU A2005 170.230 20.498 83.992 1.00141.10 N
ANISOU 3600 N LEU A2005 15365 24254 13994 -3515 502 2641 N
ATOM 3601 CA LEU A2005 170.502 19.578 82.884 1.00142.50 C
ANISOU 3601 CA LEU A2005 15427 24837 13878 -3517 655 2457 C
ATOM 3602 C LEU A2005 169.229 19.319 82.067 1.00146.15 C
ANISOU 3602 C LEU A2005 15994 25342 14195 -3515 590 2448 C
ATOM 3603 O LEU A2005 169.319 18.958 80.892 1.00147.79 O
ANISOU 3603 O LEU A2005 16129 25918 14106 -3602 676 2402 O
ATOM 3604 CB LEU A2005 171.071 18.256 83.416 1.00141.57 C
ANISOU 3604 CB LEU A2005 15227 24735 13827 -3296 805 2092 C
ATOM 3605 N PHE A2006 168.050 19.511 82.697 1.00140.35 N
ANISOU 3605 N PHE A2006 15422 24240 13662 -3420 440 2490 N
ATOM 3606 CA PHE A2006 166.716 19.337 82.113 1.00139.93 C
ANISOU 3606 CA PHE A2006 15476 24166 13525 -3406 348 2501 C
ATOM 3607 C PHE A2006 166.430 20.396 81.047 1.00145.36 C
ANISOU 3607 C PHE A2006 16173 25044 14015 -3643 251 2837 C
ATOM 3608 O PHE A2006 165.790 20.088 80.041 1.00146.19 O
ANISOU 3608 O PHE A2006 16287 25366 13892 -3696 240 2826 O
ATOM 3609 CB PHE A2006 165.656 19.417 83.222 1.00139.08 C
ANISOU 3609 CB PHE A2006 15520 23602 13722 -3246 213 2490 C
ATOM 3610 CG PHE A2006 164.386 18.635 82.998 1.00139.95 C
ANISOU 3610 CG PHE A2006 15715 23652 13807 -3132 170 2336 C
ATOM 3611 CD1 PHE A2006 164.375 17.249 83.109 1.00142.38 C
ANISOU 3611 CD1 PHE A2006 16003 24002 14093 -2971 284 1988 C
ATOM 3612 CD2 PHE A2006 163.183 19.287 82.759 1.00142.32 C
ANISOU 3612 CD2 PHE A2006 16116 23825 14132 -3177 6 2541 C
ATOM 3613 CE1 PHE A2006 163.191 16.527 82.933 1.00142.67 C
ANISOU 3613 CE1 PHE A2006 16122 23972 14115 -2881 236 1848 C
ATOM 3614 CE2 PHE A2006 161.999 18.565 82.590 1.00144.49 C
ANISOU 3614 CE2 PHE A2006 16459 24049 14393 -3078 -40 2403 C
ATOM 3615 CZ PHE A2006 162.010 17.191 82.681 1.00141.83 C
ANISOU 3615 CZ PHE A2006 16103 23762 14022 -2939 74 2057 C
ATOM 3616 N GLN A2007 166.889 21.642 81.279 1.00141.97 N
ANISOU 3616 N GLN A2007 15745 24524 13672 -3790 171 3139 N
ATOM 3617 CA GLN A2007 166.705 22.772 80.361 1.00143.82 C
ANISOU 3617 CA GLN A2007 15994 24903 13750 -4027 64 3500 C
ATOM 3618 C GLN A2007 167.904 22.907 79.409 1.00149.97 C
ANISOU 3618 C GLN A2007 16613 26130 14239 -4233 194 3576 C
ATOM 3619 O GLN A2007 167.747 23.409 78.296 1.00151.94 O
ANISOU 3619 O GLN A2007 16846 26645 14241 -4428 154 3795 O
ATOM 3620 CB GLN A2007 166.487 24.093 81.131 1.00144.46 C
ANISOU 3620 CB GLN A2007 16181 24610 14098 -4081 -106 3797 C
ATOM 3621 CG GLN A2007 165.416 24.061 82.235 1.00155.71 C
ANISOU 3621 CG GLN A2007 17754 25573 15837 -3872 -223 3725 C
ATOM 3622 CD GLN A2007 164.012 23.792 81.744 1.00174.00 C
ANISOU 3622 CD GLN A2007 20153 27860 18101 -3805 -319 3723 C
ATOM 3623 OE1 GLN A2007 163.471 24.499 80.886 1.00171.24 O
ANISOU 3623 OE1 GLN A2007 19832 27609 17623 -3947 -431 3987 O
ATOM 3624 NE2 GLN A2007 163.375 22.782 82.318 1.00163.34 N
ANISOU 3624 NE2 GLN A2007 18841 26362 16858 -3591 -287 3438 N
ATOM 3625 N GLY A2008 169.078 22.467 79.866 1.00145.86 N
ANISOU 3625 N GLY A2008 15971 25697 13751 -4189 344 3403 N
ATOM 3626 CA GLY A2008 170.320 22.508 79.104 1.00171.50 C
ANISOU 3626 CA GLY A2008 19040 29372 16749 -4359 491 3439 C
ATOM 3627 C GLY A2008 171.099 21.213 79.192 1.00186.18 C
ANISOU 3627 C GLY A2008 20765 31434 18542 -4202 702 3061 C
ATOM 3628 O GLY A2008 172.302 21.185 78.931 1.00143.43 O
ANISOU 3628 O GLY A2008 15182 26309 13006 -4290 840 3046 O
TER 3629 GLY A2008
HETATM 3630 C ACE B 0 129.460 4.593 97.151 1.00 88.36 C
HETATM 3631 O ACE B 0 129.314 4.979 98.314 1.00 88.33 O
HETATM 3632 CH3 ACE B 0 128.270 4.594 96.186 1.00 88.53 C
HETATM 3633 N NLE B 1 130.615 4.163 96.607 1.00 87.51 N
HETATM 3634 CA NLE B 1 131.903 4.067 97.331 1.00 85.77 C
HETATM 3635 C NLE B 1 132.369 5.419 97.816 1.00 84.50 C
HETATM 3636 O NLE B 1 132.147 6.440 97.157 1.00 84.91 O
HETATM 3637 CB NLE B 1 132.982 3.322 96.513 1.00 85.22 C
HETATM 3638 CG NLE B 1 133.503 4.108 95.297 1.00 84.91 C
HETATM 3639 CD NLE B 1 134.927 4.601 95.579 1.00 84.70 C
HETATM 3640 CE NLE B 1 135.806 4.367 94.353 1.00 84.66 C
ATOM 3641 N ASP B 2 133.005 5.392 98.990 1.00 82.49 N
ATOM 3642 CA ASP B 2 133.482 6.599 99.660 1.00 80.41 C
ATOM 3643 C ASP B 2 134.949 6.532 99.997 1.00 78.20 C
ATOM 3644 O ASP B 2 135.600 5.501 99.808 1.00 76.83 O
ATOM 3645 CB ASP B 2 132.646 6.820 100.932 1.00 80.62 C
ATOM 3646 CG ASP B 2 132.480 8.292 101.288 1.00 81.03 C
ATOM 3647 OD1 ASP B 2 133.169 9.166 100.756 1.00 81.54 O
ATOM 3648 N HIS B 3 135.510 7.664 100.467 1.00 77.64 N
ATOM 3649 CA HIS B 3 136.876 7.885 100.945 1.00 76.96 C
ATOM 3650 C HIS B 3 137.121 6.952 102.098 1.00 74.50 C
ATOM 3651 O HIS B 3 136.249 6.793 102.956 1.00 74.42 O
ATOM 3652 CB HIS B 3 137.016 9.321 101.461 1.00 78.54 C
ATOM 3653 CG HIS B 3 136.959 10.349 100.335 1.00 80.24 C
ATOM 3654 ND1 HIS B 3 135.847 10.911 99.876 1.00 81.11 N
ATOM 3655 CD2 HIS B 3 138.019 10.845 99.713 1.00 80.92 C
ATOM 3656 CE1 HIS B 3 136.224 11.761 98.924 1.00 81.66 C
ATOM 3657 NE2 HIS B 3 137.555 11.721 98.825 1.00 81.64 N
HETATM 3658 N 4J2 B 4 138.269 6.258 102.119 1.00 72.26 N
HETATM 3659 CA 4J2 B 4 138.659 5.276 103.139 1.00 69.80 C
HETATM 3660 CB 4J2 B 4 140.071 4.732 102.876 1.00 67.46 C
HETATM 3661 CG 4J2 B 4 140.594 4.045 103.979 1.00 65.62 C
HETATM 3662 CD1 4J2 B 4 141.127 4.745 105.073 1.00 65.18 C
HETATM 3663 CD2 4J2 B 4 140.623 2.645 103.966 1.00 64.36 C
HETATM 3664 CE1 4J2 B 4 141.634 4.051 106.176 1.00 64.62 C
HETATM 3665 CZ1 4J2 B 4 141.632 2.652 106.176 1.00 63.71 C
HETATM 3666 CZ2 4J2 B 4 142.179 1.952 107.257 1.00 62.93 C
HETATM 3667 CZ3 4J2 B 4 142.173 0.555 107.250 1.00 62.82 C
HETATM 3668 CE2 4J2 B 4 141.122 1.949 105.067 1.00 63.80 C
HETATM 3669 CE3 4J2 B 4 141.128 0.552 105.057 1.00 63.70 C
HETATM 3670 CE4 4J2 B 4 141.641 -0.138 106.159 1.00 63.28 C
HETATM 3671 C 4J2 B 4 137.668 4.147 103.230 1.00 69.78 C
HETATM 3672 O 4J2 B 4 137.147 3.666 102.222 1.00 70.01 O
ATOM 3673 N ARG B 5 137.394 3.690 104.448 1.00 69.66 N
ATOM 3674 CA ARG B 5 136.436 2.635 104.742 1.00 70.69 C
ATOM 3675 C ARG B 5 135.844 2.891 106.097 1.00 71.71 C
ATOM 3676 O ARG B 5 136.484 3.518 106.947 1.00 72.65 O
ATOM 3677 CB ARG B 5 137.078 1.244 104.680 1.00 70.89 C
ATOM 3678 CG ARG B 5 136.000 0.212 104.342 1.00 71.39 C
ATOM 3679 CD ARG B 5 136.650 -1.036 103.778 1.00 72.36 C
ATOM 3680 NE ARG B 5 136.612 -0.977 102.310 1.00 73.33 N
ATOM 3681 CZ ARG B 5 135.964 -1.833 101.500 1.00 74.32 C
ATOM 3682 NH1 ARG B 5 136.035 -1.655 100.174 1.00 75.19 N
ATOM 3683 NH2 ARG B 5 135.268 -2.872 101.992 1.00 74.54 N
ATOM 3684 N TRP B 6 134.609 2.409 106.327 1.00 71.14 N
ATOM 3685 CA TRP B 6 133.820 2.495 107.558 1.00 70.63 C
ATOM 3686 C TRP B 6 133.483 3.926 107.883 1.00 71.36 C
ATOM 3687 O TRP B 6 133.564 4.327 109.042 1.00 72.07 O
ATOM 3688 CB TRP B 6 134.471 1.770 108.763 1.00 69.81 C
ATOM 3689 CG TRP B 6 134.945 0.351 108.411 1.00 69.16 C
ATOM 3690 CD1 TRP B 6 134.131 -0.691 108.292 1.00 68.70 C
ATOM 3691 CD2 TRP B 6 136.214 -0.038 108.258 1.00 68.98 C
ATOM 3692 NE1 TRP B 6 134.896 -1.744 108.024 1.00 68.62 N
ATOM 3693 CE2 TRP B 6 136.173 -1.360 107.998 1.00 68.69 C
ATOM 3694 CE3 TRP B 6 137.390 0.620 108.299 1.00 68.43 C
ATOM 3695 CZ2 TRP B 6 137.299 -2.059 107.775 1.00 68.15 C
ATOM 3696 CZ3 TRP B 6 138.594 -0.055 108.082 1.00 67.61 C
ATOM 3697 CH2 TRP B 6 138.545 -1.423 107.806 1.00 67.74 C
ATOM 3698 N LYS B 7 133.068 4.751 106.908 1.00 71.92 N
ATOM 3699 CA LYS B 7 132.690 6.153 107.151 1.00 73.43 C
ATOM 3700 C LYS B 7 131.317 6.284 107.769 1.00 73.04 C
ATOM 3701 O LYS B 7 130.434 5.456 107.544 1.00 73.11 O
ATOM 3702 CB LYS B 7 132.842 7.035 105.904 1.00 75.76 C
ATOM 3703 CG LYS B 7 131.924 6.647 104.756 1.00 78.19 C
ATOM 3704 CD LYS B 7 131.048 7.839 104.436 1.00 79.38 C
ATOM 3705 CE LYS B 7 130.703 7.823 102.966 1.00 79.87 C
ATOM 3706 NZ LYS B 7 131.611 8.696 102.223 1.00 80.46 N
HETATM 3707 N NH2 B 8 131.155 7.337 108.570 1.00 72.58 N
TER 3708 NH2 B 8
HETATM 3709 CA CA A2101 137.027 3.376 99.983 1.00 84.90 CA2+
HETATM 3710 C1 OLA A2102 164.005 14.742 122.855 1.00 95.85 C
HETATM 3711 O1 OLA A2102 164.598 15.277 121.889 1.00 95.88 O
HETATM 3712 O2 OLA A2102 164.694 14.364 123.831 1.00 96.31 O
HETATM 3713 C2 OLA A2102 162.504 14.525 122.866 1.00 94.93 C
HETATM 3714 C3 OLA A2102 161.721 15.602 122.119 1.00 94.25 C
HETATM 3715 C4 OLA A2102 160.237 15.255 122.078 1.00 93.88 C
HETATM 3716 C1 OLA A2103 160.394 -1.166 135.263 1.00 75.95 C
HETATM 3717 O1 OLA A2103 160.900 -0.265 134.562 1.00 75.81 O
HETATM 3718 O2 OLA A2103 160.825 -2.332 135.138 1.00 76.71 O
HETATM 3719 C2 OLA A2103 159.285 -0.852 136.242 1.00 75.01 C
HETATM 3720 C3 OLA A2103 159.882 -0.375 137.563 1.00 73.71 C
HETATM 3721 C4 OLA A2103 158.804 -0.093 138.604 1.00 72.14 C
HETATM 3722 C5 OLA A2103 158.883 -1.080 139.762 1.00 70.48 C
HETATM 3723 C6 OLA A2103 157.556 -1.141 140.510 1.00 69.37 C
HETATM 3724 C7 OLA A2103 157.447 -2.414 141.342 1.00 68.44 C
HETATM 3725 C8 OLA A2103 156.212 -3.220 140.957 1.00 67.87 C
HETATM 3726 C1 OLA A2104 164.136 -2.283 132.591 1.00 94.74 C
HETATM 3727 O1 OLA A2104 165.348 -2.516 132.796 1.00 94.64 O
HETATM 3728 O2 OLA A2104 163.509 -1.560 133.396 1.00 95.09 O
HETATM 3729 C2 OLA A2104 163.437 -2.879 131.392 1.00 94.10 C
HETATM 3730 C3 OLA A2104 163.488 -1.917 130.212 1.00 93.38 C
HETATM 3731 C4 OLA A2104 162.912 -2.568 128.959 1.00 92.86 C
HETATM 3732 C5 OLA A2104 161.623 -1.882 128.523 1.00 92.41 C
HETATM 3733 C1 OLA A2105 168.247 0.387 131.970 1.00 89.84 C
HETATM 3734 O1 OLA A2105 167.538 -0.626 132.170 1.00 90.20 O
HETATM 3735 O2 OLA A2105 168.930 0.832 132.919 1.00 90.25 O
HETATM 3736 C2 OLA A2105 168.316 1.041 130.607 1.00 88.47 C
HETATM 3737 C3 OLA A2105 166.973 1.632 130.194 1.00 87.00 C
HETATM 3738 C4 OLA A2105 166.417 0.893 128.988 1.00 85.83 C
HETATM 3739 C5 OLA A2105 165.322 1.686 128.289 1.00 84.98 C
HETATM 3740 C6 OLA A2105 164.290 0.746 127.673 1.00 84.32 C
HETATM 3741 C7 OLA A2105 164.457 0.610 126.163 1.00 83.58 C
HETATM 3742 C8 OLA A2105 163.254 -0.097 125.548 1.00 83.14 C
HETATM 3743 C9 OLA A2105 163.343 -0.065 124.034 1.00 82.76 C
HETATM 3744 C10 OLA A2105 162.331 -0.370 123.208 1.00 82.21 C
HETATM 3745 C11 OLA A2105 160.947 -0.788 123.666 1.00 81.78 C
HETATM 3746 C12 OLA A2105 160.352 -1.793 122.689 1.00 81.38 C
HETATM 3747 C13 OLA A2105 160.121 -3.139 123.364 1.00 80.99 C
HETATM 3748 C14 OLA A2105 159.577 -4.175 122.384 1.00 80.49 C
HETATM 3749 C15 OLA A2105 160.549 -5.336 122.193 1.00 79.90 C
HETATM 3750 C16 OLA A2105 160.189 -6.537 123.062 1.00 79.56 C
HETATM 3751 C1 OLA A2106 163.609 14.287 128.795 1.00110.72 C
HETATM 3752 O1 OLA A2106 163.714 13.793 127.651 1.00110.98 O
HETATM 3753 O2 OLA A2106 164.522 14.085 129.625 1.00110.89 O
HETATM 3754 C2 OLA A2106 162.403 15.122 129.163 1.00110.06 C
HETATM 3755 C3 OLA A2106 161.408 14.295 129.970 1.00109.24 C
HETATM 3756 C4 OLA A2106 160.034 14.956 129.977 1.00108.60 C
HETATM 3757 C5 OLA A2106 159.142 14.365 131.063 1.00107.86 C
HETATM 3758 C6 OLA A2106 157.680 14.728 130.833 1.00107.16 C
HETATM 3759 C7 OLA A2106 156.916 14.746 132.152 1.00106.42 C
HETATM 3760 C8 OLA A2106 155.624 15.546 132.035 1.00105.71 C
HETATM 3761 C9 OLA A2106 154.517 14.807 132.749 1.00105.09 C
HETATM 3762 C10 OLA A2106 153.260 14.916 132.328 1.00104.64 C
HETATM 3763 C1 OLA A2107 166.222 -3.737 102.283 1.00 93.56 C
HETATM 3764 O1 OLA A2107 166.796 -4.107 101.235 1.00 93.70 O
HETATM 3765 O2 OLA A2107 166.410 -4.389 103.334 1.00 93.91 O
HETATM 3766 C2 OLA A2107 165.335 -2.511 102.280 1.00 92.88 C
HETATM 3767 C3 OLA A2107 163.857 -2.890 102.275 1.00 92.10 C
HETATM 3768 C4 OLA A2107 163.038 -1.800 101.591 1.00 91.33 C
HETATM 3769 C5 OLA A2107 161.612 -1.749 102.123 1.00 90.73 C
HETATM 3770 C6 OLA A2107 160.605 -1.752 100.979 1.00 90.30 C
HETATM 3771 C7 OLA A2107 159.257 -2.304 101.427 1.00 89.69 C
HETATM 3772 C8 OLA A2107 158.300 -2.430 100.248 1.00 89.14 C
HETATM 3773 C9 OLA A2107 158.050 -3.893 99.945 1.00 89.08 C
HETATM 3774 C10 OLA A2107 157.059 -4.351 99.167 1.00 88.97 C
HETATM 3775 C11 OLA A2107 156.037 -3.478 98.468 1.00 88.72 C
HETATM 3776 C12 OLA A2107 154.695 -4.199 98.414 1.00 88.62 C
HETATM 3777 C13 OLA A2107 153.555 -3.199 98.261 1.00 88.59 C
HETATM 3778 C14 OLA A2107 152.216 -3.899 98.063 1.00 88.22 C
HETATM 3779 C15 OLA A2107 151.095 -3.153 98.776 1.00 87.92 C
HETATM 3780 C1 OLA A2108 132.472 -10.775 117.435 1.00 86.56 C
HETATM 3781 O1 OLA A2108 131.482 -11.259 116.840 1.00 86.45 O
HETATM 3782 O2 OLA A2108 132.365 -10.494 118.652 1.00 86.93 O
HETATM 3783 C2 OLA A2108 133.761 -10.519 116.681 1.00 85.64 C
HETATM 3784 C3 OLA A2108 134.928 -11.312 117.265 1.00 84.55 C
HETATM 3785 C4 OLA A2108 136.077 -10.379 117.633 1.00 83.96 C
HETATM 3786 C5 OLA A2108 137.360 -11.150 117.914 1.00 83.42 C
HETATM 3787 C6 OLA A2108 138.568 -10.453 117.299 1.00 83.02 C
HETATM 3788 C1 OLA A2109 163.295 -7.474 131.624 1.00107.22 C
HETATM 3789 O1 OLA A2109 163.598 -8.543 131.050 1.00107.36 O
HETATM 3790 O2 OLA A2109 163.751 -7.253 132.768 1.00107.25 O
HETATM 3791 C2 OLA A2109 162.400 -6.465 130.938 1.00106.68 C
HETATM 3792 C3 OLA A2109 160.981 -6.531 131.498 1.00106.02 C
HETATM 3793 C4 OLA A2109 160.493 -5.163 131.972 1.00105.43 C
HETATM 3794 C5 OLA A2109 159.550 -4.521 130.957 1.00104.83 C
HETATM 3795 C6 OLA A2109 158.616 -3.502 131.606 1.00103.96 C
HETATM 3796 C7 OLA A2109 157.179 -4.014 131.669 1.00103.23 C
HETATM 3797 C8 OLA A2109 156.315 -3.447 130.545 1.00102.74 C
HETATM 3798 C9 OLA A2109 155.438 -2.333 131.081 1.00102.37 C
HETATM 3799 C10 OLA A2109 154.146 -2.151 130.771 1.00102.02 C
HETATM 3800 C11 OLA A2109 153.336 -3.028 129.835 1.00101.60 C
HETATM 3801 C12 OLA A2109 152.459 -2.155 128.942 1.00101.16 C
HETATM 3802 C13 OLA A2109 151.017 -2.113 129.437 1.00100.69 C
HETATM 3803 O HOH A2201 142.781 9.935 111.953 1.00 45.99 O
HETATM 3804 O HOH A2202 169.556 1.004 139.984 1.00 47.63 O
HETATM 3805 O HOH A2203 191.128 9.171 134.729 1.00 66.02 O
HETATM 3806 O HOH A2204 171.071 2.533 113.050 1.00 66.78 O
HETATM 3807 O HOH A2205 173.343 8.172 137.421 1.00 52.40 O
HETATM 3808 O HOH A2206 190.918 -0.554 132.308 1.00 71.88 O
HETATM 3809 O HOH A2207 168.394 9.555 116.702 1.00 61.40 O
HETATM 3810 O HOH A2208 189.901 2.590 135.112 1.00 59.05 O
HETATM 3811 O HOH A2209 181.221 0.701 160.978 1.00 66.51 O
HETATM 3812 O HOH A2210 184.528 -11.679 129.707 1.00 56.70 O
HETATM 3813 O HOH A2211 122.187 9.366 122.789 1.00 49.21 O
HETATM 3814 O HOH A2212 191.022 6.170 134.952 1.00 81.67 O
HETATM 3815 O HOH A2213 172.831 9.294 111.794 1.00 59.89 O
HETATM 3816 O HOH A2214 162.031 -9.862 134.372 1.00 72.90 O
HETATM 3817 O HOH A2215 192.501 -1.609 134.661 1.00 54.22 O
HETATM 3818 O HOH A2216 169.962 4.603 114.439 1.00 73.81 O
HETATM 3819 O HOH B 101 133.058 11.564 100.573 1.00 87.70 O
HETATM 3820 O HOH B 102 132.430 0.582 104.921 1.00 57.84 O
HETATM 3821 O HOH B 103 130.819 2.767 105.794 1.00 74.67 O
HETATM 3822 O HOH B 104 133.623 3.643 103.076 1.00 76.95 O
HETATM 3823 O HOH B 105 130.735 4.497 102.366 1.00 66.32 O
CONECT 432 3709
CONECT 578 3709
CONECT 609 3709
CONECT 610 3709
CONECT 1372 1378
CONECT 1378 1372 1379
CONECT 1379 1378 1380 1386
CONECT 1380 1379 1381
CONECT 1381 1380 1382
CONECT 1382 1381 1383
CONECT 1383 1382 1384 1385
CONECT 1384 1383
CONECT 1385 1383
CONECT 1386 1379 1387 1388
CONECT 1387 1386
CONECT 1388 1386
CONECT 3171 3220
CONECT 3220 3171
CONECT 3630 3631 3632 3633
CONECT 3631 3630
CONECT 3632 3630
CONECT 3633 3630 3634
CONECT 3634 3633 3635 3637
CONECT 3635 3634 3636 3641
CONECT 3636 3635
CONECT 3637 3634 3638
CONECT 3638 3637 3639
CONECT 3639 3638 3640
CONECT 3640 3639
CONECT 3641 3635
CONECT 3644 3709
CONECT 3650 3658
CONECT 3658 3650 3659
CONECT 3659 3658 3660 3671
CONECT 3660 3659 3661
CONECT 3661 3660 3662 3663
CONECT 3662 3661 3664
CONECT 3663 3661 3668
CONECT 3664 3662 3665
CONECT 3665 3664 3666 3668
CONECT 3666 3665 3667
CONECT 3667 3666 3670
CONECT 3668 3663 3665 3669
CONECT 3669 3668 3670
CONECT 3670 3667 3669
CONECT 3671 3659 3672 3673
CONECT 3672 3671 3709
CONECT 3673 3671
CONECT 3700 3707
CONECT 3707 3700
CONECT 3709 432 578 609 610
CONECT 3709 3644 3672
CONECT 3710 3711 3712 3713
CONECT 3711 3710
CONECT 3712 3710
CONECT 3713 3710 3714
CONECT 3714 3713 3715
CONECT 3715 3714
CONECT 3716 3717 3718 3719
CONECT 3717 3716
CONECT 3718 3716
CONECT 3719 3716 3720
CONECT 3720 3719 3721
CONECT 3721 3720 3722
CONECT 3722 3721 3723
CONECT 3723 3722 3724
CONECT 3724 3723 3725
CONECT 3725 3724
CONECT 3726 3727 3728 3729
CONECT 3727 3726
CONECT 3728 3726
CONECT 3729 3726 3730
CONECT 3730 3729 3731
CONECT 3731 3730 3732
CONECT 3732 3731
CONECT 3733 3734 3735 3736
CONECT 3734 3733
CONECT 3735 3733
CONECT 3736 3733 3737
CONECT 3737 3736 3738
CONECT 3738 3737 3739
CONECT 3739 3738 3740
CONECT 3740 3739 3741
CONECT 3741 3740 3742
CONECT 3742 3741 3743
CONECT 3743 3742 3744
CONECT 3744 3743 3745
CONECT 3745 3744 3746
CONECT 3746 3745 3747
CONECT 3747 3746 3748
CONECT 3748 3747 3749
CONECT 3749 3748 3750
CONECT 3750 3749
CONECT 3751 3752 3753 3754
CONECT 3752 3751
CONECT 3753 3751
CONECT 3754 3751 3755
CONECT 3755 3754 3756
CONECT 3756 3755 3757
CONECT 3757 3756 3758
CONECT 3758 3757 3759
CONECT 3759 3758 3760
CONECT 3760 3759 3761
CONECT 3761 3760 3762
CONECT 3762 3761
CONECT 3763 3764 3765 3766
CONECT 3764 3763
CONECT 3765 3763
CONECT 3766 3763 3767
CONECT 3767 3766 3768
CONECT 3768 3767 3769
CONECT 3769 3768 3770
CONECT 3770 3769 3771
CONECT 3771 3770 3772
CONECT 3772 3771 3773
CONECT 3773 3772 3774
CONECT 3774 3773 3775
CONECT 3775 3774 3776
CONECT 3776 3775 3777
CONECT 3777 3776 3778
CONECT 3778 3777 3779
CONECT 3779 3778
CONECT 3780 3781 3782 3783
CONECT 3781 3780
CONECT 3782 3780
CONECT 3783 3780 3784
CONECT 3784 3783 3785
CONECT 3785 3784 3786
CONECT 3786 3785 3787
CONECT 3787 3786
CONECT 3788 3789 3790 3791
CONECT 3789 3788
CONECT 3790 3788
CONECT 3791 3788 3792
CONECT 3792 3791 3793
CONECT 3793 3792 3794
CONECT 3794 3793 3795
CONECT 3795 3794 3796
CONECT 3796 3795 3797
CONECT 3797 3796 3798
CONECT 3798 3797 3799
CONECT 3799 3798 3800
CONECT 3800 3799 3801
CONECT 3801 3800 3802
CONECT 3802 3801
MASTER 449 0 14 22 6 0 12 6 3812 2 145 43
END