HEADER MEMBRANE PROTEIN 14-APR-22 7ZL9
TITLE CRYSTAL STRUCTURE OF HUMAN GPCR NIACIN RECEPTOR (HCA2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROXYCARBOXYLIC ACID RECEPTOR 2,SOLUBLE CYTOCHROME B562;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: G-PROTEIN COUPLED RECEPTOR 109A,G-PROTEIN COUPLED RECEPTOR
COMPND 5 HM74A,NIACIN RECEPTOR 1,NICOTINIC ACID RECEPTOR,CYTOCHROME B-562;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 562;
SOURCE 5 GENE: HCAR2, GPR109A, HCA2, HM74A, NIACR1, CYBC;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS NIACIN RECEPTOR, HYDROXYCARBOXYLIC ACID RECEPTOR 2, HCA2, GPCR,
KEYWDS 2 MEMBRANE PROTEIN STRUCTURE, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YANG,H.J.KANG,R.G.GAO,J.J.WANG,G.W.HAN,J.F.FIBERTO,L.J.WU,J.H.TONG,
AUTHOR 2 L.QU,Y.R.WU,R.PILESKI,X.M.LI,X.C.ZHANG,S.W.ZHAO,T.KENAKIN,Q.WANG,
AUTHOR 3 R.C.STEVENS,W.PENG,B.L.ROTH,Z.H.RAO,Z.J.LIU
REVDAT 1 12-APR-23 7ZL9 0
JRNL AUTH Y.YANG,H.J.KANG,R.GAO,J.WANG,G.W.HAN,J.F.DIBERTO,L.WU,
JRNL AUTH 2 J.TONG,L.QU,Y.WU,R.PILESKI,X.LI,X.C.ZHANG,S.ZHAO,T.KENAKIN,
JRNL AUTH 3 Q.WANG,R.C.STEVENS,W.PENG,B.L.ROTH,Z.RAO,Z.J.LIU
JRNL TITL STRUCTURAL INSIGHTS INTO THE HUMAN NIACIN RECEPTOR HCA2-G I
JRNL TITL 2 SIGNALLING COMPLEX.
JRNL REF NAT COMMUN V. 14 1692 2023
JRNL REFN ESSN 2041-1723
JRNL PMID 36973264
JRNL DOI 10.1038/S41467-023-37177-6
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 16005
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.750
REMARK 3 FREE R VALUE TEST SET COUNT : 760
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.89
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.02
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2824
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2260
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2658
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.88
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 166
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 : 3100
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 93
REMARK 3 SOLVENT ATOMS : 3
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.02690
REMARK 3 B22 (A**2) : 13.20760
REMARK 3 B33 (A**2) : -8.18070
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.470
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.601
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.294
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.614
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.299
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 : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : NULL ; NULL ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL
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 : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|11- A|312 }
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8710 80.5849 187.719
REMARK 3 T TENSOR
REMARK 3 T11: -0.3237 T22: -0.3707
REMARK 3 T33: 0.0806 T12: -0.0167
REMARK 3 T13: -0.0431 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 3.4345 L22: 5.1903
REMARK 3 L33: 1.3492 L12: 0.8796
REMARK 3 L13: -0.1971 L23: -0.7090
REMARK 3 S TENSOR
REMARK 3 S11: -0.0027 S12: -0.0451 S13: -0.1313
REMARK 3 S21: 0.2524 S22: 0.0558 S23: -0.1132
REMARK 3 S31: 0.0058 S32: 0.0937 S33: -0.0531
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|1001- A|1106 }
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2679 124.713 168.958
REMARK 3 T TENSOR
REMARK 3 T11: -0.3396 T22: -0.4714
REMARK 3 T33: 0.5867 T12: 0.0571
REMARK 3 T13: 0.0146 T23: 0.1528
REMARK 3 L TENSOR
REMARK 3 L11: 9.4141 L22: 10.0620
REMARK 3 L33: 0.0138 L12: 2.6398
REMARK 3 L13: -0.5670 L23: -1.1179
REMARK 3 S TENSOR
REMARK 3 S11: -0.1458 S12: 0.4310 S13: 0.8055
REMARK 3 S21: -0.1318 S22: 0.2617 S23: -0.1035
REMARK 3 S31: 0.3789 S32: 0.1158 S33: -0.1159
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7ZL9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1292122373.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16035
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 47.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4PXZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM PH5.4 SODIUM CITRATE, 60MM
REMARK 280 AMMONIUM CITRATE, 36% PEG400, AND 3% ADDITIVE 80 (40% PPG),
REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
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,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,Z+1/2
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 40.44000
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.89000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 40.44000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.89000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 1
REMARK 465 ASN A 2
REMARK 465 ARG A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 LEU A 6
REMARK 465 GLN A 7
REMARK 465 ASP A 8
REMARK 465 HIS A 9
REMARK 465 PHE A 10
REMARK 465 GLY A 172
REMARK 465 GLY A 173
REMARK 465 LEU A 988
REMARK 465 GLN A 989
REMARK 465 ARG A 990
REMARK 465 LYS A 991
REMARK 465 MET A 992
REMARK 465 THR A 993
REMARK 465 GLY A 994
REMARK 465 GLU A 995
REMARK 465 PRO A 996
REMARK 465 ASP A 997
REMARK 465 ASN A 998
REMARK 465 ASN A 999
REMARK 465 ARG A 1000
REMARK 465 GLU A 1049
REMARK 465 ASP A 1050
REMARK 465 LYS A 1051
REMARK 465 SER A 1052
REMARK 465 PRO A 1053
REMARK 465 ASP A 1054
REMARK 465 SER A 1055
REMARK 465 PRO A 1056
REMARK 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 GLU A 12 CG CD OE1 OE2
REMARK 470 ASP A 14 CG OD1 OD2
REMARK 470 LYS A 15 CG CD CE NZ
REMARK 470 LYS A 16 CG CD CE NZ
REMARK 470 ARG A 22 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 24 CG OD1 OD2
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 LYS A 60 CG CD CE NZ
REMARK 470 ARG A 90 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 94 CG CD CE NZ
REMARK 470 LYS A 138 CG CD CE NZ
REMARK 470 ARG A 142 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 165 CG CD CE NZ
REMARK 470 LYS A 166 CG CD CE NZ
REMARK 470 GLN A 170 CG CD OE1 NE2
REMARK 470 ASN A 171 CG OD1 ND2
REMARK 470 ARG A 218 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 264 CG CD OE1 NE2
REMARK 470 LYS A1015 CG CD CE NZ
REMARK 470 LYS A1019 CG CD CE NZ
REMARK 470 LYS A1042 CG CD CE NZ
REMARK 470 THR A1044 OG1 CG2
REMARK 470 LEU A1048 CG CD1 CD2
REMARK 470 GLU A1057 CG CD OE1 OE2
REMARK 470 MET A1058 CG SD CE
REMARK 470 LYS A1059 CD CE NZ
REMARK 470 PHE A1061 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1078 CG CD1 CD2
REMARK 470 LYS A1083 CG CD CE NZ
REMARK 470 LYS A1085 CG CD CE NZ
REMARK 470 GLU A1086 CG CD OE1 OE2
REMARK 470 LYS A1104 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N MET A 220 C LEU A 1106 1.35
REMARK 500 C GLN A 219 N ALA A 1001 1.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 17 70.54 57.86
REMARK 500 LYS A 138 34.59 -87.02
REMARK 500 GLN A 187 -164.56 -129.23
REMARK 500 ALA A1043 49.14 -86.91
REMARK 500 LYS A1083 88.66 -69.20
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 1201
REMARK 610 OLA A 1202
REMARK 610 OLA A 1203
REMARK 610 OLA A 1204
REMARK 610 OLA A 1205
DBREF 7ZL9 A 1 1000 UNP Q8TDS4 HCAR2_HUMAN 1 325
DBREF 7ZL9 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
SEQADV 7ZL9 VAL A 70 UNP Q8TDS4 ALA 70 CONFLICT
SEQADV 7ZL9 VAL A 287 UNP Q8TDS4 SER 287 CONFLICT
SEQADV 7ZL9 TRP A 1007 UNP P0ABE7 MET 29 CONFLICT
SEQADV 7ZL9 ILE A 1102 UNP P0ABE7 HIS 124 CONFLICT
SEQADV 7ZL9 LEU A 1106 UNP P0ABE7 ARG 128 CONFLICT
SEQRES 1 A 431 MET ASN ARG HIS HIS LEU GLN ASP HIS PHE LEU GLU ILE
SEQRES 2 A 431 ASP LYS LYS ASN CYS CYS VAL PHE ARG ASP ASP PHE ILE
SEQRES 3 A 431 VAL LYS VAL LEU PRO PRO VAL LEU GLY LEU GLU PHE ILE
SEQRES 4 A 431 PHE GLY LEU LEU GLY ASN GLY LEU ALA LEU TRP ILE PHE
SEQRES 5 A 431 CYS PHE HIS LEU LYS SER TRP LYS SER SER ARG ILE PHE
SEQRES 6 A 431 LEU PHE ASN LEU VAL VAL ALA ASP PHE LEU LEU ILE ILE
SEQRES 7 A 431 CYS LEU PRO PHE LEU MET ASP ASN TYR VAL ARG ARG TRP
SEQRES 8 A 431 ASP TRP LYS PHE GLY ASP ILE PRO CYS ARG LEU MET LEU
SEQRES 9 A 431 PHE MET LEU ALA MET ASN ARG GLN GLY SER ILE ILE PHE
SEQRES 10 A 431 LEU THR VAL VAL ALA VAL ASP ARG TYR PHE ARG VAL VAL
SEQRES 11 A 431 HIS PRO HIS HIS ALA LEU ASN LYS ILE SER ASN ARG THR
SEQRES 12 A 431 ALA ALA ILE ILE SER CYS LEU LEU TRP GLY ILE THR ILE
SEQRES 13 A 431 GLY LEU THR VAL HIS LEU LEU LYS LYS LYS MET PRO ILE
SEQRES 14 A 431 GLN ASN GLY GLY ALA ASN LEU CYS SER SER PHE SER ILE
SEQRES 15 A 431 CYS HIS THR PHE GLN TRP HIS GLU ALA MET PHE LEU LEU
SEQRES 16 A 431 GLU PHE PHE LEU PRO LEU GLY ILE ILE LEU PHE CYS SER
SEQRES 17 A 431 ALA ARG ILE ILE TRP SER LEU ARG GLN ARG GLN MET ASP
SEQRES 18 A 431 ARG HIS ALA LYS ILE LYS ARG ALA ILE THR PHE ILE MET
SEQRES 19 A 431 VAL VAL ALA ILE VAL PHE VAL ILE CYS PHE LEU PRO SER
SEQRES 20 A 431 VAL VAL VAL ARG ILE ARG ILE PHE TRP LEU LEU HIS THR
SEQRES 21 A 431 SER GLY THR GLN ASN CYS GLU VAL TYR ARG SER VAL ASP
SEQRES 22 A 431 LEU ALA PHE PHE ILE THR LEU SER PHE THR TYR MET ASN
SEQRES 23 A 431 VAL MET LEU ASP PRO VAL VAL TYR TYR PHE SER SER PRO
SEQRES 24 A 431 SER PHE PRO ASN PHE PHE SER THR LEU ILE ASN ARG CYS
SEQRES 25 A 431 LEU GLN ARG LYS MET THR GLY GLU PRO ASP ASN ASN ARG
SEQRES 26 A 431 ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN
SEQRES 27 A 431 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL
SEQRES 28 A 431 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP
SEQRES 29 A 431 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER
SEQRES 30 A 431 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE
SEQRES 31 A 431 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU
SEQRES 32 A 431 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA
SEQRES 33 A 431 GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS
SEQRES 34 A 431 TYR LEU
HET OLA A1201 18
HET OLA A1202 7
HET OLA A1203 7
HET OLA A1204 8
HET OLA A1205 16
HET OLC A1206 25
HET PEG A1207 7
HET UNX A1208 1
HET UNX A1209 1
HET UNX A1210 1
HET UNX A1211 1
HET UNX A1212 1
HETNAM OLA OLEIC ACID
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 OLA 5(C18 H34 O2)
FORMUL 7 OLC C21 H40 O4
FORMUL 8 PEG C4 H10 O3
FORMUL 9 UNX 5(X)
FORMUL 14 HOH *3(H2 O)
HELIX 1 AA1 PHE A 25 PHE A 54 1 30
HELIX 2 AA2 LYS A 60 ARG A 89 1 30
HELIX 3 AA3 GLY A 96 VAL A 130 1 35
HELIX 4 AA4 SER A 140 VAL A 160 1 21
HELIX 5 AA5 HIS A 161 LYS A 164 5 4
HELIX 6 AA6 GLN A 187 GLN A 219 1 33
HELIX 7 AA7 ASP A 221 SER A 261 1 41
HELIX 8 AA8 ASN A 265 VAL A 268 5 4
HELIX 9 AA9 TYR A 269 MET A 285 1 17
HELIX 10 AB1 MET A 285 PHE A 296 1 12
HELIX 11 AB2 PRO A 299 CYS A 312 1 14
HELIX 12 AB3 ASP A 1002 LYS A 1019 1 18
HELIX 13 AB4 ASN A 1022 ALA A 1043 1 22
HELIX 14 AB5 MET A 1058 ASN A 1080 1 23
HELIX 15 AB6 LYS A 1083 GLU A 1092 1 10
HELIX 16 AB7 GLU A 1092 ILE A 1102 1 11
SSBOND 1 CYS A 18 CYS A 183 1555 1555 2.03
SSBOND 2 CYS A 19 CYS A 266 1555 1555 2.04
SSBOND 3 CYS A 100 CYS A 177 1555 1555 2.03
CISPEP 1 MET A 167 PRO A 168 0 -1.62
CRYST1 80.880 81.990 85.780 90.00 90.00 90.00 P 21 2 21 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 0.012364 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012197 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011658 0.00000
ATOM 1 N LEU A 11 23.847 53.596 183.491 1.00124.20 N
ANISOU 1 N LEU A 11 13683 9952 23557 354 319 -1240 N
ATOM 2 CA LEU A 11 23.033 52.705 182.666 1.00126.10 C
ANISOU 2 CA LEU A 11 14033 9969 23908 231 379 -1528 C
ATOM 3 C LEU A 11 22.149 51.787 183.529 1.00131.02 C
ANISOU 3 C LEU A 11 14608 10367 24806 177 243 -1277 C
ATOM 4 O LEU A 11 20.976 51.588 183.202 1.00130.44 O
ANISOU 4 O LEU A 11 14638 10284 24639 11 179 -1374 O
ATOM 5 CB LEU A 11 23.932 51.864 181.740 1.00129.59 C
ANISOU 5 CB LEU A 11 14454 10105 24680 315 622 -1877 C
ATOM 6 CG LEU A 11 23.229 51.070 180.636 1.00136.89 C
ANISOU 6 CG LEU A 11 15548 10820 25642 170 711 -2283 C
ATOM 7 CD1 LEU A 11 23.239 51.829 179.325 1.00136.66 C
ANISOU 7 CD1 LEU A 11 15730 11030 25162 72 831 -2662 C
ATOM 8 CD2 LEU A 11 23.877 49.710 180.448 1.00143.97 C
ANISOU 8 CD2 LEU A 11 16351 11239 27111 275 891 -2446 C
ATOM 9 N GLU A 12 22.716 51.238 184.621 1.00128.98 N
ANISOU 9 N GLU A 12 14188 9926 24892 309 191 -940 N
ATOM 10 CA GLU A 12 22.069 50.283 185.525 1.00130.39 C
ANISOU 10 CA GLU A 12 14308 9854 25381 279 86 -650 C
ATOM 11 C GLU A 12 21.072 50.914 186.518 1.00131.63 C
ANISOU 11 C GLU A 12 14515 10269 25230 180 -75 -304 C
ATOM 12 O GLU A 12 21.101 52.122 186.772 1.00128.23 O
ANISOU 12 O GLU A 12 14135 10203 24385 178 -129 -217 O
ATOM 13 CB GLU A 12 23.141 49.510 186.313 1.00134.20 C
ANISOU 13 CB GLU A 12 14605 10052 26334 463 78 -388 C
ATOM 14 N ILE A 13 20.187 50.054 187.073 1.00129.53 N
ANISOU 14 N ILE A 13 14230 9784 25199 97 -128 -113 N
ATOM 15 CA ILE A 13 19.183 50.362 188.095 1.00127.93 C
ANISOU 15 CA ILE A 13 14059 9735 24813 3 -227 239 C
ATOM 16 C ILE A 13 19.793 49.881 189.442 1.00133.23 C
ANISOU 16 C ILE A 13 14649 10275 25698 120 -300 694 C
ATOM 17 O ILE A 13 19.472 48.804 189.958 1.00135.53 O
ANISOU 17 O ILE A 13 14885 10256 26354 101 -313 902 O
ATOM 18 CB ILE A 13 17.767 49.774 187.737 1.00131.96 C
ANISOU 18 CB ILE A 13 14595 10097 25445 -186 -225 145 C
ATOM 19 CG1 ILE A 13 16.719 50.051 188.856 1.00131.39 C
ANISOU 19 CG1 ILE A 13 14529 10160 25234 -278 -275 533 C
ATOM 20 CG2 ILE A 13 17.816 48.278 187.340 1.00136.40 C
ANISOU 20 CG2 ILE A 13 15092 10178 26556 -196 -177 14 C
ATOM 21 CD1 ILE A 13 15.243 50.033 188.419 1.00137.58 C
ANISOU 21 CD1 ILE A 13 15321 10950 26002 -478 -282 425 C
ATOM 22 N ASP A 14 20.745 50.680 189.956 1.00128.05 N
ANISOU 22 N ASP A 14 13984 9843 24825 238 -364 842 N
ATOM 23 CA ASP A 14 21.503 50.392 191.176 1.00129.01 C
ANISOU 23 CA ASP A 14 14043 9889 25084 349 -485 1264 C
ATOM 24 C ASP A 14 20.773 50.853 192.445 1.00130.74 C
ANISOU 24 C ASP A 14 14377 10322 24975 268 -572 1660 C
ATOM 25 O ASP A 14 20.687 50.083 193.405 1.00133.00 O
ANISOU 25 O ASP A 14 14653 10420 25460 272 -637 2029 O
ATOM 26 CB ASP A 14 22.889 51.040 191.095 1.00130.14 C
ANISOU 26 CB ASP A 14 14115 10165 25168 497 -535 1222 C
ATOM 27 N LYS A 15 20.254 52.097 192.451 1.00122.65 N
ANISOU 27 N LYS A 15 13470 9675 23457 194 -556 1589 N
ATOM 28 CA LYS A 15 19.524 52.664 193.587 1.00120.95 C
ANISOU 28 CA LYS A 15 13384 9682 22891 114 -584 1907 C
ATOM 29 C LYS A 15 18.097 52.095 193.656 1.00123.61 C
ANISOU 29 C LYS A 15 13737 9894 23334 -31 -476 1966 C
ATOM 30 O LYS A 15 17.661 51.414 192.722 1.00123.90 O
ANISOU 30 O LYS A 15 13695 9712 23670 -82 -413 1717 O
ATOM 31 CB LYS A 15 19.496 54.200 193.489 1.00120.29 C
ANISOU 31 CB LYS A 15 13398 10005 22301 95 -581 1774 C
ATOM 32 N LYS A 16 17.377 52.366 194.768 1.00118.66 N
ANISOU 32 N LYS A 16 13217 9398 22469 -105 -448 2291 N
ATOM 33 CA LYS A 16 16.001 51.906 194.975 1.00118.42 C
ANISOU 33 CA LYS A 16 13184 9266 22545 -246 -322 2398 C
ATOM 34 C LYS A 16 15.047 52.683 194.053 1.00116.41 C
ANISOU 34 C LYS A 16 12908 9188 22135 -344 -235 2072 C
ATOM 35 O LYS A 16 14.732 53.848 194.321 1.00113.75 O
ANISOU 35 O LYS A 16 12654 9163 21401 -363 -193 2072 O
ATOM 36 CB LYS A 16 15.590 52.041 196.453 1.00122.28 C
ANISOU 36 CB LYS A 16 13809 9860 22793 -290 -277 2841 C
ATOM 37 N ASN A 17 14.632 52.027 192.940 1.00110.78 N
ANISOU 37 N ASN A 17 12085 8258 21747 -406 -225 1788 N
ATOM 38 CA ASN A 17 13.742 52.536 191.886 1.00107.56 C
ANISOU 38 CA ASN A 17 11640 7954 21273 -514 -200 1467 C
ATOM 39 C ASN A 17 14.321 53.822 191.253 1.00104.58 C
ANISOU 39 C ASN A 17 11326 7899 20511 -450 -241 1213 C
ATOM 40 O ASN A 17 13.805 54.924 191.473 1.00102.32 O
ANISOU 40 O ASN A 17 11086 7893 19898 -482 -207 1242 O
ATOM 41 CB ASN A 17 12.308 52.744 192.415 1.00108.58 C
ANISOU 41 CB ASN A 17 11741 8145 21371 -651 -97 1652 C
ATOM 42 CG ASN A 17 11.552 51.465 192.718 1.00134.61 C
ANISOU 42 CG ASN A 17 14942 11099 25105 -753 -46 1832 C
ATOM 43 OD1 ASN A 17 12.128 50.390 192.940 1.00130.74 O
ANISOU 43 OD1 ASN A 17 14434 10323 24919 -707 -77 1942 O
ATOM 44 ND2 ASN A 17 10.232 51.560 192.752 1.00126.91 N
ANISOU 44 ND2 ASN A 17 13884 10129 24208 -895 38 1884 N
ATOM 45 N CYS A 18 15.420 53.664 190.481 1.00 98.01 N
ANISOU 45 N CYS A 18 10490 7006 19745 -356 -296 972 N
ATOM 46 CA CYS A 18 16.121 54.765 189.814 1.00 93.90 C
ANISOU 46 CA CYS A 18 10021 6750 18909 -293 -321 735 C
ATOM 47 C CYS A 18 16.808 54.288 188.527 1.00 95.34 C
ANISOU 47 C CYS A 18 10179 6778 19268 -261 -320 367 C
ATOM 48 O CYS A 18 17.586 53.335 188.560 1.00 96.90 O
ANISOU 48 O CYS A 18 10323 6711 19785 -177 -309 373 O
ATOM 49 CB CYS A 18 17.119 55.423 190.765 1.00 93.13 C
ANISOU 49 CB CYS A 18 9972 6829 18583 -168 -358 956 C
ATOM 50 SG CYS A 18 18.000 56.842 190.057 1.00 94.09 S
ANISOU 50 SG CYS A 18 10140 7270 18342 -98 -381 706 S
ATOM 51 N CYS A 19 16.530 54.974 187.403 1.00 88.45 N
ANISOU 51 N CYS A 19 9355 6069 18184 -328 -321 53 N
ATOM 52 CA CYS A 19 17.101 54.666 186.089 1.00 88.39 C
ANISOU 52 CA CYS A 19 9375 5959 18248 -322 -290 -331 C
ATOM 53 C CYS A 19 17.957 55.841 185.599 1.00 89.23 C
ANISOU 53 C CYS A 19 9540 6351 18013 -248 -266 -473 C
ATOM 54 O CYS A 19 17.415 56.864 185.174 1.00 87.22 O
ANISOU 54 O CYS A 19 9348 6355 17436 -322 -301 -551 O
ATOM 55 CB CYS A 19 16.001 54.321 185.088 1.00 89.55 C
ANISOU 55 CB CYS A 19 9558 6022 18443 -497 -329 -584 C
ATOM 56 SG CYS A 19 14.920 52.960 185.604 1.00 96.11 S
ANISOU 56 SG CYS A 19 10297 6500 19720 -612 -358 -424 S
ATOM 57 N VAL A 20 19.294 55.701 185.682 1.00 85.49 N
ANISOU 57 N VAL A 20 9024 5814 17645 -100 -210 -484 N
ATOM 58 CA VAL A 20 20.252 56.732 185.256 1.00 83.26 C
ANISOU 58 CA VAL A 20 8766 5763 17105 -23 -168 -601 C
ATOM 59 C VAL A 20 21.020 56.224 184.033 1.00 87.10 C
ANISOU 59 C VAL A 20 9267 6093 17735 11 -32 -960 C
ATOM 60 O VAL A 20 21.391 55.056 183.999 1.00 88.43 O
ANISOU 60 O VAL A 20 9370 5941 18288 64 30 -1013 O
ATOM 61 CB VAL A 20 21.223 57.176 186.391 1.00 86.63 C
ANISOU 61 CB VAL A 20 9116 6280 17519 114 -216 -307 C
ATOM 62 CG1 VAL A 20 22.000 58.432 186.001 1.00 84.45 C
ANISOU 62 CG1 VAL A 20 8861 6277 16952 159 -191 -406 C
ATOM 63 CG2 VAL A 20 20.482 57.414 187.699 1.00 85.62 C
ANISOU 63 CG2 VAL A 20 9008 6246 17279 78 -319 47 C
ATOM 64 N PHE A 21 21.264 57.105 183.043 1.00 82.36 N
ANISOU 64 N PHE A 21 8757 5706 16828 -21 31 -1202 N
ATOM 65 CA PHE A 21 21.995 56.766 181.824 1.00 83.80 C
ANISOU 65 CA PHE A 21 8993 5780 17067 -1 205 -1561 C
ATOM 66 C PHE A 21 23.098 57.790 181.530 1.00 86.34 C
ANISOU 66 C PHE A 21 9297 6316 17191 88 307 -1604 C
ATOM 67 O PHE A 21 22.838 58.997 181.505 1.00 83.61 O
ANISOU 67 O PHE A 21 9012 6274 16482 38 239 -1538 O
ATOM 68 CB PHE A 21 21.038 56.645 180.625 1.00 86.26 C
ANISOU 68 CB PHE A 21 9485 6104 17184 -180 198 -1872 C
ATOM 69 CG PHE A 21 20.104 55.460 180.687 1.00 89.60 C
ANISOU 69 CG PHE A 21 9913 6249 17882 -278 125 -1907 C
ATOM 70 CD1 PHE A 21 20.479 54.230 180.160 1.00 95.69 C
ANISOU 70 CD1 PHE A 21 10697 6674 18987 -261 253 -2155 C
ATOM 71 CD2 PHE A 21 18.841 55.578 181.254 1.00 90.43 C
ANISOU 71 CD2 PHE A 21 10001 6418 17941 -390 -54 -1700 C
ATOM 72 CE1 PHE A 21 19.613 53.135 180.216 1.00 98.58 C
ANISOU 72 CE1 PHE A 21 11062 6759 19634 -363 178 -2190 C
ATOM 73 CE2 PHE A 21 17.977 54.482 181.311 1.00 95.11 C
ANISOU 73 CE2 PHE A 21 10575 6738 18823 -492 -119 -1721 C
ATOM 74 CZ PHE A 21 18.368 53.268 180.790 1.00 96.36 C
ANISOU 74 CZ PHE A 21 10752 6551 19308 -483 -15 -1965 C
ATOM 75 N ARG A 22 24.331 57.289 181.313 1.00 84.67 N
ANISOU 75 N ARG A 22 8984 5922 17265 221 481 -1708 N
ATOM 76 CA ARG A 22 25.513 58.082 180.983 1.00 84.23 C
ANISOU 76 CA ARG A 22 8870 6007 17129 313 619 -1762 C
ATOM 77 C ARG A 22 25.867 57.868 179.516 1.00 91.19 C
ANISOU 77 C ARG A 22 9877 6826 17943 276 879 -2175 C
ATOM 78 O ARG A 22 26.655 56.975 179.187 1.00 93.98 O
ANISOU 78 O ARG A 22 10151 6902 18655 373 1083 -2342 O
ATOM 79 CB ARG A 22 26.697 57.720 181.897 1.00 85.46 C
ANISOU 79 CB ARG A 22 8778 5997 17695 496 624 -1539 C
ATOM 80 N ASP A 23 25.258 58.675 178.632 1.00 87.29 N
ANISOU 80 N ASP A 23 9592 6582 16992 133 875 -2338 N
ATOM 81 CA ASP A 23 25.473 58.606 177.186 1.00 89.75 C
ANISOU 81 CA ASP A 23 10096 6891 17116 60 1106 -2727 C
ATOM 82 C ASP A 23 26.917 58.958 176.834 1.00 95.85 C
ANISOU 82 C ASP A 23 10765 7670 17982 189 1387 -2807 C
ATOM 83 O ASP A 23 27.543 59.767 177.528 1.00 93.37 O
ANISOU 83 O ASP A 23 10282 7502 17694 280 1335 -2554 O
ATOM 84 CB ASP A 23 24.500 59.550 176.455 1.00 90.11 C
ANISOU 84 CB ASP A 23 10377 7238 16624 -126 979 -2795 C
ATOM 85 CG ASP A 23 24.281 59.232 174.986 1.00103.74 C
ANISOU 85 CG ASP A 23 12380 8938 18101 -265 1125 -3195 C
ATOM 86 OD1 ASP A 23 25.234 59.399 174.191 1.00106.46 O
ANISOU 86 OD1 ASP A 23 12790 9296 18365 -227 1412 -3402 O
ATOM 87 OD2 ASP A 23 23.140 58.873 174.620 1.00109.94 O
ANISOU 87 OD2 ASP A 23 13324 9702 18748 -426 948 -3295 O
ATOM 88 N ASP A 24 27.436 58.360 175.741 1.00 96.84 N
ANISOU 88 N ASP A 24 10999 7633 18162 188 1696 -3170 N
ATOM 89 CA ASP A 24 28.793 58.597 175.238 1.00 98.98 C
ANISOU 89 CA ASP A 24 11177 7879 18552 302 2038 -3294 C
ATOM 90 C ASP A 24 28.980 60.063 174.793 1.00102.06 C
ANISOU 90 C ASP A 24 11656 8639 18485 235 2062 -3236 C
ATOM 91 O ASP A 24 30.112 60.505 174.612 1.00102.96 O
ANISOU 91 O ASP A 24 11635 8779 18706 331 2301 -3238 O
ATOM 92 CB ASP A 24 29.117 57.640 174.081 1.00105.11 C
ANISOU 92 CB ASP A 24 12111 8406 19420 287 2394 -3737 C
ATOM 93 N PHE A 25 27.869 60.808 174.641 1.00 96.31 N
ANISOU 93 N PHE A 25 11128 8174 17293 72 1814 -3167 N
ATOM 94 CA PHE A 25 27.835 62.210 174.236 1.00 94.41 C
ANISOU 94 CA PHE A 25 10989 8272 16609 -10 1786 -3084 C
ATOM 95 C PHE A 25 28.131 63.139 175.421 1.00 95.55 C
ANISOU 95 C PHE A 25 10892 8563 16849 80 1594 -2706 C
ATOM 96 O PHE A 25 28.819 64.141 175.237 1.00 94.67 O
ANISOU 96 O PHE A 25 10733 8623 16613 98 1695 -2638 O
ATOM 97 CB PHE A 25 26.462 62.536 173.626 1.00 95.42 C
ANISOU 97 CB PHE A 25 11407 8579 16271 -216 1566 -3149 C
ATOM 98 CG PHE A 25 26.341 63.858 172.907 1.00 96.02 C
ANISOU 98 CG PHE A 25 11649 8973 15861 -327 1558 -3116 C
ATOM 99 CD1 PHE A 25 26.949 64.056 171.672 1.00101.92 C
ANISOU 99 CD1 PHE A 25 12594 9780 16350 -384 1861 -3363 C
ATOM 100 CD2 PHE A 25 25.553 64.879 173.425 1.00 94.92 C
ANISOU 100 CD2 PHE A 25 11489 9059 15516 -383 1258 -2842 C
ATOM 101 CE1 PHE A 25 26.812 65.271 170.993 1.00102.33 C
ANISOU 101 CE1 PHE A 25 12813 10119 15947 -496 1844 -3302 C
ATOM 102 CE2 PHE A 25 25.401 66.086 172.737 1.00 97.16 C
ANISOU 102 CE2 PHE A 25 11925 9610 15381 -487 1237 -2795 C
ATOM 103 CZ PHE A 25 26.040 66.278 171.531 1.00 97.96 C
ANISOU 103 CZ PHE A 25 12218 9774 15229 -545 1519 -3010 C
ATOM 104 N ILE A 26 27.622 62.804 176.628 1.00 90.44 N
ANISOU 104 N ILE A 26 10107 7842 16415 126 1326 -2467 N
ATOM 105 CA ILE A 26 27.809 63.586 177.860 1.00 87.38 C
ANISOU 105 CA ILE A 26 9530 7577 16094 196 1119 -2120 C
ATOM 106 C ILE A 26 29.301 63.577 178.265 1.00 91.70 C
ANISOU 106 C ILE A 26 9814 8018 17008 357 1267 -2041 C
ATOM 107 O ILE A 26 29.850 64.628 178.580 1.00 90.03 O
ANISOU 107 O ILE A 26 9507 7978 16724 378 1229 -1885 O
ATOM 108 CB ILE A 26 26.876 63.075 179.004 1.00 89.25 C
ANISOU 108 CB ILE A 26 9724 7737 16452 195 839 -1906 C
ATOM 109 CG1 ILE A 26 25.384 63.179 178.597 1.00 88.71 C
ANISOU 109 CG1 ILE A 26 9869 7775 16063 30 688 -1964 C
ATOM 110 CG2 ILE A 26 27.127 63.825 180.324 1.00 87.97 C
ANISOU 110 CG2 ILE A 26 9402 7690 16331 262 642 -1568 C
ATOM 111 CD1 ILE A 26 24.443 62.165 179.277 1.00 97.38 C
ANISOU 111 CD1 ILE A 26 10950 8691 17360 8 527 -1882 C
ATOM 112 N VAL A 27 29.955 62.409 178.210 1.00 90.80 N
ANISOU 112 N VAL A 27 9576 7610 17314 465 1435 -2155 N
ATOM 113 CA VAL A 27 31.376 62.246 178.545 1.00 92.01 C
ANISOU 113 CA VAL A 27 9438 7613 17909 627 1578 -2083 C
ATOM 114 C VAL A 27 32.270 62.904 177.447 1.00 96.94 C
ANISOU 114 C VAL A 27 10071 8331 18432 622 1919 -2278 C
ATOM 115 O VAL A 27 33.415 63.269 177.727 1.00 97.34 O
ANISOU 115 O VAL A 27 9867 8358 18761 725 2005 -2165 O
ATOM 116 CB VAL A 27 31.711 60.735 178.782 1.00 98.47 C
ANISOU 116 CB VAL A 27 10112 8050 19251 748 1662 -2143 C
ATOM 117 CG1 VAL A 27 31.497 59.889 177.531 1.00101.09 C
ANISOU 117 CG1 VAL A 27 10635 8212 19564 703 1967 -2544 C
ATOM 118 CG2 VAL A 27 33.114 60.527 179.344 1.00100.18 C
ANISOU 118 CG2 VAL A 27 9972 8087 20003 928 1730 -1991 C
ATOM 119 N LYS A 28 31.719 63.097 176.230 1.00 93.65 N
ANISOU 119 N LYS A 28 9949 8029 17603 489 2091 -2547 N
ATOM 120 CA LYS A 28 32.433 63.633 175.071 1.00 95.28 C
ANISOU 120 CA LYS A 28 10234 8326 17644 459 2450 -2752 C
ATOM 121 C LYS A 28 32.323 65.162 174.892 1.00 96.41 C
ANISOU 121 C LYS A 28 10460 8804 17367 357 2367 -2609 C
ATOM 122 O LYS A 28 33.354 65.801 174.666 1.00 96.96 O
ANISOU 122 O LYS A 28 10385 8924 17534 402 2576 -2577 O
ATOM 123 CB LYS A 28 31.922 62.943 173.796 1.00100.43 C
ANISOU 123 CB LYS A 28 11207 8908 18045 354 2687 -3133 C
ATOM 124 CG LYS A 28 32.904 62.920 172.628 1.00118.67 C
ANISOU 124 CG LYS A 28 13571 11166 20351 369 3181 -3414 C
ATOM 125 CD LYS A 28 32.370 62.098 171.446 1.00130.62 C
ANISOU 125 CD LYS A 28 15440 12581 21608 256 3397 -3820 C
ATOM 126 CE LYS A 28 31.400 62.857 170.565 1.00138.67 C
ANISOU 126 CE LYS A 28 16855 13900 21933 34 3285 -3899 C
ATOM 127 NZ LYS A 28 30.824 61.990 169.505 1.00149.87 N
ANISOU 127 NZ LYS A 28 18633 15212 23097 -96 3424 -4290 N
ATOM 128 N VAL A 29 31.101 65.741 174.935 1.00 89.76 N
ANISOU 128 N VAL A 29 9837 8173 16097 221 2087 -2529 N
ATOM 129 CA VAL A 29 30.921 67.170 174.645 1.00 87.51 C
ANISOU 129 CA VAL A 29 9651 8179 15419 119 2022 -2410 C
ATOM 130 C VAL A 29 30.699 68.048 175.897 1.00 87.35 C
ANISOU 130 C VAL A 29 9475 8285 15430 143 1684 -2077 C
ATOM 131 O VAL A 29 30.933 69.253 175.802 1.00 86.01 O
ANISOU 131 O VAL A 29 9298 8301 15081 99 1674 -1961 O
ATOM 132 CB VAL A 29 29.804 67.441 173.594 1.00 91.68 C
ANISOU 132 CB VAL A 29 10544 8874 15415 -64 1981 -2557 C
ATOM 133 CG1 VAL A 29 30.013 66.615 172.325 1.00 95.37 C
ANISOU 133 CG1 VAL A 29 11226 9231 15780 -113 2312 -2914 C
ATOM 134 CG2 VAL A 29 28.407 67.223 174.168 1.00 89.29 C
ANISOU 134 CG2 VAL A 29 10328 8597 15000 -131 1613 -2458 C
ATOM 135 N LEU A 30 30.239 67.489 177.035 1.00 81.95 N
ANISOU 135 N LEU A 30 8688 7499 14951 200 1424 -1929 N
ATOM 136 CA LEU A 30 30.014 68.302 178.236 1.00 78.74 C
ANISOU 136 CA LEU A 30 8176 7209 14531 212 1129 -1640 C
ATOM 137 C LEU A 30 31.339 68.810 178.854 1.00 82.06 C
ANISOU 137 C LEU A 30 8326 7610 15242 311 1154 -1489 C
ATOM 138 O LEU A 30 31.380 70.002 179.158 1.00 80.19 O
ANISOU 138 O LEU A 30 8078 7547 14844 267 1041 -1346 O
ATOM 139 CB LEU A 30 29.159 67.584 179.289 1.00 77.70 C
ANISOU 139 CB LEU A 30 8036 6984 14503 233 871 -1511 C
ATOM 140 CG LEU A 30 27.692 68.015 179.369 1.00 80.30 C
ANISOU 140 CG LEU A 30 8558 7462 14492 115 670 -1456 C
ATOM 141 CD1 LEU A 30 26.857 67.373 178.268 1.00 81.59 C
ANISOU 141 CD1 LEU A 30 8929 7590 14483 16 747 -1689 C
ATOM 142 CD2 LEU A 30 27.108 67.665 180.713 1.00 81.79 C
ANISOU 142 CD2 LEU A 30 8681 7593 14803 149 432 -1246 C
ATOM 143 N PRO A 31 32.439 68.013 178.994 1.00 80.33 N
ANISOU 143 N PRO A 31 7879 7179 15463 436 1299 -1517 N
ATOM 144 CA PRO A 31 33.680 68.576 179.567 1.00 80.36 C
ANISOU 144 CA PRO A 31 7601 7169 15761 512 1282 -1354 C
ATOM 145 C PRO A 31 34.211 69.841 178.852 1.00 83.29 C
ANISOU 145 C PRO A 31 7975 7717 15953 444 1447 -1376 C
ATOM 146 O PRO A 31 34.450 70.796 179.594 1.00 81.45 O
ANISOU 146 O PRO A 31 7645 7592 15712 425 1242 -1180 O
ATOM 147 CB PRO A 31 34.673 67.414 179.482 1.00 85.25 C
ANISOU 147 CB PRO A 31 7988 7509 16894 651 1478 -1433 C
ATOM 148 CG PRO A 31 33.823 66.205 179.504 1.00 90.03 C
ANISOU 148 CG PRO A 31 8729 7964 17513 663 1443 -1531 C
ATOM 149 CD PRO A 31 32.608 66.570 178.712 1.00 84.18 C
ANISOU 149 CD PRO A 31 8328 7404 16251 515 1461 -1683 C
ATOM 150 N PRO A 32 34.358 69.958 177.491 1.00 80.62 N
ANISOU 150 N PRO A 32 7769 7420 15441 391 1793 -1593 N
ATOM 151 CA PRO A 32 34.840 71.235 176.920 1.00 80.02 C
ANISOU 151 CA PRO A 32 7694 7515 15195 316 1928 -1558 C
ATOM 152 C PRO A 32 33.862 72.394 177.134 1.00 79.47 C
ANISOU 152 C PRO A 32 7816 7677 14704 196 1669 -1426 C
ATOM 153 O PRO A 32 34.306 73.531 177.276 1.00 78.45 O
ANISOU 153 O PRO A 32 7601 7653 14553 159 1635 -1294 O
ATOM 154 CB PRO A 32 34.999 70.931 175.426 1.00 84.51 C
ANISOU 154 CB PRO A 32 8436 8076 15597 272 2348 -1823 C
ATOM 155 CG PRO A 32 35.011 69.453 175.321 1.00 91.00 C
ANISOU 155 CG PRO A 32 9247 8667 16663 360 2473 -2008 C
ATOM 156 CD PRO A 32 34.132 68.969 176.417 1.00 84.18 C
ANISOU 156 CD PRO A 32 8390 7762 15832 383 2081 -1877 C
ATOM 157 N VAL A 33 32.540 72.101 177.169 1.00 73.26 N
ANISOU 157 N VAL A 33 7265 6945 13626 138 1491 -1458 N
ATOM 158 CA VAL A 33 31.472 73.080 177.402 1.00 70.16 C
ANISOU 158 CA VAL A 33 7038 6738 12881 38 1247 -1335 C
ATOM 159 C VAL A 33 31.628 73.643 178.832 1.00 72.36 C
ANISOU 159 C VAL A 33 7147 7026 13321 83 965 -1108 C
ATOM 160 O VAL A 33 31.545 74.860 179.014 1.00 70.43 O
ANISOU 160 O VAL A 33 6918 6911 12932 24 869 -992 O
ATOM 161 CB VAL A 33 30.063 72.469 177.133 1.00 73.10 C
ANISOU 161 CB VAL A 33 7650 7128 12997 -25 1130 -1423 C
ATOM 162 CG1 VAL A 33 28.944 73.289 177.776 1.00 70.12 C
ANISOU 162 CG1 VAL A 33 7357 6883 12403 -87 840 -1255 C
ATOM 163 CG2 VAL A 33 29.812 72.317 175.635 1.00 74.75 C
ANISOU 163 CG2 VAL A 33 8093 7391 12918 -121 1353 -1631 C
ATOM 164 N LEU A 34 31.909 72.765 179.822 1.00 69.26 N
ANISOU 164 N LEU A 34 6602 6484 13229 180 839 -1046 N
ATOM 165 CA LEU A 34 32.130 73.157 181.219 1.00 67.90 C
ANISOU 165 CA LEU A 34 6298 6310 13190 213 562 -838 C
ATOM 166 C LEU A 34 33.426 73.956 181.355 1.00 73.04 C
ANISOU 166 C LEU A 34 6729 6965 14057 228 595 -759 C
ATOM 167 O LEU A 34 33.485 74.893 182.152 1.00 71.63 O
ANISOU 167 O LEU A 34 6522 6865 13829 190 387 -619 O
ATOM 168 CB LEU A 34 32.165 71.934 182.154 1.00 68.54 C
ANISOU 168 CB LEU A 34 6286 6223 13535 306 421 -772 C
ATOM 169 CG LEU A 34 30.879 71.116 182.307 1.00 72.22 C
ANISOU 169 CG LEU A 34 6933 6658 13848 288 342 -803 C
ATOM 170 CD1 LEU A 34 31.157 69.830 183.036 1.00 73.59 C
ANISOU 170 CD1 LEU A 34 6985 6628 14347 386 266 -738 C
ATOM 171 CD2 LEU A 34 29.792 71.898 183.031 1.00 73.03 C
ANISOU 171 CD2 LEU A 34 7188 6908 13654 215 127 -680 C
ATOM 172 N GLY A 35 34.436 73.579 180.568 1.00 72.02 N
ANISOU 172 N GLY A 35 6446 6740 14177 276 870 -861 N
ATOM 173 CA GLY A 35 35.731 74.248 180.521 1.00 73.39 C
ANISOU 173 CA GLY A 35 6371 6893 14620 287 958 -797 C
ATOM 174 C GLY A 35 35.610 75.652 179.977 1.00 76.31 C
ANISOU 174 C GLY A 35 6844 7436 14717 173 1019 -778 C
ATOM 175 O GLY A 35 36.157 76.590 180.561 1.00 75.91 O
ANISOU 175 O GLY A 35 6657 7417 14770 141 872 -644 O
ATOM 176 N LEU A 36 34.842 75.801 178.878 1.00 72.34 N
ANISOU 176 N LEU A 36 6593 7036 13856 102 1205 -903 N
ATOM 177 CA LEU A 36 34.548 77.076 178.224 1.00 71.34 C
ANISOU 177 CA LEU A 36 6607 7071 13429 -13 1263 -870 C
ATOM 178 C LEU A 36 33.786 77.992 179.180 1.00 71.86 C
ANISOU 178 C LEU A 36 6747 7228 13330 -62 929 -723 C
ATOM 179 O LEU A 36 34.108 79.175 179.277 1.00 71.30 O
ANISOU 179 O LEU A 36 6625 7214 13251 -122 888 -624 O
ATOM 180 CB LEU A 36 33.736 76.831 176.941 1.00 71.90 C
ANISOU 180 CB LEU A 36 6963 7225 13131 -80 1461 -1020 C
ATOM 181 CG LEU A 36 34.289 77.434 175.648 1.00 79.00 C
ANISOU 181 CG LEU A 36 7923 8195 13900 -155 1795 -1073 C
ATOM 182 CD1 LEU A 36 35.588 76.754 175.216 1.00 82.20 C
ANISOU 182 CD1 LEU A 36 8123 8463 14648 -79 2140 -1182 C
ATOM 183 CD2 LEU A 36 33.274 77.318 174.532 1.00 82.36 C
ANISOU 183 CD2 LEU A 36 8688 8733 13874 -251 1878 -1186 C
ATOM 184 N GLU A 37 32.824 77.422 179.935 1.00 66.15 N
ANISOU 184 N GLU A 37 6129 6494 12510 -34 707 -710 N
ATOM 185 CA GLU A 37 32.025 78.132 180.936 1.00 63.39 C
ANISOU 185 CA GLU A 37 5862 6208 12013 -68 425 -592 C
ATOM 186 C GLU A 37 32.889 78.590 182.107 1.00 67.30 C
ANISOU 186 C GLU A 37 6170 6654 12746 -48 235 -472 C
ATOM 187 O GLU A 37 32.579 79.607 182.717 1.00 65.75 O
ANISOU 187 O GLU A 37 6029 6518 12436 -103 71 -393 O
ATOM 188 CB GLU A 37 30.879 77.252 181.440 1.00 63.37 C
ANISOU 188 CB GLU A 37 5996 6187 11894 -40 289 -608 C
ATOM 189 CG GLU A 37 29.690 77.222 180.495 1.00 71.06 C
ANISOU 189 CG GLU A 37 7187 7242 12572 -102 360 -687 C
ATOM 190 CD GLU A 37 28.721 76.067 180.664 1.00 88.05 C
ANISOU 190 CD GLU A 37 9436 9339 14681 -79 296 -741 C
ATOM 191 OE1 GLU A 37 27.889 75.867 179.752 1.00 82.03 O
ANISOU 191 OE1 GLU A 37 8829 8621 13718 -138 353 -828 O
ATOM 192 OE2 GLU A 37 28.797 75.354 181.690 1.00 83.08 O
ANISOU 192 OE2 GLU A 37 8729 8616 14221 -13 177 -687 O
ATOM 193 N PHE A 38 33.970 77.846 182.411 1.00 65.64 N
ANISOU 193 N PHE A 38 5739 6324 12879 26 247 -460 N
ATOM 194 CA PHE A 38 34.912 78.174 183.481 1.00 65.95 C
ANISOU 194 CA PHE A 38 5576 6304 13179 37 30 -337 C
ATOM 195 C PHE A 38 35.843 79.305 183.041 1.00 71.15 C
ANISOU 195 C PHE A 38 6085 6982 13968 -27 124 -310 C
ATOM 196 O PHE A 38 36.085 80.217 183.830 1.00 70.42 O
ANISOU 196 O PHE A 38 5955 6907 13896 -87 -94 -222 O
ATOM 197 CB PHE A 38 35.720 76.932 183.918 1.00 69.25 C
ANISOU 197 CB PHE A 38 5782 6565 13966 142 -11 -305 C
ATOM 198 CG PHE A 38 36.874 77.231 184.847 1.00 72.11 C
ANISOU 198 CG PHE A 38 5891 6855 14654 146 -242 -166 C
ATOM 199 CD1 PHE A 38 36.660 77.441 186.205 1.00 74.47 C
ANISOU 199 CD1 PHE A 38 6256 7172 14867 114 -607 -42 C
ATOM 200 CD2 PHE A 38 38.177 77.312 184.364 1.00 76.24 C
ANISOU 200 CD2 PHE A 38 6112 7287 15570 169 -96 -158 C
ATOM 201 CE1 PHE A 38 37.729 77.732 187.061 1.00 77.01 C
ANISOU 201 CE1 PHE A 38 6361 7429 15468 95 -869 87 C
ATOM 202 CE2 PHE A 38 39.242 77.605 185.220 1.00 80.53 C
ANISOU 202 CE2 PHE A 38 6395 7754 16448 159 -350 -17 C
ATOM 203 CZ PHE A 38 39.011 77.808 186.564 1.00 78.04 C
ANISOU 203 CZ PHE A 38 6165 7465 16022 117 -758 104 C
ATOM 204 N ILE A 39 36.381 79.231 181.800 1.00 69.43 N
ANISOU 204 N ILE A 39 5788 6751 13842 -23 458 -390 N
ATOM 205 CA ILE A 39 37.306 80.223 181.237 1.00 70.73 C
ANISOU 205 CA ILE A 39 5795 6922 14157 -87 614 -356 C
ATOM 206 C ILE A 39 36.593 81.588 181.127 1.00 73.25 C
ANISOU 206 C ILE A 39 6306 7364 14163 -199 545 -312 C
ATOM 207 O ILE A 39 37.078 82.557 181.707 1.00 73.50 O
ANISOU 207 O ILE A 39 6230 7379 14317 -261 387 -224 O
ATOM 208 CB ILE A 39 37.920 79.747 179.881 1.00 76.06 C
ANISOU 208 CB ILE A 39 6393 7561 14946 -59 1046 -461 C
ATOM 209 CG1 ILE A 39 38.825 78.507 180.090 1.00 78.73 C
ANISOU 209 CG1 ILE A 39 6468 7729 15716 65 1121 -493 C
ATOM 210 CG2 ILE A 39 38.709 80.872 179.187 1.00 78.24 C
ANISOU 210 CG2 ILE A 39 6550 7863 15314 -145 1253 -410 C
ATOM 211 CD1 ILE A 39 38.940 77.551 178.874 1.00 87.30 C
ANISOU 211 CD1 ILE A 39 7595 8761 16813 123 1542 -670 C
ATOM 212 N PHE A 40 35.433 81.649 180.436 1.00 68.06 N
ANISOU 212 N PHE A 40 5922 6808 13128 -229 635 -370 N
ATOM 213 CA PHE A 40 34.672 82.891 180.272 1.00 66.37 C
ANISOU 213 CA PHE A 40 5881 6688 12648 -322 573 -314 C
ATOM 214 C PHE A 40 33.946 83.302 181.566 1.00 68.05 C
ANISOU 214 C PHE A 40 6180 6905 12772 -328 246 -263 C
ATOM 215 O PHE A 40 33.645 84.485 181.739 1.00 67.23 O
ANISOU 215 O PHE A 40 6138 6826 12579 -398 164 -206 O
ATOM 216 CB PHE A 40 33.683 82.786 179.101 1.00 67.80 C
ANISOU 216 CB PHE A 40 6308 6969 12485 -354 744 -370 C
ATOM 217 CG PHE A 40 34.346 82.596 177.756 1.00 72.02 C
ANISOU 217 CG PHE A 40 6826 7518 13020 -378 1094 -426 C
ATOM 218 CD1 PHE A 40 35.116 83.608 177.190 1.00 76.80 C
ANISOU 218 CD1 PHE A 40 7342 8134 13705 -452 1259 -345 C
ATOM 219 CD2 PHE A 40 34.197 81.408 177.051 1.00 75.56 C
ANISOU 219 CD2 PHE A 40 7362 7962 13386 -334 1278 -566 C
ATOM 220 CE1 PHE A 40 35.744 83.425 175.954 1.00 80.23 C
ANISOU 220 CE1 PHE A 40 7778 8585 14120 -480 1626 -393 C
ATOM 221 CE2 PHE A 40 34.823 81.225 175.813 1.00 80.97 C
ANISOU 221 CE2 PHE A 40 8065 8659 14042 -362 1639 -642 C
ATOM 222 CZ PHE A 40 35.590 82.236 175.272 1.00 80.51 C
ANISOU 222 CZ PHE A 40 7923 8624 14043 -434 1823 -551 C
ATOM 223 N GLY A 41 33.697 82.340 182.456 1.00 63.43 N
ANISOU 223 N GLY A 41 5600 6281 12219 -257 84 -282 N
ATOM 224 CA GLY A 41 33.057 82.574 183.748 1.00 61.50 C
ANISOU 224 CA GLY A 41 5456 6038 11873 -262 -192 -241 C
ATOM 225 C GLY A 41 33.970 83.286 184.724 1.00 65.59 C
ANISOU 225 C GLY A 41 5837 6500 12582 -305 -396 -178 C
ATOM 226 O GLY A 41 33.552 84.251 185.364 1.00 64.20 O
ANISOU 226 O GLY A 41 5769 6339 12283 -366 -539 -161 O
ATOM 227 N LEU A 42 35.234 82.823 184.825 1.00 63.61 N
ANISOU 227 N LEU A 42 5339 6171 12657 -278 -410 -148 N
ATOM 228 CA LEU A 42 36.274 83.396 185.684 1.00 64.65 C
ANISOU 228 CA LEU A 42 5294 6236 13034 -330 -635 -79 C
ATOM 229 C LEU A 42 36.732 84.749 185.129 1.00 69.41 C
ANISOU 229 C LEU A 42 5825 6838 13711 -429 -541 -67 C
ATOM 230 O LEU A 42 36.992 85.663 185.910 1.00 68.88 O
ANISOU 230 O LEU A 42 5750 6739 13682 -513 -759 -40 O
ATOM 231 CB LEU A 42 37.465 82.413 185.804 1.00 66.75 C
ANISOU 231 CB LEU A 42 5273 6401 13690 -261 -661 -32 C
ATOM 232 CG LEU A 42 38.714 82.839 186.596 1.00 73.51 C
ANISOU 232 CG LEU A 42 5875 7168 14888 -315 -917 60 C
ATOM 233 CD1 LEU A 42 38.444 82.901 188.094 1.00 73.73 C
ANISOU 233 CD1 LEU A 42 6043 7202 14770 -356 -1324 111 C
ATOM 234 CD2 LEU A 42 39.863 81.891 186.332 1.00 77.75 C
ANISOU 234 CD2 LEU A 42 6077 7589 15875 -231 -845 111 C
ATOM 235 N LEU A 43 36.814 84.873 183.787 1.00 67.32 N
ANISOU 235 N LEU A 43 5527 6601 13450 -430 -217 -87 N
ATOM 236 CA LEU A 43 37.236 86.092 183.090 1.00 68.57 C
ANISOU 236 CA LEU A 43 5619 6754 13679 -525 -76 -48 C
ATOM 237 C LEU A 43 36.242 87.243 183.301 1.00 69.19 C
ANISOU 237 C LEU A 43 5928 6874 13488 -597 -173 -42 C
ATOM 238 O LEU A 43 36.651 88.333 183.693 1.00 69.08 O
ANISOU 238 O LEU A 43 5852 6800 13594 -687 -288 -6 O
ATOM 239 CB LEU A 43 37.421 85.819 181.585 1.00 70.07 C
ANISOU 239 CB LEU A 43 5784 6982 13857 -510 314 -66 C
ATOM 240 CG LEU A 43 38.846 85.973 181.039 1.00 78.73 C
ANISOU 240 CG LEU A 43 6575 8000 15341 -535 517 -20 C
ATOM 241 CD1 LEU A 43 39.663 84.691 181.229 1.00 80.54 C
ANISOU 241 CD1 LEU A 43 6574 8147 15881 -430 556 -52 C
ATOM 242 CD2 LEU A 43 38.821 86.350 179.568 1.00 83.14 C
ANISOU 242 CD2 LEU A 43 7206 8618 15766 -580 902 -13 C
ATOM 243 N GLY A 44 34.959 86.975 183.064 1.00 62.96 N
ANISOU 243 N GLY A 44 5381 6165 12377 -558 -132 -80 N
ATOM 244 CA GLY A 44 33.881 87.947 183.208 1.00 60.91 C
ANISOU 244 CA GLY A 44 5325 5929 11890 -602 -197 -71 C
ATOM 245 C GLY A 44 33.592 88.360 184.636 1.00 63.07 C
ANISOU 245 C GLY A 44 5675 6153 12133 -621 -471 -101 C
ATOM 246 O GLY A 44 33.412 89.550 184.908 1.00 63.22 O
ANISOU 246 O GLY A 44 5750 6124 12149 -692 -535 -94 O
ATOM 247 N ASN A 45 33.538 87.384 185.556 1.00 58.20 N
ANISOU 247 N ASN A 45 5083 5542 11489 -564 -626 -134 N
ATOM 248 CA ASN A 45 33.280 87.631 186.975 1.00 57.46 C
ANISOU 248 CA ASN A 45 5104 5416 11311 -589 -880 -166 C
ATOM 249 C ASN A 45 34.509 88.207 187.668 1.00 62.73 C
ANISOU 249 C ASN A 45 5621 6002 12213 -674 -1083 -154 C
ATOM 250 O ASN A 45 34.359 88.930 188.653 1.00 62.39 O
ANISOU 250 O ASN A 45 5699 5918 12090 -742 -1273 -200 O
ATOM 251 CB ASN A 45 32.792 86.372 187.676 1.00 55.70 C
ANISOU 251 CB ASN A 45 4975 5230 10960 -510 -970 -175 C
ATOM 252 CG ASN A 45 31.353 86.091 187.349 1.00 68.46 C
ANISOU 252 CG ASN A 45 6778 6905 12328 -457 -837 -199 C
ATOM 253 OD1 ASN A 45 30.439 86.699 187.913 1.00 63.30 O
ANISOU 253 OD1 ASN A 45 6296 6250 11504 -476 -872 -229 O
ATOM 254 ND2 ASN A 45 31.118 85.229 186.374 1.00 56.46 N
ANISOU 254 ND2 ASN A 45 5222 5427 10802 -398 -671 -194 N
ATOM 255 N GLY A 46 35.696 87.903 187.139 1.00 60.84 N
ANISOU 255 N GLY A 46 5118 5729 12270 -676 -1035 -101 N
ATOM 256 CA GLY A 46 36.960 88.442 187.627 1.00 63.09 C
ANISOU 256 CA GLY A 46 5193 5923 12855 -765 -1224 -68 C
ATOM 257 C GLY A 46 37.062 89.910 187.270 1.00 68.20 C
ANISOU 257 C GLY A 46 5835 6513 13565 -874 -1166 -75 C
ATOM 258 O GLY A 46 37.516 90.717 188.086 1.00 69.48 O
ANISOU 258 O GLY A 46 5983 6594 13822 -980 -1400 -101 O
ATOM 259 N LEU A 47 36.601 90.264 186.045 1.00 64.21 N
ANISOU 259 N LEU A 47 5359 6044 12994 -858 -867 -50 N
ATOM 260 CA LEU A 47 36.545 91.640 185.548 1.00 64.75 C
ANISOU 260 CA LEU A 47 5440 6052 13109 -951 -775 -24 C
ATOM 261 C LEU A 47 35.487 92.416 186.318 1.00 67.28 C
ANISOU 261 C LEU A 47 6018 6344 13201 -977 -906 -100 C
ATOM 262 O LEU A 47 35.740 93.554 186.708 1.00 68.39 O
ANISOU 262 O LEU A 47 6157 6374 13455 -1079 -1009 -124 O
ATOM 263 CB LEU A 47 36.253 91.689 184.037 1.00 64.56 C
ANISOU 263 CB LEU A 47 5415 6089 13024 -925 -437 50 C
ATOM 264 CG LEU A 47 37.464 91.590 183.106 1.00 71.69 C
ANISOU 264 CG LEU A 47 6053 6971 14213 -955 -226 130 C
ATOM 265 CD1 LEU A 47 37.051 91.097 181.733 1.00 71.55 C
ANISOU 265 CD1 LEU A 47 6112 7058 14017 -903 101 166 C
ATOM 266 CD2 LEU A 47 38.188 92.928 182.985 1.00 75.95 C
ANISOU 266 CD2 LEU A 47 6453 7392 15012 -1087 -226 201 C
ATOM 267 N ALA A 48 34.320 91.784 186.573 1.00 61.42 N
ANISOU 267 N ALA A 48 5487 5683 12167 -887 -893 -146 N
ATOM 268 CA ALA A 48 33.216 92.364 187.340 1.00 60.11 C
ANISOU 268 CA ALA A 48 5563 5488 11788 -890 -969 -226 C
ATOM 269 C ALA A 48 33.673 92.685 188.763 1.00 64.81 C
ANISOU 269 C ALA A 48 6217 6007 12399 -966 -1246 -322 C
ATOM 270 O ALA A 48 33.419 93.790 189.235 1.00 65.32 O
ANISOU 270 O ALA A 48 6392 5971 12455 -1039 -1301 -397 O
ATOM 271 CB ALA A 48 32.030 91.412 187.364 1.00 58.84 C
ANISOU 271 CB ALA A 48 5563 5427 11365 -780 -896 -241 C
ATOM 272 N LEU A 49 34.410 91.750 189.408 1.00 61.55 N
ANISOU 272 N LEU A 49 5728 5631 12029 -960 -1430 -314 N
ATOM 273 CA LEU A 49 34.971 91.902 190.753 1.00 63.35 C
ANISOU 273 CA LEU A 49 6014 5805 12250 -1048 -1748 -381 C
ATOM 274 C LEU A 49 35.952 93.084 190.795 1.00 68.85 C
ANISOU 274 C LEU A 49 6570 6371 13218 -1191 -1870 -401 C
ATOM 275 O LEU A 49 35.937 93.850 191.758 1.00 69.93 O
ANISOU 275 O LEU A 49 6863 6428 13281 -1294 -2066 -514 O
ATOM 276 CB LEU A 49 35.671 90.596 191.182 1.00 64.41 C
ANISOU 276 CB LEU A 49 6032 5998 12444 -1005 -1920 -310 C
ATOM 277 CG LEU A 49 36.238 90.511 192.604 1.00 71.91 C
ANISOU 277 CG LEU A 49 7061 6919 13344 -1096 -2301 -340 C
ATOM 278 CD1 LEU A 49 35.133 90.364 193.637 1.00 71.83 C
ANISOU 278 CD1 LEU A 49 7415 6957 12921 -1084 -2354 -428 C
ATOM 279 CD2 LEU A 49 37.165 89.328 192.732 1.00 76.14 C
ANISOU 279 CD2 LEU A 49 7376 7477 14079 -1052 -2464 -215 C
ATOM 280 N TRP A 50 36.769 93.247 189.737 1.00 65.09 N
ANISOU 280 N TRP A 50 5812 5867 13053 -1205 -1734 -299 N
ATOM 281 CA TRP A 50 37.733 94.338 189.623 1.00 66.65 C
ANISOU 281 CA TRP A 50 5828 5928 13567 -1344 -1811 -289 C
ATOM 282 C TRP A 50 37.023 95.689 189.450 1.00 70.09 C
ANISOU 282 C TRP A 50 6424 6264 13944 -1402 -1701 -354 C
ATOM 283 O TRP A 50 37.392 96.654 190.125 1.00 72.03 O
ANISOU 283 O TRP A 50 6701 6373 14295 -1534 -1891 -442 O
ATOM 284 CB TRP A 50 38.708 94.092 188.457 1.00 65.96 C
ANISOU 284 CB TRP A 50 5400 5840 13822 -1332 -1620 -147 C
ATOM 285 CG TRP A 50 39.694 95.206 188.271 1.00 69.36 C
ANISOU 285 CG TRP A 50 5615 6121 14617 -1480 -1667 -112 C
ATOM 286 CD1 TRP A 50 39.647 96.194 187.333 1.00 72.45 C
ANISOU 286 CD1 TRP A 50 5956 6441 15131 -1531 -1430 -51 C
ATOM 287 CD2 TRP A 50 40.811 95.509 189.117 1.00 72.10 C
ANISOU 287 CD2 TRP A 50 5788 6357 15252 -1614 -2001 -130 C
ATOM 288 NE1 TRP A 50 40.684 97.076 187.521 1.00 74.69 N
ANISOU 288 NE1 TRP A 50 6027 6567 15783 -1685 -1567 -31 N
ATOM 289 CE2 TRP A 50 41.416 96.680 188.610 1.00 77.79 C
ANISOU 289 CE2 TRP A 50 6334 6932 16290 -1743 -1929 -87 C
ATOM 290 CE3 TRP A 50 41.378 94.887 190.244 1.00 74.81 C
ANISOU 290 CE3 TRP A 50 6096 6703 15624 -1647 -2376 -159 C
ATOM 291 CZ2 TRP A 50 42.558 97.244 189.189 1.00 80.22 C
ANISOU 291 CZ2 TRP A 50 6422 7094 16965 -1906 -2217 -90 C
ATOM 292 CZ3 TRP A 50 42.500 95.455 190.826 1.00 79.48 C
ANISOU 292 CZ3 TRP A 50 6484 7161 16553 -1810 -2689 -157 C
ATOM 293 CH2 TRP A 50 43.078 96.618 190.300 1.00 81.83 C
ANISOU 293 CH2 TRP A 50 6596 7309 17184 -1940 -2609 -131 C
ATOM 294 N ILE A 51 36.022 95.755 188.546 1.00 63.74 N
ANISOU 294 N ILE A 51 5714 5512 12991 -1309 -1414 -308 N
ATOM 295 CA ILE A 51 35.276 96.980 188.253 1.00 63.04 C
ANISOU 295 CA ILE A 51 5750 5316 12885 -1341 -1291 -330 C
ATOM 296 C ILE A 51 34.438 97.394 189.482 1.00 68.79 C
ANISOU 296 C ILE A 51 6763 5981 13393 -1353 -1429 -509 C
ATOM 297 O ILE A 51 34.528 98.552 189.891 1.00 70.35 O
ANISOU 297 O ILE A 51 7016 6011 13702 -1456 -1501 -599 O
ATOM 298 CB ILE A 51 34.429 96.862 186.950 1.00 63.52 C
ANISOU 298 CB ILE A 51 5829 5457 12848 -1242 -989 -203 C
ATOM 299 CG1 ILE A 51 35.343 96.658 185.719 1.00 63.89 C
ANISOU 299 CG1 ILE A 51 5628 5546 13101 -1260 -816 -44 C
ATOM 300 CG2 ILE A 51 33.533 98.097 186.745 1.00 64.19 C
ANISOU 300 CG2 ILE A 51 6044 5415 12929 -1259 -894 -204 C
ATOM 301 CD1 ILE A 51 34.707 95.919 184.547 1.00 67.35 C
ANISOU 301 CD1 ILE A 51 6103 6132 13356 -1156 -569 58 C
ATOM 302 N PHE A 52 33.682 96.455 190.090 1.00 64.95 N
ANISOU 302 N PHE A 52 6455 5612 12610 -1259 -1454 -567 N
ATOM 303 CA PHE A 52 32.837 96.739 191.255 1.00 65.97 C
ANISOU 303 CA PHE A 52 6875 5696 12497 -1264 -1527 -737 C
ATOM 304 C PHE A 52 33.630 97.128 192.521 1.00 73.64 C
ANISOU 304 C PHE A 52 7934 6580 13468 -1408 -1834 -883 C
ATOM 305 O PHE A 52 33.341 98.172 193.108 1.00 75.25 O
ANISOU 305 O PHE A 52 8306 6636 13652 -1485 -1861 -1038 O
ATOM 306 CB PHE A 52 31.922 95.542 191.598 1.00 66.38 C
ANISOU 306 CB PHE A 52 7078 5898 12245 -1139 -1470 -736 C
ATOM 307 CG PHE A 52 30.727 95.283 190.706 1.00 66.06 C
ANISOU 307 CG PHE A 52 7056 5919 12126 -1010 -1203 -655 C
ATOM 308 CD1 PHE A 52 29.787 96.280 190.463 1.00 69.45 C
ANISOU 308 CD1 PHE A 52 7570 6238 12581 -991 -1044 -685 C
ATOM 309 CD2 PHE A 52 30.480 94.011 190.201 1.00 66.82 C
ANISOU 309 CD2 PHE A 52 7094 6167 12126 -910 -1131 -555 C
ATOM 310 CE1 PHE A 52 28.667 96.030 189.665 1.00 68.86 C
ANISOU 310 CE1 PHE A 52 7496 6214 12452 -881 -845 -590 C
ATOM 311 CE2 PHE A 52 29.357 93.759 189.406 1.00 68.19 C
ANISOU 311 CE2 PHE A 52 7293 6394 12224 -811 -927 -486 C
ATOM 312 CZ PHE A 52 28.454 94.767 189.150 1.00 66.44 C
ANISOU 312 CZ PHE A 52 7137 6072 12035 -800 -800 -495 C
ATOM 313 N CYS A 53 34.601 96.293 192.949 1.00 71.22 N
ANISOU 313 N CYS A 53 7521 6352 13188 -1446 -2073 -839 N
ATOM 314 CA CYS A 53 35.343 96.493 194.197 1.00 74.02 C
ANISOU 314 CA CYS A 53 7973 6649 13500 -1591 -2427 -956 C
ATOM 315 C CYS A 53 36.501 97.496 194.110 1.00 80.62 C
ANISOU 315 C CYS A 53 8613 7325 14692 -1757 -2604 -973 C
ATOM 316 O CYS A 53 36.712 98.220 195.087 1.00 82.62 O
ANISOU 316 O CYS A 53 9042 7467 14885 -1901 -2834 -1142 O
ATOM 317 CB CYS A 53 35.840 95.159 194.746 1.00 74.64 C
ANISOU 317 CB CYS A 53 8018 6866 13475 -1562 -2646 -870 C
ATOM 318 SG CYS A 53 34.523 94.015 195.231 1.00 76.55 S
ANISOU 318 SG CYS A 53 8545 7266 13275 -1413 -2509 -873 S
ATOM 319 N PHE A 54 37.281 97.511 193.008 1.00 76.98 N
ANISOU 319 N PHE A 54 7804 6850 14596 -1751 -2505 -809 N
ATOM 320 CA PHE A 54 38.470 98.369 192.951 1.00 79.59 C
ANISOU 320 CA PHE A 54 7904 7024 15311 -1918 -2680 -800 C
ATOM 321 C PHE A 54 38.362 99.569 191.998 1.00 85.44 C
ANISOU 321 C PHE A 54 8545 7616 16302 -1954 -2433 -768 C
ATOM 322 O PHE A 54 38.825 100.648 192.374 1.00 87.86 O
ANISOU 322 O PHE A 54 8845 7736 16801 -2113 -2584 -864 O
ATOM 323 CB PHE A 54 39.723 97.542 192.616 1.00 81.78 C
ANISOU 323 CB PHE A 54 7818 7358 15897 -1923 -2806 -630 C
ATOM 324 CG PHE A 54 39.978 96.437 193.617 1.00 83.40 C
ANISOU 324 CG PHE A 54 8092 7673 15924 -1907 -3113 -632 C
ATOM 325 CD1 PHE A 54 40.529 96.717 194.862 1.00 88.94 C
ANISOU 325 CD1 PHE A 54 8901 8308 16585 -2070 -3544 -737 C
ATOM 326 CD2 PHE A 54 39.621 95.123 193.333 1.00 83.05 C
ANISOU 326 CD2 PHE A 54 8031 7790 15734 -1739 -2983 -526 C
ATOM 327 CE1 PHE A 54 40.733 95.699 195.799 1.00 90.73 C
ANISOU 327 CE1 PHE A 54 9216 8639 16618 -2062 -3849 -706 C
ATOM 328 CE2 PHE A 54 39.828 94.106 194.269 1.00 86.40 C
ANISOU 328 CE2 PHE A 54 8525 8299 16005 -1723 -3269 -500 C
ATOM 329 CZ PHE A 54 40.383 94.401 195.495 1.00 87.54 C
ANISOU 329 CZ PHE A 54 8776 8386 16100 -1883 -3704 -576 C
ATOM 330 N HIS A 55 37.782 99.406 190.790 1.00 80.81 N
ANISOU 330 N HIS A 55 7889 7099 15714 -1824 -2079 -629 N
ATOM 331 CA HIS A 55 37.674 100.523 189.844 1.00 81.55 C
ANISOU 331 CA HIS A 55 7896 7056 16033 -1860 -1853 -554 C
ATOM 332 C HIS A 55 36.634 101.559 190.312 1.00 87.04 C
ANISOU 332 C HIS A 55 8874 7605 16592 -1875 -1812 -710 C
ATOM 333 O HIS A 55 36.985 102.732 190.450 1.00 88.70 O
ANISOU 333 O HIS A 55 9058 7602 17042 -2007 -1875 -771 O
ATOM 334 CB HIS A 55 37.366 100.034 188.419 1.00 80.29 C
ANISOU 334 CB HIS A 55 7613 7023 15872 -1734 -1515 -349 C
ATOM 335 CG HIS A 55 37.216 101.141 187.422 1.00 84.33 C
ANISOU 335 CG HIS A 55 8060 7407 16576 -1774 -1292 -231 C
ATOM 336 ND1 HIS A 55 35.968 101.548 186.979 1.00 84.69 N
ANISOU 336 ND1 HIS A 55 8291 7441 16446 -1687 -1104 -206 N
ATOM 337 CD2 HIS A 55 38.161 101.912 186.834 1.00 88.12 C
ANISOU 337 CD2 HIS A 55 8303 7755 17425 -1896 -1243 -116 C
ATOM 338 CE1 HIS A 55 36.194 102.537 186.129 1.00 85.25 C
ANISOU 338 CE1 HIS A 55 8247 7378 16764 -1757 -960 -65 C
ATOM 339 NE2 HIS A 55 37.498 102.791 186.009 1.00 87.69 N
ANISOU 339 NE2 HIS A 55 8308 7612 17397 -1885 -1023 -8 N
ATOM 340 N LEU A 56 35.376 101.131 190.562 1.00 82.96 N
ANISOU 340 N LEU A 56 8608 7182 15732 -1740 -1697 -776 N
ATOM 341 CA LEU A 56 34.295 102.016 191.010 1.00 83.67 C
ANISOU 341 CA LEU A 56 8952 7128 15712 -1725 -1611 -926 C
ATOM 342 C LEU A 56 34.397 102.290 192.509 1.00 92.07 C
ANISOU 342 C LEU A 56 10255 8102 16624 -1831 -1861 -1192 C
ATOM 343 O LEU A 56 34.438 101.353 193.312 1.00 91.55 O
ANISOU 343 O LEU A 56 10312 8183 16291 -1815 -2017 -1258 O
ATOM 344 CB LEU A 56 32.909 101.437 190.670 1.00 80.87 C
ANISOU 344 CB LEU A 56 8737 6897 15093 -1543 -1378 -880 C
ATOM 345 CG LEU A 56 32.568 101.263 189.189 1.00 83.59 C
ANISOU 345 CG LEU A 56 8917 7321 15521 -1447 -1137 -636 C
ATOM 346 CD1 LEU A 56 31.300 100.456 189.023 1.00 82.89 C
ANISOU 346 CD1 LEU A 56 8958 7379 15159 -1286 -990 -606 C
ATOM 347 CD2 LEU A 56 32.424 102.607 188.489 1.00 85.14 C
ANISOU 347 CD2 LEU A 56 9049 7311 15989 -1493 -1011 -553 C
ATOM 348 N LYS A 57 34.443 103.583 192.874 1.00 92.77 N
ANISOU 348 N LYS A 57 10427 7942 16882 -1949 -1898 -1343 N
ATOM 349 CA LYS A 57 34.556 104.051 194.258 1.00 95.92 C
ANISOU 349 CA LYS A 57 11091 8217 17138 -2081 -2125 -1632 C
ATOM 350 C LYS A 57 33.186 104.147 194.934 1.00100.41 C
ANISOU 350 C LYS A 57 12003 8759 17390 -1981 -1942 -1820 C
ATOM 351 O LYS A 57 33.081 103.896 196.137 1.00101.72 O
ANISOU 351 O LYS A 57 12450 8955 17243 -2037 -2090 -2031 O
ATOM 352 CB LYS A 57 35.262 105.414 194.304 1.00101.32 C
ANISOU 352 CB LYS A 57 11700 8614 18182 -2264 -2236 -1727 C
ATOM 353 N SER A 58 32.146 104.512 194.164 1.00 95.62 N
ANISOU 353 N SER A 58 11370 8091 16868 -1840 -1621 -1733 N
ATOM 354 CA SER A 58 30.785 104.667 194.670 1.00 95.32 C
ANISOU 354 CA SER A 58 11594 7998 16625 -1727 -1395 -1884 C
ATOM 355 C SER A 58 29.989 103.358 194.568 1.00 95.29 C
ANISOU 355 C SER A 58 11628 8257 16321 -1561 -1272 -1770 C
ATOM 356 O SER A 58 29.872 102.782 193.482 1.00 92.13 O
ANISOU 356 O SER A 58 11011 7994 16002 -1459 -1176 -1520 O
ATOM 357 CB SER A 58 30.063 105.791 193.928 1.00 99.70 C
ANISOU 357 CB SER A 58 12073 8317 17493 -1663 -1142 -1834 C
ATOM 358 OG SER A 58 29.979 105.534 192.535 1.00107.33 O
ANISOU 358 OG SER A 58 12766 9380 18635 -1568 -1022 -1514 O
ATOM 359 N TRP A 59 29.458 102.894 195.716 1.00 91.90 N
ANISOU 359 N TRP A 59 11492 7888 15535 -1548 -1275 -1959 N
ATOM 360 CA TRP A 59 28.622 101.695 195.826 1.00 89.08 C
ANISOU 360 CA TRP A 59 11210 7748 14889 -1406 -1150 -1881 C
ATOM 361 C TRP A 59 27.160 102.108 195.984 1.00 91.75 C
ANISOU 361 C TRP A 59 11691 7970 15198 -1282 -820 -1974 C
ATOM 362 O TRP A 59 26.820 102.804 196.941 1.00 93.80 O
ANISOU 362 O TRP A 59 12209 8066 15366 -1333 -749 -2234 O
ATOM 363 CB TRP A 59 29.060 100.813 197.013 1.00 88.85 C
ANISOU 363 CB TRP A 59 11402 7873 14483 -1482 -1374 -1988 C
ATOM 364 CG TRP A 59 30.085 99.773 196.680 1.00 88.56 C
ANISOU 364 CG TRP A 59 11165 8035 14450 -1506 -1623 -1794 C
ATOM 365 CD1 TRP A 59 31.419 99.820 196.956 1.00 93.20 C
ANISOU 365 CD1 TRP A 59 11669 8619 15124 -1658 -1957 -1799 C
ATOM 366 CD2 TRP A 59 29.849 98.505 196.050 1.00 85.50 C
ANISOU 366 CD2 TRP A 59 10627 7857 14003 -1374 -1556 -1576 C
ATOM 367 NE1 TRP A 59 32.034 98.669 196.524 1.00 91.13 N
ANISOU 367 NE1 TRP A 59 11197 8545 14885 -1615 -2082 -1589 N
ATOM 368 CE2 TRP A 59 31.094 97.845 195.960 1.00 89.62 C
ANISOU 368 CE2 TRP A 59 10974 8483 14594 -1442 -1834 -1460 C
ATOM 369 CE3 TRP A 59 28.705 97.863 195.547 1.00 84.34 C
ANISOU 369 CE3 TRP A 59 10463 7803 13778 -1209 -1294 -1470 C
ATOM 370 CZ2 TRP A 59 31.229 96.576 195.384 1.00 86.66 C
ANISOU 370 CZ2 TRP A 59 10425 8291 14210 -1342 -1829 -1261 C
ATOM 371 CZ3 TRP A 59 28.840 96.607 194.977 1.00 83.58 C
ANISOU 371 CZ3 TRP A 59 10210 7897 13651 -1127 -1315 -1277 C
ATOM 372 CH2 TRP A 59 30.089 95.977 194.899 1.00 84.43 C
ANISOU 372 CH2 TRP A 59 10161 8093 13824 -1189 -1567 -1183 C
ATOM 373 N LYS A 60 26.309 101.708 195.034 1.00 85.03 N
ANISOU 373 N LYS A 60 10670 7191 14448 -1125 -619 -1768 N
ATOM 374 CA LYS A 60 24.876 102.001 195.058 1.00 84.47 C
ANISOU 374 CA LYS A 60 10662 7014 14419 -990 -311 -1804 C
ATOM 375 C LYS A 60 24.096 100.734 195.445 1.00 85.48 C
ANISOU 375 C LYS A 60 10882 7347 14250 -890 -212 -1764 C
ATOM 376 O LYS A 60 24.660 99.639 195.397 1.00 83.33 O
ANISOU 376 O LYS A 60 10573 7296 13795 -908 -381 -1657 O
ATOM 377 CB LYS A 60 24.415 102.545 193.696 1.00 85.88 C
ANISOU 377 CB LYS A 60 10570 7100 14959 -900 -187 -1578 C
ATOM 378 N SER A 61 22.811 100.888 195.842 1.00 81.87 N
ANISOU 378 N SER A 61 10530 6798 13780 -786 73 -1848 N
ATOM 379 CA SER A 61 21.921 99.793 196.253 1.00 80.22 C
ANISOU 379 CA SER A 61 10403 6743 13333 -693 219 -1813 C
ATOM 380 C SER A 61 21.787 98.733 195.155 1.00 79.61 C
ANISOU 380 C SER A 61 10074 6868 13307 -610 158 -1525 C
ATOM 381 O SER A 61 21.884 97.539 195.445 1.00 78.04 O
ANISOU 381 O SER A 61 9926 6866 12861 -605 87 -1469 O
ATOM 382 CB SER A 61 20.544 100.331 196.632 1.00 85.52 C
ANISOU 382 CB SER A 61 11146 7233 14115 -586 575 -1921 C
ATOM 383 OG SER A 61 19.883 100.901 195.515 1.00 94.58 O
ANISOU 383 OG SER A 61 12019 8254 15662 -480 686 -1751 O
ATOM 384 N SER A 62 21.604 99.180 193.895 1.00 73.88 N
ANISOU 384 N SER A 62 9094 6084 12893 -556 175 -1344 N
ATOM 385 CA SER A 62 21.484 98.329 192.710 1.00 70.28 C
ANISOU 385 CA SER A 62 8417 5798 12490 -494 116 -1087 C
ATOM 386 C SER A 62 22.756 97.512 192.488 1.00 71.44 C
ANISOU 386 C SER A 62 8526 6134 12485 -575 -126 -1023 C
ATOM 387 O SER A 62 22.654 96.338 192.137 1.00 70.07 O
ANISOU 387 O SER A 62 8290 6140 12195 -531 -160 -904 O
ATOM 388 CB SER A 62 21.182 99.170 191.474 1.00 73.54 C
ANISOU 388 CB SER A 62 8617 6093 13233 -455 152 -917 C
ATOM 389 OG SER A 62 20.009 99.949 191.649 1.00 84.10 O
ANISOU 389 OG SER A 62 9948 7225 14780 -369 367 -955 O
ATOM 390 N ARG A 63 23.944 98.120 192.720 1.00 67.51 N
ANISOU 390 N ARG A 63 8053 5578 12021 -692 -289 -1107 N
ATOM 391 CA ARG A 63 25.248 97.467 192.568 1.00 66.10 C
ANISOU 391 CA ARG A 63 7803 5543 11772 -772 -518 -1050 C
ATOM 392 C ARG A 63 25.483 96.403 193.648 1.00 68.72 C
ANISOU 392 C ARG A 63 8300 6010 11799 -793 -628 -1129 C
ATOM 393 O ARG A 63 26.080 95.369 193.344 1.00 67.22 O
ANISOU 393 O ARG A 63 8012 5977 11553 -789 -752 -1015 O
ATOM 394 CB ARG A 63 26.393 98.490 192.573 1.00 68.40 C
ANISOU 394 CB ARG A 63 8050 5704 12237 -901 -665 -1112 C
ATOM 395 CG ARG A 63 26.851 98.869 191.170 1.00 79.97 C
ANISOU 395 CG ARG A 63 9263 7156 13965 -907 -656 -916 C
ATOM 396 CD ARG A 63 28.196 99.571 191.164 1.00 94.85 C
ANISOU 396 CD ARG A 63 11062 8951 16028 -1048 -823 -944 C
ATOM 397 NE ARG A 63 28.077 101.010 191.407 1.00108.19 N
ANISOU 397 NE ARG A 63 12806 10387 17914 -1109 -781 -1056 N
ATOM 398 CZ ARG A 63 27.961 101.929 190.453 1.00125.12 C
ANISOU 398 CZ ARG A 63 14812 12395 20332 -1107 -679 -927 C
ATOM 399 NH1 ARG A 63 27.862 103.214 190.769 1.00117.04 N
ANISOU 399 NH1 ARG A 63 13845 11114 19513 -1163 -645 -1041 N
ATOM 400 NH2 ARG A 63 27.942 101.571 189.174 1.00109.10 N
ANISOU 400 NH2 ARG A 63 12603 10478 18370 -1056 -611 -682 N
ATOM 401 N ILE A 64 25.003 96.645 194.891 1.00 65.61 N
ANISOU 401 N ILE A 64 8168 5549 11213 -816 -569 -1317 N
ATOM 402 CA ILE A 64 25.129 95.708 196.017 1.00 65.60 C
ANISOU 402 CA ILE A 64 8377 5669 10880 -847 -665 -1380 C
ATOM 403 C ILE A 64 24.326 94.431 195.696 1.00 67.84 C
ANISOU 403 C ILE A 64 8598 6102 11076 -729 -547 -1225 C
ATOM 404 O ILE A 64 24.862 93.332 195.859 1.00 67.03 O
ANISOU 404 O ILE A 64 8483 6143 10841 -739 -703 -1136 O
ATOM 405 CB ILE A 64 24.722 96.367 197.372 1.00 71.11 C
ANISOU 405 CB ILE A 64 9408 6251 11359 -909 -583 -1628 C
ATOM 406 CG1 ILE A 64 25.750 97.447 197.776 1.00 73.60 C
ANISOU 406 CG1 ILE A 64 9801 6431 11734 -1062 -785 -1794 C
ATOM 407 CG2 ILE A 64 24.567 95.329 198.501 1.00 72.29 C
ANISOU 407 CG2 ILE A 64 9808 6539 11119 -929 -622 -1655 C
ATOM 408 CD1 ILE A 64 25.211 98.560 198.623 1.00 81.26 C
ANISOU 408 CD1 ILE A 64 11034 7200 12641 -1108 -621 -2062 C
ATOM 409 N PHE A 65 23.075 94.583 195.195 1.00 63.72 N
ANISOU 409 N PHE A 65 8011 5529 10671 -620 -289 -1181 N
ATOM 410 CA PHE A 65 22.203 93.469 194.802 1.00 61.77 C
ANISOU 410 CA PHE A 65 7681 5394 10394 -517 -174 -1038 C
ATOM 411 C PHE A 65 22.791 92.705 193.622 1.00 64.23 C
ANISOU 411 C PHE A 65 7760 5829 10815 -498 -311 -858 C
ATOM 412 O PHE A 65 22.714 91.476 193.587 1.00 63.44 O
ANISOU 412 O PHE A 65 7637 5854 10614 -464 -344 -768 O
ATOM 413 CB PHE A 65 20.785 93.959 194.439 1.00 63.47 C
ANISOU 413 CB PHE A 65 7832 5499 10784 -418 97 -1021 C
ATOM 414 CG PHE A 65 19.953 94.568 195.545 1.00 67.28 C
ANISOU 414 CG PHE A 65 8525 5847 11192 -405 328 -1197 C
ATOM 415 CD1 PHE A 65 19.890 93.974 196.802 1.00 71.87 C
ANISOU 415 CD1 PHE A 65 9364 6490 11455 -442 370 -1297 C
ATOM 416 CD2 PHE A 65 19.168 95.690 195.306 1.00 70.70 C
ANISOU 416 CD2 PHE A 65 8896 6085 11880 -350 528 -1249 C
ATOM 417 CE1 PHE A 65 19.103 94.527 197.816 1.00 75.59 C
ANISOU 417 CE1 PHE A 65 10054 6836 11829 -434 633 -1475 C
ATOM 418 CE2 PHE A 65 18.381 96.243 196.322 1.00 76.22 C
ANISOU 418 CE2 PHE A 65 9785 6639 12537 -329 792 -1432 C
ATOM 419 CZ PHE A 65 18.352 95.658 197.570 1.00 75.90 C
ANISOU 419 CZ PHE A 65 10023 6671 12145 -373 859 -1555 C
ATOM 420 N LEU A 66 23.388 93.435 192.666 1.00 60.50 N
ANISOU 420 N LEU A 66 7127 5309 10550 -525 -374 -810 N
ATOM 421 CA LEU A 66 23.996 92.875 191.461 1.00 58.96 C
ANISOU 421 CA LEU A 66 6728 5216 10457 -517 -458 -659 C
ATOM 422 C LEU A 66 25.321 92.139 191.768 1.00 63.04 C
ANISOU 422 C LEU A 66 7225 5826 10902 -577 -663 -656 C
ATOM 423 O LEU A 66 25.630 91.150 191.094 1.00 61.10 O
ANISOU 423 O LEU A 66 6856 5686 10672 -544 -694 -551 O
ATOM 424 CB LEU A 66 24.221 94.001 190.437 1.00 59.02 C
ANISOU 424 CB LEU A 66 6600 5131 10695 -542 -433 -601 C
ATOM 425 CG LEU A 66 24.584 93.616 189.008 1.00 62.35 C
ANISOU 425 CG LEU A 66 6837 5645 11210 -532 -446 -438 C
ATOM 426 CD1 LEU A 66 23.461 92.850 188.319 1.00 61.39 C
ANISOU 426 CD1 LEU A 66 6677 5601 11046 -448 -352 -335 C
ATOM 427 CD2 LEU A 66 24.896 94.836 188.217 1.00 65.49 C
ANISOU 427 CD2 LEU A 66 7142 5936 11805 -577 -424 -376 C
ATOM 428 N PHE A 67 26.086 92.609 192.783 1.00 60.84 N
ANISOU 428 N PHE A 67 7064 5494 10559 -668 -808 -772 N
ATOM 429 CA PHE A 67 27.360 92.000 193.180 1.00 60.87 C
ANISOU 429 CA PHE A 67 7030 5563 10536 -732 -1044 -755 C
ATOM 430 C PHE A 67 27.164 90.593 193.764 1.00 63.18 C
ANISOU 430 C PHE A 67 7399 5970 10636 -685 -1093 -701 C
ATOM 431 O PHE A 67 28.071 89.766 193.654 1.00 62.55 O
ANISOU 431 O PHE A 67 7202 5956 10610 -691 -1248 -618 O
ATOM 432 CB PHE A 67 28.123 92.889 194.179 1.00 65.09 C
ANISOU 432 CB PHE A 67 7691 6003 11036 -859 -1226 -895 C
ATOM 433 CG PHE A 67 29.481 92.355 194.574 1.00 67.69 C
ANISOU 433 CG PHE A 67 7945 6383 11392 -937 -1517 -855 C
ATOM 434 CD1 PHE A 67 30.551 92.404 193.688 1.00 70.63 C
ANISOU 434 CD1 PHE A 67 8042 6751 12045 -962 -1595 -761 C
ATOM 435 CD2 PHE A 67 29.684 91.784 195.825 1.00 71.37 C
ANISOU 435 CD2 PHE A 67 8606 6896 11615 -987 -1708 -893 C
ATOM 436 CE1 PHE A 67 31.801 91.894 194.049 1.00 73.03 C
ANISOU 436 CE1 PHE A 67 8229 7080 12438 -1025 -1862 -709 C
ATOM 437 CE2 PHE A 67 30.937 91.278 196.186 1.00 75.60 C
ANISOU 437 CE2 PHE A 67 9045 7466 12213 -1057 -2015 -826 C
ATOM 438 CZ PHE A 67 31.986 91.337 195.296 1.00 73.54 C
ANISOU 438 CZ PHE A 67 8471 7184 12285 -1071 -2090 -736 C
ATOM 439 N ASN A 68 25.984 90.313 194.360 1.00 58.88 N
ANISOU 439 N ASN A 68 7033 5435 9904 -635 -946 -734 N
ATOM 440 CA ASN A 68 25.669 88.994 194.923 1.00 58.05 C
ANISOU 440 CA ASN A 68 7010 5422 9623 -593 -963 -664 C
ATOM 441 C ASN A 68 25.748 87.909 193.852 1.00 59.09 C
ANISOU 441 C ASN A 68 6925 5628 9897 -516 -943 -523 C
ATOM 442 O ASN A 68 26.126 86.782 194.169 1.00 59.12 O
ANISOU 442 O ASN A 68 6922 5691 9851 -501 -1052 -445 O
ATOM 443 CB ASN A 68 24.303 88.988 195.584 1.00 58.17 C
ANISOU 443 CB ASN A 68 7219 5417 9465 -553 -746 -714 C
ATOM 444 CG ASN A 68 24.251 89.817 196.838 1.00 79.08 C
ANISOU 444 CG ASN A 68 10143 8000 11906 -633 -748 -874 C
ATOM 445 OD1 ASN A 68 24.763 89.431 197.896 1.00 75.14 O
ANISOU 445 OD1 ASN A 68 9834 7545 11172 -705 -914 -893 O
ATOM 446 ND2 ASN A 68 23.628 90.975 196.744 1.00 69.66 N
ANISOU 446 ND2 ASN A 68 8986 6689 10792 -627 -569 -993 N
ATOM 447 N LEU A 69 25.448 88.270 192.582 1.00 53.38 N
ANISOU 447 N LEU A 69 6038 4892 9352 -476 -816 -492 N
ATOM 448 CA LEU A 69 25.543 87.384 191.423 1.00 51.54 C
ANISOU 448 CA LEU A 69 5626 4721 9237 -421 -780 -393 C
ATOM 449 C LEU A 69 27.005 86.996 191.164 1.00 56.73 C
ANISOU 449 C LEU A 69 6137 5400 10016 -450 -935 -357 C
ATOM 450 O LEU A 69 27.250 85.866 190.757 1.00 56.14 O
ANISOU 450 O LEU A 69 5968 5370 9991 -403 -941 -295 O
ATOM 451 CB LEU A 69 24.922 88.022 190.164 1.00 50.31 C
ANISOU 451 CB LEU A 69 5370 4548 9196 -397 -633 -366 C
ATOM 452 CG LEU A 69 23.394 88.010 190.068 1.00 54.06 C
ANISOU 452 CG LEU A 69 5900 5007 9634 -343 -480 -350 C
ATOM 453 CD1 LEU A 69 22.897 89.138 189.199 1.00 53.98 C
ANISOU 453 CD1 LEU A 69 5824 4937 9747 -344 -395 -326 C
ATOM 454 CD2 LEU A 69 22.880 86.687 189.525 1.00 55.72 C
ANISOU 454 CD2 LEU A 69 6054 5287 9831 -292 -447 -279 C
ATOM 455 N VAL A 70 27.972 87.903 191.437 1.00 55.22 N
ANISOU 455 N VAL A 70 5916 5160 9905 -529 -1059 -400 N
ATOM 456 CA VAL A 70 29.407 87.619 191.278 1.00 56.32 C
ANISOU 456 CA VAL A 70 5880 5300 10218 -563 -1213 -358 C
ATOM 457 C VAL A 70 29.815 86.575 192.341 1.00 61.55 C
ANISOU 457 C VAL A 70 6599 5988 10799 -559 -1407 -318 C
ATOM 458 O VAL A 70 30.489 85.599 192.004 1.00 61.09 O
ANISOU 458 O VAL A 70 6380 5947 10885 -516 -1456 -238 O
ATOM 459 CB VAL A 70 30.291 88.900 191.329 1.00 61.69 C
ANISOU 459 CB VAL A 70 6497 5903 11039 -664 -1310 -406 C
ATOM 460 CG1 VAL A 70 31.779 88.565 191.211 1.00 62.86 C
ANISOU 460 CG1 VAL A 70 6423 6039 11420 -701 -1471 -347 C
ATOM 461 CG2 VAL A 70 29.884 89.893 190.245 1.00 60.70 C
ANISOU 461 CG2 VAL A 70 6316 5740 11008 -667 -1118 -407 C
ATOM 462 N VAL A 71 29.356 86.763 193.601 1.00 59.53 N
ANISOU 462 N VAL A 71 6582 5728 10308 -600 -1498 -367 N
ATOM 463 CA VAL A 71 29.603 85.860 194.734 1.00 60.93 C
ANISOU 463 CA VAL A 71 6875 5935 10339 -613 -1693 -307 C
ATOM 464 C VAL A 71 28.985 84.488 194.407 1.00 64.39 C
ANISOU 464 C VAL A 71 7279 6416 10770 -508 -1575 -207 C
ATOM 465 O VAL A 71 29.666 83.468 194.545 1.00 65.11 O
ANISOU 465 O VAL A 71 7268 6510 10962 -481 -1716 -102 O
ATOM 466 CB VAL A 71 29.072 86.449 196.075 1.00 66.30 C
ANISOU 466 CB VAL A 71 7876 6608 10706 -690 -1752 -398 C
ATOM 467 CG1 VAL A 71 29.187 85.447 197.224 1.00 67.64 C
ANISOU 467 CG1 VAL A 71 8209 6824 10668 -708 -1936 -304 C
ATOM 468 CG2 VAL A 71 29.792 87.748 196.430 1.00 67.75 C
ANISOU 468 CG2 VAL A 71 8099 6726 10917 -810 -1904 -516 C
ATOM 469 N ALA A 72 27.720 84.479 193.919 1.00 59.12 N
ANISOU 469 N ALA A 72 6670 5763 10030 -451 -1325 -237 N
ATOM 470 CA ALA A 72 26.986 83.273 193.514 1.00 57.42 C
ANISOU 470 CA ALA A 72 6421 5571 9825 -367 -1199 -163 C
ATOM 471 C ALA A 72 27.714 82.535 192.383 1.00 60.15 C
ANISOU 471 C ALA A 72 6523 5913 10420 -315 -1192 -117 C
ATOM 472 O ALA A 72 27.801 81.305 192.413 1.00 59.83 O
ANISOU 472 O ALA A 72 6433 5862 10438 -264 -1218 -40 O
ATOM 473 CB ALA A 72 25.574 83.640 193.072 1.00 56.67 C
ANISOU 473 CB ALA A 72 6390 5478 9665 -335 -961 -209 C
ATOM 474 N ASP A 73 28.269 83.294 191.415 1.00 55.80 N
ANISOU 474 N ASP A 73 5827 5354 10020 -332 -1142 -163 N
ATOM 475 CA ASP A 73 28.996 82.758 190.267 1.00 55.03 C
ANISOU 475 CA ASP A 73 5515 5250 10142 -293 -1079 -145 C
ATOM 476 C ASP A 73 30.329 82.128 190.650 1.00 59.69 C
ANISOU 476 C ASP A 73 5954 5801 10926 -287 -1254 -82 C
ATOM 477 O ASP A 73 30.675 81.092 190.085 1.00 59.67 O
ANISOU 477 O ASP A 73 5815 5771 11085 -221 -1197 -51 O
ATOM 478 CB ASP A 73 29.222 83.842 189.210 1.00 56.19 C
ANISOU 478 CB ASP A 73 5575 5403 10371 -329 -961 -192 C
ATOM 479 CG ASP A 73 27.998 84.155 188.372 1.00 61.65 C
ANISOU 479 CG ASP A 73 6343 6128 10954 -314 -779 -217 C
ATOM 480 OD1 ASP A 73 26.910 83.623 188.684 1.00 61.17 O
ANISOU 480 OD1 ASP A 73 6394 6080 10768 -280 -742 -211 O
ATOM 481 OD2 ASP A 73 28.119 84.960 187.430 1.00 65.78 O
ANISOU 481 OD2 ASP A 73 6808 6657 11528 -343 -684 -225 O
ATOM 482 N PHE A 74 31.063 82.725 191.609 1.00 56.99 N
ANISOU 482 N PHE A 74 5630 5438 10584 -357 -1477 -65 N
ATOM 483 CA PHE A 74 32.352 82.194 192.053 1.00 58.73 C
ANISOU 483 CA PHE A 74 5683 5610 11023 -360 -1698 21 C
ATOM 484 C PHE A 74 32.189 80.842 192.753 1.00 64.90 C
ANISOU 484 C PHE A 74 6513 6375 11771 -301 -1806 129 C
ATOM 485 O PHE A 74 33.098 80.019 192.665 1.00 66.24 O
ANISOU 485 O PHE A 74 6479 6482 12208 -254 -1900 217 O
ATOM 486 CB PHE A 74 33.100 83.192 192.945 1.00 62.08 C
ANISOU 486 CB PHE A 74 6136 6016 11436 -473 -1956 13 C
ATOM 487 CG PHE A 74 34.117 84.009 192.180 1.00 63.99 C
ANISOU 487 CG PHE A 74 6138 6214 11961 -518 -1935 -14 C
ATOM 488 CD1 PHE A 74 35.420 83.550 192.014 1.00 68.64 C
ANISOU 488 CD1 PHE A 74 6437 6740 12903 -506 -2054 71 C
ATOM 489 CD2 PHE A 74 33.767 85.226 191.606 1.00 64.82 C
ANISOU 489 CD2 PHE A 74 6288 6325 12016 -569 -1780 -108 C
ATOM 490 CE1 PHE A 74 36.355 84.295 191.290 1.00 70.19 C
ANISOU 490 CE1 PHE A 74 6393 6889 13388 -551 -1997 56 C
ATOM 491 CE2 PHE A 74 34.703 85.972 190.883 1.00 68.36 C
ANISOU 491 CE2 PHE A 74 6514 6725 12734 -619 -1739 -111 C
ATOM 492 CZ PHE A 74 35.991 85.502 190.731 1.00 68.18 C
ANISOU 492 CZ PHE A 74 6206 6649 13052 -613 -1837 -32 C
ATOM 493 N LEU A 75 31.019 80.586 193.383 1.00 61.44 N
ANISOU 493 N LEU A 75 6323 5977 11044 -298 -1765 134 N
ATOM 494 CA LEU A 75 30.712 79.300 194.022 1.00 62.17 C
ANISOU 494 CA LEU A 75 6483 6048 11090 -248 -1833 254 C
ATOM 495 C LEU A 75 30.777 78.176 192.980 1.00 65.93 C
ANISOU 495 C LEU A 75 6764 6465 11823 -145 -1673 271 C
ATOM 496 O LEU A 75 31.345 77.123 193.260 1.00 66.96 O
ANISOU 496 O LEU A 75 6786 6519 12135 -94 -1791 387 O
ATOM 497 CB LEU A 75 29.323 79.320 194.701 1.00 61.51 C
ANISOU 497 CB LEU A 75 6687 6014 10670 -267 -1733 244 C
ATOM 498 CG LEU A 75 29.124 80.257 195.901 1.00 67.27 C
ANISOU 498 CG LEU A 75 7675 6790 11096 -367 -1855 213 C
ATOM 499 CD1 LEU A 75 27.655 80.523 196.135 1.00 66.23 C
ANISOU 499 CD1 LEU A 75 7763 6693 10709 -367 -1623 150 C
ATOM 500 CD2 LEU A 75 29.751 79.692 197.167 1.00 72.46 C
ANISOU 500 CD2 LEU A 75 8439 7442 11649 -414 -2157 358 C
ATOM 501 N LEU A 76 30.238 78.432 191.764 1.00 61.13 N
ANISOU 501 N LEU A 76 6113 5879 11236 -120 -1415 153 N
ATOM 502 CA LEU A 76 30.238 77.497 190.636 1.00 60.58 C
ANISOU 502 CA LEU A 76 5899 5757 11361 -42 -1233 117 C
ATOM 503 C LEU A 76 31.621 77.446 189.961 1.00 66.01 C
ANISOU 503 C LEU A 76 6324 6384 12372 -14 -1225 105 C
ATOM 504 O LEU A 76 32.042 76.362 189.553 1.00 66.69 O
ANISOU 504 O LEU A 76 6266 6378 12693 63 -1164 120 O
ATOM 505 CB LEU A 76 29.141 77.875 189.612 1.00 58.66 C
ANISOU 505 CB LEU A 76 5740 5572 10975 -51 -997 1 C
ATOM 506 CG LEU A 76 29.005 77.022 188.328 1.00 63.00 C
ANISOU 506 CG LEU A 76 6201 6083 11653 0 -800 -76 C
ATOM 507 CD1 LEU A 76 28.806 75.556 188.640 1.00 63.84 C
ANISOU 507 CD1 LEU A 76 6296 6093 11866 62 -822 -23 C
ATOM 508 CD2 LEU A 76 27.851 77.490 187.486 1.00 63.88 C
ANISOU 508 CD2 LEU A 76 6425 6264 11581 -34 -647 -159 C
ATOM 509 N ILE A 77 32.319 78.607 189.845 1.00 62.43 N
ANISOU 509 N ILE A 77 5796 5964 11959 -75 -1266 76 N
ATOM 510 CA ILE A 77 33.651 78.724 189.230 1.00 63.48 C
ANISOU 510 CA ILE A 77 5658 6038 12424 -62 -1236 73 C
ATOM 511 C ILE A 77 34.642 77.797 189.964 1.00 69.55 C
ANISOU 511 C ILE A 77 6246 6698 13483 -11 -1451 205 C
ATOM 512 O ILE A 77 35.395 77.086 189.301 1.00 70.41 O
ANISOU 512 O ILE A 77 6122 6711 13920 65 -1332 204 O
ATOM 513 CB ILE A 77 34.128 80.209 189.176 1.00 66.66 C
ANISOU 513 CB ILE A 77 6030 6484 12814 -159 -1277 42 C
ATOM 514 CG1 ILE A 77 33.330 80.997 188.103 1.00 65.11 C
ANISOU 514 CG1 ILE A 77 5942 6363 12434 -188 -1019 -63 C
ATOM 515 CG2 ILE A 77 35.649 80.329 188.921 1.00 69.09 C
ANISOU 515 CG2 ILE A 77 6025 6712 13516 -162 -1319 86 C
ATOM 516 CD1 ILE A 77 33.231 82.520 188.323 1.00 68.84 C
ANISOU 516 CD1 ILE A 77 6496 6875 12785 -288 -1077 -87 C
ATOM 517 N ILE A 78 34.590 77.765 191.314 1.00 66.89 N
ANISOU 517 N ILE A 78 6027 6369 13018 -51 -1755 320 N
ATOM 518 CA ILE A 78 35.431 76.910 192.165 1.00 69.17 C
ANISOU 518 CA ILE A 78 6178 6560 13543 -16 -2030 491 C
ATOM 519 C ILE A 78 35.115 75.415 191.891 1.00 73.93 C
ANISOU 519 C ILE A 78 6736 7064 14288 102 -1910 536 C
ATOM 520 O ILE A 78 36.038 74.604 191.833 1.00 75.63 O
ANISOU 520 O ILE A 78 6698 7145 14893 179 -1972 628 O
ATOM 521 CB ILE A 78 35.251 77.285 193.674 1.00 72.94 C
ANISOU 521 CB ILE A 78 6884 7096 13735 -113 -2377 599 C
ATOM 522 CG1 ILE A 78 35.753 78.721 193.960 1.00 73.53 C
ANISOU 522 CG1 ILE A 78 6974 7227 13739 -237 -2525 538 C
ATOM 523 CG2 ILE A 78 35.934 76.275 194.615 1.00 76.29 C
ANISOU 523 CG2 ILE A 78 7218 7427 14343 -82 -2695 817 C
ATOM 524 CD1 ILE A 78 35.113 79.417 195.189 1.00 78.63 C
ANISOU 524 CD1 ILE A 78 7968 7962 13946 -353 -2725 531 C
ATOM 525 N CYS A 79 33.826 75.077 191.695 1.00 69.39 N
ANISOU 525 N CYS A 79 6385 6537 13441 115 -1734 470 N
ATOM 526 CA CYS A 79 33.333 73.715 191.462 1.00 69.88 C
ANISOU 526 CA CYS A 79 6448 6501 13603 204 -1619 495 C
ATOM 527 C CYS A 79 33.632 73.182 190.057 1.00 74.16 C
ANISOU 527 C CYS A 79 6803 6955 14418 284 -1320 352 C
ATOM 528 O CYS A 79 33.916 71.992 189.927 1.00 74.91 O
ANISOU 528 O CYS A 79 6771 6898 14794 375 -1284 393 O
ATOM 529 CB CYS A 79 31.836 73.640 191.744 1.00 68.66 C
ANISOU 529 CB CYS A 79 6583 6426 13081 169 -1541 472 C
ATOM 530 SG CYS A 79 31.396 73.889 193.480 1.00 73.64 S
ANISOU 530 SG CYS A 79 7472 7127 13380 89 -1829 647 S
ATOM 531 N LEU A 80 33.507 74.035 189.014 1.00 70.04 N
ANISOU 531 N LEU A 80 6292 6521 13799 246 -1097 185 N
ATOM 532 CA LEU A 80 33.653 73.682 187.595 1.00 70.05 C
ANISOU 532 CA LEU A 80 6195 6475 13946 293 -779 21 C
ATOM 533 C LEU A 80 34.880 72.785 187.281 1.00 76.46 C
ANISOU 533 C LEU A 80 6710 7105 15235 396 -709 38 C
ATOM 534 O LEU A 80 34.643 71.774 186.621 1.00 76.17 O
ANISOU 534 O LEU A 80 6667 6962 15311 463 -512 -59 O
ATOM 535 CB LEU A 80 33.643 74.918 186.684 1.00 69.05 C
ANISOU 535 CB LEU A 80 6102 6473 13660 221 -607 -99 C
ATOM 536 CG LEU A 80 32.245 75.387 186.255 1.00 71.41 C
ANISOU 536 CG LEU A 80 6664 6898 13569 158 -511 -187 C
ATOM 537 CD1 LEU A 80 32.244 76.854 185.901 1.00 70.69 C
ANISOU 537 CD1 LEU A 80 6620 6929 13311 73 -476 -217 C
ATOM 538 CD2 LEU A 80 31.701 74.556 185.092 1.00 73.78 C
ANISOU 538 CD2 LEU A 80 7022 7163 13847 186 -264 -332 C
ATOM 539 N PRO A 81 36.140 73.035 187.750 1.00 75.39 N
ANISOU 539 N PRO A 81 6322 6905 15416 413 -867 155 N
ATOM 540 CA PRO A 81 37.231 72.089 187.436 1.00 78.08 C
ANISOU 540 CA PRO A 81 6351 7043 16273 529 -776 178 C
ATOM 541 C PRO A 81 37.005 70.690 188.032 1.00 83.18 C
ANISOU 541 C PRO A 81 6988 7527 17091 620 -892 285 C
ATOM 542 O PRO A 81 37.317 69.703 187.363 1.00 84.63 O
ANISOU 542 O PRO A 81 7026 7535 17593 723 -669 203 O
ATOM 543 CB PRO A 81 38.473 72.758 188.041 1.00 81.79 C
ANISOU 543 CB PRO A 81 6560 7492 17026 505 -1011 326 C
ATOM 544 CG PRO A 81 38.106 74.195 188.187 1.00 84.11 C
ANISOU 544 CG PRO A 81 7031 7981 16945 370 -1091 294 C
ATOM 545 CD PRO A 81 36.656 74.170 188.542 1.00 77.01 C
ANISOU 545 CD PRO A 81 6495 7199 15568 326 -1132 263 C
ATOM 546 N PHE A 82 36.439 70.598 189.262 1.00 79.00 N
ANISOU 546 N PHE A 82 6627 7045 16344 579 -1214 462 N
ATOM 547 CA PHE A 82 36.131 69.320 189.923 1.00 80.05 C
ANISOU 547 CA PHE A 82 6784 7031 16602 648 -1342 606 C
ATOM 548 C PHE A 82 35.046 68.573 189.160 1.00 83.45 C
ANISOU 548 C PHE A 82 7385 7424 16898 672 -1064 437 C
ATOM 549 O PHE A 82 35.117 67.351 189.023 1.00 85.27 O
ANISOU 549 O PHE A 82 7522 7452 17426 765 -992 451 O
ATOM 550 CB PHE A 82 35.676 69.534 191.376 1.00 81.59 C
ANISOU 550 CB PHE A 82 7180 7320 16499 571 -1712 828 C
ATOM 551 CG PHE A 82 36.703 70.131 192.304 1.00 85.05 C
ANISOU 551 CG PHE A 82 7488 7781 17048 529 -2070 1015 C
ATOM 552 CD1 PHE A 82 37.576 69.318 193.017 1.00 91.04 C
ANISOU 552 CD1 PHE A 82 8032 8369 18190 595 -2344 1256 C
ATOM 553 CD2 PHE A 82 36.769 71.506 192.501 1.00 85.74 C
ANISOU 553 CD2 PHE A 82 7669 8046 16860 412 -2163 962 C
ATOM 554 CE1 PHE A 82 38.515 69.871 193.891 1.00 94.04 C
ANISOU 554 CE1 PHE A 82 8293 8771 18667 537 -2728 1440 C
ATOM 555 CE2 PHE A 82 37.708 72.059 193.375 1.00 90.46 C
ANISOU 555 CE2 PHE A 82 8159 8657 17556 351 -2525 1121 C
ATOM 556 CZ PHE A 82 38.573 71.238 194.065 1.00 91.83 C
ANISOU 556 CZ PHE A 82 8121 8675 18095 408 -2819 1360 C
ATOM 557 N LEU A 83 34.044 69.324 188.669 1.00 77.51 N
ANISOU 557 N LEU A 83 6874 6854 15722 582 -924 282 N
ATOM 558 CA LEU A 83 32.908 68.831 187.896 1.00 76.19 C
ANISOU 558 CA LEU A 83 6889 6687 15374 568 -697 113 C
ATOM 559 C LEU A 83 33.370 68.327 186.528 1.00 82.16 C
ANISOU 559 C LEU A 83 7519 7325 16372 629 -371 -111 C
ATOM 560 O LEU A 83 32.988 67.232 186.133 1.00 82.40 O
ANISOU 560 O LEU A 83 7573 7203 16530 675 -244 -197 O
ATOM 561 CB LEU A 83 31.872 69.956 187.740 1.00 73.47 C
ANISOU 561 CB LEU A 83 6787 6569 14558 454 -672 35 C
ATOM 562 CG LEU A 83 30.439 69.529 187.470 1.00 76.50 C
ANISOU 562 CG LEU A 83 7386 6977 14705 412 -582 -43 C
ATOM 563 CD1 LEU A 83 29.668 69.349 188.767 1.00 76.20 C
ANISOU 563 CD1 LEU A 83 7488 6960 14505 382 -790 151 C
ATOM 564 CD2 LEU A 83 29.746 70.544 186.610 1.00 76.90 C
ANISOU 564 CD2 LEU A 83 7576 7199 14445 328 -445 -196 C
ATOM 565 N MET A 84 34.225 69.107 185.834 1.00 80.70 N
ANISOU 565 N MET A 84 7203 7196 16263 625 -227 -204 N
ATOM 566 CA MET A 84 34.807 68.779 184.528 1.00 82.99 C
ANISOU 566 CA MET A 84 7383 7391 16760 673 126 -420 C
ATOM 567 C MET A 84 35.561 67.440 184.599 1.00 90.57 C
ANISOU 567 C MET A 84 8110 8066 18238 811 190 -401 C
ATOM 568 O MET A 84 35.467 66.628 183.675 1.00 91.61 O
ANISOU 568 O MET A 84 8262 8063 18484 855 475 -608 O
ATOM 569 CB MET A 84 35.749 69.912 184.093 1.00 86.14 C
ANISOU 569 CB MET A 84 7638 7888 17203 644 223 -440 C
ATOM 570 CG MET A 84 36.030 69.956 182.615 1.00 91.45 C
ANISOU 570 CG MET A 84 8314 8555 17879 641 634 -682 C
ATOM 571 SD MET A 84 36.944 71.462 182.197 1.00 96.49 S
ANISOU 571 SD MET A 84 8822 9337 18504 574 732 -660 S
ATOM 572 CE MET A 84 37.690 70.961 180.652 1.00 96.33 C
ANISOU 572 CE MET A 84 8707 9199 18696 627 1261 -908 C
ATOM 573 N ASP A 85 36.270 67.209 185.726 1.00 88.35 N
ANISOU 573 N ASP A 85 7621 7685 18263 873 -95 -148 N
ATOM 574 CA ASP A 85 37.020 65.990 186.021 1.00 90.96 C
ANISOU 574 CA ASP A 85 7694 7728 19138 1011 -115 -54 C
ATOM 575 C ASP A 85 36.070 64.810 186.260 1.00 93.91 C
ANISOU 575 C ASP A 85 8228 7966 19486 1036 -144 -47 C
ATOM 576 O ASP A 85 36.414 63.678 185.918 1.00 96.31 O
ANISOU 576 O ASP A 85 8390 8005 20200 1146 14 -111 O
ATOM 577 CB ASP A 85 37.926 66.206 187.245 1.00 94.43 C
ANISOU 577 CB ASP A 85 7903 8133 19844 1040 -494 259 C
ATOM 578 CG ASP A 85 38.722 64.985 187.654 1.00110.60 C
ANISOU 578 CG ASP A 85 9657 9872 22494 1187 -575 417 C
ATOM 579 OD1 ASP A 85 39.673 64.623 186.926 1.00114.53 O
ANISOU 579 OD1 ASP A 85 9866 10184 23468 1293 -316 312 O
ATOM 580 OD2 ASP A 85 38.381 64.377 188.691 1.00117.59 O
ANISOU 580 OD2 ASP A 85 10601 10691 23386 1197 -880 651 O
ATOM 581 N ASN A 86 34.888 65.067 186.854 1.00 86.89 N
ANISOU 581 N ASN A 86 7621 7239 18155 936 -329 30 N
ATOM 582 CA ASN A 86 33.902 64.018 187.119 1.00 86.27 C
ANISOU 582 CA ASN A 86 7694 7041 18042 938 -359 55 C
ATOM 583 C ASN A 86 33.304 63.500 185.807 1.00 89.67 C
ANISOU 583 C ASN A 86 8244 7402 18423 925 -17 -269 C
ATOM 584 O ASN A 86 33.126 62.292 185.666 1.00 91.04 O
ANISOU 584 O ASN A 86 8392 7334 18864 985 64 -317 O
ATOM 585 CB ASN A 86 32.800 64.512 188.064 1.00 83.15 C
ANISOU 585 CB ASN A 86 7555 6842 17196 827 -601 216 C
ATOM 586 CG ASN A 86 31.852 63.430 188.530 1.00 98.91 C
ANISOU 586 CG ASN A 86 9674 8703 19203 825 -656 307 C
ATOM 587 OD1 ASN A 86 30.695 63.362 188.107 1.00 91.65 O
ANISOU 587 OD1 ASN A 86 8955 7844 18023 748 -544 173 O
ATOM 588 ND2 ASN A 86 32.314 62.563 189.419 1.00 90.52 N
ANISOU 588 ND2 ASN A 86 8485 7448 18462 901 -844 557 N
ATOM 589 N TYR A 87 33.044 64.400 184.841 1.00 84.35 N
ANISOU 589 N TYR A 87 7702 6925 17423 842 172 -488 N
ATOM 590 CA TYR A 87 32.468 64.028 183.551 1.00 84.40 C
ANISOU 590 CA TYR A 87 7865 6900 17303 800 466 -801 C
ATOM 591 C TYR A 87 33.488 63.339 182.624 1.00 91.03 C
ANISOU 591 C TYR A 87 8530 7516 18542 904 789 -1010 C
ATOM 592 O TYR A 87 33.056 62.575 181.768 1.00 92.00 O
ANISOU 592 O TYR A 87 8775 7514 18668 890 1005 -1258 O
ATOM 593 CB TYR A 87 31.821 65.235 182.852 1.00 83.51 C
ANISOU 593 CB TYR A 87 7967 7075 16687 668 529 -928 C
ATOM 594 CG TYR A 87 30.493 65.648 183.457 1.00 83.07 C
ANISOU 594 CG TYR A 87 8122 7185 16256 564 306 -813 C
ATOM 595 CD1 TYR A 87 30.436 66.566 184.499 1.00 83.31 C
ANISOU 595 CD1 TYR A 87 8153 7378 16124 536 66 -584 C
ATOM 596 CD2 TYR A 87 29.295 65.122 182.984 1.00 83.75 C
ANISOU 596 CD2 TYR A 87 8402 7251 16167 489 343 -942 C
ATOM 597 CE1 TYR A 87 29.220 66.955 185.057 1.00 82.36 C
ANISOU 597 CE1 TYR A 87 8217 7393 15684 449 -88 -491 C
ATOM 598 CE2 TYR A 87 28.070 65.499 183.539 1.00 82.66 C
ANISOU 598 CE2 TYR A 87 8418 7248 15740 399 163 -827 C
ATOM 599 CZ TYR A 87 28.038 66.419 184.575 1.00 89.40 C
ANISOU 599 CZ TYR A 87 9265 8258 16444 386 -30 -603 C
ATOM 600 OH TYR A 87 26.842 66.806 185.133 1.00 89.68 O
ANISOU 600 OH TYR A 87 9444 8412 16218 307 -159 -500 O
ATOM 601 N VAL A 88 34.813 63.567 182.791 1.00 89.02 N
ANISOU 601 N VAL A 88 7988 7193 18643 1002 829 -921 N
ATOM 602 CA VAL A 88 35.807 62.881 181.942 1.00 92.26 C
ANISOU 602 CA VAL A 88 8201 7362 19493 1115 1182 -1118 C
ATOM 603 C VAL A 88 36.045 61.454 182.471 1.00 98.14 C
ANISOU 603 C VAL A 88 8771 7757 20759 1248 1131 -1034 C
ATOM 604 O VAL A 88 36.370 60.556 181.689 1.00100.32 O
ANISOU 604 O VAL A 88 8990 7784 21345 1326 1447 -1268 O
ATOM 605 CB VAL A 88 37.157 63.632 181.718 1.00 97.88 C
ANISOU 605 CB VAL A 88 8635 8102 20452 1170 1320 -1086 C
ATOM 606 CG1 VAL A 88 36.954 64.962 181.010 1.00 95.62 C
ANISOU 606 CG1 VAL A 88 8525 8119 19685 1039 1436 -1194 C
ATOM 607 CG2 VAL A 88 37.955 63.813 183.008 1.00 98.34 C
ANISOU 607 CG2 VAL A 88 8395 8114 20853 1241 967 -733 C
ATOM 608 N ARG A 89 35.866 61.255 183.794 1.00 93.68 N
ANISOU 608 N ARG A 89 8143 7169 20280 1267 740 -701 N
ATOM 609 CA ARG A 89 36.073 59.977 184.479 1.00 95.84 C
ANISOU 609 CA ARG A 89 8250 7121 21042 1385 620 -534 C
ATOM 610 C ARG A 89 34.771 59.144 184.564 1.00 98.50 C
ANISOU 610 C ARG A 89 8845 7382 21198 1322 573 -582 C
ATOM 611 O ARG A 89 34.690 58.231 185.387 1.00 99.34 O
ANISOU 611 O ARG A 89 8870 7274 21600 1384 385 -362 O
ATOM 612 CB ARG A 89 36.670 60.215 185.882 1.00 96.11 C
ANISOU 612 CB ARG A 89 8083 7171 21264 1429 205 -115 C
ATOM 613 CG ARG A 89 38.098 60.750 185.841 1.00109.65 C
ANISOU 613 CG ARG A 89 9456 8862 23344 1511 230 -47 C
ATOM 614 CD ARG A 89 38.768 60.754 187.200 1.00123.63 C
ANISOU 614 CD ARG A 89 11004 10584 25387 1558 -213 368 C
ATOM 615 NE ARG A 89 40.128 61.294 187.124 1.00135.89 N
ANISOU 615 NE ARG A 89 12199 12106 27326 1624 -206 431 N
ATOM 616 CZ ARG A 89 41.011 61.258 188.117 1.00154.46 C
ANISOU 616 CZ ARG A 89 14267 14367 30055 1681 -570 770 C
ATOM 617 NH1 ARG A 89 42.220 61.777 187.956 1.00146.42 N
ANISOU 617 NH1 ARG A 89 12903 13316 29415 1729 -547 808 N
ATOM 618 NH2 ARG A 89 40.693 60.698 189.278 1.00141.88 N
ANISOU 618 NH2 ARG A 89 12731 12711 28466 1680 -967 1085 N
ATOM 619 N ARG A 90 33.786 59.425 183.674 1.00 93.24 N
ANISOU 619 N ARG A 90 8474 6872 20082 1195 743 -861 N
ATOM 620 CA ARG A 90 32.482 58.746 183.563 1.00 92.39 C
ANISOU 620 CA ARG A 90 8611 6710 19782 1105 719 -952 C
ATOM 621 C ARG A 90 31.746 58.698 184.926 1.00 94.65 C
ANISOU 621 C ARG A 90 8955 7059 19948 1063 351 -594 C
ATOM 622 O ARG A 90 31.283 57.636 185.362 1.00 95.43 O
ANISOU 622 O ARG A 90 9060 6931 20269 1082 278 -499 O
ATOM 623 CB ARG A 90 32.640 57.335 182.955 1.00 95.90 C
ANISOU 623 CB ARG A 90 8995 6768 20673 1188 958 -1168 C
ATOM 624 N TRP A 91 31.653 59.878 185.582 1.00 88.59 N
ANISOU 624 N TRP A 91 8241 6594 18824 999 142 -405 N
ATOM 625 CA TRP A 91 31.019 60.151 186.882 1.00 86.88 C
ANISOU 625 CA TRP A 91 8118 6508 18383 941 -176 -81 C
ATOM 626 C TRP A 91 31.700 59.432 188.066 1.00 92.44 C
ANISOU 626 C TRP A 91 8636 7012 19476 1044 -413 265 C
ATOM 627 O TRP A 91 31.078 59.291 189.123 1.00 91.53 O
ANISOU 627 O TRP A 91 8629 6934 19213 995 -640 531 O
ATOM 628 CB TRP A 91 29.511 59.843 186.873 1.00 84.40 C
ANISOU 628 CB TRP A 91 8046 6229 17791 824 -183 -123 C
ATOM 629 CG TRP A 91 28.696 60.628 185.888 1.00 83.34 C
ANISOU 629 CG TRP A 91 8108 6316 17241 703 -42 -390 C
ATOM 630 CD1 TRP A 91 28.976 61.864 185.378 1.00 84.55 C
ANISOU 630 CD1 TRP A 91 8298 6720 17108 664 16 -497 C
ATOM 631 CD2 TRP A 91 27.419 60.256 185.362 1.00 82.73 C
ANISOU 631 CD2 TRP A 91 8212 6229 16993 595 19 -544 C
ATOM 632 NE1 TRP A 91 27.972 62.262 184.528 1.00 82.50 N
ANISOU 632 NE1 TRP A 91 8236 6602 16510 545 110 -703 N
ATOM 633 CE2 TRP A 91 26.995 61.300 184.510 1.00 84.59 C
ANISOU 633 CE2 TRP A 91 8587 6715 16837 498 100 -737 C
ATOM 634 CE3 TRP A 91 26.591 59.129 185.517 1.00 85.28 C
ANISOU 634 CE3 TRP A 91 8581 6338 17482 563 2 -526 C
ATOM 635 CZ2 TRP A 91 25.788 61.246 183.805 1.00 83.19 C
ANISOU 635 CZ2 TRP A 91 8587 6588 16432 371 137 -908 C
ATOM 636 CZ3 TRP A 91 25.387 59.085 184.835 1.00 85.97 C
ANISOU 636 CZ3 TRP A 91 8838 6474 17352 432 49 -709 C
ATOM 637 CH2 TRP A 91 24.995 60.134 183.991 1.00 84.75 C
ANISOU 637 CH2 TRP A 91 8814 6578 16808 337 103 -895 C
ATOM 638 N ASP A 92 32.979 59.032 187.921 1.00 91.39 N
ANISOU 638 N ASP A 92 8220 6674 19830 1180 -365 283 N
ATOM 639 CA ASP A 92 33.702 58.404 189.025 1.00 93.66 C
ANISOU 639 CA ASP A 92 8304 6769 20513 1279 -633 642 C
ATOM 640 C ASP A 92 34.328 59.505 189.889 1.00 96.84 C
ANISOU 640 C ASP A 92 8656 7410 20729 1248 -924 881 C
ATOM 641 O ASP A 92 35.331 60.117 189.504 1.00 96.99 O
ANISOU 641 O ASP A 92 8479 7471 20902 1293 -870 808 O
ATOM 642 CB ASP A 92 34.749 57.380 188.536 1.00 99.07 C
ANISOU 642 CB ASP A 92 8675 7080 21886 1449 -467 579 C
ATOM 643 CG ASP A 92 35.545 56.689 189.635 1.00110.03 C
ANISOU 643 CG ASP A 92 9817 8238 23752 1561 -770 979 C
ATOM 644 OD1 ASP A 92 34.968 56.426 190.717 1.00109.74 O
ANISOU 644 OD1 ASP A 92 9915 8226 23555 1507 -1061 1291 O
ATOM 645 OD2 ASP A 92 36.732 56.381 189.402 1.00118.74 O
ANISOU 645 OD2 ASP A 92 10589 9125 25403 1702 -708 991 O
ATOM 646 N TRP A 93 33.690 59.780 191.039 1.00 91.97 N
ANISOU 646 N TRP A 93 8234 6949 19762 1157 -1215 1150 N
ATOM 647 CA TRP A 93 34.128 60.793 191.994 1.00 91.13 C
ANISOU 647 CA TRP A 93 8149 7069 19407 1098 -1525 1375 C
ATOM 648 C TRP A 93 35.272 60.239 192.843 1.00 99.26 C
ANISOU 648 C TRP A 93 8917 7903 20894 1196 -1829 1707 C
ATOM 649 O TRP A 93 35.085 59.267 193.581 1.00100.76 O
ANISOU 649 O TRP A 93 9118 7912 21254 1228 -1995 1970 O
ATOM 650 CB TRP A 93 32.949 61.248 192.867 1.00 87.44 C
ANISOU 650 CB TRP A 93 8023 6828 18371 959 -1672 1506 C
ATOM 651 CG TRP A 93 33.252 62.432 193.735 1.00 87.48 C
ANISOU 651 CG TRP A 93 8122 7090 18026 873 -1942 1652 C
ATOM 652 CD1 TRP A 93 33.519 62.420 195.071 1.00 92.25 C
ANISOU 652 CD1 TRP A 93 8790 7724 18538 837 -2306 1995 C
ATOM 653 CD2 TRP A 93 33.303 63.806 193.327 1.00 84.75 C
ANISOU 653 CD2 TRP A 93 7838 6998 17365 798 -1875 1455 C
ATOM 654 NE1 TRP A 93 33.739 63.700 195.522 1.00 90.62 N
ANISOU 654 NE1 TRP A 93 8689 7770 17971 740 -2470 1995 N
ATOM 655 CE2 TRP A 93 33.599 64.573 194.474 1.00 89.15 C
ANISOU 655 CE2 TRP A 93 8494 7716 17661 719 -2205 1670 C
ATOM 656 CE3 TRP A 93 33.115 64.467 192.101 1.00 83.56 C
ANISOU 656 CE3 TRP A 93 7687 6948 17115 782 -1575 1124 C
ATOM 657 CZ2 TRP A 93 33.730 65.966 194.431 1.00 86.45 C
ANISOU 657 CZ2 TRP A 93 8228 7609 17010 631 -2233 1549 C
ATOM 658 CZ3 TRP A 93 33.247 65.847 192.059 1.00 83.04 C
ANISOU 658 CZ3 TRP A 93 7687 7119 16745 700 -1607 1039 C
ATOM 659 CH2 TRP A 93 33.562 66.579 193.212 1.00 84.14 C
ANISOU 659 CH2 TRP A 93 7901 7391 16675 630 -1928 1242 C
ATOM 660 N LYS A 94 36.460 60.846 192.716 1.00 97.61 N
ANISOU 660 N LYS A 94 8457 7716 20915 1240 -1907 1711 N
ATOM 661 CA LYS A 94 37.653 60.424 193.446 1.00101.64 C
ANISOU 661 CA LYS A 94 8664 8040 21914 1331 -2224 2027 C
ATOM 662 C LYS A 94 38.177 61.550 194.359 1.00106.53 C
ANISOU 662 C LYS A 94 9312 8900 22265 1228 -2610 2223 C
ATOM 663 O LYS A 94 39.393 61.703 194.511 1.00109.12 O
ANISOU 663 O LYS A 94 9320 9140 23000 1285 -2800 2352 O
ATOM 664 CB LYS A 94 38.737 59.964 192.455 1.00106.66 C
ANISOU 664 CB LYS A 94 8895 8411 23219 1491 -1967 1867 C
ATOM 665 N PHE A 95 37.259 62.317 194.993 1.00101.05 N
ANISOU 665 N PHE A 95 8993 8490 20910 1073 -2731 2246 N
ATOM 666 CA PHE A 95 37.633 63.423 195.881 1.00101.10 C
ANISOU 666 CA PHE A 95 9093 8727 20592 953 -3086 2390 C
ATOM 667 C PHE A 95 37.222 63.191 197.352 1.00106.79 C
ANISOU 667 C PHE A 95 10083 9513 20980 861 -3479 2742 C
ATOM 668 O PHE A 95 37.839 63.783 198.238 1.00108.33 O
ANISOU 668 O PHE A 95 10295 9813 21054 781 -3870 2939 O
ATOM 669 CB PHE A 95 37.077 64.761 195.377 1.00 99.12 C
ANISOU 669 CB PHE A 95 9052 8764 19846 838 -2887 2093 C
ATOM 670 CG PHE A 95 37.664 65.232 194.065 1.00 99.93 C
ANISOU 670 CG PHE A 95 8909 8847 20213 896 -2567 1796 C
ATOM 671 CD1 PHE A 95 38.922 65.825 194.018 1.00105.01 C
ANISOU 671 CD1 PHE A 95 9256 9476 21167 908 -2709 1834 C
ATOM 672 CD2 PHE A 95 36.946 65.113 192.881 1.00 99.77 C
ANISOU 672 CD2 PHE A 95 8965 8829 20113 921 -2130 1487 C
ATOM 673 CE1 PHE A 95 39.460 66.269 192.805 1.00105.35 C
ANISOU 673 CE1 PHE A 95 9080 9501 21445 953 -2375 1574 C
ATOM 674 CE2 PHE A 95 37.483 65.560 191.669 1.00102.11 C
ANISOU 674 CE2 PHE A 95 9076 9121 20600 960 -1821 1224 C
ATOM 675 CZ PHE A 95 38.735 66.136 191.639 1.00102.04 C
ANISOU 675 CZ PHE A 95 8775 9096 20901 978 -1924 1271 C
ATOM 676 N GLY A 96 36.231 62.334 197.602 1.00102.96 N
ANISOU 676 N GLY A 96 9804 8957 20358 864 -3380 2825 N
ATOM 677 CA GLY A 96 35.805 62.013 198.963 1.00104.82 C
ANISOU 677 CA GLY A 96 10310 9239 20277 778 -3701 3176 C
ATOM 678 C GLY A 96 34.395 62.414 199.352 1.00107.14 C
ANISOU 678 C GLY A 96 11039 9752 19918 647 -3552 3107 C
ATOM 679 O GLY A 96 33.627 62.910 198.522 1.00103.57 O
ANISOU 679 O GLY A 96 10675 9409 19267 626 -3201 2783 O
ATOM 680 N ASP A 97 34.068 62.221 200.650 1.00105.98 N
ANISOU 680 N ASP A 97 11166 9668 19432 552 -3829 3430 N
ATOM 681 CA ASP A 97 32.770 62.486 201.284 1.00104.32 C
ANISOU 681 CA ASP A 97 11378 9642 18616 424 -3711 3444 C
ATOM 682 C ASP A 97 32.447 63.982 201.400 1.00106.24 C
ANISOU 682 C ASP A 97 11856 10189 18320 299 -3665 3212 C
ATOM 683 O ASP A 97 31.484 64.440 200.779 1.00102.91 O
ANISOU 683 O ASP A 97 11545 9869 17686 276 -3313 2937 O
ATOM 684 CB ASP A 97 32.713 61.814 202.681 1.00109.78 C
ANISOU 684 CB ASP A 97 12288 10298 19124 359 -4035 3892 C
ATOM 685 CG ASP A 97 31.584 62.242 203.615 1.00118.14 C
ANISOU 685 CG ASP A 97 13817 11575 19494 202 -3970 3957 C
ATOM 686 OD1 ASP A 97 31.872 62.546 204.792 1.00121.30 O
ANISOU 686 OD1 ASP A 97 14465 12100 19525 89 -4307 4205 O
ATOM 687 OD2 ASP A 97 30.412 62.242 203.176 1.00121.22 O
ANISOU 687 OD2 ASP A 97 14327 12003 19726 188 -3580 3766 O
ATOM 688 N ILE A 98 33.227 64.726 202.214 1.00104.38 N
ANISOU 688 N ILE A 98 11698 10082 17880 212 -4035 3332 N
ATOM 689 CA ILE A 98 33.000 66.138 202.500 1.00102.42 C
ANISOU 689 CA ILE A 98 11696 10094 17123 80 -4041 3138 C
ATOM 690 C ILE A 98 33.218 67.046 201.239 1.00102.21 C
ANISOU 690 C ILE A 98 11450 10118 17266 124 -3791 2755 C
ATOM 691 O ILE A 98 32.439 67.996 201.130 1.00 99.34 O
ANISOU 691 O ILE A 98 11306 9931 16507 47 -3583 2531 O
ATOM 692 CB ILE A 98 33.808 66.616 203.751 1.00109.27 C
ANISOU 692 CB ILE A 98 12725 11064 17729 -45 -4545 3372 C
ATOM 693 CG1 ILE A 98 33.176 67.865 204.398 1.00108.89 C
ANISOU 693 CG1 ILE A 98 13092 11274 17006 -211 -4512 3213 C
ATOM 694 CG2 ILE A 98 35.316 66.802 203.512 1.00112.20 C
ANISOU 694 CG2 ILE A 98 12722 11345 18563 -1 -4883 3421 C
ATOM 695 CD1 ILE A 98 32.058 67.566 205.442 1.00118.09 C
ANISOU 695 CD1 ILE A 98 14713 12531 17626 -311 -4429 3375 C
ATOM 696 N PRO A 99 34.134 66.797 200.253 1.00 98.10 N
ANISOU 696 N PRO A 99 10524 9447 17304 245 -3754 2667 N
ATOM 697 CA PRO A 99 34.214 67.708 199.093 1.00 94.56 C
ANISOU 697 CA PRO A 99 9933 9071 16926 264 -3482 2318 C
ATOM 698 C PRO A 99 33.041 67.542 198.117 1.00 94.34 C
ANISOU 698 C PRO A 99 9972 9049 16822 303 -3026 2074 C
ATOM 699 O PRO A 99 32.760 68.462 197.351 1.00 91.43 O
ANISOU 699 O PRO A 99 9616 8798 16325 278 -2805 1805 O
ATOM 700 CB PRO A 99 35.549 67.336 198.428 1.00 97.93 C
ANISOU 700 CB PRO A 99 9916 9314 17979 379 -3561 2338 C
ATOM 701 CG PRO A 99 36.239 66.417 199.383 1.00106.63 C
ANISOU 701 CG PRO A 99 10927 10265 19323 408 -3951 2710 C
ATOM 702 CD PRO A 99 35.156 65.739 200.135 1.00102.50 C
ANISOU 702 CD PRO A 99 10730 9755 18460 368 -3935 2877 C
ATOM 703 N CYS A 100 32.363 66.371 198.137 1.00 90.51 N
ANISOU 703 N CYS A 100 9526 8429 16435 357 -2905 2179 N
ATOM 704 CA CYS A 100 31.203 66.092 197.290 1.00 87.55 C
ANISOU 704 CA CYS A 100 9216 8041 16006 378 -2524 1974 C
ATOM 705 C CYS A 100 30.005 66.834 197.844 1.00 88.52 C
ANISOU 705 C CYS A 100 9684 8366 15585 260 -2430 1931 C
ATOM 706 O CYS A 100 29.263 67.459 197.085 1.00 85.43 O
ANISOU 706 O CYS A 100 9341 8070 15048 239 -2168 1684 O
ATOM 707 CB CYS A 100 30.942 64.590 197.191 1.00 89.58 C
ANISOU 707 CB CYS A 100 9386 8059 16593 462 -2456 2109 C
ATOM 708 SG CYS A 100 29.364 64.150 196.411 1.00 91.11 S
ANISOU 708 SG CYS A 100 9705 8229 16683 447 -2062 1909 S
ATOM 709 N ARG A 101 29.839 66.777 199.184 1.00 86.10 N
ANISOU 709 N ARG A 101 9617 8117 14979 182 -2646 2182 N
ATOM 710 CA ARG A 101 28.758 67.440 199.922 1.00 84.55 C
ANISOU 710 CA ARG A 101 9771 8098 14257 67 -2550 2171 C
ATOM 711 C ARG A 101 28.844 68.947 199.742 1.00 84.66 C
ANISOU 711 C ARG A 101 9859 8298 14010 2 -2522 1935 C
ATOM 712 O ARG A 101 27.813 69.589 199.512 1.00 82.51 O
ANISOU 712 O ARG A 101 9732 8129 13490 -38 -2264 1762 O
ATOM 713 CB ARG A 101 28.817 67.072 201.410 1.00 88.32 C
ANISOU 713 CB ARG A 101 10499 8597 14463 -10 -2813 2497 C
ATOM 714 CG ARG A 101 28.141 65.756 201.755 1.00 98.41 C
ANISOU 714 CG ARG A 101 11829 9727 15833 14 -2731 2731 C
ATOM 715 CD ARG A 101 27.613 65.786 203.172 1.00109.70 C
ANISOU 715 CD ARG A 101 13641 11263 16777 -106 -2820 2972 C
ATOM 716 NE ARG A 101 28.317 64.835 204.031 1.00120.51 N
ANISOU 716 NE ARG A 101 15022 12515 18252 -105 -3158 3354 N
ATOM 717 CZ ARG A 101 28.023 64.616 205.308 1.00137.22 C
ANISOU 717 CZ ARG A 101 17471 14693 19973 -210 -3288 3639 C
ATOM 718 NH1 ARG A 101 27.035 65.281 205.893 1.00125.46 N
ANISOU 718 NH1 ARG A 101 16332 13379 17959 -322 -3070 3563 N
ATOM 719 NH2 ARG A 101 28.716 63.732 206.013 1.00126.27 N
ANISOU 719 NH2 ARG A 101 16073 13187 18716 -206 -3628 4011 N
ATOM 720 N LEU A 102 30.076 69.506 199.813 1.00 80.02 N
ANISOU 720 N LEU A 102 9144 7732 13528 -6 -2787 1934 N
ATOM 721 CA LEU A 102 30.361 70.927 199.645 1.00 77.48 C
ANISOU 721 CA LEU A 102 8857 7553 13027 -72 -2802 1727 C
ATOM 722 C LEU A 102 30.088 71.386 198.216 1.00 76.22 C
ANISOU 722 C LEU A 102 8517 7398 13047 -14 -2490 1448 C
ATOM 723 O LEU A 102 29.501 72.454 198.044 1.00 73.78 O
ANISOU 723 O LEU A 102 8341 7211 12481 -71 -2339 1266 O
ATOM 724 CB LEU A 102 31.813 71.252 200.035 1.00 79.73 C
ANISOU 724 CB LEU A 102 8999 7824 13470 -99 -3185 1825 C
ATOM 725 CG LEU A 102 32.082 71.454 201.529 1.00 87.46 C
ANISOU 725 CG LEU A 102 10257 8883 14093 -223 -3550 2031 C
ATOM 726 CD1 LEU A 102 33.546 71.253 201.845 1.00 90.47 C
ANISOU 726 CD1 LEU A 102 10409 9182 14784 -222 -3979 2214 C
ATOM 727 CD2 LEU A 102 31.611 72.833 202.007 1.00 89.71 C
ANISOU 727 CD2 LEU A 102 10849 9344 13894 -355 -3508 1843 C
ATOM 728 N MET A 103 30.484 70.582 197.198 1.00 71.19 N
ANISOU 728 N MET A 103 7593 6619 12838 96 -2384 1413 N
ATOM 729 CA MET A 103 30.283 70.910 195.783 1.00 68.11 C
ANISOU 729 CA MET A 103 7051 6230 12597 143 -2095 1159 C
ATOM 730 C MET A 103 28.790 70.982 195.433 1.00 68.74 C
ANISOU 730 C MET A 103 7308 6370 12442 119 -1816 1040 C
ATOM 731 O MET A 103 28.346 72.020 194.944 1.00 66.51 O
ANISOU 731 O MET A 103 7083 6200 11988 78 -1676 865 O
ATOM 732 CB MET A 103 31.002 69.911 194.861 1.00 70.92 C
ANISOU 732 CB MET A 103 7107 6406 13435 259 -2025 1143 C
ATOM 733 CG MET A 103 30.940 70.306 193.395 1.00 72.58 C
ANISOU 733 CG MET A 103 7191 6631 13755 289 -1738 879 C
ATOM 734 SD MET A 103 31.297 68.994 192.211 1.00 77.63 S
ANISOU 734 SD MET A 103 7583 7053 14859 413 -1529 789 S
ATOM 735 CE MET A 103 29.890 67.923 192.465 1.00 73.93 C
ANISOU 735 CE MET A 103 7299 6513 14278 407 -1436 845 C
ATOM 736 N LEU A 104 28.025 69.900 195.709 1.00 64.80 N
ANISOU 736 N LEU A 104 6877 5781 11962 140 -1749 1155 N
ATOM 737 CA LEU A 104 26.586 69.809 195.435 1.00 62.59 C
ANISOU 737 CA LEU A 104 6727 5529 11527 113 -1504 1076 C
ATOM 738 C LEU A 104 25.815 70.981 196.067 1.00 65.90 C
ANISOU 738 C LEU A 104 7381 6115 11544 25 -1452 1033 C
ATOM 739 O LEU A 104 24.914 71.533 195.430 1.00 63.63 O
ANISOU 739 O LEU A 104 7118 5884 11174 8 -1246 878 O
ATOM 740 CB LEU A 104 26.010 68.462 195.909 1.00 63.60 C
ANISOU 740 CB LEU A 104 6894 5520 11751 132 -1487 1259 C
ATOM 741 CG LEU A 104 26.446 67.209 195.132 1.00 68.19 C
ANISOU 741 CG LEU A 104 7252 5894 12763 223 -1459 1257 C
ATOM 742 CD1 LEU A 104 25.995 65.953 195.845 1.00 70.29 C
ANISOU 742 CD1 LEU A 104 7572 6010 13124 229 -1491 1488 C
ATOM 743 CD2 LEU A 104 25.925 67.213 193.695 1.00 67.14 C
ANISOU 743 CD2 LEU A 104 7021 5740 12749 240 -1218 992 C
ATOM 744 N PHE A 105 26.214 71.383 197.291 1.00 63.96 N
ANISOU 744 N PHE A 105 7305 5936 11061 -33 -1648 1165 N
ATOM 745 CA PHE A 105 25.642 72.509 198.021 1.00 63.25 C
ANISOU 745 CA PHE A 105 7463 5983 10584 -119 -1604 1110 C
ATOM 746 C PHE A 105 25.943 73.813 197.279 1.00 66.02 C
ANISOU 746 C PHE A 105 7738 6413 10932 -131 -1561 887 C
ATOM 747 O PHE A 105 25.023 74.592 197.036 1.00 64.62 O
ANISOU 747 O PHE A 105 7645 6297 10609 -156 -1358 755 O
ATOM 748 CB PHE A 105 26.191 72.540 199.463 1.00 67.64 C
ANISOU 748 CB PHE A 105 8234 6581 10884 -191 -1865 1294 C
ATOM 749 CG PHE A 105 25.979 73.821 200.236 1.00 69.33 C
ANISOU 749 CG PHE A 105 8712 6927 10705 -290 -1871 1197 C
ATOM 750 CD1 PHE A 105 24.720 74.164 200.715 1.00 71.93 C
ANISOU 750 CD1 PHE A 105 9275 7310 10745 -334 -1614 1153 C
ATOM 751 CD2 PHE A 105 27.043 74.671 200.509 1.00 72.33 C
ANISOU 751 CD2 PHE A 105 9098 7357 11026 -345 -2125 1144 C
ATOM 752 CE1 PHE A 105 24.528 75.343 201.437 1.00 73.69 C
ANISOU 752 CE1 PHE A 105 9752 7630 10617 -421 -1587 1037 C
ATOM 753 CE2 PHE A 105 26.849 75.851 201.231 1.00 75.91 C
ANISOU 753 CE2 PHE A 105 9814 7909 11120 -446 -2129 1028 C
ATOM 754 CZ PHE A 105 25.594 76.177 201.692 1.00 73.88 C
ANISOU 754 CZ PHE A 105 9806 7699 10567 -480 -1850 966 C
ATOM 755 N MET A 106 27.221 74.017 196.886 1.00 62.96 N
ANISOU 755 N MET A 106 7168 6006 10748 -111 -1740 863 N
ATOM 756 CA MET A 106 27.722 75.193 196.167 1.00 61.46 C
ANISOU 756 CA MET A 106 6876 5871 10605 -128 -1721 685 C
ATOM 757 C MET A 106 27.125 75.337 194.762 1.00 62.35 C
ANISOU 757 C MET A 106 6859 5979 10853 -81 -1456 523 C
ATOM 758 O MET A 106 26.956 76.469 194.307 1.00 59.98 O
ANISOU 758 O MET A 106 6571 5744 10474 -114 -1368 387 O
ATOM 759 CB MET A 106 29.246 75.152 196.069 1.00 65.37 C
ANISOU 759 CB MET A 106 7163 6318 11355 -113 -1959 733 C
ATOM 760 CG MET A 106 29.941 75.700 197.283 1.00 71.64 C
ANISOU 760 CG MET A 106 8091 7158 11972 -203 -2264 822 C
ATOM 761 SD MET A 106 31.726 75.532 197.119 1.00 78.39 S
ANISOU 761 SD MET A 106 8629 7929 13226 -182 -2564 911 S
ATOM 762 CE MET A 106 32.270 76.615 198.430 1.00 77.58 C
ANISOU 762 CE MET A 106 8741 7911 12825 -335 -2912 939 C
ATOM 763 N LEU A 107 26.828 74.205 194.073 1.00 59.22 N
ANISOU 763 N LEU A 107 6346 5496 10658 -15 -1345 540 N
ATOM 764 CA LEU A 107 26.198 74.187 192.741 1.00 57.45 C
ANISOU 764 CA LEU A 107 6033 5267 10529 12 -1122 393 C
ATOM 765 C LEU A 107 24.761 74.684 192.847 1.00 60.15 C
ANISOU 765 C LEU A 107 6531 5671 10654 -30 -969 352 C
ATOM 766 O LEU A 107 24.304 75.458 192.001 1.00 58.26 O
ANISOU 766 O LEU A 107 6268 5483 10386 -44 -849 228 O
ATOM 767 CB LEU A 107 26.198 72.775 192.121 1.00 58.13 C
ANISOU 767 CB LEU A 107 5994 5225 10868 76 -1061 410 C
ATOM 768 CG LEU A 107 27.529 72.124 191.782 1.00 64.68 C
ANISOU 768 CG LEU A 107 6622 5951 12005 142 -1144 429 C
ATOM 769 CD1 LEU A 107 27.399 70.626 191.817 1.00 66.17 C
ANISOU 769 CD1 LEU A 107 6753 5979 12408 200 -1132 512 C
ATOM 770 CD2 LEU A 107 28.015 72.541 190.421 1.00 67.01 C
ANISOU 770 CD2 LEU A 107 6775 6258 12426 159 -1001 250 C
ATOM 771 N ALA A 108 24.057 74.222 193.903 1.00 57.64 N
ANISOU 771 N ALA A 108 6363 5339 10198 -49 -970 475 N
ATOM 772 CA ALA A 108 22.676 74.570 194.216 1.00 57.17 C
ANISOU 772 CA ALA A 108 6437 5314 9970 -83 -803 466 C
ATOM 773 C ALA A 108 22.578 76.010 194.712 1.00 61.17 C
ANISOU 773 C ALA A 108 7076 5912 10254 -129 -785 392 C
ATOM 774 O ALA A 108 21.636 76.714 194.335 1.00 59.97 O
ANISOU 774 O ALA A 108 6936 5785 10065 -139 -622 308 O
ATOM 775 CB ALA A 108 22.126 73.616 195.254 1.00 59.38 C
ANISOU 775 CB ALA A 108 6839 5544 10181 -93 -790 637 C
ATOM 776 N MET A 109 23.558 76.451 195.539 1.00 58.94 N
ANISOU 776 N MET A 109 6883 5664 9848 -162 -966 422 N
ATOM 777 CA MET A 109 23.659 77.822 196.059 1.00 59.27 C
ANISOU 777 CA MET A 109 7064 5770 9688 -219 -981 328 C
ATOM 778 C MET A 109 23.770 78.813 194.897 1.00 61.19 C
ANISOU 778 C MET A 109 7162 6029 10060 -209 -912 180 C
ATOM 779 O MET A 109 23.119 79.849 194.928 1.00 60.68 O
ANISOU 779 O MET A 109 7175 5983 9898 -232 -789 89 O
ATOM 780 CB MET A 109 24.865 77.972 196.999 1.00 63.62 C
ANISOU 780 CB MET A 109 7702 6340 10130 -271 -1252 387 C
ATOM 781 CG MET A 109 24.585 77.551 198.422 1.00 69.57 C
ANISOU 781 CG MET A 109 8718 7111 10606 -322 -1312 514 C
ATOM 782 SD MET A 109 24.171 78.929 199.512 1.00 75.37 S
ANISOU 782 SD MET A 109 9777 7909 10951 -421 -1251 389 S
ATOM 783 CE MET A 109 25.787 79.696 199.703 1.00 73.30 C
ANISOU 783 CE MET A 109 9482 7666 10704 -492 -1610 338 C
ATOM 784 N ASN A 110 24.564 78.466 193.862 1.00 56.62 N
ANISOU 784 N ASN A 110 6375 5430 9709 -173 -971 164 N
ATOM 785 CA ASN A 110 24.748 79.263 192.653 1.00 54.99 C
ANISOU 785 CA ASN A 110 6034 5240 9619 -169 -899 53 C
ATOM 786 C ASN A 110 23.441 79.355 191.859 1.00 57.70 C
ANISOU 786 C ASN A 110 6366 5587 9970 -152 -704 10 C
ATOM 787 O ASN A 110 23.080 80.450 191.439 1.00 57.16 O
ANISOU 787 O ASN A 110 6301 5541 9877 -172 -631 -58 O
ATOM 788 CB ASN A 110 25.863 78.672 191.779 1.00 55.75 C
ANISOU 788 CB ASN A 110 5930 5308 9945 -133 -962 54 C
ATOM 789 CG ASN A 110 25.874 79.201 190.363 1.00 75.17 C
ANISOU 789 CG ASN A 110 8273 7789 12501 -130 -836 -42 C
ATOM 790 OD1 ASN A 110 25.404 78.548 189.429 1.00 68.68 O
ANISOU 790 OD1 ASN A 110 7396 6954 11747 -102 -725 -70 O
ATOM 791 ND2 ASN A 110 26.363 80.414 190.178 1.00 67.30 N
ANISOU 791 ND2 ASN A 110 7256 6820 11496 -171 -853 -91 N
ATOM 792 N ARG A 111 22.746 78.211 191.649 1.00 53.74 N
ANISOU 792 N ARG A 111 5839 5050 9529 -122 -639 60 N
ATOM 793 CA ARG A 111 21.490 78.136 190.897 1.00 52.33 C
ANISOU 793 CA ARG A 111 5628 4864 9392 -119 -499 36 C
ATOM 794 C ARG A 111 20.391 78.936 191.603 1.00 57.40 C
ANISOU 794 C ARG A 111 6377 5512 9919 -136 -387 43 C
ATOM 795 O ARG A 111 19.870 79.879 191.009 1.00 57.10 O
ANISOU 795 O ARG A 111 6304 5487 9906 -143 -319 -8 O
ATOM 796 CB ARG A 111 21.056 76.676 190.686 1.00 50.76 C
ANISOU 796 CB ARG A 111 5382 4603 9303 -98 -478 87 C
ATOM 797 CG ARG A 111 20.089 76.492 189.515 1.00 54.47 C
ANISOU 797 CG ARG A 111 5772 5060 9863 -111 -399 36 C
ATOM 798 CD ARG A 111 19.260 75.227 189.637 1.00 55.92 C
ANISOU 798 CD ARG A 111 5938 5162 10145 -113 -362 94 C
ATOM 799 NE ARG A 111 18.217 75.362 190.655 1.00 56.83 N
ANISOU 799 NE ARG A 111 6125 5262 10205 -125 -270 185 N
ATOM 800 CZ ARG A 111 16.925 75.523 190.393 1.00 67.65 C
ANISOU 800 CZ ARG A 111 7448 6612 11642 -147 -176 197 C
ATOM 801 NH1 ARG A 111 16.055 75.670 191.382 1.00 59.89 N
ANISOU 801 NH1 ARG A 111 6522 5606 10627 -152 -49 279 N
ATOM 802 NH2 ARG A 111 16.494 75.552 189.137 1.00 47.14 N
ANISOU 802 NH2 ARG A 111 4749 4016 9147 -172 -208 133 N
ATOM 803 N GLN A 112 20.077 78.595 192.874 1.00 55.13 N
ANISOU 803 N GLN A 112 6226 5209 9512 -144 -358 114 N
ATOM 804 CA GLN A 112 19.054 79.287 193.667 1.00 55.76 C
ANISOU 804 CA GLN A 112 6426 5280 9480 -157 -198 109 C
ATOM 805 C GLN A 112 19.421 80.765 193.873 1.00 59.50 C
ANISOU 805 C GLN A 112 6972 5776 9861 -178 -201 6 C
ATOM 806 O GLN A 112 18.559 81.631 193.708 1.00 58.94 O
ANISOU 806 O GLN A 112 6888 5677 9831 -169 -55 -43 O
ATOM 807 CB GLN A 112 18.825 78.585 195.016 1.00 58.82 C
ANISOU 807 CB GLN A 112 6984 5655 9711 -174 -157 209 C
ATOM 808 CG GLN A 112 17.865 77.394 194.939 1.00 76.94 C
ANISOU 808 CG GLN A 112 9213 7893 12126 -161 -51 316 C
ATOM 809 CD GLN A 112 16.390 77.759 194.908 1.00100.57 C
ANISOU 809 CD GLN A 112 12168 10847 15198 -158 184 312 C
ATOM 810 OE1 GLN A 112 15.985 78.924 195.045 1.00 95.43 O
ANISOU 810 OE1 GLN A 112 11552 10201 14507 -155 299 232 O
ATOM 811 NE2 GLN A 112 15.544 76.750 194.748 1.00 95.42 N
ANISOU 811 NE2 GLN A 112 11424 10133 14697 -159 263 405 N
ATOM 812 N GLY A 113 20.698 81.025 194.174 1.00 55.79 N
ANISOU 812 N GLY A 113 6550 5336 9313 -205 -374 -22 N
ATOM 813 CA GLY A 113 21.250 82.363 194.361 1.00 55.59 C
ANISOU 813 CA GLY A 113 6585 5315 9224 -241 -418 -125 C
ATOM 814 C GLY A 113 21.079 83.227 193.130 1.00 57.93 C
ANISOU 814 C GLY A 113 6728 5596 9688 -225 -365 -182 C
ATOM 815 O GLY A 113 20.575 84.345 193.241 1.00 58.77 O
ANISOU 815 O GLY A 113 6878 5661 9789 -232 -262 -250 O
ATOM 816 N SER A 114 21.441 82.697 191.939 1.00 52.20 N
ANISOU 816 N SER A 114 5832 4893 9109 -204 -419 -151 N
ATOM 817 CA SER A 114 21.273 83.412 190.670 1.00 50.76 C
ANISOU 817 CA SER A 114 5525 4711 9051 -201 -379 -175 C
ATOM 818 C SER A 114 19.792 83.671 190.386 1.00 53.84 C
ANISOU 818 C SER A 114 5892 5066 9497 -178 -235 -153 C
ATOM 819 O SER A 114 19.445 84.780 189.987 1.00 53.89 O
ANISOU 819 O SER A 114 5868 5040 9568 -181 -187 -172 O
ATOM 820 CB SER A 114 21.902 82.646 189.510 1.00 53.75 C
ANISOU 820 CB SER A 114 5770 5125 9526 -194 -438 -156 C
ATOM 821 OG SER A 114 23.318 82.640 189.594 1.00 63.62 O
ANISOU 821 OG SER A 114 6984 6389 10800 -210 -550 -173 O
ATOM 822 N ILE A 115 18.916 82.675 190.649 1.00 49.14 N
ANISOU 822 N ILE A 115 5300 4460 8912 -157 -171 -100 N
ATOM 823 CA ILE A 115 17.472 82.803 190.439 1.00 48.33 C
ANISOU 823 CA ILE A 115 5137 4310 8915 -138 -42 -61 C
ATOM 824 C ILE A 115 16.923 83.953 191.307 1.00 52.16 C
ANISOU 824 C ILE A 115 5705 4732 9381 -126 102 -103 C
ATOM 825 O ILE A 115 16.276 84.855 190.772 1.00 51.83 O
ANISOU 825 O ILE A 115 5578 4639 9478 -109 160 -99 O
ATOM 826 CB ILE A 115 16.735 81.451 190.685 1.00 51.22 C
ANISOU 826 CB ILE A 115 5483 4661 9319 -130 2 9 C
ATOM 827 CG1 ILE A 115 16.959 80.492 189.498 1.00 50.57 C
ANISOU 827 CG1 ILE A 115 5292 4605 9318 -144 -114 23 C
ATOM 828 CG2 ILE A 115 15.227 81.648 190.944 1.00 52.48 C
ANISOU 828 CG2 ILE A 115 5588 4750 9601 -113 171 56 C
ATOM 829 CD1 ILE A 115 16.785 79.010 189.809 1.00 54.65 C
ANISOU 829 CD1 ILE A 115 5809 5092 9862 -145 -118 72 C
ATOM 830 N ILE A 116 17.230 83.936 192.618 1.00 48.90 N
ANISOU 830 N ILE A 116 5469 4316 8795 -138 150 -144 N
ATOM 831 CA ILE A 116 16.770 84.922 193.595 1.00 49.63 C
ANISOU 831 CA ILE A 116 5695 4340 8821 -135 317 -222 C
ATOM 832 C ILE A 116 17.339 86.321 193.282 1.00 52.90 C
ANISOU 832 C ILE A 116 6108 4714 9276 -150 269 -315 C
ATOM 833 O ILE A 116 16.565 87.277 193.219 1.00 52.73 O
ANISOU 833 O ILE A 116 6050 4597 9387 -120 417 -349 O
ATOM 834 CB ILE A 116 17.112 84.450 195.046 1.00 53.98 C
ANISOU 834 CB ILE A 116 6486 4918 9106 -170 344 -243 C
ATOM 835 CG1 ILE A 116 16.166 83.303 195.486 1.00 54.72 C
ANISOU 835 CG1 ILE A 116 6584 5008 9198 -153 486 -137 C
ATOM 836 CG2 ILE A 116 17.079 85.609 196.063 1.00 56.28 C
ANISOU 836 CG2 ILE A 116 6982 5151 9250 -195 471 -381 C
ATOM 837 CD1 ILE A 116 16.730 82.332 196.534 1.00 59.88 C
ANISOU 837 CD1 ILE A 116 7429 5716 9606 -194 416 -76 C
ATOM 838 N PHE A 117 18.662 86.440 193.071 1.00 48.72 N
ANISOU 838 N PHE A 117 5596 4238 8677 -193 73 -344 N
ATOM 839 CA PHE A 117 19.275 87.744 192.853 1.00 48.62 C
ANISOU 839 CA PHE A 117 5585 4174 8715 -222 25 -426 C
ATOM 840 C PHE A 117 19.009 88.308 191.454 1.00 53.56 C
ANISOU 840 C PHE A 117 6016 4774 9559 -199 19 -362 C
ATOM 841 O PHE A 117 19.054 89.534 191.316 1.00 53.70 O
ANISOU 841 O PHE A 117 6026 4705 9674 -208 50 -408 O
ATOM 842 CB PHE A 117 20.766 87.739 193.197 1.00 50.08 C
ANISOU 842 CB PHE A 117 5837 4407 8783 -288 -179 -470 C
ATOM 843 CG PHE A 117 20.941 87.743 194.702 1.00 52.67 C
ANISOU 843 CG PHE A 117 6410 4727 8875 -333 -183 -555 C
ATOM 844 CD1 PHE A 117 20.711 88.899 195.444 1.00 56.87 C
ANISOU 844 CD1 PHE A 117 7101 5165 9344 -365 -83 -695 C
ATOM 845 CD2 PHE A 117 21.255 86.573 195.384 1.00 54.06 C
ANISOU 845 CD2 PHE A 117 6676 4980 8883 -347 -275 -491 C
ATOM 846 CE1 PHE A 117 20.832 88.891 196.837 1.00 59.67 C
ANISOU 846 CE1 PHE A 117 7729 5520 9423 -423 -79 -789 C
ATOM 847 CE2 PHE A 117 21.380 86.568 196.776 1.00 58.88 C
ANISOU 847 CE2 PHE A 117 7548 5595 9227 -404 -292 -548 C
ATOM 848 CZ PHE A 117 21.171 87.727 197.493 1.00 58.87 C
ANISOU 848 CZ PHE A 117 7732 5518 9119 -447 -194 -705 C
ATOM 849 N LEU A 118 18.641 87.468 190.452 1.00 50.09 N
ANISOU 849 N LEU A 118 5439 4396 9197 -176 -15 -256 N
ATOM 850 CA LEU A 118 18.255 88.013 189.141 1.00 49.98 C
ANISOU 850 CA LEU A 118 5277 4365 9349 -168 -33 -179 C
ATOM 851 C LEU A 118 16.878 88.668 189.277 1.00 55.77 C
ANISOU 851 C LEU A 118 5958 4986 10245 -120 113 -149 C
ATOM 852 O LEU A 118 16.626 89.700 188.650 1.00 56.52 O
ANISOU 852 O LEU A 118 5973 5008 10496 -113 115 -106 O
ATOM 853 CB LEU A 118 18.245 86.958 188.020 1.00 49.03 C
ANISOU 853 CB LEU A 118 5059 4339 9233 -176 -124 -97 C
ATOM 854 CG LEU A 118 19.565 86.682 187.294 1.00 52.69 C
ANISOU 854 CG LEU A 118 5505 4883 9631 -217 -237 -106 C
ATOM 855 CD1 LEU A 118 19.501 85.358 186.563 1.00 52.27 C
ANISOU 855 CD1 LEU A 118 5409 4904 9547 -219 -282 -77 C
ATOM 856 CD2 LEU A 118 19.919 87.797 186.316 1.00 54.54 C
ANISOU 856 CD2 LEU A 118 5684 5105 9936 -249 -262 -64 C
ATOM 857 N THR A 119 16.014 88.086 190.148 1.00 52.72 N
ANISOU 857 N THR A 119 5613 4573 9845 -87 248 -162 N
ATOM 858 CA THR A 119 14.669 88.580 190.465 1.00 53.95 C
ANISOU 858 CA THR A 119 5703 4606 10189 -31 437 -141 C
ATOM 859 C THR A 119 14.786 89.909 191.216 1.00 59.28 C
ANISOU 859 C THR A 119 6478 5155 10890 -19 568 -260 C
ATOM 860 O THR A 119 14.105 90.862 190.842 1.00 60.14 O
ANISOU 860 O THR A 119 6472 5137 11242 24 645 -226 O
ATOM 861 CB THR A 119 13.864 87.526 191.264 1.00 62.77 C
ANISOU 861 CB THR A 119 6848 5732 11270 -11 577 -125 C
ATOM 862 OG1 THR A 119 13.849 86.288 190.554 1.00 59.13 O
ANISOU 862 OG1 THR A 119 6301 5365 10799 -34 438 -33 O
ATOM 863 CG2 THR A 119 12.432 87.961 191.552 1.00 63.36 C
ANISOU 863 CG2 THR A 119 6812 5669 11593 50 805 -91 C
ATOM 864 N VAL A 120 15.670 89.979 192.244 1.00 55.89 N
ANISOU 864 N VAL A 120 6262 4749 10223 -61 572 -396 N
ATOM 865 CA VAL A 120 15.909 91.175 193.072 1.00 56.92 C
ANISOU 865 CA VAL A 120 6541 4759 10328 -74 679 -553 C
ATOM 866 C VAL A 120 16.374 92.331 192.178 1.00 60.45 C
ANISOU 866 C VAL A 120 6881 5128 10959 -86 577 -537 C
ATOM 867 O VAL A 120 15.931 93.464 192.376 1.00 61.57 O
ANISOU 867 O VAL A 120 7021 5101 11273 -56 715 -603 O
ATOM 868 CB VAL A 120 16.896 90.896 194.240 1.00 61.09 C
ANISOU 868 CB VAL A 120 7330 5354 10529 -148 618 -685 C
ATOM 869 CG1 VAL A 120 17.214 92.164 195.027 1.00 62.83 C
ANISOU 869 CG1 VAL A 120 7724 5442 10705 -185 694 -874 C
ATOM 870 CG2 VAL A 120 16.332 89.837 195.176 1.00 61.58 C
ANISOU 870 CG2 VAL A 120 7517 5475 10405 -139 747 -674 C
ATOM 871 N VAL A 121 17.208 92.027 191.164 1.00 55.19 N
ANISOU 871 N VAL A 121 6121 4571 10278 -125 361 -441 N
ATOM 872 CA VAL A 121 17.712 92.990 190.180 1.00 54.61 C
ANISOU 872 CA VAL A 121 5943 4447 10361 -150 260 -382 C
ATOM 873 C VAL A 121 16.530 93.527 189.336 1.00 59.41 C
ANISOU 873 C VAL A 121 6373 4952 11249 -85 329 -244 C
ATOM 874 O VAL A 121 16.416 94.743 189.162 1.00 60.66 O
ANISOU 874 O VAL A 121 6488 4954 11605 -73 372 -241 O
ATOM 875 CB VAL A 121 18.833 92.348 189.321 1.00 56.51 C
ANISOU 875 CB VAL A 121 6135 4842 10495 -207 63 -309 C
ATOM 876 CG1 VAL A 121 18.983 93.027 187.966 1.00 55.97 C
ANISOU 876 CG1 VAL A 121 5928 4755 10583 -224 -9 -174 C
ATOM 877 CG2 VAL A 121 20.158 92.349 190.073 1.00 56.50 C
ANISOU 877 CG2 VAL A 121 6257 4874 10336 -277 -34 -430 C
ATOM 878 N ALA A 122 15.636 92.626 188.872 1.00 55.23 N
ANISOU 878 N ALA A 122 5735 4490 10759 -47 327 -127 N
ATOM 879 CA ALA A 122 14.449 92.961 188.077 1.00 55.60 C
ANISOU 879 CA ALA A 122 5592 4453 11083 7 342 31 C
ATOM 880 C ALA A 122 13.424 93.777 188.886 1.00 61.10 C
ANISOU 880 C ALA A 122 6251 4940 12022 87 577 -25 C
ATOM 881 O ALA A 122 12.830 94.699 188.327 1.00 62.09 O
ANISOU 881 O ALA A 122 6230 4920 12442 129 585 82 O
ATOM 882 CB ALA A 122 13.803 91.692 187.540 1.00 55.59 C
ANISOU 882 CB ALA A 122 5498 4571 11052 7 265 139 C
ATOM 883 N VAL A 123 13.229 93.451 190.189 1.00 58.06 N
ANISOU 883 N VAL A 123 6006 4532 11520 106 777 -184 N
ATOM 884 CA VAL A 123 12.305 94.165 191.089 1.00 60.28 C
ANISOU 884 CA VAL A 123 6291 4613 12001 181 1067 -279 C
ATOM 885 C VAL A 123 12.879 95.567 191.369 1.00 66.59 C
ANISOU 885 C VAL A 123 7182 5248 12871 172 1116 -409 C
ATOM 886 O VAL A 123 12.123 96.541 191.390 1.00 68.61 O
ANISOU 886 O VAL A 123 7330 5285 13452 245 1278 -408 O
ATOM 887 CB VAL A 123 12.005 93.371 192.398 1.00 64.35 C
ANISOU 887 CB VAL A 123 6977 5169 12306 185 1285 -411 C
ATOM 888 CG1 VAL A 123 11.189 94.196 193.396 1.00 66.58 C
ANISOU 888 CG1 VAL A 123 7310 5236 12750 253 1638 -553 C
ATOM 889 CG2 VAL A 123 11.288 92.061 192.092 1.00 63.19 C
ANISOU 889 CG2 VAL A 123 6700 5135 12175 197 1258 -265 C
ATOM 890 N ASP A 124 14.214 95.663 191.547 1.00 62.64 N
ANISOU 890 N ASP A 124 6857 4834 12108 81 968 -513 N
ATOM 891 CA ASP A 124 14.924 96.923 191.771 1.00 63.65 C
ANISOU 891 CA ASP A 124 7077 4814 12294 43 967 -641 C
ATOM 892 C ASP A 124 14.699 97.861 190.591 1.00 67.77 C
ANISOU 892 C ASP A 124 7382 5206 13160 74 886 -464 C
ATOM 893 O ASP A 124 14.344 99.017 190.811 1.00 69.38 O
ANISOU 893 O ASP A 124 7562 5171 13627 116 1026 -526 O
ATOM 894 CB ASP A 124 16.432 96.681 191.993 1.00 64.52 C
ANISOU 894 CB ASP A 124 7354 5064 12097 -73 763 -733 C
ATOM 895 CG ASP A 124 17.251 97.946 192.175 1.00 76.93 C
ANISOU 895 CG ASP A 124 9004 6480 13745 -136 724 -859 C
ATOM 896 OD1 ASP A 124 17.368 98.416 193.326 1.00 80.40 O
ANISOU 896 OD1 ASP A 124 9653 6812 14084 -166 845 -1090 O
ATOM 897 OD2 ASP A 124 17.773 98.466 191.164 1.00 81.61 O
ANISOU 897 OD2 ASP A 124 9463 7054 14492 -166 578 -728 O
ATOM 898 N ARG A 125 14.871 97.363 189.344 1.00 62.74 N
ANISOU 898 N ARG A 125 6601 4718 12521 52 669 -243 N
ATOM 899 CA ARG A 125 14.678 98.197 188.160 1.00 63.36 C
ANISOU 899 CA ARG A 125 6499 4698 12878 64 563 -35 C
ATOM 900 C ARG A 125 13.185 98.471 187.909 1.00 68.61 C
ANISOU 900 C ARG A 125 6960 5207 13902 173 668 103 C
ATOM 901 O ARG A 125 12.863 99.525 187.362 1.00 69.06 O
ANISOU 901 O ARG A 125 6886 5077 14277 208 655 229 O
ATOM 902 CB ARG A 125 15.361 97.617 186.914 1.00 62.01 C
ANISOU 902 CB ARG A 125 6280 4734 12546 -10 316 145 C
ATOM 903 CG ARG A 125 15.751 98.735 185.940 1.00 77.17 C
ANISOU 903 CG ARG A 125 8119 6550 14651 -45 213 306 C
ATOM 904 CD ARG A 125 17.072 98.537 185.221 1.00 83.40 C
ANISOU 904 CD ARG A 125 8966 7502 15221 -153 58 354 C
ATOM 905 NE ARG A 125 18.225 98.481 186.124 1.00 85.00 N
ANISOU 905 NE ARG A 125 9316 7734 15248 -214 84 132 N
ATOM 906 CZ ARG A 125 19.470 98.785 185.769 1.00 96.44 C
ANISOU 906 CZ ARG A 125 10789 9220 16634 -307 -2 139 C
ATOM 907 NH1 ARG A 125 19.735 99.204 184.537 1.00 81.77 N
ANISOU 907 NH1 ARG A 125 8844 7376 14850 -349 -82 351 N
ATOM 908 NH2 ARG A 125 20.461 98.676 186.644 1.00 82.41 N
ANISOU 908 NH2 ARG A 125 9123 7464 14724 -365 -13 -55 N
ATOM 909 N TYR A 126 12.283 97.556 188.345 1.00 65.50 N
ANISOU 909 N TYR A 126 6525 4870 13493 226 776 90 N
ATOM 910 CA TYR A 126 10.826 97.730 188.226 1.00 67.00 C
ANISOU 910 CA TYR A 126 6488 4902 14067 331 894 216 C
ATOM 911 C TYR A 126 10.391 98.936 189.038 1.00 73.38 C
ANISOU 911 C TYR A 126 7291 5413 15179 414 1172 80 C
ATOM 912 O TYR A 126 9.618 99.754 188.542 1.00 75.67 O
ANISOU 912 O TYR A 126 7362 5494 15896 491 1191 233 O
ATOM 913 CB TYR A 126 10.065 96.463 188.675 1.00 67.61 C
ANISOU 913 CB TYR A 126 6534 5094 14060 354 986 204 C
ATOM 914 CG TYR A 126 8.555 96.602 188.710 1.00 71.27 C
ANISOU 914 CG TYR A 126 6740 5380 14959 460 1143 318 C
ATOM 915 CD1 TYR A 126 7.799 96.524 187.545 1.00 73.63 C
ANISOU 915 CD1 TYR A 126 6772 5672 15534 474 924 594 C
ATOM 916 CD2 TYR A 126 7.879 96.762 189.918 1.00 73.77 C
ANISOU 916 CD2 TYR A 126 7081 5540 15409 539 1512 152 C
ATOM 917 CE1 TYR A 126 6.409 96.632 187.575 1.00 76.25 C
ANISOU 917 CE1 TYR A 126 6823 5827 16319 569 1044 718 C
ATOM 918 CE2 TYR A 126 6.490 96.876 189.959 1.00 76.80 C
ANISOU 918 CE2 TYR A 126 7190 5744 16246 642 1689 261 C
ATOM 919 CZ TYR A 126 5.759 96.809 188.785 1.00 84.46 C
ANISOU 919 CZ TYR A 126 7854 6697 17540 660 1441 552 C
ATOM 920 OH TYR A 126 4.390 96.913 188.811 1.00 88.94 O
ANISOU 920 OH TYR A 126 8109 7075 18608 759 1588 681 O
ATOM 921 N PHE A 127 10.913 99.061 190.269 1.00 69.61 N
ANISOU 921 N PHE A 127 7062 4905 14483 392 1374 -207 N
ATOM 922 CA PHE A 127 10.594 100.180 191.141 1.00 72.18 C
ANISOU 922 CA PHE A 127 7444 4943 15040 456 1668 -401 C
ATOM 923 C PHE A 127 11.303 101.458 190.692 1.00 76.74 C
ANISOU 923 C PHE A 127 8024 5351 15780 424 1561 -397 C
ATOM 924 O PHE A 127 10.784 102.532 190.951 1.00 79.25 O
ANISOU 924 O PHE A 127 8273 5372 16467 502 1758 -456 O
ATOM 925 CB PHE A 127 10.902 99.850 192.606 1.00 74.62 C
ANISOU 925 CB PHE A 127 8061 5288 15003 420 1905 -715 C
ATOM 926 CG PHE A 127 9.755 99.125 193.270 1.00 77.47 C
ANISOU 926 CG PHE A 127 8375 5645 15414 498 2187 -735 C
ATOM 927 CD1 PHE A 127 8.746 99.830 193.916 1.00 83.82 C
ANISOU 927 CD1 PHE A 127 9115 6174 16558 607 2568 -843 C
ATOM 928 CD2 PHE A 127 9.659 97.739 193.211 1.00 77.69 C
ANISOU 928 CD2 PHE A 127 8402 5924 15192 464 2092 -636 C
ATOM 929 CE1 PHE A 127 7.671 99.161 194.508 1.00 86.16 C
ANISOU 929 CE1 PHE A 127 9344 6459 16933 677 2863 -846 C
ATOM 930 CE2 PHE A 127 8.584 97.070 193.804 1.00 81.84 C
ANISOU 930 CE2 PHE A 127 8864 6433 15796 527 2363 -633 C
ATOM 931 CZ PHE A 127 7.597 97.785 194.448 1.00 83.28 C
ANISOU 931 CZ PHE A 127 8978 6353 16311 631 2753 -732 C
ATOM 932 N ARG A 128 12.442 101.363 189.984 1.00 71.10 N
ANISOU 932 N ARG A 128 7369 4803 14843 316 1269 -314 N
ATOM 933 CA ARG A 128 13.132 102.565 189.505 1.00 71.58 C
ANISOU 933 CA ARG A 128 7417 4700 15080 274 1169 -280 C
ATOM 934 C ARG A 128 12.415 103.176 188.300 1.00 76.09 C
ANISOU 934 C ARG A 128 7705 5134 16071 341 1063 43 C
ATOM 935 O ARG A 128 12.364 104.401 188.196 1.00 78.35 O
ANISOU 935 O ARG A 128 7926 5144 16701 371 1120 63 O
ATOM 936 CB ARG A 128 14.604 102.293 189.168 1.00 70.09 C
ANISOU 936 CB ARG A 128 7365 4718 14547 132 926 -290 C
ATOM 937 CG ARG A 128 15.480 102.056 190.397 1.00 84.90 C
ANISOU 937 CG ARG A 128 9520 6657 16082 50 985 -605 C
ATOM 938 CD ARG A 128 16.920 102.506 190.214 1.00103.09 C
ANISOU 938 CD ARG A 128 11914 8987 18267 -82 796 -650 C
ATOM 939 NE ARG A 128 17.583 101.872 189.071 1.00115.67 N
ANISOU 939 NE ARG A 128 13404 10812 19731 -140 557 -419 N
ATOM 940 CZ ARG A 128 18.880 101.981 188.801 1.00131.90 C
ANISOU 940 CZ ARG A 128 15502 12945 21668 -256 394 -422 C
ATOM 941 NH1 ARG A 128 19.677 102.678 189.603 1.00123.84 N
ANISOU 941 NH1 ARG A 128 14618 11795 20640 -338 398 -638 N
ATOM 942 NH2 ARG A 128 19.393 101.386 187.734 1.00114.81 N
ANISOU 942 NH2 ARG A 128 13245 10981 19398 -298 234 -217 N
ATOM 943 N VAL A 129 11.835 102.333 187.422 1.00 70.84 N
ANISOU 943 N VAL A 129 6879 4648 15391 358 900 295 N
ATOM 944 CA VAL A 129 11.139 102.750 186.199 1.00 71.66 C
ANISOU 944 CA VAL A 129 6726 4667 15833 400 728 641 C
ATOM 945 C VAL A 129 9.644 103.034 186.470 1.00 79.42 C
ANISOU 945 C VAL A 129 7472 5413 17290 548 909 708 C
ATOM 946 O VAL A 129 9.187 104.142 186.192 1.00 81.76 O
ANISOU 946 O VAL A 129 7605 5425 18037 620 941 834 O
ATOM 947 CB VAL A 129 11.326 101.711 185.049 1.00 72.79 C
ANISOU 947 CB VAL A 129 6840 5123 15693 319 425 871 C
ATOM 948 CG1 VAL A 129 10.459 102.040 183.834 1.00 73.93 C
ANISOU 948 CG1 VAL A 129 6741 5199 16152 351 218 1237 C
ATOM 949 CG2 VAL A 129 12.792 101.597 184.639 1.00 70.64 C
ANISOU 949 CG2 VAL A 129 6754 5039 15048 185 277 840 C
ATOM 950 N VAL A 130 8.892 102.044 186.983 1.00 76.84 N
ANISOU 950 N VAL A 130 7107 5186 16902 593 1029 641 N
ATOM 951 CA VAL A 130 7.443 102.156 187.189 1.00 79.79 C
ANISOU 951 CA VAL A 130 7215 5355 17749 728 1205 727 C
ATOM 952 C VAL A 130 7.095 103.080 188.384 1.00 88.71 C
ANISOU 952 C VAL A 130 8378 6161 19169 834 1622 466 C
ATOM 953 O VAL A 130 6.215 103.929 188.227 1.00 91.59 O
ANISOU 953 O VAL A 130 8489 6223 20086 952 1728 587 O
ATOM 954 CB VAL A 130 6.758 100.765 187.299 1.00 82.20 C
ANISOU 954 CB VAL A 130 7450 5866 17915 727 1201 759 C
ATOM 955 CG1 VAL A 130 5.239 100.889 187.390 1.00 84.91 C
ANISOU 955 CG1 VAL A 130 7459 5988 18813 860 1360 892 C
ATOM 956 CG2 VAL A 130 7.134 99.885 186.110 1.00 79.52 C
ANISOU 956 CG2 VAL A 130 7109 5823 17282 615 800 978 C
ATOM 957 N HIS A 131 7.776 102.949 189.543 1.00 86.08 N
ANISOU 957 N HIS A 131 8355 5874 18479 789 1848 115 N
ATOM 958 CA HIS A 131 7.483 103.795 190.714 1.00 89.49 C
ANISOU 958 CA HIS A 131 8879 6006 19115 869 2260 -177 C
ATOM 959 C HIS A 131 8.724 104.622 191.147 1.00 93.55 C
ANISOU 959 C HIS A 131 9687 6450 19409 776 2255 -422 C
ATOM 960 O HIS A 131 9.275 104.341 192.213 1.00 92.84 O
ANISOU 960 O HIS A 131 9905 6441 18929 711 2411 -732 O
ATOM 961 CB HIS A 131 6.977 102.929 191.887 1.00 90.89 C
ANISOU 961 CB HIS A 131 9188 6265 19081 894 2589 -400 C
ATOM 962 CG HIS A 131 5.929 101.933 191.509 1.00 94.23 C
ANISOU 962 CG HIS A 131 9349 6800 19653 948 2565 -175 C
ATOM 963 ND1 HIS A 131 6.267 100.659 191.090 1.00 93.06 N
ANISOU 963 ND1 HIS A 131 9249 6994 19114 853 2298 -61 N
ATOM 964 CD2 HIS A 131 4.581 102.051 191.509 1.00 98.96 C
ANISOU 964 CD2 HIS A 131 9630 7191 20779 1082 2777 -53 C
ATOM 965 CE1 HIS A 131 5.120 100.044 190.853 1.00 93.38 C
ANISOU 965 CE1 HIS A 131 9015 7028 19437 919 2341 119 C
ATOM 966 NE2 HIS A 131 4.077 100.842 191.087 1.00 97.24 N
ANISOU 966 NE2 HIS A 131 9263 7196 20489 1057 2620 140 N
ATOM 967 N PRO A 132 9.182 105.645 190.374 1.00 91.13 N
ANISOU 967 N PRO A 132 9296 5985 19345 758 2071 -284 N
ATOM 968 CA PRO A 132 10.416 106.366 190.757 1.00 91.31 C
ANISOU 968 CA PRO A 132 9579 5946 19167 648 2038 -509 C
ATOM 969 C PRO A 132 10.385 107.128 192.089 1.00 99.05 C
ANISOU 969 C PRO A 132 10775 6651 20208 672 2408 -912 C
ATOM 970 O PRO A 132 11.457 107.409 192.629 1.00 98.27 O
ANISOU 970 O PRO A 132 10955 6573 19811 548 2364 -1155 O
ATOM 971 CB PRO A 132 10.622 107.350 189.602 1.00 93.68 C
ANISOU 971 CB PRO A 132 9683 6077 19834 646 1814 -225 C
ATOM 972 CG PRO A 132 9.890 106.756 188.457 1.00 96.95 C
ANISOU 972 CG PRO A 132 9818 6634 20384 695 1593 170 C
ATOM 973 CD PRO A 132 8.683 106.124 189.069 1.00 93.37 C
ANISOU 973 CD PRO A 132 9255 6162 20058 812 1841 109 C
ATOM 974 N HIS A 133 9.192 107.449 192.622 1.00 99.53 N
ANISOU 974 N HIS A 133 10715 6453 20650 821 2772 -992 N
ATOM 975 CA HIS A 133 9.060 108.200 193.876 1.00103.18 C
ANISOU 975 CA HIS A 133 11396 6627 21182 852 3180 -1398 C
ATOM 976 C HIS A 133 8.745 107.291 195.089 1.00108.43 C
ANISOU 976 C HIS A 133 12309 7451 21438 844 3479 -1669 C
ATOM 977 O HIS A 133 8.410 107.804 196.161 1.00111.51 O
ANISOU 977 O HIS A 133 12885 7609 21875 882 3884 -2004 O
ATOM 978 CB HIS A 133 7.990 109.299 193.730 1.00107.87 C
ANISOU 978 CB HIS A 133 11704 6768 22513 1028 3452 -1340 C
ATOM 979 CG HIS A 133 8.208 110.204 192.556 1.00111.40 C
ANISOU 979 CG HIS A 133 11904 7036 23387 1041 3166 -1034 C
ATOM 980 ND1 HIS A 133 9.305 111.043 192.483 1.00113.28 N
ANISOU 980 ND1 HIS A 133 12314 7167 23561 925 3016 -1141 N
ATOM 981 CD2 HIS A 133 7.456 110.370 191.443 1.00113.45 C
ANISOU 981 CD2 HIS A 133 11767 7207 24130 1146 2999 -614 C
ATOM 982 CE1 HIS A 133 9.191 111.683 191.332 1.00113.08 C
ANISOU 982 CE1 HIS A 133 12001 6994 23969 965 2788 -777 C
ATOM 983 NE2 HIS A 133 8.092 111.314 190.673 1.00113.60 N
ANISOU 983 NE2 HIS A 133 11731 7071 24362 1096 2757 -448 N
ATOM 984 N HIS A 134 8.896 105.957 194.933 1.00102.33 N
ANISOU 984 N HIS A 134 11565 7065 20249 784 3289 -1534 N
ATOM 985 CA HIS A 134 8.645 104.976 195.996 1.00102.55 C
ANISOU 985 CA HIS A 134 11824 7276 19865 762 3529 -1726 C
ATOM 986 C HIS A 134 9.824 104.913 196.990 1.00107.03 C
ANISOU 986 C HIS A 134 12860 7971 19835 597 3489 -2061 C
ATOM 987 O HIS A 134 10.951 105.276 196.639 1.00105.25 O
ANISOU 987 O HIS A 134 12728 7796 19465 482 3170 -2070 O
ATOM 988 CB HIS A 134 8.358 103.587 195.397 1.00100.09 C
ANISOU 988 CB HIS A 134 11345 7297 19388 759 3318 -1434 C
ATOM 989 CG HIS A 134 7.679 102.645 196.341 1.00104.32 C
ANISOU 989 CG HIS A 134 11992 7940 19704 783 3631 -1543 C
ATOM 990 ND1 HIS A 134 8.366 101.604 196.940 1.00104.18 N
ANISOU 990 ND1 HIS A 134 12274 8231 19080 661 3534 -1636 N
ATOM 991 CD2 HIS A 134 6.395 102.624 196.769 1.00108.95 C
ANISOU 991 CD2 HIS A 134 12417 8351 20629 914 4043 -1553 C
ATOM 992 CE1 HIS A 134 7.481 100.982 197.702 1.00105.28 C
ANISOU 992 CE1 HIS A 134 12444 8379 19180 714 3886 -1692 C
ATOM 993 NE2 HIS A 134 6.282 101.561 197.633 1.00108.55 N
ANISOU 993 NE2 HIS A 134 12582 8508 20153 864 4216 -1652 N
ATOM 994 N ALA A 135 9.543 104.461 198.232 1.00105.90 N
ANISOU 994 N ALA A 135 13007 7872 19360 580 3814 -2323 N
ATOM 995 CA ALA A 135 10.489 104.343 199.348 1.00106.62 C
ANISOU 995 CA ALA A 135 13577 8078 18856 420 3806 -2649 C
ATOM 996 C ALA A 135 11.618 103.330 199.095 1.00106.90 C
ANISOU 996 C ALA A 135 13724 8498 18397 275 3348 -2517 C
ATOM 997 O ALA A 135 12.717 103.516 199.624 1.00106.89 O
ANISOU 997 O ALA A 135 14028 8559 18026 124 3163 -2716 O
ATOM 998 CB ALA A 135 9.743 103.959 200.616 1.00110.38 C
ANISOU 998 CB ALA A 135 14309 8536 19096 446 4275 -2884 C
ATOM 999 N LEU A 136 11.354 102.267 198.302 1.00100.12 N
ANISOU 999 N LEU A 136 12612 7875 17552 315 3164 -2193 N
ATOM 1000 CA LEU A 136 12.333 101.215 197.991 1.00 96.31 C
ANISOU 1000 CA LEU A 136 12193 7737 16663 201 2765 -2052 C
ATOM 1001 C LEU A 136 13.476 101.719 197.082 1.00 98.20 C
ANISOU 1001 C LEU A 136 12345 8002 16966 119 2364 -1956 C
ATOM 1002 O LEU A 136 14.502 101.043 196.964 1.00 95.81 O
ANISOU 1002 O LEU A 136 12132 7941 16330 9 2052 -1904 O
ATOM 1003 CB LEU A 136 11.650 99.988 197.353 1.00 93.88 C
ANISOU 1003 CB LEU A 136 11633 7631 16404 270 2712 -1754 C
ATOM 1004 CG LEU A 136 10.655 99.201 198.225 1.00100.19 C
ANISOU 1004 CG LEU A 136 12511 8468 17089 324 3066 -1799 C
ATOM 1005 CD1 LEU A 136 9.846 98.236 197.387 1.00 98.35 C
ANISOU 1005 CD1 LEU A 136 11942 8353 17073 401 3004 -1487 C
ATOM 1006 CD2 LEU A 136 11.358 98.434 199.341 1.00102.88 C
ANISOU 1006 CD2 LEU A 136 13254 9015 16820 197 3044 -1962 C
ATOM 1007 N ASN A 137 13.304 102.900 196.457 1.00 95.53 N
ANISOU 1007 N ASN A 137 11821 7399 17076 174 2388 -1921 N
ATOM 1008 CA ASN A 137 14.307 103.525 195.590 1.00 93.88 C
ANISOU 1008 CA ASN A 137 11519 7168 16982 98 2065 -1819 C
ATOM 1009 C ASN A 137 15.381 104.222 196.418 1.00 99.10 C
ANISOU 1009 C ASN A 137 12488 7740 17425 -45 2002 -2124 C
ATOM 1010 O ASN A 137 16.561 104.153 196.067 1.00 97.50 O
ANISOU 1010 O ASN A 137 12310 7667 17068 -168 1677 -2076 O
ATOM 1011 CB ASN A 137 13.654 104.520 194.639 1.00 95.43 C
ANISOU 1011 CB ASN A 137 11407 7099 17754 207 2117 -1636 C
ATOM 1012 CG ASN A 137 12.697 103.877 193.681 1.00111.76 C
ANISOU 1012 CG ASN A 137 13155 9261 20049 321 2085 -1303 C
ATOM 1013 OD1 ASN A 137 13.096 103.228 192.714 1.00103.13 O
ANISOU 1013 OD1 ASN A 137 11934 8396 18854 281 1789 -1054 O
ATOM 1014 ND2 ASN A 137 11.416 104.015 193.953 1.00103.51 N
ANISOU 1014 ND2 ASN A 137 11977 8038 19314 458 2393 -1304 N
ATOM 1015 N LYS A 138 14.973 104.880 197.523 1.00 98.27 N
ANISOU 1015 N LYS A 138 12618 7408 17311 -37 2317 -2447 N
ATOM 1016 CA LYS A 138 15.870 105.594 198.431 1.00100.11 C
ANISOU 1016 CA LYS A 138 13186 7525 17327 -186 2276 -2786 C
ATOM 1017 C LYS A 138 16.437 104.640 199.511 1.00102.79 C
ANISOU 1017 C LYS A 138 13886 8131 17040 -313 2190 -2954 C
ATOM 1018 O LYS A 138 16.676 105.058 200.647 1.00105.87 O
ANISOU 1018 O LYS A 138 14638 8421 17168 -411 2302 -3295 O
ATOM 1019 CB LYS A 138 15.140 106.792 199.064 1.00107.06 C
ANISOU 1019 CB LYS A 138 14167 8009 18501 -120 2670 -3071 C
ATOM 1020 N ILE A 139 16.678 103.365 199.136 1.00 94.87 N
ANISOU 1020 N ILE A 139 12791 7458 15797 -320 1974 -2711 N
ATOM 1021 CA ILE A 139 17.235 102.333 200.011 1.00 93.86 C
ANISOU 1021 CA ILE A 139 12951 7597 15115 -430 1841 -2785 C
ATOM 1022 C ILE A 139 18.736 102.616 200.212 1.00 96.95 C
ANISOU 1022 C ILE A 139 13496 8040 15302 -618 1452 -2891 C
ATOM 1023 O ILE A 139 19.457 102.898 199.248 1.00 94.74 O
ANISOU 1023 O ILE A 139 12976 7760 15260 -646 1189 -2728 O
ATOM 1024 CB ILE A 139 16.922 100.905 199.455 1.00 93.40 C
ANISOU 1024 CB ILE A 139 12699 7826 14963 -358 1757 -2476 C
ATOM 1025 CG1 ILE A 139 15.661 100.336 200.144 1.00 95.27 C
ANISOU 1025 CG1 ILE A 139 13025 8069 15106 -260 2148 -2512 C
ATOM 1026 CG2 ILE A 139 18.110 99.925 199.559 1.00 91.90 C
ANISOU 1026 CG2 ILE A 139 12604 7922 14391 -484 1370 -2392 C
ATOM 1027 CD1 ILE A 139 15.102 99.006 199.583 1.00 99.81 C
ANISOU 1027 CD1 ILE A 139 13378 8866 15680 -177 2123 -2214 C
ATOM 1028 N SER A 140 19.180 102.576 201.480 1.00 95.15 N
ANISOU 1028 N SER A 140 13673 7842 14636 -755 1424 -3162 N
ATOM 1029 CA SER A 140 20.566 102.813 201.882 1.00 95.38 C
ANISOU 1029 CA SER A 140 13884 7913 14443 -955 1038 -3289 C
ATOM 1030 C SER A 140 21.465 101.627 201.517 1.00 94.68 C
ANISOU 1030 C SER A 140 13675 8138 14160 -1008 651 -3030 C
ATOM 1031 O SER A 140 20.968 100.530 201.241 1.00 91.71 O
ANISOU 1031 O SER A 140 13183 7957 13705 -908 711 -2813 O
ATOM 1032 CB SER A 140 20.636 103.076 203.385 1.00103.49 C
ANISOU 1032 CB SER A 140 15413 8884 15025 -1090 1126 -3654 C
ATOM 1033 OG SER A 140 21.966 103.318 203.817 1.00114.80 O
ANISOU 1033 OG SER A 140 17023 10348 16248 -1301 709 -3779 O
ATOM 1034 N ASN A 141 22.795 101.848 201.537 1.00 90.47 N
ANISOU 1034 N ASN A 141 13159 7633 13582 -1169 257 -3060 N
ATOM 1035 CA ASN A 141 23.796 100.817 201.259 1.00 87.40 C
ANISOU 1035 CA ASN A 141 12648 7503 13056 -1230 -121 -2839 C
ATOM 1036 C ASN A 141 23.760 99.729 202.328 1.00 91.10 C
ANISOU 1036 C ASN A 141 13416 8181 13015 -1277 -179 -2859 C
ATOM 1037 O ASN A 141 23.949 98.558 202.002 1.00 87.85 O
ANISOU 1037 O ASN A 141 12862 7989 12527 -1232 -314 -2615 O
ATOM 1038 CB ASN A 141 25.197 101.422 201.155 1.00 87.87 C
ANISOU 1038 CB ASN A 141 12654 7503 13229 -1401 -505 -2888 C
ATOM 1039 CG ASN A 141 25.511 102.058 199.820 1.00103.20 C
ANISOU 1039 CG ASN A 141 14209 9333 15671 -1356 -533 -2721 C
ATOM 1040 OD1 ASN A 141 24.768 101.936 198.835 1.00 90.49 O
ANISOU 1040 OD1 ASN A 141 12348 7725 14308 -1197 -323 -2526 O
ATOM 1041 ND2 ASN A 141 26.640 102.744 199.754 1.00 98.18 N
ANISOU 1041 ND2 ASN A 141 13518 8596 15189 -1508 -810 -2782 N
ATOM 1042 N ARG A 142 23.492 100.119 203.594 1.00 91.24 N
ANISOU 1042 N ARG A 142 13862 8122 12686 -1370 -59 -3151 N
ATOM 1043 CA ARG A 142 23.366 99.215 204.738 1.00 92.62 C
ANISOU 1043 CA ARG A 142 14395 8475 12323 -1432 -73 -3188 C
ATOM 1044 C ARG A 142 22.104 98.359 204.589 1.00 94.02 C
ANISOU 1044 C ARG A 142 14501 8743 12478 -1254 304 -3028 C
ATOM 1045 O ARG A 142 22.170 97.145 204.784 1.00 92.40 O
ANISOU 1045 O ARG A 142 14317 8756 12034 -1245 195 -2832 O
ATOM 1046 CB ARG A 142 23.337 100.006 206.055 1.00 97.62 C
ANISOU 1046 CB ARG A 142 15529 8974 12587 -1586 7 -3568 C
ATOM 1047 N THR A 143 20.973 98.996 204.192 1.00 89.70 N
ANISOU 1047 N THR A 143 13834 8011 12237 -1110 731 -3093 N
ATOM 1048 CA THR A 143 19.664 98.370 203.969 1.00 87.79 C
ANISOU 1048 CA THR A 143 13468 7803 12086 -937 1118 -2953 C
ATOM 1049 C THR A 143 19.758 97.314 202.851 1.00 86.07 C
ANISOU 1049 C THR A 143 12859 7770 12076 -840 939 -2590 C
ATOM 1050 O THR A 143 19.302 96.188 203.058 1.00 85.09 O
ANISOU 1050 O THR A 143 12753 7808 11771 -793 1014 -2435 O
ATOM 1051 CB THR A 143 18.598 99.442 203.654 1.00 97.63 C
ANISOU 1051 CB THR A 143 14597 8769 13727 -811 1541 -3086 C
ATOM 1052 OG1 THR A 143 18.647 100.472 204.644 1.00101.84 O
ANISOU 1052 OG1 THR A 143 15499 9105 14089 -911 1692 -3456 O
ATOM 1053 CG2 THR A 143 17.183 98.868 203.583 1.00 95.91 C
ANISOU 1053 CG2 THR A 143 14263 8557 13620 -645 1962 -2968 C
ATOM 1054 N ALA A 144 20.364 97.669 201.691 1.00 78.69 N
ANISOU 1054 N ALA A 144 11591 6805 11505 -821 713 -2461 N
ATOM 1055 CA ALA A 144 20.540 96.768 200.544 1.00 73.91 C
ANISOU 1055 CA ALA A 144 10631 6357 11093 -742 547 -2150 C
ATOM 1056 C ALA A 144 21.417 95.565 200.906 1.00 75.33 C
ANISOU 1056 C ALA A 144 10891 6770 10960 -822 234 -2027 C
ATOM 1057 O ALA A 144 21.150 94.464 200.426 1.00 72.52 O
ANISOU 1057 O ALA A 144 10369 6559 10627 -743 227 -1809 O
ATOM 1058 CB ALA A 144 21.138 97.517 199.365 1.00 73.04 C
ANISOU 1058 CB ALA A 144 10224 6158 11370 -738 383 -2071 C
ATOM 1059 N ALA A 145 22.437 95.771 201.773 1.00 73.03 N
ANISOU 1059 N ALA A 145 10854 6501 10395 -981 -34 -2166 N
ATOM 1060 CA ALA A 145 23.328 94.714 202.260 1.00 72.71 C
ANISOU 1060 CA ALA A 145 10905 6655 10066 -1069 -367 -2048 C
ATOM 1061 C ALA A 145 22.577 93.782 203.222 1.00 77.93 C
ANISOU 1061 C ALA A 145 11838 7427 10345 -1053 -192 -2019 C
ATOM 1062 O ALA A 145 22.774 92.564 203.168 1.00 75.71 O
ANISOU 1062 O ALA A 145 11487 7307 9973 -1030 -332 -1803 O
ATOM 1063 CB ALA A 145 24.539 95.320 202.947 1.00 76.05 C
ANISOU 1063 CB ALA A 145 11523 7045 10329 -1255 -715 -2206 C
ATOM 1064 N ILE A 146 21.702 94.361 204.084 1.00 77.40 N
ANISOU 1064 N ILE A 146 12076 7255 10077 -1063 141 -2236 N
ATOM 1065 CA ILE A 146 20.860 93.640 205.045 1.00 78.88 C
ANISOU 1065 CA ILE A 146 12550 7520 9900 -1053 400 -2231 C
ATOM 1066 C ILE A 146 19.889 92.740 204.258 1.00 79.51 C
ANISOU 1066 C ILE A 146 12323 7654 10234 -883 634 -1989 C
ATOM 1067 O ILE A 146 19.759 91.562 204.594 1.00 79.02 O
ANISOU 1067 O ILE A 146 12318 7737 9967 -879 608 -1811 O
ATOM 1068 CB ILE A 146 20.144 94.634 206.020 1.00 85.91 C
ANISOU 1068 CB ILE A 146 13810 8249 10582 -1096 767 -2554 C
ATOM 1069 CG1 ILE A 146 21.106 95.072 207.149 1.00 90.08 C
ANISOU 1069 CG1 ILE A 146 14776 8791 10659 -1309 486 -2773 C
ATOM 1070 CG2 ILE A 146 18.841 94.054 206.609 1.00 88.00 C
ANISOU 1070 CG2 ILE A 146 14228 8535 10672 -1015 1232 -2528 C
ATOM 1071 CD1 ILE A 146 20.792 96.445 207.812 1.00100.75 C
ANISOU 1071 CD1 ILE A 146 16439 9921 11922 -1378 744 -3165 C
ATOM 1072 N ILE A 147 19.260 93.282 203.187 1.00 73.90 N
ANISOU 1072 N ILE A 147 11280 6820 9979 -755 824 -1966 N
ATOM 1073 CA ILE A 147 18.336 92.550 202.305 1.00 71.01 C
ANISOU 1073 CA ILE A 147 10593 6485 9902 -607 1002 -1746 C
ATOM 1074 C ILE A 147 19.105 91.397 201.623 1.00 71.73 C
ANISOU 1074 C ILE A 147 10475 6752 10028 -607 657 -1497 C
ATOM 1075 O ILE A 147 18.618 90.264 201.613 1.00 70.32 O
ANISOU 1075 O ILE A 147 10242 6671 9806 -558 722 -1324 O
ATOM 1076 CB ILE A 147 17.638 93.502 201.279 1.00 72.74 C
ANISOU 1076 CB ILE A 147 10512 6527 10599 -493 1197 -1767 C
ATOM 1077 CG1 ILE A 147 16.639 94.443 201.991 1.00 75.98 C
ANISOU 1077 CG1 ILE A 147 11096 6740 11034 -459 1622 -1991 C
ATOM 1078 CG2 ILE A 147 16.930 92.715 200.162 1.00 70.48 C
ANISOU 1078 CG2 ILE A 147 9861 6295 10622 -370 1242 -1513 C
ATOM 1079 CD1 ILE A 147 16.181 95.662 201.181 1.00 82.63 C
ANISOU 1079 CD1 ILE A 147 11697 7358 12341 -372 1763 -2051 C
ATOM 1080 N SER A 148 20.323 91.687 201.115 1.00 67.26 N
ANISOU 1080 N SER A 148 9799 6208 9547 -668 308 -1489 N
ATOM 1081 CA SER A 148 21.210 90.724 200.452 1.00 64.61 C
ANISOU 1081 CA SER A 148 9257 6009 9282 -670 -9 -1285 C
ATOM 1082 C SER A 148 21.598 89.582 201.393 1.00 69.87 C
ANISOU 1082 C SER A 148 10131 6812 9604 -732 -167 -1189 C
ATOM 1083 O SER A 148 21.613 88.430 200.963 1.00 67.61 O
ANISOU 1083 O SER A 148 9683 6618 9386 -677 -238 -990 O
ATOM 1084 CB SER A 148 22.462 91.420 199.930 1.00 66.74 C
ANISOU 1084 CB SER A 148 9402 6249 9706 -740 -306 -1326 C
ATOM 1085 OG SER A 148 22.129 92.383 198.943 1.00 71.75 O
ANISOU 1085 OG SER A 148 9824 6760 10676 -681 -174 -1362 O
ATOM 1086 N CYS A 149 21.883 89.902 202.676 1.00 70.18 N
ANISOU 1086 N CYS A 149 10541 6853 9270 -851 -222 -1330 N
ATOM 1087 CA CYS A 149 22.235 88.925 203.706 1.00 72.23 C
ANISOU 1087 CA CYS A 149 11057 7237 9150 -930 -389 -1229 C
ATOM 1088 C CYS A 149 21.040 88.029 204.014 1.00 76.48 C
ANISOU 1088 C CYS A 149 11661 7815 9583 -853 -65 -1111 C
ATOM 1089 O CYS A 149 21.211 86.812 204.103 1.00 76.09 O
ANISOU 1089 O CYS A 149 11577 7865 9467 -843 -194 -896 O
ATOM 1090 CB CYS A 149 22.751 89.614 204.966 1.00 76.75 C
ANISOU 1090 CB CYS A 149 12045 7797 9319 -1094 -522 -1426 C
ATOM 1091 SG CYS A 149 24.525 89.978 204.938 1.00 81.58 S
ANISOU 1091 SG CYS A 149 12600 8426 9970 -1235 -1095 -1441 S
ATOM 1092 N LEU A 150 19.831 88.625 204.144 1.00 73.66 N
ANISOU 1092 N LEU A 150 11369 7358 9260 -795 363 -1242 N
ATOM 1093 CA LEU A 150 18.588 87.897 204.415 1.00 73.94 C
ANISOU 1093 CA LEU A 150 11433 7403 9259 -723 726 -1141 C
ATOM 1094 C LEU A 150 18.270 86.913 203.288 1.00 74.79 C
ANISOU 1094 C LEU A 150 11148 7546 9723 -609 700 -905 C
ATOM 1095 O LEU A 150 17.960 85.754 203.573 1.00 74.34 O
ANISOU 1095 O LEU A 150 11115 7560 9571 -599 733 -723 O
ATOM 1096 CB LEU A 150 17.405 88.860 204.627 1.00 75.52 C
ANISOU 1096 CB LEU A 150 11701 7455 9539 -669 1194 -1335 C
ATOM 1097 CG LEU A 150 17.353 89.633 205.950 1.00 84.32 C
ANISOU 1097 CG LEU A 150 13280 8520 10236 -777 1369 -1587 C
ATOM 1098 CD1 LEU A 150 16.304 90.718 205.892 1.00 85.55 C
ANISOU 1098 CD1 LEU A 150 13408 8483 10613 -698 1821 -1796 C
ATOM 1099 CD2 LEU A 150 17.079 88.711 207.137 1.00 89.72 C
ANISOU 1099 CD2 LEU A 150 14319 9317 10454 -851 1486 -1497 C
ATOM 1100 N LEU A 151 18.394 87.359 202.015 1.00 68.90 N
ANISOU 1100 N LEU A 151 10062 6747 9370 -537 623 -907 N
ATOM 1101 CA LEU A 151 18.146 86.519 200.837 1.00 65.73 C
ANISOU 1101 CA LEU A 151 9308 6376 9292 -445 576 -719 C
ATOM 1102 C LEU A 151 19.176 85.397 200.726 1.00 69.10 C
ANISOU 1102 C LEU A 151 9687 6915 9652 -478 237 -556 C
ATOM 1103 O LEU A 151 18.816 84.305 200.285 1.00 67.43 O
ANISOU 1103 O LEU A 151 9318 6735 9567 -424 253 -390 O
ATOM 1104 CB LEU A 151 18.116 87.336 199.543 1.00 63.36 C
ANISOU 1104 CB LEU A 151 8712 6002 9361 -383 558 -761 C
ATOM 1105 CG LEU A 151 16.967 88.324 199.402 1.00 68.23 C
ANISOU 1105 CG LEU A 151 9275 6478 10170 -320 889 -866 C
ATOM 1106 CD1 LEU A 151 17.355 89.448 198.493 1.00 67.02 C
ANISOU 1106 CD1 LEU A 151 8953 6243 10268 -306 792 -940 C
ATOM 1107 CD2 LEU A 151 15.685 87.641 198.936 1.00 69.43 C
ANISOU 1107 CD2 LEU A 151 9224 6609 10549 -230 1115 -728 C
ATOM 1108 N TRP A 152 20.440 85.649 201.148 1.00 67.15 N
ANISOU 1108 N TRP A 152 9566 6710 9236 -567 -71 -601 N
ATOM 1109 CA TRP A 152 21.481 84.619 201.158 1.00 67.26 C
ANISOU 1109 CA TRP A 152 9528 6808 9219 -595 -402 -438 C
ATOM 1110 C TRP A 152 21.155 83.575 202.224 1.00 73.44 C
ANISOU 1110 C TRP A 152 10545 7648 9712 -627 -369 -298 C
ATOM 1111 O TRP A 152 21.352 82.386 201.982 1.00 71.67 O
ANISOU 1111 O TRP A 152 10193 7457 9582 -592 -484 -107 O
ATOM 1112 CB TRP A 152 22.886 85.199 201.372 1.00 67.19 C
ANISOU 1112 CB TRP A 152 9565 6814 9149 -689 -752 -507 C
ATOM 1113 CG TRP A 152 23.607 85.534 200.098 1.00 65.99 C
ANISOU 1113 CG TRP A 152 9082 6637 9356 -649 -888 -512 C
ATOM 1114 CD1 TRP A 152 24.019 86.769 199.694 1.00 68.79 C
ANISOU 1114 CD1 TRP A 152 9375 6927 9834 -683 -922 -661 C
ATOM 1115 CD2 TRP A 152 23.999 84.620 199.061 1.00 63.68 C
ANISOU 1115 CD2 TRP A 152 8489 6371 9337 -575 -981 -364 C
ATOM 1116 NE1 TRP A 152 24.630 86.687 198.465 1.00 66.16 N
ANISOU 1116 NE1 TRP A 152 8724 6593 9820 -636 -1018 -596 N
ATOM 1117 CE2 TRP A 152 24.628 85.380 198.050 1.00 66.25 C
ANISOU 1117 CE2 TRP A 152 8593 6662 9918 -569 -1047 -429 C
ATOM 1118 CE3 TRP A 152 23.867 83.230 198.880 1.00 64.29 C
ANISOU 1118 CE3 TRP A 152 8470 6484 9474 -516 -996 -188 C
ATOM 1119 CZ2 TRP A 152 25.134 84.799 196.879 1.00 63.65 C
ANISOU 1119 CZ2 TRP A 152 7973 6346 9867 -508 -1107 -336 C
ATOM 1120 CZ3 TRP A 152 24.359 82.656 197.716 1.00 63.87 C
ANISOU 1120 CZ3 TRP A 152 8121 6427 9718 -452 -1066 -116 C
ATOM 1121 CH2 TRP A 152 24.990 83.435 196.734 1.00 63.35 C
ANISOU 1121 CH2 TRP A 152 7861 6341 9869 -449 -1111 -195 C
ATOM 1122 N GLY A 153 20.601 84.031 203.355 1.00 73.21 N
ANISOU 1122 N GLY A 153 10856 7614 9346 -692 -179 -397 N
ATOM 1123 CA GLY A 153 20.155 83.190 204.461 1.00 75.63 C
ANISOU 1123 CA GLY A 153 11443 7973 9322 -737 -78 -270 C
ATOM 1124 C GLY A 153 19.048 82.235 204.051 1.00 78.25 C
ANISOU 1124 C GLY A 153 11599 8281 9853 -642 198 -112 C
ATOM 1125 O GLY A 153 19.001 81.101 204.536 1.00 78.73 O
ANISOU 1125 O GLY A 153 11738 8382 9793 -659 158 93 O
ATOM 1126 N ILE A 154 18.160 82.687 203.129 1.00 72.78 N
ANISOU 1126 N ILE A 154 10652 7510 9492 -548 457 -192 N
ATOM 1127 CA ILE A 154 17.065 81.891 202.566 1.00 71.35 C
ANISOU 1127 CA ILE A 154 10248 7288 9576 -464 694 -61 C
ATOM 1128 C ILE A 154 17.678 80.866 201.601 1.00 73.51 C
ANISOU 1128 C ILE A 154 10242 7585 10104 -422 415 96 C
ATOM 1129 O ILE A 154 17.345 79.681 201.692 1.00 73.56 O
ANISOU 1129 O ILE A 154 10206 7590 10153 -410 442 276 O
ATOM 1130 CB ILE A 154 15.976 82.776 201.888 1.00 73.44 C
ANISOU 1130 CB ILE A 154 10323 7454 10129 -387 1003 -188 C
ATOM 1131 CG1 ILE A 154 15.336 83.752 202.901 1.00 76.63 C
ANISOU 1131 CG1 ILE A 154 11003 7802 10309 -418 1333 -359 C
ATOM 1132 CG2 ILE A 154 14.895 81.911 201.208 1.00 73.00 C
ANISOU 1132 CG2 ILE A 154 9995 7352 10391 -315 1178 -39 C
ATOM 1133 CD1 ILE A 154 14.716 85.006 202.286 1.00 82.15 C
ANISOU 1133 CD1 ILE A 154 11540 8382 11292 -350 1536 -530 C
ATOM 1134 N THR A 155 18.608 81.318 200.716 1.00 67.96 N
ANISOU 1134 N THR A 155 9360 6890 9569 -407 164 24 N
ATOM 1135 CA THR A 155 19.329 80.474 199.747 1.00 65.45 C
ANISOU 1135 CA THR A 155 8787 6585 9494 -367 -78 129 C
ATOM 1136 C THR A 155 20.073 79.359 200.495 1.00 69.78 C
ANISOU 1136 C THR A 155 9453 7171 9888 -406 -297 303 C
ATOM 1137 O THR A 155 20.049 78.216 200.046 1.00 68.49 O
ANISOU 1137 O THR A 155 9132 6982 9909 -363 -344 444 O
ATOM 1138 CB THR A 155 20.285 81.313 198.874 1.00 71.64 C
ANISOU 1138 CB THR A 155 9416 7375 10428 -362 -271 12 C
ATOM 1139 OG1 THR A 155 19.625 82.502 198.435 1.00 70.26 O
ANISOU 1139 OG1 THR A 155 9196 7155 10344 -342 -80 -134 O
ATOM 1140 CG2 THR A 155 20.802 80.540 197.664 1.00 66.53 C
ANISOU 1140 CG2 THR A 155 8486 6726 10068 -308 -414 85 C
ATOM 1141 N ILE A 156 20.694 79.697 201.651 1.00 68.48 N
ANISOU 1141 N ILE A 156 9575 7055 9388 -493 -438 295 N
ATOM 1142 CA ILE A 156 21.383 78.764 202.546 1.00 70.28 C
ANISOU 1142 CA ILE A 156 9963 7319 9420 -547 -676 485 C
ATOM 1143 C ILE A 156 20.353 77.737 203.036 1.00 75.13 C
ANISOU 1143 C ILE A 156 10665 7913 9967 -536 -445 657 C
ATOM 1144 O ILE A 156 20.580 76.547 202.871 1.00 74.39 O
ANISOU 1144 O ILE A 156 10453 7788 10022 -505 -565 850 O
ATOM 1145 CB ILE A 156 22.098 79.513 203.721 1.00 76.26 C
ANISOU 1145 CB ILE A 156 11057 8139 9781 -669 -869 419 C
ATOM 1146 CG1 ILE A 156 23.412 80.210 203.254 1.00 76.01 C
ANISOU 1146 CG1 ILE A 156 10883 8111 9885 -693 -1202 319 C
ATOM 1147 CG2 ILE A 156 22.326 78.616 204.963 1.00 80.22 C
ANISOU 1147 CG2 ILE A 156 11844 8688 9950 -748 -1020 638 C
ATOM 1148 CD1 ILE A 156 24.723 79.372 203.235 1.00 84.59 C
ANISOU 1148 CD1 ILE A 156 11832 9205 11105 -701 -1615 504 C
ATOM 1149 N GLY A 157 19.219 78.212 203.557 1.00 72.85 N
ANISOU 1149 N GLY A 157 10551 7620 9507 -554 -95 582 N
ATOM 1150 CA GLY A 157 18.137 77.377 204.075 1.00 74.13 C
ANISOU 1150 CA GLY A 157 10800 7755 9613 -554 188 738 C
ATOM 1151 C GLY A 157 17.544 76.379 203.097 1.00 75.29 C
ANISOU 1151 C GLY A 157 10617 7823 10169 -472 269 854 C
ATOM 1152 O GLY A 157 17.211 75.258 203.490 1.00 75.85 O
ANISOU 1152 O GLY A 157 10718 7860 10241 -483 316 1064 O
ATOM 1153 N LEU A 158 17.412 76.777 201.815 1.00 68.61 N
ANISOU 1153 N LEU A 158 9467 6939 9664 -400 276 722 N
ATOM 1154 CA LEU A 158 16.847 75.938 200.751 1.00 66.24 C
ANISOU 1154 CA LEU A 158 8859 6562 9746 -336 328 788 C
ATOM 1155 C LEU A 158 17.853 74.926 200.190 1.00 69.11 C
ANISOU 1155 C LEU A 158 9071 6903 10286 -311 23 890 C
ATOM 1156 O LEU A 158 17.437 73.972 199.526 1.00 68.09 O
ANISOU 1156 O LEU A 158 8747 6694 10429 -277 54 967 O
ATOM 1157 CB LEU A 158 16.327 76.808 199.586 1.00 63.92 C
ANISOU 1157 CB LEU A 158 8333 6244 9708 -284 429 612 C
ATOM 1158 CG LEU A 158 15.242 77.839 199.882 1.00 69.36 C
ANISOU 1158 CG LEU A 158 9081 6914 10360 -282 747 502 C
ATOM 1159 CD1 LEU A 158 15.205 78.899 198.805 1.00 67.43 C
ANISOU 1159 CD1 LEU A 158 8645 6657 10319 -238 725 339 C
ATOM 1160 CD2 LEU A 158 13.879 77.188 200.048 1.00 72.87 C
ANISOU 1160 CD2 LEU A 158 9449 7283 10953 -275 1042 615 C
ATOM 1161 N THR A 159 19.166 75.138 200.428 1.00 65.80 N
ANISOU 1161 N THR A 159 8722 6534 9747 -329 -267 883 N
ATOM 1162 CA THR A 159 20.218 74.279 199.869 1.00 65.04 C
ANISOU 1162 CA THR A 159 8447 6396 9867 -291 -540 965 C
ATOM 1163 C THR A 159 21.075 73.528 200.922 1.00 71.34 C
ANISOU 1163 C THR A 159 9406 7195 10505 -329 -784 1176 C
ATOM 1164 O THR A 159 21.732 72.553 200.558 1.00 70.51 O
ANISOU 1164 O THR A 159 9138 7014 10639 -285 -961 1292 O
ATOM 1165 CB THR A 159 21.145 75.113 198.965 1.00 70.02 C
ANISOU 1165 CB THR A 159 8919 7059 10626 -264 -696 794 C
ATOM 1166 OG1 THR A 159 21.769 76.131 199.748 1.00 71.45 O
ANISOU 1166 OG1 THR A 159 9295 7317 10536 -326 -816 728 O
ATOM 1167 CG2 THR A 159 20.413 75.738 197.772 1.00 64.90 C
ANISOU 1167 CG2 THR A 159 8094 6403 10163 -226 -508 625 C
ATOM 1168 N VAL A 160 21.060 73.960 202.202 1.00 70.94 N
ANISOU 1168 N VAL A 160 9676 7219 10059 -413 -796 1228 N
ATOM 1169 CA VAL A 160 21.859 73.398 203.306 1.00 74.24 C
ANISOU 1169 CA VAL A 160 10299 7658 10252 -474 -1068 1444 C
ATOM 1170 C VAL A 160 21.567 71.887 203.550 1.00 80.87 C
ANISOU 1170 C VAL A 160 11105 8399 11221 -453 -1060 1722 C
ATOM 1171 O VAL A 160 22.444 71.195 204.071 1.00 82.39 O
ANISOU 1171 O VAL A 160 11337 8567 11403 -468 -1357 1931 O
ATOM 1172 CB VAL A 160 21.722 74.238 204.613 1.00 80.85 C
ANISOU 1172 CB VAL A 160 11544 8602 10573 -590 -1039 1413 C
ATOM 1173 CG1 VAL A 160 20.426 73.944 205.370 1.00 82.40 C
ANISOU 1173 CG1 VAL A 160 11972 8800 10535 -628 -679 1499 C
ATOM 1174 CG2 VAL A 160 22.944 74.089 205.515 1.00 83.52 C
ANISOU 1174 CG2 VAL A 160 12065 8988 10682 -670 -1458 1564 C
ATOM 1175 N HIS A 161 20.381 71.377 203.131 1.00 77.61 N
ANISOU 1175 N HIS A 161 10593 7916 10980 -419 -747 1732 N
ATOM 1176 CA HIS A 161 19.989 69.967 203.285 1.00 79.10 C
ANISOU 1176 CA HIS A 161 10730 7984 11340 -405 -704 1981 C
ATOM 1177 C HIS A 161 20.934 69.009 202.522 1.00 83.73 C
ANISOU 1177 C HIS A 161 11038 8447 12329 -326 -967 2057 C
ATOM 1178 O HIS A 161 20.961 67.814 202.827 1.00 85.36 O
ANISOU 1178 O HIS A 161 11226 8536 12672 -319 -1028 2299 O
ATOM 1179 CB HIS A 161 18.531 69.748 202.833 1.00 78.78 C
ANISOU 1179 CB HIS A 161 10587 7880 11465 -392 -326 1934 C
ATOM 1180 CG HIS A 161 18.300 69.916 201.362 1.00 78.87 C
ANISOU 1180 CG HIS A 161 10277 7840 11850 -320 -271 1720 C
ATOM 1181 ND1 HIS A 161 18.353 68.839 200.496 1.00 79.67 N
ANISOU 1181 ND1 HIS A 161 10130 7802 12340 -268 -330 1762 N
ATOM 1182 CD2 HIS A 161 17.993 71.028 200.655 1.00 78.64 C
ANISOU 1182 CD2 HIS A 161 10164 7876 11839 -301 -163 1473 C
ATOM 1183 CE1 HIS A 161 18.091 69.328 199.295 1.00 76.58 C
ANISOU 1183 CE1 HIS A 161 9536 7413 12149 -230 -265 1535 C
ATOM 1184 NE2 HIS A 161 17.867 70.640 199.340 1.00 76.17 N
ANISOU 1184 NE2 HIS A 161 9565 7483 11893 -245 -172 1374 N
ATOM 1185 N LEU A 162 21.705 69.542 201.545 1.00 78.86 N
ANISOU 1185 N LEU A 162 10209 7844 11913 -269 -1097 1855 N
ATOM 1186 CA LEU A 162 22.662 68.803 200.711 1.00 78.54 C
ANISOU 1186 CA LEU A 162 9889 7683 12268 -185 -1295 1870 C
ATOM 1187 C LEU A 162 23.956 68.466 201.470 1.00 86.97 C
ANISOU 1187 C LEU A 162 10999 8734 13310 -191 -1658 2074 C
ATOM 1188 O LEU A 162 24.711 67.591 201.032 1.00 86.96 O
ANISOU 1188 O LEU A 162 10776 8593 13670 -117 -1814 2162 O
ATOM 1189 CB LEU A 162 22.987 69.598 199.436 1.00 75.49 C
ANISOU 1189 CB LEU A 162 9289 7332 12062 -135 -1261 1584 C
ATOM 1190 CG LEU A 162 21.893 69.602 198.368 1.00 77.55 C
ANISOU 1190 CG LEU A 162 9419 7560 12485 -112 -983 1413 C
ATOM 1191 CD1 LEU A 162 21.871 70.898 197.630 1.00 75.13 C
ANISOU 1191 CD1 LEU A 162 9066 7363 12117 -113 -913 1166 C
ATOM 1192 CD2 LEU A 162 22.071 68.461 197.391 1.00 79.84 C
ANISOU 1192 CD2 LEU A 162 9472 7689 13176 -44 -989 1405 C
ATOM 1193 N LEU A 163 24.202 69.151 202.604 1.00 87.11 N
ANISOU 1193 N LEU A 163 11299 8882 12915 -283 -1797 2146 N
ATOM 1194 CA LEU A 163 25.363 68.928 203.473 1.00 90.60 C
ANISOU 1194 CA LEU A 163 11825 9329 13271 -318 -2191 2364 C
ATOM 1195 C LEU A 163 25.014 67.922 204.589 1.00100.05 C
ANISOU 1195 C LEU A 163 13245 10477 14291 -370 -2242 2707 C
ATOM 1196 O LEU A 163 25.784 67.767 205.539 1.00102.74 O
ANISOU 1196 O LEU A 163 13742 10844 14451 -430 -2576 2933 O
ATOM 1197 CB LEU A 163 25.859 70.261 204.082 1.00 91.22 C
ANISOU 1197 CB LEU A 163 12114 9573 12970 -415 -2352 2240 C
ATOM 1198 CG LEU A 163 26.414 71.312 203.115 1.00 93.02 C
ANISOU 1198 CG LEU A 163 12131 9841 13370 -381 -2363 1949 C
ATOM 1199 CD1 LEU A 163 26.337 72.701 203.719 1.00 93.61 C
ANISOU 1199 CD1 LEU A 163 12476 10066 13027 -490 -2367 1777 C
ATOM 1200 CD2 LEU A 163 27.841 70.994 202.701 1.00 95.76 C
ANISOU 1200 CD2 LEU A 163 12188 10105 14093 -324 -2694 2018 C
ATOM 1201 N LYS A 164 23.862 67.229 204.459 1.00 97.98 N
ANISOU 1201 N LYS A 164 12992 10139 14097 -355 -1928 2762 N
ATOM 1202 CA LYS A 164 23.368 66.247 205.431 1.00101.97 C
ANISOU 1202 CA LYS A 164 13699 10582 14461 -407 -1903 3094 C
ATOM 1203 C LYS A 164 23.590 64.804 204.956 1.00107.90 C
ANISOU 1203 C LYS A 164 14182 11098 15716 -316 -1975 3293 C
ATOM 1204 O LYS A 164 24.219 64.029 205.680 1.00110.66 O
ANISOU 1204 O LYS A 164 14590 11369 16088 -328 -2250 3615 O
ATOM 1205 CB LYS A 164 21.872 66.472 205.738 1.00104.82 C
ANISOU 1205 CB LYS A 164 14261 11002 14565 -469 -1473 3043 C
ATOM 1206 CG LYS A 164 21.577 67.709 206.576 1.00123.55 C
ANISOU 1206 CG LYS A 164 16987 13575 16381 -575 -1375 2921 C
ATOM 1207 CD LYS A 164 20.080 67.991 206.617 1.00134.44 C
ANISOU 1207 CD LYS A 164 18462 14979 17640 -604 -892 2817 C
ATOM 1208 CE LYS A 164 19.763 69.239 207.397 1.00147.64 C
ANISOU 1208 CE LYS A 164 20475 16821 18799 -695 -743 2659 C
ATOM 1209 NZ LYS A 164 18.348 69.651 207.221 1.00155.75 N
ANISOU 1209 NZ LYS A 164 21503 17848 19824 -694 -254 2509 N
ATOM 1210 N LYS A 165 23.066 64.450 203.753 1.00102.85 N
ANISOU 1210 N LYS A 165 13262 10339 15478 -234 -1740 3103 N
ATOM 1211 CA LYS A 165 23.130 63.114 203.139 1.00103.45 C
ANISOU 1211 CA LYS A 165 13079 10166 16064 -149 -1743 3212 C
ATOM 1212 C LYS A 165 24.575 62.611 202.963 1.00109.41 C
ANISOU 1212 C LYS A 165 13623 10794 17154 -62 -2096 3320 C
ATOM 1213 O LYS A 165 25.444 63.375 202.540 1.00107.63 O
ANISOU 1213 O LYS A 165 13286 10651 16959 -28 -2243 3140 O
ATOM 1214 CB LYS A 165 22.406 63.117 201.784 1.00102.71 C
ANISOU 1214 CB LYS A 165 12752 10005 16268 -98 -1460 2905 C
ATOM 1215 N LYS A 166 24.815 61.320 203.302 1.00109.33 N
ANISOU 1215 N LYS A 166 13544 10567 17430 -26 -2222 3627 N
ATOM 1216 CA LYS A 166 26.117 60.645 203.229 1.00111.44 C
ANISOU 1216 CA LYS A 166 13584 10658 18098 69 -2548 3792 C
ATOM 1217 C LYS A 166 26.531 60.417 201.769 1.00113.46 C
ANISOU 1217 C LYS A 166 13472 10761 18878 197 -2438 3494 C
ATOM 1218 O LYS A 166 25.809 59.762 201.011 1.00112.17 O
ANISOU 1218 O LYS A 166 13196 10446 18976 230 -2182 3370 O
ATOM 1219 CB LYS A 166 26.083 59.315 204.003 1.00117.82 C
ANISOU 1219 CB LYS A 166 14435 11255 19079 69 -2673 4218 C
ATOM 1220 N MET A 167 27.679 60.996 201.375 1.00109.41 N
ANISOU 1220 N MET A 167 12783 10289 18497 256 -2623 3367 N
ATOM 1221 CA MET A 167 28.215 60.926 200.010 1.00107.24 C
ANISOU 1221 CA MET A 167 12182 9897 18669 371 -2505 3073 C
ATOM 1222 C MET A 167 29.627 60.318 199.995 1.00114.04 C
ANISOU 1222 C MET A 167 12761 10557 20011 484 -2779 3234 C
ATOM 1223 O MET A 167 30.324 60.457 200.989 1.00116.38 O
ANISOU 1223 O MET A 167 13121 10902 20195 452 -3121 3511 O
ATOM 1224 CB MET A 167 28.248 62.338 199.394 1.00106.25 C
ANISOU 1224 CB MET A 167 12074 10010 18286 337 -2400 2734 C
ATOM 1225 CG MET A 167 26.881 62.921 199.114 1.00106.81 C
ANISOU 1225 CG MET A 167 12335 10232 18015 257 -2096 2529 C
ATOM 1226 SD MET A 167 26.070 62.159 197.693 1.00108.85 S
ANISOU 1226 SD MET A 167 12418 10315 18626 312 -1759 2271 S
ATOM 1227 CE MET A 167 24.389 62.474 198.105 1.00104.37 C
ANISOU 1227 CE MET A 167 12110 9879 17665 193 -1528 2270 C
ATOM 1228 N PRO A 168 30.111 59.667 198.911 1.00110.39 N
ANISOU 1228 N PRO A 168 11986 9866 20092 612 -2649 3069 N
ATOM 1229 CA PRO A 168 29.458 59.380 197.624 1.00107.81 C
ANISOU 1229 CA PRO A 168 11567 9447 19950 651 -2281 2727 C
ATOM 1230 C PRO A 168 28.690 58.051 197.635 1.00112.94 C
ANISOU 1230 C PRO A 168 12226 9840 20846 666 -2156 2845 C
ATOM 1231 O PRO A 168 28.901 57.218 198.523 1.00115.52 O
ANISOU 1231 O PRO A 168 12559 10006 21326 683 -2354 3206 O
ATOM 1232 CB PRO A 168 30.645 59.334 196.641 1.00109.91 C
ANISOU 1232 CB PRO A 168 11502 9578 20682 778 -2252 2535 C
ATOM 1233 CG PRO A 168 31.919 59.268 197.494 1.00117.52 C
ANISOU 1233 CG PRO A 168 12320 10482 21852 829 -2630 2849 C
ATOM 1234 CD PRO A 168 31.480 59.122 198.923 1.00114.83 C
ANISOU 1234 CD PRO A 168 12246 10219 21167 731 -2889 3229 C
ATOM 1235 N ILE A 169 27.809 57.843 196.632 1.00107.24 N
ANISOU 1235 N ILE A 169 11501 9068 20175 652 -1846 2548 N
ATOM 1236 CA ILE A 169 27.040 56.603 196.505 1.00108.09 C
ANISOU 1236 CA ILE A 169 11601 8913 20554 651 -1713 2608 C
ATOM 1237 C ILE A 169 27.949 55.564 195.808 1.00113.66 C
ANISOU 1237 C ILE A 169 12016 9271 21898 796 -1694 2545 C
ATOM 1238 O ILE A 169 28.350 55.756 194.657 1.00111.80 O
ANISOU 1238 O ILE A 169 11637 9005 21836 855 -1526 2199 O
ATOM 1239 CB ILE A 169 25.661 56.819 195.802 1.00108.44 C
ANISOU 1239 CB ILE A 169 11770 9046 20386 552 -1432 2335 C
ATOM 1240 CG1 ILE A 169 24.701 57.629 196.704 1.00107.41 C
ANISOU 1240 CG1 ILE A 169 11908 9191 19713 423 -1433 2473 C
ATOM 1241 CG2 ILE A 169 25.002 55.483 195.423 1.00110.88 C
ANISOU 1241 CG2 ILE A 169 12015 9036 21078 553 -1293 2329 C
ATOM 1242 CD1 ILE A 169 24.437 59.048 196.287 1.00113.75 C
ANISOU 1242 CD1 ILE A 169 12800 10302 20116 369 -1347 2212 C
ATOM 1243 N GLN A 170 28.280 54.483 196.550 1.00113.66 N
ANISOU 1243 N GLN A 170 11941 9004 22239 851 -1859 2896 N
ATOM 1244 CA GLN A 170 29.156 53.360 196.179 1.00116.49 C
ANISOU 1244 CA GLN A 170 12017 8976 23268 1001 -1877 2936 C
ATOM 1245 C GLN A 170 28.892 52.773 194.779 1.00119.36 C
ANISOU 1245 C GLN A 170 12260 9117 23975 1047 -1548 2516 C
ATOM 1246 O GLN A 170 29.841 52.315 194.139 1.00120.83 O
ANISOU 1246 O GLN A 170 12197 9067 24647 1183 -1486 2385 O
ATOM 1247 CB GLN A 170 29.020 52.240 197.215 1.00121.49 C
ANISOU 1247 CB GLN A 170 12669 9358 24134 1007 -2057 3393 C
ATOM 1248 N ASN A 171 27.628 52.765 194.316 1.00113.40 N
ANISOU 1248 N ASN A 171 11677 8423 22988 931 -1341 2308 N
ATOM 1249 CA ASN A 171 27.243 52.229 193.009 1.00135.46 C
ANISOU 1249 CA ASN A 171 14414 11025 26030 936 -1061 1900 C
ATOM 1250 C ASN A 171 27.699 53.139 191.874 1.00147.80 C
ANISOU 1250 C ASN A 171 15938 12775 27445 958 -902 1486 C
ATOM 1251 O ASN A 171 27.830 52.690 190.737 1.00103.77 O
ANISOU 1251 O ASN A 171 10282 7016 22130 997 -682 1139 O
ATOM 1252 CB ASN A 171 25.737 52.034 192.945 1.00134.98 C
ANISOU 1252 CB ASN A 171 14542 10996 25746 784 -947 1843 C
ATOM 1253 N ALA A 174 33.005 52.048 191.684 1.00112.97 N
ANISOU 1253 N ALA A 174 10432 7601 24891 1588 -1077 1722 N
ATOM 1254 CA ALA A 174 32.998 53.426 191.198 1.00109.19 C
ANISOU 1254 CA ALA A 174 10063 7517 23908 1507 -998 1481 C
ATOM 1255 C ALA A 174 32.007 54.283 191.993 1.00108.79 C
ANISOU 1255 C ALA A 174 10318 7836 23181 1338 -1188 1645 C
ATOM 1256 O ALA A 174 30.811 53.990 192.005 1.00106.77 O
ANISOU 1256 O ALA A 174 10278 7598 22693 1234 -1116 1606 O
ATOM 1257 CB ALA A 174 32.656 53.456 189.715 1.00108.81 C
ANISOU 1257 CB ALA A 174 10078 7453 23812 1486 -596 963 C
ATOM 1258 N ASN A 175 32.513 55.336 192.659 1.00103.98 N
ANISOU 1258 N ASN A 175 9718 7504 22285 1307 -1422 1819 N
ATOM 1259 CA ASN A 175 31.721 56.252 193.485 1.00100.99 C
ANISOU 1259 CA ASN A 175 9625 7472 21274 1157 -1593 1968 C
ATOM 1260 C ASN A 175 31.045 57.340 192.651 1.00100.84 C
ANISOU 1260 C ASN A 175 9779 7750 20784 1055 -1374 1610 C
ATOM 1261 O ASN A 175 31.645 57.860 191.708 1.00 99.50 O
ANISOU 1261 O ASN A 175 9491 7629 20685 1096 -1210 1335 O
ATOM 1262 CB ASN A 175 32.598 56.895 194.557 1.00102.14 C
ANISOU 1262 CB ASN A 175 9719 7761 21327 1159 -1955 2290 C
ATOM 1263 CG ASN A 175 33.163 55.921 195.562 1.00123.20 C
ANISOU 1263 CG ASN A 175 12259 10178 24373 1233 -2252 2721 C
ATOM 1264 OD1 ASN A 175 32.436 55.286 196.336 1.00116.25 O
ANISOU 1264 OD1 ASN A 175 11549 9232 23389 1179 -2351 2980 O
ATOM 1265 ND2 ASN A 175 34.482 55.799 195.585 1.00115.80 N
ANISOU 1265 ND2 ASN A 175 11009 9091 23898 1353 -2407 2830 N
ATOM 1266 N LEU A 176 29.804 57.695 193.026 1.00 95.07 N
ANISOU 1266 N LEU A 176 9323 7212 19589 922 -1371 1638 N
ATOM 1267 CA LEU A 176 28.993 58.714 192.358 1.00 91.14 C
ANISOU 1267 CA LEU A 176 8998 6986 18644 817 -1199 1354 C
ATOM 1268 C LEU A 176 28.715 59.903 193.264 1.00 92.70 C
ANISOU 1268 C LEU A 176 9382 7503 18338 721 -1369 1506 C
ATOM 1269 O LEU A 176 28.345 59.711 194.422 1.00 93.03 O
ANISOU 1269 O LEU A 176 9555 7567 18225 675 -1540 1805 O
ATOM 1270 CB LEU A 176 27.656 58.113 191.904 1.00 90.42 C
ANISOU 1270 CB LEU A 176 9044 6818 18494 741 -1017 1220 C
ATOM 1271 CG LEU A 176 27.647 57.369 190.580 1.00 95.82 C
ANISOU 1271 CG LEU A 176 9632 7282 19495 781 -772 888 C
ATOM 1272 CD1 LEU A 176 26.662 56.234 190.621 1.00 97.29 C
ANISOU 1272 CD1 LEU A 176 9879 7240 19848 735 -715 921 C
ATOM 1273 CD2 LEU A 176 27.281 58.295 189.440 1.00 95.37 C
ANISOU 1273 CD2 LEU A 176 9666 7442 19130 711 -591 532 C
ATOM 1274 N CYS A 177 28.857 61.127 192.729 1.00 87.10 N
ANISOU 1274 N CYS A 177 8702 7032 17361 684 -1302 1294 N
ATOM 1275 CA CYS A 177 28.570 62.352 193.469 1.00 85.62 C
ANISOU 1275 CA CYS A 177 8696 7133 16702 590 -1426 1376 C
ATOM 1276 C CYS A 177 27.373 63.034 192.831 1.00 87.93 C
ANISOU 1276 C CYS A 177 9153 7598 16659 498 -1220 1146 C
ATOM 1277 O CYS A 177 27.522 63.798 191.871 1.00 86.04 O
ANISOU 1277 O CYS A 177 8877 7468 16344 490 -1093 896 O
ATOM 1278 CB CYS A 177 29.784 63.275 193.529 1.00 85.94 C
ANISOU 1278 CB CYS A 177 8618 7286 16748 617 -1567 1370 C
ATOM 1279 SG CYS A 177 29.518 64.792 194.488 1.00 88.20 S
ANISOU 1279 SG CYS A 177 9143 7895 16476 494 -1735 1448 S
ATOM 1280 N SER A 178 26.177 62.716 193.345 1.00 84.81 N
ANISOU 1280 N SER A 178 8924 7209 16091 426 -1183 1249 N
ATOM 1281 CA SER A 178 24.907 63.248 192.866 1.00 82.71 C
ANISOU 1281 CA SER A 178 8789 7076 15561 337 -1011 1082 C
ATOM 1282 C SER A 178 23.865 63.224 193.968 1.00 87.55 C
ANISOU 1282 C SER A 178 9586 7746 15932 259 -1027 1298 C
ATOM 1283 O SER A 178 23.881 62.326 194.812 1.00 89.89 O
ANISOU 1283 O SER A 178 9905 7904 16344 269 -1113 1550 O
ATOM 1284 CB SER A 178 24.410 62.441 191.668 1.00 86.37 C
ANISOU 1284 CB SER A 178 9174 7376 16266 341 -834 861 C
ATOM 1285 OG SER A 178 23.272 63.032 191.060 1.00 93.44 O
ANISOU 1285 OG SER A 178 10165 8404 16934 252 -706 691 O
ATOM 1286 N SER A 179 22.948 64.199 193.947 1.00 82.11 N
ANISOU 1286 N SER A 179 9025 7249 14925 181 -926 1208 N
ATOM 1287 CA SER A 179 21.832 64.294 194.890 1.00 82.25 C
ANISOU 1287 CA SER A 179 9214 7329 14710 103 -865 1373 C
ATOM 1288 C SER A 179 20.751 63.268 194.526 1.00 86.75 C
ANISOU 1288 C SER A 179 9738 7729 15493 68 -726 1376 C
ATOM 1289 O SER A 179 19.947 62.886 195.381 1.00 87.59 O
ANISOU 1289 O SER A 179 9944 7803 15534 15 -669 1576 O
ATOM 1290 CB SER A 179 21.251 65.705 194.883 1.00 83.87 C
ANISOU 1290 CB SER A 179 9528 7761 14579 47 -778 1250 C
ATOM 1291 OG SER A 179 20.868 66.092 193.574 1.00 91.66 O
ANISOU 1291 OG SER A 179 10416 8777 15634 41 -670 991 O
ATOM 1292 N PHE A 180 20.764 62.814 193.246 1.00 82.46 N
ANISOU 1292 N PHE A 180 9054 7072 15205 88 -667 1148 N
ATOM 1293 CA PHE A 180 19.853 61.857 192.610 1.00 82.67 C
ANISOU 1293 CA PHE A 180 9016 6919 15475 44 -564 1074 C
ATOM 1294 C PHE A 180 18.403 62.361 192.669 1.00 85.47 C
ANISOU 1294 C PHE A 180 9433 7377 15664 -56 -444 1067 C
ATOM 1295 O PHE A 180 17.486 61.617 193.028 1.00 86.34 O
ANISOU 1295 O PHE A 180 9540 7360 15905 -114 -375 1195 O
ATOM 1296 CB PHE A 180 19.997 60.433 193.188 1.00 87.04 C
ANISOU 1296 CB PHE A 180 9529 7210 16334 69 -605 1288 C
ATOM 1297 CG PHE A 180 21.184 59.680 192.635 1.00 89.77 C
ANISOU 1297 CG PHE A 180 9739 7365 17005 170 -672 1207 C
ATOM 1298 CD1 PHE A 180 21.130 59.093 191.376 1.00 93.00 C
ANISOU 1298 CD1 PHE A 180 10051 7617 17669 173 -584 932 C
ATOM 1299 CD2 PHE A 180 22.356 59.563 193.368 1.00 92.96 C
ANISOU 1299 CD2 PHE A 180 10112 7737 17471 257 -823 1400 C
ATOM 1300 CE1 PHE A 180 22.234 58.412 190.857 1.00 95.20 C
ANISOU 1300 CE1 PHE A 180 10202 7701 18267 274 -596 834 C
ATOM 1301 CE2 PHE A 180 23.457 58.874 192.851 1.00 97.11 C
ANISOU 1301 CE2 PHE A 180 10474 8063 18361 362 -863 1330 C
ATOM 1302 CZ PHE A 180 23.388 58.303 191.600 1.00 95.39 C
ANISOU 1302 CZ PHE A 180 10159 7682 18403 376 -724 1039 C
ATOM 1303 N SER A 181 18.206 63.637 192.283 1.00 79.87 N
ANISOU 1303 N SER A 181 8759 6881 14705 -76 -413 922 N
ATOM 1304 CA SER A 181 16.889 64.274 192.228 1.00 78.69 C
ANISOU 1304 CA SER A 181 8632 6830 14438 -155 -302 899 C
ATOM 1305 C SER A 181 16.124 63.794 190.985 1.00 81.70 C
ANISOU 1305 C SER A 181 8903 7109 15031 -217 -279 711 C
ATOM 1306 O SER A 181 14.892 63.828 190.969 1.00 81.50 O
ANISOU 1306 O SER A 181 8843 7073 15052 -294 -206 741 O
ATOM 1307 CB SER A 181 17.023 65.796 192.235 1.00 80.46 C
ANISOU 1307 CB SER A 181 8921 7287 14365 -146 -293 818 C
ATOM 1308 OG SER A 181 17.861 66.278 191.196 1.00 87.40 O
ANISOU 1308 OG SER A 181 9752 8228 15227 -110 -363 610 O
ATOM 1309 N ILE A 182 16.872 63.312 189.968 1.00 77.83 N
ANISOU 1309 N ILE A 182 8360 6532 14679 -188 -341 519 N
ATOM 1310 CA ILE A 182 16.394 62.783 188.688 1.00 77.90 C
ANISOU 1310 CA ILE A 182 8308 6437 14853 -253 -348 297 C
ATOM 1311 C ILE A 182 15.351 61.651 188.896 1.00 84.48 C
ANISOU 1311 C ILE A 182 9084 7058 15957 -333 -323 388 C
ATOM 1312 O ILE A 182 14.349 61.632 188.186 1.00 84.54 O
ANISOU 1312 O ILE A 182 9047 7047 16028 -434 -336 281 O
ATOM 1313 CB ILE A 182 17.605 62.325 187.801 1.00 81.08 C
ANISOU 1313 CB ILE A 182 8696 6754 15357 -190 -372 92 C
ATOM 1314 CG1 ILE A 182 17.168 61.990 186.353 1.00 81.73 C
ANISOU 1314 CG1 ILE A 182 8777 6772 15506 -275 -375 -191 C
ATOM 1315 CG2 ILE A 182 18.429 61.178 188.435 1.00 83.25 C
ANISOU 1315 CG2 ILE A 182 8928 6809 15895 -108 -381 217 C
ATOM 1316 CD1 ILE A 182 18.268 62.094 185.287 1.00 86.69 C
ANISOU 1316 CD1 ILE A 182 9433 7416 16090 -229 -343 -443 C
ATOM 1317 N CYS A 183 15.563 60.749 189.875 1.00 82.74 N
ANISOU 1317 N CYS A 183 8860 6677 15901 -299 -304 605 N
ATOM 1318 CA CYS A 183 14.644 59.636 190.107 1.00 84.81 C
ANISOU 1318 CA CYS A 183 9060 6714 16452 -378 -269 714 C
ATOM 1319 C CYS A 183 13.643 59.898 191.245 1.00 88.83 C
ANISOU 1319 C CYS A 183 9582 7279 16890 -428 -167 988 C
ATOM 1320 O CYS A 183 12.887 58.987 191.595 1.00 90.24 O
ANISOU 1320 O CYS A 183 9702 7268 17317 -496 -114 1128 O
ATOM 1321 CB CYS A 183 15.387 58.320 190.318 1.00 87.47 C
ANISOU 1321 CB CYS A 183 9369 6782 17085 -323 -295 781 C
ATOM 1322 SG CYS A 183 17.111 58.495 190.837 1.00 91.28 S
ANISOU 1322 SG CYS A 183 9893 7312 17478 -164 -361 861 S
ATOM 1323 N HIS A 184 13.590 61.129 191.788 1.00 83.96 N
ANISOU 1323 N HIS A 184 9041 6905 15955 -402 -118 1051 N
ATOM 1324 CA HIS A 184 12.592 61.418 192.814 1.00 84.37 C
ANISOU 1324 CA HIS A 184 9116 7005 15936 -451 31 1276 C
ATOM 1325 C HIS A 184 11.261 61.750 192.140 1.00 86.27 C
ANISOU 1325 C HIS A 184 9226 7254 16298 -547 83 1178 C
ATOM 1326 O HIS A 184 11.220 62.570 191.218 1.00 83.73 O
ANISOU 1326 O HIS A 184 8873 7059 15881 -551 11 972 O
ATOM 1327 CB HIS A 184 13.023 62.542 193.772 1.00 84.42 C
ANISOU 1327 CB HIS A 184 9274 7235 15567 -392 85 1379 C
ATOM 1328 CG HIS A 184 12.325 62.480 195.100 1.00 89.81 C
ANISOU 1328 CG HIS A 184 10042 7918 16163 -429 264 1654 C
ATOM 1329 ND1 HIS A 184 10.950 62.639 195.208 1.00 92.45 N
ANISOU 1329 ND1 HIS A 184 10290 8233 16602 -507 447 1706 N
ATOM 1330 CD2 HIS A 184 12.834 62.261 196.335 1.00 93.21 C
ANISOU 1330 CD2 HIS A 184 10640 8361 16414 -405 288 1892 C
ATOM 1331 CE1 HIS A 184 10.672 62.517 196.495 1.00 93.78 C
ANISOU 1331 CE1 HIS A 184 10585 8405 16642 -524 618 1959 C
ATOM 1332 NE2 HIS A 184 11.772 62.287 197.213 1.00 94.67 N
ANISOU 1332 NE2 HIS A 184 10872 8543 16555 -471 518 2082 N
ATOM 1333 N THR A 185 10.179 61.089 192.594 1.00 83.90 N
ANISOU 1333 N THR A 185 8838 6808 16232 -631 199 1346 N
ATOM 1334 CA THR A 185 8.816 61.278 192.085 1.00 83.88 C
ANISOU 1334 CA THR A 185 8667 6777 16429 -733 243 1304 C
ATOM 1335 C THR A 185 8.292 62.654 192.513 1.00 85.44 C
ANISOU 1335 C THR A 185 8875 7184 16405 -709 381 1344 C
ATOM 1336 O THR A 185 8.835 63.250 193.448 1.00 84.74 O
ANISOU 1336 O THR A 185 8946 7227 16023 -634 485 1444 O
ATOM 1337 CB THR A 185 7.890 60.139 192.553 1.00 95.50 C
ANISOU 1337 CB THR A 185 10023 8010 18254 -830 347 1499 C
ATOM 1338 OG1 THR A 185 7.912 60.059 193.978 1.00 96.81 O
ANISOU 1338 OG1 THR A 185 10300 8188 18295 -798 551 1787 O
ATOM 1339 CG2 THR A 185 8.261 58.790 191.944 1.00 95.58 C
ANISOU 1339 CG2 THR A 185 9994 7771 18553 -869 200 1417 C
ATOM 1340 N PHE A 186 7.252 63.163 191.826 1.00 80.60 N
ANISOU 1340 N PHE A 186 8093 6589 15943 -774 368 1264 N
ATOM 1341 CA PHE A 186 6.688 64.479 192.117 1.00 79.03 C
ANISOU 1341 CA PHE A 186 7866 6552 15609 -744 503 1288 C
ATOM 1342 C PHE A 186 5.897 64.481 193.428 1.00 83.31 C
ANISOU 1342 C PHE A 186 8399 7057 16198 -754 814 1534 C
ATOM 1343 O PHE A 186 4.789 63.949 193.492 1.00 85.54 O
ANISOU 1343 O PHE A 186 8493 7192 16817 -840 915 1646 O
ATOM 1344 CB PHE A 186 5.819 64.984 190.953 1.00 80.72 C
ANISOU 1344 CB PHE A 186 7879 6776 16016 -810 366 1155 C
ATOM 1345 CG PHE A 186 5.331 66.400 191.138 1.00 81.86 C
ANISOU 1345 CG PHE A 186 7978 7067 16058 -761 484 1169 C
ATOM 1346 CD1 PHE A 186 6.187 67.479 190.951 1.00 82.84 C
ANISOU 1346 CD1 PHE A 186 8247 7374 15855 -674 428 1049 C
ATOM 1347 CD2 PHE A 186 4.016 66.657 191.505 1.00 86.08 C
ANISOU 1347 CD2 PHE A 186 8308 7535 16863 -802 665 1304 C
ATOM 1348 CE1 PHE A 186 5.736 68.785 191.133 1.00 83.47 C
ANISOU 1348 CE1 PHE A 186 8284 7558 15875 -626 544 1058 C
ATOM 1349 CE2 PHE A 186 3.567 67.966 191.686 1.00 88.54 C
ANISOU 1349 CE2 PHE A 186 8565 7951 17126 -743 797 1311 C
ATOM 1350 CZ PHE A 186 4.428 69.020 191.491 1.00 84.52 C
ANISOU 1350 CZ PHE A 186 8216 7613 16286 -656 729 1183 C
ATOM 1351 N GLN A 187 6.483 65.086 194.469 1.00 78.31 N
ANISOU 1351 N GLN A 187 7979 6555 15221 -675 968 1612 N
ATOM 1352 CA GLN A 187 5.881 65.212 195.796 1.00 79.86 C
ANISOU 1352 CA GLN A 187 8245 6748 15349 -681 1299 1826 C
ATOM 1353 C GLN A 187 5.948 66.686 196.253 1.00 83.34 C
ANISOU 1353 C GLN A 187 8805 7376 15486 -609 1448 1758 C
ATOM 1354 O GLN A 187 6.138 67.560 195.403 1.00 80.74 O
ANISOU 1354 O GLN A 187 8416 7140 15122 -571 1298 1571 O
ATOM 1355 CB GLN A 187 6.541 64.247 196.797 1.00 82.43 C
ANISOU 1355 CB GLN A 187 8773 7013 15532 -683 1344 2022 C
ATOM 1356 CG GLN A 187 6.156 62.784 196.557 1.00 96.08 C
ANISOU 1356 CG GLN A 187 10357 8505 17643 -766 1291 2139 C
ATOM 1357 CD GLN A 187 6.662 61.841 197.619 1.00115.11 C
ANISOU 1357 CD GLN A 187 12951 10831 19954 -773 1357 2388 C
ATOM 1358 OE1 GLN A 187 7.842 61.844 197.989 1.00108.76 O
ANISOU 1358 OE1 GLN A 187 12357 10106 18859 -706 1225 2403 O
ATOM 1359 NE2 GLN A 187 5.784 60.972 198.094 1.00110.99 N
ANISOU 1359 NE2 GLN A 187 12333 10132 19707 -859 1543 2607 N
ATOM 1360 N TRP A 188 5.740 66.967 197.562 1.00 82.51 N
ANISOU 1360 N TRP A 188 8871 7310 15167 -599 1754 1905 N
ATOM 1361 CA TRP A 188 5.697 68.322 198.127 1.00 82.70 C
ANISOU 1361 CA TRP A 188 9027 7477 14918 -542 1950 1831 C
ATOM 1362 C TRP A 188 7.000 69.123 197.922 1.00 83.32 C
ANISOU 1362 C TRP A 188 9302 7719 14637 -472 1718 1657 C
ATOM 1363 O TRP A 188 6.918 70.275 197.497 1.00 81.08 O
ANISOU 1363 O TRP A 188 8971 7514 14321 -427 1716 1501 O
ATOM 1364 CB TRP A 188 5.317 68.298 199.619 1.00 84.89 C
ANISOU 1364 CB TRP A 188 9512 7758 14985 -564 2329 2014 C
ATOM 1365 CG TRP A 188 5.357 69.646 200.285 1.00 86.53 C
ANISOU 1365 CG TRP A 188 9909 8096 14872 -511 2546 1909 C
ATOM 1366 CD1 TRP A 188 6.205 70.043 201.277 1.00 90.09 C
ANISOU 1366 CD1 TRP A 188 10727 8673 14830 -499 2584 1907 C
ATOM 1367 CD2 TRP A 188 4.560 70.794 199.955 1.00 86.45 C
ANISOU 1367 CD2 TRP A 188 9730 8088 15028 -468 2723 1776 C
ATOM 1368 NE1 TRP A 188 5.961 71.354 201.613 1.00 89.97 N
ANISOU 1368 NE1 TRP A 188 10801 8732 14653 -457 2800 1760 N
ATOM 1369 CE2 TRP A 188 4.964 71.844 200.810 1.00 91.04 C
ANISOU 1369 CE2 TRP A 188 10601 8786 15203 -428 2898 1681 C
ATOM 1370 CE3 TRP A 188 3.532 71.036 199.026 1.00 87.75 C
ANISOU 1370 CE3 TRP A 188 9522 8155 15665 -464 2735 1736 C
ATOM 1371 CZ2 TRP A 188 4.376 73.115 200.767 1.00 90.81 C
ANISOU 1371 CZ2 TRP A 188 10497 8760 15248 -371 3116 1539 C
ATOM 1372 CZ3 TRP A 188 2.958 72.299 198.977 1.00 89.77 C
ANISOU 1372 CZ3 TRP A 188 9685 8422 16002 -404 2926 1625 C
ATOM 1373 CH2 TRP A 188 3.381 73.322 199.837 1.00 90.87 C
ANISOU 1373 CH2 TRP A 188 10113 8660 15755 -352 3129 1523 C
ATOM 1374 N HIS A 189 8.175 68.532 198.229 1.00 79.50 N
ANISOU 1374 N HIS A 189 9015 7269 13922 -464 1526 1700 N
ATOM 1375 CA HIS A 189 9.485 69.183 198.071 1.00 77.29 C
ANISOU 1375 CA HIS A 189 8895 7126 13345 -407 1294 1559 C
ATOM 1376 C HIS A 189 9.770 69.485 196.589 1.00 77.55 C
ANISOU 1376 C HIS A 189 8733 7173 13561 -379 1046 1357 C
ATOM 1377 O HIS A 189 10.369 70.516 196.273 1.00 75.69 O
ANISOU 1377 O HIS A 189 8550 7053 13155 -335 954 1206 O
ATOM 1378 CB HIS A 189 10.600 68.305 198.672 1.00 79.04 C
ANISOU 1378 CB HIS A 189 9306 7343 13384 -409 1124 1688 C
ATOM 1379 CG HIS A 189 11.985 68.839 198.459 1.00 80.99 C
ANISOU 1379 CG HIS A 189 9664 7704 13404 -357 862 1561 C
ATOM 1380 ND1 HIS A 189 12.792 68.366 197.438 1.00 81.19 N
ANISOU 1380 ND1 HIS A 189 9559 7691 13598 -324 597 1467 N
ATOM 1381 CD2 HIS A 189 12.653 69.806 199.130 1.00 82.90 C
ANISOU 1381 CD2 HIS A 189 10123 8084 13290 -340 844 1509 C
ATOM 1382 CE1 HIS A 189 13.921 69.049 197.527 1.00 79.65 C
ANISOU 1382 CE1 HIS A 189 9481 7611 13171 -285 436 1381 C
ATOM 1383 NE2 HIS A 189 13.885 69.926 198.529 1.00 80.92 N
ANISOU 1383 NE2 HIS A 189 9851 7879 13016 -298 554 1403 N
ATOM 1384 N GLU A 190 9.330 68.587 195.693 1.00 73.21 N
ANISOU 1384 N GLU A 190 7973 6499 13345 -418 945 1356 N
ATOM 1385 CA GLU A 190 9.494 68.705 194.244 1.00 70.75 C
ANISOU 1385 CA GLU A 190 7501 6190 13192 -416 717 1174 C
ATOM 1386 C GLU A 190 8.571 69.804 193.705 1.00 74.10 C
ANISOU 1386 C GLU A 190 7778 6659 13719 -418 788 1091 C
ATOM 1387 O GLU A 190 8.960 70.521 192.780 1.00 71.97 O
ANISOU 1387 O GLU A 190 7475 6469 13400 -395 626 939 O
ATOM 1388 CB GLU A 190 9.228 67.355 193.557 1.00 72.64 C
ANISOU 1388 CB GLU A 190 7596 6263 13741 -477 598 1192 C
ATOM 1389 CG GLU A 190 10.319 66.313 193.783 1.00 80.90 C
ANISOU 1389 CG GLU A 190 8754 7242 14743 -456 475 1236 C
ATOM 1390 CD GLU A 190 10.547 65.818 195.202 1.00 98.00 C
ANISOU 1390 CD GLU A 190 11083 9378 16774 -449 604 1467 C
ATOM 1391 OE1 GLU A 190 9.553 65.593 195.930 1.00 90.96 O
ANISOU 1391 OE1 GLU A 190 10172 8424 15964 -498 823 1632 O
ATOM 1392 OE2 GLU A 190 11.727 65.642 195.582 1.00 89.10 O
ANISOU 1392 OE2 GLU A 190 10101 8286 15468 -399 482 1496 O
ATOM 1393 N ALA A 191 7.364 69.953 194.313 1.00 72.13 N
ANISOU 1393 N ALA A 191 7435 6347 13623 -442 1044 1208 N
ATOM 1394 CA ALA A 191 6.386 71.003 193.997 1.00 71.75 C
ANISOU 1394 CA ALA A 191 7220 6310 13733 -431 1153 1170 C
ATOM 1395 C ALA A 191 6.930 72.350 194.469 1.00 74.48 C
ANISOU 1395 C ALA A 191 7737 6787 13776 -355 1242 1081 C
ATOM 1396 O ALA A 191 6.798 73.353 193.767 1.00 72.31 O
ANISOU 1396 O ALA A 191 7369 6556 13551 -325 1170 979 O
ATOM 1397 CB ALA A 191 5.054 70.702 194.668 1.00 75.00 C
ANISOU 1397 CB ALA A 191 7483 6599 14416 -470 1449 1331 C
ATOM 1398 N MET A 192 7.582 72.341 195.653 1.00 72.37 N
ANISOU 1398 N MET A 192 7733 6574 13189 -335 1373 1127 N
ATOM 1399 CA MET A 192 8.249 73.474 196.287 1.00 72.13 C
ANISOU 1399 CA MET A 192 7924 6659 12823 -283 1441 1037 C
ATOM 1400 C MET A 192 9.400 73.954 195.396 1.00 72.00 C
ANISOU 1400 C MET A 192 7936 6737 12683 -253 1134 886 C
ATOM 1401 O MET A 192 9.594 75.162 195.245 1.00 70.84 O
ANISOU 1401 O MET A 192 7819 6652 12444 -215 1139 772 O
ATOM 1402 CB MET A 192 8.769 73.061 197.673 1.00 76.71 C
ANISOU 1402 CB MET A 192 8797 7273 13077 -300 1566 1140 C
ATOM 1403 CG MET A 192 8.966 74.213 198.608 1.00 82.52 C
ANISOU 1403 CG MET A 192 9769 8090 13496 -275 1749 1063 C
ATOM 1404 SD MET A 192 7.450 74.621 199.492 1.00 91.19 S
ANISOU 1404 SD MET A 192 10842 9102 14703 -280 2251 1126 S
ATOM 1405 CE MET A 192 7.932 74.144 201.156 1.00 90.81 C
ANISOU 1405 CE MET A 192 11213 9113 14176 -335 2421 1251 C
ATOM 1406 N PHE A 193 10.140 72.998 194.788 1.00 65.99 N
ANISOU 1406 N PHE A 193 7155 5968 11950 -271 889 886 N
ATOM 1407 CA PHE A 193 11.249 73.254 193.870 1.00 63.00 C
ANISOU 1407 CA PHE A 193 6783 5663 11490 -248 627 752 C
ATOM 1408 C PHE A 193 10.753 73.995 192.616 1.00 65.00 C
ANISOU 1408 C PHE A 193 6855 5929 11914 -249 546 648 C
ATOM 1409 O PHE A 193 11.425 74.920 192.160 1.00 63.20 O
ANISOU 1409 O PHE A 193 6666 5785 11561 -221 449 542 O
ATOM 1410 CB PHE A 193 11.945 71.930 193.489 1.00 64.35 C
ANISOU 1410 CB PHE A 193 6943 5779 11727 -265 447 778 C
ATOM 1411 CG PHE A 193 12.928 72.022 192.343 1.00 64.08 C
ANISOU 1411 CG PHE A 193 6873 5792 11682 -248 223 632 C
ATOM 1412 CD1 PHE A 193 14.232 72.457 192.556 1.00 66.03 C
ANISOU 1412 CD1 PHE A 193 7242 6124 11722 -207 123 579 C
ATOM 1413 CD2 PHE A 193 12.552 71.667 191.051 1.00 65.79 C
ANISOU 1413 CD2 PHE A 193 6938 5965 12095 -283 115 547 C
ATOM 1414 CE1 PHE A 193 15.140 72.542 191.496 1.00 65.57 C
ANISOU 1414 CE1 PHE A 193 7137 6102 11676 -191 -37 451 C
ATOM 1415 CE2 PHE A 193 13.456 71.767 189.989 1.00 67.36 C
ANISOU 1415 CE2 PHE A 193 7132 6212 12249 -274 -48 406 C
ATOM 1416 CZ PHE A 193 14.742 72.209 190.217 1.00 64.43 C
ANISOU 1416 CZ PHE A 193 6866 5921 11695 -223 -101 362 C
ATOM 1417 N LEU A 194 9.593 73.579 192.060 1.00 61.95 N
ANISOU 1417 N LEU A 194 6269 5453 11818 -291 568 696 N
ATOM 1418 CA LEU A 194 9.001 74.190 190.865 1.00 60.85 C
ANISOU 1418 CA LEU A 194 5950 5316 11854 -309 451 636 C
ATOM 1419 C LEU A 194 8.438 75.577 191.174 1.00 65.07 C
ANISOU 1419 C LEU A 194 6445 5869 12409 -261 606 638 C
ATOM 1420 O LEU A 194 8.580 76.476 190.345 1.00 64.10 O
ANISOU 1420 O LEU A 194 6274 5796 12285 -248 482 572 O
ATOM 1421 CB LEU A 194 7.914 73.294 190.244 1.00 61.89 C
ANISOU 1421 CB LEU A 194 5871 5332 12310 -384 390 697 C
ATOM 1422 CG LEU A 194 8.376 71.996 189.564 1.00 65.85 C
ANISOU 1422 CG LEU A 194 6384 5787 12848 -444 197 648 C
ATOM 1423 CD1 LEU A 194 7.201 71.237 189.020 1.00 67.39 C
ANISOU 1423 CD1 LEU A 194 6372 5855 13378 -536 133 699 C
ATOM 1424 CD2 LEU A 194 9.348 72.266 188.422 1.00 66.34 C
ANISOU 1424 CD2 LEU A 194 6518 5942 12746 -444 -26 492 C
ATOM 1425 N LEU A 195 7.832 75.759 192.373 1.00 62.55 N
ANISOU 1425 N LEU A 195 6160 5501 12105 -237 894 715 N
ATOM 1426 CA LEU A 195 7.301 77.049 192.828 1.00 62.82 C
ANISOU 1426 CA LEU A 195 6175 5522 12172 -182 1104 697 C
ATOM 1427 C LEU A 195 8.438 78.046 193.053 1.00 65.86 C
ANISOU 1427 C LEU A 195 6773 6007 12245 -138 1060 575 C
ATOM 1428 O LEU A 195 8.268 79.228 192.763 1.00 65.58 O
ANISOU 1428 O LEU A 195 6683 5964 12269 -99 1085 520 O
ATOM 1429 CB LEU A 195 6.464 76.899 194.108 1.00 65.07 C
ANISOU 1429 CB LEU A 195 6486 5727 12509 -173 1468 788 C
ATOM 1430 CG LEU A 195 5.011 76.457 193.916 1.00 71.74 C
ANISOU 1430 CG LEU A 195 7039 6438 13782 -201 1596 913 C
ATOM 1431 CD1 LEU A 195 4.479 75.783 195.163 1.00 74.22 C
ANISOU 1431 CD1 LEU A 195 7422 6686 14092 -221 1931 1028 C
ATOM 1432 CD2 LEU A 195 4.112 77.629 193.523 1.00 74.77 C
ANISOU 1432 CD2 LEU A 195 7199 6752 14460 -151 1686 905 C
ATOM 1433 N GLU A 196 9.615 77.556 193.505 1.00 61.64 N
ANISOU 1433 N GLU A 196 6455 5550 11416 -150 968 543 N
ATOM 1434 CA GLU A 196 10.822 78.360 193.731 1.00 60.36 C
ANISOU 1434 CA GLU A 196 6483 5478 10973 -127 882 435 C
ATOM 1435 C GLU A 196 11.468 78.813 192.407 1.00 61.70 C
ANISOU 1435 C GLU A 196 6563 5701 11180 -125 630 356 C
ATOM 1436 O GLU A 196 12.467 79.537 192.428 1.00 60.94 O
ANISOU 1436 O GLU A 196 6580 5668 10905 -113 547 271 O
ATOM 1437 CB GLU A 196 11.834 77.582 194.575 1.00 61.96 C
ANISOU 1437 CB GLU A 196 6901 5732 10909 -147 823 460 C
ATOM 1438 CG GLU A 196 11.595 77.734 196.065 1.00 75.36 C
ANISOU 1438 CG GLU A 196 8810 7422 12402 -153 1066 497 C
ATOM 1439 CD GLU A 196 12.063 76.576 196.924 1.00 97.95 C
ANISOU 1439 CD GLU A 196 11835 10296 15086 -189 1037 616 C
ATOM 1440 OE1 GLU A 196 13.085 75.936 196.580 1.00 92.38 O
ANISOU 1440 OE1 GLU A 196 11140 9625 14334 -195 786 630 O
ATOM 1441 OE2 GLU A 196 11.413 76.324 197.963 1.00 94.91 O
ANISOU 1441 OE2 GLU A 196 11568 9879 14616 -210 1281 704 O
ATOM 1442 N PHE A 197 10.893 78.391 191.265 1.00 56.47 N
ANISOU 1442 N PHE A 197 5705 5010 10739 -150 509 388 N
ATOM 1443 CA PHE A 197 11.340 78.777 189.934 1.00 54.29 C
ANISOU 1443 CA PHE A 197 5360 4787 10482 -164 292 331 C
ATOM 1444 C PHE A 197 10.255 79.574 189.210 1.00 58.93 C
ANISOU 1444 C PHE A 197 5760 5324 11305 -163 288 375 C
ATOM 1445 O PHE A 197 10.570 80.608 188.625 1.00 57.88 O
ANISOU 1445 O PHE A 197 5623 5225 11145 -149 212 342 O
ATOM 1446 CB PHE A 197 11.748 77.550 189.097 1.00 54.98 C
ANISOU 1446 CB PHE A 197 5422 4890 10578 -212 110 315 C
ATOM 1447 CG PHE A 197 11.912 77.839 187.621 1.00 55.11 C
ANISOU 1447 CG PHE A 197 5371 4953 10617 -248 -84 265 C
ATOM 1448 CD1 PHE A 197 13.076 78.423 187.134 1.00 56.47 C
ANISOU 1448 CD1 PHE A 197 5632 5210 10613 -238 -167 185 C
ATOM 1449 CD2 PHE A 197 10.892 77.550 186.721 1.00 57.73 C
ANISOU 1449 CD2 PHE A 197 5553 5242 11139 -304 -186 306 C
ATOM 1450 CE1 PHE A 197 13.218 78.705 185.773 1.00 56.98 C
ANISOU 1450 CE1 PHE A 197 5663 5324 10661 -281 -317 152 C
ATOM 1451 CE2 PHE A 197 11.037 77.833 185.361 1.00 60.16 C
ANISOU 1451 CE2 PHE A 197 5841 5606 11412 -354 -378 268 C
ATOM 1452 CZ PHE A 197 12.198 78.407 184.897 1.00 56.87 C
ANISOU 1452 CZ PHE A 197 5539 5281 10788 -341 -426 193 C
ATOM 1453 N PHE A 198 8.998 79.073 189.209 1.00 56.69 N
ANISOU 1453 N PHE A 198 5307 4951 11280 -184 350 467 N
ATOM 1454 CA PHE A 198 7.887 79.701 188.498 1.00 57.44 C
ANISOU 1454 CA PHE A 198 5180 4981 11664 -188 306 542 C
ATOM 1455 C PHE A 198 7.465 81.036 189.108 1.00 63.99 C
ANISOU 1455 C PHE A 198 5975 5749 12590 -111 513 552 C
ATOM 1456 O PHE A 198 7.105 81.931 188.343 1.00 64.41 O
ANISOU 1456 O PHE A 198 5898 5775 12799 -98 411 592 O
ATOM 1457 CB PHE A 198 6.690 78.757 188.370 1.00 60.28 C
ANISOU 1457 CB PHE A 198 5339 5245 12318 -239 304 643 C
ATOM 1458 CG PHE A 198 6.896 77.679 187.329 1.00 60.98 C
ANISOU 1458 CG PHE A 198 5416 5367 12387 -331 33 619 C
ATOM 1459 CD1 PHE A 198 7.080 78.006 185.989 1.00 63.44 C
ANISOU 1459 CD1 PHE A 198 5706 5740 12660 -380 -239 592 C
ATOM 1460 CD2 PHE A 198 6.883 76.336 187.685 1.00 62.80 C
ANISOU 1460 CD2 PHE A 198 5672 5554 12636 -376 58 623 C
ATOM 1461 CE1 PHE A 198 7.274 77.009 185.028 1.00 64.17 C
ANISOU 1461 CE1 PHE A 198 5826 5856 12700 -476 -466 536 C
ATOM 1462 CE2 PHE A 198 7.070 75.340 186.723 1.00 65.40 C
ANISOU 1462 CE2 PHE A 198 6002 5887 12961 -463 -175 569 C
ATOM 1463 CZ PHE A 198 7.260 75.683 185.400 1.00 63.22 C
ANISOU 1463 CZ PHE A 198 5726 5677 12620 -514 -430 511 C
ATOM 1464 N LEU A 199 7.530 81.191 190.453 1.00 61.73 N
ANISOU 1464 N LEU A 199 5819 5433 12203 -64 796 516 N
ATOM 1465 CA LEU A 199 7.209 82.464 191.110 1.00 62.53 C
ANISOU 1465 CA LEU A 199 5929 5458 12371 8 1029 481 C
ATOM 1466 C LEU A 199 8.269 83.517 190.698 1.00 63.87 C
ANISOU 1466 C LEU A 199 6224 5690 12353 24 891 386 C
ATOM 1467 O LEU A 199 7.847 84.510 190.104 1.00 63.98 O
ANISOU 1467 O LEU A 199 6097 5638 12576 56 856 419 O
ATOM 1468 CB LEU A 199 7.062 82.334 192.644 1.00 64.21 C
ANISOU 1468 CB LEU A 199 6306 5633 12458 33 1374 443 C
ATOM 1469 CG LEU A 199 6.893 83.628 193.461 1.00 71.03 C
ANISOU 1469 CG LEU A 199 7254 6414 13319 101 1653 349 C
ATOM 1470 CD1 LEU A 199 5.617 84.382 193.085 1.00 73.14 C
ANISOU 1470 CD1 LEU A 199 7225 6523 14043 162 1788 421 C
ATOM 1471 CD2 LEU A 199 6.895 83.332 194.946 1.00 75.80 C
ANISOU 1471 CD2 LEU A 199 8095 7013 13692 97 1968 298 C
ATOM 1472 N PRO A 200 9.614 83.301 190.857 1.00 58.11 N
ANISOU 1472 N PRO A 200 5716 5075 11287 -4 778 294 N
ATOM 1473 CA PRO A 200 10.583 84.294 190.357 1.00 56.21 C
ANISOU 1473 CA PRO A 200 5551 4880 10926 -1 643 222 C
ATOM 1474 C PRO A 200 10.471 84.532 188.846 1.00 58.16 C
ANISOU 1474 C PRO A 200 5637 5149 11312 -25 405 297 C
ATOM 1475 O PRO A 200 10.611 85.677 188.422 1.00 58.08 O
ANISOU 1475 O PRO A 200 5598 5106 11364 -6 370 298 O
ATOM 1476 CB PRO A 200 11.937 83.672 190.708 1.00 56.79 C
ANISOU 1476 CB PRO A 200 5829 5067 10684 -37 541 147 C
ATOM 1477 CG PRO A 200 11.658 82.792 191.850 1.00 62.62 C
ANISOU 1477 CG PRO A 200 6664 5793 11334 -39 700 160 C
ATOM 1478 CD PRO A 200 10.328 82.190 191.522 1.00 59.43 C
ANISOU 1478 CD PRO A 200 6057 5318 11205 -38 769 270 C
ATOM 1479 N LEU A 201 10.188 83.473 188.046 1.00 53.60 N
ANISOU 1479 N LEU A 201 4969 4616 10780 -77 244 360 N
ATOM 1480 CA LEU A 201 9.998 83.563 186.588 1.00 53.17 C
ANISOU 1480 CA LEU A 201 4798 4595 10810 -125 1 432 C
ATOM 1481 C LEU A 201 8.821 84.487 186.261 1.00 57.74 C
ANISOU 1481 C LEU A 201 5170 5060 11708 -93 10 551 C
ATOM 1482 O LEU A 201 8.945 85.341 185.384 1.00 57.61 O
ANISOU 1482 O LEU A 201 5117 5051 11722 -102 -134 608 O
ATOM 1483 CB LEU A 201 9.773 82.164 185.964 1.00 53.26 C
ANISOU 1483 CB LEU A 201 4771 4648 10817 -197 -150 449 C
ATOM 1484 CG LEU A 201 9.442 82.102 184.464 1.00 58.30 C
ANISOU 1484 CG LEU A 201 5322 5323 11506 -273 -416 513 C
ATOM 1485 CD1 LEU A 201 10.691 82.196 183.619 1.00 57.15 C
ANISOU 1485 CD1 LEU A 201 5337 5298 11081 -313 -545 437 C
ATOM 1486 CD2 LEU A 201 8.691 80.835 184.130 1.00 61.63 C
ANISOU 1486 CD2 LEU A 201 5654 5718 12045 -344 -520 538 C
ATOM 1487 N GLY A 202 7.713 84.312 186.986 1.00 54.71 N
ANISOU 1487 N GLY A 202 4648 4563 11576 -55 191 602 N
ATOM 1488 CA GLY A 202 6.508 85.118 186.853 1.00 56.08 C
ANISOU 1488 CA GLY A 202 4580 4594 12134 -8 245 723 C
ATOM 1489 C GLY A 202 6.769 86.574 187.164 1.00 60.01 C
ANISOU 1489 C GLY A 202 5113 5014 12673 69 374 690 C
ATOM 1490 O GLY A 202 6.308 87.449 186.430 1.00 60.87 O
ANISOU 1490 O GLY A 202 5063 5047 13017 88 259 804 O
ATOM 1491 N ILE A 203 7.560 86.837 188.223 1.00 55.88 N
ANISOU 1491 N ILE A 203 4810 4505 11917 102 584 537 N
ATOM 1492 CA ILE A 203 7.946 88.184 188.648 1.00 56.49 C
ANISOU 1492 CA ILE A 203 4966 4498 11999 160 718 458 C
ATOM 1493 C ILE A 203 8.839 88.838 187.570 1.00 60.87 C
ANISOU 1493 C ILE A 203 5565 5121 12443 122 458 487 C
ATOM 1494 O ILE A 203 8.533 89.951 187.146 1.00 61.70 O
ANISOU 1494 O ILE A 203 5558 5114 12771 159 438 561 O
ATOM 1495 CB ILE A 203 8.627 88.171 190.048 1.00 59.20 C
ANISOU 1495 CB ILE A 203 5570 4856 12067 173 960 275 C
ATOM 1496 CG1 ILE A 203 7.640 87.703 191.142 1.00 61.27 C
ANISOU 1496 CG1 ILE A 203 5803 5032 12446 212 1276 264 C
ATOM 1497 CG2 ILE A 203 9.204 89.549 190.397 1.00 60.15 C
ANISOU 1497 CG2 ILE A 203 5805 4891 12157 207 1047 163 C
ATOM 1498 CD1 ILE A 203 8.288 87.056 192.371 1.00 67.54 C
ANISOU 1498 CD1 ILE A 203 6881 5908 12875 182 1427 139 C
ATOM 1499 N ILE A 204 9.908 88.141 187.114 1.00 56.72 N
ANISOU 1499 N ILE A 204 5185 4763 11601 48 277 443 N
ATOM 1500 CA ILE A 204 10.851 88.635 186.100 1.00 56.17 C
ANISOU 1500 CA ILE A 204 5175 4774 11394 0 71 467 C
ATOM 1501 C ILE A 204 10.127 88.926 184.773 1.00 63.02 C
ANISOU 1501 C ILE A 204 5866 5624 12455 -26 -141 655 C
ATOM 1502 O ILE A 204 10.310 90.017 184.234 1.00 63.65 O
ANISOU 1502 O ILE A 204 5920 5653 12612 -21 -206 730 O
ATOM 1503 CB ILE A 204 12.056 87.673 185.910 1.00 57.43 C
ANISOU 1503 CB ILE A 204 5499 5102 11221 -65 -35 379 C
ATOM 1504 CG1 ILE A 204 12.961 87.712 187.159 1.00 57.17 C
ANISOU 1504 CG1 ILE A 204 5644 5077 11002 -47 114 223 C
ATOM 1505 CG2 ILE A 204 12.868 88.013 184.638 1.00 57.90 C
ANISOU 1505 CG2 ILE A 204 5588 5250 11160 -126 -230 429 C
ATOM 1506 CD1 ILE A 204 13.906 86.585 187.296 1.00 62.21 C
ANISOU 1506 CD1 ILE A 204 6399 5838 11397 -88 46 154 C
ATOM 1507 N LEU A 205 9.294 87.984 184.273 1.00 60.78 N
ANISOU 1507 N LEU A 205 5464 5370 12258 -64 -263 741 N
ATOM 1508 CA LEU A 205 8.556 88.168 183.018 1.00 62.14 C
ANISOU 1508 CA LEU A 205 5482 5535 12594 -111 -517 928 C
ATOM 1509 C LEU A 205 7.569 89.341 183.100 1.00 68.33 C
ANISOU 1509 C LEU A 205 6051 6131 13781 -33 -469 1073 C
ATOM 1510 O LEU A 205 7.445 90.082 182.123 1.00 69.25 O
ANISOU 1510 O LEU A 205 6101 6228 13983 -58 -670 1234 O
ATOM 1511 CB LEU A 205 7.820 86.887 182.586 1.00 62.68 C
ANISOU 1511 CB LEU A 205 5464 5652 12698 -180 -667 969 C
ATOM 1512 CG LEU A 205 8.682 85.711 182.091 1.00 66.09 C
ANISOU 1512 CG LEU A 205 6082 6250 12778 -272 -783 857 C
ATOM 1513 CD1 LEU A 205 7.836 84.473 181.900 1.00 67.16 C
ANISOU 1513 CD1 LEU A 205 6120 6382 13015 -334 -888 875 C
ATOM 1514 CD2 LEU A 205 9.409 86.038 180.785 1.00 68.39 C
ANISOU 1514 CD2 LEU A 205 6497 6658 12831 -353 -1000 897 C
ATOM 1515 N PHE A 206 6.899 89.529 184.262 1.00 65.34 N
ANISOU 1515 N PHE A 206 5572 5605 13650 61 -188 1020 N
ATOM 1516 CA PHE A 206 5.949 90.631 184.474 1.00 67.16 C
ANISOU 1516 CA PHE A 206 5580 5618 14320 156 -75 1131 C
ATOM 1517 C PHE A 206 6.689 91.968 184.507 1.00 71.33 C
ANISOU 1517 C PHE A 206 6208 6073 14823 198 -16 1099 C
ATOM 1518 O PHE A 206 6.261 92.906 183.835 1.00 72.95 O
ANISOU 1518 O PHE A 206 6257 6159 15301 223 -138 1274 O
ATOM 1519 CB PHE A 206 5.126 90.430 185.765 1.00 69.78 C
ANISOU 1519 CB PHE A 206 5812 5812 14889 243 278 1048 C
ATOM 1520 CG PHE A 206 4.295 91.618 186.203 1.00 73.43 C
ANISOU 1520 CG PHE A 206 6074 6022 15805 362 496 1101 C
ATOM 1521 CD1 PHE A 206 3.029 91.835 185.672 1.00 78.55 C
ANISOU 1521 CD1 PHE A 206 6376 6523 16948 399 401 1319 C
ATOM 1522 CD2 PHE A 206 4.770 92.504 187.165 1.00 75.36 C
ANISOU 1522 CD2 PHE A 206 6469 6160 16005 435 796 925 C
ATOM 1523 CE1 PHE A 206 2.263 92.931 186.079 1.00 81.97 C
ANISOU 1523 CE1 PHE A 206 6595 6693 17855 525 626 1370 C
ATOM 1524 CE2 PHE A 206 4.006 93.602 187.567 1.00 80.56 C
ANISOU 1524 CE2 PHE A 206 6948 6558 17104 551 1030 949 C
ATOM 1525 CZ PHE A 206 2.754 93.804 187.027 1.00 81.13 C
ANISOU 1525 CZ PHE A 206 6654 6472 17697 604 958 1174 C
ATOM 1526 N CYS A 207 7.783 92.053 185.299 1.00 66.05 N
ANISOU 1526 N CYS A 207 5787 5459 13850 197 153 888 N
ATOM 1527 CA CYS A 207 8.603 93.256 185.447 1.00 65.60 C
ANISOU 1527 CA CYS A 207 5844 5327 13754 218 216 822 C
ATOM 1528 C CYS A 207 9.233 93.638 184.116 1.00 68.03 C
ANISOU 1528 C CYS A 207 6174 5723 13952 143 -75 971 C
ATOM 1529 O CYS A 207 9.171 94.805 183.752 1.00 69.21 O
ANISOU 1529 O CYS A 207 6250 5733 14315 172 -104 1079 O
ATOM 1530 CB CYS A 207 9.659 93.074 186.533 1.00 64.46 C
ANISOU 1530 CB CYS A 207 5959 5247 13284 205 395 572 C
ATOM 1531 SG CYS A 207 8.978 92.959 188.207 1.00 69.70 S
ANISOU 1531 SG CYS A 207 6664 5781 14038 287 789 392 S
ATOM 1532 N SER A 208 9.775 92.657 183.366 1.00 62.21 N
ANISOU 1532 N SER A 208 5534 5199 12902 46 -276 988 N
ATOM 1533 CA SER A 208 10.379 92.883 182.051 1.00 61.57 C
ANISOU 1533 CA SER A 208 5509 5227 12657 -42 -525 1124 C
ATOM 1534 C SER A 208 9.349 93.437 181.072 1.00 67.53 C
ANISOU 1534 C SER A 208 6068 5893 13699 -44 -733 1395 C
ATOM 1535 O SER A 208 9.663 94.369 180.339 1.00 68.66 O
ANISOU 1535 O SER A 208 6219 6000 13869 -68 -845 1541 O
ATOM 1536 CB SER A 208 10.999 91.601 181.508 1.00 63.32 C
ANISOU 1536 CB SER A 208 5871 5674 12515 -138 -652 1060 C
ATOM 1537 OG SER A 208 12.035 91.160 182.370 1.00 69.88 O
ANISOU 1537 OG SER A 208 6864 6573 13115 -134 -490 844 O
ATOM 1538 N ALA A 209 8.109 92.919 181.110 1.00 64.78 N
ANISOU 1538 N ALA A 209 5526 5490 13598 -17 -784 1479 N
ATOM 1539 CA ALA A 209 7.015 93.396 180.265 1.00 66.91 C
ANISOU 1539 CA ALA A 209 5565 5655 14202 -17 -1013 1756 C
ATOM 1540 C ALA A 209 6.609 94.821 180.658 1.00 72.09 C
ANISOU 1540 C ALA A 209 6061 6053 15279 99 -876 1849 C
ATOM 1541 O ALA A 209 6.421 95.653 179.777 1.00 73.86 O
ANISOU 1541 O ALA A 209 6201 6206 15656 84 -1082 2088 O
ATOM 1542 CB ALA A 209 5.821 92.460 180.370 1.00 68.57 C
ANISOU 1542 CB ALA A 209 5579 5849 14628 -17 -1076 1801 C
ATOM 1543 N ARG A 210 6.529 95.107 181.975 1.00 67.57 N
ANISOU 1543 N ARG A 210 5470 5333 14869 208 -523 1655 N
ATOM 1544 CA ARG A 210 6.148 96.408 182.535 1.00 68.97 C
ANISOU 1544 CA ARG A 210 5513 5232 15459 329 -317 1674 C
ATOM 1545 C ARG A 210 7.191 97.503 182.276 1.00 71.15 C
ANISOU 1545 C ARG A 210 5942 5465 15628 310 -329 1672 C
ATOM 1546 O ARG A 210 6.806 98.615 181.929 1.00 72.77 O
ANISOU 1546 O ARG A 210 5996 5462 16193 364 -371 1849 O
ATOM 1547 CB ARG A 210 5.892 96.286 184.042 1.00 70.35 C
ANISOU 1547 CB ARG A 210 5704 5293 15734 425 90 1418 C
ATOM 1548 CG ARG A 210 4.504 95.748 184.384 1.00 84.95 C
ANISOU 1548 CG ARG A 210 7284 7041 17952 491 189 1487 C
ATOM 1549 CD ARG A 210 3.611 96.796 185.026 1.00 98.39 C
ANISOU 1549 CD ARG A 210 8758 8418 20207 639 472 1503 C
ATOM 1550 NE ARG A 210 3.357 97.926 184.131 1.00109.69 N
ANISOU 1550 NE ARG A 210 10007 9679 21990 672 265 1754 N
ATOM 1551 CZ ARG A 210 2.704 99.028 184.483 1.00130.86 C
ANISOU 1551 CZ ARG A 210 12480 12043 25198 805 467 1800 C
ATOM 1552 NH1 ARG A 210 2.222 99.158 185.714 1.00123.01 N
ANISOU 1552 NH1 ARG A 210 11445 10871 24422 915 911 1588 N
ATOM 1553 NH2 ARG A 210 2.522 100.006 183.607 1.00120.77 N
ANISOU 1553 NH2 ARG A 210 11039 10612 24235 829 240 2062 N
ATOM 1554 N ILE A 211 8.496 97.188 182.434 1.00 64.64 N
ANISOU 1554 N ILE A 211 5392 4818 14351 231 -299 1488 N
ATOM 1555 CA ILE A 211 9.621 98.112 182.244 1.00 63.68 C
ANISOU 1555 CA ILE A 211 5419 4670 14108 193 -298 1464 C
ATOM 1556 C ILE A 211 9.775 98.467 180.750 1.00 69.13 C
ANISOU 1556 C ILE A 211 6085 5427 14754 108 -610 1763 C
ATOM 1557 O ILE A 211 9.801 99.654 180.430 1.00 70.84 O
ANISOU 1557 O ILE A 211 6236 5464 15216 131 -635 1913 O
ATOM 1558 CB ILE A 211 10.937 97.536 182.855 1.00 63.72 C
ANISOU 1558 CB ILE A 211 5687 4849 13674 128 -193 1196 C
ATOM 1559 CG1 ILE A 211 10.866 97.478 184.395 1.00 63.57 C
ANISOU 1559 CG1 ILE A 211 5734 4732 13686 200 112 917 C
ATOM 1560 CG2 ILE A 211 12.173 98.323 182.410 1.00 63.85 C
ANISOU 1560 CG2 ILE A 211 5832 4876 13551 55 -248 1211 C
ATOM 1561 CD1 ILE A 211 11.801 96.427 185.028 1.00 66.22 C
ANISOU 1561 CD1 ILE A 211 6287 5278 13597 139 158 697 C
ATOM 1562 N ILE A 212 9.880 97.455 179.853 1.00 65.27 N
ANISOU 1562 N ILE A 212 5666 5184 13948 6 -838 1846 N
ATOM 1563 CA ILE A 212 10.037 97.644 178.402 1.00 66.48 C
ANISOU 1563 CA ILE A 212 5855 5441 13962 -99 -1134 2117 C
ATOM 1564 C ILE A 212 8.877 98.499 177.859 1.00 75.56 C
ANISOU 1564 C ILE A 212 6762 6390 15557 -49 -1309 2434 C
ATOM 1565 O ILE A 212 9.137 99.458 177.135 1.00 76.81 O
ANISOU 1565 O ILE A 212 6929 6475 15780 -81 -1428 2655 O
ATOM 1566 CB ILE A 212 10.180 96.287 177.638 1.00 68.16 C
ANISOU 1566 CB ILE A 212 6196 5935 13765 -216 -1321 2103 C
ATOM 1567 CG1 ILE A 212 11.543 95.618 177.942 1.00 65.57 C
ANISOU 1567 CG1 ILE A 212 6104 5789 13019 -271 -1170 1844 C
ATOM 1568 CG2 ILE A 212 9.990 96.460 176.114 1.00 70.82 C
ANISOU 1568 CG2 ILE A 212 6566 6365 13976 -330 -1653 2408 C
ATOM 1569 CD1 ILE A 212 11.622 94.107 177.662 1.00 69.20 C
ANISOU 1569 CD1 ILE A 212 6669 6470 13154 -344 -1246 1725 C
ATOM 1570 N TRP A 213 7.619 98.179 178.243 1.00 75.10 N
ANISOU 1570 N TRP A 213 6473 6223 15838 32 -1315 2469 N
ATOM 1571 CA TRP A 213 6.414 98.898 177.810 1.00 79.21 C
ANISOU 1571 CA TRP A 213 6704 6529 16863 95 -1488 2776 C
ATOM 1572 C TRP A 213 6.432 100.366 178.284 1.00 83.83 C
ANISOU 1572 C TRP A 213 7180 6804 17867 211 -1299 2821 C
ATOM 1573 O TRP A 213 6.100 101.253 177.496 1.00 86.27 O
ANISOU 1573 O TRP A 213 7367 6978 18435 212 -1507 3137 O
ATOM 1574 CB TRP A 213 5.146 98.172 178.306 1.00 79.60 C
ANISOU 1574 CB TRP A 213 6505 6514 17224 163 -1465 2757 C
ATOM 1575 CG TRP A 213 3.829 98.729 177.835 1.00 85.04 C
ANISOU 1575 CG TRP A 213 6846 6990 18474 223 -1676 3086 C
ATOM 1576 CD1 TRP A 213 3.596 99.464 176.708 1.00 90.74 C
ANISOU 1576 CD1 TRP A 213 7491 7658 19329 176 -2021 3447 C
ATOM 1577 CD2 TRP A 213 2.548 98.514 178.445 1.00 86.98 C
ANISOU 1577 CD2 TRP A 213 6762 7055 19233 331 -1576 3106 C
ATOM 1578 NE1 TRP A 213 2.260 99.781 176.616 1.00 93.83 N
ANISOU 1578 NE1 TRP A 213 7505 7825 20320 260 -2158 3696 N
ATOM 1579 CE2 TRP A 213 1.589 99.200 177.662 1.00 94.85 C
ANISOU 1579 CE2 TRP A 213 7460 7871 20709 357 -1878 3487 C
ATOM 1580 CE3 TRP A 213 2.116 97.829 179.597 1.00 87.36 C
ANISOU 1580 CE3 TRP A 213 6730 7063 19399 408 -1246 2855 C
ATOM 1581 CZ2 TRP A 213 0.228 99.219 177.990 1.00 97.07 C
ANISOU 1581 CZ2 TRP A 213 7335 7927 21622 464 -1856 3615 C
ATOM 1582 CZ3 TRP A 213 0.767 97.848 179.920 1.00 91.77 C
ANISOU 1582 CZ3 TRP A 213 6908 7407 20555 509 -1192 2975 C
ATOM 1583 CH2 TRP A 213 -0.160 98.539 179.125 1.00 96.25 C
ANISOU 1583 CH2 TRP A 213 7151 7788 21634 540 -1491 3346 C
ATOM 1584 N SER A 214 6.849 100.619 179.541 1.00 78.09 N
ANISOU 1584 N SER A 214 6517 5964 17189 297 -921 2510 N
ATOM 1585 CA SER A 214 6.927 101.964 180.121 1.00 79.17 C
ANISOU 1585 CA SER A 214 6586 5790 17706 401 -700 2478 C
ATOM 1586 C SER A 214 8.063 102.788 179.508 1.00 82.60 C
ANISOU 1586 C SER A 214 7195 6234 17953 316 -788 2565 C
ATOM 1587 O SER A 214 7.884 103.989 179.275 1.00 84.12 O
ANISOU 1587 O SER A 214 7268 6166 18529 367 -803 2750 O
ATOM 1588 CB SER A 214 7.104 101.892 181.633 1.00 81.66 C
ANISOU 1588 CB SER A 214 6980 6012 18034 485 -289 2089 C
ATOM 1589 OG SER A 214 6.022 101.211 182.247 1.00 91.57 O
ANISOU 1589 OG SER A 214 8064 7229 19499 567 -155 2024 O
ATOM 1590 N LEU A 215 9.227 102.150 179.251 1.00 76.15 N
ANISOU 1590 N LEU A 215 6646 5699 16588 188 -831 2441 N
ATOM 1591 CA LEU A 215 10.388 102.830 178.672 1.00 75.66 C
ANISOU 1591 CA LEU A 215 6748 5667 16332 92 -883 2516 C
ATOM 1592 C LEU A 215 10.218 103.093 177.178 1.00 81.29 C
ANISOU 1592 C LEU A 215 7437 6449 17001 2 -1218 2923 C
ATOM 1593 O LEU A 215 10.661 104.142 176.711 1.00 82.28 O
ANISOU 1593 O LEU A 215 7576 6441 17245 -27 -1254 3107 O
ATOM 1594 CB LEU A 215 11.689 102.056 178.917 1.00 72.55 C
ANISOU 1594 CB LEU A 215 6614 5533 15420 -8 -794 2254 C
ATOM 1595 CG LEU A 215 12.212 101.993 180.357 1.00 75.61 C
ANISOU 1595 CG LEU A 215 7090 5857 15780 43 -496 1870 C
ATOM 1596 CD1 LEU A 215 13.411 101.101 180.435 1.00 72.97 C
ANISOU 1596 CD1 LEU A 215 6969 5792 14963 -58 -481 1678 C
ATOM 1597 CD2 LEU A 215 12.579 103.373 180.897 1.00 79.92 C
ANISOU 1597 CD2 LEU A 215 7623 6109 16636 83 -336 1809 C
ATOM 1598 N ARG A 216 9.582 102.158 176.432 1.00 78.30 N
ANISOU 1598 N ARG A 216 7035 6269 16444 -53 -1470 3068 N
ATOM 1599 CA ARG A 216 9.334 102.309 174.993 1.00 80.71 C
ANISOU 1599 CA ARG A 216 7354 6665 16647 -158 -1827 3457 C
ATOM 1600 C ARG A 216 8.317 103.423 174.735 1.00 89.36 C
ANISOU 1600 C ARG A 216 8178 7453 18321 -69 -1971 3795 C
ATOM 1601 O ARG A 216 8.369 104.060 173.682 1.00 91.58 O
ANISOU 1601 O ARG A 216 8485 7719 18592 -145 -2216 4148 O
ATOM 1602 CB ARG A 216 8.858 100.993 174.364 1.00 80.91 C
ANISOU 1602 CB ARG A 216 7433 6962 16348 -249 -2068 3481 C
ATOM 1603 CG ARG A 216 9.506 100.702 173.017 1.00 94.24 C
ANISOU 1603 CG ARG A 216 9374 8909 17523 -431 -2305 3659 C
ATOM 1604 CD ARG A 216 9.990 99.267 172.924 1.00105.15 C
ANISOU 1604 CD ARG A 216 10964 10594 18393 -524 -2281 3399 C
ATOM 1605 NE ARG A 216 11.074 99.126 171.947 1.00117.56 N
ANISOU 1605 NE ARG A 216 12828 12388 19451 -679 -2317 3444 N
ATOM 1606 CZ ARG A 216 11.868 98.062 171.847 1.00129.65 C
ANISOU 1606 CZ ARG A 216 14573 14158 20528 -758 -2215 3196 C
ATOM 1607 NH1 ARG A 216 11.713 97.027 172.664 1.00113.59 N
ANISOU 1607 NH1 ARG A 216 12503 12177 18480 -703 -2099 2900 N
ATOM 1608 NH2 ARG A 216 12.829 98.029 170.932 1.00116.03 N
ANISOU 1608 NH2 ARG A 216 13098 12608 18378 -892 -2208 3250 N
ATOM 1609 N GLN A 217 7.406 103.663 175.704 1.00 87.22 N
ANISOU 1609 N GLN A 217 7649 6928 18563 94 -1803 3695 N
ATOM 1610 CA GLN A 217 6.389 104.715 175.644 1.00 90.83 C
ANISOU 1610 CA GLN A 217 7796 7038 19677 215 -1878 3977 C
ATOM 1611 C GLN A 217 7.040 106.078 175.919 1.00 96.32 C
ANISOU 1611 C GLN A 217 8513 7462 20622 264 -1686 3987 C
ATOM 1612 O GLN A 217 6.742 107.041 175.211 1.00 99.07 O
ANISOU 1612 O GLN A 217 8737 7616 21291 273 -1878 4355 O
ATOM 1613 CB GLN A 217 5.242 104.426 176.636 1.00 92.55 C
ANISOU 1613 CB GLN A 217 7733 7076 20357 373 -1694 3826 C
ATOM 1614 CG GLN A 217 4.078 105.424 176.603 1.00108.66 C
ANISOU 1614 CG GLN A 217 9395 8733 23158 519 -1751 4114 C
ATOM 1615 CD GLN A 217 3.404 105.530 175.254 1.00129.32 C
ANISOU 1615 CD GLN A 217 11868 11380 25887 445 -2255 4611 C
ATOM 1616 OE1 GLN A 217 2.890 104.550 174.704 1.00123.44 O
ANISOU 1616 OE1 GLN A 217 11101 10859 24942 358 -2541 4709 O
ATOM 1617 NE2 GLN A 217 3.382 106.735 174.699 1.00124.70 N
ANISOU 1617 NE2 GLN A 217 11190 10558 25634 471 -2392 4941 N
ATOM 1618 N ARG A 218 7.943 106.145 176.932 1.00 90.72 N
ANISOU 1618 N ARG A 218 7967 6736 19766 283 -1332 3595 N
ATOM 1619 CA ARG A 218 8.686 107.353 177.311 1.00 91.31 C
ANISOU 1619 CA ARG A 218 8093 6558 20041 306 -1132 3530 C
ATOM 1620 C ARG A 218 9.573 107.814 176.152 1.00 97.51 C
ANISOU 1620 C ARG A 218 9038 7449 20562 156 -1345 3817 C
ATOM 1621 O ARG A 218 9.693 109.020 175.915 1.00 99.89 O
ANISOU 1621 O ARG A 218 9269 7477 21209 176 -1349 4021 O
ATOM 1622 CB ARG A 218 9.527 107.109 178.572 1.00 87.58 C
ANISOU 1622 CB ARG A 218 7802 6115 19359 316 -778 3041 C
ATOM 1623 N GLN A 219 10.154 106.846 175.410 1.00 92.96 N
ANISOU 1623 N GLN A 219 8676 7256 19390 7 -1508 3842 N
ATOM 1624 CA GLN A 219 10.979 107.094 174.229 1.00 94.24 C
ANISOU 1624 CA GLN A 219 9020 7572 19214 -153 -1687 4112 C
ATOM 1625 C GLN A 219 10.100 107.592 173.074 1.00103.49 C
ANISOU 1625 C GLN A 219 10064 8665 20594 -174 -2046 4624 C
ATOM 1626 O GLN A 219 10.503 108.505 172.351 1.00105.15 O
ANISOU 1626 O GLN A 219 10319 8774 20858 -241 -2139 4929 O
ATOM 1627 CB GLN A 219 11.743 105.824 173.821 1.00 92.79 C
ANISOU 1627 CB GLN A 219 9095 7806 18356 -293 -1719 3956 C
ATOM 1628 CG GLN A 219 12.981 106.107 172.979 1.00110.59 C
ANISOU 1628 CG GLN A 219 11576 10203 20241 -451 -1722 4082 C
ATOM 1629 CD GLN A 219 13.369 104.921 172.138 1.00132.45 C
ANISOU 1629 CD GLN A 219 14569 13360 22396 -592 -1842 4074 C
ATOM 1630 OE1 GLN A 219 12.757 104.636 171.102 1.00130.41 O
ANISOU 1630 OE1 GLN A 219 14351 13230 21967 -666 -2134 4360 O
ATOM 1631 NE2 GLN A 219 14.409 104.214 172.554 1.00123.58 N
ANISOU 1631 NE2 GLN A 219 13601 12421 20934 -637 -1628 3745 N
ATOM 1632 N MET A 220 19.905 112.843 172.702 1.00111.59 N
ANISOU 1632 N MET A 220 11903 9182 21316 -967 -766 4491 N
ATOM 1633 CA MET A 220 20.593 111.633 172.244 1.00108.24 C
ANISOU 1633 CA MET A 220 11648 9183 20295 -1067 -731 4391 C
ATOM 1634 C MET A 220 21.045 110.808 173.459 1.00105.98 C
ANISOU 1634 C MET A 220 11366 8999 19902 -1017 -585 3866 C
ATOM 1635 O MET A 220 20.902 109.579 173.456 1.00102.76 O
ANISOU 1635 O MET A 220 11041 8895 19107 -999 -612 3704 O
ATOM 1636 CB MET A 220 21.787 111.978 171.336 1.00112.35 C
ANISOU 1636 CB MET A 220 12272 9786 20632 -1251 -629 4623 C
ATOM 1637 CG MET A 220 21.397 112.272 169.894 1.00119.42 C
ANISOU 1637 CG MET A 220 13265 10760 21350 -1337 -790 5151 C
ATOM 1638 SD MET A 220 22.781 112.807 168.844 1.00126.48 S
ANISOU 1638 SD MET A 220 14284 11713 22060 -1559 -612 5456 S
ATOM 1639 CE MET A 220 23.551 111.252 168.486 1.00120.55 C
ANISOU 1639 CE MET A 220 13728 11445 20630 -1642 -471 5204 C
ATOM 1640 N ASP A 221 21.578 111.493 174.514 1.00100.81 N
ANISOU 1640 N ASP A 221 10630 8078 19595 -1001 -446 3604 N
ATOM 1641 CA ASP A 221 22.045 110.904 175.781 1.00 97.11 C
ANISOU 1641 CA ASP A 221 10173 7656 19068 -967 -332 3121 C
ATOM 1642 C ASP A 221 20.889 110.231 176.529 1.00 96.95 C
ANISOU 1642 C ASP A 221 10134 7671 19033 -808 -377 2907 C
ATOM 1643 O ASP A 221 21.086 109.183 177.152 1.00 93.45 O
ANISOU 1643 O ASP A 221 9755 7442 18310 -787 -337 2605 O
ATOM 1644 CB ASP A 221 22.739 111.954 176.663 1.00100.23 C
ANISOU 1644 CB ASP A 221 10503 7717 19862 -1003 -220 2930 C
ATOM 1645 CG ASP A 221 24.051 112.483 176.106 1.00113.12 C
ANISOU 1645 CG ASP A 221 12133 9326 21522 -1175 -148 3076 C
ATOM 1646 OD1 ASP A 221 24.804 111.691 175.496 1.00113.13 O
ANISOU 1646 OD1 ASP A 221 12201 9635 21148 -1267 -113 3123 O
ATOM 1647 OD2 ASP A 221 24.353 113.673 176.332 1.00120.86 O
ANISOU 1647 OD2 ASP A 221 13036 9965 22920 -1220 -107 3120 O
ATOM 1648 N ARG A 222 19.689 110.825 176.439 1.00 93.83 N
ANISOU 1648 N ARG A 222 9635 7055 18960 -697 -457 3088 N
ATOM 1649 CA ARG A 222 18.468 110.320 177.054 1.00 91.83 C
ANISOU 1649 CA ARG A 222 9321 6791 18780 -543 -482 2945 C
ATOM 1650 C ARG A 222 17.994 109.057 176.315 1.00 92.47 C
ANISOU 1650 C ARG A 222 9462 7239 18434 -549 -628 3061 C
ATOM 1651 O ARG A 222 17.642 108.074 176.971 1.00 89.80 O
ANISOU 1651 O ARG A 222 9146 7053 17920 -483 -596 2797 O
ATOM 1652 CB ARG A 222 17.371 111.416 177.070 1.00 95.03 C
ANISOU 1652 CB ARG A 222 9555 6817 19735 -425 -518 3148 C
ATOM 1653 CG ARG A 222 16.133 111.119 177.919 1.00106.02 C
ANISOU 1653 CG ARG A 222 10840 8104 21338 -252 -468 2960 C
ATOM 1654 CD ARG A 222 16.430 110.959 179.397 1.00116.22 C
ANISOU 1654 CD ARG A 222 12198 9320 22639 -207 -242 2461 C
ATOM 1655 NE ARG A 222 15.865 109.707 179.904 1.00124.20 N
ANISOU 1655 NE ARG A 222 13241 10576 23372 -139 -220 2254 N
ATOM 1656 CZ ARG A 222 16.143 109.180 181.091 1.00135.96 C
ANISOU 1656 CZ ARG A 222 14837 12122 24700 -121 -59 1844 C
ATOM 1657 NH1 ARG A 222 15.584 108.037 181.462 1.00117.78 N
ANISOU 1657 NH1 ARG A 222 12556 10035 22159 -64 -45 1710 N
ATOM 1658 NH2 ARG A 222 16.988 109.789 181.915 1.00125.60 N
ANISOU 1658 NH2 ARG A 222 13618 10647 23458 -173 74 1575 N
ATOM 1659 N HIS A 223 18.042 109.069 174.957 1.00 89.08 N
ANISOU 1659 N HIS A 223 9081 6951 17814 -643 -783 3446 N
ATOM 1660 CA HIS A 223 17.655 107.944 174.091 1.00 87.40 C
ANISOU 1660 CA HIS A 223 8962 7079 17168 -682 -944 3573 C
ATOM 1661 C HIS A 223 18.540 106.715 174.350 1.00 86.67 C
ANISOU 1661 C HIS A 223 9013 7301 16619 -742 -832 3260 C
ATOM 1662 O HIS A 223 18.029 105.594 174.381 1.00 84.52 O
ANISOU 1662 O HIS A 223 8777 7239 16097 -709 -899 3146 O
ATOM 1663 CB HIS A 223 17.719 108.342 172.606 1.00 90.92 C
ANISOU 1663 CB HIS A 223 9484 7599 17463 -802 -1109 4036 C
ATOM 1664 CG HIS A 223 17.313 107.246 171.668 1.00 94.10 C
ANISOU 1664 CG HIS A 223 10018 8338 17397 -864 -1292 4158 C
ATOM 1665 ND1 HIS A 223 18.249 106.395 171.104 1.00 94.72 N
ANISOU 1665 ND1 HIS A 223 10299 8730 16959 -991 -1214 4075 N
ATOM 1666 CD2 HIS A 223 16.083 106.892 171.233 1.00 97.05 C
ANISOU 1666 CD2 HIS A 223 10342 8758 17775 -820 -1545 4340 C
ATOM 1667 CE1 HIS A 223 17.562 105.556 170.347 1.00 94.57 C
ANISOU 1667 CE1 HIS A 223 10377 8937 16619 -1025 -1417 4189 C
ATOM 1668 NE2 HIS A 223 16.254 105.815 170.392 1.00 96.25 N
ANISOU 1668 NE2 HIS A 223 10441 9006 17126 -932 -1641 4357 N
ATOM 1669 N ALA A 224 19.858 106.937 174.535 1.00 81.71 N
ANISOU 1669 N ALA A 224 8442 6680 15924 -831 -669 3134 N
ATOM 1670 CA ALA A 224 20.855 105.904 174.823 1.00 78.20 C
ANISOU 1670 CA ALA A 224 8096 6484 15133 -886 -550 2852 C
ATOM 1671 C ALA A 224 20.625 105.295 176.209 1.00 78.63 C
ANISOU 1671 C ALA A 224 8113 6520 15241 -779 -487 2460 C
ATOM 1672 O ALA A 224 20.819 104.091 176.380 1.00 76.60 O
ANISOU 1672 O ALA A 224 7926 6502 14675 -777 -471 2271 O
ATOM 1673 CB ALA A 224 22.257 106.488 174.729 1.00 79.47 C
ANISOU 1673 CB ALA A 224 8269 6593 15333 -1003 -404 2851 C
ATOM 1674 N LYS A 225 20.201 106.123 177.188 1.00 74.91 N
ANISOU 1674 N LYS A 225 7548 5759 15158 -693 -439 2340 N
ATOM 1675 CA LYS A 225 19.907 105.702 178.558 1.00 72.97 C
ANISOU 1675 CA LYS A 225 7295 5465 14966 -596 -358 1981 C
ATOM 1676 C LYS A 225 18.660 104.815 178.575 1.00 76.18 C
ANISOU 1676 C LYS A 225 7677 5988 15282 -495 -433 1985 C
ATOM 1677 O LYS A 225 18.600 103.871 179.362 1.00 73.83 O
ANISOU 1677 O LYS A 225 7425 5816 14812 -453 -380 1724 O
ATOM 1678 CB LYS A 225 19.721 106.918 179.473 1.00 77.42 C
ANISOU 1678 CB LYS A 225 7789 5664 15964 -542 -265 1866 C
ATOM 1679 CG LYS A 225 20.131 106.675 180.919 1.00 93.01 C
ANISOU 1679 CG LYS A 225 9831 7598 17911 -522 -146 1452 C
ATOM 1680 CD LYS A 225 19.984 107.950 181.738 1.00110.40 C
ANISOU 1680 CD LYS A 225 11999 9422 20527 -488 -44 1323 C
ATOM 1681 CE LYS A 225 20.695 107.890 183.068 1.00124.95 C
ANISOU 1681 CE LYS A 225 13955 11219 22301 -524 44 925 C
ATOM 1682 NZ LYS A 225 20.654 109.201 183.770 1.00136.25 N
ANISOU 1682 NZ LYS A 225 15380 12266 24123 -518 141 785 N
ATOM 1683 N ILE A 226 17.683 105.106 177.689 1.00 74.40 N
ANISOU 1683 N ILE A 226 7372 5717 15178 -466 -573 2300 N
ATOM 1684 CA ILE A 226 16.458 104.317 177.530 1.00 73.74 C
ANISOU 1684 CA ILE A 226 7233 5733 15052 -389 -686 2359 C
ATOM 1685 C ILE A 226 16.834 102.983 176.857 1.00 75.35 C
ANISOU 1685 C ILE A 226 7569 6294 14766 -474 -769 2343 C
ATOM 1686 O ILE A 226 16.455 101.923 177.360 1.00 73.31 O
ANISOU 1686 O ILE A 226 7324 6167 14364 -429 -756 2152 O
ATOM 1687 CB ILE A 226 15.360 105.106 176.733 1.00 79.83 C
ANISOU 1687 CB ILE A 226 7861 6331 16141 -347 -858 2735 C
ATOM 1688 CG1 ILE A 226 14.878 106.392 177.481 1.00 82.31 C
ANISOU 1688 CG1 ILE A 226 8019 6245 17012 -236 -743 2724 C
ATOM 1689 CG2 ILE A 226 14.173 104.217 176.315 1.00 80.42 C
ANISOU 1689 CG2 ILE A 226 7868 6543 16144 -307 -1040 2849 C
ATOM 1690 CD1 ILE A 226 14.156 106.233 178.878 1.00 88.48 C
ANISOU 1690 CD1 ILE A 226 8716 6870 18033 -92 -554 2403 C
ATOM 1691 N LYS A 227 17.604 103.052 175.742 1.00 72.25 N
ANISOU 1691 N LYS A 227 7282 6042 14129 -601 -827 2537 N
ATOM 1692 CA LYS A 227 18.068 101.911 174.944 1.00 70.97 C
ANISOU 1692 CA LYS A 227 7269 6195 13501 -696 -873 2530 C
ATOM 1693 C LYS A 227 18.785 100.869 175.809 1.00 71.67 C
ANISOU 1693 C LYS A 227 7414 6423 13396 -681 -727 2168 C
ATOM 1694 O LYS A 227 18.438 99.694 175.724 1.00 70.20 O
ANISOU 1694 O LYS A 227 7276 6419 12976 -673 -779 2071 O
ATOM 1695 CB LYS A 227 18.988 102.380 173.801 1.00 75.35 C
ANISOU 1695 CB LYS A 227 7935 6827 13869 -834 -863 2759 C
ATOM 1696 CG LYS A 227 19.269 101.312 172.739 1.00 90.91 C
ANISOU 1696 CG LYS A 227 10083 9104 15353 -939 -911 2801 C
ATOM 1697 CD LYS A 227 20.311 101.762 171.709 1.00106.15 C
ANISOU 1697 CD LYS A 227 12140 11111 17080 -1080 -822 2993 C
ATOM 1698 CE LYS A 227 19.705 102.465 170.512 1.00125.51 C
ANISOU 1698 CE LYS A 227 14656 13545 19485 -1156 -1011 3410 C
ATOM 1699 NZ LYS A 227 20.747 103.020 169.606 1.00137.32 N
ANISOU 1699 NZ LYS A 227 16277 15089 20809 -1296 -880 3612 N
ATOM 1700 N ARG A 228 19.750 101.294 176.649 1.00 67.23 N
ANISOU 1700 N ARG A 228 6836 5760 12947 -682 -569 1979 N
ATOM 1701 CA ARG A 228 20.498 100.379 177.516 1.00 64.92 C
ANISOU 1701 CA ARG A 228 6587 5581 12498 -673 -463 1666 C
ATOM 1702 C ARG A 228 19.632 99.813 178.639 1.00 67.58 C
ANISOU 1702 C ARG A 228 6889 5881 12910 -560 -458 1459 C
ATOM 1703 O ARG A 228 19.838 98.662 179.025 1.00 65.90 O
ANISOU 1703 O ARG A 228 6727 5826 12485 -549 -435 1278 O
ATOM 1704 CB ARG A 228 21.756 101.042 178.103 1.00 65.72 C
ANISOU 1704 CB ARG A 228 6674 5575 12722 -722 -344 1542 C
ATOM 1705 CG ARG A 228 22.906 101.225 177.104 1.00 78.24 C
ANISOU 1705 CG ARG A 228 8294 7253 14182 -847 -289 1685 C
ATOM 1706 CD ARG A 228 23.401 99.912 176.520 1.00 84.57 C
ANISOU 1706 CD ARG A 228 9179 8327 14625 -887 -255 1626 C
ATOM 1707 NE ARG A 228 24.716 100.030 175.889 1.00 92.81 N
ANISOU 1707 NE ARG A 228 10234 9437 15594 -995 -128 1681 N
ATOM 1708 CZ ARG A 228 25.870 99.750 176.489 1.00102.57 C
ANISOU 1708 CZ ARG A 228 11414 10684 16875 -1018 -28 1494 C
ATOM 1709 NH1 ARG A 228 27.014 99.876 175.832 1.00 93.95 N
ANISOU 1709 NH1 ARG A 228 10301 9640 15756 -1115 109 1569 N
ATOM 1710 NH2 ARG A 228 25.887 99.341 177.754 1.00 80.71 N
ANISOU 1710 NH2 ARG A 228 8605 7875 14186 -949 -65 1244 N
ATOM 1711 N ALA A 229 18.664 100.600 179.148 1.00 64.75 N
ANISOU 1711 N ALA A 229 6438 5302 12863 -475 -459 1494 N
ATOM 1712 CA ALA A 229 17.760 100.172 180.217 1.00 63.52 C
ANISOU 1712 CA ALA A 229 6243 5085 12807 -367 -406 1315 C
ATOM 1713 C ALA A 229 16.837 99.045 179.736 1.00 66.43 C
ANISOU 1713 C ALA A 229 6594 5623 13025 -343 -514 1386 C
ATOM 1714 O ALA A 229 16.574 98.110 180.499 1.00 64.10 O
ANISOU 1714 O ALA A 229 6319 5401 12635 -298 -459 1198 O
ATOM 1715 CB ALA A 229 16.948 101.350 180.724 1.00 66.02 C
ANISOU 1715 CB ALA A 229 6451 5103 13529 -281 -347 1354 C
ATOM 1716 N ILE A 230 16.386 99.117 178.459 1.00 64.31 N
ANISOU 1716 N ILE A 230 6301 5415 12718 -389 -680 1662 N
ATOM 1717 CA ILE A 230 15.549 98.096 177.818 1.00 63.99 C
ANISOU 1717 CA ILE A 230 6255 5534 12525 -400 -833 1748 C
ATOM 1718 C ILE A 230 16.421 96.859 177.563 1.00 66.70 C
ANISOU 1718 C ILE A 230 6746 6129 12466 -475 -814 1596 C
ATOM 1719 O ILE A 230 16.005 95.747 177.894 1.00 65.73 O
ANISOU 1719 O ILE A 230 6630 6103 12241 -450 -825 1466 O
ATOM 1720 CB ILE A 230 14.863 98.626 176.518 1.00 69.51 C
ANISOU 1720 CB ILE A 230 6909 6218 13282 -449 -1056 2099 C
ATOM 1721 CG1 ILE A 230 13.808 99.710 176.851 1.00 71.72 C
ANISOU 1721 CG1 ILE A 230 6990 6217 14042 -346 -1082 2254 C
ATOM 1722 CG2 ILE A 230 14.233 97.476 175.700 1.00 70.68 C
ANISOU 1722 CG2 ILE A 230 7104 6570 13182 -507 -1254 2169 C
ATOM 1723 CD1 ILE A 230 13.292 100.551 175.664 1.00 80.24 C
ANISOU 1723 CD1 ILE A 230 8010 7223 15257 -390 -1310 2645 C
ATOM 1724 N THR A 231 17.642 97.067 177.011 1.00 63.18 N
ANISOU 1724 N THR A 231 6405 5766 11833 -563 -763 1612 N
ATOM 1725 CA THR A 231 18.620 96.016 176.703 1.00 61.63 C
ANISOU 1725 CA THR A 231 6333 5779 11306 -630 -704 1474 C
ATOM 1726 C THR A 231 18.981 95.234 177.975 1.00 63.38 C
ANISOU 1726 C THR A 231 6544 6010 11527 -565 -589 1187 C
ATOM 1727 O THR A 231 19.013 94.008 177.928 1.00 61.89 O
ANISOU 1727 O THR A 231 6408 5963 11144 -570 -597 1073 O
ATOM 1728 CB THR A 231 19.871 96.611 176.022 1.00 68.13 C
ANISOU 1728 CB THR A 231 7223 6634 12028 -724 -619 1554 C
ATOM 1729 OG1 THR A 231 19.470 97.346 174.865 1.00 68.45 O
ANISOU 1729 OG1 THR A 231 7295 6664 12050 -790 -733 1851 O
ATOM 1730 CG2 THR A 231 20.872 95.545 175.596 1.00 66.28 C
ANISOU 1730 CG2 THR A 231 7097 6598 11490 -786 -526 1423 C
ATOM 1731 N PHE A 232 19.206 95.938 179.104 1.00 59.52 N
ANISOU 1731 N PHE A 232 6001 5361 11251 -510 -496 1076 N
ATOM 1732 CA PHE A 232 19.556 95.331 180.389 1.00 57.39 C
ANISOU 1732 CA PHE A 232 5748 5091 10965 -461 -408 827 C
ATOM 1733 C PHE A 232 18.474 94.377 180.899 1.00 61.18 C
ANISOU 1733 C PHE A 232 6212 5603 11429 -392 -428 757 C
ATOM 1734 O PHE A 232 18.790 93.228 181.207 1.00 59.67 O
ANISOU 1734 O PHE A 232 6071 5532 11071 -391 -413 627 O
ATOM 1735 CB PHE A 232 19.837 96.407 181.453 1.00 59.04 C
ANISOU 1735 CB PHE A 232 5935 5106 11392 -433 -325 728 C
ATOM 1736 CG PHE A 232 20.018 95.861 182.850 1.00 58.82 C
ANISOU 1736 CG PHE A 232 5957 5071 11321 -391 -259 488 C
ATOM 1737 CD1 PHE A 232 21.197 95.226 183.219 1.00 60.49 C
ANISOU 1737 CD1 PHE A 232 6221 5385 11378 -434 -258 357 C
ATOM 1738 CD2 PHE A 232 18.996 95.946 183.785 1.00 60.57 C
ANISOU 1738 CD2 PHE A 232 6173 5181 11658 -310 -195 409 C
ATOM 1739 CE1 PHE A 232 21.360 94.713 184.507 1.00 60.42 C
ANISOU 1739 CE1 PHE A 232 6276 5374 11306 -406 -233 167 C
ATOM 1740 CE2 PHE A 232 19.159 95.425 185.070 1.00 62.69 C
ANISOU 1740 CE2 PHE A 232 6527 5456 11835 -285 -128 203 C
ATOM 1741 CZ PHE A 232 20.351 94.838 185.428 1.00 59.73 C
ANISOU 1741 CZ PHE A 232 6222 5189 11283 -338 -167 91 C
ATOM 1742 N ILE A 233 17.218 94.856 181.023 1.00 59.27 N
ANISOU 1742 N ILE A 233 5883 5237 11402 -331 -451 851 N
ATOM 1743 CA ILE A 233 16.117 94.048 181.546 1.00 58.79 C
ANISOU 1743 CA ILE A 233 5772 5177 11388 -267 -445 803 C
ATOM 1744 C ILE A 233 15.804 92.876 180.586 1.00 62.45 C
ANISOU 1744 C ILE A 233 6252 5814 11661 -318 -582 871 C
ATOM 1745 O ILE A 233 15.447 91.796 181.064 1.00 60.86 O
ANISOU 1745 O ILE A 233 6056 5670 11399 -295 -562 767 O
ATOM 1746 CB ILE A 233 14.873 94.898 181.926 1.00 63.28 C
ANISOU 1746 CB ILE A 233 6206 5543 12296 -184 -406 888 C
ATOM 1747 CG1 ILE A 233 13.941 94.146 182.905 1.00 63.63 C
ANISOU 1747 CG1 ILE A 233 6204 5557 12417 -110 -303 778 C
ATOM 1748 CG2 ILE A 233 14.117 95.440 180.715 1.00 65.68 C
ANISOU 1748 CG2 ILE A 233 6401 5807 12747 -202 -576 1161 C
ATOM 1749 CD1 ILE A 233 14.537 93.839 184.316 1.00 69.86 C
ANISOU 1749 CD1 ILE A 233 7115 6341 13086 -85 -124 529 C
ATOM 1750 N MET A 234 16.016 93.069 179.260 1.00 60.13 N
ANISOU 1750 N MET A 234 5993 5603 11251 -399 -710 1033 N
ATOM 1751 CA MET A 234 15.858 92.018 178.254 1.00 60.23 C
ANISOU 1751 CA MET A 234 6072 5782 11031 -472 -841 1070 C
ATOM 1752 C MET A 234 16.872 90.912 178.523 1.00 60.54 C
ANISOU 1752 C MET A 234 6216 5947 10841 -492 -744 863 C
ATOM 1753 O MET A 234 16.484 89.754 178.633 1.00 59.29 O
ANISOU 1753 O MET A 234 6069 5850 10609 -489 -773 775 O
ATOM 1754 CB MET A 234 16.035 92.574 176.837 1.00 64.84 C
ANISOU 1754 CB MET A 234 6722 6429 11485 -569 -969 1276 C
ATOM 1755 CG MET A 234 14.743 92.906 176.158 1.00 71.31 C
ANISOU 1755 CG MET A 234 7457 7200 12437 -584 -1184 1505 C
ATOM 1756 SD MET A 234 15.028 93.513 174.483 1.00 79.08 S
ANISOU 1756 SD MET A 234 8574 8281 13192 -720 -1353 1770 S
ATOM 1757 CE MET A 234 13.361 94.009 174.030 1.00 78.54 C
ANISOU 1757 CE MET A 234 8342 8100 13399 -709 -1647 2060 C
ATOM 1758 N VAL A 235 18.157 91.287 178.703 1.00 55.81 N
ANISOU 1758 N VAL A 235 5667 5359 10179 -507 -628 791 N
ATOM 1759 CA VAL A 235 19.269 90.383 179.015 1.00 54.17 C
ANISOU 1759 CA VAL A 235 5520 5239 9822 -515 -532 614 C
ATOM 1760 C VAL A 235 18.954 89.628 180.326 1.00 57.35 C
ANISOU 1760 C VAL A 235 5893 5602 10295 -438 -491 465 C
ATOM 1761 O VAL A 235 19.025 88.403 180.330 1.00 56.86 O
ANISOU 1761 O VAL A 235 5863 5616 10124 -439 -493 373 O
ATOM 1762 CB VAL A 235 20.638 91.127 179.062 1.00 57.49 C
ANISOU 1762 CB VAL A 235 5948 5642 10252 -545 -431 595 C
ATOM 1763 CG1 VAL A 235 21.732 90.263 179.681 1.00 56.24 C
ANISOU 1763 CG1 VAL A 235 5798 5532 10037 -531 -348 418 C
ATOM 1764 CG2 VAL A 235 21.059 91.586 177.672 1.00 58.65 C
ANISOU 1764 CG2 VAL A 235 6153 5858 10275 -636 -433 742 C
ATOM 1765 N VAL A 236 18.542 90.343 181.397 1.00 53.49 N
ANISOU 1765 N VAL A 236 5354 4985 9983 -377 -444 445 N
ATOM 1766 CA VAL A 236 18.185 89.757 182.700 1.00 52.24 C
ANISOU 1766 CA VAL A 236 5198 4786 9866 -313 -381 322 C
ATOM 1767 C VAL A 236 17.113 88.656 182.502 1.00 55.99 C
ANISOU 1767 C VAL A 236 5642 5302 10331 -301 -430 345 C
ATOM 1768 O VAL A 236 17.279 87.551 183.027 1.00 54.95 O
ANISOU 1768 O VAL A 236 5545 5215 10120 -288 -404 248 O
ATOM 1769 CB VAL A 236 17.745 90.856 183.712 1.00 56.32 C
ANISOU 1769 CB VAL A 236 5691 5145 10564 -260 -296 301 C
ATOM 1770 CG1 VAL A 236 16.981 90.276 184.903 1.00 55.87 C
ANISOU 1770 CG1 VAL A 236 5646 5044 10540 -199 -207 213 C
ATOM 1771 CG2 VAL A 236 18.949 91.660 184.193 1.00 56.00 C
ANISOU 1771 CG2 VAL A 236 5702 5060 10514 -286 -259 220 C
ATOM 1772 N ALA A 237 16.070 88.942 181.692 1.00 53.38 N
ANISOU 1772 N ALA A 237 5239 4949 10096 -315 -524 487 N
ATOM 1773 CA ALA A 237 14.987 88.005 181.381 1.00 53.33 C
ANISOU 1773 CA ALA A 237 5177 4965 10122 -324 -609 527 C
ATOM 1774 C ALA A 237 15.458 86.834 180.493 1.00 57.33 C
ANISOU 1774 C ALA A 237 5770 5606 10405 -398 -694 475 C
ATOM 1775 O ALA A 237 15.117 85.693 180.797 1.00 56.73 O
ANISOU 1775 O ALA A 237 5691 5545 10320 -395 -695 402 O
ATOM 1776 CB ALA A 237 13.839 88.738 180.708 1.00 55.50 C
ANISOU 1776 CB ALA A 237 5335 5170 10584 -330 -729 714 C
ATOM 1777 N ILE A 238 16.235 87.112 179.411 1.00 54.47 N
ANISOU 1777 N ILE A 238 5493 5330 9872 -467 -742 507 N
ATOM 1778 CA ILE A 238 16.750 86.114 178.456 1.00 54.45 C
ANISOU 1778 CA ILE A 238 5601 5446 9640 -543 -781 436 C
ATOM 1779 C ILE A 238 17.717 85.147 179.169 1.00 57.10 C
ANISOU 1779 C ILE A 238 5972 5800 9923 -505 -651 257 C
ATOM 1780 O ILE A 238 17.586 83.934 178.996 1.00 56.50 O
ANISOU 1780 O ILE A 238 5930 5751 9786 -523 -672 167 O
ATOM 1781 CB ILE A 238 17.399 86.783 177.201 1.00 58.56 C
ANISOU 1781 CB ILE A 238 6220 6048 9982 -625 -807 521 C
ATOM 1782 CG1 ILE A 238 16.319 87.431 176.304 1.00 60.70 C
ANISOU 1782 CG1 ILE A 238 6477 6316 10272 -684 -1002 725 C
ATOM 1783 CG2 ILE A 238 18.248 85.786 176.380 1.00 59.51 C
ANISOU 1783 CG2 ILE A 238 6478 6280 9851 -692 -752 393 C
ATOM 1784 CD1 ILE A 238 16.807 88.622 175.433 1.00 69.33 C
ANISOU 1784 CD1 ILE A 238 7630 7434 11277 -742 -1016 889 C
ATOM 1785 N VAL A 239 18.661 85.682 179.973 1.00 52.67 N
ANISOU 1785 N VAL A 239 5397 5208 9409 -456 -539 213 N
ATOM 1786 CA VAL A 239 19.644 84.904 180.734 1.00 51.48 C
ANISOU 1786 CA VAL A 239 5256 5059 9244 -418 -451 80 C
ATOM 1787 C VAL A 239 18.901 83.941 181.670 1.00 55.77 C
ANISOU 1787 C VAL A 239 5775 5556 9859 -371 -461 35 C
ATOM 1788 O VAL A 239 19.196 82.754 181.643 1.00 55.59 O
ANISOU 1788 O VAL A 239 5774 5550 9799 -370 -451 -47 O
ATOM 1789 CB VAL A 239 20.659 85.815 181.486 1.00 54.53 C
ANISOU 1789 CB VAL A 239 5620 5408 9692 -392 -385 66 C
ATOM 1790 CG1 VAL A 239 21.342 85.092 182.647 1.00 53.51 C
ANISOU 1790 CG1 VAL A 239 5484 5255 9593 -344 -354 -35 C
ATOM 1791 CG2 VAL A 239 21.697 86.388 180.524 1.00 55.01 C
ANISOU 1791 CG2 VAL A 239 5694 5517 9691 -448 -339 92 C
ATOM 1792 N PHE A 240 17.897 84.433 182.425 1.00 52.86 N
ANISOU 1792 N PHE A 240 5357 5116 9611 -334 -463 95 N
ATOM 1793 CA PHE A 240 17.114 83.621 183.358 1.00 52.65 C
ANISOU 1793 CA PHE A 240 5306 5038 9662 -295 -435 76 C
ATOM 1794 C PHE A 240 16.404 82.456 182.657 1.00 58.36 C
ANISOU 1794 C PHE A 240 6011 5778 10387 -336 -512 75 C
ATOM 1795 O PHE A 240 16.495 81.333 183.153 1.00 58.33 O
ANISOU 1795 O PHE A 240 6020 5756 10387 -322 -485 16 O
ATOM 1796 CB PHE A 240 16.088 84.483 184.119 1.00 54.53 C
ANISOU 1796 CB PHE A 240 5486 5186 10048 -252 -380 143 C
ATOM 1797 CG PHE A 240 15.361 83.787 185.250 1.00 55.80 C
ANISOU 1797 CG PHE A 240 5634 5289 10281 -212 -291 130 C
ATOM 1798 CD1 PHE A 240 15.880 83.790 186.539 1.00 58.70 C
ANISOU 1798 CD1 PHE A 240 6085 5633 10584 -176 -190 67 C
ATOM 1799 CD2 PHE A 240 14.146 83.148 185.031 1.00 58.25 C
ANISOU 1799 CD2 PHE A 240 5851 5562 10719 -223 -315 192 C
ATOM 1800 CE1 PHE A 240 15.194 83.167 187.589 1.00 59.88 C
ANISOU 1800 CE1 PHE A 240 6250 5734 10767 -148 -85 74 C
ATOM 1801 CE2 PHE A 240 13.471 82.512 186.078 1.00 61.13 C
ANISOU 1801 CE2 PHE A 240 6197 5866 11165 -193 -201 197 C
ATOM 1802 CZ PHE A 240 13.992 82.536 187.352 1.00 59.04 C
ANISOU 1802 CZ PHE A 240 6039 5587 10806 -154 -71 143 C
ATOM 1803 N VAL A 241 15.715 82.705 181.519 1.00 56.17 N
ANISOU 1803 N VAL A 241 5709 5525 10108 -395 -626 146 N
ATOM 1804 CA VAL A 241 14.963 81.648 180.831 1.00 57.29 C
ANISOU 1804 CA VAL A 241 5841 5672 10253 -457 -736 135 C
ATOM 1805 C VAL A 241 15.887 80.604 180.162 1.00 60.97 C
ANISOU 1805 C VAL A 241 6417 6195 10552 -501 -733 -1 C
ATOM 1806 O VAL A 241 15.711 79.422 180.442 1.00 60.75 O
ANISOU 1806 O VAL A 241 6386 6124 10574 -502 -727 -73 O
ATOM 1807 CB VAL A 241 13.873 82.138 179.835 1.00 63.10 C
ANISOU 1807 CB VAL A 241 6522 6413 11038 -526 -911 260 C
ATOM 1808 CG1 VAL A 241 12.692 82.753 180.571 1.00 63.21 C
ANISOU 1808 CG1 VAL A 241 6375 6326 11317 -473 -899 384 C
ATOM 1809 CG2 VAL A 241 14.422 83.104 178.788 1.00 63.86 C
ANISOU 1809 CG2 VAL A 241 6699 6589 10977 -574 -972 320 C
ATOM 1810 N ILE A 242 16.867 81.013 179.328 1.00 57.22 N
ANISOU 1810 N ILE A 242 6033 5799 9909 -533 -710 -37 N
ATOM 1811 CA ILE A 242 17.729 80.059 178.611 1.00 57.66 C
ANISOU 1811 CA ILE A 242 6191 5894 9825 -571 -661 -181 C
ATOM 1812 C ILE A 242 18.682 79.302 179.572 1.00 60.53 C
ANISOU 1812 C ILE A 242 6524 6203 10270 -490 -531 -278 C
ATOM 1813 O ILE A 242 19.179 78.233 179.206 1.00 60.82 O
ANISOU 1813 O ILE A 242 6607 6221 10280 -500 -484 -403 O
ATOM 1814 CB ILE A 242 18.493 80.686 177.404 1.00 62.00 C
ANISOU 1814 CB ILE A 242 6849 6540 10167 -636 -630 -186 C
ATOM 1815 CG1 ILE A 242 19.624 81.651 177.844 1.00 61.85 C
ANISOU 1815 CG1 ILE A 242 6793 6533 10174 -581 -501 -152 C
ATOM 1816 CG2 ILE A 242 17.511 81.353 176.418 1.00 64.38 C
ANISOU 1816 CG2 ILE A 242 7198 6894 10370 -729 -803 -58 C
ATOM 1817 CD1 ILE A 242 20.604 82.083 176.718 1.00 72.51 C
ANISOU 1817 CD1 ILE A 242 8241 7967 11344 -642 -404 -167 C
ATOM 1818 N CYS A 243 18.896 79.820 180.796 1.00 55.20 N
ANISOU 1818 N CYS A 243 5780 5492 9699 -414 -486 -220 N
ATOM 1819 CA CYS A 243 19.755 79.150 181.768 1.00 53.73 C
ANISOU 1819 CA CYS A 243 5571 5258 9588 -346 -414 -274 C
ATOM 1820 C CYS A 243 18.981 78.164 182.634 1.00 56.72 C
ANISOU 1820 C CYS A 243 5921 5556 10073 -320 -435 -260 C
ATOM 1821 O CYS A 243 19.479 77.064 182.835 1.00 57.43 O
ANISOU 1821 O CYS A 243 6011 5594 10216 -296 -409 -322 O
ATOM 1822 CB CYS A 243 20.512 80.150 182.638 1.00 53.08 C
ANISOU 1822 CB CYS A 243 5461 5181 9526 -301 -379 -230 C
ATOM 1823 SG CYS A 243 21.948 80.903 181.835 1.00 57.28 S
ANISOU 1823 SG CYS A 243 5990 5772 10002 -323 -313 -262 S
ATOM 1824 N PHE A 244 17.797 78.535 183.170 1.00 52.01 N
ANISOU 1824 N PHE A 244 5290 4934 9539 -320 -463 -170 N
ATOM 1825 CA PHE A 244 17.105 77.665 184.126 1.00 51.62 C
ANISOU 1825 CA PHE A 244 5212 4804 9599 -296 -443 -134 C
ATOM 1826 C PHE A 244 15.808 76.984 183.631 1.00 55.97 C
ANISOU 1826 C PHE A 244 5711 5306 10251 -353 -506 -113 C
ATOM 1827 O PHE A 244 15.452 75.951 184.200 1.00 55.05 O
ANISOU 1827 O PHE A 244 5572 5109 10236 -348 -484 -103 O
ATOM 1828 CB PHE A 244 16.804 78.441 185.420 1.00 52.84 C
ANISOU 1828 CB PHE A 244 5363 4940 9774 -248 -373 -53 C
ATOM 1829 CG PHE A 244 18.008 79.163 185.983 1.00 53.75 C
ANISOU 1829 CG PHE A 244 5532 5093 9798 -212 -349 -76 C
ATOM 1830 CD1 PHE A 244 19.095 78.453 186.487 1.00 56.94 C
ANISOU 1830 CD1 PHE A 244 5965 5487 10183 -185 -360 -106 C
ATOM 1831 CD2 PHE A 244 18.069 80.551 185.984 1.00 55.55 C
ANISOU 1831 CD2 PHE A 244 5765 5347 9992 -211 -334 -61 C
ATOM 1832 CE1 PHE A 244 20.219 79.121 186.985 1.00 57.74 C
ANISOU 1832 CE1 PHE A 244 6093 5615 10229 -167 -377 -119 C
ATOM 1833 CE2 PHE A 244 19.188 81.217 186.493 1.00 58.49 C
ANISOU 1833 CE2 PHE A 244 6180 5740 10302 -196 -333 -90 C
ATOM 1834 CZ PHE A 244 20.258 80.498 186.985 1.00 56.63 C
ANISOU 1834 CZ PHE A 244 5966 5506 10045 -179 -365 -119 C
ATOM 1835 N LEU A 245 15.116 77.517 182.603 1.00 53.83 N
ANISOU 1835 N LEU A 245 5416 5072 9965 -415 -603 -92 N
ATOM 1836 CA LEU A 245 13.868 76.902 182.119 1.00 54.91 C
ANISOU 1836 CA LEU A 245 5485 5156 10222 -487 -709 -64 C
ATOM 1837 C LEU A 245 14.080 75.527 181.421 1.00 60.19 C
ANISOU 1837 C LEU A 245 6213 5787 10871 -550 -768 -193 C
ATOM 1838 O LEU A 245 13.326 74.616 181.770 1.00 60.46 O
ANISOU 1838 O LEU A 245 6183 5724 11068 -575 -787 -177 O
ATOM 1839 CB LEU A 245 13.065 77.852 181.205 1.00 55.80 C
ANISOU 1839 CB LEU A 245 5552 5313 10337 -545 -845 18 C
ATOM 1840 CG LEU A 245 11.724 77.353 180.638 1.00 62.07 C
ANISOU 1840 CG LEU A 245 6249 6053 11283 -635 -1012 70 C
ATOM 1841 CD1 LEU A 245 10.666 77.200 181.728 1.00 62.16 C
ANISOU 1841 CD1 LEU A 245 6094 5954 11570 -594 -931 177 C
ATOM 1842 CD2 LEU A 245 11.223 78.284 179.560 1.00 65.83 C
ANISOU 1842 CD2 LEU A 245 6710 6589 11713 -702 -1194 158 C
ATOM 1843 N PRO A 246 15.052 75.312 180.480 1.00 57.47 N
ANISOU 1843 N PRO A 246 5986 5497 10354 -580 -773 -325 N
ATOM 1844 CA PRO A 246 15.173 73.985 179.843 1.00 58.63 C
ANISOU 1844 CA PRO A 246 6197 5577 10502 -640 -802 -475 C
ATOM 1845 C PRO A 246 15.267 72.824 180.839 1.00 63.02 C
ANISOU 1845 C PRO A 246 6700 5999 11246 -585 -722 -486 C
ATOM 1846 O PRO A 246 14.597 71.808 180.639 1.00 64.44 O
ANISOU 1846 O PRO A 246 6862 6075 11548 -649 -787 -533 O
ATOM 1847 CB PRO A 246 16.450 74.115 179.010 1.00 60.44 C
ANISOU 1847 CB PRO A 246 6553 5879 10532 -639 -723 -608 C
ATOM 1848 CG PRO A 246 16.528 75.539 178.681 1.00 64.15 C
ANISOU 1848 CG PRO A 246 7037 6473 10866 -644 -746 -510 C
ATOM 1849 CD PRO A 246 16.050 76.245 179.914 1.00 58.40 C
ANISOU 1849 CD PRO A 246 6183 5723 10284 -567 -729 -350 C
ATOM 1850 N SER A 247 16.051 72.998 181.928 1.00 58.22 N
ANISOU 1850 N SER A 247 6068 5385 10668 -479 -603 -427 N
ATOM 1851 CA SER A 247 16.236 72.017 183.003 1.00 57.62 C
ANISOU 1851 CA SER A 247 5954 5191 10748 -421 -537 -387 C
ATOM 1852 C SER A 247 14.914 71.735 183.722 1.00 60.08 C
ANISOU 1852 C SER A 247 6183 5429 11217 -447 -554 -259 C
ATOM 1853 O SER A 247 14.617 70.576 183.990 1.00 59.85 O
ANISOU 1853 O SER A 247 6125 5269 11346 -465 -550 -259 O
ATOM 1854 CB SER A 247 17.283 72.512 183.997 1.00 60.35 C
ANISOU 1854 CB SER A 247 6306 5574 11048 -322 -457 -322 C
ATOM 1855 OG SER A 247 17.412 71.658 185.121 1.00 69.70 O
ANISOU 1855 OG SER A 247 7470 6656 12356 -273 -421 -239 O
ATOM 1856 N VAL A 248 14.118 72.787 184.006 1.00 55.65 N
ANISOU 1856 N VAL A 248 5569 4931 10643 -450 -556 -150 N
ATOM 1857 CA VAL A 248 12.817 72.691 184.678 1.00 55.92 C
ANISOU 1857 CA VAL A 248 5498 4896 10855 -471 -529 -20 C
ATOM 1858 C VAL A 248 11.842 71.898 183.785 1.00 61.53 C
ANISOU 1858 C VAL A 248 6135 5524 11719 -581 -663 -60 C
ATOM 1859 O VAL A 248 11.154 71.004 184.286 1.00 61.56 O
ANISOU 1859 O VAL A 248 6062 5404 11923 -609 -635 0 O
ATOM 1860 CB VAL A 248 12.279 74.101 185.066 1.00 58.78 C
ANISOU 1860 CB VAL A 248 5811 5330 11195 -438 -478 80 C
ATOM 1861 CG1 VAL A 248 10.776 74.094 185.352 1.00 59.44 C
ANISOU 1861 CG1 VAL A 248 5741 5334 11510 -473 -457 198 C
ATOM 1862 CG2 VAL A 248 13.048 74.658 186.261 1.00 57.58 C
ANISOU 1862 CG2 VAL A 248 5738 5215 10923 -348 -338 120 C
ATOM 1863 N VAL A 249 11.837 72.192 182.466 1.00 59.27 N
ANISOU 1863 N VAL A 249 5889 5304 11327 -654 -814 -158 N
ATOM 1864 CA VAL A 249 10.985 71.527 181.472 1.00 61.23 C
ANISOU 1864 CA VAL A 249 6105 5491 11670 -785 -995 -220 C
ATOM 1865 C VAL A 249 11.302 70.016 181.440 1.00 65.88 C
ANISOU 1865 C VAL A 249 6741 5940 12349 -817 -980 -344 C
ATOM 1866 O VAL A 249 10.362 69.218 181.473 1.00 67.12 O
ANISOU 1866 O VAL A 249 6804 5970 12730 -897 -1052 -319 O
ATOM 1867 CB VAL A 249 11.088 72.186 180.062 1.00 66.06 C
ANISOU 1867 CB VAL A 249 6812 6222 12067 -865 -1165 -301 C
ATOM 1868 CG1 VAL A 249 10.302 71.405 179.008 1.00 68.05 C
ANISOU 1868 CG1 VAL A 249 7076 6413 12368 -1023 -1388 -391 C
ATOM 1869 CG2 VAL A 249 10.613 73.638 180.096 1.00 65.46 C
ANISOU 1869 CG2 VAL A 249 6656 6241 11973 -837 -1200 -145 C
ATOM 1870 N VAL A 250 12.602 69.623 181.431 1.00 61.44 N
ANISOU 1870 N VAL A 250 6299 5379 11664 -752 -879 -464 N
ATOM 1871 CA VAL A 250 12.965 68.195 181.398 1.00 62.26 C
ANISOU 1871 CA VAL A 250 6439 5320 11897 -767 -849 -583 C
ATOM 1872 C VAL A 250 12.681 67.530 182.764 1.00 65.47 C
ANISOU 1872 C VAL A 250 6743 5595 12538 -710 -746 -422 C
ATOM 1873 O VAL A 250 12.233 66.386 182.768 1.00 66.78 O
ANISOU 1873 O VAL A 250 6870 5590 12914 -769 -774 -449 O
ATOM 1874 CB VAL A 250 14.392 67.865 180.876 1.00 66.20 C
ANISOU 1874 CB VAL A 250 7069 5823 12262 -716 -762 -766 C
ATOM 1875 CG1 VAL A 250 14.653 68.506 179.516 1.00 66.41 C
ANISOU 1875 CG1 VAL A 250 7224 5984 12024 -787 -828 -915 C
ATOM 1876 CG2 VAL A 250 15.478 68.240 181.872 1.00 64.69 C
ANISOU 1876 CG2 VAL A 250 6861 5672 12046 -571 -619 -671 C
ATOM 1877 N ARG A 251 12.888 68.249 183.900 1.00 60.31 N
ANISOU 1877 N ARG A 251 6062 5015 11840 -610 -632 -255 N
ATOM 1878 CA ARG A 251 12.603 67.744 185.253 1.00 60.21 C
ANISOU 1878 CA ARG A 251 5992 4904 11982 -566 -521 -77 C
ATOM 1879 C ARG A 251 11.109 67.405 185.376 1.00 65.32 C
ANISOU 1879 C ARG A 251 6504 5454 12859 -657 -544 22 C
ATOM 1880 O ARG A 251 10.776 66.359 185.932 1.00 66.97 O
ANISOU 1880 O ARG A 251 6665 5504 13276 -679 -497 98 O
ATOM 1881 CB ARG A 251 13.022 68.753 186.346 1.00 59.10 C
ANISOU 1881 CB ARG A 251 5887 4884 11686 -468 -409 57 C
ATOM 1882 CG ARG A 251 14.522 68.787 186.659 1.00 68.44 C
ANISOU 1882 CG ARG A 251 7167 6108 12731 -376 -383 21 C
ATOM 1883 CD ARG A 251 14.901 67.996 187.904 1.00 82.10 C
ANISOU 1883 CD ARG A 251 8920 7740 14536 -323 -318 167 C
ATOM 1884 NE ARG A 251 15.455 68.844 188.967 1.00 91.29 N
ANISOU 1884 NE ARG A 251 10159 9013 15513 -257 -269 277 N
ATOM 1885 CZ ARG A 251 16.743 69.167 189.094 1.00104.05 C
ANISOU 1885 CZ ARG A 251 11828 10689 17015 -193 -311 244 C
ATOM 1886 NH1 ARG A 251 17.634 68.737 188.209 1.00 89.17 N
ANISOU 1886 NH1 ARG A 251 9917 8767 15196 -172 -365 107 N
ATOM 1887 NH2 ARG A 251 17.145 69.931 190.100 1.00 90.29 N
ANISOU 1887 NH2 ARG A 251 10165 9038 15102 -156 -294 340 N
ATOM 1888 N ILE A 252 10.225 68.262 184.803 1.00 60.69 N
ANISOU 1888 N ILE A 252 5841 4949 12270 -715 -628 32 N
ATOM 1889 CA ILE A 252 8.766 68.087 184.776 1.00 61.34 C
ANISOU 1889 CA ILE A 252 5749 4943 12614 -808 -677 129 C
ATOM 1890 C ILE A 252 8.421 66.826 183.962 1.00 66.17 C
ANISOU 1890 C ILE A 252 6337 5398 13406 -933 -832 10 C
ATOM 1891 O ILE A 252 7.564 66.047 184.387 1.00 67.26 O
ANISOU 1891 O ILE A 252 6345 5379 13832 -995 -809 106 O
ATOM 1892 CB ILE A 252 8.064 69.373 184.230 1.00 63.91 C
ANISOU 1892 CB ILE A 252 5990 5388 12906 -830 -768 168 C
ATOM 1893 CG1 ILE A 252 7.957 70.445 185.335 1.00 63.23 C
ANISOU 1893 CG1 ILE A 252 5869 5374 12780 -721 -563 317 C
ATOM 1894 CG2 ILE A 252 6.682 69.082 183.618 1.00 66.36 C
ANISOU 1894 CG2 ILE A 252 6111 5603 13501 -962 -938 210 C
ATOM 1895 CD1 ILE A 252 7.676 71.898 184.843 1.00 69.51 C
ANISOU 1895 CD1 ILE A 252 6620 6291 13501 -701 -625 340 C
ATOM 1896 N ARG A 253 9.109 66.624 182.816 1.00 62.31 N
ANISOU 1896 N ARG A 253 5985 4943 12749 -975 -968 -205 N
ATOM 1897 CA ARG A 253 8.923 65.479 181.918 1.00 64.00 C
ANISOU 1897 CA ARG A 253 6231 5009 13076 -1101 -1117 -381 C
ATOM 1898 C ARG A 253 9.277 64.159 182.634 1.00 67.69 C
ANISOU 1898 C ARG A 253 6697 5271 13753 -1071 -994 -374 C
ATOM 1899 O ARG A 253 8.539 63.184 182.480 1.00 69.52 O
ANISOU 1899 O ARG A 253 6849 5316 14251 -1182 -1072 -393 O
ATOM 1900 CB ARG A 253 9.746 65.669 180.622 1.00 64.79 C
ANISOU 1900 CB ARG A 253 6526 5209 12882 -1136 -1222 -625 C
ATOM 1901 CG ARG A 253 9.849 64.457 179.686 1.00 80.05 C
ANISOU 1901 CG ARG A 253 8565 6986 14865 -1254 -1327 -871 C
ATOM 1902 CD ARG A 253 8.567 64.094 178.960 1.00 96.28 C
ANISOU 1902 CD ARG A 253 10549 8960 17073 -1446 -1583 -908 C
ATOM 1903 NE ARG A 253 8.739 62.870 178.175 1.00110.74 N
ANISOU 1903 NE ARG A 253 12509 10616 18952 -1561 -1662 -1172 N
ATOM 1904 CZ ARG A 253 7.769 62.261 177.500 1.00129.84 C
ANISOU 1904 CZ ARG A 253 14899 12913 21520 -1752 -1902 -1262 C
ATOM 1905 NH1 ARG A 253 8.023 61.152 176.819 1.00120.07 N
ANISOU 1905 NH1 ARG A 253 13809 11502 20311 -1852 -1950 -1534 N
ATOM 1906 NH2 ARG A 253 6.537 62.757 177.501 1.00118.20 N
ANISOU 1906 NH2 ARG A 253 13242 11476 20194 -1847 -2099 -1086 N
ATOM 1907 N ILE A 254 10.363 64.144 183.441 1.00 62.00 N
ANISOU 1907 N ILE A 254 6050 4570 12938 -929 -820 -323 N
ATOM 1908 CA ILE A 254 10.787 62.960 184.202 1.00 62.33 C
ANISOU 1908 CA ILE A 254 6088 4415 13180 -884 -714 -269 C
ATOM 1909 C ILE A 254 9.754 62.677 185.319 1.00 67.71 C
ANISOU 1909 C ILE A 254 6625 4999 14103 -907 -628 -10 C
ATOM 1910 O ILE A 254 9.454 61.507 185.562 1.00 69.71 O
ANISOU 1910 O ILE A 254 6824 5033 14631 -958 -615 27 O
ATOM 1911 CB ILE A 254 12.248 63.062 184.744 1.00 63.74 C
ANISOU 1911 CB ILE A 254 6368 4644 13206 -731 -595 -259 C
ATOM 1912 CG1 ILE A 254 13.256 63.332 183.597 1.00 63.20 C
ANISOU 1912 CG1 ILE A 254 6421 4659 12934 -712 -635 -515 C
ATOM 1913 CG2 ILE A 254 12.643 61.784 185.503 1.00 65.48 C
ANISOU 1913 CG2 ILE A 254 6571 4637 13672 -687 -520 -171 C
ATOM 1914 CD1 ILE A 254 14.649 63.854 184.017 1.00 64.94 C
ANISOU 1914 CD1 ILE A 254 6701 4984 12989 -567 -536 -494 C
ATOM 1915 N PHE A 255 9.179 63.735 185.951 1.00 63.35 N
ANISOU 1915 N PHE A 255 6008 4593 13469 -876 -551 160 N
ATOM 1916 CA PHE A 255 8.142 63.594 186.987 1.00 64.69 C
ANISOU 1916 CA PHE A 255 6042 4685 13852 -900 -417 400 C
ATOM 1917 C PHE A 255 6.901 62.912 186.421 1.00 71.87 C
ANISOU 1917 C PHE A 255 6777 5428 15101 -1054 -531 389 C
ATOM 1918 O PHE A 255 6.269 62.107 187.109 1.00 72.74 O
ANISOU 1918 O PHE A 255 6783 5367 15490 -1100 -432 546 O
ATOM 1919 CB PHE A 255 7.729 64.960 187.579 1.00 65.48 C
ANISOU 1919 CB PHE A 255 6108 4965 13807 -841 -299 529 C
ATOM 1920 CG PHE A 255 8.723 65.704 188.438 1.00 65.43 C
ANISOU 1920 CG PHE A 255 6257 5107 13498 -708 -166 584 C
ATOM 1921 CD1 PHE A 255 9.475 65.037 189.399 1.00 68.77 C
ANISOU 1921 CD1 PHE A 255 6787 5469 13873 -647 -67 688 C
ATOM 1922 CD2 PHE A 255 8.834 67.087 188.357 1.00 66.40 C
ANISOU 1922 CD2 PHE A 255 6410 5414 13404 -654 -150 556 C
ATOM 1923 CE1 PHE A 255 10.384 65.730 190.203 1.00 68.64 C
ANISOU 1923 CE1 PHE A 255 6918 5589 13573 -545 12 743 C
ATOM 1924 CE2 PHE A 255 9.741 67.782 189.164 1.00 68.02 C
ANISOU 1924 CE2 PHE A 255 6761 5743 13340 -550 -47 594 C
ATOM 1925 CZ PHE A 255 10.507 67.099 190.086 1.00 66.46 C
ANISOU 1925 CZ PHE A 255 6678 5496 13079 -502 22 683 C
ATOM 1926 N TRP A 256 6.554 63.257 185.163 1.00 70.22 N
ANISOU 1926 N TRP A 256 6544 5273 14865 -1145 -751 216 N
ATOM 1927 CA TRP A 256 5.407 62.722 184.440 1.00 73.13 C
ANISOU 1927 CA TRP A 256 6753 5502 15530 -1314 -938 177 C
ATOM 1928 C TRP A 256 5.653 61.259 184.058 1.00 77.66 C
ANISOU 1928 C TRP A 256 7379 5844 16283 -1400 -1016 33 C
ATOM 1929 O TRP A 256 4.785 60.423 184.308 1.00 79.36 O
ANISOU 1929 O TRP A 256 7439 5856 16861 -1504 -1025 124 O
ATOM 1930 CB TRP A 256 5.084 63.581 183.200 1.00 72.60 C
ANISOU 1930 CB TRP A 256 6687 5580 15317 -1390 -1188 44 C
ATOM 1931 CG TRP A 256 3.900 63.082 182.429 1.00 77.09 C
ANISOU 1931 CG TRP A 256 7094 6016 16183 -1582 -1439 11 C
ATOM 1932 CD1 TRP A 256 3.921 62.413 181.240 1.00 81.99 C
ANISOU 1932 CD1 TRP A 256 7810 6559 16782 -1729 -1701 -226 C
ATOM 1933 CD2 TRP A 256 2.532 63.091 182.860 1.00 79.14 C
ANISOU 1933 CD2 TRP A 256 7060 6172 16836 -1658 -1442 219 C
ATOM 1934 NE1 TRP A 256 2.646 62.039 180.883 1.00 84.37 N
ANISOU 1934 NE1 TRP A 256 7901 6725 17430 -1904 -1914 -177 N
ATOM 1935 CE2 TRP A 256 1.772 62.454 181.854 1.00 85.99 C
ANISOU 1935 CE2 TRP A 256 7842 6910 17921 -1859 -1758 106 C
ATOM 1936 CE3 TRP A 256 1.868 63.601 183.990 1.00 80.47 C
ANISOU 1936 CE3 TRP A 256 7032 6343 17201 -1580 -1196 484 C
ATOM 1937 CZ2 TRP A 256 0.384 62.301 181.949 1.00 88.03 C
ANISOU 1937 CZ2 TRP A 256 7787 7033 18626 -1984 -1856 268 C
ATOM 1938 CZ3 TRP A 256 0.493 63.451 184.082 1.00 84.73 C
ANISOU 1938 CZ3 TRP A 256 7264 6748 18182 -1692 -1245 640 C
ATOM 1939 CH2 TRP A 256 -0.234 62.803 183.073 1.00 88.10 C
ANISOU 1939 CH2 TRP A 256 7573 7040 18860 -1891 -1583 542 C
ATOM 1940 N LEU A 257 6.840 60.945 183.491 1.00 72.43 N
ANISOU 1940 N LEU A 257 6923 5193 15403 -1353 -1046 -186 N
ATOM 1941 CA LEU A 257 7.207 59.582 183.089 1.00 73.61 C
ANISOU 1941 CA LEU A 257 7142 5102 15725 -1414 -1091 -360 C
ATOM 1942 C LEU A 257 7.284 58.635 184.286 1.00 76.93 C
ANISOU 1942 C LEU A 257 7493 5316 16420 -1359 -906 -157 C
ATOM 1943 O LEU A 257 6.930 57.465 184.147 1.00 78.73 O
ANISOU 1943 O LEU A 257 7669 5282 16964 -1459 -953 -204 O
ATOM 1944 CB LEU A 257 8.533 59.566 182.322 1.00 72.90 C
ANISOU 1944 CB LEU A 257 7274 5072 15352 -1346 -1096 -625 C
ATOM 1945 CG LEU A 257 8.470 60.032 180.869 1.00 78.20 C
ANISOU 1945 CG LEU A 257 8067 5866 15781 -1455 -1301 -887 C
ATOM 1946 CD1 LEU A 257 9.825 60.439 180.390 1.00 76.94 C
ANISOU 1946 CD1 LEU A 257 8106 5841 15286 -1345 -1213 -1063 C
ATOM 1947 CD2 LEU A 257 7.895 58.954 179.951 1.00 84.03 C
ANISOU 1947 CD2 LEU A 257 8831 6384 16714 -1646 -1490 -1111 C
ATOM 1948 N LEU A 258 7.729 59.140 185.457 1.00 71.15 N
ANISOU 1948 N LEU A 258 6775 4695 15565 -1212 -707 72 N
ATOM 1949 CA LEU A 258 7.813 58.365 186.700 1.00 71.59 C
ANISOU 1949 CA LEU A 258 6794 4589 15816 -1160 -531 318 C
ATOM 1950 C LEU A 258 6.419 57.985 187.190 1.00 77.68 C
ANISOU 1950 C LEU A 258 7367 5222 16927 -1279 -483 521 C
ATOM 1951 O LEU A 258 6.216 56.867 187.669 1.00 79.23 O
ANISOU 1951 O LEU A 258 7507 5171 17427 -1324 -422 637 O
ATOM 1952 CB LEU A 258 8.559 59.153 187.793 1.00 69.26 C
ANISOU 1952 CB LEU A 258 6593 4485 15239 -999 -364 507 C
ATOM 1953 CG LEU A 258 10.078 59.018 187.828 1.00 72.13 C
ANISOU 1953 CG LEU A 258 7111 4872 15423 -866 -359 423 C
ATOM 1954 CD1 LEU A 258 10.706 60.221 188.495 1.00 69.55 C
ANISOU 1954 CD1 LEU A 258 6875 4805 14745 -745 -281 523 C
ATOM 1955 CD2 LEU A 258 10.501 57.752 188.552 1.00 76.32 C
ANISOU 1955 CD2 LEU A 258 7645 5152 16201 -834 -296 570 C
ATOM 1956 N HIS A 259 5.460 58.919 187.044 1.00 73.87 N
ANISOU 1956 N HIS A 259 6759 4882 16426 -1332 -507 570 N
ATOM 1957 CA HIS A 259 4.065 58.763 187.442 1.00 75.92 C
ANISOU 1957 CA HIS A 259 6783 5031 17030 -1443 -448 764 C
ATOM 1958 C HIS A 259 3.302 57.809 186.500 1.00 82.54 C
ANISOU 1958 C HIS A 259 7487 5636 18238 -1634 -675 623 C
ATOM 1959 O HIS A 259 2.490 57.017 186.980 1.00 84.44 O
ANISOU 1959 O HIS A 259 7557 5659 18867 -1729 -603 788 O
ATOM 1960 CB HIS A 259 3.384 60.146 187.491 1.00 75.69 C
ANISOU 1960 CB HIS A 259 6649 5222 16888 -1419 -411 839 C
ATOM 1961 CG HIS A 259 1.901 60.108 187.691 1.00 81.56 C
ANISOU 1961 CG HIS A 259 7103 5854 18031 -1535 -369 1010 C
ATOM 1962 ND1 HIS A 259 1.338 59.580 188.842 1.00 85.19 N
ANISOU 1962 ND1 HIS A 259 7451 6172 18743 -1545 -99 1276 N
ATOM 1963 CD2 HIS A 259 0.910 60.554 186.884 1.00 84.59 C
ANISOU 1963 CD2 HIS A 259 7282 6248 18609 -1645 -565 964 C
ATOM 1964 CE1 HIS A 259 0.029 59.704 188.690 1.00 86.81 C
ANISOU 1964 CE1 HIS A 259 7369 6297 19318 -1657 -114 1372 C
ATOM 1965 NE2 HIS A 259 -0.277 60.288 187.530 1.00 86.88 N
ANISOU 1965 NE2 HIS A 259 7301 6390 19321 -1719 -409 1195 N
ATOM 1966 N THR A 260 3.566 57.880 185.177 1.00 79.14 N
ANISOU 1966 N THR A 260 7146 5245 17677 -1701 -943 322 N
ATOM 1967 CA THR A 260 2.875 57.077 184.161 1.00 81.67 C
ANISOU 1967 CA THR A 260 7384 5366 18280 -1904 -1208 140 C
ATOM 1968 C THR A 260 3.540 55.711 183.904 1.00 88.02 C
ANISOU 1968 C THR A 260 8317 5907 19220 -1939 -1232 -38 C
ATOM 1969 O THR A 260 2.869 54.687 184.031 1.00 90.57 O
ANISOU 1969 O THR A 260 8503 5951 19958 -2068 -1261 12 O
ATOM 1970 CB THR A 260 2.737 57.854 182.830 1.00 86.64 C
ANISOU 1970 CB THR A 260 8076 6174 18671 -1985 -1502 -94 C
ATOM 1971 OG1 THR A 260 4.012 58.012 182.207 1.00 84.43 O
ANISOU 1971 OG1 THR A 260 8078 6012 17991 -1898 -1522 -342 O
ATOM 1972 CG2 THR A 260 2.088 59.207 183.003 1.00 83.59 C
ANISOU 1972 CG2 THR A 260 7548 6016 18198 -1946 -1498 81 C
ATOM 1973 N SER A 261 4.829 55.694 183.513 1.00 83.75 N
ANISOU 1973 N SER A 261 8019 5432 18372 -1829 -1213 -249 N
ATOM 1974 CA SER A 261 5.547 54.473 183.147 1.00 85.63 C
ANISOU 1974 CA SER A 261 8383 5412 18741 -1844 -1223 -460 C
ATOM 1975 C SER A 261 6.190 53.741 184.330 1.00 90.47 C
ANISOU 1975 C SER A 261 8993 5859 19525 -1709 -982 -241 C
ATOM 1976 O SER A 261 6.310 52.517 184.280 1.00 92.69 O
ANISOU 1976 O SER A 261 9272 5826 20120 -1759 -982 -310 O
ATOM 1977 CB SER A 261 6.614 54.780 182.103 1.00 88.21 C
ANISOU 1977 CB SER A 261 8954 5867 18694 -1793 -1292 -798 C
ATOM 1978 OG SER A 261 6.023 55.259 180.906 1.00 97.64 O
ANISOU 1978 OG SER A 261 10190 7176 19732 -1949 -1547 -1012 O
ATOM 1979 N GLY A 262 6.624 54.477 185.349 1.00 85.31 N
ANISOU 1979 N GLY A 262 8352 5401 18660 -1546 -798 12 N
ATOM 1980 CA GLY A 262 7.277 53.891 186.515 1.00 85.62 C
ANISOU 1980 CA GLY A 262 8413 5320 18798 -1420 -604 255 C
ATOM 1981 C GLY A 262 8.696 53.437 186.235 1.00 90.68 C
ANISOU 1981 C GLY A 262 9213 5887 19356 -1294 -591 79 C
ATOM 1982 O GLY A 262 9.218 53.663 185.139 1.00 90.04 O
ANISOU 1982 O GLY A 262 9243 5873 19096 -1296 -690 -247 O
ATOM 1983 N THR A 263 9.328 52.774 187.216 1.00 88.97 N
ANISOU 1983 N THR A 263 9005 5518 19281 -1186 -464 305 N
ATOM 1984 CA THR A 263 10.715 52.308 187.097 1.00 89.21 C
ANISOU 1984 CA THR A 263 9140 5448 19309 -1045 -440 192 C
ATOM 1985 C THR A 263 10.818 50.780 186.835 1.00 96.43 C
ANISOU 1985 C THR A 263 10017 5934 20689 -1093 -451 99 C
ATOM 1986 O THR A 263 11.812 50.156 187.221 1.00 96.61 O
ANISOU 1986 O THR A 263 10063 5787 20856 -963 -389 167 O
ATOM 1987 CB THR A 263 11.523 52.725 188.333 1.00 97.08 C
ANISOU 1987 CB THR A 263 10178 6583 20125 -878 -334 508 C
ATOM 1988 OG1 THR A 263 10.765 52.435 189.508 1.00 98.71 O
ANISOU 1988 OG1 THR A 263 10315 6721 20469 -920 -245 884 O
ATOM 1989 CG2 THR A 263 11.906 54.194 188.306 1.00 93.34 C
ANISOU 1989 CG2 THR A 263 9784 6496 19184 -799 -335 472 C
ATOM 1990 N GLN A 264 9.824 50.193 186.135 1.00 95.65 N
ANISOU 1990 N GLN A 264 9854 5645 20844 -1280 -545 -69 N
ATOM 1991 CA GLN A 264 9.851 48.770 185.771 1.00 99.17 C
ANISOU 1991 CA GLN A 264 10275 5662 21745 -1348 -565 -211 C
ATOM 1992 C GLN A 264 10.795 48.582 184.577 1.00103.84 C
ANISOU 1992 C GLN A 264 11012 6191 22251 -1306 -594 -658 C
ATOM 1993 O GLN A 264 11.694 47.744 184.631 1.00105.03 O
ANISOU 1993 O GLN A 264 11183 6079 22643 -1200 -510 -714 O
ATOM 1994 CB GLN A 264 8.442 48.243 185.464 1.00102.91 C
ANISOU 1994 CB GLN A 264 10626 5951 22526 -1583 -673 -237 C
ATOM 1995 N ASN A 265 10.609 49.405 183.526 1.00 99.61 N
ANISOU 1995 N ASN A 265 10577 5902 21366 -1382 -697 -957 N
ATOM 1996 CA ASN A 265 11.431 49.450 182.318 1.00100.00 C
ANISOU 1996 CA ASN A 265 10803 5968 21224 -1360 -699 -1390 C
ATOM 1997 C ASN A 265 12.199 50.777 182.323 1.00101.50 C
ANISOU 1997 C ASN A 265 11071 6560 20936 -1217 -644 -1361 C
ATOM 1998 O ASN A 265 11.582 51.846 182.292 1.00 98.87 O
ANISOU 1998 O ASN A 265 10731 6535 20300 -1271 -731 -1275 O
ATOM 1999 CB ASN A 265 10.556 49.288 181.059 1.00101.62 C
ANISOU 1999 CB ASN A 265 11093 6125 21393 -1597 -886 -1748 C
ATOM 2000 CG ASN A 265 11.275 49.438 179.735 1.00122.39 C
ANISOU 2000 CG ASN A 265 13955 8813 23733 -1609 -882 -2209 C
ATOM 2001 OD1 ASN A 265 12.414 49.000 179.552 1.00117.36 O
ANISOU 2001 OD1 ASN A 265 13401 8037 23154 -1472 -707 -2379 O
ATOM 2002 ND2 ASN A 265 10.603 50.037 178.764 1.00114.28 N
ANISOU 2002 ND2 ASN A 265 13037 7981 22402 -1782 -1072 -2417 N
ATOM 2003 N CYS A 266 13.539 50.702 182.425 1.00 98.47 N
ANISOU 2003 N CYS A 266 10734 6149 20532 -1030 -497 -1406 N
ATOM 2004 CA CYS A 266 14.424 51.869 182.489 1.00 95.73 C
ANISOU 2004 CA CYS A 266 10441 6138 19795 -885 -432 -1370 C
ATOM 2005 C CYS A 266 14.581 52.559 181.133 1.00 98.93 C
ANISOU 2005 C CYS A 266 11015 6745 19829 -954 -460 -1744 C
ATOM 2006 O CYS A 266 14.794 53.770 181.102 1.00 95.61 O
ANISOU 2006 O CYS A 266 10631 6660 19035 -908 -467 -1685 O
ATOM 2007 CB CYS A 266 15.787 51.484 183.060 1.00 96.57 C
ANISOU 2007 CB CYS A 266 10502 6114 20076 -673 -286 -1273 C
ATOM 2008 SG CYS A 266 15.819 51.292 184.862 1.00100.03 S
ANISOU 2008 SG CYS A 266 10787 6506 20714 -561 -282 -718 S
ATOM 2009 N GLU A 267 14.489 51.793 180.024 1.00 98.51 N
ANISOU 2009 N GLU A 267 11082 6480 19867 -1070 -473 -2127 N
ATOM 2010 CA GLU A 267 14.663 52.244 178.636 1.00 98.92 C
ANISOU 2010 CA GLU A 267 11347 6679 19559 -1160 -488 -2518 C
ATOM 2011 C GLU A 267 13.829 53.490 178.273 1.00100.55 C
ANISOU 2011 C GLU A 267 11602 7255 19348 -1281 -673 -2458 C
ATOM 2012 O GLU A 267 14.259 54.266 177.418 1.00100.11 O
ANISOU 2012 O GLU A 267 11708 7428 18904 -1289 -654 -2648 O
ATOM 2013 CB GLU A 267 14.339 51.094 177.667 1.00104.43 C
ANISOU 2013 CB GLU A 267 12174 7054 20449 -1320 -520 -2906 C
ATOM 2014 CG GLU A 267 14.877 51.255 176.248 1.00116.54 C
ANISOU 2014 CG GLU A 267 13979 8655 21645 -1383 -448 -3363 C
ATOM 2015 CD GLU A 267 16.375 51.428 176.063 1.00135.20 C
ANISOU 2015 CD GLU A 267 16397 11044 23929 -1180 -153 -3490 C
ATOM 2016 OE1 GLU A 267 16.765 52.120 175.095 1.00132.62 O
ANISOU 2016 OE1 GLU A 267 16271 10939 23179 -1215 -91 -3728 O
ATOM 2017 OE2 GLU A 267 17.158 50.876 176.871 1.00123.98 O
ANISOU 2017 OE2 GLU A 267 14812 9416 22880 -991 12 -3338 O
ATOM 2018 N VAL A 268 12.680 53.708 178.945 1.00 95.34 N
ANISOU 2018 N VAL A 268 10792 6647 18787 -1364 -832 -2174 N
ATOM 2019 CA VAL A 268 11.807 54.864 178.694 1.00 92.89 C
ANISOU 2019 CA VAL A 268 10477 6646 18169 -1466 -1011 -2077 C
ATOM 2020 C VAL A 268 12.411 56.176 179.280 1.00 90.51 C
ANISOU 2020 C VAL A 268 10146 6672 17574 -1300 -913 -1850 C
ATOM 2021 O VAL A 268 11.785 57.232 179.160 1.00 89.04 O
ANISOU 2021 O VAL A 268 9941 6738 17151 -1354 -1033 -1744 O
ATOM 2022 CB VAL A 268 10.341 54.639 179.176 1.00 97.89 C
ANISOU 2022 CB VAL A 268 10929 7197 19068 -1613 -1188 -1862 C
ATOM 2023 CG1 VAL A 268 9.687 53.464 178.449 1.00101.49 C
ANISOU 2023 CG1 VAL A 268 11422 7346 19792 -1814 -1334 -2115 C
ATOM 2024 CG2 VAL A 268 10.252 54.463 180.690 1.00 96.54 C
ANISOU 2024 CG2 VAL A 268 10556 6953 19171 -1490 -1055 -1469 C
ATOM 2025 N TYR A 269 13.626 56.110 179.877 1.00 83.40 N
ANISOU 2025 N TYR A 269 9232 5747 16709 -1104 -712 -1781 N
ATOM 2026 CA TYR A 269 14.318 57.260 180.472 1.00 78.64 C
ANISOU 2026 CA TYR A 269 8603 5416 15861 -952 -627 -1585 C
ATOM 2027 C TYR A 269 15.668 57.563 179.805 1.00 81.26 C
ANISOU 2027 C TYR A 269 9057 5826 15992 -848 -482 -1801 C
ATOM 2028 O TYR A 269 16.334 58.502 180.234 1.00 78.94 O
ANISOU 2028 O TYR A 269 8737 5741 15515 -729 -417 -1660 O
ATOM 2029 CB TYR A 269 14.549 57.041 181.980 1.00 78.04 C
ANISOU 2029 CB TYR A 269 8376 5267 16007 -817 -544 -1238 C
ATOM 2030 CG TYR A 269 13.284 56.857 182.784 1.00 79.42 C
ANISOU 2030 CG TYR A 269 8425 5387 16362 -903 -622 -980 C
ATOM 2031 CD1 TYR A 269 12.543 57.954 183.217 1.00 79.24 C
ANISOU 2031 CD1 TYR A 269 8350 5609 16149 -926 -669 -782 C
ATOM 2032 CD2 TYR A 269 12.837 55.588 183.136 1.00 82.57 C
ANISOU 2032 CD2 TYR A 269 8747 5473 17154 -957 -622 -925 C
ATOM 2033 CE1 TYR A 269 11.377 57.790 183.961 1.00 80.56 C
ANISOU 2033 CE1 TYR A 269 8385 5716 16509 -1001 -694 -545 C
ATOM 2034 CE2 TYR A 269 11.677 55.411 183.887 1.00 83.79 C
ANISOU 2034 CE2 TYR A 269 8771 5568 17496 -1041 -660 -672 C
ATOM 2035 CZ TYR A 269 10.946 56.515 184.291 1.00 89.12 C
ANISOU 2035 CZ TYR A 269 9391 6497 17974 -1062 -685 -486 C
ATOM 2036 OH TYR A 269 9.802 56.338 185.026 1.00 90.91 O
ANISOU 2036 OH TYR A 269 9474 6656 18412 -1142 -677 -240 O
ATOM 2037 N ARG A 270 16.069 56.802 178.764 1.00 79.49 N
ANISOU 2037 N ARG A 270 8964 5431 15806 -898 -417 -2149 N
ATOM 2038 CA ARG A 270 17.355 56.986 178.076 1.00 79.58 C
ANISOU 2038 CA ARG A 270 9085 5484 15668 -802 -224 -2375 C
ATOM 2039 C ARG A 270 17.490 58.378 177.415 1.00 81.72 C
ANISOU 2039 C ARG A 270 9472 6109 15469 -833 -244 -2410 C
ATOM 2040 O ARG A 270 18.442 59.100 177.721 1.00 79.87 O
ANISOU 2040 O ARG A 270 9192 6019 15136 -695 -120 -2311 O
ATOM 2041 CB ARG A 270 17.575 55.881 177.032 1.00 83.82 C
ANISOU 2041 CB ARG A 270 9771 5755 16321 -876 -129 -2774 C
ATOM 2042 CG ARG A 270 19.042 55.503 176.853 1.00 95.75 C
ANISOU 2042 CG ARG A 270 11282 7130 17967 -709 156 -2934 C
ATOM 2043 CD ARG A 270 19.197 54.161 176.172 1.00107.98 C
ANISOU 2043 CD ARG A 270 12927 8317 19782 -753 279 -3284 C
ATOM 2044 NE ARG A 270 20.577 53.675 176.217 1.00119.52 N
ANISOU 2044 NE ARG A 270 14317 9586 21511 -561 570 -3385 N
ATOM 2045 CZ ARG A 270 20.942 52.424 175.946 1.00140.51 C
ANISOU 2045 CZ ARG A 270 16982 11860 24546 -529 730 -3626 C
ATOM 2046 NH1 ARG A 270 22.219 52.071 176.009 1.00131.69 N
ANISOU 2046 NH1 ARG A 270 15760 10569 23706 -338 1003 -3690 N
ATOM 2047 NH2 ARG A 270 20.031 51.515 175.614 1.00128.07 N
ANISOU 2047 NH2 ARG A 270 15501 10051 23108 -689 616 -3802 N
ATOM 2048 N SER A 271 16.532 58.747 176.537 1.00 78.30 N
ANISOU 2048 N SER A 271 9176 5801 14772 -1019 -422 -2528 N
ATOM 2049 CA SER A 271 16.502 60.005 175.785 1.00 76.74 C
ANISOU 2049 CA SER A 271 9109 5917 14133 -1079 -479 -2553 C
ATOM 2050 C SER A 271 16.363 61.233 176.686 1.00 77.94 C
ANISOU 2050 C SER A 271 9111 6305 14196 -993 -535 -2207 C
ATOM 2051 O SER A 271 16.994 62.259 176.420 1.00 76.68 O
ANISOU 2051 O SER A 271 9004 6361 13769 -940 -462 -2185 O
ATOM 2052 CB SER A 271 15.359 59.990 174.773 1.00 81.85 C
ANISOU 2052 CB SER A 271 9910 6606 14582 -1312 -723 -2705 C
ATOM 2053 OG SER A 271 14.102 59.784 175.399 1.00 89.12 O
ANISOU 2053 OG SER A 271 10669 7461 15732 -1392 -944 -2504 O
ATOM 2054 N VAL A 272 15.531 61.133 177.736 1.00 73.28 N
ANISOU 2054 N VAL A 272 8346 5665 13833 -985 -645 -1946 N
ATOM 2055 CA VAL A 272 15.262 62.219 178.683 1.00 69.97 C
ANISOU 2055 CA VAL A 272 7796 5437 13353 -912 -682 -1634 C
ATOM 2056 C VAL A 272 16.480 62.479 179.559 1.00 71.89 C
ANISOU 2056 C VAL A 272 7969 5707 13639 -723 -505 -1508 C
ATOM 2057 O VAL A 272 16.690 63.618 179.975 1.00 69.42 O
ANISOU 2057 O VAL A 272 7624 5598 13154 -661 -498 -1349 O
ATOM 2058 CB VAL A 272 14.010 61.975 179.554 1.00 73.77 C
ANISOU 2058 CB VAL A 272 8120 5841 14069 -964 -803 -1405 C
ATOM 2059 CG1 VAL A 272 13.304 63.291 179.846 1.00 71.56 C
ANISOU 2059 CG1 VAL A 272 7773 5791 13626 -976 -892 -1197 C
ATOM 2060 CG2 VAL A 272 13.054 60.986 178.896 1.00 76.51 C
ANISOU 2060 CG2 VAL A 272 8488 5999 14583 -1136 -950 -1559 C
ATOM 2061 N ASP A 273 17.278 61.431 179.839 1.00 69.51 N
ANISOU 2061 N ASP A 273 7637 5186 13590 -636 -379 -1574 N
ATOM 2062 CA ASP A 273 18.498 61.551 180.635 1.00 68.11 C
ANISOU 2062 CA ASP A 273 7374 5003 13502 -462 -247 -1451 C
ATOM 2063 C ASP A 273 19.552 62.336 179.862 1.00 70.35 C
ANISOU 2063 C ASP A 273 7733 5444 13554 -416 -129 -1599 C
ATOM 2064 O ASP A 273 20.227 63.168 180.459 1.00 67.96 O
ANISOU 2064 O ASP A 273 7362 5279 13179 -319 -98 -1442 O
ATOM 2065 CB ASP A 273 19.033 60.171 181.051 1.00 72.06 C
ANISOU 2065 CB ASP A 273 7800 5195 14385 -384 -163 -1471 C
ATOM 2066 CG ASP A 273 18.357 59.556 182.270 1.00 82.08 C
ANISOU 2066 CG ASP A 273 8956 6326 15905 -376 -243 -1200 C
ATOM 2067 OD1 ASP A 273 17.272 60.047 182.668 1.00 80.91 O
ANISOU 2067 OD1 ASP A 273 8794 6294 15656 -456 -349 -1043 O
ATOM 2068 OD2 ASP A 273 18.885 58.560 182.796 1.00 89.45 O
ANISOU 2068 OD2 ASP A 273 9813 7019 17154 -292 -189 -1140 O
ATOM 2069 N LEU A 274 19.663 62.108 178.534 1.00 68.40 N
ANISOU 2069 N LEU A 274 7637 5179 13171 -500 -64 -1900 N
ATOM 2070 CA LEU A 274 20.602 62.828 177.669 1.00 68.46 C
ANISOU 2070 CA LEU A 274 7740 5335 12936 -479 85 -2051 C
ATOM 2071 C LEU A 274 20.204 64.307 177.617 1.00 70.90 C
ANISOU 2071 C LEU A 274 8081 5941 12918 -526 -26 -1899 C
ATOM 2072 O LEU A 274 21.076 65.174 177.693 1.00 69.99 O
ANISOU 2072 O LEU A 274 7933 5962 12698 -448 71 -1836 O
ATOM 2073 CB LEU A 274 20.659 62.198 176.258 1.00 71.54 C
ANISOU 2073 CB LEU A 274 8335 5638 13209 -585 187 -2414 C
ATOM 2074 CG LEU A 274 21.571 62.853 175.194 1.00 77.05 C
ANISOU 2074 CG LEU A 274 9176 6481 13617 -589 387 -2600 C
ATOM 2075 CD1 LEU A 274 23.025 62.921 175.643 1.00 76.97 C
ANISOU 2075 CD1 LEU A 274 9007 6418 13818 -405 625 -2555 C
ATOM 2076 CD2 LEU A 274 21.491 62.110 173.882 1.00 82.98 C
ANISOU 2076 CD2 LEU A 274 10172 7129 14229 -713 488 -2971 C
ATOM 2077 N ALA A 275 18.885 64.584 177.567 1.00 66.46 N
ANISOU 2077 N ALA A 275 7550 5452 12249 -648 -233 -1820 N
ATOM 2078 CA ALA A 275 18.336 65.938 177.579 1.00 64.14 C
ANISOU 2078 CA ALA A 275 7259 5399 11713 -690 -355 -1654 C
ATOM 2079 C ALA A 275 18.586 66.607 178.931 1.00 65.28 C
ANISOU 2079 C ALA A 275 7242 5605 11956 -563 -345 -1383 C
ATOM 2080 O ALA A 275 18.884 67.796 178.962 1.00 63.84 O
ANISOU 2080 O ALA A 275 7059 5601 11594 -537 -337 -1290 O
ATOM 2081 CB ALA A 275 16.849 65.904 177.277 1.00 65.44 C
ANISOU 2081 CB ALA A 275 7448 5575 11841 -839 -581 -1623 C
ATOM 2082 N PHE A 276 18.507 65.836 180.038 1.00 61.21 N
ANISOU 2082 N PHE A 276 6609 4933 11714 -494 -342 -1259 N
ATOM 2083 CA PHE A 276 18.729 66.319 181.404 1.00 59.18 C
ANISOU 2083 CA PHE A 276 6239 4720 11527 -390 -340 -1010 C
ATOM 2084 C PHE A 276 20.146 66.880 181.574 1.00 64.11 C
ANISOU 2084 C PHE A 276 6838 5416 12107 -279 -234 -1002 C
ATOM 2085 O PHE A 276 20.290 67.992 182.079 1.00 62.52 O
ANISOU 2085 O PHE A 276 6615 5368 11774 -249 -259 -868 O
ATOM 2086 CB PHE A 276 18.466 65.197 182.433 1.00 61.22 C
ANISOU 2086 CB PHE A 276 6412 4777 12073 -351 -349 -886 C
ATOM 2087 CG PHE A 276 18.794 65.533 183.871 1.00 61.04 C
ANISOU 2087 CG PHE A 276 6316 4785 12091 -254 -348 -635 C
ATOM 2088 CD1 PHE A 276 17.841 66.102 184.703 1.00 63.07 C
ANISOU 2088 CD1 PHE A 276 6556 5125 12283 -282 -396 -445 C
ATOM 2089 CD2 PHE A 276 20.051 65.259 184.398 1.00 63.06 C
ANISOU 2089 CD2 PHE A 276 6523 4980 12459 -140 -298 -589 C
ATOM 2090 CE1 PHE A 276 18.143 66.406 186.032 1.00 63.25 C
ANISOU 2090 CE1 PHE A 276 6561 5182 12291 -209 -387 -233 C
ATOM 2091 CE2 PHE A 276 20.357 65.575 185.724 1.00 65.07 C
ANISOU 2091 CE2 PHE A 276 6741 5272 12710 -72 -338 -355 C
ATOM 2092 CZ PHE A 276 19.399 66.141 186.534 1.00 62.31 C
ANISOU 2092 CZ PHE A 276 6421 5016 12237 -113 -378 -188 C
ATOM 2093 N PHE A 277 21.180 66.117 181.168 1.00 62.83 N
ANISOU 2093 N PHE A 277 6664 5124 12085 -221 -112 -1149 N
ATOM 2094 CA PHE A 277 22.573 66.538 181.314 1.00 62.89 C
ANISOU 2094 CA PHE A 277 6602 5167 12128 -116 -7 -1138 C
ATOM 2095 C PHE A 277 22.945 67.627 180.295 1.00 67.01 C
ANISOU 2095 C PHE A 277 7204 5875 12383 -161 69 -1247 C
ATOM 2096 O PHE A 277 23.840 68.421 180.581 1.00 65.75 O
ANISOU 2096 O PHE A 277 6973 5803 12204 -99 112 -1170 O
ATOM 2097 CB PHE A 277 23.535 65.338 181.271 1.00 66.81 C
ANISOU 2097 CB PHE A 277 7017 5433 12935 -25 117 -1237 C
ATOM 2098 CG PHE A 277 23.359 64.462 182.494 1.00 68.71 C
ANISOU 2098 CG PHE A 277 7158 5504 13445 36 22 -1046 C
ATOM 2099 CD1 PHE A 277 23.892 64.839 183.724 1.00 70.85 C
ANISOU 2099 CD1 PHE A 277 7329 5813 13779 119 -66 -800 C
ATOM 2100 CD2 PHE A 277 22.602 63.298 182.434 1.00 72.14 C
ANISOU 2100 CD2 PHE A 277 7617 5743 14049 -7 2 -1098 C
ATOM 2101 CE1 PHE A 277 23.684 64.056 184.864 1.00 72.34 C
ANISOU 2101 CE1 PHE A 277 7460 5859 14165 160 -163 -594 C
ATOM 2102 CE2 PHE A 277 22.390 62.519 183.576 1.00 75.26 C
ANISOU 2102 CE2 PHE A 277 7930 5982 14683 39 -80 -887 C
ATOM 2103 CZ PHE A 277 22.926 62.906 184.784 1.00 72.56 C
ANISOU 2103 CZ PHE A 277 7507 5694 14367 122 -159 -628 C
ATOM 2104 N ILE A 278 22.214 67.720 179.160 1.00 64.48 N
ANISOU 2104 N ILE A 278 7034 5617 11850 -282 60 -1400 N
ATOM 2105 CA ILE A 278 22.419 68.776 178.168 1.00 64.06 C
ANISOU 2105 CA ILE A 278 7086 5748 11505 -345 112 -1468 C
ATOM 2106 C ILE A 278 21.878 70.081 178.775 1.00 66.61 C
ANISOU 2106 C ILE A 278 7373 6242 11694 -357 -28 -1247 C
ATOM 2107 O ILE A 278 22.619 71.062 178.829 1.00 65.61 O
ANISOU 2107 O ILE A 278 7212 6224 11493 -320 30 -1183 O
ATOM 2108 CB ILE A 278 21.802 68.423 176.780 1.00 68.93 C
ANISOU 2108 CB ILE A 278 7905 6378 11909 -486 113 -1686 C
ATOM 2109 CG1 ILE A 278 22.748 67.475 176.002 1.00 71.98 C
ANISOU 2109 CG1 ILE A 278 8356 6623 12371 -462 349 -1950 C
ATOM 2110 CG2 ILE A 278 21.487 69.686 175.947 1.00 69.04 C
ANISOU 2110 CG2 ILE A 278 8044 6614 11575 -585 57 -1651 C
ATOM 2111 CD1 ILE A 278 22.109 66.669 174.840 1.00 81.28 C
ANISOU 2111 CD1 ILE A 278 9751 7732 13399 -603 343 -2213 C
ATOM 2112 N THR A 279 20.625 70.064 179.302 1.00 62.60 N
ANISOU 2112 N THR A 279 6851 5731 11202 -402 -193 -1131 N
ATOM 2113 CA THR A 279 19.978 71.225 179.939 1.00 60.60 C
ANISOU 2113 CA THR A 279 6556 5602 10866 -406 -299 -936 C
ATOM 2114 C THR A 279 20.661 71.587 181.271 1.00 64.54 C
ANISOU 2114 C THR A 279 6949 6097 11477 -295 -272 -785 C
ATOM 2115 O THR A 279 20.521 72.720 181.735 1.00 63.24 O
ANISOU 2115 O THR A 279 6768 6039 11224 -286 -310 -665 O
ATOM 2116 CB THR A 279 18.470 71.001 180.148 1.00 65.45 C
ANISOU 2116 CB THR A 279 7157 6185 11524 -478 -444 -860 C
ATOM 2117 OG1 THR A 279 18.257 69.950 181.089 1.00 62.90 O
ANISOU 2117 OG1 THR A 279 6760 5708 11429 -434 -439 -810 O
ATOM 2118 CG2 THR A 279 17.714 70.743 178.846 1.00 65.37 C
ANISOU 2118 CG2 THR A 279 7255 6190 11394 -612 -538 -991 C
ATOM 2119 N LEU A 280 21.389 70.629 181.881 1.00 62.76 N
ANISOU 2119 N LEU A 280 6658 5739 11450 -216 -221 -791 N
ATOM 2120 CA LEU A 280 22.142 70.839 183.120 1.00 62.43 C
ANISOU 2120 CA LEU A 280 6530 5684 11506 -124 -235 -646 C
ATOM 2121 C LEU A 280 23.332 71.761 182.853 1.00 65.81 C
ANISOU 2121 C LEU A 280 6924 6204 11877 -92 -175 -668 C
ATOM 2122 O LEU A 280 23.665 72.569 183.716 1.00 64.44 O
ANISOU 2122 O LEU A 280 6715 6094 11676 -63 -232 -544 O
ATOM 2123 CB LEU A 280 22.616 69.497 183.710 1.00 64.02 C
ANISOU 2123 CB LEU A 280 6663 5700 11961 -55 -224 -628 C
ATOM 2124 CG LEU A 280 22.934 69.457 185.209 1.00 68.65 C
ANISOU 2124 CG LEU A 280 7194 6256 12635 11 -309 -422 C
ATOM 2125 CD1 LEU A 280 21.667 69.519 186.055 1.00 68.00 C
ANISOU 2125 CD1 LEU A 280 7168 6192 12476 -32 -374 -282 C
ATOM 2126 CD2 LEU A 280 23.701 68.196 185.556 1.00 73.05 C
ANISOU 2126 CD2 LEU A 280 7663 6621 13470 88 -302 -399 C
ATOM 2127 N SER A 281 23.950 71.661 181.649 1.00 63.57 N
ANISOU 2127 N SER A 281 6661 5924 11568 -109 -48 -830 N
ATOM 2128 CA SER A 281 25.073 72.514 181.248 1.00 63.72 C
ANISOU 2128 CA SER A 281 6635 6022 11554 -91 47 -852 C
ATOM 2129 C SER A 281 24.569 73.932 180.937 1.00 66.51 C
ANISOU 2129 C SER A 281 7061 6541 11669 -162 1 -791 C
ATOM 2130 O SER A 281 25.331 74.887 181.084 1.00 66.26 O
ANISOU 2130 O SER A 281 6973 6574 11628 -148 24 -734 O
ATOM 2131 CB SER A 281 25.835 71.918 180.065 1.00 69.27 C
ANISOU 2131 CB SER A 281 7352 6667 12302 -90 246 -1045 C
ATOM 2132 OG SER A 281 25.152 72.051 178.830 1.00 79.36 O
ANISOU 2132 OG SER A 281 8798 8021 13333 -194 294 -1172 O
ATOM 2133 N PHE A 282 23.277 74.067 180.552 1.00 62.43 N
ANISOU 2133 N PHE A 282 6648 6074 10999 -239 -79 -787 N
ATOM 2134 CA PHE A 282 22.620 75.355 180.302 1.00 61.49 C
ANISOU 2134 CA PHE A 282 6581 6083 10701 -299 -147 -702 C
ATOM 2135 C PHE A 282 22.497 76.153 181.608 1.00 63.09 C
ANISOU 2135 C PHE A 282 6717 6301 10955 -253 -226 -550 C
ATOM 2136 O PHE A 282 22.601 77.378 181.576 1.00 62.44 O
ANISOU 2136 O PHE A 282 6636 6295 10793 -270 -235 -487 O
ATOM 2137 CB PHE A 282 21.231 75.166 179.661 1.00 63.98 C
ANISOU 2137 CB PHE A 282 6985 6417 10908 -387 -246 -716 C
ATOM 2138 CG PHE A 282 21.236 74.977 178.163 1.00 67.75 C
ANISOU 2138 CG PHE A 282 7592 6941 11209 -478 -205 -850 C
ATOM 2139 CD1 PHE A 282 21.408 73.716 177.605 1.00 72.94 C
ANISOU 2139 CD1 PHE A 282 8311 7509 11895 -498 -137 -1026 C
ATOM 2140 CD2 PHE A 282 21.038 76.053 177.310 1.00 70.75 C
ANISOU 2140 CD2 PHE A 282 8053 7446 11383 -553 -235 -800 C
ATOM 2141 CE1 PHE A 282 21.411 73.540 176.218 1.00 75.96 C
ANISOU 2141 CE1 PHE A 282 8858 7937 12065 -598 -89 -1176 C
ATOM 2142 CE2 PHE A 282 21.041 75.877 175.922 1.00 75.70 C
ANISOU 2142 CE2 PHE A 282 8843 8129 11789 -655 -204 -915 C
ATOM 2143 CZ PHE A 282 21.227 74.621 175.387 1.00 75.47 C
ANISOU 2143 CZ PHE A 282 8899 8022 11754 -681 -127 -1115 C
ATOM 2144 N THR A 283 22.295 75.463 182.756 1.00 58.24 N
ANISOU 2144 N THR A 283 6061 5603 10464 -201 -275 -493 N
ATOM 2145 CA THR A 283 22.203 76.112 184.071 1.00 56.81 C
ANISOU 2145 CA THR A 283 5862 5433 10291 -168 -335 -369 C
ATOM 2146 C THR A 283 23.571 76.639 184.479 1.00 61.04 C
ANISOU 2146 C THR A 283 6341 5983 10869 -130 -331 -356 C
ATOM 2147 O THR A 283 23.664 77.701 185.089 1.00 59.56 O
ANISOU 2147 O THR A 283 6164 5841 10625 -137 -372 -295 O
ATOM 2148 CB THR A 283 21.626 75.175 185.162 1.00 61.86 C
ANISOU 2148 CB THR A 283 6503 5985 11015 -138 -375 -297 C
ATOM 2149 OG1 THR A 283 22.610 74.239 185.603 1.00 58.90 O
ANISOU 2149 OG1 THR A 283 6079 5526 10776 -82 -382 -295 O
ATOM 2150 CG2 THR A 283 20.357 74.459 184.732 1.00 61.20 C
ANISOU 2150 CG2 THR A 283 6439 5857 10958 -182 -379 -313 C
ATOM 2151 N TYR A 284 24.628 75.893 184.127 1.00 59.80 N
ANISOU 2151 N TYR A 284 6112 5770 10838 -94 -280 -418 N
ATOM 2152 CA TYR A 284 26.002 76.228 184.466 1.00 60.61 C
ANISOU 2152 CA TYR A 284 6113 5863 11054 -59 -286 -397 C
ATOM 2153 C TYR A 284 26.556 77.376 183.611 1.00 65.97 C
ANISOU 2153 C TYR A 284 6771 6623 11671 -102 -206 -433 C
ATOM 2154 O TYR A 284 27.517 78.017 184.042 1.00 65.72 O
ANISOU 2154 O TYR A 284 6653 6594 11724 -94 -241 -390 O
ATOM 2155 CB TYR A 284 26.910 74.989 184.376 1.00 62.97 C
ANISOU 2155 CB TYR A 284 6303 6043 11578 6 -240 -439 C
ATOM 2156 CG TYR A 284 26.528 73.858 185.312 1.00 64.90 C
ANISOU 2156 CG TYR A 284 6553 6184 11923 51 -332 -366 C
ATOM 2157 CD1 TYR A 284 26.092 74.115 186.609 1.00 66.31 C
ANISOU 2157 CD1 TYR A 284 6789 6382 12023 46 -474 -229 C
ATOM 2158 CD2 TYR A 284 26.662 72.528 184.921 1.00 66.77 C
ANISOU 2158 CD2 TYR A 284 6744 6289 12336 94 -263 -433 C
ATOM 2159 CE1 TYR A 284 25.749 73.079 187.477 1.00 68.01 C
ANISOU 2159 CE1 TYR A 284 7024 6504 12313 78 -547 -134 C
ATOM 2160 CE2 TYR A 284 26.316 71.483 185.778 1.00 68.03 C
ANISOU 2160 CE2 TYR A 284 6903 6335 12611 131 -348 -340 C
ATOM 2161 CZ TYR A 284 25.868 71.763 187.060 1.00 75.01 C
ANISOU 2161 CZ TYR A 284 7849 7255 13398 120 -491 -176 C
ATOM 2162 OH TYR A 284 25.532 70.743 187.918 1.00 76.35 O
ANISOU 2162 OH TYR A 284 8033 7315 13662 147 -563 -56 O
ATOM 2163 N MET A 285 25.934 77.689 182.449 1.00 63.51 N
ANISOU 2163 N MET A 285 6545 6376 11211 -158 -121 -491 N
ATOM 2164 CA MET A 285 26.436 78.784 181.614 1.00 64.10 C
ANISOU 2164 CA MET A 285 6616 6526 11213 -208 -37 -494 C
ATOM 2165 C MET A 285 25.950 80.164 182.115 1.00 64.80 C
ANISOU 2165 C MET A 285 6737 6667 11219 -242 -132 -393 C
ATOM 2166 O MET A 285 26.151 81.171 181.430 1.00 64.69 O
ANISOU 2166 O MET A 285 6733 6706 11142 -293 -79 -367 O
ATOM 2167 CB MET A 285 26.149 78.571 180.110 1.00 67.95 C
ANISOU 2167 CB MET A 285 7202 7063 11552 -266 90 -585 C
ATOM 2168 CG MET A 285 24.729 78.765 179.676 1.00 71.81 C
ANISOU 2168 CG MET A 285 7821 7606 11857 -328 2 -560 C
ATOM 2169 SD MET A 285 24.660 78.768 177.873 1.00 78.47 S
ANISOU 2169 SD MET A 285 8812 8532 12473 -426 120 -647 S
ATOM 2170 CE MET A 285 22.944 79.158 177.628 1.00 74.81 C
ANISOU 2170 CE MET A 285 8450 8119 11854 -498 -77 -558 C
ATOM 2171 N ASN A 286 25.399 80.214 183.345 1.00 58.77 N
ANISOU 2171 N ASN A 286 5990 5874 10468 -216 -252 -337 N
ATOM 2172 CA ASN A 286 24.953 81.452 183.979 1.00 57.02 C
ANISOU 2172 CA ASN A 286 5803 5668 10193 -238 -317 -271 C
ATOM 2173 C ASN A 286 26.179 82.299 184.373 1.00 59.42 C
ANISOU 2173 C ASN A 286 6032 5961 10585 -251 -341 -257 C
ATOM 2174 O ASN A 286 26.107 83.523 184.300 1.00 58.42 O
ANISOU 2174 O ASN A 286 5920 5844 10432 -291 -344 -226 O
ATOM 2175 CB ASN A 286 24.023 81.168 185.176 1.00 56.55 C
ANISOU 2175 CB ASN A 286 5806 5575 10105 -210 -390 -235 C
ATOM 2176 CG ASN A 286 24.695 80.848 186.491 1.00 75.74 C
ANISOU 2176 CG ASN A 286 8231 7964 12582 -181 -476 -215 C
ATOM 2177 OD1 ASN A 286 25.153 81.739 187.215 1.00 72.58 O
ANISOU 2177 OD1 ASN A 286 7847 7561 12170 -200 -538 -202 O
ATOM 2178 ND2 ASN A 286 24.699 79.583 186.866 1.00 64.65 N
ANISOU 2178 ND2 ASN A 286 6820 6520 11226 -142 -500 -204 N
ATOM 2179 N VAL A 287 27.312 81.640 184.737 1.00 56.01 N
ANISOU 2179 N VAL A 287 5500 5490 10291 -220 -366 -272 N
ATOM 2180 CA VAL A 287 28.589 82.281 185.103 1.00 56.48 C
ANISOU 2180 CA VAL A 287 5445 5523 10491 -239 -417 -253 C
ATOM 2181 C VAL A 287 29.212 82.964 183.872 1.00 61.35 C
ANISOU 2181 C VAL A 287 5989 6167 11156 -283 -270 -262 C
ATOM 2182 O VAL A 287 29.981 83.916 184.008 1.00 61.84 O
ANISOU 2182 O VAL A 287 5970 6209 11316 -327 -294 -233 O
ATOM 2183 CB VAL A 287 29.611 81.310 185.777 1.00 61.25 C
ANISOU 2183 CB VAL A 287 5927 6064 11281 -191 -505 -239 C
ATOM 2184 CG1 VAL A 287 29.103 80.808 187.116 1.00 60.85 C
ANISOU 2184 CG1 VAL A 287 5972 5991 11157 -168 -670 -193 C
ATOM 2185 CG2 VAL A 287 29.999 80.141 184.870 1.00 61.60 C
ANISOU 2185 CG2 VAL A 287 5881 6076 11446 -138 -359 -289 C
ATOM 2186 N MET A 288 28.868 82.459 182.683 1.00 58.05 N
ANISOU 2186 N MET A 288 5611 5787 10657 -282 -117 -303 N
ATOM 2187 CA MET A 288 29.334 82.915 181.383 1.00 59.04 C
ANISOU 2187 CA MET A 288 5717 5953 10761 -330 60 -310 C
ATOM 2188 C MET A 288 28.443 84.045 180.843 1.00 62.17 C
ANISOU 2188 C MET A 288 6233 6407 10982 -396 55 -244 C
ATOM 2189 O MET A 288 28.939 84.905 180.112 1.00 62.40 O
ANISOU 2189 O MET A 288 6239 6456 11013 -453 153 -195 O
ATOM 2190 CB MET A 288 29.321 81.708 180.430 1.00 62.32 C
ANISOU 2190 CB MET A 288 6167 6379 11132 -307 214 -404 C
ATOM 2191 CG MET A 288 30.011 81.933 179.113 1.00 67.82 C
ANISOU 2191 CG MET A 288 6857 7113 11799 -354 446 -434 C
ATOM 2192 SD MET A 288 30.018 80.423 178.128 1.00 73.60 S
ANISOU 2192 SD MET A 288 7661 7832 12473 -327 641 -597 S
ATOM 2193 CE MET A 288 28.318 80.383 177.566 1.00 69.43 C
ANISOU 2193 CE MET A 288 7383 7390 11609 -392 527 -602 C
ATOM 2194 N LEU A 289 27.137 84.048 181.213 1.00 57.26 N
ANISOU 2194 N LEU A 289 5721 5796 10238 -386 -55 -225 N
ATOM 2195 CA LEU A 289 26.155 85.022 180.732 1.00 56.32 C
ANISOU 2195 CA LEU A 289 5691 5708 10000 -432 -81 -146 C
ATOM 2196 C LEU A 289 25.882 86.182 181.709 1.00 60.00 C
ANISOU 2196 C LEU A 289 6146 6114 10538 -433 -178 -91 C
ATOM 2197 O LEU A 289 25.423 87.233 181.257 1.00 60.00 O
ANISOU 2197 O LEU A 289 6175 6108 10515 -472 -178 -9 O
ATOM 2198 CB LEU A 289 24.836 84.332 180.360 1.00 55.68 C
ANISOU 2198 CB LEU A 289 5711 5660 9786 -428 -128 -154 C
ATOM 2199 CG LEU A 289 24.878 83.365 179.171 1.00 61.08 C
ANISOU 2199 CG LEU A 289 6460 6399 10348 -457 -41 -222 C
ATOM 2200 CD1 LEU A 289 23.536 82.712 178.969 1.00 61.09 C
ANISOU 2200 CD1 LEU A 289 6545 6413 10254 -467 -137 -231 C
ATOM 2201 CD2 LEU A 289 25.326 84.053 177.882 1.00 64.31 C
ANISOU 2201 CD2 LEU A 289 6924 6875 10636 -535 69 -176 C
ATOM 2202 N ASP A 290 26.186 86.024 183.021 1.00 56.21 N
ANISOU 2202 N ASP A 290 5635 5580 10142 -396 -261 -135 N
ATOM 2203 CA ASP A 290 26.025 87.118 183.991 1.00 55.89 C
ANISOU 2203 CA ASP A 290 5615 5472 10148 -409 -336 -123 C
ATOM 2204 C ASP A 290 26.976 88.300 183.662 1.00 60.68 C
ANISOU 2204 C ASP A 290 6149 6041 10867 -472 -313 -88 C
ATOM 2205 O ASP A 290 26.525 89.431 183.831 1.00 61.03 O
ANISOU 2205 O ASP A 290 6228 6023 10938 -497 -329 -56 O
ATOM 2206 CB ASP A 290 26.194 86.654 185.442 1.00 57.62 C
ANISOU 2206 CB ASP A 290 5861 5656 10376 -377 -439 -181 C
ATOM 2207 CG ASP A 290 24.983 85.941 186.016 1.00 69.45 C
ANISOU 2207 CG ASP A 290 7454 7159 11774 -328 -447 -190 C
ATOM 2208 OD1 ASP A 290 23.888 86.043 185.415 1.00 69.94 O
ANISOU 2208 OD1 ASP A 290 7544 7233 11795 -320 -392 -155 O
ATOM 2209 OD2 ASP A 290 25.129 85.270 187.058 1.00 77.14 O
ANISOU 2209 OD2 ASP A 290 8466 8122 12722 -305 -514 -215 O
ATOM 2210 N PRO A 291 28.213 88.117 183.095 1.00 57.16 N
ANISOU 2210 N PRO A 291 5591 5612 10514 -500 -251 -84 N
ATOM 2211 CA PRO A 291 29.023 89.285 182.698 1.00 57.93 C
ANISOU 2211 CA PRO A 291 5607 5662 10740 -573 -208 -27 C
ATOM 2212 C PRO A 291 28.298 90.233 181.727 1.00 61.76 C
ANISOU 2212 C PRO A 291 6160 6152 11155 -613 -135 76 C
ATOM 2213 O PRO A 291 28.528 91.440 181.785 1.00 62.42 O
ANISOU 2213 O PRO A 291 6213 6153 11349 -666 -145 131 O
ATOM 2214 CB PRO A 291 30.242 88.647 182.031 1.00 60.76 C
ANISOU 2214 CB PRO A 291 5833 6054 11200 -582 -93 -32 C
ATOM 2215 CG PRO A 291 30.356 87.329 182.664 1.00 64.40 C
ANISOU 2215 CG PRO A 291 6275 6530 11666 -511 -155 -109 C
ATOM 2216 CD PRO A 291 28.954 86.869 182.823 1.00 58.63 C
ANISOU 2216 CD PRO A 291 5701 5837 10739 -467 -197 -128 C
ATOM 2217 N VAL A 292 27.400 89.693 180.872 1.00 57.83 N
ANISOU 2217 N VAL A 292 5752 5735 10486 -594 -86 111 N
ATOM 2218 CA VAL A 292 26.580 90.455 179.914 1.00 57.88 C
ANISOU 2218 CA VAL A 292 5831 5754 10405 -632 -64 240 C
ATOM 2219 C VAL A 292 25.573 91.322 180.700 1.00 60.04 C
ANISOU 2219 C VAL A 292 6132 5927 10752 -605 -168 267 C
ATOM 2220 O VAL A 292 25.339 92.471 180.320 1.00 60.95 O
ANISOU 2220 O VAL A 292 6247 5975 10938 -641 -167 382 O
ATOM 2221 CB VAL A 292 25.866 89.539 178.873 1.00 61.92 C
ANISOU 2221 CB VAL A 292 6443 6379 10705 -633 -36 256 C
ATOM 2222 CG1 VAL A 292 25.210 90.360 177.765 1.00 62.70 C
ANISOU 2222 CG1 VAL A 292 6618 6502 10704 -695 -44 423 C
ATOM 2223 CG2 VAL A 292 26.828 88.515 178.272 1.00 62.39 C
ANISOU 2223 CG2 VAL A 292 6490 6514 10703 -643 100 173 C
ATOM 2224 N VAL A 293 25.006 90.774 181.802 1.00 53.83 N
ANISOU 2224 N VAL A 293 5372 5118 9964 -540 -237 166 N
ATOM 2225 CA VAL A 293 24.063 91.456 182.700 1.00 52.87 C
ANISOU 2225 CA VAL A 293 5282 4891 9914 -503 -285 153 C
ATOM 2226 C VAL A 293 24.755 92.690 183.307 1.00 58.56 C
ANISOU 2226 C VAL A 293 5976 5487 10789 -543 -293 129 C
ATOM 2227 O VAL A 293 24.185 93.783 183.273 1.00 58.91 O
ANISOU 2227 O VAL A 293 6024 5420 10940 -547 -285 188 O
ATOM 2228 CB VAL A 293 23.517 90.498 183.804 1.00 55.25 C
ANISOU 2228 CB VAL A 293 5632 5205 10156 -439 -317 44 C
ATOM 2229 CG1 VAL A 293 22.695 91.240 184.856 1.00 55.14 C
ANISOU 2229 CG1 VAL A 293 5666 5073 10213 -404 -312 2 C
ATOM 2230 CG2 VAL A 293 22.716 89.345 183.205 1.00 54.37 C
ANISOU 2230 CG2 VAL A 293 5537 5184 9935 -409 -317 70 C
ATOM 2231 N TYR A 294 25.992 92.518 183.822 1.00 55.92 N
ANISOU 2231 N TYR A 294 5599 5155 10495 -578 -322 47 N
ATOM 2232 CA TYR A 294 26.765 93.600 184.438 1.00 57.20 C
ANISOU 2232 CA TYR A 294 5729 5193 10812 -639 -363 5 C
ATOM 2233 C TYR A 294 27.149 94.680 183.421 1.00 63.17 C
ANISOU 2233 C TYR A 294 6414 5890 11700 -706 -299 137 C
ATOM 2234 O TYR A 294 27.139 95.860 183.772 1.00 63.95 O
ANISOU 2234 O TYR A 294 6513 5840 11946 -743 -317 134 O
ATOM 2235 CB TYR A 294 28.040 93.079 185.131 1.00 58.87 C
ANISOU 2235 CB TYR A 294 5880 5425 11061 -672 -448 -85 C
ATOM 2236 CG TYR A 294 27.897 91.792 185.919 1.00 60.02 C
ANISOU 2236 CG TYR A 294 6081 5651 11075 -613 -515 -166 C
ATOM 2237 CD1 TYR A 294 26.910 91.651 186.893 1.00 61.66 C
ANISOU 2237 CD1 TYR A 294 6426 5835 11165 -568 -545 -238 C
ATOM 2238 CD2 TYR A 294 28.810 90.755 185.766 1.00 60.73 C
ANISOU 2238 CD2 TYR A 294 6075 5817 11184 -605 -538 -165 C
ATOM 2239 CE1 TYR A 294 26.783 90.472 187.627 1.00 61.66 C
ANISOU 2239 CE1 TYR A 294 6484 5902 11041 -523 -600 -284 C
ATOM 2240 CE2 TYR A 294 28.695 89.574 186.494 1.00 61.16 C
ANISOU 2240 CE2 TYR A 294 6172 5922 11143 -551 -609 -214 C
ATOM 2241 CZ TYR A 294 27.681 89.438 187.428 1.00 68.87 C
ANISOU 2241 CZ TYR A 294 7303 6887 11978 -515 -647 -264 C
ATOM 2242 OH TYR A 294 27.581 88.281 188.161 1.00 71.92 O
ANISOU 2242 OH TYR A 294 7740 7318 12270 -471 -713 -286 O
ATOM 2243 N TYR A 295 27.478 94.281 182.170 1.00 60.10 N
ANISOU 2243 N TYR A 295 5978 5606 11250 -727 -213 250 N
ATOM 2244 CA TYR A 295 27.885 95.204 181.104 1.00 61.35 C
ANISOU 2244 CA TYR A 295 6088 5729 11495 -802 -128 408 C
ATOM 2245 C TYR A 295 26.807 96.249 180.784 1.00 66.07 C
ANISOU 2245 C TYR A 295 6738 6227 12139 -797 -143 533 C
ATOM 2246 O TYR A 295 27.147 97.416 180.585 1.00 67.26 O
ANISOU 2246 O TYR A 295 6844 6249 12464 -858 -122 624 O
ATOM 2247 CB TYR A 295 28.277 94.444 179.822 1.00 62.75 C
ANISOU 2247 CB TYR A 295 6260 6058 11525 -825 -5 491 C
ATOM 2248 CG TYR A 295 28.830 95.341 178.733 1.00 66.26 C
ANISOU 2248 CG TYR A 295 6670 6478 12028 -917 112 666 C
ATOM 2249 CD1 TYR A 295 30.173 95.714 178.723 1.00 69.38 C
ANISOU 2249 CD1 TYR A 295 6931 6822 12610 -988 197 672 C
ATOM 2250 CD2 TYR A 295 28.010 95.827 177.717 1.00 67.58 C
ANISOU 2250 CD2 TYR A 295 6932 6668 12078 -941 130 848 C
ATOM 2251 CE1 TYR A 295 30.684 96.554 177.732 1.00 71.49 C
ANISOU 2251 CE1 TYR A 295 7164 7059 12941 -1081 332 852 C
ATOM 2252 CE2 TYR A 295 28.510 96.667 176.722 1.00 70.32 C
ANISOU 2252 CE2 TYR A 295 7268 6992 12457 -1035 241 1039 C
ATOM 2253 CZ TYR A 295 29.849 97.023 176.730 1.00 77.14 C
ANISOU 2253 CZ TYR A 295 8004 7804 13501 -1105 361 1039 C
ATOM 2254 OH TYR A 295 30.341 97.844 175.746 1.00 77.93 O
ANISOU 2254 OH TYR A 295 8093 7877 13638 -1205 497 1244 O
ATOM 2255 N PHE A 296 25.529 95.834 180.718 1.00 62.02 N
ANISOU 2255 N PHE A 296 6300 5755 11512 -726 -181 552 N
ATOM 2256 CA PHE A 296 24.417 96.728 180.391 1.00 62.55 C
ANISOU 2256 CA PHE A 296 6383 5717 11664 -705 -210 692 C
ATOM 2257 C PHE A 296 23.719 97.286 181.644 1.00 67.81 C
ANISOU 2257 C PHE A 296 7058 6217 12492 -641 -239 573 C
ATOM 2258 O PHE A 296 22.721 97.997 181.508 1.00 68.28 O
ANISOU 2258 O PHE A 296 7105 6159 12680 -602 -248 673 O
ATOM 2259 CB PHE A 296 23.398 96.009 179.492 1.00 63.80 C
ANISOU 2259 CB PHE A 296 6593 6003 11645 -677 -249 804 C
ATOM 2260 CG PHE A 296 23.921 95.576 178.144 1.00 65.73 C
ANISOU 2260 CG PHE A 296 6881 6401 11691 -751 -206 922 C
ATOM 2261 CD1 PHE A 296 24.079 96.493 177.113 1.00 70.08 C
ANISOU 2261 CD1 PHE A 296 7444 6926 12258 -827 -184 1140 C
ATOM 2262 CD2 PHE A 296 24.209 94.241 177.888 1.00 66.89 C
ANISOU 2262 CD2 PHE A 296 7075 6712 11630 -748 -173 817 C
ATOM 2263 CE1 PHE A 296 24.545 96.089 175.859 1.00 72.15 C
ANISOU 2263 CE1 PHE A 296 7786 7339 12288 -908 -114 1243 C
ATOM 2264 CE2 PHE A 296 24.672 93.837 176.632 1.00 70.76 C
ANISOU 2264 CE2 PHE A 296 7635 7336 11916 -821 -96 895 C
ATOM 2265 CZ PHE A 296 24.837 94.764 175.626 1.00 70.71 C
ANISOU 2265 CZ PHE A 296 7662 7319 11886 -904 -60 1105 C
ATOM 2266 N SER A 297 24.250 96.999 182.851 1.00 65.19 N
ANISOU 2266 N SER A 297 6749 5863 12158 -634 -249 366 N
ATOM 2267 CA SER A 297 23.667 97.478 184.107 1.00 65.93 C
ANISOU 2267 CA SER A 297 6897 5808 12347 -588 -245 218 C
ATOM 2268 C SER A 297 23.855 98.980 184.279 1.00 74.25 C
ANISOU 2268 C SER A 297 7927 6636 13648 -630 -226 227 C
ATOM 2269 O SER A 297 22.906 99.677 184.647 1.00 75.50 O
ANISOU 2269 O SER A 297 8103 6634 13951 -574 -178 213 O
ATOM 2270 CB SER A 297 24.253 96.732 185.301 1.00 68.16 C
ANISOU 2270 CB SER A 297 7247 6145 12505 -591 -286 13 C
ATOM 2271 OG SER A 297 25.583 97.123 185.600 1.00 76.98 O
ANISOU 2271 OG SER A 297 8334 7223 13692 -682 -345 -53 O
ATOM 2272 N SER A 298 25.074 99.470 184.007 1.00 72.30 N
ANISOU 2272 N SER A 298 7627 6360 13484 -728 -249 251 N
ATOM 2273 CA SER A 298 25.435 100.876 184.132 1.00 74.46 C
ANISOU 2273 CA SER A 298 7867 6405 14017 -792 -240 260 C
ATOM 2274 C SER A 298 26.321 101.315 182.959 1.00 79.32 C
ANISOU 2274 C SER A 298 8379 7036 14725 -885 -221 464 C
ATOM 2275 O SER A 298 26.998 100.459 182.376 1.00 78.17 O
ANISOU 2275 O SER A 298 8196 7079 14427 -914 -210 515 O
ATOM 2276 CB SER A 298 26.158 101.111 185.458 1.00 79.76 C
ANISOU 2276 CB SER A 298 8598 6980 14725 -848 -302 10 C
ATOM 2277 OG SER A 298 27.446 100.515 185.475 1.00 90.98 O
ANISOU 2277 OG SER A 298 9963 8525 16083 -927 -380 -21 O
ATOM 2278 N PRO A 299 26.393 102.632 182.620 1.00 77.64 N
ANISOU 2278 N PRO A 299 8115 6612 14771 -937 -195 581 N
ATOM 2279 CA PRO A 299 27.298 103.049 181.535 1.00 78.65 C
ANISOU 2279 CA PRO A 299 8149 6753 14981 -1040 -152 790 C
ATOM 2280 C PRO A 299 28.769 103.022 181.972 1.00 83.33 C
ANISOU 2280 C PRO A 299 8663 7340 15657 -1147 -174 671 C
ATOM 2281 O PRO A 299 29.647 103.258 181.148 1.00 83.76 O
ANISOU 2281 O PRO A 299 8619 7413 15793 -1238 -107 828 O
ATOM 2282 CB PRO A 299 26.828 104.468 181.210 1.00 82.38 C
ANISOU 2282 CB PRO A 299 8593 6968 15738 -1056 -130 949 C
ATOM 2283 CG PRO A 299 26.256 104.973 182.478 1.00 87.05 C
ANISOU 2283 CG PRO A 299 9241 7356 16477 -1002 -159 716 C
ATOM 2284 CD PRO A 299 25.681 103.791 183.203 1.00 80.47 C
ANISOU 2284 CD PRO A 299 8498 6697 15380 -907 -182 528 C
ATOM 2285 N SER A 300 29.028 102.701 183.260 1.00 79.98 N
ANISOU 2285 N SER A 300 8282 6896 15212 -1143 -271 408 N
ATOM 2286 CA SER A 300 30.351 102.611 183.882 1.00 80.78 C
ANISOU 2286 CA SER A 300 8304 6983 15405 -1244 -359 276 C
ATOM 2287 C SER A 300 31.163 101.413 183.372 1.00 83.00 C
ANISOU 2287 C SER A 300 8491 7496 15548 -1247 -332 327 C
ATOM 2288 O SER A 300 32.394 101.492 183.335 1.00 83.96 O
ANISOU 2288 O SER A 300 8467 7598 15837 -1344 -353 336 O
ATOM 2289 CB SER A 300 30.215 102.526 185.398 1.00 84.98 C
ANISOU 2289 CB SER A 300 8957 7448 15885 -1236 -496 -5 C
ATOM 2290 OG SER A 300 29.662 103.723 185.922 1.00 97.07 O
ANISOU 2290 OG SER A 300 10569 8726 17587 -1250 -493 -93 O
ATOM 2291 N PHE A 301 30.487 100.310 182.995 1.00 76.95 N
ANISOU 2291 N PHE A 301 7794 6929 14514 -1144 -283 355 N
ATOM 2292 CA PHE A 301 31.146 99.105 182.481 1.00 75.77 C
ANISOU 2292 CA PHE A 301 7573 6981 14236 -1130 -230 384 C
ATOM 2293 C PHE A 301 31.718 99.338 181.062 1.00 79.82 C
ANISOU 2293 C PHE A 301 7989 7538 14802 -1193 -54 600 C
ATOM 2294 O PHE A 301 32.920 99.115 180.908 1.00 80.10 O
ANISOU 2294 O PHE A 301 7874 7594 14967 -1256 -4 606 O
ATOM 2295 CB PHE A 301 30.217 97.882 182.532 1.00 75.43 C
ANISOU 2295 CB PHE A 301 7645 7108 13907 -1013 -232 331 C
ATOM 2296 CG PHE A 301 30.225 97.203 183.880 1.00 75.95 C
ANISOU 2296 CG PHE A 301 7765 7190 13904 -972 -375 130 C
ATOM 2297 CD1 PHE A 301 29.504 97.729 184.948 1.00 79.02 C
ANISOU 2297 CD1 PHE A 301 8277 7463 14285 -952 -460 2 C
ATOM 2298 CD2 PHE A 301 30.976 96.054 184.092 1.00 77.37 C
ANISOU 2298 CD2 PHE A 301 7877 7489 14032 -957 -413 73 C
ATOM 2299 CE1 PHE A 301 29.525 97.109 186.199 1.00 79.55 C
ANISOU 2299 CE1 PHE A 301 8431 7556 14241 -931 -585 -170 C
ATOM 2300 CE2 PHE A 301 30.997 95.434 185.343 1.00 79.74 C
ANISOU 2300 CE2 PHE A 301 8239 7802 14256 -929 -567 -77 C
ATOM 2301 CZ PHE A 301 30.275 95.968 186.388 1.00 77.98 C
ANISOU 2301 CZ PHE A 301 8169 7485 13975 -923 -654 -194 C
ATOM 2302 N PRO A 302 30.963 99.845 180.039 1.00 76.14 N
ANISOU 2302 N PRO A 302 7596 7073 14262 -1189 42 792 N
ATOM 2303 CA PRO A 302 31.601 100.112 178.734 1.00 77.46 C
ANISOU 2303 CA PRO A 302 7702 7283 14447 -1271 221 1005 C
ATOM 2304 C PRO A 302 32.637 101.233 178.819 1.00 83.38 C
ANISOU 2304 C PRO A 302 8298 7846 15537 -1393 251 1070 C
ATOM 2305 O PRO A 302 33.573 101.248 178.022 1.00 84.54 O
ANISOU 2305 O PRO A 302 8338 8030 15753 -1473 418 1194 O
ATOM 2306 CB PRO A 302 30.429 100.519 177.833 1.00 79.36 C
ANISOU 2306 CB PRO A 302 8080 7541 14532 -1247 243 1203 C
ATOM 2307 CG PRO A 302 29.205 100.102 178.552 1.00 81.75 C
ANISOU 2307 CG PRO A 302 8486 7858 14719 -1133 102 1077 C
ATOM 2308 CD PRO A 302 29.530 100.200 179.997 1.00 76.76 C
ANISOU 2308 CD PRO A 302 7805 7109 14250 -1118 -7 844 C
ATOM 2309 N ASN A 303 32.475 102.158 179.799 1.00 80.51 N
ANISOU 2309 N ASN A 303 7926 7271 15395 -1414 104 973 N
ATOM 2310 CA ASN A 303 33.387 103.281 180.045 1.00 82.70 C
ANISOU 2310 CA ASN A 303 8062 7330 16031 -1542 89 1000 C
ATOM 2311 C ASN A 303 34.733 102.801 180.594 1.00 86.49 C
ANISOU 2311 C ASN A 303 8364 7830 16670 -1608 43 872 C
ATOM 2312 O ASN A 303 35.741 103.463 180.356 1.00 88.46 O
ANISOU 2312 O ASN A 303 8440 7958 17213 -1730 97 959 O
ATOM 2313 CB ASN A 303 32.771 104.317 180.996 1.00 84.41 C
ANISOU 2313 CB ASN A 303 8349 7304 16419 -1543 -59 884 C
ATOM 2314 CG ASN A 303 31.800 105.286 180.350 1.00107.83 C
ANISOU 2314 CG ASN A 303 11392 10137 19442 -1522 1 1080 C
ATOM 2315 OD1 ASN A 303 31.726 105.431 179.121 1.00104.38 O
ANISOU 2315 OD1 ASN A 303 10949 9763 18949 -1544 133 1349 O
ATOM 2316 ND2 ASN A 303 31.020 105.970 181.175 1.00 98.10 N
ANISOU 2316 ND2 ASN A 303 10241 8709 18323 -1480 -94 953 N
ATOM 2317 N PHE A 304 34.748 101.660 181.320 1.00 80.48 N
ANISOU 2317 N PHE A 304 7628 7206 15744 -1530 -64 686 N
ATOM 2318 CA PHE A 304 35.965 101.057 181.869 1.00 80.53 C
ANISOU 2318 CA PHE A 304 7454 7239 15905 -1575 -145 583 C
ATOM 2319 C PHE A 304 36.840 100.536 180.731 1.00 85.62 C
ANISOU 2319 C PHE A 304 7930 7997 16607 -1598 98 739 C
ATOM 2320 O PHE A 304 38.037 100.820 180.708 1.00 87.40 O
ANISOU 2320 O PHE A 304 7922 8135 17150 -1699 125 780 O
ATOM 2321 CB PHE A 304 35.626 99.925 182.864 1.00 80.05 C
ANISOU 2321 CB PHE A 304 7487 7298 15629 -1475 -316 386 C
ATOM 2322 CG PHE A 304 36.801 99.078 183.305 1.00 81.88 C
ANISOU 2322 CG PHE A 304 7527 7582 16000 -1495 -406 321 C
ATOM 2323 CD1 PHE A 304 37.604 99.472 184.368 1.00 86.08 C
ANISOU 2323 CD1 PHE A 304 7955 7982 16770 -1594 -655 211 C
ATOM 2324 CD2 PHE A 304 37.101 97.882 182.659 1.00 83.11 C
ANISOU 2324 CD2 PHE A 304 7605 7907 16066 -1419 -255 369 C
ATOM 2325 CE1 PHE A 304 38.692 98.692 184.772 1.00 87.78 C
ANISOU 2325 CE1 PHE A 304 7964 8235 17155 -1612 -774 182 C
ATOM 2326 CE2 PHE A 304 38.189 97.103 183.062 1.00 86.61 C
ANISOU 2326 CE2 PHE A 304 7837 8370 16700 -1424 -335 326 C
ATOM 2327 CZ PHE A 304 38.977 97.514 184.116 1.00 86.18 C
ANISOU 2327 CZ PHE A 304 7656 8185 16903 -1519 -607 248 C
ATOM 2328 N PHE A 305 36.242 99.770 179.796 1.00 81.28 N
ANISOU 2328 N PHE A 305 7498 7631 15756 -1511 280 818 N
ATOM 2329 CA PHE A 305 36.948 99.193 178.653 1.00 82.64 C
ANISOU 2329 CA PHE A 305 7568 7921 15909 -1525 559 939 C
ATOM 2330 C PHE A 305 37.304 100.265 177.618 1.00 90.41 C
ANISOU 2330 C PHE A 305 8503 8822 17027 -1642 771 1173 C
ATOM 2331 O PHE A 305 38.247 100.058 176.855 1.00 92.21 O
ANISOU 2331 O PHE A 305 8583 9087 17364 -1695 1019 1269 O
ATOM 2332 CB PHE A 305 36.141 98.050 178.015 1.00 82.66 C
ANISOU 2332 CB PHE A 305 7755 8135 15516 -1413 666 919 C
ATOM 2333 CG PHE A 305 35.841 96.914 178.968 1.00 82.06 C
ANISOU 2333 CG PHE A 305 7715 8136 15329 -1302 488 716 C
ATOM 2334 CD1 PHE A 305 36.846 96.048 179.385 1.00 85.48 C
ANISOU 2334 CD1 PHE A 305 7959 8588 15932 -1281 482 620 C
ATOM 2335 CD2 PHE A 305 34.554 96.715 179.454 1.00 82.02 C
ANISOU 2335 CD2 PHE A 305 7917 8169 15078 -1220 330 639 C
ATOM 2336 CE1 PHE A 305 36.571 95.011 180.281 1.00 84.73 C
ANISOU 2336 CE1 PHE A 305 7903 8551 15741 -1183 304 464 C
ATOM 2337 CE2 PHE A 305 34.279 95.675 180.348 1.00 83.04 C
ANISOU 2337 CE2 PHE A 305 8085 8362 15105 -1127 181 473 C
ATOM 2338 CZ PHE A 305 35.289 94.831 180.755 1.00 81.67 C
ANISOU 2338 CZ PHE A 305 7744 8209 15079 -1112 162 393 C
ATOM 2339 N SER A 306 36.588 101.415 177.610 1.00 88.05 N
ANISOU 2339 N SER A 306 8315 8392 16749 -1682 690 1271 N
ATOM 2340 CA SER A 306 36.888 102.535 176.712 1.00 90.96 C
ANISOU 2340 CA SER A 306 8641 8648 17273 -1801 862 1522 C
ATOM 2341 C SER A 306 38.150 103.257 177.206 1.00 98.11 C
ANISOU 2341 C SER A 306 9273 9352 18651 -1929 838 1515 C
ATOM 2342 O SER A 306 39.019 103.586 176.398 1.00100.36 O
ANISOU 2342 O SER A 306 9409 9607 19114 -2030 1077 1694 O
ATOM 2343 CB SER A 306 35.704 103.495 176.610 1.00 94.51 C
ANISOU 2343 CB SER A 306 9273 8991 17647 -1790 759 1634 C
ATOM 2344 OG SER A 306 35.596 104.353 177.734 1.00103.77 O
ANISOU 2344 OG SER A 306 10402 9933 19094 -1813 537 1508 O
ATOM 2345 N THR A 307 38.258 103.454 178.544 1.00 94.64 N
ANISOU 2345 N THR A 307 8774 8780 18405 -1933 549 1304 N
ATOM 2346 CA THR A 307 39.394 104.065 179.252 1.00 96.87 C
ANISOU 2346 CA THR A 307 8806 8864 19136 -2063 427 1245 C
ATOM 2347 C THR A 307 40.637 103.155 179.107 1.00103.20 C
ANISOU 2347 C THR A 307 9347 9763 20102 -2079 537 1233 C
ATOM 2348 O THR A 307 41.765 103.652 179.086 1.00105.21 O
ANISOU 2348 O THR A 307 9330 9878 20768 -2208 577 1303 O
ATOM 2349 CB THR A 307 39.010 104.313 180.733 1.00101.86 C
ANISOU 2349 CB THR A 307 9524 9373 19806 -2053 70 989 C
ATOM 2350 OG1 THR A 307 37.833 105.121 180.784 1.00 97.67 O
ANISOU 2350 OG1 THR A 307 9217 8739 19154 -2020 29 1001 O
ATOM 2351 CG2 THR A 307 40.114 104.997 181.539 1.00104.31 C
ANISOU 2351 CG2 THR A 307 9610 9465 20557 -2210 -123 905 C
ATOM 2352 N LEU A 308 40.413 101.829 178.990 1.00 99.50 N
ANISOU 2352 N LEU A 308 8944 9513 19346 -1947 594 1151 N
ATOM 2353 CA LEU A 308 41.452 100.813 178.826 1.00100.95 C
ANISOU 2353 CA LEU A 308 8895 9789 19674 -1925 722 1129 C
ATOM 2354 C LEU A 308 42.165 100.965 177.475 1.00109.52 C
ANISOU 2354 C LEU A 308 9843 10896 20873 -1991 1141 1346 C
ATOM 2355 O LEU A 308 43.379 100.765 177.415 1.00111.81 O
ANISOU 2355 O LEU A 308 9820 11132 21531 -2045 1257 1374 O
ATOM 2356 CB LEU A 308 40.844 99.408 178.963 1.00 98.29 C
ANISOU 2356 CB LEU A 308 8710 9659 18978 -1761 698 991 C
ATOM 2357 CG LEU A 308 41.776 98.286 179.434 1.00103.49 C
ANISOU 2357 CG LEU A 308 9133 10359 19831 -1709 653 887 C
ATOM 2358 CD1 LEU A 308 42.093 98.408 180.923 1.00103.72 C
ANISOU 2358 CD1 LEU A 308 9067 10273 20071 -1743 230 744 C
ATOM 2359 CD2 LEU A 308 41.153 96.926 179.171 1.00103.56 C
ANISOU 2359 CD2 LEU A 308 9304 10563 19480 -1553 744 801 C
ATOM 2360 N ILE A 309 41.426 101.340 176.406 1.00107.14 N
ANISOU 2360 N ILE A 309 9770 10666 20271 -1994 1365 1510 N
ATOM 2361 CA ILE A 309 42.023 101.541 175.078 1.00110.27 C
ANISOU 2361 CA ILE A 309 10101 11096 20701 -2073 1785 1733 C
ATOM 2362 C ILE A 309 42.505 103.007 174.957 1.00118.05 C
ANISOU 2362 C ILE A 309 10946 11853 22053 -2240 1809 1927 C
ATOM 2363 O ILE A 309 43.375 103.292 174.129 1.00120.85 O
ANISOU 2363 O ILE A 309 11134 12173 22611 -2341 2139 2110 O
ATOM 2364 CB ILE A 309 41.124 101.108 173.876 1.00112.69 C
ANISOU 2364 CB ILE A 309 10733 11611 20473 -2016 2027 1835 C
ATOM 2365 CG1 ILE A 309 40.172 99.911 174.210 1.00109.61 C
ANISOU 2365 CG1 ILE A 309 10560 11402 19684 -1854 1870 1629 C
ATOM 2366 CG2 ILE A 309 41.981 100.818 172.629 1.00116.60 C
ANISOU 2366 CG2 ILE A 309 11151 12189 20964 -2075 2506 1981 C
ATOM 2367 CD1 ILE A 309 40.816 98.488 174.547 1.00115.36 C
ANISOU 2367 CD1 ILE A 309 11136 12225 20472 -1753 1926 1425 C
ATOM 2368 N ASN A 310 41.979 103.920 175.814 1.00114.60 N
ANISOU 2368 N ASN A 310 10569 11245 21730 -2274 1478 1876 N
ATOM 2369 CA ASN A 310 42.416 105.324 175.892 1.00117.45 C
ANISOU 2369 CA ASN A 310 10790 11342 22492 -2435 1443 2018 C
ATOM 2370 C ASN A 310 43.865 105.355 176.392 1.00124.76 C
ANISOU 2370 C ASN A 310 11318 12131 23952 -2542 1421 1971 C
ATOM 2371 O ASN A 310 44.642 106.235 176.023 1.00127.59 O
ANISOU 2371 O ASN A 310 11467 12313 24697 -2695 1563 2150 O
ATOM 2372 CB ASN A 310 41.501 106.136 176.822 1.00117.22 C
ANISOU 2372 CB ASN A 310 10926 11151 22462 -2427 1089 1905 C
ATOM 2373 CG ASN A 310 40.292 106.770 176.168 1.00142.01 C
ANISOU 2373 CG ASN A 310 14349 14285 25322 -2393 1140 2075 C
ATOM 2374 OD1 ASN A 310 39.665 106.216 175.255 1.00136.60 O
ANISOU 2374 OD1 ASN A 310 13857 13808 24237 -2315 1317 2191 O
ATOM 2375 ND2 ASN A 310 39.908 107.939 176.661 1.00134.09 N
ANISOU 2375 ND2 ASN A 310 13380 13031 24537 -2452 961 2083 N
ATOM 2376 N ARG A 311 44.205 104.355 177.227 1.00120.81 N
ANISOU 2376 N ARG A 311 10707 11711 23483 -2461 1231 1746 N
ATOM 2377 CA ARG A 311 45.512 104.054 177.804 1.00123.06 C
ANISOU 2377 CA ARG A 311 10608 11908 24243 -2526 1145 1677 C
ATOM 2378 C ARG A 311 46.419 103.476 176.700 1.00129.67 C
ANISOU 2378 C ARG A 311 11220 12836 25215 -2528 1609 1837 C
ATOM 2379 O ARG A 311 47.621 103.749 176.684 1.00132.65 O
ANISOU 2379 O ARG A 311 11220 13070 26112 -2643 1698 1920 O
ATOM 2380 CB ARG A 311 45.305 103.051 178.962 1.00121.55 C
ANISOU 2380 CB ARG A 311 10457 11809 23917 -2408 791 1414 C
ATOM 2381 CG ARG A 311 46.552 102.448 179.598 1.00136.02 C
ANISOU 2381 CG ARG A 311 11908 13591 26184 -2437 650 1343 C
ATOM 2382 CD ARG A 311 46.190 101.136 180.270 1.00145.93 C
ANISOU 2382 CD ARG A 311 13267 15015 27166 -2274 454 1157 C
ATOM 2383 NE ARG A 311 47.288 100.588 181.068 1.00158.65 N
ANISOU 2383 NE ARG A 311 14529 16558 29192 -2299 215 1094 N
ATOM 2384 CZ ARG A 311 47.233 99.432 181.724 1.00172.43 C
ANISOU 2384 CZ ARG A 311 16285 18415 30817 -2175 18 967 C
ATOM 2385 NH1 ARG A 311 48.276 99.012 182.427 1.00163.18 N
ANISOU 2385 NH1 ARG A 311 14772 17161 30069 -2210 -226 949 N
ATOM 2386 NH2 ARG A 311 46.135 98.685 181.680 1.00154.60 N
ANISOU 2386 NH2 ARG A 311 14365 16338 28037 -2021 51 875 N
ATOM 2387 N CYS A 312 45.824 102.693 175.773 1.00124.99 N
ANISOU 2387 N CYS A 312 10862 12469 24158 -2408 1911 1873 N
ATOM 2388 CA CYS A 312 46.497 102.058 174.639 1.00157.99 C
ANISOU 2388 CA CYS A 312 14925 16760 28344 -2394 2407 1989 C
ATOM 2389 C CYS A 312 46.573 103.033 173.463 1.00184.08 C
ANISOU 2389 C CYS A 312 18293 20018 31630 -2525 2775 2275 C
ATOM 2390 O CYS A 312 47.134 104.120 173.591 1.00145.76 O
ANISOU 2390 O CYS A 312 13237 14951 27195 -2678 2743 2413 O
ATOM 2391 CB CYS A 312 45.775 100.770 174.248 1.00155.81 C
ANISOU 2391 CB CYS A 312 14917 16736 27549 -2221 2525 1863 C
ATOM 2392 SG CYS A 312 46.545 99.866 172.879 1.00162.65 S
ANISOU 2392 SG CYS A 312 15695 17738 28367 -2192 3163 1939 S
ATOM 2393 N ALA A1001 8.893 107.001 172.921 1.00 85.39 N
ANISOU 2393 N ALA A1001 8480 4766 19200 1132 196 1662 N
ATOM 2394 CA ALA A1001 7.918 107.360 171.890 1.00 83.95 C
ANISOU 2394 CA ALA A1001 8420 4699 18778 1015 313 1317 C
ATOM 2395 C ALA A1001 7.365 108.762 172.115 1.00 86.29 C
ANISOU 2395 C ALA A1001 8945 5351 18490 962 263 1395 C
ATOM 2396 O ALA A1001 7.100 109.459 171.141 1.00 85.05 O
ANISOU 2396 O ALA A1001 8868 5361 18085 866 295 1132 O
ATOM 2397 CB ALA A1001 6.782 106.353 171.864 1.00 86.24 C
ANISOU 2397 CB ALA A1001 8626 4734 19407 974 355 1347 C
ATOM 2398 N ASP A1002 7.204 109.178 173.390 1.00 83.21 N
ANISOU 2398 N ASP A1002 8656 5070 17889 1003 194 1753 N
ATOM 2399 CA ASP A1002 6.708 110.508 173.760 1.00 81.09 C
ANISOU 2399 CA ASP A1002 8569 5079 17163 953 203 1793 C
ATOM 2400 C ASP A1002 7.750 111.593 173.449 1.00 84.63 C
ANISOU 2400 C ASP A1002 9044 5736 17374 966 133 1639 C
ATOM 2401 O ASP A1002 7.369 112.695 173.051 1.00 82.46 O
ANISOU 2401 O ASP A1002 8832 5635 16865 902 167 1523 O
ATOM 2402 CB ASP A1002 6.312 110.551 175.246 1.00 83.95 C
ANISOU 2402 CB ASP A1002 9066 5493 17337 961 217 2149 C
ATOM 2403 CG ASP A1002 5.002 109.859 175.587 1.00 94.94 C
ANISOU 2403 CG ASP A1002 10445 6713 18916 927 375 2328 C
ATOM 2404 OD1 ASP A1002 4.303 109.401 174.652 1.00 95.11 O
ANISOU 2404 OD1 ASP A1002 10332 6557 19247 893 419 2159 O
ATOM 2405 OD2 ASP A1002 4.667 109.788 176.787 1.00103.28 O
ANISOU 2405 OD2 ASP A1002 11632 7812 19796 914 458 2634 O
ATOM 2406 N LEU A1003 9.055 111.278 173.628 1.00 83.53 N
ANISOU 2406 N LEU A1003 8807 5533 17397 1046 29 1671 N
ATOM 2407 CA LEU A1003 10.175 112.180 173.332 1.00 83.12 C
ANISOU 2407 CA LEU A1003 8714 5606 17260 1071 -31 1543 C
ATOM 2408 C LEU A1003 10.308 112.375 171.823 1.00 87.34 C
ANISOU 2408 C LEU A1003 9187 6158 17839 1021 136 1210 C
ATOM 2409 O LEU A1003 10.459 113.507 171.364 1.00 85.75 O
ANISOU 2409 O LEU A1003 9024 6149 17410 980 159 1115 O
ATOM 2410 CB LEU A1003 11.500 111.638 173.911 1.00 85.62 C
ANISOU 2410 CB LEU A1003 8874 5766 17894 1163 -205 1706 C
ATOM 2411 CG LEU A1003 11.736 111.785 175.417 1.00 91.98 C
ANISOU 2411 CG LEU A1003 9788 6657 18503 1166 -478 2062 C
ATOM 2412 CD1 LEU A1003 12.673 110.704 175.926 1.00 95.64 C
ANISOU 2412 CD1 LEU A1003 10042 6859 19436 1231 -697 2348 C
ATOM 2413 CD2 LEU A1003 12.310 113.149 175.757 1.00 93.41 C
ANISOU 2413 CD2 LEU A1003 10052 7064 18377 1141 -616 1989 C
ATOM 2414 N GLU A1004 10.234 111.265 171.061 1.00 86.46 N
ANISOU 2414 N GLU A1004 8988 5846 18015 1004 263 1032 N
ATOM 2415 CA GLU A1004 10.333 111.225 169.602 1.00 87.52 C
ANISOU 2415 CA GLU A1004 9127 6011 18116 905 452 669 C
ATOM 2416 C GLU A1004 9.145 111.917 168.930 1.00 91.10 C
ANISOU 2416 C GLU A1004 9750 6688 18175 752 423 613 C
ATOM 2417 O GLU A1004 9.339 112.551 167.895 1.00 90.85 O
ANISOU 2417 O GLU A1004 9785 6838 17895 645 498 444 O
ATOM 2418 CB GLU A1004 10.448 109.776 169.105 1.00 91.92 C
ANISOU 2418 CB GLU A1004 9557 6261 19106 899 601 440 C
ATOM 2419 CG GLU A1004 11.860 109.219 169.193 1.00105.97 C
ANISOU 2419 CG GLU A1004 11092 7781 21390 1012 717 383 C
ATOM 2420 CD GLU A1004 12.015 107.711 169.107 1.00137.00 C
ANISOU 2420 CD GLU A1004 14796 11291 25965 1045 844 249 C
ATOM 2421 OE1 GLU A1004 11.107 107.034 168.571 1.00131.71 O
ANISOU 2421 OE1 GLU A1004 14187 10545 25313 945 920 26 O
ATOM 2422 OE2 GLU A1004 13.067 107.207 169.563 1.00138.97 O
ANISOU 2422 OE2 GLU A1004 14767 11248 26786 1165 850 370 O
ATOM 2423 N ASP A1005 7.928 111.801 169.509 1.00 87.79 N
ANISOU 2423 N ASP A1005 9379 6238 17740 729 317 793 N
ATOM 2424 CA ASP A1005 6.723 112.435 168.966 1.00 87.31 C
ANISOU 2424 CA ASP A1005 9401 6310 17463 584 240 807 C
ATOM 2425 C ASP A1005 6.760 113.948 169.165 1.00 89.51 C
ANISOU 2425 C ASP A1005 9703 6806 17500 576 193 955 C
ATOM 2426 O ASP A1005 6.329 114.673 168.269 1.00 89.32 O
ANISOU 2426 O ASP A1005 9704 6928 17306 438 132 937 O
ATOM 2427 CB ASP A1005 5.442 111.842 169.580 1.00 89.81 C
ANISOU 2427 CB ASP A1005 9690 6447 17987 575 193 968 C
ATOM 2428 CG ASP A1005 5.033 110.481 169.028 1.00105.50 C
ANISOU 2428 CG ASP A1005 11622 8201 20264 517 198 783 C
ATOM 2429 OD1 ASP A1005 5.894 109.795 168.426 1.00108.06 O
ANISOU 2429 OD1 ASP A1005 11922 8454 20682 519 287 512 O
ATOM 2430 OD2 ASP A1005 3.865 110.083 169.236 1.00112.69 O
ANISOU 2430 OD2 ASP A1005 12481 8954 21381 472 142 890 O
ATOM 2431 N ASN A1006 7.282 114.425 170.321 1.00 85.32 N
ANISOU 2431 N ASN A1006 9157 6289 16970 700 196 1106 N
ATOM 2432 CA ASN A1006 7.416 115.858 170.622 1.00 84.23 C
ANISOU 2432 CA ASN A1006 9009 6306 16689 698 173 1184 C
ATOM 2433 C ASN A1006 8.426 116.498 169.667 1.00 89.35 C
ANISOU 2433 C ASN A1006 9607 7085 17257 675 192 1073 C
ATOM 2434 O ASN A1006 8.186 117.594 169.164 1.00 88.33 O
ANISOU 2434 O ASN A1006 9438 7079 17046 595 170 1128 O
ATOM 2435 CB ASN A1006 7.828 116.089 172.082 1.00 84.03 C
ANISOU 2435 CB ASN A1006 9022 6273 16633 799 152 1296 C
ATOM 2436 CG ASN A1006 6.684 116.082 173.068 1.00100.98 C
ANISOU 2436 CG ASN A1006 11246 8367 18754 775 224 1426 C
ATOM 2437 OD1 ASN A1006 5.583 116.578 172.801 1.00 89.14 O
ANISOU 2437 OD1 ASN A1006 9704 6839 17326 694 296 1445 O
ATOM 2438 ND2 ASN A1006 6.937 115.559 174.257 1.00 95.92 N
ANISOU 2438 ND2 ASN A1006 10710 7704 18031 829 213 1548 N
ATOM 2439 N TRP A1007 9.532 115.781 169.397 1.00 88.18 N
ANISOU 2439 N TRP A1007 9426 6873 17206 740 261 943 N
ATOM 2440 CA TRP A1007 10.602 116.160 168.477 1.00 89.32 C
ANISOU 2440 CA TRP A1007 9510 7092 17336 723 381 816 C
ATOM 2441 C TRP A1007 10.074 116.154 167.033 1.00 94.53 C
ANISOU 2441 C TRP A1007 10273 7895 17748 535 463 695 C
ATOM 2442 O TRP A1007 10.460 117.018 166.244 1.00 94.56 O
ANISOU 2442 O TRP A1007 10272 8066 17588 453 531 717 O
ATOM 2443 CB TRP A1007 11.786 115.187 168.652 1.00 90.09 C
ANISOU 2443 CB TRP A1007 9498 6988 17742 839 480 700 C
ATOM 2444 CG TRP A1007 12.759 115.128 167.511 1.00 93.31 C
ANISOU 2444 CG TRP A1007 9844 7395 18214 799 741 482 C
ATOM 2445 CD1 TRP A1007 12.737 114.259 166.459 1.00 98.72 C
ANISOU 2445 CD1 TRP A1007 10596 8041 18874 695 978 197 C
ATOM 2446 CD2 TRP A1007 13.935 115.932 167.342 1.00 93.81 C
ANISOU 2446 CD2 TRP A1007 9759 7472 18412 852 844 500 C
ATOM 2447 NE1 TRP A1007 13.807 114.493 165.628 1.00100.46 N
ANISOU 2447 NE1 TRP A1007 10750 8273 19147 668 1279 28 N
ATOM 2448 CE2 TRP A1007 14.565 115.508 166.151 1.00100.64 C
ANISOU 2448 CE2 TRP A1007 10616 8311 19310 776 1202 240 C
ATOM 2449 CE3 TRP A1007 14.515 116.979 168.079 1.00 93.94 C
ANISOU 2449 CE3 TRP A1007 9643 7504 18546 942 684 683 C
ATOM 2450 CZ2 TRP A1007 15.750 116.090 165.682 1.00101.62 C
ANISOU 2450 CZ2 TRP A1007 10583 8410 19617 803 1443 208 C
ATOM 2451 CZ3 TRP A1007 15.689 117.554 167.614 1.00 96.96 C
ANISOU 2451 CZ3 TRP A1007 9843 7843 19152 974 854 654 C
ATOM 2452 CH2 TRP A1007 16.293 117.111 166.429 1.00100.34 C
ANISOU 2452 CH2 TRP A1007 10247 8234 19645 912 1247 443 C
ATOM 2453 N GLU A1008 9.198 115.177 166.697 1.00 92.39 N
ANISOU 2453 N GLU A1008 10097 7559 17447 445 433 586 N
ATOM 2454 CA GLU A1008 8.590 115.015 165.373 1.00 94.39 C
ANISOU 2454 CA GLU A1008 10496 7957 17411 217 425 446 C
ATOM 2455 C GLU A1008 7.720 116.218 165.035 1.00 98.04 C
ANISOU 2455 C GLU A1008 10972 8611 17669 79 215 718 C
ATOM 2456 O GLU A1008 7.912 116.814 163.980 1.00 99.33 O
ANISOU 2456 O GLU A1008 11215 8999 17528 -87 224 742 O
ATOM 2457 CB GLU A1008 7.762 113.719 165.301 1.00 97.17 C
ANISOU 2457 CB GLU A1008 10899 8135 17885 158 369 275 C
ATOM 2458 CG GLU A1008 7.593 113.165 163.897 1.00111.79 C
ANISOU 2458 CG GLU A1008 12931 10099 19448 -87 416 -49 C
ATOM 2459 CD GLU A1008 8.771 112.356 163.392 1.00135.55 C
ANISOU 2459 CD GLU A1008 15957 13019 22527 -71 775 -450 C
ATOM 2460 OE1 GLU A1008 9.539 112.882 162.555 1.00134.56 O
ANISOU 2460 OE1 GLU A1008 15932 13101 22095 -170 985 -562 O
ATOM 2461 OE2 GLU A1008 8.929 111.197 163.839 1.00128.11 O
ANISOU 2461 OE2 GLU A1008 14899 11767 22010 37 878 -635 O
ATOM 2462 N THR A1009 6.798 116.596 165.948 1.00 93.11 N
ANISOU 2462 N THR A1009 10249 7881 17250 140 57 945 N
ATOM 2463 CA THR A1009 5.882 117.735 165.800 1.00 92.75 C
ANISOU 2463 CA THR A1009 10114 7902 17224 31 -129 1228 C
ATOM 2464 C THR A1009 6.651 119.060 165.738 1.00 95.75 C
ANISOU 2464 C THR A1009 10390 8409 17582 62 -75 1374 C
ATOM 2465 O THR A1009 6.207 119.989 165.066 1.00 96.50 O
ANISOU 2465 O THR A1009 10413 8611 17643 -87 -216 1610 O
ATOM 2466 CB THR A1009 4.850 117.764 166.937 1.00101.10 C
ANISOU 2466 CB THR A1009 11056 8744 18614 113 -173 1366 C
ATOM 2467 OG1 THR A1009 5.524 117.782 168.196 1.00101.20 O
ANISOU 2467 OG1 THR A1009 11050 8678 18724 316 -11 1324 O
ATOM 2468 CG2 THR A1009 3.868 116.595 166.875 1.00 99.86 C
ANISOU 2468 CG2 THR A1009 10939 8427 18577 52 -257 1304 C
ATOM 2469 N LEU A1010 7.806 119.132 166.428 1.00 90.92 N
ANISOU 2469 N LEU A1010 9736 7757 17051 243 94 1268 N
ATOM 2470 CA LEU A1010 8.692 120.295 166.468 1.00 90.18 C
ANISOU 2470 CA LEU A1010 9507 7727 17030 296 156 1362 C
ATOM 2471 C LEU A1010 9.330 120.543 165.099 1.00 96.06 C
ANISOU 2471 C LEU A1010 10302 8671 17526 159 251 1382 C
ATOM 2472 O LEU A1010 9.319 121.677 164.627 1.00 96.15 O
ANISOU 2472 O LEU A1010 10199 8781 17554 74 204 1625 O
ATOM 2473 CB LEU A1010 9.780 120.078 167.532 1.00 89.26 C
ANISOU 2473 CB LEU A1010 9340 7491 17082 501 246 1225 C
ATOM 2474 CG LEU A1010 9.988 121.196 168.546 1.00 93.18 C
ANISOU 2474 CG LEU A1010 9687 7925 17792 590 191 1298 C
ATOM 2475 CD1 LEU A1010 8.971 121.114 169.676 1.00 92.48 C
ANISOU 2475 CD1 LEU A1010 9645 7737 17756 612 136 1306 C
ATOM 2476 CD2 LEU A1010 11.382 121.122 169.135 1.00 96.18 C
ANISOU 2476 CD2 LEU A1010 10002 8240 18304 730 212 1190 C
ATOM 2477 N ASN A1011 9.860 119.479 164.458 1.00 94.51 N
ANISOU 2477 N ASN A1011 10270 8518 17121 120 418 1130 N
ATOM 2478 CA ASN A1011 10.508 119.535 163.144 1.00 97.54 C
ANISOU 2478 CA ASN A1011 10771 9107 17183 -41 619 1068 C
ATOM 2479 C ASN A1011 9.499 119.573 161.986 1.00104.60 C
ANISOU 2479 C ASN A1011 11866 10243 17633 -343 437 1183 C
ATOM 2480 O ASN A1011 9.786 120.193 160.960 1.00106.92 O
ANISOU 2480 O ASN A1011 12242 10782 17601 -528 503 1335 O
ATOM 2481 CB ASN A1011 11.448 118.341 162.963 1.00 99.77 C
ANISOU 2481 CB ASN A1011 11131 9286 17490 21 934 679 C
ATOM 2482 CG ASN A1011 12.679 118.348 163.843 1.00122.19 C
ANISOU 2482 CG ASN A1011 13742 11897 20787 271 1089 623 C
ATOM 2483 OD1 ASN A1011 12.746 119.008 164.889 1.00114.35 O
ANISOU 2483 OD1 ASN A1011 12577 10803 20066 422 906 806 O
ATOM 2484 ND2 ASN A1011 13.683 117.583 163.445 1.00116.74 N
ANISOU 2484 ND2 ASN A1011 13036 11094 20226 302 1425 345 N
ATOM 2485 N ASP A1012 8.340 118.895 162.138 1.00101.40 N
ANISOU 2485 N ASP A1012 11539 9768 17220 -412 192 1137 N
ATOM 2486 CA ASP A1012 7.286 118.824 161.119 1.00104.41 C
ANISOU 2486 CA ASP A1012 12094 10339 17239 -719 -95 1247 C
ATOM 2487 C ASP A1012 6.623 120.190 160.918 1.00108.31 C
ANISOU 2487 C ASP A1012 12420 10922 17810 -834 -396 1768 C
ATOM 2488 O ASP A1012 6.479 120.622 159.773 1.00111.53 O
ANISOU 2488 O ASP A1012 12964 11609 17804 -1113 -542 1985 O
ATOM 2489 CB ASP A1012 6.228 117.764 161.489 1.00106.05 C
ANISOU 2489 CB ASP A1012 12335 10354 17604 -729 -295 1083 C
ATOM 2490 CG ASP A1012 5.571 117.035 160.325 1.00122.04 C
ANISOU 2490 CG ASP A1012 14627 12546 19197 -1052 -497 911 C
ATOM 2491 OD1 ASP A1012 5.971 117.277 159.162 1.00126.69 O
ANISOU 2491 OD1 ASP A1012 15450 13456 19230 -1302 -455 886 O
ATOM 2492 OD2 ASP A1012 4.670 116.204 160.579 1.00128.26 O
ANISOU 2492 OD2 ASP A1012 15401 13143 20189 -1073 -689 792 O
ATOM 2493 N ASN A1013 6.246 120.875 162.025 1.00101.41 N
ANISOU 2493 N ASN A1013 11250 9806 17477 -639 -469 1968 N
ATOM 2494 CA ASN A1013 5.618 122.201 161.993 1.00101.47 C
ANISOU 2494 CA ASN A1013 10994 9781 17780 -712 -703 2437 C
ATOM 2495 C ASN A1013 6.618 123.278 161.567 1.00106.41 C
ANISOU 2495 C ASN A1013 11522 10552 18356 -717 -553 2649 C
ATOM 2496 O ASN A1013 6.207 124.319 161.058 1.00107.98 O
ANISOU 2496 O ASN A1013 11543 10801 18683 -868 -766 3098 O
ATOM 2497 CB ASN A1013 4.994 122.551 163.342 1.00 98.54 C
ANISOU 2497 CB ASN A1013 10346 9074 18019 -509 -704 2467 C
ATOM 2498 CG ASN A1013 3.655 121.896 163.564 1.00120.25 C
ANISOU 2498 CG ASN A1013 13079 11648 20962 -575 -915 2478 C
ATOM 2499 OD1 ASN A1013 2.639 122.288 162.981 1.00116.06 O
ANISOU 2499 OD1 ASN A1013 12420 11088 20591 -778 -1243 2806 O
ATOM 2500 ND2 ASN A1013 3.623 120.879 164.410 1.00110.60 N
ANISOU 2500 ND2 ASN A1013 11952 10279 19792 -415 -752 2166 N
ATOM 2501 N LEU A1014 7.924 123.014 161.756 1.00102.22 N
ANISOU 2501 N LEU A1014 11065 10052 17723 -558 -197 2364 N
ATOM 2502 CA LEU A1014 9.022 123.897 161.362 1.00103.18 C
ANISOU 2502 CA LEU A1014 11080 10273 17850 -542 16 2518 C
ATOM 2503 C LEU A1014 9.122 123.947 159.831 1.00111.74 C
ANISOU 2503 C LEU A1014 12406 11717 18332 -856 22 2715 C
ATOM 2504 O LEU A1014 9.405 125.007 159.270 1.00113.63 O
ANISOU 2504 O LEU A1014 12511 12072 18591 -959 22 3121 O
ATOM 2505 CB LEU A1014 10.333 123.392 161.990 1.00101.54 C
ANISOU 2505 CB LEU A1014 10868 9945 17767 -298 371 2136 C
ATOM 2506 CG LEU A1014 11.530 124.343 162.052 1.00106.56 C
ANISOU 2506 CG LEU A1014 11269 10533 18688 -187 591 2250 C
ATOM 2507 CD1 LEU A1014 11.228 125.578 162.886 1.00104.75 C
ANISOU 2507 CD1 LEU A1014 10690 10102 19008 -82 408 2489 C
ATOM 2508 CD2 LEU A1014 12.721 123.637 162.647 1.00108.29 C
ANISOU 2508 CD2 LEU A1014 11472 10591 19081 27 862 1878 C
ATOM 2509 N LYS A1015 8.851 122.805 159.164 1.00110.22 N
ANISOU 2509 N LYS A1015 12575 11702 17602 -1032 22 2432 N
ATOM 2510 CA LYS A1015 8.836 122.679 157.706 1.00115.53 C
ANISOU 2510 CA LYS A1015 13588 12768 17538 -1395 14 2526 C
ATOM 2511 C LYS A1015 7.564 123.317 157.134 1.00121.97 C
ANISOU 2511 C LYS A1015 14377 13722 18242 -1682 -552 3065 C
ATOM 2512 O LYS A1015 7.560 123.740 155.976 1.00126.86 O
ANISOU 2512 O LYS A1015 15192 14694 18315 -2009 -660 3399 O
ATOM 2513 CB LYS A1015 8.934 121.205 157.291 1.00119.99 C
ANISOU 2513 CB LYS A1015 14532 13420 17640 -1495 202 1941 C
ATOM 2514 N VAL A1016 6.490 123.386 157.955 1.00115.38 N
ANISOU 2514 N VAL A1016 13288 12596 17956 -1575 -906 3179 N
ATOM 2515 CA VAL A1016 5.194 123.983 157.612 1.00117.37 C
ANISOU 2515 CA VAL A1016 13381 12835 18379 -1802 -1472 3709 C
ATOM 2516 C VAL A1016 5.366 125.510 157.517 1.00121.98 C
ANISOU 2516 C VAL A1016 13603 13385 19359 -1811 -1542 4320 C
ATOM 2517 O VAL A1016 4.879 126.106 156.555 1.00126.47 O
ANISOU 2517 O VAL A1016 14174 14164 19716 -2130 -1920 4876 O
ATOM 2518 CB VAL A1016 4.079 123.558 158.616 1.00117.99 C
ANISOU 2518 CB VAL A1016 13240 12529 19063 -1649 -1691 3593 C
ATOM 2519 CG1 VAL A1016 2.830 124.432 158.500 1.00119.83 C
ANISOU 2519 CG1 VAL A1016 13123 12595 19812 -1808 -2202 4193 C
ATOM 2520 CG2 VAL A1016 3.717 122.086 158.442 1.00118.48 C
ANISOU 2520 CG2 VAL A1016 13634 12635 18749 -1729 -1737 3118 C
ATOM 2521 N ILE A1017 6.088 126.125 158.490 1.00114.32 N
ANISOU 2521 N ILE A1017 12322 12151 18965 -1483 -1205 4226 N
ATOM 2522 CA ILE A1017 6.373 127.569 158.534 1.00114.76 C
ANISOU 2522 CA ILE A1017 11970 12090 19543 -1446 -1202 4716 C
ATOM 2523 C ILE A1017 7.202 127.965 157.295 1.00124.05 C
ANISOU 2523 C ILE A1017 13338 13658 20138 -1677 -1080 5038 C
ATOM 2524 O ILE A1017 6.923 128.997 156.682 1.00127.34 O
ANISOU 2524 O ILE A1017 13533 14131 20719 -1870 -1332 5697 O
ATOM 2525 CB ILE A1017 7.074 128.000 159.863 1.00112.88 C
ANISOU 2525 CB ILE A1017 11421 11499 19968 -1066 -857 4408 C
ATOM 2526 CG1 ILE A1017 6.249 127.585 161.099 1.00109.41 C
ANISOU 2526 CG1 ILE A1017 10863 10724 19983 -877 -915 4090 C
ATOM 2527 CG2 ILE A1017 7.336 129.514 159.891 1.00114.62 C
ANISOU 2527 CG2 ILE A1017 11177 11547 20828 -1041 -860 4872 C
ATOM 2528 CD1 ILE A1017 7.055 127.366 162.384 1.00111.54 C
ANISOU 2528 CD1 ILE A1017 11098 10794 20488 -552 -569 3583 C
ATOM 2529 N GLU A1018 8.182 127.122 156.910 1.00121.68 N
ANISOU 2529 N GLU A1018 13434 13606 19192 -1675 -673 4598 N
ATOM 2530 CA GLU A1018 9.052 127.335 155.747 1.00126.72 C
ANISOU 2530 CA GLU A1018 14322 14628 19197 -1900 -405 4795 C
ATOM 2531 C GLU A1018 8.265 127.284 154.420 1.00137.17 C
ANISOU 2531 C GLU A1018 15989 16386 19745 -2381 -815 5225 C
ATOM 2532 O GLU A1018 8.673 127.927 153.450 1.00142.13 O
ANISOU 2532 O GLU A1018 16715 17327 19960 -2634 -751 5701 O
ATOM 2533 CB GLU A1018 10.195 126.309 155.728 1.00127.56 C
ANISOU 2533 CB GLU A1018 14743 14816 18908 -1781 181 4126 C
ATOM 2534 CG GLU A1018 11.275 126.596 156.757 1.00133.90 C
ANISOU 2534 CG GLU A1018 15199 15265 20411 -1384 571 3878 C
ATOM 2535 CD GLU A1018 12.390 125.572 156.804 1.00154.69 C
ANISOU 2535 CD GLU A1018 18042 17883 22850 -1253 1112 3265 C
ATOM 2536 OE1 GLU A1018 12.396 124.746 157.744 1.00145.17 O
ANISOU 2536 OE1 GLU A1018 16807 16422 21930 -1016 1126 2800 O
ATOM 2537 OE2 GLU A1018 13.261 125.598 155.904 1.00155.05 O
ANISOU 2537 OE2 GLU A1018 18259 18150 22505 -1395 1543 3275 O
ATOM 2538 N LYS A1019 7.139 126.542 154.390 1.00133.68 N
ANISOU 2538 N LYS A1019 15717 15956 19117 -2524 -1258 5093 N
ATOM 2539 CA LYS A1019 6.270 126.410 153.218 1.00139.98 C
ANISOU 2539 CA LYS A1019 16840 17140 19206 -3007 -1786 5470 C
ATOM 2540 C LYS A1019 4.912 127.118 153.455 1.00143.86 C
ANISOU 2540 C LYS A1019 16901 17371 20390 -3085 -2501 6098 C
ATOM 2541 O LYS A1019 3.888 126.695 152.908 1.00147.15 O
ANISOU 2541 O LYS A1019 17496 17922 20493 -3397 -3066 6250 O
ATOM 2542 CB LYS A1019 6.070 124.922 152.876 1.00143.84 C
ANISOU 2542 CB LYS A1019 17860 17826 18969 -3158 -1754 4782 C
ATOM 2543 N ALA A1020 4.916 128.210 154.251 1.00136.99 N
ANISOU 2543 N ALA A1020 15433 16093 20521 -2817 -2471 6449 N
ATOM 2544 CA ALA A1020 3.713 128.978 154.588 1.00137.16 C
ANISOU 2544 CA ALA A1020 14931 15749 21434 -2845 -3021 7010 C
ATOM 2545 C ALA A1020 3.640 130.313 153.842 1.00146.59 C
ANISOU 2545 C ALA A1020 15812 17017 22869 -3086 -3333 7958 C
ATOM 2546 O ALA A1020 4.673 130.891 153.493 1.00147.54 O
ANISOU 2546 O ALA A1020 15954 17319 22785 -3075 -2972 8137 O
ATOM 2547 CB ALA A1020 3.650 129.226 156.087 1.00131.11 C
ANISOU 2547 CB ALA A1020 13692 14412 21713 -2394 -2738 6664 C
ATOM 2548 N ASP A1021 2.403 130.803 153.623 1.00146.50 N
ANISOU 2548 N ASP A1021 15452 16812 23399 -3301 -4010 8601 N
ATOM 2549 CA ASP A1021 2.109 132.064 152.941 1.00152.09 C
ANISOU 2549 CA ASP A1021 15760 17505 24521 -3558 -4445 9628 C
ATOM 2550 C ASP A1021 1.321 133.022 153.852 1.00153.66 C
ANISOU 2550 C ASP A1021 15116 16985 26282 -3338 -4610 9953 C
ATOM 2551 O ASP A1021 1.585 134.225 153.840 1.00155.22 O
ANISOU 2551 O ASP A1021 14813 16961 27202 -3304 -4572 10520 O
ATOM 2552 CB ASP A1021 1.342 131.810 151.623 1.00162.17 C
ANISOU 2552 CB ASP A1021 17387 19237 24993 -4124 -5212 10240 C
ATOM 2553 CG ASP A1021 0.005 131.084 151.730 1.00171.65 C
ANISOU 2553 CG ASP A1021 18570 20254 26395 -4258 -5821 10146 C
ATOM 2554 OD1 ASP A1021 -0.226 130.401 152.754 1.00165.25 O
ANISOU 2554 OD1 ASP A1021 17685 19087 26016 -3919 -5526 9414 O
ATOM 2555 OD2 ASP A1021 -0.794 131.172 150.775 1.00180.67 O
ANISOU 2555 OD2 ASP A1021 20070 21650 26927 -4382 -6164 10185 O
ATOM 2556 N ASN A1022 0.368 132.484 154.640 1.00146.59 N
ANISOU 2556 N ASN A1022 14048 15697 25951 -3195 -4737 9575 N
ATOM 2557 CA ASN A1022 -0.486 133.242 155.559 1.00144.87 C
ANISOU 2557 CA ASN A1022 13061 14759 27223 -2999 -4801 9750 C
ATOM 2558 C ASN A1022 0.158 133.368 156.943 1.00140.89 C
ANISOU 2558 C ASN A1022 12374 13891 27265 -2518 -4047 8992 C
ATOM 2559 O ASN A1022 0.837 132.440 157.387 1.00135.72 O
ANISOU 2559 O ASN A1022 12206 13460 25902 -2323 -3615 8228 O
ATOM 2560 CB ASN A1022 -1.862 132.560 155.674 1.00147.12 C
ANISOU 2560 CB ASN A1022 13266 14805 27828 -3118 -5281 9735 C
ATOM 2561 CG ASN A1022 -2.939 133.342 156.401 1.00167.81 C
ANISOU 2561 CG ASN A1022 15310 16799 31650 -2907 -5205 9690 C
ATOM 2562 OD1 ASN A1022 -2.859 134.563 156.597 1.00162.99 O
ANISOU 2562 OD1 ASN A1022 14227 15890 31812 -2801 -5041 9960 O
ATOM 2563 ND2 ASN A1022 -4.000 132.649 156.787 1.00160.96 N
ANISOU 2563 ND2 ASN A1022 14103 15500 31552 -3009 -5609 9831 N
ATOM 2564 N ALA A1023 -0.073 134.508 157.627 1.00136.81 N
ANISOU 2564 N ALA A1023 11146 12796 28037 -2352 -3911 9203 N
ATOM 2565 CA ALA A1023 0.450 134.775 158.971 1.00130.89 C
ANISOU 2565 CA ALA A1023 10190 11675 27868 -1950 -3254 8505 C
ATOM 2566 C ALA A1023 -0.287 133.950 160.042 1.00130.63 C
ANISOU 2566 C ALA A1023 10219 11357 28059 -1761 -3051 7838 C
ATOM 2567 O ALA A1023 0.285 133.686 161.102 1.00125.34 O
ANISOU 2567 O ALA A1023 9690 10606 27329 -1467 -2515 7111 O
ATOM 2568 CB ALA A1023 0.355 136.257 159.291 1.00134.01 C
ANISOU 2568 CB ALA A1023 9800 11522 29596 -1886 -3182 8912 C
ATOM 2569 N ALA A1024 -1.544 133.540 159.764 1.00129.59 N
ANISOU 2569 N ALA A1024 9978 11074 28186 -1947 -3497 8119 N
ATOM 2570 CA ALA A1024 -2.355 132.711 160.663 1.00126.44 C
ANISOU 2570 CA ALA A1024 9617 10394 28030 -1806 -3325 7589 C
ATOM 2571 C ALA A1024 -1.886 131.250 160.626 1.00126.00 C
ANISOU 2571 C ALA A1024 10315 10829 26730 -1763 -3215 7008 C
ATOM 2572 O ALA A1024 -1.988 130.548 161.634 1.00121.46 O
ANISOU 2572 O ALA A1024 9885 10108 26156 -1538 -2827 6386 O
ATOM 2573 CB ALA A1024 -3.823 132.801 160.283 1.00132.00 C
ANISOU 2573 CB ALA A1024 9882 10727 29543 -2037 -3873 8152 C
ATOM 2574 N GLN A1025 -1.370 130.804 159.459 1.00123.95 N
ANISOU 2574 N GLN A1025 10527 11138 25432 -1996 -3530 7220 N
ATOM 2575 CA GLN A1025 -0.831 129.460 159.225 1.00121.12 C
ANISOU 2575 CA GLN A1025 10861 11244 23917 -1999 -3422 6689 C
ATOM 2576 C GLN A1025 0.455 129.265 160.042 1.00118.41 C
ANISOU 2576 C GLN A1025 10755 10999 23238 -1669 -2763 6043 C
ATOM 2577 O GLN A1025 0.699 128.171 160.557 1.00114.81 O
ANISOU 2577 O GLN A1025 10660 10629 22335 -1519 -2505 5448 O
ATOM 2578 CB GLN A1025 -0.563 129.259 157.721 1.00127.48 C
ANISOU 2578 CB GLN A1025 12068 12610 23758 -2376 -3862 7091 C
ATOM 2579 CG GLN A1025 -0.330 127.803 157.302 1.00142.02 C
ANISOU 2579 CG GLN A1025 14576 14864 24521 -2471 -3851 6563 C
ATOM 2580 CD GLN A1025 -0.002 127.630 155.832 1.00166.96 C
ANISOU 2580 CD GLN A1025 18198 18611 26629 -2878 -4191 6862 C
ATOM 2581 OE1 GLN A1025 0.342 128.578 155.111 1.00166.15 O
ANISOU 2581 OE1 GLN A1025 18003 18706 26420 -3064 -4339 7461 O
ATOM 2582 NE2 GLN A1025 -0.077 126.395 155.358 1.00160.27 N
ANISOU 2582 NE2 GLN A1025 17874 18061 24960 -3040 -4287 6430 N
ATOM 2583 N VAL A1026 1.260 130.339 160.162 1.00113.54 N
ANISOU 2583 N VAL A1026 9889 10330 22921 -1568 -2531 6201 N
ATOM 2584 CA VAL A1026 2.518 130.390 160.916 1.00108.64 C
ANISOU 2584 CA VAL A1026 9387 9746 22146 -1280 -1989 5687 C
ATOM 2585 C VAL A1026 2.192 130.295 162.422 1.00107.77 C
ANISOU 2585 C VAL A1026 9096 9220 22629 -999 -1655 5169 C
ATOM 2586 O VAL A1026 2.847 129.535 163.137 1.00103.74 O
ANISOU 2586 O VAL A1026 8904 8807 21706 -801 -1332 4600 O
ATOM 2587 CB VAL A1026 3.336 131.669 160.555 1.00114.10 C
ANISOU 2587 CB VAL A1026 9775 10434 23144 -1289 -1906 6081 C
ATOM 2588 CG1 VAL A1026 4.578 131.817 161.429 1.00110.00 C
ANISOU 2588 CG1 VAL A1026 9285 9862 22647 -992 -1404 5554 C
ATOM 2589 CG2 VAL A1026 3.724 131.680 159.077 1.00118.23 C
ANISOU 2589 CG2 VAL A1026 10563 11433 22927 -1590 -2159 6591 C
ATOM 2590 N LYS A1027 1.153 131.035 162.879 1.00104.91 N
ANISOU 2590 N LYS A1027 8227 8393 23241 -1009 -1729 5389 N
ATOM 2591 CA LYS A1027 0.682 131.070 164.268 1.00102.09 C
ANISOU 2591 CA LYS A1027 7679 7621 23490 -801 -1363 4932 C
ATOM 2592 C LYS A1027 0.141 129.694 164.712 1.00103.04 C
ANISOU 2592 C LYS A1027 8166 7801 23183 -754 -1310 4555 C
ATOM 2593 O LYS A1027 0.322 129.326 165.872 1.00 99.80 O
ANISOU 2593 O LYS A1027 7889 7288 22741 -554 -913 4035 O
ATOM 2594 CB LYS A1027 -0.392 132.160 164.437 1.00108.08 C
ANISOU 2594 CB LYS A1027 7767 7833 25465 -873 -1438 5303 C
ATOM 2595 CG LYS A1027 -0.690 132.547 165.884 1.00122.54 C
ANISOU 2595 CG LYS A1027 9348 9208 28004 -676 -919 4790 C
ATOM 2596 CD LYS A1027 -1.427 133.877 165.959 1.00138.96 C
ANISOU 2596 CD LYS A1027 10683 10710 31405 -741 -903 5131 C
ATOM 2597 CE LYS A1027 -2.053 134.127 167.309 1.00149.40 C
ANISOU 2597 CE LYS A1027 11759 11533 33471 -611 -356 4606 C
ATOM 2598 NZ LYS A1027 -3.406 133.524 167.410 1.00155.58 N
ANISOU 2598 NZ LYS A1027 12414 12036 34664 -684 -401 4716 N
ATOM 2599 N ASP A1028 -0.504 128.942 163.791 1.00100.76 N
ANISOU 2599 N ASP A1028 8044 7681 22559 -959 -1726 4830 N
ATOM 2600 CA ASP A1028 -1.047 127.605 164.056 1.00 98.89 C
ANISOU 2600 CA ASP A1028 8112 7477 21986 -941 -1729 4525 C
ATOM 2601 C ASP A1028 0.077 126.585 164.275 1.00 98.66 C
ANISOU 2601 C ASP A1028 8621 7813 21051 -797 -1476 4020 C
ATOM 2602 O ASP A1028 -0.007 125.775 165.201 1.00 95.53 O
ANISOU 2602 O ASP A1028 8389 7325 20584 -635 -1204 3616 O
ATOM 2603 CB ASP A1028 -1.959 127.146 162.902 1.00104.50 C
ANISOU 2603 CB ASP A1028 8840 8271 22594 -1238 -2315 4946 C
ATOM 2604 CG ASP A1028 -3.362 127.730 162.902 1.00118.83 C
ANISOU 2604 CG ASP A1028 10097 9603 25451 -1365 -2595 5396 C
ATOM 2605 OD1 ASP A1028 -3.743 128.375 163.908 1.00119.17 O
ANISOU 2605 OD1 ASP A1028 9738 9193 26346 -1201 -2224 5293 O
ATOM 2606 OD2 ASP A1028 -4.097 127.506 161.915 1.00128.01 O
ANISOU 2606 OD2 ASP A1028 11220 10819 26601 -1644 -3181 5824 O
ATOM 2607 N ALA A1029 1.127 126.637 163.428 1.00 95.14 N
ANISOU 2607 N ALA A1029 8419 7754 19978 -865 -1543 4079 N
ATOM 2608 CA ALA A1029 2.286 125.748 163.499 1.00 92.28 C
ANISOU 2608 CA ALA A1029 8490 7689 18882 -744 -1295 3643 C
ATOM 2609 C ALA A1029 3.148 126.048 164.728 1.00 92.46 C
ANISOU 2609 C ALA A1029 8466 7588 19077 -464 -881 3285 C
ATOM 2610 O ALA A1029 3.682 125.115 165.327 1.00 89.93 O
ANISOU 2610 O ALA A1029 8416 7332 18422 -316 -677 2889 O
ATOM 2611 CB ALA A1029 3.117 125.868 162.232 1.00 95.29 C
ANISOU 2611 CB ALA A1029 9083 8463 18660 -917 -1409 3829 C
ATOM 2612 N LEU A1030 3.269 127.339 165.111 1.00 88.89 N
ANISOU 2612 N LEU A1030 7654 6937 19182 -411 -791 3432 N
ATOM 2613 CA LEU A1030 4.045 127.776 166.277 1.00 86.25 C
ANISOU 2613 CA LEU A1030 7259 6475 19037 -193 -461 3080 C
ATOM 2614 C LEU A1030 3.372 127.366 167.589 1.00 88.11 C
ANISOU 2614 C LEU A1030 7519 6471 19487 -76 -246 2748 C
ATOM 2615 O LEU A1030 4.077 127.108 168.566 1.00 86.03 O
ANISOU 2615 O LEU A1030 7431 6236 19021 78 -23 2374 O
ATOM 2616 CB LEU A1030 4.272 129.296 166.263 1.00 87.86 C
ANISOU 2616 CB LEU A1030 7035 6488 19858 -201 -432 3301 C
ATOM 2617 CG LEU A1030 5.406 129.818 165.379 1.00 93.24 C
ANISOU 2617 CG LEU A1030 7699 7393 20334 -238 -479 3523 C
ATOM 2618 CD1 LEU A1030 5.234 131.299 165.114 1.00 96.18 C
ANISOU 2618 CD1 LEU A1030 7562 7522 21460 -308 -544 3921 C
ATOM 2619 CD2 LEU A1030 6.772 129.559 166.005 1.00 92.86 C
ANISOU 2619 CD2 LEU A1030 7841 7446 19994 -48 -240 3102 C
ATOM 2620 N THR A1031 2.019 127.309 167.611 1.00 85.44 N
ANISOU 2620 N THR A1031 7001 5894 19568 -168 -317 2914 N
ATOM 2621 CA THR A1031 1.219 126.899 168.772 1.00 84.50 C
ANISOU 2621 CA THR A1031 6891 5527 19688 -89 -50 2653 C
ATOM 2622 C THR A1031 1.508 125.424 169.078 1.00 86.41 C
ANISOU 2622 C THR A1031 7571 5979 19282 -11 -6 2403 C
ATOM 2623 O THR A1031 1.715 125.068 170.241 1.00 85.32 O
ANISOU 2623 O THR A1031 7604 5811 19004 113 275 2091 O
ATOM 2624 CB THR A1031 -0.276 127.168 168.516 1.00 92.75 C
ANISOU 2624 CB THR A1031 7571 6224 21444 -222 -154 2961 C
ATOM 2625 OG1 THR A1031 -0.475 128.574 168.346 1.00 96.51 O
ANISOU 2625 OG1 THR A1031 7575 6439 22653 -281 -164 3198 O
ATOM 2626 CG2 THR A1031 -1.168 126.671 169.648 1.00 89.12 C
ANISOU 2626 CG2 THR A1031 7114 5488 21259 -154 196 2714 C
ATOM 2627 N LYS A1032 1.553 124.585 168.021 1.00 82.55 N
ANISOU 2627 N LYS A1032 7264 5703 18398 -104 -290 2543 N
ATOM 2628 CA LYS A1032 1.846 123.152 168.099 1.00 80.70 C
ANISOU 2628 CA LYS A1032 7382 5624 17656 -49 -276 2325 C
ATOM 2629 C LYS A1032 3.281 122.934 168.578 1.00 82.07 C
ANISOU 2629 C LYS A1032 7780 5990 17415 106 -111 2055 C
ATOM 2630 O LYS A1032 3.526 122.008 169.349 1.00 81.10 O
ANISOU 2630 O LYS A1032 7858 5868 17088 216 21 1846 O
ATOM 2631 CB LYS A1032 1.610 122.475 166.739 1.00 84.61 C
ANISOU 2631 CB LYS A1032 7996 6289 17863 -229 -608 2476 C
ATOM 2632 CG LYS A1032 0.129 122.293 166.402 1.00104.48 C
ANISOU 2632 CG LYS A1032 10327 8585 20787 -385 -847 2712 C
ATOM 2633 CD LYS A1032 -0.134 122.171 164.900 1.00119.59 C
ANISOU 2633 CD LYS A1032 12297 10693 22447 -649 -1297 2959 C
ATOM 2634 CE LYS A1032 -0.087 120.747 164.394 1.00132.76 C
ANISOU 2634 CE LYS A1032 14290 12508 23644 -720 -1405 2709 C
ATOM 2635 NZ LYS A1032 -0.333 120.675 162.930 1.00145.41 N
ANISOU 2635 NZ LYS A1032 16013 14349 24889 -1031 -1848 2895 N
ATOM 2636 N MET A1033 4.212 123.814 168.155 1.00 77.88 N
ANISOU 2636 N MET A1033 7169 5584 16840 108 -135 2106 N
ATOM 2637 CA MET A1033 5.627 123.789 168.537 1.00 76.18 C
ANISOU 2637 CA MET A1033 7074 5495 16375 244 -18 1894 C
ATOM 2638 C MET A1033 5.812 124.170 170.012 1.00 79.13 C
ANISOU 2638 C MET A1033 7429 5735 16902 370 159 1675 C
ATOM 2639 O MET A1033 6.553 123.488 170.724 1.00 77.98 O
ANISOU 2639 O MET A1033 7481 5653 16496 476 206 1481 O
ATOM 2640 CB MET A1033 6.449 124.736 167.646 1.00 79.13 C
ANISOU 2640 CB MET A1033 7304 5987 16774 194 -72 2057 C
ATOM 2641 CG MET A1033 6.778 124.157 166.291 1.00 83.79 C
ANISOU 2641 CG MET A1033 8059 6813 16965 70 -163 2161 C
ATOM 2642 SD MET A1033 7.940 125.169 165.344 1.00 89.25 S
ANISOU 2642 SD MET A1033 8623 7663 17624 20 -112 2359 S
ATOM 2643 CE MET A1033 9.480 124.708 166.127 1.00 84.41 C
ANISOU 2643 CE MET A1033 8087 7024 16962 246 111 1997 C
ATOM 2644 N ARG A1034 5.135 125.254 170.461 1.00 75.93 N
ANISOU 2644 N ARG A1034 6780 5134 16936 334 251 1705 N
ATOM 2645 CA ARG A1034 5.197 125.782 171.827 1.00 75.88 C
ANISOU 2645 CA ARG A1034 6770 5002 17058 396 463 1431 C
ATOM 2646 C ARG A1034 4.601 124.805 172.845 1.00 79.51 C
ANISOU 2646 C ARG A1034 7485 5437 17287 424 625 1285 C
ATOM 2647 O ARG A1034 5.137 124.690 173.948 1.00 79.57 O
ANISOU 2647 O ARG A1034 7693 5508 17033 474 721 1050 O
ATOM 2648 CB ARG A1034 4.478 127.137 171.918 1.00 77.26 C
ANISOU 2648 CB ARG A1034 6575 4910 17871 326 588 1470 C
ATOM 2649 CG ARG A1034 4.981 128.010 173.057 1.00 86.03 C
ANISOU 2649 CG ARG A1034 7649 5926 19114 362 784 1112 C
ATOM 2650 CD ARG A1034 4.027 129.141 173.376 1.00 94.71 C
ANISOU 2650 CD ARG A1034 8386 6673 20925 287 1030 1049 C
ATOM 2651 NE ARG A1034 4.510 129.938 174.502 1.00 99.80 N
ANISOU 2651 NE ARG A1034 9038 7231 21650 292 1247 598 N
ATOM 2652 CZ ARG A1034 4.201 129.715 175.776 1.00111.18 C
ANISOU 2652 CZ ARG A1034 10741 8661 22842 263 1546 213 C
ATOM 2653 NH1 ARG A1034 3.388 128.719 176.106 1.00 93.14 N
ANISOU 2653 NH1 ARG A1034 8692 6415 20283 252 1697 270 N
ATOM 2654 NH2 ARG A1034 4.698 130.490 176.730 1.00 99.71 N
ANISOU 2654 NH2 ARG A1034 9326 7160 21400 224 1702 -238 N
ATOM 2655 N ALA A1035 3.497 124.120 172.487 1.00 76.09 N
ANISOU 2655 N ALA A1035 7040 4911 16959 371 632 1450 N
ATOM 2656 CA ALA A1035 2.843 123.144 173.362 1.00 76.71 C
ANISOU 2656 CA ALA A1035 7320 4933 16894 392 815 1383 C
ATOM 2657 C ALA A1035 3.722 121.902 173.529 1.00 80.90 C
ANISOU 2657 C ALA A1035 8154 5666 16919 475 692 1347 C
ATOM 2658 O ALA A1035 3.839 121.388 174.642 1.00 81.76 O
ANISOU 2658 O ALA A1035 8481 5809 16776 514 827 1254 O
ATOM 2659 CB ALA A1035 1.482 122.764 172.805 1.00 78.20 C
ANISOU 2659 CB ALA A1035 7342 4917 17455 311 808 1596 C
ATOM 2660 N ALA A1036 4.374 121.455 172.432 1.00 76.89 N
ANISOU 2660 N ALA A1036 7651 5285 16281 486 454 1428 N
ATOM 2661 CA ALA A1036 5.286 120.310 172.412 1.00 76.46 C
ANISOU 2661 CA ALA A1036 7790 5348 15912 564 356 1384 C
ATOM 2662 C ALA A1036 6.563 120.614 173.202 1.00 82.88 C
ANISOU 2662 C ALA A1036 8688 6263 16541 649 325 1260 C
ATOM 2663 O ALA A1036 7.098 119.718 173.855 1.00 82.79 O
ANISOU 2663 O ALA A1036 8834 6281 16342 712 279 1256 O
ATOM 2664 CB ALA A1036 5.631 119.941 170.979 1.00 76.59 C
ANISOU 2664 CB ALA A1036 7771 5448 15882 519 201 1427 C
ATOM 2665 N ALA A1037 7.033 121.883 173.159 1.00 81.96 N
ANISOU 2665 N ALA A1037 8431 6168 16543 638 314 1189 N
ATOM 2666 CA ALA A1037 8.221 122.357 173.878 1.00 83.23 C
ANISOU 2666 CA ALA A1037 8623 6392 16610 693 231 1051 C
ATOM 2667 C ALA A1037 8.000 122.338 175.395 1.00 90.94 C
ANISOU 2667 C ALA A1037 9805 7381 17367 669 306 923 C
ATOM 2668 O ALA A1037 8.952 122.105 176.139 1.00 91.63 O
ANISOU 2668 O ALA A1037 10027 7554 17234 697 139 870 O
ATOM 2669 CB ALA A1037 8.586 123.759 173.423 1.00 83.92 C
ANISOU 2669 CB ALA A1037 8460 6446 16978 669 224 1008 C
ATOM 2670 N LEU A1038 6.748 122.570 175.844 1.00 89.85 N
ANISOU 2670 N LEU A1038 9691 7152 17295 598 558 888 N
ATOM 2671 CA LEU A1038 6.374 122.560 177.260 1.00 93.01 C
ANISOU 2671 CA LEU A1038 10336 7583 17422 534 744 745 C
ATOM 2672 C LEU A1038 6.265 121.133 177.784 1.00 99.43 C
ANISOU 2672 C LEU A1038 11405 8469 17904 554 715 933 C
ATOM 2673 O LEU A1038 6.624 120.888 178.937 1.00101.76 O
ANISOU 2673 O LEU A1038 11974 8898 17792 505 687 901 O
ATOM 2674 CB LEU A1038 5.054 123.311 177.496 1.00 94.49 C
ANISOU 2674 CB LEU A1038 10405 7584 17912 447 1126 631 C
ATOM 2675 CG LEU A1038 5.084 124.833 177.327 1.00 99.98 C
ANISOU 2675 CG LEU A1038 10825 8146 19016 404 1215 417 C
ATOM 2676 CD1 LEU A1038 3.696 125.368 177.061 1.00101.02 C
ANISOU 2676 CD1 LEU A1038 10683 7991 19708 344 1535 445 C
ATOM 2677 CD2 LEU A1038 5.711 125.524 178.536 1.00105.39 C
ANISOU 2677 CD2 LEU A1038 11700 8921 19424 332 1278 46 C
ATOM 2678 N ASP A1039 5.766 120.196 176.942 1.00 95.80 N
ANISOU 2678 N ASP A1039 10855 7920 17625 604 699 1141 N
ATOM 2679 CA ASP A1039 5.630 118.773 177.275 1.00 97.04 C
ANISOU 2679 CA ASP A1039 11167 8073 17632 635 672 1350 C
ATOM 2680 C ASP A1039 7.006 118.127 177.416 1.00101.87 C
ANISOU 2680 C ASP A1039 11850 8787 18070 704 352 1433 C
ATOM 2681 O ASP A1039 7.203 117.293 178.299 1.00103.64 O
ANISOU 2681 O ASP A1039 12256 9056 18066 697 283 1609 O
ATOM 2682 CB ASP A1039 4.805 118.027 176.206 1.00 97.71 C
ANISOU 2682 CB ASP A1039 11085 7994 18047 655 701 1476 C
ATOM 2683 CG ASP A1039 3.364 118.480 176.054 1.00109.65 C
ANISOU 2683 CG ASP A1039 12463 9333 19865 582 958 1479 C
ATOM 2684 OD1 ASP A1039 2.678 118.644 177.089 1.00112.95 O
ANISOU 2684 OD1 ASP A1039 12986 9703 20229 532 1257 1464 O
ATOM 2685 OD2 ASP A1039 2.899 118.599 174.901 1.00113.88 O
ANISOU 2685 OD2 ASP A1039 12790 9772 20707 556 862 1515 O
ATOM 2686 N ALA A1040 7.956 118.536 176.550 1.00 97.63 N
ANISOU 2686 N ALA A1040 11139 8261 17693 760 166 1345 N
ATOM 2687 CA ALA A1040 9.337 118.058 176.523 1.00 98.46 C
ANISOU 2687 CA ALA A1040 11208 8386 17818 832 -111 1404 C
ATOM 2688 C ALA A1040 10.114 118.491 177.776 1.00106.77 C
ANISOU 2688 C ALA A1040 12416 9562 18591 788 -321 1391 C
ATOM 2689 O ALA A1040 11.013 117.764 178.206 1.00108.42 O
ANISOU 2689 O ALA A1040 12645 9763 18787 818 -595 1565 O
ATOM 2690 CB ALA A1040 10.034 118.564 175.274 1.00 97.25 C
ANISOU 2690 CB ALA A1040 10822 8200 17928 880 -148 1292 C
ATOM 2691 N GLN A1041 9.759 119.660 178.362 1.00105.28 N
ANISOU 2691 N GLN A1041 12321 9463 18220 695 -209 1180 N
ATOM 2692 CA GLN A1041 10.375 120.205 179.581 1.00109.01 C
ANISOU 2692 CA GLN A1041 12994 10081 18343 596 -403 1072 C
ATOM 2693 C GLN A1041 10.051 119.330 180.788 1.00118.12 C
ANISOU 2693 C GLN A1041 14493 11366 19023 500 -432 1278 C
ATOM 2694 O GLN A1041 10.934 119.058 181.604 1.00121.17 O
ANISOU 2694 O GLN A1041 15032 11871 19138 438 -803 1407 O
ATOM 2695 CB GLN A1041 9.918 121.649 179.841 1.00110.83 C
ANISOU 2695 CB GLN A1041 13223 10329 18560 502 -182 715 C
ATOM 2696 CG GLN A1041 10.618 122.680 178.970 1.00121.49 C
ANISOU 2696 CG GLN A1041 14244 11578 20339 564 -278 558 C
ATOM 2697 CD GLN A1041 10.594 124.061 179.574 1.00140.80 C
ANISOU 2697 CD GLN A1041 16685 14021 22790 455 -195 192 C
ATOM 2698 OE1 GLN A1041 11.569 124.514 180.182 1.00138.55 O
ANISOU 2698 OE1 GLN A1041 16445 13798 22400 400 -491 37 O
ATOM 2699 NE2 GLN A1041 9.486 124.770 179.406 1.00131.47 N
ANISOU 2699 NE2 GLN A1041 15409 12728 21817 410 194 34 N
ATOM 2700 N LYS A1042 8.785 118.874 180.885 1.00115.57 N
ANISOU 2700 N LYS A1042 14271 11006 18633 475 -62 1357 N
ATOM 2701 CA LYS A1042 8.310 117.988 181.947 1.00119.45 C
ANISOU 2701 CA LYS A1042 15074 11603 18708 381 12 1616 C
ATOM 2702 C LYS A1042 8.840 116.560 181.729 1.00124.94 C
ANISOU 2702 C LYS A1042 15674 12208 19591 479 -278 2039 C
ATOM 2703 O LYS A1042 8.842 115.758 182.666 1.00128.35 O
ANISOU 2703 O LYS A1042 16332 12735 19702 400 -381 2369 O
ATOM 2704 CB LYS A1042 6.774 117.995 182.004 1.00121.83 C
ANISOU 2704 CB LYS A1042 15423 11815 19051 340 555 1567 C
ATOM 2705 N ALA A1043 9.318 116.258 180.501 1.00119.06 N
ANISOU 2705 N ALA A1043 14588 11269 19379 634 -393 2032 N
ATOM 2706 CA ALA A1043 9.866 114.957 180.116 1.00119.47 C
ANISOU 2706 CA ALA A1043 14462 11148 19783 737 -601 2331 C
ATOM 2707 C ALA A1043 11.380 114.848 180.439 1.00126.21 C
ANISOU 2707 C ALA A1043 15232 12006 20717 753 -1081 2472 C
ATOM 2708 O ALA A1043 12.187 114.449 179.591 1.00124.73 O
ANISOU 2708 O ALA A1043 14738 11615 21040 872 -1203 2475 O
ATOM 2709 CB ALA A1043 9.607 114.697 178.639 1.00116.53 C
ANISOU 2709 CB ALA A1043 13799 10568 19910 854 -425 2176 C
ATOM 2710 N THR A1044 11.743 115.213 181.682 1.00126.78 N
ANISOU 2710 N THR A1044 15579 12301 20291 609 -1344 2576 N
ATOM 2711 CA THR A1044 13.085 115.119 182.253 1.00129.94 C
ANISOU 2711 CA THR A1044 15937 12721 20712 569 -1902 2784 C
ATOM 2712 C THR A1044 12.980 113.978 183.271 1.00138.13 C
ANISOU 2712 C THR A1044 17164 13813 21506 472 -2122 3323 C
ATOM 2713 O THR A1044 12.549 114.208 184.404 1.00141.45 O
ANISOU 2713 O THR A1044 18004 14527 21214 275 -2139 3411 O
ATOM 2714 CB THR A1044 13.525 116.475 182.823 1.00139.41 C
ANISOU 2714 CB THR A1044 17314 14142 21513 438 -2081 2465 C
ATOM 2715 N PRO A1045 13.231 112.717 182.855 1.00134.72 N
ANISOU 2715 N PRO A1045 16435 13090 21663 594 -2208 3680 N
ATOM 2716 CA PRO A1045 12.988 111.592 183.763 1.00139.11 C
ANISOU 2716 CA PRO A1045 17122 13655 22076 506 -2368 4262 C
ATOM 2717 C PRO A1045 14.114 111.326 184.761 1.00148.71 C
ANISOU 2717 C PRO A1045 18381 14948 23175 372 -3061 4741 C
ATOM 2718 O PRO A1045 15.279 111.242 184.363 1.00148.77 O
ANISOU 2718 O PRO A1045 18017 14716 23792 460 -3439 4793 O
ATOM 2719 CB PRO A1045 12.807 110.394 182.811 1.00138.93 C
ANISOU 2719 CB PRO A1045 16688 13217 22883 695 -2167 4392 C
ATOM 2720 CG PRO A1045 12.919 110.943 181.405 1.00137.96 C
ANISOU 2720 CG PRO A1045 16298 12934 23187 849 -1884 3835 C
ATOM 2721 CD PRO A1045 13.658 112.234 181.530 1.00132.96 C
ANISOU 2721 CD PRO A1045 15748 12502 22269 798 -2093 3552 C
ATOM 2722 N PRO A1046 13.780 111.124 186.060 1.00150.34 N
ANISOU 2722 N PRO A1046 19021 15468 22632 141 -3240 5142 N
ATOM 2723 CA PRO A1046 14.828 110.775 187.038 1.00156.86 C
ANISOU 2723 CA PRO A1046 19900 16383 23317 -31 -4005 5707 C
ATOM 2724 C PRO A1046 15.191 109.286 186.967 1.00162.74 C
ANISOU 2724 C PRO A1046 20234 16743 24856 62 -4268 6405 C
ATOM 2725 O PRO A1046 16.245 108.887 187.464 1.00167.67 O
ANISOU 2725 O PRO A1046 20681 17270 25755 -19 -4959 6915 O
ATOM 2726 CB PRO A1046 14.200 111.141 188.384 1.00163.93 C
ANISOU 2726 CB PRO A1046 21480 17804 23004 -350 -4005 5837 C
ATOM 2727 CG PRO A1046 12.724 111.108 188.158 1.00164.91 C
ANISOU 2727 CG PRO A1046 21787 17970 22900 -299 -3186 5592 C
ATOM 2728 CD PRO A1046 12.439 111.146 186.685 1.00152.66 C
ANISOU 2728 CD PRO A1046 19765 16032 22208 8 -2749 5145 C
ATOM 2729 N LYS A1047 14.308 108.475 186.341 1.00155.39 N
ANISOU 2729 N LYS A1047 19113 15554 24375 224 -3734 6425 N
ATOM 2730 CA LYS A1047 14.429 107.028 186.145 1.00157.11 C
ANISOU 2730 CA LYS A1047 18893 15331 25472 335 -3822 6985 C
ATOM 2731 C LYS A1047 15.396 106.694 184.999 1.00158.12 C
ANISOU 2731 C LYS A1047 18369 14932 26778 569 -3902 6779 C
ATOM 2732 O LYS A1047 15.713 107.568 184.191 1.00153.15 O
ANISOU 2732 O LYS A1047 17662 14302 26228 667 -3732 6157 O
ATOM 2733 CB LYS A1047 13.036 106.415 185.875 1.00157.16 C
ANISOU 2733 CB LYS A1047 18955 15253 25505 403 -3175 6958 C
ATOM 2734 CG LYS A1047 12.405 106.755 184.522 1.00158.48 C
ANISOU 2734 CG LYS A1047 18939 15234 26041 605 -2572 6213 C
ATOM 2735 CD LYS A1047 10.888 106.567 184.545 1.00162.64 C
ANISOU 2735 CD LYS A1047 19683 15828 26285 590 -1991 6140 C
ATOM 2736 CE LYS A1047 10.308 106.107 183.226 1.00164.82 C
ANISOU 2736 CE LYS A1047 19592 15718 27314 784 -1566 5739 C
ATOM 2737 NZ LYS A1047 10.604 107.048 182.112 1.00166.37 N
ANISOU 2737 NZ LYS A1047 19698 15927 27589 881 -1437 5037 N
ATOM 2738 N LEU A1048 15.855 105.429 184.932 1.00158.01 N
ANISOU 2738 N LEU A1048 17872 14450 27715 647 -4117 7307 N
ATOM 2739 CA LEU A1048 16.763 104.935 183.894 1.00185.83 C
ANISOU 2739 CA LEU A1048 20734 17395 32477 854 -4107 7129 C
ATOM 2740 C LEU A1048 16.618 103.424 183.725 1.00203.34 C
ANISOU 2740 C LEU A1048 23069 19524 34669 1082 -3652 6955 C
ATOM 2741 O LEU A1048 16.590 102.686 184.709 1.00175.09 O
ANISOU 2741 O LEU A1048 18908 15486 32135 825 -4408 8367 O
ATOM 2742 CB LEU A1048 18.222 105.296 184.213 1.00189.64 C
ANISOU 2742 CB LEU A1048 20973 17779 33302 808 -4770 7351 C
ATOM 2743 N GLU A1057 25.219 119.600 179.817 1.00126.33 N
ANISOU 2743 N GLU A1057 12008 10199 25791 1033 -4797 2422 N
ATOM 2744 CA GLU A1057 24.619 118.489 180.549 1.00127.68 C
ANISOU 2744 CA GLU A1057 12501 10537 25474 952 -5008 2746 C
ATOM 2745 C GLU A1057 23.110 118.746 180.752 1.00128.06 C
ANISOU 2745 C GLU A1057 13139 11053 24465 870 -4626 2505 C
ATOM 2746 O GLU A1057 22.410 119.020 179.772 1.00122.50 O
ANISOU 2746 O GLU A1057 12456 10393 23695 980 -3969 2222 O
ATOM 2747 CB GLU A1057 25.353 118.275 181.888 1.00135.86 C
ANISOU 2747 CB GLU A1057 13569 11577 26476 757 -5953 3130 C
ATOM 2748 N MET A1058 22.612 118.652 182.005 1.00127.92 N
ANISOU 2748 N MET A1058 13591 11371 23641 660 -5028 2635 N
ATOM 2749 CA MET A1058 21.210 118.894 182.354 1.00125.45 C
ANISOU 2749 CA MET A1058 13820 11462 22383 560 -4658 2418 C
ATOM 2750 C MET A1058 20.904 120.398 182.349 1.00127.82 C
ANISOU 2750 C MET A1058 14257 11936 22373 489 -4471 1887 C
ATOM 2751 O MET A1058 19.816 120.794 181.921 1.00123.43 O
ANISOU 2751 O MET A1058 13881 11522 21497 520 -3896 1609 O
ATOM 2752 CB MET A1058 20.878 118.280 183.722 1.00132.76 C
ANISOU 2752 CB MET A1058 15199 12678 22564 333 -5104 2754 C
ATOM 2753 N LYS A1059 21.866 121.230 182.823 1.00127.83 N
ANISOU 2753 N LYS A1059 14127 11879 22564 386 -4978 1758 N
ATOM 2754 CA LYS A1059 21.762 122.694 182.872 1.00127.01 C
ANISOU 2754 CA LYS A1059 14062 11855 22342 309 -4872 1244 C
ATOM 2755 C LYS A1059 21.697 123.278 181.458 1.00125.56 C
ANISOU 2755 C LYS A1059 13477 11438 22794 533 -4273 1046 C
ATOM 2756 O LYS A1059 20.919 124.200 181.222 1.00122.58 O
ANISOU 2756 O LYS A1059 13202 11168 22207 515 -3863 690 O
ATOM 2757 CB LYS A1059 22.934 123.307 183.655 1.00135.04 C
ANISOU 2757 CB LYS A1059 14958 12795 23554 148 -5629 1188 C
ATOM 2758 CG LYS A1059 22.786 123.196 185.166 1.00154.13 C
ANISOU 2758 CG LYS A1059 17929 15580 25053 -178 -6199 1213 C
ATOM 2759 N ASP A1060 22.477 122.708 180.514 1.00121.00 N
ANISOU 2759 N ASP A1060 12445 10536 22994 727 -4192 1297 N
ATOM 2760 CA ASP A1060 22.506 123.115 179.103 1.00116.62 C
ANISOU 2760 CA ASP A1060 11538 9787 22984 912 -3612 1182 C
ATOM 2761 C ASP A1060 21.191 122.742 178.391 1.00115.25 C
ANISOU 2761 C ASP A1060 11603 9793 22394 971 -2991 1139 C
ATOM 2762 O ASP A1060 20.867 123.330 177.359 1.00111.34 O
ANISOU 2762 O ASP A1060 10964 9266 22074 1047 -2524 1001 O
ATOM 2763 CB ASP A1060 23.705 122.479 178.378 1.00119.75 C
ANISOU 2763 CB ASP A1060 11433 9792 24275 1068 -3642 1438 C
ATOM 2764 CG ASP A1060 25.056 122.912 178.912 1.00134.47 C
ANISOU 2764 CG ASP A1060 12942 11388 26762 1027 -4244 1507 C
ATOM 2765 OD1 ASP A1060 25.427 122.466 180.020 1.00139.48 O
ANISOU 2765 OD1 ASP A1060 13697 12056 27242 895 -4908 1707 O
ATOM 2766 OD2 ASP A1060 25.757 123.670 178.208 1.00139.85 O
ANISOU 2766 OD2 ASP A1060 13209 11815 28113 1115 -4072 1402 O
ATOM 2767 N PHE A1061 20.444 121.767 178.951 1.00111.92 N
ANISOU 2767 N PHE A1061 11530 9548 21446 917 -3022 1297 N
ATOM 2768 CA PHE A1061 19.151 121.303 178.445 1.00107.98 C
ANISOU 2768 CA PHE A1061 11261 9196 20572 948 -2523 1279 C
ATOM 2769 C PHE A1061 18.006 122.119 179.052 1.00110.55 C
ANISOU 2769 C PHE A1061 11939 9786 20280 814 -2370 1021 C
ATOM 2770 O PHE A1061 17.031 122.409 178.356 1.00106.50 O
ANISOU 2770 O PHE A1061 11457 9321 19689 844 -1916 902 O
ATOM 2771 CB PHE A1061 18.957 119.813 178.749 1.00110.87 C
ANISOU 2771 CB PHE A1061 11751 9547 20827 965 -2612 1601 C
ATOM 2772 N ARG A1062 18.128 122.481 180.351 1.00110.79 N
ANISOU 2772 N ARG A1062 12230 9974 19892 642 -2748 930 N
ATOM 2773 CA ARG A1062 17.150 123.280 181.096 1.00111.29 C
ANISOU 2773 CA ARG A1062 12639 10260 19388 479 -2571 609 C
ATOM 2774 C ARG A1062 17.088 124.710 180.542 1.00113.16 C
ANISOU 2774 C ARG A1062 12628 10386 19982 498 -2328 244 C
ATOM 2775 O ARG A1062 15.991 125.230 180.322 1.00110.79 O
ANISOU 2775 O ARG A1062 12399 10125 19571 477 -1886 53 O
ATOM 2776 CB ARG A1062 17.488 123.293 182.596 1.00117.29 C
ANISOU 2776 CB ARG A1062 13760 11229 19576 250 -3062 570 C
ATOM 2777 N HIS A1063 18.264 125.329 180.292 1.00110.57 N
ANISOU 2777 N HIS A1063 11953 9871 20188 539 -2616 192 N
ATOM 2778 CA HIS A1063 18.373 126.676 179.725 1.00109.25 C
ANISOU 2778 CA HIS A1063 11466 9542 20500 566 -2425 -80 C
ATOM 2779 C HIS A1063 18.052 126.657 178.228 1.00107.57 C
ANISOU 2779 C HIS A1063 10962 9207 20702 737 -1964 102 C
ATOM 2780 O HIS A1063 17.594 127.662 177.693 1.00106.10 O
ANISOU 2780 O HIS A1063 10593 8945 20774 740 -1672 -40 O
ATOM 2781 CB HIS A1063 19.777 127.280 179.953 1.00113.44 C
ANISOU 2781 CB HIS A1063 11689 9880 21533 552 -2897 -154 C
ATOM 2782 CG HIS A1063 20.273 127.248 181.372 1.00122.48 C
ANISOU 2782 CG HIS A1063 13116 11155 22266 346 -3491 -293 C
ATOM 2783 ND1 HIS A1063 19.404 127.167 182.450 1.00126.66 N
ANISOU 2783 ND1 HIS A1063 14174 11985 21967 143 -3478 -499 N
ATOM 2784 CD2 HIS A1063 21.543 127.299 181.839 1.00128.47 C
ANISOU 2784 CD2 HIS A1063 13696 11783 23335 293 -4112 -236 C
ATOM 2785 CE1 HIS A1063 20.172 127.155 183.529 1.00131.78 C
ANISOU 2785 CE1 HIS A1063 15003 12727 22342 -49 -4111 -557 C
ATOM 2786 NE2 HIS A1063 21.465 127.236 183.211 1.00133.36 N
ANISOU 2786 NE2 HIS A1063 14772 12662 23237 34 -4555 -394 N
ATOM 2787 N GLY A1064 18.302 125.517 177.582 1.00101.64 N
ANISOU 2787 N GLY A1064 10171 8431 20019 853 -1918 413 N
ATOM 2788 CA GLY A1064 18.061 125.296 176.160 1.00 97.79 C
ANISOU 2788 CA GLY A1064 9490 7878 19787 971 -1509 576 C
ATOM 2789 C GLY A1064 16.608 125.395 175.749 1.00 98.14 C
ANISOU 2789 C GLY A1064 9708 8055 19525 934 -1131 549 C
ATOM 2790 O GLY A1064 16.302 126.000 174.717 1.00 96.13 O
ANISOU 2790 O GLY A1064 9258 7758 19508 955 -855 595 O
ATOM 2791 N PHE A1065 15.700 124.804 176.556 1.00 94.07 N
ANISOU 2791 N PHE A1065 9542 7687 18511 863 -1128 520 N
ATOM 2792 CA PHE A1065 14.260 124.864 176.296 1.00 91.64 C
ANISOU 2792 CA PHE A1065 9369 7454 17997 819 -787 502 C
ATOM 2793 C PHE A1065 13.712 126.238 176.658 1.00 95.15 C
ANISOU 2793 C PHE A1065 9740 7853 18560 728 -654 241 C
ATOM 2794 O PHE A1065 12.740 126.677 176.048 1.00 92.85 O
ANISOU 2794 O PHE A1065 9345 7513 18419 711 -371 270 O
ATOM 2795 CB PHE A1065 13.497 123.758 177.031 1.00 94.06 C
ANISOU 2795 CB PHE A1065 10025 7882 17831 778 -770 580 C
ATOM 2796 CG PHE A1065 13.394 122.474 176.242 1.00 94.06 C
ANISOU 2796 CG PHE A1065 10025 7862 17851 865 -699 826 C
ATOM 2797 CD1 PHE A1065 12.659 122.420 175.062 1.00 94.75 C
ANISOU 2797 CD1 PHE A1065 10014 7924 18064 885 -430 887 C
ATOM 2798 CD2 PHE A1065 14.026 121.318 176.680 1.00 97.83 C
ANISOU 2798 CD2 PHE A1065 10588 8327 18257 905 -926 995 C
ATOM 2799 CE1 PHE A1065 12.581 121.238 174.322 1.00 94.86 C
ANISOU 2799 CE1 PHE A1065 10045 7913 18085 935 -362 1026 C
ATOM 2800 CE2 PHE A1065 13.937 120.132 175.945 1.00 99.77 C
ANISOU 2800 CE2 PHE A1065 10792 8496 18620 979 -822 1158 C
ATOM 2801 CZ PHE A1065 13.221 120.102 174.768 1.00 95.45 C
ANISOU 2801 CZ PHE A1065 10178 7937 18151 990 -525 1129 C
ATOM 2802 N ASP A1066 14.358 126.926 177.628 1.00 94.04 N
ANISOU 2802 N ASP A1066 9619 7697 18416 654 -883 -18 N
ATOM 2803 CA ASP A1066 14.027 128.290 178.044 1.00 95.08 C
ANISOU 2803 CA ASP A1066 9635 7727 18762 556 -760 -361 C
ATOM 2804 C ASP A1066 14.265 129.234 176.869 1.00 96.50 C
ANISOU 2804 C ASP A1066 9348 7705 19611 633 -636 -256 C
ATOM 2805 O ASP A1066 13.433 130.105 176.616 1.00 96.03 O
ANISOU 2805 O ASP A1066 9111 7520 19856 590 -366 -336 O
ATOM 2806 CB ASP A1066 14.859 128.709 179.271 1.00101.14 C
ANISOU 2806 CB ASP A1066 10538 8531 19361 439 -1110 -685 C
ATOM 2807 CG ASP A1066 14.193 128.485 180.619 1.00114.62 C
ANISOU 2807 CG ASP A1066 12721 10433 20396 258 -1069 -953 C
ATOM 2808 OD1 ASP A1066 13.360 127.555 180.727 1.00114.14 O
ANISOU 2808 OD1 ASP A1066 12930 10508 19931 259 -873 -766 O
ATOM 2809 OD2 ASP A1066 14.527 129.220 181.573 1.00124.47 O
ANISOU 2809 OD2 ASP A1066 14084 11701 21508 97 -1227 -1357 O
ATOM 2810 N ILE A1067 15.372 129.015 176.116 1.00 91.73 N
ANISOU 2810 N ILE A1067 8526 7052 19277 740 -803 -30 N
ATOM 2811 CA ILE A1067 15.714 129.783 174.912 1.00 90.45 C
ANISOU 2811 CA ILE A1067 7947 6734 19685 803 -664 162 C
ATOM 2812 C ILE A1067 14.719 129.399 173.804 1.00 91.41 C
ANISOU 2812 C ILE A1067 8091 6940 19701 813 -375 459 C
ATOM 2813 O ILE A1067 14.242 130.285 173.099 1.00 90.78 O
ANISOU 2813 O ILE A1067 7748 6760 19983 781 -207 589 O
ATOM 2814 CB ILE A1067 17.205 129.602 174.463 1.00 94.12 C
ANISOU 2814 CB ILE A1067 8183 7106 20472 901 -848 305 C
ATOM 2815 CG1 ILE A1067 18.191 130.028 175.575 1.00 97.83 C
ANISOU 2815 CG1 ILE A1067 8592 7462 21117 865 -1238 29 C
ATOM 2816 CG2 ILE A1067 17.502 130.381 173.164 1.00 94.05 C
ANISOU 2816 CG2 ILE A1067 7774 6967 20994 945 -618 555 C
ATOM 2817 CD1 ILE A1067 19.593 129.393 175.507 1.00106.60 C
ANISOU 2817 CD1 ILE A1067 9562 8476 22465 951 -1518 178 C
ATOM 2818 N LEU A1068 14.378 128.092 173.688 1.00 86.39 N
ANISOU 2818 N LEU A1068 7752 6467 18605 836 -357 578 N
ATOM 2819 CA LEU A1068 13.448 127.572 172.680 1.00 84.19 C
ANISOU 2819 CA LEU A1068 7539 6280 18170 818 -157 819 C
ATOM 2820 C LEU A1068 12.051 128.198 172.828 1.00 87.32 C
ANISOU 2820 C LEU A1068 7908 6620 18648 726 -4 797 C
ATOM 2821 O LEU A1068 11.578 128.816 171.874 1.00 86.36 O
ANISOU 2821 O LEU A1068 7559 6446 18806 680 92 1024 O
ATOM 2822 CB LEU A1068 13.363 126.034 172.731 1.00 83.31 C
ANISOU 2822 CB LEU A1068 7728 6295 17630 854 -187 869 C
ATOM 2823 CG LEU A1068 12.807 125.356 171.472 1.00 86.87 C
ANISOU 2823 CG LEU A1068 8229 6835 17943 829 -32 1080 C
ATOM 2824 CD1 LEU A1068 13.882 125.206 170.402 1.00 87.93 C
ANISOU 2824 CD1 LEU A1068 8228 6980 18201 867 41 1187 C
ATOM 2825 CD2 LEU A1068 12.223 124.003 171.798 1.00 88.46 C
ANISOU 2825 CD2 LEU A1068 8710 7098 17801 836 -37 1064 C
ATOM 2826 N VAL A1069 11.422 128.074 174.023 1.00 84.40 N
ANISOU 2826 N VAL A1069 7748 6245 18075 684 27 549 N
ATOM 2827 CA VAL A1069 10.095 128.622 174.351 1.00 84.62 C
ANISOU 2827 CA VAL A1069 7731 6155 18266 597 251 464 C
ATOM 2828 C VAL A1069 10.127 130.151 174.161 1.00 89.89 C
ANISOU 2828 C VAL A1069 7990 6592 19572 558 324 399 C
ATOM 2829 O VAL A1069 9.221 130.704 173.529 1.00 89.87 O
ANISOU 2829 O VAL A1069 7730 6439 19977 507 458 596 O
ATOM 2830 CB VAL A1069 9.629 128.200 175.778 1.00 90.01 C
ANISOU 2830 CB VAL A1069 8754 6889 18558 543 343 162 C
ATOM 2831 CG1 VAL A1069 8.389 128.970 176.228 1.00 91.58 C
ANISOU 2831 CG1 VAL A1069 8845 6892 19060 446 675 -22 C
ATOM 2832 CG2 VAL A1069 9.368 126.697 175.845 1.00 88.52 C
ANISOU 2832 CG2 VAL A1069 8889 6870 17876 577 303 332 C
ATOM 2833 N GLY A1070 11.194 130.787 174.656 1.00 87.23 N
ANISOU 2833 N GLY A1070 7556 6200 19387 576 194 166 N
ATOM 2834 CA GLY A1070 11.432 132.222 174.537 1.00 88.44 C
ANISOU 2834 CA GLY A1070 7282 6095 20224 548 238 72 C
ATOM 2835 C GLY A1070 11.454 132.693 173.097 1.00 90.54 C
ANISOU 2835 C GLY A1070 7178 6286 20937 570 250 549 C
ATOM 2836 O GLY A1070 10.820 133.701 172.775 1.00 91.68 O
ANISOU 2836 O GLY A1070 6954 6189 21690 513 377 657 O
ATOM 2837 N GLN A1071 12.154 131.944 172.213 1.00 84.78 N
ANISOU 2837 N GLN A1071 6543 5755 19915 634 138 853 N
ATOM 2838 CA GLN A1071 12.250 132.247 170.780 1.00 84.50 C
ANISOU 2838 CA GLN A1071 6261 5740 20104 616 166 1331 C
ATOM 2839 C GLN A1071 10.911 132.034 170.076 1.00 88.20 C
ANISOU 2839 C GLN A1071 6757 6258 20498 518 223 1643 C
ATOM 2840 O GLN A1071 10.597 132.796 169.157 1.00 89.37 O
ANISOU 2840 O GLN A1071 6594 6324 21038 440 223 2036 O
ATOM 2841 CB GLN A1071 13.335 131.413 170.097 1.00 84.91 C
ANISOU 2841 CB GLN A1071 6462 5991 19810 683 123 1475 C
ATOM 2842 CG GLN A1071 14.751 131.943 170.297 1.00101.31 C
ANISOU 2842 CG GLN A1071 8306 7936 22252 764 61 1371 C
ATOM 2843 CD GLN A1071 15.801 130.957 169.839 1.00116.96 C
ANISOU 2843 CD GLN A1071 10433 10050 23955 839 69 1435 C
ATOM 2844 OE1 GLN A1071 15.713 129.747 170.085 1.00109.01 O
ANISOU 2844 OE1 GLN A1071 9760 9190 22468 867 33 1329 O
ATOM 2845 NE2 GLN A1071 16.834 131.459 169.179 1.00109.98 N
ANISOU 2845 NE2 GLN A1071 9260 9071 23459 875 153 1611 N
ATOM 2846 N ILE A1072 10.124 131.006 170.503 1.00 83.08 N
ANISOU 2846 N ILE A1072 6451 5724 19391 509 238 1515 N
ATOM 2847 CA ILE A1072 8.787 130.725 169.954 1.00 82.32 C
ANISOU 2847 CA ILE A1072 6367 5630 19281 409 249 1777 C
ATOM 2848 C ILE A1072 7.895 131.915 170.314 1.00 89.09 C
ANISOU 2848 C ILE A1072 6837 6151 20864 345 354 1778 C
ATOM 2849 O ILE A1072 7.204 132.428 169.439 1.00 90.08 O
ANISOU 2849 O ILE A1072 6676 6171 21379 244 285 2197 O
ATOM 2850 CB ILE A1072 8.175 129.359 170.409 1.00 83.21 C
ANISOU 2850 CB ILE A1072 6881 5880 18854 424 265 1625 C
ATOM 2851 CG1 ILE A1072 9.057 128.164 169.983 1.00 81.86 C
ANISOU 2851 CG1 ILE A1072 7021 5972 18110 484 183 1624 C
ATOM 2852 CG2 ILE A1072 6.755 129.180 169.848 1.00 83.77 C
ANISOU 2852 CG2 ILE A1072 6886 5884 19060 310 241 1900 C
ATOM 2853 CD1 ILE A1072 8.918 126.886 170.865 1.00 85.06 C
ANISOU 2853 CD1 ILE A1072 7783 6454 18082 546 199 1384 C
ATOM 2854 N ASP A1073 7.971 132.389 171.583 1.00 87.52 N
ANISOU 2854 N ASP A1073 6613 5769 20870 382 514 1310 N
ATOM 2855 CA ASP A1073 7.233 133.551 172.089 1.00 90.54 C
ANISOU 2855 CA ASP A1073 6611 5768 22023 321 714 1160 C
ATOM 2856 C ASP A1073 7.538 134.797 171.249 1.00 97.65 C
ANISOU 2856 C ASP A1073 6976 6449 23679 290 636 1504 C
ATOM 2857 O ASP A1073 6.620 135.553 170.938 1.00100.21 O
ANISOU 2857 O ASP A1073 6884 6462 24730 209 701 1745 O
ATOM 2858 CB ASP A1073 7.557 133.817 173.572 1.00 93.93 C
ANISOU 2858 CB ASP A1073 7191 6110 22388 336 901 505 C
ATOM 2859 CG ASP A1073 6.998 132.805 174.557 1.00104.04 C
ANISOU 2859 CG ASP A1073 8941 7540 23047 322 1056 201 C
ATOM 2860 OD1 ASP A1073 5.850 132.353 174.359 1.00103.96 O
ANISOU 2860 OD1 ASP A1073 8941 7468 23089 285 1186 384 O
ATOM 2861 OD2 ASP A1073 7.681 132.518 175.563 1.00111.32 O
ANISOU 2861 OD2 ASP A1073 10197 8618 23482 331 1039 -201 O
ATOM 2862 N ASP A1074 8.816 134.984 170.856 1.00 94.12 N
ANISOU 2862 N ASP A1074 6502 6132 23128 350 499 1581 N
ATOM 2863 CA ASP A1074 9.265 136.093 170.012 1.00 96.13 C
ANISOU 2863 CA ASP A1074 6265 6208 24051 324 436 1973 C
ATOM 2864 C ASP A1074 8.668 135.969 168.605 1.00 99.73 C
ANISOU 2864 C ASP A1074 6622 6788 24483 217 288 2688 C
ATOM 2865 O ASP A1074 8.247 136.974 168.033 1.00102.42 O
ANISOU 2865 O ASP A1074 6475 6869 25570 131 248 3110 O
ATOM 2866 CB ASP A1074 10.807 136.140 169.942 1.00 97.93 C
ANISOU 2866 CB ASP A1074 6528 6558 24122 416 360 1886 C
ATOM 2867 CG ASP A1074 11.532 136.411 171.255 1.00110.61 C
ANISOU 2867 CG ASP A1074 8181 8032 25815 482 386 1234 C
ATOM 2868 OD1 ASP A1074 10.849 136.649 172.280 1.00112.83 O
ANISOU 2868 OD1 ASP A1074 8495 8140 26236 440 519 788 O
ATOM 2869 OD2 ASP A1074 12.784 136.386 171.257 1.00115.99 O
ANISOU 2869 OD2 ASP A1074 8866 8775 26430 555 275 1165 O
ATOM 2870 N ALA A1075 8.612 134.735 168.067 1.00 93.67 N
ANISOU 2870 N ALA A1075 6309 6403 22878 200 185 2822 N
ATOM 2871 CA ALA A1075 8.061 134.433 166.745 1.00 94.25 C
ANISOU 2871 CA ALA A1075 6418 6677 22714 53 -2 3425 C
ATOM 2872 C ALA A1075 6.538 134.580 166.726 1.00 99.59 C
ANISOU 2872 C ALA A1075 6899 7133 23806 -63 -90 3639 C
ATOM 2873 O ALA A1075 5.986 134.971 165.697 1.00101.72 O
ANISOU 2873 O ALA A1075 6937 7394 24319 -225 -313 4250 O
ATOM 2874 CB ALA A1075 8.453 133.025 166.322 1.00 92.70 C
ANISOU 2874 CB ALA A1075 6773 6905 21543 62 -44 3347 C
ATOM 2875 N LEU A1076 5.869 134.271 167.864 1.00 95.15 N
ANISOU 2875 N LEU A1076 6421 6386 23346 3 84 3168 N
ATOM 2876 CA LEU A1076 4.416 134.361 168.041 1.00 96.77 C
ANISOU 2876 CA LEU A1076 6407 6299 24062 -84 95 3279 C
ATOM 2877 C LEU A1076 3.933 135.802 167.927 1.00105.70 C
ANISOU 2877 C LEU A1076 6856 6951 26353 -154 121 3563 C
ATOM 2878 O LEU A1076 2.899 136.043 167.305 1.00107.38 O
ANISOU 2878 O LEU A1076 6751 6967 27082 -290 -71 4062 O
ATOM 2879 CB LEU A1076 3.977 133.772 169.394 1.00 95.29 C
ANISOU 2879 CB LEU A1076 6472 6013 23719 6 398 2660 C
ATOM 2880 CG LEU A1076 3.394 132.356 169.382 1.00 97.43 C
ANISOU 2880 CG LEU A1076 7183 6520 23315 -3 336 2631 C
ATOM 2881 CD1 LEU A1076 3.199 131.850 170.793 1.00 96.69 C
ANISOU 2881 CD1 LEU A1076 7359 6367 23011 86 676 2050 C
ATOM 2882 CD2 LEU A1076 2.064 132.298 168.637 1.00101.29 C
ANISOU 2882 CD2 LEU A1076 7420 6833 24232 -151 134 3112 C
ATOM 2883 N LYS A1077 4.692 136.755 168.512 1.00104.67 N
ANISOU 2883 N LYS A1077 6467 6602 26701 -71 323 3260 N
ATOM 2884 CA LYS A1077 4.404 138.190 168.464 1.00109.23 C
ANISOU 2884 CA LYS A1077 6338 6665 28501 -121 390 3465 C
ATOM 2885 C LYS A1077 4.573 138.719 167.039 1.00116.13 C
ANISOU 2885 C LYS A1077 6897 7607 29619 -242 36 4333 C
ATOM 2886 O LYS A1077 3.791 139.568 166.619 1.00119.35 O
ANISOU 2886 O LYS A1077 6722 7622 31005 -355 -73 4828 O
ATOM 2887 CB LYS A1077 5.294 138.967 169.451 1.00112.53 C
ANISOU 2887 CB LYS A1077 6616 6866 29275 -14 672 2844 C
ATOM 2888 CG LYS A1077 4.611 139.280 170.788 1.00127.97 C
ANISOU 2888 CG LYS A1077 8468 8425 31731 -2 1086 2143 C
ATOM 2889 CD LYS A1077 4.864 138.220 171.873 1.00135.01 C
ANISOU 2889 CD LYS A1077 10050 9649 31600 68 1262 1460 C
ATOM 2890 CE LYS A1077 3.768 137.177 171.968 1.00142.92 C
ANISOU 2890 CE LYS A1077 11355 10762 32187 36 1323 1521 C
ATOM 2891 NZ LYS A1077 4.148 136.049 172.860 1.00146.25 N
ANISOU 2891 NZ LYS A1077 12459 11567 31542 100 1421 1022 N
ATOM 2892 N LEU A1078 5.558 138.187 166.288 1.00111.36 N
ANISOU 2892 N LEU A1078 6675 7495 28141 -238 -129 4545 N
ATOM 2893 CA LEU A1078 5.808 138.556 164.894 1.00113.99 C
ANISOU 2893 CA LEU A1078 6848 8011 28452 -388 -422 5368 C
ATOM 2894 C LEU A1078 4.737 137.965 163.961 1.00120.06 C
ANISOU 2894 C LEU A1078 7751 8974 28893 -595 -787 5944 C
ATOM 2895 O LEU A1078 4.406 138.584 162.947 1.00123.26 O
ANISOU 2895 O LEU A1078 7825 9343 29664 -788 -1094 6734 O
ATOM 2896 CB LEU A1078 7.201 138.084 164.461 1.00112.12 C
ANISOU 2896 CB LEU A1078 7021 8227 27351 -326 -371 5306 C
ATOM 2897 N ALA A1079 4.196 136.772 164.313 1.00114.73 N
ANISOU 2897 N ALA A1079 7545 8493 27552 -574 -787 5573 N
ATOM 2898 CA ALA A1079 3.178 136.049 163.541 1.00116.06 C
ANISOU 2898 CA ALA A1079 7890 8840 27366 -770 -1154 5989 C
ATOM 2899 C ALA A1079 1.804 136.732 163.593 1.00124.51 C
ANISOU 2899 C ALA A1079 8359 9385 29563 -884 -1329 6378 C
ATOM 2900 O ALA A1079 1.149 136.833 162.554 1.00127.66 O
ANISOU 2900 O ALA A1079 8607 9839 30060 -1122 -1795 7110 O
ATOM 2901 CB ALA A1079 3.061 134.616 164.035 1.00112.80 C
ANISOU 2901 CB ALA A1079 8077 8697 26084 -684 -1050 5423 C
ATOM 2902 N ASN A1080 1.363 137.191 164.787 1.00121.55 N
ANISOU 2902 N ASN A1080 7642 8495 30047 -739 -958 5893 N
ATOM 2903 CA ASN A1080 0.065 137.859 164.944 1.00125.72 C
ANISOU 2903 CA ASN A1080 7523 8416 31828 -827 -1009 6182 C
ATOM 2904 C ASN A1080 0.136 139.354 164.548 1.00134.25 C
ANISOU 2904 C ASN A1080 7843 9063 34103 -899 -1097 6734 C
ATOM 2905 O ASN A1080 -0.905 140.015 164.471 1.00138.68 O
ANISOU 2905 O ASN A1080 7755 9074 35864 -1003 -1212 7139 O
ATOM 2906 CB ASN A1080 -0.514 137.681 166.361 1.00127.08 C
ANISOU 2906 CB ASN A1080 7659 8201 32423 -674 -485 5407 C
ATOM 2907 CG ASN A1080 0.424 137.958 167.512 1.00151.75 C
ANISOU 2907 CG ASN A1080 10942 11301 35415 -477 33 4595 C
ATOM 2908 OD1 ASN A1080 1.027 139.034 167.628 1.00148.88 O
ANISOU 2908 OD1 ASN A1080 10194 10699 35676 -442 158 4566 O
ATOM 2909 ND2 ASN A1080 0.517 137.003 168.427 1.00140.55 N
ANISOU 2909 ND2 ASN A1080 10069 10097 33238 -364 325 3929 N
ATOM 2910 N GLU A1081 1.350 139.866 164.251 1.00129.67 N
ANISOU 2910 N GLU A1081 7297 8695 33278 -852 -1056 6804 N
ATOM 2911 CA GLU A1081 1.570 141.240 163.798 1.00133.85 C
ANISOU 2911 CA GLU A1081 7123 8853 34883 -919 -1147 7382 C
ATOM 2912 C GLU A1081 1.603 141.306 162.254 1.00140.63 C
ANISOU 2912 C GLU A1081 8024 10102 35308 -1173 -1722 8422 C
ATOM 2913 O GLU A1081 1.991 142.329 161.685 1.00140.54 O
ANISOU 2913 O GLU A1081 7987 10264 35150 -1223 -1752 8643 O
ATOM 2914 CB GLU A1081 2.860 141.815 164.403 1.00133.55 C
ANISOU 2914 CB GLU A1081 7061 8777 34906 -730 -755 6854 C
ATOM 2915 CG GLU A1081 2.643 142.537 165.724 1.00142.25 C
ANISOU 2915 CG GLU A1081 7912 9404 36731 -585 -265 6000 C
ATOM 2916 CD GLU A1081 3.886 142.792 166.559 1.00152.12 C
ANISOU 2916 CD GLU A1081 9707 11040 37051 -406 87 5045 C
ATOM 2917 OE1 GLU A1081 4.988 142.931 165.981 1.00141.93 O
ANISOU 2917 OE1 GLU A1081 7958 9540 36427 -385 -34 5608 O
ATOM 2918 OE2 GLU A1081 3.751 142.866 167.802 1.00147.53 O
ANISOU 2918 OE2 GLU A1081 8836 9912 37306 -306 483 4380 O
ATOM 2919 N GLY A1082 1.205 140.208 161.604 1.00136.31 N
ANISOU 2919 N GLY A1082 7998 10024 33770 -1324 -2077 8651 N
ATOM 2920 CA GLY A1082 1.127 140.084 160.152 1.00140.14 C
ANISOU 2920 CA GLY A1082 8642 10948 33655 -1628 -2654 9581 C
ATOM 2921 C GLY A1082 2.420 139.882 159.391 1.00144.05 C
ANISOU 2921 C GLY A1082 9639 12069 33023 -1671 -2606 9712 C
ATOM 2922 O GLY A1082 2.387 139.362 158.272 1.00146.04 O
ANISOU 2922 O GLY A1082 10311 12853 32324 -1936 -2995 10229 O
ATOM 2923 N LYS A1083 3.560 140.312 159.969 1.00138.64 N
ANISOU 2923 N LYS A1083 8902 11309 32465 -1436 -2126 9247 N
ATOM 2924 CA LYS A1083 4.882 140.202 159.351 1.00138.17 C
ANISOU 2924 CA LYS A1083 9222 11739 31537 -1439 -1969 9325 C
ATOM 2925 C LYS A1083 5.314 138.728 159.290 1.00138.04 C
ANISOU 2925 C LYS A1083 10074 12315 30058 -1405 -1848 8742 C
ATOM 2926 O LYS A1083 5.931 138.207 160.226 1.00132.45 O
ANISOU 2926 O LYS A1083 9622 11601 29102 -1146 -1461 7905 O
ATOM 2927 CB LYS A1083 5.906 141.073 160.096 1.00139.21 C
ANISOU 2927 CB LYS A1083 8969 11519 32405 -1188 -1525 8948 C
ATOM 2928 N VAL A1084 4.929 138.058 158.180 1.00137.61 N
ANISOU 2928 N VAL A1084 10453 12752 29081 -1697 -2222 9206 N
ATOM 2929 CA VAL A1084 5.203 136.647 157.875 1.00134.92 C
ANISOU 2929 CA VAL A1084 10909 12969 27385 -1741 -2165 8754 C
ATOM 2930 C VAL A1084 6.720 136.426 157.821 1.00136.87 C
ANISOU 2930 C VAL A1084 11482 13508 27016 -1597 -1677 8382 C
ATOM 2931 O VAL A1084 7.210 135.496 158.454 1.00131.60 O
ANISOU 2931 O VAL A1084 11199 12940 25861 -1396 -1373 7612 O
ATOM 2932 CB VAL A1084 4.508 136.181 156.558 1.00144.00 C
ANISOU 2932 CB VAL A1084 12407 14575 27732 -2155 -2703 9393 C
ATOM 2933 CG1 VAL A1084 4.738 134.692 156.298 1.00141.62 C
ANISOU 2933 CG1 VAL A1084 12899 14782 26128 -2203 -2606 8808 C
ATOM 2934 CG2 VAL A1084 3.014 136.490 156.573 1.00146.63 C
ANISOU 2934 CG2 VAL A1084 12309 14545 28858 -2311 -3255 9865 C
ATOM 2935 N LYS A1085 7.451 137.304 157.098 1.00137.79 N
ANISOU 2935 N LYS A1085 11385 13705 27264 -1699 -1600 8967 N
ATOM 2936 CA LYS A1085 8.907 137.253 156.935 1.00137.02 C
ANISOU 2936 CA LYS A1085 11485 13817 26759 -1585 -1118 8742 C
ATOM 2937 C LYS A1085 9.644 137.369 158.276 1.00135.32 C
ANISOU 2937 C LYS A1085 11043 13201 27173 -1192 -729 7968 C
ATOM 2938 O LYS A1085 10.661 136.700 158.461 1.00132.33 O
ANISOU 2938 O LYS A1085 11003 13001 26275 -1047 -371 7447 O
ATOM 2939 CB LYS A1085 9.377 138.361 155.984 1.00145.69 C
ANISOU 2939 CB LYS A1085 12256 14967 28131 -1773 -1126 9632 C
ATOM 2940 N GLU A1086 9.118 138.191 159.212 1.00130.72 N
ANISOU 2940 N GLU A1086 9891 12065 27710 -1045 -808 7876 N
ATOM 2941 CA GLU A1086 9.695 138.403 160.544 1.00126.56 C
ANISOU 2941 CA GLU A1086 9151 11153 27783 -728 -510 7135 C
ATOM 2942 C GLU A1086 9.561 137.164 161.439 1.00125.39 C
ANISOU 2942 C GLU A1086 9493 11116 27032 -573 -417 6312 C
ATOM 2943 O GLU A1086 10.340 137.020 162.380 1.00122.08 O
ANISOU 2943 O GLU A1086 9110 10567 26708 -347 -175 5690 O
ATOM 2944 CB GLU A1086 9.047 139.609 161.233 1.00129.35 C
ANISOU 2944 CB GLU A1086 8794 10892 29461 -673 -589 7227 C
ATOM 2945 N ALA A1087 8.582 136.282 161.152 1.00121.43 N
ANISOU 2945 N ALA A1087 9346 10839 25951 -708 -644 6346 N
ATOM 2946 CA ALA A1087 8.342 135.052 161.911 1.00116.85 C
ANISOU 2946 CA ALA A1087 9212 10360 24824 -585 -574 5669 C
ATOM 2947 C ALA A1087 8.963 133.829 161.219 1.00119.76 C
ANISOU 2947 C ALA A1087 10190 11226 24086 -644 -484 5518 C
ATOM 2948 O ALA A1087 9.556 132.992 161.898 1.00115.58 O
ANISOU 2948 O ALA A1087 9946 10745 23224 -462 -272 4918 O
ATOM 2949 CB ALA A1087 6.849 134.842 162.113 1.00117.73 C
ANISOU 2949 CB ALA A1087 9259 10314 25159 -682 -841 5753 C
ATOM 2950 N GLN A1088 8.834 133.741 159.873 1.00120.57 N
ANISOU 2950 N GLN A1088 10483 11687 23642 -918 -644 6065 N
ATOM 2951 CA GLN A1088 9.347 132.663 159.016 1.00121.56 C
ANISOU 2951 CA GLN A1088 11187 12294 22708 -1047 -519 5940 C
ATOM 2952 C GLN A1088 10.871 132.523 159.132 1.00125.20 C
ANISOU 2952 C GLN A1088 11730 12805 23037 -870 -49 5603 C
ATOM 2953 O GLN A1088 11.372 131.399 159.187 1.00123.13 O
ANISOU 2953 O GLN A1088 11867 12715 22201 -805 171 5110 O
ATOM 2954 CB GLN A1088 8.946 132.917 157.553 1.00128.88 C
ANISOU 2954 CB GLN A1088 12249 13583 23136 -1429 -782 6665 C
ATOM 2955 CG GLN A1088 8.918 131.670 156.673 1.00146.20 C
ANISOU 2955 CG GLN A1088 15102 16272 24176 -1655 -779 6474 C
ATOM 2956 CD GLN A1088 8.038 131.809 155.445 1.00171.97 C
ANISOU 2956 CD GLN A1088 18535 19871 26934 -2086 -1252 7145 C
ATOM 2957 OE1 GLN A1088 7.464 132.867 155.154 1.00171.23 O
ANISOU 2957 OE1 GLN A1088 18038 19648 27374 -2230 -1610 7872 O
ATOM 2958 NE2 GLN A1088 7.907 130.726 154.693 1.00166.16 N
ANISOU 2958 NE2 GLN A1088 18392 19561 25180 -2323 -1293 6915 N
ATOM 2959 N ALA A1089 11.597 133.661 159.170 1.00123.85 N
ANISOU 2959 N ALA A1089 11127 12427 23502 -793 99 5882 N
ATOM 2960 CA ALA A1089 13.053 133.702 159.307 1.00123.53 C
ANISOU 2960 CA ALA A1089 11037 12340 23557 -622 518 5632 C
ATOM 2961 C ALA A1089 13.470 133.414 160.754 1.00123.32 C
ANISOU 2961 C ALA A1089 10908 11986 23963 -306 590 4947 C
ATOM 2962 O ALA A1089 14.446 132.692 160.968 1.00122.00 O
ANISOU 2962 O ALA A1089 10926 11858 23570 -173 852 4538 O
ATOM 2963 CB ALA A1089 13.587 135.054 158.859 1.00127.91 C
ANISOU 2963 CB ALA A1089 11116 12744 24742 -664 606 6210 C
ATOM 2964 N ALA A1090 12.711 133.949 161.743 1.00117.95 N
ANISOU 2964 N ALA A1090 9938 10980 23896 -212 359 4826 N
ATOM 2965 CA ALA A1090 12.954 133.741 163.177 1.00114.25 C
ANISOU 2965 CA ALA A1090 9422 10243 23744 28 380 4197 C
ATOM 2966 C ALA A1090 12.638 132.292 163.597 1.00116.17 C
ANISOU 2966 C ALA A1090 10156 10670 23314 75 359 3746 C
ATOM 2967 O ALA A1090 13.060 131.861 164.672 1.00113.35 O
ANISOU 2967 O ALA A1090 9867 10184 23015 251 391 3258 O
ATOM 2968 CB ALA A1090 12.129 134.719 163.998 1.00114.71 C
ANISOU 2968 CB ALA A1090 9079 9930 24574 58 220 4184 C
ATOM 2969 N ALA A1091 11.894 131.550 162.748 1.00114.05 N
ANISOU 2969 N ALA A1091 10215 10692 22425 -104 271 3934 N
ATOM 2970 CA ALA A1091 11.554 130.144 162.966 1.00111.93 C
ANISOU 2970 CA ALA A1091 10381 10582 21564 -86 257 3559 C
ATOM 2971 C ALA A1091 12.780 129.267 162.721 1.00116.59 C
ANISOU 2971 C ALA A1091 11215 11314 21769 -9 541 3272 C
ATOM 2972 O ALA A1091 12.989 128.296 163.444 1.00113.85 O
ANISOU 2972 O ALA A1091 11054 10918 21283 127 580 2847 O
ATOM 2973 CB ALA A1091 10.417 129.729 162.048 1.00114.38 C
ANISOU 2973 CB ALA A1091 10915 11125 21420 -333 42 3851 C
ATOM 2974 N GLU A1092 13.609 129.635 161.722 1.00116.90 N
ANISOU 2974 N GLU A1092 11215 11494 21709 -100 768 3532 N
ATOM 2975 CA GLU A1092 14.838 128.920 161.367 1.00118.11 C
ANISOU 2975 CA GLU A1092 11523 11723 21630 -43 1138 3285 C
ATOM 2976 C GLU A1092 15.953 129.189 162.397 1.00120.09 C
ANISOU 2976 C GLU A1092 11467 11642 22519 220 1227 3020 C
ATOM 2977 O GLU A1092 16.957 128.476 162.407 1.00120.27 O
ANISOU 2977 O GLU A1092 11549 11616 22532 317 1482 2754 O
ATOM 2978 CB GLU A1092 15.292 129.287 159.946 1.00124.49 C
ANISOU 2978 CB GLU A1092 12397 12792 22112 -259 1415 3672 C
ATOM 2979 CG GLU A1092 14.384 128.712 158.868 1.00139.52 C
ANISOU 2979 CG GLU A1092 14728 15089 23195 -564 1322 3828 C
ATOM 2980 CD GLU A1092 14.671 129.131 157.438 1.00171.04 C
ANISOU 2980 CD GLU A1092 18865 19422 26702 -854 1545 4273 C
ATOM 2981 OE1 GLU A1092 15.014 130.315 157.213 1.00171.14 O
ANISOU 2981 OE1 GLU A1092 18537 19361 27128 -871 1581 4757 O
ATOM 2982 OE2 GLU A1092 14.496 128.283 156.533 1.00169.50 O
ANISOU 2982 OE2 GLU A1092 19134 19573 25694 -1092 1673 4149 O
ATOM 2983 N GLN A1093 15.755 130.194 163.279 1.00114.84 N
ANISOU 2983 N GLN A1093 10461 10723 22449 318 1001 3069 N
ATOM 2984 CA GLN A1093 16.672 130.551 164.366 1.00113.45 C
ANISOU 2984 CA GLN A1093 10004 10236 22868 525 963 2798 C
ATOM 2985 C GLN A1093 16.611 129.484 165.472 1.00114.93 C
ANISOU 2985 C GLN A1093 10426 10373 22869 651 810 2343 C
ATOM 2986 O GLN A1093 17.588 129.295 166.198 1.00114.86 O
ANISOU 2986 O GLN A1093 10305 10180 23156 794 780 2103 O
ATOM 2987 CB GLN A1093 16.313 131.936 164.927 1.00114.77 C
ANISOU 2987 CB GLN A1093 9776 10160 23670 539 774 2927 C
ATOM 2988 CG GLN A1093 17.456 132.654 165.640 1.00126.49 C
ANISOU 2988 CG GLN A1093 10883 11327 25849 686 764 2759 C
ATOM 2989 CD GLN A1093 17.023 133.971 166.246 1.00141.03 C
ANISOU 2989 CD GLN A1093 12343 12897 28345 682 597 2780 C
ATOM 2990 OE1 GLN A1093 16.343 134.792 165.616 1.00137.26 O
ANISOU 2990 OE1 GLN A1093 11658 12401 28095 566 612 3178 O
ATOM 2991 NE2 GLN A1093 17.437 134.218 167.478 1.00130.30 N
ANISOU 2991 NE2 GLN A1093 10865 11302 27343 788 424 2354 N
ATOM 2992 N LEU A1094 15.461 128.780 165.579 1.00109.31 N
ANISOU 2992 N LEU A1094 10020 9813 21700 583 689 2275 N
ATOM 2993 CA LEU A1094 15.208 127.705 166.544 1.00106.71 C
ANISOU 2993 CA LEU A1094 9938 9465 21143 671 560 1935 C
ATOM 2994 C LEU A1094 16.031 126.448 166.215 1.00110.11 C
ANISOU 2994 C LEU A1094 10545 9940 21353 723 736 1769 C
ATOM 2995 O LEU A1094 16.271 125.633 167.108 1.00108.55 O
ANISOU 2995 O LEU A1094 10439 9646 21160 831 622 1534 O
ATOM 2996 CB LEU A1094 13.707 127.355 166.580 1.00105.54 C
ANISOU 2996 CB LEU A1094 10007 9429 20663 569 436 1973 C
ATOM 2997 CG LEU A1094 12.769 128.419 167.159 1.00110.04 C
ANISOU 2997 CG LEU A1094 10380 9864 21565 534 293 2055 C
ATOM 2998 CD1 LEU A1094 11.450 128.446 166.422 1.00110.54 C
ANISOU 2998 CD1 LEU A1094 10500 10029 21470 368 224 2332 C
ATOM 2999 CD2 LEU A1094 12.523 128.182 168.627 1.00111.58 C
ANISOU 2999 CD2 LEU A1094 10661 9932 21803 630 194 1717 C
ATOM 3000 N LYS A1095 16.457 126.300 164.939 1.00108.30 N
ANISOU 3000 N LYS A1095 10355 9844 20949 628 1035 1901 N
ATOM 3001 CA LYS A1095 17.267 125.179 164.444 1.00109.45 C
ANISOU 3001 CA LYS A1095 10625 9990 20970 651 1327 1704 C
ATOM 3002 C LYS A1095 18.674 125.187 165.050 1.00113.59 C
ANISOU 3002 C LYS A1095 10853 10218 22089 831 1386 1582 C
ATOM 3003 O LYS A1095 19.189 124.127 165.398 1.00113.37 O
ANISOU 3003 O LYS A1095 10858 10049 22168 922 1427 1361 O
ATOM 3004 CB LYS A1095 17.385 125.213 162.908 1.00115.34 C
ANISOU 3004 CB LYS A1095 11502 10971 21352 459 1700 1854 C
ATOM 3005 CG LYS A1095 16.085 125.012 162.149 1.00128.77 C
ANISOU 3005 CG LYS A1095 13528 12983 22416 231 1593 1976 C
ATOM 3006 CD LYS A1095 16.333 124.956 160.650 1.00142.74 C
ANISOU 3006 CD LYS A1095 15500 15032 23704 -4 1958 2090 C
ATOM 3007 CE LYS A1095 15.069 124.709 159.868 1.00154.56 C
ANISOU 3007 CE LYS A1095 17341 16853 24532 -274 1759 2215 C
ATOM 3008 NZ LYS A1095 15.333 124.625 158.409 1.00169.44 N
ANISOU 3008 NZ LYS A1095 19503 19071 25804 -557 2100 2302 N
ATOM 3009 N THR A1096 19.298 126.380 165.150 1.00110.87 N
ANISOU 3009 N THR A1096 10174 9738 22212 874 1370 1751 N
ATOM 3010 CA THR A1096 20.656 126.563 165.681 1.00111.95 C
ANISOU 3010 CA THR A1096 9960 9556 23021 1027 1370 1677 C
ATOM 3011 C THR A1096 20.718 126.314 167.195 1.00113.62 C
ANISOU 3011 C THR A1096 10140 9594 23437 1146 899 1483 C
ATOM 3012 O THR A1096 21.757 125.876 167.691 1.00114.56 O
ANISOU 3012 O THR A1096 10067 9462 23998 1256 818 1388 O
ATOM 3013 CB THR A1096 21.202 127.961 165.343 1.00120.24 C
ANISOU 3013 CB THR A1096 10642 10495 24551 1020 1460 1924 C
ATOM 3014 OG1 THR A1096 20.246 128.956 165.715 1.00117.46 O
ANISOU 3014 OG1 THR A1096 10265 10214 24150 962 1180 2046 O
ATOM 3015 CG2 THR A1096 21.572 128.108 163.871 1.00121.39 C
ANISOU 3015 CG2 THR A1096 10779 10771 24573 904 1993 2155 C
ATOM 3016 N THR A1097 19.616 126.588 167.919 1.00107.47 N
ANISOU 3016 N THR A1097 9543 8941 22348 1104 598 1444 N
ATOM 3017 CA THR A1097 19.535 126.407 169.372 1.00106.19 C
ANISOU 3017 CA THR A1097 9443 8692 22212 1163 182 1262 C
ATOM 3018 C THR A1097 19.268 124.946 169.753 1.00108.30 C
ANISOU 3018 C THR A1097 9994 9013 22144 1188 113 1165 C
ATOM 3019 O THR A1097 19.808 124.486 170.761 1.00108.56 O
ANISOU 3019 O THR A1097 10005 8914 22331 1251 -189 1092 O
ATOM 3020 CB THR A1097 18.478 127.326 169.988 1.00113.96 C
ANISOU 3020 CB THR A1097 10494 9757 23047 1091 4 1222 C
ATOM 3021 OG1 THR A1097 17.247 127.173 169.281 1.00113.29 O
ANISOU 3021 OG1 THR A1097 10619 9878 22547 995 177 1339 O
ATOM 3022 CG2 THR A1097 18.911 128.785 169.997 1.00114.64 C
ANISOU 3022 CG2 THR A1097 10217 9681 23660 1086 -28 1263 C
ATOM 3023 N ARG A1098 18.441 124.220 168.967 1.00102.99 N
ANISOU 3023 N ARG A1098 9569 8518 21043 1122 348 1186 N
ATOM 3024 CA ARG A1098 18.140 122.815 169.253 1.00102.01 C
ANISOU 3024 CA ARG A1098 9669 8402 20689 1144 313 1096 C
ATOM 3025 C ARG A1098 19.361 121.923 168.969 1.00106.91 C
ANISOU 3025 C ARG A1098 10111 8794 21715 1230 466 1044 C
ATOM 3026 O ARG A1098 19.564 120.943 169.681 1.00107.26 O
ANISOU 3026 O ARG A1098 10177 8705 21873 1292 282 1017 O
ATOM 3027 CB ARG A1098 16.884 122.312 168.504 1.00101.52 C
ANISOU 3027 CB ARG A1098 9891 8554 20128 1032 484 1096 C
ATOM 3028 CG ARG A1098 16.966 122.278 166.979 1.00113.84 C
ANISOU 3028 CG ARG A1098 11480 10233 21542 928 859 1118 C
ATOM 3029 CD ARG A1098 15.831 121.472 166.384 1.00123.54 C
ANISOU 3029 CD ARG A1098 13009 11637 22293 803 923 1061 C
ATOM 3030 NE ARG A1098 16.326 120.372 165.556 1.00134.28 N
ANISOU 3030 NE ARG A1098 14448 12962 23611 770 1242 861 N
ATOM 3031 CZ ARG A1098 15.991 120.175 164.285 1.00150.31 C
ANISOU 3031 CZ ARG A1098 16671 15193 25247 589 1500 799 C
ATOM 3032 NH1 ARG A1098 15.145 120.999 163.678 1.00137.42 N
ANISOU 3032 NH1 ARG A1098 15155 13817 23243 423 1405 1012 N
ATOM 3033 NH2 ARG A1098 16.492 119.148 163.612 1.00138.98 N
ANISOU 3033 NH2 ARG A1098 15310 13692 23804 548 1845 521 N
ATOM 3034 N ASN A1099 20.187 122.290 167.969 1.00104.02 N
ANISOU 3034 N ASN A1099 9536 8354 21634 1228 817 1060 N
ATOM 3035 CA ASN A1099 21.394 121.547 167.601 1.00106.21 C
ANISOU 3035 CA ASN A1099 9575 8350 22431 1305 1078 985 C
ATOM 3036 C ASN A1099 22.542 121.803 168.584 1.00110.49 C
ANISOU 3036 C ASN A1099 9752 8567 23661 1429 736 1059 C
ATOM 3037 O ASN A1099 23.465 120.990 168.662 1.00112.91 O
ANISOU 3037 O ASN A1099 9820 8559 24522 1511 794 1034 O
ATOM 3038 CB ASN A1099 21.834 121.907 166.176 1.00108.32 C
ANISOU 3038 CB ASN A1099 9771 8665 22721 1230 1650 975 C
ATOM 3039 CG ASN A1099 20.890 121.452 165.085 1.00130.16 C
ANISOU 3039 CG ASN A1099 12910 11741 24804 1063 1976 878 C
ATOM 3040 OD1 ASN A1099 20.277 120.377 165.147 1.00126.24 O
ANISOU 3040 OD1 ASN A1099 12639 11281 24045 1036 1950 713 O
ATOM 3041 ND2 ASN A1099 20.781 122.249 164.035 1.00121.25 N
ANISOU 3041 ND2 ASN A1099 11842 10833 23393 927 2272 999 N
ATOM 3042 N ALA A1100 22.480 122.919 169.336 1.00105.18 N
ANISOU 3042 N ALA A1100 9015 7940 23010 1427 363 1137 N
ATOM 3043 CA ALA A1100 23.515 123.319 170.290 1.00106.89 C
ANISOU 3043 CA ALA A1100 8908 7880 23825 1499 -56 1187 C
ATOM 3044 C ALA A1100 23.155 123.025 171.757 1.00110.28 C
ANISOU 3044 C ALA A1100 9531 8367 24004 1480 -664 1187 C
ATOM 3045 O ALA A1100 24.069 122.881 172.571 1.00112.56 O
ANISOU 3045 O ALA A1100 9597 8416 24753 1515 -1082 1256 O
ATOM 3046 CB ALA A1100 23.815 124.802 170.132 1.00107.88 C
ANISOU 3046 CB ALA A1100 8801 7979 24207 1483 -55 1224 C
ATOM 3047 N TYR A1101 21.853 122.954 172.104 1.00104.26 N
ANISOU 3047 N TYR A1101 9170 7909 22534 1403 -722 1134 N
ATOM 3048 CA TYR A1101 21.435 122.745 173.495 1.00104.32 C
ANISOU 3048 CA TYR A1101 9419 8019 22197 1350 -1212 1132 C
ATOM 3049 C TYR A1101 20.577 121.495 173.750 1.00106.34 C
ANISOU 3049 C TYR A1101 9994 8401 22008 1334 -1194 1191 C
ATOM 3050 O TYR A1101 20.744 120.866 174.797 1.00107.65 O
ANISOU 3050 O TYR A1101 10250 8537 22113 1315 -1591 1307 O
ATOM 3051 CB TYR A1101 20.629 123.956 173.993 1.00104.38 C
ANISOU 3051 CB TYR A1101 9595 8231 21833 1255 -1305 988 C
ATOM 3052 CG TYR A1101 21.389 125.258 174.107 1.00108.16 C
ANISOU 3052 CG TYR A1101 9767 8564 22764 1248 -1447 903 C
ATOM 3053 CD1 TYR A1101 22.058 125.597 175.280 1.00113.20 C
ANISOU 3053 CD1 TYR A1101 10351 9112 23548 1197 -1975 823 C
ATOM 3054 CD2 TYR A1101 21.348 126.202 173.086 1.00108.14 C
ANISOU 3054 CD2 TYR A1101 9547 8530 23013 1263 -1086 910 C
ATOM 3055 CE1 TYR A1101 22.721 126.817 175.410 1.00115.91 C
ANISOU 3055 CE1 TYR A1101 10391 9290 24361 1178 -2130 698 C
ATOM 3056 CE2 TYR A1101 22.006 127.425 173.203 1.00110.96 C
ANISOU 3056 CE2 TYR A1101 9577 8712 23871 1258 -1205 846 C
ATOM 3057 CZ TYR A1101 22.692 127.729 174.367 1.00121.80 C
ANISOU 3057 CZ TYR A1101 10867 9955 25456 1222 -1722 709 C
ATOM 3058 OH TYR A1101 23.343 128.933 174.485 1.00125.99 O
ANISOU 3058 OH TYR A1101 11047 10275 26548 1209 -1860 606 O
ATOM 3059 N ILE A1102 19.617 121.184 172.855 1.00100.14 N
ANISOU 3059 N ILE A1102 9385 7764 20900 1317 -784 1140 N
ATOM 3060 CA ILE A1102 18.645 120.103 173.059 1.00 98.90 C
ANISOU 3060 CA ILE A1102 9512 7710 20354 1292 -748 1176 C
ATOM 3061 C ILE A1102 19.124 118.729 172.525 1.00104.80 C
ANISOU 3061 C ILE A1102 10134 8241 21444 1360 -581 1217 C
ATOM 3062 O ILE A1102 19.170 117.779 173.309 1.00106.28 O
ANISOU 3062 O ILE A1102 10355 8329 21697 1380 -828 1361 O
ATOM 3063 CB ILE A1102 17.257 120.502 172.465 1.00 98.85 C
ANISOU 3063 CB ILE A1102 9739 7943 19877 1212 -474 1095 C
ATOM 3064 CG1 ILE A1102 16.707 121.771 173.156 1.00 98.27 C
ANISOU 3064 CG1 ILE A1102 9747 8006 19586 1143 -615 1037 C
ATOM 3065 CG2 ILE A1102 16.241 119.353 172.570 1.00 98.89 C
ANISOU 3065 CG2 ILE A1102 9987 8006 19580 1188 -412 1129 C
ATOM 3066 CD1 ILE A1102 15.817 122.628 172.304 1.00103.23 C
ANISOU 3066 CD1 ILE A1102 10379 8751 20093 1077 -354 1009 C
ATOM 3067 N GLN A1103 19.435 118.625 171.211 1.00101.39 N
ANISOU 3067 N GLN A1103 9567 7736 21221 1375 -141 1091 N
ATOM 3068 CA GLN A1103 19.824 117.400 170.495 1.00103.11 C
ANISOU 3068 CA GLN A1103 9667 7731 21781 1413 166 1004 C
ATOM 3069 C GLN A1103 20.899 116.554 171.204 1.00109.35 C
ANISOU 3069 C GLN A1103 10146 8144 23259 1512 -76 1150 C
ATOM 3070 O GLN A1103 20.811 115.326 171.151 1.00109.80 O
ANISOU 3070 O GLN A1103 10163 8013 23542 1536 13 1144 O
ATOM 3071 CB GLN A1103 20.289 117.726 169.071 1.00105.72 C
ANISOU 3071 CB GLN A1103 9886 8049 22235 1383 693 821 C
ATOM 3072 CG GLN A1103 19.817 116.706 168.043 1.00126.51 C
ANISOU 3072 CG GLN A1103 12668 10692 24709 1313 1122 587 C
ATOM 3073 CD GLN A1103 20.410 116.956 166.681 1.00151.73 C
ANISOU 3073 CD GLN A1103 15792 13887 27971 1246 1683 390 C
ATOM 3074 OE1 GLN A1103 21.583 116.661 166.421 1.00150.56 O
ANISOU 3074 OE1 GLN A1103 15327 13418 28463 1316 1960 310 O
ATOM 3075 NE2 GLN A1103 19.609 117.498 165.776 1.00144.13 N
ANISOU 3075 NE2 GLN A1103 15117 13277 26370 1091 1871 333 N
ATOM 3076 N LYS A1104 21.889 117.191 171.864 1.00107.50 N
ANISOU 3076 N LYS A1104 9660 7765 23422 1557 -415 1297 N
ATOM 3077 CA LYS A1104 22.957 116.486 172.588 1.00111.15 C
ANISOU 3077 CA LYS A1104 9775 7843 24614 1628 -764 1518 C
ATOM 3078 C LYS A1104 22.397 115.717 173.796 1.00114.75 C
ANISOU 3078 C LYS A1104 10434 8367 24799 1591 -1253 1781 C
ATOM 3079 O LYS A1104 22.737 114.546 173.974 1.00117.29 O
ANISOU 3079 O LYS A1104 10550 8384 25632 1636 -1322 1950 O
ATOM 3080 CB LYS A1104 24.055 117.460 173.038 1.00115.94 C
ANISOU 3080 CB LYS A1104 10082 8305 25665 1649 -1104 1621 C
ATOM 3081 N TYR A1105 21.531 116.368 174.609 1.00108.38 N
ANISOU 3081 N TYR A1105 10013 7936 23229 1498 -1543 1822 N
ATOM 3082 CA TYR A1105 20.891 115.781 175.793 1.00108.54 C
ANISOU 3082 CA TYR A1105 10308 8100 22830 1427 -1942 2078 C
ATOM 3083 C TYR A1105 19.804 114.792 175.374 1.00108.46 C
ANISOU 3083 C TYR A1105 10487 8136 22588 1433 -1594 2042 C
ATOM 3084 O TYR A1105 19.559 113.802 176.068 1.00109.89 O
ANISOU 3084 O TYR A1105 10715 8243 22795 1418 -1810 2320 O
ATOM 3085 CB TYR A1105 20.303 116.885 176.694 1.00108.89 C
ANISOU 3085 CB TYR A1105 10712 8521 22140 1305 -2215 2030 C
ATOM 3086 CG TYR A1105 19.650 116.382 177.965 1.00112.40 C
ANISOU 3086 CG TYR A1105 11502 9164 22041 1193 -2565 2283 C
ATOM 3087 CD1 TYR A1105 20.406 116.124 179.105 1.00118.99 C
ANISOU 3087 CD1 TYR A1105 12307 9950 22953 1112 -3189 2614 C
ATOM 3088 CD2 TYR A1105 18.265 116.268 178.061 1.00110.64 C
ANISOU 3088 CD2 TYR A1105 11645 9194 21197 1139 -2287 2210 C
ATOM 3089 CE1 TYR A1105 19.808 115.683 180.286 1.00122.06 C
ANISOU 3089 CE1 TYR A1105 13067 10574 22736 970 -3493 2888 C
ATOM 3090 CE2 TYR A1105 17.656 115.827 179.236 1.00113.62 C
ANISOU 3090 CE2 TYR A1105 12353 9760 21056 1022 -2525 2457 C
ATOM 3091 CZ TYR A1105 18.432 115.537 180.348 1.00125.72 C
ANISOU 3091 CZ TYR A1105 13900 11285 22583 930 -3114 2800 C
ATOM 3092 OH TYR A1105 17.835 115.109 181.509 1.00129.40 O
ANISOU 3092 OH TYR A1105 14741 11984 22442 779 -3330 3083 O
ATOM 3093 N LEU A1106 19.161 115.068 174.219 1.00100.18 N
ANISOU 3093 N LEU A1106 9531 7199 21334 1437 -1084 1725 N
ATOM 3094 CA LEU A1106 18.101 114.244 173.639 1.00 97.72 C
ANISOU 3094 CA LEU A1106 9386 6926 20819 1420 -753 1617 C
ATOM 3095 C LEU A1106 18.636 112.882 173.150 1.00101.84 C
ANISOU 3095 C LEU A1106 9615 7054 22028 1491 -571 1611 C
ATOM 3096 O LEU A1106 17.905 111.890 173.188 1.00101.43 O
ANISOU 3096 O LEU A1106 9640 6934 21965 1480 -497 1648 O
ATOM 3097 CB LEU A1106 17.432 114.990 172.483 1.00 94.91 C
ANISOU 3097 CB LEU A1106 9178 6789 20095 1368 -351 1310 C
ATOM 3098 CG LEU A1106 15.944 114.733 172.292 1.00 97.66 C
ANISOU 3098 CG LEU A1106 9821 7331 19953 1291 -214 1248 C
ATOM 3099 CD1 LEU A1106 15.100 115.753 173.054 1.00 95.68 C
ANISOU 3099 CD1 LEU A1106 9813 7360 19181 1226 -386 1325 C
ATOM 3100 CD2 LEU A1106 15.574 114.770 170.831 1.00 99.85 C
ANISOU 3100 CD2 LEU A1106 10136 7673 20128 1228 182 968 C
TER 3101 LEU A1106
HETATM 3102 C1 OLA A1201 1.358 62.957 191.160 1.00 79.71 C
HETATM 3103 O1 OLA A1201 1.702 63.531 192.219 1.00 80.18 O
HETATM 3104 O2 OLA A1201 0.199 62.482 191.078 1.00 80.29 O1-
HETATM 3105 C2 OLA A1201 2.335 62.830 190.011 1.00 77.48 C
HETATM 3106 C3 OLA A1201 1.906 63.699 188.833 1.00 75.15 C
HETATM 3107 C4 OLA A1201 3.109 64.367 188.179 1.00 74.50 C
HETATM 3108 C5 OLA A1201 2.870 65.865 188.030 1.00 74.42 C
HETATM 3109 C6 OLA A1201 4.150 66.621 187.686 1.00 73.48 C
HETATM 3110 C7 OLA A1201 3.839 67.914 186.940 1.00 72.84 C
HETATM 3111 C8 OLA A1201 4.015 69.138 187.835 1.00 72.34 C
HETATM 3112 C9 OLA A1201 3.322 70.332 187.208 1.00 71.34 C
HETATM 3113 C10 OLA A1201 3.064 71.486 187.836 1.00 71.05 C
HETATM 3114 C11 OLA A1201 3.426 71.786 189.277 1.00 70.74 C
HETATM 3115 C12 OLA A1201 2.863 73.143 189.694 1.00 69.70 C
HETATM 3116 C13 OLA A1201 3.090 73.404 191.182 1.00 68.73 C
HETATM 3117 C14 OLA A1201 1.800 73.238 191.985 1.00 67.85 C
HETATM 3118 C15 OLA A1201 2.076 73.138 193.483 1.00 66.37 C
HETATM 3119 C16 OLA A1201 0.777 73.059 194.277 1.00 65.35 C
HETATM 3120 C11 OLA A1202 12.155 89.742 196.316 1.00 72.74 C
HETATM 3121 C12 OLA A1202 12.178 88.415 195.568 1.00 73.10 C
HETATM 3122 C13 OLA A1202 12.408 87.251 196.525 1.00 73.31 C
HETATM 3123 C14 OLA A1202 11.831 85.954 195.967 1.00 73.17 C
HETATM 3124 C15 OLA A1202 12.022 84.802 196.948 1.00 73.36 C
HETATM 3125 C16 OLA A1202 11.326 83.537 196.457 1.00 73.83 C
HETATM 3126 C17 OLA A1202 11.952 82.289 197.071 1.00 73.44 C
HETATM 3127 C11 OLA A1203 26.848 89.977 201.371 1.00 68.98 C
HETATM 3128 C12 OLA A1203 27.596 88.811 200.732 1.00 69.14 C
HETATM 3129 C13 OLA A1203 27.444 87.540 201.563 1.00 69.76 C
HETATM 3130 C14 OLA A1203 27.900 86.306 200.787 1.00 69.98 C
HETATM 3131 C15 OLA A1203 27.841 85.054 201.659 1.00 70.28 C
HETATM 3132 C16 OLA A1203 27.309 83.846 200.890 1.00 69.66 C
HETATM 3133 C17 OLA A1203 28.404 82.818 200.634 1.00 68.79 C
HETATM 3134 C1 OLA A1204 29.640 92.790 176.016 1.00 57.43 C
HETATM 3135 C2 OLA A1204 29.452 91.397 176.571 1.00 58.36 C
HETATM 3136 C3 OLA A1204 30.722 90.949 177.285 1.00 59.69 C
HETATM 3137 C4 OLA A1204 30.627 91.155 178.795 1.00 60.75 C
HETATM 3138 C5 OLA A1204 31.831 91.940 179.311 1.00 61.51 C
HETATM 3139 C6 OLA A1204 32.180 91.576 180.753 1.00 61.33 C
HETATM 3140 C7 OLA A1204 32.079 92.783 181.683 1.00 60.38 C
HETATM 3141 C8 OLA A1204 32.377 92.394 183.127 1.00 59.83 C
HETATM 3142 C1 OLA A1205 8.973 89.889 178.045 1.00 90.81 C
HETATM 3143 O1 OLA A1205 8.862 90.995 177.468 1.00 91.38 O
HETATM 3144 O2 OLA A1205 9.997 89.676 178.734 1.00 89.86 O
HETATM 3145 C2 OLA A1205 7.908 88.821 177.896 1.00 90.78 C
HETATM 3146 C3 OLA A1205 6.558 89.281 178.445 1.00 90.67 C
HETATM 3147 C4 OLA A1205 6.058 88.335 179.532 1.00 90.96 C
HETATM 3148 C5 OLA A1205 4.535 88.175 179.534 1.00 90.79 C
HETATM 3149 C6 OLA A1205 3.843 88.971 180.643 1.00 90.35 C
HETATM 3150 C7 OLA A1205 4.050 88.363 182.030 1.00 89.79 C
HETATM 3151 C8 OLA A1205 2.742 87.954 182.698 1.00 89.27 C
HETATM 3152 C9 OLA A1205 3.050 87.010 183.845 1.00 88.69 C
HETATM 3153 C10 OLA A1205 2.980 85.674 183.780 1.00 88.35 C
HETATM 3154 C11 OLA A1205 2.560 84.886 182.553 1.00 87.90 C
HETATM 3155 C12 OLA A1205 3.774 84.425 181.754 1.00 87.16 C
HETATM 3156 C13 OLA A1205 3.369 83.421 180.679 1.00 86.65 C
HETATM 3157 C14 OLA A1205 3.493 84.018 179.281 1.00 86.31 C
HETATM 3158 C18 OLC A1206 0.094 77.828 194.051 1.00 80.51 C
HETATM 3159 C10 OLC A1206 -0.809 87.376 194.892 1.00 86.07 C
HETATM 3160 C9 OLC A1206 -0.547 88.649 194.566 1.00 86.31 C
HETATM 3161 C17 OLC A1206 0.372 78.984 194.985 1.00 81.36 C
HETATM 3162 C11 OLC A1206 0.250 86.321 195.152 1.00 85.89 C
HETATM 3163 C8 OLC A1206 0.849 89.222 194.407 1.00 86.65 C
HETATM 3164 C24 OLC A1206 3.728 99.475 195.879 1.00 95.57 C
HETATM 3165 C16 OLC A1206 1.018 80.146 194.237 1.00 82.85 C
HETATM 3166 C12 OLC A1206 -0.297 84.936 194.823 1.00 85.39 C
HETATM 3167 C7 OLC A1206 0.792 90.746 194.434 1.00 86.61 C
HETATM 3168 C15 OLC A1206 1.142 81.384 195.122 1.00 83.63 C
HETATM 3169 C13 OLC A1206 0.646 83.845 195.320 1.00 84.90 C
HETATM 3170 C6 OLC A1206 1.873 91.354 193.547 1.00 86.41 C
HETATM 3171 C14 OLC A1206 0.593 82.619 194.415 1.00 84.27 C
HETATM 3172 C5 OLC A1206 1.657 92.851 193.360 1.00 86.50 C
HETATM 3173 C4 OLC A1206 1.761 93.246 191.889 1.00 86.96 C
HETATM 3174 C3 OLC A1206 2.633 94.482 191.702 1.00 87.97 C
HETATM 3175 C2 OLC A1206 1.796 95.742 191.495 1.00 89.32 C
HETATM 3176 C21 OLC A1206 3.688 98.289 193.679 1.00 93.73 C
HETATM 3177 C1 OLC A1206 2.596 96.965 191.882 1.00 90.57 C
HETATM 3178 C22 OLC A1206 2.888 99.162 194.644 1.00 95.08 C
HETATM 3179 O19 OLC A1206 2.976 97.730 191.006 1.00 90.04 O
HETATM 3180 O25 OLC A1206 2.904 99.420 197.051 1.00 95.61 O
HETATM 3181 O23 OLC A1206 2.508 100.383 193.995 1.00 95.17 O
HETATM 3182 O20 OLC A1206 2.874 97.206 193.214 1.00 92.24 O
HETATM 3183 C1 PEG A1207 4.414 100.745 173.405 1.00 96.05 C
HETATM 3184 O1 PEG A1207 4.130 99.341 173.401 1.00 95.52 O
HETATM 3185 C2 PEG A1207 5.382 101.058 172.271 1.00 96.68 C
HETATM 3186 O2 PEG A1207 5.169 102.387 171.792 1.00 97.32 O
HETATM 3187 C3 PEG A1207 5.062 102.431 170.367 1.00 97.73 C
HETATM 3188 C4 PEG A1207 6.235 103.199 169.761 1.00 97.71 C
HETATM 3189 O4 PEG A1207 5.838 103.794 168.520 1.00 97.51 O
HETATM 3190 UNK UNX A1208 23.091 67.545 190.046 1.00 62.44 X
HETATM 3191 UNK UNX A1209 25.992 67.139 190.028 1.00 54.99 X
HETATM 3192 UNK UNX A1210 27.010 64.290 188.099 1.00 59.35 X
HETATM 3193 UNK UNX A1211 25.627 61.691 188.436 1.00 51.19 X
HETATM 3194 UNK UNX A1212 22.913 61.054 188.267 1.00 48.47 X
HETATM 3195 O HOH A1301 16.755 75.124 186.412 1.00 44.54 O
HETATM 3196 O HOH A1302 0.263 97.231 187.305 1.00 81.49 O
HETATM 3197 O HOH A1303 -0.803 95.280 188.884 1.00 57.33 O
CONECT 50 1322
CONECT 56 2008
CONECT 708 1279
CONECT 1279 708
CONECT 1322 50
CONECT 2008 56
CONECT 3102 3103 3104 3105
CONECT 3103 3102
CONECT 3104 3102
CONECT 3105 3102 3106
CONECT 3106 3105 3107
CONECT 3107 3106 3108
CONECT 3108 3107 3109
CONECT 3109 3108 3110
CONECT 3110 3109 3111
CONECT 3111 3110 3112
CONECT 3112 3111 3113
CONECT 3113 3112 3114
CONECT 3114 3113 3115
CONECT 3115 3114 3116
CONECT 3116 3115 3117
CONECT 3117 3116 3118
CONECT 3118 3117 3119
CONECT 3119 3118
CONECT 3120 3121
CONECT 3121 3120 3122
CONECT 3122 3121 3123
CONECT 3123 3122 3124
CONECT 3124 3123 3125
CONECT 3125 3124 3126
CONECT 3126 3125
CONECT 3127 3128
CONECT 3128 3127 3129
CONECT 3129 3128 3130
CONECT 3130 3129 3131
CONECT 3131 3130 3132
CONECT 3132 3131 3133
CONECT 3133 3132
CONECT 3134 3135
CONECT 3135 3134 3136
CONECT 3136 3135 3137
CONECT 3137 3136 3138
CONECT 3138 3137 3139
CONECT 3139 3138 3140
CONECT 3140 3139 3141
CONECT 3141 3140
CONECT 3142 3143 3144 3145
CONECT 3143 3142
CONECT 3144 3142
CONECT 3145 3142 3146
CONECT 3146 3145 3147
CONECT 3147 3146 3148
CONECT 3148 3147 3149
CONECT 3149 3148 3150
CONECT 3150 3149 3151
CONECT 3151 3150 3152
CONECT 3152 3151 3153
CONECT 3153 3152 3154
CONECT 3154 3153 3155
CONECT 3155 3154 3156
CONECT 3156 3155 3157
CONECT 3157 3156
CONECT 3158 3161
CONECT 3159 3160 3162
CONECT 3160 3159 3163
CONECT 3161 3158 3165
CONECT 3162 3159 3166
CONECT 3163 3160 3167
CONECT 3164 3178 3180
CONECT 3165 3161 3168
CONECT 3166 3162 3169
CONECT 3167 3163 3170
CONECT 3168 3165 3171
CONECT 3169 3166 3171
CONECT 3170 3167 3172
CONECT 3171 3168 3169
CONECT 3172 3170 3173
CONECT 3173 3172 3174
CONECT 3174 3173 3175
CONECT 3175 3174 3177
CONECT 3176 3178 3182
CONECT 3177 3175 3179 3182
CONECT 3178 3164 3176 3181
CONECT 3179 3177
CONECT 3180 3164
CONECT 3181 3178
CONECT 3182 3176 3177
CONECT 3183 3184 3185
CONECT 3184 3183
CONECT 3185 3183 3186
CONECT 3186 3185 3187
CONECT 3187 3186 3188
CONECT 3188 3187 3189
CONECT 3189 3188
MASTER 372 0 12 16 0 0 0 6 3196 1 94 34
END