HEADER SIGNALING PROTEIN 02-SEP-19 6KUY
TITLE CRYSTAL STRUCTURE OF THE ALPHA2A ADRENERGIC RECEPTOR IN COMPLEX WITH A
TITLE 2 PARTIAL AGONIST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA2A ADRENERGIC RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293F
KEYWDS ALPHA2A ADRENERGIC RECEPTOR, PARTIAL AGONIST, GPCR, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.QU,Q.T.ZHOU,D.WU,S.W.ZHAO
REVDAT 1 04-DEC-19 6KUY 0
JRNL AUTH L.QU,Q.T.ZHOU,D.WU,S.W.ZHAO
JRNL TITL CRYSTAL STRUCTURES OF THE ALPHA2A ADRENERGIC RECEPTOR IN
JRNL TITL 2 COMPLEX WITH A PARTIAL AGONIST
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.410
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.7
REMARK 3 NUMBER OF REFLECTIONS : 11226
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.268
REMARK 3 R VALUE (WORKING SET) : 0.267
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 539
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 3.5223 - 3.2003 0.85 2483 128 0.2668 0.2980
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.048
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 2849
REMARK 3 ANGLE : 0.628 3893
REMARK 3 CHIRALITY : 0.038 467
REMARK 3 PLANARITY : 0.004 487
REMARK 3 DIHEDRAL : 19.080 1680
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 227)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.106 2.581 37.833
REMARK 3 T TENSOR
REMARK 3 T11: 2.5900 T22: 1.4802
REMARK 3 T33: 0.7841 T12: -0.1446
REMARK 3 T13: -0.3747 T23: -0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 1.0988 L22: 1.0316
REMARK 3 L33: 6.9995 L12: -1.0465
REMARK 3 L13: -0.7700 L23: -0.0452
REMARK 3 S TENSOR
REMARK 3 S11: 0.1506 S12: -0.0553 S13: -0.1684
REMARK 3 S21: 0.7110 S22: -0.1272 S23: -0.0643
REMARK 3 S31: 1.9399 S32: 0.0221 S33: 0.0743
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 365 THROUGH 443)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.409 1.655 36.405
REMARK 3 T TENSOR
REMARK 3 T11: 0.5824 T22: 0.3719
REMARK 3 T33: 0.9272 T12: 0.0297
REMARK 3 T13: 0.0824 T23: -0.0577
REMARK 3 L TENSOR
REMARK 3 L11: 9.2203 L22: 3.2474
REMARK 3 L33: 3.5073 L12: 0.1139
REMARK 3 L13: 2.3652 L23: -0.7578
REMARK 3 S TENSOR
REMARK 3 S11: 0.2815 S12: -0.0917 S13: -0.5684
REMARK 3 S21: 0.3986 S22: 0.2286 S23: 0.6424
REMARK 3 S31: -0.2040 S32: 0.2281 S33: -0.2810
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6KUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE DEPOSITION ID IS D_1300012398.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-16
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) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11252
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 47.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
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: 2Y02
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES SODIUM PH 7.4, 310MM
REMARK 280 AMMONIUM TARTRATE DIBASIC, 36.5% PEG400, LIPIDIC CUBIC PHASE,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 143.12500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 143.12500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.60500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.81000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.60500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.81000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 143.12500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.60500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 35.81000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 143.12500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.60500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 35.81000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 20
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 ALA A 23
REMARK 465 ARG A 24
REMARK 465 ALA A 25
REMARK 465 THR A 26
REMARK 465 PRO A 27
REMARK 465 TYR A 28
REMARK 465 SER A 29
REMARK 465 LEU A 30
REMARK 465 GLN A 31
REMARK 465 VAL A 32
REMARK 465 GLU A 173
REMARK 465 LYS A 174
REMARK 465 LYS A 175
REMARK 465 GLY A 176
REMARK 465 GLY A 177
REMARK 465 GLY A 178
REMARK 465 GLY A 179
REMARK 465 GLY A 180
REMARK 465 PRO A 181
REMARK 465 GLN A 182
REMARK 465 GLY A 444
REMARK 465 ASP A 445
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 44 CG SD CE
REMARK 470 LYS A 65 CG CD CE NZ
REMARK 470 ASN A 69 CG OD1 ND2
REMARK 470 LEU A 70 CG CD1 CD2
REMARK 470 ILE A 87 CG1 CG2 CD1
REMARK 470 LEU A 91 CG CD1 CD2
REMARK 470 TYR A 98 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP A 99 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 99 CZ3 CH2
REMARK 470 TYR A 100 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP A 105 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 105 CZ3 CH2
REMARK 470 LEU A 110 CG CD1 CD2
REMARK 470 ARG A 131 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 140 CG CD OE1 OE2
REMARK 470 LEU A 143 CG CD1 CD2
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 ARG A 148 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 151 CG CD CE NZ
REMARK 470 ILE A 172 CG1 CG2 CD1
REMARK 470 ARG A 187 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 189 CG CD OE1 OE2
REMARK 470 ASP A 192 CG OD1 OD2
REMARK 470 GLN A 193 CG CD OE1 NE2
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 TRP A 195 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 195 CZ3 CH2
REMARK 470 ARG A 218 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 221 CG CD OE1 NE2
REMARK 470 VAL A1026 CG1 CG2
REMARK 470 LEU A1078 CG CD1 CD2
REMARK 470 LYS A1083 CG CD CE NZ
REMARK 470 LEU A1094 CG CD1 CD2
REMARK 470 GLN A 366 CG CD OE1 NE2
REMARK 470 LYS A 370 CG CD CE NZ
REMARK 470 ARG A 405 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 407 CG CD1 CD2
REMARK 470 LYS A 409 CG CD CE NZ
REMARK 470 PHE A 410 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 425 CG1 CG2 CD1
REMARK 470 ILE A 428 CG1 CG2 CD1
REMARK 470 ASN A 430 CG OD1 ND2
REMARK 470 HIS A 431 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 433 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 435 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 437 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 439 CG CD CE NZ
REMARK 470 ILE A 440 CG1 CG2 CD1
REMARK 470 LEU A 441 CG CD1 CD2
REMARK 470 ARG A 443 CG CD NE CZ NH1 NH2
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 THR A 60 81.43 -152.79
REMARK 500 ALA A 138 -123.70 63.38
REMARK 500 ARG A 145 44.73 -72.70
REMARK 500 ARG A 187 84.58 54.13
REMARK 500 GLN A 193 106.00 -56.30
REMARK 500 PHE A 205 -61.64 -97.13
REMARK 500 LYS A1019 62.87 -101.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E39 A 1202
DBREF 6KUY A 20 445 PDB 6KUY 6KUY 20 445
SEQRES 1 A 395 GLY GLY GLY ALA ARG ALA THR PRO TYR SER LEU GLN VAL
SEQRES 2 A 395 THR LEU THR LEU VAL CYS LEU ALA GLY LEU LEU MET LEU
SEQRES 3 A 395 LEU THR VAL PHE GLY ASN VAL LEU VAL ILE ILE ALA VAL
SEQRES 4 A 395 PHE THR SER ARG ALA LEU LYS ALA PRO GLN ASN LEU PHE
SEQRES 5 A 395 LEU VAL SER LEU ALA SER ALA ASP ILE LEU VAL ALA THR
SEQRES 6 A 395 LEU VAL ILE PRO PHE SER LEU ALA ASN GLU VAL MET GLY
SEQRES 7 A 395 TYR TRP TYR PHE GLY LYS ALA TRP CYS GLU ILE TYR LEU
SEQRES 8 A 395 ALA LEU ASP VAL LEU PHE CYS THR SER SER ALA TRP HIS
SEQRES 9 A 395 LEU CYS ALA ILE SER LEU ASP ARG TYR TRP SER ILE THR
SEQRES 10 A 395 GLN ALA ILE GLU TYR ASN LEU LYS ARG THR PRO ARG ARG
SEQRES 11 A 395 ILE LYS ALA ILE ILE LEU THR VAL TRP VAL ILE SER ALA
SEQRES 12 A 395 VAL ILE SER PHE PRO PRO LEU ILE SER ILE GLU LYS LYS
SEQRES 13 A 395 GLY GLY GLY GLY GLY PRO GLN PRO ALA GLU PRO ARG CYS
SEQRES 14 A 395 GLU ILE ASN ASP GLN LYS TRP TYR VAL ILE SER SER CYS
SEQRES 15 A 395 ILE GLY SER PHE PHE ALA PRO CYS LEU ILE MET ILE LEU
SEQRES 16 A 395 VAL TYR VAL ARG ILE TYR GLN ILE ALA LYS ARG ARG THR
SEQRES 17 A 395 ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN
SEQRES 18 A 395 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL
SEQRES 19 A 395 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP
SEQRES 20 A 395 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER
SEQRES 21 A 395 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE
SEQRES 22 A 395 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU
SEQRES 23 A 395 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA
SEQRES 24 A 395 GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS
SEQRES 25 A 395 TYR LEU ARG GLN ASN ARG GLU LYS ARG PHE THR PHE VAL
SEQRES 26 A 395 LEU ALA VAL VAL ILE GLY VAL PHE VAL VAL CYS TRP PHE
SEQRES 27 A 395 PRO PHE PHE PHE THR TYR THR LEU THR ALA VAL GLY CYS
SEQRES 28 A 395 SER VAL PRO ARG THR LEU PHE LYS PHE PHE PHE TRP PHE
SEQRES 29 A 395 GLY TYR CYS ASN SER SER LEU ASN PRO VAL ILE TYR THR
SEQRES 30 A 395 ILE PHE ASN HIS ASP PHE ARG ARG ALA PHE LYS LYS ILE
SEQRES 31 A 395 LEU CYS ARG GLY ASP
HET PEG A1201 7
HET E39 A1202 18
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM E39 (2~{S})-4-FLUORANYL-2-(1~{H}-IMIDAZOL-5-YL)-1-PROPAN-2-
HETNAM 2 E39 YL-2,3-DIHYDROINDOLE
FORMUL 2 PEG C4 H10 O3
FORMUL 3 E39 C14 H16 F N3
HELIX 1 AA1 THR A 35 THR A 60 1 26
HELIX 2 AA2 LYS A 65 VAL A 86 1 22
HELIX 3 AA3 VAL A 86 VAL A 95 1 10
HELIX 4 AA4 LYS A 103 ALA A 138 1 36
HELIX 5 AA5 ALA A 138 ARG A 145 1 8
HELIX 6 AA6 THR A 146 PHE A 166 1 21
HELIX 7 AA7 GLN A 193 PHE A 205 1 13
HELIX 8 AA8 PHE A 205 LYS A 1019 1 42
HELIX 9 AA9 ASN A 1022 LYS A 1042 1 21
HELIX 10 AB1 SER A 1055 GLU A 1081 1 27
HELIX 11 AB2 LYS A 1083 ARG A 365 1 25
HELIX 12 AB3 ASN A 367 THR A 397 1 31
HELIX 13 AB4 THR A 406 CYS A 417 1 12
HELIX 14 AB5 LEU A 421 ASN A 430 1 10
HELIX 15 AB6 ASN A 430 ARG A 443 1 14
SSBOND 1 CYS A 106 CYS A 188 1555 1555 2.04
SITE 1 AC1 2 HIS A1063 ASP A1066
SITE 1 AC2 9 ASP A 113 VAL A 114 CYS A 117 SER A 204
SITE 2 AC2 9 TRP A 387 PHE A 390 PHE A 391 PHE A 412
SITE 3 AC2 9 TYR A 416
CRYST1 71.210 71.620 286.250 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014043 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013963 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003493 0.00000
ATOM 1 N THR A 33 12.255 -13.734 56.996 1.00238.71 N
ANISOU 1 N THR A 33 50554 23608 16537 -10449 -85 1170 N
ATOM 2 CA THR A 33 13.071 -14.443 57.977 1.00243.54 C
ANISOU 2 CA THR A 33 51954 23554 17027 -9927 -84 1237 C
ATOM 3 C THR A 33 14.422 -14.841 57.368 1.00240.80 C
ANISOU 3 C THR A 33 52066 22670 16757 -9195 -313 1170 C
ATOM 4 O THR A 33 15.148 -13.984 56.870 1.00231.26 O
ANISOU 4 O THR A 33 50292 21762 15814 -8612 -542 1137 O
ATOM 5 CB THR A 33 12.328 -15.684 58.525 1.00255.53 C
ANISOU 5 CB THR A 33 54292 24602 18196 -10623 187 1255 C
ATOM 6 OG1 THR A 33 13.240 -16.520 59.249 1.00259.67 O
ANISOU 6 OG1 THR A 33 55698 24388 18579 -10053 173 1285 O
ATOM 7 CG2 THR A 33 11.665 -16.475 57.395 1.00258.93 C
ANISOU 7 CG2 THR A 33 55050 24864 18467 -11456 273 1124 C
ATOM 8 N LEU A 34 14.769 -16.128 57.409 1.00247.51 N
ANISOU 8 N LEU A 34 53932 22745 17364 -9201 -249 1140 N
ATOM 9 CA LEU A 34 16.019 -16.585 56.815 1.00246.96 C
ANISOU 9 CA LEU A 34 54328 22176 17331 -8490 -447 1078 C
ATOM 10 C LEU A 34 15.905 -16.820 55.313 1.00246.07 C
ANISOU 10 C LEU A 34 54227 22016 17252 -8824 -518 955 C
ATOM 11 O LEU A 34 16.895 -17.212 54.687 1.00248.49 O
ANISOU 11 O LEU A 34 54897 21932 17583 -8257 -679 900 O
ATOM 12 CB LEU A 34 16.503 -17.861 57.518 1.00244.66 C
ANISOU 12 CB LEU A 34 55155 21066 16738 -8241 -346 1086 C
ATOM 13 CG LEU A 34 17.978 -18.252 57.350 1.00238.99 C
ANISOU 13 CG LEU A 34 54883 19887 16033 -7240 -546 1059 C
ATOM 14 CD1 LEU A 34 18.878 -17.021 57.387 1.00226.82 C
ANISOU 14 CD1 LEU A 34 52457 18897 14828 -6433 -809 1100 C
ATOM 15 CD2 LEU A 34 18.400 -19.258 58.412 1.00227.60 C
ANISOU 15 CD2 LEU A 34 54376 17807 14295 -6887 -426 1092 C
ATOM 16 N THR A 35 14.738 -16.570 54.715 1.00249.06 N
ANISOU 16 N THR A 35 54178 22827 17626 -9699 -405 911 N
ATOM 17 CA THR A 35 14.579 -16.763 53.278 1.00249.86 C
ANISOU 17 CA THR A 35 54252 22934 17750 -10044 -473 789 C
ATOM 18 C THR A 35 15.375 -15.754 52.456 1.00242.64 C
ANISOU 18 C THR A 35 52579 22436 17179 -9367 -741 757 C
ATOM 19 O THR A 35 15.611 -15.992 51.266 1.00241.23 O
ANISOU 19 O THR A 35 52479 22141 17036 -9378 -842 660 O
ATOM 20 CB THR A 35 13.099 -16.683 52.892 1.00253.17 C
ANISOU 20 CB THR A 35 54302 23828 18065 -11153 -285 742 C
ATOM 21 OG1 THR A 35 12.482 -15.579 53.567 1.00248.98 O
ANISOU 21 OG1 THR A 35 52864 24060 17677 -11236 -229 828 O
ATOM 22 CG2 THR A 35 12.376 -17.970 53.263 1.00261.46 C
ANISOU 22 CG2 THR A 35 56271 24343 18729 -11941 -41 700 C
ATOM 23 N LEU A 36 15.808 -14.648 53.058 1.00241.00 N
ANISOU 23 N LEU A 36 51659 22698 17212 -8778 -857 822 N
ATOM 24 CA LEU A 36 16.386 -13.538 52.310 1.00233.23 C
ANISOU 24 CA LEU A 36 49834 22224 16558 -8259 -1090 766 C
ATOM 25 C LEU A 36 17.897 -13.631 52.131 1.00239.25 C
ANISOU 25 C LEU A 36 50811 22654 17439 -7285 -1324 755 C
ATOM 26 O LEU A 36 18.448 -12.891 51.308 1.00241.88 O
ANISOU 26 O LEU A 36 50551 23325 18027 -6886 -1519 685 O
ATOM 27 CB LEU A 36 16.042 -12.210 52.994 1.00216.80 C
ANISOU 27 CB LEU A 36 46844 20859 14671 -8162 -1096 817 C
ATOM 28 CG LEU A 36 14.566 -11.968 53.316 1.00207.73 C
ANISOU 28 CG LEU A 36 45348 20173 13408 -9018 -862 847 C
ATOM 29 CD1 LEU A 36 14.359 -10.542 53.797 1.00198.00 C
ANISOU 29 CD1 LEU A 36 43173 19666 12391 -8776 -903 880 C
ATOM 30 CD2 LEU A 36 13.691 -12.263 52.108 1.00208.57 C
ANISOU 30 CD2 LEU A 36 45345 20459 13441 -9774 -786 740 C
ATOM 31 N VAL A 37 18.579 -14.504 52.877 1.00240.18 N
ANISOU 31 N VAL A 37 51727 22158 17372 -6878 -1304 813 N
ATOM 32 CA VAL A 37 20.031 -14.604 52.754 1.00239.02 C
ANISOU 32 CA VAL A 37 51737 21771 17309 -5916 -1521 804 C
ATOM 33 C VAL A 37 20.422 -15.090 51.364 1.00238.41 C
ANISOU 33 C VAL A 37 51882 21458 17245 -5834 -1622 707 C
ATOM 34 O VAL A 37 21.437 -14.653 50.804 1.00235.28 O
ANISOU 34 O VAL A 37 51125 21226 17043 -5144 -1841 669 O
ATOM 35 CB VAL A 37 20.599 -15.521 53.855 1.00244.43 C
ANISOU 35 CB VAL A 37 53263 21862 17747 -5505 -1452 876 C
ATOM 36 CG1 VAL A 37 19.919 -16.880 53.828 1.00251.31 C
ANISOU 36 CG1 VAL A 37 55151 22061 18274 -6126 -1224 859 C
ATOM 37 CG2 VAL A 37 22.107 -15.677 53.703 1.00243.74 C
ANISOU 37 CG2 VAL A 37 53314 21586 17710 -4489 -1669 861 C
ATOM 38 N CYS A 38 19.625 -15.981 50.775 1.00238.55 N
ANISOU 38 N CYS A 38 52477 21112 17051 -6550 -1467 660 N
ATOM 39 CA CYS A 38 19.959 -16.507 49.460 1.00233.83 C
ANISOU 39 CA CYS A 38 52158 20248 16439 -6489 -1555 569 C
ATOM 40 C CYS A 38 19.488 -15.593 48.341 1.00226.02 C
ANISOU 40 C CYS A 38 50273 19901 15702 -6797 -1640 482 C
ATOM 41 O CYS A 38 20.102 -15.575 47.270 1.00224.51 O
ANISOU 41 O CYS A 38 49965 19708 15629 -6432 -1796 410 O
ATOM 42 CB CYS A 38 19.361 -17.903 49.289 1.00236.38 C
ANISOU 42 CB CYS A 38 53562 19853 16399 -7121 -1358 536 C
ATOM 43 SG CYS A 38 17.816 -18.168 50.187 1.00236.32 S
ANISOU 43 SG CYS A 38 53753 19880 16158 -8245 -1052 567 S
ATOM 44 N LEU A 39 18.416 -14.829 48.573 1.00218.72 N
ANISOU 44 N LEU A 39 48698 19550 14857 -7423 -1536 482 N
ATOM 45 CA LEU A 39 17.865 -13.969 47.530 1.00208.89 C
ANISOU 45 CA LEU A 39 46593 18947 13829 -7734 -1594 380 C
ATOM 46 C LEU A 39 18.883 -12.934 47.062 1.00201.21 C
ANISOU 46 C LEU A 39 44882 18371 13200 -6915 -1843 341 C
ATOM 47 O LEU A 39 19.036 -12.709 45.857 1.00197.22 O
ANISOU 47 O LEU A 39 44045 18047 12842 -6842 -1954 237 O
ATOM 48 CB LEU A 39 16.590 -13.290 48.039 1.00201.01 C
ANISOU 48 CB LEU A 39 45008 18537 12831 -8438 -1429 398 C
ATOM 49 CG LEU A 39 15.861 -12.265 47.164 1.00191.17 C
ANISOU 49 CG LEU A 39 42771 18070 11794 -8764 -1457 293 C
ATOM 50 CD1 LEU A 39 14.364 -12.346 47.409 1.00192.65 C
ANISOU 50 CD1 LEU A 39 42811 18600 11788 -9742 -1219 292 C
ATOM 51 CD2 LEU A 39 16.356 -10.857 47.453 1.00181.82 C
ANISOU 51 CD2 LEU A 39 40710 17445 10929 -8142 -1602 309 C
ATOM 52 N ALA A 40 19.588 -12.294 47.998 1.00200.54 N
ANISOU 52 N ALA A 40 44527 18431 13237 -6311 -1932 418 N
ATOM 53 CA ALA A 40 20.550 -11.260 47.623 1.00195.46 C
ANISOU 53 CA ALA A 40 43169 18192 12905 -5598 -2160 378 C
ATOM 54 C ALA A 40 21.710 -11.849 46.827 1.00193.59 C
ANISOU 54 C ALA A 40 43291 17591 12673 -4976 -2322 341 C
ATOM 55 O ALA A 40 22.063 -11.339 45.757 1.00175.63 O
ANISOU 55 O ALA A 40 40525 15603 10604 -4758 -2459 253 O
ATOM 56 CB ALA A 40 21.061 -10.539 48.870 1.00176.43 C
ANISOU 56 CB ALA A 40 40470 15984 10581 -5134 -2214 463 C
ATOM 57 N GLY A 41 22.328 -12.915 47.343 1.00194.97 N
ANISOU 57 N GLY A 41 44319 17147 12614 -4646 -2302 406 N
ATOM 58 CA GLY A 41 23.351 -13.609 46.574 1.00192.76 C
ANISOU 58 CA GLY A 41 44463 16494 12284 -4067 -2428 374 C
ATOM 59 C GLY A 41 22.823 -14.133 45.253 1.00193.50 C
ANISOU 59 C GLY A 41 44764 16429 12328 -4516 -2391 281 C
ATOM 60 O GLY A 41 23.539 -14.151 44.248 1.00193.73 O
ANISOU 60 O GLY A 41 44683 16473 12454 -4075 -2536 219 O
ATOM 61 N LEU A 42 21.562 -14.572 45.238 1.00188.56 N
ANISOU 61 N LEU A 42 44430 15678 11538 -5411 -2195 265 N
ATOM 62 CA LEU A 42 20.900 -14.923 43.986 1.00203.65 C
ANISOU 62 CA LEU A 42 46394 17566 13416 -5955 -2157 158 C
ATOM 63 C LEU A 42 20.898 -13.738 43.023 1.00198.26 C
ANISOU 63 C LEU A 42 44658 17595 13077 -5848 -2297 56 C
ATOM 64 O LEU A 42 21.325 -13.853 41.868 1.00183.00 O
ANISOU 64 O LEU A 42 42663 15643 11226 -5601 -2409 -26 O
ATOM 65 CB LEU A 42 19.474 -15.399 44.271 1.00204.19 C
ANISOU 65 CB LEU A 42 46771 17550 13261 -7005 -1917 156 C
ATOM 66 CG LEU A 42 18.587 -15.870 43.120 1.00201.33 C
ANISOU 66 CG LEU A 42 46509 17178 12808 -7747 -1839 43 C
ATOM 67 CD1 LEU A 42 19.162 -17.116 42.469 1.00204.52 C
ANISOU 67 CD1 LEU A 42 47885 16827 12996 -7542 -1859 33 C
ATOM 68 CD2 LEU A 42 17.178 -16.127 43.630 1.00203.53 C
ANISOU 68 CD2 LEU A 42 46908 17548 12875 -8794 -1598 51 C
ATOM 69 N LEU A 43 20.428 -12.578 43.494 1.00195.89 N
ANISOU 69 N LEU A 43 43537 17917 12974 -6005 -2286 62 N
ATOM 70 CA LEU A 43 20.474 -11.374 42.669 1.00190.48 C
ANISOU 70 CA LEU A 43 41868 17891 12614 -5843 -2411 -31 C
ATOM 71 C LEU A 43 21.906 -10.896 42.457 1.00191.38 C
ANISOU 71 C LEU A 43 41723 18068 12926 -4910 -2631 -20 C
ATOM 72 O LEU A 43 22.185 -10.175 41.492 1.00191.25 O
ANISOU 72 O LEU A 43 41089 18435 13142 -4685 -2750 -104 O
ATOM 73 CB LEU A 43 19.629 -10.263 43.300 1.00183.57 C
ANISOU 73 CB LEU A 43 40253 17628 11867 -6199 -2330 -18 C
ATOM 74 CG LEU A 43 18.191 -10.602 43.709 1.00182.25 C
ANISOU 74 CG LEU A 43 40223 17534 11490 -7115 -2099 -10 C
ATOM 75 CD1 LEU A 43 17.395 -9.339 44.003 1.00177.28 C
ANISOU 75 CD1 LEU A 43 38692 17645 11021 -7358 -2043 -21 C
ATOM 76 CD2 LEU A 43 17.490 -11.450 42.656 1.00183.22 C
ANISOU 76 CD2 LEU A 43 40663 17489 11462 -7723 -2021 -115 C
ATOM 77 N MET A 44 22.826 -11.288 43.343 1.00195.22 N
ANISOU 77 N MET A 44 42655 18212 13309 -4361 -2681 80 N
ATOM 78 CA MET A 44 24.229 -10.931 43.159 1.00193.23 C
ANISOU 78 CA MET A 44 42165 18051 13202 -3484 -2887 88 C
ATOM 79 C MET A 44 24.833 -11.674 41.973 1.00195.64 C
ANISOU 79 C MET A 44 42825 18059 13449 -3169 -2969 32 C
ATOM 80 O MET A 44 25.590 -11.093 41.186 1.00196.85 O
ANISOU 80 O MET A 44 42470 18523 13800 -2694 -3126 -17 O
ATOM 81 CB MET A 44 25.018 -11.222 44.435 1.00195.10 C
ANISOU 81 CB MET A 44 42774 18041 13313 -2982 -2911 199 C
ATOM 82 N LEU A 45 24.508 -12.963 41.827 1.00196.33 N
ANISOU 82 N LEU A 45 43810 17535 13252 -3434 -2858 39 N
ATOM 83 CA LEU A 45 24.959 -13.709 40.656 1.00193.87 C
ANISOU 83 CA LEU A 45 43889 16912 12863 -3189 -2920 -20 C
ATOM 84 C LEU A 45 24.342 -13.164 39.374 1.00193.45 C
ANISOU 84 C LEU A 45 43243 17259 13000 -3574 -2944 -146 C
ATOM 85 O LEU A 45 24.970 -13.232 38.311 1.00189.34 O
ANISOU 85 O LEU A 45 42634 16759 12549 -3166 -3061 -205 O
ATOM 86 CB LEU A 45 24.625 -15.194 40.812 1.00198.61 C
ANISOU 86 CB LEU A 45 45638 16728 13095 -3478 -2775 12 C
ATOM 87 CG LEU A 45 25.066 -16.098 39.656 1.00200.37 C
ANISOU 87 CG LEU A 45 46415 16531 13187 -3224 -2823 -42 C
ATOM 88 CD1 LEU A 45 26.559 -16.389 39.724 1.00199.39 C
ANISOU 88 CD1 LEU A 45 46512 16229 13020 -2176 -2965 7 C
ATOM 89 CD2 LEU A 45 24.261 -17.387 39.617 1.00194.26 C
ANISOU 89 CD2 LEU A 45 46672 15064 12073 -3866 -2640 -39 C
ATOM 90 N LEU A 46 23.126 -12.612 39.458 1.00194.58 N
ANISOU 90 N LEU A 46 42951 17758 13223 -4322 -2830 -192 N
ATOM 91 CA LEU A 46 22.466 -12.043 38.287 1.00191.90 C
ANISOU 91 CA LEU A 46 41985 17863 13064 -4688 -2841 -324 C
ATOM 92 C LEU A 46 23.328 -10.991 37.600 1.00187.64 C
ANISOU 92 C LEU A 46 40664 17804 12827 -4055 -3024 -364 C
ATOM 93 O LEU A 46 23.164 -10.756 36.399 1.00189.63 O
ANISOU 93 O LEU A 46 40564 18287 13200 -4113 -3069 -471 O
ATOM 94 CB LEU A 46 21.115 -11.439 38.687 1.00171.33 C
ANISOU 94 CB LEU A 46 38907 15686 10503 -5473 -2694 -352 C
ATOM 95 CG LEU A 46 20.056 -11.235 37.596 1.00180.29 C
ANISOU 95 CG LEU A 46 39605 17189 11706 -6087 -2634 -494 C
ATOM 96 CD1 LEU A 46 19.317 -12.536 37.302 1.00189.79 C
ANISOU 96 CD1 LEU A 46 41578 17918 12615 -6739 -2499 -532 C
ATOM 97 CD2 LEU A 46 19.076 -10.128 37.973 1.00174.05 C
ANISOU 97 CD2 LEU A 46 38004 17071 11056 -6520 -2548 -514 C
ATOM 98 N THR A 47 24.248 -10.359 38.332 1.00183.22 N
ANISOU 98 N THR A 47 39829 17407 12380 -3467 -3126 -281 N
ATOM 99 CA THR A 47 25.214 -9.457 37.713 1.00183.82 C
ANISOU 99 CA THR A 47 39252 17888 12705 -2847 -3299 -306 C
ATOM 100 C THR A 47 26.251 -10.233 36.911 1.00188.67 C
ANISOU 100 C THR A 47 40278 18184 13226 -2251 -3409 -311 C
ATOM 101 O THR A 47 26.540 -9.889 35.761 1.00185.22 O
ANISOU 101 O THR A 47 39462 17986 12928 -2046 -3495 -384 O
ATOM 102 CB THR A 47 25.905 -8.613 38.781 1.00187.05 C
ANISOU 102 CB THR A 47 39278 18560 13231 -2442 -3373 -221 C
ATOM 103 OG1 THR A 47 24.948 -8.191 39.760 1.00193.42 O
ANISOU 103 OG1 THR A 47 39945 19508 14037 -2968 -3246 -191 O
ATOM 104 CG2 THR A 47 26.579 -7.394 38.165 1.00182.16 C
ANISOU 104 CG2 THR A 47 37831 18483 12899 -2041 -3517 -259 C
ATOM 105 N VAL A 48 26.829 -11.276 37.513 1.00198.14 N
ANISOU 105 N VAL A 48 42258 18851 14176 -1933 -3400 -230 N
ATOM 106 CA VAL A 48 27.753 -12.154 36.793 1.00208.60 C
ANISOU 106 CA VAL A 48 44079 19822 15359 -1354 -3480 -230 C
ATOM 107 C VAL A 48 27.060 -12.758 35.579 1.00230.04 C
ANISOU 107 C VAL A 48 47078 22324 18002 -1766 -3426 -333 C
ATOM 108 O VAL A 48 27.555 -12.683 34.449 1.00239.61 O
ANISOU 108 O VAL A 48 48081 23665 19294 -1420 -3523 -392 O
ATOM 109 CB VAL A 48 28.290 -13.252 37.726 1.00199.15 C
ANISOU 109 CB VAL A 48 43764 18039 13866 -1015 -3440 -131 C
ATOM 110 CG1 VAL A 48 29.447 -13.997 37.069 1.00195.73 C
ANISOU 110 CG1 VAL A 48 43726 17340 13301 -238 -3537 -124 C
ATOM 111 CG2 VAL A 48 28.701 -12.652 39.058 1.00191.81 C
ANISOU 111 CG2 VAL A 48 42543 17339 12996 -775 -3466 -43 C
ATOM 112 N PHE A 49 25.903 -13.379 35.807 1.00236.62 N
ANISOU 112 N PHE A 49 48391 22844 18671 -2530 -3266 -355 N
ATOM 113 CA PHE A 49 25.123 -13.951 34.716 1.00240.11 C
ANISOU 113 CA PHE A 49 49079 23117 19035 -3038 -3204 -464 C
ATOM 114 C PHE A 49 24.821 -12.912 33.643 1.00234.88 C
ANISOU 114 C PHE A 49 47485 23093 18666 -3146 -3272 -583 C
ATOM 115 O PHE A 49 24.965 -13.180 32.445 1.00235.29 O
ANISOU 115 O PHE A 49 47562 23114 18726 -3019 -3327 -667 O
ATOM 116 CB PHE A 49 23.824 -14.539 35.271 1.00245.79 C
ANISOU 116 CB PHE A 49 50261 23566 19562 -3956 -3009 -467 C
ATOM 117 CG PHE A 49 23.035 -15.318 34.268 1.00253.34 C
ANISOU 117 CG PHE A 49 51595 24281 20381 -4527 -2932 -571 C
ATOM 118 CD1 PHE A 49 23.258 -16.673 34.100 1.00261.32 C
ANISOU 118 CD1 PHE A 49 53664 24550 21077 -4482 -2886 -536 C
ATOM 119 CD2 PHE A 49 22.070 -14.698 33.493 1.00254.37 C
ANISOU 119 CD2 PHE A 49 51029 24933 20685 -5098 -2903 -702 C
ATOM 120 CE1 PHE A 49 22.534 -17.397 33.174 1.00265.50 C
ANISOU 120 CE1 PHE A 49 54552 24857 21470 -5036 -2815 -626 C
ATOM 121 CE2 PHE A 49 21.343 -15.416 32.564 1.00258.60 C
ANISOU 121 CE2 PHE A 49 51867 25296 21095 -5635 -2838 -807 C
ATOM 122 CZ PHE A 49 21.575 -16.767 32.406 1.00263.98 C
ANISOU 122 CZ PHE A 49 53606 25231 21466 -5624 -2795 -767 C
ATOM 123 N GLY A 50 24.412 -11.717 34.058 1.00230.55 N
ANISOU 123 N GLY A 50 46133 23118 18350 -3348 -3264 -587 N
ATOM 124 CA GLY A 50 24.038 -10.674 33.128 1.00221.87 C
ANISOU 124 CA GLY A 50 44163 22624 17514 -3469 -3304 -693 C
ATOM 125 C GLY A 50 25.209 -9.988 32.458 1.00211.65 C
ANISOU 125 C GLY A 50 42387 21618 16412 -2701 -3473 -688 C
ATOM 126 O GLY A 50 25.214 -9.823 31.236 1.00214.08 O
ANISOU 126 O GLY A 50 42418 22112 16812 -2624 -3523 -780 O
ATOM 127 N ASN A 51 26.214 -9.588 33.241 1.00200.19 N
ANISOU 127 N ASN A 51 40820 20229 15014 -2136 -3559 -580 N
ATOM 128 CA ASN A 51 27.281 -8.750 32.703 1.00198.49 C
ANISOU 128 CA ASN A 51 40016 20402 14999 -1485 -3708 -567 C
ATOM 129 C ASN A 51 28.347 -9.552 31.967 1.00205.01 C
ANISOU 129 C ASN A 51 41249 20947 15700 -842 -3806 -552 C
ATOM 130 O ASN A 51 28.896 -9.062 30.974 1.00209.56 O
ANISOU 130 O ASN A 51 41381 21828 16414 -477 -3898 -586 O
ATOM 131 CB ASN A 51 27.923 -7.921 33.820 1.00196.24 C
ANISOU 131 CB ASN A 51 39360 20375 14826 -1180 -3764 -469 C
ATOM 132 CG ASN A 51 27.045 -6.767 34.266 1.00194.69 C
ANISOU 132 CG ASN A 51 38542 20612 14821 -1664 -3696 -492 C
ATOM 133 OD1 ASN A 51 27.312 -5.606 33.948 1.00192.74 O
ANISOU 133 OD1 ASN A 51 37597 20835 14802 -1502 -3759 -507 O
ATOM 134 ND2 ASN A 51 25.983 -7.084 34.997 1.00196.15 N
ANISOU 134 ND2 ASN A 51 38994 20637 14896 -2262 -3555 -491 N
ATOM 135 N VAL A 52 28.663 -10.765 32.431 1.00206.49 N
ANISOU 135 N VAL A 52 42281 20562 15615 -668 -3779 -496 N
ATOM 136 CA VAL A 52 29.659 -11.577 31.735 1.00204.42 C
ANISOU 136 CA VAL A 52 42444 20020 15205 -14 -3858 -481 C
ATOM 137 C VAL A 52 29.154 -11.959 30.352 1.00201.71 C
ANISOU 137 C VAL A 52 42215 19585 14841 -239 -3844 -597 C
ATOM 138 O VAL A 52 29.933 -12.014 29.393 1.00201.46 O
ANISOU 138 O VAL A 52 42077 19641 14828 302 -3935 -612 O
ATOM 139 CB VAL A 52 30.031 -12.819 32.569 1.00211.74 C
ANISOU 139 CB VAL A 52 44319 20312 15819 220 -3812 -398 C
ATOM 140 CG1 VAL A 52 30.957 -13.742 31.787 1.00212.89 C
ANISOU 140 CG1 VAL A 52 44974 20132 15782 889 -3872 -393 C
ATOM 141 CG2 VAL A 52 30.678 -12.406 33.884 1.00210.44 C
ANISOU 141 CG2 VAL A 52 43971 20305 15681 553 -3845 -291 C
ATOM 142 N LEU A 53 27.851 -12.216 30.222 1.00206.31 N
ANISOU 142 N LEU A 53 42978 20029 15380 -1041 -3726 -682 N
ATOM 143 CA LEU A 53 27.257 -12.412 28.905 1.00204.03 C
ANISOU 143 CA LEU A 53 42647 19770 15106 -1334 -3714 -814 C
ATOM 144 C LEU A 53 27.590 -11.234 27.995 1.00188.90 C
ANISOU 144 C LEU A 53 39810 18491 13473 -1043 -3811 -863 C
ATOM 145 O LEU A 53 27.974 -11.419 26.836 1.00189.80 O
ANISOU 145 O LEU A 53 39905 18624 13585 -722 -3875 -918 O
ATOM 146 CB LEU A 53 25.741 -12.603 29.044 1.00167.28 C
ANISOU 146 CB LEU A 53 38087 15064 10406 -2307 -3567 -900 C
ATOM 147 CG LEU A 53 24.873 -13.055 27.858 1.00169.16 C
ANISOU 147 CG LEU A 53 38417 15262 10595 -2803 -3522 -1049 C
ATOM 148 CD1 LEU A 53 23.654 -13.827 28.355 1.00173.37 C
ANISOU 148 CD1 LEU A 53 39467 15475 10932 -3684 -3360 -1080 C
ATOM 149 CD2 LEU A 53 24.430 -11.875 27.005 1.00194.15 C
ANISOU 149 CD2 LEU A 53 40601 19128 14040 -2934 -3554 -1158 C
ATOM 150 N VAL A 54 27.490 -10.012 28.526 1.00172.33 N
ANISOU 150 N VAL A 54 36971 16900 11605 -1122 -3818 -834 N
ATOM 151 CA VAL A 54 27.857 -8.825 27.757 1.00164.61 C
ANISOU 151 CA VAL A 54 35152 16506 10887 -836 -3899 -859 C
ATOM 152 C VAL A 54 29.364 -8.765 27.548 1.00166.11 C
ANISOU 152 C VAL A 54 35270 16755 11089 30 -4030 -766 C
ATOM 153 O VAL A 54 29.840 -8.418 26.459 1.00161.16 O
ANISOU 153 O VAL A 54 34292 16385 10558 385 -4098 -795 O
ATOM 154 CB VAL A 54 27.339 -7.556 28.459 1.00159.72 C
ANISOU 154 CB VAL A 54 33844 16358 10484 -1159 -3859 -842 C
ATOM 155 CG1 VAL A 54 27.731 -6.310 27.671 1.00157.40 C
ANISOU 155 CG1 VAL A 54 32744 16623 10439 -865 -3930 -857 C
ATOM 156 CG2 VAL A 54 25.834 -7.625 28.651 1.00157.30 C
ANISOU 156 CG2 VAL A 54 33551 16069 10149 -1992 -3716 -929 C
ATOM 157 N ILE A 55 30.135 -9.090 28.593 1.00173.89 N
ANISOU 157 N ILE A 55 36555 17545 11972 388 -4061 -652 N
ATOM 158 CA ILE A 55 31.596 -9.024 28.525 1.00175.95 C
ANISOU 158 CA ILE A 55 36678 17943 12232 1212 -4177 -560 C
ATOM 159 C ILE A 55 32.109 -9.775 27.303 1.00174.75 C
ANISOU 159 C ILE A 55 36822 17612 11961 1647 -4217 -593 C
ATOM 160 O ILE A 55 32.945 -9.270 26.543 1.00162.80 O
ANISOU 160 O ILE A 55 34828 16468 10562 2150 -4299 -571 O
ATOM 161 CB ILE A 55 32.217 -9.579 29.821 1.00180.34 C
ANISOU 161 CB ILE A 55 37673 18226 12623 1502 -4183 -454 C
ATOM 162 CG1 ILE A 55 31.943 -8.643 31.002 1.00176.24 C
ANISOU 162 CG1 ILE A 55 36724 17990 12250 1205 -4170 -412 C
ATOM 163 CG2 ILE A 55 33.711 -9.816 29.647 1.00183.34 C
ANISOU 163 CG2 ILE A 55 38016 18709 12936 2379 -4287 -376 C
ATOM 164 CD1 ILE A 55 33.027 -7.625 31.255 1.00171.87 C
ANISOU 164 CD1 ILE A 55 35471 17963 11866 1691 -4284 -344 C
ATOM 165 N ILE A 56 31.600 -10.987 27.088 1.00189.74 N
ANISOU 165 N ILE A 56 39529 18941 13623 1439 -4154 -645 N
ATOM 166 CA ILE A 56 32.071 -11.817 25.986 1.00194.58 C
ANISOU 166 CA ILE A 56 40544 19303 14086 1862 -4187 -678 C
ATOM 167 C ILE A 56 31.298 -11.543 24.697 1.00195.98 C
ANISOU 167 C ILE A 56 40444 19653 14367 1495 -4174 -810 C
ATOM 168 O ILE A 56 31.815 -11.795 23.603 1.00200.32 O
ANISOU 168 O ILE A 56 41010 20221 14882 1928 -4226 -837 O
ATOM 169 CB ILE A 56 31.997 -13.304 26.372 1.00200.49 C
ANISOU 169 CB ILE A 56 42383 19297 14496 1873 -4126 -665 C
ATOM 170 CG1 ILE A 56 32.495 -13.503 27.802 1.00207.48 C
ANISOU 170 CG1 ILE A 56 43526 20023 15283 2094 -4113 -549 C
ATOM 171 CG2 ILE A 56 32.834 -14.151 25.419 1.00201.44 C
ANISOU 171 CG2 ILE A 56 42938 19161 14438 2544 -4174 -668 C
ATOM 172 CD1 ILE A 56 32.386 -14.928 28.290 1.00215.51 C
ANISOU 172 CD1 ILE A 56 45661 20266 15956 2092 -4034 -525 C
ATOM 173 N ALA A 57 30.071 -11.026 24.800 1.00193.17 N
ANISOU 173 N ALA A 57 39805 19457 14132 727 -4101 -896 N
ATOM 174 CA ALA A 57 29.312 -10.664 23.607 1.00185.86 C
ANISOU 174 CA ALA A 57 38514 18788 13317 386 -4087 -1032 C
ATOM 175 C ALA A 57 30.053 -9.615 22.785 1.00175.86 C
ANISOU 175 C ALA A 57 36466 18085 12269 899 -4173 -1009 C
ATOM 176 O ALA A 57 30.269 -9.791 21.581 1.00176.73 O
ANISOU 176 O ALA A 57 36545 18242 12362 1165 -4210 -1065 O
ATOM 177 CB ALA A 57 27.921 -10.162 23.999 1.00155.69 C
ANISOU 177 CB ALA A 57 34402 15155 9598 -474 -3984 -1116 C
ATOM 178 N VAL A 58 30.461 -8.515 23.424 1.00169.10 N
ANISOU 178 N VAL A 58 34989 17652 11610 1039 -4201 -921 N
ATOM 179 CA VAL A 58 31.219 -7.480 22.725 1.00163.12 C
ANISOU 179 CA VAL A 58 33503 17421 11053 1503 -4271 -877 C
ATOM 180 C VAL A 58 32.695 -7.838 22.596 1.00166.81 C
ANISOU 180 C VAL A 58 34064 17871 11444 2328 -4357 -762 C
ATOM 181 O VAL A 58 33.387 -7.264 21.745 1.00159.05 O
ANISOU 181 O VAL A 58 32588 17265 10580 2763 -4406 -729 O
ATOM 182 CB VAL A 58 31.072 -6.122 23.434 1.00158.73 C
ANISOU 182 CB VAL A 58 32260 17319 10730 1297 -4262 -829 C
ATOM 183 CG1 VAL A 58 29.611 -5.849 23.770 1.00159.36 C
ANISOU 183 CG1 VAL A 58 32279 17415 10856 504 -4157 -929 C
ATOM 184 CG2 VAL A 58 31.930 -6.073 24.693 1.00163.62 C
ANISOU 184 CG2 VAL A 58 32934 17905 11329 1589 -4307 -700 C
ATOM 185 N PHE A 59 33.179 -8.781 23.416 1.00180.54 N
ANISOU 185 N PHE A 59 36414 19201 12980 2559 -4363 -699 N
ATOM 186 CA PHE A 59 34.592 -9.159 23.441 1.00190.48 C
ANISOU 186 CA PHE A 59 37743 20483 14146 3366 -4431 -591 C
ATOM 187 C PHE A 59 35.148 -9.373 22.040 1.00202.47 C
ANISOU 187 C PHE A 59 39176 22107 15647 3852 -4462 -611 C
ATOM 188 O PHE A 59 36.247 -8.905 21.719 1.00202.29 O
ANISOU 188 O PHE A 59 38657 22493 15711 4435 -4513 -526 O
ATOM 189 CB PHE A 59 34.751 -10.433 24.277 1.00189.93 C
ANISOU 189 CB PHE A 59 38550 19819 13794 3492 -4404 -561 C
ATOM 190 CG PHE A 59 36.173 -10.796 24.615 1.00187.71 C
ANISOU 190 CG PHE A 59 38317 19600 13403 4309 -4456 -453 C
ATOM 191 CD1 PHE A 59 37.215 -9.909 24.406 1.00186.34 C
ANISOU 191 CD1 PHE A 59 37356 20044 13401 4788 -4522 -377 C
ATOM 192 CD2 PHE A 59 36.460 -12.041 25.153 1.00185.09 C
ANISOU 192 CD2 PHE A 59 38825 18717 12782 4586 -4426 -431 C
ATOM 193 CE1 PHE A 59 38.515 -10.258 24.722 1.00187.70 C
ANISOU 193 CE1 PHE A 59 37513 20346 13460 5514 -4558 -291 C
ATOM 194 CE2 PHE A 59 37.754 -12.395 25.472 1.00185.96 C
ANISOU 194 CE2 PHE A 59 38955 18926 12775 5363 -4459 -349 C
ATOM 195 CZ PHE A 59 38.783 -11.504 25.256 1.00187.20 C
ANISOU 195 CZ PHE A 59 38257 19763 13106 5820 -4525 -283 C
ATOM 196 N THR A 60 34.396 -10.070 21.186 1.00216.37 N
ANISOU 196 N THR A 60 41393 23526 17290 3599 -4428 -726 N
ATOM 197 CA THR A 60 34.920 -10.458 19.878 1.00220.59 C
ANISOU 197 CA THR A 60 41978 24074 17761 4094 -4455 -750 C
ATOM 198 C THR A 60 33.743 -10.602 18.905 1.00230.18 C
ANISOU 198 C THR A 60 43326 25160 18971 3554 -4420 -907 C
ATOM 199 O THR A 60 33.250 -11.696 18.618 1.00229.75 O
ANISOU 199 O THR A 60 44018 24580 18697 3371 -4395 -994 O
ATOM 200 CB THR A 60 35.736 -11.746 19.967 1.00225.75 C
ANISOU 200 CB THR A 60 43383 24260 18131 4685 -4463 -709 C
ATOM 201 OG1 THR A 60 35.869 -12.316 18.661 1.00231.10 O
ANISOU 201 OG1 THR A 60 44304 24800 18703 4989 -4471 -773 O
ATOM 202 CG2 THR A 60 35.064 -12.749 20.901 1.00228.62 C
ANISOU 202 CG2 THR A 60 44634 23965 18267 4276 -4411 -739 C
ATOM 203 N SER A 61 33.295 -9.467 18.375 1.00236.36 N
ANISOU 203 N SER A 61 43369 26445 19994 3298 -4416 -947 N
ATOM 204 CA SER A 61 32.184 -9.438 17.435 1.00243.28 C
ANISOU 204 CA SER A 61 44213 27334 20889 2801 -4381 -1106 C
ATOM 205 C SER A 61 32.497 -8.442 16.331 1.00239.19 C
ANISOU 205 C SER A 61 42943 27371 20567 3105 -4403 -1098 C
ATOM 206 O SER A 61 32.841 -7.290 16.610 1.00239.30 O
ANISOU 206 O SER A 61 42277 27852 20795 3203 -4407 -1009 O
ATOM 207 CB SER A 61 30.874 -9.065 18.136 1.00150.62 C
ANISOU 207 CB SER A 61 32383 15618 9227 1948 -4311 -1192 C
ATOM 208 OG SER A 61 29.817 -8.907 17.205 1.00150.06 O
ANISOU 208 OG SER A 61 32132 15691 9194 1484 -4274 -1352 O
ATOM 209 N ARG A 62 32.387 -8.896 15.082 1.00231.59 N
ANISOU 209 N ARG A 62 42132 26342 19522 3256 -4412 -1188 N
ATOM 210 CA ARG A 62 32.636 -8.031 13.937 1.00222.79 C
ANISOU 210 CA ARG A 62 40355 25725 18570 3555 -4419 -1182 C
ATOM 211 C ARG A 62 31.620 -6.899 13.847 1.00211.76 C
ANISOU 211 C ARG A 62 38348 24740 17370 3008 -4371 -1256 C
ATOM 212 O ARG A 62 31.906 -5.871 13.226 1.00210.59 O
ANISOU 212 O ARG A 62 37542 25071 17402 3257 -4362 -1204 O
ATOM 213 CB ARG A 62 32.634 -8.871 12.654 1.00223.51 C
ANISOU 213 CB ARG A 62 40820 25604 18500 3798 -4437 -1279 C
ATOM 214 CG ARG A 62 32.974 -8.113 11.383 1.00219.82 C
ANISOU 214 CG ARG A 62 39733 25615 18172 4191 -4436 -1263 C
ATOM 215 CD ARG A 62 33.216 -9.076 10.234 1.00222.02 C
ANISOU 215 CD ARG A 62 40463 25632 18264 4562 -4462 -1333 C
ATOM 216 NE ARG A 62 32.177 -10.098 10.163 1.00224.27 N
ANISOU 216 NE ARG A 62 41446 25425 18341 4008 -4465 -1515 N
ATOM 217 CZ ARG A 62 32.165 -11.088 9.278 1.00227.97 C
ANISOU 217 CZ ARG A 62 42463 25551 18604 4176 -4491 -1608 C
ATOM 218 NH1 ARG A 62 31.180 -11.974 9.288 1.00231.53 N
ANISOU 218 NH1 ARG A 62 43529 25566 18875 3580 -4485 -1770 N
ATOM 219 NH2 ARG A 62 33.138 -11.191 8.383 1.00229.09 N
ANISOU 219 NH2 ARG A 62 42530 25793 18720 4923 -4515 -1536 N
ATOM 220 N ALA A 63 30.450 -7.052 14.468 1.00200.26 N
ANISOU 220 N ALA A 63 37088 23123 15880 2283 -4326 -1368 N
ATOM 221 CA ALA A 63 29.466 -5.976 14.443 1.00182.53 C
ANISOU 221 CA ALA A 63 34253 21298 13804 1792 -4268 -1436 C
ATOM 222 C ALA A 63 29.793 -4.892 15.461 1.00170.07 C
ANISOU 222 C ALA A 63 32098 20000 12520 1792 -4208 -1285 C
ATOM 223 O ALA A 63 29.532 -3.709 15.216 1.00158.94 O
ANISOU 223 O ALA A 63 29935 19038 11418 1719 -4113 -1252 O
ATOM 224 CB ALA A 63 28.068 -6.536 14.696 1.00183.72 C
ANISOU 224 CB ALA A 63 34716 21246 13845 997 -4210 -1605 C
ATOM 225 N LEU A 64 30.361 -5.274 16.602 1.00169.21 N
ANISOU 225 N LEU A 64 32361 19628 12304 1885 -4259 -1193 N
ATOM 226 CA LEU A 64 30.630 -4.335 17.684 1.00164.04 C
ANISOU 226 CA LEU A 64 31238 19197 11893 1830 -4214 -1070 C
ATOM 227 C LEU A 64 31.889 -3.531 17.386 1.00174.91 C
ANISOU 227 C LEU A 64 32067 20931 13462 2451 -4238 -920 C
ATOM 228 O LEU A 64 32.977 -4.099 17.236 1.00176.49 O
ANISOU 228 O LEU A 64 32549 21030 13480 3019 -4340 -846 O
ATOM 229 CB LEU A 64 30.775 -5.078 19.012 1.00148.27 C
ANISOU 229 CB LEU A 64 29858 16800 9679 1712 -4263 -1033 C
ATOM 230 CG LEU A 64 29.492 -5.334 19.813 1.00141.10 C
ANISOU 230 CG LEU A 64 29212 15690 8709 956 -4187 -1127 C
ATOM 231 CD1 LEU A 64 28.691 -4.050 19.940 1.00135.50 C
ANISOU 231 CD1 LEU A 64 27712 15435 8336 558 -4063 -1134 C
ATOM 232 CD2 LEU A 64 28.640 -6.444 19.214 1.00144.62 C
ANISOU 232 CD2 LEU A 64 30232 15788 8930 588 -4165 -1281 C
ATOM 233 N LYS A 65 31.741 -2.212 17.299 1.00181.09 N
ANISOU 233 N LYS A 65 32080 22142 14585 2342 -4137 -874 N
ATOM 234 CA LYS A 65 32.897 -1.337 17.187 1.00186.83 C
ANISOU 234 CA LYS A 65 32261 23218 15508 2809 -4140 -728 C
ATOM 235 C LYS A 65 33.698 -1.371 18.481 1.00195.61 C
ANISOU 235 C LYS A 65 33487 24264 16573 2934 -4214 -626 C
ATOM 236 O LYS A 65 33.134 -1.445 19.576 1.00194.62 O
ANISOU 236 O LYS A 65 33562 23958 16427 2530 -4201 -651 O
ATOM 237 CB LYS A 65 32.453 0.091 16.877 1.00182.13 C
ANISOU 237 CB LYS A 65 30908 23031 15262 2598 -3992 -709 C
ATOM 238 N ALA A 66 35.022 -1.339 18.349 1.00210.51 N
ANISOU 238 N ALA A 66 35237 26330 18419 3507 -4294 -509 N
ATOM 239 CA ALA A 66 35.925 -1.374 19.495 1.00213.25 C
ANISOU 239 CA ALA A 66 35640 26700 18687 3708 -4382 -412 C
ATOM 240 C ALA A 66 35.794 -0.138 20.390 1.00211.23 C
ANISOU 240 C ALA A 66 34840 26691 18725 3350 -4310 -373 C
ATOM 241 O ALA A 66 35.840 -0.277 21.618 1.00213.06 O
ANISOU 241 O ALA A 66 35280 26791 18884 3205 -4358 -358 O
ATOM 242 CB ALA A 66 37.372 -1.543 19.023 1.00215.85 C
ANISOU 242 CB ALA A 66 35841 27283 18891 4416 -4478 -297 C
ATOM 243 N PRO A 67 35.647 1.080 19.840 1.00202.25 N
ANISOU 243 N PRO A 67 33049 25895 17902 3219 -4191 -355 N
ATOM 244 CA PRO A 67 35.440 2.251 20.717 1.00194.30 C
ANISOU 244 CA PRO A 67 31616 25064 17146 2857 -4111 -330 C
ATOM 245 C PRO A 67 34.327 2.097 21.743 1.00188.14 C
ANISOU 245 C PRO A 67 31135 24011 16338 2337 -4076 -407 C
ATOM 246 O PRO A 67 34.557 2.336 22.935 1.00184.45 O
ANISOU 246 O PRO A 67 30681 23528 15875 2216 -4113 -375 O
ATOM 247 CB PRO A 67 35.138 3.366 19.710 1.00192.91 C
ANISOU 247 CB PRO A 67 30870 25182 17247 2781 -3957 -322 C
ATOM 248 CG PRO A 67 35.953 3.004 18.534 1.00192.73 C
ANISOU 248 CG PRO A 67 30781 25301 17146 3288 -3999 -274 C
ATOM 249 CD PRO A 67 35.905 1.504 18.450 1.00197.01 C
ANISOU 249 CD PRO A 67 32001 25498 17357 3485 -4127 -330 C
ATOM 250 N GLN A 68 33.121 1.715 21.320 1.00187.26 N
ANISOU 250 N GLN A 68 31247 23719 16185 2014 -4004 -509 N
ATOM 251 CA GLN A 68 32.028 1.612 22.283 1.00187.67 C
ANISOU 251 CA GLN A 68 31530 23574 16202 1493 -3953 -574 C
ATOM 252 C GLN A 68 32.192 0.388 23.177 1.00192.21 C
ANISOU 252 C GLN A 68 32791 23762 16478 1503 -4071 -580 C
ATOM 253 O GLN A 68 31.833 0.428 24.361 1.00187.50 O
ANISOU 253 O GLN A 68 32342 23046 15853 1209 -4061 -577 O
ATOM 254 CB GLN A 68 30.675 1.591 21.558 1.00189.06 C
ANISOU 254 CB GLN A 68 31683 23754 16396 1119 -3838 -684 C
ATOM 255 CG GLN A 68 30.176 0.223 21.096 1.00192.12 C
ANISOU 255 CG GLN A 68 32678 23816 16501 1032 -3897 -784 C
ATOM 256 CD GLN A 68 29.299 -0.467 22.131 1.00194.14 C
ANISOU 256 CD GLN A 68 33421 23770 16575 545 -3889 -844 C
ATOM 257 OE1 GLN A 68 29.771 -1.295 22.908 1.00198.71 O
ANISOU 257 OE1 GLN A 68 34525 24028 16947 637 -3983 -812 O
ATOM 258 NE2 GLN A 68 28.016 -0.125 22.143 1.00191.47 N
ANISOU 258 NE2 GLN A 68 32905 23557 16289 40 -3769 -924 N
ATOM 259 N ASN A 69 32.754 -0.697 22.640 1.00204.00 N
ANISOU 259 N ASN A 69 34737 25047 17725 1873 -4175 -583 N
ATOM 260 CA ASN A 69 32.834 -1.946 23.393 1.00209.23 C
ANISOU 260 CA ASN A 69 36162 25282 18055 1902 -4266 -591 C
ATOM 261 C ASN A 69 33.728 -1.798 24.616 1.00203.54 C
ANISOU 261 C ASN A 69 35447 24601 17288 2120 -4349 -491 C
ATOM 262 O ASN A 69 33.376 -2.243 25.714 1.00205.50 O
ANISOU 262 O ASN A 69 36109 24583 17390 1883 -4358 -496 O
ATOM 263 CB ASN A 69 33.341 -3.071 22.489 1.00217.71 C
ANISOU 263 CB ASN A 69 37736 26132 18851 2337 -4354 -607 C
ATOM 264 N LEU A 70 34.890 -1.174 24.441 1.00190.22 N
ANISOU 264 N LEU A 70 33295 23270 15709 2560 -4410 -403 N
ATOM 265 CA LEU A 70 35.815 -0.900 25.534 1.00182.46 C
ANISOU 265 CA LEU A 70 32200 22436 14690 2772 -4500 -318 C
ATOM 266 C LEU A 70 35.124 -0.288 26.749 1.00175.50 C
ANISOU 266 C LEU A 70 31225 21519 13939 2268 -4439 -338 C
ATOM 267 O LEU A 70 35.421 -0.652 27.892 1.00174.89 O
ANISOU 267 O LEU A 70 31451 21312 13689 2315 -4513 -306 O
ATOM 268 CB LEU A 70 36.926 0.029 25.040 1.00180.33 C
ANISOU 268 CB LEU A 70 31245 22668 14605 3127 -4530 -241 C
ATOM 269 N PHE A 71 34.192 0.636 26.511 1.00166.48 N
ANISOU 269 N PHE A 71 29681 20502 13073 1821 -4299 -387 N
ATOM 270 CA PHE A 71 33.544 1.332 27.617 1.00157.34 C
ANISOU 270 CA PHE A 71 28389 19355 12037 1383 -4230 -400 C
ATOM 271 C PHE A 71 32.478 0.461 28.270 1.00148.26 C
ANISOU 271 C PHE A 71 27827 17816 10689 1000 -4191 -453 C
ATOM 272 O PHE A 71 32.369 0.411 29.501 1.00148.15 O
ANISOU 272 O PHE A 71 28011 17685 10594 841 -4207 -434 O
ATOM 273 CB PHE A 71 32.948 2.649 27.123 1.00159.85 C
ANISOU 273 CB PHE A 71 28094 19961 12680 1105 -4082 -423 C
ATOM 274 CG PHE A 71 33.967 3.739 26.942 1.00166.86 C
ANISOU 274 CG PHE A 71 28408 21216 13774 1344 -4097 -360 C
ATOM 275 CD1 PHE A 71 35.292 3.436 26.671 1.00174.54 C
ANISOU 275 CD1 PHE A 71 29330 22332 14654 1829 -4228 -297 C
ATOM 276 CD2 PHE A 71 33.609 5.068 27.069 1.00166.20 C
ANISOU 276 CD2 PHE A 71 27857 21346 13948 1081 -3972 -362 C
ATOM 277 CE1 PHE A 71 36.231 4.438 26.519 1.00177.15 C
ANISOU 277 CE1 PHE A 71 29115 23037 15159 1985 -4235 -241 C
ATOM 278 CE2 PHE A 71 34.542 6.075 26.921 1.00168.28 C
ANISOU 278 CE2 PHE A 71 27641 21915 14384 1237 -3973 -309 C
ATOM 279 CZ PHE A 71 35.855 5.759 26.646 1.00174.15 C
ANISOU 279 CZ PHE A 71 28301 22823 15044 1660 -4105 -250 C
ATOM 280 N LEU A 72 31.683 -0.237 27.458 1.00142.25 N
ANISOU 280 N LEU A 72 27353 16860 9833 829 -4136 -524 N
ATOM 281 CA LEU A 72 30.650 -1.105 28.003 1.00140.30 C
ANISOU 281 CA LEU A 72 27675 16254 9377 402 -4087 -580 C
ATOM 282 C LEU A 72 31.237 -2.339 28.678 1.00141.60 C
ANISOU 282 C LEU A 72 28582 16023 9197 647 -4198 -541 C
ATOM 283 O LEU A 72 30.571 -2.940 29.529 1.00142.83 O
ANISOU 283 O LEU A 72 29222 15876 9172 304 -4158 -554 O
ATOM 284 CB LEU A 72 29.669 -1.502 26.894 1.00130.58 C
ANISOU 284 CB LEU A 72 26531 14964 8121 120 -4007 -683 C
ATOM 285 CG LEU A 72 28.444 -0.591 26.743 1.00128.32 C
ANISOU 285 CG LEU A 72 25754 14957 8043 -373 -3851 -741 C
ATOM 286 CD1 LEU A 72 27.715 -0.823 25.419 1.00132.53 C
ANISOU 286 CD1 LEU A 72 26221 15567 8569 -521 -3796 -843 C
ATOM 287 CD2 LEU A 72 27.505 -0.800 27.926 1.00129.30 C
ANISOU 287 CD2 LEU A 72 26142 14932 8055 -880 -3778 -754 C
ATOM 288 N VAL A 73 32.473 -2.707 28.348 1.00141.24 N
ANISOU 288 N VAL A 73 28637 15994 9034 1251 -4326 -483 N
ATOM 289 CA VAL A 73 33.076 -3.884 28.959 1.00146.93 C
ANISOU 289 CA VAL A 73 30015 16351 9462 1567 -4392 -433 C
ATOM 290 C VAL A 73 33.799 -3.533 30.261 1.00156.77 C
ANISOU 290 C VAL A 73 31140 17719 10707 1753 -4454 -349 C
ATOM 291 O VAL A 73 33.853 -4.361 31.176 1.00158.49 O
ANISOU 291 O VAL A 73 31866 17604 10750 1790 -4439 -314 O
ATOM 292 CB VAL A 73 34.008 -4.590 27.952 1.00142.34 C
ANISOU 292 CB VAL A 73 29580 15724 8780 2163 -4454 -410 C
ATOM 293 CG1 VAL A 73 35.389 -3.945 27.909 1.00139.90 C
ANISOU 293 CG1 VAL A 73 28742 15860 8554 2738 -4562 -321 C
ATOM 294 CG2 VAL A 73 34.104 -6.088 28.247 1.00145.68 C
ANISOU 294 CG2 VAL A 73 30825 15600 8929 2330 -4431 -400 C
ATOM 295 N SER A 74 34.332 -2.311 30.381 1.00161.04 N
ANISOU 295 N SER A 74 31038 18723 11426 1849 -4521 -320 N
ATOM 296 CA SER A 74 34.896 -1.883 31.657 1.00136.33 C
ANISOU 296 CA SER A 74 27767 15736 8296 1931 -4583 -264 C
ATOM 297 C SER A 74 33.796 -1.525 32.646 1.00168.73 C
ANISOU 297 C SER A 74 31941 19707 12460 1348 -4484 -296 C
ATOM 298 O SER A 74 33.971 -1.694 33.859 1.00177.50 O
ANISOU 298 O SER A 74 33254 20721 13465 1358 -4509 -258 O
ATOM 299 CB SER A 74 35.842 -0.698 31.453 1.00134.38 C
ANISOU 299 CB SER A 74 26761 16020 8277 2165 -4651 -233 C
ATOM 300 OG SER A 74 35.128 0.498 31.183 1.00140.45 O
ANISOU 300 OG SER A 74 26967 16994 9404 1725 -4524 -277 O
ATOM 301 N LEU A 75 32.659 -1.033 32.146 1.00160.36 N
ANISOU 301 N LEU A 75 30641 18674 11616 860 -4339 -361 N
ATOM 302 CA LEU A 75 31.495 -0.838 33.000 1.00160.39 C
ANISOU 302 CA LEU A 75 30740 18557 11644 306 -4219 -388 C
ATOM 303 C LEU A 75 30.953 -2.176 33.484 1.00162.49 C
ANISOU 303 C LEU A 75 31826 18343 11571 136 -4198 -390 C
ATOM 304 O LEU A 75 30.636 -2.336 34.669 1.00170.96 O
ANISOU 304 O LEU A 75 33137 19260 12559 -62 -4157 -358 O
ATOM 305 CB LEU A 75 30.426 -0.053 32.238 1.00161.38 C
ANISOU 305 CB LEU A 75 30406 18884 12029 -110 -4068 -454 C
ATOM 306 CG LEU A 75 29.187 0.454 32.977 1.00160.53 C
ANISOU 306 CG LEU A 75 30194 18811 11988 -659 -3923 -479 C
ATOM 307 CD1 LEU A 75 28.096 -0.613 33.087 1.00164.45 C
ANISOU 307 CD1 LEU A 75 31250 18985 12249 -1080 -3839 -520 C
ATOM 308 CD2 LEU A 75 29.574 0.983 34.350 1.00158.25 C
ANISOU 308 CD2 LEU A 75 29847 18575 11705 -624 -3964 -426 C
ATOM 309 N ALA A 76 30.835 -3.147 32.575 1.00160.05 N
ANISOU 309 N ALA A 76 31897 17778 11139 200 -4182 -423 N
ATOM 310 CA ALA A 76 30.421 -4.490 32.952 1.00141.33 C
ANISOU 310 CA ALA A 76 30275 14894 8532 54 -4113 -419 C
ATOM 311 C ALA A 76 31.473 -5.197 33.793 1.00182.25 C
ANISOU 311 C ALA A 76 35851 19853 13543 556 -4186 -327 C
ATOM 312 O ALA A 76 31.137 -6.129 34.533 1.00193.47 O
ANISOU 312 O ALA A 76 37895 20849 14766 414 -4117 -300 O
ATOM 313 CB ALA A 76 30.113 -5.312 31.701 1.00174.93 C
ANISOU 313 CB ALA A 76 34841 18927 12697 20 -4085 -489 C
ATOM 314 N SER A 77 32.738 -4.777 33.695 1.00169.41 N
ANISOU 314 N SER A 77 33867 18526 11975 1137 -4317 -279 N
ATOM 315 CA SER A 77 33.770 -5.371 34.532 1.00172.28 C
ANISOU 315 CA SER A 77 34511 18777 12170 1646 -4386 -198 C
ATOM 316 C SER A 77 33.732 -4.823 35.951 1.00174.06 C
ANISOU 316 C SER A 77 34602 19112 12419 1498 -4392 -160 C
ATOM 317 O SER A 77 34.061 -5.546 36.895 1.00175.31 O
ANISOU 317 O SER A 77 35201 19018 12389 1703 -4389 -105 O
ATOM 318 CB SER A 77 35.153 -5.148 33.921 1.00175.07 C
ANISOU 318 CB SER A 77 34478 19487 12555 2313 -4517 -162 C
ATOM 319 OG SER A 77 35.561 -3.801 34.063 1.00174.04 O
ANISOU 319 OG SER A 77 33604 19891 12633 2307 -4597 -159 O
ATOM 320 N ALA A 78 33.339 -3.561 36.128 1.00179.44 N
ANISOU 320 N ALA A 78 34710 20153 13317 1168 -4394 -190 N
ATOM 321 CA ALA A 78 33.174 -3.042 37.481 1.00141.82 C
ANISOU 321 CA ALA A 78 29858 15460 8567 980 -4387 -165 C
ATOM 322 C ALA A 78 31.953 -3.656 38.152 1.00147.59 C
ANISOU 322 C ALA A 78 31104 15788 9185 473 -4233 -165 C
ATOM 323 O ALA A 78 31.973 -3.935 39.356 1.00144.90 O
ANISOU 323 O ALA A 78 31039 15293 8725 475 -4215 -115 O
ATOM 324 CB ALA A 78 33.069 -1.519 37.455 1.00138.01 C
ANISOU 324 CB ALA A 78 28673 15435 8328 769 -4421 -203 C
ATOM 325 N ASP A 79 30.885 -3.884 37.384 1.00147.14 N
ANISOU 325 N ASP A 79 31172 15584 9149 27 -4119 -221 N
ATOM 326 CA ASP A 79 29.698 -4.525 37.938 1.00155.03 C
ANISOU 326 CA ASP A 79 32652 16236 10016 -509 -3963 -221 C
ATOM 327 C ASP A 79 29.986 -5.971 38.317 1.00159.36 C
ANISOU 327 C ASP A 79 34012 16254 10285 -306 -3940 -167 C
ATOM 328 O ASP A 79 29.560 -6.436 39.381 1.00159.88 O
ANISOU 328 O ASP A 79 34496 16048 10204 -518 -3854 -118 O
ATOM 329 CB ASP A 79 28.545 -4.442 36.937 1.00166.68 C
ANISOU 329 CB ASP A 79 34017 17752 11562 -1030 -3856 -308 C
ATOM 330 CG ASP A 79 28.146 -3.007 36.626 1.00171.10 C
ANISOU 330 CG ASP A 79 33818 18816 12375 -1232 -3849 -357 C
ATOM 331 OD1 ASP A 79 28.388 -2.120 37.472 1.00171.23 O
ANISOU 331 OD1 ASP A 79 33504 19067 12489 -1173 -3880 -323 O
ATOM 332 OD2 ASP A 79 27.584 -2.759 35.540 1.00170.71 O
ANISOU 332 OD2 ASP A 79 33523 18924 12415 -1442 -3808 -432 O
ATOM 333 N ILE A 80 30.725 -6.694 37.469 1.00166.02 N
ANISOU 333 N ILE A 80 35109 16933 11036 132 -4007 -171 N
ATOM 334 CA ILE A 80 31.065 -8.079 37.778 1.00174.36 C
ANISOU 334 CA ILE A 80 36986 17454 11807 396 -3979 -120 C
ATOM 335 C ILE A 80 32.084 -8.162 38.909 1.00178.74 C
ANISOU 335 C ILE A 80 37611 18036 12265 926 -4054 -36 C
ATOM 336 O ILE A 80 32.134 -9.174 39.617 1.00187.71 O
ANISOU 336 O ILE A 80 39441 18722 13157 1037 -3993 17 O
ATOM 337 CB ILE A 80 31.565 -8.810 36.513 1.00180.82 C
ANISOU 337 CB ILE A 80 38060 18099 12545 753 -4022 -154 C
ATOM 338 CG1 ILE A 80 31.608 -10.328 36.733 1.00190.11 C
ANISOU 338 CG1 ILE A 80 40223 18611 13399 888 -3950 -120 C
ATOM 339 CG2 ILE A 80 32.932 -8.317 36.102 1.00178.75 C
ANISOU 339 CG2 ILE A 80 37293 18245 12379 1465 -4178 -130 C
ATOM 340 CD1 ILE A 80 33.001 -10.896 37.004 1.00193.85 C
ANISOU 340 CD1 ILE A 80 40928 19008 13716 1738 -4041 -54 C
ATOM 341 N LEU A 81 32.886 -7.113 39.118 1.00172.90 N
ANISOU 341 N LEU A 81 36175 17821 11697 1238 -4182 -27 N
ATOM 342 CA LEU A 81 33.807 -7.111 40.250 1.00170.54 C
ANISOU 342 CA LEU A 81 35869 17626 11304 1688 -4259 37 C
ATOM 343 C LEU A 81 33.086 -6.825 41.561 1.00170.86 C
ANISOU 343 C LEU A 81 35994 17595 11331 1279 -4181 64 C
ATOM 344 O LEU A 81 33.396 -7.441 42.586 1.00168.68 O
ANISOU 344 O LEU A 81 36140 17092 10860 1509 -4165 124 O
ATOM 345 CB LEU A 81 34.930 -6.094 40.030 1.00161.99 C
ANISOU 345 CB LEU A 81 34011 17154 10383 2110 -4425 29 C
ATOM 346 CG LEU A 81 36.025 -6.470 39.027 1.00158.02 C
ANISOU 346 CG LEU A 81 33415 16791 9834 2719 -4518 34 C
ATOM 347 CD1 LEU A 81 37.326 -5.737 39.323 1.00156.40 C
ANISOU 347 CD1 LEU A 81 32582 17164 9679 3204 -4676 55 C
ATOM 348 CD2 LEU A 81 36.244 -7.976 38.982 1.00163.11 C
ANISOU 348 CD2 LEU A 81 34874 16909 10193 3072 -4456 69 C
ATOM 349 N VAL A 82 32.121 -5.904 41.553 1.00173.38 N
ANISOU 349 N VAL A 82 35921 18114 11842 703 -4122 22 N
ATOM 350 CA VAL A 82 31.469 -5.528 42.803 1.00173.04 C
ANISOU 350 CA VAL A 82 35889 18065 11792 349 -4048 49 C
ATOM 351 C VAL A 82 30.419 -6.552 43.213 1.00171.98 C
ANISOU 351 C VAL A 82 36480 17407 11458 -87 -3867 83 C
ATOM 352 O VAL A 82 30.160 -6.735 44.409 1.00156.67 O
ANISOU 352 O VAL A 82 34812 15316 9401 -191 -3802 140 O
ATOM 353 CB VAL A 82 30.873 -4.113 42.695 1.00171.73 C
ANISOU 353 CB VAL A 82 35023 18336 11891 -52 -4042 -7 C
ATOM 354 CG1 VAL A 82 29.361 -4.123 42.919 1.00147.47 C
ANISOU 354 CG1 VAL A 82 32106 15114 8814 -748 -3855 -16 C
ATOM 355 CG2 VAL A 82 31.546 -3.208 43.693 1.00146.62 C
ANISOU 355 CG2 VAL A 82 31435 15494 8780 174 -4149 5 C
ATOM 356 N ALA A 83 29.810 -7.241 42.247 1.00169.57 N
ANISOU 356 N ALA A 83 36513 16821 11094 -362 -3783 48 N
ATOM 357 CA ALA A 83 28.822 -8.257 42.585 1.00174.12 C
ANISOU 357 CA ALA A 83 37813 16892 11453 -837 -3608 75 C
ATOM 358 C ALA A 83 29.453 -9.441 43.296 1.00178.75 C
ANISOU 358 C ALA A 83 39176 16986 11755 -427 -3595 153 C
ATOM 359 O ALA A 83 28.767 -10.157 44.034 1.00186.07 O
ANISOU 359 O ALA A 83 40707 17507 12485 -771 -3449 201 O
ATOM 360 CB ALA A 83 28.111 -8.737 41.329 1.00178.37 C
ANISOU 360 CB ALA A 83 38536 17261 11977 -1221 -3538 3 C
ATOM 361 N THR A 84 30.746 -9.671 43.084 1.00180.30 N
ANISOU 361 N THR A 84 39368 17224 11912 311 -3734 166 N
ATOM 362 CA THR A 84 31.408 -10.815 43.694 1.00183.66 C
ANISOU 362 CA THR A 84 40526 17202 12052 790 -3717 230 C
ATOM 363 C THR A 84 32.154 -10.443 44.970 1.00178.74 C
ANISOU 363 C THR A 84 39701 16810 11402 1209 -3790 287 C
ATOM 364 O THR A 84 31.966 -11.085 46.007 1.00180.79 O
ANISOU 364 O THR A 84 40519 16716 11455 1195 -3694 347 O
ATOM 365 CB THR A 84 32.375 -11.463 42.699 1.00187.22 C
ANISOU 365 CB THR A 84 41169 17546 12420 1400 -3803 208 C
ATOM 366 OG1 THR A 84 33.302 -10.482 42.218 1.00168.39 O
ANISOU 366 OG1 THR A 84 37947 15783 10252 1821 -3976 181 O
ATOM 367 CG2 THR A 84 31.613 -12.061 41.531 1.00190.72 C
ANISOU 367 CG2 THR A 84 41996 17644 12824 991 -3718 151 C
ATOM 368 N LEU A 85 32.994 -9.408 44.914 1.00177.41 N
ANISOU 368 N LEU A 85 38744 17237 11426 1559 -3956 264 N
ATOM 369 CA LEU A 85 33.885 -9.114 46.028 1.00167.94 C
ANISOU 369 CA LEU A 85 37340 16299 10172 2027 -4053 303 C
ATOM 370 C LEU A 85 33.259 -8.225 47.095 1.00184.68 C
ANISOU 370 C LEU A 85 39142 18630 12398 1610 -4024 312 C
ATOM 371 O LEU A 85 33.800 -8.154 48.203 1.00191.41 O
ANISOU 371 O LEU A 85 39985 19591 13153 1916 -4074 348 O
ATOM 372 CB LEU A 85 35.173 -8.462 45.518 1.00166.39 C
ANISOU 372 CB LEU A 85 36463 16666 10090 2595 -4248 270 C
ATOM 373 CG LEU A 85 36.126 -9.359 44.725 1.00169.42 C
ANISOU 373 CG LEU A 85 37118 16934 10319 3226 -4294 276 C
ATOM 374 CD1 LEU A 85 37.512 -8.738 44.638 1.00168.89 C
ANISOU 374 CD1 LEU A 85 36366 17499 10304 3827 -4479 266 C
ATOM 375 CD2 LEU A 85 36.196 -10.747 45.344 1.00174.86 C
ANISOU 375 CD2 LEU A 85 38727 17033 10679 3514 -4186 330 C
ATOM 376 N VAL A 86 32.147 -7.548 46.809 1.00178.83 N
ANISOU 376 N VAL A 86 38135 17972 11839 949 -3944 277 N
ATOM 377 CA VAL A 86 31.605 -6.587 47.767 1.00176.69 C
ANISOU 377 CA VAL A 86 37494 17961 11681 606 -3921 279 C
ATOM 378 C VAL A 86 30.147 -6.897 48.094 1.00179.06 C
ANISOU 378 C VAL A 86 38176 17938 11919 -85 -3710 308 C
ATOM 379 O VAL A 86 29.707 -6.718 49.237 1.00180.16 O
ANISOU 379 O VAL A 86 38394 18059 11999 -272 -3637 352 O
ATOM 380 CB VAL A 86 31.762 -5.145 47.244 1.00171.48 C
ANISOU 380 CB VAL A 86 35964 17874 11318 519 -4036 202 C
ATOM 381 CG1 VAL A 86 31.014 -4.154 48.130 1.00153.43 C
ANISOU 381 CG1 VAL A 86 33353 15801 9142 104 -3982 194 C
ATOM 382 CG2 VAL A 86 33.235 -4.769 47.174 1.00155.50 C
ANISOU 382 CG2 VAL A 86 33532 16229 9321 1156 -4243 182 C
ATOM 383 N ILE A 87 29.395 -7.383 47.111 1.00176.95 N
ANISOU 383 N ILE A 87 38147 17440 11646 -474 -3607 281 N
ATOM 384 CA ILE A 87 27.960 -7.625 47.276 1.00176.90 C
ANISOU 384 CA ILE A 87 38415 17222 11578 -1209 -3404 296 C
ATOM 385 C ILE A 87 27.647 -8.572 48.436 1.00179.18 C
ANISOU 385 C ILE A 87 39440 17050 11590 -1301 -3267 388 C
ATOM 386 O ILE A 87 26.837 -8.211 49.300 1.00166.00 O
ANISOU 386 O ILE A 87 37704 15460 9910 -1705 -3154 424 O
ATOM 387 CB ILE A 87 27.341 -8.141 45.966 1.00162.28 C
ANISOU 387 CB ILE A 87 36747 15191 9722 -1573 -3333 239 C
ATOM 388 N PRO A 88 28.237 -9.775 48.517 1.00179.93 N
ANISOU 388 N PRO A 88 40257 16661 11447 -930 -3259 429 N
ATOM 389 CA PRO A 88 27.790 -10.721 49.559 1.00186.87 C
ANISOU 389 CA PRO A 88 41909 17045 12049 -1099 -3094 512 C
ATOM 390 C PRO A 88 27.998 -10.215 50.975 1.00193.13 C
ANISOU 390 C PRO A 88 42521 18032 12828 -910 -3109 571 C
ATOM 391 O PRO A 88 27.167 -10.491 51.850 1.00195.25 O
ANISOU 391 O PRO A 88 43135 18092 12961 -1320 -2941 632 O
ATOM 392 CB PRO A 88 28.632 -11.971 49.271 1.00186.56 C
ANISOU 392 CB PRO A 88 42603 16503 11777 -567 -3115 526 C
ATOM 393 CG PRO A 88 29.843 -11.452 48.569 1.00181.06 C
ANISOU 393 CG PRO A 88 41352 16201 11243 90 -3335 475 C
ATOM 394 CD PRO A 88 29.335 -10.342 47.713 1.00177.71 C
ANISOU 394 CD PRO A 88 40150 16254 11116 -314 -3385 403 C
ATOM 395 N PHE A 89 29.079 -9.471 51.228 1.00193.16 N
ANISOU 395 N PHE A 89 41983 18450 12958 -322 -3304 549 N
ATOM 396 CA PHE A 89 29.370 -9.043 52.594 1.00191.78 C
ANISOU 396 CA PHE A 89 41672 18452 12743 -99 -3335 594 C
ATOM 397 C PHE A 89 28.297 -8.095 53.108 1.00186.40 C
ANISOU 397 C PHE A 89 40581 18047 12198 -690 -3244 596 C
ATOM 398 O PHE A 89 27.956 -8.117 54.296 1.00187.06 O
ANISOU 398 O PHE A 89 40848 18061 12165 -779 -3157 659 O
ATOM 399 CB PHE A 89 30.741 -8.367 52.675 1.00192.75 C
ANISOU 399 CB PHE A 89 41235 19033 12969 583 -3574 551 C
ATOM 400 CG PHE A 89 31.879 -9.190 52.129 1.00197.68 C
ANISOU 400 CG PHE A 89 42138 19509 13462 1233 -3672 546 C
ATOM 401 CD1 PHE A 89 31.730 -10.540 51.853 1.00202.10 C
ANISOU 401 CD1 PHE A 89 43535 19467 13786 1283 -3545 584 C
ATOM 402 CD2 PHE A 89 33.111 -8.600 51.905 1.00195.91 C
ANISOU 402 CD2 PHE A 89 41340 19765 13332 1796 -3885 499 C
ATOM 403 CE1 PHE A 89 32.781 -11.276 51.349 1.00204.05 C
ANISOU 403 CE1 PHE A 89 44039 19590 13900 1929 -3626 575 C
ATOM 404 CE2 PHE A 89 34.166 -9.332 51.406 1.00196.61 C
ANISOU 404 CE2 PHE A 89 41632 19786 13286 2423 -3966 497 C
ATOM 405 CZ PHE A 89 34.002 -10.672 51.128 1.00201.01 C
ANISOU 405 CZ PHE A 89 43025 19736 13613 2518 -3835 535 C
ATOM 406 N SER A 90 27.751 -7.256 52.223 1.00184.72 N
ANISOU 406 N SER A 90 39810 18158 12218 -1072 -3254 529 N
ATOM 407 CA SER A 90 26.725 -6.300 52.625 1.00183.50 C
ANISOU 407 CA SER A 90 39223 18310 12187 -1590 -3160 524 C
ATOM 408 C SER A 90 25.490 -6.998 53.182 1.00181.53 C
ANISOU 408 C SER A 90 39498 17736 11738 -2172 -2914 601 C
ATOM 409 O SER A 90 24.791 -6.436 54.030 1.00179.48 O
ANISOU 409 O SER A 90 39047 17666 11482 -2456 -2819 636 O
ATOM 410 CB SER A 90 26.348 -5.415 51.436 1.00184.73 C
ANISOU 410 CB SER A 90 38755 18835 12599 -1864 -3196 433 C
ATOM 411 OG SER A 90 27.493 -4.782 50.890 1.00185.52 O
ANISOU 411 OG SER A 90 38386 19231 12874 -1362 -3411 365 O
ATOM 412 N LEU A 91 25.212 -8.221 52.724 1.00182.13 N
ANISOU 412 N LEU A 91 40250 17326 11625 -2364 -2803 627 N
ATOM 413 CA LEU A 91 24.058 -8.959 53.227 1.00184.86 C
ANISOU 413 CA LEU A 91 41140 17346 11753 -2974 -2559 697 C
ATOM 414 C LEU A 91 24.312 -9.479 54.637 1.00201.81 C
ANISOU 414 C LEU A 91 43785 19208 13686 -2725 -2497 793 C
ATOM 415 O LEU A 91 23.523 -9.226 55.555 1.00207.04 O
ANISOU 415 O LEU A 91 44415 19963 14286 -3074 -2357 853 O
ATOM 416 CB LEU A 91 23.720 -10.108 52.277 1.00182.52 C
ANISOU 416 CB LEU A 91 41459 16586 11303 -3286 -2463 678 C
ATOM 417 N ALA A 92 25.417 -10.204 54.827 1.00208.83 N
ANISOU 417 N ALA A 92 45121 19776 14447 -2089 -2595 808 N
ATOM 418 CA ALA A 92 25.756 -10.718 56.151 1.00213.73 C
ANISOU 418 CA ALA A 92 46215 20140 14855 -1767 -2545 890 C
ATOM 419 C ALA A 92 25.965 -9.582 57.146 1.00180.32 C
ANISOU 419 C ALA A 92 41367 16397 10749 -1557 -2637 899 C
ATOM 420 O ALA A 92 25.474 -9.637 58.278 1.00183.51 O
ANISOU 420 O ALA A 92 41965 16735 11024 -1710 -2511 972 O
ATOM 421 CB ALA A 92 27.003 -11.598 56.065 1.00186.10 C
ANISOU 421 CB ALA A 92 43202 16304 11203 -1029 -2652 886 C
ATOM 422 N ASN A 93 26.696 -8.540 56.739 1.00176.16 N
ANISOU 422 N ASN A 93 40108 16360 10464 -1218 -2854 820 N
ATOM 423 CA ASN A 93 26.870 -7.372 57.598 1.00185.86 C
ANISOU 423 CA ASN A 93 40742 18058 11818 -1074 -2950 805 C
ATOM 424 C ASN A 93 25.530 -6.741 57.947 1.00191.14 C
ANISOU 424 C ASN A 93 41171 18911 12544 -1728 -2779 831 C
ATOM 425 O ASN A 93 25.387 -6.126 59.012 1.00196.62 O
ANISOU 425 O ASN A 93 41663 19815 13229 -1690 -2771 857 O
ATOM 426 CB ASN A 93 27.780 -6.347 56.910 1.00180.34 C
ANISOU 426 CB ASN A 93 39311 17837 11372 -724 -3193 699 C
ATOM 427 CG ASN A 93 28.169 -5.197 57.821 1.00175.97 C
ANISOU 427 CG ASN A 93 38215 17727 10918 -512 -3319 664 C
ATOM 428 OD1 ASN A 93 27.338 -4.359 58.174 1.00174.92 O
ANISOU 428 OD1 ASN A 93 37757 17821 10884 -899 -3242 658 O
ATOM 429 ND2 ASN A 93 29.445 -5.141 58.190 1.00176.03 N
ANISOU 429 ND2 ASN A 93 38113 17884 10885 108 -3514 633 N
ATOM 430 N GLU A 94 24.536 -6.888 57.066 1.00198.23 N
ANISOU 430 N GLU A 94 42076 19762 13481 -2320 -2641 822 N
ATOM 431 CA GLU A 94 23.207 -6.361 57.335 1.00210.06 C
ANISOU 431 CA GLU A 94 43330 21484 14997 -2949 -2458 851 C
ATOM 432 C GLU A 94 22.422 -7.238 58.301 1.00229.40 C
ANISOU 432 C GLU A 94 46403 23587 17172 -3288 -2225 966 C
ATOM 433 O GLU A 94 21.579 -6.715 59.037 1.00231.60 O
ANISOU 433 O GLU A 94 46465 24105 17427 -3605 -2096 1013 O
ATOM 434 CB GLU A 94 22.437 -6.191 56.020 1.00202.15 C
ANISOU 434 CB GLU A 94 42054 20636 14118 -3457 -2396 790 C
ATOM 435 CG GLU A 94 21.181 -5.339 56.125 1.00197.36 C
ANISOU 435 CG GLU A 94 40959 20454 13575 -4006 -2247 793 C
ATOM 436 CD GLU A 94 21.392 -4.104 56.977 1.00192.96 C
ANISOU 436 CD GLU A 94 39873 20300 13143 -3722 -2329 783 C
ATOM 437 OE1 GLU A 94 20.784 -4.012 58.065 1.00193.65 O
ANISOU 437 OE1 GLU A 94 40043 20435 13102 -3882 -2194 862 O
ATOM 438 OE2 GLU A 94 22.180 -3.228 56.566 1.00189.41 O
ANISOU 438 OE2 GLU A 94 38943 20112 12911 -3343 -2527 694 O
ATOM 439 N VAL A 95 22.680 -8.547 58.326 1.00251.17 N
ANISOU 439 N VAL A 95 49938 25785 19709 -3217 -2159 1011 N
ATOM 440 CA VAL A 95 22.053 -9.437 59.300 1.00261.89 C
ANISOU 440 CA VAL A 95 51958 26759 20789 -3495 -1936 1118 C
ATOM 441 C VAL A 95 23.062 -10.480 59.769 1.00269.40 C
ANISOU 441 C VAL A 95 53624 27196 21540 -2915 -1983 1150 C
ATOM 442 O VAL A 95 23.438 -11.375 59.006 1.00274.62 O
ANISOU 442 O VAL A 95 54769 27457 22117 -2821 -1995 1120 O
ATOM 443 CB VAL A 95 20.802 -10.130 58.722 1.00266.08 C
ANISOU 443 CB VAL A 95 52823 27085 21192 -4327 -1697 1136 C
ATOM 444 CG1 VAL A 95 20.284 -11.173 59.693 1.00272.37 C
ANISOU 444 CG1 VAL A 95 54391 27416 21680 -4597 -1465 1238 C
ATOM 445 CG2 VAL A 95 19.699 -9.130 58.402 1.00263.27 C
ANISOU 445 CG2 VAL A 95 51748 27300 20983 -4898 -1617 1116 C
ATOM 446 N MET A 96 23.496 -10.371 61.027 1.00271.20 N
ANISOU 446 N MET A 96 53926 27441 21675 -2502 -2006 1205 N
ATOM 447 CA MET A 96 24.355 -11.353 61.687 1.00267.59 C
ANISOU 447 CA MET A 96 54152 26534 20986 -1937 -2018 1245 C
ATOM 448 C MET A 96 25.739 -11.415 61.059 1.00268.23 C
ANISOU 448 C MET A 96 54137 26640 21138 -1212 -2263 1170 C
ATOM 449 O MET A 96 26.176 -12.485 60.618 1.00274.50 O
ANISOU 449 O MET A 96 55560 26967 21771 -990 -2240 1165 O
ATOM 450 CB MET A 96 23.720 -12.748 61.662 1.00257.06 C
ANISOU 450 CB MET A 96 53758 24541 19373 -2341 -1769 1298 C
ATOM 451 CG MET A 96 22.353 -12.836 62.295 1.00243.46 C
ANISOU 451 CG MET A 96 52182 22787 17536 -3093 -1501 1377 C
ATOM 452 SD MET A 96 22.447 -12.775 64.089 1.00245.24 S
ANISOU 452 SD MET A 96 52568 23020 17591 -2764 -1428 1482 S
ATOM 453 CE MET A 96 20.730 -12.489 64.481 1.00203.95 C
ANISOU 453 CE MET A 96 47170 17999 12324 -3730 -1144 1560 C
ATOM 454 N GLY A 97 26.443 -10.288 61.031 1.00258.99 N
ANISOU 454 N GLY A 97 52199 26017 20190 -838 -2492 1107 N
ATOM 455 CA GLY A 97 27.755 -10.261 60.413 1.00251.79 C
ANISOU 455 CA GLY A 97 51092 25230 19349 -183 -2726 1034 C
ATOM 456 C GLY A 97 28.640 -9.194 60.985 1.00241.85 C
ANISOU 456 C GLY A 97 49155 24519 18218 301 -2952 985 C
ATOM 457 O GLY A 97 28.179 -8.128 61.413 1.00239.86 O
ANISOU 457 O GLY A 97 48370 24652 18115 43 -2969 967 O
ATOM 458 N TYR A 98 29.942 -9.475 60.991 1.00235.92 N
ANISOU 458 N TYR A 98 48422 23824 17392 1016 -3126 953 N
ATOM 459 CA TYR A 98 30.964 -8.498 61.309 1.00224.80 C
ANISOU 459 CA TYR A 98 46330 22985 16098 1484 -3374 881 C
ATOM 460 C TYR A 98 32.222 -8.871 60.543 1.00213.23 C
ANISOU 460 C TYR A 98 44804 21605 14610 2088 -3546 829 C
ATOM 461 O TYR A 98 32.361 -9.996 60.057 1.00187.94 O
ANISOU 461 O TYR A 98 42202 17960 11247 2257 -3462 863 O
ATOM 462 CB TYR A 98 31.246 -8.436 62.815 1.00228.52 C
ANISOU 462 CB TYR A 98 46896 23535 16394 1794 -3386 920 C
ATOM 463 N TRP A 99 33.136 -7.910 60.435 1.00199.89 N
ANISOU 463 N TRP A 99 42389 20495 13066 2400 -3782 742 N
ATOM 464 CA TRP A 99 34.425 -8.168 59.807 1.00193.20 C
ANISOU 464 CA TRP A 99 41379 19849 12179 3010 -3956 695 C
ATOM 465 C TRP A 99 35.098 -9.368 60.467 1.00203.76 C
ANISOU 465 C TRP A 99 43357 20883 13182 3622 -3916 757 C
ATOM 466 O TRP A 99 35.216 -9.438 61.697 1.00213.40 O
ANISOU 466 O TRP A 99 44729 22118 14235 3823 -3903 791 O
ATOM 467 CB TRP A 99 35.319 -6.933 59.916 1.00183.74 C
ANISOU 467 CB TRP A 99 39321 19361 11132 3227 -4208 596 C
ATOM 468 N TYR A 100 35.511 -10.326 59.642 1.00217.97 N
ANISOU 468 N TYR A 100 45560 22388 14871 3929 -3885 768 N
ATOM 469 CA TYR A 100 36.197 -11.530 60.087 1.00239.11 C
ANISOU 469 CA TYR A 100 48888 24746 17218 4569 -3834 815 C
ATOM 470 C TYR A 100 37.587 -11.574 59.470 1.00255.00 C
ANISOU 470 C TYR A 100 50533 27164 19191 5262 -4026 759 C
ATOM 471 O TYR A 100 37.858 -10.932 58.453 1.00256.61 O
ANISOU 471 O TYR A 100 50158 27724 19617 5168 -4151 698 O
ATOM 472 CB TYR A 100 35.415 -12.790 59.704 1.00200.22 C
ANISOU 472 CB TYR A 100 44917 19024 12135 4339 -3589 874 C
ATOM 473 N PHE A 101 38.470 -12.353 60.096 1.00270.12 N
ANISOU 473 N PHE A 101 52791 29037 20806 5974 -4037 782 N
ATOM 474 CA PHE A 101 39.872 -12.433 59.697 1.00276.39 C
ANISOU 474 CA PHE A 101 53218 30292 21506 6708 -4211 735 C
ATOM 475 C PHE A 101 40.468 -11.041 59.512 1.00274.71 C
ANISOU 475 C PHE A 101 51932 30913 21533 6633 -4459 655 C
ATOM 476 O PHE A 101 41.180 -10.778 58.535 1.00268.40 O
ANISOU 476 O PHE A 101 50663 30488 20831 6834 -4586 605 O
ATOM 477 CB PHE A 101 40.030 -13.259 58.418 1.00277.33 C
ANISOU 477 CB PHE A 101 53707 30075 21592 6889 -4146 730 C
ATOM 478 CG PHE A 101 41.326 -14.024 58.348 1.00283.29 C
ANISOU 478 CG PHE A 101 54594 30976 22067 7803 -4202 719 C
ATOM 479 CD1 PHE A 101 42.537 -13.362 58.254 1.00284.49 C
ANISOU 479 CD1 PHE A 101 53918 31932 22241 8262 -4427 667 C
ATOM 480 CD2 PHE A 101 41.329 -15.409 58.371 1.00289.19 C
ANISOU 480 CD2 PHE A 101 56307 31063 22511 8194 -4020 754 C
ATOM 481 CE1 PHE A 101 43.727 -14.056 58.190 1.00289.76 C
ANISOU 481 CE1 PHE A 101 54666 32795 22636 9112 -4469 657 C
ATOM 482 CE2 PHE A 101 42.520 -16.114 58.305 1.00294.23 C
ANISOU 482 CE2 PHE A 101 57074 31847 22872 9081 -4058 737 C
ATOM 483 CZ PHE A 101 43.720 -15.436 58.214 1.00294.48 C
ANISOU 483 CZ PHE A 101 56224 32734 22932 9550 -4281 692 C
ATOM 484 N GLY A 102 40.167 -10.145 60.434 1.00293.83 N
ANISOU 484 N GLY A 102 53985 33615 24043 6327 -4520 637 N
ATOM 485 CA GLY A 102 40.813 -8.850 60.426 1.00300.76 C
ANISOU 485 CA GLY A 102 53915 35267 25094 6283 -4757 545 C
ATOM 486 C GLY A 102 39.914 -7.750 59.892 1.00280.86 C
ANISOU 486 C GLY A 102 50965 32826 22924 5523 -4764 499 C
ATOM 487 O GLY A 102 38.998 -7.983 59.096 1.00187.72 O
ANISOU 487 O GLY A 102 39457 20599 11267 5092 -4620 528 O
ATOM 488 N LYS A 103 40.179 -6.521 60.346 1.00252.64 N
ANISOU 488 N LYS A 103 46698 29817 19478 5352 -4933 416 N
ATOM 489 CA LYS A 103 39.499 -5.343 59.824 1.00247.62 C
ANISOU 489 CA LYS A 103 45576 29342 19167 4707 -4962 350 C
ATOM 490 C LYS A 103 39.929 -5.022 58.397 1.00243.97 C
ANISOU 490 C LYS A 103 44681 29128 18888 4689 -5050 300 C
ATOM 491 O LYS A 103 39.235 -4.271 57.707 1.00239.89 O
ANISOU 491 O LYS A 103 43899 28609 18640 4161 -5025 260 O
ATOM 492 CB LYS A 103 39.765 -4.155 60.753 1.00242.94 C
ANISOU 492 CB LYS A 103 44424 29261 18620 4582 -5121 259 C
ATOM 493 CG LYS A 103 39.270 -2.809 60.238 1.00239.68 C
ANISOU 493 CG LYS A 103 43451 29093 18526 3996 -5176 165 C
ATOM 494 CD LYS A 103 39.644 -1.673 61.175 1.00244.84 C
ANISOU 494 CD LYS A 103 43605 30234 19189 3911 -5343 58 C
ATOM 495 CE LYS A 103 39.012 -0.357 60.738 1.00247.26 C
ANISOU 495 CE LYS A 103 43472 30679 19798 3314 -5360 -37 C
ATOM 496 NZ LYS A 103 39.063 0.665 61.821 1.00253.06 N
ANISOU 496 NZ LYS A 103 43911 31716 20525 3155 -5464 -135 N
ATOM 497 N ALA A 104 41.047 -5.584 57.937 1.00247.10 N
ANISOU 497 N ALA A 104 45004 29744 19137 5271 -5142 304 N
ATOM 498 CA ALA A 104 41.490 -5.420 56.557 1.00243.25 C
ANISOU 498 CA ALA A 104 44159 29471 18795 5315 -5209 273 C
ATOM 499 C ALA A 104 40.343 -5.680 55.592 1.00230.23 C
ANISOU 499 C ALA A 104 42863 27284 17330 4845 -5033 307 C
ATOM 500 O ALA A 104 40.222 -5.007 54.563 1.00219.56 O
ANISOU 500 O ALA A 104 41091 26115 16216 4558 -5077 257 O
ATOM 501 CB ALA A 104 42.665 -6.353 56.257 1.00252.65 C
ANISOU 501 CB ALA A 104 45454 30802 19741 6061 -5259 305 C
ATOM 502 N TRP A 105 39.492 -6.649 55.933 1.00228.66 N
ANISOU 502 N TRP A 105 43440 26431 17008 4746 -4832 388 N
ATOM 503 CA TRP A 105 38.276 -6.885 55.164 1.00223.01 C
ANISOU 503 CA TRP A 105 43079 25212 16441 4204 -4656 415 C
ATOM 504 C TRP A 105 37.368 -5.656 55.155 1.00223.36 C
ANISOU 504 C TRP A 105 42682 25418 16768 3523 -4650 363 C
ATOM 505 O TRP A 105 36.775 -5.322 54.124 1.00220.39 O
ANISOU 505 O TRP A 105 42153 24986 16601 3129 -4605 337 O
ATOM 506 CB TRP A 105 37.549 -8.104 55.729 1.00222.87 C
ANISOU 506 CB TRP A 105 43979 24499 16202 4173 -4442 506 C
ATOM 507 N CYS A 106 37.252 -4.963 56.292 1.00236.96 N
ANISOU 507 N CYS A 106 44198 27349 18487 3399 -4691 342 N
ATOM 508 CA CYS A 106 36.461 -3.737 56.358 1.00244.78 C
ANISOU 508 CA CYS A 106 44763 28516 19725 2815 -4686 283 C
ATOM 509 C CYS A 106 37.171 -2.548 55.712 1.00227.25 C
ANISOU 509 C CYS A 106 41756 26878 17710 2808 -4881 172 C
ATOM 510 O CYS A 106 36.520 -1.545 55.395 1.00223.94 O
ANISOU 510 O CYS A 106 40992 26571 17525 2330 -4864 114 O
ATOM 511 CB CYS A 106 36.109 -3.436 57.824 1.00267.30 C
ANISOU 511 CB CYS A 106 47710 31369 22482 2718 -4657 295 C
ATOM 512 SG CYS A 106 35.130 -1.935 58.135 1.00274.14 S
ANISOU 512 SG CYS A 106 48115 32438 23606 2068 -4631 222 S
ATOM 513 N GLU A 107 38.487 -2.635 55.515 1.00216.98 N
ANISOU 513 N GLU A 107 40169 25962 16311 3325 -5057 143 N
ATOM 514 CA GLU A 107 39.197 -1.595 54.778 1.00210.05 C
ANISOU 514 CA GLU A 107 38573 25630 15608 3298 -5233 46 C
ATOM 515 C GLU A 107 38.837 -1.642 53.299 1.00213.82 C
ANISOU 515 C GLU A 107 38998 25971 16274 3106 -5169 50 C
ATOM 516 O GLU A 107 38.343 -0.662 52.731 1.00215.21 O
ANISOU 516 O GLU A 107 38811 26265 16695 2671 -5168 -12 O
ATOM 517 CB GLU A 107 40.710 -1.753 54.954 1.00210.12 C
ANISOU 517 CB GLU A 107 38275 26135 15427 3897 -5428 23 C
ATOM 518 CG GLU A 107 41.241 -1.650 56.369 1.00215.79 C
ANISOU 518 CG GLU A 107 38954 27097 15939 4132 -5526 2 C
ATOM 519 CD GLU A 107 42.701 -2.074 56.461 1.00224.02 C
ANISOU 519 CD GLU A 107 39767 28604 16748 4778 -5687 0 C
ATOM 520 OE1 GLU A 107 43.174 -2.796 55.556 1.00225.91 O
ANISOU 520 OE1 GLU A 107 40089 28810 16935 5125 -5668 49 O
ATOM 521 OE2 GLU A 107 43.378 -1.681 57.434 1.00227.77 O
ANISOU 521 OE2 GLU A 107 39968 29495 17080 4944 -5830 -55 O
ATOM 522 N ILE A 108 39.080 -2.787 52.658 1.00213.28 N
ANISOU 522 N ILE A 108 39315 25640 16081 3447 -5109 120 N
ATOM 523 CA ILE A 108 38.842 -2.903 51.225 1.00202.80 C
ANISOU 523 CA ILE A 108 37947 24203 14906 3326 -5061 119 C
ATOM 524 C ILE A 108 37.354 -2.857 50.909 1.00204.37 C
ANISOU 524 C ILE A 108 38432 23959 15259 2712 -4872 132 C
ATOM 525 O ILE A 108 36.958 -2.367 49.845 1.00205.60 O
ANISOU 525 O ILE A 108 38330 24164 15623 2418 -4852 95 O
ATOM 526 CB ILE A 108 39.490 -4.188 50.674 1.00196.66 C
ANISOU 526 CB ILE A 108 37563 23231 13927 3876 -5038 183 C
ATOM 527 CG1 ILE A 108 38.955 -5.420 51.408 1.00192.70 C
ANISOU 527 CG1 ILE A 108 37895 22128 13195 3971 -4876 265 C
ATOM 528 CG2 ILE A 108 41.002 -4.114 50.799 1.00198.37 C
ANISOU 528 CG2 ILE A 108 37356 24008 14005 4479 -5225 166 C
ATOM 529 CD1 ILE A 108 39.113 -6.715 50.636 1.00190.91 C
ANISOU 529 CD1 ILE A 108 38235 21490 12811 4314 -4785 317 C
ATOM 530 N TYR A 109 36.509 -3.363 51.811 1.00210.31 N
ANISOU 530 N TYR A 109 39702 24304 15900 2507 -4727 187 N
ATOM 531 CA TYR A 109 35.070 -3.378 51.562 1.00218.75 C
ANISOU 531 CA TYR A 109 41032 25003 17080 1901 -4536 205 C
ATOM 532 C TYR A 109 34.540 -1.964 51.356 1.00231.74 C
ANISOU 532 C TYR A 109 42088 26969 18995 1439 -4556 127 C
ATOM 533 O TYR A 109 33.759 -1.708 50.433 1.00235.04 O
ANISOU 533 O TYR A 109 42413 27314 19579 1054 -4466 107 O
ATOM 534 CB TYR A 109 34.353 -4.076 52.718 1.00218.64 C
ANISOU 534 CB TYR A 109 41621 24577 16876 1768 -4385 282 C
ATOM 535 CG TYR A 109 32.851 -3.946 52.693 1.00214.20 C
ANISOU 535 CG TYR A 109 41237 23747 16402 1096 -4187 302 C
ATOM 536 CD1 TYR A 109 32.080 -4.722 51.840 1.00211.31 C
ANISOU 536 CD1 TYR A 109 41278 22993 16016 805 -4039 332 C
ATOM 537 CD2 TYR A 109 32.202 -3.055 53.536 1.00215.67 C
ANISOU 537 CD2 TYR A 109 41180 24093 16671 752 -4146 287 C
ATOM 538 CE1 TYR A 109 30.703 -4.606 51.819 1.00210.85 C
ANISOU 538 CE1 TYR A 109 41333 22768 16013 165 -3857 347 C
ATOM 539 CE2 TYR A 109 30.828 -2.932 53.523 1.00214.41 C
ANISOU 539 CE2 TYR A 109 41138 23759 16570 160 -3955 311 C
ATOM 540 CZ TYR A 109 30.082 -3.708 52.665 1.00212.10 C
ANISOU 540 CZ TYR A 109 41205 23135 16250 -143 -3811 341 C
ATOM 541 OH TYR A 109 28.712 -3.585 52.653 1.00212.40 O
ANISOU 541 OH TYR A 109 41308 23075 16319 -756 -3620 362 O
ATOM 542 N LEU A 110 34.975 -1.027 52.199 1.00242.81 N
ANISOU 542 N LEU A 110 43094 28732 20431 1486 -4673 75 N
ATOM 543 CA LEU A 110 34.604 0.370 52.005 1.00237.50 C
ANISOU 543 CA LEU A 110 41881 28358 19999 1104 -4700 -11 C
ATOM 544 C LEU A 110 35.239 0.937 50.741 1.00234.54 C
ANISOU 544 C LEU A 110 41027 28294 19793 1180 -4816 -75 C
ATOM 545 O LEU A 110 34.585 1.660 49.979 1.00233.98 O
ANISOU 545 O LEU A 110 40704 28267 19930 812 -4753 -117 O
ATOM 546 CB LEU A 110 35.013 1.188 53.232 1.00237.34 C
ANISOU 546 CB LEU A 110 41610 28626 19943 1156 -4810 -64 C
ATOM 547 N ALA A 111 36.507 0.599 50.489 1.00236.91 N
ANISOU 547 N ALA A 111 41195 28829 19990 1674 -4975 -78 N
ATOM 548 CA ALA A 111 37.257 1.248 49.418 1.00232.02 C
ANISOU 548 CA ALA A 111 40056 28591 19510 1770 -5105 -137 C
ATOM 549 C ALA A 111 36.754 0.849 48.036 1.00221.37 C
ANISOU 549 C ALA A 111 38811 27028 18273 1658 -5002 -112 C
ATOM 550 O ALA A 111 36.842 1.645 47.095 1.00215.30 O
ANISOU 550 O ALA A 111 37621 26494 17690 1518 -5043 -165 O
ATOM 551 CB ALA A 111 38.747 0.925 49.556 1.00234.70 C
ANISOU 551 CB ALA A 111 40207 29296 19673 2345 -5291 -136 C
ATOM 552 N LEU A 112 36.240 -0.369 47.882 1.00214.31 N
ANISOU 552 N LEU A 112 38489 25684 17255 1709 -4869 -36 N
ATOM 553 CA LEU A 112 35.728 -0.773 46.580 1.00205.37 C
ANISOU 553 CA LEU A 112 37479 24342 16210 1574 -4776 -26 C
ATOM 554 C LEU A 112 34.301 -0.283 46.372 1.00191.28 C
ANISOU 554 C LEU A 112 35704 22386 14589 953 -4613 -49 C
ATOM 555 O LEU A 112 33.908 0.031 45.242 1.00142.29 O
ANISOU 555 O LEU A 112 29300 16224 8539 752 -4573 -82 O
ATOM 556 CB LEU A 112 35.804 -2.291 46.437 1.00150.78 C
ANISOU 556 CB LEU A 112 31209 17006 9074 1871 -4704 48 C
ATOM 557 CG LEU A 112 37.204 -2.905 46.540 1.00154.10 C
ANISOU 557 CG LEU A 112 31649 17597 9305 2558 -4838 79 C
ATOM 558 CD1 LEU A 112 37.124 -4.424 46.546 1.00157.87 C
ANISOU 558 CD1 LEU A 112 32884 17559 9542 2825 -4733 150 C
ATOM 559 CD2 LEU A 112 38.103 -2.414 45.411 1.00152.89 C
ANISOU 559 CD2 LEU A 112 30954 17873 9264 2814 -4967 43 C
ATOM 560 N ASP A 113 33.518 -0.203 47.452 1.00176.38 N
ANISOU 560 N ASP A 113 34022 20339 12654 663 -4514 -30 N
ATOM 561 CA ASP A 113 32.135 0.246 47.350 1.00161.83 C
ANISOU 561 CA ASP A 113 32162 18393 10933 90 -4344 -43 C
ATOM 562 C ASP A 113 32.028 1.710 46.949 1.00150.77 C
ANISOU 562 C ASP A 113 30148 17367 9772 -123 -4381 -124 C
ATOM 563 O ASP A 113 30.988 2.123 46.427 1.00147.53 O
ANISOU 563 O ASP A 113 29628 16945 9482 -525 -4246 -144 O
ATOM 564 CB ASP A 113 31.407 0.010 48.674 1.00164.55 C
ANISOU 564 CB ASP A 113 32845 18529 11147 -124 -4229 7 C
ATOM 565 CG ASP A 113 30.168 -0.843 48.512 1.00165.31 C
ANISOU 565 CG ASP A 113 33412 18244 11154 -524 -4021 60 C
ATOM 566 OD1 ASP A 113 29.830 -1.190 47.360 1.00162.74 O
ANISOU 566 OD1 ASP A 113 33130 17828 10878 -663 -3971 43 O
ATOM 567 OD2 ASP A 113 29.529 -1.165 49.534 1.00170.81 O
ANISOU 567 OD2 ASP A 113 34435 18749 11718 -718 -3907 115 O
ATOM 568 N VAL A 114 33.069 2.503 47.190 1.00150.41 N
ANISOU 568 N VAL A 114 29711 17661 9776 129 -4554 -174 N
ATOM 569 CA VAL A 114 33.133 3.840 46.613 1.00152.64 C
ANISOU 569 CA VAL A 114 29460 18264 10271 -39 -4599 -254 C
ATOM 570 C VAL A 114 33.758 3.792 45.225 1.00156.37 C
ANISOU 570 C VAL A 114 29710 18878 10827 155 -4676 -269 C
ATOM 571 O VAL A 114 33.275 4.443 44.292 1.00155.47 O
ANISOU 571 O VAL A 114 29306 18847 10918 -76 -4595 -303 O
ATOM 572 CB VAL A 114 33.905 4.787 47.548 1.00153.29 C
ANISOU 572 CB VAL A 114 29247 18643 10355 54 -4745 -314 C
ATOM 573 CG1 VAL A 114 35.171 4.111 48.063 1.00155.95 C
ANISOU 573 CG1 VAL A 114 29660 19092 10502 535 -4919 -294 C
ATOM 574 CG2 VAL A 114 34.229 6.097 46.824 1.00151.48 C
ANISOU 574 CG2 VAL A 114 28498 18728 10329 -72 -4809 -398 C
ATOM 575 N LEU A 115 34.830 3.012 45.073 1.00163.05 N
ANISOU 575 N LEU A 115 30645 19766 11540 610 -4802 -237 N
ATOM 576 CA LEU A 115 35.583 2.980 43.823 1.00161.32 C
ANISOU 576 CA LEU A 115 30180 19738 11375 867 -4891 -244 C
ATOM 577 C LEU A 115 34.684 2.650 42.637 1.00152.23 C
ANISOU 577 C LEU A 115 29156 18367 10317 652 -4750 -235 C
ATOM 578 O LEU A 115 34.646 3.392 41.649 1.00146.95 O
ANISOU 578 O LEU A 115 28057 17890 9888 543 -4715 -272 O
ATOM 579 CB LEU A 115 36.726 1.968 43.944 1.00166.54 C
ANISOU 579 CB LEU A 115 31011 20438 11830 1427 -5006 -191 C
ATOM 580 CG LEU A 115 37.776 1.842 42.841 1.00162.09 C
ANISOU 580 CG LEU A 115 30170 20151 11266 1823 -5119 -184 C
ATOM 581 CD1 LEU A 115 37.302 0.911 41.730 1.00160.66 C
ANISOU 581 CD1 LEU A 115 30315 19649 11078 1876 -5007 -144 C
ATOM 582 CD2 LEU A 115 38.152 3.214 42.296 1.00156.18 C
ANISOU 582 CD2 LEU A 115 28810 19827 10702 1667 -5213 -251 C
ATOM 583 N PHE A 116 33.950 1.538 42.718 1.00155.27 N
ANISOU 583 N PHE A 116 30060 18352 10584 568 -4622 -188 N
ATOM 584 CA PHE A 116 33.133 1.116 41.585 1.00157.00 C
ANISOU 584 CA PHE A 116 30420 18376 10855 355 -4501 -194 C
ATOM 585 C PHE A 116 32.077 2.154 41.235 1.00155.38 C
ANISOU 585 C PHE A 116 29870 18297 10872 -126 -4374 -245 C
ATOM 586 O PHE A 116 31.798 2.373 40.053 1.00161.50 O
ANISOU 586 O PHE A 116 30382 19149 11830 -209 -4304 -274 O
ATOM 587 CB PHE A 116 32.472 -0.232 41.874 1.00163.30 C
ANISOU 587 CB PHE A 116 31876 18708 11463 262 -4381 -145 C
ATOM 588 CG PHE A 116 31.103 -0.124 42.490 1.00170.90 C
ANISOU 588 CG PHE A 116 33003 19505 12428 -283 -4210 -145 C
ATOM 589 CD1 PHE A 116 30.956 0.173 43.835 1.00170.97 C
ANISOU 589 CD1 PHE A 116 33058 19517 12385 -372 -4193 -121 C
ATOM 590 CD2 PHE A 116 29.964 -0.326 41.726 1.00179.75 C
ANISOU 590 CD2 PHE A 116 34208 20504 13583 -701 -4064 -172 C
ATOM 591 CE1 PHE A 116 29.699 0.269 44.407 1.00174.66 C
ANISOU 591 CE1 PHE A 116 33654 19871 12836 -853 -4025 -110 C
ATOM 592 CE2 PHE A 116 28.704 -0.228 42.293 1.00182.64 C
ANISOU 592 CE2 PHE A 116 34674 20794 13926 -1204 -3899 -168 C
ATOM 593 CZ PHE A 116 28.574 0.069 43.635 1.00179.37 C
ANISOU 593 CZ PHE A 116 34306 20385 13460 -1271 -3876 -131 C
ATOM 594 N CYS A 117 31.489 2.807 42.240 1.00150.02 N
ANISOU 594 N CYS A 117 29117 17655 10229 -409 -4307 -254 N
ATOM 595 CA CYS A 117 30.418 3.759 41.978 1.00148.89 C
ANISOU 595 CA CYS A 117 28615 17636 10320 -821 -4133 -291 C
ATOM 596 C CYS A 117 30.959 5.102 41.512 1.00148.46 C
ANISOU 596 C CYS A 117 27936 17924 10550 -752 -4160 -339 C
ATOM 597 O CYS A 117 30.311 5.780 40.707 1.00146.13 O
ANISOU 597 O CYS A 117 27313 17748 10462 -951 -4025 -366 O
ATOM 598 CB CYS A 117 29.552 3.928 43.228 1.00153.24 C
ANISOU 598 CB CYS A 117 29356 18101 10768 -1120 -4036 -274 C
ATOM 599 SG CYS A 117 28.005 4.823 42.966 1.00156.72 S
ANISOU 599 SG CYS A 117 29474 18685 11386 -1603 -3791 -299 S
ATOM 600 N THR A 118 32.137 5.500 41.999 1.00159.79 N
ANISOU 600 N THR A 118 29206 19531 11975 -481 -4327 -351 N
ATOM 601 CA THR A 118 32.786 6.678 41.440 1.00160.08 C
ANISOU 601 CA THR A 118 28686 19879 12260 -430 -4355 -395 C
ATOM 602 C THR A 118 33.247 6.410 40.013 1.00160.22 C
ANISOU 602 C THR A 118 28516 19981 12380 -229 -4369 -385 C
ATOM 603 O THR A 118 33.095 7.265 39.133 1.00162.85 O
ANISOU 603 O THR A 118 28452 20472 12952 -331 -4274 -408 O
ATOM 604 CB THR A 118 33.962 7.107 42.317 1.00168.26 C
ANISOU 604 CB THR A 118 29585 21120 13227 -233 -4541 -421 C
ATOM 605 OG1 THR A 118 33.519 7.292 43.666 1.00174.99 O
ANISOU 605 OG1 THR A 118 30653 21877 13958 -396 -4533 -432 O
ATOM 606 CG2 THR A 118 34.559 8.415 41.809 1.00163.92 C
ANISOU 606 CG2 THR A 118 28480 20877 12926 -283 -4547 -474 C
ATOM 607 N SER A 119 33.785 5.213 39.757 1.00158.91 N
ANISOU 607 N SER A 119 28668 19697 12012 81 -4476 -345 N
ATOM 608 CA SER A 119 34.207 4.872 38.402 1.00156.43 C
ANISOU 608 CA SER A 119 28223 19450 11761 307 -4490 -332 C
ATOM 609 C SER A 119 33.010 4.627 37.492 1.00144.14 C
ANISOU 609 C SER A 119 26755 17717 10295 43 -4315 -343 C
ATOM 610 O SER A 119 33.029 5.024 36.322 1.00138.07 O
ANISOU 610 O SER A 119 25659 17091 9710 71 -4258 -356 O
ATOM 611 CB SER A 119 35.128 3.653 38.419 1.00162.42 C
ANISOU 611 CB SER A 119 29349 20130 12234 766 -4651 -285 C
ATOM 612 OG SER A 119 34.401 2.465 38.668 1.00168.31 O
ANISOU 612 OG SER A 119 30731 20473 12746 705 -4602 -259 O
ATOM 613 N SER A 120 31.959 3.977 38.000 1.00139.57 N
ANISOU 613 N SER A 120 26603 16855 9573 -226 -4224 -339 N
ATOM 614 CA SER A 120 30.777 3.739 37.175 1.00133.91 C
ANISOU 614 CA SER A 120 25939 16031 8911 -525 -4062 -363 C
ATOM 615 C SER A 120 30.125 5.055 36.769 1.00130.58 C
ANISOU 615 C SER A 120 24987 15864 8762 -772 -3917 -397 C
ATOM 616 O SER A 120 29.737 5.239 35.609 1.00131.10 O
ANISOU 616 O SER A 120 24828 16026 8959 -815 -3830 -421 O
ATOM 617 CB SER A 120 29.773 2.855 37.915 1.00138.24 C
ANISOU 617 CB SER A 120 27019 16275 9233 -831 -3984 -351 C
ATOM 618 OG SER A 120 30.350 1.611 38.264 1.00130.36 O
ANISOU 618 OG SER A 120 26593 14989 7950 -583 -4097 -312 O
ATOM 619 N ALA A 121 29.990 5.984 37.719 1.00130.69 N
ANISOU 619 N ALA A 121 24829 15985 8840 -911 -3885 -402 N
ATOM 620 CA ALA A 121 29.449 7.301 37.395 1.00133.51 C
ANISOU 620 CA ALA A 121 24740 16566 9423 -1084 -3742 -428 C
ATOM 621 C ALA A 121 30.345 8.033 36.405 1.00128.31 C
ANISOU 621 C ALA A 121 23662 16119 8972 -854 -3776 -435 C
ATOM 622 O ALA A 121 29.858 8.635 35.441 1.00117.38 O
ANISOU 622 O ALA A 121 21989 14863 7745 -917 -3643 -448 O
ATOM 623 CB ALA A 121 29.271 8.128 38.670 1.00134.80 C
ANISOU 623 CB ALA A 121 24871 16768 9577 -1229 -3717 -433 C
ATOM 624 N TRP A 122 31.661 7.990 36.626 1.00136.47 N
ANISOU 624 N TRP A 122 24645 17221 9988 -581 -3948 -424 N
ATOM 625 CA TRP A 122 32.578 8.687 35.734 1.00135.00 C
ANISOU 625 CA TRP A 122 24043 17270 9981 -390 -3976 -422 C
ATOM 626 C TRP A 122 32.673 8.010 34.373 1.00134.48 C
ANISOU 626 C TRP A 122 23959 17205 9933 -195 -3970 -404 C
ATOM 627 O TRP A 122 32.944 8.681 33.371 1.00132.69 O
ANISOU 627 O TRP A 122 23369 17161 9887 -121 -3908 -399 O
ATOM 628 CB TRP A 122 33.956 8.804 36.386 1.00140.74 C
ANISOU 628 CB TRP A 122 24682 18144 10647 -174 -4167 -419 C
ATOM 629 CG TRP A 122 34.059 10.040 37.209 1.00143.73 C
ANISOU 629 CG TRP A 122 24851 18637 11121 -379 -4144 -457 C
ATOM 630 CD1 TRP A 122 34.132 10.124 38.568 1.00145.25 C
ANISOU 630 CD1 TRP A 122 25221 18782 11186 -465 -4223 -482 C
ATOM 631 CD2 TRP A 122 34.052 11.383 36.721 1.00148.70 C
ANISOU 631 CD2 TRP A 122 25108 19418 11975 -527 -4020 -479 C
ATOM 632 NE1 TRP A 122 34.190 11.441 38.956 1.00149.01 N
ANISOU 632 NE1 TRP A 122 25455 19370 11792 -667 -4168 -528 N
ATOM 633 CE2 TRP A 122 34.141 12.235 37.839 1.00148.57 C
ANISOU 633 CE2 TRP A 122 25080 19420 11949 -713 -4037 -525 C
ATOM 634 CE3 TRP A 122 33.988 11.949 35.444 1.00153.27 C
ANISOU 634 CE3 TRP A 122 25391 20100 12743 -510 -3891 -462 C
ATOM 635 CZ2 TRP A 122 34.167 13.622 37.718 1.00149.73 C
ANISOU 635 CZ2 TRP A 122 24974 19656 12261 -896 -3924 -557 C
ATOM 636 CZ3 TRP A 122 34.015 13.324 35.326 1.00152.46 C
ANISOU 636 CZ3 TRP A 122 25028 20094 12806 -677 -3771 -483 C
ATOM 637 CH2 TRP A 122 34.104 14.146 36.455 1.00150.60 C
ANISOU 637 CH2 TRP A 122 24828 19844 12548 -875 -3785 -532 C
ATOM 638 N HIS A 123 32.455 6.694 34.310 1.00139.28 N
ANISOU 638 N HIS A 123 24986 17593 10340 -111 -4025 -393 N
ATOM 639 CA HIS A 123 32.403 6.022 33.015 1.00140.72 C
ANISOU 639 CA HIS A 123 25211 17741 10516 45 -4010 -390 C
ATOM 640 C HIS A 123 31.186 6.473 32.221 1.00139.15 C
ANISOU 640 C HIS A 123 24837 17578 10455 -229 -3819 -425 C
ATOM 641 O HIS A 123 31.294 6.827 31.042 1.00138.92 O
ANISOU 641 O HIS A 123 24517 17701 10566 -112 -3764 -426 O
ATOM 642 CB HIS A 123 32.385 4.507 33.202 1.00144.57 C
ANISOU 642 CB HIS A 123 26279 17931 10720 164 -4101 -381 C
ATOM 643 CG HIS A 123 33.705 3.936 33.606 1.00153.11 C
ANISOU 643 CG HIS A 123 27519 19028 11626 586 -4292 -337 C
ATOM 644 ND1 HIS A 123 33.878 3.219 34.770 1.00158.95 N
ANISOU 644 ND1 HIS A 123 28704 19573 12118 644 -4384 -316 N
ATOM 645 CD2 HIS A 123 34.915 3.969 33.000 1.00156.73 C
ANISOU 645 CD2 HIS A 123 27743 19715 12094 997 -4403 -304 C
ATOM 646 CE1 HIS A 123 35.139 2.839 34.866 1.00161.27 C
ANISOU 646 CE1 HIS A 123 29026 19985 12264 1099 -4550 -275 C
ATOM 647 NE2 HIS A 123 35.789 3.279 33.804 1.00159.36 N
ANISOU 647 NE2 HIS A 123 28360 20017 12172 1313 -4565 -267 N
ATOM 648 N LEU A 124 30.012 6.453 32.857 1.00132.31 N
ANISOU 648 N LEU A 124 24137 16607 9528 -579 -3713 -450 N
ATOM 649 CA LEU A 124 28.810 6.991 32.230 1.00124.90 C
ANISOU 649 CA LEU A 124 22979 15788 8687 -832 -3527 -483 C
ATOM 650 C LEU A 124 29.002 8.441 31.818 1.00122.25 C
ANISOU 650 C LEU A 124 22151 15709 8587 -771 -3429 -473 C
ATOM 651 O LEU A 124 28.391 8.899 30.847 1.00119.16 O
ANISOU 651 O LEU A 124 21513 15469 8294 -800 -3294 -488 O
ATOM 652 CB LEU A 124 27.623 6.868 33.186 1.00128.68 C
ANISOU 652 CB LEU A 124 23663 16189 9040 -1202 -3430 -498 C
ATOM 653 CG LEU A 124 26.734 5.627 33.057 1.00135.37 C
ANISOU 653 CG LEU A 124 24899 16857 9678 -1442 -3406 -528 C
ATOM 654 CD1 LEU A 124 27.522 4.315 33.109 1.00140.00 C
ANISOU 654 CD1 LEU A 124 25969 17143 10084 -1251 -3569 -515 C
ATOM 655 CD2 LEU A 124 25.648 5.643 34.122 1.00141.27 C
ANISOU 655 CD2 LEU A 124 25789 17588 10300 -1818 -3301 -526 C
ATOM 656 N CYS A 125 29.837 9.179 32.554 1.00124.45 N
ANISOU 656 N CYS A 125 22308 16039 8938 -694 -3490 -452 N
ATOM 657 CA CYS A 125 30.155 10.552 32.177 1.00125.03 C
ANISOU 657 CA CYS A 125 21981 16309 9217 -654 -3396 -443 C
ATOM 658 C CYS A 125 30.957 10.587 30.882 1.00119.67 C
ANISOU 658 C CYS A 125 21056 15759 8654 -388 -3419 -419 C
ATOM 659 O CYS A 125 30.704 11.418 30.003 1.00113.55 O
ANISOU 659 O CYS A 125 19997 15123 8024 -370 -3273 -410 O
ATOM 660 CB CYS A 125 30.925 11.243 33.306 1.00127.36 C
ANISOU 660 CB CYS A 125 22244 16618 9529 -680 -3476 -442 C
ATOM 661 SG CYS A 125 30.734 13.033 33.364 1.00134.01 S
ANISOU 661 SG CYS A 125 22785 17587 10548 -816 -3298 -450 S
ATOM 662 N ALA A 126 31.928 9.682 30.744 1.00124.17 N
ANISOU 662 N ALA A 126 21746 16295 9138 -146 -3593 -400 N
ATOM 663 CA ALA A 126 32.792 9.687 29.568 1.00125.69 C
ANISOU 663 CA ALA A 126 21697 16643 9417 144 -3624 -367 C
ATOM 664 C ALA A 126 32.055 9.202 28.327 1.00135.23 C
ANISOU 664 C ALA A 126 22924 17831 10626 194 -3535 -381 C
ATOM 665 O ALA A 126 32.271 9.730 27.229 1.00130.57 O
ANISOU 665 O ALA A 126 22034 17406 10172 335 -3453 -358 O
ATOM 666 CB ALA A 126 34.029 8.828 29.815 1.00130.47 C
ANISOU 666 CB ALA A 126 22432 17260 9880 442 -3836 -338 C
ATOM 667 N ILE A 127 31.192 8.189 28.473 1.00151.36 N
ANISOU 667 N ILE A 127 25327 19679 12505 66 -3547 -421 N
ATOM 668 CA ILE A 127 30.355 7.772 27.347 1.00153.97 C
ANISOU 668 CA ILE A 127 25671 20014 12817 40 -3460 -459 C
ATOM 669 C ILE A 127 29.394 8.893 26.975 1.00148.89 C
ANISOU 669 C ILE A 127 24702 19556 12314 -142 -3255 -473 C
ATOM 670 O ILE A 127 29.126 9.140 25.793 1.00149.61 O
ANISOU 670 O ILE A 127 24576 19793 12478 -38 -3163 -480 O
ATOM 671 CB ILE A 127 29.609 6.458 27.667 1.00162.00 C
ANISOU 671 CB ILE A 127 27172 20779 13601 -141 -3512 -510 C
ATOM 672 CG1 ILE A 127 28.441 6.691 28.624 1.00169.00 C
ANISOU 672 CG1 ILE A 127 28145 21631 14435 -546 -3409 -539 C
ATOM 673 CG2 ILE A 127 30.549 5.459 28.290 1.00167.13 C
ANISOU 673 CG2 ILE A 127 28211 21214 14076 62 -3697 -482 C
ATOM 674 CD1 ILE A 127 27.728 5.430 29.053 1.00176.89 C
ANISOU 674 CD1 ILE A 127 29636 22383 15193 -792 -3444 -581 C
ATOM 675 N SER A 128 28.866 9.588 27.984 1.00142.14 N
ANISOU 675 N SER A 128 23827 18708 11473 -379 -3178 -475 N
ATOM 676 CA SER A 128 28.099 10.807 27.764 1.00130.74 C
ANISOU 676 CA SER A 128 22091 17447 10137 -478 -2977 -473 C
ATOM 677 C SER A 128 28.915 11.824 26.979 1.00125.03 C
ANISOU 677 C SER A 128 21035 16866 9604 -247 -2915 -424 C
ATOM 678 O SER A 128 28.414 12.450 26.038 1.00113.25 O
ANISOU 678 O SER A 128 19316 15532 8182 -178 -2757 -418 O
ATOM 679 CB SER A 128 27.680 11.392 29.113 1.00126.47 C
ANISOU 679 CB SER A 128 21631 16861 9560 -703 -2931 -473 C
ATOM 680 OG SER A 128 26.319 11.747 29.149 1.00121.57 O
ANISOU 680 OG SER A 128 20954 16366 8872 -889 -2762 -496 O
ATOM 681 N LEU A 129 30.183 12.005 27.359 1.00131.90 N
ANISOU 681 N LEU A 129 21870 17707 10539 -131 -3031 -387 N
ATOM 682 CA LEU A 129 31.045 12.923 26.623 1.00133.79 C
ANISOU 682 CA LEU A 129 21798 18093 10945 41 -2971 -336 C
ATOM 683 C LEU A 129 31.393 12.366 25.248 1.00137.31 C
ANISOU 683 C LEU A 129 22131 18630 11412 312 -2991 -315 C
ATOM 684 O LEU A 129 31.441 13.115 24.266 1.00137.20 O
ANISOU 684 O LEU A 129 21858 18755 11515 430 -2851 -278 O
ATOM 685 CB LEU A 129 32.317 13.218 27.417 1.00135.05 C
ANISOU 685 CB LEU A 129 21915 18260 11139 51 -3102 -312 C
ATOM 686 CG LEU A 129 32.973 14.537 26.993 1.00138.33 C
ANISOU 686 CG LEU A 129 22025 18815 11721 63 -2983 -268 C
ATOM 687 CD1 LEU A 129 32.399 15.680 27.816 1.00140.45 C
ANISOU 687 CD1 LEU A 129 22338 19008 12021 -190 -2845 -290 C
ATOM 688 CD2 LEU A 129 34.502 14.507 27.061 1.00143.92 C
ANISOU 688 CD2 LEU A 129 22566 19661 12454 177 -3133 -234 C
ATOM 689 N ASP A 130 31.641 11.055 25.156 1.00140.47 N
ANISOU 689 N ASP A 130 22757 18937 11678 431 -3155 -334 N
ATOM 690 CA ASP A 130 31.932 10.449 23.860 1.00141.03 C
ANISOU 690 CA ASP A 130 22773 19076 11735 709 -3181 -322 C
ATOM 691 C ASP A 130 30.756 10.602 22.901 1.00141.91 C
ANISOU 691 C ASP A 130 22802 19258 11859 659 -3022 -360 C
ATOM 692 O ASP A 130 30.947 10.922 21.722 1.00143.18 O
ANISOU 692 O ASP A 130 22734 19568 12101 873 -2943 -330 O
ATOM 693 CB ASP A 130 32.304 8.975 24.044 1.00136.13 C
ANISOU 693 CB ASP A 130 22515 18289 10918 843 -3379 -344 C
ATOM 694 CG ASP A 130 32.163 8.166 22.764 1.00126.67 C
ANISOU 694 CG ASP A 130 21392 17089 9646 1063 -3394 -365 C
ATOM 695 OD1 ASP A 130 31.025 7.780 22.423 1.00124.92 O
ANISOU 695 OD1 ASP A 130 21312 16799 9354 886 -3331 -437 O
ATOM 696 OD2 ASP A 130 33.191 7.915 22.097 1.00126.63 O
ANISOU 696 OD2 ASP A 130 21299 17178 9636 1411 -3470 -314 O
ATOM 697 N ARG A 131 29.533 10.386 23.393 1.00143.74 N
ANISOU 697 N ARG A 131 23199 19422 11994 382 -2970 -425 N
ATOM 698 CA ARG A 131 28.354 10.490 22.540 1.00138.84 C
ANISOU 698 CA ARG A 131 22471 18940 11341 322 -2829 -474 C
ATOM 699 C ARG A 131 28.160 11.914 22.034 1.00146.69 C
ANISOU 699 C ARG A 131 23114 20140 12481 408 -2622 -425 C
ATOM 700 O ARG A 131 27.833 12.124 20.860 1.00152.39 O
ANISOU 700 O ARG A 131 23649 21029 13223 574 -2521 -426 O
ATOM 701 CB ARG A 131 27.115 10.020 23.302 1.00133.61 C
ANISOU 701 CB ARG A 131 22019 18225 10520 -26 -2812 -546 C
ATOM 702 N TYR A 132 28.354 12.906 22.904 1.00148.64 N
ANISOU 702 N TYR A 132 23303 20364 12811 308 -2552 -383 N
ATOM 703 CA TYR A 132 28.238 14.295 22.475 1.00151.15 C
ANISOU 703 CA TYR A 132 23373 20816 13242 397 -2341 -330 C
ATOM 704 C TYR A 132 29.294 14.631 21.430 1.00156.02 C
ANISOU 704 C TYR A 132 23786 21503 13992 670 -2322 -260 C
ATOM 705 O TYR A 132 28.977 15.138 20.347 1.00156.34 O
ANISOU 705 O TYR A 132 23644 21691 14066 849 -2166 -233 O
ATOM 706 CB TYR A 132 28.358 15.224 23.684 1.00152.40 C
ANISOU 706 CB TYR A 132 23588 20880 13438 220 -2289 -308 C
ATOM 707 CG TYR A 132 28.518 16.681 23.320 1.00154.90 C
ANISOU 707 CG TYR A 132 23738 21254 13864 311 -2080 -245 C
ATOM 708 CD1 TYR A 132 29.773 17.218 23.061 1.00154.96 C
ANISOU 708 CD1 TYR A 132 23631 21236 14011 392 -2089 -183 C
ATOM 709 CD2 TYR A 132 27.420 17.524 23.245 1.00156.38 C
ANISOU 709 CD2 TYR A 132 23900 21533 13985 319 -1864 -243 C
ATOM 710 CE1 TYR A 132 29.930 18.539 22.723 1.00152.77 C
ANISOU 710 CE1 TYR A 132 23261 20969 13816 435 -1881 -124 C
ATOM 711 CE2 TYR A 132 27.567 18.855 22.912 1.00154.38 C
ANISOU 711 CE2 TYR A 132 23576 21283 13799 426 -1655 -180 C
ATOM 712 CZ TYR A 132 28.825 19.358 22.652 1.00151.40 C
ANISOU 712 CZ TYR A 132 23129 20824 13570 462 -1661 -121 C
ATOM 713 OH TYR A 132 28.980 20.683 22.320 1.00149.31 O
ANISOU 713 OH TYR A 132 22851 20523 13357 528 -1436 -56 O
ATOM 714 N TRP A 133 30.564 14.359 21.747 1.00161.21 N
ANISOU 714 N TRP A 133 24457 22089 14706 720 -2474 -225 N
ATOM 715 CA TRP A 133 31.657 14.713 20.847 1.00166.42 C
ANISOU 715 CA TRP A 133 24891 22860 15480 956 -2452 -146 C
ATOM 716 C TRP A 133 31.484 14.062 19.479 1.00173.85 C
ANISOU 716 C TRP A 133 25761 23909 16386 1226 -2448 -148 C
ATOM 717 O TRP A 133 31.753 14.688 18.447 1.00175.90 O
ANISOU 717 O TRP A 133 25800 24304 16732 1424 -2311 -84 O
ATOM 718 CB TRP A 133 32.995 14.315 21.475 1.00166.96 C
ANISOU 718 CB TRP A 133 24974 22908 15556 975 -2648 -119 C
ATOM 719 CG TRP A 133 33.546 15.312 22.473 1.00167.46 C
ANISOU 719 CG TRP A 133 24985 22947 15695 755 -2622 -99 C
ATOM 720 CD1 TRP A 133 32.833 16.125 23.308 1.00166.84 C
ANISOU 720 CD1 TRP A 133 25007 22759 15624 503 -2511 -129 C
ATOM 721 CD2 TRP A 133 34.929 15.605 22.716 1.00174.14 C
ANISOU 721 CD2 TRP A 133 25665 23905 16595 764 -2709 -50 C
ATOM 722 NE1 TRP A 133 33.686 16.899 24.059 1.00171.16 N
ANISOU 722 NE1 TRP A 133 25502 23301 16232 339 -2528 -112 N
ATOM 723 CE2 TRP A 133 34.978 16.600 23.714 1.00175.15 C
ANISOU 723 CE2 TRP A 133 25821 23960 16767 472 -2652 -67 C
ATOM 724 CE3 TRP A 133 36.130 15.119 22.189 1.00179.28 C
ANISOU 724 CE3 TRP A 133 26137 24744 17237 996 -2830 5 C
ATOM 725 CZ2 TRP A 133 36.182 17.119 24.194 1.00178.13 C
ANISOU 725 CZ2 TRP A 133 26045 24451 17185 355 -2719 -44 C
ATOM 726 CZ3 TRP A 133 37.325 15.636 22.667 1.00181.05 C
ANISOU 726 CZ3 TRP A 133 26169 25126 17495 903 -2891 39 C
ATOM 727 CH2 TRP A 133 37.341 16.625 23.659 1.00179.83 C
ANISOU 727 CH2 TRP A 133 26039 24899 17391 561 -2840 8 C
ATOM 728 N SER A 134 31.017 12.812 19.451 1.00181.00 N
ANISOU 728 N SER A 134 26880 24743 17149 1227 -2588 -224 N
ATOM 729 CA SER A 134 30.863 12.104 18.183 1.00185.30 C
ANISOU 729 CA SER A 134 27405 25368 17631 1470 -2606 -246 C
ATOM 730 C SER A 134 29.752 12.709 17.339 1.00188.62 C
ANISOU 730 C SER A 134 27665 25948 18052 1490 -2408 -269 C
ATOM 731 O SER A 134 29.867 12.779 16.109 1.00194.96 O
ANISOU 731 O SER A 134 28309 26892 18875 1756 -2342 -244 O
ATOM 732 CB SER A 134 30.593 10.623 18.442 1.00186.61 C
ANISOU 732 CB SER A 134 27917 25372 17614 1412 -2799 -334 C
ATOM 733 OG SER A 134 29.332 10.437 19.063 1.00186.80 O
ANISOU 733 OG SER A 134 28100 25336 17540 1088 -2766 -421 O
ATOM 734 N ILE A 135 28.670 13.150 17.980 1.00176.45 N
ANISOU 734 N ILE A 135 26157 24419 16466 1244 -2308 -314 N
ATOM 735 CA ILE A 135 27.524 13.653 17.234 1.00161.58 C
ANISOU 735 CA ILE A 135 24119 22747 14528 1292 -2126 -342 C
ATOM 736 C ILE A 135 27.836 15.021 16.636 1.00160.94 C
ANISOU 736 C ILE A 135 23801 22776 14574 1506 -1908 -238 C
ATOM 737 O ILE A 135 27.303 15.381 15.578 1.00159.91 O
ANISOU 737 O ILE A 135 23508 22841 14408 1716 -1765 -231 O
ATOM 738 CB ILE A 135 26.275 13.670 18.144 1.00146.02 C
ANISOU 738 CB ILE A 135 22244 20807 12429 987 -2085 -414 C
ATOM 739 CG1 ILE A 135 25.479 12.364 18.008 1.00138.02 C
ANISOU 739 CG1 ILE A 135 21387 19821 11232 816 -2214 -535 C
ATOM 740 CG2 ILE A 135 25.366 14.857 17.839 1.00144.01 C
ANISOU 740 CG2 ILE A 135 21787 20783 12147 1070 -1836 -388 C
ATOM 741 CD1 ILE A 135 26.233 11.096 18.378 1.00131.49 C
ANISOU 741 CD1 ILE A 135 20865 18727 10369 746 -2448 -565 C
ATOM 742 N THR A 136 28.732 15.786 17.262 1.00164.00 N
ANISOU 742 N THR A 136 24180 23039 15092 1457 -1877 -157 N
ATOM 743 CA THR A 136 29.030 17.141 16.809 1.00164.21 C
ANISOU 743 CA THR A 136 24054 23114 15224 1593 -1650 -56 C
ATOM 744 C THR A 136 30.328 17.225 16.010 1.00180.47 C
ANISOU 744 C THR A 136 25964 25200 17405 1798 -1662 35 C
ATOM 745 O THR A 136 30.316 17.690 14.866 1.00184.31 O
ANISOU 745 O THR A 136 26299 25816 17914 2052 -1505 95 O
ATOM 746 CB THR A 136 29.080 18.101 18.003 1.00147.08 C
ANISOU 746 CB THR A 136 21993 20798 13094 1356 -1570 -33 C
ATOM 747 OG1 THR A 136 27.783 18.165 18.610 1.00137.66 O
ANISOU 747 OG1 THR A 136 20904 19637 11764 1227 -1512 -99 O
ATOM 748 CG2 THR A 136 29.478 19.496 17.543 1.00144.66 C
ANISOU 748 CG2 THR A 136 21606 20481 12877 1465 -1327 72 C
ATOM 749 N GLN A 137 31.453 16.788 16.587 1.00193.28 N
ANISOU 749 N GLN A 137 27612 26738 19087 1713 -1841 53 N
ATOM 750 CA GLN A 137 32.736 17.005 15.923 1.00193.82 C
ANISOU 750 CA GLN A 137 27491 26895 19255 1886 -1835 153 C
ATOM 751 C GLN A 137 32.886 16.195 14.641 1.00187.21 C
ANISOU 751 C GLN A 137 26558 26199 18373 2226 -1886 163 C
ATOM 752 O GLN A 137 33.733 16.536 13.810 1.00188.02 O
ANISOU 752 O GLN A 137 26465 26429 18547 2430 -1812 263 O
ATOM 753 CB GLN A 137 33.889 16.699 16.877 1.00202.32 C
ANISOU 753 CB GLN A 137 28583 27928 20363 1737 -2026 164 C
ATOM 754 CG GLN A 137 34.376 17.922 17.632 1.00208.73 C
ANISOU 754 CG GLN A 137 29356 28682 21270 1475 -1915 209 C
ATOM 755 CD GLN A 137 35.875 17.936 17.807 1.00213.62 C
ANISOU 755 CD GLN A 137 29796 29427 21942 1448 -2024 271 C
ATOM 756 OE1 GLN A 137 36.596 18.588 17.051 1.00216.51 O
ANISOU 756 OE1 GLN A 137 29948 29930 22385 1521 -1894 367 O
ATOM 757 NE2 GLN A 137 36.355 17.220 18.814 1.00212.56 N
ANISOU 757 NE2 GLN A 137 29741 29278 21745 1344 -2258 219 N
ATOM 758 N ALA A 138 32.096 15.134 14.473 1.00181.73 N
ANISOU 758 N ALA A 138 26009 25488 17551 2272 -2006 61 N
ATOM 759 CA ALA A 138 31.923 14.434 13.194 1.00175.33 C
ANISOU 759 CA ALA A 138 25155 24799 16665 2578 -2030 41 C
ATOM 760 C ALA A 138 33.252 13.825 12.761 1.00167.03 C
ANISOU 760 C ALA A 138 24041 23800 15623 2828 -2167 108 C
ATOM 761 O ALA A 138 33.834 13.047 13.534 1.00170.27 O
ANISOU 761 O ALA A 138 24602 24113 15979 2765 -2369 83 O
ATOM 762 CB ALA A 138 31.289 15.398 12.194 1.00176.76 C
ANISOU 762 CB ALA A 138 25157 25132 16871 2742 -1774 85 C
ATOM 763 N ILE A 139 33.772 14.135 11.569 1.00157.17 N
ANISOU 763 N ILE A 139 22579 22722 14416 3139 -2060 198 N
ATOM 764 CA ILE A 139 34.882 13.379 10.987 1.00157.35 C
ANISOU 764 CA ILE A 139 22547 22847 14393 3450 -2195 253 C
ATOM 765 C ILE A 139 36.132 13.530 11.844 1.00156.61 C
ANISOU 765 C ILE A 139 22364 22786 14353 3358 -2286 330 C
ATOM 766 O ILE A 139 36.892 12.575 12.032 1.00157.40 O
ANISOU 766 O ILE A 139 22545 22911 14347 3523 -2488 329 O
ATOM 767 CB ILE A 139 35.142 13.832 9.536 1.00163.94 C
ANISOU 767 CB ILE A 139 23142 23886 15262 3795 -2028 348 C
ATOM 768 CG1 ILE A 139 33.831 14.126 8.818 1.00158.36 C
ANISOU 768 CG1 ILE A 139 22455 23197 14519 3834 -1878 282 C
ATOM 769 CG2 ILE A 139 35.946 12.767 8.789 1.00169.75 C
ANISOU 769 CG2 ILE A 139 23891 24725 15881 4182 -2186 369 C
ATOM 770 CD1 ILE A 139 34.020 14.587 7.389 1.00151.84 C
ANISOU 770 CD1 ILE A 139 21416 22569 13709 4197 -1703 376 C
ATOM 771 N GLU A 140 36.371 14.739 12.363 1.00162.05 N
ANISOU 771 N GLU A 140 22899 23492 15183 3104 -2136 395 N
ATOM 772 CA GLU A 140 37.594 15.004 13.118 1.00169.46 C
ANISOU 772 CA GLU A 140 23697 24525 16165 2979 -2212 462 C
ATOM 773 C GLU A 140 37.706 14.088 14.330 1.00178.91 C
ANISOU 773 C GLU A 140 25121 25600 17256 2855 -2464 375 C
ATOM 774 O GLU A 140 38.766 13.509 14.593 1.00185.31 O
ANISOU 774 O GLU A 140 25870 26552 17988 2998 -2633 410 O
ATOM 775 CB GLU A 140 37.632 16.470 13.544 1.00167.29 C
ANISOU 775 CB GLU A 140 23304 24223 16036 2651 -2002 515 C
ATOM 776 N TYR A 141 36.612 13.938 15.076 1.00181.93 N
ANISOU 776 N TYR A 141 25768 25744 17612 2611 -2487 267 N
ATOM 777 CA TYR A 141 36.642 13.080 16.256 1.00183.85 C
ANISOU 777 CA TYR A 141 26268 25841 17743 2482 -2706 190 C
ATOM 778 C TYR A 141 36.841 11.614 15.875 1.00184.16 C
ANISOU 778 C TYR A 141 26521 25853 17600 2799 -2902 155 C
ATOM 779 O TYR A 141 37.586 10.890 16.549 1.00186.75 O
ANISOU 779 O TYR A 141 26968 26181 17809 2884 -3093 156 O
ATOM 780 CB TYR A 141 35.356 13.270 17.056 1.00185.65 C
ANISOU 780 CB TYR A 141 26724 25842 17972 2151 -2658 92 C
ATOM 781 CG TYR A 141 35.289 12.468 18.333 1.00188.99 C
ANISOU 781 CG TYR A 141 27436 26092 18279 1982 -2855 19 C
ATOM 782 CD1 TYR A 141 36.433 12.135 19.043 1.00192.70 C
ANISOU 782 CD1 TYR A 141 27896 26625 18695 2036 -3025 51 C
ATOM 783 CD2 TYR A 141 34.075 12.037 18.824 1.00190.02 C
ANISOU 783 CD2 TYR A 141 27842 26027 18330 1777 -2864 -78 C
ATOM 784 CE1 TYR A 141 36.358 11.389 20.210 1.00195.70 C
ANISOU 784 CE1 TYR A 141 28571 26840 18947 1917 -3196 -9 C
ATOM 785 CE2 TYR A 141 33.985 11.300 19.984 1.00192.93 C
ANISOU 785 CE2 TYR A 141 28504 26220 18580 1618 -3025 -135 C
ATOM 786 CZ TYR A 141 35.126 10.976 20.677 1.00196.73 C
ANISOU 786 CZ TYR A 141 29008 26729 19011 1703 -3189 -99 C
ATOM 787 OH TYR A 141 35.029 10.239 21.838 1.00199.37 O
ANISOU 787 OH TYR A 141 29662 26881 19207 1577 -3341 -149 O
ATOM 788 N ASN A 142 36.191 11.156 14.799 1.00180.47 N
ANISOU 788 N ASN A 142 26129 25362 17079 2993 -2858 121 N
ATOM 789 CA ASN A 142 36.391 9.782 14.344 1.00180.26 C
ANISOU 789 CA ASN A 142 26359 25276 16855 3305 -3032 83 C
ATOM 790 C ASN A 142 37.862 9.507 14.061 1.00182.97 C
ANISOU 790 C ASN A 142 26539 25846 17137 3679 -3129 191 C
ATOM 791 O ASN A 142 38.370 8.422 14.368 1.00180.04 O
ANISOU 791 O ASN A 142 26426 25413 16569 3898 -3321 176 O
ATOM 792 CB ASN A 142 35.543 9.508 13.101 1.00178.98 C
ANISOU 792 CB ASN A 142 26246 25105 16652 3452 -2952 29 C
ATOM 793 CG ASN A 142 35.822 8.142 12.494 1.00178.97 C
ANISOU 793 CG ASN A 142 26538 25031 16432 3799 -3120 -11 C
ATOM 794 OD1 ASN A 142 36.133 7.185 13.205 1.00180.98 O
ANISOU 794 OD1 ASN A 142 27126 25115 16523 3830 -3300 -46 O
ATOM 795 ND2 ASN A 142 35.714 8.047 11.173 1.00177.51 N
ANISOU 795 ND2 ASN A 142 26265 24961 16221 4085 -3056 -6 N
ATOM 796 N LEU A 143 38.568 10.488 13.490 1.00188.02 N
ANISOU 796 N LEU A 143 26758 26763 17917 3762 -2988 307 N
ATOM 797 CA LEU A 143 40.006 10.343 13.295 1.00195.27 C
ANISOU 797 CA LEU A 143 27439 27985 18769 4075 -3066 421 C
ATOM 798 C LEU A 143 40.738 10.213 14.625 1.00205.72 C
ANISOU 798 C LEU A 143 28779 29356 20029 3939 -3223 423 C
ATOM 799 O LEU A 143 41.748 9.506 14.712 1.00209.82 O
ANISOU 799 O LEU A 143 29283 30068 20370 4270 -3381 472 O
ATOM 800 CB LEU A 143 40.552 11.533 12.501 1.00193.75 C
ANISOU 800 CB LEU A 143 26786 28084 18746 4089 -2855 547 C
ATOM 801 N LYS A 144 40.244 10.877 15.671 1.00211.49 N
ANISOU 801 N LYS A 144 29546 29935 20875 3489 -3185 370 N
ATOM 802 CA LYS A 144 40.882 10.817 16.979 1.00213.40 C
ANISOU 802 CA LYS A 144 29803 30226 21054 3336 -3334 359 C
ATOM 803 C LYS A 144 40.306 9.737 17.888 1.00213.21 C
ANISOU 803 C LYS A 144 30262 29888 20859 3307 -3508 257 C
ATOM 804 O LYS A 144 40.927 9.421 18.912 1.00215.13 O
ANISOU 804 O LYS A 144 30569 30184 20985 3303 -3664 253 O
ATOM 805 CB LYS A 144 40.783 12.178 17.679 1.00212.30 C
ANISOU 805 CB LYS A 144 29452 30099 21112 2863 -3200 360 C
ATOM 806 N ARG A 145 39.147 9.158 17.544 1.00194.36 N
ANISOU 806 N ARG A 145 28217 27196 18435 3277 -3482 174 N
ATOM 807 CA ARG A 145 38.559 8.076 18.333 1.00174.56 C
ANISOU 807 CA ARG A 145 26211 24368 15746 3216 -3627 80 C
ATOM 808 C ARG A 145 39.318 6.763 18.175 1.00171.70 C
ANISOU 808 C ARG A 145 26128 24003 15108 3679 -3816 100 C
ATOM 809 O ARG A 145 38.709 5.702 18.000 1.00165.48 O
ANISOU 809 O ARG A 145 25804 22925 14147 3764 -3882 28 O
ATOM 810 CB ARG A 145 37.092 7.909 17.943 1.00158.27 C
ANISOU 810 CB ARG A 145 24386 22038 13712 2995 -3529 -17 C
ATOM 811 CG ARG A 145 36.200 7.295 19.021 1.00146.48 C
ANISOU 811 CG ARG A 145 23325 20222 12110 2686 -3601 -116 C
ATOM 812 CD ARG A 145 34.736 7.578 18.720 1.00136.32 C
ANISOU 812 CD ARG A 145 22086 18812 10897 2366 -3456 -202 C
ATOM 813 NE ARG A 145 33.878 6.418 18.943 1.00134.24 N
ANISOU 813 NE ARG A 145 22309 18260 10435 2234 -3538 -305 N
ATOM 814 CZ ARG A 145 32.560 6.432 18.782 1.00128.22 C
ANISOU 814 CZ ARG A 145 21627 17419 9673 1928 -3442 -395 C
ATOM 815 NH1 ARG A 145 31.849 5.334 19.002 1.00126.95 N
ANISOU 815 NH1 ARG A 145 21919 17005 9310 1761 -3519 -490 N
ATOM 816 NH2 ARG A 145 31.954 7.549 18.402 1.00123.74 N
ANISOU 816 NH2 ARG A 145 20694 17041 9281 1789 -3262 -388 N
ATOM 817 N THR A 146 40.647 6.817 18.229 1.00179.14 N
ANISOU 817 N THR A 146 26808 25280 15979 3984 -3899 196 N
ATOM 818 CA THR A 146 41.452 5.611 18.116 1.00176.06 C
ANISOU 818 CA THR A 146 26676 24935 15283 4503 -4074 230 C
ATOM 819 C THR A 146 41.149 4.690 19.301 1.00174.58 C
ANISOU 819 C THR A 146 27031 24417 14885 4437 -4221 160 C
ATOM 820 O THR A 146 41.019 5.176 20.429 1.00183.54 O
ANISOU 820 O THR A 146 28118 25520 16098 4091 -4235 135 O
ATOM 821 CB THR A 146 42.944 5.964 18.083 1.00172.85 C
ANISOU 821 CB THR A 146 25803 25048 14825 4813 -4129 351 C
ATOM 822 OG1 THR A 146 43.153 7.128 17.275 1.00170.54 O
ANISOU 822 OG1 THR A 146 24967 25048 14781 4687 -3955 418 O
ATOM 823 CG2 THR A 146 43.758 4.819 17.502 1.00174.11 C
ANISOU 823 CG2 THR A 146 26154 25336 14663 5474 -4261 410 C
ATOM 824 N PRO A 147 40.991 3.369 19.076 1.00169.82 N
ANISOU 824 N PRO A 147 26988 23533 14002 4750 -4323 126 N
ATOM 825 CA PRO A 147 40.815 2.436 20.203 1.00171.74 C
ANISOU 825 CA PRO A 147 27800 23451 14001 4731 -4454 79 C
ATOM 826 C PRO A 147 41.834 2.631 21.314 1.00166.82 C
ANISOU 826 C PRO A 147 26997 23103 13286 4850 -4572 141 C
ATOM 827 O PRO A 147 41.534 2.393 22.488 1.00156.21 O
ANISOU 827 O PRO A 147 25951 21539 11862 4636 -4633 99 O
ATOM 828 CB PRO A 147 40.976 1.062 19.539 1.00171.61 C
ANISOU 828 CB PRO A 147 28339 23214 13650 5227 -4544 73 C
ATOM 829 CG PRO A 147 40.459 1.270 18.158 1.00165.27 C
ANISOU 829 CG PRO A 147 27391 22417 12989 5218 -4426 45 C
ATOM 830 CD PRO A 147 40.806 2.698 17.780 1.00164.53 C
ANISOU 830 CD PRO A 147 26520 22768 13224 5074 -4302 115 C
ATOM 831 N ARG A 148 43.045 3.063 20.953 1.00172.65 N
ANISOU 831 N ARG A 148 27231 24354 14016 5184 -4603 240 N
ATOM 832 CA ARG A 148 44.062 3.340 21.962 1.00174.87 C
ANISOU 832 CA ARG A 148 27244 24997 14200 5272 -4720 290 C
ATOM 833 C ARG A 148 43.711 4.584 22.772 1.00177.20 C
ANISOU 833 C ARG A 148 27183 25347 14795 4656 -4643 249 C
ATOM 834 O ARG A 148 43.963 4.635 23.982 1.00179.94 O
ANISOU 834 O ARG A 148 27575 25733 15060 4537 -4742 228 O
ATOM 835 CB ARG A 148 45.427 3.491 21.296 1.00178.84 C
ANISOU 835 CB ARG A 148 27252 26101 14598 5757 -4764 406 C
ATOM 836 N ARG A 149 43.128 5.595 22.122 1.00176.31 N
ANISOU 836 N ARG A 149 26748 25234 15008 4285 -4463 235 N
ATOM 837 CA ARG A 149 42.715 6.803 22.833 1.00176.37 C
ANISOU 837 CA ARG A 149 26491 25241 15281 3717 -4367 193 C
ATOM 838 C ARG A 149 41.660 6.489 23.889 1.00175.87 C
ANISOU 838 C ARG A 149 26899 24730 15195 3385 -4386 99 C
ATOM 839 O ARG A 149 41.756 6.945 25.034 1.00181.74 O
ANISOU 839 O ARG A 149 27591 25503 15959 3121 -4432 71 O
ATOM 840 CB ARG A 149 42.186 7.842 21.839 1.00175.69 C
ANISOU 840 CB ARG A 149 26075 25180 15498 3460 -4150 202 C
ATOM 841 CG ARG A 149 43.229 8.827 21.312 1.00179.77 C
ANISOU 841 CG ARG A 149 25981 26185 16137 3488 -4082 292 C
ATOM 842 CD ARG A 149 43.606 9.874 22.357 1.00184.60 C
ANISOU 842 CD ARG A 149 26310 26968 16860 3071 -4081 273 C
ATOM 843 NE ARG A 149 44.160 11.084 21.750 1.00187.55 N
ANISOU 843 NE ARG A 149 26165 27668 17428 2889 -3931 336 N
ATOM 844 CZ ARG A 149 43.443 12.158 21.427 1.00185.76 C
ANISOU 844 CZ ARG A 149 25855 27273 17453 2513 -3716 323 C
ATOM 845 NH1 ARG A 149 44.035 13.210 20.879 1.00186.97 N
ANISOU 845 NH1 ARG A 149 25585 27706 17747 2360 -3573 391 N
ATOM 846 NH2 ARG A 149 42.136 12.184 21.653 1.00182.17 N
ANISOU 846 NH2 ARG A 149 25746 26385 17085 2296 -3634 247 N
ATOM 847 N ILE A 150 40.643 5.707 23.522 1.00163.94 N
ANISOU 847 N ILE A 150 25848 22816 13625 3375 -4349 47 N
ATOM 848 CA ILE A 150 39.562 5.419 24.461 1.00154.25 C
ANISOU 848 CA ILE A 150 25049 21186 12373 3016 -4342 -35 C
ATOM 849 C ILE A 150 39.993 4.398 25.507 1.00152.18 C
ANISOU 849 C ILE A 150 25225 20793 11802 3232 -4521 -34 C
ATOM 850 O ILE A 150 39.441 4.369 26.613 1.00150.13 O
ANISOU 850 O ILE A 150 25214 20312 11517 2934 -4535 -80 O
ATOM 851 CB ILE A 150 38.302 4.957 23.707 1.00145.96 C
ANISOU 851 CB ILE A 150 24311 19800 11348 2868 -4235 -99 C
ATOM 852 CG1 ILE A 150 38.685 4.233 22.411 1.00124.34 C
ANISOU 852 CG1 ILE A 150 21648 17107 8491 3313 -4260 -69 C
ATOM 853 CG2 ILE A 150 37.374 6.139 23.447 1.00141.68 C
ANISOU 853 CG2 ILE A 150 23447 19283 11101 2435 -4042 -133 C
ATOM 854 CD1 ILE A 150 38.047 4.815 21.160 1.00176.94 C
ANISOU 854 CD1 ILE A 150 28040 23828 15361 3208 -4095 -86 C
ATOM 855 N LYS A 151 40.970 3.547 25.189 1.00159.67 N
ANISOU 855 N LYS A 151 26294 21880 12491 3780 -4651 26 N
ATOM 856 CA LYS A 151 41.551 2.687 26.212 1.00168.70 C
ANISOU 856 CA LYS A 151 27812 22974 13312 4064 -4819 44 C
ATOM 857 C LYS A 151 42.220 3.525 27.292 1.00187.12 C
ANISOU 857 C LYS A 151 29750 25645 15703 3916 -4887 55 C
ATOM 858 O LYS A 151 42.071 3.256 28.490 1.00192.57 O
ANISOU 858 O LYS A 151 30733 26174 16261 3810 -4962 26 O
ATOM 859 CB LYS A 151 42.550 1.719 25.579 1.00165.67 C
ANISOU 859 CB LYS A 151 27583 22749 12613 4756 -4934 117 C
ATOM 860 N ALA A 152 42.953 4.562 26.878 1.00197.79 N
ANISOU 860 N ALA A 152 30443 27467 17242 3882 -4856 91 N
ATOM 861 CA ALA A 152 43.566 5.478 27.832 1.00200.35 C
ANISOU 861 CA ALA A 152 30361 28127 17635 3656 -4912 82 C
ATOM 862 C ALA A 152 42.516 6.148 28.709 1.00199.33 C
ANISOU 862 C ALA A 152 30350 27683 17705 3069 -4823 0 C
ATOM 863 O ALA A 152 42.753 6.398 29.896 1.00200.88 O
ANISOU 863 O ALA A 152 30540 27949 17836 2922 -4912 -33 O
ATOM 864 CB ALA A 152 44.388 6.529 27.087 1.00203.14 C
ANISOU 864 CB ALA A 152 30020 28988 18177 3620 -4852 130 C
ATOM 865 N ILE A 153 41.344 6.440 28.138 1.00197.30 N
ANISOU 865 N ILE A 153 30194 27106 17665 2755 -4649 -36 N
ATOM 866 CA ILE A 153 40.293 7.130 28.882 1.00189.76 C
ANISOU 866 CA ILE A 153 29322 25895 16883 2231 -4543 -105 C
ATOM 867 C ILE A 153 39.819 6.281 30.051 1.00182.75 C
ANISOU 867 C ILE A 153 28971 24687 15780 2194 -4633 -141 C
ATOM 868 O ILE A 153 39.575 6.789 31.151 1.00185.13 O
ANISOU 868 O ILE A 153 29285 24943 16113 1897 -4641 -181 O
ATOM 869 CB ILE A 153 39.126 7.491 27.945 1.00191.30 C
ANISOU 869 CB ILE A 153 29517 25873 17295 1985 -4340 -128 C
ATOM 870 CG1 ILE A 153 39.600 8.415 26.825 1.00197.06 C
ANISOU 870 CG1 ILE A 153 29731 26910 18235 2022 -4231 -83 C
ATOM 871 CG2 ILE A 153 37.998 8.148 28.725 1.00187.79 C
ANISOU 871 CG2 ILE A 153 29173 25199 16982 1502 -4226 -191 C
ATOM 872 CD1 ILE A 153 38.513 8.780 25.833 1.00198.94 C
ANISOU 872 CD1 ILE A 153 29949 26984 18656 1853 -4032 -101 C
ATOM 873 N ILE A 154 39.679 4.975 29.831 1.00174.49 N
ANISOU 873 N ILE A 154 28409 23396 14492 2494 -4695 -125 N
ATOM 874 CA ILE A 154 39.161 4.098 30.873 1.00168.65 C
ANISOU 874 CA ILE A 154 28253 22299 13528 2445 -4753 -149 C
ATOM 875 C ILE A 154 40.138 4.022 32.039 1.00168.77 C
ANISOU 875 C ILE A 154 28257 22526 13344 2651 -4924 -129 C
ATOM 876 O ILE A 154 39.756 4.202 33.200 1.00167.10 O
ANISOU 876 O ILE A 154 28201 22183 13105 2392 -4937 -163 O
ATOM 877 CB ILE A 154 38.849 2.708 30.292 1.00162.04 C
ANISOU 877 CB ILE A 154 27993 21123 12450 2717 -4770 -137 C
ATOM 878 CG1 ILE A 154 37.659 2.798 29.334 1.00160.27 C
ANISOU 878 CG1 ILE A 154 27809 20677 12410 2401 -4602 -185 C
ATOM 879 CG2 ILE A 154 38.583 1.712 31.406 1.00161.81 C
ANISOU 879 CG2 ILE A 154 28611 20743 12124 2745 -4842 -141 C
ATOM 880 CD1 ILE A 154 36.430 3.434 29.946 1.00160.32 C
ANISOU 880 CD1 ILE A 154 27804 20517 12592 1827 -4469 -244 C
ATOM 881 N LEU A 155 41.418 3.775 31.744 1.00167.42 N
ANISOU 881 N LEU A 155 27874 22727 13010 3134 -5057 -73 N
ATOM 882 CA LEU A 155 42.427 3.662 32.795 1.00168.55 C
ANISOU 882 CA LEU A 155 27962 23163 12918 3388 -5236 -56 C
ATOM 883 C LEU A 155 42.456 4.923 33.650 1.00165.46 C
ANISOU 883 C LEU A 155 27154 22981 12732 2941 -5229 -114 C
ATOM 884 O LEU A 155 42.624 4.856 34.874 1.00173.43 O
ANISOU 884 O LEU A 155 28308 24003 13585 2915 -5332 -139 O
ATOM 885 CB LEU A 155 43.809 3.400 32.191 1.00 30.00 C
ATOM 886 CG LEU A 155 43.987 2.065 31.462 1.00 30.00 C
ATOM 887 CD1 LEU A 155 45.349 2.001 30.789 1.00 30.00 C
ATOM 888 CD2 LEU A 155 43.801 0.899 32.420 1.00 30.00 C
ATOM 889 N THR A 156 42.272 6.090 33.026 1.00156.83 N
ANISOU 889 N THR A 156 25583 22032 11972 2587 -5101 -137 N
ATOM 890 CA THR A 156 42.287 7.339 33.781 1.00157.58 C
ANISOU 890 CA THR A 156 25338 22284 12250 2147 -5079 -198 C
ATOM 891 C THR A 156 41.066 7.456 34.685 1.00155.19 C
ANISOU 891 C THR A 156 25413 21549 12005 1757 -4995 -255 C
ATOM 892 O THR A 156 41.158 8.008 35.789 1.00154.05 O
ANISOU 892 O THR A 156 25220 21467 11845 1537 -5050 -306 O
ATOM 893 CB THR A 156 42.368 8.530 32.828 1.00156.31 C
ANISOU 893 CB THR A 156 24658 22331 12403 1888 -4935 -198 C
ATOM 894 OG1 THR A 156 43.514 8.384 31.980 1.00162.00 O
ANISOU 894 OG1 THR A 156 25015 23486 13053 2255 -5005 -133 O
ATOM 895 CG2 THR A 156 42.482 9.838 33.609 1.00154.73 C
ANISOU 895 CG2 THR A 156 24158 22276 12355 1438 -4913 -266 C
ATOM 896 N VAL A 157 39.914 6.950 34.237 1.00153.73 N
ANISOU 896 N VAL A 157 25591 20950 11868 1659 -4863 -250 N
ATOM 897 CA VAL A 157 38.750 6.889 35.116 1.00148.63 C
ANISOU 897 CA VAL A 157 25323 19931 11219 1325 -4786 -291 C
ATOM 898 C VAL A 157 39.083 6.088 36.367 1.00151.25 C
ANISOU 898 C VAL A 157 26039 20183 11245 1510 -4943 -286 C
ATOM 899 O VAL A 157 38.756 6.493 37.487 1.00147.78 O
ANISOU 899 O VAL A 157 25682 19674 10794 1260 -4949 -326 O
ATOM 900 CB VAL A 157 37.534 6.301 34.377 1.00141.91 C
ANISOU 900 CB VAL A 157 24793 18715 10410 1209 -4636 -286 C
ATOM 901 CG1 VAL A 157 36.371 6.121 35.345 1.00136.86 C
ANISOU 901 CG1 VAL A 157 24543 17742 9715 874 -4561 -317 C
ATOM 902 CG2 VAL A 157 37.127 7.203 33.227 1.00137.96 C
ANISOU 902 CG2 VAL A 157 23901 18317 10202 1026 -4471 -295 C
ATOM 903 N TRP A 158 39.761 4.949 36.196 1.00154.32 N
ANISOU 903 N TRP A 158 26690 20586 11359 1987 -5069 -233 N
ATOM 904 CA TRP A 158 40.208 4.171 37.348 1.00156.57 C
ANISOU 904 CA TRP A 158 27351 20830 11310 2253 -5222 -217 C
ATOM 905 C TRP A 158 41.190 4.962 38.204 1.00160.01 C
ANISOU 905 C TRP A 158 27369 21711 11717 2271 -5365 -251 C
ATOM 906 O TRP A 158 41.149 4.888 39.438 1.00161.82 O
ANISOU 906 O TRP A 158 27811 21883 11792 2223 -5439 -275 O
ATOM 907 CB TRP A 158 40.842 2.861 36.882 1.00160.17 C
ANISOU 907 CB TRP A 158 28162 21249 11446 2836 -5320 -147 C
ATOM 908 CG TRP A 158 39.883 1.989 36.151 1.00162.68 C
ANISOU 908 CG TRP A 158 28982 21090 11740 2790 -5195 -130 C
ATOM 909 CD1 TRP A 158 39.902 1.675 34.825 1.00161.87 C
ANISOU 909 CD1 TRP A 158 28841 20970 11691 2958 -5144 -109 C
ATOM 910 CD2 TRP A 158 38.739 1.331 36.704 1.00165.20 C
ANISOU 910 CD2 TRP A 158 29911 20895 11962 2519 -5100 -140 C
ATOM 911 NE1 TRP A 158 38.845 0.853 34.519 1.00162.61 N
ANISOU 911 NE1 TRP A 158 29495 20568 11722 2797 -5035 -120 N
ATOM 912 CE2 TRP A 158 38.115 0.628 35.656 1.00165.83 C
ANISOU 912 CE2 TRP A 158 30287 20671 12050 2504 -4994 -136 C
ATOM 913 CE3 TRP A 158 38.185 1.265 37.986 1.00163.88 C
ANISOU 913 CE3 TRP A 158 30021 20509 11738 2265 -5065 -152 C
ATOM 914 CZ2 TRP A 158 36.964 -0.132 35.851 1.00167.02 C
ANISOU 914 CZ2 TRP A 158 30988 20324 12148 2201 -4858 -150 C
ATOM 915 CZ3 TRP A 158 37.044 0.512 38.176 1.00165.20 C
ANISOU 915 CZ3 TRP A 158 30724 20183 11860 1990 -4918 -151 C
ATOM 916 CH2 TRP A 158 36.445 -0.177 37.115 1.00166.68 C
ANISOU 916 CH2 TRP A 158 31190 20092 12050 1940 -4819 -152 C
ATOM 917 N VAL A 159 42.080 5.724 37.568 1.00163.00 N
ANISOU 917 N VAL A 159 27152 22550 12230 2320 -5405 -257 N
ATOM 918 CA VAL A 159 43.081 6.489 38.307 1.00168.57 C
ANISOU 918 CA VAL A 159 27421 23736 12893 2292 -5549 -303 C
ATOM 919 C VAL A 159 42.414 7.579 39.140 1.00178.42 C
ANISOU 919 C VAL A 159 28593 24857 14343 1734 -5474 -389 C
ATOM 920 O VAL A 159 42.644 7.688 40.350 1.00186.83 O
ANISOU 920 O VAL A 159 29732 26000 15254 1692 -5589 -437 O
ATOM 921 CB VAL A 159 44.126 7.081 37.345 1.00160.01 C
ANISOU 921 CB VAL A 159 25710 23176 11912 2399 -5580 -286 C
ATOM 922 CG1 VAL A 159 45.028 8.061 38.077 1.00157.17 C
ANISOU 922 CG1 VAL A 159 24860 23311 11547 2204 -5702 -357 C
ATOM 923 CG2 VAL A 159 44.954 5.973 36.708 1.00159.85 C
ANISOU 923 CG2 VAL A 159 25759 23366 11611 3044 -5688 -197 C
ATOM 924 N ILE A 160 41.580 8.404 38.503 1.00176.70 N
ANISOU 924 N ILE A 160 28241 24450 14448 1333 -5277 -410 N
ATOM 925 CA ILE A 160 40.959 9.513 39.220 1.00177.11 C
ANISOU 925 CA ILE A 160 28230 24390 14674 844 -5189 -488 C
ATOM 926 C ILE A 160 39.904 9.002 40.192 1.00180.64 C
ANISOU 926 C ILE A 160 29206 24419 15010 735 -5148 -495 C
ATOM 927 O ILE A 160 39.682 9.606 41.249 1.00185.62 O
ANISOU 927 O ILE A 160 29879 25017 15631 484 -5163 -557 O
ATOM 928 CB ILE A 160 40.382 10.536 38.223 1.00175.00 C
ANISOU 928 CB ILE A 160 27696 24056 14741 515 -4977 -495 C
ATOM 929 CG1 ILE A 160 41.469 11.003 37.257 1.00175.12 C
ANISOU 929 CG1 ILE A 160 27200 24489 14848 620 -5006 -475 C
ATOM 930 CG2 ILE A 160 39.817 11.744 38.952 1.00173.19 C
ANISOU 930 CG2 ILE A 160 27428 23720 14655 60 -4880 -574 C
ATOM 931 CD1 ILE A 160 42.588 11.776 37.930 1.00175.98 C
ANISOU 931 CD1 ILE A 160 26937 25027 14901 496 -5149 -539 C
ATOM 932 N SER A 161 39.242 7.888 39.866 1.00182.08 N
ANISOU 932 N SER A 161 29814 24277 15090 904 -5093 -433 N
ATOM 933 CA SER A 161 38.305 7.299 40.815 1.00182.78 C
ANISOU 933 CA SER A 161 30422 23992 15033 796 -5052 -428 C
ATOM 934 C SER A 161 39.025 6.792 42.055 1.00199.05 C
ANISOU 934 C SER A 161 32691 26153 16787 1047 -5246 -432 C
ATOM 935 O SER A 161 38.455 6.807 43.151 1.00212.40 O
ANISOU 935 O SER A 161 34661 27653 18388 875 -5231 -451 O
ATOM 936 CB SER A 161 37.518 6.161 40.163 1.00170.58 C
ANISOU 936 CB SER A 161 29312 22089 13413 888 -4955 -367 C
ATOM 937 OG SER A 161 36.496 5.689 41.020 1.00161.48 O
ANISOU 937 OG SER A 161 28633 20581 12141 688 -4879 -360 O
ATOM 938 N ALA A 162 40.276 6.351 41.907 1.00196.37 N
ANISOU 938 N ALA A 162 32206 26145 16261 1478 -5426 -409 N
ATOM 939 CA ALA A 162 41.034 5.913 43.074 1.00201.90 C
ANISOU 939 CA ALA A 162 33060 27017 16637 1768 -5620 -415 C
ATOM 940 C ALA A 162 41.482 7.088 43.932 1.00201.09 C
ANISOU 940 C ALA A 162 32564 27238 16602 1502 -5708 -515 C
ATOM 941 O ALA A 162 41.753 6.913 45.125 1.00202.70 O
ANISOU 941 O ALA A 162 32939 27507 16571 1603 -5836 -543 O
ATOM 942 CB ALA A 162 42.242 5.081 42.641 1.00205.54 C
ANISOU 942 CB ALA A 162 33465 27798 16831 2362 -5785 -358 C
ATOM 943 N VAL A 163 41.574 8.285 43.349 1.00193.06 N
ANISOU 943 N VAL A 163 31055 26414 15885 1164 -5639 -572 N
ATOM 944 CA VAL A 163 41.957 9.458 44.128 1.00188.36 C
ANISOU 944 CA VAL A 163 30139 26077 15352 849 -5708 -681 C
ATOM 945 C VAL A 163 40.795 9.921 44.996 1.00188.06 C
ANISOU 945 C VAL A 163 30411 25653 15391 477 -5585 -723 C
ATOM 946 O VAL A 163 40.965 10.209 46.186 1.00197.82 O
ANISOU 946 O VAL A 163 31717 26962 16485 400 -5691 -792 O
ATOM 947 CB VAL A 163 42.455 10.583 43.204 1.00181.38 C
ANISOU 947 CB VAL A 163 28690 25490 14737 595 -5655 -722 C
ATOM 948 CG1 VAL A 163 42.700 11.854 44.005 1.00183.96 C
ANISOU 948 CG1 VAL A 163 28778 25989 15130 182 -5696 -847 C
ATOM 949 CG2 VAL A 163 43.721 10.153 42.483 1.00180.34 C
ANISOU 949 CG2 VAL A 163 28200 25838 14485 977 -5795 -679 C
ATOM 950 N ILE A 164 39.596 10.000 44.411 1.00180.45 N
ANISOU 950 N ILE A 164 29623 24308 14630 258 -5361 -684 N
ATOM 951 CA ILE A 164 38.406 10.345 45.184 1.00178.58 C
ANISOU 951 CA ILE A 164 29686 23733 14433 -50 -5225 -705 C
ATOM 952 C ILE A 164 38.151 9.312 46.277 1.00194.03 C
ANISOU 952 C ILE A 164 32135 25496 16091 144 -5300 -667 C
ATOM 953 O ILE A 164 37.663 9.651 47.362 1.00201.49 O
ANISOU 953 O ILE A 164 33267 26323 16966 -35 -5285 -705 O
ATOM 954 CB ILE A 164 37.196 10.501 44.237 1.00166.00 C
ANISOU 954 CB ILE A 164 28148 21852 13071 -264 -4974 -660 C
ATOM 955 CG1 ILE A 164 37.263 11.846 43.507 1.00165.98 C
ANISOU 955 CG1 ILE A 164 27724 21991 13349 -528 -4866 -711 C
ATOM 956 CG2 ILE A 164 35.873 10.348 44.981 1.00155.62 C
ANISOU 956 CG2 ILE A 164 27229 20196 11703 -467 -4833 -642 C
ATOM 957 CD1 ILE A 164 37.367 13.038 44.442 1.00164.56 C
ANISOU 957 CD1 ILE A 164 27452 21882 13192 -810 -4883 -810 C
ATOM 958 N SER A 165 38.504 8.048 46.027 1.00197.85 N
ANISOU 958 N SER A 165 32866 25938 16371 532 -5376 -588 N
ATOM 959 CA SER A 165 38.261 6.988 47.001 1.00199.67 C
ANISOU 959 CA SER A 165 33638 25937 16289 739 -5424 -535 C
ATOM 960 C SER A 165 39.281 7.003 48.135 1.00208.20 C
ANISOU 960 C SER A 165 34666 27321 17119 980 -5645 -582 C
ATOM 961 O SER A 165 38.941 6.691 49.282 1.00210.74 O
ANISOU 961 O SER A 165 35262 27478 17332 984 -5605 -569 O
ATOM 962 CB SER A 165 38.269 5.624 46.307 1.00191.45 C
ANISOU 962 CB SER A 165 32938 24696 15107 1078 -5399 -433 C
ATOM 963 OG SER A 165 37.274 5.559 45.303 1.00180.29 O
ANISOU 963 OG SER A 165 31598 23013 13890 834 -5209 -403 O
ATOM 964 N PHE A 166 40.530 7.342 47.836 1.00213.61 N
ANISOU 964 N PHE A 166 34912 28479 17771 1173 -5825 -630 N
ATOM 965 CA PHE A 166 41.579 7.311 48.850 1.00217.15 C
ANISOU 965 CA PHE A 166 35224 29306 17975 1423 -6031 -680 C
ATOM 966 C PHE A 166 41.477 8.536 49.751 1.00215.23 C
ANISOU 966 C PHE A 166 34816 29177 17786 1023 -6090 -811 C
ATOM 967 O PHE A 166 41.573 9.666 49.255 1.00214.03 O
ANISOU 967 O PHE A 166 34240 29177 17903 670 -6043 -889 O
ATOM 968 CB PHE A 166 42.956 7.244 48.202 1.00222.19 C
ANISOU 968 CB PHE A 166 35424 30490 18509 1760 -6218 -689 C
ATOM 969 CG PHE A 166 44.084 7.190 49.190 1.00232.29 C
ANISOU 969 CG PHE A 166 36467 32250 19543 2021 -6412 -739 C
ATOM 970 CD1 PHE A 166 44.335 6.034 49.916 1.00237.42 C
ANISOU 970 CD1 PHE A 166 37401 32836 19972 2466 -6395 -652 C
ATOM 971 CD2 PHE A 166 44.890 8.295 49.398 1.00238.26 C
ANISOU 971 CD2 PHE A 166 36732 33522 20273 1804 -6610 -879 C
ATOM 972 CE1 PHE A 166 45.371 5.987 50.832 1.00243.14 C
ANISOU 972 CE1 PHE A 166 37889 34035 20456 2721 -6569 -695 C
ATOM 973 CE2 PHE A 166 45.928 8.252 50.311 1.00243.88 C
ANISOU 973 CE2 PHE A 166 37189 34734 20742 2017 -6793 -935 C
ATOM 974 CZ PHE A 166 46.168 7.097 51.029 1.00246.06 C
ANISOU 974 CZ PHE A 166 37719 34970 20801 2490 -6771 -838 C
ATOM 975 N PRO A 167 41.284 8.365 51.055 1.00210.70 N
ANISOU 975 N PRO A 167 34472 28511 17073 1049 -6095 -826 N
ATOM 976 CA PRO A 167 41.111 9.512 51.946 1.00203.44 C
ANISOU 976 CA PRO A 167 33457 27654 16188 675 -6140 -955 C
ATOM 977 C PRO A 167 42.428 9.915 52.583 1.00206.78 C
ANISOU 977 C PRO A 167 33507 28641 16420 788 -6401 -1072 C
ATOM 978 O PRO A 167 43.219 9.054 52.999 1.00209.24 O
ANISOU 978 O PRO A 167 33790 29206 16505 1228 -6505 -1028 O
ATOM 979 CB PRO A 167 40.116 8.991 52.997 1.00200.63 C
ANISOU 979 CB PRO A 167 33565 26884 15782 670 -5978 -892 C
ATOM 980 CG PRO A 167 39.977 7.469 52.727 1.00201.62 C
ANISOU 980 CG PRO A 167 34032 26771 15803 1069 -5884 -735 C
ATOM 981 CD PRO A 167 41.057 7.096 51.762 1.00207.13 C
ANISOU 981 CD PRO A 167 34443 27809 16448 1393 -6016 -716 C
ATOM 982 N PRO A 168 42.702 11.222 52.684 1.00206.12 N
ANISOU 982 N PRO A 168 33102 28774 16442 381 -6479 -1222 N
ATOM 983 CA PRO A 168 43.987 11.674 53.237 1.00216.19 C
ANISOU 983 CA PRO A 168 33974 30645 17524 410 -6742 -1357 C
ATOM 984 C PRO A 168 44.044 11.589 54.758 1.00228.06 C
ANISOU 984 C PRO A 168 35657 32197 18800 489 -6830 -1420 C
ATOM 985 O PRO A 168 43.348 12.334 55.457 1.00227.65 O
ANISOU 985 O PRO A 168 35786 31886 18826 145 -6755 -1498 O
ATOM 986 CB PRO A 168 44.080 13.124 52.745 1.00208.17 C
ANISOU 986 CB PRO A 168 32558 29725 16811 -152 -6674 -1479 C
ATOM 987 CG PRO A 168 42.645 13.566 52.652 1.00199.15 C
ANISOU 987 CG PRO A 168 31770 27974 15922 -463 -6402 -1441 C
ATOM 988 CD PRO A 168 41.861 12.345 52.231 1.00197.84 C
ANISOU 988 CD PRO A 168 31983 27443 15744 -133 -6266 -1265 C
ATOM 989 N LEU A 169 44.871 10.680 55.279 1.00239.72 N
ANISOU 989 N LEU A 169 37057 34009 20018 961 -6948 -1374 N
ATOM 990 CA LEU A 169 45.079 10.494 56.715 1.00241.14 C
ANISOU 990 CA LEU A 169 37342 34305 19976 1102 -7022 -1417 C
ATOM 991 C LEU A 169 43.785 10.196 57.461 1.00237.26 C
ANISOU 991 C LEU A 169 37400 33195 19555 1051 -6801 -1340 C
ATOM 992 O LEU A 169 43.666 10.496 58.654 1.00244.15 O
ANISOU 992 O LEU A 169 38378 34068 20320 979 -6833 -1414 O
ATOM 993 CB LEU A 169 45.772 11.711 57.335 1.00243.61 C
ANISOU 993 CB LEU A 169 37286 35067 20208 739 -7235 -1640 C
ATOM 994 CG LEU A 169 47.279 11.818 57.114 1.00247.75 C
ANISOU 994 CG LEU A 169 37228 36375 20529 862 -7502 -1726 C
ATOM 995 CD1 LEU A 169 47.734 13.234 57.391 1.00249.33 C
ANISOU 995 CD1 LEU A 169 37099 36906 20728 306 -7680 -1969 C
ATOM 996 CD2 LEU A 169 48.021 10.832 58.007 1.00251.88 C
ANISOU 996 CD2 LEU A 169 37722 37239 20743 1383 -7596 -1657 C
ATOM 997 N ILE A 170 42.803 9.616 56.778 1.00221.05 N
ANISOU 997 N ILE A 170 35685 30637 17669 1073 -6577 -1196 N
ATOM 998 CA ILE A 170 41.499 9.333 57.361 1.00203.18 C
ANISOU 998 CA ILE A 170 33912 27814 15475 975 -6351 -1112 C
ATOM 999 C ILE A 170 41.086 7.927 56.957 1.00204.55 C
ANISOU 999 C ILE A 170 34456 27651 15611 1316 -6197 -923 C
ATOM 1000 O ILE A 170 41.124 7.580 55.771 1.00205.27 O
ANISOU 1000 O ILE A 170 34492 27695 15805 1378 -6154 -860 O
ATOM 1001 CB ILE A 170 40.438 10.354 56.913 1.00185.09 C
ANISOU 1001 CB ILE A 170 31665 25203 13457 467 -6193 -1155 C
ATOM 1002 CG1 ILE A 170 40.825 11.770 57.343 1.00182.90 C
ANISOU 1002 CG1 ILE A 170 31103 25184 13206 106 -6325 -1350 C
ATOM 1003 CG2 ILE A 170 39.078 9.984 57.472 1.00182.20 C
ANISOU 1003 CG2 ILE A 170 31765 24328 13137 387 -5950 -1052 C
ATOM 1004 CD1 ILE A 170 39.874 12.823 56.824 1.00150.20 C
ANISOU 1004 CD1 ILE A 170 27010 20742 9320 -355 -6158 -1389 C
ATOM 1005 N SER A 171 40.685 7.124 57.935 1.00198.94 N
ANISOU 1005 N SER A 171 34150 26690 14748 1524 -6110 -838 N
ATOM 1006 CA SER A 171 40.303 5.739 57.701 1.00190.44 C
ANISOU 1006 CA SER A 171 33512 25249 13597 1829 -5960 -668 C
ATOM 1007 C SER A 171 38.785 5.612 57.695 1.00186.90 C
ANISOU 1007 C SER A 171 33478 24242 13295 1505 -5702 -587 C
ATOM 1008 O SER A 171 38.109 6.140 58.584 1.00188.35 O
ANISOU 1008 O SER A 171 33773 24301 13492 1266 -5635 -618 O
ATOM 1009 CB SER A 171 40.917 4.829 58.764 1.00186.08 C
ANISOU 1009 CB SER A 171 33175 24784 12743 2298 -6024 -616 C
ATOM 1010 OG SER A 171 40.424 3.509 58.646 1.00180.61 O
ANISOU 1010 OG SER A 171 33013 23642 11969 2546 -5851 -456 O
ATOM 1011 N ILE A 172 38.256 4.914 56.695 1.00177.32 N
ANISOU 1011 N ILE A 172 32478 22723 12173 1495 -5558 -485 N
ATOM 1012 CA ILE A 172 36.816 4.725 56.569 1.00171.05 C
ANISOU 1012 CA ILE A 172 32038 21456 11495 1160 -5312 -406 C
ATOM 1013 C ILE A 172 36.296 3.867 57.722 1.00171.48 C
ANISOU 1013 C ILE A 172 32600 21201 11354 1276 -5197 -309 C
ATOM 1014 O ILE A 172 35.091 3.810 57.982 1.00167.28 O
ANISOU 1014 O ILE A 172 32349 20343 10868 969 -5000 -250 O
ATOM 1015 CB ILE A 172 36.456 4.100 55.208 1.00166.30 C
ANISOU 1015 CB ILE A 172 31548 20633 11004 1126 -5203 -332 C
ATOM 1016 N PRO A 183 43.715 -4.816 64.717 1.00252.14 N
ANISOU 1016 N PRO A 183 45188 31904 18710 6675 -5644 173 N
ATOM 1017 CA PRO A 183 42.848 -4.430 65.835 1.00263.77 C
ANISOU 1017 CA PRO A 183 46870 33156 20194 6335 -5573 175 C
ATOM 1018 C PRO A 183 41.524 -5.188 65.847 1.00290.25 C
ANISOU 1018 C PRO A 183 50998 35698 23587 6066 -5287 302 C
ATOM 1019 O PRO A 183 41.246 -5.949 64.919 1.00298.55 O
ANISOU 1019 O PRO A 183 52413 36346 24676 6082 -5154 373 O
ATOM 1020 CB PRO A 183 42.627 -2.937 65.596 1.00247.26 C
ANISOU 1020 CB PRO A 183 44121 31443 18385 5744 -5708 46 C
ATOM 1021 CG PRO A 183 43.889 -2.493 64.938 1.00240.42 C
ANISOU 1021 CG PRO A 183 42585 31248 17514 5966 -5938 -50 C
ATOM 1022 CD PRO A 183 44.321 -3.643 64.062 1.00242.40 C
ANISOU 1022 CD PRO A 183 43124 31312 17666 6432 -5859 46 C
ATOM 1023 N ALA A 184 40.722 -4.971 66.888 1.00304.68 N
ANISOU 1023 N ALA A 184 53066 37305 25392 5803 -5195 326 N
ATOM 1024 CA ALA A 184 39.472 -5.697 67.056 1.00309.62 C
ANISOU 1024 CA ALA A 184 54423 37207 26013 5525 -4917 451 C
ATOM 1025 C ALA A 184 38.483 -5.346 65.946 1.00308.05 C
ANISOU 1025 C ALA A 184 54178 36748 26120 4897 -4806 458 C
ATOM 1026 O ALA A 184 38.747 -4.519 65.067 1.00303.22 O
ANISOU 1026 O ALA A 184 52986 36490 25733 4695 -4938 367 O
ATOM 1027 CB ALA A 184 38.857 -5.393 68.422 1.00309.99 C
ANISOU 1027 CB ALA A 184 54634 37171 25976 5362 -4854 470 C
ATOM 1028 N GLU A 185 37.327 -5.998 65.999 1.00310.08 N
ANISOU 1028 N GLU A 185 55061 36387 26368 4576 -4553 567 N
ATOM 1029 CA GLU A 185 36.282 -5.731 65.027 1.00308.33 C
ANISOU 1029 CA GLU A 185 54832 35915 26405 3955 -4425 579 C
ATOM 1030 C GLU A 185 35.874 -4.254 65.121 1.00305.42 C
ANISOU 1030 C GLU A 185 53822 35935 26289 3486 -4514 482 C
ATOM 1031 O GLU A 185 35.690 -3.745 66.235 1.00305.86 O
ANISOU 1031 O GLU A 185 53801 36124 26286 3438 -4530 466 O
ATOM 1032 CB GLU A 185 35.076 -6.644 65.260 1.00310.36 C
ANISOU 1032 CB GLU A 185 55857 35499 26568 3636 -4135 708 C
ATOM 1033 CG GLU A 185 34.421 -6.526 66.628 1.00313.62 C
ANISOU 1033 CG GLU A 185 56499 35802 26862 3490 -4025 762 C
ATOM 1034 CD GLU A 185 33.249 -5.568 66.622 1.00309.92 C
ANISOU 1034 CD GLU A 185 55749 35389 26620 2806 -3936 749 C
ATOM 1035 OE1 GLU A 185 32.660 -5.337 67.697 1.00310.16 O
ANISOU 1035 OE1 GLU A 185 55891 35382 26572 2655 -3846 789 O
ATOM 1036 OE2 GLU A 185 32.915 -5.047 65.536 1.00305.53 O
ANISOU 1036 OE2 GLU A 185 54856 34923 26307 2442 -3950 700 O
ATOM 1037 N PRO A 186 35.782 -3.551 64.003 1.00300.40 N
ANISOU 1037 N PRO A 186 52737 35486 25916 3181 -4575 411 N
ATOM 1038 CA PRO A 186 35.353 -2.141 64.035 1.00296.12 C
ANISOU 1038 CA PRO A 186 51638 35263 25611 2737 -4637 312 C
ATOM 1039 C PRO A 186 33.861 -1.921 63.851 1.00293.27 C
ANISOU 1039 C PRO A 186 51446 34583 25401 2118 -4413 365 C
ATOM 1040 O PRO A 186 33.434 -0.760 63.868 1.00289.49 O
ANISOU 1040 O PRO A 186 50543 34342 25110 1770 -4439 287 O
ATOM 1041 CB PRO A 186 36.126 -1.551 62.853 1.00294.65 C
ANISOU 1041 CB PRO A 186 50891 35453 25608 2779 -4815 209 C
ATOM 1042 CG PRO A 186 36.143 -2.677 61.854 1.00295.40 C
ANISOU 1042 CG PRO A 186 51368 35204 25665 2923 -4719 292 C
ATOM 1043 CD PRO A 186 36.253 -3.950 62.665 1.00299.12 C
ANISOU 1043 CD PRO A 186 52510 35312 25831 3311 -4616 402 C
ATOM 1044 N ARG A 187 33.067 -2.983 63.688 1.00295.82 N
ANISOU 1044 N ARG A 187 52373 34395 25630 1967 -4191 489 N
ATOM 1045 CA ARG A 187 31.647 -2.855 63.374 1.00295.39 C
ANISOU 1045 CA ARG A 187 52448 34091 25697 1348 -3971 541 C
ATOM 1046 C ARG A 187 31.480 -1.983 62.133 1.00297.79 C
ANISOU 1046 C ARG A 187 52223 34631 26291 1036 -4028 452 C
ATOM 1047 O ARG A 187 31.251 -0.773 62.236 1.00300.38 O
ANISOU 1047 O ARG A 187 52065 35276 26788 812 -4082 370 O
ATOM 1048 CB ARG A 187 30.877 -2.307 64.583 1.00292.71 C
ANISOU 1048 CB ARG A 187 52115 33791 25311 1115 -3875 567 C
ATOM 1049 N CYS A 188 31.593 -2.604 60.955 1.00293.99 N
ANISOU 1049 N CYS A 188 51865 33979 25857 1038 -4010 466 N
ATOM 1050 CA CYS A 188 31.902 -1.869 59.730 1.00282.74 C
ANISOU 1050 CA CYS A 188 49911 32840 24679 950 -4127 370 C
ATOM 1051 C CYS A 188 30.788 -0.897 59.347 1.00275.15 C
ANISOU 1051 C CYS A 188 48624 31982 23939 374 -4020 336 C
ATOM 1052 O CYS A 188 29.647 -1.301 59.116 1.00275.33 O
ANISOU 1052 O CYS A 188 48927 31734 23953 -40 -3810 407 O
ATOM 1053 CB CYS A 188 32.199 -2.855 58.590 1.00280.18 C
ANISOU 1053 CB CYS A 188 49859 32270 24326 1095 -4110 402 C
ATOM 1054 SG CYS A 188 33.299 -2.212 57.271 1.00277.07 S
ANISOU 1054 SG CYS A 188 48837 32302 24135 1338 -4337 290 S
ATOM 1055 N GLU A 189 31.124 0.392 59.343 1.00254.69 N
ANISOU 1055 N GLU A 189 45451 29801 21520 351 -4158 224 N
ATOM 1056 CA GLU A 189 30.337 1.454 58.719 1.00226.96 C
ANISOU 1056 CA GLU A 189 41537 26455 18242 -85 -4094 166 C
ATOM 1057 C GLU A 189 31.311 2.554 58.309 1.00201.99 C
ANISOU 1057 C GLU A 189 37798 23704 15247 74 -4314 30 C
ATOM 1058 O GLU A 189 32.523 2.429 58.496 1.00187.30 O
ANISOU 1058 O GLU A 189 35841 22019 13307 480 -4507 -13 O
ATOM 1059 CB GLU A 189 29.238 1.979 59.650 1.00225.27 C
ANISOU 1059 CB GLU A 189 41361 26229 18003 -412 -3935 197 C
ATOM 1060 N ILE A 190 30.785 3.639 57.748 1.00197.94 N
ANISOU 1060 N ILE A 190 36901 23361 14944 -251 -4278 -39 N
ATOM 1061 CA ILE A 190 31.618 4.743 57.283 1.00196.03 C
ANISOU 1061 CA ILE A 190 36144 23473 14863 -180 -4462 -171 C
ATOM 1062 C ILE A 190 31.433 5.919 58.231 1.00208.95 C
ANISOU 1062 C ILE A 190 37576 25291 16525 -307 -4482 -250 C
ATOM 1063 O ILE A 190 30.322 6.442 58.380 1.00219.79 O
ANISOU 1063 O ILE A 190 38952 26601 17958 -623 -4310 -232 O
ATOM 1064 CB ILE A 190 31.307 5.133 55.827 1.00185.14 C
ANISOU 1064 CB ILE A 190 34501 22143 13701 -405 -4415 -201 C
ATOM 1065 CG1 ILE A 190 29.843 4.858 55.473 1.00179.20 C
ANISOU 1065 CG1 ILE A 190 33943 21164 12982 -791 -4162 -120 C
ATOM 1066 CG2 ILE A 190 32.230 4.387 54.860 1.00180.16 C
ANISOU 1066 CG2 ILE A 190 33866 21522 13063 -117 -4534 -192 C
ATOM 1067 CD1 ILE A 190 28.928 6.043 55.650 1.00177.45 C
ANISOU 1067 CD1 ILE A 190 33474 21079 12871 -1113 -4044 -161 C
ATOM 1068 N ASN A 191 32.518 6.312 58.891 1.00223.42 N
ANISOU 1068 N ASN A 191 39238 27366 18285 -50 -4690 -339 N
ATOM 1069 CA ASN A 191 32.547 7.528 59.690 1.00227.72 C
ANISOU 1069 CA ASN A 191 39564 28105 18856 -162 -4749 -449 C
ATOM 1070 C ASN A 191 31.998 8.702 58.896 1.00222.96 C
ANISOU 1070 C ASN A 191 38664 27574 18477 -500 -4676 -520 C
ATOM 1071 O ASN A 191 32.583 9.114 57.891 1.00222.23 O
ANISOU 1071 O ASN A 191 38277 27637 18521 -519 -4774 -589 O
ATOM 1072 CB ASN A 191 33.978 7.809 60.137 1.00230.22 C
ANISOU 1072 CB ASN A 191 39646 28749 19080 123 -5019 -563 C
ATOM 1073 CG ASN A 191 34.981 7.608 59.020 1.00227.29 C
ANISOU 1073 CG ASN A 191 39014 28576 18768 284 -5170 -597 C
ATOM 1074 OD1 ASN A 191 34.806 6.736 58.166 1.00225.95 O
ANISOU 1074 OD1 ASN A 191 38993 28234 18625 355 -5092 -501 O
ATOM 1075 ND2 ASN A 191 36.033 8.418 59.013 1.00227.91 N
ANISOU 1075 ND2 ASN A 191 38706 29032 18855 328 -5386 -738 N
ATOM 1076 N ASP A 192 30.866 9.240 59.350 1.00217.35 N
ANISOU 1076 N ASP A 192 38038 26760 17785 -744 -4494 -497 N
ATOM 1077 CA ASP A 192 30.112 10.225 58.577 1.00208.22 C
ANISOU 1077 CA ASP A 192 36672 25635 16808 -1036 -4365 -532 C
ATOM 1078 C ASP A 192 30.620 11.641 58.852 1.00200.51 C
ANISOU 1078 C ASP A 192 35440 24849 15896 -1094 -4480 -689 C
ATOM 1079 O ASP A 192 29.881 12.536 59.265 1.00199.66 O
ANISOU 1079 O ASP A 192 35340 24725 15797 -1250 -4359 -716 O
ATOM 1080 CB ASP A 192 28.623 10.101 58.878 1.00209.44 C
ANISOU 1080 CB ASP A 192 37027 25636 16913 -1246 -4100 -425 C
ATOM 1081 N GLN A 193 31.917 11.826 58.608 1.00196.22 N
ANISOU 1081 N GLN A 193 34680 24500 15374 -965 -4714 -792 N
ATOM 1082 CA GLN A 193 32.519 13.150 58.674 1.00194.94 C
ANISOU 1082 CA GLN A 193 34272 24522 15275 -1084 -4836 -956 C
ATOM 1083 C GLN A 193 31.781 14.091 57.733 1.00198.57 C
ANISOU 1083 C GLN A 193 34618 24920 15910 -1348 -4676 -974 C
ATOM 1084 O GLN A 193 31.940 14.004 56.511 1.00202.80 O
ANISOU 1084 O GLN A 193 34991 25487 16575 -1393 -4673 -959 O
ATOM 1085 CB GLN A 193 34.009 13.085 58.324 1.00191.43 C
ANISOU 1085 CB GLN A 193 33567 24350 14817 -945 -5104 -1052 C
ATOM 1086 N LYS A 194 30.974 14.989 58.308 1.00206.82 N
ANISOU 1086 N LYS A 194 35761 25884 16937 -1487 -4536 -1002 N
ATOM 1087 CA LYS A 194 30.096 15.856 57.524 1.00220.10 C
ANISOU 1087 CA LYS A 194 37393 27502 18734 -1681 -4340 -998 C
ATOM 1088 C LYS A 194 30.847 16.576 56.412 1.00249.81 C
ANISOU 1088 C LYS A 194 40910 31364 22644 -1793 -4435 -1096 C
ATOM 1089 O LYS A 194 30.331 16.723 55.297 1.00260.71 O
ANISOU 1089 O LYS A 194 42207 32714 24136 -1879 -4301 -1050 O
ATOM 1090 CB LYS A 194 29.423 16.873 58.446 1.00213.52 C
ANISOU 1090 CB LYS A 194 36709 26606 17814 -1747 -4225 -1045 C
ATOM 1091 N TRP A 195 32.074 17.019 56.695 1.00262.57 N
ANISOU 1091 N TRP A 195 42397 33126 24242 -1805 -4664 -1234 N
ATOM 1092 CA TRP A 195 32.863 17.726 55.692 1.00263.86 C
ANISOU 1092 CA TRP A 195 42312 33407 24535 -1952 -4755 -1330 C
ATOM 1093 C TRP A 195 33.275 16.790 54.555 1.00264.91 C
ANISOU 1093 C TRP A 195 42212 33633 24808 -1830 -4784 -1241 C
ATOM 1094 O TRP A 195 32.897 16.997 53.395 1.00266.64 O
ANISOU 1094 O TRP A 195 42261 33808 25240 -1897 -4621 -1189 O
ATOM 1095 CB TRP A 195 34.090 18.356 56.353 1.00266.21 C
ANISOU 1095 CB TRP A 195 42508 33892 24746 -2034 -5003 -1504 C
ATOM 1096 N TYR A 196 34.061 15.752 54.872 1.00250.97 N
ANISOU 1096 N TYR A 196 40456 32001 22900 -1615 -4991 -1221 N
ATOM 1097 CA TYR A 196 34.567 14.841 53.845 1.00228.77 C
ANISOU 1097 CA TYR A 196 37461 29284 20176 -1448 -5040 -1144 C
ATOM 1098 C TYR A 196 33.432 14.158 53.093 1.00207.16 C
ANISOU 1098 C TYR A 196 34854 26326 17530 -1434 -4812 -999 C
ATOM 1099 O TYR A 196 33.478 14.039 51.862 1.00214.18 O
ANISOU 1099 O TYR A 196 35528 27240 18610 -1435 -4742 -958 O
ATOM 1100 CB TYR A 196 35.474 13.792 54.492 1.00227.90 C
ANISOU 1100 CB TYR A 196 37421 29331 19840 -1147 -5270 -1132 C
ATOM 1101 CG TYR A 196 35.746 12.575 53.630 1.00218.42 C
ANISOU 1101 CG TYR A 196 36213 28140 18635 -892 -5294 -1019 C
ATOM 1102 CD1 TYR A 196 34.892 11.477 53.646 1.00211.96 C
ANISOU 1102 CD1 TYR A 196 35695 27055 17784 -774 -5134 -878 C
ATOM 1103 CD2 TYR A 196 36.866 12.519 52.814 1.00217.04 C
ANISOU 1103 CD2 TYR A 196 35700 28247 18518 -771 -5443 -1051 C
ATOM 1104 CE1 TYR A 196 35.133 10.375 52.863 1.00207.33 C
ANISOU 1104 CE1 TYR A 196 35162 26434 17179 -549 -5146 -785 C
ATOM 1105 CE2 TYR A 196 37.117 11.416 52.030 1.00212.05 C
ANISOU 1105 CE2 TYR A 196 35095 27616 17861 -497 -5460 -948 C
ATOM 1106 CZ TYR A 196 36.249 10.347 52.058 1.00208.24 C
ANISOU 1106 CZ TYR A 196 34999 26817 17304 -386 -5322 -822 C
ATOM 1107 OH TYR A 196 36.499 9.245 51.274 1.00208.60 O
ANISOU 1107 OH TYR A 196 35121 26821 17315 -118 -5327 -728 O
ATOM 1108 N VAL A 197 32.416 13.690 53.828 1.00192.70 N
ANISOU 1108 N VAL A 197 33361 24303 15554 -1433 -4692 -922 N
ATOM 1109 CA VAL A 197 31.379 12.834 53.261 1.00186.69 C
ANISOU 1109 CA VAL A 197 32748 23369 14818 -1444 -4498 -787 C
ATOM 1110 C VAL A 197 30.728 13.500 52.057 1.00192.14 C
ANISOU 1110 C VAL A 197 33197 24057 15750 -1614 -4303 -777 C
ATOM 1111 O VAL A 197 30.536 12.870 51.013 1.00194.07 O
ANISOU 1111 O VAL A 197 33363 24276 16099 -1590 -4235 -710 O
ATOM 1112 CB VAL A 197 30.355 12.483 54.356 1.00178.08 C
ANISOU 1112 CB VAL A 197 31941 22119 13602 -1476 -4343 -711 C
ATOM 1113 CG1 VAL A 197 28.950 12.372 53.795 1.00131.70 C
ANISOU 1113 CG1 VAL A 197 26131 16143 7765 -1658 -4084 -619 C
ATOM 1114 CG2 VAL A 197 30.754 11.196 55.059 1.00135.42 C
ANISOU 1114 CG2 VAL A 197 26769 16640 8046 -1253 -4428 -641 C
ATOM 1115 N ILE A 198 30.417 14.793 52.169 1.00192.69 N
ANISOU 1115 N ILE A 198 33159 24151 15904 -1764 -4206 -846 N
ATOM 1116 CA ILE A 198 29.659 15.470 51.123 1.00188.15 C
ANISOU 1116 CA ILE A 198 32395 23570 15521 -1882 -3984 -824 C
ATOM 1117 C ILE A 198 30.519 15.678 49.887 1.00178.57 C
ANISOU 1117 C ILE A 198 30854 22462 14530 -1858 -4042 -855 C
ATOM 1118 O ILE A 198 30.046 15.520 48.755 1.00177.45 O
ANISOU 1118 O ILE A 198 30569 22324 14532 -1865 -3904 -796 O
ATOM 1119 CB ILE A 198 29.089 16.794 51.662 1.00192.44 C
ANISOU 1119 CB ILE A 198 32997 24083 16039 -1994 -3853 -882 C
ATOM 1120 CG1 ILE A 198 28.040 16.507 52.738 1.00196.93 C
ANISOU 1120 CG1 ILE A 198 33864 24579 16381 -1998 -3750 -822 C
ATOM 1121 CG2 ILE A 198 28.478 17.622 50.536 1.00190.79 C
ANISOU 1121 CG2 ILE A 198 32591 23890 16009 -2057 -3633 -866 C
ATOM 1122 CD1 ILE A 198 27.469 17.744 53.393 1.00201.57 C
ANISOU 1122 CD1 ILE A 198 34566 25136 16886 -2047 -3626 -873 C
ATOM 1123 N SER A 199 31.791 16.039 50.080 1.00172.93 N
ANISOU 1123 N SER A 199 30002 21871 13833 -1835 -4246 -949 N
ATOM 1124 CA SER A 199 32.706 16.157 48.950 1.00167.42 C
ANISOU 1124 CA SER A 199 28974 21319 13319 -1806 -4311 -969 C
ATOM 1125 C SER A 199 32.833 14.831 48.218 1.00164.05 C
ANISOU 1125 C SER A 199 28526 20908 12896 -1613 -4356 -874 C
ATOM 1126 O SER A 199 32.887 14.798 46.983 1.00161.97 O
ANISOU 1126 O SER A 199 28046 20690 12807 -1588 -4283 -839 O
ATOM 1127 CB SER A 199 34.073 16.646 49.431 1.00170.38 C
ANISOU 1127 CB SER A 199 29194 21889 13654 -1834 -4541 -1086 C
ATOM 1128 OG SER A 199 35.078 16.443 48.449 1.00170.16 O
ANISOU 1128 OG SER A 199 28840 22066 13746 -1756 -4640 -1084 O
ATOM 1129 N SER A 200 32.865 13.725 48.963 1.00159.31 N
ANISOU 1129 N SER A 200 28193 20251 12088 -1462 -4465 -830 N
ATOM 1130 CA SER A 200 32.882 12.413 48.328 1.00156.94 C
ANISOU 1130 CA SER A 200 27987 19897 11747 -1277 -4487 -739 C
ATOM 1131 C SER A 200 31.497 12.032 47.814 1.00152.47 C
ANISOU 1131 C SER A 200 27564 19146 11221 -1402 -4254 -656 C
ATOM 1132 O SER A 200 31.371 11.481 46.715 1.00153.04 O
ANISOU 1132 O SER A 200 27563 19200 11386 -1353 -4199 -608 O
ATOM 1133 CB SER A 200 33.402 11.355 49.301 1.00157.11 C
ANISOU 1133 CB SER A 200 28309 19893 11494 -1054 -4668 -715 C
ATOM 1134 OG SER A 200 33.279 10.062 48.734 1.00159.00 O
ANISOU 1134 OG SER A 200 28752 20005 11656 -884 -4658 -621 O
ATOM 1135 N CYS A 201 30.450 12.313 48.597 1.00147.49 N
ANISOU 1135 N CYS A 201 27127 18411 10503 -1564 -4116 -641 N
ATOM 1136 CA CYS A 201 29.084 12.093 48.128 1.00136.78 C
ANISOU 1136 CA CYS A 201 25835 16970 9167 -1719 -3884 -571 C
ATOM 1137 C CYS A 201 28.848 12.798 46.796 1.00130.29 C
ANISOU 1137 C CYS A 201 24672 16249 8582 -1774 -3751 -584 C
ATOM 1138 O CYS A 201 28.284 12.217 45.860 1.00122.36 O
ANISOU 1138 O CYS A 201 23631 15233 7629 -1803 -3651 -534 O
ATOM 1139 CB CYS A 201 28.092 12.576 49.186 1.00129.15 C
ANISOU 1139 CB CYS A 201 25039 15964 8066 -1865 -3752 -561 C
ATOM 1140 SG CYS A 201 26.442 11.869 49.072 1.00127.92 S
ANISOU 1140 SG CYS A 201 25049 15757 7797 -2058 -3508 -457 S
ATOM 1141 N ILE A 202 29.282 14.055 46.693 1.00125.03 N
ANISOU 1141 N ILE A 202 23780 15677 8048 -1795 -3747 -654 N
ATOM 1142 CA ILE A 202 29.285 14.731 45.400 1.00123.90 C
ANISOU 1142 CA ILE A 202 23331 15622 8123 -1804 -3638 -662 C
ATOM 1143 C ILE A 202 30.356 14.135 44.490 1.00132.20 C
ANISOU 1143 C ILE A 202 24208 16744 9278 -1655 -3784 -659 C
ATOM 1144 O ILE A 202 30.122 13.909 43.296 1.00129.52 O
ANISOU 1144 O ILE A 202 23715 16438 9060 -1618 -3697 -623 O
ATOM 1145 CB ILE A 202 29.480 16.247 45.587 1.00121.25 C
ANISOU 1145 CB ILE A 202 22879 15322 7868 -1884 -3577 -735 C
ATOM 1146 CG1 ILE A 202 28.153 16.929 45.934 1.00120.83 C
ANISOU 1146 CG1 ILE A 202 22941 15230 7738 -1968 -3348 -714 C
ATOM 1147 CG2 ILE A 202 30.106 16.871 44.349 1.00120.40 C
ANISOU 1147 CG2 ILE A 202 22467 15304 7978 -1861 -3548 -753 C
ATOM 1148 CD1 ILE A 202 28.286 18.412 46.207 1.00121.28 C
ANISOU 1148 CD1 ILE A 202 22996 15260 7824 -2024 -3274 -785 C
ATOM 1149 N GLY A 203 31.540 13.854 45.044 1.00137.18 N
ANISOU 1149 N GLY A 203 24855 17431 9837 -1542 -4010 -696 N
ATOM 1150 CA GLY A 203 32.652 13.404 44.220 1.00139.62 C
ANISOU 1150 CA GLY A 203 24960 17872 10216 -1360 -4152 -692 C
ATOM 1151 C GLY A 203 32.398 12.092 43.509 1.00137.68 C
ANISOU 1151 C GLY A 203 24846 17543 9924 -1210 -4149 -615 C
ATOM 1152 O GLY A 203 32.952 11.843 42.432 1.00133.00 O
ANISOU 1152 O GLY A 203 24057 17045 9432 -1068 -4180 -597 O
ATOM 1153 N SER A 204 31.552 11.240 44.086 1.00139.22 N
ANISOU 1153 N SER A 204 25394 17553 9951 -1252 -4102 -569 N
ATOM 1154 CA SER A 204 31.213 9.953 43.494 1.00137.84 C
ANISOU 1154 CA SER A 204 25436 17242 9694 -1168 -4086 -506 C
ATOM 1155 C SER A 204 29.984 10.049 42.594 1.00133.40 C
ANISOU 1155 C SER A 204 24801 16645 9240 -1360 -3866 -483 C
ATOM 1156 O SER A 204 30.063 9.748 41.396 1.00137.64 O
ANISOU 1156 O SER A 204 25204 17215 9877 -1283 -3841 -471 O
ATOM 1157 CB SER A 204 30.998 8.912 44.602 1.00142.10 C
ANISOU 1157 CB SER A 204 26442 17588 9960 -1140 -4148 -466 C
ATOM 1158 OG SER A 204 30.112 9.395 45.597 1.00140.59 O
ANISOU 1158 OG SER A 204 26370 17344 9704 -1364 -4039 -469 O
ATOM 1159 N PHE A 205 28.847 10.491 43.142 1.00121.26 N
ANISOU 1159 N PHE A 205 23327 15082 7666 -1592 -3705 -478 N
ATOM 1160 CA PHE A 205 27.580 10.475 42.410 1.00120.20 C
ANISOU 1160 CA PHE A 205 23124 14977 7568 -1774 -3497 -455 C
ATOM 1161 C PHE A 205 27.245 11.815 41.765 1.00131.44 C
ANISOU 1161 C PHE A 205 24182 16580 9178 -1807 -3349 -483 C
ATOM 1162 O PHE A 205 27.102 11.895 40.543 1.00139.86 O
ANISOU 1162 O PHE A 205 25032 17736 10374 -1769 -3276 -482 O
ATOM 1163 CB PHE A 205 26.428 10.062 43.338 1.00122.76 C
ANISOU 1163 CB PHE A 205 23725 15225 7692 -1997 -3386 -419 C
ATOM 1164 CG PHE A 205 25.050 10.200 42.715 1.00120.49 C
ANISOU 1164 CG PHE A 205 23302 15071 7409 -2209 -3163 -402 C
ATOM 1165 CD1 PHE A 205 24.493 9.150 42.007 1.00121.04 C
ANISOU 1165 CD1 PHE A 205 23481 15099 7411 -2338 -3119 -383 C
ATOM 1166 CD2 PHE A 205 24.305 11.368 42.856 1.00128.23 C
ANISOU 1166 CD2 PHE A 205 24060 16236 8425 -2272 -2999 -410 C
ATOM 1167 CE1 PHE A 205 23.232 9.265 41.440 1.00123.33 C
ANISOU 1167 CE1 PHE A 205 23603 15581 7677 -2549 -2927 -379 C
ATOM 1168 CE2 PHE A 205 23.044 11.484 42.287 1.00127.32 C
ANISOU 1168 CE2 PHE A 205 23785 16317 8273 -2424 -2798 -392 C
ATOM 1169 CZ PHE A 205 22.510 10.429 41.581 1.00125.93 C
ANISOU 1169 CZ PHE A 205 23663 16150 8035 -2576 -2768 -380 C
ATOM 1170 N PHE A 206 27.083 12.865 42.575 1.00127.11 N
ANISOU 1170 N PHE A 206 23602 16071 8622 -1862 -3294 -507 N
ATOM 1171 CA PHE A 206 26.449 14.107 42.137 1.00126.89 C
ANISOU 1171 CA PHE A 206 23346 16173 8693 -1898 -3102 -519 C
ATOM 1172 C PHE A 206 27.117 14.722 40.911 1.00134.20 C
ANISOU 1172 C PHE A 206 23977 17179 9834 -1778 -3092 -538 C
ATOM 1173 O PHE A 206 26.514 14.760 39.833 1.00144.49 O
ANISOU 1173 O PHE A 206 25109 18583 11206 -1758 -2956 -516 O
ATOM 1174 CB PHE A 206 26.437 15.123 43.281 1.00136.19 C
ANISOU 1174 CB PHE A 206 24616 17325 9804 -1935 -3081 -552 C
ATOM 1175 CG PHE A 206 25.413 14.835 44.351 1.00145.95 C
ANISOU 1175 CG PHE A 206 26085 18544 10824 -2050 -3000 -518 C
ATOM 1176 CD1 PHE A 206 25.680 13.936 45.374 1.00145.11 C
ANISOU 1176 CD1 PHE A 206 26258 18313 10564 -2082 -3141 -505 C
ATOM 1177 CD2 PHE A 206 24.187 15.482 44.341 1.00149.62 C
ANISOU 1177 CD2 PHE A 206 26491 19142 11215 -2099 -2774 -492 C
ATOM 1178 CE1 PHE A 206 24.738 13.680 46.361 1.00145.80 C
ANISOU 1178 CE1 PHE A 206 26561 18391 10443 -2198 -3052 -463 C
ATOM 1179 CE2 PHE A 206 23.241 15.230 45.325 1.00150.59 C
ANISOU 1179 CE2 PHE A 206 26797 19298 11121 -2202 -2690 -452 C
ATOM 1180 CZ PHE A 206 23.520 14.328 46.334 1.00148.96 C
ANISOU 1180 CZ PHE A 206 26868 18949 10780 -2270 -2826 -436 C
ATOM 1181 N ALA A 207 28.345 15.220 41.067 1.00132.39 N
ANISOU 1181 N ALA A 207 23674 16934 9695 -1708 -3230 -579 N
ATOM 1182 CA ALA A 207 29.059 15.846 39.953 1.00130.76 C
ANISOU 1182 CA ALA A 207 23187 16813 9683 -1621 -3212 -589 C
ATOM 1183 C ALA A 207 29.098 14.990 38.692 1.00128.92 C
ANISOU 1183 C ALA A 207 22823 16636 9524 -1504 -3219 -550 C
ATOM 1184 O ALA A 207 28.708 15.493 37.626 1.00127.95 O
ANISOU 1184 O ALA A 207 22503 16598 9514 -1464 -3065 -534 O
ATOM 1185 CB ALA A 207 30.478 16.227 40.402 1.00117.08 C
ANISOU 1185 CB ALA A 207 21392 15101 7992 -1605 -3398 -640 C
ATOM 1186 N PRO A 208 29.532 13.722 38.723 1.00128.35 N
ANISOU 1186 N PRO A 208 22880 16514 9374 -1421 -3382 -535 N
ATOM 1187 CA PRO A 208 29.544 12.945 37.472 1.00131.86 C
ANISOU 1187 CA PRO A 208 23237 16992 9872 -1299 -3380 -506 C
ATOM 1188 C PRO A 208 28.160 12.756 36.880 1.00133.78 C
ANISOU 1188 C PRO A 208 23484 17259 10087 -1407 -3194 -490 C
ATOM 1189 O PRO A 208 27.993 12.869 35.659 1.00132.34 O
ANISOU 1189 O PRO A 208 23097 17177 10009 -1329 -3109 -482 O
ATOM 1190 CB PRO A 208 30.174 11.609 37.894 1.00132.91 C
ANISOU 1190 CB PRO A 208 23629 17015 9855 -1185 -3582 -493 C
ATOM 1191 CG PRO A 208 30.890 11.903 39.174 1.00133.58 C
ANISOU 1191 CG PRO A 208 23807 17086 9861 -1188 -3718 -518 C
ATOM 1192 CD PRO A 208 30.042 12.924 39.852 1.00131.57 C
ANISOU 1192 CD PRO A 208 23553 16823 9616 -1398 -3568 -540 C
ATOM 1193 N CYS A 209 27.156 12.472 37.716 1.00134.39 N
ANISOU 1193 N CYS A 209 23771 17284 10007 -1587 -3127 -486 N
ATOM 1194 CA CYS A 209 25.790 12.354 37.217 1.00134.02 C
ANISOU 1194 CA CYS A 209 23676 17345 9901 -1722 -2945 -476 C
ATOM 1195 C CYS A 209 25.276 13.687 36.692 1.00125.23 C
ANISOU 1195 C CYS A 209 22280 16416 8887 -1678 -2751 -477 C
ATOM 1196 O CYS A 209 24.560 13.721 35.685 1.00124.24 O
ANISOU 1196 O CYS A 209 21975 16452 8778 -1661 -2622 -474 O
ATOM 1197 CB CYS A 209 24.867 11.815 38.316 1.00146.06 C
ANISOU 1197 CB CYS A 209 25466 18817 11214 -1943 -2907 -463 C
ATOM 1198 SG CYS A 209 23.862 13.062 39.153 1.00159.61 S
ANISOU 1198 SG CYS A 209 27103 20684 12856 -2036 -2711 -454 S
ATOM 1199 N LEU A 210 25.638 14.791 37.348 1.00119.95 N
ANISOU 1199 N LEU A 210 21594 15721 8260 -1647 -2727 -486 N
ATOM 1200 CA LEU A 210 25.216 16.104 36.875 1.00119.33 C
ANISOU 1200 CA LEU A 210 21329 15765 8246 -1571 -2530 -482 C
ATOM 1201 C LEU A 210 25.723 16.361 35.461 1.00124.33 C
ANISOU 1201 C LEU A 210 21716 16470 9054 -1412 -2498 -473 C
ATOM 1202 O LEU A 210 24.962 16.786 34.583 1.00111.16 O
ANISOU 1202 O LEU A 210 19881 14962 7391 -1330 -2320 -456 O
ATOM 1203 CB LEU A 210 25.703 17.187 37.844 1.00123.82 C
ANISOU 1203 CB LEU A 210 22001 16227 8817 -1584 -2533 -505 C
ATOM 1204 CG LEU A 210 25.333 18.654 37.587 1.00122.83 C
ANISOU 1204 CG LEU A 210 21810 16147 8713 -1500 -2321 -501 C
ATOM 1205 CD1 LEU A 210 26.353 19.330 36.682 1.00124.33 C
ANISOU 1205 CD1 LEU A 210 21844 16298 9097 -1412 -2322 -507 C
ATOM 1206 CD2 LEU A 210 23.928 18.790 37.012 1.00121.92 C
ANISOU 1206 CD2 LEU A 210 21590 16247 8489 -1425 -2099 -463 C
ATOM 1207 N ILE A 211 27.012 16.104 35.221 1.00123.15 N
ANISOU 1207 N ILE A 211 21528 16236 9027 -1344 -2666 -481 N
ATOM 1208 CA ILE A 211 27.581 16.330 33.893 1.00119.72 C
ANISOU 1208 CA ILE A 211 20856 15881 8753 -1185 -2637 -464 C
ATOM 1209 C ILE A 211 26.869 15.464 32.863 1.00124.79 C
ANISOU 1209 C ILE A 211 21420 16630 9366 -1126 -2595 -453 C
ATOM 1210 O ILE A 211 26.389 15.955 31.834 1.00129.17 O
ANISOU 1210 O ILE A 211 21784 17324 9972 -1021 -2437 -437 O
ATOM 1211 CB ILE A 211 29.095 16.056 33.892 1.00114.13 C
ANISOU 1211 CB ILE A 211 20101 15124 8139 -1118 -2841 -469 C
ATOM 1212 CG1 ILE A 211 29.832 16.998 34.842 1.00121.84 C
ANISOU 1212 CG1 ILE A 211 21118 16041 9136 -1219 -2885 -498 C
ATOM 1213 CG2 ILE A 211 29.645 16.194 32.495 1.00112.93 C
ANISOU 1213 CG2 ILE A 211 19697 15080 8134 -947 -2804 -438 C
ATOM 1214 CD1 ILE A 211 31.342 16.801 34.851 1.00123.28 C
ANISOU 1214 CD1 ILE A 211 21188 16270 9383 -1167 -3085 -508 C
ATOM 1215 N MET A 212 26.789 14.155 33.129 1.00139.86 N
ANISOU 1215 N MET A 212 23505 18466 11170 -1196 -2734 -465 N
ATOM 1216 CA MET A 212 26.212 13.233 32.155 1.00141.62 C
ANISOU 1216 CA MET A 212 23702 18760 11347 -1181 -2719 -473 C
ATOM 1217 C MET A 212 24.751 13.558 31.870 1.00146.11 C
ANISOU 1217 C MET A 212 24163 19528 11822 -1282 -2517 -481 C
ATOM 1218 O MET A 212 24.265 13.320 30.759 1.00153.45 O
ANISOU 1218 O MET A 212 24939 20612 12752 -1225 -2449 -493 O
ATOM 1219 CB MET A 212 26.372 11.785 32.634 1.00142.98 C
ANISOU 1219 CB MET A 212 24182 18760 11382 -1270 -2892 -486 C
ATOM 1220 CG MET A 212 25.474 11.360 33.791 1.00145.51 C
ANISOU 1220 CG MET A 212 24756 19016 11517 -1528 -2869 -493 C
ATOM 1221 SD MET A 212 26.103 9.857 34.577 1.00149.07 S
ANISOU 1221 SD MET A 212 25652 19177 11809 -1566 -3086 -491 S
ATOM 1222 CE MET A 212 24.694 9.332 35.553 1.00152.59 C
ANISOU 1222 CE MET A 212 26353 19598 12025 -1930 -2984 -491 C
ATOM 1223 N ILE A 213 24.039 14.113 32.848 1.00143.26 N
ANISOU 1223 N ILE A 213 23867 19206 11360 -1408 -2419 -475 N
ATOM 1224 CA ILE A 213 22.710 14.638 32.569 1.00136.50 C
ANISOU 1224 CA ILE A 213 22852 18618 10394 -1434 -2207 -472 C
ATOM 1225 C ILE A 213 22.813 15.890 31.705 1.00131.76 C
ANISOU 1225 C ILE A 213 22017 18139 9907 -1185 -2051 -449 C
ATOM 1226 O ILE A 213 22.025 16.083 30.771 1.00110.25 O
ANISOU 1226 O ILE A 213 19086 15668 7134 -1087 -1909 -448 O
ATOM 1227 CB ILE A 213 21.954 14.904 33.887 1.00129.57 C
ANISOU 1227 CB ILE A 213 22118 17766 9348 -1593 -2139 -461 C
ATOM 1228 CG1 ILE A 213 21.536 13.587 34.551 1.00128.33 C
ANISOU 1228 CG1 ILE A 213 22182 17545 9033 -1866 -2239 -475 C
ATOM 1229 CG2 ILE A 213 20.729 15.774 33.648 1.00127.15 C
ANISOU 1229 CG2 ILE A 213 21615 17782 8915 -1519 -1901 -444 C
ATOM 1230 CD1 ILE A 213 20.236 12.998 34.022 1.00129.10 C
ANISOU 1230 CD1 ILE A 213 22159 17931 8963 -2042 -2130 -493 C
ATOM 1231 N LEU A 214 23.811 16.737 31.975 1.00126.26 N
ANISOU 1231 N LEU A 214 21357 17269 9346 -1087 -2074 -431 N
ATOM 1232 CA LEU A 214 23.858 18.053 31.345 1.00120.36 C
ANISOU 1232 CA LEU A 214 20475 16584 8673 -887 -1891 -401 C
ATOM 1233 C LEU A 214 24.231 17.964 29.874 1.00116.16 C
ANISOU 1233 C LEU A 214 19727 16140 8268 -705 -1869 -386 C
ATOM 1234 O LEU A 214 23.844 18.833 29.085 1.00113.15 O
ANISOU 1234 O LEU A 214 19211 15892 7888 -514 -1675 -355 O
ATOM 1235 CB LEU A 214 24.844 18.957 32.085 1.00122.52 C
ANISOU 1235 CB LEU A 214 20883 16631 9037 -908 -1924 -398 C
ATOM 1236 CG LEU A 214 24.397 20.403 32.307 1.00124.31 C
ANISOU 1236 CG LEU A 214 21182 16851 9199 -811 -1701 -377 C
ATOM 1237 CD1 LEU A 214 23.186 20.441 33.229 1.00123.70 C
ANISOU 1237 CD1 LEU A 214 21225 16880 8897 -861 -1612 -381 C
ATOM 1238 CD2 LEU A 214 25.532 21.256 32.865 1.00126.67 C
ANISOU 1238 CD2 LEU A 214 21624 16905 9601 -885 -1748 -392 C
ATOM 1239 N VAL A 215 24.989 16.942 29.486 1.00116.66 N
ANISOU 1239 N VAL A 215 19779 16130 8417 -725 -2056 -401 N
ATOM 1240 CA VAL A 215 25.355 16.833 28.082 1.00121.03 C
ANISOU 1240 CA VAL A 215 20134 16775 9078 -530 -2037 -384 C
ATOM 1241 C VAL A 215 24.269 16.104 27.300 1.00122.70 C
ANISOU 1241 C VAL A 215 20245 17207 9169 -519 -1990 -416 C
ATOM 1242 O VAL A 215 24.031 16.409 26.127 1.00119.51 O
ANISOU 1242 O VAL A 215 19641 16975 8791 -325 -1876 -403 O
ATOM 1243 CB VAL A 215 26.732 16.162 27.928 1.00122.13 C
ANISOU 1243 CB VAL A 215 20293 16769 9341 -495 -2247 -380 C
ATOM 1244 CG1 VAL A 215 27.803 17.010 28.583 1.00126.73 C
ANISOU 1244 CG1 VAL A 215 20903 17220 10029 -524 -2280 -358 C
ATOM 1245 CG2 VAL A 215 26.724 14.775 28.522 1.00116.62 C
ANISOU 1245 CG2 VAL A 215 19801 15971 8538 -633 -2444 -420 C
ATOM 1246 N TYR A 216 23.575 15.153 27.935 1.00124.70 N
ANISOU 1246 N TYR A 216 20637 17473 9271 -745 -2068 -460 N
ATOM 1247 CA TYR A 216 22.527 14.418 27.232 1.00124.29 C
ANISOU 1247 CA TYR A 216 20491 17654 9080 -812 -2032 -507 C
ATOM 1248 C TYR A 216 21.301 15.284 26.963 1.00127.69 C
ANISOU 1248 C TYR A 216 20709 18425 9381 -736 -1803 -499 C
ATOM 1249 O TYR A 216 20.580 15.037 25.990 1.00128.64 O
ANISOU 1249 O TYR A 216 20637 18825 9416 -682 -1738 -533 O
ATOM 1250 CB TYR A 216 22.143 13.162 28.015 1.00127.23 C
ANISOU 1250 CB TYR A 216 21107 17930 9305 -1127 -2166 -553 C
ATOM 1251 CG TYR A 216 22.658 11.890 27.381 1.00134.43 C
ANISOU 1251 CG TYR A 216 22156 18697 10225 -1150 -2338 -594 C
ATOM 1252 CD1 TYR A 216 24.000 11.561 27.442 1.00140.59 C
ANISOU 1252 CD1 TYR A 216 23082 19207 11129 -1009 -2501 -569 C
ATOM 1253 CD2 TYR A 216 21.806 11.026 26.712 1.00133.31 C
ANISOU 1253 CD2 TYR A 216 22005 18708 9937 -1303 -2336 -662 C
ATOM 1254 CE1 TYR A 216 24.487 10.407 26.861 1.00138.70 C
ANISOU 1254 CE1 TYR A 216 23009 18830 10861 -967 -2650 -599 C
ATOM 1255 CE2 TYR A 216 22.284 9.868 26.122 1.00131.99 C
ANISOU 1255 CE2 TYR A 216 22032 18366 9751 -1310 -2489 -705 C
ATOM 1256 CZ TYR A 216 23.627 9.562 26.202 1.00130.69 C
ANISOU 1256 CZ TYR A 216 22044 17909 9703 -1115 -2642 -669 C
ATOM 1257 OH TYR A 216 24.116 8.412 25.624 1.00125.04 O
ANISOU 1257 OH TYR A 216 21562 17014 8934 -1063 -2788 -705 O
ATOM 1258 N VAL A 217 21.042 16.295 27.799 1.00136.67 N
ANISOU 1258 N VAL A 217 21885 19566 10477 -707 -1678 -459 N
ATOM 1259 CA VAL A 217 19.950 17.216 27.492 1.00141.44 C
ANISOU 1259 CA VAL A 217 22303 20508 10929 -536 -1443 -438 C
ATOM 1260 C VAL A 217 20.305 18.074 26.284 1.00147.47 C
ANISOU 1260 C VAL A 217 22904 21330 11798 -191 -1315 -399 C
ATOM 1261 O VAL A 217 19.419 18.491 25.526 1.00157.32 O
ANISOU 1261 O VAL A 217 23946 22921 12910 9 -1148 -393 O
ATOM 1262 CB VAL A 217 19.593 18.082 28.716 1.00141.53 C
ANISOU 1262 CB VAL A 217 22457 20482 10836 -551 -1336 -402 C
ATOM 1263 CG1 VAL A 217 19.161 17.206 29.881 1.00142.14 C
ANISOU 1263 CG1 VAL A 217 22684 20535 10786 -884 -1445 -431 C
ATOM 1264 CG2 VAL A 217 20.762 18.970 29.110 1.00140.12 C
ANISOU 1264 CG2 VAL A 217 22456 19945 10837 -455 -1349 -364 C
ATOM 1265 N ARG A 218 21.595 18.357 26.087 1.00141.57 N
ANISOU 1265 N ARG A 218 22237 20282 11273 -112 -1385 -367 N
ATOM 1266 CA ARG A 218 22.031 19.001 24.854 1.00134.74 C
ANISOU 1266 CA ARG A 218 21225 19454 10516 182 -1275 -324 C
ATOM 1267 C ARG A 218 21.915 18.045 23.675 1.00133.10 C
ANISOU 1267 C ARG A 218 20835 19424 10314 238 -1355 -365 C
ATOM 1268 O ARG A 218 21.596 18.466 22.557 1.00136.11 O
ANISOU 1268 O ARG A 218 21029 20018 10667 501 -1217 -345 O
ATOM 1269 CB ARG A 218 23.467 19.502 25.002 1.00130.13 C
ANISOU 1269 CB ARG A 218 20753 18540 10150 193 -1332 -280 C
ATOM 1270 N ILE A 219 22.166 16.755 23.907 1.00129.39 N
ANISOU 1270 N ILE A 219 20451 18854 9857 8 -1573 -423 N
ATOM 1271 CA ILE A 219 22.052 15.765 22.839 1.00121.29 C
ANISOU 1271 CA ILE A 219 19319 17955 8809 35 -1663 -477 C
ATOM 1272 C ILE A 219 20.615 15.690 22.343 1.00128.60 C
ANISOU 1272 C ILE A 219 20050 19297 9515 31 -1543 -530 C
ATOM 1273 O ILE A 219 20.352 15.725 21.135 1.00141.87 O
ANISOU 1273 O ILE A 219 21529 21210 11167 239 -1480 -546 O
ATOM 1274 CB ILE A 219 22.547 14.389 23.322 1.00111.75 C
ANISOU 1274 CB ILE A 219 18338 16514 7608 -215 -1908 -530 C
ATOM 1275 CG1 ILE A 219 24.048 14.422 23.615 1.00108.94 C
ANISOU 1275 CG1 ILE A 219 18109 15839 7443 -136 -2037 -478 C
ATOM 1276 CG2 ILE A 219 22.215 13.315 22.297 1.00112.46 C
ANISOU 1276 CG2 ILE A 219 18386 16727 7615 -231 -1991 -605 C
ATOM 1277 CD1 ILE A 219 24.620 13.077 24.029 1.00108.31 C
ANISOU 1277 CD1 ILE A 219 18283 15533 7338 -284 -2272 -517 C
ATOM 1278 N TYR A 220 19.665 15.584 23.278 1.00120.27 N
ANISOU 1278 N TYR A 220 19034 18381 8283 -203 -1509 -557 N
ATOM 1279 CA TYR A 220 18.251 15.492 22.929 1.00120.12 C
ANISOU 1279 CA TYR A 220 18789 18840 8013 -247 -1399 -610 C
ATOM 1280 C TYR A 220 17.801 16.694 22.112 1.00122.37 C
ANISOU 1280 C TYR A 220 18825 19437 8235 163 -1170 -559 C
ATOM 1281 O TYR A 220 17.037 16.552 21.149 1.00121.93 O
ANISOU 1281 O TYR A 220 18515 19782 8029 274 -1109 -607 O
ATOM 1282 CB TYR A 220 17.423 15.361 24.214 1.00118.84 C
ANISOU 1282 CB TYR A 220 18706 18775 7672 -542 -1376 -619 C
ATOM 1283 CG TYR A 220 15.929 15.564 24.057 1.00123.72 C
ANISOU 1283 CG TYR A 220 19042 19971 7995 -552 -1220 -649 C
ATOM 1284 CD1 TYR A 220 15.369 16.838 24.087 1.00129.23 C
ANISOU 1284 CD1 TYR A 220 19587 20940 8573 -216 -995 -582 C
ATOM 1285 CD2 TYR A 220 15.076 14.480 23.908 1.00128.63 C
ANISOU 1285 CD2 TYR A 220 19565 20882 8427 -901 -1292 -746 C
ATOM 1286 CE1 TYR A 220 14.005 17.023 23.949 1.00134.78 C
ANISOU 1286 CE1 TYR A 220 20000 22242 8966 -175 -852 -604 C
ATOM 1287 CE2 TYR A 220 13.711 14.656 23.774 1.00135.52 C
ANISOU 1287 CE2 TYR A 220 20123 22365 9002 -931 -1154 -778 C
ATOM 1288 CZ TYR A 220 13.183 15.928 23.795 1.00134.52 C
ANISOU 1288 CZ TYR A 220 19805 22555 8753 -543 -937 -703 C
ATOM 1289 OH TYR A 220 11.824 16.098 23.661 1.00129.17 O
ANISOU 1289 OH TYR A 220 18784 22555 7741 -526 -799 -730 O
ATOM 1290 N GLN A 221 18.266 17.888 22.483 1.00122.41 N
ANISOU 1290 N GLN A 221 18925 19257 8327 393 -1038 -466 N
ATOM 1291 CA GLN A 221 17.849 19.095 21.778 1.00124.25 C
ANISOU 1291 CA GLN A 221 19010 19731 8469 812 -794 -404 C
ATOM 1292 C GLN A 221 18.372 19.108 20.348 1.00126.89 C
ANISOU 1292 C GLN A 221 19208 20086 8918 1079 -782 -394 C
ATOM 1293 O GLN A 221 17.678 19.567 19.433 1.00134.65 O
ANISOU 1293 O GLN A 221 19978 21438 9746 1389 -623 -386 O
ATOM 1294 CB GLN A 221 18.321 20.333 22.541 1.00121.01 C
ANISOU 1294 CB GLN A 221 18828 19030 8120 953 -658 -312 C
ATOM 1295 N ILE A 222 19.590 18.609 20.135 1.00126.20 N
ANISOU 1295 N ILE A 222 19235 19638 9079 994 -944 -390 N
ATOM 1296 CA ILE A 222 20.142 18.543 18.785 1.00123.85 C
ANISOU 1296 CA ILE A 222 18811 19361 8886 1247 -942 -376 C
ATOM 1297 C ILE A 222 19.332 17.578 17.930 1.00125.16 C
ANISOU 1297 C ILE A 222 18769 19892 8894 1213 -1018 -480 C
ATOM 1298 O ILE A 222 18.920 17.907 16.812 1.00120.33 O
ANISOU 1298 O ILE A 222 17948 19582 8191 1519 -899 -479 O
ATOM 1299 CB ILE A 222 21.628 18.145 18.828 1.00129.69 C
ANISOU 1299 CB ILE A 222 19702 19684 9891 1162 -1111 -347 C
ATOM 1300 CG1 ILE A 222 22.450 19.205 19.562 1.00132.85 C
ANISOU 1300 CG1 ILE A 222 20272 19774 10431 1179 -1025 -254 C
ATOM 1301 CG2 ILE A 222 22.157 17.957 17.424 1.00107.39 C
ANISOU 1301 CG2 ILE A 222 16736 16916 7151 1425 -1117 -332 C
ATOM 1302 CD1 ILE A 222 23.928 18.880 19.641 1.00134.56 C
ANISOU 1302 CD1 ILE A 222 20579 19669 10879 1095 -1187 -224 C
ATOM 1303 N ALA A 223 19.091 16.369 18.444 1.00124.25 N
ANISOU 1303 N ALA A 223 18733 19752 8726 830 -1213 -577 N
ATOM 1304 CA ALA A 223 18.311 15.386 17.699 1.00125.97 C
ANISOU 1304 CA ALA A 223 18798 20294 8772 709 -1297 -697 C
ATOM 1305 C ALA A 223 16.920 15.919 17.372 1.00123.14 C
ANISOU 1305 C ALA A 223 18139 20513 8136 836 -1118 -726 C
ATOM 1306 O ALA A 223 16.424 15.746 16.253 1.00122.49 O
ANISOU 1306 O ALA A 223 17825 20788 7928 996 -1093 -786 O
ATOM 1307 CB ALA A 223 18.220 14.080 18.490 1.00131.82 C
ANISOU 1307 CB ALA A 223 19751 20868 9467 225 -1506 -788 C
ATOM 1308 N LYS A 224 16.278 16.581 18.340 1.00127.91 N
ANISOU 1308 N LYS A 224 18738 21246 8616 796 -990 -682 N
ATOM 1309 CA LYS A 224 14.945 17.133 18.109 1.00134.60 C
ANISOU 1309 CA LYS A 224 19286 22700 9156 968 -809 -696 C
ATOM 1310 C LYS A 224 14.965 18.196 17.021 1.00143.40 C
ANISOU 1310 C LYS A 224 20243 24001 10241 1533 -611 -624 C
ATOM 1311 O LYS A 224 14.011 18.323 16.246 1.00138.46 O
ANISOU 1311 O LYS A 224 19313 23934 9362 1741 -515 -668 O
ATOM 1312 CB LYS A 224 14.382 17.712 19.411 1.00131.49 C
ANISOU 1312 CB LYS A 224 18963 22365 8634 881 -700 -643 C
ATOM 1313 CG LYS A 224 13.829 16.668 20.370 1.00135.60 C
ANISOU 1313 CG LYS A 224 19526 22952 9043 339 -841 -724 C
ATOM 1314 CD LYS A 224 12.502 16.124 19.872 1.00148.11 C
ANISOU 1314 CD LYS A 224 20755 25216 10304 191 -824 -832 C
ATOM 1315 CE LYS A 224 12.070 14.902 20.662 1.00154.29 C
ANISOU 1315 CE LYS A 224 21621 26008 10992 -431 -979 -923 C
ATOM 1316 NZ LYS A 224 10.591 14.751 20.695 1.00159.59 N
ANISOU 1316 NZ LYS A 224 21928 27426 11285 -604 -892 -990 N
ATOM 1317 N ARG A 225 16.047 18.971 16.943 1.00163.29 N
ANISOU 1317 N ARG A 225 22968 26077 12998 1780 -542 -512 N
ATOM 1318 CA ARG A 225 16.118 20.021 15.933 1.00166.89 C
ANISOU 1318 CA ARG A 225 23338 26652 13422 2312 -328 -426 C
ATOM 1319 C ARG A 225 16.232 19.437 14.531 1.00161.95 C
ANISOU 1319 C ARG A 225 22513 26213 12809 2457 -400 -486 C
ATOM 1320 O ARG A 225 15.598 19.934 13.592 1.00163.74 O
ANISOU 1320 O ARG A 225 22519 26857 12839 2848 -245 -477 O
ATOM 1321 CB ARG A 225 17.295 20.950 16.219 1.00172.58 C
ANISOU 1321 CB ARG A 225 24352 26831 14390 2455 -236 -296 C
ATOM 1322 CG ARG A 225 17.509 21.980 15.126 1.00176.18 C
ANISOU 1322 CG ARG A 225 24783 27327 14830 2970 -8 -196 C
ATOM 1323 CD ARG A 225 18.732 22.824 15.391 1.00174.26 C
ANISOU 1323 CD ARG A 225 24840 26538 14831 3016 76 -76 C
ATOM 1324 NE ARG A 225 18.470 24.222 15.069 1.00172.85 N
ANISOU 1324 NE ARG A 225 24780 26389 14507 3463 389 38 N
ATOM 1325 CZ ARG A 225 19.390 25.179 15.072 1.00170.55 C
ANISOU 1325 CZ ARG A 225 24765 25674 14364 3565 535 152 C
ATOM 1326 NH1 ARG A 225 20.648 24.896 15.376 1.00169.13 N
ANISOU 1326 NH1 ARG A 225 24704 25071 14487 3251 386 164 N
ATOM 1327 NH2 ARG A 225 19.048 26.424 14.768 1.00172.20 N
ANISOU 1327 NH2 ARG A 225 25140 25898 14392 3983 838 254 N
ATOM 1328 N ARG A 226 17.035 18.383 14.369 1.00141.64 N
ANISOU 1328 N ARG A 226 20033 23344 10439 2181 -631 -546 N
ATOM 1329 CA ARG A 226 17.235 17.796 13.047 1.00129.88 C
ANISOU 1329 CA ARG A 226 18403 21983 8963 2328 -711 -605 C
ATOM 1330 C ARG A 226 15.929 17.263 12.475 1.00134.52 C
ANISOU 1330 C ARG A 226 18688 23185 9237 2287 -730 -742 C
ATOM 1331 O ARG A 226 15.532 17.623 11.360 1.00141.30 O
ANISOU 1331 O ARG A 226 19319 24413 9955 2665 -622 -747 O
ATOM 1332 CB ARG A 226 18.279 16.680 13.118 1.00121.29 C
ANISOU 1332 CB ARG A 226 17517 20467 8101 2037 -965 -650 C
ATOM 1333 CG ARG A 226 19.713 17.125 12.850 1.00122.56 C
ANISOU 1333 CG ARG A 226 17830 20191 8546 2252 -949 -526 C
ATOM 1334 CD ARG A 226 20.352 17.770 14.072 1.00124.22 C
ANISOU 1334 CD ARG A 226 18259 20024 8915 2117 -909 -429 C
ATOM 1335 NE ARG A 226 21.801 17.934 13.941 1.00129.86 N
ANISOU 1335 NE ARG A 226 19103 20344 9892 2194 -951 -336 N
ATOM 1336 CZ ARG A 226 22.451 19.073 14.163 1.00135.95 C
ANISOU 1336 CZ ARG A 226 19959 20907 10789 2335 -788 -210 C
ATOM 1337 NH1 ARG A 226 23.770 19.127 14.024 1.00136.57 N
ANISOU 1337 NH1 ARG A 226 20109 20695 11086 2355 -842 -136 N
ATOM 1338 NH2 ARG A 226 21.786 20.156 14.541 1.00138.96 N
ANISOU 1338 NH2 ARG A 226 20365 21380 11053 2450 -570 -159 N
ATOM 1339 N THR A 227 15.245 16.402 13.231 1.00134.48 N
ANISOU 1339 N THR A 227 18675 23320 9103 1815 -865 -854 N
ATOM 1340 CA THR A 227 14.032 15.744 12.765 1.00144.53 C
ANISOU 1340 CA THR A 227 19657 25191 10067 1646 -914 -1006 C
ATOM 1341 C THR A 227 12.822 16.665 12.722 1.00158.40 C
ANISOU 1341 C THR A 227 21087 27591 11507 1933 -692 -982 C
ATOM 1342 O THR A 227 11.788 16.262 12.181 1.00164.24 O
ANISOU 1342 O THR A 227 21505 28943 11954 1866 -711 -1105 O
ATOM 1343 CB THR A 227 13.704 14.553 13.665 1.00145.08 C
ANISOU 1343 CB THR A 227 19857 25182 10083 999 -1107 -1122 C
ATOM 1344 OG1 THR A 227 12.523 13.902 13.183 1.00150.61 O
ANISOU 1344 OG1 THR A 227 20267 26491 10468 767 -1153 -1282 O
ATOM 1345 CG2 THR A 227 13.461 15.022 15.094 1.00142.19 C
ANISOU 1345 CG2 THR A 227 19596 24722 9706 828 -1026 -1042 C
ATOM 1346 N ALA A1001 12.922 17.875 13.271 1.00117.37 N
ANISOU 1346 N ALA A1001 16263 14398 13936 -930 690 -2235 N
ATOM 1347 CA ALA A1001 11.777 18.761 13.459 1.00126.93 C
ANISOU 1347 CA ALA A1001 17626 15418 15183 -821 946 -2470 C
ATOM 1348 C ALA A1001 10.940 18.940 12.197 1.00119.54 C
ANISOU 1348 C ALA A1001 16619 14083 14718 -732 1081 -2359 C
ATOM 1349 O ALA A1001 9.789 18.491 12.147 1.00115.48 O
ANISOU 1349 O ALA A1001 16053 13533 14290 -553 1295 -2192 O
ATOM 1350 CB ALA A1001 12.248 20.129 13.966 1.00138.76 C
ANISOU 1350 CB ALA A1001 19319 16835 16569 -952 864 -2951 C
ATOM 1351 N ASP A1002 11.516 19.585 11.176 1.00112.98 N
ANISOU 1351 N ASP A1002 15758 12989 14180 -872 947 -2413 N
ATOM 1352 CA ASP A1002 10.768 19.943 9.972 1.00101.41 C
ANISOU 1352 CA ASP A1002 14230 11178 13124 -816 1046 -2311 C
ATOM 1353 C ASP A1002 10.147 18.722 9.308 1.00 89.75 C
ANISOU 1353 C ASP A1002 12570 9749 11782 -667 1117 -1973 C
ATOM 1354 O ASP A1002 8.994 18.763 8.869 1.00 90.66 O
ANISOU 1354 O ASP A1002 12658 9673 12117 -527 1286 -1887 O
ATOM 1355 CB ASP A1002 11.672 20.666 8.972 1.00104.11 C
ANISOU 1355 CB ASP A1002 14513 11351 13693 -1033 856 -2315 C
ATOM 1356 CG ASP A1002 12.192 21.987 9.491 1.00121.64 C
ANISOU 1356 CG ASP A1002 16898 13399 15919 -1207 748 -2641 C
ATOM 1357 OD1 ASP A1002 11.442 22.714 10.178 1.00130.34 O
ANISOU 1357 OD1 ASP A1002 18171 14320 17031 -1104 871 -2916 O
ATOM 1358 OD2 ASP A1002 13.363 22.304 9.193 1.00129.10 O
ANISOU 1358 OD2 ASP A1002 17779 14387 16888 -1445 527 -2637 O
ATOM 1359 N LEU A1003 10.910 17.631 9.196 1.00 79.71 N
ANISOU 1359 N LEU A1003 11152 8705 10429 -692 960 -1795 N
ATOM 1360 CA LEU A1003 10.357 16.416 8.602 1.00 76.81 C
ANISOU 1360 CA LEU A1003 10604 8336 10245 -548 977 -1526 C
ATOM 1361 C LEU A1003 9.157 15.924 9.399 1.00 76.88 C
ANISOU 1361 C LEU A1003 10639 8367 10204 -390 1172 -1392 C
ATOM 1362 O LEU A1003 8.156 15.473 8.831 1.00 70.87 O
ANISOU 1362 O LEU A1003 9775 7456 9698 -270 1270 -1227 O
ATOM 1363 CB LEU A1003 11.412 15.311 8.519 1.00 80.40 C
ANISOU 1363 CB LEU A1003 10889 9002 10659 -570 751 -1405 C
ATOM 1364 CG LEU A1003 10.873 14.105 7.742 1.00 85.81 C
ANISOU 1364 CG LEU A1003 11372 9603 11629 -417 719 -1201 C
ATOM 1365 CD1 LEU A1003 10.503 14.552 6.333 1.00 89.59 C
ANISOU 1365 CD1 LEU A1003 11779 9915 12347 -410 757 -1256 C
ATOM 1366 CD2 LEU A1003 11.852 12.930 7.720 1.00 86.81 C
ANISOU 1366 CD2 LEU A1003 11308 9882 11792 -386 478 -1114 C
ATOM 1367 N GLU A1004 9.246 16.007 10.727 1.00 81.06 N
ANISOU 1367 N GLU A1004 11284 9132 10384 -400 1227 -1451 N
ATOM 1368 CA GLU A1004 8.148 15.553 11.573 1.00 79.96 C
ANISOU 1368 CA GLU A1004 11132 9123 10125 -268 1437 -1284 C
ATOM 1369 C GLU A1004 6.931 16.462 11.446 1.00 81.13 C
ANISOU 1369 C GLU A1004 11350 9074 10401 -154 1708 -1439 C
ATOM 1370 O GLU A1004 5.792 15.995 11.560 1.00 69.73 O
ANISOU 1370 O GLU A1004 9801 7636 9056 -24 1894 -1231 O
ATOM 1371 CB GLU A1004 8.603 15.456 13.026 1.00 91.75 C
ANISOU 1371 CB GLU A1004 12713 11022 11126 -314 1427 -1309 C
ATOM 1372 CG GLU A1004 9.313 14.157 13.355 1.00109.43 C
ANISOU 1372 CG GLU A1004 14808 13479 13293 -359 1203 -961 C
ATOM 1373 CD GLU A1004 9.805 14.112 14.787 1.00132.46 C
ANISOU 1373 CD GLU A1004 17801 16853 15674 -425 1163 -947 C
ATOM 1374 OE1 GLU A1004 9.920 15.184 15.418 1.00141.07 O
ANISOU 1374 OE1 GLU A1004 19079 18090 16431 -464 1249 -1325 O
ATOM 1375 OE2 GLU A1004 10.076 13.001 15.284 1.00140.10 O
ANISOU 1375 OE2 GLU A1004 18632 18034 16566 -438 1020 -559 O
ATOM 1376 N ASP A1005 7.147 17.767 11.239 1.00100.12 N
ANISOU 1376 N ASP A1005 13906 11289 12846 -202 1718 -1788 N
ATOM 1377 CA ASP A1005 6.061 18.646 10.811 1.00105.75 C
ANISOU 1377 CA ASP A1005 14645 11704 13833 -81 1913 -1916 C
ATOM 1378 C ASP A1005 5.325 18.041 9.618 1.00101.97 C
ANISOU 1378 C ASP A1005 13980 11015 13749 -13 1921 -1610 C
ATOM 1379 O ASP A1005 4.106 17.834 9.657 1.00102.06 O
ANISOU 1379 O ASP A1005 13897 10984 13898 141 2120 -1480 O
ATOM 1380 CB ASP A1005 6.585 20.040 10.426 1.00119.12 C
ANISOU 1380 CB ASP A1005 16483 13103 15673 -186 1814 -2246 C
ATOM 1381 CG ASP A1005 7.142 20.822 11.605 1.00135.60 C
ANISOU 1381 CG ASP A1005 18764 15329 17430 -237 1797 -2652 C
ATOM 1382 OD1 ASP A1005 7.455 20.206 12.644 1.00143.85 O
ANISOU 1382 OD1 ASP A1005 19829 16781 18045 -240 1807 -2648 O
ATOM 1383 OD2 ASP A1005 7.274 22.061 11.488 1.00141.32 O
ANISOU 1383 OD2 ASP A1005 19609 15747 18339 -284 1747 -2971 O
ATOM 1384 N ASN A1006 6.078 17.748 8.550 1.00 92.95 N
ANISOU 1384 N ASN A1006 12761 9784 12773 -127 1698 -1508 N
ATOM 1385 CA ASN A1006 5.507 17.199 7.321 1.00 76.14 C
ANISOU 1385 CA ASN A1006 10454 7500 10978 -75 1657 -1284 C
ATOM 1386 C ASN A1006 4.737 15.910 7.589 1.00 76.15 C
ANISOU 1386 C ASN A1006 10299 7597 11038 40 1713 -1015 C
ATOM 1387 O ASN A1006 3.565 15.781 7.216 1.00 84.01 O
ANISOU 1387 O ASN A1006 11186 8453 12279 150 1831 -881 O
ATOM 1388 CB ASN A1006 6.618 16.958 6.291 1.00 72.53 C
ANISOU 1388 CB ASN A1006 9914 7077 10568 -207 1410 -1266 C
ATOM 1389 CG ASN A1006 7.590 18.126 6.190 1.00 82.88 C
ANISOU 1389 CG ASN A1006 11346 8349 11796 -380 1321 -1462 C
ATOM 1390 OD1 ASN A1006 8.811 17.942 6.189 1.00 80.53 O
ANISOU 1390 OD1 ASN A1006 11025 8229 11343 -512 1153 -1507 O
ATOM 1391 ND2 ASN A1006 7.049 19.337 6.109 1.00 92.91 N
ANISOU 1391 ND2 ASN A1006 12721 9363 13218 -382 1417 -1569 N
ATOM 1392 N TRP A1007 5.386 14.945 8.250 1.00 74.43 N
ANISOU 1392 N TRP A1007 10045 7601 10633 3 1604 -902 N
ATOM 1393 CA TRP A1007 4.742 13.662 8.525 1.00 76.87 C
ANISOU 1393 CA TRP A1007 10182 7960 11065 76 1603 -582 C
ATOM 1394 C TRP A1007 3.437 13.840 9.299 1.00 78.01 C
ANISOU 1394 C TRP A1007 10306 8161 11172 177 1894 -462 C
ATOM 1395 O TRP A1007 2.432 13.185 8.991 1.00 73.95 O
ANISOU 1395 O TRP A1007 9612 7543 10944 246 1942 -211 O
ATOM 1396 CB TRP A1007 5.700 12.751 9.292 1.00 82.33 C
ANISOU 1396 CB TRP A1007 10848 8878 11557 12 1428 -449 C
ATOM 1397 CG TRP A1007 5.279 11.311 9.325 1.00 97.30 C
ANISOU 1397 CG TRP A1007 12529 10729 13712 56 1314 -83 C
ATOM 1398 CD1 TRP A1007 4.639 10.664 10.343 1.00109.84 C
ANISOU 1398 CD1 TRP A1007 14035 12472 15229 67 1411 261 C
ATOM 1399 CD2 TRP A1007 5.476 10.338 8.293 1.00107.87 C
ANISOU 1399 CD2 TRP A1007 13687 11850 15448 88 1060 -24 C
ATOM 1400 NE1 TRP A1007 4.427 9.348 10.008 1.00115.50 N
ANISOU 1400 NE1 TRP A1007 14531 13012 16342 81 1206 573 N
ATOM 1401 CE2 TRP A1007 4.930 9.123 8.753 1.00115.80 C
ANISOU 1401 CE2 TRP A1007 14514 12802 16683 110 982 356 C
ATOM 1402 CE3 TRP A1007 6.060 10.376 7.025 1.00114.07 C
ANISOU 1402 CE3 TRP A1007 14423 12510 16408 100 888 -265 C
ATOM 1403 CZ2 TRP A1007 4.952 7.958 7.989 1.00122.40 C
ANISOU 1403 CZ2 TRP A1007 15143 13383 17982 157 706 447 C
ATOM 1404 CZ3 TRP A1007 6.080 9.220 6.268 1.00119.58 C
ANISOU 1404 CZ3 TRP A1007 14914 13039 17484 168 648 -213 C
ATOM 1405 CH2 TRP A1007 5.533 8.025 6.754 1.00122.44 C
ANISOU 1405 CH2 TRP A1007 15119 13271 18132 202 543 113 C
ATOM 1406 N GLU A1008 3.432 14.716 10.310 1.00 88.12 N
ANISOU 1406 N GLU A1008 11746 9630 12105 193 2087 -661 N
ATOM 1407 CA GLU A1008 2.196 15.033 11.025 1.00 97.15 C
ANISOU 1407 CA GLU A1008 12847 10888 13177 324 2405 -625 C
ATOM 1408 C GLU A1008 1.164 15.646 10.086 1.00 96.33 C
ANISOU 1408 C GLU A1008 12675 10458 13470 435 2519 -683 C
ATOM 1409 O GLU A1008 -0.009 15.255 10.091 1.00 84.20 O
ANISOU 1409 O GLU A1008 10951 8919 12123 533 2681 -450 O
ATOM 1410 CB GLU A1008 2.482 15.988 12.189 1.00111.64 C
ANISOU 1410 CB GLU A1008 14875 12992 14550 346 2568 -966 C
ATOM 1411 CG GLU A1008 1.245 16.360 13.016 1.00125.98 C
ANISOU 1411 CG GLU A1008 16624 15022 16221 520 2934 -1005 C
ATOM 1412 CD GLU A1008 1.404 17.660 13.796 1.00138.55 C
ANISOU 1412 CD GLU A1008 18419 16731 17493 600 3085 -1541 C
ATOM 1413 OE1 GLU A1008 1.653 18.714 13.172 1.00140.23 O
ANISOU 1413 OE1 GLU A1008 18771 16565 17946 607 3005 -1890 O
ATOM 1414 OE2 GLU A1008 1.269 17.628 15.036 1.00146.29 O
ANISOU 1414 OE2 GLU A1008 19406 18192 17987 652 3269 -1612 O
ATOM 1415 N THR A1009 1.587 16.623 9.277 1.00110.38 N
ANISOU 1415 N THR A1009 14578 11969 15392 405 2422 -951 N
ATOM 1416 CA THR A1009 0.673 17.272 8.339 1.00113.56 C
ANISOU 1416 CA THR A1009 14909 12057 16181 500 2487 -967 C
ATOM 1417 C THR A1009 0.046 16.255 7.394 1.00104.97 C
ANISOU 1417 C THR A1009 13591 10867 15425 508 2381 -634 C
ATOM 1418 O THR A1009 -1.147 16.337 7.076 1.00105.48 O
ANISOU 1418 O THR A1009 13504 10809 15763 623 2508 -512 O
ATOM 1419 CB THR A1009 1.408 18.360 7.549 1.00123.39 C
ANISOU 1419 CB THR A1009 16298 13049 17535 411 2330 -1200 C
ATOM 1420 OG1 THR A1009 1.686 19.476 8.406 1.00130.65 O
ANISOU 1420 OG1 THR A1009 17411 13958 18273 433 2433 -1554 O
ATOM 1421 CG2 THR A1009 0.566 18.828 6.365 1.00129.12 C
ANISOU 1421 CG2 THR A1009 16909 13467 18682 475 2314 -1095 C
ATOM 1422 N LEU A1010 0.842 15.286 6.932 1.00 94.51 N
ANISOU 1422 N LEU A1010 12219 9585 14104 396 2129 -516 N
ATOM 1423 CA LEU A1010 0.320 14.173 6.148 1.00 87.69 C
ANISOU 1423 CA LEU A1010 11133 8629 13557 405 1985 -263 C
ATOM 1424 C LEU A1010 -0.767 13.426 6.909 1.00 98.33 C
ANISOU 1424 C LEU A1010 12305 10058 14997 472 2147 31 C
ATOM 1425 O LEU A1010 -1.897 13.284 6.429 1.00 99.44 O
ANISOU 1425 O LEU A1010 12265 10064 15453 539 2201 186 O
ATOM 1426 CB LEU A1010 1.459 13.221 5.780 1.00 81.63 C
ANISOU 1426 CB LEU A1010 10341 7916 12758 310 1694 -259 C
ATOM 1427 CG LEU A1010 2.481 13.758 4.778 1.00 86.88 C
ANISOU 1427 CG LEU A1010 11083 8557 13370 234 1518 -488 C
ATOM 1428 CD1 LEU A1010 3.742 12.911 4.765 1.00 83.34 C
ANISOU 1428 CD1 LEU A1010 10610 8244 12813 170 1286 -536 C
ATOM 1429 CD2 LEU A1010 1.867 13.817 3.391 1.00 94.77 C
ANISOU 1429 CD2 LEU A1010 11947 9408 14651 265 1425 -469 C
ATOM 1430 N ASN A1011 -0.433 12.954 8.114 1.00105.16 N
ANISOU 1430 N ASN A1011 13198 11180 15577 439 2218 146 N
ATOM 1431 CA ASN A1011 -1.392 12.189 8.905 1.00107.76 C
ANISOU 1431 CA ASN A1011 13326 11661 15959 465 2371 513 C
ATOM 1432 C ASN A1011 -2.634 13.010 9.240 1.00100.75 C
ANISOU 1432 C ASN A1011 12367 10835 15078 603 2720 487 C
ATOM 1433 O ASN A1011 -3.757 12.499 9.154 1.00 95.08 O
ANISOU 1433 O ASN A1011 11394 10088 14643 638 2806 786 O
ATOM 1434 CB ASN A1011 -0.730 11.672 10.181 1.00117.18 C
ANISOU 1434 CB ASN A1011 14566 13197 16761 391 2387 669 C
ATOM 1435 CG ASN A1011 -0.055 10.332 9.983 1.00123.66 C
ANISOU 1435 CG ASN A1011 15282 13925 17779 284 2047 933 C
ATOM 1436 OD1 ASN A1011 1.159 10.254 9.786 1.00125.27 O
ANISOU 1436 OD1 ASN A1011 15612 14108 17875 231 1824 754 O
ATOM 1437 ND2 ASN A1011 -0.846 9.264 10.022 1.00126.90 N
ANISOU 1437 ND2 ASN A1011 15432 14256 18529 255 1990 1360 N
ATOM 1438 N ASP A1012 -2.456 14.279 9.625 1.00106.76 N
ANISOU 1438 N ASP A1012 13325 11665 15573 688 2908 119 N
ATOM 1439 CA ASP A1012 -3.598 15.140 9.926 1.00118.66 C
ANISOU 1439 CA ASP A1012 14754 13205 17127 868 3235 12 C
ATOM 1440 C ASP A1012 -4.557 15.221 8.743 1.00120.08 C
ANISOU 1440 C ASP A1012 14751 13045 17828 933 3182 124 C
ATOM 1441 O ASP A1012 -5.752 14.935 8.876 1.00115.79 O
ANISOU 1441 O ASP A1012 13947 12561 17487 1019 3360 366 O
ATOM 1442 CB ASP A1012 -3.123 16.542 10.321 1.00125.94 C
ANISOU 1442 CB ASP A1012 15933 14121 17797 953 3351 -488 C
ATOM 1443 CG ASP A1012 -2.537 16.592 11.719 1.00135.28 C
ANISOU 1443 CG ASP A1012 17247 15742 18411 938 3485 -637 C
ATOM 1444 OD1 ASP A1012 -2.944 15.770 12.565 1.00140.44 O
ANISOU 1444 OD1 ASP A1012 17737 16783 18841 931 3632 -326 O
ATOM 1445 OD2 ASP A1012 -1.676 17.460 11.977 1.00137.21 O
ANISOU 1445 OD2 ASP A1012 17742 15962 18430 919 3427 -1045 O
ATOM 1446 N ASN A1013 -4.040 15.605 7.570 1.00122.45 N
ANISOU 1446 N ASN A1013 15160 13033 18334 880 2931 -24 N
ATOM 1447 CA ASN A1013 -4.884 15.717 6.382 1.00121.59 C
ANISOU 1447 CA ASN A1013 14881 12646 18671 928 2838 87 C
ATOM 1448 C ASN A1013 -5.476 14.372 5.983 1.00114.25 C
ANISOU 1448 C ASN A1013 13686 11708 18016 860 2696 453 C
ATOM 1449 O ASN A1013 -6.569 14.316 5.411 1.00114.64 O
ANISOU 1449 O ASN A1013 13509 11630 18421 924 2707 616 O
ATOM 1450 CB ASN A1013 -4.087 16.304 5.222 1.00128.92 C
ANISOU 1450 CB ASN A1013 15962 13345 19675 849 2578 -90 C
ATOM 1451 CG ASN A1013 -3.758 17.761 5.430 1.00146.32 C
ANISOU 1451 CG ASN A1013 18372 15433 21790 909 2682 -398 C
ATOM 1452 OD1 ASN A1013 -4.550 18.641 5.093 1.00157.21 O
ANISOU 1452 OD1 ASN A1013 19690 16605 23438 1038 2770 -435 O
ATOM 1453 ND2 ASN A1013 -2.583 18.029 5.983 1.00150.89 N
ANISOU 1453 ND2 ASN A1013 19181 16113 22038 814 2642 -620 N
ATOM 1454 N LEU A1014 -4.770 13.278 6.276 1.00113.38 N
ANISOU 1454 N LEU A1014 13582 11704 17795 731 2530 586 N
ATOM 1455 CA LEU A1014 -5.297 11.948 5.992 1.00115.80 C
ANISOU 1455 CA LEU A1014 13627 11940 18432 656 2354 925 C
ATOM 1456 C LEU A1014 -6.558 11.678 6.807 1.00119.35 C
ANISOU 1456 C LEU A1014 13815 12541 18991 706 2626 1259 C
ATOM 1457 O LEU A1014 -7.617 11.363 6.254 1.00119.25 O
ANISOU 1457 O LEU A1014 13541 12389 19381 720 2589 1463 O
ATOM 1458 CB LEU A1014 -4.222 10.895 6.274 1.00117.29 C
ANISOU 1458 CB LEU A1014 13873 12176 18515 530 2115 995 C
ATOM 1459 CG LEU A1014 -3.338 10.520 5.084 1.00115.92 C
ANISOU 1459 CG LEU A1014 13760 11810 18474 476 1747 783 C
ATOM 1460 CD1 LEU A1014 -2.046 9.841 5.521 1.00119.08 C
ANISOU 1460 CD1 LEU A1014 14266 12294 18685 400 1566 746 C
ATOM 1461 CD2 LEU A1014 -4.118 9.613 4.149 1.00117.30 C
ANISOU 1461 CD2 LEU A1014 13674 11752 19142 458 1505 928 C
ATOM 1462 N LYS A1015 -6.457 11.803 8.135 1.00124.67 N
ANISOU 1462 N LYS A1015 14533 13554 19283 727 2901 1325 N
ATOM 1463 CA LYS A1015 -7.633 11.679 8.993 1.00132.06 C
ANISOU 1463 CA LYS A1015 15196 14756 20225 787 3227 1633 C
ATOM 1464 C LYS A1015 -8.726 12.654 8.573 1.00124.76 C
ANISOU 1464 C LYS A1015 14148 13738 19516 974 3445 1492 C
ATOM 1465 O LYS A1015 -9.909 12.295 8.537 1.00128.83 O
ANISOU 1465 O LYS A1015 14326 14281 20342 998 3552 1805 O
ATOM 1466 CB LYS A1015 -7.242 11.910 10.455 1.00143.30 C
ANISOU 1466 CB LYS A1015 16723 16656 21070 810 3512 1615 C
ATOM 1467 CG LYS A1015 -6.186 10.942 10.975 1.00146.77 C
ANISOU 1467 CG LYS A1015 17252 17220 21295 628 3289 1824 C
ATOM 1468 CD LYS A1015 -5.576 11.424 12.285 1.00152.92 C
ANISOU 1468 CD LYS A1015 18209 18483 21409 656 3520 1679 C
ATOM 1469 CE LYS A1015 -4.376 10.572 12.683 1.00156.11 C
ANISOU 1469 CE LYS A1015 18727 18971 21618 483 3239 1855 C
ATOM 1470 NZ LYS A1015 -3.702 11.097 13.903 1.00162.45 N
ANISOU 1470 NZ LYS A1015 19720 20267 21736 498 3416 1674 N
ATOM 1471 N VAL A1016 -8.347 13.893 8.243 1.00116.92 N
ANISOU 1471 N VAL A1016 13402 12613 18411 1100 3489 1048 N
ATOM 1472 CA VAL A1016 -9.316 14.863 7.737 1.00119.51 C
ANISOU 1472 CA VAL A1016 13614 12772 19023 1290 3633 917 C
ATOM 1473 C VAL A1016 -10.013 14.327 6.493 1.00126.97 C
ANISOU 1473 C VAL A1016 14325 13426 20491 1229 3369 1167 C
ATOM 1474 O VAL A1016 -11.214 14.541 6.295 1.00135.30 O
ANISOU 1474 O VAL A1016 15099 14447 21863 1347 3501 1310 O
ATOM 1475 CB VAL A1016 -8.628 16.212 7.458 1.00114.83 C
ANISOU 1475 CB VAL A1016 13334 11985 18311 1387 3617 446 C
ATOM 1476 CG1 VAL A1016 -9.574 17.148 6.724 1.00113.79 C
ANISOU 1476 CG1 VAL A1016 13069 11579 18587 1568 3665 374 C
ATOM 1477 CG2 VAL A1016 -8.158 16.838 8.761 1.00119.92 C
ANISOU 1477 CG2 VAL A1016 14166 12923 18473 1479 3894 137 C
ATOM 1478 N ILE A1017 -9.272 13.619 5.637 1.00122.04 N
ANISOU 1478 N ILE A1017 13793 12615 19960 1056 2985 1194 N
ATOM 1479 CA ILE A1017 -9.874 13.034 4.439 1.00117.18 C
ANISOU 1479 CA ILE A1017 12960 11764 19797 990 2691 1370 C
ATOM 1480 C ILE A1017 -10.877 11.951 4.824 1.00134.14 C
ANISOU 1480 C ILE A1017 14742 13988 22239 922 2723 1795 C
ATOM 1481 O ILE A1017 -12.036 11.968 4.393 1.00140.28 O
ANISOU 1481 O ILE A1017 15224 14687 23388 971 2738 1976 O
ATOM 1482 CB ILE A1017 -8.790 12.481 3.499 1.00 90.28 C
ANISOU 1482 CB ILE A1017 9722 8210 16371 845 2286 1227 C
ATOM 1483 CG1 ILE A1017 -8.118 13.613 2.724 1.00 81.11 C
ANISOU 1483 CG1 ILE A1017 8806 6955 15058 889 2211 910 C
ATOM 1484 CG2 ILE A1017 -9.392 11.468 2.552 1.00 89.32 C
ANISOU 1484 CG2 ILE A1017 9337 7920 16681 754 1963 1410 C
ATOM 1485 CD1 ILE A1017 -6.861 13.183 1.995 1.00 81.23 C
ANISOU 1485 CD1 ILE A1017 8992 6953 14919 762 1892 730 C
ATOM 1486 N GLU A1018 -10.439 10.981 5.633 1.00144.04 N
ANISOU 1486 N GLU A1018 15983 15387 23359 792 2709 2003 N
ATOM 1487 CA GLU A1018 -11.360 9.942 6.089 1.00152.18 C
ANISOU 1487 CA GLU A1018 16640 16490 24691 688 2733 2490 C
ATOM 1488 C GLU A1018 -12.493 10.540 6.912 1.00156.49 C
ANISOU 1488 C GLU A1018 16940 17339 25181 830 3191 2664 C
ATOM 1489 O GLU A1018 -13.627 10.049 6.871 1.00157.88 O
ANISOU 1489 O GLU A1018 16723 17526 25737 788 3225 3035 O
ATOM 1490 CB GLU A1018 -10.612 8.879 6.893 1.00161.64 C
ANISOU 1490 CB GLU A1018 17873 17797 25745 520 2631 2735 C
ATOM 1491 CG GLU A1018 -11.397 7.596 7.119 1.00177.90 C
ANISOU 1491 CG GLU A1018 19539 19802 28251 342 2501 3296 C
ATOM 1492 CD GLU A1018 -11.849 6.947 5.819 1.00189.18 C
ANISOU 1492 CD GLU A1018 20790 20796 30296 259 2074 3295 C
ATOM 1493 OE1 GLU A1018 -12.975 6.410 5.784 1.00196.49 O
ANISOU 1493 OE1 GLU A1018 21329 21664 31664 173 2051 3681 O
ATOM 1494 OE2 GLU A1018 -11.079 6.965 4.835 1.00189.45 O
ANISOU 1494 OE2 GLU A1018 21047 20579 30356 275 1756 2902 O
ATOM 1495 N LYS A1019 -12.208 11.607 7.652 1.00155.77 N
ANISOU 1495 N LYS A1019 17050 17501 24634 1004 3538 2372 N
ATOM 1496 CA LYS A1019 -13.223 12.328 8.423 1.00164.13 C
ANISOU 1496 CA LYS A1019 17886 18879 25599 1206 4002 2400 C
ATOM 1497 C LYS A1019 -13.647 13.599 7.688 1.00164.93 C
ANISOU 1497 C LYS A1019 18036 18742 25886 1439 4059 2035 C
ATOM 1498 O LYS A1019 -13.449 14.724 8.153 1.00169.07 O
ANISOU 1498 O LYS A1019 18743 19361 26136 1646 4313 1648 O
ATOM 1499 CB LYS A1019 -12.696 12.646 9.818 1.00172.43 C
ANISOU 1499 CB LYS A1019 19091 20404 26023 1271 4346 2277 C
ATOM 1500 CG LYS A1019 -12.191 11.428 10.579 1.00177.64 C
ANISOU 1500 CG LYS A1019 19708 21315 26472 1032 4261 2695 C
ATOM 1501 CD LYS A1019 -11.533 11.821 11.893 1.00182.20 C
ANISOU 1501 CD LYS A1019 20478 22400 26348 1090 4553 2528 C
ATOM 1502 CE LYS A1019 -11.142 10.583 12.688 1.00185.02 C
ANISOU 1502 CE LYS A1019 20733 23048 26517 844 4463 3060 C
ATOM 1503 NZ LYS A1019 -10.618 10.893 14.049 1.00189.23 N
ANISOU 1503 NZ LYS A1019 21395 24196 26306 886 4755 2972 N
ATOM 1504 N ALA A1020 -14.226 13.399 6.506 1.00161.87 N
ANISOU 1504 N ALA A1020 17477 18025 26001 1397 3779 2163 N
ATOM 1505 CA ALA A1020 -14.703 14.484 5.661 1.00160.08 C
ANISOU 1505 CA ALA A1020 17243 17544 26036 1587 3754 1937 C
ATOM 1506 C ALA A1020 -16.038 14.075 5.060 1.00158.86 C
ANISOU 1506 C ALA A1020 16634 17310 26416 1583 3678 2289 C
ATOM 1507 O ALA A1020 -16.326 12.885 4.918 1.00156.04 O
ANISOU 1507 O ALA A1020 16055 16956 26279 1373 3486 2646 O
ATOM 1508 CB ALA A1020 -13.703 14.815 4.545 1.00156.37 C
ANISOU 1508 CB ALA A1020 17117 16743 25554 1507 3371 1672 C
ATOM 1509 N ASP A1021 -16.860 15.063 4.705 1.00159.47 N
ANISOU 1509 N ASP A1021 16554 17287 26751 1815 3799 2195 N
ATOM 1510 CA ASP A1021 -18.171 14.753 4.156 1.00155.80 C
ANISOU 1510 CA ASP A1021 15623 16770 26804 1826 3729 2532 C
ATOM 1511 C ASP A1021 -18.402 15.264 2.742 1.00149.61 C
ANISOU 1511 C ASP A1021 14850 15637 26359 1846 3362 2472 C
ATOM 1512 O ASP A1021 -19.424 14.913 2.144 1.00147.06 O
ANISOU 1512 O ASP A1021 14220 15278 26379 1763 3177 2737 O
ATOM 1513 CB ASP A1021 -19.278 15.306 5.065 1.00168.49 C
ANISOU 1513 CB ASP A1021 16891 18671 28458 2078 4205 2594 C
ATOM 1514 CG ASP A1021 -19.398 16.810 4.989 1.00180.47 C
ANISOU 1514 CG ASP A1021 18617 20065 29888 2342 4301 2182 C
ATOM 1515 OD1 ASP A1021 -20.048 17.311 4.051 1.00185.52 O
ANISOU 1515 OD1 ASP A1021 19187 20468 30833 2362 4054 2214 O
ATOM 1516 OD2 ASP A1021 -18.838 17.491 5.870 1.00185.89 O
ANISOU 1516 OD2 ASP A1021 19528 20893 30208 2514 4597 1827 O
ATOM 1517 N ASN A1022 -17.503 16.075 2.191 1.00146.15 N
ANISOU 1517 N ASN A1022 14811 15005 25716 1868 3196 2150 N
ATOM 1518 CA ASN A1022 -17.705 16.624 0.860 1.00133.40 C
ANISOU 1518 CA ASN A1022 13253 13193 24239 1796 2816 2131 C
ATOM 1519 C ASN A1022 -16.399 16.598 0.075 1.00116.13 C
ANISOU 1519 C ASN A1022 11432 10891 21799 1640 2492 1944 C
ATOM 1520 O ASN A1022 -15.313 16.417 0.631 1.00101.00 O
ANISOU 1520 O ASN A1022 9787 8993 19596 1620 2586 1765 O
ATOM 1521 CB ASN A1022 -18.275 18.051 0.923 1.00130.88 C
ANISOU 1521 CB ASN A1022 12949 12814 23967 2007 2964 1988 C
ATOM 1522 CG ASN A1022 -17.201 19.106 1.001 1.00123.64 C
ANISOU 1522 CG ASN A1022 12444 11770 22764 2066 2972 1640 C
ATOM 1523 OD1 ASN A1022 -16.705 19.576 -0.024 1.00115.27 O
ANISOU 1523 OD1 ASN A1022 11554 10565 21679 1958 2649 1615 O
ATOM 1524 ND2 ASN A1022 -16.838 19.495 2.220 1.00129.61 N
ANISOU 1524 ND2 ASN A1022 13339 12612 23295 2231 3337 1379 N
ATOM 1525 N ALA A1023 -16.526 16.797 -1.240 1.00113.34 N
ANISOU 1525 N ALA A1023 11062 10462 21540 1535 2115 1996 N
ATOM 1526 CA ALA A1023 -15.386 16.634 -2.139 1.00103.69 C
ANISOU 1526 CA ALA A1023 10102 9215 20082 1381 1787 1863 C
ATOM 1527 C ALA A1023 -14.349 17.734 -1.942 1.00104.40 C
ANISOU 1527 C ALA A1023 10555 9246 19865 1433 1885 1621 C
ATOM 1528 O ALA A1023 -13.139 17.471 -1.983 1.00102.12 O
ANISOU 1528 O ALA A1023 10532 8977 19293 1332 1803 1459 O
ATOM 1529 CB ALA A1023 -15.869 16.598 -3.589 1.00100.25 C
ANISOU 1529 CB ALA A1023 9491 8768 19832 1297 1385 2013 C
ATOM 1530 N ALA A1024 -14.802 18.975 -1.736 1.00103.68 N
ANISOU 1530 N ALA A1024 10467 9063 19864 1584 2034 1589 N
ATOM 1531 CA ALA A1024 -13.874 20.094 -1.585 1.00106.47 C
ANISOU 1531 CA ALA A1024 11139 9304 20012 1614 2072 1370 C
ATOM 1532 C ALA A1024 -12.930 19.878 -0.406 1.00111.51 C
ANISOU 1532 C ALA A1024 12033 9986 20348 1630 2329 1105 C
ATOM 1533 O ALA A1024 -11.712 20.052 -0.527 1.00114.85 O
ANISOU 1533 O ALA A1024 12742 10384 20511 1521 2231 952 O
ATOM 1534 CB ALA A1024 -14.646 21.405 -1.428 1.00108.27 C
ANISOU 1534 CB ALA A1024 11288 9375 20473 1798 2176 1353 C
ATOM 1535 N GLN A1025 -13.484 19.491 0.747 1.00112.73 N
ANISOU 1535 N GLN A1025 12062 10232 20541 1771 2669 1075 N
ATOM 1536 CA GLN A1025 -12.655 19.195 1.912 1.00112.36 C
ANISOU 1536 CA GLN A1025 12214 10269 20207 1807 2935 860 C
ATOM 1537 C GLN A1025 -11.513 18.244 1.561 1.00110.95 C
ANISOU 1537 C GLN A1025 12220 10148 19787 1580 2708 867 C
ATOM 1538 O GLN A1025 -10.357 18.472 1.939 1.00106.28 O
ANISOU 1538 O GLN A1025 11936 9591 18856 1503 2713 637 O
ATOM 1539 CB GLN A1025 -13.518 18.609 3.025 1.00120.15 C
ANISOU 1539 CB GLN A1025 12928 11459 21266 1964 3313 956 C
ATOM 1540 CG GLN A1025 -13.682 19.543 4.206 1.00132.10 C
ANISOU 1540 CG GLN A1025 14493 13054 22646 2215 3712 651 C
ATOM 1541 CD GLN A1025 -14.569 18.963 5.277 1.00144.84 C
ANISOU 1541 CD GLN A1025 15798 15034 24200 2329 4088 781 C
ATOM 1542 OE1 GLN A1025 -14.945 17.792 5.225 1.00142.88 O
ANISOU 1542 OE1 GLN A1025 15329 14962 23998 2166 4028 1142 O
ATOM 1543 NE2 GLN A1025 -14.912 19.783 6.261 1.00155.14 N
ANISOU 1543 NE2 GLN A1025 17071 16477 25396 2598 4462 485 N
ATOM 1544 N VAL A1026 -11.822 17.173 0.825 1.00107.35 N
ANISOU 1544 N VAL A1026 11577 9746 19466 1441 2460 1099 N
ATOM 1545 CA VAL A1026 -10.794 16.219 0.406 1.00 99.74 C
ANISOU 1545 CA VAL A1026 10760 8870 18265 1222 2188 1056 C
ATOM 1546 C VAL A1026 -9.775 16.901 -0.502 1.00 89.73 C
ANISOU 1546 C VAL A1026 9734 7539 16820 1140 1963 898 C
ATOM 1547 O VAL A1026 -8.564 16.852 -0.258 1.00 98.32 O
ANISOU 1547 O VAL A1026 11076 8705 17575 1041 1935 712 O
ATOM 1548 CB VAL A1026 -11.435 15.005 -0.288 1.00 64.37 C
ANISOU 1548 CB VAL A1026 6001 4407 14049 1116 1926 1274 C
ATOM 1549 N LYS A1027 -10.261 17.563 -1.557 1.00 82.31 N
ANISOU 1549 N LYS A1027 8688 6487 16100 1169 1794 1014 N
ATOM 1550 CA LYS A1027 -9.375 18.195 -2.534 1.00 80.97 C
ANISOU 1550 CA LYS A1027 8684 6314 15767 1060 1563 967 C
ATOM 1551 C LYS A1027 -8.363 19.131 -1.878 1.00 89.32 C
ANISOU 1551 C LYS A1027 10043 7291 16602 1055 1715 763 C
ATOM 1552 O LYS A1027 -7.179 19.132 -2.238 1.00 92.91 O
ANISOU 1552 O LYS A1027 10679 7858 16763 898 1572 662 O
ATOM 1553 CB LYS A1027 -10.207 18.955 -3.561 1.00 85.80 C
ANISOU 1553 CB LYS A1027 9111 6823 16666 1110 1399 1199 C
ATOM 1554 CG LYS A1027 -9.369 19.720 -4.552 1.00 95.69 C
ANISOU 1554 CG LYS A1027 10494 8095 17770 987 1176 1254 C
ATOM 1555 CD LYS A1027 -10.204 20.116 -5.738 1.00108.10 C
ANISOU 1555 CD LYS A1027 11828 9656 19587 998 932 1561 C
ATOM 1556 CE LYS A1027 -10.480 21.601 -5.725 1.00115.46 C
ANISOU 1556 CE LYS A1027 12780 10313 20774 1088 980 1710 C
ATOM 1557 NZ LYS A1027 -9.210 22.361 -5.769 1.00115.94 N
ANISOU 1557 NZ LYS A1027 13104 10299 20648 963 952 1659 N
ATOM 1558 N ASP A1028 -8.812 19.930 -0.907 1.00 96.20 N
ANISOU 1558 N ASP A1028 10951 8046 17556 1207 1980 666 N
ATOM 1559 CA ASP A1028 -7.908 20.835 -0.204 1.00108.41 C
ANISOU 1559 CA ASP A1028 12775 9491 18924 1206 2098 414 C
ATOM 1560 C ASP A1028 -6.977 20.079 0.732 1.00 98.16 C
ANISOU 1560 C ASP A1028 11659 8357 17282 1139 2223 211 C
ATOM 1561 O ASP A1028 -5.793 20.417 0.845 1.00 94.36 O
ANISOU 1561 O ASP A1028 11411 7893 16548 1012 2156 45 O
ATOM 1562 CB ASP A1028 -8.715 21.867 0.563 1.00126.55 C
ANISOU 1562 CB ASP A1028 15037 11651 21396 1409 2313 295 C
ATOM 1563 CG ASP A1028 -9.528 22.731 -0.351 1.00137.04 C
ANISOU 1563 CG ASP A1028 16199 12828 23041 1454 2140 499 C
ATOM 1564 OD1 ASP A1028 -8.940 23.608 -1.011 1.00139.51 O
ANISOU 1564 OD1 ASP A1028 16624 12986 23396 1356 1934 547 O
ATOM 1565 OD2 ASP A1028 -10.753 22.518 -0.438 1.00140.72 O
ANISOU 1565 OD2 ASP A1028 16399 13327 23742 1576 2199 653 O
ATOM 1566 N ALA A1029 -7.499 19.068 1.435 1.00 94.73 N
ANISOU 1566 N ALA A1029 11095 8100 16796 1189 2374 260 N
ATOM 1567 CA ALA A1029 -6.639 18.199 2.225 1.00 84.32 C
ANISOU 1567 CA ALA A1029 9910 7013 15116 1084 2412 158 C
ATOM 1568 C ALA A1029 -5.538 17.609 1.350 1.00 86.77 C
ANISOU 1568 C ALA A1029 10309 7406 15253 883 2100 155 C
ATOM 1569 O ALA A1029 -4.353 17.667 1.695 1.00 87.75 O
ANISOU 1569 O ALA A1029 10642 7621 15077 782 2067 -18 O
ATOM 1570 CB ALA A1029 -7.470 17.096 2.882 1.00 69.50 C
ANISOU 1570 CB ALA A1029 7812 5300 13296 1129 2552 346 C
ATOM 1571 N LEU A1030 -5.924 17.080 0.185 1.00 88.13 N
ANISOU 1571 N LEU A1030 10301 7577 15609 835 1864 318 N
ATOM 1572 CA LEU A1030 -4.973 16.465 -0.738 1.00 85.01 C
ANISOU 1572 CA LEU A1030 9936 7323 15041 683 1573 265 C
ATOM 1573 C LEU A1030 -3.891 17.455 -1.171 1.00 75.36 C
ANISOU 1573 C LEU A1030 8907 6122 13606 584 1501 155 C
ATOM 1574 O LEU A1030 -2.690 17.175 -1.059 1.00 78.11 O
ANISOU 1574 O LEU A1030 9384 6622 13670 475 1431 8 O
ATOM 1575 CB LEU A1030 -5.727 15.909 -1.952 1.00 85.67 C
ANISOU 1575 CB LEU A1030 9776 7425 15351 674 1333 411 C
ATOM 1576 CG LEU A1030 -6.551 14.629 -1.749 1.00 86.28 C
ANISOU 1576 CG LEU A1030 9631 7487 15663 700 1283 514 C
ATOM 1577 CD1 LEU A1030 -7.733 14.543 -2.724 1.00 94.63 C
ANISOU 1577 CD1 LEU A1030 10423 8488 17043 732 1119 687 C
ATOM 1578 CD2 LEU A1030 -5.649 13.403 -1.878 1.00 77.49 C
ANISOU 1578 CD2 LEU A1030 8538 6490 14415 608 1070 365 C
ATOM 1579 N THR A1031 -4.311 18.622 -1.679 1.00 61.91 N
ANISOU 1579 N THR A1031 7191 4254 12077 612 1500 262 N
ATOM 1580 CA THR A1031 -3.376 19.682 -2.058 1.00 74.16 C
ANISOU 1580 CA THR A1031 8895 5772 13511 490 1423 238 C
ATOM 1581 C THR A1031 -2.444 20.050 -0.912 1.00 90.42 C
ANISOU 1581 C THR A1031 11194 7793 15367 454 1570 -3 C
ATOM 1582 O THR A1031 -1.275 20.394 -1.134 1.00 97.47 O
ANISOU 1582 O THR A1031 12204 8776 16053 291 1463 -65 O
ATOM 1583 CB THR A1031 -4.148 20.924 -2.501 1.00 76.14 C
ANISOU 1583 CB THR A1031 9085 5744 14100 556 1415 427 C
ATOM 1584 OG1 THR A1031 -5.162 20.551 -3.440 1.00 76.13 O
ANISOU 1584 OG1 THR A1031 8838 5793 14295 608 1282 662 O
ATOM 1585 CG2 THR A1031 -3.210 21.939 -3.132 1.00 78.81 C
ANISOU 1585 CG2 THR A1031 9522 6048 14374 378 1261 517 C
ATOM 1586 N LYS A1032 -2.955 20.020 0.318 1.00 94.17 N
ANISOU 1586 N LYS A1032 11721 8176 15883 599 1813 -134 N
ATOM 1587 CA LYS A1032 -2.111 20.264 1.481 1.00 92.39 C
ANISOU 1587 CA LYS A1032 11715 7984 15406 571 1939 -393 C
ATOM 1588 C LYS A1032 -0.969 19.254 1.561 1.00 79.64 C
ANISOU 1588 C LYS A1032 10154 6657 13451 426 1819 -451 C
ATOM 1589 O LYS A1032 0.210 19.627 1.545 1.00 70.07 O
ANISOU 1589 O LYS A1032 9078 5506 12042 279 1721 -565 O
ATOM 1590 CB LYS A1032 -2.956 20.228 2.753 1.00 98.16 C
ANISOU 1590 CB LYS A1032 12440 8699 16160 765 2232 -508 C
ATOM 1591 CG LYS A1032 -3.056 21.561 3.452 1.00111.68 C
ANISOU 1591 CG LYS A1032 14290 10177 17967 873 2382 -761 C
ATOM 1592 CD LYS A1032 -3.056 21.369 4.962 1.00123.47 C
ANISOU 1592 CD LYS A1032 15874 11870 19169 977 2640 -1015 C
ATOM 1593 CE LYS A1032 -4.330 21.896 5.603 1.00131.66 C
ANISOU 1593 CE LYS A1032 16793 12822 20410 1252 2926 -1123 C
ATOM 1594 NZ LYS A1032 -4.316 21.724 7.088 1.00134.89 N
ANISOU 1594 NZ LYS A1032 17269 13542 20441 1354 3197 -1379 N
ATOM 1595 N MET A1033 -1.308 17.959 1.642 1.00 73.90 N
ANISOU 1595 N MET A1033 9292 6085 12700 466 1806 -360 N
ATOM 1596 CA MET A1033 -0.281 16.926 1.760 1.00 70.72 C
ANISOU 1596 CA MET A1033 8910 5904 12054 367 1673 -418 C
ATOM 1597 C MET A1033 0.673 16.936 0.576 1.00 74.48 C
ANISOU 1597 C MET A1033 9362 6504 12435 234 1433 -446 C
ATOM 1598 O MET A1033 1.838 16.547 0.721 1.00 70.49 O
ANISOU 1598 O MET A1033 8911 6175 11697 144 1338 -564 O
ATOM 1599 CB MET A1033 -0.903 15.534 1.890 1.00 70.67 C
ANISOU 1599 CB MET A1033 8726 5956 12170 429 1639 -280 C
ATOM 1600 CG MET A1033 -2.417 15.480 1.931 1.00 84.57 C
ANISOU 1600 CG MET A1033 10317 7585 14232 552 1770 -98 C
ATOM 1601 SD MET A1033 -3.072 13.794 1.946 1.00 91.05 S
ANISOU 1601 SD MET A1033 10887 8426 15281 563 1652 111 S
ATOM 1602 CE MET A1033 -1.713 12.919 2.718 1.00 85.75 C
ANISOU 1602 CE MET A1033 10334 7913 14333 476 1556 28 C
ATOM 1603 N ARG A1034 0.200 17.363 -0.598 1.00 81.20 N
ANISOU 1603 N ARG A1034 10100 7313 13440 223 1332 -324 N
ATOM 1604 CA ARG A1034 1.049 17.374 -1.786 1.00 82.91 C
ANISOU 1604 CA ARG A1034 10248 7754 13500 95 1124 -323 C
ATOM 1605 C ARG A1034 2.319 18.182 -1.553 1.00 82.07 C
ANISOU 1605 C ARG A1034 10290 7716 13176 -60 1121 -405 C
ATOM 1606 O ARG A1034 3.422 17.741 -1.895 1.00 83.47 O
ANISOU 1606 O ARG A1034 10428 8169 13118 -154 1004 -496 O
ATOM 1607 CB ARG A1034 0.279 17.932 -2.982 1.00 86.63 C
ANISOU 1607 CB ARG A1034 10581 8201 14134 91 1030 -117 C
ATOM 1608 CG ARG A1034 0.946 17.604 -4.297 1.00 95.20 C
ANISOU 1608 CG ARG A1034 11521 9651 14997 -12 814 -109 C
ATOM 1609 CD ARG A1034 0.238 18.211 -5.488 1.00104.46 C
ANISOU 1609 CD ARG A1034 12550 10877 16264 -41 699 144 C
ATOM 1610 NE ARG A1034 0.758 17.643 -6.726 1.00105.75 N
ANISOU 1610 NE ARG A1034 12536 11502 16142 -106 500 100 N
ATOM 1611 CZ ARG A1034 1.884 18.040 -7.309 1.00102.96 C
ANISOU 1611 CZ ARG A1034 12155 11492 15475 -263 441 128 C
ATOM 1612 NH1 ARG A1034 2.606 19.011 -6.767 1.00102.07 N
ANISOU 1612 NH1 ARG A1034 12187 11246 15350 -397 535 223 N
ATOM 1613 NH2 ARG A1034 2.287 17.465 -8.433 1.00103.77 N
ANISOU 1613 NH2 ARG A1034 12061 12093 15275 -288 284 45 N
ATOM 1614 N ALA A1035 2.176 19.381 -0.979 1.00 84.51 N
ANISOU 1614 N ALA A1035 10748 7766 13597 -83 1236 -392 N
ATOM 1615 CA ALA A1035 3.345 20.166 -0.585 1.00 87.64 C
ANISOU 1615 CA ALA A1035 11290 8163 13845 -248 1213 -492 C
ATOM 1616 C ALA A1035 4.097 19.509 0.568 1.00 81.52 C
ANISOU 1616 C ALA A1035 10628 7514 12831 -242 1267 -717 C
ATOM 1617 O ALA A1035 5.334 19.484 0.571 1.00 74.77 O
ANISOU 1617 O ALA A1035 9794 6852 11764 -390 1166 -793 O
ATOM 1618 CB ALA A1035 2.927 21.585 -0.200 1.00 87.14 C
ANISOU 1618 CB ALA A1035 11354 7717 14039 -251 1286 -482 C
ATOM 1619 N ALA A1036 3.366 19.004 1.568 1.00 78.09 N
ANISOU 1619 N ALA A1036 10244 7004 12425 -83 1422 -788 N
ATOM 1620 CA ALA A1036 3.982 18.297 2.691 1.00 71.94 C
ANISOU 1620 CA ALA A1036 9547 6385 11402 -77 1458 -926 C
ATOM 1621 C ALA A1036 4.913 17.183 2.223 1.00 59.80 C
ANISOU 1621 C ALA A1036 7890 5115 9718 -134 1276 -919 C
ATOM 1622 O ALA A1036 6.031 17.040 2.731 1.00 56.93 O
ANISOU 1622 O ALA A1036 7584 4910 9136 -224 1206 -1028 O
ATOM 1623 CB ALA A1036 2.899 17.721 3.600 1.00 72.68 C
ANISOU 1623 CB ALA A1036 9626 6440 11551 95 1642 -886 C
ATOM 1624 N ALA A1037 4.454 16.364 1.273 1.00 54.28 N
ANISOU 1624 N ALA A1037 7003 4467 9152 -66 1181 -822 N
ATOM 1625 CA ALA A1037 5.290 15.292 0.732 1.00 53.91 C
ANISOU 1625 CA ALA A1037 6813 4656 9016 -73 993 -890 C
ATOM 1626 C ALA A1037 6.507 15.851 -0.002 1.00 58.06 C
ANISOU 1626 C ALA A1037 7304 5411 9346 -224 888 -961 C
ATOM 1627 O ALA A1037 7.628 15.353 0.160 1.00 59.72 O
ANISOU 1627 O ALA A1037 7468 5830 9393 -262 790 -1076 O
ATOM 1628 CB ALA A1037 4.474 14.398 -0.202 1.00 52.48 C
ANISOU 1628 CB ALA A1037 6433 4465 9042 38 890 -842 C
ATOM 1629 N LEU A1038 6.300 16.876 -0.834 1.00 63.65 N
ANISOU 1629 N LEU A1038 7999 6099 10085 -317 896 -852 N
ATOM 1630 CA LEU A1038 7.417 17.541 -1.510 1.00 72.91 C
ANISOU 1630 CA LEU A1038 9112 7513 11078 -505 811 -830 C
ATOM 1631 C LEU A1038 8.390 18.158 -0.508 1.00 79.32 C
ANISOU 1631 C LEU A1038 10080 8280 11778 -645 833 -914 C
ATOM 1632 O LEU A1038 9.614 18.052 -0.665 1.00 78.26 O
ANISOU 1632 O LEU A1038 9856 8423 11454 -762 741 -973 O
ATOM 1633 CB LEU A1038 6.891 18.611 -2.472 1.00 73.65 C
ANISOU 1633 CB LEU A1038 9163 7543 11276 -603 805 -598 C
ATOM 1634 CG LEU A1038 6.322 18.047 -3.767 1.00 70.69 C
ANISOU 1634 CG LEU A1038 8573 7398 10887 -526 716 -518 C
ATOM 1635 CD1 LEU A1038 5.489 19.062 -4.544 1.00 72.02 C
ANISOU 1635 CD1 LEU A1038 8710 7442 11213 -589 705 -224 C
ATOM 1636 CD2 LEU A1038 7.472 17.546 -4.617 1.00 66.73 C
ANISOU 1636 CD2 LEU A1038 7866 7408 10078 -595 603 -610 C
ATOM 1637 N ASP A1039 7.862 18.834 0.518 1.00 83.28 N
ANISOU 1637 N ASP A1039 10792 8459 12389 -630 948 -947 N
ATOM 1638 CA ASP A1039 8.713 19.301 1.612 1.00 91.51 C
ANISOU 1638 CA ASP A1039 11995 9472 13304 -741 946 -1098 C
ATOM 1639 C ASP A1039 9.397 18.135 2.320 1.00 80.36 C
ANISOU 1639 C ASP A1039 10553 8293 11686 -679 898 -1217 C
ATOM 1640 O ASP A1039 10.583 18.208 2.663 1.00 80.03 O
ANISOU 1640 O ASP A1039 10509 8425 11474 -811 798 -1301 O
ATOM 1641 CB ASP A1039 7.894 20.119 2.606 1.00113.91 C
ANISOU 1641 CB ASP A1039 15047 11965 16269 -679 1089 -1194 C
ATOM 1642 CG ASP A1039 8.764 20.875 3.598 1.00132.50 C
ANISOU 1642 CG ASP A1039 17571 14271 18502 -823 1048 -1398 C
ATOM 1643 OD1 ASP A1039 9.459 20.237 4.413 1.00139.00 O
ANISOU 1643 OD1 ASP A1039 18427 15313 19075 -830 1012 -1518 O
ATOM 1644 OD2 ASP A1039 8.773 22.123 3.539 1.00138.80 O
ANISOU 1644 OD2 ASP A1039 18458 14797 19485 -938 1017 -1432 O
ATOM 1645 N ALA A1040 8.655 17.050 2.555 1.00 67.27 N
ANISOU 1645 N ALA A1040 8851 6626 10084 -488 943 -1191 N
ATOM 1646 CA ALA A1040 9.250 15.849 3.138 1.00 66.09 C
ANISOU 1646 CA ALA A1040 8636 6653 9822 -421 854 -1235 C
ATOM 1647 C ALA A1040 10.262 15.197 2.202 1.00 69.10 C
ANISOU 1647 C ALA A1040 8795 7303 10158 -438 679 -1286 C
ATOM 1648 O ALA A1040 11.228 14.582 2.666 1.00 60.24 O
ANISOU 1648 O ALA A1040 7611 6349 8926 -440 565 -1354 O
ATOM 1649 CB ALA A1040 8.166 14.837 3.504 1.00 68.74 C
ANISOU 1649 CB ALA A1040 8935 6873 10311 -239 911 -1131 C
ATOM 1650 N GLN A1041 10.066 15.321 0.889 1.00 79.02 N
ANISOU 1650 N GLN A1041 9905 8642 11478 -439 652 -1260 N
ATOM 1651 CA GLN A1041 10.955 14.655 -0.055 1.00 80.05 C
ANISOU 1651 CA GLN A1041 9786 9105 11525 -415 512 -1364 C
ATOM 1652 C GLN A1041 12.383 15.192 0.013 1.00 93.66 C
ANISOU 1652 C GLN A1041 11454 11094 13038 -594 457 -1406 C
ATOM 1653 O GLN A1041 13.322 14.473 -0.349 1.00102.15 O
ANISOU 1653 O GLN A1041 12314 12471 14029 -542 347 -1533 O
ATOM 1654 CB GLN A1041 10.391 14.781 -1.474 1.00 79.81 C
ANISOU 1654 CB GLN A1041 9606 9194 11525 -392 506 -1325 C
ATOM 1655 CG GLN A1041 11.329 14.288 -2.555 1.00 86.92 C
ANISOU 1655 CG GLN A1041 10223 10547 12254 -371 395 -1472 C
ATOM 1656 CD GLN A1041 10.621 13.891 -3.827 1.00 91.14 C
ANISOU 1656 CD GLN A1041 10587 11237 12804 -261 348 -1522 C
ATOM 1657 OE1 GLN A1041 10.056 14.723 -4.528 1.00100.68 O
ANISOU 1657 OE1 GLN A1041 11803 12482 13970 -364 398 -1334 O
ATOM 1658 NE2 GLN A1041 10.663 12.604 -4.141 1.00 81.60 N
ANISOU 1658 NE2 GLN A1041 9209 10117 11677 -49 219 -1785 N
ATOM 1659 N LYS A1042 12.577 16.421 0.492 1.00 97.00 N
ANISOU 1659 N LYS A1042 12044 11399 13410 -798 514 -1323 N
ATOM 1660 CA LYS A1042 13.894 17.045 0.521 1.00101.47 C
ANISOU 1660 CA LYS A1042 12540 12191 13824 -1017 439 -1328 C
ATOM 1661 C LYS A1042 14.602 16.892 1.860 1.00 91.37 C
ANISOU 1661 C LYS A1042 11377 10884 12457 -1053 375 -1435 C
ATOM 1662 O LYS A1042 15.694 17.444 2.036 1.00 91.32 O
ANISOU 1662 O LYS A1042 11318 11034 12344 -1254 290 -1446 O
ATOM 1663 CB LYS A1042 13.794 18.531 0.167 1.00118.09 C
ANISOU 1663 CB LYS A1042 14724 14158 15987 -1258 475 -1162 C
ATOM 1664 CG LYS A1042 13.806 18.826 -1.319 1.00121.54 C
ANISOU 1664 CG LYS A1042 14932 14855 16392 -1338 470 -977 C
ATOM 1665 CD LYS A1042 12.426 19.214 -1.813 1.00124.78 C
ANISOU 1665 CD LYS A1042 15435 14991 16983 -1264 548 -831 C
ATOM 1666 CE LYS A1042 12.429 19.496 -3.301 1.00136.30 C
ANISOU 1666 CE LYS A1042 16653 16780 18356 -1355 521 -606 C
ATOM 1667 NZ LYS A1042 11.071 19.898 -3.738 1.00144.52 N
ANISOU 1667 NZ LYS A1042 17775 17541 19594 -1285 565 -435 N
ATOM 1668 N ALA A1043 14.007 16.179 2.810 1.00 86.83 N
ANISOU 1668 N ALA A1043 10937 10141 11914 -886 401 -1479 N
ATOM 1669 CA ALA A1043 14.674 15.914 4.073 1.00 88.72 C
ANISOU 1669 CA ALA A1043 11259 10434 12016 -912 318 -1543 C
ATOM 1670 C ALA A1043 15.515 14.646 3.963 1.00 87.44 C
ANISOU 1670 C ALA A1043 10854 10522 11849 -786 162 -1574 C
ATOM 1671 O ALA A1043 15.363 13.844 3.037 1.00 77.13 O
ANISOU 1671 O ALA A1043 9347 9288 10671 -627 135 -1600 O
ATOM 1672 CB ALA A1043 13.655 15.791 5.208 1.00 88.31 C
ANISOU 1672 CB ALA A1043 11440 10158 11956 -809 427 -1522 C
ATOM 1673 N THR A1044 16.428 14.475 4.923 1.00 91.32 N
ANISOU 1673 N THR A1044 11350 11145 12203 -847 34 -1598 N
ATOM 1674 CA THR A1044 17.121 13.209 5.087 1.00 87.91 C
ANISOU 1674 CA THR A1044 10703 10873 11825 -692 -139 -1600 C
ATOM 1675 C THR A1044 16.458 12.446 6.221 1.00 84.48 C
ANISOU 1675 C THR A1044 10405 10276 11418 -569 -159 -1465 C
ATOM 1676 O THR A1044 16.387 12.971 7.344 1.00 86.00 O
ANISOU 1676 O THR A1044 10811 10468 11398 -682 -130 -1423 O
ATOM 1677 CB THR A1044 18.604 13.424 5.384 1.00 90.48 C
ANISOU 1677 CB THR A1044 10886 11488 12005 -836 -301 -1653 C
ATOM 1678 OG1 THR A1044 19.223 14.113 4.289 1.00 94.13 O
ANISOU 1678 OG1 THR A1044 11170 12155 12442 -973 -270 -1715 O
ATOM 1679 CG2 THR A1044 19.303 12.092 5.564 1.00 91.18 C
ANISOU 1679 CG2 THR A1044 10726 11710 12209 -640 -500 -1649 C
ATOM 1680 N PRO A1045 15.921 11.254 5.981 1.00 88.04 N
ANISOU 1680 N PRO A1045 10734 10597 12120 -352 -212 -1390 N
ATOM 1681 CA PRO A1045 15.258 10.508 7.057 1.00 95.22 C
ANISOU 1681 CA PRO A1045 11736 11366 13080 -269 -237 -1165 C
ATOM 1682 C PRO A1045 16.276 10.011 8.067 1.00 99.55 C
ANISOU 1682 C PRO A1045 12218 12097 13511 -293 -450 -1054 C
ATOM 1683 O PRO A1045 17.471 9.905 7.750 1.00101.31 O
ANISOU 1683 O PRO A1045 12251 12505 13738 -302 -612 -1175 O
ATOM 1684 CB PRO A1045 14.573 9.348 6.315 1.00 97.95 C
ANISOU 1684 CB PRO A1045 11904 11489 13823 -54 -302 -1125 C
ATOM 1685 CG PRO A1045 15.358 9.182 5.064 1.00100.63 C
ANISOU 1685 CG PRO A1045 12003 11959 14272 21 -397 -1388 C
ATOM 1686 CD PRO A1045 15.822 10.563 4.684 1.00 96.78 C
ANISOU 1686 CD PRO A1045 11603 11684 13484 -183 -256 -1512 C
ATOM 1687 N PRO A1046 15.845 9.706 9.298 1.00 98.27 N
ANISOU 1687 N PRO A1046 12179 11938 13223 -307 -457 -802 N
ATOM 1688 CA PRO A1046 16.823 9.424 10.366 1.00 91.76 C
ANISOU 1688 CA PRO A1046 11315 11354 12194 -371 -668 -666 C
ATOM 1689 C PRO A1046 17.795 8.299 10.053 1.00 84.45 C
ANISOU 1689 C PRO A1046 10077 10434 11578 -229 -967 -614 C
ATOM 1690 O PRO A1046 19.001 8.447 10.289 1.00 83.15 O
ANISOU 1690 O PRO A1046 9805 10505 11282 -297 -1137 -682 O
ATOM 1691 CB PRO A1046 15.928 9.080 11.565 1.00100.53 C
ANISOU 1691 CB PRO A1046 12563 12484 13150 -375 -603 -335 C
ATOM 1692 CG PRO A1046 14.640 9.746 11.282 1.00103.29 C
ANISOU 1692 CG PRO A1046 13094 12676 13475 -378 -292 -415 C
ATOM 1693 CD PRO A1046 14.461 9.663 9.799 1.00102.56 C
ANISOU 1693 CD PRO A1046 12879 12335 13756 -280 -265 -608 C
ATOM 1694 N LYS A1047 17.303 7.172 9.532 1.00 83.90 N
ANISOU 1694 N LYS A1047 9834 10090 11954 -26 -1056 -515 N
ATOM 1695 CA LYS A1047 18.190 6.059 9.207 1.00 87.82 C
ANISOU 1695 CA LYS A1047 10010 10530 12828 158 -1360 -524 C
ATOM 1696 C LYS A1047 19.227 6.470 8.170 1.00 92.81 C
ANISOU 1696 C LYS A1047 10458 11357 13447 187 -1372 -919 C
ATOM 1697 O LYS A1047 20.412 6.141 8.292 1.00 93.37 O
ANISOU 1697 O LYS A1047 10305 11605 13567 237 -1587 -959 O
ATOM 1698 CB LYS A1047 17.374 4.861 8.713 1.00 88.31 C
ANISOU 1698 CB LYS A1047 9927 10193 13435 372 -1462 -431 C
ATOM 1699 CG LYS A1047 18.217 3.641 8.354 1.00 96.00 C
ANISOU 1699 CG LYS A1047 10551 11021 14903 611 -1807 -497 C
ATOM 1700 CD LYS A1047 17.361 2.392 8.204 1.00106.54 C
ANISOU 1700 CD LYS A1047 11762 11884 16836 785 -1981 -319 C
ATOM 1701 CE LYS A1047 18.218 1.176 7.885 1.00116.95 C
ANISOU 1701 CE LYS A1047 12721 12991 18722 1053 -2362 -428 C
ATOM 1702 NZ LYS A1047 17.454 -0.096 7.967 1.00119.74 N
ANISOU 1702 NZ LYS A1047 12945 12812 19741 1190 -2615 -174 N
ATOM 1703 N LEU A1048 18.799 7.220 7.156 1.00 96.00 N
ANISOU 1703 N LEU A1048 10931 11773 13771 147 -1142 -1176 N
ATOM 1704 CA LEU A1048 19.632 7.570 6.015 1.00100.71 C
ANISOU 1704 CA LEU A1048 11313 12605 14345 171 -1118 -1506 C
ATOM 1705 C LEU A1048 20.517 8.784 6.263 1.00106.45 C
ANISOU 1705 C LEU A1048 12102 13661 14684 -92 -1054 -1551 C
ATOM 1706 O LEU A1048 21.029 9.375 5.306 1.00115.51 O
ANISOU 1706 O LEU A1048 13109 15036 15743 -154 -967 -1752 O
ATOM 1707 CB LEU A1048 18.751 7.788 4.788 1.00 92.55 C
ANISOU 1707 CB LEU A1048 10297 11476 13391 230 -930 -1697 C
ATOM 1708 CG LEU A1048 18.202 6.433 4.358 1.00 86.24 C
ANISOU 1708 CG LEU A1048 9330 10382 13055 514 -1082 -1755 C
ATOM 1709 CD1 LEU A1048 17.314 6.535 3.131 1.00 83.03 C
ANISOU 1709 CD1 LEU A1048 8916 9905 12726 585 -942 -1967 C
ATOM 1710 CD2 LEU A1048 19.379 5.499 4.130 1.00 87.05 C
ANISOU 1710 CD2 LEU A1048 9074 10595 13408 731 -1340 -1939 C
ATOM 1711 N GLU A1049 20.712 9.162 7.521 1.00104.03 N
ANISOU 1711 N GLU A1049 11981 13407 14140 -259 -1112 -1362 N
ATOM 1712 CA GLU A1049 21.658 10.218 7.847 1.00103.22 C
ANISOU 1712 CA GLU A1049 11907 13586 13727 -515 -1128 -1428 C
ATOM 1713 C GLU A1049 23.073 9.777 7.475 1.00112.65 C
ANISOU 1713 C GLU A1049 12713 15061 15026 -449 -1331 -1523 C
ATOM 1714 O GLU A1049 23.392 8.586 7.477 1.00108.45 O
ANISOU 1714 O GLU A1049 11941 14488 14777 -201 -1519 -1488 O
ATOM 1715 CB GLU A1049 21.550 10.564 9.336 1.00106.83 C
ANISOU 1715 CB GLU A1049 12627 14072 13893 -674 -1188 -1252 C
ATOM 1716 CG GLU A1049 22.576 11.545 9.869 1.00124.56 C
ANISOU 1716 CG GLU A1049 14899 16584 15842 -944 -1287 -1338 C
ATOM 1717 CD GLU A1049 22.521 11.674 11.381 1.00141.08 C
ANISOU 1717 CD GLU A1049 17213 18778 17614 -1056 -1395 -1202 C
ATOM 1718 OE1 GLU A1049 21.448 12.036 11.909 1.00146.90 O
ANISOU 1718 OE1 GLU A1049 18246 19389 18179 -1079 -1219 -1179 O
ATOM 1719 OE2 GLU A1049 23.546 11.404 12.043 1.00147.97 O
ANISOU 1719 OE2 GLU A1049 17939 19898 18384 -1111 -1657 -1121 O
ATOM 1720 N ASP A1050 23.917 10.754 7.130 1.00129.52 N
ANISOU 1720 N ASP A1050 14762 17470 16979 -671 -1299 -1637 N
ATOM 1721 CA ASP A1050 25.283 10.558 6.644 1.00134.40 C
ANISOU 1721 CA ASP A1050 14967 18438 17659 -647 -1436 -1738 C
ATOM 1722 C ASP A1050 25.418 9.401 5.659 1.00132.53 C
ANISOU 1722 C ASP A1050 14379 18237 17740 -291 -1464 -1899 C
ATOM 1723 O ASP A1050 26.381 8.632 5.716 1.00135.59 O
ANISOU 1723 O ASP A1050 14424 18793 18302 -117 -1667 -1947 O
ATOM 1724 CB ASP A1050 26.268 10.389 7.812 1.00136.88 C
ANISOU 1724 CB ASP A1050 15204 18912 17891 -731 -1714 -1606 C
ATOM 1725 CG ASP A1050 25.895 9.268 8.756 1.00138.42 C
ANISOU 1725 CG ASP A1050 15467 18901 18226 -523 -1900 -1403 C
ATOM 1726 OD1 ASP A1050 26.045 8.088 8.378 1.00139.81 O
ANISOU 1726 OD1 ASP A1050 15371 18995 18757 -214 -2023 -1416 O
ATOM 1727 OD2 ASP A1050 25.462 9.573 9.885 1.00139.75 O
ANISOU 1727 OD2 ASP A1050 15941 19002 18154 -672 -1934 -1228 O
ATOM 1728 N LYS A1051 24.466 9.280 4.742 1.00122.32 N
ANISOU 1728 N LYS A1051 13149 16790 16537 -167 -1279 -2017 N
ATOM 1729 CA LYS A1051 24.603 8.413 3.583 1.00115.40 C
ANISOU 1729 CA LYS A1051 11930 16022 15896 144 -1278 -2283 C
ATOM 1730 C LYS A1051 24.612 9.266 2.320 1.00108.85 C
ANISOU 1730 C LYS A1051 10997 15518 14843 20 -1037 -2428 C
ATOM 1731 O LYS A1051 24.081 10.378 2.295 1.00105.09 O
ANISOU 1731 O LYS A1051 10790 14992 14147 -261 -871 -2286 O
ATOM 1732 CB LYS A1051 23.471 7.377 3.509 1.00117.93 C
ANISOU 1732 CB LYS A1051 12359 15910 16540 416 -1320 -2315 C
ATOM 1733 CG LYS A1051 23.538 6.271 4.558 1.00126.02 C
ANISOU 1733 CG LYS A1051 13366 16633 17883 589 -1600 -2136 C
ATOM 1734 CD LYS A1051 24.590 5.226 4.205 1.00138.31 C
ANISOU 1734 CD LYS A1051 14464 18312 19776 901 -1834 -2356 C
ATOM 1735 CE LYS A1051 24.703 4.156 5.281 1.00148.77 C
ANISOU 1735 CE LYS A1051 15750 19306 21468 1053 -2159 -2096 C
ATOM 1736 NZ LYS A1051 25.511 2.995 4.817 1.00155.65 N
ANISOU 1736 NZ LYS A1051 16165 20160 22816 1434 -2411 -2359 N
ATOM 1737 N SER A1052 25.223 8.736 1.263 1.00107.58 N
ANISOU 1737 N SER A1052 10422 15712 14744 242 -1028 -2707 N
ATOM 1738 CA SER A1052 25.238 9.421 -0.020 1.00100.19 C
ANISOU 1738 CA SER A1052 9328 15186 13553 145 -803 -2815 C
ATOM 1739 C SER A1052 23.846 9.397 -0.653 1.00 98.87 C
ANISOU 1739 C SER A1052 9401 14764 13402 213 -671 -2863 C
ATOM 1740 O SER A1052 23.019 8.545 -0.319 1.00 89.58 O
ANISOU 1740 O SER A1052 8384 13147 12504 427 -770 -2920 O
ATOM 1741 CB SER A1052 26.244 8.760 -0.962 1.00103.65 C
ANISOU 1741 CB SER A1052 9219 16156 14006 410 -817 -3149 C
ATOM 1742 OG SER A1052 27.558 8.770 -0.427 1.00106.44 O
ANISOU 1742 OG SER A1052 9294 16779 14369 358 -942 -3098 O
ATOM 1743 N PRO A1053 23.555 10.328 -1.564 1.00107.56 N
ANISOU 1743 N PRO A1053 10510 16130 14228 15 -467 -2798 N
ATOM 1744 CA PRO A1053 22.421 10.142 -2.472 1.00112.60 C
ANISOU 1744 CA PRO A1053 11231 16686 14864 142 -366 -2915 C
ATOM 1745 C PRO A1053 22.724 9.193 -3.618 1.00108.66 C
ANISOU 1745 C PRO A1053 10325 16591 14370 484 -384 -3345 C
ATOM 1746 O PRO A1053 21.868 8.992 -4.485 1.00106.16 O
ANISOU 1746 O PRO A1053 10026 16294 14016 599 -326 -3500 O
ATOM 1747 CB PRO A1053 22.161 11.568 -2.983 1.00110.80 C
ANISOU 1747 CB PRO A1053 11119 16644 14334 -222 -175 -2626 C
ATOM 1748 CG PRO A1053 23.511 12.176 -3.029 1.00112.50 C
ANISOU 1748 CG PRO A1053 11051 17339 14356 -436 -158 -2523 C
ATOM 1749 CD PRO A1053 24.328 11.531 -1.917 1.00113.14 C
ANISOU 1749 CD PRO A1053 11079 17275 14633 -331 -348 -2599 C
ATOM 1750 N ASP A1054 23.941 8.643 -3.631 1.00109.66 N
ANISOU 1750 N ASP A1054 10070 17063 14535 651 -469 -3560 N
ATOM 1751 CA ASP A1054 24.283 7.504 -4.466 1.00121.98 C
ANISOU 1751 CA ASP A1054 11232 18905 16210 1072 -541 -4075 C
ATOM 1752 C ASP A1054 23.827 6.191 -3.850 1.00127.92 C
ANISOU 1752 C ASP A1054 12072 19032 17499 1411 -801 -4284 C
ATOM 1753 O ASP A1054 23.717 5.188 -4.565 1.00138.42 O
ANISOU 1753 O ASP A1054 13164 20399 19031 1781 -900 -4757 O
ATOM 1754 CB ASP A1054 25.794 7.464 -4.696 1.00133.23 C
ANISOU 1754 CB ASP A1054 12167 20955 17498 1134 -525 -4221 C
ATOM 1755 CG ASP A1054 26.471 8.776 -4.339 1.00132.57 C
ANISOU 1755 CG ASP A1054 12109 21152 17112 676 -402 -3766 C
ATOM 1756 OD1 ASP A1054 25.795 9.826 -4.349 1.00129.27 O
ANISOU 1756 OD1 ASP A1054 12009 20610 16499 328 -277 -3415 O
ATOM 1757 OD2 ASP A1054 27.683 8.760 -4.043 1.00132.47 O
ANISOU 1757 OD2 ASP A1054 11778 21456 17098 664 -454 -3762 O
ATOM 1758 N SER A1055 23.562 6.179 -2.549 1.00125.98 N
ANISOU 1758 N SER A1055 12145 18230 17491 1286 -927 -3939 N
ATOM 1759 CA SER A1055 23.097 4.967 -1.889 1.00124.88 C
ANISOU 1759 CA SER A1055 12083 17484 17882 1554 -1190 -4006 C
ATOM 1760 C SER A1055 21.665 4.672 -2.317 1.00120.43 C
ANISOU 1760 C SER A1055 11749 16543 17467 1617 -1178 -4073 C
ATOM 1761 O SER A1055 20.813 5.566 -2.271 1.00108.25 O
ANISOU 1761 O SER A1055 10527 14919 15683 1342 -1000 -3788 O
ATOM 1762 CB SER A1055 23.177 5.108 -0.370 1.00123.28 C
ANISOU 1762 CB SER A1055 12145 16900 17795 1365 -1308 -3552 C
ATOM 1763 OG SER A1055 22.439 6.228 0.079 1.00119.42 O
ANISOU 1763 OG SER A1055 12065 16301 17010 1002 -1123 -3185 O
ATOM 1764 N PRO A1056 21.365 3.441 -2.732 1.00134.86 N
ANISOU 1764 N PRO A1056 13404 18110 19728 1976 -1386 -4453 N
ATOM 1765 CA PRO A1056 20.008 3.139 -3.213 1.00133.04 C
ANISOU 1765 CA PRO A1056 13352 17539 19660 2024 -1405 -4541 C
ATOM 1766 C PRO A1056 18.939 3.350 -2.162 1.00127.74 C
ANISOU 1766 C PRO A1056 13096 16297 19141 1797 -1407 -4025 C
ATOM 1767 O PRO A1056 17.767 3.533 -2.519 1.00126.94 O
ANISOU 1767 O PRO A1056 13186 16012 19034 1723 -1333 -3972 O
ATOM 1768 CB PRO A1056 20.099 1.661 -3.625 1.00145.41 C
ANISOU 1768 CB PRO A1056 14619 18844 21787 2461 -1712 -5056 C
ATOM 1769 CG PRO A1056 21.562 1.370 -3.740 1.00153.32 C
ANISOU 1769 CG PRO A1056 15225 20251 22778 2673 -1770 -5347 C
ATOM 1770 CD PRO A1056 22.238 2.259 -2.748 1.00147.21 C
ANISOU 1770 CD PRO A1056 14588 19627 21718 2358 -1648 -4827 C
ATOM 1771 N GLU A1057 19.302 3.325 -0.878 1.00112.26 N
ANISOU 1771 N GLU A1057 11257 14100 17296 1691 -1491 -3645 N
ATOM 1772 CA GLU A1057 18.340 3.637 0.173 1.00 96.83 C
ANISOU 1772 CA GLU A1057 9678 11739 15373 1463 -1444 -3148 C
ATOM 1773 C GLU A1057 17.895 5.090 0.088 1.00 87.89 C
ANISOU 1773 C GLU A1057 8822 10843 13730 1141 -1126 -2940 C
ATOM 1774 O GLU A1057 16.694 5.384 0.127 1.00 78.93 O
ANISOU 1774 O GLU A1057 7926 9461 12602 1038 -1018 -2765 O
ATOM 1775 CB GLU A1057 18.943 3.348 1.545 1.00 94.86 C
ANISOU 1775 CB GLU A1057 9468 11323 15253 1413 -1602 -2800 C
ATOM 1776 CG GLU A1057 18.969 1.894 1.948 1.00102.12 C
ANISOU 1776 CG GLU A1057 10206 11791 16805 1677 -1955 -2790 C
ATOM 1777 CD GLU A1057 19.356 1.713 3.401 1.00111.44 C
ANISOU 1777 CD GLU A1057 11469 12827 18046 1569 -2102 -2305 C
ATOM 1778 OE1 GLU A1057 20.540 1.928 3.739 1.00115.62 O
ANISOU 1778 OE1 GLU A1057 11862 13663 18406 1556 -2155 -2307 O
ATOM 1779 OE2 GLU A1057 18.471 1.361 4.205 1.00114.00 O
ANISOU 1779 OE2 GLU A1057 11975 12776 18566 1485 -2166 -1899 O
ATOM 1780 N MET A1058 18.854 6.015 -0.017 1.00 90.52 N
ANISOU 1780 N MET A1058 9100 11631 13662 977 -992 -2940 N
ATOM 1781 CA MET A1058 18.510 7.429 -0.129 1.00 90.82 C
ANISOU 1781 CA MET A1058 9373 11841 13294 667 -733 -2741 C
ATOM 1782 C MET A1058 17.681 7.695 -1.376 1.00100.01 C
ANISOU 1782 C MET A1058 10521 13113 14366 689 -605 -2893 C
ATOM 1783 O MET A1058 16.814 8.576 -1.376 1.00106.43 O
ANISOU 1783 O MET A1058 11587 13814 15037 495 -441 -2675 O
ATOM 1784 CB MET A1058 19.774 8.287 -0.143 1.00 91.00 C
ANISOU 1784 CB MET A1058 9268 12325 12983 481 -663 -2720 C
ATOM 1785 CG MET A1058 19.495 9.780 -0.076 1.00 94.31 C
ANISOU 1785 CG MET A1058 9937 12817 13080 132 -455 -2472 C
ATOM 1786 SD MET A1058 18.987 10.343 1.570 1.00 92.69 S
ANISOU 1786 SD MET A1058 10159 12197 12863 -76 -445 -2139 S
ATOM 1787 CE MET A1058 20.581 10.488 2.381 1.00 95.10 C
ANISOU 1787 CE MET A1058 10316 12780 13039 -196 -594 -2109 C
ATOM 1788 N LYS A1059 17.936 6.944 -2.450 1.00 98.18 N
ANISOU 1788 N LYS A1059 9978 13116 14209 939 -690 -3289 N
ATOM 1789 CA LYS A1059 17.136 7.073 -3.663 1.00 85.59 C
ANISOU 1789 CA LYS A1059 8343 11675 12502 980 -610 -3463 C
ATOM 1790 C LYS A1059 15.766 6.435 -3.496 1.00 84.19 C
ANISOU 1790 C LYS A1059 8342 10954 12692 1076 -709 -3427 C
ATOM 1791 O LYS A1059 14.772 6.953 -4.017 1.00 83.36 O
ANISOU 1791 O LYS A1059 8369 10823 12482 976 -602 -3332 O
ATOM 1792 CB LYS A1059 17.859 6.436 -4.846 1.00 92.53 C
ANISOU 1792 CB LYS A1059 8811 13049 13299 1238 -677 -3967 C
ATOM 1793 CG LYS A1059 19.229 7.012 -5.116 1.00102.63 C
ANISOU 1793 CG LYS A1059 9834 14951 14211 1151 -564 -3997 C
ATOM 1794 CD LYS A1059 19.744 6.489 -6.441 1.00113.55 C
ANISOU 1794 CD LYS A1059 10794 16934 15414 1410 -569 -4513 C
ATOM 1795 CE LYS A1059 21.250 6.344 -6.427 1.00119.41 C
ANISOU 1795 CE LYS A1059 11168 18153 16051 1504 -567 -4685 C
ATOM 1796 NZ LYS A1059 21.713 5.416 -7.502 1.00121.06 N
ANISOU 1796 NZ LYS A1059 10935 18823 16241 1896 -632 -5331 N
ATOM 1797 N ASP A1060 15.698 5.301 -2.792 1.00 92.68 N
ANISOU 1797 N ASP A1060 9390 11593 14230 1260 -933 -3468 N
ATOM 1798 CA ASP A1060 14.403 4.689 -2.517 1.00 97.48 C
ANISOU 1798 CA ASP A1060 10142 11663 15234 1307 -1039 -3349 C
ATOM 1799 C ASP A1060 13.497 5.656 -1.766 1.00 88.54 C
ANISOU 1799 C ASP A1060 9355 10339 13948 1034 -827 -2872 C
ATOM 1800 O ASP A1060 12.279 5.669 -1.974 1.00 86.68 O
ANISOU 1800 O ASP A1060 9227 9863 13845 1006 -796 -2774 O
ATOM 1801 CB ASP A1060 14.583 3.396 -1.726 1.00102.71 C
ANISOU 1801 CB ASP A1060 10707 11875 16443 1495 -1327 -3340 C
ATOM 1802 CG ASP A1060 13.269 2.684 -1.489 1.00104.05 C
ANISOU 1802 CG ASP A1060 10967 11490 17079 1523 -1464 -3184 C
ATOM 1803 OD1 ASP A1060 12.559 2.431 -2.483 1.00106.46 O
ANISOU 1803 OD1 ASP A1060 11191 11767 17491 1613 -1520 -3467 O
ATOM 1804 OD2 ASP A1060 12.937 2.388 -0.321 1.00102.73 O
ANISOU 1804 OD2 ASP A1060 10928 10956 17150 1439 -1520 -2761 O
ATOM 1805 N PHE A1061 14.083 6.482 -0.896 1.00 77.83 N
ANISOU 1805 N PHE A1061 8155 9098 12321 840 -691 -2607 N
ATOM 1806 CA PHE A1061 13.335 7.531 -0.212 1.00 69.47 C
ANISOU 1806 CA PHE A1061 7408 7912 11076 604 -476 -2249 C
ATOM 1807 C PHE A1061 12.697 8.489 -1.209 1.00 72.70 C
ANISOU 1807 C PHE A1061 7871 8487 11265 498 -301 -2268 C
ATOM 1808 O PHE A1061 11.508 8.816 -1.109 1.00 74.11 O
ANISOU 1808 O PHE A1061 8215 8420 11523 442 -203 -2085 O
ATOM 1809 CB PHE A1061 14.281 8.283 0.724 1.00 71.05 C
ANISOU 1809 CB PHE A1061 7721 8276 10997 426 -402 -2087 C
ATOM 1810 CG PHE A1061 13.598 9.234 1.661 1.00 73.07 C
ANISOU 1810 CG PHE A1061 8294 8369 11101 226 -218 -1791 C
ATOM 1811 CD1 PHE A1061 12.800 8.756 2.682 1.00 84.72 C
ANISOU 1811 CD1 PHE A1061 9905 9536 12748 253 -224 -1557 C
ATOM 1812 CD2 PHE A1061 13.789 10.604 1.551 1.00 75.08 C
ANISOU 1812 CD2 PHE A1061 8684 8789 11053 14 -48 -1749 C
ATOM 1813 CE1 PHE A1061 12.182 9.622 3.563 1.00 95.56 C
ANISOU 1813 CE1 PHE A1061 11540 10827 13940 106 -34 -1348 C
ATOM 1814 CE2 PHE A1061 13.175 11.479 2.429 1.00 85.34 C
ANISOU 1814 CE2 PHE A1061 10261 9915 12247 -131 106 -1563 C
ATOM 1815 CZ PHE A1061 12.371 10.988 3.438 1.00 95.70 C
ANISOU 1815 CZ PHE A1061 11704 10980 13677 -69 128 -1394 C
ATOM 1816 N ARG A1062 13.483 8.946 -2.185 1.00 74.83 N
ANISOU 1816 N ARG A1062 7971 9205 11256 468 -266 -2456 N
ATOM 1817 CA ARG A1062 13.013 9.958 -3.126 1.00 75.29 C
ANISOU 1817 CA ARG A1062 8058 9481 11068 329 -118 -2386 C
ATOM 1818 C ARG A1062 11.957 9.388 -4.063 1.00 78.60 C
ANISOU 1818 C ARG A1062 8391 9832 11642 477 -191 -2534 C
ATOM 1819 O ARG A1062 10.871 9.961 -4.214 1.00 70.84 O
ANISOU 1819 O ARG A1062 7554 8678 10683 388 -101 -2331 O
ATOM 1820 CB ARG A1062 14.195 10.515 -3.920 1.00 81.17 C
ANISOU 1820 CB ARG A1062 8587 10796 11457 239 -71 -2487 C
ATOM 1821 CG ARG A1062 15.316 11.057 -3.045 1.00 95.05 C
ANISOU 1821 CG ARG A1062 10388 12639 13089 75 -39 -2359 C
ATOM 1822 CD ARG A1062 15.350 12.576 -3.087 1.00114.75 C
ANISOU 1822 CD ARG A1062 13024 15216 15359 -240 114 -2064 C
ATOM 1823 NE ARG A1062 15.382 13.179 -1.756 1.00131.10 N
ANISOU 1823 NE ARG A1062 15374 16952 17486 -398 147 -1875 N
ATOM 1824 CZ ARG A1062 16.492 13.515 -1.105 1.00135.09 C
ANISOU 1824 CZ ARG A1062 15858 17585 17884 -537 108 -1851 C
ATOM 1825 NH1 ARG A1062 16.410 14.061 0.101 1.00130.10 N
ANISOU 1825 NH1 ARG A1062 15493 16663 17275 -669 123 -1730 N
ATOM 1826 NH2 ARG A1062 17.683 13.304 -1.650 1.00139.67 N
ANISOU 1826 NH2 ARG A1062 16129 18617 18322 -538 52 -1969 N
ATOM 1827 N HIS A1063 12.266 8.265 -4.716 1.00 93.46 N
ANISOU 1827 N HIS A1063 10017 11847 13648 713 -374 -2919 N
ATOM 1828 CA HIS A1063 11.310 7.571 -5.575 1.00 97.05 C
ANISOU 1828 CA HIS A1063 10369 12216 14289 869 -508 -3142 C
ATOM 1829 C HIS A1063 10.004 7.331 -4.829 1.00 90.96 C
ANISOU 1829 C HIS A1063 9802 10859 13901 844 -531 -2877 C
ATOM 1830 O HIS A1063 8.924 7.433 -5.415 1.00 90.95 O
ANISOU 1830 O HIS A1063 9815 10778 13963 833 -541 -2842 O
ATOM 1831 CB HIS A1063 11.900 6.240 -6.063 1.00118.78 C
ANISOU 1831 CB HIS A1063 12830 15053 17246 1163 -751 -3655 C
ATOM 1832 CG HIS A1063 11.143 5.598 -7.185 1.00139.10 C
ANISOU 1832 CG HIS A1063 15246 17684 19923 1327 -916 -4018 C
ATOM 1833 ND1 HIS A1063 10.518 6.319 -8.180 1.00142.73 N
ANISOU 1833 ND1 HIS A1063 15701 18485 20047 1222 -824 -3976 N
ATOM 1834 CD2 HIS A1063 10.944 4.293 -7.485 1.00145.57 C
ANISOU 1834 CD2 HIS A1063 15888 18264 21158 1588 -1202 -4450 C
ATOM 1835 CE1 HIS A1063 9.953 5.486 -9.036 1.00144.11 C
ANISOU 1835 CE1 HIS A1063 15709 18671 20374 1408 -1040 -4381 C
ATOM 1836 NE2 HIS A1063 10.197 4.251 -8.637 1.00145.83 N
ANISOU 1836 NE2 HIS A1063 15823 18517 21069 1633 -1276 -4701 N
ATOM 1837 N GLY A1064 10.101 7.037 -3.530 1.00 83.80 N
ANISOU 1837 N GLY A1064 9028 9591 13221 824 -537 -2659 N
ATOM 1838 CA GLY A1064 8.905 6.804 -2.733 1.00 71.88 C
ANISOU 1838 CA GLY A1064 7673 7601 12037 788 -527 -2359 C
ATOM 1839 C GLY A1064 7.990 8.013 -2.662 1.00 62.38 C
ANISOU 1839 C GLY A1064 6671 6376 10653 611 -286 -2056 C
ATOM 1840 O GLY A1064 6.764 7.877 -2.681 1.00 54.81 O
ANISOU 1840 O GLY A1064 5739 5155 9929 615 -284 -1914 O
ATOM 1841 N PHE A1065 8.566 9.213 -2.575 1.00 60.07 N
ANISOU 1841 N PHE A1065 6500 6333 9991 455 -99 -1951 N
ATOM 1842 CA PHE A1065 7.730 10.407 -2.527 1.00 61.19 C
ANISOU 1842 CA PHE A1065 6818 6400 10030 310 103 -1690 C
ATOM 1843 C PHE A1065 7.302 10.866 -3.916 1.00 63.50 C
ANISOU 1843 C PHE A1065 6998 6928 10201 292 87 -1744 C
ATOM 1844 O PHE A1065 6.273 11.537 -4.042 1.00 59.26 O
ANISOU 1844 O PHE A1065 6547 6241 9728 234 183 -1533 O
ATOM 1845 CB PHE A1065 8.453 11.520 -1.766 1.00 69.49 C
ANISOU 1845 CB PHE A1065 8052 7526 10824 139 267 -1548 C
ATOM 1846 CG PHE A1065 8.262 11.443 -0.276 1.00 77.03 C
ANISOU 1846 CG PHE A1065 9190 8215 11864 124 348 -1388 C
ATOM 1847 CD1 PHE A1065 7.003 11.630 0.275 1.00 76.55 C
ANISOU 1847 CD1 PHE A1065 9247 7875 11965 137 478 -1192 C
ATOM 1848 CD2 PHE A1065 9.325 11.167 0.568 1.00 85.33 C
ANISOU 1848 CD2 PHE A1065 10264 9350 12807 102 295 -1425 C
ATOM 1849 CE1 PHE A1065 6.811 11.548 1.641 1.00 81.85 C
ANISOU 1849 CE1 PHE A1065 10055 8407 12639 128 575 -1043 C
ATOM 1850 CE2 PHE A1065 9.138 11.085 1.936 1.00 86.96 C
ANISOU 1850 CE2 PHE A1065 10625 9397 13020 81 361 -1260 C
ATOM 1851 CZ PHE A1065 7.881 11.275 2.470 1.00 83.98 C
ANISOU 1851 CZ PHE A1065 10362 8794 12754 94 512 -1073 C
ATOM 1852 N ASP A1066 8.061 10.517 -4.961 1.00 74.69 N
ANISOU 1852 N ASP A1066 8201 8749 11429 351 -32 -2019 N
ATOM 1853 CA ASP A1066 7.549 10.633 -6.323 1.00 68.27 C
ANISOU 1853 CA ASP A1066 7234 8216 10490 370 -99 -2104 C
ATOM 1854 C ASP A1066 6.292 9.787 -6.484 1.00 65.62 C
ANISOU 1854 C ASP A1066 6855 7563 10517 500 -243 -2171 C
ATOM 1855 O ASP A1066 5.223 10.298 -6.836 1.00 71.60 O
ANISOU 1855 O ASP A1066 7649 8227 11330 444 -208 -1966 O
ATOM 1856 CB ASP A1066 8.618 10.214 -7.343 1.00 66.91 C
ANISOU 1856 CB ASP A1066 6797 8607 10017 453 -201 -2462 C
ATOM 1857 CG ASP A1066 9.734 11.242 -7.489 1.00 83.08 C
ANISOU 1857 CG ASP A1066 8822 11077 11669 269 -55 -2315 C
ATOM 1858 OD1 ASP A1066 9.520 12.400 -7.082 1.00 89.21 O
ANISOU 1858 OD1 ASP A1066 9785 11704 12406 62 90 -1939 O
ATOM 1859 OD2 ASP A1066 10.815 10.899 -8.027 1.00 92.68 O
ANISOU 1859 OD2 ASP A1066 9809 12768 12639 333 -94 -2582 O
ATOM 1860 N ILE A1067 6.412 8.482 -6.209 1.00 67.75 N
ANISOU 1860 N ILE A1067 7025 7631 11087 669 -429 -2435 N
ATOM 1861 CA ILE A1067 5.276 7.560 -6.284 1.00 79.51 C
ANISOU 1861 CA ILE A1067 8444 8756 13011 770 -612 -2491 C
ATOM 1862 C ILE A1067 4.086 8.101 -5.498 1.00 77.72 C
ANISOU 1862 C ILE A1067 8389 8151 12989 659 -454 -2050 C
ATOM 1863 O ILE A1067 2.944 8.091 -5.976 1.00 78.15 O
ANISOU 1863 O ILE A1067 8387 8091 13216 656 -513 -1972 O
ATOM 1864 CB ILE A1067 5.692 6.165 -5.784 1.00 87.57 C
ANISOU 1864 CB ILE A1067 9359 9493 14422 933 -836 -2734 C
ATOM 1865 CG1 ILE A1067 6.780 5.594 -6.687 1.00 98.86 C
ANISOU 1865 CG1 ILE A1067 10568 11313 15683 1100 -1002 -3258 C
ATOM 1866 CG2 ILE A1067 4.492 5.219 -5.742 1.00 86.56 C
ANISOU 1866 CG2 ILE A1067 9149 8908 14832 992 -1049 -2718 C
ATOM 1867 CD1 ILE A1067 6.273 5.156 -8.027 1.00113.68 C
ANISOU 1867 CD1 ILE A1067 12244 13404 17545 1213 -1206 -3652 C
ATOM 1868 N LEU A1068 4.342 8.586 -4.278 1.00 70.94 N
ANISOU 1868 N LEU A1068 7722 7131 12101 575 -253 -1779 N
ATOM 1869 CA LEU A1068 3.293 9.178 -3.450 1.00 73.89 C
ANISOU 1869 CA LEU A1068 8244 7219 12612 496 -57 -1407 C
ATOM 1870 C LEU A1068 2.622 10.365 -4.139 1.00 67.52 C
ANISOU 1870 C LEU A1068 7476 6527 11651 418 68 -1259 C
ATOM 1871 O LEU A1068 1.398 10.389 -4.313 1.00 75.58 O
ANISOU 1871 O LEU A1068 8445 7367 12905 433 67 -1106 O
ATOM 1872 CB LEU A1068 3.873 9.603 -2.097 1.00 82.86 C
ANISOU 1872 CB LEU A1068 9575 8287 13621 428 136 -1233 C
ATOM 1873 CG LEU A1068 2.892 10.233 -1.111 1.00 86.59 C
ANISOU 1873 CG LEU A1068 10191 8538 14173 378 374 -915 C
ATOM 1874 CD1 LEU A1068 1.703 9.312 -0.956 1.00 89.43 C
ANISOU 1874 CD1 LEU A1068 10412 8627 14942 440 294 -766 C
ATOM 1875 CD2 LEU A1068 3.559 10.488 0.237 1.00 87.50 C
ANISOU 1875 CD2 LEU A1068 10479 8658 14108 327 521 -822 C
ATOM 1876 N VAL A1069 3.408 11.379 -4.497 1.00 56.11 N
ANISOU 1876 N VAL A1069 6102 5364 9851 322 164 -1258 N
ATOM 1877 CA VAL A1069 2.904 12.613 -5.099 1.00 68.98 C
ANISOU 1877 CA VAL A1069 7769 7075 11365 227 261 -1049 C
ATOM 1878 C VAL A1069 1.976 12.276 -6.257 1.00 77.62 C
ANISOU 1878 C VAL A1069 8675 8258 12558 281 91 -1074 C
ATOM 1879 O VAL A1069 0.865 12.817 -6.365 1.00 78.75 O
ANISOU 1879 O VAL A1069 8820 8229 12873 270 140 -836 O
ATOM 1880 CB VAL A1069 4.057 13.519 -5.575 1.00 73.73 C
ANISOU 1880 CB VAL A1069 8393 8029 11593 93 302 -1047 C
ATOM 1881 CG1 VAL A1069 3.535 14.570 -6.544 1.00 78.82 C
ANISOU 1881 CG1 VAL A1069 8990 8809 12150 -6 305 -807 C
ATOM 1882 CG2 VAL A1069 4.748 14.173 -4.390 1.00 70.76 C
ANISOU 1882 CG2 VAL A1069 8224 7501 11159 2 468 -970 C
ATOM 1883 N GLY A1070 2.435 11.388 -7.135 1.00 76.55 N
ANISOU 1883 N GLY A1070 8358 8412 12313 354 -123 -1393 N
ATOM 1884 CA GLY A1070 1.603 10.917 -8.222 1.00 78.81 C
ANISOU 1884 CA GLY A1070 8454 8816 12673 414 -333 -1503 C
ATOM 1885 C GLY A1070 0.262 10.396 -7.743 1.00 88.01 C
ANISOU 1885 C GLY A1070 9597 9529 14315 467 -381 -1372 C
ATOM 1886 O GLY A1070 -0.775 10.721 -8.331 1.00 97.57 O
ANISOU 1886 O GLY A1070 10724 10729 15620 448 -439 -1214 O
ATOM 1887 N GLN A1071 0.261 9.604 -6.665 1.00 91.46 N
ANISOU 1887 N GLN A1071 10083 9611 15058 518 -363 -1387 N
ATOM 1888 CA GLN A1071 -0.997 9.079 -6.138 1.00 97.51 C
ANISOU 1888 CA GLN A1071 10788 9975 16288 540 -393 -1197 C
ATOM 1889 C GLN A1071 -1.882 10.189 -5.579 1.00 93.76 C
ANISOU 1889 C GLN A1071 10415 9348 15861 483 -124 -798 C
ATOM 1890 O GLN A1071 -3.112 10.124 -5.693 1.00 95.62 O
ANISOU 1890 O GLN A1071 10530 9410 16393 493 -155 -621 O
ATOM 1891 CB GLN A1071 -0.726 8.020 -5.070 1.00101.74 C
ANISOU 1891 CB GLN A1071 11330 10209 17117 581 -432 -1213 C
ATOM 1892 CG GLN A1071 -0.100 6.758 -5.625 1.00105.79 C
ANISOU 1892 CG GLN A1071 11688 10739 17768 679 -760 -1627 C
ATOM 1893 CD GLN A1071 -0.190 5.605 -4.658 1.00104.22 C
ANISOU 1893 CD GLN A1071 11435 10127 18035 707 -878 -1541 C
ATOM 1894 OE1 GLN A1071 -0.658 5.764 -3.533 1.00102.75 O
ANISOU 1894 OE1 GLN A1071 11329 9727 17983 637 -684 -1145 O
ATOM 1895 NE2 GLN A1071 0.255 4.429 -5.093 1.00105.38 N
ANISOU 1895 NE2 GLN A1071 11425 10172 18442 814 -1210 -1908 N
ATOM 1896 N ILE A1072 -1.281 11.209 -4.961 1.00 90.80 N
ANISOU 1896 N ILE A1072 10241 9025 15234 432 127 -678 N
ATOM 1897 CA ILE A1072 -2.062 12.374 -4.546 1.00 90.53 C
ANISOU 1897 CA ILE A1072 10294 8848 15257 411 363 -384 C
ATOM 1898 C ILE A1072 -2.738 13.015 -5.756 1.00 85.54 C
ANISOU 1898 C ILE A1072 9541 8338 14621 394 256 -277 C
ATOM 1899 O ILE A1072 -3.944 13.295 -5.739 1.00 79.17 O
ANISOU 1899 O ILE A1072 8643 7350 14090 433 298 -61 O
ATOM 1900 CB ILE A1072 -1.181 13.389 -3.790 1.00100.95 C
ANISOU 1900 CB ILE A1072 11848 10192 16317 354 589 -356 C
ATOM 1901 CG1 ILE A1072 -0.767 12.858 -2.415 1.00112.55 C
ANISOU 1901 CG1 ILE A1072 13430 11542 17793 373 717 -387 C
ATOM 1902 CG2 ILE A1072 -1.909 14.719 -3.629 1.00102.82 C
ANISOU 1902 CG2 ILE A1072 12155 10275 16639 354 777 -132 C
ATOM 1903 CD1 ILE A1072 -0.179 13.918 -1.512 1.00120.79 C
ANISOU 1903 CD1 ILE A1072 14700 12571 18624 325 944 -369 C
ATOM 1904 N ASP A1073 -1.969 13.252 -6.827 1.00 90.78 N
ANISOU 1904 N ASP A1073 10172 9358 14961 335 113 -400 N
ATOM 1905 CA ASP A1073 -2.523 13.878 -8.026 1.00 99.63 C
ANISOU 1905 CA ASP A1073 11164 10683 16009 296 -15 -246 C
ATOM 1906 C ASP A1073 -3.653 13.046 -8.621 1.00104.91 C
ANISOU 1906 C ASP A1073 11613 11309 16940 361 -237 -284 C
ATOM 1907 O ASP A1073 -4.687 13.584 -9.031 1.00109.13 O
ANISOU 1907 O ASP A1073 12045 11781 17640 362 -271 -29 O
ATOM 1908 CB ASP A1073 -1.423 14.095 -9.068 1.00104.11 C
ANISOU 1908 CB ASP A1073 11690 11754 16113 210 -132 -371 C
ATOM 1909 CG ASP A1073 -0.319 15.020 -8.578 1.00112.83 C
ANISOU 1909 CG ASP A1073 12973 12904 16992 103 55 -281 C
ATOM 1910 OD1 ASP A1073 -0.624 16.009 -7.883 1.00115.94 O
ANISOU 1910 OD1 ASP A1073 13511 12984 17558 70 233 -31 O
ATOM 1911 OD2 ASP A1073 0.860 14.758 -8.901 1.00116.86 O
ANISOU 1911 OD2 ASP A1073 13461 13770 17170 58 13 -485 O
ATOM 1912 N ASP A1074 -3.465 11.726 -8.686 1.00110.59 N
ANISOU 1912 N ASP A1074 12238 12039 17741 416 -421 -606 N
ATOM 1913 CA ASP A1074 -4.526 10.851 -9.176 1.00118.53 C
ANISOU 1913 CA ASP A1074 13026 12942 19068 459 -674 -677 C
ATOM 1914 C ASP A1074 -5.746 10.906 -8.268 1.00115.03 C
ANISOU 1914 C ASP A1074 12547 12067 19091 477 -531 -355 C
ATOM 1915 O ASP A1074 -6.886 10.926 -8.745 1.00115.04 O
ANISOU 1915 O ASP A1074 12367 12010 19335 478 -656 -202 O
ATOM 1916 CB ASP A1074 -4.005 9.421 -9.291 1.00126.74 C
ANISOU 1916 CB ASP A1074 13980 13978 20198 520 -916 -1111 C
ATOM 1917 CG ASP A1074 -2.844 9.309 -10.247 1.00133.71 C
ANISOU 1917 CG ASP A1074 14839 15358 20607 542 -1048 -1490 C
ATOM 1918 OD1 ASP A1074 -2.428 10.351 -10.795 1.00136.57 O
ANISOU 1918 OD1 ASP A1074 15249 16092 20548 473 -940 -1348 O
ATOM 1919 OD2 ASP A1074 -2.350 8.184 -10.456 1.00139.00 O
ANISOU 1919 OD2 ASP A1074 15417 16052 21346 630 -1263 -1920 O
ATOM 1920 N ALA A1075 -5.526 10.926 -6.954 1.00109.41 N
ANISOU 1920 N ALA A1075 11983 11102 18488 490 -270 -245 N
ATOM 1921 CA ALA A1075 -6.642 11.108 -6.039 1.00100.78 C
ANISOU 1921 CA ALA A1075 10837 9702 17754 517 -68 73 C
ATOM 1922 C ALA A1075 -7.222 12.509 -6.158 1.00 93.11 C
ANISOU 1922 C ALA A1075 9894 8734 16751 541 118 334 C
ATOM 1923 O ALA A1075 -8.399 12.720 -5.848 1.00 94.10 O
ANISOU 1923 O ALA A1075 9876 8677 17200 591 215 578 O
ATOM 1924 CB ALA A1075 -6.195 10.823 -4.605 1.00 98.22 C
ANISOU 1924 CB ALA A1075 10654 9212 17453 527 172 119 C
ATOM 1925 N LEU A1076 -6.421 13.476 -6.609 1.00 87.49 N
ANISOU 1925 N LEU A1076 9334 8214 15692 505 157 307 N
ATOM 1926 CA LEU A1076 -6.948 14.818 -6.820 1.00 97.95 C
ANISOU 1926 CA LEU A1076 10668 9483 17065 524 269 575 C
ATOM 1927 C LEU A1076 -7.855 14.873 -8.037 1.00117.04 C
ANISOU 1927 C LEU A1076 12846 12023 19601 517 9 724 C
ATOM 1928 O LEU A1076 -8.787 15.684 -8.080 1.00127.00 O
ANISOU 1928 O LEU A1076 14012 13130 21111 574 71 1005 O
ATOM 1929 CB LEU A1076 -5.802 15.817 -6.962 1.00100.22 C
ANISOU 1929 CB LEU A1076 11163 9909 17007 447 343 560 C
ATOM 1930 CG LEU A1076 -5.362 16.433 -5.637 1.00 97.19 C
ANISOU 1930 CG LEU A1076 11007 9295 16626 477 651 537 C
ATOM 1931 CD1 LEU A1076 -4.025 17.135 -5.800 1.00 83.49 C
ANISOU 1931 CD1 LEU A1076 9457 7715 14551 357 656 467 C
ATOM 1932 CD2 LEU A1076 -6.430 17.394 -5.129 1.00105.64 C
ANISOU 1932 CD2 LEU A1076 12047 10060 18033 593 842 752 C
ATOM 1933 N LYS A1077 -7.600 14.023 -9.031 1.00118.83 N
ANISOU 1933 N LYS A1077 12957 12539 19656 462 -297 517 N
ATOM 1934 CA LYS A1077 -8.487 13.957 -10.183 1.00119.69 C
ANISOU 1934 CA LYS A1077 12820 12817 19841 449 -585 621 C
ATOM 1935 C LYS A1077 -9.861 13.428 -9.798 1.00117.23 C
ANISOU 1935 C LYS A1077 12295 12202 20043 509 -615 753 C
ATOM 1936 O LYS A1077 -10.875 13.875 -10.348 1.00119.55 O
ANISOU 1936 O LYS A1077 12395 12496 20532 526 -726 1009 O
ATOM 1937 CB LYS A1077 -7.862 13.083 -11.269 1.00119.83 C
ANISOU 1937 CB LYS A1077 12756 13253 19522 397 -907 265 C
ATOM 1938 CG LYS A1077 -8.732 12.947 -12.496 1.00126.64 C
ANISOU 1938 CG LYS A1077 13360 14367 20390 374 -1246 316 C
ATOM 1939 CD LYS A1077 -7.946 12.412 -13.673 1.00134.77 C
ANISOU 1939 CD LYS A1077 14326 15955 20926 334 -1526 -57 C
ATOM 1940 CE LYS A1077 -7.822 10.905 -13.628 1.00142.08 C
ANISOU 1940 CE LYS A1077 15175 16802 22006 388 -1737 -569 C
ATOM 1941 NZ LYS A1077 -7.110 10.419 -14.836 1.00146.28 N
ANISOU 1941 NZ LYS A1077 15612 17926 22041 391 -2013 -1011 N
ATOM 1942 N LEU A1078 -9.918 12.492 -8.848 1.00116.33 N
ANISOU 1942 N LEU A1078 12187 11844 20169 531 -524 632 N
ATOM 1943 CA LEU A1078 -11.202 11.932 -8.448 1.00118.14 C
ANISOU 1943 CA LEU A1078 12172 11815 20902 556 -547 807 C
ATOM 1944 C LEU A1078 -12.040 12.956 -7.689 1.00121.48 C
ANISOU 1944 C LEU A1078 12559 12037 21560 651 -216 1163 C
ATOM 1945 O LEU A1078 -13.263 13.017 -7.866 1.00123.28 O
ANISOU 1945 O LEU A1078 12518 12173 22148 686 -273 1396 O
ATOM 1946 CB LEU A1078 -10.985 10.673 -7.607 1.00115.07 C
ANISOU 1946 CB LEU A1078 11778 11228 20716 527 -545 662 C
ATOM 1947 N ALA A1079 -11.403 13.775 -6.848 1.00121.76 N
ANISOU 1947 N ALA A1079 12842 12008 21412 707 119 1178 N
ATOM 1948 CA ALA A1079 -12.152 14.758 -6.072 1.00124.03 C
ANISOU 1948 CA ALA A1079 13095 12102 21927 839 442 1417 C
ATOM 1949 C ALA A1079 -12.732 15.846 -6.968 1.00137.29 C
ANISOU 1949 C ALA A1079 14666 13790 23709 891 332 1635 C
ATOM 1950 O ALA A1079 -13.834 16.344 -6.712 1.00146.08 O
ANISOU 1950 O ALA A1079 15576 14741 25187 1017 453 1862 O
ATOM 1951 CB ALA A1079 -11.262 15.366 -4.988 1.00117.98 C
ANISOU 1951 CB ALA A1079 12631 11273 20925 885 779 1300 C
ATOM 1952 N ASN A1080 -12.010 16.226 -8.025 1.00137.92 N
ANISOU 1952 N ASN A1080 14844 14083 23474 797 99 1599 N
ATOM 1953 CA ASN A1080 -12.548 17.213 -8.954 1.00142.01 C
ANISOU 1953 CA ASN A1080 15232 14639 24087 818 -60 1887 C
ATOM 1954 C ASN A1080 -13.607 16.612 -9.867 1.00141.27 C
ANISOU 1954 C ASN A1080 14805 14673 24197 793 -385 2015 C
ATOM 1955 O ASN A1080 -14.525 17.319 -10.292 1.00145.88 O
ANISOU 1955 O ASN A1080 15185 15189 25056 864 -466 2327 O
ATOM 1956 CB ASN A1080 -11.425 17.832 -9.779 1.00148.12 C
ANISOU 1956 CB ASN A1080 16185 15667 24426 693 -200 1887 C
ATOM 1957 CG ASN A1080 -10.905 19.116 -9.173 1.00154.84 C
ANISOU 1957 CG ASN A1080 17252 16279 25302 735 45 1988 C
ATOM 1958 OD1 ASN A1080 -11.667 19.903 -8.609 1.00160.72 O
ANISOU 1958 OD1 ASN A1080 17939 16686 26443 888 217 2152 O
ATOM 1959 ND2 ASN A1080 -9.600 19.336 -9.284 1.00154.76 N
ANISOU 1959 ND2 ASN A1080 17468 16435 24898 607 51 1866 N
ATOM 1960 N GLU A1081 -13.503 15.319 -10.179 1.00137.03 N
ANISOU 1960 N GLU A1081 14194 14298 23571 700 -604 1769 N
ATOM 1961 CA GLU A1081 -14.540 14.654 -10.958 1.00140.44 C
ANISOU 1961 CA GLU A1081 14299 14819 24242 664 -941 1834 C
ATOM 1962 C GLU A1081 -15.868 14.569 -10.220 1.00145.10 C
ANISOU 1962 C GLU A1081 14624 15104 25403 762 -792 2075 C
ATOM 1963 O GLU A1081 -16.877 14.216 -10.834 1.00149.45 O
ANISOU 1963 O GLU A1081 14859 15695 26231 735 -1065 2207 O
ATOM 1964 CB GLU A1081 -14.096 13.243 -11.348 1.00144.48 C
ANISOU 1964 CB GLU A1081 14794 15493 24609 554 -1222 1442 C
ATOM 1965 CG GLU A1081 -13.139 13.182 -12.516 1.00150.60 C
ANISOU 1965 CG GLU A1081 15667 16720 24835 469 -1495 1191 C
ATOM 1966 CD GLU A1081 -12.985 11.774 -13.042 1.00157.98 C
ANISOU 1966 CD GLU A1081 16498 17793 25732 407 -1842 752 C
ATOM 1967 OE1 GLU A1081 -13.960 10.999 -12.952 1.00161.93 O
ANISOU 1967 OE1 GLU A1081 16760 18080 26686 390 -2019 755 O
ATOM 1968 OE2 GLU A1081 -11.893 11.437 -13.539 1.00158.77 O
ANISOU 1968 OE2 GLU A1081 16733 18206 25386 379 -1946 392 O
ATOM 1969 N GLY A1082 -15.893 14.873 -8.927 1.00142.30 N
ANISOU 1969 N GLY A1082 14364 14496 25209 871 -371 2126 N
ATOM 1970 CA GLY A1082 -17.093 14.754 -8.129 1.00143.50 C
ANISOU 1970 CA GLY A1082 14236 14440 25847 972 -169 2344 C
ATOM 1971 C GLY A1082 -17.268 13.419 -7.442 1.00142.73 C
ANISOU 1971 C GLY A1082 14030 14274 25929 881 -149 2263 C
ATOM 1972 O GLY A1082 -18.227 13.257 -6.676 1.00145.51 O
ANISOU 1972 O GLY A1082 14175 14560 26553 885 66 2451 O
ATOM 1973 N LYS A1083 -16.377 12.456 -7.690 1.00137.66 N
ANISOU 1973 N LYS A1083 13547 13706 25052 739 -363 1974 N
ATOM 1974 CA LYS A1083 -16.438 11.146 -7.042 1.00133.47 C
ANISOU 1974 CA LYS A1083 12920 13046 24746 637 -397 1922 C
ATOM 1975 C LYS A1083 -15.844 11.273 -5.643 1.00128.07 C
ANISOU 1975 C LYS A1083 12454 12292 23916 694 46 1937 C
ATOM 1976 O LYS A1083 -14.703 10.895 -5.374 1.00124.16 O
ANISOU 1976 O LYS A1083 12231 11823 23122 645 53 1700 O
ATOM 1977 CB LYS A1083 -15.711 10.098 -7.874 1.00130.57 C
ANISOU 1977 CB LYS A1083 12621 12749 24239 501 -828 1565 C
ATOM 1978 N VAL A1084 -16.655 11.821 -4.736 1.00124.68 N
ANISOU 1978 N VAL A1084 11884 11826 23662 797 419 2202 N
ATOM 1979 CA VAL A1084 -16.236 12.030 -3.354 1.00114.38 C
ANISOU 1979 CA VAL A1084 10748 10536 22175 868 862 2217 C
ATOM 1980 C VAL A1084 -15.776 10.719 -2.725 1.00101.78 C
ANISOU 1980 C VAL A1084 9157 8886 20629 727 801 2223 C
ATOM 1981 O VAL A1084 -14.789 10.680 -1.981 1.00 93.75 O
ANISOU 1981 O VAL A1084 8418 7918 19283 725 977 2093 O
ATOM 1982 CB VAL A1084 -17.394 12.662 -2.558 1.00124.15 C
ANISOU 1982 CB VAL A1084 11741 11816 23614 1000 1241 2477 C
ATOM 1983 CG1 VAL A1084 -16.907 13.246 -1.242 1.00123.92 C
ANISOU 1983 CG1 VAL A1084 11905 11846 23332 1158 1720 2414 C
ATOM 1984 CG2 VAL A1084 -18.104 13.713 -3.404 1.00131.59 C
ANISOU 1984 CG2 VAL A1084 12600 12774 24623 1079 1158 2516 C
ATOM 1985 N LYS A1085 -16.468 9.621 -3.035 1.00106.49 N
ANISOU 1985 N LYS A1085 9441 9374 21647 584 510 2377 N
ATOM 1986 CA LYS A1085 -16.241 8.360 -2.334 1.00113.74 C
ANISOU 1986 CA LYS A1085 10292 10189 22734 429 442 2488 C
ATOM 1987 C LYS A1085 -15.010 7.650 -2.874 1.00106.36 C
ANISOU 1987 C LYS A1085 9618 9173 21622 345 95 2119 C
ATOM 1988 O LYS A1085 -14.199 7.115 -2.108 1.00 92.19 O
ANISOU 1988 O LYS A1085 7983 7348 19699 298 166 2102 O
ATOM 1989 CB LYS A1085 -17.473 7.461 -2.464 1.00130.69 C
ANISOU 1989 CB LYS A1085 11972 12192 25492 288 225 2812 C
ATOM 1990 CG LYS A1085 -18.798 8.209 -2.564 1.00136.44 C
ANISOU 1990 CG LYS A1085 12370 13009 26461 387 402 3082 C
ATOM 1991 CD LYS A1085 -19.155 8.563 -4.014 1.00137.89 C
ANISOU 1991 CD LYS A1085 12521 13192 26680 377 24 2884 C
ATOM 1992 CE LYS A1085 -20.125 9.735 -4.071 1.00142.39 C
ANISOU 1992 CE LYS A1085 12969 13900 27234 511 280 3057 C
ATOM 1993 NZ LYS A1085 -20.529 10.081 -5.463 1.00147.35 N
ANISOU 1993 NZ LYS A1085 13541 14549 27899 494 -104 2953 N
ATOM 1994 N GLU A1086 -14.871 7.620 -4.200 1.00124.85 N
ANISOU 1994 N GLU A1086 11976 11515 23947 334 -291 1823 N
ATOM 1995 CA GLU A1086 -13.673 7.065 -4.815 1.00134.74 C
ANISOU 1995 CA GLU A1086 13455 12768 24970 301 -595 1396 C
ATOM 1996 C GLU A1086 -12.422 7.772 -4.320 1.00122.49 C
ANISOU 1996 C GLU A1086 12287 11379 22875 388 -305 1233 C
ATOM 1997 O GLU A1086 -11.383 7.138 -4.113 1.00121.56 O
ANISOU 1997 O GLU A1086 12334 11228 22626 360 -402 1019 O
ATOM 1998 CB GLU A1086 -13.763 7.184 -6.329 1.00156.83 C
ANISOU 1998 CB GLU A1086 16201 15690 27697 305 -980 1101 C
ATOM 1999 CG GLU A1086 -14.973 6.542 -6.927 1.00175.06 C
ANISOU 1999 CG GLU A1086 18132 17862 30521 212 -1323 1209 C
ATOM 2000 CD GLU A1086 -14.790 6.306 -8.401 1.00184.06 C
ANISOU 2000 CD GLU A1086 19244 19159 31532 197 -1793 795 C
ATOM 2001 OE1 GLU A1086 -13.820 5.617 -8.778 1.00184.93 O
ANISOU 2001 OE1 GLU A1086 19492 19285 31489 194 -2032 364 O
ATOM 2002 OE2 GLU A1086 -15.605 6.825 -9.186 1.00186.63 O
ANISOU 2002 OE2 GLU A1086 19393 19629 31887 202 -1924 891 O
ATOM 2003 N ALA A1087 -12.502 9.088 -4.140 1.00105.54 N
ANISOU 2003 N ALA A1087 10267 9381 20450 496 24 1323 N
ATOM 2004 CA ALA A1087 -11.370 9.897 -3.706 1.00 93.03 C
ANISOU 2004 CA ALA A1087 9034 7932 18383 561 279 1168 C
ATOM 2005 C ALA A1087 -10.788 9.418 -2.382 1.00 82.65 C
ANISOU 2005 C ALA A1087 7839 6578 16985 538 500 1234 C
ATOM 2006 O ALA A1087 -9.647 8.948 -2.332 1.00 84.60 O
ANISOU 2006 O ALA A1087 8272 6850 17022 501 386 1010 O
ATOM 2007 CB ALA A1087 -11.797 11.361 -3.592 1.00 94.15 C
ANISOU 2007 CB ALA A1087 9231 8138 18405 682 580 1297 C
ATOM 2008 N GLN A1088 -11.568 9.551 -1.305 1.00 81.30 N
ANISOU 2008 N GLN A1088 7540 6394 16956 568 819 1552 N
ATOM 2009 CA GLN A1088 -11.117 9.113 0.013 1.00 84.33 C
ANISOU 2009 CA GLN A1088 8003 6823 17216 534 1040 1686 C
ATOM 2010 C GLN A1088 -10.663 7.653 0.001 1.00 90.01 C
ANISOU 2010 C GLN A1088 8650 7385 18166 395 705 1699 C
ATOM 2011 O GLN A1088 -9.712 7.285 0.702 1.00 81.21 O
ANISOU 2011 O GLN A1088 7706 6306 16844 365 739 1667 O
ATOM 2012 CB GLN A1088 -12.237 9.332 1.036 1.00 83.18 C
ANISOU 2012 CB GLN A1088 7625 6764 17214 578 1406 2059 C
ATOM 2013 CG GLN A1088 -13.569 8.711 0.632 1.00 91.81 C
ANISOU 2013 CG GLN A1088 8301 7732 18853 511 1250 2356 C
ATOM 2014 CD GLN A1088 -14.764 9.452 1.199 1.00112.47 C
ANISOU 2014 CD GLN A1088 10673 10491 21569 631 1635 2618 C
ATOM 2015 OE1 GLN A1088 -15.918 9.133 0.896 1.00117.77 O
ANISOU 2015 OE1 GLN A1088 10971 11097 22677 593 1553 2878 O
ATOM 2016 NE2 GLN A1088 -14.493 10.454 2.024 1.00123.00 N
ANISOU 2016 NE2 GLN A1088 12197 12024 22515 789 2048 2519 N
ATOM 2017 N ALA A1089 -11.326 6.808 -0.793 1.00 95.86 N
ANISOU 2017 N ALA A1089 9125 7925 19371 313 345 1735 N
ATOM 2018 CA ALA A1089 -10.871 5.434 -0.982 1.00100.07 C
ANISOU 2018 CA ALA A1089 9585 8332 20104 188 -52 1628 C
ATOM 2019 C ALA A1089 -9.441 5.402 -1.513 1.00 95.60 C
ANISOU 2019 C ALA A1089 9307 7811 19205 244 -228 1168 C
ATOM 2020 O ALA A1089 -8.563 4.745 -0.943 1.00 99.19 O
ANISOU 2020 O ALA A1089 9857 8240 19589 215 -292 1133 O
ATOM 2021 CB ALA A1089 -11.820 4.698 -1.931 1.00107.95 C
ANISOU 2021 CB ALA A1089 10265 9182 21569 98 -444 1607 C
ATOM 2022 N ALA A1090 -9.192 6.124 -2.609 1.00100.41 N
ANISOU 2022 N ALA A1090 10025 8497 19630 332 -309 847 N
ATOM 2023 CA ALA A1090 -7.839 6.222 -3.150 1.00105.96 C
ANISOU 2023 CA ALA A1090 10962 9332 19965 391 -428 424 C
ATOM 2024 C ALA A1090 -6.879 6.901 -2.178 1.00 93.98 C
ANISOU 2024 C ALA A1090 9725 7973 18008 423 -88 462 C
ATOM 2025 O ALA A1090 -5.668 6.665 -2.242 1.00 78.94 O
ANISOU 2025 O ALA A1090 7974 6145 15876 444 -183 196 O
ATOM 2026 CB ALA A1090 -7.859 6.974 -4.481 1.00115.52 C
ANISOU 2026 CB ALA A1090 12198 10770 20925 438 -540 161 C
ATOM 2027 N ALA A1091 -7.391 7.750 -1.282 1.00 97.42 N
ANISOU 2027 N ALA A1091 10213 8478 18322 439 298 753 N
ATOM 2028 CA ALA A1091 -6.522 8.408 -0.309 1.00 96.73 C
ANISOU 2028 CA ALA A1091 10388 8548 17817 465 599 748 C
ATOM 2029 C ALA A1091 -5.944 7.406 0.680 1.00 99.00 C
ANISOU 2029 C ALA A1091 10680 8774 18160 407 557 876 C
ATOM 2030 O ALA A1091 -4.794 7.548 1.113 1.00 92.90 O
ANISOU 2030 O ALA A1091 10118 8122 17056 413 604 733 O
ATOM 2031 CB ALA A1091 -7.288 9.508 0.424 1.00 94.22 C
ANISOU 2031 CB ALA A1091 10095 8319 17386 525 1003 959 C
ATOM 2032 N GLU A1092 -6.726 6.385 1.044 1.00105.58 N
ANISOU 2032 N GLU A1092 11259 9418 19437 336 444 1186 N
ATOM 2033 CA GLU A1092 -6.194 5.311 1.877 1.00112.98 C
ANISOU 2033 CA GLU A1092 12159 10252 20517 262 322 1376 C
ATOM 2034 C GLU A1092 -5.061 4.588 1.167 1.00115.62 C
ANISOU 2034 C GLU A1092 12558 10456 20918 289 -59 997 C
ATOM 2035 O GLU A1092 -4.075 4.191 1.800 1.00116.88 O
ANISOU 2035 O GLU A1092 12820 10634 20957 285 -101 1002 O
ATOM 2036 CB GLU A1092 -7.300 4.322 2.253 1.00122.89 C
ANISOU 2036 CB GLU A1092 13080 11290 22324 147 215 1827 C
ATOM 2037 CG GLU A1092 -6.816 3.054 2.958 1.00134.30 C
ANISOU 2037 CG GLU A1092 14426 12636 23964 43 -16 2056 C
ATOM 2038 CD GLU A1092 -6.594 3.246 4.452 1.00141.92 C
ANISOU 2038 CD GLU A1092 15461 13780 24682 -2 321 2502 C
ATOM 2039 OE1 GLU A1092 -6.731 4.384 4.942 1.00140.99 O
ANISOU 2039 OE1 GLU A1092 15493 14011 24067 66 739 2481 O
ATOM 2040 OE2 GLU A1092 -6.288 2.253 5.141 1.00145.90 O
ANISOU 2040 OE2 GLU A1092 15857 14161 25416 -106 149 2843 O
ATOM 2041 N GLN A1093 -5.182 4.407 -0.151 1.00118.80 N
ANISOU 2041 N GLN A1093 12881 10834 21423 320 -341 640 N
ATOM 2042 CA GLN A1093 -4.088 3.818 -0.915 1.00123.86 C
ANISOU 2042 CA GLN A1093 13565 11478 22019 380 -664 188 C
ATOM 2043 C GLN A1093 -2.819 4.653 -0.795 1.00115.65 C
ANISOU 2043 C GLN A1093 12794 10640 20509 461 -481 -36 C
ATOM 2044 O GLN A1093 -1.709 4.108 -0.758 1.00113.06 O
ANISOU 2044 O GLN A1093 12506 10307 20142 510 -649 -253 O
ATOM 2045 CB GLN A1093 -4.487 3.667 -2.380 1.00136.06 C
ANISOU 2045 CB GLN A1093 14978 13018 23699 418 -950 -177 C
ATOM 2046 CG GLN A1093 -3.451 2.946 -3.202 1.00143.36 C
ANISOU 2046 CG GLN A1093 15887 13965 24617 511 -1290 -692 C
ATOM 2047 CD GLN A1093 -3.974 2.563 -4.555 1.00143.32 C
ANISOU 2047 CD GLN A1093 15700 13928 24829 551 -1626 -1060 C
ATOM 2048 OE1 GLN A1093 -3.844 3.314 -5.521 1.00135.28 O
ANISOU 2048 OE1 GLN A1093 14732 13121 23546 634 -1612 -1350 O
ATOM 2049 NE2 GLN A1093 -4.578 1.385 -4.637 1.00148.49 N
ANISOU 2049 NE2 GLN A1093 16120 14362 25938 482 -1948 -1041 N
ATOM 2050 N LEU A1094 -2.961 5.980 -0.743 1.00110.01 N
ANISOU 2050 N LEU A1094 12243 10176 19380 460 -153 9 N
ATOM 2051 CA LEU A1094 -1.810 6.848 -0.516 1.00 97.15 C
ANISOU 2051 CA LEU A1094 10860 8814 17238 477 30 -152 C
ATOM 2052 C LEU A1094 -1.130 6.514 0.807 1.00 97.56 C
ANISOU 2052 C LEU A1094 11006 8865 17196 447 125 33 C
ATOM 2053 O LEU A1094 0.097 6.374 0.873 1.00 91.07 O
ANISOU 2053 O LEU A1094 10277 8151 16175 468 38 -168 O
ATOM 2054 CB LEU A1094 -2.244 8.313 -0.540 1.00 87.18 C
ANISOU 2054 CB LEU A1094 9733 7714 15677 469 343 -78 C
ATOM 2055 N LYS A1095 -1.923 6.377 1.874 1.00100.42 N
ANISOU 2055 N LYS A1095 11317 9154 17682 395 303 437 N
ATOM 2056 CA LYS A1095 -1.368 6.108 3.198 1.00 97.71 C
ANISOU 2056 CA LYS A1095 11051 8894 17182 351 406 678 C
ATOM 2057 C LYS A1095 -0.511 4.847 3.197 1.00101.70 C
ANISOU 2057 C LYS A1095 11463 9227 17953 356 49 637 C
ATOM 2058 O LYS A1095 0.672 4.882 3.553 1.00108.12 O
ANISOU 2058 O LYS A1095 12402 10176 18503 372 16 513 O
ATOM 2059 CB LYS A1095 -2.490 5.984 4.230 1.00 92.75 C
ANISOU 2059 CB LYS A1095 10300 8271 16669 289 629 1158 C
ATOM 2060 CG LYS A1095 -1.991 5.516 5.584 1.00 97.16 C
ANISOU 2060 CG LYS A1095 10884 8965 17069 224 688 1481 C
ATOM 2061 CD LYS A1095 -3.051 5.643 6.657 1.00109.52 C
ANISOU 2061 CD LYS A1095 12333 10705 18573 168 1001 1941 C
ATOM 2062 CE LYS A1095 -2.416 5.555 8.030 1.00118.95 C
ANISOU 2062 CE LYS A1095 13615 12206 19373 112 1130 2196 C
ATOM 2063 NZ LYS A1095 -3.372 5.895 9.115 1.00126.21 N
ANISOU 2063 NZ LYS A1095 14437 13456 20062 82 1511 2570 N
ATOM 2064 N THR A1096 -1.106 3.718 2.796 1.00102.31 N
ANISOU 2064 N THR A1096 11296 8974 18604 346 -248 734 N
ATOM 2065 CA THR A1096 -0.393 2.442 2.751 1.00102.61 C
ANISOU 2065 CA THR A1096 11205 8746 19035 376 -641 678 C
ATOM 2066 C THR A1096 0.904 2.545 1.959 1.00102.89 C
ANISOU 2066 C THR A1096 11336 8901 18857 503 -795 132 C
ATOM 2067 O THR A1096 1.944 2.016 2.368 1.00107.25 O
ANISOU 2067 O THR A1096 11892 9431 19428 547 -949 96 O
ATOM 2068 CB THR A1096 -1.282 1.362 2.133 1.00109.69 C
ANISOU 2068 CB THR A1096 11827 9415 20435 328 -958 695 C
ATOM 2069 OG1 THR A1096 -2.494 1.243 2.884 1.00103.31 O
ANISOU 2069 OG1 THR A1096 10879 8550 19826 194 -809 1238 O
ATOM 2070 CG2 THR A1096 -0.555 0.023 2.123 1.00121.22 C
ANISOU 2070 CG2 THR A1096 13140 10707 22209 344 -1363 597 C
ATOM 2071 N THR A1097 0.851 3.199 0.799 1.00101.64 N
ANISOU 2071 N THR A1097 11218 8899 18501 564 -765 -270 N
ATOM 2072 CA THR A1097 2.049 3.348 -0.020 1.00104.66 C
ANISOU 2072 CA THR A1097 11646 9494 18627 676 -876 -769 C
ATOM 2073 C THR A1097 3.126 4.125 0.727 1.00 86.83 C
ANISOU 2073 C THR A1097 9593 7537 15861 644 -647 -725 C
ATOM 2074 O THR A1097 4.302 3.739 0.735 1.00 80.58 O
ANISOU 2074 O THR A1097 8779 6818 15018 718 -795 -934 O
ATOM 2075 CB THR A1097 1.693 4.039 -1.337 1.00116.18 C
ANISOU 2075 CB THR A1097 13099 11160 19884 707 -845 -1093 C
ATOM 2076 OG1 THR A1097 0.852 3.172 -2.111 1.00127.28 O
ANISOU 2076 OG1 THR A1097 14289 12300 21770 748 -1140 -1228 O
ATOM 2077 CG2 THR A1097 2.955 4.372 -2.128 1.00116.31 C
ANISOU 2077 CG2 THR A1097 13147 11530 19517 794 -882 -1540 C
ATOM 2078 N ARG A1098 2.732 5.225 1.371 1.00 82.34 N
ANISOU 2078 N ARG A1098 9207 7140 14940 542 -301 -478 N
ATOM 2079 CA ARG A1098 3.671 6.026 2.148 1.00 77.85 C
ANISOU 2079 CA ARG A1098 8839 6836 13903 491 -101 -452 C
ATOM 2080 C ARG A1098 4.362 5.188 3.219 1.00 74.67 C
ANISOU 2080 C ARG A1098 8408 6375 13589 485 -230 -246 C
ATOM 2081 O ARG A1098 5.587 5.234 3.365 1.00 67.88 O
ANISOU 2081 O ARG A1098 7593 5681 12518 505 -299 -407 O
ATOM 2082 CB ARG A1098 2.928 7.208 2.776 1.00 86.61 C
ANISOU 2082 CB ARG A1098 10122 8058 14728 406 260 -239 C
ATOM 2083 CG ARG A1098 3.776 8.129 3.643 1.00100.16 C
ANISOU 2083 CG ARG A1098 12058 10025 15974 341 457 -250 C
ATOM 2084 CD ARG A1098 2.911 8.807 4.695 1.00115.51 C
ANISOU 2084 CD ARG A1098 14113 12019 17755 296 767 5 C
ATOM 2085 NE ARG A1098 2.500 7.862 5.733 1.00122.05 N
ANISOU 2085 NE ARG A1098 14837 12805 18731 278 750 377 N
ATOM 2086 CZ ARG A1098 1.748 8.168 6.788 1.00122.07 C
ANISOU 2086 CZ ARG A1098 14869 12934 18577 248 1013 648 C
ATOM 2087 NH1 ARG A1098 1.436 7.229 7.672 1.00123.29 N
ANISOU 2087 NH1 ARG A1098 14886 13103 18857 205 973 1056 N
ATOM 2088 NH2 ARG A1098 1.305 9.406 6.965 1.00121.61 N
ANISOU 2088 NH2 ARG A1098 14954 13001 18251 267 1310 522 N
ATOM 2089 N ASN A1099 3.588 4.399 3.968 1.00 79.82 N
ANISOU 2089 N ASN A1099 8952 6805 14570 446 -280 154 N
ATOM 2090 CA ASN A1099 4.163 3.597 5.046 1.00 90.71 C
ANISOU 2090 CA ASN A1099 10283 8140 16042 418 -419 463 C
ATOM 2091 C ASN A1099 5.168 2.582 4.513 1.00 95.96 C
ANISOU 2091 C ASN A1099 10793 8617 17050 541 -810 207 C
ATOM 2092 O ASN A1099 6.288 2.477 5.021 1.00 96.94 O
ANISOU 2092 O ASN A1099 10948 8878 17008 561 -891 196 O
ATOM 2093 CB ASN A1099 3.059 2.885 5.826 1.00100.02 C
ANISOU 2093 CB ASN A1099 11319 9123 17563 329 -421 1009 C
ATOM 2094 CG ASN A1099 2.198 3.838 6.617 1.00110.44 C
ANISOU 2094 CG ASN A1099 12759 10716 18488 236 -6 1278 C
ATOM 2095 OD1 ASN A1099 2.483 4.138 7.776 1.00116.00 O
ANISOU 2095 OD1 ASN A1099 13564 11705 18805 169 167 1527 O
ATOM 2096 ND2 ASN A1099 1.132 4.322 5.992 1.00115.69 N
ANISOU 2096 ND2 ASN A1099 13396 11319 19241 245 149 1205 N
ATOM 2097 N ALA A1100 4.786 1.813 3.492 1.00 98.25 N
ANISOU 2097 N ALA A1100 10895 8598 17836 639 -1073 -31 N
ATOM 2098 CA ALA A1100 5.713 0.805 2.980 1.00 99.27 C
ANISOU 2098 CA ALA A1100 10848 8529 18339 802 -1456 -349 C
ATOM 2099 C ALA A1100 6.979 1.444 2.416 1.00 89.42 C
ANISOU 2099 C ALA A1100 9674 7657 16646 900 -1395 -821 C
ATOM 2100 O ALA A1100 8.076 0.895 2.568 1.00 78.29 O
ANISOU 2100 O ALA A1100 8167 6243 15338 1009 -1600 -951 O
ATOM 2101 CB ALA A1100 5.032 -0.062 1.924 1.00106.01 C
ANISOU 2101 CB ALA A1100 11494 9079 19705 878 -1740 -618 C
ATOM 2102 N TYR A1101 6.857 2.610 1.779 1.00 88.77 N
ANISOU 2102 N TYR A1101 9734 7905 16091 854 -1123 -1041 N
ATOM 2103 CA TYR A1101 8.031 3.239 1.180 1.00 79.03 C
ANISOU 2103 CA TYR A1101 8527 7056 14444 910 -1064 -1432 C
ATOM 2104 C TYR A1101 8.877 3.953 2.226 1.00 68.12 C
ANISOU 2104 C TYR A1101 7313 5931 12637 796 -888 -1220 C
ATOM 2105 O TYR A1101 10.114 3.850 2.215 1.00 63.67 O
ANISOU 2105 O TYR A1101 6680 5554 11958 860 -988 -1411 O
ATOM 2106 CB TYR A1101 7.618 4.210 0.071 1.00 83.93 C
ANISOU 2106 CB TYR A1101 9205 7934 14749 877 -879 -1678 C
ATOM 2107 CG TYR A1101 7.723 3.599 -1.307 1.00 92.97 C
ANISOU 2107 CG TYR A1101 10131 9119 16076 1050 -1107 -2169 C
ATOM 2108 CD1 TYR A1101 8.954 3.212 -1.824 1.00101.42 C
ANISOU 2108 CD1 TYR A1101 11037 10414 17084 1207 -1255 -2576 C
ATOM 2109 CD2 TYR A1101 6.593 3.400 -2.086 1.00 96.72 C
ANISOU 2109 CD2 TYR A1101 10537 9445 16768 1067 -1181 -2253 C
ATOM 2110 CE1 TYR A1101 9.051 2.646 -3.079 1.00109.18 C
ANISOU 2110 CE1 TYR A1101 11799 11502 18184 1393 -1452 -3094 C
ATOM 2111 CE2 TYR A1101 6.685 2.837 -3.342 1.00103.90 C
ANISOU 2111 CE2 TYR A1101 11242 10443 17792 1230 -1407 -2757 C
ATOM 2112 CZ TYR A1101 7.914 2.461 -3.833 1.00110.60 C
ANISOU 2112 CZ TYR A1101 11935 11545 18542 1401 -1534 -3197 C
ATOM 2113 OH TYR A1101 8.006 1.899 -5.087 1.00116.43 O
ANISOU 2113 OH TYR A1101 12451 12441 19345 1592 -1748 -3767 O
ATOM 2114 N ILE A1102 8.234 4.664 3.148 1.00 71.69 N
ANISOU 2114 N ILE A1102 7966 6416 12856 637 -636 -855 N
ATOM 2115 CA ILE A1102 8.925 5.641 3.991 1.00 79.74 C
ANISOU 2115 CA ILE A1102 9182 7734 13381 511 -437 -759 C
ATOM 2116 C ILE A1102 9.170 5.126 5.406 1.00 78.96 C
ANISOU 2116 C ILE A1102 9105 7609 13285 460 -503 -377 C
ATOM 2117 O ILE A1102 10.267 5.288 5.943 1.00 69.51 O
ANISOU 2117 O ILE A1102 7941 6625 11845 430 -555 -396 O
ATOM 2118 CB ILE A1102 8.144 6.972 4.002 1.00 70.53 C
ANISOU 2118 CB ILE A1102 8228 6682 11888 389 -106 -715 C
ATOM 2119 CG1 ILE A1102 7.833 7.397 2.563 1.00 62.76 C
ANISOU 2119 CG1 ILE A1102 7188 5727 10931 429 -84 -1003 C
ATOM 2120 CG2 ILE A1102 8.934 8.033 4.738 1.00 63.74 C
ANISOU 2120 CG2 ILE A1102 7564 6097 10559 263 53 -725 C
ATOM 2121 CD1 ILE A1102 9.060 7.512 1.690 1.00 58.47 C
ANISOU 2121 CD1 ILE A1102 6543 5444 10229 469 -194 -1347 C
ATOM 2122 N GLN A1103 8.156 4.511 6.027 1.00 78.23 N
ANISOU 2122 N GLN A1103 8972 7297 13453 435 -508 9 N
ATOM 2123 CA GLN A1103 8.228 4.145 7.447 1.00 84.13 C
ANISOU 2123 CA GLN A1103 9741 8116 14108 349 -522 471 C
ATOM 2124 C GLN A1103 9.555 3.491 7.832 1.00 83.32 C
ANISOU 2124 C GLN A1103 9536 8061 14061 398 -810 487 C
ATOM 2125 O GLN A1103 10.105 3.765 8.907 1.00 90.97 O
ANISOU 2125 O GLN A1103 10599 9302 14662 304 -772 705 O
ATOM 2126 CB GLN A1103 7.078 3.202 7.811 1.00103.39 C
ANISOU 2126 CB GLN A1103 12029 10265 16988 328 -595 918 C
ATOM 2127 CG GLN A1103 7.247 2.518 9.148 1.00123.28 C
ANISOU 2127 CG GLN A1103 14482 12848 19509 245 -703 1472 C
ATOM 2128 CD GLN A1103 6.261 1.402 9.368 1.00134.18 C
ANISOU 2128 CD GLN A1103 15640 13886 21456 208 -861 1959 C
ATOM 2129 OE1 GLN A1103 6.633 0.312 9.807 1.00134.63 O
ANISOU 2129 OE1 GLN A1103 15515 13733 21904 209 -1187 2306 O
ATOM 2130 NE2 GLN A1103 4.991 1.665 9.079 1.00136.14 N
ANISOU 2130 NE2 GLN A1103 15876 14057 21792 166 -652 2026 N
ATOM 2131 N LYS A1104 10.078 2.614 6.973 1.00 80.83 N
ANISOU 2131 N LYS A1104 9009 7498 14205 560 -1114 238 N
ATOM 2132 CA LYS A1104 11.313 1.899 7.279 1.00 90.53 C
ANISOU 2132 CA LYS A1104 10086 8722 15589 651 -1418 242 C
ATOM 2133 C LYS A1104 12.529 2.815 7.347 1.00 81.58 C
ANISOU 2133 C LYS A1104 9052 8010 13933 613 -1321 -23 C
ATOM 2134 O LYS A1104 13.593 2.377 7.805 1.00 72.09 O
ANISOU 2134 O LYS A1104 7735 6886 12771 660 -1543 38 O
ATOM 2135 CB LYS A1104 11.550 0.813 6.232 1.00103.83 C
ANISOU 2135 CB LYS A1104 11500 10042 17909 878 -1751 -82 C
ATOM 2136 CG LYS A1104 11.695 1.367 4.826 1.00108.92 C
ANISOU 2136 CG LYS A1104 12134 10827 18423 980 -1643 -695 C
ATOM 2137 CD LYS A1104 11.929 0.241 3.846 1.00112.53 C
ANISOU 2137 CD LYS A1104 12307 10974 19477 1234 -1982 -1085 C
ATOM 2138 CE LYS A1104 11.800 0.720 2.417 1.00111.48 C
ANISOU 2138 CE LYS A1104 12146 11030 19181 1322 -1866 -1649 C
ATOM 2139 NZ LYS A1104 10.399 1.079 2.091 1.00106.88 N
ANISOU 2139 NZ LYS A1104 11688 10326 18595 1208 -1700 -1540 N
ATOM 2140 N TYR A1105 12.410 4.061 6.891 1.00 82.02 N
ANISOU 2140 N TYR A1105 9293 8316 13553 523 -1024 -291 N
ATOM 2141 CA TYR A1105 13.513 5.005 6.982 1.00 82.79 C
ANISOU 2141 CA TYR A1105 9478 8788 13191 438 -941 -500 C
ATOM 2142 C TYR A1105 13.362 5.981 8.135 1.00 77.03 C
ANISOU 2142 C TYR A1105 9011 8304 11954 235 -724 -283 C
ATOM 2143 O TYR A1105 14.353 6.599 8.538 1.00 69.35 O
ANISOU 2143 O TYR A1105 8097 7614 10637 139 -735 -377 O
ATOM 2144 CB TYR A1105 13.666 5.777 5.666 1.00 85.59 C
ANISOU 2144 CB TYR A1105 9826 9270 13423 455 -804 -936 C
ATOM 2145 CG TYR A1105 13.975 4.865 4.511 1.00 84.72 C
ANISOU 2145 CG TYR A1105 9436 9042 13710 676 -1015 -1251 C
ATOM 2146 CD1 TYR A1105 15.123 4.092 4.511 1.00 87.40 C
ANISOU 2146 CD1 TYR A1105 9537 9427 14244 823 -1276 -1376 C
ATOM 2147 CD2 TYR A1105 13.109 4.759 3.434 1.00 77.79 C
ANISOU 2147 CD2 TYR A1105 8514 8023 13021 756 -968 -1451 C
ATOM 2148 CE1 TYR A1105 15.406 3.246 3.473 1.00 85.16 C
ANISOU 2148 CE1 TYR A1105 8978 9049 14331 1066 -1469 -1743 C
ATOM 2149 CE2 TYR A1105 13.383 3.916 2.386 1.00 80.68 C
ANISOU 2149 CE2 TYR A1105 8618 8322 13715 975 -1174 -1815 C
ATOM 2150 CZ TYR A1105 14.534 3.160 2.412 1.00 85.19 C
ANISOU 2150 CZ TYR A1105 8954 8936 14476 1141 -1416 -1986 C
ATOM 2151 OH TYR A1105 14.823 2.313 1.371 1.00 95.30 O
ANISOU 2151 OH TYR A1105 9955 10166 16091 1401 -1621 -2431 O
ATOM 2152 N LEU A1106 12.158 6.103 8.696 1.00 80.07 N
ANISOU 2152 N LEU A1106 9528 8605 12289 174 -541 -17 N
ATOM 2153 CA LEU A1106 11.980 6.950 9.869 1.00 81.01 C
ANISOU 2153 CA LEU A1106 9872 8998 11908 20 -337 138 C
ATOM 2154 C LEU A1106 12.645 6.349 11.098 1.00 97.13 C
ANISOU 2154 C LEU A1106 11864 11236 13804 -27 -532 475 C
ATOM 2155 O LEU A1106 12.938 7.070 12.058 1.00100.37 O
ANISOU 2155 O LEU A1106 12441 11980 13716 -154 -436 500 O
ATOM 2156 CB LEU A1106 10.496 7.182 10.127 1.00 70.08 C
ANISOU 2156 CB LEU A1106 8585 7529 10512 1 -71 324 C
ATOM 2157 CG LEU A1106 9.758 7.706 8.897 1.00 76.72 C
ANISOU 2157 CG LEU A1106 9447 8162 11541 53 83 50 C
ATOM 2158 CD1 LEU A1106 8.264 7.811 9.152 1.00 81.57 C
ANISOU 2158 CD1 LEU A1106 10098 8678 12217 55 320 265 C
ATOM 2159 CD2 LEU A1106 10.343 9.047 8.454 1.00 78.07 C
ANISOU 2159 CD2 LEU A1106 9781 8488 11396 -24 211 -327 C
ATOM 2160 N ARG A 365 12.898 5.042 11.084 1.00173.68 N
ANISOU 2160 N ARG A 365 24920 28167 12901 -2034 -2497 -2342 N
ATOM 2161 CA ARG A 365 13.578 4.386 12.192 1.00132.90 C
ANISOU 2161 CA ARG A 365 20305 22329 7861 -2317 -2580 -2278 C
ATOM 2162 C ARG A 365 14.964 4.989 12.405 1.00150.89 C
ANISOU 2162 C ARG A 365 22744 24102 10487 -1751 -2563 -2078 C
ATOM 2163 O ARG A 365 15.630 5.422 11.461 1.00127.35 O
ANISOU 2163 O ARG A 365 19647 21099 7640 -1221 -2556 -2029 O
ATOM 2164 CB ARG A 365 13.673 2.883 11.924 1.00135.83 C
ANISOU 2164 CB ARG A 365 21224 22319 8066 -2768 -2771 -2451 C
ATOM 2165 CG ARG A 365 12.308 2.235 11.724 1.00140.22 C
ANISOU 2165 CG ARG A 365 21642 23379 8258 -3426 -2793 -2668 C
ATOM 2166 CD ARG A 365 12.390 0.869 11.067 1.00143.45 C
ANISOU 2166 CD ARG A 365 22564 23465 8473 -3787 -2975 -2868 C
ATOM 2167 NE ARG A 365 11.061 0.341 10.767 1.00159.19 N
ANISOU 2167 NE ARG A 365 24360 26021 10103 -4438 -2992 -3091 N
ATOM 2168 CZ ARG A 365 10.831 -0.713 9.990 1.00159.13 C
ANISOU 2168 CZ ARG A 365 24644 25901 9919 -4766 -3119 -3296 C
ATOM 2169 NH1 ARG A 365 9.587 -1.120 9.773 1.00159.95 N
ANISOU 2169 NH1 ARG A 365 24443 26468 9862 -5292 -3082 -3446 N
ATOM 2170 NH2 ARG A 365 11.843 -1.358 9.424 1.00157.07 N
ANISOU 2170 NH2 ARG A 365 24956 25036 9686 -4524 -3266 -3330 N
ATOM 2171 N GLN A 366 15.394 5.018 13.665 1.00149.85 N
ANISOU 2171 N GLN A 366 22866 23586 10484 -1882 -2556 -1961 N
ATOM 2172 CA GLN A 366 16.594 5.747 14.051 1.00135.98 C
ANISOU 2172 CA GLN A 366 21174 21455 9035 -1409 -2522 -1770 C
ATOM 2173 C GLN A 366 17.856 5.048 13.550 1.00134.08 C
ANISOU 2173 C GLN A 366 21344 20686 8914 -1152 -2676 -1757 C
ATOM 2174 O GLN A 366 17.882 3.831 13.340 1.00137.59 O
ANISOU 2174 O GLN A 366 22204 20871 9203 -1423 -2824 -1880 O
ATOM 2175 CB GLN A 366 16.652 5.909 15.571 1.00125.09 C
ANISOU 2175 CB GLN A 366 19957 19848 7723 -1649 -2486 -1669 C
ATOM 2176 N ASN A 367 18.913 5.839 13.365 1.00132.31 N
ANISOU 2176 N ASN A 367 21017 20310 8944 -623 -2633 -1604 N
ATOM 2177 CA ASN A 367 20.172 5.333 12.838 1.00134.41 C
ANISOU 2177 CA ASN A 367 21582 20170 9319 -286 -2759 -1566 C
ATOM 2178 C ASN A 367 20.848 4.412 13.857 1.00151.61 C
ANISOU 2178 C ASN A 367 24306 21806 11492 -495 -2899 -1543 C
ATOM 2179 O ASN A 367 20.429 4.297 15.012 1.00157.26 O
ANISOU 2179 O ASN A 367 25152 22437 12162 -872 -2885 -1536 O
ATOM 2180 CB ASN A 367 21.097 6.492 12.456 1.00126.28 C
ANISOU 2180 CB ASN A 367 20254 19177 8549 281 -2654 -1396 C
ATOM 2181 CG ASN A 367 22.268 6.051 11.588 1.00132.61 C
ANISOU 2181 CG ASN A 367 21235 19729 9423 690 -2761 -1364 C
ATOM 2182 OD1 ASN A 367 23.371 5.811 12.083 1.00120.03 O
ANISOU 2182 OD1 ASN A 367 19894 17772 7942 834 -2844 -1270 O
ATOM 2183 ND2 ASN A 367 22.029 5.934 10.288 1.00150.09 N
ANISOU 2183 ND2 ASN A 367 23307 22173 11547 898 -2759 -1442 N
ATOM 2184 N ARG A 368 21.910 3.741 13.404 1.00162.48 N
ANISOU 2184 N ARG A 368 26016 22828 12891 -207 -3030 -1527 N
ATOM 2185 CA ARG A 368 22.595 2.766 14.245 1.00173.96 C
ANISOU 2185 CA ARG A 368 28041 23771 14286 -320 -3170 -1509 C
ATOM 2186 C ARG A 368 23.313 3.437 15.413 1.00186.28 C
ANISOU 2186 C ARG A 368 29546 25187 16043 -211 -3135 -1345 C
ATOM 2187 O ARG A 368 23.379 2.874 16.512 1.00187.82 O
ANISOU 2187 O ARG A 368 30111 25086 16165 -474 -3197 -1336 O
ATOM 2188 CB ARG A 368 23.574 1.948 13.397 1.00170.51 C
ANISOU 2188 CB ARG A 368 27950 23046 13788 56 -3309 -1522 C
ATOM 2189 CG ARG A 368 22.903 1.087 12.326 1.00167.93 C
ANISOU 2189 CG ARG A 368 27813 22772 13221 -97 -3374 -1708 C
ATOM 2190 CD ARG A 368 22.997 1.697 10.933 1.00157.16 C
ANISOU 2190 CD ARG A 368 26022 21758 11932 327 -3322 -1712 C
ATOM 2191 NE ARG A 368 22.185 0.955 9.973 1.00155.78 N
ANISOU 2191 NE ARG A 368 25976 21703 11509 114 -3381 -1913 N
ATOM 2192 CZ ARG A 368 22.307 1.064 8.655 1.00159.06 C
ANISOU 2192 CZ ARG A 368 26209 22323 11903 474 -3387 -1957 C
ATOM 2193 NH1 ARG A 368 21.527 0.355 7.849 1.00163.19 N
ANISOU 2193 NH1 ARG A 368 26868 22961 12176 231 -3454 -2160 N
ATOM 2194 NH2 ARG A 368 23.218 1.877 8.144 1.00157.65 N
ANISOU 2194 NH2 ARG A 368 25718 22241 11940 1059 -3323 -1800 N
ATOM 2195 N GLU A 369 23.858 4.637 15.200 1.00202.03 N
ANISOU 2195 N GLU A 369 31106 27383 18273 162 -3033 -1219 N
ATOM 2196 CA GLU A 369 24.509 5.346 16.297 1.00204.32 C
ANISOU 2196 CA GLU A 369 31328 27566 18739 223 -2999 -1081 C
ATOM 2197 C GLU A 369 23.493 6.004 17.221 1.00210.65 C
ANISOU 2197 C GLU A 369 31944 28555 19539 -141 -2874 -1084 C
ATOM 2198 O GLU A 369 23.741 6.120 18.427 1.00208.36 O
ANISOU 2198 O GLU A 369 31790 28086 19292 -280 -2888 -1023 O
ATOM 2199 CB GLU A 369 25.484 6.393 15.753 1.00203.88 C
ANISOU 2199 CB GLU A 369 30913 27637 18914 698 -2926 -949 C
ATOM 2200 CG GLU A 369 26.211 7.187 16.832 1.00209.26 C
ANISOU 2200 CG GLU A 369 31510 28230 19771 737 -2895 -820 C
ATOM 2201 CD GLU A 369 27.647 6.748 17.013 1.00217.03 C
ANISOU 2201 CD GLU A 369 32691 28973 20799 1023 -3038 -740 C
ATOM 2202 OE1 GLU A 369 28.358 6.628 15.996 1.00219.35 O
ANISOU 2202 OE1 GLU A 369 32909 29316 21118 1389 -3068 -709 O
ATOM 2203 OE2 GLU A 369 28.071 6.523 18.165 1.00219.21 O
ANISOU 2203 OE2 GLU A 369 33183 29044 21063 906 -3119 -706 O
ATOM 2204 N LYS A 370 22.349 6.432 16.682 1.00217.62 N
ANISOU 2204 N LYS A 370 32514 29825 20348 -271 -2751 -1155 N
ATOM 2205 CA LYS A 370 21.317 7.014 17.532 1.00219.38 C
ANISOU 2205 CA LYS A 370 32554 30280 20520 -586 -2626 -1157 C
ATOM 2206 C LYS A 370 20.767 5.995 18.520 1.00232.12 C
ANISOU 2206 C LYS A 370 34549 31700 21947 -1092 -2709 -1231 C
ATOM 2207 O LYS A 370 20.367 6.362 19.631 1.00238.28 O
ANISOU 2207 O LYS A 370 35311 32505 22721 -1317 -2643 -1188 O
ATOM 2208 CB LYS A 370 20.189 7.586 16.675 1.00215.40 C
ANISOU 2208 CB LYS A 370 31631 30296 19918 -578 -2484 -1222 C
ATOM 2209 N ARG A 371 20.738 4.715 18.139 1.00230.73 N
ANISOU 2209 N ARG A 371 34754 31312 21601 -1278 -2844 -1339 N
ATOM 2210 CA ARG A 371 20.248 3.689 19.054 1.00230.65 C
ANISOU 2210 CA ARG A 371 35180 31066 21392 -1784 -2909 -1404 C
ATOM 2211 C ARG A 371 21.162 3.552 20.262 1.00226.27 C
ANISOU 2211 C ARG A 371 34961 30089 20922 -1721 -2977 -1292 C
ATOM 2212 O ARG A 371 20.689 3.419 21.397 1.00227.76 O
ANISOU 2212 O ARG A 371 35298 30210 21030 -2072 -2947 -1278 O
ATOM 2213 CB ARG A 371 20.123 2.346 18.335 1.00235.38 C
ANISOU 2213 CB ARG A 371 36201 31459 21773 -1975 -3035 -1545 C
ATOM 2214 CG ARG A 371 19.019 2.272 17.291 1.00241.71 C
ANISOU 2214 CG ARG A 371 36723 32699 22416 -2188 -2989 -1695 C
ATOM 2215 CD ARG A 371 18.768 0.824 16.895 1.00251.76 C
ANISOU 2215 CD ARG A 371 38533 33701 23422 -2547 -3115 -1854 C
ATOM 2216 NE ARG A 371 17.963 0.692 15.684 1.00260.16 N
ANISOU 2216 NE ARG A 371 39352 35160 24337 -2665 -3109 -2013 N
ATOM 2217 CZ ARG A 371 18.472 0.521 14.468 1.00265.56 C
ANISOU 2217 CZ ARG A 371 40050 35815 25034 -2290 -3183 -2062 C
ATOM 2218 NH1 ARG A 371 19.786 0.467 14.300 1.00265.74 N
ANISOU 2218 NH1 ARG A 371 40303 35455 25212 -1772 -3259 -1954 N
ATOM 2219 NH2 ARG A 371 17.669 0.405 13.420 1.00268.84 N
ANISOU 2219 NH2 ARG A 371 40234 36623 25290 -2425 -3180 -2218 N
ATOM 2220 N PHE A 372 22.477 3.580 20.034 1.00202.89 N
ANISOU 2220 N PHE A 372 32105 26879 18104 -1268 -3067 -1210 N
ATOM 2221 CA PHE A 372 23.430 3.426 21.127 1.00182.41 C
ANISOU 2221 CA PHE A 372 29807 23937 15565 -1161 -3149 -1110 C
ATOM 2222 C PHE A 372 23.343 4.592 22.104 1.00165.68 C
ANISOU 2222 C PHE A 372 27369 21980 13602 -1188 -3041 -1016 C
ATOM 2223 O PHE A 372 23.429 4.396 23.321 1.00165.01 O
ANISOU 2223 O PHE A 372 27531 21693 13473 -1366 -3070 -977 O
ATOM 2224 CB PHE A 372 24.845 3.284 20.560 1.00176.66 C
ANISOU 2224 CB PHE A 372 29164 23027 14933 -638 -3262 -1044 C
ATOM 2225 CG PHE A 372 25.843 4.245 21.149 1.00170.92 C
ANISOU 2225 CG PHE A 372 28191 22328 14424 -338 -3252 -909 C
ATOM 2226 CD1 PHE A 372 26.541 3.925 22.303 1.00169.66 C
ANISOU 2226 CD1 PHE A 372 28331 21900 14232 -324 -3347 -846 C
ATOM 2227 CD2 PHE A 372 26.100 5.462 20.535 1.00165.90 C
ANISOU 2227 CD2 PHE A 372 27042 21989 14003 -76 -3146 -848 C
ATOM 2228 CE1 PHE A 372 27.464 4.807 22.838 1.00164.89 C
ANISOU 2228 CE1 PHE A 372 27484 21359 13808 -87 -3349 -740 C
ATOM 2229 CE2 PHE A 372 27.019 6.348 21.072 1.00161.17 C
ANISOU 2229 CE2 PHE A 372 26240 21410 13587 134 -3134 -736 C
ATOM 2230 CZ PHE A 372 27.700 6.018 22.224 1.00160.31 C
ANISOU 2230 CZ PHE A 372 26399 21066 13445 114 -3243 -690 C
ATOM 2231 N THR A 373 23.167 5.812 21.590 1.00152.01 N
ANISOU 2231 N THR A 373 25128 20596 12033 -1000 -2909 -980 N
ATOM 2232 CA THR A 373 23.077 6.977 22.463 1.00141.27 C
ANISOU 2232 CA THR A 373 23510 19367 10799 -1004 -2795 -896 C
ATOM 2233 C THR A 373 21.792 6.954 23.283 1.00144.37 C
ANISOU 2233 C THR A 373 23908 19912 11034 -1441 -2704 -939 C
ATOM 2234 O THR A 373 21.821 7.203 24.494 1.00153.66 O
ANISOU 2234 O THR A 373 25186 20980 12216 -1571 -2691 -886 O
ATOM 2235 CB THR A 373 23.182 8.262 21.635 1.00129.12 C
ANISOU 2235 CB THR A 373 21499 18127 9434 -680 -2657 -845 C
ATOM 2236 OG1 THR A 373 24.562 8.591 21.430 1.00123.99 O
ANISOU 2236 OG1 THR A 373 20825 17319 8965 -318 -2721 -759 O
ATOM 2237 CG2 THR A 373 22.483 9.425 22.330 1.00128.13 C
ANISOU 2237 CG2 THR A 373 21119 18226 9337 -772 -2486 -802 C
ATOM 2238 N PHE A 374 20.658 6.643 22.647 1.00141.49 N
ANISOU 2238 N PHE A 374 23422 19830 10508 -1676 -2641 -1037 N
ATOM 2239 CA PHE A 374 19.400 6.558 23.383 1.00147.31 C
ANISOU 2239 CA PHE A 374 24128 20785 11060 -2116 -2550 -1078 C
ATOM 2240 C PHE A 374 19.434 5.437 24.413 1.00162.73 C
ANISOU 2240 C PHE A 374 26594 22368 12869 -2485 -2652 -1093 C
ATOM 2241 O PHE A 374 18.887 5.583 25.511 1.00177.29 O
ANISOU 2241 O PHE A 374 28474 24255 14633 -2750 -2586 -1061 O
ATOM 2242 CB PHE A 374 18.232 6.357 22.413 1.00144.22 C
ANISOU 2242 CB PHE A 374 23481 20825 10491 -2310 -2480 -1193 C
ATOM 2243 CG PHE A 374 16.888 6.159 23.092 1.00136.71 C
ANISOU 2243 CG PHE A 374 22460 20179 9304 -2804 -2388 -1243 C
ATOM 2244 CD1 PHE A 374 16.498 4.909 23.565 1.00138.73 C
ANISOU 2244 CD1 PHE A 374 23121 20233 9356 -3311 -2466 -1318 C
ATOM 2245 CD2 PHE A 374 16.005 7.219 23.228 1.00130.51 C
ANISOU 2245 CD2 PHE A 374 21217 19899 8473 -2755 -2212 -1212 C
ATOM 2246 CE1 PHE A 374 15.272 4.731 24.182 1.00140.41 C
ANISOU 2246 CE1 PHE A 374 23243 20765 9340 -3799 -2369 -1356 C
ATOM 2247 CE2 PHE A 374 14.774 7.044 23.841 1.00134.79 C
ANISOU 2247 CE2 PHE A 374 21650 20792 8773 -3188 -2122 -1250 C
ATOM 2248 CZ PHE A 374 14.409 5.798 24.316 1.00141.07 C
ANISOU 2248 CZ PHE A 374 22811 21407 9382 -3733 -2201 -1322 C
ATOM 2249 N VAL A 375 20.049 4.303 24.073 1.00122.04 N
ANISOU 2249 N VAL A 375 21871 16846 7653 -2488 -2802 -1137 N
ATOM 2250 CA VAL A 375 20.060 3.177 25.001 1.00124.31 C
ANISOU 2250 CA VAL A 375 22724 16746 7763 -2824 -2884 -1149 C
ATOM 2251 C VAL A 375 20.875 3.518 26.243 1.00135.87 C
ANISOU 2251 C VAL A 375 24341 17952 9333 -2658 -2920 -1030 C
ATOM 2252 O VAL A 375 20.561 3.069 27.353 1.00134.19 O
ANISOU 2252 O VAL A 375 24432 17570 8985 -2966 -2914 -1010 O
ATOM 2253 CB VAL A 375 20.573 1.910 24.292 1.00126.24 C
ANISOU 2253 CB VAL A 375 23454 16627 7885 -2795 -3028 -1221 C
ATOM 2254 CG1 VAL A 375 22.028 1.623 24.651 1.00125.57 C
ANISOU 2254 CG1 VAL A 375 23716 16111 7883 -2377 -3166 -1131 C
ATOM 2255 CG2 VAL A 375 19.682 0.727 24.626 1.00129.87 C
ANISOU 2255 CG2 VAL A 375 24364 16931 8048 -3385 -3029 -1316 C
ATOM 2256 N LEU A 376 21.924 4.332 26.083 1.00130.83 N
ANISOU 2256 N LEU A 376 23485 17303 8923 -2189 -2953 -951 N
ATOM 2257 CA LEU A 376 22.685 4.805 27.231 1.00123.15 C
ANISOU 2257 CA LEU A 376 22579 16163 8049 -2041 -2987 -853 C
ATOM 2258 C LEU A 376 21.981 5.958 27.933 1.00123.72 C
ANISOU 2258 C LEU A 376 22300 16525 8181 -2160 -2835 -815 C
ATOM 2259 O LEU A 376 22.240 6.201 29.116 1.00131.70 O
ANISOU 2259 O LEU A 376 23435 17406 9198 -2193 -2848 -756 O
ATOM 2260 CB LEU A 376 24.098 5.201 26.790 1.00118.01 C
ANISOU 2260 CB LEU A 376 21827 15422 7590 -1544 -3084 -792 C
ATOM 2261 CG LEU A 376 24.895 4.070 26.125 1.00119.38 C
ANISOU 2261 CG LEU A 376 22363 15321 7676 -1335 -3237 -816 C
ATOM 2262 CD1 LEU A 376 26.360 4.423 25.987 1.00118.28 C
ANISOU 2262 CD1 LEU A 376 22128 15128 7686 -856 -3339 -736 C
ATOM 2263 CD2 LEU A 376 24.740 2.764 26.891 1.00122.09 C
ANISOU 2263 CD2 LEU A 376 23327 15296 7766 -1587 -3319 -841 C
ATOM 2264 N ALA A 377 21.090 6.663 27.231 1.00117.84 N
ANISOU 2264 N ALA A 377 21140 16181 7453 -2195 -2691 -847 N
ATOM 2265 CA ALA A 377 20.181 7.579 27.909 1.00124.33 C
ANISOU 2265 CA ALA A 377 21696 17303 8242 -2335 -2531 -819 C
ATOM 2266 C ALA A 377 19.274 6.824 28.867 1.00130.77 C
ANISOU 2266 C ALA A 377 22763 18098 8825 -2803 -2507 -841 C
ATOM 2267 O ALA A 377 18.988 7.297 29.973 1.00141.21 O
ANISOU 2267 O ALA A 377 24085 19456 10114 -2897 -2440 -787 O
ATOM 2268 CB ALA A 377 19.349 8.354 26.888 1.00126.58 C
ANISOU 2268 CB ALA A 377 21513 18055 8527 -2242 -2379 -851 C
ATOM 2269 N VAL A 378 18.814 5.641 28.455 1.00127.83 N
ANISOU 2269 N VAL A 378 22631 17661 8276 -3115 -2556 -923 N
ATOM 2270 CA VAL A 378 17.999 4.805 29.327 1.00162.25 C
ANISOU 2270 CA VAL A 378 27288 21965 12396 -3616 -2529 -943 C
ATOM 2271 C VAL A 378 18.837 4.271 30.483 1.00125.06 C
ANISOU 2271 C VAL A 378 23078 16764 7677 -3602 -2636 -874 C
ATOM 2272 O VAL A 378 18.326 4.074 31.592 1.00126.44 O
ANISOU 2272 O VAL A 378 23427 16903 7710 -3898 -2582 -839 O
ATOM 2273 CB VAL A 378 17.338 3.677 28.504 1.00127.42 C
ANISOU 2273 CB VAL A 378 23044 17586 7784 -3988 -2553 -1061 C
ATOM 2274 CG1 VAL A 378 17.153 2.410 29.329 1.00167.78 C
ANISOU 2274 CG1 VAL A 378 28752 22329 12670 -4438 -2598 -1074 C
ATOM 2275 CG2 VAL A 378 15.999 4.142 27.946 1.00128.32 C
ANISOU 2275 CG2 VAL A 378 22654 18322 7778 -4218 -2404 -1127 C
ATOM 2276 N VAL A 379 20.138 4.064 30.261 1.00140.44 N
ANISOU 2276 N VAL A 379 25237 18366 9756 -3230 -2784 -848 N
ATOM 2277 CA VAL A 379 21.007 3.572 31.325 1.00130.24 C
ANISOU 2277 CA VAL A 379 24400 16656 8431 -3144 -2897 -783 C
ATOM 2278 C VAL A 379 21.215 4.645 32.383 1.00131.99 C
ANISOU 2278 C VAL A 379 24412 16972 8765 -3010 -2853 -703 C
ATOM 2279 O VAL A 379 21.173 4.362 33.588 1.00137.99 O
ANISOU 2279 O VAL A 379 25464 17555 9409 -3162 -2861 -658 O
ATOM 2280 CB VAL A 379 22.345 3.074 30.744 1.00124.23 C
ANISOU 2280 CB VAL A 379 23874 15585 7742 -2737 -3067 -777 C
ATOM 2281 CG1 VAL A 379 23.461 3.216 31.774 1.00123.72 C
ANISOU 2281 CG1 VAL A 379 23999 15282 7727 -2453 -3175 -692 C
ATOM 2282 CG2 VAL A 379 22.224 1.621 30.310 1.00127.09 C
ANISOU 2282 CG2 VAL A 379 24768 15639 7879 -2927 -3134 -840 C
ATOM 2283 N ILE A 380 21.451 5.889 31.957 1.00126.76 N
ANISOU 2283 N ILE A 380 23281 16569 8312 -2726 -2801 -686 N
ATOM 2284 CA ILE A 380 21.549 6.984 32.916 1.00126.53 C
ANISOU 2284 CA ILE A 380 23074 16633 8368 -2631 -2744 -626 C
ATOM 2285 C ILE A 380 20.260 7.095 33.716 1.00129.73 C
ANISOU 2285 C ILE A 380 23450 17245 8598 -2988 -2596 -618 C
ATOM 2286 O ILE A 380 20.280 7.443 34.902 1.00132.81 O
ANISOU 2286 O ILE A 380 23938 17572 8950 -3020 -2580 -568 O
ATOM 2287 CB ILE A 380 21.907 8.296 32.184 1.00130.37 C
ANISOU 2287 CB ILE A 380 23106 17350 9078 -2303 -2682 -614 C
ATOM 2288 CG1 ILE A 380 23.419 8.553 32.229 1.00131.80 C
ANISOU 2288 CG1 ILE A 380 23332 17314 9432 -1962 -2827 -579 C
ATOM 2289 CG2 ILE A 380 21.143 9.483 32.762 1.00134.84 C
ANISOU 2289 CG2 ILE A 380 23407 18187 9640 -2342 -2513 -585 C
ATOM 2290 CD1 ILE A 380 24.235 7.639 31.336 1.00133.70 C
ANISOU 2290 CD1 ILE A 380 23725 17384 9692 -1785 -2969 -599 C
ATOM 2291 N GLY A 381 19.128 6.762 33.096 1.00134.97 N
ANISOU 2291 N GLY A 381 23974 18180 9127 -3268 -2490 -671 N
ATOM 2292 CA GLY A 381 17.871 6.746 33.817 1.00134.11 C
ANISOU 2292 CA GLY A 381 23816 18328 8810 -3638 -2347 -661 C
ATOM 2293 C GLY A 381 17.874 5.799 34.998 1.00129.17 C
ANISOU 2293 C GLY A 381 23682 17384 8013 -3929 -2396 -627 C
ATOM 2294 O GLY A 381 17.239 6.076 36.016 1.00133.57 O
ANISOU 2294 O GLY A 381 24231 18071 8449 -4104 -2296 -579 O
ATOM 2295 N VAL A 382 18.584 4.680 34.890 1.00126.51 N
ANISOU 2295 N VAL A 382 23804 16624 7640 -3956 -2540 -645 N
ATOM 2296 CA VAL A 382 18.654 3.747 36.010 1.00128.74 C
ANISOU 2296 CA VAL A 382 24625 16556 7736 -4191 -2579 -602 C
ATOM 2297 C VAL A 382 19.747 4.145 36.996 1.00160.57 C
ANISOU 2297 C VAL A 382 28817 20326 11866 -3843 -2684 -530 C
ATOM 2298 O VAL A 382 19.592 3.951 38.202 1.00128.70 O
ANISOU 2298 O VAL A 382 25041 16163 7694 -3983 -2662 -474 O
ATOM 2299 CB VAL A 382 18.834 2.296 35.506 1.00131.17 C
ANISOU 2299 CB VAL A 382 25443 16504 7893 -4383 -2666 -651 C
ATOM 2300 CG1 VAL A 382 18.181 2.129 34.163 1.00196.87 C
ANISOU 2300 CG1 VAL A 382 33511 25086 16202 -4554 -2621 -750 C
ATOM 2301 CG2 VAL A 382 20.302 1.875 35.458 1.00130.55 C
ANISOU 2301 CG2 VAL A 382 25721 15987 7896 -3950 -2855 -628 C
ATOM 2302 N PHE A 383 20.859 4.723 36.523 1.00155.82 N
ANISOU 2302 N PHE A 383 28048 19671 11487 -3399 -2798 -531 N
ATOM 2303 CA PHE A 383 21.882 5.208 37.447 1.00124.21 C
ANISOU 2303 CA PHE A 383 24123 15504 7566 -3098 -2901 -479 C
ATOM 2304 C PHE A 383 21.338 6.342 38.306 1.00164.31 C
ANISOU 2304 C PHE A 383 28932 20829 12670 -3143 -2783 -446 C
ATOM 2305 O PHE A 383 21.662 6.446 39.495 1.00164.16 O
ANISOU 2305 O PHE A 383 29112 20670 12590 -3105 -2826 -403 O
ATOM 2306 CB PHE A 383 23.119 5.664 36.671 1.00122.29 C
ANISOU 2306 CB PHE A 383 23684 15237 7545 -2667 -3029 -492 C
ATOM 2307 CG PHE A 383 24.423 5.378 37.373 1.00123.84 C
ANISOU 2307 CG PHE A 383 24156 15165 7731 -2380 -3210 -456 C
ATOM 2308 CD1 PHE A 383 24.973 4.105 37.352 1.00124.65 C
ANISOU 2308 CD1 PHE A 383 24735 14951 7675 -2300 -3332 -448 C
ATOM 2309 CD2 PHE A 383 25.108 6.384 38.036 1.00130.40 C
ANISOU 2309 CD2 PHE A 383 24785 16077 8684 -2176 -3258 -436 C
ATOM 2310 CE1 PHE A 383 26.172 3.837 37.990 1.00150.79 C
ANISOU 2310 CE1 PHE A 383 28280 18077 10937 -1981 -3498 -411 C
ATOM 2311 CE2 PHE A 383 26.309 6.122 38.677 1.00139.60 C
ANISOU 2311 CE2 PHE A 383 26158 17070 9814 -1913 -3434 -413 C
ATOM 2312 CZ PHE A 383 26.842 4.847 38.653 1.00147.10 C
ANISOU 2312 CZ PHE A 383 27546 17753 10594 -1793 -3555 -397 C
ATOM 2313 N VAL A 384 20.504 7.199 37.718 1.00122.28 N
ANISOU 2313 N VAL A 384 23174 15877 7409 -3192 -2632 -467 N
ATOM 2314 CA VAL A 384 19.833 8.236 38.493 1.00130.79 C
ANISOU 2314 CA VAL A 384 24035 17206 8455 -3222 -2494 -434 C
ATOM 2315 C VAL A 384 18.778 7.617 39.404 1.00134.70 C
ANISOU 2315 C VAL A 384 24735 17756 8690 -3606 -2392 -400 C
ATOM 2316 O VAL A 384 18.708 7.926 40.597 1.00140.32 O
ANISOU 2316 O VAL A 384 25569 18428 9318 -3617 -2368 -351 O
ATOM 2317 CB VAL A 384 19.227 9.292 37.551 1.00136.44 C
ANISOU 2317 CB VAL A 384 24261 18316 9265 -3108 -2348 -457 C
ATOM 2318 CG1 VAL A 384 18.362 10.272 38.327 1.00136.72 C
ANISOU 2318 CG1 VAL A 384 24116 18633 9197 -3127 -2180 -419 C
ATOM 2319 CG2 VAL A 384 20.330 10.023 36.802 1.00135.97 C
ANISOU 2319 CG2 VAL A 384 24026 18178 9459 -2735 -2430 -474 C
ATOM 2320 N VAL A 385 17.957 6.714 38.863 1.00126.10 N
ANISOU 2320 N VAL A 385 23698 16761 7453 -3947 -2331 -429 N
ATOM 2321 CA VAL A 385 16.858 6.148 39.643 1.00159.77 C
ANISOU 2321 CA VAL A 385 28111 21143 11452 -4378 -2207 -395 C
ATOM 2322 C VAL A 385 17.385 5.285 40.784 1.00161.65 C
ANISOU 2322 C VAL A 385 28912 20939 11569 -4468 -2297 -342 C
ATOM 2323 O VAL A 385 16.845 5.313 41.896 1.00131.73 O
ANISOU 2323 O VAL A 385 25236 17202 7615 -4642 -2208 -280 O
ATOM 2324 CB VAL A 385 15.898 5.365 38.726 1.00130.78 C
ANISOU 2324 CB VAL A 385 24361 17690 7638 -4777 -2127 -455 C
ATOM 2325 CG1 VAL A 385 15.268 4.192 39.464 1.00134.26 C
ANISOU 2325 CG1 VAL A 385 25221 17989 7803 -5283 -2076 -428 C
ATOM 2326 CG2 VAL A 385 14.812 6.288 38.204 1.00130.49 C
ANISOU 2326 CG2 VAL A 385 23741 18269 7568 -4798 -1955 -473 C
ATOM 2327 N CYS A 386 18.445 4.510 40.541 1.00157.19 N
ANISOU 2327 N CYS A 386 28717 19950 11058 -4315 -2469 -358 N
ATOM 2328 CA CYS A 386 18.949 3.615 41.579 1.00151.43 C
ANISOU 2328 CA CYS A 386 28567 18798 10170 -4356 -2550 -303 C
ATOM 2329 C CYS A 386 19.726 4.371 42.653 1.00147.46 C
ANISOU 2329 C CYS A 386 28073 18216 9741 -4018 -2629 -255 C
ATOM 2330 O CYS A 386 19.513 4.154 43.851 1.00147.16 O
ANISOU 2330 O CYS A 386 28309 18073 9532 -4133 -2594 -193 O
ATOM 2331 CB CYS A 386 19.830 2.523 40.962 1.00147.78 C
ANISOU 2331 CB CYS A 386 28529 17929 9692 -4239 -2703 -331 C
ATOM 2332 SG CYS A 386 18.985 1.373 39.844 1.00146.00 S
ANISOU 2332 SG CYS A 386 28486 17674 9312 -4694 -2632 -401 S
ATOM 2333 N TRP A 387 20.630 5.262 42.244 1.00143.53 N
ANISOU 2333 N TRP A 387 27280 17772 9481 -3622 -2734 -287 N
ATOM 2334 CA TRP A 387 21.602 5.844 43.165 1.00147.18 C
ANISOU 2334 CA TRP A 387 27798 18118 10005 -3307 -2855 -265 C
ATOM 2335 C TRP A 387 21.124 7.133 43.824 1.00143.64 C
ANISOU 2335 C TRP A 387 27036 17941 9598 -3285 -2748 -254 C
ATOM 2336 O TRP A 387 21.424 7.364 45.002 1.00135.04 O
ANISOU 2336 O TRP A 387 26120 16757 8431 -3205 -2792 -224 O
ATOM 2337 CB TRP A 387 22.921 6.118 42.440 1.00151.57 C
ANISOU 2337 CB TRP A 387 28220 18598 10771 -2922 -3029 -306 C
ATOM 2338 CG TRP A 387 23.676 4.901 42.038 1.00154.54 C
ANISOU 2338 CG TRP A 387 28972 18673 11071 -2807 -3169 -306 C
ATOM 2339 CD1 TRP A 387 23.881 4.447 40.772 1.00151.60 C
ANISOU 2339 CD1 TRP A 387 28554 18276 10772 -2746 -3202 -343 C
ATOM 2340 CD2 TRP A 387 24.338 3.979 42.910 1.00157.32 C
ANISOU 2340 CD2 TRP A 387 29842 18704 11228 -2692 -3290 -262 C
ATOM 2341 NE1 TRP A 387 24.629 3.295 40.799 1.00154.00 N
ANISOU 2341 NE1 TRP A 387 29332 18250 10930 -2592 -3335 -326 N
ATOM 2342 CE2 TRP A 387 24.922 2.986 42.101 1.00160.86 C
ANISOU 2342 CE2 TRP A 387 30558 18934 11627 -2546 -3387 -273 C
ATOM 2343 CE3 TRP A 387 24.490 3.895 44.298 1.00149.58 C
ANISOU 2343 CE3 TRP A 387 29144 17601 10088 -2667 -3321 -213 C
ATOM 2344 CZ2 TRP A 387 25.651 1.925 42.633 1.00162.50 C
ANISOU 2344 CZ2 TRP A 387 31321 18805 11616 -2351 -3508 -231 C
ATOM 2345 CZ3 TRP A 387 25.209 2.841 44.823 1.00149.74 C
ANISOU 2345 CZ3 TRP A 387 29689 17300 9905 -2487 -3442 -172 C
ATOM 2346 CH2 TRP A 387 25.778 1.868 43.993 1.00155.06 C
ANISOU 2346 CH2 TRP A 387 30614 17757 10542 -2317 -3521 -177 C
ATOM 2347 N PHE A 388 20.409 7.990 43.087 1.00149.13 N
ANISOU 2347 N PHE A 388 27300 18972 10392 -3317 -2609 -280 N
ATOM 2348 CA PHE A 388 19.991 9.276 43.649 1.00150.38 C
ANISOU 2348 CA PHE A 388 27203 19369 10566 -3230 -2499 -270 C
ATOM 2349 C PHE A 388 19.239 9.152 44.967 1.00146.72 C
ANISOU 2349 C PHE A 388 26940 18940 9866 -3418 -2404 -208 C
ATOM 2350 O PHE A 388 19.533 9.932 45.889 1.00146.17 O
ANISOU 2350 O PHE A 388 26901 18848 9789 -3254 -2424 -200 O
ATOM 2351 CB PHE A 388 19.157 10.062 42.632 1.00154.77 C
ANISOU 2351 CB PHE A 388 27316 20301 11190 -3228 -2333 -292 C
ATOM 2352 CG PHE A 388 18.515 11.294 43.205 1.00155.40 C
ANISOU 2352 CG PHE A 388 27194 20640 11211 -3133 -2182 -270 C
ATOM 2353 CD1 PHE A 388 19.246 12.460 43.368 1.00153.47 C
ANISOU 2353 CD1 PHE A 388 26871 20331 11111 -2840 -2222 -294 C
ATOM 2354 CD2 PHE A 388 17.182 11.286 43.589 1.00158.39 C
ANISOU 2354 CD2 PHE A 388 27482 21337 11363 -3341 -1993 -225 C
ATOM 2355 CE1 PHE A 388 18.661 13.595 43.899 1.00151.25 C
ANISOU 2355 CE1 PHE A 388 26480 20243 10744 -2727 -2076 -277 C
ATOM 2356 CE2 PHE A 388 16.592 12.418 44.122 1.00157.33 C
ANISOU 2356 CE2 PHE A 388 27190 21452 11138 -3193 -1848 -197 C
ATOM 2357 CZ PHE A 388 17.332 13.574 44.277 1.00154.06 C
ANISOU 2357 CZ PHE A 388 26757 20916 10864 -2872 -1889 -225 C
ATOM 2358 N PRO A 389 18.268 8.243 45.133 1.00155.19 N
ANISOU 2358 N PRO A 389 28157 20079 10728 -3771 -2294 -166 N
ATOM 2359 CA PRO A 389 17.640 8.116 46.458 1.00163.63 C
ANISOU 2359 CA PRO A 389 29434 21174 11562 -3937 -2202 -94 C
ATOM 2360 C PRO A 389 18.652 7.844 47.558 1.00165.80 C
ANISOU 2360 C PRO A 389 30115 21075 11805 -3766 -2365 -73 C
ATOM 2361 O PRO A 389 18.609 8.498 48.608 1.00164.98 O
ANISOU 2361 O PRO A 389 30045 21014 11627 -3659 -2343 -46 O
ATOM 2362 CB PRO A 389 16.658 6.949 46.271 1.00132.80 C
ANISOU 2362 CB PRO A 389 25673 17336 7450 -4395 -2085 -60 C
ATOM 2363 CG PRO A 389 17.177 6.198 45.092 1.00132.37 C
ANISOU 2363 CG PRO A 389 25688 17091 7515 -4419 -2193 -121 C
ATOM 2364 CD PRO A 389 17.715 7.257 44.189 1.00161.07 C
ANISOU 2364 CD PRO A 389 28916 20868 11416 -4066 -2248 -184 C
ATOM 2365 N PHE A 390 19.587 6.918 47.328 1.00162.28 N
ANISOU 2365 N PHE A 390 29982 20285 11394 -3700 -2533 -87 N
ATOM 2366 CA PHE A 390 20.614 6.626 48.323 1.00160.35 C
ANISOU 2366 CA PHE A 390 30107 19729 11090 -3483 -2701 -69 C
ATOM 2367 C PHE A 390 21.458 7.858 48.627 1.00158.14 C
ANISOU 2367 C PHE A 390 29595 19516 10977 -3143 -2814 -122 C
ATOM 2368 O PHE A 390 21.629 8.236 49.791 1.00158.94 O
ANISOU 2368 O PHE A 390 29830 19581 10977 -3051 -2846 -106 O
ATOM 2369 CB PHE A 390 21.507 5.484 47.840 1.00162.39 C
ANISOU 2369 CB PHE A 390 30703 19656 11342 -3390 -2859 -77 C
ATOM 2370 CG PHE A 390 22.567 5.087 48.830 1.00167.58 C
ANISOU 2370 CG PHE A 390 31701 20033 11938 -3111 -3019 -52 C
ATOM 2371 CD1 PHE A 390 23.766 5.779 48.910 1.00166.85 C
ANISOU 2371 CD1 PHE A 390 31449 19963 11985 -2742 -3208 -108 C
ATOM 2372 CD2 PHE A 390 22.357 4.025 49.690 1.00177.27 C
ANISOU 2372 CD2 PHE A 390 33385 20997 12972 -3220 -2968 27 C
ATOM 2373 CE1 PHE A 390 24.729 5.423 49.831 1.00171.75 C
ANISOU 2373 CE1 PHE A 390 32312 20400 12546 -2468 -3352 -92 C
ATOM 2374 CE2 PHE A 390 23.322 3.656 50.608 1.00181.18 C
ANISOU 2374 CE2 PHE A 390 34168 21263 13411 -2913 -3103 53 C
ATOM 2375 CZ PHE A 390 24.510 4.355 50.678 1.00178.55 C
ANISOU 2375 CZ PHE A 390 33624 21004 13211 -2526 -3300 -9 C
ATOM 2376 N PHE A 391 22.023 8.483 47.592 1.00160.64 N
ANISOU 2376 N PHE A 391 29583 19919 11534 -2968 -2877 -190 N
ATOM 2377 CA PHE A 391 22.957 9.581 47.827 1.00160.83 C
ANISOU 2377 CA PHE A 391 29428 19971 11708 -2693 -2995 -249 C
ATOM 2378 C PHE A 391 22.256 10.796 48.411 1.00161.41 C
ANISOU 2378 C PHE A 391 29326 20247 11755 -2710 -2854 -253 C
ATOM 2379 O PHE A 391 22.831 11.511 49.238 1.00154.47 O
ANISOU 2379 O PHE A 391 28495 19326 10871 -2563 -2940 -288 O
ATOM 2380 CB PHE A 391 23.682 9.947 46.535 1.00157.12 C
ANISOU 2380 CB PHE A 391 28659 19552 11488 -2535 -3068 -308 C
ATOM 2381 CG PHE A 391 24.790 9.006 46.191 1.00152.48 C
ANISOU 2381 CG PHE A 391 28249 18766 10919 -2376 -3264 -316 C
ATOM 2382 CD1 PHE A 391 24.537 7.870 45.448 1.00153.53 C
ANISOU 2382 CD1 PHE A 391 28543 18792 11001 -2471 -3248 -289 C
ATOM 2383 CD2 PHE A 391 26.082 9.249 46.625 1.00148.58 C
ANISOU 2383 CD2 PHE A 391 27775 18216 10464 -2125 -3465 -353 C
ATOM 2384 CE1 PHE A 391 25.552 6.998 45.131 1.00154.71 C
ANISOU 2384 CE1 PHE A 391 28899 18753 11129 -2268 -3419 -290 C
ATOM 2385 CE2 PHE A 391 27.103 8.378 46.308 1.00148.12 C
ANISOU 2385 CE2 PHE A 391 27864 18031 10382 -1921 -3641 -351 C
ATOM 2386 CZ PHE A 391 26.833 7.252 45.560 1.00151.85 C
ANISOU 2386 CZ PHE A 391 28528 18371 10795 -1969 -3613 -315 C
ATOM 2387 N PHE A 392 21.011 11.038 48.008 1.00172.57 N
ANISOU 2387 N PHE A 392 30548 21901 13121 -2877 -2639 -221 N
ATOM 2388 CA PHE A 392 20.299 12.199 48.526 1.00175.15 C
ANISOU 2388 CA PHE A 392 30727 22441 13380 -2832 -2488 -215 C
ATOM 2389 C PHE A 392 19.903 12.002 49.985 1.00177.20 C
ANISOU 2389 C PHE A 392 31273 22659 13395 -2901 -2458 -161 C
ATOM 2390 O PHE A 392 19.977 12.944 50.783 1.00178.64 O
ANISOU 2390 O PHE A 392 31482 22864 13529 -2758 -2450 -181 O
ATOM 2391 CB PHE A 392 19.077 12.497 47.664 1.00180.24 C
ANISOU 2391 CB PHE A 392 31056 23425 14002 -2937 -2265 -191 C
ATOM 2392 CG PHE A 392 18.499 13.857 47.898 1.00187.54 C
ANISOU 2392 CG PHE A 392 31800 24581 14877 -2776 -2111 -192 C
ATOM 2393 CD1 PHE A 392 19.187 14.993 47.500 1.00190.06 C
ANISOU 2393 CD1 PHE A 392 31999 24842 15371 -2533 -2148 -257 C
ATOM 2394 CD2 PHE A 392 17.271 14.001 48.515 1.00193.70 C
ANISOU 2394 CD2 PHE A 392 32551 25636 15409 -2863 -1918 -125 C
ATOM 2395 CE1 PHE A 392 18.658 16.248 47.717 1.00192.41 C
ANISOU 2395 CE1 PHE A 392 32214 25302 15590 -2361 -1992 -258 C
ATOM 2396 CE2 PHE A 392 16.735 15.254 48.733 1.00196.84 C
ANISOU 2396 CE2 PHE A 392 32822 26247 15721 -2653 -1768 -121 C
ATOM 2397 CZ PHE A 392 17.431 16.379 48.334 1.00195.49 C
ANISOU 2397 CZ PHE A 392 32595 25964 15719 -2392 -1804 -189 C
ATOM 2398 N THR A 393 19.481 10.790 50.360 1.00177.85 N
ANISOU 2398 N THR A 393 31606 22664 13306 -3126 -2435 -91 N
ATOM 2399 CA THR A 393 19.188 10.534 51.769 1.00178.39 C
ANISOU 2399 CA THR A 393 31980 22667 13133 -3180 -2408 -28 C
ATOM 2400 C THR A 393 20.471 10.475 52.591 1.00173.09 C
ANISOU 2400 C THR A 393 31561 21702 12504 -2950 -2632 -68 C
ATOM 2401 O THR A 393 20.497 10.908 53.750 1.00174.58 O
ANISOU 2401 O THR A 393 31852 21871 12610 -2844 -2631 -59 O
ATOM 2402 CB THR A 393 18.374 9.243 51.935 1.00184.58 C
ANISOU 2402 CB THR A 393 32978 23433 13722 -3514 -2295 64 C
ATOM 2403 OG1 THR A 393 17.770 9.228 53.236 1.00193.07 O
ANISOU 2403 OG1 THR A 393 34198 24552 14609 -3567 -2181 142 O
ATOM 2404 CG2 THR A 393 19.247 7.999 51.799 1.00181.85 C
ANISOU 2404 CG2 THR A 393 32963 22714 13419 -3523 -2453 66 C
ATOM 2405 N TYR A 394 21.550 9.960 52.000 1.00162.85 N
ANISOU 2405 N TYR A 394 30326 20210 11341 -2844 -2821 -113 N
ATOM 2406 CA TYR A 394 22.828 9.903 52.694 1.00157.05 C
ANISOU 2406 CA TYR A 394 29745 19276 10650 -2594 -3038 -157 C
ATOM 2407 C TYR A 394 23.429 11.293 52.851 1.00150.74 C
ANISOU 2407 C TYR A 394 28743 18577 9955 -2419 -3127 -255 C
ATOM 2408 O TYR A 394 24.106 11.570 53.850 1.00149.53 O
ANISOU 2408 O TYR A 394 28693 18352 9769 -2267 -3248 -293 O
ATOM 2409 CB TYR A 394 23.770 8.972 51.932 1.00165.32 C
ANISOU 2409 CB TYR A 394 30885 20151 11780 -2499 -3200 -171 C
ATOM 2410 CG TYR A 394 25.190 8.958 52.418 1.00173.55 C
ANISOU 2410 CG TYR A 394 31996 21086 12861 -2202 -3439 -224 C
ATOM 2411 CD1 TYR A 394 25.588 8.096 53.427 1.00178.18 C
ANISOU 2411 CD1 TYR A 394 32906 21490 13304 -2079 -3507 -175 C
ATOM 2412 CD2 TYR A 394 26.141 9.797 51.858 1.00176.23 C
ANISOU 2412 CD2 TYR A 394 32070 21535 13354 -2048 -3592 -322 C
ATOM 2413 CE1 TYR A 394 26.892 8.078 53.871 1.00180.02 C
ANISOU 2413 CE1 TYR A 394 33161 21699 13539 -1781 -3728 -227 C
ATOM 2414 CE2 TYR A 394 27.446 9.783 52.294 1.00177.69 C
ANISOU 2414 CE2 TYR A 394 32268 21703 13545 -1800 -3815 -377 C
ATOM 2415 CZ TYR A 394 27.821 8.925 53.304 1.00177.20 C
ANISOU 2415 CZ TYR A 394 32493 21505 13331 -1653 -3887 -331 C
ATOM 2416 OH TYR A 394 29.125 8.910 53.740 1.00174.35 O
ANISOU 2416 OH TYR A 394 32105 21197 12943 -1380 -4112 -389 O
ATOM 2417 N THR A 395 23.178 12.177 51.881 1.00156.71 N
ANISOU 2417 N THR A 395 29189 19493 10862 -2436 -3046 -299 N
ATOM 2418 CA THR A 395 23.625 13.560 51.997 1.00159.77 C
ANISOU 2418 CA THR A 395 29408 19941 11355 -2306 -3079 -389 C
ATOM 2419 C THR A 395 22.841 14.301 53.071 1.00163.44 C
ANISOU 2419 C THR A 395 29988 20478 11633 -2310 -2952 -374 C
ATOM 2420 O THR A 395 23.410 15.094 53.830 1.00169.42 O
ANISOU 2420 O THR A 395 30831 21181 12359 -2203 -3049 -450 O
ATOM 2421 CB THR A 395 23.484 14.269 50.652 1.00168.55 C
ANISOU 2421 CB THR A 395 30174 21180 12687 -2299 -2979 -419 C
ATOM 2422 OG1 THR A 395 24.226 13.557 49.655 1.00172.22 O
ANISOU 2422 OG1 THR A 395 30538 21586 13312 -2275 -3098 -430 O
ATOM 2423 CG2 THR A 395 24.002 15.700 50.740 1.00170.21 C
ANISOU 2423 CG2 THR A 395 30279 21400 12993 -2190 -3000 -512 C
ATOM 2424 N LEU A 396 21.533 14.047 53.154 1.00165.46 N
ANISOU 2424 N LEU A 396 30247 20880 11742 -2436 -2734 -281 N
ATOM 2425 CA LEU A 396 20.714 14.670 54.186 1.00174.02 C
ANISOU 2425 CA LEU A 396 31427 22071 12622 -2407 -2593 -247 C
ATOM 2426 C LEU A 396 21.125 14.258 55.593 1.00167.39 C
ANISOU 2426 C LEU A 396 30842 21067 11691 -2345 -2693 -236 C
ATOM 2427 O LEU A 396 20.790 14.965 56.549 1.00168.23 O
ANISOU 2427 O LEU A 396 31023 21215 11680 -2251 -2627 -241 O
ATOM 2428 CB LEU A 396 19.236 14.334 53.976 1.00181.88 C
ANISOU 2428 CB LEU A 396 32320 23327 13458 -2569 -2338 -137 C
ATOM 2429 CG LEU A 396 18.385 15.270 53.118 1.00181.98 C
ANISOU 2429 CG LEU A 396 32012 23630 13502 -2512 -2134 -136 C
ATOM 2430 CD1 LEU A 396 16.920 15.144 53.512 1.00183.25 C
ANISOU 2430 CD1 LEU A 396 32113 24121 13394 -2614 -1889 -27 C
ATOM 2431 CD2 LEU A 396 18.853 16.709 53.242 1.00181.86 C
ANISOU 2431 CD2 LEU A 396 31990 23557 13552 -2265 -2154 -225 C
ATOM 2432 N THR A 397 21.834 13.137 55.748 1.00162.67 N
ANISOU 2432 N THR A 397 30398 20287 11124 -2364 -2844 -219 N
ATOM 2433 CA THR A 397 22.232 12.707 57.085 1.00159.94 C
ANISOU 2433 CA THR A 397 30305 19798 10667 -2269 -2933 -201 C
ATOM 2434 C THR A 397 23.150 13.726 57.747 1.00164.12 C
ANISOU 2434 C THR A 397 30832 20289 11237 -2079 -3096 -324 C
ATOM 2435 O THR A 397 23.198 13.808 58.980 1.00171.16 O
ANISOU 2435 O THR A 397 31894 21137 12003 -1986 -3120 -323 O
ATOM 2436 CB THR A 397 22.886 11.323 57.017 1.00149.64 C
ANISOU 2436 CB THR A 397 29192 18300 9367 -2269 -3059 -160 C
ATOM 2437 OG1 THR A 397 22.082 10.381 57.736 1.00149.93 O
ANISOU 2437 OG1 THR A 397 29477 18275 9215 -2394 -2919 -35 O
ATOM 2438 CG2 THR A 397 24.298 11.329 57.596 1.00150.83 C
ANISOU 2438 CG2 THR A 397 29422 18331 9554 -2030 -3317 -244 C
ATOM 2439 N ALA A 398 23.861 14.529 56.949 1.00164.67 N
ANISOU 2439 N ALA A 398 30720 20382 11465 -2041 -3202 -433 N
ATOM 2440 CA ALA A 398 24.699 15.584 57.510 1.00170.78 C
ANISOU 2440 CA ALA A 398 31497 21130 12263 -1933 -3346 -566 C
ATOM 2441 C ALA A 398 23.875 16.566 58.335 1.00177.28 C
ANISOU 2441 C ALA A 398 32409 21998 12950 -1898 -3189 -571 C
ATOM 2442 O ALA A 398 24.337 17.058 59.371 1.00182.07 O
ANISOU 2442 O ALA A 398 33144 22550 13487 -1809 -3288 -647 O
ATOM 2443 CB ALA A 398 25.443 16.312 56.391 1.00168.02 C
ANISOU 2443 CB ALA A 398 30947 20806 12086 -1960 -3442 -670 C
ATOM 2444 N VAL A 399 22.649 16.864 57.892 1.00177.97 N
ANISOU 2444 N VAL A 399 32427 22214 12980 -1947 -2943 -492 N
ATOM 2445 CA VAL A 399 21.732 17.672 58.693 1.00177.13 C
ANISOU 2445 CA VAL A 399 32410 22190 12702 -1862 -2764 -469 C
ATOM 2446 C VAL A 399 20.733 16.818 59.464 1.00180.98 C
ANISOU 2446 C VAL A 399 32984 22773 13009 -1896 -2614 -325 C
ATOM 2447 O VAL A 399 20.046 17.342 60.356 1.00180.31 O
ANISOU 2447 O VAL A 399 32989 22768 12753 -1795 -2485 -295 O
ATOM 2448 CB VAL A 399 20.983 18.697 57.818 1.00171.05 C
ANISOU 2448 CB VAL A 399 31506 21559 11926 -1827 -2567 -471 C
ATOM 2449 CG1 VAL A 399 21.974 19.633 57.142 1.00168.47 C
ANISOU 2449 CG1 VAL A 399 31156 21103 11751 -1813 -2698 -612 C
ATOM 2450 CG2 VAL A 399 20.105 17.996 56.791 1.00165.99 C
ANISOU 2450 CG2 VAL A 399 30662 21115 11291 -1946 -2408 -358 C
ATOM 2451 N GLY A 400 20.632 15.525 59.150 1.00186.76 N
ANISOU 2451 N GLY A 400 33713 23493 13756 -2040 -2619 -235 N
ATOM 2452 CA GLY A 400 19.879 14.571 59.945 1.00193.10 C
ANISOU 2452 CA GLY A 400 34658 24331 14381 -2123 -2502 -104 C
ATOM 2453 C GLY A 400 18.402 14.878 60.083 1.00202.57 C
ANISOU 2453 C GLY A 400 35759 25814 15395 -2175 -2220 0 C
ATOM 2454 O GLY A 400 17.877 14.946 61.200 1.00207.64 O
ANISOU 2454 O GLY A 400 36524 26517 15853 -2107 -2127 59 O
ATOM 2455 N CYS A 401 17.711 15.037 58.954 1.00207.11 N
ANISOU 2455 N CYS A 401 36091 26604 15997 -2279 -2079 27 N
ATOM 2456 CA CYS A 401 16.341 15.532 59.002 1.00215.26 C
ANISOU 2456 CA CYS A 401 36959 27995 16835 -2267 -1811 112 C
ATOM 2457 C CYS A 401 15.319 14.415 59.161 1.00226.67 C
ANISOU 2457 C CYS A 401 38377 29641 18107 -2535 -1642 258 C
ATOM 2458 O CYS A 401 14.386 14.540 59.960 1.00234.32 O
ANISOU 2458 O CYS A 401 39334 30847 18851 -2510 -1464 349 O
ATOM 2459 CB CYS A 401 16.040 16.346 57.746 1.00211.27 C
ANISOU 2459 CB CYS A 401 36188 27684 16401 -2210 -1723 70 C
ATOM 2460 SG CYS A 401 16.651 18.047 57.818 1.00208.92 S
ANISOU 2460 SG CYS A 401 35953 27258 16168 -1876 -1778 -65 S
ATOM 2461 N SER A 402 15.463 13.324 58.424 1.00225.58 N
ANISOU 2461 N SER A 402 38240 29417 18051 -2803 -1688 281 N
ATOM 2462 CA SER A 402 14.394 12.339 58.316 1.00227.80 C
ANISOU 2462 CA SER A 402 38467 29922 18164 -3136 -1503 405 C
ATOM 2463 C SER A 402 14.869 10.963 58.768 1.00229.54 C
ANISOU 2463 C SER A 402 39031 29806 18379 -3342 -1597 453 C
ATOM 2464 O SER A 402 16.035 10.759 59.119 1.00228.38 O
ANISOU 2464 O SER A 402 39129 29290 18356 -3181 -1811 392 O
ATOM 2465 CB SER A 402 13.856 12.278 56.884 1.00226.14 C
ANISOU 2465 CB SER A 402 37944 29977 18004 -3321 -1415 394 C
ATOM 2466 OG SER A 402 12.981 11.177 56.716 1.00227.42 O
ANISOU 2466 OG SER A 402 38079 30310 18019 -3723 -1272 491 O
ATOM 2467 N VAL A 403 13.932 10.018 58.736 1.00229.79 N
ANISOU 2467 N VAL A 403 39078 29989 18243 -3702 -1424 563 N
ATOM 2468 CA VAL A 403 14.115 8.652 59.219 1.00225.21 C
ANISOU 2468 CA VAL A 403 38882 29102 17587 -3944 -1444 636 C
ATOM 2469 C VAL A 403 15.152 7.929 58.369 1.00224.10 C
ANISOU 2469 C VAL A 403 38919 28589 17642 -3970 -1644 563 C
ATOM 2470 O VAL A 403 14.973 7.803 57.148 1.00222.87 O
ANISOU 2470 O VAL A 403 38565 28540 17574 -4140 -1633 523 O
ATOM 2471 CB VAL A 403 12.785 7.880 59.200 1.00219.44 C
ANISOU 2471 CB VAL A 403 38096 28657 16624 -4400 -1189 760 C
ATOM 2472 CG1 VAL A 403 12.772 6.804 60.277 1.00217.60 C
ANISOU 2472 CG1 VAL A 403 38310 28145 16224 -4571 -1144 868 C
ATOM 2473 CG2 VAL A 403 11.605 8.830 59.345 1.00216.83 C
ANISOU 2473 CG2 VAL A 403 37352 28900 16134 -4362 -974 806 C
ATOM 2474 N PRO A 404 16.246 7.448 58.959 1.00221.31 N
ANISOU 2474 N PRO A 404 38920 27825 17343 -3776 -1828 544 N
ATOM 2475 CA PRO A 404 17.153 6.572 58.210 1.00221.40 C
ANISOU 2475 CA PRO A 404 39141 27499 17483 -3788 -1993 501 C
ATOM 2476 C PRO A 404 16.832 5.101 58.429 1.00225.22 C
ANISOU 2476 C PRO A 404 40047 27733 17795 -4101 -1900 605 C
ATOM 2477 O PRO A 404 17.125 4.264 57.571 1.00228.00 O
ANISOU 2477 O PRO A 404 40558 27877 18196 -4240 -1951 587 O
ATOM 2478 CB PRO A 404 18.527 6.941 58.778 1.00216.56 C
ANISOU 2478 CB PRO A 404 38648 26646 16990 -3357 -2238 423 C
ATOM 2479 CG PRO A 404 18.230 7.272 60.210 1.00216.52 C
ANISOU 2479 CG PRO A 404 38758 26687 16822 -3245 -2171 478 C
ATOM 2480 CD PRO A 404 16.838 7.886 60.237 1.00217.61 C
ANISOU 2480 CD PRO A 404 38618 27225 16838 -3450 -1924 536 C
ATOM 2481 N ARG A 405 16.206 4.787 59.568 1.00225.66 N
ANISOU 2481 N ARG A 405 40309 27798 17634 -4217 -1751 714 N
ATOM 2482 CA ARG A 405 16.004 3.398 59.972 1.00226.03 C
ANISOU 2482 CA ARG A 405 40850 27537 17495 -4490 -1660 819 C
ATOM 2483 C ARG A 405 15.290 2.589 58.891 1.00223.33 C
ANISOU 2483 C ARG A 405 40526 27225 17106 -4985 -1534 835 C
ATOM 2484 O ARG A 405 15.750 1.509 58.503 1.00221.88 O
ANISOU 2484 O ARG A 405 40748 26651 16906 -5087 -1589 839 O
ATOM 2485 CB ARG A 405 15.221 3.352 61.286 1.00227.89 C
ANISOU 2485 CB ARG A 405 41210 27881 17496 -4589 -1475 940 C
ATOM 2486 N THR A 406 14.169 3.103 58.381 1.00222.79 N
ANISOU 2486 N THR A 406 40020 27634 16997 -5283 -1365 840 N
ATOM 2487 CA THR A 406 13.383 2.341 57.416 1.00222.39 C
ANISOU 2487 CA THR A 406 39949 27683 16868 -5813 -1234 848 C
ATOM 2488 C THR A 406 13.894 2.507 55.989 1.00220.90 C
ANISOU 2488 C THR A 406 39553 27486 16895 -5738 -1382 723 C
ATOM 2489 O THR A 406 13.725 1.599 55.166 1.00221.43 O
ANISOU 2489 O THR A 406 39795 27413 16925 -6086 -1358 705 O
ATOM 2490 CB THR A 406 11.909 2.753 57.492 1.00218.69 C
ANISOU 2490 CB THR A 406 39055 27810 16225 -6174 -978 910 C
ATOM 2491 OG1 THR A 406 11.803 4.124 57.894 1.00215.09 O
ANISOU 2491 OG1 THR A 406 38178 27719 15825 -5783 -980 893 O
ATOM 2492 CG2 THR A 406 11.154 1.877 58.486 1.00217.43 C
ANISOU 2492 CG2 THR A 406 39226 27597 15790 -6566 -773 1050 C
ATOM 2493 N LEU A 407 14.534 3.634 55.680 1.00214.85 N
ANISOU 2493 N LEU A 407 38444 26847 16343 -5299 -1532 634 N
ATOM 2494 CA LEU A 407 14.853 3.963 54.296 1.00206.97 C
ANISOU 2494 CA LEU A 407 37156 25941 15541 -5237 -1636 523 C
ATOM 2495 C LEU A 407 16.259 3.536 53.896 1.00202.27 C
ANISOU 2495 C LEU A 407 36847 24886 15122 -4926 -1881 456 C
ATOM 2496 O LEU A 407 16.477 3.130 52.749 1.00193.30 O
ANISOU 2496 O LEU A 407 35695 23674 14076 -5013 -1943 394 O
ATOM 2497 CB LEU A 407 14.686 5.469 54.070 1.00203.37 C
ANISOU 2497 CB LEU A 407 36163 25907 15203 -4960 -1633 466 C
ATOM 2498 N PHE A 408 17.215 3.634 54.824 1.00208.34 N
ANISOU 2498 N PHE A 408 37850 25384 15925 -4547 -2021 466 N
ATOM 2499 CA PHE A 408 18.608 3.320 54.520 1.00210.55 C
ANISOU 2499 CA PHE A 408 38333 25315 16351 -4187 -2258 405 C
ATOM 2500 C PHE A 408 18.747 1.938 53.891 1.00218.03 C
ANISOU 2500 C PHE A 408 39701 25915 17224 -4383 -2262 425 C
ATOM 2501 O PHE A 408 19.471 1.762 52.904 1.00215.73 O
ANISOU 2501 O PHE A 408 39387 25509 17073 -4223 -2403 354 O
ATOM 2502 CB PHE A 408 19.431 3.438 55.805 1.00205.60 C
ANISOU 2502 CB PHE A 408 37931 24496 15690 -3818 -2372 429 C
ATOM 2503 CG PHE A 408 20.815 2.861 55.721 1.00196.28 C
ANISOU 2503 CG PHE A 408 37027 22976 14575 -3453 -2593 394 C
ATOM 2504 CD1 PHE A 408 21.040 1.522 56.004 1.00192.88 C
ANISOU 2504 CD1 PHE A 408 37151 22154 13980 -3478 -2581 467 C
ATOM 2505 CD2 PHE A 408 21.899 3.667 55.417 1.00186.94 C
ANISOU 2505 CD2 PHE A 408 35559 21879 13590 -3070 -2804 293 C
ATOM 2506 CE1 PHE A 408 22.311 0.991 55.945 1.00186.65 C
ANISOU 2506 CE1 PHE A 408 36608 21095 13217 -3076 -2775 442 C
ATOM 2507 CE2 PHE A 408 23.176 3.142 55.361 1.00181.70 C
ANISOU 2507 CE2 PHE A 408 35097 20986 12955 -2712 -3004 266 C
ATOM 2508 CZ PHE A 408 23.381 1.801 55.626 1.00181.18 C
ANISOU 2508 CZ PHE A 408 35565 20559 12716 -2685 -2990 343 C
ATOM 2509 N LYS A 409 18.044 0.946 54.444 1.00227.98 N
ANISOU 2509 N LYS A 409 41373 26999 18251 -4738 -2099 522 N
ATOM 2510 CA LYS A 409 18.145 -0.418 53.931 1.00232.71 C
ANISOU 2510 CA LYS A 409 42479 27200 18739 -4949 -2085 541 C
ATOM 2511 C LYS A 409 17.642 -0.510 52.495 1.00233.17 C
ANISOU 2511 C LYS A 409 42300 27428 18865 -5266 -2050 466 C
ATOM 2512 O LYS A 409 18.260 -1.168 51.649 1.00233.60 O
ANISOU 2512 O LYS A 409 42586 27203 18968 -5178 -2157 417 O
ATOM 2513 CB LYS A 409 17.366 -1.375 54.834 1.00237.07 C
ANISOU 2513 CB LYS A 409 43519 27548 19009 -5343 -1884 660 C
ATOM 2514 N PHE A 410 16.515 0.141 52.204 1.00225.91 N
ANISOU 2514 N PHE A 410 40911 26991 17932 -5608 -1897 454 N
ATOM 2515 CA PHE A 410 15.949 0.075 50.861 1.00217.50 C
ANISOU 2515 CA PHE A 410 39577 26154 16908 -5922 -1855 376 C
ATOM 2516 C PHE A 410 16.855 0.761 49.846 1.00206.07 C
ANISOU 2516 C PHE A 410 37804 24762 15732 -5497 -2052 268 C
ATOM 2517 O PHE A 410 17.090 0.232 48.753 1.00205.55 O
ANISOU 2517 O PHE A 410 37814 24566 15719 -5557 -2116 202 O
ATOM 2518 CB PHE A 410 14.556 0.706 50.852 1.00216.15 C
ANISOU 2518 CB PHE A 410 38913 26574 16638 -6311 -1646 392 C
ATOM 2519 N PHE A 411 17.378 1.938 50.193 1.00197.99 N
ANISOU 2519 N PHE A 411 36434 23922 14872 -5076 -2145 248 N
ATOM 2520 CA PHE A 411 18.214 2.699 49.276 1.00185.06 C
ANISOU 2520 CA PHE A 411 34462 22369 13483 -4704 -2314 151 C
ATOM 2521 C PHE A 411 19.600 2.092 49.112 1.00173.96 C
ANISOU 2521 C PHE A 411 33396 20537 12165 -4332 -2526 130 C
ATOM 2522 O PHE A 411 20.217 2.264 48.053 1.00161.98 O
ANISOU 2522 O PHE A 411 31702 19033 10810 -4137 -2648 55 O
ATOM 2523 CB PHE A 411 18.333 4.149 49.755 1.00187.53 C
ANISOU 2523 CB PHE A 411 34360 22981 13912 -4415 -2334 134 C
ATOM 2524 CG PHE A 411 17.080 4.961 49.570 1.00188.33 C
ANISOU 2524 CG PHE A 411 34022 23580 13954 -4649 -2141 138 C
ATOM 2525 CD1 PHE A 411 15.939 4.403 49.018 1.00192.62 C
ANISOU 2525 CD1 PHE A 411 34488 24345 14353 -5110 -1972 152 C
ATOM 2526 CD2 PHE A 411 17.048 6.292 49.938 1.00184.84 C
ANISOU 2526 CD2 PHE A 411 33239 23404 13590 -4392 -2124 124 C
ATOM 2527 CE1 PHE A 411 14.792 5.161 48.847 1.00192.65 C
ANISOU 2527 CE1 PHE A 411 34008 24881 14311 -5262 -1786 159 C
ATOM 2528 CE2 PHE A 411 15.911 7.057 49.766 1.00183.94 C
ANISOU 2528 CE2 PHE A 411 32701 23761 13427 -4514 -1930 136 C
ATOM 2529 CZ PHE A 411 14.781 6.492 49.223 1.00187.67 C
ANISOU 2529 CZ PHE A 411 33039 24507 13761 -4929 -1761 157 C
ATOM 2530 N PHE A 412 20.105 1.394 50.135 1.00181.45 N
ANISOU 2530 N PHE A 412 34814 21138 12990 -4199 -2566 198 N
ATOM 2531 CA PHE A 412 21.391 0.723 49.999 1.00181.03 C
ANISOU 2531 CA PHE A 412 35096 20719 12969 -3809 -2753 188 C
ATOM 2532 C PHE A 412 21.302 -0.439 49.019 1.00175.17 C
ANISOU 2532 C PHE A 412 34700 19706 12150 -3997 -2733 176 C
ATOM 2533 O PHE A 412 22.254 -0.690 48.273 1.00170.58 O
ANISOU 2533 O PHE A 412 34169 18984 11661 -3670 -2888 130 O
ATOM 2534 CB PHE A 412 21.889 0.251 51.366 1.00189.53 C
ANISOU 2534 CB PHE A 412 36596 21519 13898 -3595 -2784 267 C
ATOM 2535 CG PHE A 412 23.278 -0.337 51.339 1.00194.18 C
ANISOU 2535 CG PHE A 412 37474 21812 14492 -3103 -2980 260 C
ATOM 2536 CD1 PHE A 412 24.396 0.470 51.488 1.00190.46 C
ANISOU 2536 CD1 PHE A 412 36689 21506 14171 -2637 -3178 206 C
ATOM 2537 CD2 PHE A 412 23.466 -1.700 51.170 1.00200.20 C
ANISOU 2537 CD2 PHE A 412 38833 22151 15084 -3105 -2961 306 C
ATOM 2538 CE1 PHE A 412 25.675 -0.071 51.467 1.00191.33 C
ANISOU 2538 CE1 PHE A 412 37009 21431 14255 -2167 -3355 201 C
ATOM 2539 CE2 PHE A 412 24.738 -2.247 51.146 1.00201.12 C
ANISOU 2539 CE2 PHE A 412 39208 22035 15174 -2591 -3131 306 C
ATOM 2540 CZ PHE A 412 25.844 -1.432 51.295 1.00197.15 C
ANISOU 2540 CZ PHE A 412 38324 21770 14817 -2112 -3329 256 C
ATOM 2541 N TRP A 413 20.172 -1.149 48.993 1.00179.13 N
ANISOU 2541 N TRP A 413 35442 20151 12470 -4532 -2543 212 N
ATOM 2542 CA TRP A 413 19.985 -2.186 47.982 1.00187.42 C
ANISOU 2542 CA TRP A 413 36812 20961 13439 -4782 -2517 178 C
ATOM 2543 C TRP A 413 19.719 -1.572 46.614 1.00180.48 C
ANISOU 2543 C TRP A 413 35405 20432 12736 -4863 -2542 72 C
ATOM 2544 O TRP A 413 20.262 -2.026 45.599 1.00171.60 O
ANISOU 2544 O TRP A 413 34389 19141 11670 -4717 -2642 13 O
ATOM 2545 CB TRP A 413 18.832 -3.108 48.372 1.00196.05 C
ANISOU 2545 CB TRP A 413 38317 21911 14264 -5405 -2301 237 C
ATOM 2546 CG TRP A 413 18.991 -3.829 49.665 1.00199.35 C
ANISOU 2546 CG TRP A 413 39321 21946 14478 -5373 -2245 349 C
ATOM 2547 CD1 TRP A 413 20.152 -4.092 50.332 1.00198.66 C
ANISOU 2547 CD1 TRP A 413 39568 21527 14386 -4824 -2382 392 C
ATOM 2548 CD2 TRP A 413 17.937 -4.378 50.460 1.00200.83 C
ANISOU 2548 CD2 TRP A 413 39814 22076 14419 -5910 -2025 434 C
ATOM 2549 NE1 TRP A 413 19.884 -4.776 51.495 1.00200.16 N
ANISOU 2549 NE1 TRP A 413 40277 21428 14348 -4961 -2261 498 N
ATOM 2550 CE2 TRP A 413 18.530 -4.963 51.596 1.00201.23 C
ANISOU 2550 CE2 TRP A 413 40415 21708 14334 -5638 -2038 529 C
ATOM 2551 CE3 TRP A 413 16.546 -4.432 50.320 1.00200.05 C
ANISOU 2551 CE3 TRP A 413 39549 22276 14185 -6597 -1815 439 C
ATOM 2552 CZ2 TRP A 413 17.780 -5.595 52.586 1.00203.07 C
ANISOU 2552 CZ2 TRP A 413 41071 21772 14316 -6034 -1840 633 C
ATOM 2553 CZ3 TRP A 413 15.804 -5.058 51.302 1.00201.73 C
ANISOU 2553 CZ3 TRP A 413 40151 22354 14141 -7018 -1620 543 C
ATOM 2554 CH2 TRP A 413 16.422 -5.632 52.421 1.00203.73 C
ANISOU 2554 CH2 TRP A 413 40986 22144 14277 -6738 -1630 641 C
ATOM 2555 N PHE A 414 18.872 -0.540 46.573 1.00177.18 N
ANISOU 2555 N PHE A 414 34425 20510 12387 -5065 -2443 50 N
ATOM 2556 CA PHE A 414 18.439 0.048 45.310 1.00165.17 C
ANISOU 2556 CA PHE A 414 32396 19364 10996 -5173 -2432 -44 C
ATOM 2557 C PHE A 414 19.624 0.531 44.486 1.00160.62 C
ANISOU 2557 C PHE A 414 31617 18756 10655 -4656 -2632 -110 C
ATOM 2558 O PHE A 414 19.729 0.230 43.292 1.00170.27 O
ANISOU 2558 O PHE A 414 32790 19966 11937 -4668 -2678 -181 O
ATOM 2559 CB PHE A 414 17.470 1.200 45.582 1.00164.77 C
ANISOU 2559 CB PHE A 414 31784 19860 10961 -5333 -2294 -38 C
ATOM 2560 CG PHE A 414 16.289 1.240 44.648 1.00173.56 C
ANISOU 2560 CG PHE A 414 32515 21377 12055 -5755 -2144 -94 C
ATOM 2561 CD1 PHE A 414 15.163 0.471 44.902 1.00179.37 C
ANISOU 2561 CD1 PHE A 414 33438 22195 12520 -6350 -1971 -65 C
ATOM 2562 CD2 PHE A 414 16.298 2.055 43.525 1.00176.42 C
ANISOU 2562 CD2 PHE A 414 32319 22065 12647 -5565 -2169 -175 C
ATOM 2563 CE1 PHE A 414 14.073 0.507 44.051 1.00182.46 C
ANISOU 2563 CE1 PHE A 414 33434 23030 12864 -6753 -1843 -127 C
ATOM 2564 CE2 PHE A 414 15.207 2.095 42.669 1.00176.53 C
ANISOU 2564 CE2 PHE A 414 31961 22499 12613 -5920 -2037 -230 C
ATOM 2565 CZ PHE A 414 14.096 1.319 42.934 1.00179.17 C
ANISOU 2565 CZ PHE A 414 32452 22956 12670 -6517 -1881 -212 C
ATOM 2566 N GLY A 415 20.523 1.296 45.104 1.00160.91 N
ANISOU 2566 N GLY A 415 31519 18802 10819 -4215 -2752 -90 N
ATOM 2567 CA GLY A 415 21.737 1.672 44.407 1.00169.91 C
ANISOU 2567 CA GLY A 415 32495 19911 12153 -3746 -2944 -142 C
ATOM 2568 C GLY A 415 22.542 0.469 43.965 1.00186.24 C
ANISOU 2568 C GLY A 415 35036 21571 14156 -3561 -3054 -140 C
ATOM 2569 O GLY A 415 23.107 0.461 42.869 1.00195.69 O
ANISOU 2569 O GLY A 415 36107 22782 15463 -3351 -3155 -197 O
ATOM 2570 N TYR A 416 22.558 -0.587 44.781 1.00196.08 N
ANISOU 2570 N TYR A 416 36856 22444 15200 -3630 -3021 -70 N
ATOM 2571 CA TYR A 416 23.399 -1.741 44.489 1.00199.72 C
ANISOU 2571 CA TYR A 416 37841 22481 15564 -3369 -3119 -56 C
ATOM 2572 C TYR A 416 22.903 -2.555 43.301 1.00196.46 C
ANISOU 2572 C TYR A 416 37630 21930 15088 -3653 -3063 -110 C
ATOM 2573 O TYR A 416 23.719 -3.088 42.541 1.00195.95 O
ANISOU 2573 O TYR A 416 37755 21663 15033 -3329 -3178 -136 O
ATOM 2574 CB TYR A 416 23.505 -2.644 45.716 1.00216.46 C
ANISOU 2574 CB TYR A 416 40574 24213 17456 -3356 -3076 40 C
ATOM 2575 CG TYR A 416 24.877 -3.243 45.852 1.00231.09 C
ANISOU 2575 CG TYR A 416 42768 25775 19262 -2767 -3241 68 C
ATOM 2576 CD1 TYR A 416 25.361 -4.129 44.905 1.00237.99 C
ANISOU 2576 CD1 TYR A 416 43969 26379 20076 -2589 -3299 45 C
ATOM 2577 CD2 TYR A 416 25.701 -2.906 46.910 1.00236.87 C
ANISOU 2577 CD2 TYR A 416 43471 26539 19991 -2364 -3342 112 C
ATOM 2578 CE1 TYR A 416 26.620 -4.671 45.011 1.00244.34 C
ANISOU 2578 CE1 TYR A 416 45057 26970 20812 -1997 -3441 75 C
ATOM 2579 CE2 TYR A 416 26.967 -3.448 47.026 1.00242.71 C
ANISOU 2579 CE2 TYR A 416 44465 27092 20662 -1795 -3492 135 C
ATOM 2580 CZ TYR A 416 27.420 -4.329 46.071 1.00248.35 C
ANISOU 2580 CZ TYR A 416 45492 27559 21310 -1599 -3536 121 C
ATOM 2581 OH TYR A 416 28.676 -4.875 46.166 1.00254.53 O
ANISOU 2581 OH TYR A 416 46506 28202 22001 -987 -3674 148 O
ATOM 2582 N CYS A 417 21.587 -2.679 43.121 1.00192.45 N
ANISOU 2582 N CYS A 417 37077 21550 14495 -4249 -2889 -133 N
ATOM 2583 CA CYS A 417 21.082 -3.482 42.012 1.00187.87 C
ANISOU 2583 CA CYS A 417 36697 20850 13837 -4570 -2840 -202 C
ATOM 2584 C CYS A 417 21.357 -2.849 40.653 1.00191.99 C
ANISOU 2584 C CYS A 417 36717 21664 14568 -4370 -2933 -300 C
ATOM 2585 O CYS A 417 21.134 -3.505 39.629 1.00198.24 O
ANISOU 2585 O CYS A 417 37664 22346 15312 -4534 -2927 -370 O
ATOM 2586 CB CYS A 417 19.581 -3.724 42.170 1.00178.80 C
ANISOU 2586 CB CYS A 417 35552 19857 12527 -5299 -2631 -211 C
ATOM 2587 SG CYS A 417 18.562 -2.277 41.826 1.00166.42 S
ANISOU 2587 SG CYS A 417 33079 19042 11111 -5537 -2537 -266 S
ATOM 2588 N ASN A 418 21.831 -1.600 40.626 1.00182.82 N
ANISOU 2588 N ASN A 418 34986 20854 13623 -4030 -3015 -308 N
ATOM 2589 CA ASN A 418 22.180 -0.941 39.371 1.00170.27 C
ANISOU 2589 CA ASN A 418 32914 19529 12253 -3793 -3092 -384 C
ATOM 2590 C ASN A 418 23.164 -1.768 38.555 1.00164.35 C
ANISOU 2590 C ASN A 418 32520 18461 11465 -3442 -3236 -408 C
ATOM 2591 O ASN A 418 23.089 -1.800 37.322 1.00159.96 O
ANISOU 2591 O ASN A 418 31780 18005 10991 -3436 -3251 -483 O
ATOM 2592 CB ASN A 418 22.765 0.441 39.668 1.00162.40 C
ANISOU 2592 CB ASN A 418 31341 18843 11520 -3427 -3147 -365 C
ATOM 2593 CG ASN A 418 23.266 1.145 38.428 1.00157.55 C
ANISOU 2593 CG ASN A 418 30227 18467 11169 -3133 -3209 -422 C
ATOM 2594 OD1 ASN A 418 22.517 1.861 37.765 1.00150.65 O
ANISOU 2594 OD1 ASN A 418 28872 17936 10432 -3301 -3101 -466 O
ATOM 2595 ND2 ASN A 418 24.542 0.950 38.108 1.00160.25 N
ANISOU 2595 ND2 ASN A 418 30675 18654 11560 -2670 -3377 -414 N
ATOM 2596 N SER A 419 24.094 -2.448 39.230 1.00165.07 N
ANISOU 2596 N SER A 419 33079 18183 11456 -3099 -3325 -339 N
ATOM 2597 CA SER A 419 25.124 -3.202 38.525 1.00163.20 C
ANISOU 2597 CA SER A 419 33154 17674 11181 -2659 -3454 -344 C
ATOM 2598 C SER A 419 24.559 -4.451 37.860 1.00164.58 C
ANISOU 2598 C SER A 419 33866 17496 11172 -2965 -3379 -386 C
ATOM 2599 O SER A 419 25.029 -4.847 36.788 1.00167.34 O
ANISOU 2599 O SER A 419 34297 17754 11529 -2727 -3454 -434 O
ATOM 2600 CB SER A 419 26.252 -3.570 39.491 1.00163.61 C
ANISOU 2600 CB SER A 419 33535 17483 11144 -2172 -3560 -255 C
ATOM 2601 OG SER A 419 27.099 -2.461 39.739 1.00161.80 O
ANISOU 2601 OG SER A 419 32783 17598 11096 -1789 -3684 -244 O
ATOM 2602 N SER A 420 23.557 -5.082 38.472 1.00167.51 N
ANISOU 2602 N SER A 420 34616 17667 11362 -3504 -3227 -369 N
ATOM 2603 CA SER A 420 22.953 -6.274 37.893 1.00171.17 C
ANISOU 2603 CA SER A 420 35629 17779 11628 -3891 -3143 -416 C
ATOM 2604 C SER A 420 21.984 -5.953 36.766 1.00176.19 C
ANISOU 2604 C SER A 420 35838 18760 12346 -4330 -3078 -537 C
ATOM 2605 O SER A 420 21.792 -6.786 35.874 1.00178.34 O
ANISOU 2605 O SER A 420 36437 18807 12516 -4491 -3070 -609 O
ATOM 2606 CB SER A 420 22.220 -7.071 38.976 1.00172.45 C
ANISOU 2606 CB SER A 420 36367 17612 11544 -4366 -2992 -351 C
ATOM 2607 OG SER A 420 21.685 -8.274 38.449 1.00159.17 O
ANISOU 2607 OG SER A 420 35294 15538 9647 -4774 -2908 -396 O
ATOM 2608 N LEU A 421 21.375 -4.770 36.783 1.00170.87 N
ANISOU 2608 N LEU A 421 34455 18630 11837 -4504 -3031 -563 N
ATOM 2609 CA LEU A 421 20.307 -4.434 35.855 1.00168.48 C
ANISOU 2609 CA LEU A 421 33712 18726 11576 -4946 -2945 -672 C
ATOM 2610 C LEU A 421 20.786 -3.670 34.631 1.00163.82 C
ANISOU 2610 C LEU A 421 32597 18448 11199 -4564 -3051 -744 C
ATOM 2611 O LEU A 421 19.953 -3.228 33.833 1.00166.01 O
ANISOU 2611 O LEU A 421 32419 19127 11529 -4845 -2985 -832 O
ATOM 2612 CB LEU A 421 19.224 -3.628 36.576 1.00166.36 C
ANISOU 2612 CB LEU A 421 32995 18906 11309 -5364 -2800 -652 C
ATOM 2613 CG LEU A 421 18.614 -4.297 37.808 1.00166.57 C
ANISOU 2613 CG LEU A 421 33480 18698 11109 -5800 -2669 -574 C
ATOM 2614 CD1 LEU A 421 17.615 -3.369 38.478 1.00165.60 C
ANISOU 2614 CD1 LEU A 421 32835 19096 10991 -6119 -2532 -546 C
ATOM 2615 CD2 LEU A 421 17.963 -5.622 37.441 1.00169.63 C
ANISOU 2615 CD2 LEU A 421 34430 18762 11260 -6346 -2582 -626 C
ATOM 2616 N ASN A 422 22.106 -3.491 34.449 1.00163.43 N
ANISOU 2616 N ASN A 422 32574 18261 11261 -3923 -3209 -705 N
ATOM 2617 CA ASN A 422 22.585 -2.863 33.233 1.00158.63 C
ANISOU 2617 CA ASN A 422 31485 17918 10870 -3564 -3287 -758 C
ATOM 2618 C ASN A 422 22.326 -3.733 32.011 1.00160.22 C
ANISOU 2618 C ASN A 422 31963 17972 10940 -3709 -3305 -866 C
ATOM 2619 O ASN A 422 21.709 -3.249 31.040 1.00139.69 O
ANISOU 2619 O ASN A 422 28870 15741 8466 -3861 -3254 -950 O
ATOM 2620 CB ASN A 422 24.062 -2.473 33.378 1.00161.64 C
ANISOU 2620 CB ASN A 422 31791 18235 11389 -2877 -3440 -682 C
ATOM 2621 CG ASN A 422 24.246 -1.138 34.070 1.00159.91 C
ANISOU 2621 CG ASN A 422 30983 18364 11413 -2730 -3420 -622 C
ATOM 2622 OD1 ASN A 422 23.628 -0.140 33.697 1.00156.08 O
ANISOU 2622 OD1 ASN A 422 29898 18281 11124 -2868 -3326 -652 O
ATOM 2623 ND2 ASN A 422 25.102 -1.113 35.084 1.00166.54 N
ANISOU 2623 ND2 ASN A 422 32014 19050 12213 -2435 -3508 -541 N
ATOM 2624 N PRO A 423 22.729 -5.012 31.970 1.00159.04 N
ANISOU 2624 N PRO A 423 32517 17299 10612 -3643 -3341 -859 N
ATOM 2625 CA PRO A 423 22.366 -5.857 30.823 1.00157.50 C
ANISOU 2625 CA PRO A 423 32582 16946 10314 -3837 -3332 -968 C
ATOM 2626 C PRO A 423 20.872 -6.098 30.697 1.00159.73 C
ANISOU 2626 C PRO A 423 32797 17397 10497 -4617 -3180 -1060 C
ATOM 2627 O PRO A 423 20.426 -6.574 29.646 1.00156.68 O
ANISOU 2627 O PRO A 423 32456 17020 10055 -4838 -3171 -1175 O
ATOM 2628 CB PRO A 423 23.121 -7.166 31.090 1.00150.33 C
ANISOU 2628 CB PRO A 423 32533 15386 9201 -3591 -3381 -913 C
ATOM 2629 CG PRO A 423 24.231 -6.773 32.011 1.00148.73 C
ANISOU 2629 CG PRO A 423 32322 15132 9056 -3029 -3471 -784 C
ATOM 2630 CD PRO A 423 23.610 -5.748 32.899 1.00168.79 C
ANISOU 2630 CD PRO A 423 34361 18056 11717 -3323 -3395 -751 C
ATOM 2631 N VAL A 424 20.092 -5.783 31.730 1.00174.64 N
ANISOU 2631 N VAL A 424 34557 19452 12347 -5037 -3062 -1015 N
ATOM 2632 CA VAL A 424 18.643 -5.927 31.646 1.00184.35 C
ANISOU 2632 CA VAL A 424 35623 20955 13466 -5787 -2909 -1095 C
ATOM 2633 C VAL A 424 18.074 -4.933 30.638 1.00179.86 C
ANISOU 2633 C VAL A 424 34256 21038 13046 -5819 -2899 -1195 C
ATOM 2634 O VAL A 424 17.519 -5.322 29.603 1.00177.99 O
ANISOU 2634 O VAL A 424 33954 20920 12753 -6086 -2885 -1319 O
ATOM 2635 CB VAL A 424 18.013 -5.770 33.042 1.00192.65 C
ANISOU 2635 CB VAL A 424 36704 22070 14423 -6162 -2782 -1004 C
ATOM 2636 CG1 VAL A 424 16.497 -5.714 32.958 1.00197.15 C
ANISOU 2636 CG1 VAL A 424 36942 23086 14878 -6908 -2619 -1079 C
ATOM 2637 CG2 VAL A 424 18.458 -6.916 33.949 1.00198.77 C
ANISOU 2637 CG2 VAL A 424 38355 22168 14999 -6189 -2772 -912 C
ATOM 2638 N ILE A 425 18.237 -3.634 30.908 1.00178.79 N
ANISOU 2638 N ILE A 425 33525 21321 13088 -5519 -2907 -1142 N
ATOM 2639 CA ILE A 425 17.804 -2.620 29.948 1.00176.80 C
ANISOU 2639 CA ILE A 425 32492 21659 13026 -5420 -2872 -1204 C
ATOM 2640 C ILE A 425 18.574 -2.755 28.643 1.00172.76 C
ANISOU 2640 C ILE A 425 31979 21047 12615 -4993 -2998 -1269 C
ATOM 2641 O ILE A 425 18.075 -2.385 27.572 1.00164.74 O
ANISOU 2641 O ILE A 425 30513 20424 11657 -5031 -2973 -1363 O
ATOM 2642 CB ILE A 425 17.963 -1.208 30.550 1.00175.18 C
ANISOU 2642 CB ILE A 425 31672 21814 13074 -5085 -2819 -1099 C
ATOM 2643 N TYR A 426 19.790 -3.299 28.710 1.00173.67 N
ANISOU 2643 N TYR A 426 32595 20664 12726 -4557 -3131 -1218 N
ATOM 2644 CA TYR A 426 20.647 -3.404 27.534 1.00169.53 C
ANISOU 2644 CA TYR A 426 32072 20050 12291 -4071 -3252 -1257 C
ATOM 2645 C TYR A 426 19.999 -4.260 26.450 1.00161.92 C
ANISOU 2645 C TYR A 426 31349 19045 11129 -4422 -3257 -1414 C
ATOM 2646 O TYR A 426 19.953 -3.866 25.280 1.00160.49 O
ANISOU 2646 O TYR A 426 30760 19161 11059 -4246 -3278 -1487 O
ATOM 2647 CB TYR A 426 22.007 -3.968 27.955 1.00175.77 C
ANISOU 2647 CB TYR A 426 33418 20332 13034 -3564 -3385 -1165 C
ATOM 2648 CG TYR A 426 23.070 -4.017 26.883 1.00178.25 C
ANISOU 2648 CG TYR A 426 33715 20577 13434 -2963 -3512 -1172 C
ATOM 2649 CD1 TYR A 426 23.022 -4.962 25.876 1.00176.79 C
ANISOU 2649 CD1 TYR A 426 33939 20163 13070 -2998 -3562 -1277 C
ATOM 2650 CD2 TYR A 426 24.150 -3.149 26.907 1.00179.37 C
ANISOU 2650 CD2 TYR A 426 33452 20877 13822 -2367 -3577 -1071 C
ATOM 2651 CE1 TYR A 426 23.995 -5.019 24.899 1.00174.20 C
ANISOU 2651 CE1 TYR A 426 33611 19788 12790 -2420 -3675 -1277 C
ATOM 2652 CE2 TYR A 426 25.135 -3.204 25.933 1.00179.11 C
ANISOU 2652 CE2 TYR A 426 33383 20822 13850 -1820 -3682 -1065 C
ATOM 2653 CZ TYR A 426 25.052 -4.141 24.931 1.00175.55 C
ANISOU 2653 CZ TYR A 426 33335 20157 13209 -1825 -3730 -1163 C
ATOM 2654 OH TYR A 426 26.025 -4.203 23.959 1.00172.63 O
ANISOU 2654 OH TYR A 426 32929 19783 12879 -1252 -3829 -1150 O
ATOM 2655 N THR A 427 19.490 -5.437 26.816 1.00164.41 N
ANISOU 2655 N THR A 427 32238 18984 11245 -4893 -3198 -1444 N
ATOM 2656 CA THR A 427 18.802 -6.271 25.838 1.00170.12 C
ANISOU 2656 CA THR A 427 33141 19663 11833 -5285 -3174 -1589 C
ATOM 2657 C THR A 427 17.359 -5.836 25.623 1.00169.15 C
ANISOU 2657 C THR A 427 32456 20137 11676 -5902 -3049 -1689 C
ATOM 2658 O THR A 427 16.793 -6.105 24.557 1.00168.70 O
ANISOU 2658 O THR A 427 32254 20282 11563 -6125 -3048 -1829 O
ATOM 2659 CB THR A 427 18.834 -7.744 26.262 1.00181.24 C
ANISOU 2659 CB THR A 427 35450 20399 13014 -5573 -3150 -1578 C
ATOM 2660 OG1 THR A 427 18.200 -7.889 27.536 1.00189.65 O
ANISOU 2660 OG1 THR A 427 36676 21405 13978 -6057 -3029 -1506 O
ATOM 2661 CG2 THR A 427 20.269 -8.258 26.352 1.00155.25 C
ANISOU 2661 CG2 THR A 427 32731 16548 9709 -4891 -3275 -1483 C
ATOM 2662 N ILE A 428 16.757 -5.159 26.603 1.00169.70 N
ANISOU 2662 N ILE A 428 32186 20531 11762 -6154 -2945 -1621 N
ATOM 2663 CA ILE A 428 15.356 -4.774 26.498 1.00172.60 C
ANISOU 2663 CA ILE A 428 32009 21519 12053 -6723 -2812 -1701 C
ATOM 2664 C ILE A 428 15.125 -3.765 25.385 1.00172.53 C
ANISOU 2664 C ILE A 428 31261 22134 12157 -6463 -2833 -1782 C
ATOM 2665 O ILE A 428 14.004 -3.652 24.879 1.00170.74 O
ANISOU 2665 O ILE A 428 30605 22435 11834 -6878 -2750 -1888 O
ATOM 2666 CB ILE A 428 14.853 -4.217 27.845 1.00175.37 C
ANISOU 2666 CB ILE A 428 32170 22085 12379 -6953 -2694 -1590 C
ATOM 2667 N PHE A 429 16.158 -3.028 24.985 1.00173.75 N
ANISOU 2667 N PHE A 429 31237 22263 12515 -5774 -2931 -1723 N
ATOM 2668 CA PHE A 429 16.005 -1.966 23.996 1.00178.61 C
ANISOU 2668 CA PHE A 429 31104 23439 13322 -5431 -2905 -1751 C
ATOM 2669 C PHE A 429 16.888 -2.131 22.769 1.00189.61 C
ANISOU 2669 C PHE A 429 32584 24649 14812 -4939 -3031 -1798 C
ATOM 2670 O PHE A 429 16.430 -1.866 21.653 1.00188.38 O
ANISOU 2670 O PHE A 429 32033 24892 14652 -4916 -3023 -1902 O
ATOM 2671 CB PHE A 429 16.283 -0.602 24.644 1.00167.87 C
ANISOU 2671 CB PHE A 429 29213 22344 12225 -5019 -2827 -1598 C
ATOM 2672 CG PHE A 429 15.218 -0.161 25.602 1.00159.72 C
ANISOU 2672 CG PHE A 429 27891 21696 11098 -5431 -2676 -1562 C
ATOM 2673 CD1 PHE A 429 15.218 -0.606 26.913 1.00156.67 C
ANISOU 2673 CD1 PHE A 429 27922 20992 10613 -5707 -2652 -1485 C
ATOM 2674 CD2 PHE A 429 14.216 0.700 25.190 1.00156.42 C
ANISOU 2674 CD2 PHE A 429 26787 21982 10664 -5505 -2553 -1599 C
ATOM 2675 CE1 PHE A 429 14.237 -0.199 27.795 1.00156.19 C
ANISOU 2675 CE1 PHE A 429 27588 21308 10450 -6067 -2507 -1444 C
ATOM 2676 CE2 PHE A 429 13.235 1.111 26.065 1.00154.24 C
ANISOU 2676 CE2 PHE A 429 26231 22104 10269 -5839 -2408 -1558 C
ATOM 2677 CZ PHE A 429 13.244 0.661 27.369 1.00156.26 C
ANISOU 2677 CZ PHE A 429 26896 22037 10437 -6130 -2385 -1480 C
ATOM 2678 N ASN A 430 18.138 -2.558 22.935 1.00202.15 N
ANISOU 2678 N ASN A 430 34662 25680 16466 -4517 -3147 -1721 N
ATOM 2679 CA ASN A 430 19.045 -2.671 21.798 1.00211.73 C
ANISOU 2679 CA ASN A 430 35932 26751 17765 -3990 -3260 -1746 C
ATOM 2680 C ASN A 430 18.716 -3.908 20.971 1.00229.00 C
ANISOU 2680 C ASN A 430 38642 28699 19670 -4306 -3335 -1916 C
ATOM 2681 O ASN A 430 18.589 -5.013 21.509 1.00232.68 O
ANISOU 2681 O ASN A 430 39741 28707 19958 -4661 -3335 -1936 O
ATOM 2682 CB ASN A 430 20.495 -2.724 22.278 1.00209.57 C
ANISOU 2682 CB ASN A 430 35981 26032 17615 -3416 -3358 -1604 C
ATOM 2683 N HIS A 431 18.579 -3.717 19.656 1.00242.53 N
ANISOU 2683 N HIS A 431 40038 30703 21410 -4139 -3363 -2018 N
ATOM 2684 CA HIS A 431 18.197 -4.824 18.786 1.00255.51 C
ANISOU 2684 CA HIS A 431 42090 32165 22826 -4437 -3418 -2190 C
ATOM 2685 C HIS A 431 19.345 -5.805 18.585 1.00269.52 C
ANISOU 2685 C HIS A 431 44584 33262 24559 -4037 -3530 -2155 C
ATOM 2686 O HIS A 431 19.108 -7.003 18.396 1.00274.44 O
ANISOU 2686 O HIS A 431 45770 33490 25015 -4347 -3535 -2240 O
ATOM 2687 CB HIS A 431 17.705 -4.287 17.441 1.00255.00 C
ANISOU 2687 CB HIS A 431 41477 32654 22758 -4356 -3428 -2320 C
ATOM 2688 N ASP A 432 20.586 -5.322 18.622 1.00275.41 N
ANISOU 2688 N ASP A 432 45327 33881 25435 -3345 -3615 -2025 N
ATOM 2689 CA ASP A 432 21.737 -6.208 18.520 1.00278.44 C
ANISOU 2689 CA ASP A 432 46356 33682 25758 -2886 -3714 -1968 C
ATOM 2690 C ASP A 432 21.956 -7.016 19.787 1.00280.39 C
ANISOU 2690 C ASP A 432 47234 33396 25907 -3061 -3689 -1876 C
ATOM 2691 O ASP A 432 22.632 -8.049 19.742 1.00284.88 O
ANISOU 2691 O ASP A 432 48481 33421 26341 -2826 -3744 -1852 O
ATOM 2692 CB ASP A 432 22.997 -5.403 18.214 1.00277.92 C
ANISOU 2692 CB ASP A 432 45994 33730 25873 -2090 -3796 -1839 C
ATOM 2693 CG ASP A 432 22.934 -4.721 16.866 1.00279.57 C
ANISOU 2693 CG ASP A 432 45604 34386 26235 -1810 -3788 -1892 C
ATOM 2694 OD1 ASP A 432 22.281 -3.662 16.762 1.00279.22 O
ANISOU 2694 OD1 ASP A 432 44838 34866 26388 -1942 -3682 -1887 O
ATOM 2695 OD2 ASP A 432 23.539 -5.248 15.908 1.00282.33 O
ANISOU 2695 OD2 ASP A 432 46228 34560 26485 -1428 -3881 -1934 O
ATOM 2696 N PHE A 433 21.387 -6.576 20.907 1.00269.43 N
ANISOU 2696 N PHE A 433 45658 32152 24559 -3445 -3601 -1820 N
ATOM 2697 CA PHE A 433 21.646 -7.232 22.181 1.00262.26 C
ANISOU 2697 CA PHE A 433 45323 30767 23559 -3560 -3574 -1715 C
ATOM 2698 C PHE A 433 20.911 -8.561 22.277 1.00258.97 C
ANISOU 2698 C PHE A 433 45567 29924 22908 -4154 -3506 -1796 C
ATOM 2699 O PHE A 433 21.488 -9.570 22.699 1.00260.86 O
ANISOU 2699 O PHE A 433 46567 29554 22992 -4021 -3527 -1731 O
ATOM 2700 CB PHE A 433 21.242 -6.303 23.321 1.00260.05 C
ANISOU 2700 CB PHE A 433 44619 30799 23388 -3778 -3495 -1630 C
ATOM 2701 N ARG A 434 19.630 -8.577 21.896 1.00255.86 N
ANISOU 2701 N ARG A 434 44894 29858 22463 -4812 -3418 -1930 N
ATOM 2702 CA ARG A 434 18.833 -9.798 21.982 1.00259.01 C
ANISOU 2702 CA ARG A 434 45879 29902 22632 -5478 -3339 -2009 C
ATOM 2703 C ARG A 434 19.491 -10.938 21.215 1.00273.24 C
ANISOU 2703 C ARG A 434 48414 31123 24283 -5208 -3418 -2047 C
ATOM 2704 O ARG A 434 19.601 -12.062 21.719 1.00281.43 O
ANISOU 2704 O ARG A 434 50278 31536 25117 -5392 -3383 -2000 O
ATOM 2705 CB ARG A 434 17.423 -9.534 21.451 1.00247.23 C
ANISOU 2705 CB ARG A 434 43834 28987 21113 -6151 -3252 -2164 C
ATOM 2706 CG ARG A 434 16.770 -8.297 22.047 1.00232.40 C
ANISOU 2706 CG ARG A 434 41161 27772 19370 -6318 -3172 -2126 C
ATOM 2707 CD ARG A 434 15.448 -7.979 21.375 1.00225.68 C
ANISOU 2707 CD ARG A 434 39691 27585 18471 -6856 -3098 -2280 C
ATOM 2708 NE ARG A 434 14.989 -6.628 21.685 1.00216.55 N
ANISOU 2708 NE ARG A 434 37709 27125 17445 -6798 -3038 -2239 N
ATOM 2709 CZ ARG A 434 13.895 -6.075 21.170 1.00213.28 C
ANISOU 2709 CZ ARG A 434 36616 27424 16997 -7120 -2969 -2345 C
ATOM 2710 NH1 ARG A 434 13.552 -4.838 21.505 1.00204.79 N
ANISOU 2710 NH1 ARG A 434 34853 26943 16015 -6986 -2904 -2284 N
ATOM 2711 NH2 ARG A 434 13.142 -6.758 20.319 1.00220.94 N
ANISOU 2711 NH2 ARG A 434 37601 28528 17820 -7559 -2961 -2510 N
ATOM 2712 N ARG A 435 19.954 -10.658 19.996 1.00276.12 N
ANISOU 2712 N ARG A 435 48516 31672 24723 -4739 -3520 -2121 N
ATOM 2713 CA ARG A 435 20.585 -11.697 19.191 1.00279.67 C
ANISOU 2713 CA ARG A 435 49636 31607 25020 -4429 -3597 -2159 C
ATOM 2714 C ARG A 435 21.929 -12.112 19.778 1.00276.90 C
ANISOU 2714 C ARG A 435 49879 30710 24619 -3750 -3663 -1989 C
ATOM 2715 O ARG A 435 22.284 -13.297 19.759 1.00288.93 O
ANISOU 2715 O ARG A 435 52257 31601 25923 -3679 -3670 -1967 O
ATOM 2716 CB ARG A 435 20.743 -11.211 17.750 1.00280.54 C
ANISOU 2716 CB ARG A 435 49263 32109 25221 -4065 -3685 -2274 C
ATOM 2717 N ALA A 436 22.691 -11.151 20.306 1.00253.74 N
ANISOU 2717 N ALA A 436 46513 28027 21871 -3237 -3709 -1863 N
ATOM 2718 CA ALA A 436 23.967 -11.471 20.933 1.00239.74 C
ANISOU 2718 CA ALA A 436 45205 25839 20045 -2579 -3774 -1700 C
ATOM 2719 C ALA A 436 23.789 -12.268 22.218 1.00226.94 C
ANISOU 2719 C ALA A 436 44271 23710 18247 -2909 -3693 -1611 C
ATOM 2720 O ALA A 436 24.707 -12.996 22.617 1.00231.07 O
ANISOU 2720 O ALA A 436 45452 23727 18617 -2439 -3732 -1502 O
ATOM 2721 CB ALA A 436 24.750 -10.185 21.207 1.00232.05 C
ANISOU 2721 CB ALA A 436 43529 25326 19313 -2031 -3837 -1593 C
ATOM 2722 N PHE A 437 22.631 -12.153 22.869 1.00223.20 N
ANISOU 2722 N PHE A 437 43657 23377 17771 -3683 -3573 -1649 N
ATOM 2723 CA PHE A 437 22.379 -12.928 24.076 1.00217.68 C
ANISOU 2723 CA PHE A 437 43629 22197 16884 -4052 -3477 -1560 C
ATOM 2724 C PHE A 437 21.944 -14.350 23.741 1.00226.39 C
ANISOU 2724 C PHE A 437 45616 22706 17697 -4467 -3415 -1616 C
ATOM 2725 O PHE A 437 22.338 -15.303 24.421 1.00221.24 O
ANISOU 2725 O PHE A 437 45827 21417 16818 -4383 -3382 -1508 O
ATOM 2726 CB PHE A 437 21.324 -12.229 24.932 1.00210.54 C
ANISOU 2726 CB PHE A 437 42215 21706 16074 -4706 -3362 -1562 C
ATOM 2727 N LYS A 438 21.139 -14.511 22.692 1.00244.20 N
ANISOU 2727 N LYS A 438 47689 25159 19938 -4906 -3397 -1778 N
ATOM 2728 CA LYS A 438 20.698 -15.837 22.285 1.00265.98 C
ANISOU 2728 CA LYS A 438 51267 27377 22416 -5340 -3339 -1838 C
ATOM 2729 C LYS A 438 21.785 -16.607 21.549 1.00307.86 C
ANISOU 2729 C LYS A 438 57228 32166 27581 -4627 -3445 -1810 C
ATOM 2730 O LYS A 438 21.742 -17.842 21.519 1.00325.27 O
ANISOU 2730 O LYS A 438 60367 33722 29498 -4809 -3396 -1788 O
ATOM 2731 CB LYS A 438 19.451 -15.729 21.402 1.00244.15 C
ANISOU 2731 CB LYS A 438 48030 25064 19673 -6059 -3290 -2033 C
ATOM 2732 CG LYS A 438 18.253 -16.505 21.923 1.00229.52 C
ANISOU 2732 CG LYS A 438 46571 23032 17603 -7054 -3126 -2060 C
ATOM 2733 CD LYS A 438 18.511 -18.001 21.893 1.00224.43 C
ANISOU 2733 CD LYS A 438 47118 21529 16626 -7142 -3087 -2007 C
ATOM 2734 CE LYS A 438 17.405 -18.772 22.593 1.00223.71 C
ANISOU 2734 CE LYS A 438 47488 21221 16290 -8136 -2900 -1988 C
ATOM 2735 NZ LYS A 438 16.110 -18.685 21.863 1.00223.06 N
ANISOU 2735 NZ LYS A 438 46871 21677 16204 -8949 -2840 -2179 N
ATOM 2736 N LYS A 439 22.757 -15.911 20.960 1.00324.29 N
ANISOU 2736 N LYS A 439 58857 34523 29837 -3818 -3579 -1798 N
ATOM 2737 CA LYS A 439 23.818 -16.576 20.218 1.00326.32 C
ANISOU 2737 CA LYS A 439 59659 34368 29959 -3078 -3680 -1767 C
ATOM 2738 C LYS A 439 25.067 -16.826 21.051 1.00324.75 C
ANISOU 2738 C LYS A 439 59933 33784 29674 -2321 -3724 -1576 C
ATOM 2739 O LYS A 439 25.885 -17.673 20.673 1.00328.29 O
ANISOU 2739 O LYS A 439 61073 33744 29918 -1759 -3775 -1523 O
ATOM 2740 CB LYS A 439 24.192 -15.759 18.978 1.00324.74 C
ANISOU 2740 CB LYS A 439 58719 34704 29962 -2601 -3793 -1860 C
ATOM 2741 N ILE A 440 25.242 -16.107 22.162 1.00319.53 N
ANISOU 2741 N ILE A 440 58906 33353 29150 -2264 -3707 -1474 N
ATOM 2742 CA ILE A 440 26.355 -16.397 23.063 1.00305.21 C
ANISOU 2742 CA ILE A 440 57544 31193 27230 -1597 -3742 -1300 C
ATOM 2743 C ILE A 440 26.181 -17.773 23.696 1.00291.42 C
ANISOU 2743 C ILE A 440 56954 28641 25133 -1843 -3646 -1229 C
ATOM 2744 O ILE A 440 27.139 -18.545 23.817 1.00288.79 O
ANISOU 2744 O ILE A 440 57331 27811 24586 -1187 -3683 -1125 O
ATOM 2745 CB ILE A 440 26.483 -15.299 24.134 1.00303.40 C
ANISOU 2745 CB ILE A 440 56641 31416 27223 -1559 -3742 -1217 C
ATOM 2746 N LEU A 441 24.953 -18.104 24.103 1.00273.52 N
ANISOU 2746 N LEU A 441 54896 26246 22782 -2785 -3510 -1275 N
ATOM 2747 CA LEU A 441 24.723 -19.348 24.836 1.00288.61 C
ANISOU 2747 CA LEU A 441 57912 27399 24348 -3100 -3391 -1178 C
ATOM 2748 C LEU A 441 24.844 -20.569 23.928 1.00292.51 C
ANISOU 2748 C LEU A 441 59296 27297 24549 -3018 -3391 -1199 C
ATOM 2749 O LEU A 441 25.594 -21.505 24.229 1.00307.18 O
ANISOU 2749 O LEU A 441 62091 28500 26124 -2519 -3387 -1069 O
ATOM 2750 CB LEU A 441 23.352 -19.312 25.514 1.00197.36 C
ANISOU 2750 CB LEU A 441 46265 15944 12777 -4170 -3231 -1211 C
ATOM 2751 N CYS A 442 24.116 -20.576 22.810 1.00271.45 N
ANISOU 2751 N CYS A 442 56356 24852 21930 -3477 -3394 -1363 N
ATOM 2752 CA CYS A 442 24.093 -21.752 21.941 1.00278.48 C
ANISOU 2752 CA CYS A 442 58099 25184 22525 -3512 -3384 -1391 C
ATOM 2753 C CYS A 442 25.416 -21.931 21.201 1.00276.32 C
ANISOU 2753 C CYS A 442 58039 24740 22209 -2422 -3530 -1349 C
ATOM 2754 O CYS A 442 25.957 -23.043 21.139 1.00283.98 O
ANISOU 2754 O CYS A 442 60041 25012 22848 -2051 -3520 -1245 O
ATOM 2755 CB CYS A 442 22.937 -21.648 20.944 1.00282.68 C
ANISOU 2755 CB CYS A 442 58190 26082 23133 -4301 -3355 -1597 C
ATOM 2756 SG CYS A 442 21.306 -21.457 21.698 1.00286.54 S
ANISOU 2756 SG CYS A 442 58346 26877 23650 -5603 -3173 -1661 S
ATOM 2757 N ARG A 443 25.943 -20.852 20.626 1.00266.92 N
ANISOU 2757 N ARG A 443 55896 24192 21328 -1894 -3656 -1416 N
ATOM 2758 CA ARG A 443 27.188 -20.891 19.858 1.00257.36 C
ANISOU 2758 CA ARG A 443 54726 22955 20103 -861 -3789 -1382 C
ATOM 2759 C ARG A 443 27.108 -21.893 18.706 1.00256.23 C
ANISOU 2759 C ARG A 443 55264 22379 19714 -842 -3804 -1449 C
ATOM 2760 O ARG A 443 26.275 -21.757 17.809 1.00258.30 O
ANISOU 2760 O ARG A 443 55183 22906 20052 -1391 -3802 -1617 O
ATOM 2761 CB ARG A 443 28.374 -21.226 20.768 1.00254.79 C
ANISOU 2761 CB ARG A 443 54907 22266 19635 -39 -3811 -1193 C
TER 2762 ARG A 443
HETATM 2763 C1 PEG A1201 15.014 5.190 -9.578 1.00134.47 C
HETATM 2764 O1 PEG A1201 14.621 3.854 -9.437 1.00134.91 O
HETATM 2765 C2 PEG A1201 15.040 5.849 -8.203 1.00131.88 C
HETATM 2766 O2 PEG A1201 15.400 7.190 -8.350 1.00130.73 O
HETATM 2767 C3 PEG A1201 14.620 8.063 -7.588 1.00127.75 C
HETATM 2768 C4 PEG A1201 14.723 9.467 -8.174 1.00123.28 C
HETATM 2769 O4 PEG A1201 13.660 10.236 -7.684 1.00119.21 O
HETATM 2770 C4 E39 A1202 28.155 4.452 51.724 1.00153.36 C
HETATM 2771 C3 E39 A1202 29.527 2.438 51.023 1.00151.73 C
HETATM 2772 C2 E39 A1202 28.281 3.279 50.750 1.00155.95 C
HETATM 2773 C1 E39 A1202 30.760 6.557 47.273 1.00167.33 C
HETATM 2774 C10 E39 A1202 28.931 4.964 47.458 1.00168.18 C
HETATM 2775 C11 E39 A1202 25.842 0.239 48.141 1.00150.68 C
HETATM 2776 C12 E39 A1202 29.239 4.756 48.796 1.00168.35 C
HETATM 2777 C13 E39 A1202 30.319 5.461 49.370 1.00169.83 C
HETATM 2778 C14 E39 A1202 31.073 6.355 48.623 1.00169.64 C
HETATM 2779 C5 E39 A1202 27.220 3.580 48.406 1.00163.64 C
HETATM 2780 C6 E39 A1202 27.736 4.086 47.104 1.00168.20 C
HETATM 2781 C7 E39 A1202 26.892 2.107 48.253 1.00154.30 C
HETATM 2782 C8 E39 A1202 27.797 1.097 47.968 1.00150.09 C
HETATM 2783 C9 E39 A1202 29.698 5.867 46.692 1.00166.17 C
HETATM 2784 F1 E39 A1202 29.398 6.065 45.376 1.00165.75 F
HETATM 2785 N1 E39 A1202 28.290 3.764 49.374 1.00164.54 N
HETATM 2786 N2 E39 A1202 25.703 1.535 48.348 1.00150.73 N
HETATM 2787 N3 E39 A1202 27.114 -0.033 47.911 1.00151.30 N
CONECT 512 1054
CONECT 1054 512
CONECT 2763 2764 2765
CONECT 2764 2763
CONECT 2765 2763 2766
CONECT 2766 2765 2767
CONECT 2767 2766 2768
CONECT 2768 2767 2769
CONECT 2769 2768
CONECT 2770 2772
CONECT 2771 2772
CONECT 2772 2770 2771 2785
CONECT 2773 2778 2783
CONECT 2774 2776 2780 2783
CONECT 2775 2786 2787
CONECT 2776 2774 2777 2785
CONECT 2777 2776 2778
CONECT 2778 2773 2777
CONECT 2779 2780 2781 2785
CONECT 2780 2774 2779
CONECT 2781 2779 2782 2786
CONECT 2782 2781 2787
CONECT 2783 2773 2774 2784
CONECT 2784 2783
CONECT 2785 2772 2776 2779
CONECT 2786 2775 2781
CONECT 2787 2775 2782
MASTER 355 0 2 15 0 0 4 6 2786 1 27 31
END