pub_soft/fpocket
3
0
Fork 0
mirror of https://github.com/Discngine/fpocket.git synced 2026-06-04 20:04:22 +08:00
Code Issues Packages Projects Releases Wiki Activity
Files
1d186a45c971d820f36d5335a3f292736c8d0bb2
fpocket/data/sample/5WA6.pdb
pschmidtke 7ec07dc24d dev-13 wrapping up final build with new qhull
2018-07-23 21:53:46 +00:00

3445 lines
272 KiB
Plaintext
Raw Blame History

HEADER HYDROLASE/HYDROLASE INHIBITOR 25-JUN-17 5WA6
TITLE CRYSTAL STRUCTURE OF THE INFLUENZA VIRUS PA ENDONUCLEASE IN COMPLEX
TITLE 2 WITH AN INHIBITOR - SRI-30007
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYMERASE ACIDIC PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE 3 ORGANISM_TAXID: 641501;
SOURCE 4 STRAIN: SWL A/CALIFORNIA/04/2009 H1N1;
SOURCE 5 GENE: PA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS VIRUS, NUCLEASE, TRANSCRIPTION, CAP-SNATCHING, HYDROLASE, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.KUMAR,S.W.WHITE
REVDAT 1 02-MAY-18 5WA6 0
JRNL AUTH G.KUMAR,S.WHITE
JRNL TITL CRYSTAL STRUCTURE OF THE INFLUENZA VIRUS PA ENDONUCLEASE IN
JRNL TITL 2 COMPLEX WITH AN INHIBITOR - SRI-30007
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 13733
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.370
REMARK 3 FREE R VALUE TEST SET COUNT : 737
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 38.8026 - 3.8442 1.00 2719 168 0.2070 0.2352
REMARK 3 2 3.8442 - 3.0516 1.00 2609 134 0.2556 0.2686
REMARK 3 3 3.0516 - 2.6660 1.00 2543 162 0.2597 0.2654
REMARK 3 4 2.6660 - 2.4223 1.00 2580 143 0.2528 0.2951
REMARK 3 5 2.4223 - 2.2487 1.00 2545 130 0.2886 0.3188
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 57.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 91.58
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 1476
REMARK 3 ANGLE : 0.593 1993
REMARK 3 CHIRALITY : 0.040 211
REMARK 3 PLANARITY : 0.004 258
REMARK 3 DIHEDRAL : 3.637 889
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND ( RESID -2:176 OR RESID 201:202 OR
REMARK 3 RESID 302:304 OR RESID 203:203 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 490.908 202.292 558.793
REMARK 3 T TENSOR
REMARK 3 T11: 1.0251 T22: 0.6365
REMARK 3 T33: 0.6975 T12: -0.1443
REMARK 3 T13: 0.4617 T23: 0.1221
REMARK 3 L TENSOR
REMARK 3 L11: 3.8983 L22: 1.7595
REMARK 3 L33: 2.4610 L12: -0.3477
REMARK 3 L13: 0.2297 L23: -0.3266
REMARK 3 S TENSOR
REMARK 3 S11: 0.0455 S12: -0.6157 S13: -0.5015
REMARK 3 S21: 0.6827 S22: -0.4818 S23: 0.1653
REMARK 3 S31: 0.9833 S32: -0.1313 S33: 0.3089
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 5WA6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000228663.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13745
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 1.12600
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.8, 1.0 M AMSO4, 10 MM
REMARK 280 MNCL2, 10 MM MGCL2, 1% PVP K15, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 45.28150
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 45.28150
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 67.58350
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 45.28150
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 45.28150
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 67.58350
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 45.28150
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 45.28150
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 67.58350
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 45.28150
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 45.28150
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 67.58350
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 45.28150
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 45.28150
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 67.58350
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 45.28150
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 45.28150
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 67.58350
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 45.28150
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 45.28150
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 67.58350
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 45.28150
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 45.28150
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 67.58350
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 LYS A 139
REMARK 465 SER A 140
REMARK 465 ARG A 196
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 ARG A -3 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 73 CG CD CE NZ
REMARK 470 ARG A 84 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 104 CG CD CE NZ
REMARK 470 ARG A 124 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 125 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 126 CG CD OE1 OE2
REMARK 470 VAL A 127 CG1 CG2
REMARK 470 LEU A 132 CG CD1 CD2
REMARK 470 LYS A 134 CG CD CE NZ
REMARK 470 LYS A 137 CG CD CE NZ
REMARK 470 ILE A 138 CG1 CG2 CD1
REMARK 470 GLU A 141 CG CD OE1 OE2
REMARK 470 LYS A 142 CG CD CE NZ
REMARK 470 MET A 155 CG SD CE
REMARK 470 GLN A 193 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 24 -1.69 68.19
REMARK 500 THR A 162 -66.70 60.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 201 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 41 NE2
REMARK 620 2 ASP A 108 OD1 109.4
REMARK 620 3 ASP A 108 OD2 75.9 48.8
REMARK 620 4 GLU A 119 OE2 176.1 74.0 105.7
REMARK 620 5 ILE A 120 O 92.3 97.7 134.1 89.1
REMARK 620 6 KU7 A 203 O2 96.8 152.4 135.4 79.6 89.5
REMARK 620 7 KU7 A 203 O1 94.9 95.0 63.4 82.7 162.4 73.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 202 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 80 OE2
REMARK 620 2 ASP A 108 OD2 103.7
REMARK 620 3 KU7 A 203 O3 95.7 157.4
REMARK 620 4 HOH A 302 O 70.8 103.4 93.7
REMARK 620 5 KU7 A 203 O1 136.4 79.1 78.9 152.0
REMARK 620 6 HOH A 301 O 148.4 84.8 84.7 77.6 74.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KU7 A 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5W3I RELATED DB: PDB
REMARK 900 RELATED ID: 5W44 RELATED DB: PDB
REMARK 900 RELATED ID: 5W73 RELATED DB: PDB
REMARK 900 RELATED ID: 5W7U RELATED DB: PDB
REMARK 900 RELATED ID: 5W92 RELATED DB: PDB
REMARK 900 RELATED ID: 5W9G RELATED DB: PDB
REMARK 900 RELATED ID: 5WA7 RELATED DB: PDB
REMARK 900 RELATED ID: 5WB3 RELATED DB: PDB
REMARK 900 RELATED ID: 5WAP RELATED DB: PDB
DBREF 5WA6 A 1 50 UNP C3W5S0 C3W5S0_I09A0 1 50
DBREF 5WA6 A 73 196 UNP C3W5S0 C3W5S0_I09A0 73 196
SEQADV 5WA6 MET A -19 UNP C3W5S0 INITIATING METHIONINE
SEQADV 5WA6 GLY A -18 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 SER A -17 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 SER A -16 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 HIS A -15 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 HIS A -14 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 HIS A -13 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 HIS A -12 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 HIS A -11 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 HIS A -10 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 SER A -9 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 SER A -8 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 GLY A -7 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 LEU A -6 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 VAL A -5 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 PRO A -4 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 ARG A -3 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 GLY A -2 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 SER A -1 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 HIS A 0 UNP C3W5S0 EXPRESSION TAG
SEQADV 5WA6 GLY A 51 UNP C3W5S0 LINKER
SEQADV 5WA6 GLY A 52 UNP C3W5S0 LINKER
SEQADV 5WA6 SER A 53 UNP C3W5S0 LINKER
SEQRES 1 A 197 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 197 LEU VAL PRO ARG GLY SER HIS MET GLU ASP PHE VAL ARG
SEQRES 3 A 197 GLN CYS PHE ASN PRO MET ILE VAL GLU LEU ALA GLU LYS
SEQRES 4 A 197 ALA MET LYS GLU TYR GLY GLU ASP PRO LYS ILE GLU THR
SEQRES 5 A 197 ASN LYS PHE ALA ALA ILE CYS THR HIS LEU GLU VAL CYS
SEQRES 6 A 197 PHE MET TYR SER ASP GLY GLY SER LYS HIS ARG PHE GLU
SEQRES 7 A 197 ILE ILE GLU GLY ARG ASP ARG ILE MET ALA TRP THR VAL
SEQRES 8 A 197 VAL ASN SER ILE CYS ASN THR THR GLY VAL GLU LYS PRO
SEQRES 9 A 197 LYS PHE LEU PRO ASP LEU TYR ASP TYR LYS GLU ASN ARG
SEQRES 10 A 197 PHE ILE GLU ILE GLY VAL THR ARG ARG GLU VAL HIS ILE
SEQRES 11 A 197 TYR TYR LEU GLU LYS ALA ASN LYS ILE LYS SER GLU LYS
SEQRES 12 A 197 THR HIS ILE HIS ILE PHE SER PHE THR GLY GLU GLU MET
SEQRES 13 A 197 ALA THR LYS ALA ASP TYR THR LEU ASP GLU GLU SER ARG
SEQRES 14 A 197 ALA ARG ILE LYS THR ARG LEU PHE THR ILE ARG GLN GLU
SEQRES 15 A 197 MET ALA SER ARG SER LEU TRP ASP SER PHE ARG GLN SER
SEQRES 16 A 197 GLU ARG
HET MN A 201 1
HET MN A 202 1
HET KU7 A 203 36
HETNAM MN MANGANESE (II) ION
HETNAM KU7 2-{(2S)-1-[(2-FLUOROPHENOXY)ACETYL]PYRROLIDIN-2-YL}-5-
HETNAM 2 KU7 HYDROXY-6-OXO-N-(2-PHENOXYETHYL)-1,6-
HETNAM 3 KU7 DIHYDROPYRIMIDINE-4-CARBOXAMIDE
FORMUL 2 MN 2(MN 2+)
FORMUL 4 KU7 C25 H25 F N4 O6
FORMUL 5 HOH *8(H2 O)
HELIX 1 AA1 SER A -1 PHE A 9 1 11
HELIX 2 AA2 ASN A 10 GLU A 23 1 14
HELIX 3 AA3 GLU A 31 GLY A 52 1 22
HELIX 4 AA4 ASP A 83 GLY A 99 1 17
HELIX 5 AA5 GLU A 126 LYS A 137 1 12
HELIX 6 AA6 LYS A 158 ASP A 160 5 3
HELIX 7 AA7 ASP A 164 ARG A 185 1 22
HELIX 8 AA8 LEU A 187 GLN A 193 1 7
SHEET 1 AA1 5 PHE A 76 ILE A 78 0
SHEET 2 AA1 5 LEU A 109 ASP A 111 -1 O TYR A 110 N GLU A 77
SHEET 3 AA1 5 ARG A 116 THR A 123 -1 O ARG A 116 N ASP A 111
SHEET 4 AA1 5 HIS A 144 SER A 149 1 O PHE A 148 N GLY A 121
SHEET 5 AA1 5 GLU A 154 ALA A 156 -1 O MET A 155 N ILE A 147
LINK NE2 HIS A 41 MN MN A 201 1555 1555 2.28
LINK OE2 GLU A 80 MN MN A 202 1555 1555 2.16
LINK OD1 ASP A 108 MN MN A 201 1555 1555 2.45
LINK OD2 ASP A 108 MN MN A 202 1555 1555 2.26
LINK OD2 ASP A 108 MN MN A 201 1555 1555 2.80
LINK OE2 GLU A 119 MN MN A 201 1555 1555 2.29
LINK O ILE A 120 MN MN A 201 1555 1555 2.28
LINK MN MN A 201 O2 KU7 A 203 1555 1555 2.02
LINK MN MN A 201 O1 KU7 A 203 1555 1555 2.41
LINK MN MN A 202 O3 KU7 A 203 1555 1555 2.11
LINK MN MN A 202 O HOH A 302 1555 1555 2.43
LINK MN MN A 202 O1 KU7 A 203 1555 1555 2.06
LINK MN MN A 202 O HOH A 301 1555 1555 2.27
SITE 1 AC1 5 HIS A 41 ASP A 108 GLU A 119 ILE A 120
SITE 2 AC1 5 KU7 A 203
SITE 1 AC2 5 GLU A 80 ASP A 108 KU7 A 203 HOH A 301
SITE 2 AC2 5 HOH A 302
SITE 1 AC3 13 ALA A 20 TYR A 24 LYS A 34 ILE A 38
SITE 2 AC3 13 HIS A 41 GLU A 80 ASP A 108 GLU A 119
SITE 3 AC3 13 ILE A 120 MN A 201 MN A 202 HOH A 301
SITE 4 AC3 13 HOH A 304
CRYST1 90.563 90.563 135.167 90.00 90.00 90.00 I 4 2 2 16
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 0.011042 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011042 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007398 0.00000
ATOM 1 N ARG A -3 480.909 194.223 534.038 1.00102.41 N
ATOM 2 CA ARG A -3 479.709 194.283 534.867 1.00104.62 C
ATOM 3 C ARG A -3 479.840 195.357 535.948 1.00 93.95 C
ATOM 4 O ARG A -3 480.213 195.064 537.085 1.00103.43 O
ATOM 5 CB ARG A -3 479.432 192.918 535.505 1.00102.20 C
ATOM 6 N GLY A -2 479.528 196.600 535.585 1.00145.48 N
ANISOU 6 N GLY A -2 18890 17719 18668 -1476 4049 -3696 N
ATOM 7 CA GLY A -2 479.663 197.719 536.499 1.00124.03 C
ANISOU 7 CA GLY A -2 16047 15104 15975 -1462 4108 -3355 C
ATOM 8 C GLY A -2 478.562 197.807 537.536 1.00111.17 C
ANISOU 8 C GLY A -2 14355 13371 14513 -1839 4204 -3355 C
ATOM 9 O GLY A -2 477.388 197.982 537.195 1.00110.62 O
ANISOU 9 O GLY A -2 14057 13492 14482 -2042 4164 -3565 O
ATOM 10 N SER A -1 478.934 197.698 538.808 1.00100.74 N
ANISOU 10 N SER A -1 13221 11775 13279 -1927 4331 -3116 N
ATOM 11 CA SER A -1 477.972 197.728 539.898 1.00 94.19 C
ANISOU 11 CA SER A -1 12354 10846 12587 -2276 4450 -3090 C
ATOM 12 C SER A -1 477.614 199.163 540.271 1.00 93.16 C
ANISOU 12 C SER A -1 11929 11037 12431 -2244 4451 -2938 C
ATOM 13 O SER A -1 478.301 200.122 539.908 1.00 90.02 O
ANISOU 13 O SER A -1 11409 10862 11932 -1953 4372 -2780 O
ATOM 14 CB SER A -1 478.531 197.007 541.122 1.00 97.67 C
ANISOU 14 CB SER A -1 13122 10884 13105 -2373 4587 -2883 C
ATOM 15 OG SER A -1 479.712 197.650 541.569 1.00 95.65 O
ANISOU 15 OG SER A -1 12934 10652 12755 -2097 4586 -2574 O
ATOM 16 N HIS A 0 476.511 199.300 541.013 1.00 90.83 N
ANISOU 16 N HIS A 0 11512 10757 12241 -2551 4546 -2987 N
ATOM 17 CA HIS A 0 476.125 200.606 541.536 1.00 79.32 C
ANISOU 17 CA HIS A 0 9797 9556 10785 -2535 4571 -2858 C
ATOM 18 C HIS A 0 477.038 201.040 542.672 1.00 87.48 C
ANISOU 18 C HIS A 0 10991 10458 11788 -2431 4652 -2551 C
ATOM 19 O HIS A 0 477.341 202.233 542.806 1.00 91.95 O
ANISOU 19 O HIS A 0 11395 11224 12318 -2251 4612 -2403 O
ATOM 20 CB HIS A 0 474.664 200.573 542.000 1.00 83.49 C
ANISOU 20 CB HIS A 0 10138 10153 11429 -2886 4663 -3016 C
ATOM 21 CG HIS A 0 474.136 201.900 542.457 1.00 88.17 C
ANISOU 21 CG HIS A 0 10442 11021 12039 -2861 4689 -2936 C
ATOM 22 ND1 HIS A 0 472.953 202.029 543.152 1.00 91.32 N
ANISOU 22 ND1 HIS A 0 10720 11459 12518 -3082 4686 -2984 N
ATOM 23 CD2 HIS A 0 474.625 203.155 542.315 1.00 91.49 C
ANISOU 23 CD2 HIS A 0 10746 11616 12399 -2538 4491 -2743 C
ATOM 24 CE1 HIS A 0 472.739 203.304 543.422 1.00 90.18 C
ANISOU 24 CE1 HIS A 0 10408 11504 12354 -2883 4515 -2852 C
ATOM 25 NE2 HIS A 0 473.740 204.009 542.927 1.00 87.89 N
ANISOU 25 NE2 HIS A 0 10116 11283 11994 -2572 4397 -2701 N
ATOM 26 N MET A 1 477.497 200.091 543.487 1.00 87.84 N
ANISOU 26 N MET A 1 11354 10169 11854 -2540 4755 -2449 N
ATOM 27 CA MET A 1 478.338 200.443 544.623 1.00 87.58 C
ANISOU 27 CA MET A 1 11476 10028 11773 -2459 4824 -2161 C
ATOM 28 C MET A 1 479.708 200.935 544.166 1.00 81.38 C
ANISOU 28 C MET A 1 10738 9293 10891 -2086 4707 -1982 C
ATOM 29 O MET A 1 480.312 201.799 544.807 1.00 80.62 O
ANISOU 29 O MET A 1 10615 9266 10752 -1960 4703 -1771 O
ATOM 30 CB MET A 1 478.476 199.243 545.553 1.00 87.65 C
ANISOU 30 CB MET A 1 11807 9674 11820 -2662 4955 -2076 C
ATOM 31 CG MET A 1 479.643 199.319 546.511 1.00 92.87 C
ANISOU 31 CG MET A 1 12693 10191 12402 -2517 4988 -1770 C
ATOM 32 SD MET A 1 479.211 200.520 547.782 1.00 88.43 S
ANISOU 32 SD MET A 1 11976 9833 11791 -2559 4957 -1637 S
ATOM 33 CE MET A 1 478.758 199.473 549.167 1.00 89.49 C
ANISOU 33 CE MET A 1 12356 9716 11929 -2845 5085 -1542 C
ATOM 34 N GLU A 2 480.212 200.411 543.051 1.00 74.25 N
ANISOU 34 N GLU A 2 9892 8369 9952 -1908 4609 -2070 N
ATOM 35 CA GLU A 2 481.465 200.915 542.500 1.00 74.83 C
ANISOU 35 CA GLU A 2 9963 8542 9929 -1549 4504 -1902 C
ATOM 36 C GLU A 2 481.344 202.385 542.128 1.00 76.71 C
ANISOU 36 C GLU A 2 9878 9126 10143 -1407 4418 -1840 C
ATOM 37 O GLU A 2 482.219 203.191 542.457 1.00 79.44 O
ANISOU 37 O GLU A 2 10197 9529 10457 -1220 4382 -1604 O
ATOM 38 CB GLU A 2 481.877 200.082 541.285 1.00 68.62 C
ANISOU 38 CB GLU A 2 9265 7717 9091 -1387 4427 -2053 C
ATOM 39 CG GLU A 2 482.991 200.744 540.503 1.00 73.21 C
ANISOU 39 CG GLU A 2 9757 8502 9559 -1015 4318 -1901 C
ATOM 40 CD GLU A 2 483.515 199.883 539.378 1.00 89.79 C
ANISOU 40 CD GLU A 2 11964 10572 11579 -824 4262 -2045 C
ATOM 41 OE1 GLU A 2 482.731 199.495 538.481 1.00 90.71 O
ANISOU 41 OE1 GLU A 2 11999 10787 11681 -901 4218 -2334 O
ATOM 42 OE2 GLU A 2 484.730 199.617 539.385 1.00 86.48 O
ANISOU 42 OE2 GLU A 2 11703 10051 11107 -586 4257 -1874 O
ATOM 43 N ASP A 3 480.265 202.751 541.431 1.00 80.01 N
ANISOU 43 N ASP A 3 10039 9773 10589 -1494 4376 -2045 N
ATOM 44 CA ASP A 3 480.100 204.142 541.025 1.00 78.82 C
ANISOU 44 CA ASP A 3 9583 9927 10438 -1339 4233 -1955 C
ATOM 45 C ASP A 3 479.821 205.043 542.221 1.00 78.48 C
ANISOU 45 C ASP A 3 9491 9861 10468 -1407 4165 -1790 C
ATOM 46 O ASP A 3 480.226 206.212 542.226 1.00 80.35 O
ANISOU 46 O ASP A 3 9590 10229 10709 -1215 4011 -1602 O
ATOM 47 CB ASP A 3 478.980 204.258 539.991 1.00 83.77 C
ANISOU 47 CB ASP A 3 9949 10809 11073 -1405 4182 -2204 C
ATOM 48 CG ASP A 3 479.358 203.655 538.642 1.00 84.44 C
ANISOU 48 CG ASP A 3 10050 10993 11040 -1242 4115 -2338 C
ATOM 49 OD1 ASP A 3 478.439 203.347 537.855 1.00 86.30 O
ANISOU 49 OD1 ASP A 3 10148 11377 11263 -1344 4063 -2592 O
ATOM 50 OD2 ASP A 3 480.566 203.489 538.367 1.00 73.59 O
ANISOU 50 OD2 ASP A 3 8822 9561 9577 -1003 4084 -2188 O
ATOM 51 N PHE A 4 479.142 204.520 543.243 1.00 71.48 N
ANISOU 51 N PHE A 4 8716 8808 9634 -1677 4284 -1865 N
ATOM 52 CA PHE A 4 478.901 205.314 544.441 1.00 72.02 C
ANISOU 52 CA PHE A 4 8762 8864 9737 -1718 4223 -1738 C
ATOM 53 C PHE A 4 480.199 205.579 545.193 1.00 71.97 C
ANISOU 53 C PHE A 4 8930 8737 9678 -1563 4193 -1486 C
ATOM 54 O PHE A 4 480.400 206.677 545.723 1.00 69.76 O
ANISOU 54 O PHE A 4 8558 8537 9410 -1458 4073 -1359 O
ATOM 55 CB PHE A 4 477.892 204.612 545.351 1.00 75.74 C
ANISOU 55 CB PHE A 4 9317 9213 10249 -2030 4360 -1866 C
ATOM 56 CG PHE A 4 477.944 205.082 546.774 1.00 74.93 C
ANISOU 56 CG PHE A 4 9295 9050 10126 -2058 4342 -1727 C
ATOM 57 CD1 PHE A 4 477.420 206.316 547.128 1.00 78.96 C
ANISOU 57 CD1 PHE A 4 9605 9731 10666 -1987 4218 -1714 C
ATOM 58 CD2 PHE A 4 478.533 204.304 547.755 1.00 77.13 C
ANISOU 58 CD2 PHE A 4 9851 9107 10347 -2143 4455 -1611 C
ATOM 59 CE1 PHE A 4 477.474 206.758 548.434 1.00 81.25 C
ANISOU 59 CE1 PHE A 4 9964 9986 10920 -2008 4218 -1625 C
ATOM 60 CE2 PHE A 4 478.591 204.744 549.062 1.00 82.15 C
ANISOU 60 CE2 PHE A 4 10549 9732 10932 -2158 4434 -1497 C
ATOM 61 CZ PHE A 4 478.061 205.972 549.401 1.00 79.60 C
ANISOU 61 CZ PHE A 4 10019 9594 10630 -2094 4322 -1521 C
ATOM 62 N VAL A 5 481.091 204.587 545.246 1.00 73.10 N
ANISOU 62 N VAL A 5 9324 8685 9767 -1547 4310 -1420 N
ATOM 63 CA VAL A 5 482.360 204.758 545.949 1.00 72.04 C
ANISOU 63 CA VAL A 5 9351 8444 9577 -1399 4283 -1174 C
ATOM 64 C VAL A 5 483.171 205.886 545.325 1.00 73.71 C
ANISOU 64 C VAL A 5 9387 8836 9782 -1119 4109 -1025 C
ATOM 65 O VAL A 5 483.716 206.742 546.033 1.00 68.94 O
ANISOU 65 O VAL A 5 8758 8255 9180 -1039 4018 -865 O
ATOM 66 CB VAL A 5 483.143 203.432 545.957 1.00 74.21 C
ANISOU 66 CB VAL A 5 9921 8474 9801 -1405 4453 -1129 C
ATOM 67 CG1 VAL A 5 484.627 203.682 546.176 1.00 78.76 C
ANISOU 67 CG1 VAL A 5 10599 9010 10315 -1161 4395 -869 C
ATOM 68 CG2 VAL A 5 482.593 202.502 547.019 1.00 75.56 C
ANISOU 68 CG2 VAL A 5 10303 8425 9980 -1684 4615 -1159 C
ATOM 69 N ARG A 6 483.254 205.912 543.989 1.00 70.26 N
ANISOU 69 N ARG A 6 8819 8542 9334 -974 4066 -1081 N
ATOM 70 CA ARG A 6 484.052 206.925 543.303 1.00 65.88 C
ANISOU 70 CA ARG A 6 8091 8170 8768 -709 3911 -909 C
ATOM 71 C ARG A 6 483.476 208.326 543.477 1.00 70.64 C
ANISOU 71 C ARG A 6 8450 8936 9452 -701 3770 -878 C
ATOM 72 O ARG A 6 484.224 209.308 543.434 1.00 89.03 O
ANISOU 72 O ARG A 6 10677 11344 11807 -535 3660 -692 O
ATOM 73 CB ARG A 6 484.164 206.585 541.816 1.00 72.49 C
ANISOU 73 CB ARG A 6 8840 9159 9545 -556 3902 -986 C
ATOM 74 CG ARG A 6 484.637 205.165 541.552 1.00 66.97 C
ANISOU 74 CG ARG A 6 8388 8284 8771 -549 4058 -1077 C
ATOM 75 CD ARG A 6 484.992 204.911 540.094 1.00 79.27 C
ANISOU 75 CD ARG A 6 9868 10017 10234 -332 4028 -1144 C
ATOM 76 NE ARG A 6 485.669 203.624 539.962 1.00 76.45 N
ANISOU 76 NE ARG A 6 9785 9451 9812 -266 4111 -1194 N
ATOM 77 CZ ARG A 6 486.970 203.443 540.166 1.00 78.68 C
ANISOU 77 CZ ARG A 6 10206 9638 10052 -64 4104 -975 C
ATOM 78 NH1 ARG A 6 487.744 204.474 540.486 1.00 75.93 N
ANISOU 78 NH1 ARG A 6 9738 9395 9717 70 4053 -704 N
ATOM 79 NH2 ARG A 6 487.498 202.234 540.043 1.00 83.20 N
ANISOU 79 NH2 ARG A 6 11027 10002 10582 5 4142 -1029 N
ATOM 80 N GLN A 7 482.161 208.446 543.654 1.00 78.28 N
ANISOU 80 N GLN A 7 9318 9949 10475 -874 3782 -1057 N
ATOM 81 CA GLN A 7 481.545 209.743 543.899 1.00 80.06 C
ANISOU 81 CA GLN A 7 9332 10301 10788 -857 3670 -1042 C
ATOM 82 C GLN A 7 481.545 210.119 545.375 1.00 80.35 C
ANISOU 82 C GLN A 7 9468 10210 10850 -959 3691 -1010 C
ATOM 83 O GLN A 7 481.553 211.313 545.701 1.00 82.69 O
ANISOU 83 O GLN A 7 9633 10568 11217 -886 3603 -948 O
ATOM 84 CB GLN A 7 480.109 209.752 543.354 1.00 74.79 C
ANISOU 84 CB GLN A 7 8484 9770 10163 -967 3669 -1246 C
ATOM 85 CG GLN A 7 479.274 210.975 543.731 1.00 92.34 C
ANISOU 85 CG GLN A 7 10507 12093 12485 -967 3585 -1261 C
ATOM 86 CD GLN A 7 478.316 210.703 544.882 1.00103.44 C
ANISOU 86 CD GLN A 7 11981 13406 13915 -1192 3673 -1407 C
ATOM 87 OE1 GLN A 7 477.956 209.556 545.148 1.00109.18 O
ANISOU 87 OE1 GLN A 7 12850 14033 14599 -1380 3793 -1527 O
ATOM 88 NE2 GLN A 7 477.898 211.762 545.570 1.00110.35 N
ANISOU 88 NE2 GLN A 7 12753 14315 14862 -1173 3626 -1400 N
ATOM 89 N CYS A 8 481.574 209.128 546.269 1.00 79.54 N
ANISOU 89 N CYS A 8 9598 9934 10690 -1121 3814 -1049 N
ATOM 90 CA CYS A 8 481.485 209.384 547.703 1.00 79.32 C
ANISOU 90 CA CYS A 8 9667 9821 10649 -1228 3847 -1035 C
ATOM 91 C CYS A 8 482.831 209.773 548.306 1.00 81.47 C
ANISOU 91 C CYS A 8 10045 10026 10884 -1106 3810 -838 C
ATOM 92 O CYS A 8 482.889 210.631 549.193 1.00 80.68 O
ANISOU 92 O CYS A 8 9911 9941 10802 -1110 3777 -818 O
ATOM 93 CB CYS A 8 480.929 208.149 548.411 1.00 80.56 C
ANISOU 93 CB CYS A 8 10020 9840 10747 -1457 3998 -1132 C
ATOM 94 SG CYS A 8 480.881 208.240 550.211 1.00 80.58 S
ANISOU 94 SG CYS A 8 10171 9770 10677 -1587 4058 -1095 S
ATOM 95 N PHE A 9 483.918 209.153 547.858 1.00 76.78 N
ANISOU 95 N PHE A 9 9574 9360 10238 -998 3825 -703 N
ATOM 96 CA PHE A 9 485.223 209.392 548.450 1.00 71.04 C
ANISOU 96 CA PHE A 9 8950 8569 9471 -893 3800 -505 C
ATOM 97 C PHE A 9 486.123 210.166 547.500 1.00 68.72 C
ANISOU 97 C PHE A 9 8498 8379 9232 -668 3688 -356 C
ATOM 98 O PHE A 9 485.924 210.186 546.284 1.00 72.13 O
ANISOU 98 O PHE A 9 8796 8920 9690 -573 3648 -381 O
ATOM 99 CB PHE A 9 485.899 208.079 548.852 1.00 66.25 C
ANISOU 99 CB PHE A 9 8622 7787 8761 -928 3914 -419 C
ATOM 100 CG PHE A 9 485.128 207.289 549.868 1.00 75.23 C
ANISOU 100 CG PHE A 9 9929 8814 9842 -1155 4029 -516 C
ATOM 101 CD1 PHE A 9 485.449 207.373 551.212 1.00 64.40 C
ANISOU 101 CD1 PHE A 9 8684 7396 8389 -1222 4046 -432 C
ATOM 102 CD2 PHE A 9 484.100 206.444 549.478 1.00 71.26 C
ANISOU 102 CD2 PHE A 9 9452 8265 9360 -1309 4127 -683 C
ATOM 103 CE1 PHE A 9 484.746 206.636 552.156 1.00 63.85 C
ANISOU 103 CE1 PHE A 9 8761 7249 8249 -1424 4151 -492 C
ATOM 104 CE2 PHE A 9 483.400 205.709 550.410 1.00 69.26 C
ANISOU 104 CE2 PHE A 9 9343 7911 9064 -1527 4240 -747 C
ATOM 105 CZ PHE A 9 483.724 205.804 551.753 1.00 60.13 C
ANISOU 105 CZ PHE A 9 8309 6722 7815 -1576 4248 -639 C
ATOM 106 N ASN A 10 487.128 210.803 548.089 1.00 61.30 N
ANISOU 106 N ASN A 10 7569 7418 8304 -589 3642 -194 N
ATOM 107 CA ASN A 10 488.051 211.637 547.354 1.00 68.54 C
ANISOU 107 CA ASN A 10 8324 8423 9294 -394 3539 -20 C
ATOM 108 C ASN A 10 488.943 210.775 546.459 1.00 73.43 C
ANISOU 108 C ASN A 10 9016 9042 9841 -239 3556 112 C
ATOM 109 O ASN A 10 489.209 209.610 546.766 1.00 60.21 O
ANISOU 109 O ASN A 10 7565 7243 8069 -273 3658 116 O
ATOM 110 CB ASN A 10 488.865 212.475 548.337 1.00 76.22 C
ANISOU 110 CB ASN A 10 9296 9353 10312 -386 3508 103 C
ATOM 111 CG ASN A 10 490.205 212.898 547.785 1.00105.46 C
ANISOU 111 CG ASN A 10 12911 13092 14065 -196 3432 353 C
ATOM 112 OD1 ASN A 10 490.295 213.680 546.837 1.00120.05 O
ANISOU 112 OD1 ASN A 10 14547 15047 16020 -78 3339 425 O
ATOM 113 ND2 ASN A 10 491.268 212.405 548.405 1.00110.47 N
ANISOU 113 ND2 ASN A 10 13704 13648 14623 -164 3463 510 N
ATOM 114 N PRO A 11 489.363 211.318 545.310 1.00 63.39 N
ANISOU 114 N PRO A 11 7556 7913 8615 -62 3465 220 N
ATOM 115 CA PRO A 11 490.134 210.510 544.346 1.00 58.31 C
ANISOU 115 CA PRO A 11 6961 7310 7886 109 3485 319 C
ATOM 116 C PRO A 11 491.420 209.921 544.897 1.00 60.06 C
ANISOU 116 C PRO A 11 7359 7413 8047 198 3529 507 C
ATOM 117 O PRO A 11 491.801 208.812 544.496 1.00 67.88 O
ANISOU 117 O PRO A 11 8497 8350 8945 285 3614 515 O
ATOM 118 CB PRO A 11 490.428 211.508 543.214 1.00 56.83 C
ANISOU 118 CB PRO A 11 6509 7326 7759 277 3352 444 C
ATOM 119 CG PRO A 11 489.301 212.483 543.280 1.00 62.61 C
ANISOU 119 CG PRO A 11 7071 8121 8596 166 3297 317 C
ATOM 120 CD PRO A 11 488.936 212.609 544.740 1.00 70.31 C
ANISOU 120 CD PRO A 11 8166 8934 9614 -17 3351 225 C
ATOM 121 N MET A 12 492.119 210.634 545.783 1.00 58.23 N
ANISOU 121 N MET A 12 7112 7143 7871 191 3478 659 N
ATOM 122 CA MET A 12 493.355 210.087 546.337 1.00 53.89 C
ANISOU 122 CA MET A 12 6714 6504 7257 281 3509 859 C
ATOM 123 C MET A 12 493.067 208.887 547.231 1.00 56.73 C
ANISOU 123 C MET A 12 7366 6681 7508 150 3645 771 C
ATOM 124 O MET A 12 493.846 207.927 547.268 1.00 58.94 O
ANISOU 124 O MET A 12 7818 6870 7706 256 3713 893 O
ATOM 125 CB MET A 12 494.118 211.172 547.102 1.00 64.57 C
ANISOU 125 CB MET A 12 7964 7874 8697 280 3420 1032 C
ATOM 126 CG MET A 12 495.365 210.686 547.844 1.00 90.09 C
ANISOU 126 CG MET A 12 11339 11035 11856 352 3434 1251 C
ATOM 127 SD MET A 12 495.135 210.741 549.640 1.00110.88 S
ANISOU 127 SD MET A 12 14158 13545 14428 124 3477 1192 S
ATOM 128 CE MET A 12 496.820 210.861 550.246 1.00105.89 C
ANISOU 128 CE MET A 12 13537 12926 13768 251 3329 1493 C
ATOM 129 N ILE A 13 491.944 208.907 547.944 1.00 57.27 N
ANISOU 129 N ILE A 13 7492 6691 7576 -73 3689 573 N
ATOM 130 CA ILE A 13 491.587 207.739 548.741 1.00 58.78 C
ANISOU 130 CA ILE A 13 7954 6711 7668 -216 3815 505 C
ATOM 131 C ILE A 13 491.163 206.594 547.833 1.00 64.41 C
ANISOU 131 C ILE A 13 8765 7352 8354 -194 3927 391 C
ATOM 132 O ILE A 13 491.531 205.434 548.058 1.00 64.23 O
ANISOU 132 O ILE A 13 8982 7158 8262 -182 4046 448 O
ATOM 133 CB ILE A 13 490.495 208.099 549.762 1.00 60.01 C
ANISOU 133 CB ILE A 13 8121 6856 7823 -456 3827 333 C
ATOM 134 CG1 ILE A 13 491.098 208.931 550.897 1.00 58.71 C
ANISOU 134 CG1 ILE A 13 7948 6720 7640 -481 3767 444 C
ATOM 135 CG2 ILE A 13 489.844 206.842 550.311 1.00 60.36 C
ANISOU 135 CG2 ILE A 13 8405 6743 7785 -624 3960 241 C
ATOM 136 CD1 ILE A 13 490.090 209.393 551.908 1.00 71.28 C
ANISOU 136 CD1 ILE A 13 9535 8336 9214 -685 3789 268 C
ATOM 137 N VAL A 14 490.409 206.904 546.775 1.00 65.87 N
ANISOU 137 N VAL A 14 8771 7662 8595 -182 3896 234 N
ATOM 138 CA VAL A 14 489.948 205.863 545.859 1.00 75.17 C
ANISOU 138 CA VAL A 14 10026 8791 9743 -173 4008 82 C
ATOM 139 C VAL A 14 491.134 205.187 545.183 1.00 76.36 C
ANISOU 139 C VAL A 14 10269 8912 9834 82 4052 227 C
ATOM 140 O VAL A 14 491.193 203.954 545.085 1.00 73.65 O
ANISOU 140 O VAL A 14 10144 8391 9449 89 4117 163 O
ATOM 141 CB VAL A 14 488.964 206.454 544.833 1.00 67.88 C
ANISOU 141 CB VAL A 14 8858 8062 8870 -190 3933 -98 C
ATOM 142 CG1 VAL A 14 488.681 205.455 543.722 1.00 72.61 C
ANISOU 142 CG1 VAL A 14 9511 8655 9421 -137 4030 -260 C
ATOM 143 CG2 VAL A 14 487.671 206.870 545.523 1.00 69.89 C
ANISOU 143 CG2 VAL A 14 9053 8319 9181 -437 3925 -265 C
ATOM 144 N GLU A 15 492.110 205.979 544.733 1.00 60.08 N
ANISOU 144 N GLU A 15 8034 7012 7781 298 3924 423 N
ATOM 145 CA GLU A 15 493.265 205.416 544.040 1.00 66.74 C
ANISOU 145 CA GLU A 15 8922 7872 8564 569 3919 567 C
ATOM 146 C GLU A 15 494.127 204.585 544.984 1.00 60.20 C
ANISOU 146 C GLU A 15 8347 6829 7696 602 3940 720 C
ATOM 147 O GLU A 15 494.653 203.536 544.590 1.00 59.11 O
ANISOU 147 O GLU A 15 8365 6584 7512 755 3975 728 O
ATOM 148 CB GLU A 15 494.080 206.537 543.383 1.00 72.95 C
ANISOU 148 CB GLU A 15 9434 8904 9381 764 3772 766 C
ATOM 149 CG GLU A 15 495.312 207.012 544.158 1.00 95.59 C
ANISOU 149 CG GLU A 15 12286 11759 12273 851 3704 1055 C
ATOM 150 CD GLU A 15 495.784 208.401 543.745 1.00113.73 C
ANISOU 150 CD GLU A 15 14288 14265 14658 926 3524 1215 C
ATOM 151 OE1 GLU A 15 496.428 208.524 542.682 1.00110.01 O
ANISOU 151 OE1 GLU A 15 13674 13961 14163 1132 3455 1326 O
ATOM 152 OE2 GLU A 15 495.525 209.370 544.490 1.00118.08 O
ANISOU 152 OE2 GLU A 15 14755 14807 15303 778 3455 1231 O
ATOM 153 N LEU A 16 494.278 205.023 546.237 1.00 56.05 N
ANISOU 153 N LEU A 16 7869 6243 7186 470 3916 838 N
ATOM 154 CA LEU A 16 495.032 204.218 547.195 1.00 70.95 C
ANISOU 154 CA LEU A 16 9997 7942 9019 491 3929 998 C
ATOM 155 C LEU A 16 494.300 202.920 547.503 1.00 64.67 C
ANISOU 155 C LEU A 16 9476 6895 8199 345 4055 847 C
ATOM 156 O LEU A 16 494.930 201.867 547.659 1.00 79.55 O
ANISOU 156 O LEU A 16 11572 8597 10055 454 4082 943 O
ATOM 157 CB LEU A 16 495.287 205.012 548.477 1.00 67.88 C
ANISOU 157 CB LEU A 16 9590 7579 8623 369 3867 1136 C
ATOM 158 CG LEU A 16 496.308 206.152 548.407 1.00 69.02 C
ANISOU 158 CG LEU A 16 9506 7908 8810 514 3723 1342 C
ATOM 159 CD1 LEU A 16 496.407 206.859 549.749 1.00 63.01 C
ANISOU 159 CD1 LEU A 16 8755 7151 8035 357 3660 1411 C
ATOM 160 CD2 LEU A 16 497.675 205.656 547.959 1.00 61.47 C
ANISOU 160 CD2 LEU A 16 8560 6970 7828 794 3670 1568 C
ATOM 161 N ALA A 17 492.968 202.970 547.578 1.00 64.11 N
ANISOU 161 N ALA A 17 9396 6806 8156 99 4132 617 N
ATOM 162 CA ALA A 17 492.200 201.753 547.816 1.00 66.18 C
ANISOU 162 CA ALA A 17 9897 6827 8423 -72 4254 471 C
ATOM 163 C ALA A 17 492.342 200.778 546.656 1.00 70.52 C
ANISOU 163 C ALA A 17 10522 7280 8991 88 4274 352 C
ATOM 164 O ALA A 17 492.446 199.563 546.864 1.00 73.16 O
ANISOU 164 O ALA A 17 11112 7347 9340 80 4339 349 O
ATOM 165 CB ALA A 17 490.729 202.096 548.051 1.00 63.97 C
ANISOU 165 CB ALA A 17 9539 6590 8177 -368 4329 246 C
ATOM 166 N GLU A 18 492.355 201.292 545.425 1.00 72.78 N
ANISOU 166 N GLU A 18 10592 7782 9278 242 4218 253 N
ATOM 167 CA GLU A 18 492.521 200.426 544.261 1.00 69.90 C
ANISOU 167 CA GLU A 18 10285 7372 8902 417 4230 112 C
ATOM 168 C GLU A 18 493.883 199.744 544.274 1.00 63.78 C
ANISOU 168 C GLU A 18 9658 6478 8097 695 4213 311 C
ATOM 169 O GLU A 18 493.975 198.521 544.105 1.00 73.84 O
ANISOU 169 O GLU A 18 11158 7503 9393 748 4269 223 O
ATOM 170 CB GLU A 18 492.334 201.232 542.978 1.00 81.97 C
ANISOU 170 CB GLU A 18 11529 9218 10399 544 4167 5 C
ATOM 171 CG GLU A 18 490.912 201.711 542.770 1.00 98.20 C
ANISOU 171 CG GLU A 18 13439 11380 12491 298 4184 -229 C
ATOM 172 CD GLU A 18 490.676 202.240 541.373 1.00103.49 C
ANISOU 172 CD GLU A 18 13861 12345 13113 437 4123 -350 C
ATOM 173 OE1 GLU A 18 491.190 203.333 541.055 1.00105.96 O
ANISOU 173 OE1 GLU A 18 13945 12904 13410 585 4046 -173 O
ATOM 174 OE2 GLU A 18 489.974 201.563 540.595 1.00110.31 O
ANISOU 174 OE2 GLU A 18 14758 13199 13956 393 4147 -617 O
ATOM 175 N LYS A 19 494.955 200.519 544.468 1.00 68.21 N
ANISOU 175 N LYS A 19 10084 7206 8626 876 4131 577 N
ATOM 176 CA LYS A 19 496.292 199.932 544.525 1.00 75.85 C
ANISOU 176 CA LYS A 19 11158 8091 9569 1151 4110 790 C
ATOM 177 C LYS A 19 496.405 198.925 545.662 1.00 79.93 C
ANISOU 177 C LYS A 19 11982 8274 10112 1056 4164 883 C
ATOM 178 O LYS A 19 497.097 197.908 545.532 1.00 85.75 O
ANISOU 178 O LYS A 19 12898 8821 10861 1251 4188 939 O
ATOM 179 CB LYS A 19 497.345 201.030 544.679 1.00 78.37 C
ANISOU 179 CB LYS A 19 11254 8658 9866 1307 4004 1073 C
ATOM 180 CG LYS A 19 497.512 201.907 543.452 1.00 99.20 C
ANISOU 180 CG LYS A 19 13592 11619 12481 1467 3953 1057 C
ATOM 181 CD LYS A 19 498.681 202.871 543.610 1.00107.99 C
ANISOU 181 CD LYS A 19 14492 12938 13599 1624 3851 1368 C
ATOM 182 CE LYS A 19 499.882 202.195 544.258 1.00111.06 C
ANISOU 182 CE LYS A 19 15026 13196 13975 1794 3834 1598 C
ATOM 183 NZ LYS A 19 501.157 202.899 543.936 1.00109.86 N
ANISOU 183 NZ LYS A 19 14634 13288 13822 2030 3745 1875 N
ATOM 184 N ALA A 20 495.728 199.188 546.784 1.00 76.05 N
ANISOU 184 N ALA A 20 11555 7712 9629 767 4187 907 N
ATOM 185 CA ALA A 20 495.765 198.250 547.902 1.00 75.17 C
ANISOU 185 CA ALA A 20 11732 7304 9524 657 4245 1023 C
ATOM 186 C ALA A 20 495.046 196.952 547.569 1.00 83.42 C
ANISOU 186 C ALA A 20 13008 8043 10645 565 4352 814 C
ATOM 187 O ALA A 20 495.431 195.890 548.069 1.00 90.43 O
ANISOU 187 O ALA A 20 14152 8639 11569 609 4393 931 O
ATOM 188 CB ALA A 20 495.154 198.884 549.152 1.00 68.27 C
ANISOU 188 CB ALA A 20 10855 6475 8611 366 4256 1085 C
ATOM 189 N MET A 21 494.006 197.010 546.735 1.00 82.19 N
ANISOU 189 N MET A 21 12762 7939 10526 436 4390 511 N
ATOM 190 CA MET A 21 493.282 195.805 546.351 1.00 88.39 C
ANISOU 190 CA MET A 21 13749 8434 11401 326 4476 277 C
ATOM 191 C MET A 21 493.926 195.078 545.181 1.00 94.16 C
ANISOU 191 C MET A 21 14530 9095 12152 632 4458 160 C
ATOM 192 O MET A 21 493.872 193.844 545.129 1.00101.46 O
ANISOU 192 O MET A 21 15704 9676 13168 637 4516 71 O
ATOM 193 CB MET A 21 491.832 196.141 545.997 1.00 82.95 C
ANISOU 193 CB MET A 21 12933 7842 10743 36 4517 -15 C
ATOM 194 CG MET A 21 490.992 196.555 547.185 1.00 85.49 C
ANISOU 194 CG MET A 21 13254 8166 11062 -298 4576 45 C
ATOM 195 SD MET A 21 489.281 196.863 546.725 1.00 82.19 S
ANISOU 195 SD MET A 21 12667 7864 10699 -621 4629 -303 S
ATOM 196 CE MET A 21 488.686 195.192 546.465 1.00 67.75 C
ANISOU 196 CE MET A 21 11117 5620 9004 -775 4720 -503 C
ATOM 197 N LYS A 22 494.523 195.805 544.235 1.00 89.45 N
ANISOU 197 N LYS A 22 13701 8812 11475 888 4385 154 N
ATOM 198 CA LYS A 22 495.243 195.141 543.154 1.00 89.90 C
ANISOU 198 CA LYS A 22 13795 8845 11518 1214 4377 56 C
ATOM 199 C LYS A 22 496.454 194.397 543.701 1.00 90.92 C
ANISOU 199 C LYS A 22 14119 8748 11678 1453 4382 311 C
ATOM 200 O LYS A 22 496.671 193.220 543.387 1.00 91.20 O
ANISOU 200 O LYS A 22 14373 8494 11787 1586 4427 202 O
ATOM 201 CB LYS A 22 495.638 196.161 542.085 1.00 93.16 C
ANISOU 201 CB LYS A 22 13892 9687 11817 1430 4307 45 C
ATOM 202 CG LYS A 22 494.457 196.600 541.221 1.00 98.84 C
ANISOU 202 CG LYS A 22 14445 10605 12507 1264 4301 -260 C
ATOM 203 CD LYS A 22 494.765 197.849 540.410 1.00 98.03 C
ANISOU 203 CD LYS A 22 14004 10948 12295 1424 4227 -184 C
ATOM 204 CE LYS A 22 493.530 198.341 539.665 1.00 93.91 C
ANISOU 204 CE LYS A 22 13306 10629 11744 1245 4211 -453 C
ATOM 205 NZ LYS A 22 493.709 199.717 539.119 1.00 88.70 N
ANISOU 205 NZ LYS A 22 12312 10381 11009 1344 4136 -316 N
ATOM 206 N GLU A 23 497.248 195.061 544.536 1.00 86.77 N
ANISOU 206 N GLU A 23 13515 8345 11107 1513 4328 646 N
ATOM 207 CA GLU A 23 498.124 194.327 545.434 1.00 93.40 C
ANISOU 207 CA GLU A 23 14569 8932 11988 1633 4332 914 C
ATOM 208 C GLU A 23 497.262 193.465 546.350 1.00107.78 C
ANISOU 208 C GLU A 23 16673 10376 13901 1331 4412 879 C
ATOM 209 O GLU A 23 496.123 193.814 546.664 1.00121.50 O
ANISOU 209 O GLU A 23 18382 12138 15644 997 4448 748 O
ATOM 210 CB GLU A 23 498.989 195.293 546.244 1.00 92.62 C
ANISOU 210 CB GLU A 23 14315 9065 11812 1692 4242 1260 C
ATOM 211 CG GLU A 23 500.185 194.649 546.920 1.00108.84 C
ANISOU 211 CG GLU A 23 16516 10959 13879 1921 4214 1565 C
ATOM 212 CD GLU A 23 500.832 195.560 547.946 1.00114.73 C
ANISOU 212 CD GLU A 23 17135 11908 14548 1888 4115 1883 C
ATOM 213 OE1 GLU A 23 500.355 196.703 548.111 1.00115.66 O
ANISOU 213 OE1 GLU A 23 17059 12272 14616 1693 4073 1850 O
ATOM 214 OE2 GLU A 23 501.814 195.133 548.588 1.00120.85 O
ANISOU 214 OE2 GLU A 23 18003 12594 15318 2062 4073 2159 O
ATOM 215 N TYR A 24 497.796 192.314 546.755 1.00105.44 N
ANISOU 215 N TYR A 24 16644 9730 13690 1454 4446 1004 N
ATOM 216 CA TYR A 24 497.060 191.242 547.429 1.00111.88 C
ANISOU 216 CA TYR A 24 17759 10121 14629 1210 4534 973 C
ATOM 217 C TYR A 24 496.049 190.564 546.507 1.00116.59 C
ANISOU 217 C TYR A 24 18435 10527 15338 1077 4600 570 C
ATOM 218 O TYR A 24 495.367 189.630 546.944 1.00115.67 O
ANISOU 218 O TYR A 24 18557 10035 15356 852 4676 514 O
ATOM 219 CB TYR A 24 496.323 191.709 548.696 1.00110.42 C
ANISOU 219 CB TYR A 24 17591 9969 14396 840 4561 1120 C
ATOM 220 CG TYR A 24 497.204 192.312 549.769 1.00112.31 C
ANISOU 220 CG TYR A 24 17783 10374 14515 917 4489 1499 C
ATOM 221 CD1 TYR A 24 497.755 191.519 550.770 1.00111.92 C
ANISOU 221 CD1 TYR A 24 17971 10067 14486 960 4500 1800 C
ATOM 222 CD2 TYR A 24 497.468 193.676 549.794 1.00111.35 C
ANISOU 222 CD2 TYR A 24 17377 10665 14265 936 4402 1556 C
ATOM 223 CE1 TYR A 24 498.555 192.066 551.757 1.00108.01 C
ANISOU 223 CE1 TYR A 24 17425 9752 13861 1025 4417 2136 C
ATOM 224 CE2 TYR A 24 498.268 194.232 550.778 1.00109.21 C
ANISOU 224 CE2 TYR A 24 17058 10547 13888 990 4320 1873 C
ATOM 225 CZ TYR A 24 498.808 193.422 551.756 1.00113.70 C
ANISOU 225 CZ TYR A 24 17860 10887 14455 1034 4324 2155 C
ATOM 226 OH TYR A 24 499.603 193.972 552.736 1.00120.10 O
ANISOU 226 OH TYR A 24 18615 11877 15140 1085 4226 2460 O
ATOM 227 N GLY A 25 495.914 191.010 545.258 1.00119.18 N
ANISOU 227 N GLY A 25 18563 11109 15612 1195 4568 295 N
ATOM 228 CA GLY A 25 495.108 190.321 544.268 1.00121.49 C
ANISOU 228 CA GLY A 25 18923 11247 15991 1124 4607 -109 C
ATOM 229 C GLY A 25 493.607 190.371 544.474 1.00123.41 C
ANISOU 229 C GLY A 25 19163 11436 16293 682 4654 -320 C
ATOM 230 O GLY A 25 492.976 189.334 544.695 1.00130.98 O
ANISOU 230 O GLY A 25 20354 12001 17412 481 4720 -442 O
ATOM 231 N GLU A 26 493.021 191.565 544.395 1.00115.01 N
ANISOU 231 N GLU A 26 17826 10755 15116 527 4623 -361 N
ATOM 232 CA GLU A 26 491.575 191.731 544.463 1.00107.57 C
ANISOU 232 CA GLU A 26 16821 9832 14219 134 4664 -583 C
ATOM 233 C GLU A 26 491.145 192.756 543.420 1.00103.81 C
ANISOU 233 C GLU A 26 16026 9787 13631 168 4599 -800 C
ATOM 234 O GLU A 26 491.940 193.584 542.968 1.00102.18 O
ANISOU 234 O GLU A 26 15628 9895 13301 437 4529 -687 O
ATOM 235 CB GLU A 26 491.112 192.166 545.863 1.00107.36 C
ANISOU 235 CB GLU A 26 16806 9801 14184 -163 4716 -343 C
ATOM 236 CG GLU A 26 491.492 191.204 546.980 1.00115.92 C
ANISOU 236 CG GLU A 26 18197 10493 15355 -214 4782 -80 C
ATOM 237 CD GLU A 26 490.285 190.558 547.635 1.00127.57 C
ANISOU 237 CD GLU A 26 19814 11702 16952 -630 4890 -151 C
ATOM 238 OE1 GLU A 26 490.427 190.033 548.760 1.00130.56 O
ANISOU 238 OE1 GLU A 26 20399 11841 17368 -739 4954 122 O
ATOM 239 OE2 GLU A 26 489.195 190.575 547.025 1.00132.26 O
ANISOU 239 OE2 GLU A 26 20305 12343 17604 -849 4911 -466 O
ATOM 240 N ASP A 27 489.869 192.693 543.042 1.00103.10 N
ANISOU 240 N ASP A 27 15869 9714 13592 -114 4619 -1097 N
ATOM 241 CA ASP A 27 489.316 193.557 542.003 1.00101.01 C
ANISOU 241 CA ASP A 27 15308 9844 13230 -100 4552 -1323 C
ATOM 242 C ASP A 27 488.258 194.480 542.593 1.00 93.87 C
ANISOU 242 C ASP A 27 14209 9134 12322 -417 4571 -1309 C
ATOM 243 O ASP A 27 487.237 193.992 543.109 1.00100.30 O
ANISOU 243 O ASP A 27 15108 9755 13246 -754 4643 -1420 O
ATOM 244 CB ASP A 27 488.720 192.719 540.867 1.00106.58 C
ANISOU 244 CB ASP A 27 16061 10454 13980 -123 4537 -1730 C
ATOM 245 CG ASP A 27 488.496 193.524 539.599 1.00108.47 C
ANISOU 245 CG ASP A 27 16005 11137 14071 13 4447 -1930 C
ATOM 246 OD1 ASP A 27 488.625 194.766 539.643 1.00104.12 O
ANISOU 246 OD1 ASP A 27 15203 10942 13416 73 4406 -1753 O
ATOM 247 OD2 ASP A 27 488.194 192.911 538.552 1.00112.40 O
ANISOU 247 OD2 ASP A 27 16525 11627 14556 61 4414 -2265 O
ATOM 248 N PRO A 28 488.445 195.803 542.543 1.00 87.22 N
ANISOU 248 N PRO A 28 13101 8665 11373 -325 4513 -1176 N
ATOM 249 CA PRO A 28 487.396 196.715 543.030 1.00 84.45 C
ANISOU 249 CA PRO A 28 12551 8505 11033 -600 4530 -1199 C
ATOM 250 C PRO A 28 486.131 196.691 542.189 1.00 92.52 C
ANISOU 250 C PRO A 28 13417 9652 12085 -785 4517 -1543 C
ATOM 251 O PRO A 28 485.074 197.105 542.683 1.00 94.09 O
ANISOU 251 O PRO A 28 13498 9922 12332 -1067 4560 -1603 O
ATOM 252 CB PRO A 28 488.070 198.094 542.975 1.00 81.10 C
ANISOU 252 CB PRO A 28 11885 8421 10508 -393 4450 -987 C
ATOM 253 CG PRO A 28 489.544 197.812 542.889 1.00 74.94 C
ANISOU 253 CG PRO A 28 11224 7574 9677 -65 4415 -771 C
ATOM 254 CD PRO A 28 489.664 196.525 542.142 1.00 82.62 C
ANISOU 254 CD PRO A 28 12392 8321 10678 31 4435 -972 C
ATOM 255 N LYS A 29 486.205 196.237 540.935 1.00 95.83 N
ANISOU 255 N LYS A 29 13820 10124 12467 -629 4457 -1776 N
ATOM 256 CA LYS A 29 485.013 196.116 540.104 1.00 90.76 C
ANISOU 256 CA LYS A 29 13037 9604 11844 -808 4426 -2123 C
ATOM 257 C LYS A 29 484.113 194.969 540.545 1.00 90.11 C
ANISOU 257 C LYS A 29 13152 9165 11922 -1147 4507 -2315 C
ATOM 258 O LYS A 29 482.919 194.979 540.226 1.00 97.08 O
ANISOU 258 O LYS A 29 13892 10141 12853 -1398 4498 -2563 O
ATOM 259 CB LYS A 29 485.408 195.919 538.637 1.00 92.21 C
ANISOU 259 CB LYS A 29 13158 9966 11911 -530 4332 -2328 C
ATOM 260 CG LYS A 29 485.970 197.161 537.964 1.00 99.73 C
ANISOU 260 CG LYS A 29 13834 11355 12705 -249 4246 -2178 C
ATOM 261 CD LYS A 29 485.105 197.597 536.788 1.00109.45 C
ANISOU 261 CD LYS A 29 14799 12940 13846 -267 4158 -2440 C
ATOM 262 CE LYS A 29 485.668 198.841 536.109 1.00110.44 C
ANISOU 262 CE LYS A 29 14647 13494 13822 13 4076 -2249 C
ATOM 263 NZ LYS A 29 485.403 198.831 534.639 1.00113.31 N
ANISOU 263 NZ LYS A 29 14849 14178 14026 158 3984 -2493 N
ATOM 264 N ILE A 30 484.654 193.984 541.260 1.00 90.18 N
ANISOU 264 N ILE A 30 13473 8767 12023 -1164 4581 -2193 N
ATOM 265 CA ILE A 30 483.906 192.800 541.680 1.00 96.09 C
ANISOU 265 CA ILE A 30 14436 9122 12951 -1480 4662 -2339 C
ATOM 266 C ILE A 30 483.670 192.801 543.190 1.00101.29 C
ANISOU 266 C ILE A 30 15199 9602 13683 -1732 4783 -2062 C
ATOM 267 O ILE A 30 482.529 192.747 543.647 1.00104.16 O
ANISOU 267 O ILE A 30 15496 9945 14135 -2087 4853 -2147 O
ATOM 268 CB ILE A 30 484.610 191.505 541.221 1.00102.64 C
ANISOU 268 CB ILE A 30 15563 9579 13858 -1313 4653 -2448 C
ATOM 269 CG1 ILE A 30 484.481 191.339 539.706 1.00104.69 C
ANISOU 269 CG1 ILE A 30 15719 10010 14047 -1158 4546 -2825 C
ATOM 270 CG2 ILE A 30 484.027 190.295 541.937 1.00101.61 C
ANISOU 270 CG2 ILE A 30 15695 8963 13949 -1639 4750 -2487 C
ATOM 271 CD1 ILE A 30 485.727 190.804 539.040 1.00106.58 C
ANISOU 271 CD1 ILE A 30 16121 10150 14224 -753 4508 -2838 C
ATOM 272 N GLU A 31 484.745 192.851 543.979 1.00100.11 N
ANISOU 272 N GLU A 31 15203 9345 13487 -1550 4810 -1728 N
ATOM 273 CA GLU A 31 484.619 192.969 545.433 1.00 97.90 C
ANISOU 273 CA GLU A 31 15008 8965 13223 -1753 4915 -1442 C
ATOM 274 C GLU A 31 484.340 194.433 545.771 1.00 90.06 C
ANISOU 274 C GLU A 31 13724 8387 12106 -1772 4899 -1353 C
ATOM 275 O GLU A 31 485.175 195.168 546.306 1.00 89.58 O
ANISOU 275 O GLU A 31 13634 8462 11939 -1591 4872 -1096 O
ATOM 276 CB GLU A 31 485.865 192.446 546.133 1.00 99.20 C
ANISOU 276 CB GLU A 31 15441 8873 13376 -1547 4933 -1125 C
ATOM 277 CG GLU A 31 485.830 190.950 546.412 1.00106.08 C
ANISOU 277 CG GLU A 31 16640 9243 14422 -1668 5005 -1126 C
ATOM 278 CD GLU A 31 485.184 190.610 547.746 1.00120.43 C
ANISOU 278 CD GLU A 31 18578 10876 16304 -2021 5139 -928 C
ATOM 279 OE1 GLU A 31 485.586 189.595 548.352 1.00126.39 O
ANISOU 279 OE1 GLU A 31 19624 11240 17160 -2040 5198 -739 O
ATOM 280 OE2 GLU A 31 484.279 191.352 548.191 1.00118.18 O
ANISOU 280 OE2 GLU A 31 18095 10841 15968 -2269 5192 -951 O
ATOM 281 N THR A 32 483.121 194.853 545.434 1.00 84.30 N
ANISOU 281 N THR A 32 12767 7856 11409 -1999 4908 -1586 N
ATOM 282 CA THR A 32 482.776 196.267 545.496 1.00 85.42 C
ANISOU 282 CA THR A 32 12601 8395 11459 -1984 4875 -1564 C
ATOM 283 C THR A 32 482.447 196.708 546.916 1.00 84.16 C
ANISOU 283 C THR A 32 12444 8255 11279 -2188 4986 -1364 C
ATOM 284 O THR A 32 482.757 197.841 547.302 1.00 86.15 O
ANISOU 284 O THR A 32 12544 8750 11438 -2076 4954 -1227 O
ATOM 285 CB THR A 32 481.611 196.552 544.551 1.00 86.45 C
ANISOU 285 CB THR A 32 12471 8748 11630 -2119 4833 -1886 C
ATOM 286 OG1 THR A 32 480.470 195.786 544.959 1.00 91.87 O
ANISOU 286 OG1 THR A 32 13207 9255 12444 -2497 4939 -2029 O
ATOM 287 CG2 THR A 32 481.994 196.153 543.132 1.00 85.47 C
ANISOU 287 CG2 THR A 32 12344 8650 11482 -1894 4715 -2091 C
ATOM 288 N ASN A 33 481.824 195.834 547.708 1.00 74.75 N
ANISOU 288 N ASN A 33 11419 6814 10170 -2489 5117 -1344 N
ATOM 289 CA ASN A 33 481.613 196.155 549.115 1.00 83.31 C
ANISOU 289 CA ASN A 33 12533 7924 11196 -2664 5236 -1131 C
ATOM 290 C ASN A 33 482.944 196.289 549.843 1.00 87.07 C
ANISOU 290 C ASN A 33 13189 8337 11558 -2430 5206 -810 C
ATOM 291 O ASN A 33 483.129 197.201 550.659 1.00 83.10 O
ANISOU 291 O ASN A 33 12600 8033 10940 -2407 5216 -661 O
ATOM 292 CB ASN A 33 480.734 195.090 549.766 1.00 80.45 C
ANISOU 292 CB ASN A 33 12322 7302 10944 -3032 5390 -1140 C
ATOM 293 CG ASN A 33 479.324 195.085 549.208 1.00 93.99 C
ANISOU 293 CG ASN A 33 13812 9130 12770 -3304 5425 -1446 C
ATOM 294 OD1 ASN A 33 478.939 194.183 548.463 1.00104.77 O
ANISOU 294 OD1 ASN A 33 15239 10296 14274 -3411 5404 -1645 O
ATOM 295 ND2 ASN A 33 478.547 196.106 549.556 1.00 96.66 N
ANISOU 295 ND2 ASN A 33 13874 9811 13042 -3366 5414 -1502 N
ATOM 296 N LYS A 34 483.891 195.396 549.545 1.00 76.77 N
ANISOU 296 N LYS A 34 12124 6761 10286 -2246 5160 -715 N
ATOM 297 CA LYS A 34 485.231 195.504 550.113 1.00 80.88 C
ANISOU 297 CA LYS A 34 12789 7237 10703 -1991 5109 -412 C
ATOM 298 C LYS A 34 485.928 196.773 549.638 1.00 82.10 C
ANISOU 298 C LYS A 34 12718 7719 10758 -1709 4976 -389 C
ATOM 299 O LYS A 34 486.652 197.418 550.406 1.00 87.72 O
ANISOU 299 O LYS A 34 13426 8543 11361 -1601 4943 -162 O
ATOM 300 CB LYS A 34 486.045 194.270 549.733 1.00 92.38 C
ANISOU 300 CB LYS A 34 14520 8339 12241 -1826 5085 -348 C
ATOM 301 CG LYS A 34 487.443 194.248 550.293 1.00102.21 C
ANISOU 301 CG LYS A 34 15916 9525 13396 -1553 5030 -25 C
ATOM 302 CD LYS A 34 487.865 192.827 550.591 1.00111.17 C
ANISOU 302 CD LYS A 34 17382 10225 14632 -1542 5081 114 C
ATOM 303 CE LYS A 34 489.042 192.825 551.524 1.00114.64 C
ANISOU 303 CE LYS A 34 17965 10628 14965 -1353 5050 488 C
ATOM 304 NZ LYS A 34 488.552 193.179 552.872 1.00118.09 N
ANISOU 304 NZ LYS A 34 18411 11164 15292 -1611 5137 670 N
ATOM 305 N PHE A 35 485.735 197.127 548.366 1.00 80.73 N
ANISOU 305 N PHE A 35 12354 7702 10619 -1590 4894 -617 N
ATOM 306 CA PHE A 35 486.211 198.404 547.848 1.00 72.65 C
ANISOU 306 CA PHE A 35 11078 7004 9523 -1362 4777 -597 C
ATOM 307 C PHE A 35 485.726 199.556 548.719 1.00 75.34 C
ANISOU 307 C PHE A 35 11243 7569 9815 -1499 4802 -543 C
ATOM 308 O PHE A 35 486.505 200.436 549.101 1.00 70.21 O
ANISOU 308 O PHE A 35 10521 7062 9093 -1341 4730 -367 O
ATOM 309 CB PHE A 35 485.730 198.567 546.403 1.00 68.05 C
ANISOU 309 CB PHE A 35 10300 6577 8979 -1290 4709 -868 C
ATOM 310 CG PHE A 35 486.340 199.728 545.671 1.00 76.38 C
ANISOU 310 CG PHE A 35 11111 7939 9970 -1019 4585 -818 C
ATOM 311 CD1 PHE A 35 487.582 200.228 546.027 1.00 80.86 C
ANISOU 311 CD1 PHE A 35 11696 8553 10473 -789 4521 -550 C
ATOM 312 CD2 PHE A 35 485.670 200.307 544.604 1.00 77.82 C
ANISOU 312 CD2 PHE A 35 11037 8370 10162 -1000 4526 -1025 C
ATOM 313 CE1 PHE A 35 488.139 201.293 545.337 1.00 78.24 C
ANISOU 313 CE1 PHE A 35 11129 8492 10105 -559 4410 -483 C
ATOM 314 CE2 PHE A 35 486.219 201.368 543.912 1.00 74.90 C
ANISOU 314 CE2 PHE A 35 10440 8276 9742 -757 4416 -946 C
ATOM 315 CZ PHE A 35 487.455 201.864 544.279 1.00 78.17 C
ANISOU 315 CZ PHE A 35 10875 8717 10111 -543 4362 -670 C
ATOM 316 N ALA A 36 484.435 199.551 549.057 1.00 81.60 N
ANISOU 316 N ALA A 36 11961 8393 10652 -1797 4906 -703 N
ATOM 317 CA ALA A 36 483.886 200.604 549.903 1.00 77.42 C
ANISOU 317 CA ALA A 36 11253 8080 10082 -1878 4836 -696 C
ATOM 318 C ALA A 36 484.498 200.571 551.296 1.00 79.60 C
ANISOU 318 C ALA A 36 11693 8296 10257 -1863 4791 -458 C
ATOM 319 O ALA A 36 484.787 201.623 551.880 1.00 73.53 O
ANISOU 319 O ALA A 36 10799 7716 9424 -1763 4651 -385 O
ATOM 320 CB ALA A 36 482.365 200.469 549.984 1.00 69.53 C
ANISOU 320 CB ALA A 36 10135 7131 9152 -2154 4886 -919 C
ATOM 321 N ALA A 37 484.702 199.370 551.847 1.00 75.77 N
ANISOU 321 N ALA A 37 11485 7546 9758 -1964 4905 -333 N
ATOM 322 CA ALA A 37 485.241 199.259 553.199 1.00 76.63 C
ANISOU 322 CA ALA A 37 11740 7629 9747 -1949 4853 -100 C
ATOM 323 C ALA A 37 486.663 199.802 553.278 1.00 78.56 C
ANISOU 323 C ALA A 37 12005 7932 9913 -1674 4739 107 C
ATOM 324 O ALA A 37 487.023 200.474 554.253 1.00 68.83 O
ANISOU 324 O ALA A 37 10731 6851 8571 -1633 4632 222 O
ATOM 325 CB ALA A 37 485.193 197.804 553.665 1.00 67.13 C
ANISOU 325 CB ALA A 37 10822 6119 8565 -2088 4973 17 C
ATOM 326 N ILE A 38 487.483 199.531 552.259 1.00 76.92 N
ANISOU 326 N ILE A 38 11852 7619 9755 -1486 4772 153 N
ATOM 327 CA ILE A 38 488.860 200.012 552.274 1.00 69.23 C
ANISOU 327 CA ILE A 38 10877 6711 8715 -1214 4665 365 C
ATOM 328 C ILE A 38 488.894 201.534 552.204 1.00 66.04 C
ANISOU 328 C ILE A 38 10179 6615 8298 -1130 4506 304 C
ATOM 329 O ILE A 38 489.640 202.185 552.945 1.00 71.70 O
ANISOU 329 O ILE A 38 10866 7440 8937 -1040 4388 460 O
ATOM 330 CB ILE A 38 489.667 199.374 551.128 1.00 72.56 C
ANISOU 330 CB ILE A 38 11374 6995 9199 -976 4659 393 C
ATOM 331 CG1 ILE A 38 489.949 197.902 551.425 1.00 78.74 C
ANISOU 331 CG1 ILE A 38 12471 7436 10011 -988 4728 507 C
ATOM 332 CG2 ILE A 38 490.985 200.102 550.943 1.00 58.82 C
ANISOU 332 CG2 ILE A 38 9532 5407 7410 -678 4513 578 C
ATOM 333 CD1 ILE A 38 490.896 197.692 552.585 1.00 93.67 C
ANISOU 333 CD1 ILE A 38 14538 9254 11798 -918 4708 831 C
ATOM 334 N CYS A 39 488.095 202.124 551.308 1.00 70.41 N
ANISOU 334 N CYS A 39 10511 7305 8936 -1161 4496 81 N
ATOM 335 CA CYS A 39 488.003 203.579 551.228 1.00 61.76 C
ANISOU 335 CA CYS A 39 9137 6465 7862 -1093 4340 26 C
ATOM 336 C CYS A 39 487.553 204.167 552.558 1.00 68.89 C
ANISOU 336 C CYS A 39 10016 7459 8701 -1236 4287 18 C
ATOM 337 O CYS A 39 488.109 205.164 553.032 1.00 63.44 O
ANISOU 337 O CYS A 39 9228 6898 7978 -1153 4178 97 O
ATOM 338 CB CYS A 39 487.032 203.988 550.116 1.00 62.87 C
ANISOU 338 CB CYS A 39 9056 6728 8104 -1123 4329 -207 C
ATOM 339 SG CYS A 39 487.587 203.661 548.418 1.00 69.29 S
ANISOU 339 SG CYS A 39 9815 7554 8959 -902 4358 -230 S
ATOM 340 N THR A 40 486.532 203.562 553.168 1.00 67.88 N
ANISOU 340 N THR A 40 9971 7270 8551 -1458 4380 -83 N
ATOM 341 CA THR A 40 486.036 204.044 554.452 1.00 66.35 C
ANISOU 341 CA THR A 40 9754 7185 8269 -1587 4359 -99 C
ATOM 342 C THR A 40 487.142 204.045 555.499 1.00 59.65 C
ANISOU 342 C THR A 40 9054 6329 7280 -1516 4315 131 C
ATOM 343 O THR A 40 487.400 205.067 556.148 1.00 59.44 O
ANISOU 343 O THR A 40 8931 6460 7195 -1485 4238 142 O
ATOM 344 CB THR A 40 484.868 203.177 554.920 1.00 69.23 C
ANISOU 344 CB THR A 40 10204 7477 8624 -1826 4483 -196 C
ATOM 345 OG1 THR A 40 483.727 203.414 554.087 1.00 73.64 O
ANISOU 345 OG1 THR A 40 10575 8101 9303 -1911 4503 -431 O
ATOM 346 CG2 THR A 40 484.513 203.516 556.348 1.00 69.80 C
ANISOU 346 CG2 THR A 40 10287 7670 8565 -1939 4485 -168 C
ATOM 347 N HIS A 41 487.811 202.901 555.669 1.00 61.32 N
ANISOU 347 N HIS A 41 9504 6355 7442 -1488 4370 316 N
ATOM 348 CA HIS A 41 488.840 202.780 556.695 1.00 70.55 C
ANISOU 348 CA HIS A 41 10819 7523 8465 -1422 4318 558 C
ATOM 349 C HIS A 41 490.042 203.661 556.383 1.00 69.83 C
ANISOU 349 C HIS A 41 10630 7526 8376 -1207 4196 668 C
ATOM 350 O HIS A 41 490.677 204.191 557.302 1.00 73.87 O
ANISOU 350 O HIS A 41 11153 8146 8768 -1184 4125 787 O
ATOM 351 CB HIS A 41 489.244 201.312 556.829 1.00 64.75 C
ANISOU 351 CB HIS A 41 10353 6543 7707 -1420 4395 741 C
ATOM 352 CG HIS A 41 490.516 201.082 557.588 1.00 75.20 C
ANISOU 352 CG HIS A 41 11821 7847 8904 -1286 4317 1027 C
ATOM 353 ND1 HIS A 41 491.761 201.218 557.014 1.00 72.34 N
ANISOU 353 ND1 HIS A 41 11460 7457 8570 -1045 4239 1176 N
ATOM 354 CD2 HIS A 41 490.734 200.680 558.865 1.00 74.26 C
ANISOU 354 CD2 HIS A 41 11842 7748 8625 -1353 4304 1206 C
ATOM 355 CE1 HIS A 41 492.690 200.934 557.908 1.00 74.10 C
ANISOU 355 CE1 HIS A 41 11811 7679 8663 -970 4168 1426 C
ATOM 356 NE2 HIS A 41 492.094 200.603 559.040 1.00 76.69 N
ANISOU 356 NE2 HIS A 41 12230 8039 8870 -1156 4205 1449 N
ATOM 357 N LEU A 42 490.357 203.846 555.102 1.00 63.48 N
ANISOU 357 N LEU A 42 9721 6698 7701 -1057 4177 634 N
ATOM 358 CA LEU A 42 491.414 204.784 554.735 1.00 62.33 C
ANISOU 358 CA LEU A 42 9437 6665 7581 -861 4062 742 C
ATOM 359 C LEU A 42 491.061 206.202 555.173 1.00 65.75 C
ANISOU 359 C LEU A 42 9664 7293 8024 -926 3990 621 C
ATOM 360 O LEU A 42 491.875 206.897 555.795 1.00 62.04 O
ANISOU 360 O LEU A 42 9169 6907 7495 -875 3918 741 O
ATOM 361 CB LEU A 42 491.660 204.728 553.228 1.00 70.41 C
ANISOU 361 CB LEU A 42 10357 7662 8732 -693 4070 717 C
ATOM 362 CG LEU A 42 492.982 204.099 552.787 1.00 83.33 C
ANISOU 362 CG LEU A 42 12105 9203 10353 -461 4066 956 C
ATOM 363 CD1 LEU A 42 493.164 204.278 551.293 1.00 85.06 C
ANISOU 363 CD1 LEU A 42 12170 9473 10674 -284 4077 910 C
ATOM 364 CD2 LEU A 42 494.158 204.701 553.547 1.00 83.30 C
ANISOU 364 CD2 LEU A 42 12080 9291 10279 -357 3942 1183 C
ATOM 365 N GLU A 43 489.838 206.648 554.866 1.00 58.41 N
ANISOU 365 N GLU A 43 8589 6429 7176 -1040 4016 382 N
ATOM 366 CA GLU A 43 489.430 207.994 555.254 1.00 59.50 C
ANISOU 366 CA GLU A 43 8537 6724 7347 -1089 3965 251 C
ATOM 367 C GLU A 43 489.439 208.158 556.768 1.00 66.28 C
ANISOU 367 C GLU A 43 9504 7641 8039 -1213 3993 270 C
ATOM 368 O GLU A 43 489.788 209.227 557.282 1.00 56.51 O
ANISOU 368 O GLU A 43 8177 6507 6787 -1205 3956 253 O
ATOM 369 CB GLU A 43 488.042 208.319 554.696 1.00 58.13 C
ANISOU 369 CB GLU A 43 8198 6604 7285 -1178 3987 2 C
ATOM 370 CG GLU A 43 487.692 209.804 554.792 1.00 65.63 C
ANISOU 370 CG GLU A 43 8921 7691 8325 -1171 3928 -129 C
ATOM 371 CD GLU A 43 486.348 210.149 554.178 1.00 74.32 C
ANISOU 371 CD GLU A 43 9844 8851 9542 -1229 3930 -347 C
ATOM 372 OE1 GLU A 43 485.624 209.220 553.768 1.00 82.06 O
ANISOU 372 OE1 GLU A 43 10879 9781 10520 -1306 3986 -412 O
ATOM 373 OE2 GLU A 43 486.008 211.352 554.118 1.00 79.45 O
ANISOU 373 OE2 GLU A 43 10300 9592 10296 -1201 3882 -453 O
ATOM 374 N VAL A 44 489.061 207.108 557.499 1.00 63.63 N
ANISOU 374 N VAL A 44 9360 7243 7575 -1335 4071 307 N
ATOM 375 CA VAL A 44 489.075 207.180 558.958 1.00 59.65 C
ANISOU 375 CA VAL A 44 8964 6827 6873 -1447 4103 347 C
ATOM 376 C VAL A 44 490.505 207.297 559.472 1.00 58.00 C
ANISOU 376 C VAL A 44 8859 6633 6547 -1340 4033 582 C
ATOM 377 O VAL A 44 490.784 208.068 560.400 1.00 61.98 O
ANISOU 377 O VAL A 44 9357 7270 6924 -1384 4024 571 O
ATOM 378 CB VAL A 44 488.351 205.961 559.560 1.00 59.60 C
ANISOU 378 CB VAL A 44 9127 6751 6766 -1597 4202 374 C
ATOM 379 CG1 VAL A 44 488.618 205.861 561.052 1.00 64.30 C
ANISOU 379 CG1 VAL A 44 9862 7450 7121 -1680 4225 493 C
ATOM 380 CG2 VAL A 44 486.856 206.048 559.299 1.00 59.89 C
ANISOU 380 CG2 VAL A 44 9035 6823 6896 -1734 4275 130 C
ATOM 381 N CYS A 45 491.434 206.545 558.875 1.00 59.75 N
ANISOU 381 N CYS A 45 9177 6723 6804 -1195 3990 790 N
ATOM 382 CA CYS A 45 492.833 206.639 559.281 1.00 65.84 C
ANISOU 382 CA CYS A 45 10025 7512 7478 -1070 3906 1039 C
ATOM 383 C CYS A 45 493.375 208.045 559.051 1.00 71.06 C
ANISOU 383 C CYS A 45 10494 8287 8219 -1002 3841 1003 C
ATOM 384 O CYS A 45 494.119 208.577 559.884 1.00 61.52 O
ANISOU 384 O CYS A 45 9306 7175 6893 -997 3764 1095 O
ATOM 385 CB CYS A 45 493.673 205.603 558.526 1.00 66.63 C
ANISOU 385 CB CYS A 45 10231 7447 7637 -893 3875 1250 C
ATOM 386 SG CYS A 45 493.517 203.898 559.156 1.00 70.77 S
ANISOU 386 SG CYS A 45 11044 7799 8046 -955 3945 1401 S
ATOM 387 N PHE A 46 492.993 208.671 557.934 1.00 59.10 N
ANISOU 387 N PHE A 46 8772 6768 6914 -947 3831 862 N
ATOM 388 CA PHE A 46 493.471 210.018 557.642 1.00 61.87 C
ANISOU 388 CA PHE A 46 8900 7208 7399 -870 3716 830 C
ATOM 389 C PHE A 46 492.882 211.037 558.611 1.00 65.25 C
ANISOU 389 C PHE A 46 9261 7751 7781 -1017 3713 617 C
ATOM 390 O PHE A 46 493.602 211.907 559.116 1.00 59.22 O
ANISOU 390 O PHE A 46 8421 7059 7021 -983 3552 635 O
ATOM 391 CB PHE A 46 493.131 210.398 556.200 1.00 53.87 C
ANISOU 391 CB PHE A 46 7680 6173 6615 -774 3714 753 C
ATOM 392 CG PHE A 46 493.903 209.623 555.167 1.00 62.55 C
ANISOU 392 CG PHE A 46 8803 7199 7764 -585 3683 947 C
ATOM 393 CD1 PHE A 46 494.953 208.798 555.535 1.00 69.60 C
ANISOU 393 CD1 PHE A 46 9865 8038 8540 -487 3635 1185 C
ATOM 394 CD2 PHE A 46 493.571 209.717 553.826 1.00 76.02 C
ANISOU 394 CD2 PHE A 46 10354 8907 9622 -491 3690 885 C
ATOM 395 CE1 PHE A 46 495.662 208.086 554.584 1.00 88.50 C
ANISOU 395 CE1 PHE A 46 12275 10368 10982 -292 3617 1344 C
ATOM 396 CE2 PHE A 46 494.274 209.005 552.873 1.00 79.65 C
ANISOU 396 CE2 PHE A 46 10837 9324 10105 -306 3675 1039 C
ATOM 397 CZ PHE A 46 495.322 208.189 553.252 1.00 80.42 C
ANISOU 397 CZ PHE A 46 11104 9355 10098 -201 3645 1261 C
ATOM 398 N MET A 47 491.573 210.965 558.867 1.00 60.66 N
ANISOU 398 N MET A 47 8694 7191 7163 -1180 3889 399 N
ATOM 399 CA MET A 47 490.970 211.876 559.836 1.00 77.42 C
ANISOU 399 CA MET A 47 10760 9435 9221 -1305 3911 174 C
ATOM 400 C MET A 47 491.602 211.709 561.212 1.00 65.20 C
ANISOU 400 C MET A 47 9389 7976 7408 -1359 3861 265 C
ATOM 401 O MET A 47 491.941 212.700 561.870 1.00 61.58 O
ANISOU 401 O MET A 47 8857 7614 6927 -1362 3736 163 O
ATOM 402 CB MET A 47 489.459 211.657 559.909 1.00 69.39 C
ANISOU 402 CB MET A 47 9713 8448 8203 -1434 4037 -53 C
ATOM 403 CG MET A 47 488.733 211.857 558.585 1.00 64.18 C
ANISOU 403 CG MET A 47 8859 7734 7795 -1365 4000 -163 C
ATOM 404 SD MET A 47 486.998 211.371 558.687 1.00 73.58 S
ANISOU 404 SD MET A 47 10023 8957 8978 -1503 4075 -380 S
ATOM 405 CE MET A 47 486.263 212.887 559.298 1.00 86.72 C
ANISOU 405 CE MET A 47 11497 10754 10698 -1555 4112 -663 C
ATOM 406 N TYR A 48 491.777 210.459 561.655 1.00 72.56 N
ANISOU 406 N TYR A 48 10555 8874 8141 -1401 3948 459 N
ATOM 407 CA TYR A 48 492.444 210.181 562.925 1.00 68.77 C
ANISOU 407 CA TYR A 48 10252 8495 7383 -1435 3891 598 C
ATOM 408 C TYR A 48 493.798 210.878 563.005 1.00 68.58 C
ANISOU 408 C TYR A 48 10147 8513 7397 -1292 3629 714 C
ATOM 409 O TYR A 48 494.104 211.559 563.990 1.00 71.96 O
ANISOU 409 O TYR A 48 10571 9088 7684 -1337 3525 634 O
ATOM 410 CB TYR A 48 492.608 208.671 563.094 1.00 64.64 C
ANISOU 410 CB TYR A 48 9967 7874 6718 -1444 3978 858 C
ATOM 411 CG TYR A 48 492.695 208.170 564.525 1.00 75.69 C
ANISOU 411 CG TYR A 48 11564 9402 7793 -1544 4003 969 C
ATOM 412 CD1 TYR A 48 493.871 208.290 565.253 1.00 72.16 C
ANISOU 412 CD1 TYR A 48 11202 9052 7165 -1472 3855 1158 C
ATOM 413 CD2 TYR A 48 491.616 207.537 565.128 1.00 70.47 C
ANISOU 413 CD2 TYR A 48 10956 8784 7034 -1678 4098 896 C
ATOM 414 CE1 TYR A 48 493.965 207.812 566.549 1.00 75.91 C
ANISOU 414 CE1 TYR A 48 11867 9670 7307 -1562 3890 1284 C
ATOM 415 CE2 TYR A 48 491.701 207.057 566.427 1.00 79.92 C
ANISOU 415 CE2 TYR A 48 12317 10120 7927 -1759 4122 1029 C
ATOM 416 CZ TYR A 48 492.879 207.199 567.132 1.00 79.44 C
ANISOU 416 CZ TYR A 48 12381 10163 7638 -1705 4034 1225 C
ATOM 417 OH TYR A 48 492.974 206.724 568.423 1.00 72.52 O
ANISOU 417 OH TYR A 48 11662 9456 6436 -1776 4044 1372 O
ATOM 418 N SER A 49 494.620 210.726 561.963 1.00 58.35 N
ANISOU 418 N SER A 49 8774 7105 6292 -1121 3519 893 N
ATOM 419 CA SER A 49 495.943 211.343 561.944 1.00 75.37 C
ANISOU 419 CA SER A 49 10824 9302 8510 -988 3273 1033 C
ATOM 420 C SER A 49 495.883 212.863 561.982 1.00 68.12 C
ANISOU 420 C SER A 49 9683 8448 7750 -1016 3144 806 C
ATOM 421 O SER A 49 496.859 213.504 562.388 1.00 69.57 O
ANISOU 421 O SER A 49 9796 8699 7937 -975 2936 865 O
ATOM 422 CB SER A 49 496.711 210.900 560.698 1.00 70.35 C
ANISOU 422 CB SER A 49 10119 8550 8061 -795 3216 1255 C
ATOM 423 OG SER A 49 498.051 211.344 560.760 1.00 85.37 O
ANISOU 423 OG SER A 49 11924 10510 10002 -673 2990 1435 O
ATOM 424 N ASP A 50 494.771 213.454 561.551 1.00 62.90 N
ANISOU 424 N ASP A 50 8902 7757 7238 -1082 3256 550 N
ATOM 425 CA ASP A 50 494.607 214.899 561.582 1.00 73.05 C
ANISOU 425 CA ASP A 50 9983 9067 8706 -1103 3147 321 C
ATOM 426 C ASP A 50 494.096 215.406 562.926 1.00 75.12 C
ANISOU 426 C ASP A 50 10313 9458 8771 -1246 3172 66 C
ATOM 427 O ASP A 50 494.051 216.623 563.135 1.00 72.99 O
ANISOU 427 O ASP A 50 9896 9198 8637 -1262 3063 -147 O
ATOM 428 CB ASP A 50 493.653 215.325 560.461 1.00 78.73 C
ANISOU 428 CB ASP A 50 10526 9700 9687 -1081 3247 176 C
ATOM 429 CG ASP A 50 493.682 216.816 560.199 1.00 90.66 C
ANISOU 429 CG ASP A 50 11799 11181 11469 -1053 3107 17 C
ATOM 430 OD1 ASP A 50 494.754 217.437 560.367 1.00 95.83 O
ANISOU 430 OD1 ASP A 50 12381 11832 12201 -1004 2896 114 O
ATOM 431 OD2 ASP A 50 492.623 217.366 559.833 1.00 94.93 O
ANISOU 431 OD2 ASP A 50 12217 11695 12158 -1082 3204 -200 O
ATOM 432 N GLY A 51 493.728 214.508 563.844 1.00 75.97 N
ANISOU 432 N GLY A 51 10640 9664 8561 -1346 3313 87 N
ATOM 433 CA GLY A 51 493.109 214.936 565.086 1.00 81.99 C
ANISOU 433 CA GLY A 51 11463 10587 9101 -1479 3376 -169 C
ATOM 434 C GLY A 51 494.074 215.450 566.133 1.00 89.10 C
ANISOU 434 C GLY A 51 12404 11621 9828 -1484 3165 -175 C
ATOM 435 O GLY A 51 493.706 216.303 566.946 1.00 90.16 O
ANISOU 435 O GLY A 51 12504 11870 9881 -1558 3144 -468 O
ATOM 436 N GLY A 52 495.303 214.948 566.142 1.00 95.58 N
ANISOU 436 N GLY A 52 13290 12440 10585 -1402 3004 128 N
ATOM 437 CA GLY A 52 496.298 215.357 567.110 1.00 96.09 C
ANISOU 437 CA GLY A 52 13383 12650 10476 -1407 2779 149 C
ATOM 438 C GLY A 52 497.080 216.571 566.657 1.00 96.34 C
ANISOU 438 C GLY A 52 13188 12605 10812 -1345 2526 79 C
ATOM 439 O GLY A 52 496.667 217.320 565.768 1.00 89.90 O
ANISOU 439 O GLY A 52 12189 11642 10327 -1316 2537 -54 O
ATOM 440 N SER A 53 498.235 216.765 567.287 1.00100.92 N
ANISOU 440 N SER A 53 13772 13290 11282 -1330 2286 185 N
ATOM 441 CA SER A 53 499.132 217.842 566.900 1.00100.77 C
ANISOU 441 CA SER A 53 13534 13198 11556 -1288 2024 167 C
ATOM 442 C SER A 53 499.772 217.530 565.547 1.00 93.48 C
ANISOU 442 C SER A 53 12480 12117 10920 -1146 1990 482 C
ATOM 443 O SER A 53 499.547 216.475 564.946 1.00 95.01 O
ANISOU 443 O SER A 53 12766 12259 11074 -1072 2158 687 O
ATOM 444 CB SER A 53 500.191 218.065 567.977 1.00 99.68 C
ANISOU 444 CB SER A 53 13430 13241 11204 -1325 1770 195 C
ATOM 445 OG SER A 53 500.606 216.834 568.542 1.00102.61 O
ANISOU 445 OG SER A 53 14001 13759 11225 -1294 1806 474 O
ATOM 446 N LYS A 73 500.601 218.466 565.076 1.00 96.16 N
ANISOU 446 N LYS A 73 12597 12385 11552 -1110 1768 518 N
ATOM 447 CA LYS A 73 501.118 218.402 563.710 1.00 96.42 C
ANISOU 447 CA LYS A 73 12460 12286 11889 -976 1746 781 C
ATOM 448 C LYS A 73 501.991 217.169 563.491 1.00 88.91 C
ANISOU 448 C LYS A 73 11600 11397 10787 -848 1746 1162 C
ATOM 449 O LYS A 73 501.784 216.409 562.538 1.00 81.64 O
ANISOU 449 O LYS A 73 10698 10393 9927 -737 1900 1329 O
ATOM 450 CB LYS A 73 501.899 219.678 563.391 1.00101.83 C
ANISOU 450 CB LYS A 73 12883 12902 12905 -986 1498 768 C
ATOM 451 N HIS A 74 502.980 216.959 564.359 1.00 97.93 N
ANISOU 451 N HIS A 74 12794 12684 11731 -851 1566 1295 N
ATOM 452 CA HIS A 74 503.944 215.878 564.201 1.00102.74 C
ANISOU 452 CA HIS A 74 13462 13352 12221 -707 1533 1669 C
ATOM 453 C HIS A 74 503.606 214.658 565.051 1.00 94.73 C
ANISOU 453 C HIS A 74 12743 12426 10825 -717 1670 1742 C
ATOM 454 O HIS A 74 504.505 213.878 565.385 1.00 97.24 O
ANISOU 454 O HIS A 74 13134 12833 10979 -621 1585 2024 O
ATOM 455 CB HIS A 74 505.352 216.374 564.541 1.00115.32 C
ANISOU 455 CB HIS A 74 14894 15060 13862 -686 1230 1826 C
ATOM 456 CG HIS A 74 505.836 217.487 563.663 1.00127.29 C
ANISOU 456 CG HIS A 74 16106 16483 15776 -677 1088 1831 C
ATOM 457 ND1 HIS A 74 505.347 217.702 562.392 1.00127.55 N
ANISOU 457 ND1 HIS A 74 16016 16358 16090 -610 1225 1843 N
ATOM 458 CD2 HIS A 74 506.772 218.444 563.872 1.00130.34 C
ANISOU 458 CD2 HIS A 74 16280 16916 16328 -734 816 1842 C
ATOM 459 CE1 HIS A 74 505.958 218.745 561.858 1.00128.14 C
ANISOU 459 CE1 HIS A 74 15819 16384 16484 -622 1054 1884 C
ATOM 460 NE2 HIS A 74 506.827 219.213 562.735 1.00129.85 N
ANISOU 460 NE2 HIS A 74 15975 16709 16653 -704 805 1881 N
ATOM 461 N ARG A 75 502.332 214.469 565.401 1.00 85.38 N
ANISOU 461 N ARG A 75 11717 11218 9504 -827 1884 1513 N
ATOM 462 CA ARG A 75 501.990 213.444 566.382 1.00 74.32 C
ANISOU 462 CA ARG A 75 10588 9922 7727 -874 2005 1577 C
ATOM 463 C ARG A 75 501.972 212.047 565.770 1.00 74.94 C
ANISOU 463 C ARG A 75 10812 9882 7780 -749 2175 1864 C
ATOM 464 O ARG A 75 502.531 211.105 566.343 1.00 85.89 O
ANISOU 464 O ARG A 75 12359 11335 8938 -689 2152 2120 O
ATOM 465 CB ARG A 75 500.636 213.753 567.022 1.00 78.93 C
ANISOU 465 CB ARG A 75 11272 10548 8169 -1046 2182 1236 C
ATOM 466 CG ARG A 75 500.032 212.563 567.750 1.00 83.53 C
ANISOU 466 CG ARG A 75 12128 11199 8412 -1100 2386 1333 C
ATOM 467 CD ARG A 75 499.187 212.987 568.938 1.00 88.41 C
ANISOU 467 CD ARG A 75 12838 12000 8754 -1273 2461 1039 C
ATOM 468 NE ARG A 75 498.991 211.890 569.882 1.00 87.65 N
ANISOU 468 NE ARG A 75 12995 12037 8272 -1322 2585 1216 N
ATOM 469 CZ ARG A 75 498.145 211.932 570.907 1.00 96.52 C
ANISOU 469 CZ ARG A 75 14237 13342 9094 -1468 2719 1027 C
ATOM 470 NH1 ARG A 75 497.418 213.019 571.124 1.00 92.51 N
ANISOU 470 NH1 ARG A 75 13618 12898 8633 -1564 2746 626 N
ATOM 471 NH2 ARG A 75 498.024 210.891 571.717 1.00 77.48 N
ANISOU 471 NH2 ARG A 75 12049 11050 6338 -1509 2833 1245 N
ATOM 472 N PHE A 76 501.339 211.890 564.611 1.00 72.76 N
ANISOU 472 N PHE A 76 10482 9426 7738 -704 2339 1821 N
ATOM 473 CA PHE A 76 501.048 210.576 564.060 1.00 75.46 C
ANISOU 473 CA PHE A 76 10985 9630 8055 -620 2532 2003 C
ATOM 474 C PHE A 76 501.885 210.286 562.822 1.00 79.76 C
ANISOU 474 C PHE A 76 11402 10067 8837 -409 2477 2226 C
ATOM 475 O PHE A 76 502.043 211.141 561.948 1.00 67.15 O
ANISOU 475 O PHE A 76 9573 8443 7499 -363 2408 2154 O
ATOM 476 CB PHE A 76 499.565 210.451 563.712 1.00 69.48 C
ANISOU 476 CB PHE A 76 10286 8770 7344 -741 2784 1764 C
ATOM 477 CG PHE A 76 498.670 210.420 564.913 1.00 72.17 C
ANISOU 477 CG PHE A 76 10783 9223 7414 -933 2898 1590 C
ATOM 478 CD1 PHE A 76 498.635 209.304 565.732 1.00 72.22 C
ANISOU 478 CD1 PHE A 76 11039 9264 7138 -969 2991 1776 C
ATOM 479 CD2 PHE A 76 497.867 211.504 565.225 1.00 65.85 C
ANISOU 479 CD2 PHE A 76 9877 8499 6643 -1069 2920 1251 C
ATOM 480 CE1 PHE A 76 497.814 209.268 566.843 1.00 79.83 C
ANISOU 480 CE1 PHE A 76 12137 10366 7829 -1147 3112 1638 C
ATOM 481 CE2 PHE A 76 497.040 211.473 566.334 1.00 75.70 C
ANISOU 481 CE2 PHE A 76 11258 9884 7622 -1233 3042 1083 C
ATOM 482 CZ PHE A 76 497.015 210.353 567.145 1.00 71.80 C
ANISOU 482 CZ PHE A 76 11005 9453 6823 -1277 3142 1283 C
ATOM 483 N GLU A 77 502.414 209.069 562.762 1.00 85.44 N
ANISOU 483 N GLU A 77 12272 10726 9464 -273 2516 2503 N
ATOM 484 CA GLU A 77 502.982 208.505 561.547 1.00 78.89 C
ANISOU 484 CA GLU A 77 11375 9776 8825 -57 2536 2688 C
ATOM 485 C GLU A 77 501.953 207.564 560.934 1.00 83.30 C
ANISOU 485 C GLU A 77 12096 10143 9410 -71 2787 2615 C
ATOM 486 O GLU A 77 501.383 206.722 561.637 1.00 80.60 O
ANISOU 486 O GLU A 77 11994 9744 8885 -165 2916 2633 O
ATOM 487 CB GLU A 77 504.283 207.759 561.845 1.00 74.89 C
ANISOU 487 CB GLU A 77 10918 9312 8224 130 2409 3032 C
ATOM 488 CG GLU A 77 505.064 207.366 560.610 1.00 77.25 C
ANISOU 488 CG GLU A 77 11094 9535 8724 382 2400 3216 C
ATOM 489 CD GLU A 77 505.894 208.510 560.069 1.00 79.47 C
ANISOU 489 CD GLU A 77 11051 9945 9198 444 2214 3240 C
ATOM 490 OE1 GLU A 77 506.968 208.791 560.644 1.00 76.62 O
ANISOU 490 OE1 GLU A 77 10593 9732 8788 492 2008 3414 O
ATOM 491 OE2 GLU A 77 505.464 209.132 559.075 1.00 73.99 O
ANISOU 491 OE2 GLU A 77 10194 9211 8708 437 2269 3096 O
ATOM 492 N ILE A 78 501.703 207.717 559.639 1.00 64.36 N
ANISOU 492 N ILE A 78 9560 7658 7237 12 2853 2535 N
ATOM 493 CA ILE A 78 500.663 206.967 558.942 1.00 72.54 C
ANISOU 493 CA ILE A 78 10712 8526 8324 -18 3071 2412 C
ATOM 494 C ILE A 78 501.305 205.768 558.257 1.00 73.51 C
ANISOU 494 C ILE A 78 10936 8512 8483 204 3113 2627 C
ATOM 495 O ILE A 78 502.181 205.929 557.400 1.00 76.00 O
ANISOU 495 O ILE A 78 11086 8863 8929 410 3025 2747 O
ATOM 496 CB ILE A 78 499.920 207.852 557.929 1.00 74.10 C
ANISOU 496 CB ILE A 78 10699 8731 8726 -60 3115 2173 C
ATOM 497 CG1 ILE A 78 499.239 209.022 558.642 1.00 70.21 C
ANISOU 497 CG1 ILE A 78 10115 8345 8217 -265 3082 1941 C
ATOM 498 CG2 ILE A 78 498.898 207.033 557.157 1.00 80.84 C
ANISOU 498 CG2 ILE A 78 11656 9431 9628 -86 3320 2045 C
ATOM 499 CD1 ILE A 78 499.197 210.304 557.825 1.00 70.20 C
ANISOU 499 CD1 ILE A 78 9825 8399 8449 -242 2996 1819 C
ATOM 500 N ILE A 79 500.867 204.568 558.627 1.00 68.67 N
ANISOU 500 N ILE A 79 10588 7739 7763 165 3254 2679 N
ATOM 501 CA ILE A 79 501.375 203.334 558.041 1.00 73.39 C
ANISOU 501 CA ILE A 79 11306 8166 8414 371 3287 2835 C
ATOM 502 C ILE A 79 500.437 202.795 556.968 1.00 75.24 C
ANISOU 502 C ILE A 79 11577 8229 8783 356 3449 2628 C
ATOM 503 O ILE A 79 500.892 202.300 555.936 1.00 76.10 O
ANISOU 503 O ILE A 79 11663 8249 9001 569 3477 2682 O
ATOM 504 CB ILE A 79 501.620 202.279 559.142 1.00 76.60 C
ANISOU 504 CB ILE A 79 11948 8495 8661 354 3256 3008 C
ATOM 505 CG1 ILE A 79 502.380 202.892 560.322 1.00 83.31 C
ANISOU 505 CG1 ILE A 79 12771 9552 9329 327 3103 3187 C
ATOM 506 CG2 ILE A 79 502.367 201.076 558.579 1.00 67.24 C
ANISOU 506 CG2 ILE A 79 10854 7133 7560 608 3246 3177 C
ATOM 507 CD1 ILE A 79 503.758 203.410 559.966 1.00 78.41 C
ANISOU 507 CD1 ILE A 79 11956 9063 8771 557 2934 3391 C
ATOM 508 N GLU A 80 499.130 202.870 557.205 1.00 69.44 N
ANISOU 508 N GLU A 80 10895 7460 8030 109 3563 2392 N
ATOM 509 CA GLU A 80 498.157 202.423 556.220 1.00 73.76 C
ANISOU 509 CA GLU A 80 11462 7865 8699 64 3712 2180 C
ATOM 510 C GLU A 80 498.187 203.345 555.008 1.00 70.31 C
ANISOU 510 C GLU A 80 10776 7539 8399 162 3707 2074 C
ATOM 511 O GLU A 80 498.533 204.524 555.107 1.00 65.35 O
ANISOU 511 O GLU A 80 9940 7100 7791 165 3589 2078 O
ATOM 512 CB GLU A 80 496.751 202.388 556.833 1.00 73.47 C
ANISOU 512 CB GLU A 80 11492 7811 8613 -231 3809 1958 C
ATOM 513 CG GLU A 80 495.654 201.855 555.909 1.00 80.94 C
ANISOU 513 CG GLU A 80 12463 8610 9680 -313 3960 1735 C
ATOM 514 CD GLU A 80 495.523 200.342 555.963 1.00 91.11 C
ANISOU 514 CD GLU A 80 14015 9627 10977 -317 4063 1812 C
ATOM 515 OE1 GLU A 80 494.403 199.825 555.762 1.00 96.63 O
ANISOU 515 OE1 GLU A 80 14783 10202 11731 -496 4192 1632 O
ATOM 516 OE2 GLU A 80 496.543 199.668 556.213 1.00 97.42 O
ANISOU 516 OE2 GLU A 80 14946 10327 11742 -142 4010 2057 O
ATOM 517 N GLY A 81 497.837 202.791 553.851 1.00 66.86 N
ANISOU 517 N GLY A 81 10341 6994 8066 245 3798 1961 N
ATOM 518 CA GLY A 81 497.881 203.534 552.613 1.00 66.15 C
ANISOU 518 CA GLY A 81 9998 7041 8097 364 3753 1855 C
ATOM 519 C GLY A 81 499.215 203.511 551.903 1.00 75.23 C
ANISOU 519 C GLY A 81 11035 8260 9287 670 3650 2054 C
ATOM 520 O GLY A 81 499.341 204.133 550.842 1.00 76.85 O
ANISOU 520 O GLY A 81 11017 8605 9578 786 3615 2005 O
ATOM 521 N ARG A 82 500.213 202.824 552.446 1.00 73.55 N
ANISOU 521 N ARG A 82 10958 7975 9013 812 3604 2292 N
ATOM 522 CA ARG A 82 501.503 202.689 551.788 1.00 75.18 C
ANISOU 522 CA ARG A 82 11055 8253 9258 1122 3522 2489 C
ATOM 523 C ARG A 82 501.638 201.320 551.137 1.00 83.72 C
ANISOU 523 C ARG A 82 12322 9128 10358 1308 3626 2481 C
ATOM 524 O ARG A 82 500.899 200.379 551.440 1.00 81.87 O
ANISOU 524 O ARG A 82 12339 8659 10110 1188 3740 2381 O
ATOM 525 CB ARG A 82 502.657 202.889 552.773 1.00 71.84 C
ANISOU 525 CB ARG A 82 10617 7912 8767 1195 3379 2772 C
ATOM 526 CG ARG A 82 502.589 204.139 553.625 1.00 68.97 C
ANISOU 526 CG ARG A 82 10112 7720 8372 1000 3260 2770 C
ATOM 527 CD ARG A 82 503.888 204.288 554.398 1.00 71.89 C
ANISOU 527 CD ARG A 82 10435 8198 8682 1112 3094 3052 C
ATOM 528 NE ARG A 82 503.936 205.514 555.187 1.00 76.80 N
ANISOU 528 NE ARG A 82 10911 8987 9282 937 2956 3033 N
ATOM 529 CZ ARG A 82 504.782 206.511 554.958 1.00 79.65 C
ANISOU 529 CZ ARG A 82 11001 9529 9735 1006 2797 3136 C
ATOM 530 NH1 ARG A 82 505.639 206.437 553.949 1.00 73.23 N
ANISOU 530 NH1 ARG A 82 10017 8783 9024 1250 2771 3285 N
ATOM 531 NH2 ARG A 82 504.762 207.587 555.729 1.00 89.32 N
ANISOU 531 NH2 ARG A 82 12118 10867 10952 829 2669 3084 N
ATOM 532 N ASP A 83 502.602 201.228 550.224 1.00 85.96 N
ANISOU 532 N ASP A 83 12473 9503 10685 1606 3588 2584 N
ATOM 533 CA ASP A 83 503.049 199.938 549.727 1.00 84.67 C
ANISOU 533 CA ASP A 83 12480 9152 10539 1847 3661 2616 C
ATOM 534 C ASP A 83 503.544 199.087 550.890 1.00 83.11 C
ANISOU 534 C ASP A 83 12524 8760 10293 1867 3644 2834 C
ATOM 535 O ASP A 83 504.117 199.596 551.856 1.00 91.76 O
ANISOU 535 O ASP A 83 13568 9972 11326 1823 3529 3044 O
ATOM 536 CB ASP A 83 504.155 200.135 548.685 1.00 96.86 C
ANISOU 536 CB ASP A 83 13798 10891 12113 2183 3614 2728 C
ATOM 537 CG ASP A 83 504.975 198.886 548.456 1.00116.77 C
ANISOU 537 CG ASP A 83 16476 13244 14646 2487 3657 2836 C
ATOM 538 OD1 ASP A 83 504.666 198.134 547.507 1.00126.04 O
ANISOU 538 OD1 ASP A 83 17737 14300 15850 2613 3763 2640 O
ATOM 539 OD2 ASP A 83 505.932 198.658 549.226 1.00128.02 O
ANISOU 539 OD2 ASP A 83 17934 14657 16052 2606 3578 3107 O
ATOM 540 N ARG A 84 503.305 197.775 550.793 1.00 83.75 N
ANISOU 540 N ARG A 84 12873 8539 10408 1929 3752 2782 N
ATOM 541 CA ARG A 84 503.601 196.879 551.906 1.00 86.21 C
ANISOU 541 CA ARG A 84 13446 8626 10686 1924 3752 2996 C
ATOM 542 C ARG A 84 505.065 196.939 552.322 1.00 95.02 C
ANISOU 542 C ARG A 84 14470 9869 11765 2188 3618 3331 C
ATOM 543 O ARG A 84 505.373 196.802 553.511 1.00100.98 O
ANISOU 543 O ARG A 84 15308 10620 12442 2110 3527 3518 O
ATOM 544 CB ARG A 84 503.215 195.443 551.543 1.00 92.72 C
ANISOU 544 CB ARG A 84 14553 9074 11601 1991 3885 2891 C
ATOM 545 N ILE A 85 505.979 197.143 551.372 1.00 89.95 N
ANISOU 545 N ILE A 85 13616 9389 11171 2487 3576 3376 N
ATOM 546 CA ILE A 85 507.403 197.116 551.700 1.00 91.25 C
ANISOU 546 CA ILE A 85 13675 9679 11318 2758 3455 3698 C
ATOM 547 C ILE A 85 507.807 198.393 552.427 1.00 84.70 C
ANISOU 547 C ILE A 85 12584 9178 10421 2595 3264 3795 C
ATOM 548 O ILE A 85 508.519 198.355 553.437 1.00 93.11 O
ANISOU 548 O ILE A 85 13620 10326 11430 2583 3101 3959 O
ATOM 549 CB ILE A 85 508.250 196.892 550.432 1.00101.74 C
ANISOU 549 CB ILE A 85 14836 11101 12720 3131 3480 3699 C
ATOM 550 CG1 ILE A 85 508.315 195.401 550.073 1.00106.62 C
ANISOU 550 CG1 ILE A 85 15720 11379 13410 3362 3598 3652 C
ATOM 551 CG2 ILE A 85 509.651 197.469 550.609 1.00 96.77 C
ANISOU 551 CG2 ILE A 85 13910 10782 12076 3320 3311 3958 C
ATOM 552 CD1 ILE A 85 507.042 194.849 549.459 1.00109.14 C
ANISOU 552 CD1 ILE A 85 16237 11452 13781 3206 3747 3299 C
ATOM 553 N MET A 86 507.355 199.545 551.931 1.00 73.86 N
ANISOU 553 N MET A 86 11014 7990 9059 2463 3272 3684 N
ATOM 554 CA MET A 86 507.741 200.797 552.570 1.00 80.79 C
ANISOU 554 CA MET A 86 11649 9141 9906 2313 3089 3762 C
ATOM 555 C MET A 86 507.007 201.004 553.891 1.00 79.53 C
ANISOU 555 C MET A 86 11645 8928 9646 1988 3044 3700 C
ATOM 556 O MET A 86 507.544 201.646 554.802 1.00 78.61 O
ANISOU 556 O MET A 86 11422 8979 9465 1902 2872 3818 O
ATOM 557 CB MET A 86 507.502 201.967 551.620 1.00 78.51 C
ANISOU 557 CB MET A 86 11084 9055 9690 2273 3096 3656 C
ATOM 558 CG MET A 86 507.764 203.322 552.243 1.00 87.68 C
ANISOU 558 CG MET A 86 12021 10439 10854 2097 2931 3730 C
ATOM 559 SD MET A 86 509.526 203.675 552.384 1.00105.10 S
ANISOU 559 SD MET A 86 13936 12895 13100 2315 2710 4020 S
ATOM 560 CE MET A 86 509.477 205.408 552.836 1.00114.95 C
ANISOU 560 CE MET A 86 14929 14348 14398 2057 2556 4033 C
ATOM 561 N ALA A 87 505.797 200.458 554.029 1.00 72.62 N
ANISOU 561 N ALA A 87 11016 7832 8744 1804 3200 3520 N
ATOM 562 CA ALA A 87 505.131 200.492 555.327 1.00 75.99 C
ANISOU 562 CA ALA A 87 11599 8222 9053 1517 3172 3477 C
ATOM 563 C ALA A 87 505.923 199.703 556.364 1.00 79.91 C
ANISOU 563 C ALA A 87 12224 8680 9460 1596 3054 3700 C
ATOM 564 O ALA A 87 506.090 200.154 557.502 1.00 70.45 O
ANISOU 564 O ALA A 87 11018 7619 8131 1451 2928 3787 O
ATOM 565 CB ALA A 87 503.705 199.952 555.208 1.00 71.62 C
ANISOU 565 CB ALA A 87 11261 7445 8508 1310 3368 3247 C
ATOM 566 N TRP A 88 506.433 198.527 555.985 1.00 86.92 N
ANISOU 566 N TRP A 88 13230 9386 10410 1835 3097 3801 N
ATOM 567 CA TRP A 88 507.294 197.770 556.888 1.00 84.24 C
ANISOU 567 CA TRP A 88 12978 9022 10006 1944 2972 4032 C
ATOM 568 C TRP A 88 508.637 198.464 557.094 1.00 85.65 C
ANISOU 568 C TRP A 88 12893 9489 10162 2099 2762 4225 C
ATOM 569 O TRP A 88 509.276 198.282 558.137 1.00 88.77 O
ANISOU 569 O TRP A 88 13312 9963 10451 2097 2613 4411 O
ATOM 570 CB TRP A 88 507.496 196.348 556.361 1.00 79.72 C
ANISOU 570 CB TRP A 88 12592 8161 9539 2177 3078 4076 C
ATOM 571 CG TRP A 88 506.410 195.403 556.783 1.00 92.26 C
ANISOU 571 CG TRP A 88 14489 9445 11122 1987 3216 3992 C
ATOM 572 CD1 TRP A 88 505.462 194.828 555.986 1.00 97.21 C
ANISOU 572 CD1 TRP A 88 15282 9797 11855 1945 3420 3799 C
ATOM 573 CD2 TRP A 88 506.157 194.930 558.112 1.00 89.22 C
ANISOU 573 CD2 TRP A 88 14273 9007 10619 1799 3159 4110 C
ATOM 574 NE1 TRP A 88 504.637 194.022 556.737 1.00 97.31 N
ANISOU 574 NE1 TRP A 88 15544 9583 11847 1729 3489 3785 N
ATOM 575 CE2 TRP A 88 505.042 194.069 558.044 1.00 93.06 C
ANISOU 575 CE2 TRP A 88 15006 9186 11166 1642 3334 3985 C
ATOM 576 CE3 TRP A 88 506.766 195.150 559.351 1.00 99.14 C
ANISOU 576 CE3 TRP A 88 15494 10457 11718 1745 2977 4319 C
ATOM 577 CZ2 TRP A 88 504.525 193.429 559.169 1.00 97.15 C
ANISOU 577 CZ2 TRP A 88 15717 9598 11599 1435 3334 4078 C
ATOM 578 CZ3 TRP A 88 506.250 194.511 560.467 1.00 97.69 C
ANISOU 578 CZ3 TRP A 88 15518 10174 11425 1552 2981 4411 C
ATOM 579 CH2 TRP A 88 505.142 193.663 560.367 1.00 95.94 C
ANISOU 579 CH2 TRP A 88 15522 9657 11275 1399 3159 4298 C
ATOM 580 N THR A 89 509.078 199.258 556.116 1.00 73.74 N
ANISOU 580 N THR A 89 11121 8148 8748 2226 2746 4193 N
ATOM 581 CA THR A 89 510.308 200.028 556.271 1.00 74.04 C
ANISOU 581 CA THR A 89 10872 8472 8789 2335 2548 4367 C
ATOM 582 C THR A 89 510.164 201.085 557.360 1.00 71.47 C
ANISOU 582 C THR A 89 10490 8325 8341 2071 2407 4391 C
ATOM 583 O THR A 89 511.059 201.247 558.199 1.00 78.01 O
ANISOU 583 O THR A 89 11242 9310 9088 2097 2223 4580 O
ATOM 584 CB THR A 89 510.681 200.678 554.935 1.00 76.68 C
ANISOU 584 CB THR A 89 10926 8948 9259 2496 2581 4326 C
ATOM 585 OG1 THR A 89 510.814 199.665 553.929 1.00 84.59 O
ANISOU 585 OG1 THR A 89 12002 9796 10342 2765 2728 4301 O
ATOM 586 CG2 THR A 89 511.990 201.461 555.047 1.00 70.19 C
ANISOU 586 CG2 THR A 89 9779 8423 8468 2595 2379 4512 C
ATOM 587 N VAL A 90 509.037 201.801 557.370 1.00 73.82 N
ANISOU 587 N VAL A 90 10827 8604 8616 1820 2498 4199 N
ATOM 588 CA VAL A 90 508.849 202.885 558.328 1.00 78.20 C
ANISOU 588 CA VAL A 90 11329 9328 9057 1582 2393 4201 C
ATOM 589 C VAL A 90 508.714 202.341 559.745 1.00 74.59 C
ANISOU 589 C VAL A 90 11108 8847 8388 1455 2344 4289 C
ATOM 590 O VAL A 90 509.209 202.949 560.702 1.00 72.00 O
ANISOU 590 O VAL A 90 10721 8713 7922 1380 2186 4419 O
ATOM 591 CB VAL A 90 507.636 203.744 557.928 1.00 74.14 C
ANISOU 591 CB VAL A 90 10792 8790 8586 1362 2529 3954 C
ATOM 592 CG1 VAL A 90 507.397 204.838 558.952 1.00 75.54 C
ANISOU 592 CG1 VAL A 90 10917 9131 8654 1114 2423 3896 C
ATOM 593 CG2 VAL A 90 507.851 204.350 556.543 1.00 80.68 C
ANISOU 593 CG2 VAL A 90 11361 9682 9612 1494 2555 3906 C
ATOM 594 N VAL A 91 508.056 201.191 559.913 1.00 73.48 N
ANISOU 594 N VAL A 91 11230 8478 8210 1426 2474 4239 N
ATOM 595 CA VAL A 91 507.917 200.655 561.263 1.00 79.05 C
ANISOU 595 CA VAL A 91 12148 9177 8709 1299 2428 4349 C
ATOM 596 C VAL A 91 509.253 200.124 561.766 1.00 79.69 C
ANISOU 596 C VAL A 91 12192 9343 8743 1510 2241 4631 C
ATOM 597 O VAL A 91 509.548 200.212 562.965 1.00 83.69 O
ANISOU 597 O VAL A 91 12758 9994 9046 1424 2113 4778 O
ATOM 598 CB VAL A 91 506.806 199.586 561.324 1.00 90.30 C
ANISOU 598 CB VAL A 91 13845 10333 10132 1183 2616 4237 C
ATOM 599 CG1 VAL A 91 506.947 198.587 560.204 1.00103.91 C
ANISOU 599 CG1 VAL A 91 15611 11814 12057 1409 2718 4219 C
ATOM 600 CG2 VAL A 91 506.808 198.881 562.679 1.00115.26 C
ANISOU 600 CG2 VAL A 91 17210 13493 13091 1086 2560 4410 C
ATOM 601 N ASN A 92 510.086 199.580 560.876 1.00 82.97 N
ANISOU 601 N ASN A 92 12500 9693 9330 1793 2224 4707 N
ATOM 602 CA ASN A 92 511.445 199.221 561.269 1.00 88.02 C
ANISOU 602 CA ASN A 92 13043 10451 9950 2007 2038 4960 C
ATOM 603 C ASN A 92 512.188 200.435 561.809 1.00 94.98 C
ANISOU 603 C ASN A 92 13691 11655 10743 1953 1830 5061 C
ATOM 604 O ASN A 92 512.791 200.382 562.886 1.00 98.92 O
ANISOU 604 O ASN A 92 14211 12299 11076 1939 1662 5246 O
ATOM 605 CB ASN A 92 512.201 198.623 560.083 1.00 99.19 C
ANISOU 605 CB ASN A 92 14332 11783 11572 2324 2081 4989 C
ATOM 606 CG ASN A 92 511.706 197.248 559.709 1.00105.32 C
ANISOU 606 CG ASN A 92 15361 12231 12426 2423 2254 4948 C
ATOM 607 OD1 ASN A 92 510.834 196.686 560.372 1.00105.19 O
ANISOU 607 OD1 ASN A 92 15604 12041 12323 2245 2330 4921 O
ATOM 608 ND2 ASN A 92 512.260 196.695 558.637 1.00108.93 N
ANISOU 608 ND2 ASN A 92 15739 12604 13046 2708 2323 4948 N
ATOM 609 N SER A 93 512.143 201.548 561.071 1.00 90.45 N
ANISOU 609 N SER A 93 12888 11198 10279 1917 1834 4950 N
ATOM 610 CA SER A 93 512.791 202.770 561.534 1.00 88.09 C
ANISOU 610 CA SER A 93 12356 11187 9929 1846 1637 5047 C
ATOM 611 C SER A 93 512.186 203.248 562.849 1.00 83.64 C
ANISOU 611 C SER A 93 11950 10723 9106 1584 1592 5045 C
ATOM 612 O SER A 93 512.911 203.666 563.759 1.00 77.54 O
ANISOU 612 O SER A 93 11096 10182 8182 1563 1385 5215 O
ATOM 613 CB SER A 93 512.684 203.860 560.467 1.00 84.36 C
ANISOU 613 CB SER A 93 11624 10781 9646 1827 1673 4931 C
ATOM 614 OG SER A 93 513.193 203.411 559.222 1.00 77.63 O
ANISOU 614 OG SER A 93 10628 9872 8996 2072 1739 4927 O
ATOM 615 N ILE A 94 510.858 203.200 562.963 1.00 74.50 N
ANISOU 615 N ILE A 94 11007 9419 7880 1384 1785 4848 N
ATOM 616 CA ILE A 94 510.198 203.582 564.211 1.00 81.39 C
ANISOU 616 CA ILE A 94 12045 10403 8475 1139 1786 4824 C
ATOM 617 C ILE A 94 510.715 202.725 565.361 1.00 84.03 C
ANISOU 617 C ILE A 94 12542 10800 8587 1179 1664 5037 C
ATOM 618 O ILE A 94 511.261 203.238 566.350 1.00 93.30 O
ANISOU 618 O ILE A 94 13666 12241 9543 1132 1480 5180 O
ATOM 619 CB ILE A 94 508.667 203.472 564.064 1.00 73.73 C
ANISOU 619 CB ILE A 94 11273 9247 7495 931 2043 4557 C
ATOM 620 CG1 ILE A 94 508.112 204.643 563.258 1.00 82.24 C
ANISOU 620 CG1 ILE A 94 12136 10343 8768 802 2069 4233 C
ATOM 621 CG2 ILE A 94 507.986 203.397 565.430 1.00 75.50 C
ANISOU 621 CG2 ILE A 94 11713 9559 7413 700 2064 4516 C
ATOM 622 CD1 ILE A 94 506.658 204.479 562.849 1.00 77.02 C
ANISOU 622 CD1 ILE A 94 11620 9492 8154 639 2319 3963 C
ATOM 623 N CYS A 95 510.599 201.397 565.217 1.00 83.81 N
ANISOU 623 N CYS A 95 12694 10536 8615 1277 1752 5076 N
ATOM 624 CA CYS A 95 511.015 200.474 566.272 1.00 88.11 C
ANISOU 624 CA CYS A 95 13405 11100 8972 1314 1654 5293 C
ATOM 625 C CYS A 95 512.500 200.611 566.602 1.00 96.67 C
ANISOU 625 C CYS A 95 14297 12405 10028 1509 1391 5535 C
ATOM 626 O CYS A 95 512.908 200.432 567.755 1.00 97.62 O
ANISOU 626 O CYS A 95 14493 12692 9905 1482 1243 5714 O
ATOM 627 CB CYS A 95 510.739 199.037 565.855 1.00 88.99 C
ANISOU 627 CB CYS A 95 13699 10889 9224 1419 1789 5314 C
ATOM 628 SG CYS A 95 508.994 198.617 565.626 1.00 97.78 S
ANISOU 628 SG CYS A 95 15050 11737 10364 1175 2078 5065 S
ATOM 629 N ASN A 96 513.338 200.873 565.596 1.00101.30 N
ANISOU 629 N ASN A 96 14624 13008 10857 1711 1330 5547 N
ATOM 630 CA ASN A 96 514.758 201.070 565.850 1.00102.83 C
ANISOU 630 CA ASN A 96 14589 13432 11050 1884 1082 5761 C
ATOM 631 C ASN A 96 515.055 202.439 566.443 1.00107.33 C
ANISOU 631 C ASN A 96 14968 14334 11477 1740 892 5789 C
ATOM 632 O ASN A 96 516.140 202.630 566.991 1.00112.21 O
ANISOU 632 O ASN A 96 15423 15190 12021 1824 652 5978 O
ATOM 633 CB ASN A 96 515.543 200.864 564.557 1.00108.66 C
ANISOU 633 CB ASN A 96 15095 14098 12092 2143 1101 5762 C
ATOM 634 CG ASN A 96 515.856 199.393 564.296 1.00117.74 C
ANISOU 634 CG ASN A 96 16382 15020 13334 2368 1178 5852 C
ATOM 635 OD1 ASN A 96 516.847 198.864 564.800 1.00119.45 O
ANISOU 635 OD1 ASN A 96 16554 15321 13508 2525 1030 6063 O
ATOM 636 ND2 ASN A 96 515.019 198.732 563.499 1.00118.17 N
ANISOU 636 ND2 ASN A 96 16595 14785 13518 2388 1407 5697 N
ATOM 637 N THR A 97 514.126 203.393 566.349 1.00103.26 N
ANISOU 637 N THR A 97 14460 13849 10926 1525 987 5610 N
ATOM 638 CA THR A 97 514.304 204.705 566.966 1.00 98.94 C
ANISOU 638 CA THR A 97 13737 13604 10251 1347 795 5573 C
ATOM 639 C THR A 97 513.693 204.779 568.362 1.00100.85 C
ANISOU 639 C THR A 97 14197 13986 10136 1116 754 5485 C
ATOM 640 O THR A 97 514.279 205.400 569.262 1.00 97.69 O
ANISOU 640 O THR A 97 13683 13877 9558 1027 498 5497 O
ATOM 641 CB THR A 97 513.700 205.791 566.064 1.00103.99 C
ANISOU 641 CB THR A 97 14204 14168 11141 1191 870 5229 C
ATOM 642 OG1 THR A 97 514.622 206.124 565.018 1.00118.59 O
ANISOU 642 OG1 THR A 97 15741 16042 13274 1372 793 5337 O
ATOM 643 CG2 THR A 97 513.356 207.042 566.853 1.00 94.39 C
ANISOU 643 CG2 THR A 97 12909 13138 9817 893 719 4943 C
ATOM 644 N THR A 98 512.551 204.113 568.558 1.00 97.32 N
ANISOU 644 N THR A 98 14055 13350 9572 1022 1003 5407 N
ATOM 645 CA THR A 98 511.790 204.122 569.801 1.00 95.48 C
ANISOU 645 CA THR A 98 14044 13244 8991 797 1028 5312 C
ATOM 646 C THR A 98 512.094 202.957 570.737 1.00102.99 C
ANISOU 646 C THR A 98 15229 14239 9664 903 1009 5666 C
ATOM 647 O THR A 98 511.751 203.033 571.927 1.00 96.33 O
ANISOU 647 O THR A 98 14528 13608 8464 744 969 5668 O
ATOM 648 CB THR A 98 510.289 204.102 569.482 1.00 94.89 C
ANISOU 648 CB THR A 98 14145 12950 8959 607 1325 5017 C
ATOM 649 OG1 THR A 98 509.910 202.799 568.989 1.00 90.32 O
ANISOU 649 OG1 THR A 98 13787 12067 8462 739 1557 5199 O
ATOM 650 CG2 THR A 98 509.929 205.174 568.475 1.00 93.99 C
ANISOU 650 CG2 THR A 98 13808 12760 9145 521 1357 4679 C
ATOM 651 N GLY A 99 512.694 201.881 570.235 1.00106.46 N
ANISOU 651 N GLY A 99 15684 14443 10323 1118 1001 5798 N
ATOM 652 CA GLY A 99 512.880 200.709 571.066 1.00106.73 C
ANISOU 652 CA GLY A 99 15929 14422 10201 1166 967 5992 C
ATOM 653 C GLY A 99 511.598 199.981 571.402 1.00118.76 C
ANISOU 653 C GLY A 99 17756 15742 11626 983 1207 5907 C
ATOM 654 O GLY A 99 511.505 199.367 572.467 1.00126.04 O
ANISOU 654 O GLY A 99 18865 16734 12291 918 1174 6059 O
ATOM 655 N VAL A 100 510.598 200.045 570.528 1.00116.29 N
ANISOU 655 N VAL A 100 17480 15195 11512 889 1442 5673 N
ATOM 656 CA VAL A 100 509.324 199.355 570.713 1.00121.35 C
ANISOU 656 CA VAL A 100 18363 15632 12112 699 1676 5572 C
ATOM 657 C VAL A 100 509.345 198.046 569.932 1.00121.67 C
ANISOU 657 C VAL A 100 18480 15299 12448 849 1765 5636 C
ATOM 658 O VAL A 100 509.982 197.954 568.874 1.00122.26 O
ANISOU 658 O VAL A 100 18406 15244 12804 1068 1736 5621 O
ATOM 659 CB VAL A 100 508.156 200.264 570.276 1.00111.54 C
ANISOU 659 CB VAL A 100 17097 14385 10897 493 1875 5254 C
ATOM 660 CG1 VAL A 100 506.847 199.472 570.091 1.00117.42 C
ANISOU 660 CG1 VAL A 100 18025 14867 11724 325 2125 5118 C
ATOM 661 CG2 VAL A 100 507.961 201.376 571.305 1.00114.35 C
ANISOU 661 CG2 VAL A 100 17443 15116 10889 322 1822 5197 C
ATOM 662 N GLU A 101 508.672 197.020 570.469 1.00119.38 N
ANISOU 662 N GLU A 101 18415 14854 12089 737 1872 5719 N
ATOM 663 CA GLU A 101 508.559 195.722 569.805 1.00118.86 C
ANISOU 663 CA GLU A 101 18450 14419 12293 859 1973 5781 C
ATOM 664 C GLU A 101 508.025 195.870 568.387 1.00113.84 C
ANISOU 664 C GLU A 101 17732 13554 11967 897 2139 5511 C
ATOM 665 O GLU A 101 507.068 196.605 568.146 1.00117.50 O
ANISOU 665 O GLU A 101 18170 14056 12418 703 2272 5262 O
ATOM 666 CB GLU A 101 507.630 194.799 570.602 1.00111.91 C
ANISOU 666 CB GLU A 101 17809 13422 11291 657 2094 5876 C
ATOM 667 CG GLU A 101 508.313 193.649 571.305 1.00120.58 C
ANISOU 667 CG GLU A 101 19038 14441 12334 780 1980 6219 C
ATOM 668 CD GLU A 101 507.419 192.951 572.328 1.00122.35 C
ANISOU 668 CD GLU A 101 19478 14644 12365 537 2075 6353 C
ATOM 669 OE1 GLU A 101 506.203 193.232 572.395 1.00122.51 O
ANISOU 669 OE1 GLU A 101 19537 14679 12333 279 2254 6167 O
ATOM 670 OE2 GLU A 101 507.937 192.099 573.074 1.00135.46 O
ANISOU 670 OE2 GLU A 101 21259 16280 13932 607 1973 6658 O
ATOM 671 N LYS A 102 508.633 195.144 567.455 1.00109.06 N
ANISOU 671 N LYS A 102 17090 12718 11630 1156 2138 5558 N
ATOM 672 CA LYS A 102 508.141 195.126 566.085 1.00108.25 C
ANISOU 672 CA LYS A 102 16936 12392 11803 1215 2302 5317 C
ATOM 673 C LYS A 102 506.842 194.330 566.028 1.00107.88 C
ANISOU 673 C LYS A 102 17098 12073 11818 1028 2514 5211 C
ATOM 674 O LYS A 102 506.833 193.156 566.416 1.00115.55 O
ANISOU 674 O LYS A 102 18245 12845 12815 1058 2533 5393 O
ATOM 675 CB LYS A 102 509.182 194.524 565.141 1.00105.61 C
ANISOU 675 CB LYS A 102 16511 11911 11705 1562 2255 5400 C
ATOM 676 CG LYS A 102 508.766 194.539 563.671 1.00108.15 C
ANISOU 676 CG LYS A 102 16775 12038 12280 1652 2422 5156 C
ATOM 677 CD LYS A 102 509.957 194.397 562.718 1.00110.10 C
ANISOU 677 CD LYS A 102 16844 12282 12706 2004 2355 5214 C
ATOM 678 CE LYS A 102 511.221 194.999 563.295 1.00110.94 C
ANISOU 678 CE LYS A 102 16750 12701 12702 2118 2117 5409 C
ATOM 679 NZ LYS A 102 512.344 194.953 562.325 1.00118.24 N
ANISOU 679 NZ LYS A 102 17457 13663 13805 2443 2067 5449 N
ATOM 680 N PRO A 103 505.742 194.912 565.556 1.00108.73 N
ANISOU 680 N PRO A 103 17187 12161 11966 834 2672 4930 N
ATOM 681 CA PRO A 103 504.473 194.179 565.551 1.00 91.39 C
ANISOU 681 CA PRO A 103 15168 9729 9829 633 2868 4826 C
ATOM 682 C PRO A 103 504.511 193.031 564.559 1.00 94.91 C
ANISOU 682 C PRO A 103 15714 9796 10552 816 2966 4820 C
ATOM 683 O PRO A 103 505.203 193.080 563.538 1.00 91.22 O
ANISOU 683 O PRO A 103 15145 9262 10251 1070 2946 4771 O
ATOM 684 CB PRO A 103 503.443 195.237 565.133 1.00 92.21 C
ANISOU 684 CB PRO A 103 15171 9937 9929 425 2990 4502 C
ATOM 685 CG PRO A 103 504.176 196.563 565.176 1.00 94.65 C
ANISOU 685 CG PRO A 103 15275 10555 10133 487 2848 4475 C
ATOM 686 CD PRO A 103 505.614 196.247 564.945 1.00 83.54 C
ANISOU 686 CD PRO A 103 13797 9150 8794 796 2679 4697 C
ATOM 687 N LYS A 104 503.758 191.979 564.880 1.00100.49 N
ANISOU 687 N LYS A 104 16623 10256 11304 685 3080 4877 N
ATOM 688 CA LYS A 104 503.678 190.834 563.980 1.00 98.10 C
ANISOU 688 CA LYS A 104 16453 9553 11269 832 3192 4854 C
ATOM 689 C LYS A 104 502.965 191.201 562.686 1.00 97.17 C
ANISOU 689 C LYS A 104 16282 9314 11322 810 3352 4515 C
ATOM 690 O LYS A 104 503.328 190.713 561.608 1.00104.73 O
ANISOU 690 O LYS A 104 17262 10046 12485 1041 3405 4451 O
ATOM 691 CB LYS A 104 502.970 189.669 564.674 1.00 98.57 C
ANISOU 691 CB LYS A 104 16735 9369 11346 658 3274 5000 C
ATOM 692 N PHE A 105 501.959 192.067 562.768 1.00 93.80 N
ANISOU 692 N PHE A 105 15783 9048 10808 544 3432 4295 N
ATOM 693 CA PHE A 105 501.184 192.490 561.613 1.00 97.74 C
ANISOU 693 CA PHE A 105 16223 9465 11450 489 3579 3973 C
ATOM 694 C PHE A 105 501.248 194.004 561.473 1.00 93.74 C
ANISOU 694 C PHE A 105 15483 9299 10836 450 3517 3822 C
ATOM 695 O PHE A 105 501.516 194.729 562.435 1.00 89.03 O
ANISOU 695 O PHE A 105 14803 8986 10036 366 3399 3916 O
ATOM 696 CB PHE A 105 499.722 192.037 561.723 1.00103.03 C
ANISOU 696 CB PHE A 105 17016 9966 12165 184 3754 3815 C
ATOM 697 CG PHE A 105 499.559 190.556 561.910 1.00117.34 C
ANISOU 697 CG PHE A 105 19059 11422 14104 179 3817 3968 C
ATOM 698 CD1 PHE A 105 499.660 189.986 563.170 1.00118.22 C
ANISOU 698 CD1 PHE A 105 19271 11560 14087 87 3749 4250 C
ATOM 699 CD2 PHE A 105 499.306 189.733 560.825 1.00123.30 C
ANISOU 699 CD2 PHE A 105 19936 11808 15106 265 3943 3836 C
ATOM 700 CE1 PHE A 105 499.512 188.624 563.345 1.00121.79 C
ANISOU 700 CE1 PHE A 105 19929 11669 14678 78 3800 4413 C
ATOM 701 CE2 PHE A 105 499.155 188.368 560.993 1.00123.86 C
ANISOU 701 CE2 PHE A 105 20222 11518 15320 254 3994 3969 C
ATOM 702 CZ PHE A 105 499.258 187.813 562.255 1.00127.28 C
ANISOU 702 CZ PHE A 105 20742 11972 15645 160 3920 4267 C
ATOM 703 N LEU A 106 500.993 194.472 560.258 1.00 92.91 N
ANISOU 703 N LEU A 106 15278 9156 10868 509 3602 3589 N
ATOM 704 CA LEU A 106 501.058 195.895 559.961 1.00 83.57 C
ANISOU 704 CA LEU A 106 13861 8259 9632 488 3549 3447 C
ATOM 705 C LEU A 106 499.981 196.650 560.734 1.00 84.98 C
ANISOU 705 C LEU A 106 13999 8618 9671 160 3589 3292 C
ATOM 706 O LEU A 106 498.790 196.327 560.602 1.00 78.81 O
ANISOU 706 O LEU A 106 13291 7710 8942 -44 3738 3113 O
ATOM 707 CB LEU A 106 500.892 196.131 558.461 1.00 83.85 C
ANISOU 707 CB LEU A 106 13808 8204 9846 608 3651 3243 C
ATOM 708 CG LEU A 106 502.144 196.385 557.612 1.00 94.04 C
ANISOU 708 CG LEU A 106 14954 9563 11212 946 3564 3348 C
ATOM 709 CD1 LEU A 106 501.763 196.925 556.238 1.00 93.24 C
ANISOU 709 CD1 LEU A 106 14728 9464 11233 999 3675 3132 C
ATOM 710 CD2 LEU A 106 503.112 197.335 558.309 1.00 91.44 C
ANISOU 710 CD2 LEU A 106 14437 9550 10756 1001 3360 3511 C
ATOM 711 N PRO A 107 500.343 197.634 561.552 1.00 82.17 N
ANISOU 711 N PRO A 107 13528 8556 9138 104 3466 3350 N
ATOM 712 CA PRO A 107 499.325 198.502 562.149 1.00 79.64 C
ANISOU 712 CA PRO A 107 13144 8421 8693 -175 3522 3159 C
ATOM 713 C PRO A 107 499.013 199.657 561.216 1.00 81.72 C
ANISOU 713 C PRO A 107 13203 8782 9066 -183 3552 2906 C
ATOM 714 O PRO A 107 499.595 199.743 560.128 1.00 75.19 O
ANISOU 714 O PRO A 107 12285 7891 8393 23 3530 2903 O
ATOM 715 CB PRO A 107 499.994 198.970 563.443 1.00 83.08 C
ANISOU 715 CB PRO A 107 13577 9110 8878 -200 3382 3356 C
ATOM 716 CG PRO A 107 501.445 199.050 563.068 1.00 85.07 C
ANISOU 716 CG PRO A 107 13753 9392 9180 86 3220 3554 C
ATOM 717 CD PRO A 107 501.698 197.988 562.009 1.00 89.55 C
ANISOU 717 CD PRO A 107 14385 9668 9972 290 3274 3588 C
ATOM 718 N ASP A 108 498.117 200.556 561.619 1.00 71.69 N
ANISOU 718 N ASP A 108 11846 7676 7717 -404 3603 2702 N
ATOM 719 CA ASP A 108 497.704 201.649 560.746 1.00 78.63 C
ANISOU 719 CA ASP A 108 12522 8633 8719 -425 3634 2455 C
ATOM 720 C ASP A 108 498.432 202.958 561.027 1.00 76.40 C
ANISOU 720 C ASP A 108 12081 8581 8366 -380 3518 2491 C
ATOM 721 O ASP A 108 498.750 203.693 560.089 1.00 70.80 O
ANISOU 721 O ASP A 108 11194 7903 7806 -269 3488 2431 O
ATOM 722 CB ASP A 108 496.192 201.871 560.853 1.00 74.19 C
ANISOU 722 CB ASP A 108 11933 8090 8165 -680 3770 2174 C
ATOM 723 CG ASP A 108 495.398 200.614 560.553 1.00 78.85 C
ANISOU 723 CG ASP A 108 12671 8445 8842 -755 3895 2134 C
ATOM 724 OD1 ASP A 108 494.985 199.925 561.508 1.00 88.72 O
ANISOU 724 OD1 ASP A 108 14064 9671 9976 -893 3938 2220 O
ATOM 725 OD2 ASP A 108 495.209 200.296 559.362 1.00 69.39 O
ANISOU 725 OD2 ASP A 108 11451 7086 7827 -677 3959 2030 O
ATOM 726 N LEU A 109 498.711 203.267 562.291 1.00 74.75 N
ANISOU 726 N LEU A 109 11934 8538 7930 -465 3459 2599 N
ATOM 727 CA LEU A 109 499.330 204.526 562.681 1.00 68.94 C
ANISOU 727 CA LEU A 109 11076 8010 7107 -456 3367 2617 C
ATOM 728 C LEU A 109 500.447 204.270 563.681 1.00 80.16 C
ANISOU 728 C LEU A 109 12584 9549 8323 -366 3205 2904 C
ATOM 729 O LEU A 109 500.578 203.177 564.239 1.00 84.03 O
ANISOU 729 O LEU A 109 13257 9972 8700 -348 3210 3094 O
ATOM 730 CB LEU A 109 498.318 205.470 563.334 1.00 76.93 C
ANISOU 730 CB LEU A 109 12027 9180 8024 -694 3423 2329 C
ATOM 731 CG LEU A 109 497.014 205.898 562.675 1.00 83.59 C
ANISOU 731 CG LEU A 109 12771 9971 9019 -832 3583 2013 C
ATOM 732 CD1 LEU A 109 496.508 207.106 563.434 1.00 90.46 C
ANISOU 732 CD1 LEU A 109 13526 11048 9797 -988 3550 1765 C
ATOM 733 CD2 LEU A 109 497.198 206.220 561.203 1.00 85.83 C
ANISOU 733 CD2 LEU A 109 12862 10159 9591 -683 3543 1946 C
ATOM 734 N TYR A 110 501.238 205.313 563.935 1.00 75.56 N
ANISOU 734 N TYR A 110 11813 9168 7729 -322 2990 2889 N
ATOM 735 CA TYR A 110 502.110 205.357 565.101 1.00 87.58 C
ANISOU 735 CA TYR A 110 13385 10882 9009 -303 2816 3083 C
ATOM 736 C TYR A 110 501.942 206.697 565.801 1.00 90.23 C
ANISOU 736 C TYR A 110 13578 11452 9252 -461 2695 2836 C
ATOM 737 O TYR A 110 501.942 207.746 565.150 1.00 90.20 O
ANISOU 737 O TYR A 110 13347 11464 9461 -463 2621 2637 O
ATOM 738 CB TYR A 110 503.584 205.139 564.743 1.00 85.54 C
ANISOU 738 CB TYR A 110 13030 10637 8833 -46 2621 3371 C
ATOM 739 CG TYR A 110 504.462 205.109 565.977 1.00 90.82 C
ANISOU 739 CG TYR A 110 13751 11520 9238 -28 2431 3585 C
ATOM 740 CD1 TYR A 110 505.218 206.215 566.348 1.00 93.22 C
ANISOU 740 CD1 TYR A 110 13844 12054 9521 -39 2185 3530 C
ATOM 741 CD2 TYR A 110 504.498 203.988 566.796 1.00 91.39 C
ANISOU 741 CD2 TYR A 110 14079 11566 9078 -12 2491 3841 C
ATOM 742 CE1 TYR A 110 506.008 206.193 567.485 1.00 87.64 C
ANISOU 742 CE1 TYR A 110 13175 11569 8554 -30 1994 3709 C
ATOM 743 CE2 TYR A 110 505.282 203.955 567.934 1.00 89.40 C
ANISOU 743 CE2 TYR A 110 13869 11540 8557 10 2309 4048 C
ATOM 744 CZ TYR A 110 506.034 205.060 568.274 1.00 98.84 C
ANISOU 744 CZ TYR A 110 14848 12988 9720 1 2056 3971 C
ATOM 745 OH TYR A 110 506.812 205.021 569.411 1.00101.61 O
ANISOU 745 OH TYR A 110 15233 13588 9787 18 1858 4165 O
ATOM 746 N ASP A 111 501.808 206.656 567.125 1.00 84.05 N
ANISOU 746 N ASP A 111 12932 10851 8152 -587 2675 2852 N
ATOM 747 CA ASP A 111 501.632 207.849 567.947 1.00 84.87 C
ANISOU 747 CA ASP A 111 12935 11189 8122 -737 2564 2592 C
ATOM 748 C ASP A 111 502.978 208.204 568.572 1.00 90.15 C
ANISOU 748 C ASP A 111 13523 12058 8672 -646 2269 2759 C
ATOM 749 O ASP A 111 503.463 207.492 569.457 1.00 90.51 O
ANISOU 749 O ASP A 111 13726 12223 8441 -614 2214 3010 O
ATOM 750 CB ASP A 111 500.571 207.608 569.020 1.00 90.78 C
ANISOU 750 CB ASP A 111 13874 12054 8562 -938 2740 2472 C
ATOM 751 CG ASP A 111 500.161 208.881 569.747 1.00 92.51 C
ANISOU 751 CG ASP A 111 13988 12496 8667 -1092 2671 2118 C
ATOM 752 OD1 ASP A 111 500.940 209.857 569.769 1.00 97.58 O
ANISOU 752 OD1 ASP A 111 14450 13235 9392 -1051 2429 2027 O
ATOM 753 OD2 ASP A 111 499.041 208.906 570.298 1.00 95.22 O
ANISOU 753 OD2 ASP A 111 14421 12912 8846 -1257 2863 1922 O
ATOM 754 N TYR A 112 503.577 209.307 568.117 1.00 84.80 N
ANISOU 754 N TYR A 112 12591 11420 8210 -612 2073 2633 N
ATOM 755 CA TYR A 112 504.830 209.761 568.711 1.00 90.39 C
ANISOU 755 CA TYR A 112 13187 12330 8829 -556 1774 2757 C
ATOM 756 C TYR A 112 504.637 210.329 570.111 1.00 95.22 C
ANISOU 756 C TYR A 112 13863 13207 9109 -726 1676 2568 C
ATOM 757 O TYR A 112 505.607 210.410 570.872 1.00 99.31 O
ANISOU 757 O TYR A 112 14357 13934 9442 -694 1441 2707 O
ATOM 758 CB TYR A 112 505.493 210.810 567.818 1.00 91.88 C
ANISOU 758 CB TYR A 112 13070 12473 9366 -497 1598 2679 C
ATOM 759 CG TYR A 112 506.210 210.223 566.626 1.00 94.03 C
ANISOU 759 CG TYR A 112 13247 12591 9890 -276 1606 2960 C
ATOM 760 CD1 TYR A 112 507.337 209.428 566.792 1.00 97.91 C
ANISOU 760 CD1 TYR A 112 13761 13146 10293 -98 1487 3321 C
ATOM 761 CD2 TYR A 112 505.759 210.462 565.334 1.00 82.56 C
ANISOU 761 CD2 TYR A 112 11673 10947 8751 -232 1735 2862 C
ATOM 762 CE1 TYR A 112 507.995 208.888 565.704 1.00102.97 C
ANISOU 762 CE1 TYR A 112 14309 13660 11156 125 1507 3558 C
ATOM 763 CE2 TYR A 112 506.410 209.925 564.240 1.00 86.69 C
ANISOU 763 CE2 TYR A 112 12106 11359 9473 -19 1752 3100 C
ATOM 764 CZ TYR A 112 507.528 209.140 564.431 1.00 94.60 C
ANISOU 764 CZ TYR A 112 13134 12423 10387 162 1644 3439 C
ATOM 765 OH TYR A 112 508.180 208.603 563.344 1.00 98.05 O
ANISOU 765 OH TYR A 112 13475 12763 11015 394 1672 3658 O
ATOM 766 N LYS A 113 503.413 210.721 570.469 1.00 93.01 N
ANISOU 766 N LYS A 113 13656 12945 8740 -900 1848 2247 N
ATOM 767 CA LYS A 113 503.181 211.325 571.776 1.00 91.47 C
ANISOU 767 CA LYS A 113 13514 13022 8218 -1053 1768 2020 C
ATOM 768 C LYS A 113 502.989 210.268 572.857 1.00 95.61 C
ANISOU 768 C LYS A 113 14305 13719 8303 -1084 1870 2232 C
ATOM 769 O LYS A 113 503.452 210.447 573.989 1.00 96.86 O
ANISOU 769 O LYS A 113 14510 14165 8127 -1127 1704 2240 O
ATOM 770 CB LYS A 113 501.971 212.260 571.715 1.00 92.29 C
ANISOU 770 CB LYS A 113 13560 13090 8416 -1207 1910 1572 C
ATOM 771 CG LYS A 113 501.739 213.074 572.982 1.00100.42 C
ANISOU 771 CG LYS A 113 14612 14399 9145 -1351 1817 1259 C
ATOM 772 CD LYS A 113 500.343 213.682 572.999 1.00102.78 C
ANISOU 772 CD LYS A 113 14904 14664 9484 -1482 2039 853 C
ATOM 773 CE LYS A 113 500.027 214.325 574.341 1.00102.40 C
ANISOU 773 CE LYS A 113 14914 14919 9074 -1610 1990 538 C
ATOM 774 NZ LYS A 113 498.566 214.561 574.508 1.00 96.64 N
ANISOU 774 NZ LYS A 113 14225 14200 8291 -1721 2273 212 N
ATOM 775 N GLU A 114 502.315 209.164 572.530 1.00 94.24 N
ANISOU 775 N GLU A 114 14305 13378 8124 -1070 2135 2410 N
ATOM 776 CA GLU A 114 502.082 208.082 573.478 1.00 96.25 C
ANISOU 776 CA GLU A 114 14817 13754 7998 -1104 2257 2661 C
ATOM 777 C GLU A 114 502.941 206.856 573.203 1.00100.59 C
ANISOU 777 C GLU A 114 15472 14173 8575 -918 2220 3138 C
ATOM 778 O GLU A 114 502.888 205.892 573.976 1.00 87.85 O
ANISOU 778 O GLU A 114 14074 12637 6668 -924 2298 3414 O
ATOM 779 CB GLU A 114 500.602 207.689 573.480 1.00 90.97 C
ANISOU 779 CB GLU A 114 14283 12996 7283 -1257 2598 2518 C
ATOM 780 CG GLU A 114 499.670 208.880 573.593 1.00 91.17 C
ANISOU 780 CG GLU A 114 14185 13114 7340 -1412 2665 2034 C
ATOM 781 CD GLU A 114 499.078 209.032 574.979 1.00105.99 C
ANISOU 781 CD GLU A 114 16183 15322 8764 -1566 2740 1892 C
ATOM 782 OE1 GLU A 114 497.958 209.574 575.086 1.00106.40 O
ANISOU 782 OE1 GLU A 114 16200 15418 8808 -1701 2921 1549 O
ATOM 783 OE2 GLU A 114 499.731 208.607 575.958 1.00110.18 O
ANISOU 783 OE2 GLU A 114 16837 16090 8939 -1544 2621 2128 O
ATOM 784 N ASN A 115 503.715 206.865 572.115 1.00 96.11 N
ANISOU 784 N ASN A 115 14754 13409 8356 -744 2112 3248 N
ATOM 785 CA ASN A 115 504.753 205.864 571.858 1.00102.10 C
ANISOU 785 CA ASN A 115 15564 14072 9157 -525 2024 3679 C
ATOM 786 C ASN A 115 504.168 204.458 571.721 1.00 92.01 C
ANISOU 786 C ASN A 115 14540 12564 7855 -496 2282 3926 C
ATOM 787 O ASN A 115 504.561 203.525 572.424 1.00109.10 O
ANISOU 787 O ASN A 115 16883 14779 9791 -429 2267 4270 O
ATOM 788 CB ASN A 115 505.829 205.913 572.945 1.00116.88 C
ANISOU 788 CB ASN A 115 17434 16254 10723 -469 1752 3889 C
ATOM 789 CG ASN A 115 506.351 207.319 573.183 1.00132.70 C
ANISOU 789 CG ASN A 115 19195 18483 12744 -535 1487 3612 C
ATOM 790 OD1 ASN A 115 505.581 208.279 573.245 1.00138.62 O
ANISOU 790 OD1 ASN A 115 19877 19272 13522 -705 1537 3218 O
ATOM 791 ND2 ASN A 115 507.666 207.448 573.314 1.00136.96 N
ANISOU 791 ND2 ASN A 115 19594 19160 13283 -399 1200 3816 N
ATOM 792 N ARG A 116 503.229 204.307 570.789 1.00 89.43 N
ANISOU 792 N ARG A 116 14224 11975 7782 -550 2513 3754 N
ATOM 793 CA ARG A 116 502.641 203.003 570.515 1.00 89.80 C
ANISOU 793 CA ARG A 116 14494 11754 7872 -540 2754 3949 C
ATOM 794 C ARG A 116 502.011 203.016 569.130 1.00 81.85 C
ANISOU 794 C ARG A 116 13404 10457 7238 -528 2912 3745 C
ATOM 795 O ARG A 116 501.662 204.071 568.592 1.00 80.17 O
ANISOU 795 O ARG A 116 12993 10282 7185 -593 2893 3421 O
ATOM 796 CB ARG A 116 501.601 202.616 571.573 1.00 93.82 C
ANISOU 796 CB ARG A 116 15173 12380 8096 -768 2914 3912 C
ATOM 797 CG ARG A 116 500.326 203.443 571.523 1.00 94.78 C
ANISOU 797 CG ARG A 116 15257 12551 8204 -990 3114 3516 C
ATOM 798 CD ARG A 116 499.767 203.709 572.921 1.00 91.07 C
ANISOU 798 CD ARG A 116 14884 12406 7314 -1183 3167 3442 C
ATOM 799 NE ARG A 116 498.597 204.579 572.863 1.00 87.15 N
ANISOU 799 NE ARG A 116 14284 11980 6848 -1373 3316 3013 N
ATOM 800 CZ ARG A 116 497.919 205.012 573.923 1.00 96.04 C
ANISOU 800 CZ ARG A 116 15449 13396 7648 -1547 3397 2838 C
ATOM 801 NH1 ARG A 116 498.286 204.658 575.151 1.00 95.35 N
ANISOU 801 NH1 ARG A 116 15507 13576 7147 -1568 3340 3060 N
ATOM 802 NH2 ARG A 116 496.867 205.803 573.750 1.00 85.95 N
ANISOU 802 NH2 ARG A 116 14056 12154 6447 -1688 3536 2440 N
ATOM 803 N PHE A 117 501.877 201.825 568.557 1.00 88.02 N
ANISOU 803 N PHE A 117 14228 10977 8239 -460 2945 3835 N
ATOM 804 CA PHE A 117 501.158 201.673 567.303 1.00 76.76 C
ANISOU 804 CA PHE A 117 12730 9298 7139 -463 3077 3615 C
ATOM 805 C PHE A 117 499.658 201.553 567.560 1.00 96.18 C
ANISOU 805 C PHE A 117 15239 11737 9567 -715 3274 3383 C
ATOM 806 O PHE A 117 499.215 201.126 568.631 1.00 86.95 O
ANISOU 806 O PHE A 117 14185 10680 8173 -856 3317 3464 O
ATOM 807 CB PHE A 117 501.651 200.444 566.542 1.00 88.03 C
ANISOU 807 CB PHE A 117 14202 10449 8797 -269 3041 3783 C
ATOM 808 CG PHE A 117 503.085 200.531 566.121 1.00 86.39 C
ANISOU 808 CG PHE A 117 13897 10258 8669 4 2856 3981 C
ATOM 809 CD1 PHE A 117 503.436 201.162 564.939 1.00 77.31 C
ANISOU 809 CD1 PHE A 117 12564 9065 7746 143 2839 3872 C
ATOM 810 CD2 PHE A 117 504.083 199.979 566.903 1.00 83.35 C
ANISOU 810 CD2 PHE A 117 13579 9952 8137 125 2693 4287 C
ATOM 811 CE1 PHE A 117 504.757 201.239 564.547 1.00 74.94 C
ANISOU 811 CE1 PHE A 117 12136 8810 7529 397 2669 4062 C
ATOM 812 CE2 PHE A 117 505.406 200.058 566.517 1.00 85.29 C
ANISOU 812 CE2 PHE A 117 13700 10235 8470 382 2513 4462 C
ATOM 813 CZ PHE A 117 505.742 200.687 565.341 1.00 80.05 C
ANISOU 813 CZ PHE A 117 12840 9538 8038 517 2504 4349 C
ATOM 814 N ILE A 118 498.876 201.926 566.550 1.00 74.29 N
ANISOU 814 N ILE A 118 12359 8840 7029 -764 3388 3105 N
ATOM 815 CA ILE A 118 497.420 201.917 566.622 1.00 81.41 C
ANISOU 815 CA ILE A 118 13254 9728 7950 -985 3563 2852 C
ATOM 816 C ILE A 118 496.880 201.085 565.466 1.00 88.63 C
ANISOU 816 C ILE A 118 14168 10347 9160 -950 3647 2770 C
ATOM 817 O ILE A 118 497.278 201.286 564.313 1.00 84.18 O
ANISOU 817 O ILE A 118 13512 9662 8811 -799 3615 2711 O
ATOM 818 CB ILE A 118 496.836 203.343 566.567 1.00 78.09 C
ANISOU 818 CB ILE A 118 12685 9478 7508 -1104 3623 2538 C
ATOM 819 CG1 ILE A 118 497.357 204.192 567.729 1.00 75.50 C
ANISOU 819 CG1 ILE A 118 12395 9437 6856 -1152 3560 2581 C
ATOM 820 CG2 ILE A 118 495.318 203.301 566.591 1.00 76.08 C
ANISOU 820 CG2 ILE A 118 12390 9217 7299 -1306 3790 2275 C
ATOM 821 CD1 ILE A 118 497.152 205.695 567.537 1.00 71.62 C
ANISOU 821 CD1 ILE A 118 11722 9082 6410 -1210 3540 2264 C
ATOM 822 N GLU A 119 495.967 200.161 565.771 1.00 79.15 N
ANISOU 822 N GLU A 119 13071 9043 7961 -1092 3762 2770 N
ATOM 823 CA GLU A 119 495.214 199.437 564.750 1.00 86.17 C
ANISOU 823 CA GLU A 119 13973 9663 9104 -1115 3873 2639 C
ATOM 824 C GLU A 119 493.777 199.941 564.797 1.00 84.39 C
ANISOU 824 C GLU A 119 13645 9528 8890 -1341 4008 2343 C
ATOM 825 O GLU A 119 493.034 199.633 565.737 1.00 86.68 O
ANISOU 825 O GLU A 119 13988 9910 9038 -1518 4088 2368 O
ATOM 826 CB GLU A 119 495.280 197.919 564.944 1.00 89.19 C
ANISOU 826 CB GLU A 119 14554 9808 9528 -1101 3905 2874 C
ATOM 827 CG GLU A 119 494.266 197.192 564.088 1.00 87.27 C
ANISOU 827 CG GLU A 119 14347 9303 9508 -1194 4052 2707 C
ATOM 828 CD GLU A 119 494.670 197.229 562.630 1.00 84.81 C
ANISOU 828 CD GLU A 119 13988 8806 9428 -1008 4044 2589 C
ATOM 829 OE1 GLU A 119 495.886 197.213 562.355 1.00 82.01 O
ANISOU 829 OE1 GLU A 119 13647 8425 9089 -771 3930 2753 O
ATOM 830 OE2 GLU A 119 493.774 197.352 561.768 1.00 82.67 O
ANISOU 830 OE2 GLU A 119 13648 8454 9309 -1096 4150 2331 O
ATOM 831 N ILE A 120 493.393 200.725 563.788 1.00 71.70 N
ANISOU 831 N ILE A 120 11876 7914 7454 -1326 4031 2078 N
ATOM 832 CA ILE A 120 492.048 201.277 563.722 1.00 83.17 C
ANISOU 832 CA ILE A 120 13199 9456 8946 -1511 4140 1782 C
ATOM 833 C ILE A 120 491.118 200.266 563.067 1.00 95.87 C
ANISOU 833 C ILE A 120 14860 10835 10730 -1604 4256 1705 C
ATOM 834 O ILE A 120 491.485 199.574 562.105 1.00 70.41 O
ANISOU 834 O ILE A 120 11705 7373 7675 -1488 4257 1750 O
ATOM 835 CB ILE A 120 492.052 202.628 562.982 1.00 80.05 C
ANISOU 835 CB ILE A 120 12591 9168 8654 -1453 4098 1547 C
ATOM 836 CG1 ILE A 120 493.235 203.478 563.461 1.00 81.62 C
ANISOU 836 CG1 ILE A 120 12770 9526 8716 -1339 3978 1671 C
ATOM 837 CG2 ILE A 120 490.736 203.375 563.211 1.00 90.53 C
ANISOU 837 CG2 ILE A 120 13772 10645 9980 -1632 4188 1256 C
ATOM 838 CD1 ILE A 120 493.085 204.965 563.164 1.00 89.83 C
ANISOU 838 CD1 ILE A 120 13607 10713 9811 -1348 3963 1436 C
ATOM 839 N GLY A 121 489.918 200.155 563.611 1.00 91.19 N
ANISOU 839 N GLY A 121 14242 10316 10091 -1813 4366 1590 N
ATOM 840 CA GLY A 121 488.903 199.268 563.060 1.00 77.18 C
ANISOU 840 CA GLY A 121 12500 8345 8479 -1943 4487 1497 C
ATOM 841 C GLY A 121 487.632 200.012 562.747 1.00 73.55 C
ANISOU 841 C GLY A 121 11842 8012 8093 -2082 4557 1182 C
ATOM 842 O GLY A 121 487.191 200.872 563.513 1.00 72.31 O
ANISOU 842 O GLY A 121 11569 8104 7800 -2156 4565 1084 O
ATOM 843 N VAL A 122 487.029 199.682 561.598 1.00 75.54 N
ANISOU 843 N VAL A 122 12048 8094 8558 -2111 4612 1014 N
ATOM 844 CA VAL A 122 485.720 200.201 561.212 1.00 80.98 C
ANISOU 844 CA VAL A 122 12547 8881 9341 -2249 4678 727 C
ATOM 845 C VAL A 122 484.826 199.010 560.905 1.00 93.53 C
ANISOU 845 C VAL A 122 14221 10267 11048 -2424 4805 705 C
ATOM 846 O VAL A 122 485.074 198.277 559.938 1.00 89.16 O
ANISOU 846 O VAL A 122 13764 9466 10648 -2379 4828 705 O
ATOM 847 CB VAL A 122 485.792 201.158 560.011 1.00 76.26 C
ANISOU 847 CB VAL A 122 11763 8321 8891 -2123 4608 513 C
ATOM 848 CG1 VAL A 122 484.417 201.750 559.720 1.00 71.62 C
ANISOU 848 CG1 VAL A 122 10963 7862 8389 -2256 4657 234 C
ATOM 849 CG2 VAL A 122 486.801 202.277 560.271 1.00 66.53 C
ANISOU 849 CG2 VAL A 122 10460 7251 7570 -1954 4483 564 C
ATOM 850 N THR A 123 483.781 198.831 561.712 1.00 98.02 N
ANISOU 850 N THR A 123 14751 10943 11549 -2626 4898 681 N
ATOM 851 CA THR A 123 483.006 197.600 561.750 1.00106.50 C
ANISOU 851 CA THR A 123 15926 11833 12706 -2822 5022 735 C
ATOM 852 C THR A 123 481.526 197.868 561.499 1.00106.89 C
ANISOU 852 C THR A 123 15778 11992 12842 -3010 5109 480 C
ATOM 853 O THR A 123 480.994 198.919 561.869 1.00104.00 O
ANISOU 853 O THR A 123 15222 11894 12399 -3017 5094 334 O
ATOM 854 CB THR A 123 483.205 196.899 563.108 1.00113.85 C
ANISOU 854 CB THR A 123 17011 12786 13460 -2902 5062 1037 C
ATOM 855 OG1 THR A 123 484.444 196.189 563.086 1.00130.04 O
ANISOU 855 OG1 THR A 123 19278 14627 15505 -2755 4997 1290 O
ATOM 856 CG2 THR A 123 482.109 195.906 563.408 1.00108.43 C
ANISOU 856 CG2 THR A 123 16357 12005 12838 -3152 5201 1081 C
ATOM 857 N ARG A 124 480.869 196.904 560.847 1.00109.13 N
ANISOU 857 N ARG A 124 16109 12059 13298 -3160 5198 423 N
ATOM 858 CA ARG A 124 479.426 196.917 560.644 1.00112.31 C
ANISOU 858 CA ARG A 124 16336 12544 13793 -3369 5289 217 C
ATOM 859 C ARG A 124 478.651 196.229 561.764 1.00114.23 C
ANISOU 859 C ARG A 124 16612 12835 13957 -3590 5405 376 C
ATOM 860 O ARG A 124 477.500 196.599 562.018 1.00121.13 O
ANISOU 860 O ARG A 124 17295 13904 14825 -3732 5472 239 O
ATOM 861 CB ARG A 124 479.078 196.253 559.307 1.00116.07 C
ANISOU 861 CB ARG A 124 16825 12775 14501 -3440 5328 50 C
ATOM 862 N ARG A 125 479.244 195.236 562.433 1.00114.93 N
ANISOU 862 N ARG A 125 16925 12755 13989 -3616 5431 678 N
ATOM 863 CA ARG A 125 478.639 194.593 563.599 1.00114.20 C
ANISOU 863 CA ARG A 125 16865 12728 13799 -3811 5538 893 C
ATOM 864 C ARG A 125 478.861 195.420 564.865 1.00121.38 C
ANISOU 864 C ARG A 125 17715 13975 14428 -3741 5523 1005 C
ATOM 865 O ARG A 125 479.202 196.605 564.780 1.00 88.54 O
ANISOU 865 O ARG A 125 13445 10012 10184 -3579 5438 846 O
ATOM 866 CB ARG A 125 479.205 193.182 563.779 1.00114.97 C
ANISOU 866 CB ARG A 125 17225 12495 13965 -3859 5561 1194 C
ATOM 867 N GLU A 126 478.673 194.813 566.041 1.00 95.12 N
ANISOU 867 N GLU A 126 14460 10723 10958 -3865 5608 1279 N
ATOM 868 CA GLU A 126 478.841 195.541 567.293 1.00115.05 C
ANISOU 868 CA GLU A 126 16932 13591 13190 -3812 5616 1383 C
ATOM 869 C GLU A 126 480.310 195.585 567.701 1.00118.76 C
ANISOU 869 C GLU A 126 17579 14038 13506 -3611 5495 1601 C
ATOM 870 O GLU A 126 481.083 194.665 567.425 1.00113.45 O
ANISOU 870 O GLU A 126 17103 13081 12923 -3563 5447 1807 O
ATOM 871 CB GLU A 126 478.005 194.912 568.410 1.00131.06 C
ANISOU 871 CB GLU A 126 18941 15757 15100 -4025 5770 1601 C
ATOM 872 N VAL A 127 480.685 196.674 568.380 1.00125.36 N
ANISOU 872 N VAL A 127 18340 15179 14112 -3492 5447 1551 N
ATOM 873 CA VAL A 127 482.090 196.962 568.649 1.00124.69 C
ANISOU 873 CA VAL A 127 18381 15111 13884 -3288 5311 1697 C
ATOM 874 C VAL A 127 482.730 195.934 569.571 1.00124.99 C
ANISOU 874 C VAL A 127 18618 15098 13775 -3306 5318 2112 C
ATOM 875 O VAL A 127 483.957 195.777 569.560 1.00122.00 O
ANISOU 875 O VAL A 127 18380 14622 13351 -3143 5194 2286 O
ATOM 876 CB VAL A 127 482.236 198.383 569.234 1.00121.92 C
ANISOU 876 CB VAL A 127 17897 15109 13317 -3190 5272 1527 C
ATOM 877 N HIS A 128 481.930 195.226 570.374 1.00126.55 N
ANISOU 877 N HIS A 128 18819 15366 13900 -3497 5456 2295 N
ATOM 878 CA HIS A 128 482.486 194.229 571.286 1.00126.98 C
ANISOU 878 CA HIS A 128 19049 15382 13817 -3520 5462 2724 C
ATOM 879 C HIS A 128 483.108 193.067 570.521 1.00103.59 C
ANISOU 879 C HIS A 128 16280 11977 11104 -3486 5396 2897 C
ATOM 880 O HIS A 128 484.232 192.645 570.818 1.00104.27 O
ANISOU 880 O HIS A 128 16527 11975 11114 -3350 5291 3168 O
ATOM 881 CB HIS A 128 481.409 193.704 572.240 1.00136.44 C
ANISOU 881 CB HIS A 128 20186 16746 14907 -3745 5640 2896 C
ATOM 882 CG HIS A 128 480.336 194.696 572.568 1.00143.58 C
ANISOU 882 CG HIS A 128 20865 17991 15698 -3821 5753 2619 C
ATOM 883 ND1 HIS A 128 479.103 194.690 571.952 1.00146.32 N
ANISOU 883 ND1 HIS A 128 21060 18282 16253 -3979 5856 2384 N
ATOM 884 CD2 HIS A 128 480.303 195.709 573.467 1.00146.26 C
ANISOU 884 CD2 HIS A 128 21104 18731 15737 -3756 5780 2537 C
ATOM 885 CE1 HIS A 128 478.360 195.663 572.449 1.00147.36 C
ANISOU 885 CE1 HIS A 128 21002 18762 16228 -3996 5939 2178 C
ATOM 886 NE2 HIS A 128 479.065 196.296 573.370 1.00147.56 N
ANISOU 886 NE2 HIS A 128 21062 19060 15945 -3861 5899 2256 N
ATOM 887 N ILE A 129 482.386 192.536 569.533 1.00103.71 N
ANISOU 887 N ILE A 129 16280 11710 11416 -3602 5456 2736 N
ATOM 888 CA ILE A 129 482.821 191.318 568.854 1.00110.88 C
ANISOU 888 CA ILE A 129 17382 12174 12573 -3595 5424 2888 C
ATOM 889 C ILE A 129 484.087 191.569 568.041 1.00101.04 C
ANISOU 889 C ILE A 129 16236 10759 11395 -3327 5269 2824 C
ATOM 890 O ILE A 129 485.034 190.775 568.085 1.00102.35 O
ANISOU 890 O ILE A 129 16593 10694 11600 -3212 5194 3089 O
ATOM 891 CB ILE A 129 481.688 190.762 567.974 1.00113.71 C
ANISOU 891 CB ILE A 129 17688 12295 13221 -3797 5532 2687 C
ATOM 892 CG1 ILE A 129 480.401 190.624 568.789 1.00117.62 C
ANISOU 892 CG1 ILE A 129 18047 13002 13643 -4059 5689 2746 C
ATOM 893 CG2 ILE A 129 482.088 189.421 567.372 1.00114.92 C
ANISOU 893 CG2 ILE A 129 18061 11971 13634 -3806 5513 2849 C
ATOM 894 CD1 ILE A 129 479.378 191.690 568.486 1.00114.44 C
ANISOU 894 CD1 ILE A 129 17389 12865 13226 -4124 5749 2371 C
ATOM 895 N TYR A 130 484.127 192.667 567.279 1.00 99.81 N
ANISOU 895 N TYR A 130 15944 10715 11264 -3216 5218 2488 N
ATOM 896 CA TYR A 130 485.274 192.877 566.398 1.00 98.37 C
ANISOU 896 CA TYR A 130 15837 10368 11171 -2968 5087 2432 C
ATOM 897 C TYR A 130 486.552 193.102 567.194 1.00 97.45 C
ANISOU 897 C TYR A 130 15806 10389 10831 -2779 4959 2697 C
ATOM 898 O TYR A 130 487.617 192.603 566.812 1.00 93.70 O
ANISOU 898 O TYR A 130 15478 9691 10433 -2598 4864 2849 O
ATOM 899 CB TYR A 130 485.037 194.050 565.449 1.00106.84 C
ANISOU 899 CB TYR A 130 16725 11556 12313 -2896 5058 2049 C
ATOM 900 CG TYR A 130 486.249 194.377 564.591 1.00101.76 C
ANISOU 900 CG TYR A 130 16131 10795 11737 -2633 4929 2015 C
ATOM 901 CD1 TYR A 130 486.837 195.634 564.641 1.00110.27 C
ANISOU 901 CD1 TYR A 130 17086 12126 12687 -2482 4825 1915 C
ATOM 902 CD2 TYR A 130 486.802 193.433 563.731 1.00106.95 C
ANISOU 902 CD2 TYR A 130 16955 11087 12595 -2535 4918 2084 C
ATOM 903 CE1 TYR A 130 487.940 195.948 563.862 1.00109.19 C
ANISOU 903 CE1 TYR A 130 16972 11900 12614 -2246 4712 1908 C
ATOM 904 CE2 TYR A 130 487.914 193.741 562.943 1.00104.80 C
ANISOU 904 CE2 TYR A 130 16713 10730 12375 -2278 4814 2065 C
ATOM 905 CZ TYR A 130 488.476 195.002 563.017 1.00103.23 C
ANISOU 905 CZ TYR A 130 16372 10808 12043 -2139 4710 1988 C
ATOM 906 OH TYR A 130 489.574 195.330 562.251 1.00106.31 O
ANISOU 906 OH TYR A 130 16768 11136 12487 -1889 4610 1993 O
ATOM 907 N TYR A 131 486.468 193.846 568.303 1.00101.84 N
ANISOU 907 N TYR A 131 16270 11319 11106 -2814 4958 2749 N
ATOM 908 CA TYR A 131 487.652 194.055 569.131 1.00101.71 C
ANISOU 908 CA TYR A 131 16329 11464 10851 -2657 4835 3003 C
ATOM 909 C TYR A 131 488.234 192.721 569.582 1.00113.05 C
ANISOU 909 C TYR A 131 17973 12680 12300 -2641 4809 3407 C
ATOM 910 O TYR A 131 489.455 192.526 569.546 1.00116.05 O
ANISOU 910 O TYR A 131 18462 12974 12658 -2442 4672 3593 O
ATOM 911 CB TYR A 131 487.311 194.954 570.327 1.00 98.07 C
ANISOU 911 CB TYR A 131 15749 11445 10068 -2730 4871 2987 C
ATOM 912 CG TYR A 131 488.498 195.341 571.206 1.00110.28 C
ANISOU 912 CG TYR A 131 17354 13217 11329 -2580 4741 3205 C
ATOM 913 CD1 TYR A 131 489.146 194.400 572.008 1.00119.41 C
ANISOU 913 CD1 TYR A 131 18668 14346 12357 -2557 4696 3617 C
ATOM 914 CD2 TYR A 131 488.986 196.642 571.210 1.00 93.66 C
ANISOU 914 CD2 TYR A 131 15146 11347 9092 -2464 4655 3004 C
ATOM 915 CE1 TYR A 131 490.226 194.746 572.801 1.00115.16 C
ANISOU 915 CE1 TYR A 131 18174 14035 11545 -2424 4565 3818 C
ATOM 916 CE2 TYR A 131 490.075 197.000 571.997 1.00 98.45 C
ANISOU 916 CE2 TYR A 131 15809 12165 9432 -2340 4532 3193 C
ATOM 917 CZ TYR A 131 490.689 196.046 572.794 1.00111.19 C
ANISOU 917 CZ TYR A 131 17572 13773 10902 -2318 4484 3599 C
ATOM 918 OH TYR A 131 491.769 196.390 573.581 1.00107.18 O
ANISOU 918 OH TYR A 131 17112 13498 10112 -2198 4349 3792 O
ATOM 919 N LEU A 132 487.374 191.786 569.996 1.00105.14 N
ANISOU 919 N LEU A 132 17019 11580 11349 -2848 4935 3557 N
ATOM 920 CA LEU A 132 487.840 190.444 570.332 1.00109.47 C
ANISOU 920 CA LEU A 132 17766 11863 11965 -2847 4914 3942 C
ATOM 921 C LEU A 132 488.613 189.830 569.171 1.00107.02 C
ANISOU 921 C LEU A 132 17597 11127 11939 -2667 4831 3915 C
ATOM 922 O LEU A 132 489.743 189.361 569.343 1.00105.66 O
ANISOU 922 O LEU A 132 17561 10839 11747 -2483 4709 4175 O
ATOM 923 CB LEU A 132 486.655 189.557 570.724 1.00109.88 C
ANISOU 923 CB LEU A 132 17826 11823 12099 -3123 5075 4061 C
ATOM 924 N GLU A 133 488.021 189.839 567.974 1.00102.52 N
ANISOU 924 N GLU A 133 16988 10338 11628 -2705 4898 3595 N
ATOM 925 CA GLU A 133 488.715 189.313 566.803 1.00116.72 C
ANISOU 925 CA GLU A 133 18911 11753 13683 -2520 4842 3531 C
ATOM 926 C GLU A 133 489.995 190.092 566.523 1.00124.99 C
ANISOU 926 C GLU A 133 19938 12919 14636 -2225 4689 3513 C
ATOM 927 O GLU A 133 491.028 189.502 566.183 1.00130.72 O
ANISOU 927 O GLU A 133 20802 13408 15456 -2011 4599 3674 O
ATOM 928 CB GLU A 133 487.790 189.347 565.587 1.00119.21 C
ANISOU 928 CB GLU A 133 19160 11887 14246 -2627 4947 3161 C
ATOM 929 CG GLU A 133 486.425 188.724 565.822 1.00131.19 C
ANISOU 929 CG GLU A 133 20653 13331 15861 -2942 5096 3138 C
ATOM 930 CD GLU A 133 485.553 188.764 564.584 1.00142.11 C
ANISOU 930 CD GLU A 133 21962 14550 17484 -3048 5182 2763 C
ATOM 931 OE1 GLU A 133 484.357 189.105 564.706 1.00148.52 O
ANISOU 931 OE1 GLU A 133 22613 15535 18284 -3274 5281 2592 O
ATOM 932 OE2 GLU A 133 486.066 188.457 563.487 1.00146.28 O
ANISOU 932 OE2 GLU A 133 22586 14790 18205 -2900 5152 2640 O
ATOM 933 N LYS A 134 489.949 191.420 566.666 1.00125.48 N
ANISOU 933 N LYS A 134 19818 13340 14519 -2207 4655 3321 N
ATOM 934 CA LYS A 134 491.138 192.229 566.413 1.00125.32 C
ANISOU 934 CA LYS A 134 19754 13445 14415 -1951 4506 3307 C
ATOM 935 C LYS A 134 492.215 191.976 567.462 1.00130.92 C
ANISOU 935 C LYS A 134 20557 14268 14917 -1830 4378 3679 C
ATOM 936 O LYS A 134 493.404 191.903 567.132 1.00135.60 O
ANISOU 936 O LYS A 134 21206 14773 15542 -1585 4249 3795 O
ATOM 937 CB LYS A 134 490.765 193.712 566.367 1.00115.06 C
ANISOU 937 CB LYS A 134 18238 12486 12994 -1985 4501 3016 C
ATOM 938 N ALA A 135 491.822 191.836 568.730 1.00134.04 N
ANISOU 938 N ALA A 135 20961 14879 15090 -1994 4412 3878 N
ATOM 939 CA ALA A 135 492.801 191.544 569.772 1.00136.89 C
ANISOU 939 CA ALA A 135 21411 15368 15231 -1897 4288 4251 C
ATOM 940 C ALA A 135 493.273 190.096 569.709 1.00144.51 C
ANISOU 940 C ALA A 135 22579 15963 16367 -1825 4259 4560 C
ATOM 941 O ALA A 135 494.399 189.795 570.122 1.00142.54 O
ANISOU 941 O ALA A 135 22414 15716 16029 -1648 4113 4839 O
ATOM 942 CB ALA A 135 492.219 191.858 571.149 1.00126.29 C
ANISOU 942 CB ALA A 135 20011 14404 13570 -2090 4345 4373 C
ATOM 943 N ASN A 136 492.428 189.194 569.201 1.00148.11 N
ANISOU 943 N ASN A 136 23112 16091 17073 -1962 4391 4511 N
ATOM 944 CA ASN A 136 492.832 187.803 569.015 1.00153.89 C
ANISOU 944 CA ASN A 136 24044 16408 18018 -1889 4372 4767 C
ATOM 945 C ASN A 136 494.041 187.712 568.089 1.00147.21 C
ANISOU 945 C ASN A 136 23261 15345 17328 -1564 4250 4737 C
ATOM 946 O ASN A 136 495.037 187.051 568.408 1.00148.04 O
ANISOU 946 O ASN A 136 23486 15329 17435 -1384 4132 5038 O
ATOM 947 CB ASN A 136 491.644 186.997 568.474 1.00159.65 C
ANISOU 947 CB ASN A 136 24828 16819 19015 -2108 4540 4642 C
ATOM 948 CG ASN A 136 492.059 185.739 567.722 1.00163.78 C
ANISOU 948 CG ASN A 136 25548 16823 19859 -1986 4529 4735 C
ATOM 949 OD1 ASN A 136 492.975 185.023 568.127 1.00169.71 O
ANISOU 949 OD1 ASN A 136 26436 17432 20615 -1828 4422 5058 O
ATOM 950 ND2 ASN A 136 491.371 185.465 566.617 1.00160.69 N
ANISOU 950 ND2 ASN A 136 25172 16144 19739 -2057 4637 4441 N
ATOM 951 N LYS A 137 493.984 188.393 566.947 1.00142.08 N
ANISOU 951 N LYS A 137 22517 14663 16802 -1475 4276 4385 N
ATOM 952 CA LYS A 137 495.114 188.459 566.029 1.00138.82 C
ANISOU 952 CA LYS A 137 22125 14107 16514 -1155 4175 4341 C
ATOM 953 C LYS A 137 496.210 189.409 566.505 1.00135.29 C
ANISOU 953 C LYS A 137 21569 14007 15829 -971 4005 4441 C
ATOM 954 O LYS A 137 497.159 189.661 565.755 1.00133.99 O
ANISOU 954 O LYS A 137 21371 13795 15745 -705 3916 4395 O
ATOM 955 CB LYS A 137 494.637 188.877 564.634 1.00133.81 C
ANISOU 955 CB LYS A 137 21419 13345 16078 -1137 4271 3947 C
ATOM 956 N ILE A 138 496.102 189.936 567.721 1.00137.93 N
ANISOU 956 N ILE A 138 21841 14696 15872 -1108 3960 4576 N
ATOM 957 CA ILE A 138 497.101 190.853 568.257 1.00133.19 C
ANISOU 957 CA ILE A 138 21142 14435 15029 -968 3794 4665 C
ATOM 958 C ILE A 138 497.608 190.346 569.603 1.00129.97 C
ANISOU 958 C ILE A 138 20826 14168 14388 -987 3693 5060 C
ATOM 959 O ILE A 138 498.783 190.008 569.748 1.00125.51 O
ANISOU 959 O ILE A 138 20317 13566 13806 -766 3537 5295 O
ATOM 960 CB ILE A 138 496.535 192.278 568.391 1.00130.92 C
ANISOU 960 CB ILE A 138 20668 14506 14570 -1104 3827 4386 C
ATOM 961 N GLU A 141 499.944 192.640 570.414 1.00139.18 N
ANISOU 961 N GLU A 141 21749 16076 15056 -668 3294 5134 N
ATOM 962 CA GLU A 141 499.982 192.392 571.851 1.00141.71 C
ANISOU 962 CA GLU A 141 22146 16637 15062 -794 3242 5419 C
ATOM 963 C GLU A 141 500.205 193.683 572.629 1.00137.28 C
ANISOU 963 C GLU A 141 21473 16533 14153 -856 3162 5348 C
ATOM 964 O GLU A 141 499.635 193.880 573.701 1.00140.64 O
ANISOU 964 O GLU A 141 21911 17240 14288 -1054 3216 5406 O
ATOM 965 CB GLU A 141 501.079 191.381 572.192 1.00146.65 C
ANISOU 965 CB GLU A 141 22902 17118 15700 -603 3085 5794 C
ATOM 966 N LYS A 142 501.041 194.563 572.080 1.00130.73 N
ANISOU 966 N LYS A 142 20533 15785 13355 -682 3040 5223 N
ATOM 967 CA LYS A 142 501.401 195.810 572.739 1.00124.43 C
ANISOU 967 CA LYS A 142 19642 15387 12248 -714 2945 5154 C
ATOM 968 C LYS A 142 500.958 197.050 571.974 1.00109.85 C
ANISOU 968 C LYS A 142 17640 13604 10493 -748 3023 4776 C
ATOM 969 O LYS A 142 501.146 198.166 572.472 1.00102.37 O
ANISOU 969 O LYS A 142 16622 12968 9304 -788 2970 4676 O
ATOM 970 CB LYS A 142 502.917 195.869 572.967 1.00126.67 C
ANISOU 970 CB LYS A 142 19927 15762 12442 -482 2695 5388 C
ATOM 971 N THR A 143 500.382 196.894 570.788 1.00 99.80 N
ANISOU 971 N THR A 143 16321 12046 9552 -734 3145 4559 N
ATOM 972 CA THR A 143 499.897 198.028 570.020 1.00101.61 C
ANISOU 972 CA THR A 143 16404 12318 9887 -776 3221 4205 C
ATOM 973 C THR A 143 498.476 198.384 570.442 1.00 97.77 C
ANISOU 973 C THR A 143 15894 11951 9301 -1040 3410 3973 C
ATOM 974 O THR A 143 497.677 197.517 570.807 1.00 91.81 O
ANISOU 974 O THR A 143 15223 11111 8548 -1175 3525 4044 O
ATOM 975 CB THR A 143 499.943 197.722 568.521 1.00108.73 C
ANISOU 975 CB THR A 143 17256 12890 11168 -631 3258 4075 C
ATOM 976 OG1 THR A 143 498.894 196.805 568.186 1.00121.35 O
ANISOU 976 OG1 THR A 143 18938 14239 12932 -751 3424 4003 O
ATOM 977 CG2 THR A 143 501.283 197.101 568.151 1.00105.12 C
ANISOU 977 CG2 THR A 143 16827 12294 10820 -351 3096 4328 C
ATOM 978 N HIS A 144 498.170 199.678 570.396 1.00 90.35 N
ANISOU 978 N HIS A 144 14835 11209 8284 -1109 3442 3698 N
ATOM 979 CA HIS A 144 496.865 200.167 570.820 1.00 91.62 C
ANISOU 979 CA HIS A 144 14948 11519 8345 -1334 3613 3442 C
ATOM 980 C HIS A 144 495.807 199.877 569.760 1.00 95.06 C
ANISOU 980 C HIS A 144 15321 11695 9104 -1406 3758 3207 C
ATOM 981 O HIS A 144 496.090 199.844 568.560 1.00 83.28 O
ANISOU 981 O HIS A 144 13779 9974 7889 -1280 3729 3129 O
ATOM 982 CB HIS A 144 496.926 201.666 571.110 1.00 85.06 C
ANISOU 982 CB HIS A 144 14022 10963 7333 -1374 3598 3201 C
ATOM 983 CG HIS A 144 496.154 202.075 572.325 1.00 92.31 C
ANISOU 983 CG HIS A 144 14957 12193 7923 -1556 3698 3094 C
ATOM 984 ND1 HIS A 144 496.496 201.665 573.596 1.00100.39 N
ANISOU 984 ND1 HIS A 144 16092 13455 8596 -1576 3650 3352 N
ATOM 985 CD2 HIS A 144 495.057 202.856 572.463 1.00 96.75 C
ANISOU 985 CD2 HIS A 144 15426 12884 8450 -1711 3842 2752 C
ATOM 986 CE1 HIS A 144 495.642 202.177 574.465 1.00103.35 C
ANISOU 986 CE1 HIS A 144 16447 14103 8719 -1729 3771 3167 C
ATOM 987 NE2 HIS A 144 494.758 202.902 573.803 1.00 97.58 N
ANISOU 987 NE2 HIS A 144 15591 13303 8182 -1813 3888 2795 N
ATOM 988 N ILE A 145 494.575 199.667 570.219 1.00 84.66 N
ANISOU 988 N ILE A 145 13997 10436 7734 -1604 3915 3099 N
ATOM 989 CA ILE A 145 493.467 199.250 569.367 1.00 89.70 C
ANISOU 989 CA ILE A 145 14589 10846 8645 -1700 4053 2905 C
ATOM 990 C ILE A 145 492.311 200.226 569.556 1.00 85.54 C
ANISOU 990 C ILE A 145 13916 10522 8065 -1864 4174 2570 C
ATOM 991 O ILE A 145 491.917 200.510 570.693 1.00 85.68 O
ANISOU 991 O ILE A 145 13934 10812 7809 -1975 4231 2577 O
ATOM 992 CB ILE A 145 493.017 197.811 569.691 1.00 95.17 C
ANISOU 992 CB ILE A 145 15419 11363 9378 -1789 4132 3136 C
ATOM 993 CG1 ILE A 145 494.212 196.856 569.720 1.00103.43 C
ANISOU 993 CG1 ILE A 145 16619 12234 10445 -1618 4002 3490 C
ATOM 994 CG2 ILE A 145 492.018 197.324 568.676 1.00 85.86 C
ANISOU 994 CG2 ILE A 145 14212 9913 8498 -1875 4256 2941 C
ATOM 995 CD1 ILE A 145 493.811 195.386 569.795 1.00 92.48 C
ANISOU 995 CD1 ILE A 145 15378 10581 9178 -1690 4080 3704 C
ATOM 996 N HIS A 146 491.765 200.731 568.448 1.00 86.31 N
ANISOU 996 N HIS A 146 13882 10497 8415 -1866 4214 2278 N
ATOM 997 CA HIS A 146 490.653 201.682 568.468 1.00 82.03 C
ANISOU 997 CA HIS A 146 13176 10114 7876 -1996 4315 1941 C
ATOM 998 C HIS A 146 489.656 201.288 567.386 1.00 87.95 C
ANISOU 998 C HIS A 146 13850 10644 8923 -2060 4402 1758 C
ATOM 999 O HIS A 146 490.004 201.276 566.200 1.00 93.18 O
ANISOU 999 O HIS A 146 14480 11107 9818 -1947 4349 1697 O
ATOM 1000 CB HIS A 146 491.149 203.119 568.245 1.00 87.10 C
ANISOU 1000 CB HIS A 146 13697 10901 8496 -1916 4238 1738 C
ATOM 1001 CG HIS A 146 490.158 204.175 568.636 1.00 88.14 C
ANISOU 1001 CG HIS A 146 13684 11249 8556 -2039 4332 1418 C
ATOM 1002 ND1 HIS A 146 490.523 205.338 569.282 1.00 76.19 N
ANISOU 1002 ND1 HIS A 146 12133 9974 6841 -2036 4301 1285 N
ATOM 1003 CD2 HIS A 146 488.815 204.244 568.470 1.00 85.99 C
ANISOU 1003 CD2 HIS A 146 13293 10987 8390 -2163 4454 1193 C
ATOM 1004 CE1 HIS A 146 489.448 206.076 569.497 1.00 85.84 C
ANISOU 1004 CE1 HIS A 146 13220 11336 8058 -2142 4404 982 C
ATOM 1005 NE2 HIS A 146 488.399 205.434 569.016 1.00 82.20 N
ANISOU 1005 NE2 HIS A 146 12700 10748 7785 -2213 4493 935 N
ATOM 1006 N ILE A 147 488.420 200.984 567.791 1.00 91.09 N
ANISOU 1006 N ILE A 147 14212 11098 9302 -2240 4539 1672 N
ATOM 1007 CA ILE A 147 487.376 200.494 566.893 1.00 82.22 C
ANISOU 1007 CA ILE A 147 13027 9782 8430 -2335 4631 1516 C
ATOM 1008 C ILE A 147 486.315 201.573 566.718 1.00 79.03 C
ANISOU 1008 C ILE A 147 12407 9548 8073 -2414 4689 1171 C
ATOM 1009 O ILE A 147 485.879 202.191 567.696 1.00 79.87 O
ANISOU 1009 O ILE A 147 12451 9916 7981 -2488 4743 1099 O
ATOM 1010 CB ILE A 147 486.736 199.191 567.418 1.00 91.41 C
ANISOU 1010 CB ILE A 147 14311 10848 9573 -2493 4745 1710 C
ATOM 1011 CG1 ILE A 147 487.508 197.953 566.959 1.00110.37 C
ANISOU 1011 CG1 ILE A 147 16906 12932 12098 -2412 4700 1967 C
ATOM 1012 CG2 ILE A 147 485.297 199.069 566.943 1.00 84.67 C
ANISOU 1012 CG2 ILE A 147 13335 9951 8885 -2663 4873 1482 C
ATOM 1013 CD1 ILE A 147 488.948 197.909 567.332 1.00118.42 C
ANISOU 1013 CD1 ILE A 147 18045 13964 12986 -2230 4563 2222 C
ATOM 1014 N PHE A 148 485.901 201.801 565.471 1.00 81.76 N
ANISOU 1014 N PHE A 148 12636 9753 8675 -2388 4680 959 N
ATOM 1015 CA PHE A 148 484.762 202.652 565.162 1.00 82.88 C
ANISOU 1015 CA PHE A 148 12564 10015 8910 -2463 4733 647 C
ATOM 1016 C PHE A 148 483.672 201.822 564.492 1.00 87.82 C
ANISOU 1016 C PHE A 148 13161 10484 9721 -2597 4828 569 C
ATOM 1017 O PHE A 148 483.956 200.839 563.801 1.00 74.96 O
ANISOU 1017 O PHE A 148 11654 8604 8224 -2585 4827 677 O
ATOM 1018 CB PHE A 148 485.160 203.816 564.245 1.00 84.61 C
ANISOU 1018 CB PHE A 148 12632 10246 9270 -2316 4627 453 C
ATOM 1019 CG PHE A 148 486.058 204.830 564.897 1.00 80.19 C
ANISOU 1019 CG PHE A 148 12065 9859 8546 -2220 4551 468 C
ATOM 1020 CD1 PHE A 148 487.411 204.862 564.601 1.00 72.20 C
ANISOU 1020 CD1 PHE A 148 11139 8765 7530 -2066 4438 635 C
ATOM 1021 CD2 PHE A 148 485.553 205.749 565.806 1.00 79.29 C
ANISOU 1021 CD2 PHE A 148 11859 9991 8279 -2285 4600 306 C
ATOM 1022 CE1 PHE A 148 488.249 205.792 565.197 1.00 68.53 C
ANISOU 1022 CE1 PHE A 148 10670 8456 6911 -2000 4373 647 C
ATOM 1023 CE2 PHE A 148 486.387 206.687 566.406 1.00 81.40 C
ANISOU 1023 CE2 PHE A 148 12135 10409 8386 -2216 4542 290 C
ATOM 1024 CZ PHE A 148 487.738 206.707 566.099 1.00 69.57 C
ANISOU 1024 CZ PHE A 148 10726 8823 6886 -2084 4428 463 C
ATOM 1025 N SER A 149 482.415 202.214 564.708 1.00 87.29 N
ANISOU 1025 N SER A 149 12935 10566 9666 -2727 4917 373 N
ATOM 1026 CA SER A 149 481.283 201.544 564.081 1.00 84.81 C
ANISOU 1026 CA SER A 149 12561 10137 9525 -2874 5008 272 C
ATOM 1027 C SER A 149 480.448 202.549 563.298 1.00 79.61 C
ANISOU 1027 C SER A 149 11656 9572 9020 -2858 4986 -41 C
ATOM 1028 O SER A 149 480.495 203.760 563.539 1.00 82.57 O
ANISOU 1028 O SER A 149 11898 10130 9344 -2770 4935 -178 O
ATOM 1029 CB SER A 149 480.392 200.826 565.109 1.00 90.16 C
ANISOU 1029 CB SER A 149 13271 10903 10082 -3077 5155 381 C
ATOM 1030 OG SER A 149 479.937 201.722 566.104 1.00 95.38 O
ANISOU 1030 OG SER A 149 13812 11868 10560 -3098 5199 295 O
ATOM 1031 N PHE A 150 479.678 202.021 562.348 1.00 74.76 N
ANISOU 1031 N PHE A 150 10982 8824 8598 -2945 5026 -153 N
ATOM 1032 CA PHE A 150 478.740 202.819 561.570 1.00 93.51 C
ANISOU 1032 CA PHE A 150 13115 11291 11125 -2947 5009 -429 C
ATOM 1033 C PHE A 150 477.509 203.230 562.366 1.00 97.48 C
ANISOU 1033 C PHE A 150 13458 12020 11558 -3077 5106 -544 C
ATOM 1034 O PHE A 150 476.641 203.918 561.818 1.00102.71 O
ANISOU 1034 O PHE A 150 13906 12779 12342 -3077 5094 -766 O
ATOM 1035 CB PHE A 150 478.307 202.049 560.318 1.00 84.76 C
ANISOU 1035 CB PHE A 150 11997 9986 10222 -3015 5029 -511 C
ATOM 1036 CG PHE A 150 479.365 201.977 559.258 1.00 90.09 C
ANISOU 1036 CG PHE A 150 12751 10486 10994 -2850 4931 -481 C
ATOM 1037 CD1 PHE A 150 480.267 200.928 559.236 1.00 91.55 C
ANISOU 1037 CD1 PHE A 150 13180 10445 11160 -2830 4950 -274 C
ATOM 1038 CD2 PHE A 150 479.464 202.962 558.288 1.00 76.83 C
ANISOU 1038 CD2 PHE A 150 10894 8870 9426 -2702 4825 -642 C
ATOM 1039 CE1 PHE A 150 481.246 200.858 558.265 1.00 82.45 C
ANISOU 1039 CE1 PHE A 150 12095 9143 10090 -2664 4878 -244 C
ATOM 1040 CE2 PHE A 150 480.443 202.898 557.311 1.00 84.97 C
ANISOU 1040 CE2 PHE A 150 11984 9768 10535 -2544 4749 -597 C
ATOM 1041 CZ PHE A 150 481.335 201.844 557.301 1.00 86.54 C
ANISOU 1041 CZ PHE A 150 12426 9751 10704 -2523 4783 -405 C
ATOM 1042 N THR A 151 477.402 202.826 563.632 1.00 86.12 N
ANISOU 1042 N THR A 151 12113 10684 9925 -3178 5206 -390 N
ATOM 1043 CA THR A 151 476.291 203.230 564.481 1.00 94.16 C
ANISOU 1043 CA THR A 151 12981 11948 10848 -3285 5317 -484 C
ATOM 1044 C THR A 151 476.715 204.206 565.572 1.00 94.44 C
ANISOU 1044 C THR A 151 13006 12213 10664 -3188 5308 -492 C
ATOM 1045 O THR A 151 475.909 204.528 566.450 1.00 99.59 O
ANISOU 1045 O THR A 151 13557 13092 11191 -3261 5418 -553 O
ATOM 1046 CB THR A 151 475.620 202.003 565.105 1.00 84.26 C
ANISOU 1046 CB THR A 151 11806 10675 9536 -3503 5470 -310 C
ATOM 1047 OG1 THR A 151 476.366 201.573 566.251 1.00 88.36 O
ANISOU 1047 OG1 THR A 151 12511 11238 9821 -3504 5505 -45 O
ATOM 1048 CG2 THR A 151 475.538 200.865 564.093 1.00 84.30 C
ANISOU 1048 CG2 THR A 151 11896 10390 9743 -3601 5474 -263 C
ATOM 1049 N GLY A 152 477.959 204.678 565.545 1.00 82.14 N
ANISOU 1049 N GLY A 152 11546 10613 9052 -3028 5191 -440 N
ATOM 1050 CA GLY A 152 478.410 205.687 566.481 1.00 86.22 C
ANISOU 1050 CA GLY A 152 12050 11339 9372 -2940 5175 -490 C
ATOM 1051 C GLY A 152 479.130 205.176 567.710 1.00 93.68 C
ANISOU 1051 C GLY A 152 13191 12374 10030 -2966 5219 -244 C
ATOM 1052 O GLY A 152 479.515 205.986 568.561 1.00101.65 O
ANISOU 1052 O GLY A 152 14201 13581 10839 -2903 5215 -298 O
ATOM 1053 N GLU A 153 479.327 203.870 567.840 1.00100.20 N
ANISOU 1053 N GLU A 153 14183 13064 10824 -3055 5261 22 N
ATOM 1054 CA GLU A 153 480.018 203.324 568.996 1.00107.02 C
ANISOU 1054 CA GLU A 153 15231 14017 11413 -3071 5293 297 C
ATOM 1055 C GLU A 153 481.518 203.250 568.740 1.00100.83 C
ANISOU 1055 C GLU A 153 14613 13091 10608 -2924 5147 456 C
ATOM 1056 O GLU A 153 481.969 203.073 567.606 1.00 93.10 O
ANISOU 1056 O GLU A 153 13651 11872 9849 -2848 5053 442 O
ATOM 1057 CB GLU A 153 479.478 201.937 569.346 1.00117.67 C
ANISOU 1057 CB GLU A 153 16675 15289 12746 -3243 5413 541 C
ATOM 1058 CG GLU A 153 478.004 201.745 569.021 1.00129.70 C
ANISOU 1058 CG GLU A 153 18029 16829 14421 -3400 5535 390 C
ATOM 1059 CD GLU A 153 477.577 200.288 569.064 1.00137.55 C
ANISOU 1059 CD GLU A 153 19124 17659 15479 -3580 5636 631 C
ATOM 1060 OE1 GLU A 153 476.363 200.029 569.201 1.00135.79 O
ANISOU 1060 OE1 GLU A 153 18775 17518 15303 -3743 5769 578 O
ATOM 1061 OE2 GLU A 153 478.454 199.403 568.960 1.00141.43 O
ANISOU 1061 OE2 GLU A 153 19817 17934 15985 -3559 5583 877 O
ATOM 1062 N GLU A 154 482.291 203.395 569.812 1.00 97.75 N
ANISOU 1062 N GLU A 154 14335 12870 9934 -2880 5131 610 N
ATOM 1063 CA GLU A 154 483.734 203.238 569.738 1.00 96.02 C
ANISOU 1063 CA GLU A 154 14277 12548 9658 -2749 4998 807 C
ATOM 1064 C GLU A 154 484.226 202.521 570.984 1.00102.53 C
ANISOU 1064 C GLU A 154 15274 13503 10181 -2782 5030 1128 C
ATOM 1065 O GLU A 154 483.627 202.621 572.058 1.00110.00 O
ANISOU 1065 O GLU A 154 16193 14708 10894 -2869 5142 1134 O
ATOM 1066 CB GLU A 154 484.450 204.585 569.587 1.00 94.78 C
ANISOU 1066 CB GLU A 154 14051 12489 9473 -2613 4890 612 C
ATOM 1067 CG GLU A 154 484.258 205.519 570.764 1.00 94.58 C
ANISOU 1067 CG GLU A 154 13978 12794 9164 -2635 4944 469 C
ATOM 1068 CD GLU A 154 485.101 206.775 570.656 1.00 96.41 C
ANISOU 1068 CD GLU A 154 14174 13095 9365 -2519 4836 292 C
ATOM 1069 OE1 GLU A 154 484.750 207.780 571.310 1.00 92.13 O
ANISOU 1069 OE1 GLU A 154 13544 12783 8677 -2533 4880 47 O
ATOM 1070 OE2 GLU A 154 486.116 206.756 569.924 1.00 93.46 O
ANISOU 1070 OE2 GLU A 154 13857 12543 9112 -2414 4713 393 O
ATOM 1071 N MET A 155 485.324 201.788 570.825 1.00103.86 N
ANISOU 1071 N MET A 155 15612 13497 10353 -2698 4930 1406 N
ATOM 1072 CA MET A 155 485.949 201.066 571.923 1.00 96.86 C
ANISOU 1072 CA MET A 155 14893 12715 9196 -2702 4927 1755 C
ATOM 1073 C MET A 155 487.454 201.112 571.728 1.00 93.42 C
ANISOU 1073 C MET A 155 14577 12193 8725 -2529 4754 1922 C
ATOM 1074 O MET A 155 487.949 200.783 570.646 1.00 94.32 O
ANISOU 1074 O MET A 155 14722 12022 9094 -2440 4671 1944 O
ATOM 1075 CB MET A 155 485.459 199.615 571.986 1.00 94.03 C
ANISOU 1075 CB MET A 155 14627 12177 8925 -2823 5017 2020 C
ATOM 1076 N ALA A 156 488.175 201.528 572.765 1.00 89.77 N
ANISOU 1076 N ALA A 156 14181 11992 7936 -2477 4701 2033 N
ATOM 1077 CA ALA A 156 489.622 201.651 572.699 1.00103.06 C
ANISOU 1077 CA ALA A 156 15967 13642 9549 -2318 4529 2200 C
ATOM 1078 C ALA A 156 490.273 200.886 573.842 1.00101.43 C
ANISOU 1078 C ALA A 156 15918 13579 9043 -2301 4492 2586 C
ATOM 1079 O ALA A 156 489.667 200.660 574.894 1.00100.04 O
ANISOU 1079 O ALA A 156 15752 13635 8622 -2405 4602 2668 O
ATOM 1080 CB ALA A 156 490.073 203.120 572.731 1.00 98.33 C
ANISOU 1080 CB ALA A 156 15289 13229 8843 -2254 4457 1930 C
ATOM 1081 N THR A 157 491.523 200.495 573.608 1.00101.23 N
ANISOU 1081 N THR A 157 16000 13423 9038 -2157 4333 2834 N
ATOM 1082 CA THR A 157 492.286 199.710 574.566 1.00105.09 C
ANISOU 1082 CA THR A 157 16634 14019 9278 -2113 4259 3239 C
ATOM 1083 C THR A 157 492.475 200.496 575.858 1.00109.58 C
ANISOU 1083 C THR A 157 17210 15025 9402 -2125 4250 3218 C
ATOM 1084 O THR A 157 492.860 201.670 575.830 1.00 95.86 O
ANISOU 1084 O THR A 157 15426 13435 7560 -2079 4184 2972 O
ATOM 1085 CB THR A 157 493.639 199.342 573.948 1.00105.51 C
ANISOU 1085 CB THR A 157 16770 13855 9464 -1927 4067 3453 C
ATOM 1086 OG1 THR A 157 493.459 198.301 572.978 1.00 98.04 O
ANISOU 1086 OG1 THR A 157 15865 12513 8873 -1912 4091 3534 O
ATOM 1087 CG2 THR A 157 494.631 198.879 575.015 1.00106.57 C
ANISOU 1087 CG2 THR A 157 17026 14179 9288 -1853 3940 3839 C
ATOM 1088 N LYS A 158 492.186 199.849 576.991 1.00102.91 N
ANISOU 1088 N LYS A 158 16426 14388 8287 -2190 4324 3471 N
ATOM 1089 CA LYS A 158 492.225 200.461 578.321 1.00104.75 C
ANISOU 1089 CA LYS A 158 16678 15067 8055 -2197 4344 3456 C
ATOM 1090 C LYS A 158 491.410 201.745 578.397 1.00103.44 C
ANISOU 1090 C LYS A 158 16395 15094 7814 -2273 4447 2975 C
ATOM 1091 O LYS A 158 491.733 202.641 579.184 1.00104.58 O
ANISOU 1091 O LYS A 158 16560 15560 7614 -2247 4401 2821 O
ATOM 1092 CB LYS A 158 493.664 200.725 578.780 1.00116.76 C
ANISOU 1092 CB LYS A 158 18299 16747 9316 -2045 4129 3641 C
ATOM 1093 CG LYS A 158 494.634 199.603 578.458 1.00122.00 C
ANISOU 1093 CG LYS A 158 19053 17173 10128 -1943 3979 4071 C
ATOM 1094 CD LYS A 158 495.718 199.494 579.520 1.00129.61 C
ANISOU 1094 CD LYS A 158 20112 18436 10697 -1830 3816 4391 C
ATOM 1095 CE LYS A 158 496.686 200.664 579.449 1.00130.06 C
ANISOU 1095 CE LYS A 158 20178 18639 10600 -1719 3639 4197 C
ATOM 1096 NZ LYS A 158 498.078 200.246 579.796 1.00138.24 N
ANISOU 1096 NZ LYS A 158 21293 19751 11482 -1565 3397 4579 N
ATOM 1097 N ALA A 159 490.360 201.853 577.584 1.00104.99 N
ANISOU 1097 N ALA A 159 16467 15097 8329 -2367 4573 2720 N
ATOM 1098 CA ALA A 159 489.462 203.006 577.566 1.00105.13 C
ANISOU 1098 CA ALA A 159 16343 15264 8337 -2439 4676 2264 C
ATOM 1099 C ALA A 159 490.194 204.321 577.311 1.00 97.62 C
ANISOU 1099 C ALA A 159 15369 14387 7336 -2368 4542 1966 C
ATOM 1100 O ALA A 159 489.688 205.391 577.663 1.00 97.76 O
ANISOU 1100 O ALA A 159 15298 14620 7227 -2414 4596 1601 O
ATOM 1101 CB ALA A 159 488.651 203.096 578.865 1.00104.27 C
ANISOU 1101 CB ALA A 159 16219 15526 7872 -2518 4830 2234 C
ATOM 1102 N ASP A 160 491.385 204.268 576.714 1.00 98.25 N
ANISOU 1102 N ASP A 160 15521 14291 7517 -2258 4367 2114 N
ATOM 1103 CA ASP A 160 492.133 205.464 576.340 1.00 98.53 C
ANISOU 1103 CA ASP A 160 15532 14357 7548 -2208 4238 1865 C
ATOM 1104 C ASP A 160 491.947 205.669 574.841 1.00104.21 C
ANISOU 1104 C ASP A 160 16133 14724 8736 -2179 4244 1709 C
ATOM 1105 O ASP A 160 492.557 204.967 574.027 1.00 87.29 O
ANISOU 1105 O ASP A 160 14032 12305 6829 -2083 4164 1946 O
ATOM 1106 CB ASP A 160 493.611 205.341 576.716 1.00 98.74 C
ANISOU 1106 CB ASP A 160 15706 14463 7347 -2101 4033 2147 C
ATOM 1107 CG ASP A 160 494.459 206.518 576.213 1.00108.92 C
ANISOU 1107 CG ASP A 160 16972 15753 8660 -2072 3887 1924 C
ATOM 1108 OD1 ASP A 160 495.697 206.463 576.375 1.00109.13 O
ANISOU 1108 OD1 ASP A 160 17104 15825 8535 -1987 3696 2152 O
ATOM 1109 OD2 ASP A 160 493.907 207.499 575.663 1.00105.35 O
ANISOU 1109 OD2 ASP A 160 16389 15262 8379 -2136 3955 1536 O
ATOM 1110 N TYR A 161 491.113 206.643 574.483 1.00 96.07 N
ANISOU 1110 N TYR A 161 14948 13717 7838 -2245 4332 1305 N
ATOM 1111 CA TYR A 161 490.721 206.881 573.103 1.00101.33 C
ANISOU 1111 CA TYR A 161 15472 14092 8937 -2221 4354 1135 C
ATOM 1112 C TYR A 161 491.683 207.813 572.367 1.00 91.58 C
ANISOU 1112 C TYR A 161 14204 12770 7823 -2138 4230 1026 C
ATOM 1113 O TYR A 161 491.324 208.350 571.313 1.00 93.65 O
ANISOU 1113 O TYR A 161 14315 12859 8408 -2119 4254 817 O
ATOM 1114 CB TYR A 161 489.292 207.432 573.053 1.00 98.57 C
ANISOU 1114 CB TYR A 161 14949 13808 8696 -2318 4505 784 C
ATOM 1115 CG TYR A 161 488.246 206.540 573.705 1.00 99.78 C
ANISOU 1115 CG TYR A 161 15112 14046 8756 -2415 4647 892 C
ATOM 1116 CD1 TYR A 161 488.220 206.339 575.081 1.00106.17 C
ANISOU 1116 CD1 TYR A 161 16015 15157 9169 -2460 4694 1004 C
ATOM 1117 CD2 TYR A 161 487.289 205.894 572.937 1.00100.91 C
ANISOU 1117 CD2 TYR A 161 15167 13977 9197 -2466 4733 890 C
ATOM 1118 CE1 TYR A 161 487.266 205.521 575.669 1.00104.29 C
ANISOU 1118 CE1 TYR A 161 15773 15001 8850 -2551 4842 1133 C
ATOM 1119 CE2 TYR A 161 486.335 205.081 573.512 1.00100.88 C
ANISOU 1119 CE2 TYR A 161 15166 14045 9116 -2577 4871 1000 C
ATOM 1120 CZ TYR A 161 486.326 204.896 574.877 1.00104.23 C
ANISOU 1120 CZ TYR A 161 15675 14765 9162 -2618 4933 1134 C
ATOM 1121 OH TYR A 161 485.371 204.082 575.439 1.00103.70 O
ANISOU 1121 OH TYR A 161 15600 14776 9026 -2730 5085 1271 O
ATOM 1122 N THR A 162 492.889 208.014 572.909 1.00 94.12 N
ANISOU 1122 N THR A 162 14657 13221 7884 -2095 4095 1178 N
ATOM 1123 CA THR A 162 493.985 208.746 572.272 1.00 88.13 C
ANISOU 1123 CA THR A 162 13784 12368 7332 -1944 3836 1147 C
ATOM 1124 C THR A 162 493.640 210.198 571.958 1.00 84.21 C
ANISOU 1124 C THR A 162 13053 11907 7035 -1946 3764 710 C
ATOM 1125 O THR A 162 494.234 211.116 572.534 1.00 83.58 O
ANISOU 1125 O THR A 162 12904 11997 6854 -1915 3559 552 O
ATOM 1126 CB THR A 162 494.439 208.039 570.993 1.00 85.67 C
ANISOU 1126 CB THR A 162 13466 11721 7362 -1816 3808 1386 C
ATOM 1127 OG1 THR A 162 494.935 206.737 571.321 1.00 86.81 O
ANISOU 1127 OG1 THR A 162 13831 11808 7345 -1782 3835 1799 O
ATOM 1128 CG2 THR A 162 495.549 208.834 570.311 1.00 88.35 C
ANISOU 1128 CG2 THR A 162 13631 11989 7949 -1644 3524 1361 C
ATOM 1129 N LEU A 163 492.708 210.420 571.037 1.00 75.91 N
ANISOU 1129 N LEU A 163 11875 10687 6281 -1978 3917 516 N
ATOM 1130 CA LEU A 163 492.342 211.772 570.647 1.00 79.04 C
ANISOU 1130 CA LEU A 163 12044 11079 6911 -1962 3855 129 C
ATOM 1131 C LEU A 163 491.252 212.329 571.556 1.00 91.84 C
ANISOU 1131 C LEU A 163 13644 12935 8315 -2097 4027 -208 C
ATOM 1132 O LEU A 163 490.606 211.609 572.321 1.00100.96 O
ANISOU 1132 O LEU A 163 14943 14249 9170 -2219 4239 -138 O
ATOM 1133 CB LEU A 163 491.874 211.806 569.195 1.00 71.34 C
ANISOU 1133 CB LEU A 163 10919 9834 6353 -1911 3922 86 C
ATOM 1134 CG LEU A 163 492.849 211.198 568.191 1.00 76.74 C
ANISOU 1134 CG LEU A 163 11615 10294 7249 -1766 3791 400 C
ATOM 1135 CD1 LEU A 163 492.141 210.916 566.880 1.00 71.05 C
ANISOU 1135 CD1 LEU A 163 10799 9355 6843 -1749 3926 370 C
ATOM 1136 CD2 LEU A 163 494.024 212.137 567.987 1.00 72.52 C
ANISOU 1136 CD2 LEU A 163 10941 9754 6859 -1634 3492 393 C
ATOM 1137 N ASP A 164 491.048 213.639 571.454 1.00 88.66 N
ANISOU 1137 N ASP A 164 13053 12551 8083 -2067 3939 -574 N
ATOM 1138 CA ASP A 164 489.984 214.294 572.190 1.00 90.64 C
ANISOU 1138 CA ASP A 164 13250 13006 8184 -2161 4102 -947 C
ATOM 1139 C ASP A 164 488.629 213.982 571.554 1.00 91.20 C
ANISOU 1139 C ASP A 164 13240 12992 8421 -2235 4388 -1037 C
ATOM 1140 O ASP A 164 488.532 213.398 570.470 1.00 90.44 O
ANISOU 1140 O ASP A 164 13114 12663 8586 -2210 4431 -854 O
ATOM 1141 CB ASP A 164 490.224 215.802 572.250 1.00 97.49 C
ANISOU 1141 CB ASP A 164 13943 13877 9222 -2092 3904 -1317 C
ATOM 1142 CG ASP A 164 490.492 216.407 570.888 1.00111.44 C
ANISOU 1142 CG ASP A 164 15514 15338 11491 -1980 3766 -1329 C
ATOM 1143 OD1 ASP A 164 490.571 215.650 569.897 1.00115.59 O
ANISOU 1143 OD1 ASP A 164 16042 15674 12203 -1945 3809 -1057 O
ATOM 1144 OD2 ASP A 164 490.627 217.646 570.811 1.00120.45 O
ANISOU 1144 OD2 ASP A 164 16499 16427 12840 -1927 3612 -1612 O
ATOM 1145 N GLU A 165 487.570 214.404 572.246 1.00 83.89 N
ANISOU 1145 N GLU A 165 12264 12276 7334 -2323 4583 -1342 N
ATOM 1146 CA GLU A 165 486.217 213.981 571.895 1.00 85.89 C
ANISOU 1146 CA GLU A 165 12388 12458 7789 -2330 4691 -1355 C
ATOM 1147 C GLU A 165 485.765 214.557 570.556 1.00 78.40 C
ANISOU 1147 C GLU A 165 11225 11269 7296 -2264 4680 -1504 C
ATOM 1148 O GLU A 165 485.055 213.887 569.797 1.00 80.32 O
ANISOU 1148 O GLU A 165 11397 11362 7758 -2262 4707 -1375 O
ATOM 1149 CB GLU A 165 485.248 214.381 573.008 1.00 90.40 C
ANISOU 1149 CB GLU A 165 12904 13301 8142 -2369 4791 -1611 C
ATOM 1150 CG GLU A 165 485.451 215.801 573.534 1.00111.63 C
ANISOU 1150 CG GLU A 165 15523 16141 10750 -2335 4752 -2038 C
ATOM 1151 CD GLU A 165 486.495 215.888 574.637 1.00136.57 C
ANISOU 1151 CD GLU A 165 18876 19543 13471 -2369 4669 -2031 C
ATOM 1152 OE1 GLU A 165 486.901 214.830 575.163 1.00145.25 O
ANISOU 1152 OE1 GLU A 165 20157 20735 14295 -2413 4665 -1676 O
ATOM 1153 OE2 GLU A 165 486.911 217.017 574.976 1.00145.33 O
ANISOU 1153 OE2 GLU A 165 19941 20731 14547 -2331 4557 -2372 O
ATOM 1154 N GLU A 166 486.158 215.795 570.246 1.00 82.18 N
ANISOU 1154 N GLU A 166 11591 11713 7922 -2211 4633 -1781 N
ATOM 1155 CA GLU A 166 485.666 216.437 569.028 1.00 84.93 C
ANISOU 1155 CA GLU A 166 11710 11854 8706 -2132 4622 -1923 C
ATOM 1156 C GLU A 166 486.225 215.770 567.777 1.00 80.08 C
ANISOU 1156 C GLU A 166 11104 10995 8329 -2079 4548 -1607 C
ATOM 1157 O GLU A 166 485.511 215.617 566.778 1.00 74.94 O
ANISOU 1157 O GLU A 166 10311 10200 7963 -2038 4549 -1587 O
ATOM 1158 CB GLU A 166 486.007 217.928 569.043 1.00 89.47 C
ANISOU 1158 CB GLU A 166 12132 12381 9481 -2021 4435 -2227 C
ATOM 1159 CG GLU A 166 485.499 218.665 570.279 1.00109.35 C
ANISOU 1159 CG GLU A 166 14646 15142 11760 -2056 4511 -2600 C
ATOM 1160 CD GLU A 166 486.531 218.728 571.390 1.00117.03 C
ANISOU 1160 CD GLU A 166 15793 16272 12402 -2070 4340 -2575 C
ATOM 1161 OE1 GLU A 166 487.337 217.781 571.509 1.00118.56 O
ANISOU 1161 OE1 GLU A 166 16160 16479 12408 -2102 4275 -2219 O
ATOM 1162 OE2 GLU A 166 486.532 219.722 572.147 1.00122.55 O
ANISOU 1162 OE2 GLU A 166 16452 17084 13029 -2042 4265 -2920 O
ATOM 1163 N SER A 167 487.496 215.365 567.805 1.00 78.34 N
ANISOU 1163 N SER A 167 11019 10710 8037 -2025 4357 -1328 N
ATOM 1164 CA SER A 167 488.064 214.684 566.645 1.00 79.05 C
ANISOU 1164 CA SER A 167 11118 10581 8336 -1950 4282 -1027 C
ATOM 1165 C SER A 167 487.403 213.328 566.423 1.00 80.72 C
ANISOU 1165 C SER A 167 11435 10751 8483 -2027 4439 -834 C
ATOM 1166 O SER A 167 487.095 212.961 565.283 1.00 68.63 O
ANISOU 1166 O SER A 167 9813 9048 7217 -1966 4402 -759 O
ATOM 1167 CB SER A 167 489.575 214.528 566.807 1.00 74.07 C
ANISOU 1167 CB SER A 167 10595 9912 7635 -1859 4038 -769 C
ATOM 1168 OG SER A 167 490.168 215.737 567.256 1.00 80.96 O
ANISOU 1168 OG SER A 167 11375 10838 8549 -1804 3829 -952 O
ATOM 1169 N ARG A 168 487.164 212.573 567.496 1.00 78.11 N
ANISOU 1169 N ARG A 168 11262 10562 7853 -2113 4492 -740 N
ATOM 1170 CA ARG A 168 486.501 211.283 567.337 1.00 72.19 C
ANISOU 1170 CA ARG A 168 10571 9736 7121 -2153 4527 -549 C
ATOM 1171 C ARG A 168 485.065 211.460 566.860 1.00 76.19 C
ANISOU 1171 C ARG A 168 10888 10226 7835 -2187 4591 -761 C
ATOM 1172 O ARG A 168 484.606 210.727 565.975 1.00 73.77 O
ANISOU 1172 O ARG A 168 10547 9764 7718 -2184 4580 -672 O
ATOM 1173 CB ARG A 168 486.549 210.504 568.650 1.00 83.13 C
ANISOU 1173 CB ARG A 168 12145 11291 8150 -2239 4583 -385 C
ATOM 1174 CG ARG A 168 487.933 209.981 568.999 1.00 77.48 C
ANISOU 1174 CG ARG A 168 11638 10562 7240 -2196 4496 -84 C
ATOM 1175 CD ARG A 168 488.221 210.136 570.478 1.00 83.62 C
ANISOU 1175 CD ARG A 168 12545 11622 7606 -2259 4520 -78 C
ATOM 1176 NE ARG A 168 487.205 209.481 571.294 1.00 87.08 N
ANISOU 1176 NE ARG A 168 13003 12199 7886 -2352 4638 -51 N
ATOM 1177 CZ ARG A 168 486.910 209.836 572.539 1.00 84.73 C
ANISOU 1177 CZ ARG A 168 12733 12194 7265 -2412 4702 -166 C
ATOM 1178 NH1 ARG A 168 487.559 210.840 573.110 1.00 92.69 N
ANISOU 1178 NH1 ARG A 168 13765 13385 8068 -2396 4644 -353 N
ATOM 1179 NH2 ARG A 168 485.968 209.190 573.211 1.00 87.85 N
ANISOU 1179 NH2 ARG A 168 13130 12713 7537 -2491 4824 -105 N
ATOM 1180 N ALA A 169 484.355 212.448 567.414 1.00 70.68 N
ANISOU 1180 N ALA A 169 10061 9692 7101 -2213 4653 -1055 N
ATOM 1181 CA ALA A 169 482.976 212.709 567.009 1.00 83.36 C
ANISOU 1181 CA ALA A 169 11471 11302 8899 -2234 4708 -1253 C
ATOM 1182 C ALA A 169 482.880 213.050 565.525 1.00 79.07 C
ANISOU 1182 C ALA A 169 10766 10562 8713 -2141 4621 -1295 C
ATOM 1183 O ALA A 169 481.907 212.676 564.860 1.00 82.36 O
ANISOU 1183 O ALA A 169 11079 10922 9292 -2164 4635 -1318 O
ATOM 1184 CB ALA A 169 482.387 213.840 567.856 1.00 72.73 C
ANISOU 1184 CB ALA A 169 10011 10160 7464 -2240 4775 -1572 C
ATOM 1185 N ARG A 170 483.870 213.769 564.989 1.00 76.08 N
ANISOU 1185 N ARG A 170 10357 10095 8454 -2041 4534 -1301 N
ATOM 1186 CA ARG A 170 483.873 214.050 563.556 1.00 82.70 C
ANISOU 1186 CA ARG A 170 11041 10765 9614 -1938 4447 -1294 C
ATOM 1187 C ARG A 170 483.959 212.763 562.747 1.00 75.04 C
ANISOU 1187 C ARG A 170 10162 9655 8693 -1935 4405 -1049 C
ATOM 1188 O ARG A 170 483.312 212.628 561.701 1.00 68.32 O
ANISOU 1188 O ARG A 170 9187 8723 8049 -1903 4369 -1082 O
ATOM 1189 CB ARG A 170 485.033 214.979 563.201 1.00 85.19 C
ANISOU 1189 CB ARG A 170 11310 11019 10040 -1838 4380 -1299 C
ATOM 1190 CG ARG A 170 484.796 216.445 563.530 1.00 94.22 C
ANISOU 1190 CG ARG A 170 12284 12230 11284 -1811 4408 -1614 C
ATOM 1191 CD ARG A 170 485.622 217.340 562.616 1.00103.08 C
ANISOU 1191 CD ARG A 170 13261 13214 12690 -1685 4299 -1598 C
ATOM 1192 NE ARG A 170 486.898 216.720 562.261 1.00109.46 N
ANISOU 1192 NE ARG A 170 14198 13926 13465 -1624 4145 -1272 N
ATOM 1193 CZ ARG A 170 487.260 216.399 561.021 1.00105.82 C
ANISOU 1193 CZ ARG A 170 13675 13336 13196 -1530 4076 -1072 C
ATOM 1194 NH1 ARG A 170 486.443 216.641 560.004 1.00113.05 N
ANISOU 1194 NH1 ARG A 170 14404 14208 14340 -1492 4136 -1156 N
ATOM 1195 NH2 ARG A 170 488.441 215.836 560.797 1.00 81.45 N
ANISOU 1195 NH2 ARG A 170 10704 10183 10060 -1462 3948 -788 N
ATOM 1196 N ILE A 171 484.755 211.804 563.219 1.00 70.32 N
ANISOU 1196 N ILE A 171 9784 9032 7904 -1964 4408 -813 N
ATOM 1197 CA ILE A 171 484.869 210.521 562.535 1.00 66.69 C
ANISOU 1197 CA ILE A 171 9429 8421 7490 -1959 4383 -602 C
ATOM 1198 C ILE A 171 483.548 209.763 562.596 1.00 69.15 C
ANISOU 1198 C ILE A 171 9722 8745 7808 -2084 4470 -664 C
ATOM 1199 O ILE A 171 483.121 209.151 561.609 1.00 65.85 O
ANISOU 1199 O ILE A 171 9267 8205 7549 -2083 4454 -650 O
ATOM 1200 CB ILE A 171 486.025 209.709 563.143 1.00 71.85 C
ANISOU 1200 CB ILE A 171 10320 9041 7939 -1951 4368 -328 C
ATOM 1201 CG1 ILE A 171 487.367 210.297 562.699 1.00 70.11 C
ANISOU 1201 CG1 ILE A 171 10097 8768 7775 -1815 4269 -226 C
ATOM 1202 CG2 ILE A 171 485.909 208.234 562.777 1.00 63.49 C
ANISOU 1202 CG2 ILE A 171 9397 7833 6894 -1983 4385 -140 C
ATOM 1203 CD1 ILE A 171 488.559 209.674 563.384 1.00 72.30 C
ANISOU 1203 CD1 ILE A 171 10594 9043 7836 -1793 4239 44 C
ATOM 1204 N LYS A 172 482.877 209.790 563.749 1.00 66.49 N
ANISOU 1204 N LYS A 172 9405 8568 7291 -2198 4572 -738 N
ATOM 1205 CA LYS A 172 481.613 209.071 563.872 1.00 71.58 C
ANISOU 1205 CA LYS A 172 10018 9240 7941 -2330 4671 -778 C
ATOM 1206 C LYS A 172 480.540 209.680 562.981 1.00 73.40 C
ANISOU 1206 C LYS A 172 10012 9471 8404 -2316 4658 -1002 C
ATOM 1207 O LYS A 172 479.744 208.953 562.374 1.00 70.09 O
ANISOU 1207 O LYS A 172 9556 8983 8092 -2390 4690 -1006 O
ATOM 1208 CB LYS A 172 481.146 209.061 565.325 1.00 74.06 C
ANISOU 1208 CB LYS A 172 10380 9761 7998 -2439 4790 -798 C
ATOM 1209 CG LYS A 172 482.142 208.494 566.313 1.00 78.78 C
ANISOU 1209 CG LYS A 172 11204 10402 8327 -2454 4800 -564 C
ATOM 1210 CD LYS A 172 481.527 208.474 567.698 1.00 88.31 C
ANISOU 1210 CD LYS A 172 12435 11851 9269 -2561 4928 -589 C
ATOM 1211 CE LYS A 172 482.277 209.375 568.663 1.00101.59 C
ANISOU 1211 CE LYS A 172 14165 13721 10713 -2507 4909 -659 C
ATOM 1212 NZ LYS A 172 482.796 208.642 569.849 1.00101.27 N
ANISOU 1212 NZ LYS A 172 14327 13812 10340 -2561 4953 -419 N
ATOM 1213 N THR A 173 480.499 211.013 562.901 1.00 70.86 N
ANISOU 1213 N THR A 173 9528 9228 8167 -2226 4615 -1193 N
ATOM 1214 CA THR A 173 479.530 211.681 562.036 1.00 85.68 C
ANISOU 1214 CA THR A 173 11170 11110 10273 -2187 4585 -1385 C
ATOM 1215 C THR A 173 479.730 211.302 560.573 1.00 75.17 C
ANISOU 1215 C THR A 173 9800 9618 9143 -2116 4486 -1309 C
ATOM 1216 O THR A 173 478.759 211.040 559.853 1.00 66.32 O
ANISOU 1216 O THR A 173 8562 8489 8147 -2156 4491 -1385 O
ATOM 1217 CB THR A 173 479.627 213.197 562.219 1.00 90.93 C
ANISOU 1217 CB THR A 173 11684 11854 11010 -2085 4553 -1581 C
ATOM 1218 OG1 THR A 173 479.430 213.527 563.604 1.00 78.86 O
ANISOU 1218 OG1 THR A 173 10199 10496 9268 -2149 4655 -1683 O
ATOM 1219 CG2 THR A 173 478.597 213.918 561.349 1.00 88.56 C
ANISOU 1219 CG2 THR A 173 11134 11563 10951 -2029 4516 -1757 C
ATOM 1220 N ARG A 174 480.980 211.264 560.115 1.00 68.02 N
ANISOU 1220 N ARG A 174 8984 8602 8257 -2011 4399 -1163 N
ATOM 1221 CA ARG A 174 481.235 210.894 558.726 1.00 68.81 C
ANISOU 1221 CA ARG A 174 9048 8573 8522 -1928 4313 -1090 C
ATOM 1222 C ARG A 174 480.786 209.464 558.449 1.00 70.56 C
ANISOU 1222 C ARG A 174 9387 8706 8715 -2043 4375 -1014 C
ATOM 1223 O ARG A 174 480.139 209.194 557.430 1.00 64.16 O
ANISOU 1223 O ARG A 174 8476 7860 8042 -2052 4358 -1085 O
ATOM 1224 CB ARG A 174 482.719 211.076 558.406 1.00 65.02 C
ANISOU 1224 CB ARG A 174 8647 8010 8047 -1792 4227 -925 C
ATOM 1225 CG ARG A 174 483.151 210.520 557.059 1.00 64.83 C
ANISOU 1225 CG ARG A 174 8621 7867 8145 -1696 4156 -817 C
ATOM 1226 CD ARG A 174 482.587 211.324 555.898 1.00 66.53 C
ANISOU 1226 CD ARG A 174 8593 8121 8565 -1606 4078 -938 C
ATOM 1227 NE ARG A 174 483.228 210.944 554.642 1.00 68.52 N
ANISOU 1227 NE ARG A 174 8838 8297 8901 -1487 4006 -821 N
ATOM 1228 CZ ARG A 174 482.591 210.831 553.481 1.00 72.83 C
ANISOU 1228 CZ ARG A 174 9253 8857 9560 -1458 3971 -890 C
ATOM 1229 NH1 ARG A 174 481.286 211.067 553.415 1.00 68.41 N
ANISOU 1229 NH1 ARG A 174 8556 8380 9059 -1543 3993 -1065 N
ATOM 1230 NH2 ARG A 174 483.256 210.473 552.389 1.00 67.35 N
ANISOU 1230 NH2 ARG A 174 8561 8117 8911 -1342 3921 -785 N
ATOM 1231 N LEU A 175 481.095 208.540 559.364 1.00 74.64 N
ANISOU 1231 N LEU A 175 10114 9191 9055 -2141 4455 -876 N
ATOM 1232 CA LEU A 175 480.691 207.147 559.196 1.00 77.38 C
ANISOU 1232 CA LEU A 175 10587 9423 9389 -2268 4536 -799 C
ATOM 1233 C LEU A 175 479.182 207.021 559.020 1.00 78.33 C
ANISOU 1233 C LEU A 175 10561 9612 9588 -2407 4611 -973 C
ATOM 1234 O LEU A 175 478.707 206.294 558.139 1.00 76.98 O
ANISOU 1234 O LEU A 175 10376 9342 9529 -2469 4632 -1008 O
ATOM 1235 CB LEU A 175 481.158 206.321 560.395 1.00 76.13 C
ANISOU 1235 CB LEU A 175 10656 9246 9022 -2354 4613 -608 C
ATOM 1236 CG LEU A 175 482.659 206.042 560.465 1.00 76.94 C
ANISOU 1236 CG LEU A 175 10940 9246 9048 -2233 4547 -388 C
ATOM 1237 CD1 LEU A 175 483.001 205.341 561.768 1.00 76.37 C
ANISOU 1237 CD1 LEU A 175 11068 9199 8749 -2318 4615 -195 C
ATOM 1238 CD2 LEU A 175 483.104 205.213 559.270 1.00 68.00 C
ANISOU 1238 CD2 LEU A 175 9881 7904 8051 -2170 4518 -311 C
ATOM 1239 N PHE A 176 478.406 207.722 559.853 1.00 70.52 N
ANISOU 1239 N PHE A 176 9456 8800 8539 -2459 4661 -1092 N
ATOM 1240 CA PHE A 176 476.953 207.623 559.748 1.00 72.58 C
ANISOU 1240 CA PHE A 176 9561 9147 8869 -2587 4738 -1245 C
ATOM 1241 C PHE A 176 476.434 208.280 558.476 1.00 70.07 C
ANISOU 1241 C PHE A 176 9023 8840 8760 -2501 4647 -1404 C
ATOM 1242 O PHE A 176 475.411 207.849 557.932 1.00 68.53 O
ANISOU 1242 O PHE A 176 8724 8657 8656 -2605 4689 -1498 O
ATOM 1243 CB PHE A 176 476.284 208.244 560.975 1.00 80.43 C
ANISOU 1243 CB PHE A 176 10478 10344 9736 -2642 4825 -1332 C
ATOM 1244 CG PHE A 176 474.919 207.684 561.269 1.00 77.73 C
ANISOU 1244 CG PHE A 176 10052 10092 9390 -2821 4956 -1397 C
ATOM 1245 CD1 PHE A 176 473.776 208.331 560.824 1.00 89.22 C
ANISOU 1245 CD1 PHE A 176 11261 11661 10977 -2822 4958 -1593 C
ATOM 1246 CD2 PHE A 176 474.777 206.509 561.989 1.00 82.18 C
ANISOU 1246 CD2 PHE A 176 10772 10629 9822 -2989 5080 -1243 C
ATOM 1247 CE1 PHE A 176 472.518 207.820 561.096 1.00 95.00 C
ANISOU 1247 CE1 PHE A 176 11899 12491 11707 -2990 5084 -1646 C
ATOM 1248 CE2 PHE A 176 473.521 205.993 562.265 1.00 93.59 C
ANISOU 1248 CE2 PHE A 176 12125 12164 11272 -3166 5210 -1287 C
ATOM 1249 CZ PHE A 176 472.391 206.649 561.816 1.00 93.09 C
ANISOU 1249 CZ PHE A 176 11808 12224 11337 -3169 5213 -1494 C
ATOM 1250 N THR A 177 477.114 209.320 557.993 1.00 68.71 N
ANISOU 1250 N THR A 177 8768 8673 8665 -2318 4523 -1426 N
ATOM 1251 CA THR A 177 476.724 209.921 556.723 1.00 76.69 C
ANISOU 1251 CA THR A 177 9574 9699 9866 -2218 4425 -1531 C
ATOM 1252 C THR A 177 476.911 208.936 555.576 1.00 77.05 C
ANISOU 1252 C THR A 177 9678 9617 9980 -2236 4403 -1475 C
ATOM 1253 O THR A 177 476.041 208.812 554.705 1.00 71.17 O
ANISOU 1253 O THR A 177 8787 8909 9345 -2276 4395 -1586 O
ATOM 1254 CB THR A 177 477.524 211.203 556.485 1.00 81.17 C
ANISOU 1254 CB THR A 177 10054 10284 10504 -2022 4307 -1528 C
ATOM 1255 OG1 THR A 177 477.016 212.242 557.332 1.00 88.41 O
ANISOU 1255 OG1 THR A 177 10856 11326 11410 -2013 4340 -1661 O
ATOM 1256 CG2 THR A 177 477.421 211.650 555.036 1.00 58.70 C
ANISOU 1256 CG2 THR A 177 7032 7434 7837 -1897 4191 -1557 C
ATOM 1257 N ILE A 178 478.032 208.209 555.573 1.00 65.96 N
ANISOU 1257 N ILE A 178 8486 8070 8507 -2210 4403 -1311 N
ATOM 1258 CA ILE A 178 478.271 207.204 554.542 1.00 70.04 C
ANISOU 1258 CA ILE A 178 9082 8449 9079 -2228 4412 -1273 C
ATOM 1259 C ILE A 178 477.156 206.167 554.547 1.00 74.77 C
ANISOU 1259 C ILE A 178 9700 9017 9693 -2452 4537 -1364 C
ATOM 1260 O ILE A 178 476.627 205.790 553.494 1.00 75.36 O
ANISOU 1260 O ILE A 178 9686 9073 9873 -2498 4542 -1472 O
ATOM 1261 CB ILE A 178 479.649 206.548 554.737 1.00 70.31 C
ANISOU 1261 CB ILE A 178 9361 8327 9026 -2163 4416 -1070 C
ATOM 1262 CG1 ILE A 178 480.765 207.564 554.464 1.00 62.16 C
ANISOU 1262 CG1 ILE A 178 8275 7332 8012 -1942 4286 -984 C
ATOM 1263 CG2 ILE A 178 479.798 205.335 553.820 1.00 66.85 C
ANISOU 1263 CG2 ILE A 178 9040 7720 8638 -2212 4475 -1052 C
ATOM 1264 CD1 ILE A 178 482.156 207.036 554.757 1.00 59.00 C
ANISOU 1264 CD1 ILE A 178 8093 6807 7517 -1862 4283 -772 C
ATOM 1265 N ARG A 179 476.773 205.699 555.736 1.00 79.65 N
ANISOU 1265 N ARG A 179 10420 9642 10201 -2602 4647 -1323 N
ATOM 1266 CA ARG A 179 475.725 204.689 555.814 1.00 76.57 C
ANISOU 1266 CA ARG A 179 10043 9219 9831 -2832 4776 -1385 C
ATOM 1267 C ARG A 179 474.402 205.229 555.283 1.00 73.53 C
ANISOU 1267 C ARG A 179 9385 8996 9559 -2885 4766 -1593 C
ATOM 1268 O ARG A 179 473.659 204.510 554.606 1.00 78.48 O
ANISOU 1268 O ARG A 179 9959 9585 10273 -3030 4822 -1694 O
ATOM 1269 CB ARG A 179 475.580 204.198 557.253 1.00 82.75 C
ANISOU 1269 CB ARG A 179 10963 10017 10460 -2967 4891 -1266 C
ATOM 1270 CG ARG A 179 474.254 203.536 557.548 1.00 88.95 C
ANISOU 1270 CG ARG A 179 11679 10850 11267 -3203 5023 -1339 C
ATOM 1271 CD ARG A 179 474.225 202.982 558.956 1.00 97.84 C
ANISOU 1271 CD ARG A 179 12949 11998 12227 -3326 5139 -1173 C
ATOM 1272 NE ARG A 179 472.911 203.139 559.568 1.00104.75 N
ANISOU 1272 NE ARG A 179 13654 13065 13082 -3472 5240 -1262 N
ATOM 1273 CZ ARG A 179 472.301 202.196 560.276 1.00108.44 C
ANISOU 1273 CZ ARG A 179 14182 13525 13494 -3683 5383 -1160 C
ATOM 1274 NH1 ARG A 179 472.885 201.021 560.461 1.00110.56 N
ANISOU 1274 NH1 ARG A 179 14689 13584 13734 -3775 5435 -964 N
ATOM 1275 NH2 ARG A 179 471.105 202.427 560.796 1.00111.45 N
ANISOU 1275 NH2 ARG A 179 14380 14107 13857 -3799 5477 -1240 N
ATOM 1276 N GLN A 180 474.101 206.500 555.562 1.00 73.34 N
ANISOU 1276 N GLN A 180 9180 9148 9540 -2769 4697 -1665 N
ATOM 1277 CA GLN A 180 472.879 207.107 555.041 1.00 77.94 C
ANISOU 1277 CA GLN A 180 9490 9889 10234 -2784 4675 -1846 C
ATOM 1278 C GLN A 180 472.901 207.171 553.518 1.00 81.03 C
ANISOU 1278 C GLN A 180 9764 10262 10762 -2705 4574 -1919 C
ATOM 1279 O GLN A 180 471.905 206.856 552.857 1.00 80.92 O
ANISOU 1279 O GLN A 180 9602 10311 10833 -2815 4599 -2052 O
ATOM 1280 CB GLN A 180 472.696 208.505 555.633 1.00 76.47 C
ANISOU 1280 CB GLN A 180 9153 9863 10038 -2648 4623 -1898 C
ATOM 1281 CG GLN A 180 472.209 208.517 557.069 1.00 83.19 C
ANISOU 1281 CG GLN A 180 10037 10814 10758 -2754 4750 -1896 C
ATOM 1282 CD GLN A 180 471.673 209.871 557.478 1.00 81.65 C
ANISOU 1282 CD GLN A 180 9641 10792 10590 -2644 4728 -2021 C
ATOM 1283 OE1 GLN A 180 470.520 210.204 557.201 1.00 92.63 O
ANISOU 1283 OE1 GLN A 180 10817 12310 12069 -2671 4747 -2154 O
ATOM 1284 NE2 GLN A 180 472.513 210.668 558.128 1.00 79.01 N
ANISOU 1284 NE2 GLN A 180 9373 10462 10187 -2519 4692 -1988 N
ATOM 1285 N GLU A 181 474.036 207.579 552.944 1.00 73.42 N
ANISOU 1285 N GLU A 181 8852 9233 9812 -2515 4463 -1831 N
ATOM 1286 CA GLU A 181 474.122 207.718 551.493 1.00 77.61 C
ANISOU 1286 CA GLU A 181 9257 9784 10448 -2415 4366 -1882 C
ATOM 1287 C GLU A 181 473.950 206.373 550.796 1.00 78.17 C
ANISOU 1287 C GLU A 181 9418 9742 10540 -2582 4455 -1940 C
ATOM 1288 O GLU A 181 473.335 206.295 549.726 1.00 87.80 O
ANISOU 1288 O GLU A 181 10472 11042 11845 -2609 4428 -2074 O
ATOM 1289 CB GLU A 181 475.453 208.364 551.107 1.00 77.29 C
ANISOU 1289 CB GLU A 181 9263 9702 10403 -2181 4246 -1743 C
ATOM 1290 CG GLU A 181 475.567 209.834 551.488 1.00 79.64 C
ANISOU 1290 CG GLU A 181 9421 10108 10730 -2015 4148 -1723 C
ATOM 1291 CD GLU A 181 474.590 210.711 550.728 1.00 92.96 C
ANISOU 1291 CD GLU A 181 10824 11958 12539 -1947 4071 -1840 C
ATOM 1292 OE1 GLU A 181 474.903 211.094 549.580 1.00 97.20 O
ANISOU 1292 OE1 GLU A 181 11248 12539 13145 -1802 3964 -1805 O
ATOM 1293 OE2 GLU A 181 473.511 211.020 551.276 1.00104.64 O
ANISOU 1293 OE2 GLU A 181 12186 13534 14037 -2029 4121 -1956 O
ATOM 1294 N MET A 182 474.482 205.302 551.391 1.00 68.01 N
ANISOU 1294 N MET A 182 8392 8270 9180 -2699 4568 -1847 N
ATOM 1295 CA MET A 182 474.266 203.962 550.852 1.00 83.57 C
ANISOU 1295 CA MET A 182 10471 10093 11191 -2892 4686 -1916 C
ATOM 1296 C MET A 182 472.806 203.551 550.962 1.00 93.33 C
ANISOU 1296 C MET A 182 11570 11410 12483 -3133 4772 -2076 C
ATOM 1297 O MET A 182 472.216 203.052 549.996 1.00100.39 O
ANISOU 1297 O MET A 182 12361 12314 13468 -3252 4798 -2239 O
ATOM 1298 CB MET A 182 475.144 202.948 551.582 1.00 84.14 C
ANISOU 1298 CB MET A 182 10862 9927 11180 -2956 4791 -1747 C
ATOM 1299 CG MET A 182 476.610 203.286 551.609 1.00 78.74 C
ANISOU 1299 CG MET A 182 10319 9169 10431 -2725 4714 -1568 C
ATOM 1300 SD MET A 182 477.579 201.777 551.729 1.00 90.35 S
ANISOU 1300 SD MET A 182 12144 10318 11865 -2798 4848 -1418 S
ATOM 1301 CE MET A 182 477.946 201.724 553.473 1.00 85.30 C
ANISOU 1301 CE MET A 182 11683 9655 11073 -2819 4870 -1196 C
ATOM 1302 N ALA A 183 472.218 203.725 552.147 1.00 93.94 N
ANISOU 1302 N ALA A 183 11637 11558 12500 -3215 4826 -2035 N
ATOM 1303 CA ALA A 183 470.825 203.344 552.348 1.00 84.91 C
ANISOU 1303 CA ALA A 183 10350 10509 11402 -3440 4916 -2160 C
ATOM 1304 C ALA A 183 469.909 204.094 551.392 1.00 84.80 C
ANISOU 1304 C ALA A 183 10023 10705 11494 -3394 4825 -2347 C
ATOM 1305 O ALA A 183 468.979 203.510 550.824 1.00 83.86 O
ANISOU 1305 O ALA A 183 9779 10624 11459 -3580 4874 -2496 O
ATOM 1306 CB ALA A 183 470.416 203.597 553.799 1.00 79.09 C
ANISOU 1306 CB ALA A 183 9628 9861 10562 -3490 4988 -2069 C
ATOM 1307 N SER A 184 470.169 205.389 551.186 1.00 82.33 N
ANISOU 1307 N SER A 184 9572 10525 11185 -3148 4687 -2333 N
ATOM 1308 CA SER A 184 469.380 206.170 550.241 1.00 92.31 C
ANISOU 1308 CA SER A 184 10537 11988 12548 -3067 4583 -2473 C
ATOM 1309 C SER A 184 469.431 205.600 548.829 1.00 93.18 C
ANISOU 1309 C SER A 184 10592 12083 12729 -3106 4548 -2584 C
ATOM 1310 O SER A 184 468.523 205.862 548.033 1.00 98.50 O
ANISOU 1310 O SER A 184 11012 12933 13480 -3128 4495 -2730 O
ATOM 1311 CB SER A 184 469.859 207.622 550.235 1.00 97.13 C
ANISOU 1311 CB SER A 184 11048 12694 13161 -2783 4441 -2399 C
ATOM 1312 OG SER A 184 469.714 208.196 548.948 1.00 98.20 O
ANISOU 1312 OG SER A 184 10977 12950 13383 -2646 4311 -2460 O
ATOM 1313 N ARG A 185 470.467 204.832 548.496 1.00 90.58 N
ANISOU 1313 N ARG A 185 10483 11562 12370 -3113 4582 -2527 N
ATOM 1314 CA ARG A 185 470.559 204.168 547.202 1.00 92.91 C
ANISOU 1314 CA ARG A 185 10744 11837 12721 -3173 4585 -2661 C
ATOM 1315 C ARG A 185 470.336 202.665 547.305 1.00 96.46 C
ANISOU 1315 C ARG A 185 11363 12088 13200 -3478 4757 -2748 C
ATOM 1316 O ARG A 185 470.542 201.951 546.317 1.00 96.48 O
ANISOU 1316 O ARG A 185 11384 12023 13250 -3562 4794 -2879 O
ATOM 1317 CB ARG A 185 471.915 204.440 546.552 1.00 84.88 C
ANISOU 1317 CB ARG A 185 9827 10760 11662 -2935 4507 -2549 C
ATOM 1318 CG ARG A 185 472.357 205.886 546.516 1.00 85.52 C
ANISOU 1318 CG ARG A 185 9785 10985 11725 -2632 4336 -2412 C
ATOM 1319 CD ARG A 185 473.875 205.941 546.469 1.00 80.30 C
ANISOU 1319 CD ARG A 185 9320 10191 10998 -2439 4302 -2227 C
ATOM 1320 NE ARG A 185 474.391 207.178 545.891 1.00 75.81 N
ANISOU 1320 NE ARG A 185 8599 9768 10436 -2153 4131 -2118 N
ATOM 1321 CZ ARG A 185 474.470 208.330 546.548 1.00 79.74 C
ANISOU 1321 CZ ARG A 185 9031 10323 10945 -2016 4043 -2009 C
ATOM 1322 NH1 ARG A 185 474.048 208.409 547.807 1.00 62.59 N
ANISOU 1322 NH1 ARG A 185 6923 8104 8755 -2126 4109 -2012 N
ATOM 1323 NH2 ARG A 185 474.962 209.404 545.945 1.00 71.31 N
ANISOU 1323 NH2 ARG A 185 7827 9364 9903 -1774 3901 -1903 N
ATOM 1324 N SER A 186 469.946 202.170 548.483 1.00 94.38 N
ANISOU 1324 N SER A 186 11223 11727 12911 -3645 4866 -2673 N
ATOM 1325 CA SER A 186 469.624 200.761 548.715 1.00102.03 C
ANISOU 1325 CA SER A 186 12350 12491 13925 -3947 5020 -2713 C
ATOM 1326 C SER A 186 470.847 199.850 548.612 1.00 97.24 C
ANISOU 1326 C SER A 186 12064 11578 13305 -3950 5096 -2613 C
ATOM 1327 O SER A 186 470.721 198.676 548.254 1.00102.67 O
ANISOU 1327 O SER A 186 12867 12062 14081 -4176 5194 -2701 O
ATOM 1328 CB SER A 186 468.519 200.273 547.770 1.00106.95 C
ANISOU 1328 CB SER A 186 12755 13208 14672 -4169 5031 -2971 C
ATOM 1329 OG SER A 186 467.422 201.169 547.762 1.00111.71 O
ANISOU 1329 OG SER A 186 13047 14107 15291 -4133 4951 -3054 O
ATOM 1330 N LEU A 187 472.033 200.368 548.938 1.00 92.83 N
ANISOU 1330 N LEU A 187 11653 10967 12650 -3702 5046 -2426 N
ATOM 1331 CA LEU A 187 473.245 199.558 549.006 1.00 90.00 C
ANISOU 1331 CA LEU A 187 11610 10319 12265 -3672 5121 -2286 C
ATOM 1332 C LEU A 187 473.634 199.165 550.424 1.00 83.51 C
ANISOU 1332 C LEU A 187 11031 9348 11350 -3699 5181 -2041 C
ATOM 1333 O LEU A 187 474.588 198.397 550.592 1.00 81.40 O
ANISOU 1333 O LEU A 187 11042 8822 11066 -3681 5242 -1895 O
ATOM 1334 CB LEU A 187 474.437 200.291 548.372 1.00 81.67 C
ANISOU 1334 CB LEU A 187 10564 9309 11157 -3366 5025 -2213 C
ATOM 1335 CG LEU A 187 474.570 200.422 546.854 1.00 94.97 C
ANISOU 1335 CG LEU A 187 12095 11093 12897 -3287 4991 -2394 C
ATOM 1336 CD1 LEU A 187 474.137 199.135 546.149 1.00 90.99 C
ANISOU 1336 CD1 LEU A 187 11648 10414 12509 -3577 5140 -2605 C
ATOM 1337 CD2 LEU A 187 473.839 201.637 546.321 1.00106.51 C
ANISOU 1337 CD2 LEU A 187 13209 12892 14369 -3162 4827 -2498 C
ATOM 1338 N TRP A 188 472.946 199.683 551.443 1.00 83.40 N
ANISOU 1338 N TRP A 188 10915 9501 11271 -3728 5166 -1987 N
ATOM 1339 CA TRP A 188 473.376 199.437 552.816 1.00 86.09 C
ANISOU 1339 CA TRP A 188 11457 9760 11491 -3730 5213 -1749 C
ATOM 1340 C TRP A 188 473.166 197.982 553.214 1.00100.02 C
ANISOU 1340 C TRP A 188 13429 11275 13300 -3980 5351 -1665 C
ATOM 1341 O TRP A 188 474.063 197.354 553.789 1.00105.37 O
ANISOU 1341 O TRP A 188 14373 11745 13917 -3947 5387 -1451 O
ATOM 1342 CB TRP A 188 472.635 200.357 553.784 1.00 79.25 C
ANISOU 1342 CB TRP A 188 10414 9154 10542 -3713 5186 -1737 C
ATOM 1343 CG TRP A 188 472.914 199.992 555.202 1.00 88.18 C
ANISOU 1343 CG TRP A 188 11727 10239 11539 -3762 5259 -1513 C
ATOM 1344 CD1 TRP A 188 472.048 199.428 556.093 1.00 90.83 C
ANISOU 1344 CD1 TRP A 188 12057 10608 11845 -3977 5374 -1454 C
ATOM 1345 CD2 TRP A 188 474.161 200.135 555.888 1.00 93.14 C
ANISOU 1345 CD2 TRP A 188 12558 10796 12036 -3597 5220 -1302 C
ATOM 1346 NE1 TRP A 188 472.677 199.225 557.298 1.00 95.43 N
ANISOU 1346 NE1 TRP A 188 12827 11156 12275 -3951 5411 -1216 N
ATOM 1347 CE2 TRP A 188 473.976 199.651 557.197 1.00 92.44 C
ANISOU 1347 CE2 TRP A 188 12579 10714 11831 -3721 5314 -1126 C
ATOM 1348 CE3 TRP A 188 475.416 200.634 555.523 1.00 96.08 C
ANISOU 1348 CE3 TRP A 188 13014 11117 12376 -3357 5115 -1234 C
ATOM 1349 CZ2 TRP A 188 474.999 199.650 558.144 1.00 90.88 C
ANISOU 1349 CZ2 TRP A 188 12571 10481 11476 -3613 5298 -897 C
ATOM 1350 CZ3 TRP A 188 476.431 200.633 556.464 1.00 92.67 C
ANISOU 1350 CZ3 TRP A 188 12769 10640 11801 -3254 5098 -1010 C
ATOM 1351 CH2 TRP A 188 476.215 200.145 557.760 1.00 94.59 C
ANISOU 1351 CH2 TRP A 188 13119 10899 11921 -3382 5186 -850 C
ATOM 1352 N ASP A 189 471.977 197.436 552.934 1.00 99.85 N
ANISOU 1352 N ASP A 189 13279 11269 13391 -4229 5415 -1816 N
ATOM 1353 CA ASP A 189 471.676 196.060 553.323 1.00105.79 C
ANISOU 1353 CA ASP A 189 14205 11774 14215 -4485 5529 -1724 C
ATOM 1354 C ASP A 189 472.711 195.088 552.768 1.00 99.78 C
ANISOU 1354 C ASP A 189 13731 10652 13529 -4467 5551 -1666 C
ATOM 1355 O ASP A 189 473.170 194.186 553.479 1.00100.45 O
ANISOU 1355 O ASP A 189 14068 10494 13603 -4524 5607 -1442 O
ATOM 1356 CB ASP A 189 470.274 195.671 552.851 1.00113.64 C
ANISOU 1356 CB ASP A 189 14985 12841 15353 -4752 5569 -1931 C
ATOM 1357 CG ASP A 189 469.177 196.267 553.715 1.00115.48 C
ANISOU 1357 CG ASP A 189 14991 13365 15519 -4823 5593 -1915 C
ATOM 1358 OD1 ASP A 189 469.426 196.526 554.912 1.00115.12 O
ANISOU 1358 OD1 ASP A 189 15024 13386 15329 -4757 5624 -1704 O
ATOM 1359 OD2 ASP A 189 468.061 196.473 553.193 1.00115.60 O
ANISOU 1359 OD2 ASP A 189 14742 13554 15625 -4944 5583 -2118 O
ATOM 1360 N SER A 190 473.099 195.261 551.503 1.00 88.96 N
ANISOU 1360 N SER A 190 12322 9243 12236 -4379 5509 -1856 N
ATOM 1361 CA SER A 190 474.114 194.389 550.924 1.00 95.11 C
ANISOU 1361 CA SER A 190 13374 9671 13092 -4339 5536 -1818 C
ATOM 1362 C SER A 190 475.477 194.627 551.565 1.00102.64 C
ANISOU 1362 C SER A 190 14549 10545 13904 -4079 5514 -1541 C
ATOM 1363 O SER A 190 476.259 193.685 551.737 1.00101.18 O
ANISOU 1363 O SER A 190 14655 10034 13756 -4062 5551 -1379 O
ATOM 1364 CB SER A 190 474.185 194.597 549.412 1.00 97.04 C
ANISOU 1364 CB SER A 190 13496 9935 13438 -4310 5506 -2101 C
ATOM 1365 OG SER A 190 475.316 193.945 548.862 1.00109.08 O
ANISOU 1365 OG SER A 190 15291 11133 15021 -4215 5529 -2062 O
ATOM 1366 N PHE A 191 475.775 195.878 551.932 1.00100.39 N
ANISOU 1366 N PHE A 191 14125 10547 13470 -3866 5434 -1482 N
ATOM 1367 CA PHE A 191 477.057 196.183 552.562 1.00 97.92 C
ANISOU 1367 CA PHE A 191 13988 10196 13020 -3622 5386 -1228 C
ATOM 1368 C PHE A 191 477.108 195.698 554.003 1.00104.98 C
ANISOU 1368 C PHE A 191 15043 11032 13814 -3690 5417 -969 C
ATOM 1369 O PHE A 191 478.174 195.293 554.481 1.00111.36 O
ANISOU 1369 O PHE A 191 16087 11670 14555 -3566 5409 -733 O
ATOM 1370 CB PHE A 191 477.331 197.688 552.504 1.00 97.69 C
ANISOU 1370 CB PHE A 191 13747 10482 12889 -3386 5261 -1257 C
ATOM 1371 CG PHE A 191 478.684 198.083 553.036 1.00 92.90 C
ANISOU 1371 CG PHE A 191 13287 9857 12154 -3134 5188 -1020 C
ATOM 1372 CD1 PHE A 191 479.806 198.018 552.226 1.00 88.34 C
ANISOU 1372 CD1 PHE A 191 12814 9153 11596 -2943 5172 -972 C
ATOM 1373 CD2 PHE A 191 478.834 198.526 554.341 1.00 96.65 C
ANISOU 1373 CD2 PHE A 191 13782 10458 12484 -3093 5141 -848 C
ATOM 1374 CE1 PHE A 191 481.052 198.384 552.708 1.00 83.12 C
ANISOU 1374 CE1 PHE A 191 12267 8491 10822 -2710 5095 -746 C
ATOM 1375 CE2 PHE A 191 480.078 198.896 554.826 1.00 96.88 C
ANISOU 1375 CE2 PHE A 191 13926 10488 12397 -2878 5062 -643 C
ATOM 1376 CZ PHE A 191 481.187 198.825 554.008 1.00 83.55 C
ANISOU 1376 CZ PHE A 191 12333 8673 10741 -2685 5030 -587 C
ATOM 1377 N ARG A 192 475.976 195.732 554.710 1.00106.33 N
ANISOU 1377 N ARG A 192 15077 11357 13965 -3879 5455 -994 N
ATOM 1378 CA ARG A 192 475.964 195.301 556.104 1.00110.32 C
ANISOU 1378 CA ARG A 192 15706 11850 14358 -3957 5499 -738 C
ATOM 1379 C ARG A 192 476.193 193.800 556.221 1.00114.03 C
ANISOU 1379 C ARG A 192 16441 11955 14929 -4099 5576 -575 C
ATOM 1380 O ARG A 192 476.939 193.347 557.097 1.00124.06 O
ANISOU 1380 O ARG A 192 17918 13113 16108 -4039 5577 -292 O
ATOM 1381 CB ARG A 192 474.642 195.698 556.762 1.00113.03 C
ANISOU 1381 CB ARG A 192 15821 12459 14665 -4128 5543 -809 C
ATOM 1382 CG ARG A 192 474.575 195.415 558.259 1.00124.15 C
ANISOU 1382 CG ARG A 192 17316 13928 15926 -4205 5602 -544 C
ATOM 1383 CD ARG A 192 473.281 195.945 558.871 1.00131.58 C
ANISOU 1383 CD ARG A 192 18007 15166 16820 -4345 5658 -629 C
ATOM 1384 NE ARG A 192 473.505 196.576 560.170 1.00131.59 N
ANISOU 1384 NE ARG A 192 18003 15392 16603 -4260 5660 -464 N
ATOM 1385 CZ ARG A 192 472.672 197.444 560.739 1.00124.03 C
ANISOU 1385 CZ ARG A 192 16824 14742 15559 -4277 5686 -556 C
ATOM 1386 NH1 ARG A 192 471.548 197.791 560.125 1.00119.39 N
ANISOU 1386 NH1 ARG A 192 15993 14278 15091 -4367 5702 -793 N
ATOM 1387 NH2 ARG A 192 472.965 197.967 561.922 1.00122.19 N
ANISOU 1387 NH2 ARG A 192 16609 14699 15118 -4199 5698 -414 N
ATOM 1388 N GLN A 193 475.572 193.013 555.345 1.00109.28 N
ANISOU 1388 N GLN A 193 15834 11159 14527 -4286 5627 -748 N
ATOM 1389 CA GLN A 193 475.648 191.561 555.412 1.00111.56 C
ANISOU 1389 CA GLN A 193 16359 11068 14959 -4443 5684 -619 C
ATOM 1390 C GLN A 193 476.769 190.979 554.558 1.00118.58 C
ANISOU 1390 C GLN A 193 17489 11616 15950 -4287 5656 -621 C
ATOM 1391 O GLN A 193 476.811 189.760 554.367 1.00119.41 O
ANISOU 1391 O GLN A 193 17788 11358 16225 -4401 5683 -576 O
ATOM 1392 CB GLN A 193 474.307 190.945 554.998 1.00106.61 C
ANISOU 1392 CB GLN A 193 15596 10395 14518 -4755 5740 -809 C
ATOM 1393 N SER A 194 477.674 191.814 554.043 1.00116.21 N
ANISOU 1393 N SER A 194 17179 11412 15563 -4023 5599 -667 N
ATOM 1394 CA SER A 194 478.811 191.330 553.271 1.00119.38 C
ANISOU 1394 CA SER A 194 17807 11508 16045 -3842 5582 -648 C
ATOM 1395 C SER A 194 480.075 191.170 554.103 1.00117.13 C
ANISOU 1395 C SER A 194 17750 11120 15635 -3615 5543 -304 C
ATOM 1396 O SER A 194 481.021 190.524 553.642 1.00129.58 O
ANISOU 1396 O SER A 194 19555 12386 17292 -3463 5533 -233 O
ATOM 1397 CB SER A 194 479.109 192.270 552.094 1.00125.98 C
ANISOU 1397 CB SER A 194 18491 12498 16878 -3687 5553 -882 C
ATOM 1398 OG SER A 194 478.924 193.624 552.461 1.00128.12 O
ANISOU 1398 OG SER A 194 18513 13185 16983 -3591 5500 -892 O
ATOM 1399 N GLU A 195 480.119 191.742 555.302 1.00109.00 N
ANISOU 1399 N GLU A 195 16658 10346 14411 -3578 5511 -102 N
ATOM 1400 CA GLU A 195 481.302 191.656 556.152 1.00109.18 C
ANISOU 1400 CA GLU A 195 16865 10324 14295 -3372 5454 221 C
ATOM 1401 C GLU A 195 481.521 190.231 556.655 1.00115.66 C
ANISOU 1401 C GLU A 195 17949 10784 15214 -3451 5487 461 C
ATOM 1402 O GLU A 195 480.637 189.380 556.547 1.00121.72 O
ANISOU 1402 O GLU A 195 18735 11370 16142 -3697 5553 394 O
ATOM 1403 CB GLU A 195 481.181 192.623 557.334 1.00104.45 C
ANISOU 1403 CB GLU A 195 16117 10104 13466 -3348 5406 341 C
ATOM 1404 CG GLU A 195 482.351 192.576 558.309 1.00110.89 C
ANISOU 1404 CG GLU A 195 17094 10922 14118 -3161 5333 671 C
ATOM 1405 CD GLU A 195 482.454 193.833 559.158 1.00107.63 C
ANISOU 1405 CD GLU A 195 16511 10905 13480 -3078 5259 703 C
ATOM 1406 OE1 GLU A 195 481.959 194.890 558.714 1.00101.06 O
ANISOU 1406 OE1 GLU A 195 15451 10307 12639 -3068 5235 460 O
ATOM 1407 OE2 GLU A 195 483.021 193.764 560.270 1.00107.92 O
ANISOU 1407 OE2 GLU A 195 16638 11014 13352 -3025 5218 969 O
TER 1408 GLU A 195
HETATM 1409 MN MN A 201 492.962 199.037 560.447 1.00 76.64 MN
ANISOU 1409 MN MN A 201 12559 7872 8688 -1132 4182 1876 MN
HETATM 1410 MN MN A 202 495.905 198.634 558.004 1.00 83.30 MN
ANISOU 1410 MN MN A 202 13417 8438 9795 -406 4035 2170 MN
HETATM 1411 C1 KU7 A 203 491.977 194.444 558.183 1.00 86.93 C
ANISOU 1411 C1 KU7 A 203 14500 7962 10567 -1171 4585 1893 C
HETATM 1412 C10 KU7 A 203 491.199 193.161 557.973 1.00 97.51 C
ANISOU 1412 C10 KU7 A 203 16021 8966 12063 -1335 4720 1851 C
HETATM 1413 C11 KU7 A 203 492.600 191.241 557.435 1.00109.19 C
ANISOU 1413 C11 KU7 A 203 17880 9860 13746 -1004 4720 2144 C
HETATM 1414 C12 KU7 A 203 491.515 192.522 555.593 1.00112.71 C
ANISOU 1414 C12 KU7 A 203 18063 10462 14301 -1113 4855 1606 C
HETATM 1415 C13 KU7 A 203 490.512 193.578 555.217 1.00120.83 C
ANISOU 1415 C13 KU7 A 203 18847 11758 15304 -1299 4897 1324 C
HETATM 1416 C14 KU7 A 203 488.886 197.946 557.013 1.00133.22 C
ANISOU 1416 C14 KU7 A 203 19578 14582 16459 -1603 4647 965 C
HETATM 1417 C15 KU7 A 203 490.174 198.165 556.558 1.00135.63 C
ANISOU 1417 C15 KU7 A 203 19902 14870 16760 -1338 4565 1106 C
HETATM 1418 C16 KU7 A 203 490.873 197.128 555.988 1.00133.96 C
ANISOU 1418 C16 KU7 A 203 19892 14375 16632 -1195 4615 1237 C
HETATM 1419 C17 KU7 A 203 490.326 195.858 555.850 1.00136.71 C
ANISOU 1419 C17 KU7 A 203 20440 14420 17085 -1324 4742 1222 C
HETATM 1420 C18 KU7 A 203 489.033 195.657 556.318 1.00136.44 C
ANISOU 1420 C18 KU7 A 203 20375 14406 17060 -1615 4816 1085 C
HETATM 1421 C19 KU7 A 203 488.320 196.701 556.893 1.00132.40 C
ANISOU 1421 C19 KU7 A 203 19648 14209 16449 -1745 4771 962 C
HETATM 1422 C2 KU7 A 203 493.887 195.670 557.753 1.00 74.59 C
ANISOU 1422 C2 KU7 A 203 12779 6647 8913 -744 4385 2045 C
HETATM 1423 C20 KU7 A 203 492.761 193.778 550.377 1.00107.35 C
ANISOU 1423 C20 KU7 A 203 16897 10023 13868 -286 4707 854 C
HETATM 1424 C21 KU7 A 203 492.861 192.618 551.108 1.00112.74 C
ANISOU 1424 C21 KU7 A 203 17876 10344 14617 -351 4777 1025 C
HETATM 1425 C22 KU7 A 203 493.701 192.547 552.207 1.00114.51 C
ANISOU 1425 C22 KU7 A 203 18218 10540 14751 -267 4750 1385 C
HETATM 1426 C23 KU7 A 203 494.451 193.657 552.564 1.00111.09 C
ANISOU 1426 C23 KU7 A 203 17599 10444 14165 -129 4644 1547 C
HETATM 1427 C24 KU7 A 203 494.348 194.831 551.832 1.00106.11 C
ANISOU 1427 C24 KU7 A 203 16674 10149 13493 -79 4575 1367 C
HETATM 1428 C25 KU7 A 203 493.502 194.878 550.737 1.00102.32 C
ANISOU 1428 C25 KU7 A 203 16083 9694 13100 -151 4611 1034 C
HETATM 1429 C3 KU7 A 203 493.450 196.706 558.523 1.00 70.43 C
ANISOU 1429 C3 KU7 A 203 12087 6427 8247 -894 4327 1973 C
HETATM 1430 C4 KU7 A 203 492.218 196.619 559.166 1.00 74.56 C
ANISOU 1430 C4 KU7 A 203 12603 6997 8729 -1176 4407 1856 C
HETATM 1431 C5 KU7 A 203 495.210 195.731 557.036 1.00 80.06 C
ANISOU 1431 C5 KU7 A 203 13467 7305 9649 -412 4311 2179 C
HETATM 1432 C6 KU7 A 203 496.598 194.637 555.338 1.00 94.20 C
ANISOU 1432 C6 KU7 A 203 15427 8713 11652 66 4367 2301 C
HETATM 1433 C7 KU7 A 203 496.159 194.695 553.897 1.00102.60 C
ANISOU 1433 C7 KU7 A 203 16430 9702 12853 111 4466 2035 C
HETATM 1434 C8 KU7 A 203 492.654 191.545 558.916 1.00107.26 C
ANISOU 1434 C8 KU7 A 203 17588 9875 13291 -1103 4625 2361 C
HETATM 1435 C9 KU7 A 203 491.294 192.182 559.154 1.00102.69 C
ANISOU 1435 C9 KU7 A 203 16851 9504 12662 -1411 4702 2132 C
HETATM 1436 F1 KU7 A 203 492.128 197.328 555.541 1.00131.03 F
ANISOU 1436 F1 KU7 A 203 19525 14006 16256 -916 4539 1387 F
HETATM 1437 N1 KU7 A 203 493.164 194.554 557.583 1.00 82.02 N
ANISOU 1437 N1 KU7 A 203 13892 7302 9971 -879 4514 1996 N
HETATM 1438 N2 KU7 A 203 491.501 195.458 558.969 1.00 73.82 N
ANISOU 1438 N2 KU7 A 203 12665 6630 8754 -1310 4535 1828 N
HETATM 1439 N3 KU7 A 203 495.466 194.689 556.249 1.00 88.48 N
ANISOU 1439 N3 KU7 A 203 14706 8051 10861 -273 4397 2207 N
HETATM 1440 N4 KU7 A 203 491.767 192.327 556.898 1.00106.91 N
ANISOU 1440 N4 KU7 A 203 17375 9812 13435 -1147 4770 1850 N
HETATM 1441 O1 KU7 A 203 494.142 197.838 558.720 1.00 68.48 O
ANISOU 1441 O1 KU7 A 203 11677 6441 7903 -784 4198 2008 O
HETATM 1442 O2 KU7 A 203 491.751 197.515 559.886 1.00 70.87 O
ANISOU 1442 O2 KU7 A 203 11995 6796 8135 -1305 4374 1777 O
HETATM 1443 O3 KU7 A 203 495.957 196.701 557.158 1.00 72.81 O
ANISOU 1443 O3 KU7 A 203 12386 6634 8645 -284 4184 2246 O
HETATM 1444 O4 KU7 A 203 495.278 193.595 553.653 1.00111.39 O
ANISOU 1444 O4 KU7 A 203 17743 10482 14099 -53 4599 1891 O
HETATM 1445 O5 KU7 A 203 491.089 194.875 555.282 1.00132.88 O
ANISOU 1445 O5 KU7 A 203 20165 13626 16698 -1151 4784 1346 O
HETATM 1446 O6 KU7 A 203 492.068 191.836 554.740 1.00115.83 O
ANISOU 1446 O6 KU7 A 203 18608 10567 14834 -930 4897 1610 O
HETATM 1447 O HOH A 301 496.473 197.576 559.933 1.00 65.23 O
HETATM 1448 O HOH A 302 498.323 198.860 558.029 1.00 80.30 O
ANISOU 1448 O HOH A 302 12983 8166 9362 36 3799 2572 O
HETATM 1449 O HOH A 303 492.653 205.170 570.996 1.00 90.21 O
HETATM 1450 O HOH A 304 489.025 197.983 560.146 1.00 74.55 O
ANISOU 1450 O HOH A 304 12256 7435 8633 -1776 4559 1336 O
HETATM 1451 O HOH A 305 509.171 210.188 559.402 1.00 69.93 O
HETATM 1452 O HOH A 306 493.916 219.858 561.800 1.00 90.11 O
HETATM 1453 O HOH A 307 485.140 213.688 547.602 1.00 90.07 O
HETATM 1454 O HOH A 308 484.641 213.007 544.380 1.00 98.75 O
CONECT 356 1409
CONECT 516 1410
CONECT 724 1409
CONECT 725 1409 1410
CONECT 830 1409
CONECT 834 1409
CONECT 1409 356 724 725 830
CONECT 1409 834 1441 1442
CONECT 1410 516 725 1441 1443
CONECT 1410 1447 1448
CONECT 1411 1412 1437 1438
CONECT 1412 1411 1435 1440
CONECT 1413 1434 1440
CONECT 1414 1415 1440 1446
CONECT 1415 1414 1445
CONECT 1416 1417 1421
CONECT 1417 1416 1418
CONECT 1418 1417 1419 1436
CONECT 1419 1418 1420 1445
CONECT 1420 1419 1421
CONECT 1421 1416 1420
CONECT 1422 1429 1431 1437
CONECT 1423 1424 1428
CONECT 1424 1423 1425
CONECT 1425 1424 1426
CONECT 1426 1425 1427 1444
CONECT 1427 1426 1428
CONECT 1428 1423 1427
CONECT 1429 1422 1430 1441
CONECT 1430 1429 1438 1442
CONECT 1431 1422 1439 1443
CONECT 1432 1433 1439
CONECT 1433 1432 1444
CONECT 1434 1413 1435
CONECT 1435 1412 1434
CONECT 1436 1418
CONECT 1437 1411 1422
CONECT 1438 1411 1430
CONECT 1439 1431 1432
CONECT 1440 1412 1413 1414
CONECT 1441 1409 1410 1429
CONECT 1442 1409 1430
CONECT 1443 1410 1431
CONECT 1444 1426 1433
CONECT 1445 1415 1419
CONECT 1446 1414
CONECT 1447 1410
CONECT 1448 1410
MASTER 379 0 3 8 5 0 8 6 1453 1 48 16
END
Reference in New Issue View Git Blame Copy Permalink