*** TLR4/MD2/Jor ***
Job options:
ID = 2403031258591421088
JOBID = TLR4/MD2/Jor
USERID = unknown
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = 0
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
HEADER TLR4/MD2/Jor
HEADER IMMUNE SYSTEM 17-MAR-12 3VQ1
TITLE CRYSTAL STRUCTURE OF MOUSE TLR4/MD-2/LIPID IVA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOLL-LIKE RECEPTOR 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 22-627;
COMPND 5 SYNONYM: TLR4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: LYMPHOCYTE ANTIGEN 96;
COMPND 9 CHAIN: C, D;
COMPND 10 SYNONYM: LY-96, ESOP-1, PROTEIN MD-2;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: TLR4;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7215;
SOURCE 8 EXPRESSION_SYSTEM_CELL: S2;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 GENE: MD2;
SOURCE 14 EXPRESSION_SYSTEM: DROSOPHILA;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7215;
SOURCE 16 EXPRESSION_SYSTEM_CELL: S2
KEYWDS LEUCINE RICH REPEAT MD-2 RELATED LIPID RECOGNITION, RECEPTOR INNATE
KEYWDS 2 IMMUNITY, LIPID BINDING, GLYCOSYLATION, SECRETED, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR U.OHTO,T.SHIMIZU
REVDAT 4 08-NOV-23 3VQ1 1 REMARK HETSYN
REVDAT 3 29-JUL-20 3VQ1 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 17-JUL-13 3VQ1 1 JRNL
REVDAT 1 09-MAY-12 3VQ1 0
JRNL AUTH U.OHTO,K.FUKASE,K.MIYAKE,T.SHIMIZU
JRNL TITL STRUCTURAL BASIS OF SPECIES-SPECIFIC ENDOTOXIN SENSING BY
JRNL TITL 2 INNATE IMMUNE RECEPTOR TLR4/MD-2
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 7421 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22532668
JRNL DOI 10.1073/PNAS.1201193109
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 54275
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2877
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3678
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.3200
REMARK 3 BIN FREE R VALUE SET COUNT : 200
REMARK 3 BIN FREE R VALUE : 0.3730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11682
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 298
REMARK 3 SOLVENT ATOMS : 37
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.76000
REMARK 3 B22 (A**2) : -1.25000
REMARK 3 B33 (A**2) : 3.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.947
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.364
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.268
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.394
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12396 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 42 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16788 ; 1.424 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 72 ; 0.742 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1468 ; 6.306 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 554 ;38.677 ;24.982
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2096 ;19.569 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;22.476 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1949 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9099 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 27 A 625
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7453 18.1942 29.5376
REMARK 3 T TENSOR
REMARK 3 T11: 0.0857 T22: 0.1255
REMARK 3 T33: 0.1097 T12: -0.0069
REMARK 3 T13: 0.0031 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 0.1650 L22: 0.2250
REMARK 3 L33: 0.0154 L12: 0.1201
REMARK 3 L13: 0.0366 L23: 0.0109
REMARK 3 S TENSOR
REMARK 3 S11: 0.0273 S12: -0.0440 S13: -0.0171
REMARK 3 S21: 0.0132 S22: -0.0222 S23: -0.0006
REMARK 3 S31: -0.0145 S32: -0.0095 S33: -0.0051
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 21 C 155
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2451 35.0950 20.3753
REMARK 3 T TENSOR
REMARK 3 T11: 0.0690 T22: 0.1045
REMARK 3 T33: 0.1431 T12: 0.0131
REMARK 3 T13: 0.0138 T23: -0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 0.5577 L22: 0.4034
REMARK 3 L33: 0.2873 L12: 0.1973
REMARK 3 L13: 0.2494 L23: 0.1127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0631 S12: -0.0363 S13: 0.0566
REMARK 3 S21: 0.0080 S22: -0.1623 S23: 0.0792
REMARK 3 S31: -0.0268 S32: -0.0104 S33: 0.0992
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 27 B 625
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2332 -4.4280 -13.5706
REMARK 3 T TENSOR
REMARK 3 T11: 0.1107 T22: 0.1029
REMARK 3 T33: 0.1211 T12: 0.0275
REMARK 3 T13: -0.0133 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.0811 L22: 0.1196
REMARK 3 L33: 0.0904 L12: -0.0341
REMARK 3 L13: -0.0651 L23: -0.0125
REMARK 3 S TENSOR
REMARK 3 S11: 0.0222 S12: -0.0187 S13: -0.0048
REMARK 3 S21: -0.0898 S22: -0.0292 S23: 0.0283
REMARK 3 S31: 0.0038 S32: -0.0081 S33: 0.0070
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 21 D 155
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2528 -20.9925 -4.8714
REMARK 3 T TENSOR
REMARK 3 T11: 0.1817 T22: 0.0319
REMARK 3 T33: 0.1101 T12: 0.0059
REMARK 3 T13: 0.0203 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 0.4041 L22: 0.2083
REMARK 3 L33: 0.7400 L12: -0.1956
REMARK 3 L13: 0.0984 L23: 0.0714
REMARK 3 S TENSOR
REMARK 3 S11: 0.0614 S12: 0.0314 S13: -0.0033
REMARK 3 S21: -0.0141 S22: -0.0775 S23: -0.0326
REMARK 3 S31: 0.1727 S32: -0.0275 S33: 0.0160
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3VQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000095357.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54275
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 116.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.14700
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: MOLREP
REMARK 200 STARTING MODEL: 2Z64
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG4000, 0.2M NA ACETATE, 0.1M
REMARK 280 TRIS-HCL, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 38.58000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.92350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.25950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.92350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.58000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 75.25950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D, E, F, G
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 PRO A 22
REMARK 465 GLY A 23
REMARK 465 SER A 24
REMARK 465 LEU A 25
REMARK 465 ASN A 26
REMARK 465 VAL A 610
REMARK 465 GLU A 611
REMARK 465 MET A 612
REMARK 465 TYR A 626
REMARK 465 MET A 627
REMARK 465 GLU C 17
REMARK 465 SER C 18
REMARK 465 GLU C 19
REMARK 465 LYS C 20
REMARK 465 ARG C 156
REMARK 465 ARG C 157
REMARK 465 ASP C 158
REMARK 465 VAL C 159
REMARK 465 ASN C 160
REMARK 465 PRO B 22
REMARK 465 GLY B 23
REMARK 465 SER B 24
REMARK 465 LEU B 25
REMARK 465 ASN B 26
REMARK 465 VAL B 610
REMARK 465 GLU B 611
REMARK 465 MET B 612
REMARK 465 TYR B 626
REMARK 465 MET B 627
REMARK 465 GLU D 17
REMARK 465 SER D 18
REMARK 465 GLU D 19
REMARK 465 LYS D 20
REMARK 465 ARG D 156
REMARK 465 ARG D 157
REMARK 465 ASP D 158
REMARK 465 VAL D 159
REMARK 465 ASN D 160
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 THR A 614 CB OG1 CG2
REMARK 480 THR B 614 CB OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND2 ASN A 204 O5 NAG E 1 1.47
REMARK 500 ND2 ASN A 524 C2 NAG F 1 1.48
REMARK 500 OD1 ASN A 524 C1 NAG F 1 1.49
REMARK 500 CG ASN A 524 C1 NAG F 1 1.58
REMARK 500 O5 LP4 C 300 O6 LP5 C 301 1.90
REMARK 500 O5 LP4 D 300 O6 LP5 D 301 1.94
REMARK 500 NZ LYS A 263 O46 LP4 C 300 2.04
REMARK 500 ND2 ASN A 524 N2 NAG F 1 2.08
REMARK 500 C2 LP4 D 300 O6 LP5 D 301 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 34 -3.16 68.80
REMARK 500 ILE A 35 -52.02 -131.46
REMARK 500 LYS A 43 41.74 -103.36
REMARK 500 PRO A 52 122.75 -37.49
REMARK 500 SER A 54 -11.44 -153.45
REMARK 500 PRO A 64 71.65 -68.76
REMARK 500 LYS A 66 -54.37 68.41
REMARK 500 TYR A 71 -3.30 74.53
REMARK 500 THR A 109 131.55 -35.93
REMARK 500 ASN A 159 -158.84 -128.99
REMARK 500 ASN A 184 -163.31 -122.68
REMARK 500 ASN A 200 77.76 -113.71
REMARK 500 PRO A 201 2.20 -69.08
REMARK 500 PHE A 216 119.58 -162.56
REMARK 500 GLU A 265 72.57 -165.20
REMARK 500 ARG A 266 -97.48 -86.09
REMARK 500 ASN A 267 -45.77 97.07
REMARK 500 SER A 317 5.01 -67.76
REMARK 500 GLU A 322 -17.92 -140.96
REMARK 500 CYS A 338 -168.97 -104.87
REMARK 500 LYS A 367 127.70 -31.19
REMARK 500 SER A 413 -15.26 -143.47
REMARK 500 GLU A 420 1.32 -68.82
REMARK 500 GLN A 428 130.34 -36.74
REMARK 500 ASN A 456 47.12 70.83
REMARK 500 LEU A 468 52.69 -90.28
REMARK 500 MET A 476 38.08 -141.01
REMARK 500 ASN A 479 -140.53 -119.73
REMARK 500 ASN A 484 26.68 46.77
REMARK 500 ASN A 528 -165.24 -110.11
REMARK 500 GLN A 540 -5.34 91.03
REMARK 500 ASN A 552 -150.42 -101.60
REMARK 500 ILE A 560 107.54 65.60
REMARK 500 LEU A 568 101.77 -57.97
REMARK 500 ASN A 576 -160.99 -106.61
REMARK 500 CYS A 580 47.34 -93.54
REMARK 500 GLN A 594 40.99 -88.32
REMARK 500 THR A 608 -162.85 -121.61
REMARK 500 SER A 615 -127.56 -109.96
REMARK 500 LEU A 616 -56.59 -143.17
REMARK 500 ASN A 622 -101.86 -133.12
REMARK 500 THR A 624 -53.73 54.76
REMARK 500 SER C 28 -9.95 -56.74
REMARK 500 ASP C 29 14.47 -149.59
REMARK 500 SER C 84 -8.26 67.75
REMARK 500 LYS C 128 52.71 75.17
REMARK 500 GLU C 143 18.67 58.99
REMARK 500 CYS B 28 -144.07 -120.12
REMARK 500 ASN B 34 5.09 59.30
REMARK 500 ILE B 35 -54.96 -131.08
REMARK 500
REMARK 500 THIS ENTRY HAS 91 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 323 VAL A 324 -149.72
REMARK 500 THR A 608 PRO A 609 -146.23
REMARK 500 THR B 608 PRO B 609 -141.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG A 705
REMARK 610 LP4 C 300
REMARK 610 LP4 D 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VQ2 RELATED DB: PDB
DBREF 3VQ1 A 22 627 UNP Q9QUK6 TLR4_MOUSE 22 627
DBREF 3VQ1 C 17 160 UNP Q9JHF9 LY96_MOUSE 17 160
DBREF 3VQ1 B 22 627 UNP Q9QUK6 TLR4_MOUSE 22 627
DBREF 3VQ1 D 17 160 UNP Q9JHF9 LY96_MOUSE 17 160
SEQRES 1 A 606 PRO GLY SER LEU ASN PRO CYS ILE GLU VAL VAL PRO ASN
SEQRES 2 A 606 ILE THR TYR GLN CYS MET ASP GLN LYS LEU SER LYS VAL
SEQRES 3 A 606 PRO ASP ASP ILE PRO SER SER THR LYS ASN ILE ASP LEU
SEQRES 4 A 606 SER PHE ASN PRO LEU LYS ILE LEU LYS SER TYR SER PHE
SEQRES 5 A 606 SER ASN PHE SER GLU LEU GLN TRP LEU ASP LEU SER ARG
SEQRES 6 A 606 CYS GLU ILE GLU THR ILE GLU ASP LYS ALA TRP HIS GLY
SEQRES 7 A 606 LEU HIS HIS LEU SER ASN LEU ILE LEU THR GLY ASN PRO
SEQRES 8 A 606 ILE GLN SER PHE SER PRO GLY SER PHE SER GLY LEU THR
SEQRES 9 A 606 SER LEU GLU ASN LEU VAL ALA VAL GLU THR LYS LEU ALA
SEQRES 10 A 606 SER LEU GLU SER PHE PRO ILE GLY GLN LEU ILE THR LEU
SEQRES 11 A 606 LYS LYS LEU ASN VAL ALA HIS ASN PHE ILE HIS SER CYS
SEQRES 12 A 606 LYS LEU PRO ALA TYR PHE SER ASN LEU THR ASN LEU VAL
SEQRES 13 A 606 HIS VAL ASP LEU SER TYR ASN TYR ILE GLN THR ILE THR
SEQRES 14 A 606 VAL ASN ASP LEU GLN PHE LEU ARG GLU ASN PRO GLN VAL
SEQRES 15 A 606 ASN LEU SER LEU ASP MET SER LEU ASN PRO ILE ASP PHE
SEQRES 16 A 606 ILE GLN ASP GLN ALA PHE GLN GLY ILE LYS LEU HIS GLU
SEQRES 17 A 606 LEU THR LEU ARG GLY ASN PHE ASN SER SER ASN ILE MET
SEQRES 18 A 606 LYS THR CYS LEU GLN ASN LEU ALA GLY LEU HIS VAL HIS
SEQRES 19 A 606 ARG LEU ILE LEU GLY GLU PHE LYS ASP GLU ARG ASN LEU
SEQRES 20 A 606 GLU ILE PHE GLU PRO SER ILE MET GLU GLY LEU CYS ASP
SEQRES 21 A 606 VAL THR ILE ASP GLU PHE ARG LEU THR TYR THR ASN ASP
SEQRES 22 A 606 PHE SER ASP ASP ILE VAL LYS PHE HIS CYS LEU ALA ASN
SEQRES 23 A 606 VAL SER ALA MET SER LEU ALA GLY VAL SER ILE LYS TYR
SEQRES 24 A 606 LEU GLU ASP VAL PRO LYS HIS PHE LYS TRP GLN SER LEU
SEQRES 25 A 606 SER ILE ILE ARG CYS GLN LEU LYS GLN PHE PRO THR LEU
SEQRES 26 A 606 ASP LEU PRO PHE LEU LYS SER LEU THR LEU THR MET ASN
SEQRES 27 A 606 LYS GLY SER ILE SER PHE LYS LYS VAL ALA LEU PRO SER
SEQRES 28 A 606 LEU SER TYR LEU ASP LEU SER ARG ASN ALA LEU SER PHE
SEQRES 29 A 606 SER GLY CYS CYS SER TYR SER ASP LEU GLY THR ASN SER
SEQRES 30 A 606 LEU ARG HIS LEU ASP LEU SER PHE ASN GLY ALA ILE ILE
SEQRES 31 A 606 MET SER ALA ASN PHE MET GLY LEU GLU GLU LEU GLN HIS
SEQRES 32 A 606 LEU ASP PHE GLN HIS SER THR LEU LYS ARG VAL THR GLU
SEQRES 33 A 606 PHE SER ALA PHE LEU SER LEU GLU LYS LEU LEU TYR LEU
SEQRES 34 A 606 ASP ILE SER TYR THR ASN THR LYS ILE ASP PHE ASP GLY
SEQRES 35 A 606 ILE PHE LEU GLY LEU THR SER LEU ASN THR LEU LYS MET
SEQRES 36 A 606 ALA GLY ASN SER PHE LYS ASP ASN THR LEU SER ASN VAL
SEQRES 37 A 606 PHE ALA ASN THR THR ASN LEU THR PHE LEU ASP LEU SER
SEQRES 38 A 606 LYS CYS GLN LEU GLU GLN ILE SER TRP GLY VAL PHE ASP
SEQRES 39 A 606 THR LEU HIS ARG LEU GLN LEU LEU ASN MET SER HIS ASN
SEQRES 40 A 606 ASN LEU LEU PHE LEU ASP SER SER HIS TYR ASN GLN LEU
SEQRES 41 A 606 TYR SER LEU SER THR LEU ASP CYS SER PHE ASN ARG ILE
SEQRES 42 A 606 GLU THR SER LYS GLY ILE LEU GLN HIS PHE PRO LYS SER
SEQRES 43 A 606 LEU ALA PHE PHE ASN LEU THR ASN ASN SER VAL ALA CYS
SEQRES 44 A 606 ILE CYS GLU HIS GLN LYS PHE LEU GLN TRP VAL LYS GLU
SEQRES 45 A 606 GLN LYS GLN PHE LEU VAL ASN VAL GLU GLN MET THR CYS
SEQRES 46 A 606 ALA THR PRO VAL GLU MET ASN THR SER LEU VAL LEU ASP
SEQRES 47 A 606 PHE ASN ASN SER THR CYS TYR MET
SEQRES 1 C 144 GLU SER GLU LYS GLN GLN TRP PHE CYS ASN SER SER ASP
SEQRES 2 C 144 ALA ILE ILE SER TYR SER TYR CYS ASP HIS LEU LYS PHE
SEQRES 3 C 144 PRO ILE SER ILE SER SER GLU PRO CYS ILE ARG LEU ARG
SEQRES 4 C 144 GLY THR ASN GLY PHE VAL HIS VAL GLU PHE ILE PRO ARG
SEQRES 5 C 144 GLY ASN LEU LYS TYR LEU TYR PHE ASN LEU PHE ILE SER
SEQRES 6 C 144 VAL ASN SER ILE GLU LEU PRO LYS ARG LYS GLU VAL LEU
SEQRES 7 C 144 CYS HIS GLY HIS ASP ASP ASP TYR SER PHE CYS ARG ALA
SEQRES 8 C 144 LEU LYS GLY GLU THR VAL ASN THR SER ILE PRO PHE SER
SEQRES 9 C 144 PHE GLU GLY ILE LEU PHE PRO LYS GLY HIS TYR ARG CYS
SEQRES 10 C 144 VAL ALA GLU ALA ILE ALA GLY ASP THR GLU GLU LYS LEU
SEQRES 11 C 144 PHE CYS LEU ASN PHE THR ILE ILE HIS ARG ARG ASP VAL
SEQRES 12 C 144 ASN
SEQRES 1 B 606 PRO GLY SER LEU ASN PRO CYS ILE GLU VAL VAL PRO ASN
SEQRES 2 B 606 ILE THR TYR GLN CYS MET ASP GLN LYS LEU SER LYS VAL
SEQRES 3 B 606 PRO ASP ASP ILE PRO SER SER THR LYS ASN ILE ASP LEU
SEQRES 4 B 606 SER PHE ASN PRO LEU LYS ILE LEU LYS SER TYR SER PHE
SEQRES 5 B 606 SER ASN PHE SER GLU LEU GLN TRP LEU ASP LEU SER ARG
SEQRES 6 B 606 CYS GLU ILE GLU THR ILE GLU ASP LYS ALA TRP HIS GLY
SEQRES 7 B 606 LEU HIS HIS LEU SER ASN LEU ILE LEU THR GLY ASN PRO
SEQRES 8 B 606 ILE GLN SER PHE SER PRO GLY SER PHE SER GLY LEU THR
SEQRES 9 B 606 SER LEU GLU ASN LEU VAL ALA VAL GLU THR LYS LEU ALA
SEQRES 10 B 606 SER LEU GLU SER PHE PRO ILE GLY GLN LEU ILE THR LEU
SEQRES 11 B 606 LYS LYS LEU ASN VAL ALA HIS ASN PHE ILE HIS SER CYS
SEQRES 12 B 606 LYS LEU PRO ALA TYR PHE SER ASN LEU THR ASN LEU VAL
SEQRES 13 B 606 HIS VAL ASP LEU SER TYR ASN TYR ILE GLN THR ILE THR
SEQRES 14 B 606 VAL ASN ASP LEU GLN PHE LEU ARG GLU ASN PRO GLN VAL
SEQRES 15 B 606 ASN LEU SER LEU ASP MET SER LEU ASN PRO ILE ASP PHE
SEQRES 16 B 606 ILE GLN ASP GLN ALA PHE GLN GLY ILE LYS LEU HIS GLU
SEQRES 17 B 606 LEU THR LEU ARG GLY ASN PHE ASN SER SER ASN ILE MET
SEQRES 18 B 606 LYS THR CYS LEU GLN ASN LEU ALA GLY LEU HIS VAL HIS
SEQRES 19 B 606 ARG LEU ILE LEU GLY GLU PHE LYS ASP GLU ARG ASN LEU
SEQRES 20 B 606 GLU ILE PHE GLU PRO SER ILE MET GLU GLY LEU CYS ASP
SEQRES 21 B 606 VAL THR ILE ASP GLU PHE ARG LEU THR TYR THR ASN ASP
SEQRES 22 B 606 PHE SER ASP ASP ILE VAL LYS PHE HIS CYS LEU ALA ASN
SEQRES 23 B 606 VAL SER ALA MET SER LEU ALA GLY VAL SER ILE LYS TYR
SEQRES 24 B 606 LEU GLU ASP VAL PRO LYS HIS PHE LYS TRP GLN SER LEU
SEQRES 25 B 606 SER ILE ILE ARG CYS GLN LEU LYS GLN PHE PRO THR LEU
SEQRES 26 B 606 ASP LEU PRO PHE LEU LYS SER LEU THR LEU THR MET ASN
SEQRES 27 B 606 LYS GLY SER ILE SER PHE LYS LYS VAL ALA LEU PRO SER
SEQRES 28 B 606 LEU SER TYR LEU ASP LEU SER ARG ASN ALA LEU SER PHE
SEQRES 29 B 606 SER GLY CYS CYS SER TYR SER ASP LEU GLY THR ASN SER
SEQRES 30 B 606 LEU ARG HIS LEU ASP LEU SER PHE ASN GLY ALA ILE ILE
SEQRES 31 B 606 MET SER ALA ASN PHE MET GLY LEU GLU GLU LEU GLN HIS
SEQRES 32 B 606 LEU ASP PHE GLN HIS SER THR LEU LYS ARG VAL THR GLU
SEQRES 33 B 606 PHE SER ALA PHE LEU SER LEU GLU LYS LEU LEU TYR LEU
SEQRES 34 B 606 ASP ILE SER TYR THR ASN THR LYS ILE ASP PHE ASP GLY
SEQRES 35 B 606 ILE PHE LEU GLY LEU THR SER LEU ASN THR LEU LYS MET
SEQRES 36 B 606 ALA GLY ASN SER PHE LYS ASP ASN THR LEU SER ASN VAL
SEQRES 37 B 606 PHE ALA ASN THR THR ASN LEU THR PHE LEU ASP LEU SER
SEQRES 38 B 606 LYS CYS GLN LEU GLU GLN ILE SER TRP GLY VAL PHE ASP
SEQRES 39 B 606 THR LEU HIS ARG LEU GLN LEU LEU ASN MET SER HIS ASN
SEQRES 40 B 606 ASN LEU LEU PHE LEU ASP SER SER HIS TYR ASN GLN LEU
SEQRES 41 B 606 TYR SER LEU SER THR LEU ASP CYS SER PHE ASN ARG ILE
SEQRES 42 B 606 GLU THR SER LYS GLY ILE LEU GLN HIS PHE PRO LYS SER
SEQRES 43 B 606 LEU ALA PHE PHE ASN LEU THR ASN ASN SER VAL ALA CYS
SEQRES 44 B 606 ILE CYS GLU HIS GLN LYS PHE LEU GLN TRP VAL LYS GLU
SEQRES 45 B 606 GLN LYS GLN PHE LEU VAL ASN VAL GLU GLN MET THR CYS
SEQRES 46 B 606 ALA THR PRO VAL GLU MET ASN THR SER LEU VAL LEU ASP
SEQRES 47 B 606 PHE ASN ASN SER THR CYS TYR MET
SEQRES 1 D 144 GLU SER GLU LYS GLN GLN TRP PHE CYS ASN SER SER ASP
SEQRES 2 D 144 ALA ILE ILE SER TYR SER TYR CYS ASP HIS LEU LYS PHE
SEQRES 3 D 144 PRO ILE SER ILE SER SER GLU PRO CYS ILE ARG LEU ARG
SEQRES 4 D 144 GLY THR ASN GLY PHE VAL HIS VAL GLU PHE ILE PRO ARG
SEQRES 5 D 144 GLY ASN LEU LYS TYR LEU TYR PHE ASN LEU PHE ILE SER
SEQRES 6 D 144 VAL ASN SER ILE GLU LEU PRO LYS ARG LYS GLU VAL LEU
SEQRES 7 D 144 CYS HIS GLY HIS ASP ASP ASP TYR SER PHE CYS ARG ALA
SEQRES 8 D 144 LEU LYS GLY GLU THR VAL ASN THR SER ILE PRO PHE SER
SEQRES 9 D 144 PHE GLU GLY ILE LEU PHE PRO LYS GLY HIS TYR ARG CYS
SEQRES 10 D 144 VAL ALA GLU ALA ILE ALA GLY ASP THR GLU GLU LYS LEU
SEQRES 11 D 144 PHE CYS LEU ASN PHE THR ILE ILE HIS ARG ARG ASP VAL
SEQRES 12 D 144 ASN
MODRES 3VQ1 ASN A 204 ASN GLYCOSYLATION SITE
MODRES 3VQ1 ASN A 524 ASN GLYCOSYLATION SITE
MODRES 3VQ1 ASN B 524 ASN GLYCOSYLATION SITE
MODRES 3VQ1 ASN B 572 ASN GLYCOSYLATION SITE
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG A 705 14
HET LP4 C 300 45
HET LP5 C 301 48
HET NAG B 802 14
HET LP4 D 300 45
HET LP5 D 301 48
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM LP4 2-DEOXY-3-O-[(3R)-3-HYDROXYTETRADECANOYL]-2-{[(3R)-3-
HETNAM 2 LP4 HYDROXYTETRADECANOYL]AMINO}-4-O-PHOSPHONO-BETA-D-
HETNAM 3 LP4 GLUCOPYRANOSE
HETNAM LP5 (R)-((2R,3S,4R,5R,6R)-3-HYDROXY-2-(HYDROXYMETHYL)-5-
HETNAM 2 LP5 ((R)-3-HYDROXYTETRADECANAMIDO)-6-(PHOSPHONOOXY)
HETNAM 3 LP5 TETRAHYDRO-2H-PYRAN-4-YL) 3-HYDROXYTETRADECANOATE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 5 NAG 8(C8 H15 N O6)
FORMUL 9 LP4 2(C34 H66 N O12 P)
FORMUL 10 LP5 2(C34 H66 N O12 P)
FORMUL 14 HOH *37(H2 O)
HELIX 1 1 PRO A 167 ASN A 172 5 6
HELIX 2 2 LEU A 194 ASN A 200 1 7
HELIX 3 3 SER A 238 GLN A 247 1 10
HELIX 4 4 ASN A 248 ALA A 250 5 3
HELIX 5 5 GLU A 272 ASP A 281 5 10
HELIX 6 6 SER A 296 VAL A 300 5 5
HELIX 7 7 PHE A 302 ALA A 306 5 5
HELIX 8 8 SER A 390 GLY A 395 1 6
HELIX 9 9 SER A 536 TYR A 538 5 3
HELIX 10 10 ILE A 560 PHE A 564 5 5
HELIX 11 11 ILE A 581 GLU A 583 5 3
HELIX 12 12 HIS A 584 GLN A 594 1 11
HELIX 13 13 ASN A 600 MET A 604 5 5
HELIX 14 14 TYR C 102 ALA C 107 5 6
HELIX 15 15 PRO B 167 ASN B 172 5 6
HELIX 16 16 LEU B 194 GLU B 199 1 6
HELIX 17 17 SER B 238 ASN B 248 1 11
HELIX 18 18 GLU B 272 VAL B 282 5 11
HELIX 19 19 SER B 296 VAL B 300 5 5
HELIX 20 20 PHE B 302 ALA B 306 5 5
HELIX 21 21 SER B 390 GLY B 395 1 6
HELIX 22 22 SER B 536 ASN B 539 5 4
HELIX 23 23 ILE B 560 PHE B 564 5 5
HELIX 24 24 ILE B 581 GLU B 583 5 3
HELIX 25 25 HIS B 584 GLN B 594 1 11
HELIX 26 26 TYR D 102 ALA D 107 5 6
SHEET 1 A25 ILE A 29 VAL A 32 0
SHEET 2 A25 THR A 36 GLN A 38 -1 O THR A 36 N VAL A 32
SHEET 3 A25 ASN A 57 ASP A 59 1 O ASN A 57 N TYR A 37
SHEET 4 A25 TRP A 81 ASP A 83 1 O TRP A 81 N ILE A 58
SHEET 5 A25 ASN A 105 ILE A 107 1 O ILE A 107 N LEU A 82
SHEET 6 A25 ASN A 129 VAL A 131 1 O VAL A 131 N LEU A 106
SHEET 7 A25 LYS A 153 ASN A 155 1 O ASN A 155 N LEU A 130
SHEET 8 A25 HIS A 178 ASP A 180 1 O ASP A 180 N LEU A 154
SHEET 9 A25 SER A 206 ASP A 208 1 O SER A 206 N VAL A 179
SHEET 10 A25 LYS A 226 ARG A 233 1 O GLU A 229 N LEU A 207
SHEET 11 A25 HIS A 253 GLY A 260 1 O ILE A 258 N LEU A 232
SHEET 12 A25 THR A 283 LEU A 289 1 O ARG A 288 N LEU A 257
SHEET 13 A25 ALA A 310 ALA A 314 1 O ALA A 310 N PHE A 287
SHEET 14 A25 SER A 332 ILE A 336 1 O ILE A 336 N LEU A 313
SHEET 15 A25 SER A 353 THR A 357 1 O THR A 355 N ILE A 335
SHEET 16 A25 TYR A 375 ASP A 377 1 O ASP A 377 N LEU A 356
SHEET 17 A25 HIS A 401 ASP A 403 1 O ASP A 403 N LEU A 376
SHEET 18 A25 HIS A 424 ASP A 426 1 O HIS A 424 N LEU A 402
SHEET 19 A25 TYR A 449 ASP A 451 1 O TYR A 449 N LEU A 425
SHEET 20 A25 THR A 473 LYS A 475 1 O THR A 473 N LEU A 450
SHEET 21 A25 PHE A 498 ASP A 500 1 O ASP A 500 N LEU A 474
SHEET 22 A25 LEU A 522 ASN A 524 1 O LEU A 522 N LEU A 499
SHEET 23 A25 THR A 546 ASP A 548 1 O ASP A 548 N LEU A 523
SHEET 24 A25 PHE A 570 ASN A 572 1 O PHE A 570 N LEU A 547
SHEET 25 A25 LEU A 598 VAL A 599 1 O VAL A 599 N PHE A 571
SHEET 1 B 2 ILE A 67 LEU A 68 0
SHEET 2 B 2 THR A 91 ILE A 92 1 O THR A 91 N LEU A 68
SHEET 1 C 2 THR A 188 ILE A 189 0
SHEET 2 C 2 PHE A 216 ILE A 217 1 O PHE A 216 N ILE A 189
SHEET 1 D 3 PHE A 385 CYS A 388 0
SHEET 2 D 3 ALA A 409 MET A 412 1 O ALA A 409 N PHE A 385
SHEET 3 D 3 THR A 431 LYS A 433 1 O THR A 431 N ILE A 410
SHEET 1 E 2 LYS A 458 ILE A 459 0
SHEET 2 E 2 SER A 480 PHE A 481 1 O SER A 480 N ILE A 459
SHEET 1 F 2 THR A 485 LEU A 486 0
SHEET 2 F 2 GLN A 508 ILE A 509 1 O GLN A 508 N LEU A 486
SHEET 1 G 2 LEU A 533 ASP A 534 0
SHEET 2 G 2 SER A 557 LYS A 558 1 O LYS A 558 N LEU A 533
SHEET 1 H 6 TRP C 23 SER C 27 0
SHEET 2 H 6 ALA C 30 TYR C 36 -1 O ALA C 30 N SER C 27
SHEET 3 H 6 GLU C 144 HIS C 155 -1 O ASN C 150 N SER C 35
SHEET 4 H 6 GLY C 129 ALA C 139 -1 N ALA C 137 O LEU C 146
SHEET 5 H 6 LEU C 74 VAL C 82 -1 N TYR C 75 O ILE C 138
SHEET 6 H 6 ILE C 85 GLU C 86 -1 O ILE C 85 N VAL C 82
SHEET 1 I 6 TRP C 23 SER C 27 0
SHEET 2 I 6 ALA C 30 TYR C 36 -1 O ALA C 30 N SER C 27
SHEET 3 I 6 GLU C 144 HIS C 155 -1 O ASN C 150 N SER C 35
SHEET 4 I 6 GLY C 129 ALA C 139 -1 N ALA C 137 O LEU C 146
SHEET 5 I 6 LEU C 74 VAL C 82 -1 N TYR C 75 O ILE C 138
SHEET 6 I 6 ARG C 90 VAL C 93 -1 O ARG C 90 N LEU C 78
SHEET 1 J 3 ILE C 44 GLU C 49 0
SHEET 2 J 3 THR C 57 PHE C 65 -1 O GLU C 64 N SER C 45
SHEET 3 J 3 VAL C 113 PHE C 121 -1 O ILE C 117 N VAL C 61
SHEET 1 K24 ILE B 29 VAL B 32 0
SHEET 2 K24 THR B 36 GLN B 38 -1 O GLN B 38 N ILE B 29
SHEET 3 K24 ASN B 57 ASP B 59 1 O ASN B 57 N TYR B 37
SHEET 4 K24 TRP B 81 ASP B 83 1 O TRP B 81 N ILE B 58
SHEET 5 K24 ASN B 105 ILE B 107 1 O ASN B 105 N LEU B 82
SHEET 6 K24 ASN B 129 VAL B 131 1 O VAL B 131 N LEU B 106
SHEET 7 K24 LYS B 153 ASN B 155 1 O ASN B 155 N LEU B 130
SHEET 8 K24 HIS B 178 ASP B 180 1 O HIS B 178 N LEU B 154
SHEET 9 K24 SER B 206 ASP B 208 1 O SER B 206 N VAL B 179
SHEET 10 K24 ILE B 225 ARG B 233 1 O GLU B 229 N LEU B 207
SHEET 11 K24 LEU B 252 GLY B 260 1 O ILE B 258 N LEU B 232
SHEET 12 K24 THR B 283 LEU B 289 1 O ARG B 288 N LEU B 259
SHEET 13 K24 ALA B 310 ALA B 314 1 O SER B 312 N LEU B 289
SHEET 14 K24 SER B 332 ILE B 336 1 O SER B 334 N LEU B 313
SHEET 15 K24 SER B 353 THR B 357 1 O THR B 355 N ILE B 335
SHEET 16 K24 TYR B 375 ASP B 377 1 O ASP B 377 N LEU B 356
SHEET 17 K24 HIS B 401 ASP B 403 1 O ASP B 403 N LEU B 376
SHEET 18 K24 HIS B 424 ASP B 426 1 O HIS B 424 N LEU B 402
SHEET 19 K24 TYR B 449 ASP B 451 1 O TYR B 449 N LEU B 425
SHEET 20 K24 THR B 473 LYS B 475 1 O LYS B 475 N LEU B 450
SHEET 21 K24 PHE B 498 ASP B 500 1 O PHE B 498 N LEU B 474
SHEET 22 K24 LEU B 522 ASN B 524 1 O ASN B 524 N LEU B 499
SHEET 23 K24 THR B 546 ASP B 548 1 O ASP B 548 N LEU B 523
SHEET 24 K24 PHE B 570 ASN B 572 1 O ASN B 572 N LEU B 547
SHEET 1 L 2 ILE B 67 LEU B 68 0
SHEET 2 L 2 THR B 91 ILE B 92 1 O THR B 91 N LEU B 68
SHEET 1 M 2 THR B 188 ILE B 189 0
SHEET 2 M 2 PHE B 216 ILE B 217 1 O PHE B 216 N ILE B 189
SHEET 1 N 3 PHE B 385 CYS B 388 0
SHEET 2 N 3 ALA B 409 MET B 412 1 O ILE B 411 N PHE B 385
SHEET 3 N 3 THR B 431 LYS B 433 1 O THR B 431 N ILE B 410
SHEET 1 O 2 LYS B 458 ILE B 459 0
SHEET 2 O 2 SER B 480 PHE B 481 1 O SER B 480 N ILE B 459
SHEET 1 P 2 THR B 485 LEU B 486 0
SHEET 2 P 2 GLN B 508 ILE B 509 1 O GLN B 508 N LEU B 486
SHEET 1 Q 2 LEU B 533 ASP B 534 0
SHEET 2 Q 2 SER B 557 LYS B 558 1 O LYS B 558 N LEU B 533
SHEET 1 R 6 TRP D 23 SER D 27 0
SHEET 2 R 6 ALA D 30 TYR D 36 -1 O ILE D 32 N CYS D 25
SHEET 3 R 6 GLU D 144 HIS D 155 -1 O ASN D 150 N SER D 35
SHEET 4 R 6 GLY D 129 ALA D 139 -1 N ALA D 137 O LEU D 146
SHEET 5 R 6 LEU D 74 VAL D 82 -1 N TYR D 75 O ILE D 138
SHEET 6 R 6 ILE D 85 GLU D 86 -1 O ILE D 85 N VAL D 82
SHEET 1 S 6 TRP D 23 SER D 27 0
SHEET 2 S 6 ALA D 30 TYR D 36 -1 O ILE D 32 N CYS D 25
SHEET 3 S 6 GLU D 144 HIS D 155 -1 O ASN D 150 N SER D 35
SHEET 4 S 6 GLY D 129 ALA D 139 -1 N ALA D 137 O LEU D 146
SHEET 5 S 6 LEU D 74 VAL D 82 -1 N TYR D 75 O ILE D 138
SHEET 6 S 6 ARG D 90 VAL D 93 -1 O GLU D 92 N PHE D 76
SHEET 1 T 3 ILE D 44 GLU D 49 0
SHEET 2 T 3 THR D 57 PHE D 65 -1 O HIS D 62 N SER D 47
SHEET 3 T 3 VAL D 113 PHE D 121 -1 O ILE D 117 N VAL D 61
SSBOND 1 CYS A 28 CYS A 39 1555 1555 2.04
SSBOND 2 CYS A 280 CYS A 304 1555 1555 2.03
SSBOND 3 CYS A 388 CYS A 389 1555 1555 2.07
SSBOND 4 CYS A 580 CYS A 606 1555 1555 2.05
SSBOND 5 CYS A 582 CYS A 625 1555 1555 2.05
SSBOND 6 CYS C 25 CYS C 51 1555 1555 2.03
SSBOND 7 CYS C 37 CYS C 148 1555 1555 2.06
SSBOND 8 CYS C 95 CYS C 105 1555 1555 2.07
SSBOND 9 CYS B 28 CYS B 39 1555 1555 2.04
SSBOND 10 CYS B 280 CYS B 304 1555 1555 2.05
SSBOND 11 CYS B 388 CYS B 389 1555 1555 2.02
SSBOND 12 CYS B 580 CYS B 606 1555 1555 2.05
SSBOND 13 CYS B 582 CYS B 625 1555 1555 2.05
SSBOND 14 CYS D 25 CYS D 51 1555 1555 2.05
SSBOND 15 CYS D 37 CYS D 148 1555 1555 2.05
SSBOND 16 CYS D 95 CYS D 105 1555 1555 2.04
LINK ND2 ASN A 204 C1 NAG E 1 1555 1555 1.37
LINK ND2 ASN A 524 C1 NAG F 1 1555 1555 1.40
LINK C1 LP4 C 300 O6 LP5 C 301 1555 1555 1.44
LINK ND2 ASN B 524 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN B 572 C1 NAG B 802 1555 1555 1.46
LINK C1 LP4 D 300 O6 LP5 D 301 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
CISPEP 1 CYS A 388 CYS A 389 0 -17.57
CISPEP 2 THR A 614 SER A 615 0 -8.37
CISPEP 3 GLU C 49 PRO C 50 0 -0.80
CISPEP 4 PRO C 127 LYS C 128 0 23.58
CISPEP 5 CYS B 388 CYS B 389 0 -8.07
CISPEP 6 THR B 614 SER B 615 0 -6.24
CISPEP 7 GLU D 49 PRO D 50 0 -3.65
CRYST1 77.160 150.519 181.847 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012960 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006644 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005499 0.00000
ATOM 1 N PRO A 27 -4.097 37.234 52.631 1.00 93.84 N
ANISOU 1 N PRO A 27 11585 12226 11840 -333 586 -297 N
ATOM 2 CA PRO A 27 -4.443 35.815 52.601 1.00 96.01 C
ANISOU 2 CA PRO A 27 11862 12514 12102 -339 578 -271 C
ATOM 3 C PRO A 27 -3.648 35.087 51.521 1.00 96.65 C
ANISOU 3 C PRO A 27 11950 12589 12182 -319 537 -231 C
ATOM 4 O PRO A 27 -3.946 35.222 50.333 1.00 95.20 O
ANISOU 4 O PRO A 27 11752 12383 12036 -290 521 -223 O
ATOM 5 CB PRO A 27 -5.939 35.830 52.267 1.00 97.08 C
ANISOU 5 CB PRO A 27 11970 12634 12281 -327 598 -289 C
ATOM 6 CG PRO A 27 -6.423 37.145 52.786 1.00 95.85 C
ANISOU 6 CG PRO A 27 11802 12469 12145 -331 629 -332 C
ATOM 7 CD PRO A 27 -5.288 38.100 52.551 1.00 95.32 C
ANISOU 7 CD PRO A 27 11748 12396 12074 -324 613 -332 C
ATOM 8 N CYS A 28 -2.644 34.321 51.942 1.00 97.30 N
ANISOU 8 N CYS A 28 12054 12691 12221 -335 521 -206 N
ATOM 9 CA CYS A 28 -1.690 33.701 51.020 1.00 97.46 C
ANISOU 9 CA CYS A 28 12084 12708 12239 -319 483 -169 C
ATOM 10 C CYS A 28 -1.982 32.234 50.704 1.00 96.97 C
ANISOU 10 C CYS A 28 12021 12652 12172 -318 468 -140 C
ATOM 11 O CYS A 28 -2.342 31.456 51.591 1.00 99.05 O
ANISOU 11 O CYS A 28 12289 12934 12411 -342 481 -138 O
ATOM 12 CB CYS A 28 -0.262 33.828 51.566 1.00102.92 C
ANISOU 12 CB CYS A 28 12800 13412 12891 -335 469 -158 C
ATOM 13 SG CYS A 28 0.449 35.490 51.480 1.00109.77 S
ANISOU 13 SG CYS A 28 13670 14267 13769 -326 471 -181 S
ATOM 14 N ILE A 29 -1.801 31.874 49.432 1.00 94.82 N
ANISOU 14 N ILE A 29 11742 12363 11922 -291 441 -118 N
ATOM 15 CA ILE A 29 -1.888 30.489 48.943 1.00 89.99 C
ANISOU 15 CA ILE A 29 11129 11754 11307 -287 421 -87 C
ATOM 16 C ILE A 29 -0.814 29.602 49.590 1.00 90.41 C
ANISOU 16 C ILE A 29 11204 11828 11318 -308 406 -62 C
ATOM 17 O ILE A 29 0.314 30.040 49.819 1.00 95.50 O
ANISOU 17 O ILE A 29 11864 12477 11943 -314 396 -59 O
ATOM 18 CB ILE A 29 -1.782 30.445 47.397 1.00 86.28 C
ANISOU 18 CB ILE A 29 10650 11261 10870 -254 395 -71 C
ATOM 19 CG1 ILE A 29 -2.961 31.200 46.766 1.00 86.18 C
ANISOU 19 CG1 ILE A 29 10616 11227 10901 -234 408 -93 C
ATOM 20 CG2 ILE A 29 -1.717 29.010 46.881 1.00 81.70 C
ANISOU 20 CG2 ILE A 29 10072 10685 10285 -250 373 -39 C
ATOM 21 CD1 ILE A 29 -2.694 31.743 45.377 1.00 87.74 C
ANISOU 21 CD1 ILE A 29 10807 11400 11129 -205 385 -85 C
ATOM 22 N GLU A 30 -1.173 28.356 49.880 1.00 88.97 N
ANISOU 22 N GLU A 30 11022 11658 11123 -319 403 -45 N
ATOM 23 CA GLU A 30 -0.297 27.449 50.609 1.00 87.48 C
ANISOU 23 CA GLU A 30 10852 11489 10895 -342 390 -21 C
ATOM 24 C GLU A 30 0.054 26.223 49.763 1.00 86.75 C
ANISOU 24 C GLU A 30 10759 11392 10809 -329 360 12 C
ATOM 25 O GLU A 30 -0.709 25.257 49.716 1.00 84.24 O
ANISOU 25 O GLU A 30 10432 11077 10496 -331 361 22 O
ATOM 26 CB GLU A 30 -0.993 27.036 51.905 1.00 85.42 C
ANISOU 26 CB GLU A 30 10595 11250 10610 -374 415 -31 C
ATOM 27 CG GLU A 30 -0.125 26.309 52.913 1.00 84.84 C
ANISOU 27 CG GLU A 30 10544 11199 10492 -405 405 -12 C
ATOM 28 CD GLU A 30 -0.843 26.122 54.234 1.00 84.05 C
ANISOU 28 CD GLU A 30 10449 11120 10366 -438 433 -26 C
ATOM 29 OE1 GLU A 30 -1.158 27.137 54.892 1.00 82.11 O
ANISOU 29 OE1 GLU A 30 10204 10878 10114 -450 461 -58 O
ATOM 30 OE2 GLU A 30 -1.105 24.962 54.610 1.00 82.97 O
ANISOU 30 OE2 GLU A 30 10314 10995 10213 -454 429 -7 O
ATOM 31 N VAL A 31 1.206 26.263 49.094 1.00 86.35 N
ANISOU 31 N VAL A 31 10715 11333 10757 -316 334 29 N
ATOM 32 CA VAL A 31 1.595 25.168 48.192 1.00 85.34 C
ANISOU 32 CA VAL A 31 10586 11199 10639 -302 306 59 C
ATOM 33 C VAL A 31 2.167 23.985 48.982 1.00 88.17 C
ANISOU 33 C VAL A 31 10957 11576 10967 -326 293 84 C
ATOM 34 O VAL A 31 1.833 22.831 48.704 1.00 91.39 O
ANISOU 34 O VAL A 31 11359 11984 11379 -324 282 103 O
ATOM 35 CB VAL A 31 2.516 25.622 47.017 1.00 80.77 C
ANISOU 35 CB VAL A 31 10008 10602 10077 -277 284 68 C
ATOM 36 CG1 VAL A 31 2.588 27.141 46.925 1.00 78.13 C
ANISOU 36 CG1 VAL A 31 9673 10259 9753 -269 297 42 C
ATOM 37 CG2 VAL A 31 3.915 25.030 47.121 1.00 78.68 C
ANISOU 37 CG2 VAL A 31 9758 10344 9792 -285 259 93 C
ATOM 38 N VAL A 32 3.025 24.277 49.959 1.00 87.12 N
ANISOU 38 N VAL A 32 10841 11457 10803 -349 293 84 N
ATOM 39 CA VAL A 32 3.462 23.284 50.939 1.00 89.93 C
ANISOU 39 CA VAL A 32 11209 11831 11127 -378 284 105 C
ATOM 40 C VAL A 32 3.332 23.905 52.331 1.00 96.52 C
ANISOU 40 C VAL A 32 12057 12685 11931 -409 307 86 C
ATOM 41 O VAL A 32 4.144 24.759 52.702 1.00100.19 O
ANISOU 41 O VAL A 32 12532 13152 12381 -416 307 77 O
ATOM 42 CB VAL A 32 4.917 22.801 50.714 1.00 88.43 C
ANISOU 42 CB VAL A 32 11031 11640 10929 -377 252 133 C
ATOM 43 CG1 VAL A 32 5.294 21.746 51.748 1.00 86.86 C
ANISOU 43 CG1 VAL A 32 10843 11459 10699 -408 240 155 C
ATOM 44 CG2 VAL A 32 5.111 22.249 49.308 1.00 87.07 C
ANISOU 44 CG2 VAL A 32 10846 11449 10786 -347 231 149 C
ATOM 45 N PRO A 33 2.292 23.500 53.094 1.00100.81 N
ANISOU 45 N PRO A 33 12598 13242 12464 -428 328 77 N
ATOM 46 CA PRO A 33 2.103 23.890 54.495 1.00 97.96 C
ANISOU 46 CA PRO A 33 12250 12901 12069 -462 352 60 C
ATOM 47 C PRO A 33 3.407 23.892 55.300 1.00 96.72 C
ANISOU 47 C PRO A 33 12115 12757 11877 -487 335 75 C
ATOM 48 O PRO A 33 4.182 22.932 55.225 1.00 97.06 O
ANISOU 48 O PRO A 33 12164 12801 11910 -491 306 107 O
ATOM 49 CB PRO A 33 1.157 22.809 55.025 1.00 97.10 C
ANISOU 49 CB PRO A 33 12136 12804 11950 -480 361 69 C
ATOM 50 CG PRO A 33 0.393 22.335 53.827 1.00 98.70 C
ANISOU 50 CG PRO A 33 12318 12990 12193 -449 357 74 C
ATOM 51 CD PRO A 33 1.117 22.769 52.579 1.00100.15 C
ANISOU 51 CD PRO A 33 12496 13152 12402 -416 335 80 C
ATOM 52 N ASN A 34 3.640 24.977 56.042 1.00 93.83 N
ANISOU 52 N ASN A 34 11760 12398 11492 -502 352 51 N
ATOM 53 CA ASN A 34 4.840 25.155 56.881 1.00 95.98 C
ANISOU 53 CA ASN A 34 12054 12683 11730 -527 338 61 C
ATOM 54 C ASN A 34 6.181 25.337 56.130 1.00 95.30 C
ANISOU 54 C ASN A 34 11971 12582 11654 -508 306 79 C
ATOM 55 O ASN A 34 7.217 25.563 56.765 1.00 93.89 O
ANISOU 55 O ASN A 34 11809 12412 11451 -526 293 86 O
ATOM 56 CB ASN A 34 4.961 24.031 57.939 1.00 95.13 C
ANISOU 56 CB ASN A 34 11962 12597 11586 -563 329 84 C
ATOM 57 CG ASN A 34 4.023 24.220 59.129 1.00 95.56 C
ANISOU 57 CG ASN A 34 12023 12670 11612 -596 363 61 C
ATOM 58 OD1 ASN A 34 3.641 25.340 59.470 1.00 94.45 O
ANISOU 58 OD1 ASN A 34 11882 12531 11470 -599 391 27 O
ATOM 59 ND2 ASN A 34 3.664 23.115 59.780 1.00 95.02 N
ANISOU 59 ND2 ASN A 34 11960 12617 11523 -621 361 79 N
ATOM 60 N ILE A 35 6.167 25.256 54.797 1.00 89.72 N
ANISOU 60 N ILE A 35 11248 11855 10984 -472 294 85 N
ATOM 61 CA ILE A 35 7.415 25.277 54.018 1.00 86.21 C
ANISOU 61 CA ILE A 35 10805 11397 10551 -454 264 104 C
ATOM 62 C ILE A 35 7.414 26.258 52.831 1.00 83.96 C
ANISOU 62 C ILE A 35 10508 11091 10301 -419 267 88 C
ATOM 63 O ILE A 35 8.333 27.074 52.701 1.00 85.80 O
ANISOU 63 O ILE A 35 10748 11318 10534 -414 260 84 O
ATOM 64 CB ILE A 35 7.854 23.847 53.596 1.00 88.31 C
ANISOU 64 CB ILE A 35 11069 11661 10822 -450 235 141 C
ATOM 65 CG1 ILE A 35 8.400 23.082 54.810 1.00 89.03 C
ANISOU 65 CG1 ILE A 35 11177 11772 10878 -487 222 161 C
ATOM 66 CG2 ILE A 35 8.916 23.890 52.501 1.00 86.38 C
ANISOU 66 CG2 ILE A 35 10820 11398 10600 -425 209 156 C
ATOM 67 CD1 ILE A 35 8.302 21.575 54.704 1.00 88.99 C
ANISOU 67 CD1 ILE A 35 11167 11768 10874 -491 202 192 C
ATOM 68 N THR A 36 6.400 26.180 51.970 1.00 77.47 N
ANISOU 68 N THR A 36 9668 10257 9508 -396 277 80 N
ATOM 69 CA THR A 36 6.324 27.062 50.800 1.00 70.26 C
ANISOU 69 CA THR A 36 8744 9323 8629 -364 279 67 C
ATOM 70 C THR A 36 4.994 27.808 50.750 1.00 69.08 C
ANISOU 70 C THR A 36 8581 9169 8497 -356 308 36 C
ATOM 71 O THR A 36 3.921 27.198 50.776 1.00 70.01 O
ANISOU 71 O THR A 36 8689 9289 8622 -357 320 35 O
ATOM 72 CB THR A 36 6.559 26.302 49.467 1.00 68.03 C
ANISOU 72 CB THR A 36 8451 9024 8372 -337 255 90 C
ATOM 73 OG1 THR A 36 7.644 25.379 49.611 1.00 66.80 O
ANISOU 73 OG1 THR A 36 8304 8873 8200 -346 229 119 O
ATOM 74 CG2 THR A 36 6.882 27.273 48.328 1.00 64.01 C
ANISOU 74 CG2 THR A 36 7935 8495 7889 -308 250 81 C
ATOM 75 N TYR A 37 5.080 29.133 50.682 1.00 70.34 N
ANISOU 75 N TYR A 37 8740 9320 8665 -349 320 12 N
ATOM 76 CA TYR A 37 3.897 29.990 50.599 1.00 73.75 C
ANISOU 76 CA TYR A 37 9158 9744 9119 -340 348 -18 C
ATOM 77 C TYR A 37 3.993 30.925 49.401 1.00 71.30 C
ANISOU 77 C TYR A 37 8837 9410 8842 -309 342 -26 C
ATOM 78 O TYR A 37 5.063 31.441 49.093 1.00 73.90 O
ANISOU 78 O TYR A 37 9174 9733 9169 -303 327 -20 O
ATOM 79 CB TYR A 37 3.693 30.773 51.907 1.00 75.64 C
ANISOU 79 CB TYR A 37 9405 9998 9335 -367 375 -46 C
ATOM 80 CG TYR A 37 3.297 29.886 53.065 1.00 76.72 C
ANISOU 80 CG TYR A 37 9550 10157 9440 -399 386 -41 C
ATOM 81 CD1 TYR A 37 4.247 29.112 53.732 1.00 77.56 C
ANISOU 81 CD1 TYR A 37 9676 10280 9512 -421 368 -16 C
ATOM 82 CD2 TYR A 37 1.969 29.801 53.480 1.00 79.33 C
ANISOU 82 CD2 TYR A 37 9871 10493 9777 -406 415 -61 C
ATOM 83 CE1 TYR A 37 3.888 28.281 54.780 1.00 81.44 C
ANISOU 83 CE1 TYR A 37 10176 10793 9974 -452 376 -10 C
ATOM 84 CE2 TYR A 37 1.599 28.974 54.532 1.00 81.20 C
ANISOU 84 CE2 TYR A 37 10116 10752 9985 -437 425 -56 C
ATOM 85 CZ TYR A 37 2.565 28.218 55.177 1.00 82.56 C
ANISOU 85 CZ TYR A 37 10307 10940 10120 -460 406 -30 C
ATOM 86 OH TYR A 37 2.217 27.394 56.219 1.00 86.14 O
ANISOU 86 OH TYR A 37 10771 11415 10543 -491 414 -23 O
ATOM 87 N GLN A 38 2.869 31.132 48.728 1.00 70.66 N
ANISOU 87 N GLN A 38 8738 9315 8794 -291 353 -39 N
ATOM 88 CA GLN A 38 2.838 31.920 47.511 1.00 76.16 C
ANISOU 88 CA GLN A 38 9423 9987 9524 -262 344 -44 C
ATOM 89 C GLN A 38 1.916 33.121 47.699 1.00 78.59 C
ANISOU 89 C GLN A 38 9719 10286 9855 -258 370 -78 C
ATOM 90 O GLN A 38 0.700 32.967 47.838 1.00 78.91 O
ANISOU 90 O GLN A 38 9746 10326 9911 -258 389 -92 O
ATOM 91 CB GLN A 38 2.375 31.042 46.344 1.00 80.61 C
ANISOU 91 CB GLN A 38 9976 10540 10112 -240 328 -24 C
ATOM 92 CG GLN A 38 3.281 31.080 45.120 1.00 84.43 C
ANISOU 92 CG GLN A 38 10462 11008 10607 -219 301 -5 C
ATOM 93 CD GLN A 38 2.829 32.080 44.072 1.00 87.23 C
ANISOU 93 CD GLN A 38 10805 11340 10998 -194 301 -18 C
ATOM 94 OE1 GLN A 38 2.583 33.249 44.371 1.00 84.35 O
ANISOU 94 OE1 GLN A 38 10436 10969 10642 -194 316 -42 O
ATOM 95 NE2 GLN A 38 2.726 31.623 42.827 1.00 87.98 N
ANISOU 95 NE2 GLN A 38 10894 11420 11112 -174 282 -1 N
ATOM 96 N CYS A 39 2.504 34.316 47.708 1.00 80.34 N
ANISOU 96 N CYS A 39 9944 10500 10079 -255 372 -93 N
ATOM 97 CA CYS A 39 1.762 35.548 47.983 1.00 80.60 C
ANISOU 97 CA CYS A 39 9966 10524 10133 -253 397 -127 C
ATOM 98 C CYS A 39 1.748 36.518 46.802 1.00 77.25 C
ANISOU 98 C CYS A 39 9530 10073 9746 -225 387 -132 C
ATOM 99 O CYS A 39 1.563 37.720 46.984 1.00 79.28 O
ANISOU 99 O CYS A 39 9782 10321 10019 -223 401 -158 O
ATOM 100 CB CYS A 39 2.331 36.236 49.224 1.00 84.87 C
ANISOU 100 CB CYS A 39 10521 11080 10645 -278 413 -146 C
ATOM 101 SG CYS A 39 2.313 35.198 50.702 1.00104.11 S
ANISOU 101 SG CYS A 39 12973 13549 13035 -315 426 -142 S
ATOM 102 N MET A 40 1.934 35.987 45.596 1.00 74.93 N
ANISOU 102 N MET A 40 9234 9768 9467 -205 362 -108 N
ATOM 103 CA MET A 40 1.926 36.791 44.371 1.00 74.53 C
ANISOU 103 CA MET A 40 9174 9693 9451 -179 349 -108 C
ATOM 104 C MET A 40 0.600 37.521 44.190 1.00 74.96 C
ANISOU 104 C MET A 40 9207 9729 9543 -169 366 -133 C
ATOM 105 O MET A 40 -0.451 37.006 44.567 1.00 81.90 O
ANISOU 105 O MET A 40 10075 10613 10429 -175 382 -141 O
ATOM 106 CB MET A 40 2.193 35.902 43.153 1.00 71.51 C
ANISOU 106 CB MET A 40 8793 9302 9075 -162 321 -78 C
ATOM 107 CG MET A 40 2.688 36.642 41.923 1.00 73.17 C
ANISOU 107 CG MET A 40 9001 9491 9306 -140 302 -71 C
ATOM 108 SD MET A 40 2.661 35.677 40.397 1.00 76.69 S
ANISOU 108 SD MET A 40 9446 9926 9767 -120 275 -41 S
ATOM 109 CE MET A 40 3.773 34.322 40.764 1.00 73.96 C
ANISOU 109 CE MET A 40 9117 9601 9382 -133 262 -14 C
ATOM 110 N ASP A 41 0.665 38.726 43.630 1.00 76.48 N
ANISOU 110 N ASP A 41 9394 9903 9762 -155 363 -146 N
ATOM 111 CA ASP A 41 -0.517 39.495 43.218 1.00 77.15 C
ANISOU 111 CA ASP A 41 9455 9965 9890 -141 373 -166 C
ATOM 112 C ASP A 41 -1.691 39.478 44.211 1.00 78.83 C
ANISOU 112 C ASP A 41 9656 10185 10111 -155 405 -193 C
ATOM 113 O ASP A 41 -2.850 39.305 43.829 1.00 80.21 O
ANISOU 113 O ASP A 41 9812 10347 10317 -145 410 -199 O
ATOM 114 CB ASP A 41 -0.967 39.069 41.810 1.00 77.41 C
ANISOU 114 CB ASP A 41 9480 9980 9952 -118 350 -146 C
ATOM 115 CG ASP A 41 -2.001 40.015 41.200 1.00 78.56 C
ANISOU 115 CG ASP A 41 9603 10098 10146 -102 353 -163 C
ATOM 116 OD1 ASP A 41 -2.167 41.158 41.686 1.00 76.95 O
ANISOU 116 OD1 ASP A 41 9392 9886 9957 -105 369 -190 O
ATOM 117 OD2 ASP A 41 -2.654 39.604 40.219 1.00 80.49 O
ANISOU 117 OD2 ASP A 41 9837 10328 10415 -87 338 -150 O
ATOM 118 N GLN A 42 -1.373 39.630 45.492 1.00 81.09 N
ANISOU 118 N GLN A 42 9952 10491 10367 -178 426 -209 N
ATOM 119 CA GLN A 42 -2.337 40.132 46.466 1.00 82.14 C
ANISOU 119 CA GLN A 42 10072 10626 10511 -191 460 -244 C
ATOM 120 C GLN A 42 -2.167 41.652 46.407 1.00 83.90 C
ANISOU 120 C GLN A 42 10289 10831 10758 -184 466 -268 C
ATOM 121 O GLN A 42 -1.361 42.154 45.609 1.00 90.46 O
ANISOU 121 O GLN A 42 11125 11649 11594 -170 443 -255 O
ATOM 122 CB GLN A 42 -2.039 39.598 47.870 1.00 81.15 C
ANISOU 122 CB GLN A 42 9962 10530 10339 -222 480 -250 C
ATOM 123 CG GLN A 42 -1.932 38.077 47.970 1.00 81.67 C
ANISOU 123 CG GLN A 42 10038 10614 10376 -231 469 -222 C
ATOM 124 CD GLN A 42 -3.279 37.371 47.968 1.00 81.08 C
ANISOU 124 CD GLN A 42 9946 10539 10321 -231 483 -226 C
ATOM 125 OE1 GLN A 42 -3.609 36.644 47.030 1.00 72.43 O
ANISOU 125 OE1 GLN A 42 8843 9433 9241 -214 464 -204 O
ATOM 126 NE2 GLN A 42 -4.065 37.583 49.024 1.00 82.98 N
ANISOU 126 NE2 GLN A 42 10180 10789 10559 -250 517 -255 N
ATOM 127 N LYS A 43 -2.904 42.402 47.214 1.00 77.67 N
ANISOU 127 N LYS A 43 9487 10040 9983 -194 497 -304 N
ATOM 128 CA LYS A 43 -2.684 43.845 47.211 1.00 79.41 C
ANISOU 128 CA LYS A 43 9702 10243 10226 -188 503 -328 C
ATOM 129 C LYS A 43 -1.886 44.278 48.439 1.00 80.57 C
ANISOU 129 C LYS A 43 9867 10410 10334 -213 520 -345 C
ATOM 130 O LYS A 43 -2.160 45.314 49.049 1.00 87.17 O
ANISOU 130 O LYS A 43 10695 11240 11184 -220 543 -379 O
ATOM 131 CB LYS A 43 -3.995 44.615 47.033 1.00 77.52 C
ANISOU 131 CB LYS A 43 9433 9980 10040 -177 521 -357 C
ATOM 132 CG LYS A 43 -4.649 44.363 45.683 1.00 76.58 C
ANISOU 132 CG LYS A 43 9297 9836 9961 -151 498 -338 C
ATOM 133 CD LYS A 43 -5.433 45.569 45.197 1.00 78.89 C
ANISOU 133 CD LYS A 43 9564 10097 10312 -134 502 -361 C
ATOM 134 CE LYS A 43 -5.989 45.324 43.803 1.00 79.68 C
ANISOU 134 CE LYS A 43 9651 10174 10450 -110 474 -339 C
ATOM 135 NZ LYS A 43 -6.698 46.521 43.274 1.00 79.34 N
ANISOU 135 NZ LYS A 43 9582 10097 10465 -93 473 -358 N
ATOM 136 N LEU A 44 -0.872 43.476 48.763 1.00 79.58 N
ANISOU 136 N LEU A 44 9766 10308 10163 -226 507 -321 N
ATOM 137 CA LEU A 44 -0.080 43.626 49.984 1.00 81.08 C
ANISOU 137 CA LEU A 44 9976 10520 10308 -253 520 -331 C
ATOM 138 C LEU A 44 0.796 44.878 50.040 1.00 83.53 C
ANISOU 138 C LEU A 44 10294 10823 10621 -252 516 -344 C
ATOM 139 O LEU A 44 1.294 45.351 49.013 1.00 80.61 O
ANISOU 139 O LEU A 44 9921 10434 10272 -230 492 -330 O
ATOM 140 CB LEU A 44 0.789 42.384 50.209 1.00 79.68 C
ANISOU 140 CB LEU A 44 9821 10366 10084 -267 502 -298 C
ATOM 141 CG LEU A 44 0.107 41.053 50.535 1.00 78.75 C
ANISOU 141 CG LEU A 44 9704 10266 9952 -278 508 -286 C
ATOM 142 CD1 LEU A 44 1.162 39.988 50.787 1.00 78.21 C
ANISOU 142 CD1 LEU A 44 9658 10218 9838 -291 488 -253 C
ATOM 143 CD2 LEU A 44 -0.824 41.168 51.733 1.00 81.85 C
ANISOU 143 CD2 LEU A 44 10091 10671 10338 -301 547 -319 C
ATOM 144 N SER A 45 0.973 45.393 51.259 1.00 87.79 N
ANISOU 144 N SER A 45 10842 11375 11136 -276 540 -371 N
ATOM 145 CA SER A 45 1.795 46.579 51.535 1.00 84.70 C
ANISOU 145 CA SER A 45 10459 10980 10743 -279 540 -387 C
ATOM 146 C SER A 45 3.100 46.209 52.239 1.00 84.20 C
ANISOU 146 C SER A 45 10424 10940 10627 -300 529 -371 C
ATOM 147 O SER A 45 4.100 46.916 52.109 1.00 84.16 O
ANISOU 147 O SER A 45 10428 10929 10617 -297 515 -368 O
ATOM 148 CB SER A 45 1.018 47.583 52.387 1.00 81.83 C
ANISOU 148 CB SER A 45 10082 10611 10396 -291 577 -433 C
ATOM 149 OG SER A 45 -0.263 47.832 51.837 1.00 85.02 O
ANISOU 149 OG SER A 45 10459 10993 10850 -273 589 -449 O
ATOM 150 N LYS A 46 3.071 45.112 52.994 1.00 82.58 N
ANISOU 150 N LYS A 46 10232 10759 10383 -323 535 -360 N
ATOM 151 CA LYS A 46 4.261 44.548 53.629 1.00 86.28 C
ANISOU 151 CA LYS A 46 10728 11252 10803 -344 520 -339 C
ATOM 152 C LYS A 46 4.106 43.043 53.773 1.00 85.09 C
ANISOU 152 C LYS A 46 10584 11119 10627 -354 513 -312 C
ATOM 153 O LYS A 46 3.072 42.477 53.410 1.00 82.29 O
ANISOU 153 O LYS A 46 10214 10760 10292 -345 520 -311 O
ATOM 154 CB LYS A 46 4.510 45.180 55.003 1.00 96.75 C
ANISOU 154 CB LYS A 46 12068 12593 12098 -375 544 -368 C
ATOM 155 CG LYS A 46 5.447 46.379 54.982 1.00104.66 C
ANISOU 155 CG LYS A 46 13076 13585 13104 -371 536 -379 C
ATOM 156 CD LYS A 46 5.220 47.275 56.191 1.00106.71 C
ANISOU 156 CD LYS A 46 13340 13852 13350 -396 568 -420 C
ATOM 157 CE LYS A 46 5.697 48.695 55.924 1.00107.50 C
ANISOU 157 CE LYS A 46 13436 13933 13475 -384 567 -439 C
ATOM 158 NZ LYS A 46 5.059 49.682 56.842 1.00107.82 N
ANISOU 158 NZ LYS A 46 13471 13973 13522 -400 603 -486 N
ATOM 159 N VAL A 47 5.144 42.402 54.299 1.00 85.55 N
ANISOU 159 N VAL A 47 10665 11196 10642 -373 496 -289 N
ATOM 160 CA VAL A 47 5.102 40.982 54.612 1.00 92.34 C
ANISOU 160 CA VAL A 47 11534 12076 11474 -388 489 -263 C
ATOM 161 C VAL A 47 4.129 40.752 55.770 1.00105.32 C
ANISOU 161 C VAL A 47 13178 13737 13099 -415 523 -288 C
ATOM 162 O VAL A 47 4.319 41.320 56.852 1.00110.05 O
ANISOU 162 O VAL A 47 13791 14349 13674 -441 541 -311 O
ATOM 163 CB VAL A 47 6.485 40.460 55.036 1.00 87.21 C
ANISOU 163 CB VAL A 47 10909 11442 10784 -405 464 -236 C
ATOM 164 CG1 VAL A 47 6.551 38.950 54.874 1.00 87.96 C
ANISOU 164 CG1 VAL A 47 11009 11548 10864 -408 445 -201 C
ATOM 165 CG2 VAL A 47 7.586 41.143 54.241 1.00 83.79 C
ANISOU 165 CG2 VAL A 47 10478 10993 10365 -385 439 -225 C
ATOM 166 N PRO A 48 3.076 39.937 55.547 1.00113.85 N
ANISOU 166 N PRO A 48 14246 14818 14193 -411 532 -284 N
ATOM 167 CA PRO A 48 2.136 39.610 56.625 1.00117.59 C
ANISOU 167 CA PRO A 48 14720 15309 14648 -438 564 -304 C
ATOM 168 C PRO A 48 2.773 38.712 57.686 1.00118.86 C
ANISOU 168 C PRO A 48 14907 15499 14754 -473 559 -286 C
ATOM 169 O PRO A 48 3.416 37.712 57.353 1.00115.12 O
ANISOU 169 O PRO A 48 14442 15031 14266 -471 529 -249 O
ATOM 170 CB PRO A 48 1.000 38.874 55.898 1.00117.08 C
ANISOU 170 CB PRO A 48 14634 15235 14614 -420 567 -297 C
ATOM 171 CG PRO A 48 1.142 39.258 54.463 1.00114.26 C
ANISOU 171 CG PRO A 48 14262 14851 14300 -382 544 -285 C
ATOM 172 CD PRO A 48 2.619 39.402 54.253 1.00114.18 C
ANISOU 172 CD PRO A 48 14270 14842 14270 -380 515 -263 C
ATOM 173 N ASP A 49 2.594 39.088 58.951 1.00123.27 N
ANISOU 173 N ASP A 49 15478 16076 15284 -506 587 -313 N
ATOM 174 CA ASP A 49 3.203 38.388 60.090 1.00125.02 C
ANISOU 174 CA ASP A 49 15726 16325 15450 -544 583 -299 C
ATOM 175 C ASP A 49 2.548 37.036 60.386 1.00119.56 C
ANISOU 175 C ASP A 49 15036 15650 14742 -559 586 -281 C
ATOM 176 O ASP A 49 3.145 36.175 61.044 1.00112.55 O
ANISOU 176 O ASP A 49 14169 14782 13813 -585 571 -256 O
ATOM 177 CB ASP A 49 3.175 39.278 61.341 1.00129.50 C
ANISOU 177 CB ASP A 49 16306 16905 15990 -576 613 -336 C
ATOM 178 CG ASP A 49 1.775 39.788 61.671 1.00133.78 C
ANISOU 178 CG ASP A 49 16831 17445 16554 -579 658 -378 C
ATOM 179 OD1 ASP A 49 1.091 40.309 60.761 1.00135.09 O
ANISOU 179 OD1 ASP A 49 16970 17586 16770 -547 664 -392 O
ATOM 180 OD2 ASP A 49 1.364 39.676 62.846 1.00134.11 O
ANISOU 180 OD2 ASP A 49 16884 17507 16562 -615 686 -398 O
ATOM 181 N ASP A 50 1.323 36.861 59.894 1.00114.37 N
ANISOU 181 N ASP A 50 14354 14981 14118 -542 603 -292 N
ATOM 182 CA ASP A 50 0.574 35.614 60.066 1.00108.52 C
ANISOU 182 CA ASP A 50 13610 14252 13368 -553 608 -276 C
ATOM 183 C ASP A 50 1.056 34.491 59.137 1.00101.77 C
ANISOU 183 C ASP A 50 12754 13392 12520 -533 569 -231 C
ATOM 184 O ASP A 50 0.389 33.466 58.989 1.00100.28 O
ANISOU 184 O ASP A 50 12558 13207 12334 -533 568 -216 O
ATOM 185 CB ASP A 50 -0.946 35.852 59.934 1.00109.44 C
ANISOU 185 CB ASP A 50 13701 14359 13520 -544 643 -306 C
ATOM 186 CG ASP A 50 -1.314 36.771 58.769 1.00108.65 C
ANISOU 186 CG ASP A 50 13576 14228 13476 -504 642 -321 C
ATOM 187 OD1 ASP A 50 -0.743 37.882 58.658 1.00106.23 O
ANISOU 187 OD1 ASP A 50 13271 13911 13178 -496 640 -337 O
ATOM 188 OD2 ASP A 50 -2.202 36.387 57.977 1.00104.95 O
ANISOU 188 OD2 ASP A 50 13086 13746 13044 -482 642 -317 O
ATOM 189 N ILE A 51 2.215 34.696 58.515 1.00 99.79 N
ANISOU 189 N ILE A 51 12510 13132 12272 -517 536 -210 N
ATOM 190 CA ILE A 51 2.896 33.641 57.768 1.00 99.63 C
ANISOU 190 CA ILE A 51 12493 13109 12252 -503 499 -168 C
ATOM 191 C ILE A 51 3.832 32.911 58.732 1.00 98.36 C
ANISOU 191 C ILE A 51 12358 12971 12042 -536 482 -144 C
ATOM 192 O ILE A 51 4.741 33.524 59.297 1.00 97.02 O
ANISOU 192 O ILE A 51 12206 12808 11849 -551 477 -149 O
ATOM 193 CB ILE A 51 3.689 34.185 56.549 1.00 98.05 C
ANISOU 193 CB ILE A 51 12286 12886 12082 -468 472 -157 C
ATOM 194 CG1 ILE A 51 2.748 34.884 55.556 1.00 96.99 C
ANISOU 194 CG1 ILE A 51 12126 12728 11997 -436 485 -177 C
ATOM 195 CG2 ILE A 51 4.458 33.061 55.857 1.00 90.39 C
ANISOU 195 CG2 ILE A 51 11319 11914 11109 -457 435 -114 C
ATOM 196 CD1 ILE A 51 3.442 35.819 54.587 1.00 95.22 C
ANISOU 196 CD1 ILE A 51 11897 12482 11800 -408 468 -178 C
ATOM 197 N PRO A 52 3.598 31.601 58.936 1.00 99.62 N
ANISOU 197 N PRO A 52 12521 13143 12186 -549 473 -119 N
ATOM 198 CA PRO A 52 4.422 30.770 59.809 1.00100.37 C
ANISOU 198 CA PRO A 52 12640 13259 12237 -581 454 -92 C
ATOM 199 C PRO A 52 5.915 31.101 59.754 1.00 97.26 C
ANISOU 199 C PRO A 52 12260 12862 11830 -581 424 -76 C
ATOM 200 O PRO A 52 6.520 31.077 58.683 1.00 97.38 O
ANISOU 200 O PRO A 52 12268 12860 11872 -551 399 -58 O
ATOM 201 CB PRO A 52 4.160 29.362 59.272 1.00100.49 C
ANISOU 201 CB PRO A 52 12646 13273 12261 -572 435 -59 C
ATOM 202 CG PRO A 52 2.738 29.419 58.813 1.00102.24 C
ANISOU 202 CG PRO A 52 12846 13486 12514 -555 461 -80 C
ATOM 203 CD PRO A 52 2.455 30.841 58.392 1.00 99.40 C
ANISOU 203 CD PRO A 52 12474 13110 12183 -535 481 -115 C
ATOM 204 N SER A 53 6.487 31.427 60.910 1.00 98.38 N
ANISOU 204 N SER A 53 12424 13021 11932 -615 428 -82 N
ATOM 205 CA SER A 53 7.919 31.683 61.036 1.00 98.69 C
ANISOU 205 CA SER A 53 12480 13060 11956 -620 399 -65 C
ATOM 206 C SER A 53 8.683 30.361 60.978 1.00100.91 C
ANISOU 206 C SER A 53 12769 13346 12224 -627 362 -20 C
ATOM 207 O SER A 53 9.390 29.988 61.922 1.00102.59 O
ANISOU 207 O SER A 53 13003 13575 12399 -660 347 -5 O
ATOM 208 CB SER A 53 8.219 32.436 62.338 1.00 99.92 C
ANISOU 208 CB SER A 53 12658 13233 12072 -657 415 -87 C
ATOM 209 OG SER A 53 7.736 31.726 63.467 1.00 98.37 O
ANISOU 209 OG SER A 53 12476 13061 11838 -696 427 -85 O
ATOM 210 N SER A 54 8.525 29.663 59.854 1.00 98.33 N
ANISOU 210 N SER A 54 12425 13005 11930 -597 346 0 N
ATOM 211 CA SER A 54 9.066 28.318 59.664 1.00 94.72 C
ANISOU 211 CA SER A 54 11970 12549 11468 -599 313 40 C
ATOM 212 C SER A 54 9.327 28.009 58.190 1.00 92.36 C
ANISOU 212 C SER A 54 11653 12228 11211 -558 293 57 C
ATOM 213 O SER A 54 9.980 27.010 57.867 1.00 87.70 O
ANISOU 213 O SER A 54 11063 11634 10622 -555 262 90 O
ATOM 214 CB SER A 54 8.094 27.288 60.229 1.00 92.99 C
ANISOU 214 CB SER A 54 11752 12346 11234 -620 325 46 C
ATOM 215 OG SER A 54 6.811 27.467 59.659 1.00 94.47 O
ANISOU 215 OG SER A 54 11919 12525 11449 -599 352 25 O
ATOM 216 N THR A 55 8.818 28.875 57.312 1.00 90.84 N
ANISOU 216 N THR A 55 11444 12019 11051 -528 308 33 N
ATOM 217 CA THR A 55 8.879 28.679 55.857 1.00 88.13 C
ANISOU 217 CA THR A 55 11083 11653 10747 -489 293 45 C
ATOM 218 C THR A 55 10.306 28.753 55.279 1.00 88.68 C
ANISOU 218 C THR A 55 11157 11711 10824 -476 262 66 C
ATOM 219 O THR A 55 11.196 29.389 55.864 1.00 90.10 O
ANISOU 219 O THR A 55 11351 11896 10986 -491 256 63 O
ATOM 220 CB THR A 55 7.954 29.664 55.104 1.00 83.99 C
ANISOU 220 CB THR A 55 10541 11114 10256 -462 318 15 C
ATOM 221 OG1 THR A 55 8.636 30.901 54.885 1.00 84.17 O
ANISOU 221 OG1 THR A 55 10566 11126 10286 -452 317 0 O
ATOM 222 CG2 THR A 55 6.694 29.934 55.893 1.00 83.05 C
ANISOU 222 CG2 THR A 55 10419 11006 10128 -479 353 -13 C
ATOM 223 N LYS A 56 10.503 28.099 54.132 1.00 83.68 N
ANISOU 223 N LYS A 56 10511 11063 10217 -450 242 87 N
ATOM 224 CA LYS A 56 11.805 28.049 53.463 1.00 79.61 C
ANISOU 224 CA LYS A 56 9998 10536 9714 -436 213 107 C
ATOM 225 C LYS A 56 11.807 28.826 52.146 1.00 78.85 C
ANISOU 225 C LYS A 56 9888 10418 9652 -400 215 96 C
ATOM 226 O LYS A 56 12.858 29.278 51.680 1.00 76.83 O
ANISOU 226 O LYS A 56 9634 10151 9404 -390 200 102 O
ATOM 227 CB LYS A 56 12.246 26.599 53.222 1.00 79.57 C
ANISOU 227 CB LYS A 56 9991 10531 9710 -437 186 142 C
ATOM 228 CG LYS A 56 12.318 25.755 54.487 1.00 80.97 C
ANISOU 228 CG LYS A 56 10182 10728 9853 -474 180 158 C
ATOM 229 CD LYS A 56 13.610 24.958 54.573 1.00 77.72 C
ANISOU 229 CD LYS A 56 9778 10316 9437 -482 145 191 C
ATOM 230 CE LYS A 56 13.844 24.492 56.002 1.00 76.72 C
ANISOU 230 CE LYS A 56 9668 10209 9271 -523 138 203 C
ATOM 231 NZ LYS A 56 15.287 24.516 56.370 1.00 77.93 N
ANISOU 231 NZ LYS A 56 9833 10361 9414 -536 110 221 N
ATOM 232 N ASN A 57 10.626 28.972 51.550 1.00 75.06 N
ANISOU 232 N ASN A 57 9394 9930 9193 -383 233 80 N
ATOM 233 CA ASN A 57 10.474 29.686 50.289 1.00 69.80 C
ANISOU 233 CA ASN A 57 8715 9244 8562 -350 235 70 C
ATOM 234 C ASN A 57 9.201 30.506 50.335 1.00 67.41 C
ANISOU 234 C ASN A 57 8402 8938 8271 -345 264 39 C
ATOM 235 O ASN A 57 8.176 30.034 50.816 1.00 71.22 O
ANISOU 235 O ASN A 57 8880 9430 8747 -355 280 33 O
ATOM 236 CB ASN A 57 10.425 28.708 49.100 1.00 68.34 C
ANISOU 236 CB ASN A 57 8518 9046 8400 -327 217 93 C
ATOM 237 CG ASN A 57 11.419 27.559 49.233 1.00 67.48 C
ANISOU 237 CG ASN A 57 8416 8942 8279 -337 191 124 C
ATOM 238 OD1 ASN A 57 12.632 27.744 49.115 1.00 63.63 O
ANISOU 238 OD1 ASN A 57 7935 8450 7788 -337 173 135 O
ATOM 239 ND2 ASN A 57 10.901 26.359 49.483 1.00 67.63 N
ANISOU 239 ND2 ASN A 57 8433 8970 8292 -347 187 139 N
ATOM 240 N ILE A 58 9.272 31.739 49.850 1.00 66.78 N
ANISOU 240 N ILE A 58 8319 8846 8209 -329 272 20 N
ATOM 241 CA ILE A 58 8.090 32.591 49.734 1.00 66.16 C
ANISOU 241 CA ILE A 58 8228 8760 8150 -320 298 -9 C
ATOM 242 C ILE A 58 8.179 33.481 48.502 1.00 64.58 C
ANISOU 242 C ILE A 58 8018 8537 7983 -290 292 -15 C
ATOM 243 O ILE A 58 9.228 34.058 48.215 1.00 65.42 O
ANISOU 243 O ILE A 58 8130 8635 8088 -284 279 -11 O
ATOM 244 CB ILE A 58 7.818 33.422 51.021 1.00 70.84 C
ANISOU 244 CB ILE A 58 8828 9366 8722 -344 323 -37 C
ATOM 245 CG1 ILE A 58 6.873 34.596 50.734 1.00 75.50 C
ANISOU 245 CG1 ILE A 58 9403 9941 9339 -330 347 -70 C
ATOM 246 CG2 ILE A 58 9.107 33.934 51.641 1.00 69.83 C
ANISOU 246 CG2 ILE A 58 8718 9244 8570 -360 313 -34 C
ATOM 247 CD1 ILE A 58 6.033 35.018 51.923 1.00 81.19 C
ANISOU 247 CD1 ILE A 58 10125 10675 10045 -354 379 -99 C
ATOM 248 N ASP A 59 7.075 33.563 47.768 1.00 63.52 N
ANISOU 248 N ASP A 59 7867 8389 7877 -271 301 -25 N
ATOM 249 CA ASP A 59 6.978 34.460 46.629 1.00 63.38 C
ANISOU 249 CA ASP A 59 7838 8349 7892 -244 298 -33 C
ATOM 250 C ASP A 59 6.059 35.624 46.973 1.00 63.02 C
ANISOU 250 C ASP A 59 7784 8298 7863 -244 324 -66 C
ATOM 251 O ASP A 59 4.852 35.446 47.122 1.00 63.90 O
ANISOU 251 O ASP A 59 7883 8408 7986 -244 341 -79 O
ATOM 252 CB ASP A 59 6.485 33.717 45.377 1.00 61.67 C
ANISOU 252 CB ASP A 59 7610 8119 7700 -222 284 -16 C
ATOM 253 CG ASP A 59 6.235 34.653 44.197 1.00 63.54 C
ANISOU 253 CG ASP A 59 7837 8333 7971 -196 281 -24 C
ATOM 254 OD1 ASP A 59 7.047 35.577 43.966 1.00 63.56 O
ANISOU 254 OD1 ASP A 59 7845 8328 7976 -191 275 -28 O
ATOM 255 OD2 ASP A 59 5.219 34.468 43.496 1.00 65.02 O
ANISOU 255 OD2 ASP A 59 8010 8509 8183 -182 283 -26 O
ATOM 256 N LEU A 60 6.646 36.812 47.095 1.00 62.19 N
ANISOU 256 N LEU A 60 7683 8186 7759 -243 326 -81 N
ATOM 257 CA LEU A 60 5.902 38.033 47.397 1.00 59.96 C
ANISOU 257 CA LEU A 60 7390 7895 7494 -242 350 -115 C
ATOM 258 C LEU A 60 5.783 38.977 46.203 1.00 61.81 C
ANISOU 258 C LEU A 60 7613 8104 7767 -215 342 -120 C
ATOM 259 O LEU A 60 5.435 40.148 46.374 1.00 65.01 O
ANISOU 259 O LEU A 60 8011 8500 8189 -213 357 -146 O
ATOM 260 CB LEU A 60 6.547 38.772 48.575 1.00 58.37 C
ANISOU 260 CB LEU A 60 7203 7707 7267 -265 361 -132 C
ATOM 261 CG LEU A 60 6.182 38.311 49.987 1.00 58.03 C
ANISOU 261 CG LEU A 60 7168 7687 7192 -296 382 -143 C
ATOM 262 CD1 LEU A 60 7.263 38.694 50.990 1.00 56.50 C
ANISOU 262 CD1 LEU A 60 6994 7507 6964 -319 381 -146 C
ATOM 263 CD2 LEU A 60 4.832 38.880 50.396 1.00 57.66 C
ANISOU 263 CD2 LEU A 60 7107 7637 7164 -298 413 -176 C
ATOM 264 N SER A 61 6.059 38.472 45.000 1.00 62.66 N
ANISOU 264 N SER A 61 7719 8201 7887 -196 319 -96 N
ATOM 265 CA SER A 61 6.049 39.302 43.785 1.00 62.23 C
ANISOU 265 CA SER A 61 7655 8122 7866 -171 308 -96 C
ATOM 266 C SER A 61 4.714 40.011 43.528 1.00 61.96 C
ANISOU 266 C SER A 61 7602 8072 7868 -160 323 -119 C
ATOM 267 O SER A 61 3.694 39.655 44.114 1.00 61.46 O
ANISOU 267 O SER A 61 7530 8015 7807 -169 342 -132 O
ATOM 268 CB SER A 61 6.475 38.490 42.554 1.00 62.66 C
ANISOU 268 CB SER A 61 7712 8169 7925 -155 282 -66 C
ATOM 269 OG SER A 61 5.695 37.319 42.392 1.00 63.72 O
ANISOU 269 OG SER A 61 7840 8308 8061 -154 281 -55 O
ATOM 270 N PHE A 62 4.745 41.021 42.660 1.00 63.44 N
ANISOU 270 N PHE A 62 7783 8238 8084 -143 315 -124 N
ATOM 271 CA PHE A 62 3.550 41.789 42.243 1.00 65.03 C
ANISOU 271 CA PHE A 62 7963 8418 8325 -129 325 -144 C
ATOM 272 C PHE A 62 2.702 42.351 43.390 1.00 66.71 C
ANISOU 272 C PHE A 62 8167 8636 8544 -143 356 -178 C
ATOM 273 O PHE A 62 1.469 42.300 43.352 1.00 68.70 O
ANISOU 273 O PHE A 62 8401 8879 8821 -139 368 -191 O
ATOM 274 CB PHE A 62 2.692 40.990 41.247 1.00 61.13 C
ANISOU 274 CB PHE A 62 7458 7914 7852 -114 313 -128 C
ATOM 275 CG PHE A 62 3.345 40.793 39.909 1.00 59.05 C
ANISOU 275 CG PHE A 62 7201 7638 7594 -97 285 -102 C
ATOM 276 CD1 PHE A 62 4.217 39.728 39.693 1.00 57.79 C
ANISOU 276 CD1 PHE A 62 7056 7493 7407 -101 270 -76 C
ATOM 277 CD2 PHE A 62 3.095 41.676 38.864 1.00 56.83 C
ANISOU 277 CD2 PHE A 62 6911 7333 7347 -79 273 -103 C
ATOM 278 CE1 PHE A 62 4.822 39.549 38.459 1.00 55.80 C
ANISOU 278 CE1 PHE A 62 6809 7230 7160 -86 246 -53 C
ATOM 279 CE2 PHE A 62 3.699 41.500 37.629 1.00 56.33 C
ANISOU 279 CE2 PHE A 62 6856 7260 7287 -66 248 -79 C
ATOM 280 CZ PHE A 62 4.562 40.435 37.426 1.00 55.37 C
ANISOU 280 CZ PHE A 62 6748 7152 7136 -70 236 -55 C
ATOM 281 N ASN A 63 3.386 42.884 44.402 1.00 69.61 N
ANISOU 281 N ASN A 63 8545 9015 8887 -160 368 -192 N
ATOM 282 CA ASN A 63 2.759 43.573 45.533 1.00 69.29 C
ANISOU 282 CA ASN A 63 8498 8979 8848 -175 398 -227 C
ATOM 283 C ASN A 63 3.305 44.995 45.687 1.00 70.81 C
ANISOU 283 C ASN A 63 8692 9161 9052 -174 402 -247 C
ATOM 284 O ASN A 63 4.507 45.205 45.534 1.00 69.83 O
ANISOU 284 O ASN A 63 8582 9039 8909 -175 385 -233 O
ATOM 285 CB ASN A 63 3.005 42.792 46.824 1.00 65.17 C
ANISOU 285 CB ASN A 63 7991 8486 8283 -203 413 -228 C
ATOM 286 CG ASN A 63 2.232 41.494 46.875 1.00 63.16 C
ANISOU 286 CG ASN A 63 7732 8242 8022 -207 416 -216 C
ATOM 287 OD1 ASN A 63 1.033 41.469 46.614 1.00 63.48 O
ANISOU 287 OD1 ASN A 63 7754 8272 8092 -199 427 -227 O
ATOM 288 ND2 ASN A 63 2.911 40.411 47.223 1.00 58.73 N
ANISOU 288 ND2 ASN A 63 7187 7701 7424 -220 405 -192 N
ATOM 289 N PRO A 64 2.431 45.978 45.985 1.00 72.58 N
ANISOU 289 N PRO A 64 8899 9371 9306 -173 423 -279 N
ATOM 290 CA PRO A 64 2.943 47.321 46.280 1.00 72.31 C
ANISOU 290 CA PRO A 64 8866 9328 9280 -174 429 -300 C
ATOM 291 C PRO A 64 3.714 47.381 47.608 1.00 69.83 C
ANISOU 291 C PRO A 64 8570 9037 8922 -201 443 -312 C
ATOM 292 O PRO A 64 3.223 47.953 48.582 1.00 70.51 O
ANISOU 292 O PRO A 64 8653 9128 9009 -216 471 -345 O
ATOM 293 CB PRO A 64 1.670 48.184 46.342 1.00 74.49 C
ANISOU 293 CB PRO A 64 9116 9584 9600 -168 450 -333 C
ATOM 294 CG PRO A 64 0.615 47.397 45.642 1.00 71.72 C
ANISOU 294 CG PRO A 64 8750 9225 9273 -155 446 -322 C
ATOM 295 CD PRO A 64 0.959 45.959 45.888 1.00 73.73 C
ANISOU 295 CD PRO A 64 9022 9505 9486 -166 440 -296 C
ATOM 296 N LEU A 65 4.910 46.793 47.633 1.00 68.36 N
ANISOU 296 N LEU A 65 8405 8866 8700 -208 424 -286 N
ATOM 297 CA LEU A 65 5.762 46.779 48.824 1.00 67.80 C
ANISOU 297 CA LEU A 65 8355 8819 8587 -234 432 -292 C
ATOM 298 C LEU A 65 6.452 48.121 49.046 1.00 71.60 C
ANISOU 298 C LEU A 65 8840 9291 9074 -235 433 -310 C
ATOM 299 O LEU A 65 6.605 48.562 50.186 1.00 76.03 O
ANISOU 299 O LEU A 65 9409 9864 9614 -257 453 -333 O
ATOM 300 CB LEU A 65 6.805 45.667 48.741 1.00 64.53 C
ANISOU 300 CB LEU A 65 7960 8421 8137 -240 408 -256 C
ATOM 301 CG LEU A 65 6.346 44.218 48.904 1.00 64.70 C
ANISOU 301 CG LEU A 65 7983 8459 8139 -248 408 -238 C
ATOM 302 CD1 LEU A 65 7.549 43.289 48.877 1.00 62.62 C
ANISOU 302 CD1 LEU A 65 7739 8210 7842 -255 384 -204 C
ATOM 303 CD2 LEU A 65 5.551 44.012 50.185 1.00 63.48 C
ANISOU 303 CD2 LEU A 65 7829 8321 7966 -273 439 -262 C
ATOM 304 N LYS A 66 6.881 48.745 47.951 1.00 71.50 N
ANISOU 304 N LYS A 66 8822 9257 9088 -213 413 -299 N
ATOM 305 CA LYS A 66 7.344 50.143 47.928 1.00 70.05 C
ANISOU 305 CA LYS A 66 8637 9058 8922 -208 413 -317 C
ATOM 306 C LYS A 66 8.670 50.425 48.666 1.00 69.11 C
ANISOU 306 C LYS A 66 8538 8952 8766 -225 408 -315 C
ATOM 307 O LYS A 66 9.596 50.988 48.082 1.00 71.18 O
ANISOU 307 O LYS A 66 8806 9204 9035 -215 389 -303 O
ATOM 308 CB LYS A 66 6.216 51.101 48.370 1.00 69.70 C
ANISOU 308 CB LYS A 66 8572 9000 8908 -209 441 -357 C
ATOM 309 CG LYS A 66 5.019 51.170 47.419 1.00 70.71 C
ANISOU 309 CG LYS A 66 8676 9105 9084 -186 441 -359 C
ATOM 310 CD LYS A 66 5.287 52.071 46.212 1.00 73.45 C
ANISOU 310 CD LYS A 66 9014 9423 9468 -162 419 -350 C
ATOM 311 CE LYS A 66 4.264 51.902 45.085 1.00 70.90 C
ANISOU 311 CE LYS A 66 8671 9080 9187 -140 409 -341 C
ATOM 312 NZ LYS A 66 3.061 52.783 45.165 1.00 69.51 N
ANISOU 312 NZ LYS A 66 8469 8882 9057 -133 428 -373 N
ATOM 313 N ILE A 67 8.749 50.044 49.940 1.00 68.44 N
ANISOU 313 N ILE A 67 8466 8891 8645 -252 425 -327 N
ATOM 314 CA ILE A 67 9.954 50.216 50.753 1.00 67.29 C
ANISOU 314 CA ILE A 67 8342 8760 8462 -272 419 -325 C
ATOM 315 C ILE A 67 10.230 48.900 51.465 1.00 65.44 C
ANISOU 315 C ILE A 67 8124 8553 8184 -294 417 -306 C
ATOM 316 O ILE A 67 9.304 48.221 51.906 1.00 67.89 O
ANISOU 316 O ILE A 67 8430 8875 8488 -303 434 -313 O
ATOM 317 CB ILE A 67 9.778 51.322 51.824 1.00 71.81 C
ANISOU 317 CB ILE A 67 8915 9335 9033 -290 445 -365 C
ATOM 318 CG1 ILE A 67 9.243 52.617 51.203 1.00 71.72 C
ANISOU 318 CG1 ILE A 67 8883 9294 9070 -269 452 -388 C
ATOM 319 CG2 ILE A 67 11.092 51.592 52.555 1.00 70.66 C
ANISOU 319 CG2 ILE A 67 8792 9202 8852 -309 436 -361 C
ATOM 320 CD1 ILE A 67 8.160 53.291 52.020 1.00 72.67 C
ANISOU 320 CD1 ILE A 67 8991 9413 9206 -280 487 -431 C
ATOM 321 N LEU A 68 11.501 48.536 51.576 1.00 65.74 N
ANISOU 321 N LEU A 68 8180 8602 8194 -302 395 -282 N
ATOM 322 CA LEU A 68 11.885 47.352 52.335 1.00 67.52 C
ANISOU 322 CA LEU A 68 8423 8853 8379 -325 390 -263 C
ATOM 323 C LEU A 68 12.333 47.741 53.735 1.00 69.64 C
ANISOU 323 C LEU A 68 8709 9139 8612 -356 403 -282 C
ATOM 324 O LEU A 68 13.527 47.774 54.041 1.00 68.23 O
ANISOU 324 O LEU A 68 8546 8966 8410 -367 385 -268 O
ATOM 325 CB LEU A 68 12.956 46.543 51.598 1.00 68.45 C
ANISOU 325 CB LEU A 68 8549 8971 8488 -315 357 -223 C
ATOM 326 CG LEU A 68 12.525 45.237 50.918 1.00 68.32 C
ANISOU 326 CG LEU A 68 8526 8956 8475 -305 347 -196 C
ATOM 327 CD1 LEU A 68 11.067 45.249 50.475 1.00 66.61 C
ANISOU 327 CD1 LEU A 68 8289 8729 8287 -291 365 -212 C
ATOM 328 CD2 LEU A 68 13.443 44.924 49.747 1.00 68.70 C
ANISOU 328 CD2 LEU A 68 8574 8992 8534 -285 318 -165 C
ATOM 329 N LYS A 69 11.338 48.039 54.568 1.00 72.94 N
ANISOU 329 N LYS A 69 9122 9563 9026 -371 434 -314 N
ATOM 330 CA LYS A 69 11.525 48.468 55.951 1.00 73.64 C
ANISOU 330 CA LYS A 69 9227 9669 9083 -403 452 -339 C
ATOM 331 C LYS A 69 12.517 47.568 56.685 1.00 73.21 C
ANISOU 331 C LYS A 69 9197 9637 8980 -429 434 -313 C
ATOM 332 O LYS A 69 12.540 46.353 56.477 1.00 74.09 O
ANISOU 332 O LYS A 69 9312 9759 9080 -430 420 -284 O
ATOM 333 CB LYS A 69 10.176 48.462 56.677 1.00 75.10 C
ANISOU 333 CB LYS A 69 9404 9861 9267 -417 488 -371 C
ATOM 334 CG LYS A 69 9.949 49.646 57.604 1.00 78.42 C
ANISOU 334 CG LYS A 69 9827 10283 9686 -435 517 -414 C
ATOM 335 CD LYS A 69 9.072 50.716 56.962 1.00 78.59 C
ANISOU 335 CD LYS A 69 9822 10277 9759 -410 534 -443 C
ATOM 336 CE LYS A 69 9.159 52.043 57.710 1.00 82.41 C
ANISOU 336 CE LYS A 69 10308 10757 10245 -423 555 -483 C
ATOM 337 NZ LYS A 69 8.721 51.977 59.137 1.00 81.52 N
ANISOU 337 NZ LYS A 69 10207 10667 10097 -459 587 -512 N
ATOM 338 N SER A 70 13.337 48.179 57.536 1.00 71.34 N
ANISOU 338 N SER A 70 8977 9409 8719 -450 433 -323 N
ATOM 339 CA SER A 70 14.354 47.461 58.292 1.00 69.82 C
ANISOU 339 CA SER A 70 8808 9236 8481 -477 414 -300 C
ATOM 340 C SER A 70 13.724 46.365 59.137 1.00 68.13 C
ANISOU 340 C SER A 70 8604 9046 8236 -503 426 -296 C
ATOM 341 O SER A 70 12.681 46.575 59.744 1.00 70.90 O
ANISOU 341 O SER A 70 8951 9404 8584 -515 458 -326 O
ATOM 342 CB SER A 70 15.122 48.432 59.185 1.00 70.57 C
ANISOU 342 CB SER A 70 8920 9336 8556 -498 417 -319 C
ATOM 343 OG SER A 70 16.385 47.903 59.533 1.00 74.44 O
ANISOU 343 OG SER A 70 9429 9837 9016 -514 387 -289 O
ATOM 344 N TYR A 71 14.358 45.194 59.159 1.00 70.21 N
ANISOU 344 N TYR A 71 8879 9321 8477 -511 400 -259 N
ATOM 345 CA TYR A 71 13.906 44.039 59.962 1.00 71.64 C
ANISOU 345 CA TYR A 71 9070 9525 8624 -538 406 -248 C
ATOM 346 C TYR A 71 12.673 43.290 59.429 1.00 71.76 C
ANISOU 346 C TYR A 71 9067 9537 8658 -523 419 -247 C
ATOM 347 O TYR A 71 12.283 42.267 60.001 1.00 68.45 O
ANISOU 347 O TYR A 71 8656 9137 8214 -544 423 -235 O
ATOM 348 CB TYR A 71 13.709 44.426 61.441 1.00 70.93 C
ANISOU 348 CB TYR A 71 8998 9455 8494 -578 429 -276 C
ATOM 349 CG TYR A 71 14.954 44.997 62.063 1.00 73.51 C
ANISOU 349 CG TYR A 71 9345 9786 8797 -596 413 -274 C
ATOM 350 CD1 TYR A 71 15.107 46.374 62.237 1.00 73.02 C
ANISOU 350 CD1 TYR A 71 9283 9715 8745 -594 427 -307 C
ATOM 351 CD2 TYR A 71 15.999 44.162 62.453 1.00 75.52 C
ANISOU 351 CD2 TYR A 71 9619 10053 9020 -615 382 -240 C
ATOM 352 CE1 TYR A 71 16.262 46.899 62.792 1.00 72.22 C
ANISOU 352 CE1 TYR A 71 9200 9617 8622 -611 410 -304 C
ATOM 353 CE2 TYR A 71 17.161 44.676 63.007 1.00 75.37 C
ANISOU 353 CE2 TYR A 71 9618 10037 8980 -632 364 -236 C
ATOM 354 CZ TYR A 71 17.289 46.041 63.174 1.00 74.05 C
ANISOU 354 CZ TYR A 71 9451 9862 8823 -630 379 -269 C
ATOM 355 OH TYR A 71 18.449 46.531 63.725 1.00 74.52 O
ANISOU 355 OH TYR A 71 9528 9924 8861 -647 361 -265 O
ATOM 356 N SER A 72 12.082 43.784 58.335 1.00 71.77 N
ANISOU 356 N SER A 72 9046 9518 8705 -489 426 -256 N
ATOM 357 CA SER A 72 10.879 43.182 57.729 1.00 70.80 C
ANISOU 357 CA SER A 72 8904 9389 8606 -473 438 -256 C
ATOM 358 C SER A 72 10.851 41.660 57.824 1.00 69.46 C
ANISOU 358 C SER A 72 8740 9234 8415 -483 423 -223 C
ATOM 359 O SER A 72 9.836 41.074 58.196 1.00 69.63 O
ANISOU 359 O SER A 72 8758 9267 8431 -493 443 -230 O
ATOM 360 CB SER A 72 10.735 43.594 56.256 1.00 71.13 C
ANISOU 360 CB SER A 72 8925 9404 8697 -432 427 -251 C
ATOM 361 OG SER A 72 10.037 44.821 56.105 1.00 69.59 O
ANISOU 361 OG SER A 72 8714 9193 8531 -420 451 -286 O
ATOM 362 N PHE A 73 11.981 41.037 57.503 1.00 69.42 N
ANISOU 362 N PHE A 73 8745 9230 8400 -480 390 -188 N
ATOM 363 CA PHE A 73 12.074 39.588 57.387 1.00 70.26 C
ANISOU 363 CA PHE A 73 8854 9346 8493 -485 371 -154 C
ATOM 364 C PHE A 73 12.805 38.936 58.554 1.00 72.94 C
ANISOU 364 C PHE A 73 9218 9708 8787 -521 359 -137 C
ATOM 365 O PHE A 73 13.110 37.745 58.503 1.00 77.23 O
ANISOU 365 O PHE A 73 9766 10259 9319 -527 338 -105 O
ATOM 366 CB PHE A 73 12.780 39.212 56.078 1.00 68.96 C
ANISOU 366 CB PHE A 73 8680 9164 8355 -454 341 -123 C
ATOM 367 CG PHE A 73 12.134 39.783 54.846 1.00 67.31 C
ANISOU 367 CG PHE A 73 8450 8932 8191 -418 348 -135 C
ATOM 368 CD1 PHE A 73 11.097 39.105 54.210 1.00 65.47 C
ANISOU 368 CD1 PHE A 73 8201 8694 7978 -403 354 -130 C
ATOM 369 CD2 PHE A 73 12.568 40.991 54.314 1.00 66.38 C
ANISOU 369 CD2 PHE A 73 8328 8798 8096 -401 346 -148 C
ATOM 370 CE1 PHE A 73 10.501 39.626 53.072 1.00 65.40 C
ANISOU 370 CE1 PHE A 73 8174 8665 8011 -372 358 -139 C
ATOM 371 CE2 PHE A 73 11.972 41.517 53.176 1.00 68.43 C
ANISOU 371 CE2 PHE A 73 8568 9036 8396 -370 350 -157 C
ATOM 372 CZ PHE A 73 10.936 40.834 52.556 1.00 65.34 C
ANISOU 372 CZ PHE A 73 8162 8639 8024 -355 356 -152 C
ATOM 373 N SER A 74 13.083 39.705 59.602 1.00 76.52 N
ANISOU 373 N SER A 74 9687 10172 9214 -548 371 -159 N
ATOM 374 CA SER A 74 13.849 39.200 60.748 1.00 79.38 C
ANISOU 374 CA SER A 74 10074 10555 9530 -585 358 -144 C
ATOM 375 C SER A 74 13.253 37.940 61.381 1.00 80.13 C
ANISOU 375 C SER A 74 10176 10670 9599 -609 361 -129 C
ATOM 376 O SER A 74 13.984 37.111 61.928 1.00 76.18 O
ANISOU 376 O SER A 74 9692 10183 9070 -631 337 -101 O
ATOM 377 CB SER A 74 14.015 40.286 61.809 1.00 81.20 C
ANISOU 377 CB SER A 74 10319 10795 9735 -611 376 -176 C
ATOM 378 OG SER A 74 14.889 39.848 62.831 1.00 85.23 O
ANISOU 378 OG SER A 74 10855 11323 10203 -646 358 -158 O
ATOM 379 N ASN A 75 11.928 37.811 61.297 1.00 85.77 N
ANISOU 379 N ASN A 75 10876 11386 10325 -604 389 -148 N
ATOM 380 CA ASN A 75 11.207 36.646 61.810 1.00 91.54 C
ANISOU 380 CA ASN A 75 11610 12133 11035 -624 396 -136 C
ATOM 381 C ASN A 75 11.618 35.335 61.124 1.00 94.73 C
ANISOU 381 C ASN A 75 12010 12534 11447 -611 363 -93 C
ATOM 382 O ASN A 75 12.162 34.437 61.776 1.00 94.82 O
ANISOU 382 O ASN A 75 12038 12560 11428 -637 343 -66 O
ATOM 383 CB ASN A 75 9.683 36.862 61.719 1.00 92.48 C
ANISOU 383 CB ASN A 75 11712 12251 11173 -616 434 -167 C
ATOM 384 CG ASN A 75 9.101 37.528 62.961 1.00 92.23 C
ANISOU 384 CG ASN A 75 11693 12236 11114 -649 470 -204 C
ATOM 385 OD1 ASN A 75 9.502 37.233 64.088 1.00 91.89 O
ANISOU 385 OD1 ASN A 75 11673 12214 11026 -688 468 -199 O
ATOM 386 ND2 ASN A 75 8.134 38.417 62.758 1.00 89.14 N
ANISOU 386 ND2 ASN A 75 11284 11833 10749 -636 503 -242 N
ATOM 387 N PHE A 76 11.371 35.245 59.813 1.00 94.43 N
ANISOU 387 N PHE A 76 11951 12476 11452 -572 356 -86 N
ATOM 388 CA PHE A 76 11.613 34.020 59.038 1.00 92.78 C
ANISOU 388 CA PHE A 76 11734 12261 11255 -557 329 -48 C
ATOM 389 C PHE A 76 13.105 33.781 58.839 1.00 93.68 C
ANISOU 389 C PHE A 76 11858 12371 11365 -556 292 -18 C
ATOM 390 O PHE A 76 13.689 34.246 57.861 1.00 94.97 O
ANISOU 390 O PHE A 76 12012 12516 11556 -528 279 -14 O
ATOM 391 CB PHE A 76 10.913 34.072 57.670 1.00 89.00 C
ANISOU 391 CB PHE A 76 11231 11762 10822 -517 334 -52 C
ATOM 392 CG PHE A 76 9.674 34.925 57.643 1.00 89.92 C
ANISOU 392 CG PHE A 76 11334 11874 10957 -509 370 -90 C
ATOM 393 CD1 PHE A 76 8.479 34.469 58.197 1.00 89.92 C
ANISOU 393 CD1 PHE A 76 11330 11885 10948 -524 395 -102 C
ATOM 394 CD2 PHE A 76 9.698 36.184 57.048 1.00 89.15 C
ANISOU 394 CD2 PHE A 76 11227 11759 10887 -486 378 -113 C
ATOM 395 CE1 PHE A 76 7.336 35.258 58.167 1.00 90.02 C
ANISOU 395 CE1 PHE A 76 11329 11892 10982 -516 429 -138 C
ATOM 396 CE2 PHE A 76 8.559 36.976 57.013 1.00 88.02 C
ANISOU 396 CE2 PHE A 76 11070 11609 10764 -479 410 -148 C
ATOM 397 CZ PHE A 76 7.376 36.511 57.572 1.00 91.55 C
ANISOU 397 CZ PHE A 76 11512 12067 11205 -493 436 -161 C
ATOM 398 N SER A 77 13.711 33.048 59.767 1.00 94.73 N
ANISOU 398 N SER A 77 12009 12520 11462 -588 275 2 N
ATOM 399 CA SER A 77 15.156 32.830 59.765 1.00 96.02 C
ANISOU 399 CA SER A 77 12183 12680 11619 -592 239 30 C
ATOM 400 C SER A 77 15.610 31.678 58.864 1.00 94.54 C
ANISOU 400 C SER A 77 11984 12482 11453 -573 209 66 C
ATOM 401 O SER A 77 16.768 31.635 58.445 1.00 93.49 O
ANISOU 401 O SER A 77 11853 12339 11330 -563 182 86 O
ATOM 402 CB SER A 77 15.651 32.594 61.192 1.00103.50 C
ANISOU 402 CB SER A 77 13155 13649 12520 -637 231 37 C
ATOM 403 OG SER A 77 15.097 31.403 61.727 1.00109.55 O
ANISOU 403 OG SER A 77 13926 14430 13267 -658 230 54 O
ATOM 404 N GLU A 78 14.698 30.753 58.571 1.00 95.22 N
ANISOU 404 N GLU A 78 12061 12571 11548 -567 216 74 N
ATOM 405 CA GLU A 78 15.035 29.532 57.829 1.00 93.01 C
ANISOU 405 CA GLU A 78 11770 12282 11284 -552 189 108 C
ATOM 406 C GLU A 78 14.783 29.677 56.328 1.00 88.58 C
ANISOU 406 C GLU A 78 11188 11699 10767 -510 190 105 C
ATOM 407 O GLU A 78 14.936 28.717 55.563 1.00 86.69 O
ANISOU 407 O GLU A 78 10940 11452 10547 -494 172 130 O
ATOM 408 CB GLU A 78 14.232 28.355 58.370 1.00 95.60 C
ANISOU 408 CB GLU A 78 12100 12625 11596 -572 192 121 C
ATOM 409 CG GLU A 78 14.072 28.358 59.876 1.00 97.83 C
ANISOU 409 CG GLU A 78 12403 12931 11834 -615 202 115 C
ATOM 410 CD GLU A 78 12.657 28.026 60.282 1.00103.25 C
ANISOU 410 CD GLU A 78 13087 13630 12511 -626 231 100 C
ATOM 411 OE1 GLU A 78 12.093 28.762 61.117 1.00101.51 O
ANISOU 411 OE1 GLU A 78 12876 13423 12268 -647 260 71 O
ATOM 412 OE2 GLU A 78 12.103 27.041 59.748 1.00107.51 O
ANISOU 412 OE2 GLU A 78 13615 14167 13067 -614 227 116 O
ATOM 413 N LEU A 79 14.400 30.886 55.926 1.00 81.79 N
ANISOU 413 N LEU A 79 10322 10831 9923 -493 211 76 N
ATOM 414 CA LEU A 79 14.110 31.216 54.538 1.00 74.07 C
ANISOU 414 CA LEU A 79 9325 9832 8984 -454 214 70 C
ATOM 415 C LEU A 79 15.316 30.976 53.636 1.00 72.40 C
ANISOU 415 C LEU A 79 9111 9605 8791 -436 185 94 C
ATOM 416 O LEU A 79 16.460 31.231 54.026 1.00 72.57 O
ANISOU 416 O LEU A 79 9143 9628 8801 -447 168 103 O
ATOM 417 CB LEU A 79 13.661 32.674 54.444 1.00 71.30 C
ANISOU 417 CB LEU A 79 8971 9474 8643 -444 239 35 C
ATOM 418 CG LEU A 79 12.575 33.063 53.446 1.00 69.72 C
ANISOU 418 CG LEU A 79 8751 9259 8477 -415 257 17 C
ATOM 419 CD1 LEU A 79 11.383 32.132 53.567 1.00 72.50 C
ANISOU 419 CD1 LEU A 79 9097 9620 8829 -419 270 19 C
ATOM 420 CD2 LEU A 79 12.139 34.503 53.668 1.00 69.23 C
ANISOU 420 CD2 LEU A 79 8688 9194 8421 -413 282 -18 C
ATOM 421 N GLN A 80 15.044 30.474 52.434 1.00 67.43 N
ANISOU 421 N GLN A 80 8467 8962 8192 -408 179 104 N
ATOM 422 CA GLN A 80 16.081 30.133 51.469 1.00 62.13 C
ANISOU 422 CA GLN A 80 7789 8275 7539 -389 153 126 C
ATOM 423 C GLN A 80 15.865 30.806 50.125 1.00 57.19 C
ANISOU 423 C GLN A 80 7150 7630 6947 -355 159 115 C
ATOM 424 O GLN A 80 16.826 31.051 49.409 1.00 54.66 O
ANISOU 424 O GLN A 80 6828 7297 6641 -341 144 124 O
ATOM 425 CB GLN A 80 16.124 28.629 51.257 1.00 64.10 C
ANISOU 425 CB GLN A 80 8035 8527 7792 -390 135 155 C
ATOM 426 CG GLN A 80 17.055 27.883 52.190 1.00 66.34 C
ANISOU 426 CG GLN A 80 8330 8821 8053 -417 113 179 C
ATOM 427 CD GLN A 80 17.321 26.467 51.712 1.00 68.98 C
ANISOU 427 CD GLN A 80 8657 9150 8400 -412 90 209 C
ATOM 428 OE1 GLN A 80 16.395 25.731 51.341 1.00 68.70 O
ANISOU 428 OE1 GLN A 80 8613 9115 8374 -404 97 212 O
ATOM 429 NE2 GLN A 80 18.592 26.077 51.710 1.00 68.95 N
ANISOU 429 NE2 GLN A 80 8656 9141 8399 -416 64 231 N
ATOM 430 N TRP A 81 14.604 31.107 49.809 1.00 56.24 N
ANISOU 430 N TRP A 81 7021 7507 6838 -344 181 96 N
ATOM 431 CA TRP A 81 14.192 31.604 48.495 1.00 55.94 C
ANISOU 431 CA TRP A 81 6970 7451 6833 -312 186 87 C
ATOM 432 C TRP A 81 13.137 32.660 48.645 1.00 54.38 C
ANISOU 432 C TRP A 81 6767 7252 6642 -309 212 56 C
ATOM 433 O TRP A 81 12.021 32.368 49.070 1.00 55.28 O
ANISOU 433 O TRP A 81 6877 7374 6752 -316 229 46 O
ATOM 434 CB TRP A 81 13.654 30.437 47.663 1.00 60.14 C
ANISOU 434 CB TRP A 81 7491 7978 7381 -298 178 104 C
ATOM 435 CG TRP A 81 13.325 30.737 46.213 1.00 61.42 C
ANISOU 435 CG TRP A 81 7640 8120 7575 -267 178 101 C
ATOM 436 CD1 TRP A 81 14.167 30.616 45.112 1.00 61.32 C
ANISOU 436 CD1 TRP A 81 7626 8094 7579 -249 160 116 C
ATOM 437 CD2 TRP A 81 12.032 31.185 45.654 1.00 61.61 C
ANISOU 437 CD2 TRP A 81 7653 8137 7619 -251 195 83 C
ATOM 438 NE1 TRP A 81 13.516 30.963 43.956 1.00 61.38 N
ANISOU 438 NE1 TRP A 81 7622 8085 7611 -225 165 108 N
ATOM 439 CE2 TRP A 81 12.236 31.311 44.206 1.00 60.71 C
ANISOU 439 CE2 TRP A 81 7531 8003 7531 -225 184 89 C
ATOM 440 CE3 TRP A 81 10.782 31.493 46.190 1.00 62.29 C
ANISOU 440 CE3 TRP A 81 7733 8228 7704 -257 218 62 C
ATOM 441 CZ2 TRP A 81 11.221 31.726 43.351 1.00 62.35 C
ANISOU 441 CZ2 TRP A 81 7728 8198 7763 -205 194 77 C
ATOM 442 CZ3 TRP A 81 9.767 31.911 45.317 1.00 63.29 C
ANISOU 442 CZ3 TRP A 81 7846 8340 7858 -236 228 49 C
ATOM 443 CH2 TRP A 81 9.983 32.022 43.931 1.00 63.38 C
ANISOU 443 CH2 TRP A 81 7851 8333 7894 -211 215 57 C
ATOM 444 N LEU A 82 13.478 33.900 48.298 1.00 53.28 N
ANISOU 444 N LEU A 82 6627 7101 6514 -298 216 40 N
ATOM 445 CA LEU A 82 12.554 35.030 48.423 1.00 52.83 C
ANISOU 445 CA LEU A 82 6564 7040 6467 -293 241 9 C
ATOM 446 C LEU A 82 12.431 35.779 47.107 1.00 52.47 C
ANISOU 446 C LEU A 82 6507 6972 6455 -264 239 3 C
ATOM 447 O LEU A 82 13.427 36.255 46.563 1.00 56.44 O
ANISOU 447 O LEU A 82 7013 7465 6964 -254 225 11 O
ATOM 448 CB LEU A 82 12.994 35.992 49.543 1.00 53.13 C
ANISOU 448 CB LEU A 82 6614 7087 6484 -314 251 -9 C
ATOM 449 CG LEU A 82 12.158 37.258 49.817 1.00 52.73 C
ANISOU 449 CG LEU A 82 6558 7032 6444 -313 278 -44 C
ATOM 450 CD1 LEU A 82 10.781 36.950 50.388 1.00 51.93 C
ANISOU 450 CD1 LEU A 82 6450 6940 6340 -323 302 -60 C
ATOM 451 CD2 LEU A 82 12.900 38.198 50.746 1.00 53.84 C
ANISOU 451 CD2 LEU A 82 6712 7179 6565 -331 282 -59 C
ATOM 452 N ASP A 83 11.199 35.897 46.617 1.00 51.98 N
ANISOU 452 N ASP A 83 6431 6902 6414 -250 252 -8 N
ATOM 453 CA ASP A 83 10.925 36.492 45.314 1.00 51.05 C
ANISOU 453 CA ASP A 83 6303 6763 6330 -223 249 -11 C
ATOM 454 C ASP A 83 10.100 37.772 45.449 1.00 50.49 C
ANISOU 454 C ASP A 83 6223 6683 6276 -218 269 -42 C
ATOM 455 O ASP A 83 8.897 37.735 45.721 1.00 49.27 O
ANISOU 455 O ASP A 83 6059 6530 6131 -220 287 -58 O
ATOM 456 CB ASP A 83 10.216 35.470 44.416 1.00 51.89 C
ANISOU 456 CB ASP A 83 6399 6863 6452 -208 242 3 C
ATOM 457 CG ASP A 83 10.123 35.905 42.962 1.00 50.60 C
ANISOU 457 CG ASP A 83 6227 6679 6319 -182 232 6 C
ATOM 458 OD1 ASP A 83 10.190 37.113 42.652 1.00 50.17 O
ANISOU 458 OD1 ASP A 83 6170 6611 6279 -173 236 -8 O
ATOM 459 OD2 ASP A 83 9.966 35.010 42.112 1.00 53.48 O
ANISOU 459 OD2 ASP A 83 6588 7039 6693 -170 220 24 O
ATOM 460 N LEU A 84 10.767 38.901 45.226 1.00 50.91 N
ANISOU 460 N LEU A 84 6279 6726 6338 -212 266 -51 N
ATOM 461 CA LEU A 84 10.153 40.214 45.343 1.00 50.72 C
ANISOU 461 CA LEU A 84 6247 6691 6332 -208 284 -80 C
ATOM 462 C LEU A 84 10.120 40.940 43.992 1.00 51.18 C
ANISOU 462 C LEU A 84 6296 6726 6424 -182 273 -79 C
ATOM 463 O LEU A 84 10.237 42.166 43.938 1.00 52.86 O
ANISOU 463 O LEU A 84 6506 6926 6651 -177 278 -96 O
ATOM 464 CB LEU A 84 10.896 41.052 46.399 1.00 51.30 C
ANISOU 464 CB LEU A 84 6332 6773 6386 -226 291 -96 C
ATOM 465 CG LEU A 84 11.207 40.401 47.761 1.00 54.31 C
ANISOU 465 CG LEU A 84 6727 7178 6728 -256 297 -94 C
ATOM 466 CD1 LEU A 84 12.336 41.120 48.481 1.00 52.51 C
ANISOU 466 CD1 LEU A 84 6514 6957 6480 -270 294 -99 C
ATOM 467 CD2 LEU A 84 9.977 40.304 48.659 1.00 53.89 C
ANISOU 467 CD2 LEU A 84 6669 7137 6670 -270 324 -116 C
ATOM 468 N SER A 85 9.955 40.186 42.906 1.00 49.89 N
ANISOU 468 N SER A 85 6128 6554 6273 -166 259 -58 N
ATOM 469 CA SER A 85 9.831 40.771 41.567 1.00 52.05 C
ANISOU 469 CA SER A 85 6393 6805 6577 -143 248 -55 C
ATOM 470 C SER A 85 8.645 41.724 41.470 1.00 52.22 C
ANISOU 470 C SER A 85 6399 6812 6628 -134 263 -79 C
ATOM 471 O SER A 85 7.594 41.470 42.052 1.00 56.76 O
ANISOU 471 O SER A 85 6965 7392 7206 -140 279 -93 O
ATOM 472 CB SER A 85 9.673 39.677 40.513 1.00 53.33 C
ANISOU 472 CB SER A 85 6553 6964 6746 -130 232 -30 C
ATOM 473 OG SER A 85 10.778 38.795 40.515 1.00 57.62 O
ANISOU 473 OG SER A 85 7108 7517 7267 -136 218 -8 O
ATOM 474 N ARG A 86 8.818 42.816 40.733 1.00 51.14 N
ANISOU 474 N ARG A 86 6258 6656 6514 -120 256 -85 N
ATOM 475 CA ARG A 86 7.752 43.798 40.509 1.00 52.83 C
ANISOU 475 CA ARG A 86 6457 6852 6762 -111 267 -107 C
ATOM 476 C ARG A 86 6.995 44.236 41.773 1.00 54.91 C
ANISOU 476 C ARG A 86 6714 7124 7026 -125 294 -137 C
ATOM 477 O ARG A 86 5.776 44.129 41.836 1.00 58.56 O
ANISOU 477 O ARG A 86 7161 7581 7507 -122 306 -150 O
ATOM 478 CB ARG A 86 6.752 43.262 39.483 1.00 51.07 C
ANISOU 478 CB ARG A 86 6222 6616 6564 -95 259 -97 C
ATOM 479 CG ARG A 86 6.238 44.328 38.537 1.00 48.88 C
ANISOU 479 CG ARG A 86 5932 6313 6325 -77 252 -104 C
ATOM 480 CD ARG A 86 7.318 44.633 37.525 1.00 48.85 C
ANISOU 480 CD ARG A 86 5940 6300 6321 -68 230 -84 C
ATOM 481 NE ARG A 86 7.251 46.003 37.062 1.00 49.58 N
ANISOU 481 NE ARG A 86 6024 6370 6441 -58 226 -95 N
ATOM 482 CZ ARG A 86 8.182 46.585 36.319 1.00 50.38 C
ANISOU 482 CZ ARG A 86 6134 6462 6544 -52 211 -84 C
ATOM 483 NH1 ARG A 86 9.265 45.915 35.946 1.00 50.04 N
ANISOU 483 NH1 ARG A 86 6106 6428 6475 -54 198 -61 N
ATOM 484 NH2 ARG A 86 8.024 47.847 35.947 1.00 53.03 N
ANISOU 484 NH2 ARG A 86 6462 6777 6907 -44 208 -95 N
ATOM 485 N CYS A 87 7.713 44.726 42.777 1.00 56.37 N
ANISOU 485 N CYS A 87 6908 7319 7188 -141 303 -149 N
ATOM 486 CA CYS A 87 7.081 45.143 44.027 1.00 55.43 C
ANISOU 486 CA CYS A 87 6785 7209 7065 -157 330 -180 C
ATOM 487 C CYS A 87 7.152 46.649 44.239 1.00 57.16 C
ANISOU 487 C CYS A 87 6999 7414 7302 -156 340 -206 C
ATOM 488 O CYS A 87 6.807 47.154 45.309 1.00 58.02 O
ANISOU 488 O CYS A 87 7107 7531 7407 -171 363 -233 O
ATOM 489 CB CYS A 87 7.689 44.399 45.210 1.00 54.03 C
ANISOU 489 CB CYS A 87 6624 7059 6844 -182 337 -176 C
ATOM 490 SG CYS A 87 7.231 42.657 45.265 1.00 52.82 S
ANISOU 490 SG CYS A 87 6473 6922 6671 -188 334 -153 S
ATOM 491 N GLU A 88 7.595 47.355 43.201 1.00 58.42 N
ANISOU 491 N GLU A 88 7157 7555 7485 -138 322 -197 N
ATOM 492 CA GLU A 88 7.684 48.817 43.197 1.00 59.65 C
ANISOU 492 CA GLU A 88 7306 7693 7664 -133 326 -218 C
ATOM 493 C GLU A 88 8.600 49.374 44.307 1.00 59.91 C
ANISOU 493 C GLU A 88 7353 7740 7670 -152 336 -232 C
ATOM 494 O GLU A 88 8.446 50.522 44.742 1.00 62.21 O
ANISOU 494 O GLU A 88 7637 8021 7977 -154 349 -259 O
ATOM 495 CB GLU A 88 6.283 49.439 43.249 1.00 61.97 C
ANISOU 495 CB GLU A 88 7577 7971 7996 -127 344 -245 C
ATOM 496 CG GLU A 88 5.266 48.746 42.352 1.00 65.60 C
ANISOU 496 CG GLU A 88 8024 8420 8479 -112 337 -232 C
ATOM 497 CD GLU A 88 3.835 49.142 42.664 1.00 68.37 C
ANISOU 497 CD GLU A 88 8353 8760 8864 -110 358 -260 C
ATOM 498 OE1 GLU A 88 3.447 50.276 42.314 1.00 70.92 O
ANISOU 498 OE1 GLU A 88 8661 9059 9224 -100 359 -277 O
ATOM 499 OE2 GLU A 88 3.094 48.318 43.246 1.00 66.83 O
ANISOU 499 OE2 GLU A 88 8153 8578 8658 -120 374 -266 O
ATOM 500 N ILE A 89 9.559 48.553 44.739 1.00 55.45 N
ANISOU 500 N ILE A 89 6805 7195 7066 -165 328 -214 N
ATOM 501 CA ILE A 89 10.548 48.931 45.750 1.00 53.48 C
ANISOU 501 CA ILE A 89 6571 6959 6787 -184 332 -222 C
ATOM 502 C ILE A 89 11.502 50.017 45.252 1.00 54.27 C
ANISOU 502 C ILE A 89 6675 7044 6900 -175 318 -220 C
ATOM 503 O ILE A 89 12.150 49.869 44.208 1.00 52.44 O
ANISOU 503 O ILE A 89 6446 6803 6674 -161 296 -195 O
ATOM 504 CB ILE A 89 11.363 47.711 46.222 1.00 50.60 C
ANISOU 504 CB ILE A 89 6225 6618 6382 -200 322 -198 C
ATOM 505 CG1 ILE A 89 10.439 46.686 46.882 1.00 50.87 C
ANISOU 505 CG1 ILE A 89 6256 6668 6401 -213 337 -201 C
ATOM 506 CG2 ILE A 89 12.459 48.136 47.189 1.00 50.03 C
ANISOU 506 CG2 ILE A 89 6169 6558 6281 -219 322 -203 C
ATOM 507 CD1 ILE A 89 10.942 45.261 46.802 1.00 52.05 C
ANISOU 507 CD1 ILE A 89 6417 6834 6525 -218 322 -170 C
ATOM 508 N GLU A 90 11.571 51.112 46.005 1.00 54.44 N
ANISOU 508 N GLU A 90 6696 7063 6925 -184 332 -248 N
ATOM 509 CA GLU A 90 12.502 52.189 45.701 1.00 56.37 C
ANISOU 509 CA GLU A 90 6944 7295 7178 -179 321 -249 C
ATOM 510 C GLU A 90 13.578 52.312 46.771 1.00 56.54 C
ANISOU 510 C GLU A 90 6984 7334 7165 -200 322 -252 C
ATOM 511 O GLU A 90 14.618 52.928 46.540 1.00 57.63 O
ANISOU 511 O GLU A 90 7129 7465 7302 -198 309 -246 O
ATOM 512 CB GLU A 90 11.772 53.521 45.529 1.00 57.06 C
ANISOU 512 CB GLU A 90 7014 7359 7305 -168 332 -277 C
ATOM 513 CG GLU A 90 11.044 53.666 44.201 1.00 62.14 C
ANISOU 513 CG GLU A 90 7641 7979 7988 -144 321 -267 C
ATOM 514 CD GLU A 90 10.646 55.102 43.888 1.00 67.87 C
ANISOU 514 CD GLU A 90 8352 8679 8756 -133 325 -289 C
ATOM 515 OE1 GLU A 90 9.789 55.304 42.999 1.00 65.81 O
ANISOU 515 OE1 GLU A 90 8075 8398 8531 -116 319 -287 O
ATOM 516 OE2 GLU A 90 11.183 56.038 44.526 1.00 75.57 O
ANISOU 516 OE2 GLU A 90 9331 9653 9728 -141 331 -308 O
ATOM 517 N THR A 91 13.332 51.720 47.935 1.00 55.29 N
ANISOU 517 N THR A 91 6833 7196 6976 -223 338 -263 N
ATOM 518 CA THR A 91 14.247 51.869 49.054 1.00 55.18 C
ANISOU 518 CA THR A 91 6838 7200 6929 -246 340 -269 C
ATOM 519 C THR A 91 14.476 50.565 49.800 1.00 55.78 C
ANISOU 519 C THR A 91 6928 7302 6964 -267 339 -253 C
ATOM 520 O THR A 91 13.528 49.885 50.175 1.00 57.92 O
ANISOU 520 O THR A 91 7194 7582 7229 -274 354 -259 O
ATOM 521 CB THR A 91 13.759 52.970 50.020 1.00 53.43 C
ANISOU 521 CB THR A 91 6612 6976 6711 -259 366 -309 C
ATOM 522 OG1 THR A 91 13.779 54.227 49.338 1.00 52.64 O
ANISOU 522 OG1 THR A 91 6500 6852 6649 -241 363 -321 O
ATOM 523 CG2 THR A 91 14.645 53.070 51.258 1.00 50.80 C
ANISOU 523 CG2 THR A 91 6299 6662 6339 -287 369 -316 C
ATOM 524 N ILE A 92 15.746 50.223 49.989 1.00 56.77 N
ANISOU 524 N ILE A 92 7069 7436 7064 -276 320 -231 N
ATOM 525 CA ILE A 92 16.133 49.132 50.867 1.00 59.28 C
ANISOU 525 CA ILE A 92 7402 7778 7342 -300 316 -217 C
ATOM 526 C ILE A 92 16.804 49.760 52.075 1.00 61.29 C
ANISOU 526 C ILE A 92 7673 8044 7570 -325 322 -234 C
ATOM 527 O ILE A 92 17.909 50.289 51.988 1.00 61.85 O
ANISOU 527 O ILE A 92 7750 8109 7638 -324 306 -226 O
ATOM 528 CB ILE A 92 17.073 48.112 50.181 1.00 59.16 C
ANISOU 528 CB ILE A 92 7393 7765 7319 -293 288 -178 C
ATOM 529 CG1 ILE A 92 16.327 47.345 49.091 1.00 59.51 C
ANISOU 529 CG1 ILE A 92 7424 7801 7384 -271 284 -162 C
ATOM 530 CG2 ILE A 92 17.634 47.119 51.190 1.00 59.89 C
ANISOU 530 CG2 ILE A 92 7503 7881 7371 -319 281 -163 C
ATOM 531 CD1 ILE A 92 17.236 46.637 48.111 1.00 61.08 C
ANISOU 531 CD1 ILE A 92 7625 7995 7587 -258 258 -128 C
ATOM 532 N GLU A 93 16.107 49.706 53.200 1.00 65.69 N
ANISOU 532 N GLU A 93 8235 8617 8107 -347 345 -257 N
ATOM 533 CA GLU A 93 16.586 50.253 54.454 1.00 68.33 C
ANISOU 533 CA GLU A 93 8585 8964 8412 -375 353 -276 C
ATOM 534 C GLU A 93 17.835 49.503 54.874 1.00 67.88 C
ANISOU 534 C GLU A 93 8547 8921 8321 -392 329 -246 C
ATOM 535 O GLU A 93 18.120 48.432 54.341 1.00 66.87 O
ANISOU 535 O GLU A 93 8420 8797 8191 -385 310 -215 O
ATOM 536 CB GLU A 93 15.499 50.070 55.509 1.00 72.46 C
ANISOU 536 CB GLU A 93 9110 9503 8918 -398 384 -302 C
ATOM 537 CG GLU A 93 15.435 51.158 56.562 1.00 79.53 C
ANISOU 537 CG GLU A 93 10012 10403 9802 -418 406 -340 C
ATOM 538 CD GLU A 93 14.056 51.269 57.180 1.00 81.05 C
ANISOU 538 CD GLU A 93 10196 10600 9997 -429 441 -374 C
ATOM 539 OE1 GLU A 93 13.143 51.798 56.512 1.00 80.72 O
ANISOU 539 OE1 GLU A 93 10133 10541 9996 -407 455 -391 O
ATOM 540 OE2 GLU A 93 13.885 50.829 58.336 1.00 84.11 O
ANISOU 540 OE2 GLU A 93 10599 11011 10347 -460 455 -383 O
ATOM 541 N ASP A 94 18.584 50.068 55.817 1.00 70.68 N
ANISOU 541 N ASP A 94 8918 9285 8653 -415 328 -257 N
ATOM 542 CA ASP A 94 19.666 49.333 56.467 1.00 74.06 C
ANISOU 542 CA ASP A 94 9366 9729 9045 -437 306 -232 C
ATOM 543 C ASP A 94 19.071 48.113 57.155 1.00 71.10 C
ANISOU 543 C ASP A 94 8998 9375 8640 -458 312 -223 C
ATOM 544 O ASP A 94 17.880 48.100 57.469 1.00 66.36 O
ANISOU 544 O ASP A 94 8391 8780 8040 -463 339 -246 O
ATOM 545 CB ASP A 94 20.388 50.207 57.498 1.00 81.00 C
ANISOU 545 CB ASP A 94 10261 10614 9901 -461 307 -250 C
ATOM 546 CG ASP A 94 21.370 51.183 56.865 1.00 89.01 C
ANISOU 546 CG ASP A 94 11271 11609 10938 -444 291 -247 C
ATOM 547 OD1 ASP A 94 22.313 51.610 57.572 1.00 92.03 O
ANISOU 547 OD1 ASP A 94 11670 11997 11301 -463 281 -248 O
ATOM 548 OD2 ASP A 94 21.205 51.526 55.671 1.00 92.06 O
ANISOU 548 OD2 ASP A 94 11641 11976 11362 -413 288 -243 O
ATOM 549 N LYS A 95 19.896 47.092 57.375 1.00 71.84 N
ANISOU 549 N LYS A 95 9104 9480 8710 -471 287 -191 N
ATOM 550 CA LYS A 95 19.470 45.873 58.066 1.00 73.91 C
ANISOU 550 CA LYS A 95 9374 9762 8943 -493 289 -178 C
ATOM 551 C LYS A 95 18.061 45.416 57.650 1.00 74.10 C
ANISOU 551 C LYS A 95 9383 9787 8983 -480 311 -187 C
ATOM 552 O LYS A 95 17.265 44.963 58.482 1.00 73.74 O
ANISOU 552 O LYS A 95 9344 9758 8915 -502 329 -198 O
ATOM 553 CB LYS A 95 19.586 46.057 59.588 1.00 73.88 C
ANISOU 553 CB LYS A 95 9393 9781 8897 -533 299 -194 C
ATOM 554 CG LYS A 95 20.889 45.530 60.182 1.00 77.14 C
ANISOU 554 CG LYS A 95 9825 10203 9279 -556 268 -166 C
ATOM 555 CD LYS A 95 21.348 46.327 61.399 1.00 76.63 C
ANISOU 555 CD LYS A 95 9781 10150 9184 -588 273 -187 C
ATOM 556 CE LYS A 95 22.313 47.437 60.999 1.00 76.91 C
ANISOU 556 CE LYS A 95 9815 10168 9239 -574 261 -192 C
ATOM 557 NZ LYS A 95 22.567 48.415 62.096 1.00 76.73 N
ANISOU 557 NZ LYS A 95 9809 10153 9192 -601 272 -220 N
ATOM 558 N ALA A 96 17.763 45.550 56.356 1.00 74.35 N
ANISOU 558 N ALA A 96 9395 9798 9054 -446 308 -182 N
ATOM 559 CA ALA A 96 16.474 45.129 55.797 1.00 74.54 C
ANISOU 559 CA ALA A 96 9403 9819 9099 -430 325 -188 C
ATOM 560 C ALA A 96 16.410 43.611 55.738 1.00 75.74 C
ANISOU 560 C ALA A 96 9557 9982 9236 -435 311 -157 C
ATOM 561 O ALA A 96 15.335 43.009 55.882 1.00 78.33 O
ANISOU 561 O ALA A 96 9879 10318 9563 -438 327 -163 O
ATOM 562 CB ALA A 96 16.263 45.723 54.413 1.00 69.78 C
ANISOU 562 CB ALA A 96 8781 9191 8541 -393 322 -190 C
ATOM 563 N TRP A 97 17.581 43.008 55.548 1.00 72.04 N
ANISOU 563 N TRP A 97 9097 9514 8758 -436 281 -125 N
ATOM 564 CA TRP A 97 17.720 41.571 55.424 1.00 69.37 C
ANISOU 564 CA TRP A 97 8761 9185 8410 -440 263 -93 C
ATOM 565 C TRP A 97 18.217 40.955 56.698 1.00 71.73 C
ANISOU 565 C TRP A 97 9080 9506 8667 -476 255 -82 C
ATOM 566 O TRP A 97 18.693 39.820 56.692 1.00 75.54 O
ANISOU 566 O TRP A 97 9567 9994 9139 -483 233 -51 O
ATOM 567 CB TRP A 97 18.700 41.242 54.301 1.00 66.16 C
ANISOU 567 CB TRP A 97 8349 8763 8025 -417 235 -64 C
ATOM 568 CG TRP A 97 18.485 41.975 52.992 1.00 61.41 C
ANISOU 568 CG TRP A 97 7730 8139 7464 -382 238 -71 C
ATOM 569 CD1 TRP A 97 19.357 42.862 52.367 1.00 59.67 C
ANISOU 569 CD1 TRP A 97 7507 7902 7260 -367 227 -71 C
ATOM 570 CD2 TRP A 97 17.324 41.890 52.090 1.00 56.83 C
ANISOU 570 CD2 TRP A 97 7132 7548 6910 -359 252 -79 C
ATOM 571 NE1 TRP A 97 18.830 43.321 51.189 1.00 57.84 N
ANISOU 571 NE1 TRP A 97 7260 7653 7064 -338 233 -77 N
ATOM 572 CE2 TRP A 97 17.619 42.778 50.960 1.00 55.86 C
ANISOU 572 CE2 TRP A 97 6998 7403 6820 -331 246 -82 C
ATOM 573 CE3 TRP A 97 16.120 41.203 52.110 1.00 54.77 C
ANISOU 573 CE3 TRP A 97 6864 7294 6652 -358 266 -83 C
ATOM 574 CZ2 TRP A 97 16.733 42.951 49.912 1.00 55.27 C
ANISOU 574 CZ2 TRP A 97 6908 7314 6777 -306 254 -88 C
ATOM 575 CZ3 TRP A 97 15.232 41.389 51.048 1.00 54.73 C
ANISOU 575 CZ3 TRP A 97 6841 7272 6679 -332 274 -89 C
ATOM 576 CH2 TRP A 97 15.535 42.241 49.975 1.00 55.56 C
ANISOU 576 CH2 TRP A 97 6938 7357 6815 -306 268 -91 C
ATOM 577 N HIS A 98 18.094 41.688 57.803 1.00 76.01 N
ANISOU 577 N HIS A 98 9635 10059 9185 -502 272 -108 N
ATOM 578 CA HIS A 98 18.732 41.337 59.081 1.00 80.08 C
ANISOU 578 CA HIS A 98 10173 10594 9658 -540 262 -100 C
ATOM 579 C HIS A 98 18.685 39.886 59.501 1.00 81.13 C
ANISOU 579 C HIS A 98 10313 10743 9768 -558 249 -71 C
ATOM 580 O HIS A 98 19.734 39.280 59.744 1.00 81.35 O
ANISOU 580 O HIS A 98 10352 10774 9781 -571 219 -42 O
ATOM 581 CB HIS A 98 18.214 42.245 60.201 1.00 86.77 C
ANISOU 581 CB HIS A 98 11032 11454 10482 -565 291 -137 C
ATOM 582 CG HIS A 98 18.590 41.784 61.598 1.00 91.31 C
ANISOU 582 CG HIS A 98 11631 12052 11008 -609 285 -131 C
ATOM 583 ND1 HIS A 98 19.841 41.894 62.089 1.00 91.12 N
ANISOU 583 ND1 HIS A 98 11624 12031 10965 -626 260 -115 N
ATOM 584 CD2 HIS A 98 17.820 41.207 62.613 1.00 91.15 C
ANISOU 584 CD2 HIS A 98 11623 12054 10955 -640 303 -138 C
ATOM 585 CE1 HIS A 98 19.874 41.408 63.346 1.00 93.42 C
ANISOU 585 CE1 HIS A 98 11937 12345 11212 -666 259 -112 C
ATOM 586 NE2 HIS A 98 18.635 40.990 63.665 1.00 93.82 N
ANISOU 586 NE2 HIS A 98 11985 12407 11253 -675 286 -126 N
ATOM 587 N GLY A 99 17.489 39.307 59.587 1.00 78.05 N
ANISOU 587 N GLY A 99 9917 10360 9376 -560 269 -78 N
ATOM 588 CA GLY A 99 17.333 37.983 60.197 1.00 78.14 C
ANISOU 588 CA GLY A 99 9938 10390 9361 -584 259 -54 C
ATOM 589 C GLY A 99 17.648 36.763 59.348 1.00 80.40 C
ANISOU 589 C GLY A 99 10214 10668 9664 -566 233 -17 C
ATOM 590 O GLY A 99 17.578 35.634 59.839 1.00 85.39 O
ANISOU 590 O GLY A 99 10854 11314 10277 -586 222 4 O
ATOM 591 N LEU A 100 18.019 36.984 58.089 1.00 79.23 N
ANISOU 591 N LEU A 100 10050 10499 9552 -531 221 -9 N
ATOM 592 CA LEU A 100 18.073 35.916 57.084 1.00 76.31 C
ANISOU 592 CA LEU A 100 9667 10120 9206 -509 203 18 C
ATOM 593 C LEU A 100 19.430 35.212 56.955 1.00 75.00 C
ANISOU 593 C LEU A 100 9507 9951 9038 -512 166 54 C
ATOM 594 O LEU A 100 20.190 35.469 56.023 1.00 72.52 O
ANISOU 594 O LEU A 100 9184 9619 8750 -488 152 63 O
ATOM 595 CB LEU A 100 17.610 36.460 55.731 1.00 74.37 C
ANISOU 595 CB LEU A 100 9401 9854 9001 -470 213 7 C
ATOM 596 CG LEU A 100 16.182 37.012 55.695 1.00 74.84 C
ANISOU 596 CG LEU A 100 9450 9913 9070 -463 247 -24 C
ATOM 597 CD1 LEU A 100 16.033 38.127 54.673 1.00 74.44 C
ANISOU 597 CD1 LEU A 100 9386 9842 9055 -432 256 -43 C
ATOM 598 CD2 LEU A 100 15.194 35.896 55.418 1.00 76.00 C
ANISOU 598 CD2 LEU A 100 9588 10065 9223 -458 252 -14 C
ATOM 599 N HIS A 101 19.712 34.312 57.894 1.00 79.00 N
ANISOU 599 N HIS A 101 10026 10473 9515 -542 152 73 N
ATOM 600 CA HIS A 101 20.966 33.557 57.921 1.00 81.45 C
ANISOU 600 CA HIS A 101 10342 10781 9825 -549 116 108 C
ATOM 601 C HIS A 101 21.166 32.748 56.673 1.00 79.79 C
ANISOU 601 C HIS A 101 10114 10554 9648 -520 100 131 C
ATOM 602 O HIS A 101 22.255 32.745 56.102 1.00 78.24 O
ANISOU 602 O HIS A 101 9914 10344 9470 -507 78 147 O
ATOM 603 CB HIS A 101 21.002 32.585 59.105 1.00 91.18 C
ANISOU 603 CB HIS A 101 11590 12032 11021 -587 103 127 C
ATOM 604 CG HIS A 101 20.965 33.243 60.467 1.00 98.91 C
ANISOU 604 CG HIS A 101 12591 13029 11960 -623 115 109 C
ATOM 605 ND1 HIS A 101 21.990 33.154 61.339 1.00101.88 N
ANISOU 605 ND1 HIS A 101 12984 13412 12311 -652 90 125 N
ATOM 606 CD2 HIS A 101 19.967 33.979 61.106 1.00101.42 C
ANISOU 606 CD2 HIS A 101 12915 13359 12259 -636 149 75 C
ATOM 607 CE1 HIS A 101 21.674 33.813 62.470 1.00104.56 C
ANISOU 607 CE1 HIS A 101 13343 13769 12616 -682 108 102 C
ATOM 608 NE2 HIS A 101 20.437 34.318 62.326 1.00107.24 N
ANISOU 608 NE2 HIS A 101 13675 14112 12959 -673 145 71 N
ATOM 609 N HIS A 102 20.113 32.050 56.243 1.00 78.88 N
ANISOU 609 N HIS A 102 9987 10440 9542 -509 112 131 N
ATOM 610 CA HIS A 102 20.263 30.934 55.304 1.00 75.10 C
ANISOU 610 CA HIS A 102 9495 9950 9087 -489 94 157 C
ATOM 611 C HIS A 102 19.890 31.208 53.872 1.00 68.20 C
ANISOU 611 C HIS A 102 8603 9058 8250 -451 103 149 C
ATOM 612 O HIS A 102 20.172 30.380 52.999 1.00 66.69 O
ANISOU 612 O HIS A 102 8400 8856 8080 -434 88 170 O
ATOM 613 CB HIS A 102 19.529 29.695 55.825 1.00 78.44 C
ANISOU 613 CB HIS A 102 9919 10387 9495 -507 94 172 C
ATOM 614 CG HIS A 102 20.081 29.162 57.129 1.00 84.18 C
ANISOU 614 CG HIS A 102 10665 11131 10188 -545 76 189 C
ATOM 615 ND1 HIS A 102 21.332 28.672 57.241 1.00 85.76 N
ANISOU 615 ND1 HIS A 102 10868 11325 10389 -553 43 217 N
ATOM 616 CD2 HIS A 102 19.503 29.058 58.395 1.00 84.80 C
ANISOU 616 CD2 HIS A 102 10759 11230 10229 -580 87 182 C
ATOM 617 CE1 HIS A 102 21.547 28.278 58.512 1.00 86.56 C
ANISOU 617 CE1 HIS A 102 10988 11443 10457 -591 32 229 C
ATOM 618 NE2 HIS A 102 20.426 28.514 59.217 1.00 86.22 N
ANISOU 618 NE2 HIS A 102 10952 11417 10387 -608 60 207 N
ATOM 619 N LEU A 103 19.275 32.365 53.614 1.00 59.72 N
ANISOU 619 N LEU A 103 7526 7981 7184 -439 128 119 N
ATOM 620 CA LEU A 103 18.824 32.742 52.267 1.00 54.96 C
ANISOU 620 CA LEU A 103 6907 7360 6615 -404 137 110 C
ATOM 621 C LEU A 103 19.891 32.510 51.184 1.00 53.56 C
ANISOU 621 C LEU A 103 6721 7165 6462 -382 114 130 C
ATOM 622 O LEU A 103 21.012 33.011 51.277 1.00 50.58 O
ANISOU 622 O LEU A 103 6350 6782 6084 -385 101 135 O
ATOM 623 CB LEU A 103 18.350 34.197 52.248 1.00 52.07 C
ANISOU 623 CB LEU A 103 6540 6990 6254 -396 161 77 C
ATOM 624 CG LEU A 103 17.575 34.692 51.024 1.00 52.68 C
ANISOU 624 CG LEU A 103 6601 7051 6364 -364 175 63 C
ATOM 625 CD1 LEU A 103 16.143 34.176 51.015 1.00 52.99 C
ANISOU 625 CD1 LEU A 103 6631 7095 6405 -362 193 54 C
ATOM 626 CD2 LEU A 103 17.583 36.213 50.964 1.00 51.59 C
ANISOU 626 CD2 LEU A 103 6463 6904 6233 -357 189 36 C
ATOM 627 N SER A 104 19.537 31.732 50.169 1.00 51.18 N
ANISOU 627 N SER A 104 6408 6855 6183 -361 110 142 N
ATOM 628 CA SER A 104 20.456 31.482 49.065 1.00 51.97 C
ANISOU 628 CA SER A 104 6499 6937 6307 -341 92 159 C
ATOM 629 C SER A 104 20.041 32.216 47.789 1.00 49.25 C
ANISOU 629 C SER A 104 6144 6577 5989 -311 104 145 C
ATOM 630 O SER A 104 20.876 32.476 46.919 1.00 48.91 O
ANISOU 630 O SER A 104 6097 6519 5965 -294 94 151 O
ATOM 631 CB SER A 104 20.606 29.980 48.808 1.00 53.85 C
ANISOU 631 CB SER A 104 6732 7175 6551 -341 74 186 C
ATOM 632 OG SER A 104 19.344 29.370 48.607 1.00 55.56 O
ANISOU 632 OG SER A 104 6942 7397 6771 -336 87 183 O
ATOM 633 N ASN A 105 18.758 32.562 47.703 1.00 45.91 N
ANISOU 633 N ASN A 105 5717 6157 5570 -304 125 125 N
ATOM 634 CA ASN A 105 18.187 33.165 46.511 1.00 46.10 C
ANISOU 634 CA ASN A 105 5730 6165 5620 -277 135 113 C
ATOM 635 C ASN A 105 17.358 34.415 46.789 1.00 46.63 C
ANISOU 635 C ASN A 105 5796 6232 5687 -276 158 83 C
ATOM 636 O ASN A 105 16.426 34.380 47.585 1.00 50.00 O
ANISOU 636 O ASN A 105 6224 6670 6101 -289 174 70 O
ATOM 637 CB ASN A 105 17.348 32.132 45.756 1.00 47.44 C
ANISOU 637 CB ASN A 105 5889 6332 5803 -264 135 123 C
ATOM 638 CG ASN A 105 18.195 31.220 44.885 1.00 49.42 C
ANISOU 638 CG ASN A 105 6135 6573 6066 -253 114 148 C
ATOM 639 OD1 ASN A 105 18.251 31.387 43.666 1.00 49.32 O
ANISOU 639 OD1 ASN A 105 6117 6546 6076 -231 112 148 O
ATOM 640 ND2 ASN A 105 18.876 30.264 45.507 1.00 49.11 N
ANISOU 640 ND2 ASN A 105 6101 6542 6015 -269 99 167 N
ATOM 641 N LEU A 106 17.701 35.516 46.124 1.00 44.99 N
ANISOU 641 N LEU A 106 5586 6010 5495 -261 160 72 N
ATOM 642 CA LEU A 106 16.960 36.766 46.254 1.00 43.20 C
ANISOU 642 CA LEU A 106 5358 5780 5276 -257 180 44 C
ATOM 643 C LEU A 106 16.642 37.360 44.879 1.00 43.20 C
ANISOU 643 C LEU A 106 5347 5760 5307 -229 181 39 C
ATOM 644 O LEU A 106 17.544 37.623 44.082 1.00 42.88 O
ANISOU 644 O LEU A 106 5307 5707 5278 -217 168 49 O
ATOM 645 CB LEU A 106 17.746 37.764 47.109 1.00 43.06 C
ANISOU 645 CB LEU A 106 5350 5766 5243 -272 182 32 C
ATOM 646 CG LEU A 106 17.158 39.166 47.304 1.00 42.84 C
ANISOU 646 CG LEU A 106 5321 5733 5224 -269 202 1 C
ATOM 647 CD1 LEU A 106 15.886 39.131 48.143 1.00 41.44 C
ANISOU 647 CD1 LEU A 106 5141 5567 5037 -282 224 -18 C
ATOM 648 CD2 LEU A 106 18.203 40.076 47.929 1.00 42.48 C
ANISOU 648 CD2 LEU A 106 5285 5688 5166 -281 197 -5 C
ATOM 649 N ILE A 107 15.359 37.574 44.606 1.00 42.53 N
ANISOU 649 N ILE A 107 5252 5671 5236 -219 196 24 N
ATOM 650 CA ILE A 107 14.942 38.021 43.281 1.00 44.64 C
ANISOU 650 CA ILE A 107 5509 5919 5532 -194 195 22 C
ATOM 651 C ILE A 107 14.338 39.424 43.357 1.00 45.38 C
ANISOU 651 C ILE A 107 5598 6004 5641 -189 211 -5 C
ATOM 652 O ILE A 107 13.316 39.622 44.010 1.00 47.30 O
ANISOU 652 O ILE A 107 5836 6252 5883 -196 229 -24 O
ATOM 653 CB ILE A 107 13.987 37.001 42.614 1.00 43.74 C
ANISOU 653 CB ILE A 107 5386 5803 5429 -184 194 31 C
ATOM 654 CG1 ILE A 107 14.642 35.619 42.588 1.00 43.74 C
ANISOU 654 CG1 ILE A 107 5390 5811 5416 -190 178 58 C
ATOM 655 CG2 ILE A 107 13.632 37.434 41.196 1.00 42.85 C
ANISOU 655 CG2 ILE A 107 5264 5670 5345 -159 190 32 C
ATOM 656 CD1 ILE A 107 13.661 34.471 42.505 1.00 47.36 C
ANISOU 656 CD1 ILE A 107 5842 6276 5877 -189 181 65 C
ATOM 657 N LEU A 108 14.984 40.382 42.686 1.00 44.29 N
ANISOU 657 N LEU A 108 5460 5851 5517 -177 204 -6 N
ATOM 658 CA LEU A 108 14.647 41.808 42.798 1.00 44.56 C
ANISOU 658 CA LEU A 108 5490 5875 5565 -174 216 -31 C
ATOM 659 C LEU A 108 14.241 42.442 41.470 1.00 45.42 C
ANISOU 659 C LEU A 108 5590 5962 5706 -150 212 -32 C
ATOM 660 O LEU A 108 14.003 43.650 41.390 1.00 44.98 O
ANISOU 660 O LEU A 108 5529 5894 5667 -145 219 -50 O
ATOM 661 CB LEU A 108 15.821 42.587 43.398 1.00 44.23 C
ANISOU 661 CB LEU A 108 5458 5835 5510 -184 213 -35 C
ATOM 662 CG LEU A 108 16.163 42.284 44.857 1.00 45.63 C
ANISOU 662 CG LEU A 108 5646 6033 5655 -211 219 -40 C
ATOM 663 CD1 LEU A 108 17.513 42.882 45.230 1.00 43.32 C
ANISOU 663 CD1 LEU A 108 5365 5741 5351 -219 209 -37 C
ATOM 664 CD2 LEU A 108 15.058 42.781 45.781 1.00 44.54 C
ANISOU 664 CD2 LEU A 108 5505 5901 5515 -222 243 -68 C
ATOM 665 N THR A 109 14.169 41.614 40.434 1.00 46.05 N
ANISOU 665 N THR A 109 5666 6036 5793 -137 199 -12 N
ATOM 666 CA THR A 109 13.786 42.033 39.094 1.00 43.62 C
ANISOU 666 CA THR A 109 5351 5709 5513 -117 192 -9 C
ATOM 667 C THR A 109 12.720 43.113 39.113 1.00 45.72 C
ANISOU 667 C THR A 109 5606 5963 5803 -111 205 -33 C
ATOM 668 O THR A 109 11.724 42.991 39.833 1.00 49.01 O
ANISOU 668 O THR A 109 6015 6384 6219 -117 220 -48 O
ATOM 669 CB THR A 109 13.230 40.831 38.330 1.00 41.94 C
ANISOU 669 CB THR A 109 5134 5496 5305 -109 185 7 C
ATOM 670 OG1 THR A 109 14.081 39.703 38.560 1.00 41.24 O
ANISOU 670 OG1 THR A 109 5054 5420 5194 -117 176 26 O
ATOM 671 CG2 THR A 109 13.113 41.119 36.840 1.00 40.82 C
ANISOU 671 CG2 THR A 109 4988 5334 5185 -89 173 16 C
ATOM 672 N GLY A 110 12.940 44.177 38.345 1.00 45.60 N
ANISOU 672 N GLY A 110 5588 5928 5807 -99 199 -36 N
ATOM 673 CA GLY A 110 11.882 45.146 38.052 1.00 46.91 C
ANISOU 673 CA GLY A 110 5741 6078 6003 -89 206 -54 C
ATOM 674 C GLY A 110 11.515 46.149 39.134 1.00 48.53 C
ANISOU 674 C GLY A 110 5942 6284 6213 -98 224 -83 C
ATOM 675 O GLY A 110 10.553 46.898 38.976 1.00 50.70 O
ANISOU 675 O GLY A 110 6203 6544 6515 -90 232 -100 O
ATOM 676 N ASN A 111 12.269 46.162 40.230 1.00 48.72 N
ANISOU 676 N ASN A 111 5976 6324 6211 -115 232 -89 N
ATOM 677 CA ASN A 111 12.125 47.185 41.266 1.00 48.80 C
ANISOU 677 CA ASN A 111 5984 6335 6221 -126 249 -117 C
ATOM 678 C ASN A 111 13.024 48.387 40.969 1.00 47.97 C
ANISOU 678 C ASN A 111 5882 6217 6126 -121 241 -120 C
ATOM 679 O ASN A 111 14.232 48.220 40.801 1.00 48.38 O
ANISOU 679 O ASN A 111 5947 6274 6162 -123 227 -103 O
ATOM 680 CB ASN A 111 12.489 46.606 42.636 1.00 50.33 C
ANISOU 680 CB ASN A 111 6189 6554 6380 -149 260 -122 C
ATOM 681 CG ASN A 111 11.531 45.520 43.092 1.00 50.03 C
ANISOU 681 CG ASN A 111 6146 6529 6333 -156 270 -122 C
ATOM 682 OD1 ASN A 111 11.893 44.350 43.177 1.00 49.18 O
ANISOU 682 OD1 ASN A 111 6047 6435 6203 -162 262 -102 O
ATOM 683 ND2 ASN A 111 10.304 45.907 43.395 1.00 51.35 N
ANISOU 683 ND2 ASN A 111 6300 6691 6518 -155 289 -146 N
ATOM 684 N PRO A 112 12.452 49.604 40.906 1.00 47.29 N
ANISOU 684 N PRO A 112 5785 6114 6068 -114 249 -142 N
ATOM 685 CA PRO A 112 13.296 50.768 40.598 1.00 47.23 C
ANISOU 685 CA PRO A 112 5780 6093 6070 -110 240 -145 C
ATOM 686 C PRO A 112 14.103 51.300 41.793 1.00 48.34 C
ANISOU 686 C PRO A 112 5931 6246 6189 -127 249 -160 C
ATOM 687 O PRO A 112 13.978 52.464 42.162 1.00 48.77 O
ANISOU 687 O PRO A 112 5980 6290 6259 -129 258 -183 O
ATOM 688 CB PRO A 112 12.293 51.806 40.083 1.00 46.70 C
ANISOU 688 CB PRO A 112 5697 6003 6044 -96 244 -162 C
ATOM 689 CG PRO A 112 11.000 51.437 40.721 1.00 47.17 C
ANISOU 689 CG PRO A 112 5744 6067 6109 -101 264 -181 C
ATOM 690 CD PRO A 112 11.022 49.954 40.984 1.00 47.18 C
ANISOU 690 CD PRO A 112 5753 6090 6080 -109 264 -164 C
ATOM 691 N ILE A 113 14.926 50.435 42.382 1.00 51.30 N
ANISOU 691 N ILE A 113 6320 6641 6530 -141 246 -146 N
ATOM 692 CA ILE A 113 15.880 50.805 43.431 1.00 51.39 C
ANISOU 692 CA ILE A 113 6343 6664 6517 -159 249 -154 C
ATOM 693 C ILE A 113 17.094 51.402 42.748 1.00 53.51 C
ANISOU 693 C ILE A 113 6618 6922 6791 -152 231 -140 C
ATOM 694 O ILE A 113 18.104 50.717 42.602 1.00 60.51 O
ANISOU 694 O ILE A 113 7514 7816 7658 -155 217 -117 O
ATOM 695 CB ILE A 113 16.382 49.552 44.179 1.00 50.38 C
ANISOU 695 CB ILE A 113 6228 6560 6352 -177 246 -140 C
ATOM 696 CG1 ILE A 113 15.210 48.639 44.556 1.00 50.99 C
ANISOU 696 CG1 ILE A 113 6300 6648 6424 -182 260 -144 C
ATOM 697 CG2 ILE A 113 17.254 49.939 45.375 1.00 50.29 C
ANISOU 697 CG2 ILE A 113 6231 6562 6315 -198 250 -150 C
ATOM 698 CD1 ILE A 113 15.600 47.191 44.755 1.00 51.18 C
ANISOU 698 CD1 ILE A 113 6333 6690 6420 -191 251 -120 C
ATOM 699 N GLN A 114 17.028 52.649 42.309 1.00 52.35 N
ANISOU 699 N GLN A 114 6464 6755 6671 -141 230 -153 N
ATOM 700 CA GLN A 114 18.085 53.114 41.414 1.00 56.81 C
ANISOU 700 CA GLN A 114 7033 7308 7243 -132 212 -135 C
ATOM 701 C GLN A 114 19.488 53.027 42.034 1.00 59.28 C
ANISOU 701 C GLN A 114 7360 7632 7530 -146 204 -126 C
ATOM 702 O GLN A 114 20.435 52.585 41.376 1.00 60.30 O
ANISOU 702 O GLN A 114 7495 7761 7652 -142 188 -102 O
ATOM 703 CB GLN A 114 17.798 54.503 40.859 1.00 59.74 C
ANISOU 703 CB GLN A 114 7394 7656 7649 -120 211 -149 C
ATOM 704 CG GLN A 114 18.374 54.713 39.468 1.00 57.75 C
ANISOU 704 CG GLN A 114 7142 7387 7411 -104 192 -126 C
ATOM 705 CD GLN A 114 18.358 56.165 39.040 1.00 60.12 C
ANISOU 705 CD GLN A 114 7435 7664 7741 -95 188 -137 C
ATOM 706 OE1 GLN A 114 17.379 56.888 39.263 1.00 59.73 O
ANISOU 706 OE1 GLN A 114 7374 7604 7716 -92 199 -160 O
ATOM 707 NE2 GLN A 114 19.451 56.606 38.424 1.00 61.31 N
ANISOU 707 NE2 GLN A 114 7593 7808 7894 -92 174 -122 N
ATOM 708 N SER A 115 19.610 53.425 43.298 1.00 58.10 N
ANISOU 708 N SER A 115 7216 7493 7364 -163 216 -147 N
ATOM 709 CA SER A 115 20.887 53.363 43.999 1.00 56.07 C
ANISOU 709 CA SER A 115 6973 7248 7083 -178 208 -140 C
ATOM 710 C SER A 115 20.886 52.318 45.091 1.00 54.69 C
ANISOU 710 C SER A 115 6807 7097 6874 -198 214 -138 C
ATOM 711 O SER A 115 19.892 52.130 45.786 1.00 53.58 O
ANISOU 711 O SER A 115 6664 6966 6728 -207 231 -156 O
ATOM 712 CB SER A 115 21.242 54.715 44.608 1.00 58.70 C
ANISOU 712 CB SER A 115 7307 7574 7421 -185 214 -163 C
ATOM 713 OG SER A 115 22.012 55.480 43.709 1.00 63.31 O
ANISOU 713 OG SER A 115 7889 8140 8023 -172 200 -153 O
ATOM 714 N PHE A 116 22.023 51.650 45.230 1.00 56.67 N
ANISOU 714 N PHE A 116 7069 7357 7104 -207 199 -116 N
ATOM 715 CA PHE A 116 22.250 50.700 46.301 1.00 60.99 C
ANISOU 715 CA PHE A 116 7627 7926 7619 -228 199 -111 C
ATOM 716 C PHE A 116 23.382 51.229 47.180 1.00 62.29 C
ANISOU 716 C PHE A 116 7803 8096 7765 -246 192 -114 C
ATOM 717 O PHE A 116 24.526 51.364 46.726 1.00 63.60 O
ANISOU 717 O PHE A 116 7973 8256 7936 -242 175 -97 O
ATOM 718 CB PHE A 116 22.614 49.328 45.726 1.00 61.61 C
ANISOU 718 CB PHE A 116 7707 8011 7690 -224 184 -80 C
ATOM 719 CG PHE A 116 21.477 48.635 45.029 1.00 61.67 C
ANISOU 719 CG PHE A 116 7704 8015 7709 -211 190 -76 C
ATOM 720 CD1 PHE A 116 21.166 48.931 43.701 1.00 61.10 C
ANISOU 720 CD1 PHE A 116 7622 7926 7665 -188 186 -70 C
ATOM 721 CD2 PHE A 116 20.725 47.671 45.692 1.00 62.34 C
ANISOU 721 CD2 PHE A 116 7790 8117 7777 -222 199 -77 C
ATOM 722 CE1 PHE A 116 20.122 48.287 43.055 1.00 60.69 C
ANISOU 722 CE1 PHE A 116 7562 7872 7625 -176 191 -66 C
ATOM 723 CE2 PHE A 116 19.677 47.022 45.048 1.00 64.23 C
ANISOU 723 CE2 PHE A 116 8020 8354 8028 -210 204 -73 C
ATOM 724 CZ PHE A 116 19.374 47.332 43.730 1.00 62.02 C
ANISOU 724 CZ PHE A 116 7730 8055 7777 -187 199 -68 C
ATOM 725 N SER A 117 23.058 51.537 48.432 1.00 61.81 N
ANISOU 725 N SER A 117 7749 8047 7685 -266 206 -136 N
ATOM 726 CA SER A 117 24.044 52.086 49.363 1.00 62.96 C
ANISOU 726 CA SER A 117 7908 8200 7813 -285 201 -142 C
ATOM 727 C SER A 117 24.830 50.967 50.063 1.00 63.10 C
ANISOU 727 C SER A 117 7939 8235 7799 -305 186 -120 C
ATOM 728 O SER A 117 24.332 49.844 50.183 1.00 59.88 O
ANISOU 728 O SER A 117 7532 7840 7380 -310 187 -109 O
ATOM 729 CB SER A 117 23.356 52.988 50.394 1.00 62.12 C
ANISOU 729 CB SER A 117 7804 8098 7700 -300 223 -178 C
ATOM 730 OG SER A 117 22.413 52.256 51.159 1.00 59.69 O
ANISOU 730 OG SER A 117 7498 7806 7372 -315 239 -187 O
ATOM 731 N PRO A 118 26.068 51.264 50.517 1.00 63.52 N
ANISOU 731 N PRO A 118 8003 8289 7841 -318 171 -113 N
ATOM 732 CA PRO A 118 26.812 50.284 51.313 1.00 63.53 C
ANISOU 732 CA PRO A 118 8017 8307 7814 -340 156 -93 C
ATOM 733 C PRO A 118 25.933 49.672 52.405 1.00 65.62 C
ANISOU 733 C PRO A 118 8290 8592 8049 -362 170 -104 C
ATOM 734 O PRO A 118 25.158 50.390 53.047 1.00 68.27 O
ANISOU 734 O PRO A 118 8626 8931 8379 -371 191 -134 O
ATOM 735 CB PRO A 118 27.943 51.117 51.945 1.00 61.40 C
ANISOU 735 CB PRO A 118 7758 8036 7535 -354 145 -97 C
ATOM 736 CG PRO A 118 27.784 52.519 51.437 1.00 59.70 C
ANISOU 736 CG PRO A 118 7534 7802 7345 -338 155 -119 C
ATOM 737 CD PRO A 118 26.876 52.467 50.248 1.00 61.46 C
ANISOU 737 CD PRO A 118 7741 8013 7596 -311 165 -120 C
ATOM 738 N GLY A 119 26.035 48.358 52.595 1.00 63.79 N
ANISOU 738 N GLY A 119 8062 8373 7801 -371 159 -81 N
ATOM 739 CA GLY A 119 25.230 47.663 53.603 1.00 63.51 C
ANISOU 739 CA GLY A 119 8034 8357 7736 -394 171 -88 C
ATOM 740 C GLY A 119 23.801 47.350 53.179 1.00 64.10 C
ANISOU 740 C GLY A 119 8098 8433 7823 -381 192 -99 C
ATOM 741 O GLY A 119 22.996 46.915 54.006 1.00 63.68 O
ANISOU 741 O GLY A 119 8049 8395 7748 -399 206 -109 O
ATOM 742 N SER A 120 23.492 47.570 51.896 1.00 64.52 N
ANISOU 742 N SER A 120 8135 8468 7909 -351 193 -96 N
ATOM 743 CA SER A 120 22.185 47.227 51.300 1.00 65.14 C
ANISOU 743 CA SER A 120 8201 8544 8004 -335 209 -103 C
ATOM 744 C SER A 120 21.879 45.734 51.386 1.00 64.98 C
ANISOU 744 C SER A 120 8181 8536 7968 -342 203 -81 C
ATOM 745 O SER A 120 20.721 45.338 51.527 1.00 65.76 O
ANISOU 745 O SER A 120 8275 8642 8066 -343 220 -91 O
ATOM 746 CB SER A 120 22.113 47.653 49.823 1.00 63.49 C
ANISOU 746 CB SER A 120 7977 8313 7832 -303 205 -98 C
ATOM 747 OG SER A 120 21.969 49.056 49.670 1.00 64.92 O
ANISOU 747 OG SER A 120 8153 8481 8032 -295 215 -122 O
ATOM 748 N PHE A 121 22.926 44.917 51.290 1.00 62.03 N
ANISOU 748 N PHE A 121 7814 8166 7587 -346 179 -52 N
ATOM 749 CA PHE A 121 22.797 43.468 51.292 1.00 58.25 C
ANISOU 749 CA PHE A 121 7336 7698 7098 -351 170 -28 C
ATOM 750 C PHE A 121 23.440 42.853 52.527 1.00 60.19 C
ANISOU 750 C PHE A 121 7597 7961 7309 -382 158 -16 C
ATOM 751 O PHE A 121 23.897 41.715 52.489 1.00 61.14 O
ANISOU 751 O PHE A 121 7719 8086 7423 -387 139 10 O
ATOM 752 CB PHE A 121 23.427 42.884 50.021 1.00 54.54 C
ANISOU 752 CB PHE A 121 6856 7214 6651 -328 151 -1 C
ATOM 753 CG PHE A 121 22.743 43.313 48.759 1.00 51.20 C
ANISOU 753 CG PHE A 121 6419 6775 6259 -299 160 -9 C
ATOM 754 CD1 PHE A 121 21.520 42.760 48.391 1.00 51.49 C
ANISOU 754 CD1 PHE A 121 6447 6812 6303 -290 172 -12 C
ATOM 755 CD2 PHE A 121 23.311 44.278 47.943 1.00 50.37 C
ANISOU 755 CD2 PHE A 121 6309 6651 6175 -282 156 -12 C
ATOM 756 CE1 PHE A 121 20.872 43.165 47.227 1.00 51.79 C
ANISOU 756 CE1 PHE A 121 6472 6834 6369 -265 179 -18 C
ATOM 757 CE2 PHE A 121 22.674 44.682 46.775 1.00 51.47 C
ANISOU 757 CE2 PHE A 121 6437 6776 6343 -257 163 -17 C
ATOM 758 CZ PHE A 121 21.451 44.128 46.416 1.00 50.51 C
ANISOU 758 CZ PHE A 121 6306 6655 6228 -249 174 -20 C
ATOM 759 N SER A 122 23.476 43.611 53.620 1.00 63.14 N
ANISOU 759 N SER A 122 7984 8345 7662 -405 167 -37 N
ATOM 760 CA SER A 122 24.098 43.151 54.860 1.00 62.56 C
ANISOU 760 CA SER A 122 7927 8288 7554 -437 155 -27 C
ATOM 761 C SER A 122 23.190 42.148 55.563 1.00 61.75 C
ANISOU 761 C SER A 122 7830 8204 7427 -456 164 -25 C
ATOM 762 O SER A 122 21.987 42.390 55.716 1.00 61.93 O
ANISOU 762 O SER A 122 7849 8232 7450 -456 191 -48 O
ATOM 763 CB SER A 122 24.413 44.342 55.771 1.00 65.58 C
ANISOU 763 CB SER A 122 8323 8674 7920 -456 163 -52 C
ATOM 764 OG SER A 122 24.978 43.922 57.002 1.00 66.25 O
ANISOU 764 OG SER A 122 8426 8776 7969 -490 151 -43 O
ATOM 765 N GLY A 123 23.766 41.020 55.972 1.00 59.97 N
ANISOU 765 N GLY A 123 7612 7988 7185 -473 142 3 N
ATOM 766 CA GLY A 123 23.008 39.956 56.631 1.00 61.44 C
ANISOU 766 CA GLY A 123 7804 8192 7348 -492 147 10 C
ATOM 767 C GLY A 123 22.893 38.679 55.811 1.00 63.99 C
ANISOU 767 C GLY A 123 8114 8510 7687 -476 134 38 C
ATOM 768 O GLY A 123 22.828 37.574 56.375 1.00 62.81 O
ANISOU 768 O GLY A 123 7971 8373 7518 -495 124 57 O
ATOM 769 N LEU A 124 22.862 38.829 54.483 1.00 61.40 N
ANISOU 769 N LEU A 124 7770 8164 7394 -442 134 40 N
ATOM 770 CA LEU A 124 22.781 37.691 53.560 1.00 58.51 C
ANISOU 770 CA LEU A 124 7391 7791 7046 -425 122 64 C
ATOM 771 C LEU A 124 24.091 36.912 53.500 1.00 58.63 C
ANISOU 771 C LEU A 124 7410 7803 7063 -430 90 97 C
ATOM 772 O LEU A 124 24.789 36.924 52.480 1.00 57.76 O
ANISOU 772 O LEU A 124 7289 7676 6979 -408 78 109 O
ATOM 773 CB LEU A 124 22.398 38.139 52.147 1.00 56.37 C
ANISOU 773 CB LEU A 124 7104 7501 6811 -389 131 57 C
ATOM 774 CG LEU A 124 20.994 38.620 51.780 1.00 55.33 C
ANISOU 774 CG LEU A 124 6963 7368 6692 -375 158 32 C
ATOM 775 CD1 LEU A 124 19.959 38.252 52.835 1.00 54.17 C
ANISOU 775 CD1 LEU A 124 6822 7240 6520 -398 176 19 C
ATOM 776 CD2 LEU A 124 21.005 40.112 51.511 1.00 53.32 C
ANISOU 776 CD2 LEU A 124 6705 7101 6451 -363 171 6 C
ATOM 777 N THR A 125 24.402 36.218 54.591 1.00 58.51 N
ANISOU 777 N THR A 125 7408 7803 7021 -460 77 111 N
ATOM 778 CA THR A 125 25.679 35.517 54.733 1.00 59.48 C
ANISOU 778 CA THR A 125 7533 7922 7143 -469 45 141 C
ATOM 779 C THR A 125 25.691 34.141 54.051 1.00 56.01 C
ANISOU 779 C THR A 125 7082 7477 6720 -458 30 168 C
ATOM 780 O THR A 125 26.661 33.384 54.176 1.00 53.50 O
ANISOU 780 O THR A 125 6764 7156 6405 -466 3 195 O
ATOM 781 CB THR A 125 26.088 35.396 56.220 1.00 60.96 C
ANISOU 781 CB THR A 125 7741 8127 7294 -508 33 147 C
ATOM 782 OG1 THR A 125 25.001 34.844 56.976 1.00 60.80 O
ANISOU 782 OG1 THR A 125 7727 8125 7248 -528 48 141 O
ATOM 783 CG2 THR A 125 26.445 36.773 56.788 1.00 61.93 C
ANISOU 783 CG2 THR A 125 7875 8250 7404 -518 42 123 C
ATOM 784 N SER A 126 24.615 33.833 53.329 1.00 54.45 N
ANISOU 784 N SER A 126 6874 7278 6536 -439 47 161 N
ATOM 785 CA SER A 126 24.487 32.552 52.632 1.00 55.99 C
ANISOU 785 CA SER A 126 7057 7468 6748 -427 36 184 C
ATOM 786 C SER A 126 24.101 32.688 51.166 1.00 53.45 C
ANISOU 786 C SER A 126 6719 7130 6459 -391 46 178 C
ATOM 787 O SER A 126 23.891 31.678 50.493 1.00 55.06 O
ANISOU 787 O SER A 126 6912 7329 6677 -380 40 193 O
ATOM 788 CB SER A 126 23.451 31.670 53.330 1.00 56.22 C
ANISOU 788 CB SER A 126 7089 7513 6755 -444 43 187 C
ATOM 789 OG SER A 126 23.916 31.252 54.593 1.00 58.19 O
ANISOU 789 OG SER A 126 7354 7777 6976 -478 28 200 O
ATOM 790 N LEU A 127 24.009 33.926 50.679 1.00 51.53 N
ANISOU 790 N LEU A 127 6474 6879 6226 -376 61 156 N
ATOM 791 CA LEU A 127 23.422 34.203 49.368 1.00 50.96 C
ANISOU 791 CA LEU A 127 6387 6792 6180 -345 74 146 C
ATOM 792 C LEU A 127 24.250 33.604 48.239 1.00 52.00 C
ANISOU 792 C LEU A 127 6509 6908 6338 -326 56 167 C
ATOM 793 O LEU A 127 25.442 33.886 48.109 1.00 52.37 O
ANISOU 793 O LEU A 127 6558 6947 6393 -326 42 176 O
ATOM 794 CB LEU A 127 23.217 35.710 49.162 1.00 49.58 C
ANISOU 794 CB LEU A 127 6214 6611 6012 -335 91 120 C
ATOM 795 CG LEU A 127 22.416 36.187 47.941 1.00 48.51 C
ANISOU 795 CG LEU A 127 6066 6462 5901 -306 106 106 C
ATOM 796 CD1 LEU A 127 20.921 35.966 48.118 1.00 49.22 C
ANISOU 796 CD1 LEU A 127 6152 6560 5987 -307 126 92 C
ATOM 797 CD2 LEU A 127 22.698 37.651 47.650 1.00 46.28 C
ANISOU 797 CD2 LEU A 127 5785 6170 5630 -297 114 87 C
ATOM 798 N GLU A 128 23.608 32.765 47.435 1.00 52.22 N
ANISOU 798 N GLU A 128 6528 6933 6381 -311 58 175 N
ATOM 799 CA GLU A 128 24.281 32.116 46.315 1.00 53.07 C
ANISOU 799 CA GLU A 128 6625 7026 6513 -293 44 193 C
ATOM 800 C GLU A 128 23.897 32.747 44.978 1.00 48.30 C
ANISOU 800 C GLU A 128 6012 6406 5930 -265 57 180 C
ATOM 801 O GLU A 128 24.683 32.714 44.034 1.00 46.46 O
ANISOU 801 O GLU A 128 5774 6160 5718 -251 48 189 O
ATOM 802 CB GLU A 128 23.972 30.618 46.290 1.00 57.54 C
ANISOU 802 CB GLU A 128 7186 7596 7080 -296 35 212 C
ATOM 803 CG GLU A 128 24.610 29.796 47.402 1.00 61.23 C
ANISOU 803 CG GLU A 128 7659 8072 7530 -322 16 231 C
ATOM 804 CD GLU A 128 24.129 28.355 47.385 1.00 65.70 C
ANISOU 804 CD GLU A 128 8219 8643 8098 -325 8 249 C
ATOM 805 OE1 GLU A 128 24.435 27.624 46.419 1.00 66.41 O
ANISOU 805 OE1 GLU A 128 8298 8720 8212 -309 0 262 O
ATOM 806 OE2 GLU A 128 23.431 27.951 48.336 1.00 71.36 O
ANISOU 806 OE2 GLU A 128 8943 9376 8794 -345 11 250 O
ATOM 807 N ASN A 129 22.691 33.310 44.908 1.00 44.95 N
ANISOU 807 N ASN A 129 5587 5985 5504 -259 76 161 N
ATOM 808 CA ASN A 129 22.168 33.888 43.672 1.00 43.98 C
ANISOU 808 CA ASN A 129 5457 5850 5404 -234 87 150 C
ATOM 809 C ASN A 129 21.439 35.218 43.879 1.00 42.55 C
ANISOU 809 C ASN A 129 5278 5668 5220 -232 105 124 C
ATOM 810 O ASN A 129 20.388 35.270 44.521 1.00 43.40 O
ANISOU 810 O ASN A 129 5386 5786 5318 -240 119 110 O
ATOM 811 CB ASN A 129 21.270 32.874 42.939 1.00 44.28 C
ANISOU 811 CB ASN A 129 5486 5885 5451 -222 89 157 C
ATOM 812 CG ASN A 129 20.541 33.475 41.739 1.00 45.97 C
ANISOU 812 CG ASN A 129 5693 6087 5685 -199 99 145 C
ATOM 813 OD1 ASN A 129 19.382 33.149 41.491 1.00 47.20 O
ANISOU 813 OD1 ASN A 129 5844 6244 5845 -193 108 140 O
ATOM 814 ND2 ASN A 129 21.212 34.354 40.990 1.00 47.05 N
ANISOU 814 ND2 ASN A 129 5830 6210 5834 -187 97 142 N
ATOM 815 N LEU A 130 22.006 36.286 43.322 1.00 39.81 N
ANISOU 815 N LEU A 130 4931 5309 4886 -221 105 116 N
ATOM 816 CA LEU A 130 21.387 37.599 43.368 1.00 39.23 C
ANISOU 816 CA LEU A 130 4857 5231 4815 -216 121 92 C
ATOM 817 C LEU A 130 20.858 38.013 41.993 1.00 40.08 C
ANISOU 817 C LEU A 130 4956 5322 4948 -192 126 87 C
ATOM 818 O LEU A 130 21.610 38.092 41.013 1.00 40.33 O
ANISOU 818 O LEU A 130 4986 5342 4994 -179 116 98 O
ATOM 819 CB LEU A 130 22.359 38.651 43.924 1.00 38.86 C
ANISOU 819 CB LEU A 130 4818 5183 4763 -225 119 84 C
ATOM 820 CG LEU A 130 21.846 40.085 44.143 1.00 37.71 C
ANISOU 820 CG LEU A 130 4672 5033 4620 -223 134 58 C
ATOM 821 CD1 LEU A 130 20.467 40.119 44.780 1.00 38.78 C
ANISOU 821 CD1 LEU A 130 4807 5179 4749 -230 153 39 C
ATOM 822 CD2 LEU A 130 22.814 40.886 44.987 1.00 37.32 C
ANISOU 822 CD2 LEU A 130 4633 4986 4558 -238 130 52 C
ATOM 823 N VAL A 131 19.560 38.287 41.936 1.00 38.43 N
ANISOU 823 N VAL A 131 4742 5114 4745 -186 140 72 N
ATOM 824 CA VAL A 131 18.922 38.658 40.695 1.00 38.59 C
ANISOU 824 CA VAL A 131 4754 5119 4789 -165 143 68 C
ATOM 825 C VAL A 131 18.429 40.093 40.825 1.00 40.85 C
ANISOU 825 C VAL A 131 5038 5397 5084 -161 156 44 C
ATOM 826 O VAL A 131 17.432 40.366 41.501 1.00 43.59 O
ANISOU 826 O VAL A 131 5382 5750 5428 -167 171 26 O
ATOM 827 CB VAL A 131 17.783 37.684 40.336 1.00 38.58 C
ANISOU 827 CB VAL A 131 4745 5119 4792 -159 147 72 C
ATOM 828 CG1 VAL A 131 17.043 38.140 39.086 1.00 38.39 C
ANISOU 828 CG1 VAL A 131 4714 5080 4793 -138 149 67 C
ATOM 829 CG2 VAL A 131 18.335 36.278 40.140 1.00 38.17 C
ANISOU 829 CG2 VAL A 131 4694 5072 4733 -161 133 96 C
ATOM 830 N ALA A 132 19.155 41.003 40.183 1.00 39.09 N
ANISOU 830 N ALA A 132 4817 5162 4873 -152 150 43 N
ATOM 831 CA ALA A 132 18.884 42.425 40.272 1.00 37.62 C
ANISOU 831 CA ALA A 132 4629 4966 4698 -148 160 22 C
ATOM 832 C ALA A 132 18.644 42.970 38.875 1.00 38.31 C
ANISOU 832 C ALA A 132 4710 5034 4810 -128 155 25 C
ATOM 833 O ALA A 132 19.200 43.999 38.470 1.00 37.81 O
ANISOU 833 O ALA A 132 4648 4959 4757 -122 152 21 O
ATOM 834 CB ALA A 132 20.037 43.137 40.950 1.00 37.48 C
ANISOU 834 CB ALA A 132 4620 4951 4670 -160 156 19 C
ATOM 835 N VAL A 133 17.797 42.248 38.149 1.00 38.66 N
ANISOU 835 N VAL A 133 4748 5075 4864 -118 155 31 N
ATOM 836 CA VAL A 133 17.414 42.581 36.787 1.00 37.92 C
ANISOU 836 CA VAL A 133 4650 4964 4793 -100 149 36 C
ATOM 837 C VAL A 133 16.461 43.758 36.815 1.00 38.07 C
ANISOU 837 C VAL A 133 4661 4972 4830 -94 159 14 C
ATOM 838 O VAL A 133 15.619 43.852 37.700 1.00 38.72 O
ANISOU 838 O VAL A 133 4738 5061 4911 -101 172 -1 O
ATOM 839 CB VAL A 133 16.775 41.352 36.092 1.00 37.22 C
ANISOU 839 CB VAL A 133 4557 4877 4706 -93 144 49 C
ATOM 840 CG1 VAL A 133 16.151 41.708 34.749 1.00 36.26 C
ANISOU 840 CG1 VAL A 133 4431 4737 4607 -76 139 52 C
ATOM 841 CG2 VAL A 133 17.820 40.259 35.920 1.00 37.01 C
ANISOU 841 CG2 VAL A 133 4537 4858 4666 -97 134 70 C
ATOM 842 N GLU A 134 16.616 44.658 35.850 1.00 39.47 N
ANISOU 842 N GLU A 134 4837 5132 5026 -82 152 15 N
ATOM 843 CA GLU A 134 15.780 45.854 35.736 1.00 43.30 C
ANISOU 843 CA GLU A 134 5313 5602 5534 -75 158 -2 C
ATOM 844 C GLU A 134 15.602 46.571 37.079 1.00 44.63 C
ANISOU 844 C GLU A 134 5480 5777 5698 -87 173 -26 C
ATOM 845 O GLU A 134 14.482 46.838 37.517 1.00 45.30 O
ANISOU 845 O GLU A 134 5555 5861 5794 -87 186 -44 O
ATOM 846 CB GLU A 134 14.429 45.539 35.085 1.00 43.80 C
ANISOU 846 CB GLU A 134 5366 5657 5616 -65 159 -3 C
ATOM 847 CG GLU A 134 13.819 46.737 34.368 1.00 47.14 C
ANISOU 847 CG GLU A 134 5782 6059 6070 -53 156 -12 C
ATOM 848 CD GLU A 134 12.341 46.572 34.042 1.00 51.76 C
ANISOU 848 CD GLU A 134 6354 6635 6676 -45 158 -19 C
ATOM 849 OE1 GLU A 134 11.739 47.539 33.526 1.00 55.08 O
ANISOU 849 OE1 GLU A 134 6766 7036 7124 -36 155 -27 O
ATOM 850 OE2 GLU A 134 11.767 45.490 34.300 1.00 54.37 O
ANISOU 850 OE2 GLU A 134 6682 6976 6997 -48 163 -15 O
ATOM 851 N THR A 135 16.723 46.863 37.728 1.00 43.66 N
ANISOU 851 N THR A 135 5367 5663 5559 -98 172 -27 N
ATOM 852 CA THR A 135 16.714 47.610 38.974 1.00 45.18 C
ANISOU 852 CA THR A 135 5560 5862 5745 -111 186 -49 C
ATOM 853 C THR A 135 17.228 49.037 38.738 1.00 46.63 C
ANISOU 853 C THR A 135 5743 6030 5944 -106 183 -59 C
ATOM 854 O THR A 135 17.368 49.826 39.678 1.00 46.53 O
ANISOU 854 O THR A 135 5731 6020 5927 -116 193 -78 O
ATOM 855 CB THR A 135 17.508 46.891 40.096 1.00 45.22 C
ANISOU 855 CB THR A 135 5575 5888 5717 -129 187 -45 C
ATOM 856 OG1 THR A 135 18.787 46.470 39.607 1.00 47.37 O
ANISOU 856 OG1 THR A 135 5856 6161 5981 -129 171 -22 O
ATOM 857 CG2 THR A 135 16.758 45.677 40.593 1.00 43.94 C
ANISOU 857 CG2 THR A 135 5411 5740 5541 -137 194 -42 C
ATOM 858 N LYS A 136 17.472 49.369 37.470 1.00 46.97 N
ANISOU 858 N LYS A 136 5784 6056 6004 -92 170 -46 N
ATOM 859 CA LYS A 136 18.001 50.681 37.071 1.00 46.37 C
ANISOU 859 CA LYS A 136 5708 5964 5945 -86 165 -51 C
ATOM 860 C LYS A 136 19.462 50.897 37.486 1.00 44.50 C
ANISOU 860 C LYS A 136 5482 5733 5690 -96 159 -45 C
ATOM 861 O LYS A 136 19.982 52.010 37.363 1.00 44.97 O
ANISOU 861 O LYS A 136 5543 5782 5761 -94 156 -51 O
ATOM 862 CB LYS A 136 17.128 51.835 37.590 1.00 48.41 C
ANISOU 862 CB LYS A 136 5956 6212 6224 -86 177 -79 C
ATOM 863 CG LYS A 136 15.798 52.027 36.884 1.00 51.27 C
ANISOU 863 CG LYS A 136 6305 6559 6615 -73 178 -84 C
ATOM 864 CD LYS A 136 15.133 53.327 37.322 1.00 54.21 C
ANISOU 864 CD LYS A 136 6666 6918 7013 -71 189 -111 C
ATOM 865 CE LYS A 136 13.732 53.485 36.744 1.00 56.50 C
ANISOU 865 CE LYS A 136 6940 7191 7333 -59 190 -118 C
ATOM 866 NZ LYS A 136 13.722 53.632 35.258 1.00 60.62 N
ANISOU 866 NZ LYS A 136 7461 7695 7875 -45 170 -97 N
ATOM 867 N LEU A 137 20.122 49.839 37.954 1.00 42.71 N
ANISOU 867 N LEU A 137 5264 5524 5438 -106 157 -32 N
ATOM 868 CA LEU A 137 21.549 49.895 38.307 1.00 44.45 C
ANISOU 868 CA LEU A 137 5494 5750 5643 -115 149 -23 C
ATOM 869 C LEU A 137 22.406 50.569 37.219 1.00 42.51 C
ANISOU 869 C LEU A 137 5250 5488 5412 -105 137 -11 C
ATOM 870 O LEU A 137 22.229 50.301 36.042 1.00 42.24 O
ANISOU 870 O LEU A 137 5214 5445 5389 -93 130 1 O
ATOM 871 CB LEU A 137 22.076 48.485 38.573 1.00 44.75 C
ANISOU 871 CB LEU A 137 5538 5804 5659 -123 144 -5 C
ATOM 872 CG LEU A 137 23.010 48.240 39.763 1.00 47.36 C
ANISOU 872 CG LEU A 137 5877 6149 5966 -141 143 -5 C
ATOM 873 CD1 LEU A 137 23.536 46.814 39.700 1.00 49.01 C
ANISOU 873 CD1 LEU A 137 6090 6370 6161 -146 133 17 C
ATOM 874 CD2 LEU A 137 24.172 49.215 39.836 1.00 47.88 C
ANISOU 874 CD2 LEU A 137 5948 6209 6035 -144 136 -6 C
ATOM 875 N ALA A 138 23.334 51.434 37.619 1.00 43.20 N
ANISOU 875 N ALA A 138 5342 5573 5498 -111 135 -17 N
ATOM 876 CA ALA A 138 24.168 52.170 36.655 1.00 45.17 C
ANISOU 876 CA ALA A 138 5593 5807 5762 -102 125 -7 C
ATOM 877 C ALA A 138 25.605 51.643 36.531 1.00 46.25 C
ANISOU 877 C ALA A 138 5737 5948 5886 -108 115 11 C
ATOM 878 O ALA A 138 26.263 51.863 35.502 1.00 45.12 O
ANISOU 878 O ALA A 138 5595 5794 5752 -100 107 25 O
ATOM 879 CB ALA A 138 24.174 53.660 36.976 1.00 43.17 C
ANISOU 879 CB ALA A 138 5336 5541 5523 -103 128 -25 C
ATOM 880 N SER A 139 26.077 50.947 37.569 1.00 47.59 N
ANISOU 880 N SER A 139 5911 6134 6035 -121 116 13 N
ATOM 881 CA SER A 139 27.475 50.506 37.649 1.00 48.98 C
ANISOU 881 CA SER A 139 6094 6315 6201 -128 106 29 C
ATOM 882 C SER A 139 27.690 49.313 38.595 1.00 48.89 C
ANISOU 882 C SER A 139 6085 6321 6167 -142 104 35 C
ATOM 883 O SER A 139 27.119 49.270 39.681 1.00 48.48 O
ANISOU 883 O SER A 139 6035 6280 6103 -153 111 22 O
ATOM 884 CB SER A 139 28.361 51.696 38.065 1.00 48.99 C
ANISOU 884 CB SER A 139 6098 6310 6207 -134 103 21 C
ATOM 885 OG SER A 139 29.367 51.333 39.001 1.00 50.51 O
ANISOU 885 OG SER A 139 6295 6512 6382 -149 97 26 O
ATOM 886 N LEU A 140 28.521 48.356 38.180 1.00 48.67 N
ANISOU 886 N LEU A 140 6059 6296 6137 -142 95 56 N
ATOM 887 CA LEU A 140 28.969 47.289 39.082 1.00 48.81 C
ANISOU 887 CA LEU A 140 6080 6328 6136 -157 89 65 C
ATOM 888 C LEU A 140 29.848 47.837 40.207 1.00 50.23 C
ANISOU 888 C LEU A 140 6266 6513 6306 -172 85 60 C
ATOM 889 O LEU A 140 29.669 47.471 41.367 1.00 50.78 O
ANISOU 889 O LEU A 140 6340 6597 6357 -188 85 55 O
ATOM 890 CB LEU A 140 29.741 46.201 38.325 1.00 47.48 C
ANISOU 890 CB LEU A 140 5909 6158 5971 -153 80 88 C
ATOM 891 CG LEU A 140 29.010 45.152 37.486 1.00 46.26 C
ANISOU 891 CG LEU A 140 5751 6005 5821 -143 82 97 C
ATOM 892 CD1 LEU A 140 30.010 44.331 36.693 1.00 45.66 C
ANISOU 892 CD1 LEU A 140 5673 5923 5751 -139 73 117 C
ATOM 893 CD2 LEU A 140 28.168 44.241 38.358 1.00 46.76 C
ANISOU 893 CD2 LEU A 140 5814 6082 5868 -151 85 95 C
ATOM 894 N GLU A 141 30.784 48.719 39.854 1.00 53.17 N
ANISOU 894 N GLU A 141 6638 6873 6689 -169 80 61 N
ATOM 895 CA GLU A 141 31.780 49.275 40.787 1.00 57.09 C
ANISOU 895 CA GLU A 141 7141 7372 7179 -184 73 58 C
ATOM 896 C GLU A 141 31.190 49.847 42.085 1.00 55.71 C
ANISOU 896 C GLU A 141 6971 7207 6988 -198 80 37 C
ATOM 897 O GLU A 141 31.814 49.763 43.144 1.00 51.58 O
ANISOU 897 O GLU A 141 6454 6692 6448 -215 73 37 O
ATOM 898 CB GLU A 141 32.641 50.331 40.081 1.00 61.54 C
ANISOU 898 CB GLU A 141 7703 7919 7760 -176 69 59 C
ATOM 899 CG GLU A 141 33.475 49.799 38.914 1.00 69.52 C
ANISOU 899 CG GLU A 141 8709 8920 8783 -166 62 79 C
ATOM 900 CD GLU A 141 34.958 49.637 39.246 1.00 76.47 C
ANISOU 900 CD GLU A 141 9590 9799 9664 -176 49 92 C
ATOM 901 OE1 GLU A 141 35.793 50.229 38.524 1.00 77.47 O
ANISOU 901 OE1 GLU A 141 9714 9913 9806 -170 46 97 O
ATOM 902 OE2 GLU A 141 35.297 48.927 40.222 1.00 78.99 O
ANISOU 902 OE2 GLU A 141 9912 10129 9970 -190 41 97 O
ATOM 903 N SER A 142 29.984 50.405 41.992 1.00 56.30 N
ANISOU 903 N SER A 142 7043 7280 7067 -191 94 18 N
ATOM 904 CA SER A 142 29.287 50.978 43.146 1.00 57.66 C
ANISOU 904 CA SER A 142 7219 7461 7227 -203 105 -4 C
ATOM 905 C SER A 142 28.193 50.064 43.737 1.00 57.24 C
ANISOU 905 C SER A 142 7166 7423 7158 -210 114 -9 C
ATOM 906 O SER A 142 27.424 50.481 44.612 1.00 58.01 O
ANISOU 906 O SER A 142 7266 7528 7246 -220 127 -30 O
ATOM 907 CB SER A 142 28.691 52.340 42.772 1.00 60.20 C
ANISOU 907 CB SER A 142 7535 7768 7567 -192 115 -25 C
ATOM 908 OG SER A 142 27.707 52.210 41.757 1.00 61.49 O
ANISOU 908 OG SER A 142 7691 7924 7748 -175 121 -24 O
ATOM 909 N PHE A 143 28.137 48.824 43.261 1.00 54.11 N
ANISOU 909 N PHE A 143 6768 7031 6759 -206 109 10 N
ATOM 910 CA PHE A 143 27.178 47.838 43.747 1.00 53.52 C
ANISOU 910 CA PHE A 143 6693 6971 6670 -213 116 9 C
ATOM 911 C PHE A 143 27.794 47.132 44.954 1.00 52.20 C
ANISOU 911 C PHE A 143 6535 6820 6477 -236 107 17 C
ATOM 912 O PHE A 143 28.871 46.549 44.829 1.00 54.92 O
ANISOU 912 O PHE A 143 6882 7164 6820 -239 91 37 O
ATOM 913 CB PHE A 143 26.861 46.843 42.619 1.00 53.30 C
ANISOU 913 CB PHE A 143 6658 6939 6653 -197 112 27 C
ATOM 914 CG PHE A 143 25.552 46.119 42.769 1.00 51.72 C
ANISOU 914 CG PHE A 143 6454 6747 6447 -197 123 22 C
ATOM 915 CD1 PHE A 143 24.415 46.765 43.250 1.00 52.49 C
ANISOU 915 CD1 PHE A 143 6550 6847 6545 -198 139 -1 C
ATOM 916 CD2 PHE A 143 25.444 44.792 42.375 1.00 51.72 C
ANISOU 916 CD2 PHE A 143 6452 6753 6445 -194 117 41 C
ATOM 917 CE1 PHE A 143 23.207 46.086 43.371 1.00 52.22 C
ANISOU 917 CE1 PHE A 143 6511 6821 6507 -198 150 -6 C
ATOM 918 CE2 PHE A 143 24.237 44.111 42.487 1.00 51.98 C
ANISOU 918 CE2 PHE A 143 6481 6793 6473 -193 126 37 C
ATOM 919 CZ PHE A 143 23.116 44.759 42.986 1.00 51.52 C
ANISOU 919 CZ PHE A 143 6420 6737 6414 -195 143 13 C
ATOM 920 N PRO A 144 27.121 47.185 46.126 1.00 51.16 N
ANISOU 920 N PRO A 144 6410 6703 6326 -253 118 0 N
ATOM 921 CA PRO A 144 27.670 46.714 47.403 1.00 50.14 C
ANISOU 921 CA PRO A 144 6292 6589 6169 -279 110 5 C
ATOM 922 C PRO A 144 27.528 45.204 47.629 1.00 50.24 C
ANISOU 922 C PRO A 144 6305 6614 6167 -287 103 25 C
ATOM 923 O PRO A 144 26.897 44.777 48.600 1.00 50.18 O
ANISOU 923 O PRO A 144 6304 6622 6137 -304 110 18 O
ATOM 924 CB PRO A 144 26.828 47.474 48.422 1.00 51.39 C
ANISOU 924 CB PRO A 144 6455 6756 6313 -292 129 -23 C
ATOM 925 CG PRO A 144 25.487 47.554 47.771 1.00 51.18 C
ANISOU 925 CG PRO A 144 6418 6724 6302 -275 146 -36 C
ATOM 926 CD PRO A 144 25.758 47.724 46.298 1.00 51.92 C
ANISOU 926 CD PRO A 144 6501 6799 6424 -250 139 -24 C
ATOM 927 N ILE A 145 28.123 44.410 46.742 1.00 49.57 N
ANISOU 927 N ILE A 145 6215 6522 6096 -275 89 49 N
ATOM 928 CA ILE A 145 28.068 42.948 46.846 1.00 49.03 C
ANISOU 928 CA ILE A 145 6146 6463 6019 -281 80 69 C
ATOM 929 C ILE A 145 29.425 42.330 47.223 1.00 49.26 C
ANISOU 929 C ILE A 145 6179 6493 6043 -294 57 92 C
ATOM 930 O ILE A 145 29.535 41.110 47.404 1.00 47.55 O
ANISOU 930 O ILE A 145 5962 6284 5820 -301 46 111 O
ATOM 931 CB ILE A 145 27.470 42.295 45.569 1.00 48.96 C
ANISOU 931 CB ILE A 145 6126 6446 6030 -258 83 78 C
ATOM 932 CG1 ILE A 145 28.343 42.572 44.335 1.00 49.50 C
ANISOU 932 CG1 ILE A 145 6188 6497 6123 -240 75 89 C
ATOM 933 CG2 ILE A 145 26.045 42.786 45.347 1.00 47.42 C
ANISOU 933 CG2 ILE A 145 5926 6250 5839 -249 104 57 C
ATOM 934 CD1 ILE A 145 28.070 41.675 43.146 1.00 47.78 C
ANISOU 934 CD1 ILE A 145 5961 6272 5920 -222 73 103 C
ATOM 935 N GLY A 146 30.440 43.188 47.363 1.00 49.68 N
ANISOU 935 N GLY A 146 6236 6539 6100 -297 49 90 N
ATOM 936 CA GLY A 146 31.803 42.772 47.696 1.00 49.78 C
ANISOU 936 CA GLY A 146 6251 6549 6111 -309 26 111 C
ATOM 937 C GLY A 146 31.934 42.017 49.008 1.00 51.08 C
ANISOU 937 C GLY A 146 6426 6730 6250 -336 15 120 C
ATOM 938 O GLY A 146 32.980 41.432 49.281 1.00 47.79 O
ANISOU 938 O GLY A 146 6011 6313 5835 -347 -6 140 O
ATOM 939 N GLN A 147 30.870 42.036 49.812 1.00 55.88 N
ANISOU 939 N GLN A 147 7042 7354 6836 -349 29 104 N
ATOM 940 CA GLN A 147 30.825 41.338 51.097 1.00 62.10 C
ANISOU 940 CA GLN A 147 7841 8158 7593 -378 20 112 C
ATOM 941 C GLN A 147 30.288 39.906 50.926 1.00 64.06 C
ANISOU 941 C GLN A 147 8084 8414 7841 -378 16 129 C
ATOM 942 O GLN A 147 30.635 39.014 51.697 1.00 65.30 O
ANISOU 942 O GLN A 147 8248 8580 7982 -398 0 147 O
ATOM 943 CB GLN A 147 29.939 42.106 52.097 1.00 68.62 C
ANISOU 943 CB GLN A 147 8678 8998 8394 -395 39 84 C
ATOM 944 CG GLN A 147 30.158 41.733 53.568 1.00 76.53 C
ANISOU 944 CG GLN A 147 9697 10018 9362 -430 29 89 C
ATOM 945 CD GLN A 147 28.885 41.279 54.308 1.00 81.65 C
ANISOU 945 CD GLN A 147 10352 10685 9985 -445 47 77 C
ATOM 946 OE1 GLN A 147 27.849 40.986 53.692 1.00 80.05 O
ANISOU 946 OE1 GLN A 147 10139 10482 9792 -429 63 71 O
ATOM 947 NE2 GLN A 147 28.973 41.197 55.640 1.00 75.12 N
ANISOU 947 NE2 GLN A 147 9541 9874 9124 -478 42 76 N
ATOM 948 N LEU A 148 29.449 39.700 49.913 1.00 62.10 N
ANISOU 948 N LEU A 148 7825 8160 7609 -355 30 125 N
ATOM 949 CA LEU A 148 28.699 38.450 49.735 1.00 59.38 C
ANISOU 949 CA LEU A 148 7475 7822 7263 -353 31 137 C
ATOM 950 C LEU A 148 29.558 37.300 49.194 1.00 57.53 C
ANISOU 950 C LEU A 148 7233 7579 7045 -348 9 166 C
ATOM 951 O LEU A 148 29.419 36.903 48.038 1.00 55.40 O
ANISOU 951 O LEU A 148 6951 7298 6797 -326 12 172 O
ATOM 952 CB LEU A 148 27.497 38.700 48.814 1.00 57.53 C
ANISOU 952 CB LEU A 148 7231 7583 7043 -330 53 121 C
ATOM 953 CG LEU A 148 26.278 39.488 49.313 1.00 58.33 C
ANISOU 953 CG LEU A 148 7337 7693 7132 -334 78 93 C
ATOM 954 CD1 LEU A 148 26.631 40.558 50.336 1.00 62.12 C
ANISOU 954 CD1 LEU A 148 7829 8179 7595 -352 82 75 C
ATOM 955 CD2 LEU A 148 25.549 40.117 48.132 1.00 59.05 C
ANISOU 955 CD2 LEU A 148 7417 7770 7248 -306 94 79 C
ATOM 956 N ILE A 149 30.420 36.756 50.050 1.00 56.57 N
ANISOU 956 N ILE A 149 7118 7464 6912 -370 -11 184 N
ATOM 957 CA ILE A 149 31.454 35.801 49.638 1.00 56.91 C
ANISOU 957 CA ILE A 149 7153 7496 6974 -367 -35 211 C
ATOM 958 C ILE A 149 30.891 34.465 49.130 1.00 57.03 C
ANISOU 958 C ILE A 149 7158 7512 6997 -359 -36 226 C
ATOM 959 O ILE A 149 31.543 33.756 48.357 1.00 57.67 O
ANISOU 959 O ILE A 149 7228 7581 7103 -347 -49 243 O
ATOM 960 CB ILE A 149 32.502 35.592 50.757 1.00 58.67 C
ANISOU 960 CB ILE A 149 7384 7723 7183 -394 -60 227 C
ATOM 961 CG1 ILE A 149 33.088 36.947 51.189 1.00 59.78 C
ANISOU 961 CG1 ILE A 149 7533 7861 7316 -401 -58 212 C
ATOM 962 CG2 ILE A 149 33.627 34.680 50.283 1.00 59.94 C
ANISOU 962 CG2 ILE A 149 7534 7870 7369 -390 -84 254 C
ATOM 963 CD1 ILE A 149 33.800 36.946 52.530 1.00 61.60 C
ANISOU 963 CD1 ILE A 149 7779 8102 7525 -432 -78 221 C
ATOM 964 N THR A 150 29.671 34.140 49.543 1.00 56.83 N
ANISOU 964 N THR A 150 7137 7501 6954 -365 -23 218 N
ATOM 965 CA THR A 150 29.005 32.918 49.093 1.00 55.36 C
ANISOU 965 CA THR A 150 6942 7316 6775 -358 -23 230 C
ATOM 966 C THR A 150 28.414 33.035 47.685 1.00 53.98 C
ANISOU 966 C THR A 150 6755 7129 6623 -328 -7 221 C
ATOM 967 O THR A 150 28.008 32.030 47.097 1.00 56.08 O
ANISOU 967 O THR A 150 7013 7393 6900 -318 -8 231 O
ATOM 968 CB THR A 150 27.877 32.492 50.059 1.00 56.68 C
ANISOU 968 CB THR A 150 7118 7502 6913 -377 -14 225 C
ATOM 969 OG1 THR A 150 27.025 33.613 50.337 1.00 56.82 O
ANISOU 969 OG1 THR A 150 7143 7527 6918 -377 10 197 O
ATOM 970 CG2 THR A 150 28.450 31.932 51.357 1.00 57.13 C
ANISOU 970 CG2 THR A 150 7187 7571 6948 -409 -34 242 C
ATOM 971 N LEU A 151 28.372 34.256 47.153 1.00 51.43 N
ANISOU 971 N LEU A 151 6433 6799 6308 -313 6 202 N
ATOM 972 CA LEU A 151 27.701 34.549 45.887 1.00 47.54 C
ANISOU 972 CA LEU A 151 5931 6297 5835 -287 22 191 C
ATOM 973 C LEU A 151 28.281 33.753 44.738 1.00 47.48 C
ANISOU 973 C LEU A 151 5911 6274 5852 -270 12 208 C
ATOM 974 O LEU A 151 29.499 33.588 44.637 1.00 48.91 O
ANISOU 974 O LEU A 151 6090 6447 6044 -272 -3 222 O
ATOM 975 CB LEU A 151 27.775 36.041 45.572 1.00 46.31 C
ANISOU 975 CB LEU A 151 5778 6134 5684 -277 34 171 C
ATOM 976 CG LEU A 151 26.861 36.588 44.476 1.00 45.79 C
ANISOU 976 CG LEU A 151 5704 6058 5632 -254 51 156 C
ATOM 977 CD1 LEU A 151 25.384 36.475 44.846 1.00 45.19 C
ANISOU 977 CD1 LEU A 151 5629 5994 5545 -256 68 142 C
ATOM 978 CD2 LEU A 151 27.237 38.024 44.158 1.00 43.86 C
ANISOU 978 CD2 LEU A 151 5462 5804 5396 -246 58 140 C
ATOM 979 N LYS A 152 27.393 33.264 43.878 1.00 47.94 N
ANISOU 979 N LYS A 152 5963 6331 5921 -254 21 207 N
ATOM 980 CA LYS A 152 27.770 32.400 42.766 1.00 48.67 C
ANISOU 980 CA LYS A 152 6045 6411 6036 -239 14 221 C
ATOM 981 C LYS A 152 27.271 32.954 41.438 1.00 46.93 C
ANISOU 981 C LYS A 152 5820 6180 5831 -215 28 209 C
ATOM 982 O LYS A 152 28.014 33.006 40.457 1.00 44.66 O
ANISOU 982 O LYS A 152 5527 5878 5562 -202 25 214 O
ATOM 983 CB LYS A 152 27.222 30.981 42.985 1.00 50.21 C
ANISOU 983 CB LYS A 152 6236 6613 6227 -244 8 235 C
ATOM 984 CG LYS A 152 27.855 30.254 44.158 1.00 52.15 C
ANISOU 984 CG LYS A 152 6484 6867 6460 -268 -10 252 C
ATOM 985 CD LYS A 152 27.520 28.774 44.186 1.00 52.55 C
ANISOU 985 CD LYS A 152 6529 6921 6515 -272 -19 269 C
ATOM 986 CE LYS A 152 28.316 28.113 45.301 1.00 54.92 C
ANISOU 986 CE LYS A 152 6833 7227 6806 -296 -41 288 C
ATOM 987 NZ LYS A 152 28.379 26.634 45.171 1.00 57.24 N
ANISOU 987 NZ LYS A 152 7118 7518 7113 -298 -55 309 N
ATOM 988 N LYS A 153 26.006 33.359 41.425 1.00 46.04 N
ANISOU 988 N LYS A 153 5709 6073 5711 -210 44 194 N
ATOM 989 CA LYS A 153 25.348 33.833 40.225 1.00 45.45 C
ANISOU 989 CA LYS A 153 5629 5987 5650 -189 55 184 C
ATOM 990 C LYS A 153 24.908 35.269 40.442 1.00 44.13 C
ANISOU 990 C LYS A 153 5468 5821 5479 -188 68 163 C
ATOM 991 O LYS A 153 24.135 35.551 41.348 1.00 45.21 O
ANISOU 991 O LYS A 153 5608 5968 5601 -198 77 151 O
ATOM 992 CB LYS A 153 24.126 32.965 39.901 1.00 47.56 C
ANISOU 992 CB LYS A 153 5892 6259 5919 -183 61 185 C
ATOM 993 CG LYS A 153 24.407 31.482 39.723 1.00 50.85 C
ANISOU 993 CG LYS A 153 6303 6676 6340 -185 49 204 C
ATOM 994 CD LYS A 153 23.109 30.702 39.564 1.00 54.55 C
ANISOU 994 CD LYS A 153 6767 7150 6807 -181 56 204 C
ATOM 995 CE LYS A 153 23.354 29.199 39.523 1.00 57.07 C
ANISOU 995 CE LYS A 153 7081 7471 7132 -185 43 223 C
ATOM 996 NZ LYS A 153 22.077 28.425 39.547 1.00 57.49 N
ANISOU 996 NZ LYS A 153 7131 7531 7181 -183 49 223 N
ATOM 997 N LEU A 154 25.411 36.171 39.606 1.00 41.97 N
ANISOU 997 N LEU A 154 5193 5533 5218 -176 70 158 N
ATOM 998 CA LEU A 154 25.033 37.565 39.655 1.00 40.23 C
ANISOU 998 CA LEU A 154 4975 5309 4998 -172 81 138 C
ATOM 999 C LEU A 154 24.331 37.935 38.356 1.00 40.93 C
ANISOU 999 C LEU A 154 5059 5386 5104 -152 88 133 C
ATOM 1000 O LEU A 154 24.901 37.847 37.269 1.00 41.44 O
ANISOU 1000 O LEU A 154 5122 5439 5182 -141 83 142 O
ATOM 1001 CB LEU A 154 26.265 38.439 39.914 1.00 41.31 C
ANISOU 1001 CB LEU A 154 5117 5441 5136 -177 75 138 C
ATOM 1002 CG LEU A 154 26.169 39.924 40.298 1.00 42.15 C
ANISOU 1002 CG LEU A 154 5228 5545 5240 -179 83 118 C
ATOM 1003 CD1 LEU A 154 26.283 40.805 39.071 1.00 43.94 C
ANISOU 1003 CD1 LEU A 154 5452 5756 5487 -161 86 114 C
ATOM 1004 CD2 LEU A 154 24.912 40.278 41.078 1.00 42.13 C
ANISOU 1004 CD2 LEU A 154 5227 5553 5227 -185 97 100 C
ATOM 1005 N ASN A 155 23.073 38.330 38.482 1.00 41.61 N
ANISOU 1005 N ASN A 155 5144 5475 5190 -149 100 118 N
ATOM 1006 CA ASN A 155 22.258 38.676 37.336 1.00 40.29 C
ANISOU 1006 CA ASN A 155 4972 5296 5039 -131 105 113 C
ATOM 1007 C ASN A 155 21.904 40.161 37.381 1.00 41.39 C
ANISOU 1007 C ASN A 155 5112 5428 5185 -127 114 94 C
ATOM 1008 O ASN A 155 21.039 40.579 38.162 1.00 42.94 O
ANISOU 1008 O ASN A 155 5307 5629 5376 -133 124 78 O
ATOM 1009 CB ASN A 155 20.994 37.804 37.311 1.00 39.12 C
ANISOU 1009 CB ASN A 155 4819 5153 4890 -129 110 113 C
ATOM 1010 CG ASN A 155 20.289 37.812 35.964 1.00 39.61 C
ANISOU 1010 CG ASN A 155 4876 5202 4969 -111 111 114 C
ATOM 1011 OD1 ASN A 155 19.397 37.005 35.733 1.00 41.29 O
ANISOU 1011 OD1 ASN A 155 5085 5418 5184 -107 112 117 O
ATOM 1012 ND2 ASN A 155 20.676 38.720 35.072 1.00 39.16 N
ANISOU 1012 ND2 ASN A 155 4822 5133 4925 -101 109 112 N
ATOM 1013 N VAL A 156 22.580 40.949 36.546 1.00 39.82 N
ANISOU 1013 N VAL A 156 4915 5216 4998 -118 110 95 N
ATOM 1014 CA VAL A 156 22.287 42.375 36.420 1.00 39.35 C
ANISOU 1014 CA VAL A 156 4854 5145 4948 -113 116 79 C
ATOM 1015 C VAL A 156 21.857 42.775 35.003 1.00 39.46 C
ANISOU 1015 C VAL A 156 4865 5143 4981 -96 114 81 C
ATOM 1016 O VAL A 156 22.128 43.894 34.549 1.00 40.73 O
ANISOU 1016 O VAL A 156 5028 5293 5154 -91 113 76 O
ATOM 1017 CB VAL A 156 23.469 43.261 36.890 1.00 39.14 C
ANISOU 1017 CB VAL A 156 4833 5117 4919 -120 112 76 C
ATOM 1018 CG1 VAL A 156 23.592 43.239 38.409 1.00 37.53 C
ANISOU 1018 CG1 VAL A 156 4633 4928 4696 -138 116 68 C
ATOM 1019 CG2 VAL A 156 24.766 42.835 36.221 1.00 37.63 C
ANISOU 1019 CG2 VAL A 156 4645 4921 4730 -119 101 95 C
ATOM 1020 N ALA A 157 21.183 41.867 34.306 1.00 38.11 N
ANISOU 1020 N ALA A 157 4692 4972 4814 -89 112 90 N
ATOM 1021 CA ALA A 157 20.627 42.190 32.998 1.00 38.08 C
ANISOU 1021 CA ALA A 157 4686 4954 4827 -75 109 92 C
ATOM 1022 C ALA A 157 19.606 43.331 33.087 1.00 39.15 C
ANISOU 1022 C ALA A 157 4816 5081 4976 -70 116 74 C
ATOM 1023 O ALA A 157 18.984 43.545 34.137 1.00 37.53 O
ANISOU 1023 O ALA A 157 4607 4883 4767 -77 125 60 O
ATOM 1024 CB ALA A 157 19.990 40.963 32.379 1.00 36.80 C
ANISOU 1024 CB ALA A 157 4522 4795 4665 -70 107 103 C
ATOM 1025 N HIS A 158 19.443 44.061 31.983 1.00 38.36 N
ANISOU 1025 N HIS A 158 4716 4965 4892 -60 111 76 N
ATOM 1026 CA HIS A 158 18.379 45.052 31.866 1.00 39.46 C
ANISOU 1026 CA HIS A 158 4849 5093 5050 -53 114 62 C
ATOM 1027 C HIS A 158 18.571 46.178 32.857 1.00 39.90 C
ANISOU 1027 C HIS A 158 4903 5148 5107 -59 121 44 C
ATOM 1028 O HIS A 158 17.665 46.513 33.616 1.00 42.27 O
ANISOU 1028 O HIS A 158 5197 5451 5414 -61 131 27 O
ATOM 1029 CB HIS A 158 16.996 44.388 32.025 1.00 38.58 C
ANISOU 1029 CB HIS A 158 4729 4984 4943 -50 119 57 C
ATOM 1030 CG HIS A 158 15.853 45.173 31.404 1.00 39.78 C
ANISOU 1030 CG HIS A 158 4873 5120 5120 -40 117 48 C
ATOM 1031 ND1 HIS A 158 14.735 44.579 30.943 1.00 40.62 N
ANISOU 1031 ND1 HIS A 158 4974 5223 5235 -34 116 51 N
ATOM 1032 CD2 HIS A 158 15.698 46.539 31.161 1.00 38.94 C
ANISOU 1032 CD2 HIS A 158 4763 4997 5032 -35 116 39 C
ATOM 1033 CE1 HIS A 158 13.904 45.512 30.437 1.00 40.03 C
ANISOU 1033 CE1 HIS A 158 4892 5131 5185 -26 113 43 C
ATOM 1034 NE2 HIS A 158 14.495 46.710 30.568 1.00 40.15 N
ANISOU 1034 NE2 HIS A 158 4909 5139 5207 -27 112 36 N
ATOM 1035 N ASN A 159 19.760 46.766 32.867 1.00 39.19 N
ANISOU 1035 N ASN A 159 4819 5055 5013 -63 117 47 N
ATOM 1036 CA ASN A 159 20.036 47.924 33.716 1.00 39.21 C
ANISOU 1036 CA ASN A 159 4821 5057 5019 -68 123 30 C
ATOM 1037 C ASN A 159 20.658 49.064 32.881 1.00 39.18 C
ANISOU 1037 C ASN A 159 4820 5036 5030 -62 115 33 C
ATOM 1038 O ASN A 159 20.488 49.085 31.660 1.00 37.09 O
ANISOU 1038 O ASN A 159 4556 4760 4776 -53 107 45 O
ATOM 1039 CB ASN A 159 20.903 47.510 34.916 1.00 38.51 C
ANISOU 1039 CB ASN A 159 4738 4985 4908 -83 127 29 C
ATOM 1040 CG ASN A 159 20.158 46.610 35.897 1.00 38.93 C
ANISOU 1040 CG ASN A 159 4788 5054 4947 -91 136 23 C
ATOM 1041 OD1 ASN A 159 19.001 46.862 36.232 1.00 39.81 O
ANISOU 1041 OD1 ASN A 159 4893 5165 5067 -90 145 8 O
ATOM 1042 ND2 ASN A 159 20.827 45.563 36.373 1.00 37.96 N
ANISOU 1042 ND2 ASN A 159 4671 4945 4804 -101 133 35 N
ATOM 1043 N PHE A 160 21.357 50.003 33.523 1.00 40.37 N
ANISOU 1043 N PHE A 160 4973 5186 5180 -68 117 23 N
ATOM 1044 CA PHE A 160 21.983 51.127 32.811 1.00 41.57 C
ANISOU 1044 CA PHE A 160 5127 5321 5346 -63 110 26 C
ATOM 1045 C PHE A 160 23.503 51.106 32.835 1.00 40.11 C
ANISOU 1045 C PHE A 160 4950 5140 5149 -70 105 37 C
ATOM 1046 O PHE A 160 24.147 52.152 32.822 1.00 41.65 O
ANISOU 1046 O PHE A 160 5146 5325 5351 -70 102 33 O
ATOM 1047 CB PHE A 160 21.440 52.470 33.308 1.00 43.81 C
ANISOU 1047 CB PHE A 160 5403 5594 5646 -62 115 5 C
ATOM 1048 CG PHE A 160 19.978 52.650 33.043 1.00 48.61 C
ANISOU 1048 CG PHE A 160 6001 6192 6274 -54 118 -4 C
ATOM 1049 CD1 PHE A 160 19.490 52.666 31.731 1.00 51.21 C
ANISOU 1049 CD1 PHE A 160 6329 6508 6619 -43 108 7 C
ATOM 1050 CD2 PHE A 160 19.081 52.790 34.092 1.00 50.85 C
ANISOU 1050 CD2 PHE A 160 6277 6482 6561 -58 132 -26 C
ATOM 1051 CE1 PHE A 160 18.135 52.820 31.473 1.00 52.47 C
ANISOU 1051 CE1 PHE A 160 6478 6657 6798 -36 109 0 C
ATOM 1052 CE2 PHE A 160 17.722 52.950 33.842 1.00 54.48 C
ANISOU 1052 CE2 PHE A 160 6726 6932 7042 -51 135 -35 C
ATOM 1053 CZ PHE A 160 17.249 52.961 32.533 1.00 54.75 C
ANISOU 1053 CZ PHE A 160 6758 6951 7094 -39 122 -22 C
ATOM 1054 N ILE A 161 24.059 49.902 32.835 1.00 39.12 N
ANISOU 1054 N ILE A 161 4828 5026 5007 -74 103 51 N
ATOM 1055 CA ILE A 161 25.499 49.692 32.847 1.00 38.72 C
ANISOU 1055 CA ILE A 161 4784 4979 4947 -80 98 63 C
ATOM 1056 C ILE A 161 26.146 49.998 31.483 1.00 40.58 C
ANISOU 1056 C ILE A 161 5023 5201 5192 -73 91 77 C
ATOM 1057 O ILE A 161 25.746 49.450 30.449 1.00 40.25 O
ANISOU 1057 O ILE A 161 4982 5155 5154 -66 88 87 O
ATOM 1058 CB ILE A 161 25.820 48.268 33.340 1.00 37.29 C
ANISOU 1058 CB ILE A 161 4604 4814 4748 -87 98 73 C
ATOM 1059 CG1 ILE A 161 25.474 48.154 34.826 1.00 36.83 C
ANISOU 1059 CG1 ILE A 161 4545 4769 4677 -98 105 59 C
ATOM 1060 CG2 ILE A 161 27.290 47.942 33.125 1.00 38.15 C
ANISOU 1060 CG2 ILE A 161 4718 4924 4853 -91 92 87 C
ATOM 1061 CD1 ILE A 161 25.075 46.766 35.288 1.00 37.52 C
ANISOU 1061 CD1 ILE A 161 4632 4872 4751 -103 106 65 C
ATOM 1062 N HIS A 162 27.137 50.888 31.500 1.00 43.41 N
ANISOU 1062 N HIS A 162 5384 5553 5555 -76 88 77 N
ATOM 1063 CA HIS A 162 27.829 51.325 30.293 1.00 44.95 C
ANISOU 1063 CA HIS A 162 5583 5735 5759 -71 82 89 C
ATOM 1064 C HIS A 162 29.205 50.736 30.251 1.00 45.25 C
ANISOU 1064 C HIS A 162 5625 5777 5789 -77 80 101 C
ATOM 1065 O HIS A 162 29.902 50.834 29.240 1.00 46.27 O
ANISOU 1065 O HIS A 162 5758 5899 5923 -75 78 113 O
ATOM 1066 CB HIS A 162 27.933 52.850 30.246 1.00 49.81 C
ANISOU 1066 CB HIS A 162 6199 6337 6390 -70 80 80 C
ATOM 1067 CG HIS A 162 26.601 53.571 30.360 1.00 60.41 C
ANISOU 1067 CG HIS A 162 7535 7672 7745 -64 82 65 C
ATOM 1068 ND1 HIS A 162 25.804 53.815 29.288 1.00 63.55 N
ANISOU 1068 ND1 HIS A 162 7932 8057 8156 -55 77 70 N
ATOM 1069 CD2 HIS A 162 25.949 54.127 31.468 1.00 65.22 C
ANISOU 1069 CD2 HIS A 162 8138 8283 8357 -66 88 45 C
ATOM 1070 CE1 HIS A 162 24.696 54.481 29.690 1.00 63.85 C
ANISOU 1070 CE1 HIS A 162 7962 8089 8208 -52 79 54 C
ATOM 1071 NE2 HIS A 162 24.784 54.671 31.023 1.00 68.97 N
ANISOU 1071 NE2 HIS A 162 8608 8747 8851 -58 87 38 N
ATOM 1072 N SER A 163 29.611 50.108 31.351 1.00 45.61 N
ANISOU 1072 N SER A 163 5669 5836 5822 -85 82 99 N
ATOM 1073 CA SER A 163 30.984 49.642 31.505 1.00 44.98 C
ANISOU 1073 CA SER A 163 5591 5760 5739 -92 78 110 C
ATOM 1074 C SER A 163 31.100 48.136 31.653 1.00 45.47 C
ANISOU 1074 C SER A 163 5651 5833 5790 -95 78 120 C
ATOM 1075 O SER A 163 30.382 47.506 32.438 1.00 45.48 O
ANISOU 1075 O SER A 163 5651 5846 5782 -99 80 115 O
ATOM 1076 CB SER A 163 31.651 50.319 32.700 1.00 45.04 C
ANISOU 1076 CB SER A 163 5598 5770 5742 -102 77 101 C
ATOM 1077 OG SER A 163 32.964 49.819 32.882 1.00 46.37 O
ANISOU 1077 OG SER A 163 5768 5942 5909 -109 72 112 O
ATOM 1078 N CYS A 164 32.037 47.567 30.907 1.00 45.39 N
ANISOU 1078 N CYS A 164 5641 5819 5783 -95 76 134 N
ATOM 1079 CA CYS A 164 32.279 46.138 30.964 1.00 44.68 C
ANISOU 1079 CA CYS A 164 5549 5738 5687 -98 75 144 C
ATOM 1080 C CYS A 164 33.293 45.795 32.055 1.00 43.24 C
ANISOU 1080 C CYS A 164 5364 5562 5501 -109 69 147 C
ATOM 1081 O CYS A 164 33.630 44.628 32.253 1.00 42.96 O
ANISOU 1081 O CYS A 164 5325 5533 5463 -113 66 156 O
ATOM 1082 CB CYS A 164 32.752 45.632 29.601 1.00 45.49 C
ANISOU 1082 CB CYS A 164 5652 5833 5797 -92 77 155 C
ATOM 1083 SG CYS A 164 32.700 43.838 29.415 1.00 45.79 S
ANISOU 1083 SG CYS A 164 5686 5879 5832 -93 77 166 S
ATOM 1084 N LYS A 165 33.766 46.808 32.774 1.00 41.88 N
ANISOU 1084 N LYS A 165 5193 5388 5329 -115 67 140 N
ATOM 1085 CA LYS A 165 34.749 46.594 33.832 1.00 42.03 C
ANISOU 1085 CA LYS A 165 5211 5413 5345 -127 60 143 C
ATOM 1086 C LYS A 165 34.269 45.567 34.861 1.00 41.23 C
ANISOU 1086 C LYS A 165 5109 5326 5229 -135 56 144 C
ATOM 1087 O LYS A 165 33.178 45.679 35.415 1.00 41.94 O
ANISOU 1087 O LYS A 165 5201 5423 5308 -136 61 133 O
ATOM 1088 CB LYS A 165 35.133 47.923 34.498 1.00 42.14 C
ANISOU 1088 CB LYS A 165 5228 5422 5359 -132 58 132 C
ATOM 1089 CG LYS A 165 36.010 47.814 35.739 1.00 40.94 C
ANISOU 1089 CG LYS A 165 5076 5276 5200 -146 49 134 C
ATOM 1090 CD LYS A 165 37.452 47.460 35.416 1.00 41.80 C
ANISOU 1090 CD LYS A 165 5180 5378 5321 -149 41 148 C
ATOM 1091 CE LYS A 165 38.352 47.743 36.616 1.00 42.50 C
ANISOU 1091 CE LYS A 165 5270 5470 5406 -163 31 148 C
ATOM 1092 NZ LYS A 165 39.784 47.407 36.392 1.00 40.28 N
ANISOU 1092 NZ LYS A 165 4984 5181 5140 -167 22 162 N
ATOM 1093 N LEU A 166 35.088 44.543 35.056 1.00 41.64 N
ANISOU 1093 N LEU A 166 5157 5380 5282 -141 49 157 N
ATOM 1094 CA LEU A 166 34.927 43.566 36.120 1.00 41.03 C
ANISOU 1094 CA LEU A 166 5079 5315 5192 -152 42 162 C
ATOM 1095 C LEU A 166 35.713 44.058 37.349 1.00 40.68 C
ANISOU 1095 C LEU A 166 5038 5275 5142 -166 33 160 C
ATOM 1096 O LEU A 166 36.945 44.092 37.326 1.00 40.39 O
ANISOU 1096 O LEU A 166 4998 5231 5116 -170 25 168 O
ATOM 1097 CB LEU A 166 35.439 42.210 35.634 1.00 41.45 C
ANISOU 1097 CB LEU A 166 5126 5368 5255 -151 38 178 C
ATOM 1098 CG LEU A 166 34.415 41.220 35.057 1.00 43.68 C
ANISOU 1098 CG LEU A 166 5406 5654 5534 -143 43 180 C
ATOM 1099 CD1 LEU A 166 33.491 41.822 34.013 1.00 43.43 C
ANISOU 1099 CD1 LEU A 166 5377 5617 5505 -129 54 171 C
ATOM 1100 CD2 LEU A 166 35.143 40.017 34.485 1.00 45.39 C
ANISOU 1100 CD2 LEU A 166 5615 5866 5763 -142 39 195 C
ATOM 1101 N PRO A 167 35.001 44.458 38.417 1.00 40.64 N
ANISOU 1101 N PRO A 167 5039 5280 5120 -175 35 148 N
ATOM 1102 CA PRO A 167 35.606 45.185 39.552 1.00 41.92 C
ANISOU 1102 CA PRO A 167 5206 5445 5274 -190 28 142 C
ATOM 1103 C PRO A 167 36.728 44.475 40.325 1.00 43.70 C
ANISOU 1103 C PRO A 167 5431 5674 5498 -204 11 157 C
ATOM 1104 O PRO A 167 36.926 43.266 40.194 1.00 45.15 O
ANISOU 1104 O PRO A 167 5609 5860 5685 -206 4 172 O
ATOM 1105 CB PRO A 167 34.415 45.476 40.478 1.00 41.83 C
ANISOU 1105 CB PRO A 167 5201 5447 5244 -197 35 126 C
ATOM 1106 CG PRO A 167 33.289 44.634 39.989 1.00 41.64 C
ANISOU 1106 CG PRO A 167 5173 5428 5217 -188 43 127 C
ATOM 1107 CD PRO A 167 33.539 44.332 38.544 1.00 40.97 C
ANISOU 1107 CD PRO A 167 5082 5331 5151 -172 45 137 C
ATOM 1108 N ALA A 168 37.459 45.247 41.123 1.00 45.55 N
ANISOU 1108 N ALA A 168 5670 5908 5729 -216 3 153 N
ATOM 1109 CA ALA A 168 38.546 44.719 41.943 1.00 44.41 C
ANISOU 1109 CA ALA A 168 5524 5765 5583 -232 -14 167 C
ATOM 1110 C ALA A 168 38.007 43.787 43.018 1.00 44.81 C
ANISOU 1110 C ALA A 168 5580 5831 5613 -248 -20 171 C
ATOM 1111 O ALA A 168 38.662 42.809 43.382 1.00 44.53 O
ANISOU 1111 O ALA A 168 5542 5797 5580 -257 -36 188 O
ATOM 1112 CB ALA A 168 39.335 45.855 42.573 1.00 42.35 C
ANISOU 1112 CB ALA A 168 5268 5499 5322 -241 -20 160 C
ATOM 1113 N TYR A 169 36.800 44.081 43.501 1.00 45.99 N
ANISOU 1113 N TYR A 169 5737 5993 5744 -250 -9 155 N
ATOM 1114 CA TYR A 169 36.211 43.334 44.612 1.00 48.16 C
ANISOU 1114 CA TYR A 169 6019 6285 5995 -267 -13 157 C
ATOM 1115 C TYR A 169 35.758 41.926 44.225 1.00 49.00 C
ANISOU 1115 C TYR A 169 6119 6395 6104 -263 -14 171 C
ATOM 1116 O TYR A 169 35.352 41.133 45.087 1.00 49.70 O
ANISOU 1116 O TYR A 169 6212 6497 6175 -278 -20 176 O
ATOM 1117 CB TYR A 169 35.076 44.125 45.284 1.00 47.22 C
ANISOU 1117 CB TYR A 169 5908 6176 5855 -273 1 134 C
ATOM 1118 CG TYR A 169 33.818 44.292 44.458 1.00 48.42 C
ANISOU 1118 CG TYR A 169 6056 6326 6012 -255 21 121 C
ATOM 1119 CD1 TYR A 169 32.999 43.203 44.156 1.00 47.40 C
ANISOU 1119 CD1 TYR A 169 5923 6204 5882 -250 25 128 C
ATOM 1120 CD2 TYR A 169 33.428 45.551 44.007 1.00 49.31 C
ANISOU 1120 CD2 TYR A 169 6169 6432 6134 -243 34 102 C
ATOM 1121 CE1 TYR A 169 31.848 43.362 43.412 1.00 46.85 C
ANISOU 1121 CE1 TYR A 169 5850 6133 5818 -234 41 117 C
ATOM 1122 CE2 TYR A 169 32.271 45.720 43.267 1.00 47.07 C
ANISOU 1122 CE2 TYR A 169 5881 6146 5857 -228 50 92 C
ATOM 1123 CZ TYR A 169 31.490 44.624 42.973 1.00 47.48 C
ANISOU 1123 CZ TYR A 169 5929 6203 5906 -223 53 99 C
ATOM 1124 OH TYR A 169 30.345 44.792 42.232 1.00 49.05 O
ANISOU 1124 OH TYR A 169 6123 6399 6112 -208 67 89 O
ATOM 1125 N PHE A 170 35.833 41.618 42.933 1.00 47.85 N
ANISOU 1125 N PHE A 170 5963 6237 5979 -244 -9 177 N
ATOM 1126 CA PHE A 170 35.542 40.268 42.454 1.00 48.02 C
ANISOU 1126 CA PHE A 170 5977 6260 6006 -239 -12 191 C
ATOM 1127 C PHE A 170 36.468 39.229 43.077 1.00 48.57 C
ANISOU 1127 C PHE A 170 6044 6331 6078 -253 -32 212 C
ATOM 1128 O PHE A 170 36.095 38.061 43.196 1.00 48.44 O
ANISOU 1128 O PHE A 170 6024 6320 6059 -256 -37 223 O
ATOM 1129 CB PHE A 170 35.621 40.198 40.925 1.00 44.41 C
ANISOU 1129 CB PHE A 170 5511 5789 5572 -217 -3 193 C
ATOM 1130 CG PHE A 170 34.302 40.398 40.233 1.00 42.65 C
ANISOU 1130 CG PHE A 170 5289 5569 5346 -203 13 181 C
ATOM 1131 CD1 PHE A 170 33.258 41.084 40.854 1.00 42.71 C
ANISOU 1131 CD1 PHE A 170 5304 5586 5337 -207 23 164 C
ATOM 1132 CD2 PHE A 170 34.114 39.929 38.942 1.00 41.77 C
ANISOU 1132 CD2 PHE A 170 5171 5449 5250 -187 19 186 C
ATOM 1133 CE1 PHE A 170 32.047 41.278 40.207 1.00 40.82 C
ANISOU 1133 CE1 PHE A 170 5064 5346 5098 -194 38 153 C
ATOM 1134 CE2 PHE A 170 32.911 40.125 38.287 1.00 40.91 C
ANISOU 1134 CE2 PHE A 170 5062 5340 5138 -174 33 175 C
ATOM 1135 CZ PHE A 170 31.877 40.797 38.921 1.00 41.32 C
ANISOU 1135 CZ PHE A 170 5120 5401 5176 -177 41 159 C
ATOM 1136 N SER A 171 37.665 39.656 43.479 1.00 49.85 N
ANISOU 1136 N SER A 171 6206 6486 6246 -262 -46 217 N
ATOM 1137 CA SER A 171 38.651 38.739 44.052 1.00 51.46 C
ANISOU 1137 CA SER A 171 6406 6689 6458 -276 -68 238 C
ATOM 1138 C SER A 171 38.285 38.310 45.473 1.00 51.35 C
ANISOU 1138 C SER A 171 6402 6691 6417 -300 -80 242 C
ATOM 1139 O SER A 171 38.923 37.432 46.043 1.00 49.01 O
ANISOU 1139 O SER A 171 6103 6394 6123 -314 -100 261 O
ATOM 1140 CB SER A 171 40.053 39.340 43.998 1.00 53.39 C
ANISOU 1140 CB SER A 171 6645 6918 6719 -278 -79 243 C
ATOM 1141 OG SER A 171 40.130 40.524 44.767 1.00 56.81 O
ANISOU 1141 OG SER A 171 7090 7356 7137 -289 -79 230 O
ATOM 1142 N ASN A 172 37.252 38.936 46.029 1.00 52.75 N
ANISOU 1142 N ASN A 172 6591 6881 6569 -305 -66 224 N
ATOM 1143 CA ASN A 172 36.684 38.520 47.299 1.00 55.33 C
ANISOU 1143 CA ASN A 172 6928 7225 6867 -328 -72 225 C
ATOM 1144 C ASN A 172 35.514 37.579 47.086 1.00 54.40 C
ANISOU 1144 C ASN A 172 6808 7116 6742 -323 -62 227 C
ATOM 1145 O ASN A 172 35.239 36.713 47.918 1.00 55.15 O
ANISOU 1145 O ASN A 172 6908 7223 6821 -340 -72 237 O
ATOM 1146 CB ASN A 172 36.324 39.742 48.164 1.00 61.08 C
ANISOU 1146 CB ASN A 172 7671 7963 7572 -340 -63 204 C
ATOM 1147 CG ASN A 172 37.519 40.237 48.958 1.00 68.39 C
ANISOU 1147 CG ASN A 172 8603 8885 8495 -357 -82 210 C
ATOM 1148 OD1 ASN A 172 38.576 39.610 48.906 1.00 67.12 O
ANISOU 1148 OD1 ASN A 172 8435 8716 8350 -361 -103 231 O
ATOM 1149 ND2 ASN A 172 37.382 41.343 49.691 1.00 85.49 N
ANISOU 1149 ND2 ASN A 172 10781 11058 10643 -368 -76 192 N
ATOM 1150 N LEU A 173 34.854 37.743 45.943 1.00 54.66 N
ANISOU 1150 N LEU A 173 6835 7144 6789 -299 -44 217 N
ATOM 1151 CA LEU A 173 33.769 36.873 45.499 1.00 51.94 C
ANISOU 1151 CA LEU A 173 6485 6804 6442 -291 -34 218 C
ATOM 1152 C LEU A 173 34.378 35.649 44.845 1.00 51.44 C
ANISOU 1152 C LEU A 173 6411 6732 6401 -284 -47 239 C
ATOM 1153 O LEU A 173 34.310 35.467 43.636 1.00 53.83 O
ANISOU 1153 O LEU A 173 6704 7024 6724 -264 -39 239 O
ATOM 1154 CB LEU A 173 32.879 37.616 44.508 1.00 48.76 C
ANISOU 1154 CB LEU A 173 6081 6398 6047 -269 -12 199 C
ATOM 1155 CG LEU A 173 31.734 38.481 45.028 1.00 49.56 C
ANISOU 1155 CG LEU A 173 6190 6509 6129 -272 5 176 C
ATOM 1156 CD1 LEU A 173 31.886 38.853 46.498 1.00 49.03 C
ANISOU 1156 CD1 LEU A 173 6136 6455 6037 -298 0 171 C
ATOM 1157 CD2 LEU A 173 31.600 39.720 44.152 1.00 48.69 C
ANISOU 1157 CD2 LEU A 173 6078 6388 6032 -254 19 160 C
ATOM 1158 N THR A 174 34.978 34.803 45.665 1.00 52.40 N
ANISOU 1158 N THR A 174 6532 6857 6519 -302 -68 258 N
ATOM 1159 CA THR A 174 35.791 33.716 45.168 1.00 51.77 C
ANISOU 1159 CA THR A 174 6440 6766 6464 -298 -83 279 C
ATOM 1160 C THR A 174 34.970 32.530 44.648 1.00 49.89 C
ANISOU 1160 C THR A 174 6194 6530 6231 -290 -79 285 C
ATOM 1161 O THR A 174 35.518 31.619 44.029 1.00 47.72 O
ANISOU 1161 O THR A 174 5907 6243 5979 -283 -88 299 O
ATOM 1162 CB THR A 174 36.808 33.282 46.237 1.00 54.43 C
ANISOU 1162 CB THR A 174 6778 7103 6799 -321 -110 297 C
ATOM 1163 OG1 THR A 174 37.898 32.614 45.597 1.00 59.24 O
ANISOU 1163 OG1 THR A 174 7371 7694 7440 -314 -124 314 O
ATOM 1164 CG2 THR A 174 36.164 32.368 47.278 1.00 54.95 C
ANISOU 1164 CG2 THR A 174 6851 7184 6842 -342 -120 307 C
ATOM 1165 N ASN A 175 33.659 32.562 44.887 1.00 49.90 N
ANISOU 1165 N ASN A 175 6203 6545 6212 -290 -64 274 N
ATOM 1166 CA ASN A 175 32.743 31.514 44.436 1.00 48.08 C
ANISOU 1166 CA ASN A 175 5967 6318 5984 -283 -59 278 C
ATOM 1167 C ASN A 175 31.856 31.940 43.281 1.00 47.55 C
ANISOU 1167 C ASN A 175 5896 6247 5923 -260 -37 262 C
ATOM 1168 O ASN A 175 30.898 31.250 42.935 1.00 49.38 O
ANISOU 1168 O ASN A 175 6124 6482 6153 -253 -29 262 O
ATOM 1169 CB ASN A 175 31.871 31.052 45.600 1.00 50.49 C
ANISOU 1169 CB ASN A 175 6280 6641 6260 -302 -61 280 C
ATOM 1170 CG ASN A 175 32.620 30.149 46.550 1.00 51.40 C
ANISOU 1170 CG ASN A 175 6397 6760 6373 -325 -86 303 C
ATOM 1171 OD1 ASN A 175 33.237 30.617 47.508 1.00 54.70 O
ANISOU 1171 OD1 ASN A 175 6823 7181 6777 -344 -98 305 O
ATOM 1172 ND2 ASN A 175 32.604 28.850 46.271 1.00 50.33 N
ANISOU 1172 ND2 ASN A 175 6251 6620 6251 -323 -97 320 N
ATOM 1173 N LEU A 176 32.172 33.085 42.690 1.00 48.56 N
ANISOU 1173 N LEU A 176 6026 6367 6058 -248 -27 249 N
ATOM 1174 CA LEU A 176 31.374 33.639 41.600 1.00 46.35 C
ANISOU 1174 CA LEU A 176 5744 6081 5784 -228 -8 234 C
ATOM 1175 C LEU A 176 31.767 32.973 40.273 1.00 44.45 C
ANISOU 1175 C LEU A 176 5492 5827 5569 -211 -8 243 C
ATOM 1176 O LEU A 176 32.944 32.983 39.885 1.00 44.98 O
ANISOU 1176 O LEU A 176 5554 5882 5654 -208 -16 251 O
ATOM 1177 CB LEU A 176 31.529 35.163 41.554 1.00 43.69 C
ANISOU 1177 CB LEU A 176 5413 5742 5445 -224 1 217 C
ATOM 1178 CG LEU A 176 30.716 35.954 40.530 1.00 44.41 C
ANISOU 1178 CG LEU A 176 5504 5826 5542 -205 19 201 C
ATOM 1179 CD1 LEU A 176 29.237 35.998 40.888 1.00 42.43 C
ANISOU 1179 CD1 LEU A 176 5257 5587 5276 -205 31 189 C
ATOM 1180 CD2 LEU A 176 31.282 37.360 40.418 1.00 44.23 C
ANISOU 1180 CD2 LEU A 176 5485 5796 5523 -202 22 190 C
ATOM 1181 N VAL A 177 30.779 32.378 39.605 1.00 40.90 N
ANISOU 1181 N VAL A 177 5039 5379 5122 -199 0 241 N
ATOM 1182 CA VAL A 177 31.016 31.568 38.400 1.00 39.20 C
ANISOU 1182 CA VAL A 177 4814 5152 4927 -185 0 249 C
ATOM 1183 C VAL A 177 30.220 32.029 37.180 1.00 38.02 C
ANISOU 1183 C VAL A 177 4665 4997 4783 -167 16 237 C
ATOM 1184 O VAL A 177 30.529 31.637 36.051 1.00 37.84 O
ANISOU 1184 O VAL A 177 4637 4964 4777 -155 18 240 O
ATOM 1185 CB VAL A 177 30.764 30.052 38.639 1.00 38.13 C
ANISOU 1185 CB VAL A 177 4672 5020 4794 -191 -9 264 C
ATOM 1186 CG1 VAL A 177 31.856 29.449 39.511 1.00 36.85 C
ANISOU 1186 CG1 VAL A 177 4506 4857 4636 -207 -29 280 C
ATOM 1187 CG2 VAL A 177 29.380 29.799 39.226 1.00 36.57 C
ANISOU 1187 CG2 VAL A 177 4480 4838 4577 -196 -3 259 C
ATOM 1188 N HIS A 178 29.197 32.848 37.418 1.00 38.86 N
ANISOU 1188 N HIS A 178 4778 5110 4874 -165 27 223 N
ATOM 1189 CA HIS A 178 28.370 33.403 36.349 1.00 39.87 C
ANISOU 1189 CA HIS A 178 4907 5232 5007 -149 40 211 C
ATOM 1190 C HIS A 178 27.893 34.817 36.595 1.00 39.95 C
ANISOU 1190 C HIS A 178 4924 5244 5009 -148 50 194 C
ATOM 1191 O HIS A 178 27.241 35.097 37.605 1.00 38.39 O
ANISOU 1191 O HIS A 178 4730 5057 4797 -157 53 186 O
ATOM 1192 CB HIS A 178 27.172 32.500 36.083 1.00 41.03 C
ANISOU 1192 CB HIS A 178 5051 5385 5152 -144 44 212 C
ATOM 1193 CG HIS A 178 26.347 32.938 34.899 1.00 44.73 C
ANISOU 1193 CG HIS A 178 5520 5845 5627 -128 55 203 C
ATOM 1194 ND1 HIS A 178 25.139 33.522 35.032 1.00 44.89 N
ANISOU 1194 ND1 HIS A 178 5544 5871 5641 -125 64 191 N
ATOM 1195 CD2 HIS A 178 26.615 32.888 33.526 1.00 45.20 C
ANISOU 1195 CD2 HIS A 178 5578 5893 5701 -115 57 205 C
ATOM 1196 CE1 HIS A 178 24.647 33.809 33.810 1.00 46.19 C
ANISOU 1196 CE1 HIS A 178 5708 6025 5815 -110 69 186 C
ATOM 1197 NE2 HIS A 178 25.555 33.421 32.890 1.00 45.28 N
ANISOU 1197 NE2 HIS A 178 5591 5901 5711 -105 65 196 N
ATOM 1198 N VAL A 179 28.199 35.711 35.652 1.00 40.38 N
ANISOU 1198 N VAL A 179 4980 5287 5074 -137 55 189 N
ATOM 1199 CA VAL A 179 27.691 37.089 35.667 1.00 39.72 C
ANISOU 1199 CA VAL A 179 4901 5201 4987 -133 63 172 C
ATOM 1200 C VAL A 179 26.897 37.400 34.393 1.00 40.34 C
ANISOU 1200 C VAL A 179 4979 5271 5076 -117 71 167 C
ATOM 1201 O VAL A 179 27.423 37.321 33.277 1.00 40.91 O
ANISOU 1201 O VAL A 179 5051 5333 5160 -109 70 173 O
ATOM 1202 CB VAL A 179 28.832 38.118 35.821 1.00 40.13 C
ANISOU 1202 CB VAL A 179 4955 5246 5043 -137 61 170 C
ATOM 1203 CG1 VAL A 179 28.306 39.544 35.670 1.00 38.60 C
ANISOU 1203 CG1 VAL A 179 4766 5048 4850 -131 69 154 C
ATOM 1204 CG2 VAL A 179 29.545 37.932 37.157 1.00 39.64 C
ANISOU 1204 CG2 VAL A 179 4896 5194 4971 -154 51 174 C
ATOM 1205 N ASP A 180 25.633 37.763 34.569 1.00 39.53 N
ANISOU 1205 N ASP A 180 4876 5171 4969 -114 79 156 N
ATOM 1206 CA ASP A 180 24.775 38.141 33.454 1.00 38.26 C
ANISOU 1206 CA ASP A 180 4715 5001 4818 -100 84 151 C
ATOM 1207 C ASP A 180 24.703 39.671 33.286 1.00 36.55 C
ANISOU 1207 C ASP A 180 4502 4776 4607 -96 88 138 C
ATOM 1208 O ASP A 180 24.131 40.374 34.126 1.00 35.79 O
ANISOU 1208 O ASP A 180 4406 4685 4507 -100 94 124 O
ATOM 1209 CB ASP A 180 23.379 37.531 33.650 1.00 39.62 C
ANISOU 1209 CB ASP A 180 4885 5181 4988 -98 88 147 C
ATOM 1210 CG ASP A 180 22.489 37.652 32.411 1.00 41.12 C
ANISOU 1210 CG ASP A 180 5073 5360 5188 -84 91 145 C
ATOM 1211 OD1 ASP A 180 22.526 38.682 31.704 1.00 40.44 O
ANISOU 1211 OD1 ASP A 180 4989 5263 5111 -77 92 140 O
ATOM 1212 OD2 ASP A 180 21.722 36.704 32.157 1.00 43.90 O
ANISOU 1212 OD2 ASP A 180 5422 5716 5541 -81 90 150 O
ATOM 1213 N LEU A 181 25.277 40.167 32.188 1.00 35.22 N
ANISOU 1213 N LEU A 181 4335 4595 4449 -88 86 142 N
ATOM 1214 CA LEU A 181 25.346 41.599 31.908 1.00 34.49 C
ANISOU 1214 CA LEU A 181 4246 4493 4364 -84 89 132 C
ATOM 1215 C LEU A 181 24.535 41.988 30.675 1.00 35.93 C
ANISOU 1215 C LEU A 181 4429 4664 4558 -72 89 131 C
ATOM 1216 O LEU A 181 24.774 43.039 30.066 1.00 36.25 O
ANISOU 1216 O LEU A 181 4472 4692 4606 -68 89 129 O
ATOM 1217 CB LEU A 181 26.804 42.036 31.743 1.00 33.28 C
ANISOU 1217 CB LEU A 181 4095 4334 4213 -88 85 138 C
ATOM 1218 CG LEU A 181 27.647 42.174 33.011 1.00 32.10 C
ANISOU 1218 CG LEU A 181 3946 4192 4056 -100 82 136 C
ATOM 1219 CD1 LEU A 181 29.131 42.119 32.704 1.00 31.42 C
ANISOU 1219 CD1 LEU A 181 3861 4101 3975 -103 77 147 C
ATOM 1220 CD2 LEU A 181 27.310 43.475 33.711 1.00 33.08 C
ANISOU 1220 CD2 LEU A 181 4072 4315 4179 -103 86 120 C
ATOM 1221 N SER A 182 23.564 41.143 30.330 1.00 37.61 N
ANISOU 1221 N SER A 182 4639 4879 4770 -68 90 134 N
ATOM 1222 CA SER A 182 22.749 41.301 29.118 1.00 38.82 C
ANISOU 1222 CA SER A 182 4794 5022 4934 -57 88 135 C
ATOM 1223 C SER A 182 21.915 42.561 29.119 1.00 40.40 C
ANISOU 1223 C SER A 182 4991 5213 5144 -53 90 123 C
ATOM 1224 O SER A 182 21.574 43.094 30.184 1.00 42.23 O
ANISOU 1224 O SER A 182 5220 5450 5375 -57 95 110 O
ATOM 1225 CB SER A 182 21.775 40.133 28.962 1.00 38.39 C
ANISOU 1225 CB SER A 182 4735 4973 4877 -54 88 139 C
ATOM 1226 OG SER A 182 22.414 38.904 29.174 1.00 40.38 O
ANISOU 1226 OG SER A 182 4987 5234 5121 -59 87 149 O
ATOM 1227 N TYR A 183 21.552 42.997 27.913 1.00 40.59 N
ANISOU 1227 N TYR A 183 5019 5224 5179 -45 85 127 N
ATOM 1228 CA TYR A 183 20.605 44.089 27.707 1.00 40.83 C
ANISOU 1228 CA TYR A 183 5046 5243 5223 -39 84 117 C
ATOM 1229 C TYR A 183 20.959 45.299 28.578 1.00 39.62 C
ANISOU 1229 C TYR A 183 4891 5088 5074 -43 88 104 C
ATOM 1230 O TYR A 183 20.146 45.807 29.354 1.00 39.32 O
ANISOU 1230 O TYR A 183 4846 5050 5041 -43 93 89 O
ATOM 1231 CB TYR A 183 19.149 43.609 27.891 1.00 42.32 C
ANISOU 1231 CB TYR A 183 5227 5433 5417 -35 86 111 C
ATOM 1232 CG TYR A 183 18.112 44.592 27.379 1.00 45.92 C
ANISOU 1232 CG TYR A 183 5679 5874 5892 -27 82 105 C
ATOM 1233 CD1 TYR A 183 18.338 45.341 26.218 1.00 48.57 C
ANISOU 1233 CD1 TYR A 183 6021 6195 6238 -23 73 112 C
ATOM 1234 CD2 TYR A 183 16.904 44.772 28.046 1.00 47.78 C
ANISOU 1234 CD2 TYR A 183 5904 6110 6138 -25 87 91 C
ATOM 1235 CE1 TYR A 183 17.397 46.244 25.752 1.00 49.03 C
ANISOU 1235 CE1 TYR A 183 6075 6238 6316 -17 66 107 C
ATOM 1236 CE2 TYR A 183 15.954 45.671 27.581 1.00 48.11 C
ANISOU 1236 CE2 TYR A 183 5940 6136 6202 -19 82 85 C
ATOM 1237 CZ TYR A 183 16.210 46.402 26.439 1.00 49.19 C
ANISOU 1237 CZ TYR A 183 6083 6257 6348 -14 71 93 C
ATOM 1238 OH TYR A 183 15.278 47.295 25.979 1.00 54.62 O
ANISOU 1238 OH TYR A 183 6764 6927 7059 -8 64 89 O
ATOM 1239 N ASN A 184 22.214 45.716 28.452 1.00 38.61 N
ANISOU 1239 N ASN A 184 4769 4958 4942 -46 86 109 N
ATOM 1240 CA ASN A 184 22.717 46.929 29.070 1.00 37.88 C
ANISOU 1240 CA ASN A 184 4676 4862 4855 -50 88 99 C
ATOM 1241 C ASN A 184 23.269 47.805 27.959 1.00 37.85 C
ANISOU 1241 C ASN A 184 4677 4843 4860 -46 81 106 C
ATOM 1242 O ASN A 184 22.950 47.570 26.792 1.00 38.15 O
ANISOU 1242 O ASN A 184 4718 4872 4902 -41 76 116 O
ATOM 1243 CB ASN A 184 23.760 46.599 30.136 1.00 37.19 C
ANISOU 1243 CB ASN A 184 4590 4787 4753 -60 92 98 C
ATOM 1244 CG ASN A 184 23.125 46.139 31.438 1.00 37.74 C
ANISOU 1244 CG ASN A 184 4655 4870 4814 -66 98 87 C
ATOM 1245 OD1 ASN A 184 22.481 46.922 32.122 1.00 37.30 O
ANISOU 1245 OD1 ASN A 184 4595 4814 4763 -67 104 71 O
ATOM 1246 ND2 ASN A 184 23.299 44.866 31.781 1.00 37.37 N
ANISOU 1246 ND2 ASN A 184 4608 4836 4754 -71 99 96 N
ATOM 1247 N TYR A 185 24.080 48.804 28.297 1.00 38.92 N
ANISOU 1247 N TYR A 185 4814 4973 4999 -50 82 101 N
ATOM 1248 CA TYR A 185 24.533 49.797 27.302 1.00 38.51 C
ANISOU 1248 CA TYR A 185 4767 4906 4958 -47 75 107 C
ATOM 1249 C TYR A 185 26.045 49.767 27.060 1.00 37.52 C
ANISOU 1249 C TYR A 185 4647 4781 4825 -52 75 117 C
ATOM 1250 O TYR A 185 26.651 50.779 26.714 1.00 37.49 O
ANISOU 1250 O TYR A 185 4647 4767 4829 -53 72 118 O
ATOM 1251 CB TYR A 185 24.079 51.201 27.711 1.00 39.88 C
ANISOU 1251 CB TYR A 185 4936 5069 5147 -45 74 93 C
ATOM 1252 CG TYR A 185 22.575 51.376 27.699 1.00 43.33 C
ANISOU 1252 CG TYR A 185 5366 5500 5597 -39 74 84 C
ATOM 1253 CD1 TYR A 185 21.776 50.848 28.725 1.00 42.46 C
ANISOU 1253 CD1 TYR A 185 5248 5401 5483 -40 82 71 C
ATOM 1254 CD2 TYR A 185 21.947 52.069 26.663 1.00 44.85 C
ANISOU 1254 CD2 TYR A 185 5557 5675 5806 -32 65 88 C
ATOM 1255 CE1 TYR A 185 20.399 50.998 28.712 1.00 44.39 C
ANISOU 1255 CE1 TYR A 185 5483 5638 5741 -34 83 62 C
ATOM 1256 CE2 TYR A 185 20.567 52.230 26.644 1.00 46.96 C
ANISOU 1256 CE2 TYR A 185 5816 5935 6089 -26 63 80 C
ATOM 1257 CZ TYR A 185 19.795 51.694 27.667 1.00 47.17 C
ANISOU 1257 CZ TYR A 185 5834 5972 6114 -27 73 66 C
ATOM 1258 OH TYR A 185 18.421 51.857 27.644 1.00 47.10 O
ANISOU 1258 OH TYR A 185 5815 5955 6122 -21 72 58 O
ATOM 1259 N ILE A 186 26.644 48.596 27.244 1.00 35.60 N
ANISOU 1259 N ILE A 186 4405 4550 4569 -56 78 124 N
ATOM 1260 CA ILE A 186 28.069 48.426 27.049 1.00 33.77 C
ANISOU 1260 CA ILE A 186 4178 4319 4333 -62 78 133 C
ATOM 1261 C ILE A 186 28.364 48.520 25.563 1.00 34.01 C
ANISOU 1261 C ILE A 186 4215 4339 4368 -59 75 145 C
ATOM 1262 O ILE A 186 27.776 47.804 24.751 1.00 34.47 O
ANISOU 1262 O ILE A 186 4275 4397 4422 -56 75 151 O
ATOM 1263 CB ILE A 186 28.567 47.082 27.623 1.00 32.46 C
ANISOU 1263 CB ILE A 186 4009 4166 4155 -67 81 138 C
ATOM 1264 CG1 ILE A 186 28.176 46.976 29.104 1.00 32.29 C
ANISOU 1264 CG1 ILE A 186 3982 4156 4128 -71 83 127 C
ATOM 1265 CG2 ILE A 186 30.073 46.948 27.428 1.00 31.23 C
ANISOU 1265 CG2 ILE A 186 3855 4009 3999 -72 81 147 C
ATOM 1266 CD1 ILE A 186 28.239 45.585 29.694 1.00 31.84 C
ANISOU 1266 CD1 ILE A 186 3923 4113 4060 -76 83 132 C
ATOM 1267 N GLN A 187 29.266 49.420 25.210 1.00 33.73 N
ANISOU 1267 N GLN A 187 4182 4294 4337 -62 74 147 N
ATOM 1268 CA GLN A 187 29.635 49.581 23.824 1.00 35.13 C
ANISOU 1268 CA GLN A 187 4368 4462 4516 -62 73 158 C
ATOM 1269 C GLN A 187 31.041 49.099 23.560 1.00 34.99 C
ANISOU 1269 C GLN A 187 4353 4447 4495 -68 78 166 C
ATOM 1270 O GLN A 187 31.415 48.872 22.407 1.00 35.07 O
ANISOU 1270 O GLN A 187 4368 4451 4502 -69 80 175 O
ATOM 1271 CB GLN A 187 29.482 51.033 23.395 1.00 36.84 C
ANISOU 1271 CB GLN A 187 4588 4665 4744 -61 67 157 C
ATOM 1272 CG GLN A 187 28.068 51.555 23.554 1.00 38.99 C
ANISOU 1272 CG GLN A 187 4857 4932 5025 -54 62 149 C
ATOM 1273 CD GLN A 187 27.950 52.982 23.097 1.00 41.07 C
ANISOU 1273 CD GLN A 187 5122 5179 5302 -53 54 148 C
ATOM 1274 OE1 GLN A 187 28.014 53.264 21.895 1.00 42.06 O
ANISOU 1274 OE1 GLN A 187 5255 5295 5430 -55 49 159 O
ATOM 1275 NE2 GLN A 187 27.789 53.901 24.053 1.00 40.82 N
ANISOU 1275 NE2 GLN A 187 5083 5145 5281 -52 54 135 N
ATOM 1276 N THR A 188 31.820 48.948 24.627 1.00 35.46 N
ANISOU 1276 N THR A 188 4406 4513 4553 -72 80 163 N
ATOM 1277 CA THR A 188 33.229 48.618 24.479 1.00 36.73 C
ANISOU 1277 CA THR A 188 4566 4674 4715 -77 84 169 C
ATOM 1278 C THR A 188 33.734 47.633 25.532 1.00 36.79 C
ANISOU 1278 C THR A 188 4567 4693 4719 -81 85 169 C
ATOM 1279 O THR A 188 33.276 47.626 26.677 1.00 37.04 O
ANISOU 1279 O THR A 188 4594 4731 4746 -82 82 161 O
ATOM 1280 CB THR A 188 34.130 49.876 24.508 1.00 37.39 C
ANISOU 1280 CB THR A 188 4651 4748 4807 -81 83 168 C
ATOM 1281 OG1 THR A 188 34.471 50.179 25.863 1.00 40.25 O
ANISOU 1281 OG1 THR A 188 5007 5115 5170 -84 80 161 O
ATOM 1282 CG2 THR A 188 33.458 51.105 23.850 1.00 35.29 C
ANISOU 1282 CG2 THR A 188 4390 4470 4546 -78 78 167 C
ATOM 1283 N ILE A 189 34.683 46.798 25.119 1.00 36.76 N
ANISOU 1283 N ILE A 189 4560 4688 4716 -85 89 177 N
ATOM 1284 CA ILE A 189 35.409 45.928 26.036 1.00 35.45 C
ANISOU 1284 CA ILE A 189 4387 4530 4551 -90 88 179 C
ATOM 1285 C ILE A 189 36.892 46.282 25.900 1.00 34.76 C
ANISOU 1285 C ILE A 189 4297 4436 4473 -95 89 183 C
ATOM 1286 O ILE A 189 37.476 46.117 24.827 1.00 32.80 O
ANISOU 1286 O ILE A 189 4051 4181 4231 -95 96 188 O
ATOM 1287 CB ILE A 189 35.154 44.439 25.720 1.00 35.08 C
ANISOU 1287 CB ILE A 189 4337 4490 4501 -88 90 184 C
ATOM 1288 CG1 ILE A 189 33.650 44.139 25.782 1.00 34.16 C
ANISOU 1288 CG1 ILE A 189 4224 4380 4376 -83 89 180 C
ATOM 1289 CG2 ILE A 189 35.939 43.546 26.679 1.00 34.43 C
ANISOU 1289 CG2 ILE A 189 4245 4413 4421 -94 87 188 C
ATOM 1290 CD1 ILE A 189 33.247 42.819 25.159 1.00 33.53 C
ANISOU 1290 CD1 ILE A 189 4143 4303 4293 -80 91 185 C
ATOM 1291 N THR A 190 37.477 46.785 26.987 1.00 34.76 N
ANISOU 1291 N THR A 190 4293 4437 4477 -100 84 180 N
ATOM 1292 CA THR A 190 38.848 47.313 26.987 1.00 35.97 C
ANISOU 1292 CA THR A 190 4443 4582 4640 -105 84 183 C
ATOM 1293 C THR A 190 39.785 46.310 27.653 1.00 36.76 C
ANISOU 1293 C THR A 190 4534 4685 4747 -111 80 189 C
ATOM 1294 O THR A 190 39.309 45.393 28.322 1.00 36.46 O
ANISOU 1294 O THR A 190 4492 4657 4702 -112 76 189 O
ATOM 1295 CB THR A 190 38.930 48.635 27.777 1.00 35.90 C
ANISOU 1295 CB THR A 190 4435 4570 4632 -107 78 176 C
ATOM 1296 OG1 THR A 190 38.858 48.345 29.174 1.00 37.07 O
ANISOU 1296 OG1 THR A 190 4580 4729 4775 -112 71 172 O
ATOM 1297 CG2 THR A 190 37.792 49.583 27.418 1.00 35.95 C
ANISOU 1297 CG2 THR A 190 4450 4575 4635 -101 79 168 C
ATOM 1298 N VAL A 191 41.105 46.476 27.504 1.00 38.02 N
ANISOU 1298 N VAL A 191 4687 4836 4919 -116 81 193 N
ATOM 1299 CA VAL A 191 42.030 45.568 28.212 1.00 39.35 C
ANISOU 1299 CA VAL A 191 4846 5007 5098 -122 76 199 C
ATOM 1300 C VAL A 191 41.983 45.750 29.734 1.00 41.05 C
ANISOU 1300 C VAL A 191 5060 5230 5307 -128 62 197 C
ATOM 1301 O VAL A 191 42.178 44.784 30.472 1.00 43.38 O
ANISOU 1301 O VAL A 191 5348 5529 5602 -133 55 202 O
ATOM 1302 CB VAL A 191 43.503 45.516 27.677 1.00 38.16 C
ANISOU 1302 CB VAL A 191 4687 4844 4967 -126 80 205 C
ATOM 1303 CG1 VAL A 191 43.647 46.130 26.290 1.00 37.24 C
ANISOU 1303 CG1 VAL A 191 4576 4719 4854 -123 93 204 C
ATOM 1304 CG2 VAL A 191 44.492 46.120 28.661 1.00 36.63 C
ANISOU 1304 CG2 VAL A 191 4488 4646 4782 -133 70 206 C
ATOM 1305 N ASN A 192 41.706 46.961 30.211 1.00 42.85 N
ANISOU 1305 N ASN A 192 5294 5457 5528 -129 59 189 N
ATOM 1306 CA ASN A 192 41.551 47.137 31.658 1.00 46.13 C
ANISOU 1306 CA ASN A 192 5710 5881 5935 -136 48 185 C
ATOM 1307 C ASN A 192 40.170 46.750 32.206 1.00 46.44 C
ANISOU 1307 C ASN A 192 5755 5934 5957 -135 48 179 C
ATOM 1308 O ASN A 192 40.015 46.592 33.424 1.00 46.67 O
ANISOU 1308 O ASN A 192 5784 5972 5976 -143 40 177 O
ATOM 1309 CB ASN A 192 42.015 48.524 32.141 1.00 49.91 C
ANISOU 1309 CB ASN A 192 6191 6354 6415 -140 44 178 C
ATOM 1310 CG ASN A 192 43.543 48.611 32.299 1.00 56.51 C
ANISOU 1310 CG ASN A 192 7020 7181 7267 -147 38 186 C
ATOM 1311 OD1 ASN A 192 44.157 47.826 33.043 1.00 56.56 O
ANISOU 1311 OD1 ASN A 192 7021 7191 7278 -155 29 193 O
ATOM 1312 ND2 ASN A 192 44.165 49.567 31.593 1.00 55.46 N
ANISOU 1312 ND2 ASN A 192 6887 7036 7146 -145 43 185 N
ATOM 1313 N ASP A 193 39.189 46.563 31.312 1.00 44.71 N
ANISOU 1313 N ASP A 193 5538 5715 5733 -126 57 177 N
ATOM 1314 CA ASP A 193 37.875 46.013 31.698 1.00 45.38 C
ANISOU 1314 CA ASP A 193 5626 5812 5804 -124 57 172 C
ATOM 1315 C ASP A 193 38.011 44.569 32.176 1.00 44.10 C
ANISOU 1315 C ASP A 193 5459 5658 5640 -128 52 181 C
ATOM 1316 O ASP A 193 37.306 44.137 33.088 1.00 44.88 O
ANISOU 1316 O ASP A 193 5558 5767 5725 -133 48 178 O
ATOM 1317 CB ASP A 193 36.862 46.063 30.540 1.00 45.19 C
ANISOU 1317 CB ASP A 193 5606 5784 5778 -113 66 170 C
ATOM 1318 CG ASP A 193 36.202 47.426 30.379 1.00 45.36 C
ANISOU 1318 CG ASP A 193 5633 5801 5799 -108 69 159 C
ATOM 1319 OD1 ASP A 193 36.280 48.258 31.309 1.00 45.76 O
ANISOU 1319 OD1 ASP A 193 5684 5852 5847 -113 65 151 O
ATOM 1320 OD2 ASP A 193 35.604 47.667 29.306 1.00 45.84 O
ANISOU 1320 OD2 ASP A 193 5697 5855 5862 -101 74 159 O
ATOM 1321 N LEU A 194 38.925 43.833 31.554 1.00 41.04 N
ANISOU 1321 N LEU A 194 5065 5263 5265 -128 53 191 N
ATOM 1322 CA LEU A 194 39.116 42.426 31.862 1.00 42.08 C
ANISOU 1322 CA LEU A 194 5188 5399 5398 -132 47 200 C
ATOM 1323 C LEU A 194 40.356 42.122 32.720 1.00 44.41 C
ANISOU 1323 C LEU A 194 5477 5693 5704 -143 35 209 C
ATOM 1324 O LEU A 194 40.761 40.966 32.834 1.00 45.05 O
ANISOU 1324 O LEU A 194 5550 5774 5793 -146 30 218 O
ATOM 1325 CB LEU A 194 39.127 41.613 30.564 1.00 39.53 C
ANISOU 1325 CB LEU A 194 4862 5071 5085 -124 56 205 C
ATOM 1326 CG LEU A 194 37.836 41.634 29.740 1.00 37.65 C
ANISOU 1326 CG LEU A 194 4631 4835 4837 -115 65 200 C
ATOM 1327 CD1 LEU A 194 37.971 40.695 28.561 1.00 36.25 C
ANISOU 1327 CD1 LEU A 194 4451 4653 4668 -110 73 205 C
ATOM 1328 CD2 LEU A 194 36.607 41.267 30.564 1.00 37.86 C
ANISOU 1328 CD2 LEU A 194 4660 4874 4848 -116 61 196 C
ATOM 1329 N GLN A 195 40.930 43.156 33.336 1.00 46.85 N
ANISOU 1329 N GLN A 195 5788 5998 6013 -149 30 205 N
ATOM 1330 CA GLN A 195 42.149 43.031 34.133 1.00 48.58 C
ANISOU 1330 CA GLN A 195 6000 6214 6242 -160 17 213 C
ATOM 1331 C GLN A 195 42.002 42.031 35.279 1.00 48.35 C
ANISOU 1331 C GLN A 195 5969 6195 6205 -170 3 220 C
ATOM 1332 O GLN A 195 42.926 41.265 35.549 1.00 47.68 O
ANISOU 1332 O GLN A 195 5875 6105 6134 -177 -6 232 O
ATOM 1333 CB GLN A 195 42.575 44.395 34.686 1.00 55.64 C
ANISOU 1333 CB GLN A 195 6900 7105 7134 -165 13 206 C
ATOM 1334 CG GLN A 195 44.027 44.467 35.149 1.00 64.33 C
ANISOU 1334 CG GLN A 195 7993 8197 8251 -174 1 214 C
ATOM 1335 CD GLN A 195 44.317 45.690 36.015 1.00 74.69 C
ANISOU 1335 CD GLN A 195 9311 9509 9556 -181 -5 207 C
ATOM 1336 OE1 GLN A 195 43.978 45.728 37.206 1.00 77.15 O
ANISOU 1336 OE1 GLN A 195 9629 9831 9852 -192 -15 204 O
ATOM 1337 NE2 GLN A 195 44.965 46.694 35.420 1.00 74.54 N
ANISOU 1337 NE2 GLN A 195 9291 9479 9550 -177 0 204 N
ATOM 1338 N PHE A 196 40.852 42.031 35.952 1.00 46.95 N
ANISOU 1338 N PHE A 196 5800 6031 6006 -173 3 214 N
ATOM 1339 CA PHE A 196 40.627 41.074 37.029 1.00 45.41 C
ANISOU 1339 CA PHE A 196 5604 5847 5801 -184 -8 221 C
ATOM 1340 C PHE A 196 40.902 39.637 36.581 1.00 46.58 C
ANISOU 1340 C PHE A 196 5742 5991 5963 -182 -12 234 C
ATOM 1341 O PHE A 196 41.639 38.911 37.255 1.00 48.30 O
ANISOU 1341 O PHE A 196 5954 6208 6189 -193 -27 246 O
ATOM 1342 CB PHE A 196 39.227 41.202 37.624 1.00 44.42 C
ANISOU 1342 CB PHE A 196 5489 5737 5651 -186 -3 211 C
ATOM 1343 CG PHE A 196 38.821 40.022 38.462 1.00 45.39 C
ANISOU 1343 CG PHE A 196 5611 5870 5762 -196 -13 219 C
ATOM 1344 CD1 PHE A 196 39.440 39.770 39.679 1.00 45.78 C
ANISOU 1344 CD1 PHE A 196 5662 5925 5807 -213 -30 227 C
ATOM 1345 CD2 PHE A 196 37.820 39.153 38.027 1.00 46.28 C
ANISOU 1345 CD2 PHE A 196 5723 5989 5871 -189 -6 220 C
ATOM 1346 CE1 PHE A 196 39.074 38.669 40.443 1.00 46.68 C
ANISOU 1346 CE1 PHE A 196 5775 6049 5910 -224 -40 237 C
ATOM 1347 CE2 PHE A 196 37.442 38.057 38.789 1.00 44.80 C
ANISOU 1347 CE2 PHE A 196 5534 5812 5674 -198 -15 229 C
ATOM 1348 CZ PHE A 196 38.074 37.815 40.002 1.00 45.52 C
ANISOU 1348 CZ PHE A 196 5627 5908 5759 -216 -32 237 C
ATOM 1349 N LEU A 197 40.320 39.235 35.449 1.00 46.12 N
ANISOU 1349 N LEU A 197 5682 5931 5909 -169 1 232 N
ATOM 1350 CA LEU A 197 40.537 37.891 34.886 1.00 44.02 C
ANISOU 1350 CA LEU A 197 5405 5660 5657 -166 0 242 C
ATOM 1351 C LEU A 197 41.981 37.633 34.483 1.00 43.66 C
ANISOU 1351 C LEU A 197 5348 5600 5639 -167 -3 250 C
ATOM 1352 O LEU A 197 42.482 36.529 34.669 1.00 44.24 O
ANISOU 1352 O LEU A 197 5410 5669 5727 -171 -13 262 O
ATOM 1353 CB LEU A 197 39.624 37.639 33.686 1.00 42.97 C
ANISOU 1353 CB LEU A 197 5275 5528 5523 -152 16 236 C
ATOM 1354 CG LEU A 197 38.350 36.809 33.817 1.00 41.19 C
ANISOU 1354 CG LEU A 197 5052 5313 5283 -150 17 236 C
ATOM 1355 CD1 LEU A 197 37.702 36.917 35.186 1.00 41.17 C
ANISOU 1355 CD1 LEU A 197 5057 5326 5261 -161 8 235 C
ATOM 1356 CD2 LEU A 197 37.390 37.269 32.740 1.00 41.33 C
ANISOU 1356 CD2 LEU A 197 5077 5331 5295 -137 33 226 C
ATOM 1357 N ARG A 198 42.639 38.646 33.927 1.00 43.66 N
ANISOU 1357 N ARG A 198 5349 5591 5648 -163 3 245 N
ATOM 1358 CA ARG A 198 44.047 38.537 33.559 1.00 46.66 C
ANISOU 1358 CA ARG A 198 5716 5955 6055 -165 1 252 C
ATOM 1359 C ARG A 198 44.895 38.275 34.800 1.00 49.12 C
ANISOU 1359 C ARG A 198 6022 6266 6374 -179 -20 262 C
ATOM 1360 O ARG A 198 45.814 37.459 34.771 1.00 49.76 O
ANISOU 1360 O ARG A 198 6089 6337 6480 -182 -27 272 O
ATOM 1361 CB ARG A 198 44.522 39.809 32.858 1.00 44.26 C
ANISOU 1361 CB ARG A 198 5416 5643 5756 -160 12 244 C
ATOM 1362 CG ARG A 198 45.818 39.641 32.077 1.00 43.26 C
ANISOU 1362 CG ARG A 198 5278 5501 5659 -159 17 248 C
ATOM 1363 CD ARG A 198 46.046 40.784 31.100 1.00 42.69 C
ANISOU 1363 CD ARG A 198 5211 5421 5588 -153 32 240 C
ATOM 1364 NE ARG A 198 44.983 40.868 30.102 1.00 43.62 N
ANISOU 1364 NE ARG A 198 5337 5543 5691 -143 48 232 N
ATOM 1365 CZ ARG A 198 43.993 41.757 30.126 1.00 42.45 C
ANISOU 1365 CZ ARG A 198 5203 5403 5523 -139 51 224 C
ATOM 1366 NH1 ARG A 198 43.922 42.665 31.096 1.00 41.95 N
ANISOU 1366 NH1 ARG A 198 5145 5344 5449 -144 42 221 N
ATOM 1367 NH2 ARG A 198 43.074 41.736 29.174 1.00 41.51 N
ANISOU 1367 NH2 ARG A 198 5091 5286 5393 -131 63 219 N
ATOM 1368 N GLU A 199 44.549 38.974 35.879 1.00 53.53 N
ANISOU 1368 N GLU A 199 6591 6834 6912 -188 -29 259 N
ATOM 1369 CA GLU A 199 45.215 38.902 37.175 1.00 56.56 C
ANISOU 1369 CA GLU A 199 6973 7220 7297 -203 -51 268 C
ATOM 1370 C GLU A 199 45.082 37.515 37.790 1.00 57.87 C
ANISOU 1370 C GLU A 199 7132 7389 7464 -211 -65 281 C
ATOM 1371 O GLU A 199 46.070 36.938 38.229 1.00 58.48 O
ANISOU 1371 O GLU A 199 7198 7458 7561 -220 -82 294 O
ATOM 1372 CB GLU A 199 44.550 39.895 38.122 1.00 62.12 C
ANISOU 1372 CB GLU A 199 7692 7936 7972 -211 -53 259 C
ATOM 1373 CG GLU A 199 45.481 40.691 39.006 1.00 66.97 C
ANISOU 1373 CG GLU A 199 8308 8547 8588 -223 -68 261 C
ATOM 1374 CD GLU A 199 45.768 42.056 38.423 1.00 69.01 C
ANISOU 1374 CD GLU A 199 8571 8798 8851 -216 -56 249 C
ATOM 1375 OE1 GLU A 199 45.349 43.060 39.046 1.00 68.38 O
ANISOU 1375 OE1 GLU A 199 8502 8725 8752 -220 -56 239 O
ATOM 1376 OE2 GLU A 199 46.393 42.114 37.337 1.00 67.57 O
ANISOU 1376 OE2 GLU A 199 8379 8602 8690 -206 -46 250 O
ATOM 1377 N ASN A 200 43.848 37.002 37.819 1.00 57.78 N
ANISOU 1377 N ASN A 200 7128 7391 7433 -208 -59 278 N
ATOM 1378 CA ASN A 200 43.513 35.743 38.481 1.00 54.68 C
ANISOU 1378 CA ASN A 200 6732 7005 7037 -217 -73 290 C
ATOM 1379 C ASN A 200 43.076 34.660 37.487 1.00 54.93 C
ANISOU 1379 C ASN A 200 6756 7034 7081 -205 -62 292 C
ATOM 1380 O ASN A 200 41.877 34.371 37.370 1.00 53.78 O
ANISOU 1380 O ASN A 200 6617 6900 6917 -200 -54 287 O
ATOM 1381 CB ASN A 200 42.394 35.954 39.507 1.00 54.19 C
ANISOU 1381 CB ASN A 200 6685 6963 6941 -226 -75 285 C
ATOM 1382 CG ASN A 200 42.691 37.071 40.495 1.00 57.79 C
ANISOU 1382 CG ASN A 200 7151 7423 7381 -239 -83 280 C
ATOM 1383 OD1 ASN A 200 43.060 36.813 41.642 1.00 57.31 O
ANISOU 1383 OD1 ASN A 200 7093 7366 7314 -256 -103 290 O
ATOM 1384 ND2 ASN A 200 42.508 38.321 40.061 1.00 55.53 N
ANISOU 1384 ND2 ASN A 200 6872 7136 7090 -230 -69 265 N
ATOM 1385 N PRO A 201 44.043 34.033 36.787 1.00 54.32 N
ANISOU 1385 N PRO A 201 6662 6941 7035 -201 -63 299 N
ATOM 1386 CA PRO A 201 43.691 33.057 35.744 1.00 55.03 C
ANISOU 1386 CA PRO A 201 6744 7026 7137 -189 -51 299 C
ATOM 1387 C PRO A 201 43.078 31.757 36.279 1.00 54.52 C
ANISOU 1387 C PRO A 201 6676 6969 7069 -195 -63 309 C
ATOM 1388 O PRO A 201 42.766 30.858 35.502 1.00 56.66 O
ANISOU 1388 O PRO A 201 6940 7237 7351 -186 -55 309 O
ATOM 1389 CB PRO A 201 45.037 32.775 35.042 1.00 53.80 C
ANISOU 1389 CB PRO A 201 6571 6850 7018 -186 -50 303 C
ATOM 1390 CG PRO A 201 46.005 33.788 35.575 1.00 53.94 C
ANISOU 1390 CG PRO A 201 6589 6862 7041 -194 -58 304 C
ATOM 1391 CD PRO A 201 45.503 34.155 36.940 1.00 53.96 C
ANISOU 1391 CD PRO A 201 6605 6880 7017 -207 -74 307 C
ATOM 1392 N GLN A 202 42.891 31.668 37.590 1.00 57.08 N
ANISOU 1392 N GLN A 202 7006 7303 7377 -209 -81 317 N
ATOM 1393 CA GLN A 202 42.334 30.465 38.215 1.00 58.25 C
ANISOU 1393 CA GLN A 202 7152 7459 7521 -217 -94 329 C
ATOM 1394 C GLN A 202 40.810 30.536 38.406 1.00 57.09 C
ANISOU 1394 C GLN A 202 7019 7330 7340 -215 -84 321 C
ATOM 1395 O GLN A 202 40.205 29.620 38.966 1.00 59.30 O
ANISOU 1395 O GLN A 202 7299 7619 7612 -222 -93 329 O
ATOM 1396 CB GLN A 202 43.027 30.200 39.560 1.00 59.94 C
ANISOU 1396 CB GLN A 202 7363 7672 7735 -237 -122 345 C
ATOM 1397 CG GLN A 202 42.476 31.008 40.743 1.00 62.30 C
ANISOU 1397 CG GLN A 202 7682 7990 8000 -251 -128 342 C
ATOM 1398 CD GLN A 202 42.975 32.449 40.819 1.00 61.17 C
ANISOU 1398 CD GLN A 202 7546 7845 7851 -251 -123 331 C
ATOM 1399 OE1 GLN A 202 43.792 32.894 40.009 1.00 59.74 O
ANISOU 1399 OE1 GLN A 202 7357 7649 7692 -241 -115 327 O
ATOM 1400 NE2 GLN A 202 42.486 33.183 41.815 1.00 60.22 N
ANISOU 1400 NE2 GLN A 202 7441 7738 7699 -263 -126 326 N
ATOM 1401 N VAL A 203 40.194 31.617 37.937 1.00 54.92 N
ANISOU 1401 N VAL A 203 6756 7061 7050 -206 -66 304 N
ATOM 1402 CA VAL A 203 38.766 31.855 38.174 1.00 51.44 C
ANISOU 1402 CA VAL A 203 6327 6636 6579 -204 -56 295 C
ATOM 1403 C VAL A 203 37.875 31.270 37.081 1.00 47.20 C
ANISOU 1403 C VAL A 203 5788 6099 6045 -189 -41 290 C
ATOM 1404 O VAL A 203 38.082 31.523 35.896 1.00 45.16 O
ANISOU 1404 O VAL A 203 5527 5831 5800 -176 -27 283 O
ATOM 1405 CB VAL A 203 38.467 33.363 38.366 1.00 50.84 C
ANISOU 1405 CB VAL A 203 6264 6566 6484 -204 -46 280 C
ATOM 1406 CG1 VAL A 203 36.990 33.606 38.637 1.00 49.62 C
ANISOU 1406 CG1 VAL A 203 6122 6428 6304 -202 -36 269 C
ATOM 1407 CG2 VAL A 203 39.298 33.920 39.507 1.00 51.64 C
ANISOU 1407 CG2 VAL A 203 6369 6669 6581 -220 -62 284 C
ATOM 1408 N ASN A 204 36.888 30.482 37.502 1.00 46.01 N
ANISOU 1408 N ASN A 204 5640 5960 5881 -193 -43 293 N
ATOM 1409 CA ASN A 204 35.874 29.964 36.600 1.00 45.62 C
ANISOU 1409 CA ASN A 204 5589 5912 5830 -180 -30 288 C
ATOM 1410 C ASN A 204 34.763 30.994 36.433 1.00 44.60 C
ANISOU 1410 C ASN A 204 5473 5792 5679 -173 -15 272 C
ATOM 1411 O ASN A 204 33.876 31.098 37.281 1.00 46.83 O
ANISOU 1411 O ASN A 204 5763 6088 5941 -180 -15 269 O
ATOM 1412 CB ASN A 204 35.274 28.656 37.134 1.00 47.63 C
ANISOU 1412 CB ASN A 204 5840 6174 6081 -186 -40 299 C
ATOM 1413 CG ASN A 204 34.648 27.820 36.039 1.00 48.47 C
ANISOU 1413 CG ASN A 204 5941 6277 6198 -173 -30 297 C
ATOM 1414 OD1 ASN A 204 34.722 28.184 34.871 1.00 49.50 O
ANISOU 1414 OD1 ASN A 204 6071 6399 6338 -159 -16 288 O
ATOM 1415 ND2 ASN A 204 34.025 26.702 36.402 1.00 52.51 N
ANISOU 1415 ND2 ASN A 204 6449 6794 6706 -177 -37 306 N
ATOM 1416 N LEU A 205 34.804 31.765 35.353 1.00 40.63 N
ANISOU 1416 N LEU A 205 4972 5282 5183 -160 -1 261 N
ATOM 1417 CA LEU A 205 33.750 32.747 35.122 1.00 37.88 C
ANISOU 1417 CA LEU A 205 4634 4940 4818 -153 11 247 C
ATOM 1418 C LEU A 205 33.045 32.571 33.779 1.00 36.74 C
ANISOU 1418 C LEU A 205 4490 4790 4679 -138 24 241 C
ATOM 1419 O LEU A 205 33.680 32.316 32.748 1.00 35.06 O
ANISOU 1419 O LEU A 205 4271 4565 4482 -130 28 243 O
ATOM 1420 CB LEU A 205 34.273 34.182 35.300 1.00 35.82 C
ANISOU 1420 CB LEU A 205 4380 4676 4554 -154 14 238 C
ATOM 1421 CG LEU A 205 33.260 35.332 35.385 1.00 33.62 C
ANISOU 1421 CG LEU A 205 4111 4403 4259 -151 25 223 C
ATOM 1422 CD1 LEU A 205 32.269 35.156 36.517 1.00 33.77 C
ANISOU 1422 CD1 LEU A 205 4135 4437 4258 -160 23 219 C
ATOM 1423 CD2 LEU A 205 33.977 36.654 35.541 1.00 34.28 C
ANISOU 1423 CD2 LEU A 205 4199 4481 4344 -153 25 216 C
ATOM 1424 N SER A 206 31.720 32.679 33.829 1.00 36.34 N
ANISOU 1424 N SER A 206 4445 4748 4614 -134 31 234 N
ATOM 1425 CA SER A 206 30.903 32.785 32.635 1.00 38.27 C
ANISOU 1425 CA SER A 206 4692 4989 4860 -120 42 227 C
ATOM 1426 C SER A 206 30.310 34.182 32.560 1.00 38.81 C
ANISOU 1426 C SER A 206 4768 5057 4919 -116 50 214 C
ATOM 1427 O SER A 206 29.865 34.750 33.572 1.00 39.97 O
ANISOU 1427 O SER A 206 4919 5213 5053 -123 50 207 O
ATOM 1428 CB SER A 206 29.799 31.728 32.614 1.00 38.95 C
ANISOU 1428 CB SER A 206 4776 5082 4941 -118 42 230 C
ATOM 1429 OG SER A 206 30.337 30.480 32.240 1.00 39.64 O
ANISOU 1429 OG SER A 206 4854 5164 5042 -118 37 240 O
ATOM 1430 N LEU A 207 30.291 34.718 31.348 1.00 37.72 N
ANISOU 1430 N LEU A 207 4633 4910 4788 -105 58 209 N
ATOM 1431 CA LEU A 207 29.920 36.101 31.123 1.00 37.24 C
ANISOU 1431 CA LEU A 207 4580 4846 4724 -101 64 198 C
ATOM 1432 C LEU A 207 28.874 36.133 30.021 1.00 34.98 C
ANISOU 1432 C LEU A 207 4296 4556 4438 -90 71 194 C
ATOM 1433 O LEU A 207 29.145 35.699 28.911 1.00 34.30 O
ANISOU 1433 O LEU A 207 4210 4462 4360 -84 73 198 O
ATOM 1434 CB LEU A 207 31.178 36.866 30.703 1.00 38.29 C
ANISOU 1434 CB LEU A 207 4713 4969 4866 -101 65 199 C
ATOM 1435 CG LEU A 207 31.593 38.224 31.270 1.00 38.50 C
ANISOU 1435 CG LEU A 207 4744 4994 4890 -105 64 191 C
ATOM 1436 CD1 LEU A 207 31.531 38.283 32.793 1.00 39.24 C
ANISOU 1436 CD1 LEU A 207 4838 5099 4973 -117 58 189 C
ATOM 1437 CD2 LEU A 207 32.993 38.541 30.760 1.00 36.94 C
ANISOU 1437 CD2 LEU A 207 4545 4786 4704 -106 64 196 C
ATOM 1438 N ASP A 208 27.668 36.597 30.340 1.00 35.02 N
ANISOU 1438 N ASP A 208 4303 4565 4435 -87 73 185 N
ATOM 1439 CA ASP A 208 26.632 36.771 29.327 1.00 35.24 C
ANISOU 1439 CA ASP A 208 4334 4588 4465 -77 78 181 C
ATOM 1440 C ASP A 208 26.570 38.234 28.911 1.00 35.10 C
ANISOU 1440 C ASP A 208 4322 4561 4451 -73 80 173 C
ATOM 1441 O ASP A 208 26.176 39.106 29.690 1.00 34.53 O
ANISOU 1441 O ASP A 208 4250 4492 4376 -75 82 164 O
ATOM 1442 CB ASP A 208 25.266 36.265 29.812 1.00 36.10 C
ANISOU 1442 CB ASP A 208 4441 4705 4568 -76 78 178 C
ATOM 1443 CG ASP A 208 24.197 36.256 28.699 1.00 37.49 C
ANISOU 1443 CG ASP A 208 4619 4875 4749 -66 80 176 C
ATOM 1444 OD1 ASP A 208 24.407 36.862 27.615 1.00 36.55 O
ANISOU 1444 OD1 ASP A 208 4505 4746 4636 -60 81 176 O
ATOM 1445 OD2 ASP A 208 23.124 35.643 28.917 1.00 37.73 O
ANISOU 1445 OD2 ASP A 208 4646 4911 4778 -64 81 175 O
ATOM 1446 N MET A 209 26.965 38.478 27.667 1.00 35.91 N
ANISOU 1446 N MET A 209 4429 4654 4561 -68 82 177 N
ATOM 1447 CA MET A 209 27.150 39.820 27.144 1.00 37.45 C
ANISOU 1447 CA MET A 209 4630 4839 4760 -65 83 172 C
ATOM 1448 C MET A 209 26.114 40.171 26.082 1.00 36.73 C
ANISOU 1448 C MET A 209 4543 4740 4672 -57 83 170 C
ATOM 1449 O MET A 209 26.273 41.157 25.363 1.00 39.81 O
ANISOU 1449 O MET A 209 4938 5120 5066 -55 82 170 O
ATOM 1450 CB MET A 209 28.561 39.938 26.546 1.00 40.22 C
ANISOU 1450 CB MET A 209 4982 5183 5115 -68 84 178 C
ATOM 1451 CG MET A 209 29.282 41.229 26.902 1.00 45.64 C
ANISOU 1451 CG MET A 209 5671 5865 5805 -71 84 174 C
ATOM 1452 SD MET A 209 29.617 41.256 28.674 1.00 48.85 S
ANISOU 1452 SD MET A 209 6072 6282 6206 -80 81 169 S
ATOM 1453 CE MET A 209 30.294 39.610 28.802 1.00 46.10 C
ANISOU 1453 CE MET A 209 5717 5939 5857 -84 78 181 C
ATOM 1454 N SER A 210 25.057 39.371 25.987 1.00 34.90 N
ANISOU 1454 N SER A 210 4308 4512 4438 -54 82 171 N
ATOM 1455 CA SER A 210 24.014 39.547 24.972 1.00 33.84 C
ANISOU 1455 CA SER A 210 4178 4371 4307 -47 80 171 C
ATOM 1456 C SER A 210 23.329 40.900 24.997 1.00 33.42 C
ANISOU 1456 C SER A 210 4126 4309 4260 -43 78 163 C
ATOM 1457 O SER A 210 23.288 41.566 26.025 1.00 34.84 O
ANISOU 1457 O SER A 210 4302 4493 4442 -45 80 154 O
ATOM 1458 CB SER A 210 22.939 38.477 25.131 1.00 32.56 C
ANISOU 1458 CB SER A 210 4011 4215 4142 -44 79 172 C
ATOM 1459 OG SER A 210 23.504 37.201 24.981 1.00 32.17 O
ANISOU 1459 OG SER A 210 3961 4171 4089 -47 79 180 O
ATOM 1460 N LEU A 211 22.773 41.282 23.851 1.00 33.14 N
ANISOU 1460 N LEU A 211 4096 4263 4230 -38 73 166 N
ATOM 1461 CA LEU A 211 21.940 42.471 23.729 1.00 32.12 C
ANISOU 1461 CA LEU A 211 3967 4125 4111 -34 69 159 C
ATOM 1462 C LEU A 211 22.645 43.718 24.258 1.00 32.06 C
ANISOU 1462 C LEU A 211 3959 4113 4108 -37 71 153 C
ATOM 1463 O LEU A 211 22.034 44.593 24.856 1.00 34.07 O
ANISOU 1463 O LEU A 211 4208 4364 4370 -35 71 143 O
ATOM 1464 CB LEU A 211 20.572 42.261 24.401 1.00 32.06 C
ANISOU 1464 CB LEU A 211 3950 4120 4108 -30 69 151 C
ATOM 1465 CG LEU A 211 19.353 41.587 23.723 1.00 31.19 C
ANISOU 1465 CG LEU A 211 3839 4007 4002 -25 64 155 C
ATOM 1466 CD1 LEU A 211 19.310 41.759 22.215 1.00 30.79 C
ANISOU 1466 CD1 LEU A 211 3798 3945 3954 -23 56 165 C
ATOM 1467 CD2 LEU A 211 19.239 40.122 24.084 1.00 30.70 C
ANISOU 1467 CD2 LEU A 211 3774 3958 3931 -26 68 158 C
ATOM 1468 N ASN A 212 23.948 43.773 24.034 1.00 31.90 N
ANISOU 1468 N ASN A 212 3944 4093 4083 -42 73 158 N
ATOM 1469 CA ASN A 212 24.742 44.961 24.299 1.00 31.80 C
ANISOU 1469 CA ASN A 212 3932 4074 4075 -44 73 155 C
ATOM 1470 C ASN A 212 25.275 45.529 22.979 1.00 30.97 C
ANISOU 1470 C ASN A 212 3836 3957 3972 -45 70 163 C
ATOM 1471 O ASN A 212 25.845 44.795 22.174 1.00 29.73 O
ANISOU 1471 O ASN A 212 3685 3801 3809 -47 72 173 O
ATOM 1472 CB ASN A 212 25.886 44.625 25.260 1.00 31.88 C
ANISOU 1472 CB ASN A 212 3939 4094 4078 -51 78 154 C
ATOM 1473 CG ASN A 212 25.487 44.777 26.719 1.00 31.53 C
ANISOU 1473 CG ASN A 212 3888 4059 4032 -53 81 142 C
ATOM 1474 OD1 ASN A 212 25.456 45.881 27.253 1.00 31.71 O
ANISOU 1474 OD1 ASN A 212 3909 4077 4060 -54 81 133 O
ATOM 1475 ND2 ASN A 212 25.196 43.665 27.371 1.00 31.75 N
ANISOU 1475 ND2 ASN A 212 3912 4099 4052 -56 83 143 N
ATOM 1476 N PRO A 213 25.082 46.839 22.741 1.00 31.51 N
ANISOU 1476 N PRO A 213 3907 4014 4051 -44 65 160 N
ATOM 1477 CA PRO A 213 25.501 47.416 21.459 1.00 31.57 C
ANISOU 1477 CA PRO A 213 3925 4010 4060 -46 60 170 C
ATOM 1478 C PRO A 213 27.031 47.561 21.365 1.00 32.46 C
ANISOU 1478 C PRO A 213 4041 4123 4168 -52 66 174 C
ATOM 1479 O PRO A 213 27.559 48.670 21.419 1.00 34.10 O
ANISOU 1479 O PRO A 213 4250 4323 4383 -54 65 173 O
ATOM 1480 CB PRO A 213 24.807 48.775 21.454 1.00 30.26 C
ANISOU 1480 CB PRO A 213 3757 3831 3909 -42 53 165 C
ATOM 1481 CG PRO A 213 24.711 49.143 22.886 1.00 30.88 C
ANISOU 1481 CG PRO A 213 3824 3915 3991 -41 57 151 C
ATOM 1482 CD PRO A 213 24.562 47.866 23.665 1.00 31.44 C
ANISOU 1482 CD PRO A 213 3890 4001 4052 -41 64 148 C
ATOM 1483 N ILE A 214 27.729 46.440 21.241 1.00 32.66 N
ANISOU 1483 N ILE A 214 4067 4156 4184 -55 73 179 N
ATOM 1484 CA ILE A 214 29.182 46.444 21.259 1.00 34.75 C
ANISOU 1484 CA ILE A 214 4332 4422 4448 -61 79 182 C
ATOM 1485 C ILE A 214 29.647 46.861 19.881 1.00 36.12 C
ANISOU 1485 C ILE A 214 4516 4585 4620 -65 79 191 C
ATOM 1486 O ILE A 214 29.235 46.274 18.877 1.00 37.69 O
ANISOU 1486 O ILE A 214 4723 4784 4814 -66 79 196 O
ATOM 1487 CB ILE A 214 29.769 45.053 21.617 1.00 34.48 C
ANISOU 1487 CB ILE A 214 4293 4399 4408 -63 86 184 C
ATOM 1488 CG1 ILE A 214 29.366 44.633 23.025 1.00 33.96 C
ANISOU 1488 CG1 ILE A 214 4218 4343 4341 -62 84 177 C
ATOM 1489 CG2 ILE A 214 31.289 45.063 21.545 1.00 34.16 C
ANISOU 1489 CG2 ILE A 214 4253 4357 4370 -70 92 188 C
ATOM 1490 CD1 ILE A 214 29.845 43.243 23.379 1.00 35.32 C
ANISOU 1490 CD1 ILE A 214 4385 4525 4510 -64 88 181 C
ATOM 1491 N ASP A 215 30.490 47.882 19.823 1.00 36.53 N
ANISOU 1491 N ASP A 215 4571 4631 4678 -69 80 191 N
ATOM 1492 CA ASP A 215 30.989 48.328 18.538 1.00 38.40 C
ANISOU 1492 CA ASP A 215 4818 4858 4912 -75 81 200 C
ATOM 1493 C ASP A 215 32.513 48.385 18.511 1.00 38.72 C
ANISOU 1493 C ASP A 215 4858 4898 4954 -82 90 202 C
ATOM 1494 O ASP A 215 33.101 48.736 17.489 1.00 39.75 O
ANISOU 1494 O ASP A 215 4997 5021 5082 -88 94 208 O
ATOM 1495 CB ASP A 215 30.344 49.663 18.137 1.00 40.67 C
ANISOU 1495 CB ASP A 215 5112 5134 5207 -74 70 201 C
ATOM 1496 CG ASP A 215 30.868 50.847 18.939 1.00 42.12 C
ANISOU 1496 CG ASP A 215 5289 5312 5401 -74 68 196 C
ATOM 1497 OD1 ASP A 215 32.100 51.031 18.996 1.00 41.50 O
ANISOU 1497 OD1 ASP A 215 5210 5233 5322 -79 75 197 O
ATOM 1498 OD2 ASP A 215 30.043 51.613 19.491 1.00 44.40 O
ANISOU 1498 OD2 ASP A 215 5573 5596 5698 -69 60 189 O
ATOM 1499 N PHE A 216 33.139 48.012 19.629 1.00 37.31 N
ANISOU 1499 N PHE A 216 4669 4727 4779 -81 94 196 N
ATOM 1500 CA PHE A 216 34.583 48.134 19.787 1.00 35.75 C
ANISOU 1500 CA PHE A 216 4469 4528 4587 -87 101 198 C
ATOM 1501 C PHE A 216 35.129 47.275 20.939 1.00 34.55 C
ANISOU 1501 C PHE A 216 4304 4384 4436 -86 103 194 C
ATOM 1502 O PHE A 216 34.744 47.442 22.095 1.00 33.32 O
ANISOU 1502 O PHE A 216 4143 4234 4283 -84 97 188 O
ATOM 1503 CB PHE A 216 34.942 49.624 19.941 1.00 35.15 C
ANISOU 1503 CB PHE A 216 4393 4442 4517 -88 96 197 C
ATOM 1504 CG PHE A 216 36.317 49.891 20.497 1.00 34.88 C
ANISOU 1504 CG PHE A 216 4354 4407 4492 -93 101 196 C
ATOM 1505 CD1 PHE A 216 37.448 49.312 19.934 1.00 34.37 C
ANISOU 1505 CD1 PHE A 216 4288 4341 4429 -99 111 201 C
ATOM 1506 CD2 PHE A 216 36.477 50.766 21.566 1.00 33.85 C
ANISOU 1506 CD2 PHE A 216 4217 4275 4368 -92 95 190 C
ATOM 1507 CE1 PHE A 216 38.706 49.585 20.443 1.00 34.44 C
ANISOU 1507 CE1 PHE A 216 4290 4348 4448 -103 114 200 C
ATOM 1508 CE2 PHE A 216 37.729 51.038 22.080 1.00 33.79 C
ANISOU 1508 CE2 PHE A 216 4204 4266 4368 -97 97 190 C
ATOM 1509 CZ PHE A 216 38.847 50.451 21.515 1.00 34.62 C
ANISOU 1509 CZ PHE A 216 4307 4369 4476 -102 106 195 C
ATOM 1510 N ILE A 217 36.021 46.351 20.587 1.00 34.75 N
ANISOU 1510 N ILE A 217 4327 4412 4464 -90 112 198 N
ATOM 1511 CA ILE A 217 36.824 45.575 21.542 1.00 34.57 C
ANISOU 1511 CA ILE A 217 4293 4394 4447 -92 113 197 C
ATOM 1512 C ILE A 217 38.305 45.934 21.364 1.00 35.07 C
ANISOU 1512 C ILE A 217 4353 4450 4522 -99 119 199 C
ATOM 1513 O ILE A 217 38.885 45.712 20.295 1.00 35.58 O
ANISOU 1513 O ILE A 217 4420 4509 4588 -103 129 203 O
ATOM 1514 CB ILE A 217 36.639 44.050 21.354 1.00 33.90 C
ANISOU 1514 CB ILE A 217 4204 4316 4360 -91 117 199 C
ATOM 1515 CG1 ILE A 217 35.166 43.661 21.536 1.00 33.73 C
ANISOU 1515 CG1 ILE A 217 4184 4301 4328 -85 111 197 C
ATOM 1516 CG2 ILE A 217 37.548 43.279 22.310 1.00 33.65 C
ANISOU 1516 CG2 ILE A 217 4159 4287 4337 -94 116 200 C
ATOM 1517 CD1 ILE A 217 34.882 42.182 21.370 1.00 33.49 C
ANISOU 1517 CD1 ILE A 217 4151 4277 4296 -84 114 199 C
ATOM 1518 N GLN A 218 38.913 46.484 22.411 1.00 35.51 N
ANISOU 1518 N GLN A 218 4402 4506 4584 -100 114 197 N
ATOM 1519 CA GLN A 218 40.289 46.973 22.341 1.00 36.41 C
ANISOU 1519 CA GLN A 218 4512 4612 4711 -106 118 199 C
ATOM 1520 C GLN A 218 41.292 45.892 21.942 1.00 37.53 C
ANISOU 1520 C GLN A 218 4645 4751 4861 -110 127 203 C
ATOM 1521 O GLN A 218 41.069 44.707 22.161 1.00 36.18 O
ANISOU 1521 O GLN A 218 4469 4587 4691 -109 127 203 O
ATOM 1522 CB GLN A 218 40.697 47.632 23.660 1.00 37.31 C
ANISOU 1522 CB GLN A 218 4619 4726 4829 -108 108 196 C
ATOM 1523 CG GLN A 218 42.111 48.204 23.638 1.00 39.53 C
ANISOU 1523 CG GLN A 218 4896 4999 5125 -114 111 199 C
ATOM 1524 CD GLN A 218 42.447 49.087 24.830 1.00 39.27 C
ANISOU 1524 CD GLN A 218 4858 4965 5095 -116 100 195 C
ATOM 1525 OE1 GLN A 218 41.783 49.050 25.874 1.00 41.95 O
ANISOU 1525 OE1 GLN A 218 5197 5312 5427 -114 91 191 O
ATOM 1526 NE2 GLN A 218 43.494 49.884 24.680 1.00 37.92 N
ANISOU 1526 NE2 GLN A 218 4686 4785 4936 -120 102 197 N
ATOM 1527 N ASP A 219 42.398 46.318 21.345 1.00 41.03 N
ANISOU 1527 N ASP A 219 5088 5186 5316 -116 136 205 N
ATOM 1528 CA ASP A 219 43.417 45.394 20.886 1.00 43.71 C
ANISOU 1528 CA ASP A 219 5418 5521 5668 -120 147 207 C
ATOM 1529 C ASP A 219 44.047 44.720 22.093 1.00 44.54 C
ANISOU 1529 C ASP A 219 5508 5628 5786 -121 139 208 C
ATOM 1530 O ASP A 219 44.344 45.380 23.088 1.00 46.36 O
ANISOU 1530 O ASP A 219 5735 5859 6020 -122 128 208 O
ATOM 1531 CB ASP A 219 44.475 46.133 20.072 1.00 45.44 C
ANISOU 1531 CB ASP A 219 5638 5729 5895 -126 158 208 C
ATOM 1532 CG ASP A 219 45.305 45.204 19.221 1.00 47.94 C
ANISOU 1532 CG ASP A 219 5950 6041 6223 -131 174 207 C
ATOM 1533 OD1 ASP A 219 46.427 44.846 19.641 1.00 49.66 O
ANISOU 1533 OD1 ASP A 219 6153 6254 6461 -134 177 208 O
ATOM 1534 OD2 ASP A 219 44.826 44.821 18.134 1.00 50.78 O
ANISOU 1534 OD2 ASP A 219 6319 6403 6573 -133 185 206 O
ATOM 1535 N GLN A 220 44.221 43.404 22.004 1.00 44.96 N
ANISOU 1535 N GLN A 220 5553 5683 5846 -121 143 209 N
ATOM 1536 CA GLN A 220 44.793 42.597 23.088 1.00 46.58 C
ANISOU 1536 CA GLN A 220 5743 5889 6065 -122 133 212 C
ATOM 1537 C GLN A 220 43.919 42.507 24.351 1.00 43.23 C
ANISOU 1537 C GLN A 220 5320 5476 5629 -120 117 212 C
ATOM 1538 O GLN A 220 44.400 42.090 25.402 1.00 43.39 O
ANISOU 1538 O GLN A 220 5330 5497 5658 -123 106 216 O
ATOM 1539 CB GLN A 220 46.213 43.075 23.453 1.00 51.13 C
ANISOU 1539 CB GLN A 220 6308 6455 6661 -128 132 214 C
ATOM 1540 CG GLN A 220 47.307 42.674 22.471 1.00 57.25 C
ANISOU 1540 CG GLN A 220 7076 7219 7456 -132 149 213 C
ATOM 1541 CD GLN A 220 48.637 42.398 23.169 1.00 64.21 C
ANISOU 1541 CD GLN A 220 7940 8092 8365 -137 144 217 C
ATOM 1542 OE1 GLN A 220 49.464 43.295 23.348 1.00 68.45 O
ANISOU 1542 OE1 GLN A 220 8473 8621 8911 -141 143 218 O
ATOM 1543 NE2 GLN A 220 48.839 41.153 23.583 1.00 66.97 N
ANISOU 1543 NE2 GLN A 220 8276 8441 8728 -137 139 219 N
ATOM 1544 N ALA A 221 42.640 42.869 24.244 1.00 41.20 N
ANISOU 1544 N ALA A 221 5074 5226 5352 -115 115 209 N
ATOM 1545 CA ALA A 221 41.736 42.919 25.413 1.00 39.95 C
ANISOU 1545 CA ALA A 221 4918 5078 5182 -113 102 208 C
ATOM 1546 C ALA A 221 41.455 41.562 26.052 1.00 39.03 C
ANISOU 1546 C ALA A 221 4793 4969 5065 -113 96 211 C
ATOM 1547 O ALA A 221 41.224 41.482 27.253 1.00 39.03 O
ANISOU 1547 O ALA A 221 4791 4976 5060 -116 84 212 O
ATOM 1548 CB ALA A 221 40.430 43.620 25.065 1.00 36.67 C
ANISOU 1548 CB ALA A 221 4515 4667 4748 -107 103 203 C
ATOM 1549 N PHE A 222 41.477 40.507 25.239 1.00 39.95 N
ANISOU 1549 N PHE A 222 4907 5084 5188 -112 104 213 N
ATOM 1550 CA PHE A 222 41.230 39.133 25.697 1.00 41.34 C
ANISOU 1550 CA PHE A 222 5074 5265 5366 -112 98 217 C
ATOM 1551 C PHE A 222 42.512 38.296 25.780 1.00 43.07 C
ANISOU 1551 C PHE A 222 5279 5476 5610 -117 98 222 C
ATOM 1552 O PHE A 222 42.468 37.068 26.003 1.00 43.19 O
ANISOU 1552 O PHE A 222 5284 5492 5632 -117 94 226 O
ATOM 1553 CB PHE A 222 40.211 38.439 24.782 1.00 39.81 C
ANISOU 1553 CB PHE A 222 4886 5074 5162 -106 106 215 C
ATOM 1554 CG PHE A 222 38.794 38.723 25.144 1.00 37.60 C
ANISOU 1554 CG PHE A 222 4616 4805 4863 -101 101 212 C
ATOM 1555 CD1 PHE A 222 38.146 39.827 24.633 1.00 37.70 C
ANISOU 1555 CD1 PHE A 222 4641 4818 4865 -98 104 207 C
ATOM 1556 CD2 PHE A 222 38.106 37.880 26.004 1.00 38.77 C
ANISOU 1556 CD2 PHE A 222 4760 4963 5005 -101 92 214 C
ATOM 1557 CE1 PHE A 222 36.826 40.090 24.970 1.00 39.07 C
ANISOU 1557 CE1 PHE A 222 4822 5000 5024 -94 99 204 C
ATOM 1558 CE2 PHE A 222 36.790 38.130 26.350 1.00 38.90 C
ANISOU 1558 CE2 PHE A 222 4784 4988 5005 -98 88 211 C
ATOM 1559 CZ PHE A 222 36.146 39.241 25.828 1.00 39.42 C
ANISOU 1559 CZ PHE A 222 4861 5053 5062 -94 92 205 C
ATOM 1560 N GLN A 223 43.649 38.968 25.600 1.00 43.24 N
ANISOU 1560 N GLN A 223 5295 5487 5644 -120 102 222 N
ATOM 1561 CA GLN A 223 44.939 38.315 25.683 1.00 42.48 C
ANISOU 1561 CA GLN A 223 5184 5381 5575 -125 102 226 C
ATOM 1562 C GLN A 223 45.144 37.834 27.106 1.00 41.01 C
ANISOU 1562 C GLN A 223 4989 5199 5395 -130 82 234 C
ATOM 1563 O GLN A 223 44.992 38.604 28.064 1.00 39.07 O
ANISOU 1563 O GLN A 223 4748 4958 5137 -133 70 235 O
ATOM 1564 CB GLN A 223 46.064 39.252 25.256 1.00 44.29 C
ANISOU 1564 CB GLN A 223 5410 5599 5818 -128 110 225 C
ATOM 1565 CG GLN A 223 47.183 38.536 24.520 1.00 46.93 C
ANISOU 1565 CG GLN A 223 5731 5920 6179 -131 122 225 C
ATOM 1566 CD GLN A 223 46.838 38.242 23.067 1.00 47.55 C
ANISOU 1566 CD GLN A 223 5816 5997 6253 -128 142 218 C
ATOM 1567 OE1 GLN A 223 46.851 37.090 22.636 1.00 45.50 O
ANISOU 1567 OE1 GLN A 223 5549 5735 6003 -127 149 217 O
ATOM 1568 NE2 GLN A 223 46.534 39.291 22.303 1.00 50.85 N
ANISOU 1568 NE2 GLN A 223 6249 6416 6655 -127 152 214 N
ATOM 1569 N GLY A 224 45.431 36.538 27.219 1.00 40.70 N
ANISOU 1569 N GLY A 224 4937 5156 5372 -132 78 239 N
ATOM 1570 CA GLY A 224 45.622 35.868 28.496 1.00 39.32 C
ANISOU 1570 CA GLY A 224 4752 4984 5203 -138 58 248 C
ATOM 1571 C GLY A 224 44.380 35.748 29.356 1.00 39.62 C
ANISOU 1571 C GLY A 224 4800 5037 5215 -138 47 250 C
ATOM 1572 O GLY A 224 44.498 35.629 30.566 1.00 41.87 O
ANISOU 1572 O GLY A 224 5083 5327 5498 -146 30 257 O
ATOM 1573 N ILE A 225 43.184 35.780 28.765 1.00 39.24 N
ANISOU 1573 N ILE A 225 4763 4997 5146 -131 57 244 N
ATOM 1574 CA ILE A 225 41.977 35.602 29.587 1.00 38.43 C
ANISOU 1574 CA ILE A 225 4669 4910 5022 -131 48 244 C
ATOM 1575 C ILE A 225 41.205 34.322 29.260 1.00 37.91 C
ANISOU 1575 C ILE A 225 4599 4848 4954 -127 50 247 C
ATOM 1576 O ILE A 225 41.065 33.931 28.094 1.00 36.91 O
ANISOU 1576 O ILE A 225 4472 4716 4833 -121 63 242 O
ATOM 1577 CB ILE A 225 41.045 36.857 29.675 1.00 38.43 C
ANISOU 1577 CB ILE A 225 4685 4919 4998 -128 52 236 C
ATOM 1578 CG1 ILE A 225 39.867 36.754 28.720 1.00 38.62 C
ANISOU 1578 CG1 ILE A 225 4717 4947 5008 -119 64 230 C
ATOM 1579 CG2 ILE A 225 41.792 38.178 29.519 1.00 37.86 C
ANISOU 1579 CG2 ILE A 225 4616 4839 4929 -129 55 232 C
ATOM 1580 CD1 ILE A 225 38.646 36.143 29.369 1.00 38.73 C
ANISOU 1580 CD1 ILE A 225 4734 4973 5006 -119 57 230 C
ATOM 1581 N LYS A 226 40.733 33.673 30.322 1.00 38.06 N
ANISOU 1581 N LYS A 226 4617 4876 4966 -133 35 253 N
ATOM 1582 CA LYS A 226 40.076 32.376 30.254 1.00 37.11 C
ANISOU 1582 CA LYS A 226 4493 4760 4847 -131 33 257 C
ATOM 1583 C LYS A 226 38.618 32.556 30.643 1.00 35.54 C
ANISOU 1583 C LYS A 226 4306 4576 4621 -129 33 254 C
ATOM 1584 O LYS A 226 38.308 33.281 31.585 1.00 35.00 O
ANISOU 1584 O LYS A 226 4245 4517 4537 -134 26 252 O
ATOM 1585 CB LYS A 226 40.754 31.412 31.225 1.00 39.87 C
ANISOU 1585 CB LYS A 226 4829 5107 5212 -141 15 270 C
ATOM 1586 CG LYS A 226 40.613 29.934 30.893 1.00 44.99 C
ANISOU 1586 CG LYS A 226 5466 5752 5875 -139 14 276 C
ATOM 1587 CD LYS A 226 40.862 29.076 32.134 1.00 48.48 C
ANISOU 1587 CD LYS A 226 5899 6196 6323 -150 -7 290 C
ATOM 1588 CE LYS A 226 41.763 27.873 31.855 1.00 51.36 C
ANISOU 1588 CE LYS A 226 6244 6546 6722 -151 -12 298 C
ATOM 1589 NZ LYS A 226 41.216 26.910 30.853 1.00 52.35 N
ANISOU 1589 NZ LYS A 226 6366 6669 6855 -142 0 294 N
ATOM 1590 N LEU A 227 37.719 31.925 29.897 1.00 34.62 N
ANISOU 1590 N LEU A 227 4191 4462 4499 -121 41 251 N
ATOM 1591 CA LEU A 227 36.302 31.923 30.250 1.00 33.07 C
ANISOU 1591 CA LEU A 227 4004 4279 4282 -119 41 248 C
ATOM 1592 C LEU A 227 35.696 30.540 30.038 1.00 32.39 C
ANISOU 1592 C LEU A 227 3911 4195 4198 -117 39 252 C
ATOM 1593 O LEU A 227 36.113 29.794 29.156 1.00 31.95 O
ANISOU 1593 O LEU A 227 3849 4131 4160 -113 44 254 O
ATOM 1594 CB LEU A 227 35.531 32.976 29.451 1.00 32.84 C
ANISOU 1594 CB LEU A 227 3987 4251 4239 -111 53 236 C
ATOM 1595 CG LEU A 227 35.616 34.468 29.798 1.00 33.74 C
ANISOU 1595 CG LEU A 227 4109 4366 4344 -112 54 230 C
ATOM 1596 CD1 LEU A 227 34.918 35.313 28.739 1.00 32.88 C
ANISOU 1596 CD1 LEU A 227 4010 4255 4228 -103 66 221 C
ATOM 1597 CD2 LEU A 227 35.036 34.779 31.169 1.00 34.07 C
ANISOU 1597 CD2 LEU A 227 4154 4420 4370 -119 45 229 C
ATOM 1598 N HIS A 228 34.723 30.192 30.870 1.00 32.72 N
ANISOU 1598 N HIS A 228 3956 4249 4226 -120 32 255 N
ATOM 1599 CA HIS A 228 33.973 28.969 30.668 1.00 32.55 C
ANISOU 1599 CA HIS A 228 3930 4231 4205 -118 31 259 C
ATOM 1600 C HIS A 228 33.035 29.131 29.501 1.00 32.47 C
ANISOU 1600 C HIS A 228 3927 4220 4188 -106 44 250 C
ATOM 1601 O HIS A 228 33.226 28.512 28.460 1.00 33.31 O
ANISOU 1601 O HIS A 228 4030 4318 4307 -100 51 249 O
ATOM 1602 CB HIS A 228 33.214 28.560 31.934 1.00 32.71 C
ANISOU 1602 CB HIS A 228 3951 4264 4210 -126 20 265 C
ATOM 1603 CG HIS A 228 32.419 27.282 31.772 1.00 32.29 C
ANISOU 1603 CG HIS A 228 3894 4214 4159 -124 18 270 C
ATOM 1604 ND1 HIS A 228 33.006 26.073 31.670 1.00 32.22 N
ANISOU 1604 ND1 HIS A 228 3873 4199 4170 -126 10 279 N
ATOM 1605 CD2 HIS A 228 31.048 27.063 31.661 1.00 31.91 C
ANISOU 1605 CD2 HIS A 228 3851 4175 4097 -119 22 266 C
ATOM 1606 CE1 HIS A 228 32.062 25.129 31.509 1.00 31.69 C
ANISOU 1606 CE1 HIS A 228 3804 4136 4100 -123 10 282 C
ATOM 1607 NE2 HIS A 228 30.864 25.735 31.504 1.00 31.72 N
ANISOU 1607 NE2 HIS A 228 3818 4149 4082 -119 17 273 N
ATOM 1608 N GLU A 229 32.027 29.979 29.667 1.00 31.77 N
ANISOU 1608 N GLU A 229 3850 4140 4082 -103 48 243 N
ATOM 1609 CA GLU A 229 31.012 30.207 28.654 1.00 31.44 C
ANISOU 1609 CA GLU A 229 3815 4098 4033 -94 58 235 C
ATOM 1610 C GLU A 229 30.949 31.710 28.395 1.00 31.10 C
ANISOU 1610 C GLU A 229 3781 4052 3981 -91 64 226 C
ATOM 1611 O GLU A 229 30.928 32.504 29.339 1.00 31.99 O
ANISOU 1611 O GLU A 229 3896 4170 4086 -96 60 223 O
ATOM 1612 CB GLU A 229 29.668 29.656 29.142 1.00 32.59 C
ANISOU 1612 CB GLU A 229 3961 4253 4167 -93 55 235 C
ATOM 1613 CG GLU A 229 28.446 30.009 28.304 1.00 35.21 C
ANISOU 1613 CG GLU A 229 4301 4586 4491 -84 62 228 C
ATOM 1614 CD GLU A 229 27.185 29.242 28.724 1.00 37.85 C
ANISOU 1614 CD GLU A 229 4633 4929 4818 -83 59 229 C
ATOM 1615 OE1 GLU A 229 27.060 28.024 28.401 1.00 37.98 O
ANISOU 1615 OE1 GLU A 229 4644 4944 4841 -82 57 235 O
ATOM 1616 OE2 GLU A 229 26.302 29.864 29.366 1.00 38.03 O
ANISOU 1616 OE2 GLU A 229 4660 4960 4829 -84 60 223 O
ATOM 1617 N LEU A 230 30.965 32.098 27.122 1.00 29.95 N
ANISOU 1617 N LEU A 230 3641 3898 3839 -84 73 222 N
ATOM 1618 CA LEU A 230 30.815 33.496 26.732 1.00 29.42 C
ANISOU 1618 CA LEU A 230 3583 3828 3767 -81 78 214 C
ATOM 1619 C LEU A 230 29.700 33.616 25.708 1.00 29.73 C
ANISOU 1619 C LEU A 230 3630 3865 3800 -73 83 210 C
ATOM 1620 O LEU A 230 29.765 33.004 24.643 1.00 30.60 O
ANISOU 1620 O LEU A 230 3741 3970 3914 -70 87 212 O
ATOM 1621 CB LEU A 230 32.115 34.057 26.158 1.00 29.52 C
ANISOU 1621 CB LEU A 230 3596 3830 3789 -82 83 214 C
ATOM 1622 CG LEU A 230 32.033 35.444 25.484 1.00 30.03 C
ANISOU 1622 CG LEU A 230 3670 3889 3849 -79 88 208 C
ATOM 1623 CD1 LEU A 230 31.543 36.525 26.437 1.00 29.04 C
ANISOU 1623 CD1 LEU A 230 3549 3769 3715 -80 84 203 C
ATOM 1624 CD2 LEU A 230 33.369 35.847 24.871 1.00 29.56 C
ANISOU 1624 CD2 LEU A 230 3611 3820 3800 -82 94 209 C
ATOM 1625 N THR A 231 28.669 34.390 26.038 1.00 29.73 N
ANISOU 1625 N THR A 231 3635 3870 3791 -70 82 204 N
ATOM 1626 CA THR A 231 27.523 34.539 25.150 1.00 29.73 C
ANISOU 1626 CA THR A 231 3641 3867 3787 -63 84 201 C
ATOM 1627 C THR A 231 27.511 35.914 24.500 1.00 29.54 C
ANISOU 1627 C THR A 231 3625 3835 3762 -60 86 196 C
ATOM 1628 O THR A 231 27.480 36.940 25.186 1.00 28.48 O
ANISOU 1628 O THR A 231 3492 3701 3626 -61 85 191 O
ATOM 1629 CB THR A 231 26.180 34.266 25.862 1.00 29.84 C
ANISOU 1629 CB THR A 231 3653 3890 3795 -61 80 198 C
ATOM 1630 OG1 THR A 231 26.180 32.930 26.386 1.00 31.00 O
ANISOU 1630 OG1 THR A 231 3791 4043 3941 -64 77 204 O
ATOM 1631 CG2 THR A 231 25.031 34.400 24.882 1.00 28.74 C
ANISOU 1631 CG2 THR A 231 3519 3745 3654 -54 81 196 C
ATOM 1632 N LEU A 232 27.559 35.907 23.171 1.00 29.11 N
ANISOU 1632 N LEU A 232 3578 3772 3709 -58 89 198 N
ATOM 1633 CA LEU A 232 27.461 37.119 22.381 1.00 29.61 C
ANISOU 1633 CA LEU A 232 3650 3826 3771 -56 90 196 C
ATOM 1634 C LEU A 232 26.338 36.969 21.358 1.00 29.39 C
ANISOU 1634 C LEU A 232 3629 3795 3740 -51 88 197 C
ATOM 1635 O LEU A 232 26.583 36.638 20.199 1.00 30.78 O
ANISOU 1635 O LEU A 232 3813 3966 3915 -52 91 200 O
ATOM 1636 CB LEU A 232 28.794 37.419 21.677 1.00 29.54 C
ANISOU 1636 CB LEU A 232 3645 3811 3766 -60 96 198 C
ATOM 1637 CG LEU A 232 30.017 37.828 22.507 1.00 29.37 C
ANISOU 1637 CG LEU A 232 3618 3790 3750 -65 97 198 C
ATOM 1638 CD1 LEU A 232 31.270 37.745 21.643 1.00 29.92 C
ANISOU 1638 CD1 LEU A 232 3690 3852 3826 -69 105 201 C
ATOM 1639 CD2 LEU A 232 29.876 39.218 23.106 1.00 29.06 C
ANISOU 1639 CD2 LEU A 232 3581 3749 3710 -65 94 193 C
ATOM 1640 N ARG A 233 25.105 37.189 21.798 1.00 28.57 N
ANISOU 1640 N ARG A 233 3524 3694 3636 -47 83 193 N
ATOM 1641 CA ARG A 233 23.960 37.159 20.900 1.00 28.47 C
ANISOU 1641 CA ARG A 233 3517 3676 3622 -42 78 194 C
ATOM 1642 C ARG A 233 23.362 38.539 20.814 1.00 28.98 C
ANISOU 1642 C ARG A 233 3585 3734 3690 -40 73 190 C
ATOM 1643 O ARG A 233 23.215 39.211 21.828 1.00 29.26 O
ANISOU 1643 O ARG A 233 3615 3772 3729 -39 73 184 O
ATOM 1644 CB ARG A 233 22.898 36.168 21.374 1.00 28.18 C
ANISOU 1644 CB ARG A 233 3474 3647 3585 -39 75 194 C
ATOM 1645 CG ARG A 233 23.347 34.716 21.330 1.00 28.08 C
ANISOU 1645 CG ARG A 233 3457 3640 3570 -41 78 198 C
ATOM 1646 CD ARG A 233 22.196 33.765 21.595 1.00 27.33 C
ANISOU 1646 CD ARG A 233 3357 3551 3476 -37 75 199 C
ATOM 1647 NE ARG A 233 21.198 33.830 20.539 1.00 27.28 N
ANISOU 1647 NE ARG A 233 3357 3537 3468 -33 70 200 N
ATOM 1648 CZ ARG A 233 20.016 33.225 20.585 1.00 27.73 C
ANISOU 1648 CZ ARG A 233 3410 3597 3527 -29 65 200 C
ATOM 1649 NH1 ARG A 233 19.684 32.499 21.644 1.00 27.27 N
ANISOU 1649 NH1 ARG A 233 3342 3548 3470 -29 66 199 N
ATOM 1650 NH2 ARG A 233 19.167 33.344 19.567 1.00 27.13 N
ANISOU 1650 NH2 ARG A 233 3342 3514 3452 -27 59 202 N
ATOM 1651 N GLY A 234 23.017 38.959 19.602 1.00 29.99 N
ANISOU 1651 N GLY A 234 3723 3852 3818 -39 69 194 N
ATOM 1652 CA GLY A 234 22.391 40.266 19.388 1.00 31.51 C
ANISOU 1652 CA GLY A 234 3919 4035 4017 -37 61 192 C
ATOM 1653 C GLY A 234 23.244 41.425 19.869 1.00 32.12 C
ANISOU 1653 C GLY A 234 3995 4108 4098 -39 64 189 C
ATOM 1654 O GLY A 234 22.764 42.310 20.573 1.00 33.97 O
ANISOU 1654 O GLY A 234 4224 4341 4340 -37 61 182 O
ATOM 1655 N ASN A 235 24.516 41.408 19.487 1.00 32.07 N
ANISOU 1655 N ASN A 235 3994 4102 4087 -45 70 193 N
ATOM 1656 CA ASN A 235 25.483 42.413 19.912 1.00 31.59 C
ANISOU 1656 CA ASN A 235 3933 4039 4030 -48 73 190 C
ATOM 1657 C ASN A 235 25.848 43.417 18.827 1.00 31.60 C
ANISOU 1657 C ASN A 235 3945 4028 4032 -52 70 195 C
ATOM 1658 O ASN A 235 26.199 44.548 19.127 1.00 31.49 O
ANISOU 1658 O ASN A 235 3931 4008 4024 -52 68 193 O
ATOM 1659 CB ASN A 235 26.774 41.728 20.388 1.00 31.15 C
ANISOU 1659 CB ASN A 235 3872 3989 3971 -53 81 191 C
ATOM 1660 CG ASN A 235 26.696 41.251 21.829 1.00 30.69 C
ANISOU 1660 CG ASN A 235 3803 3942 3913 -52 82 185 C
ATOM 1661 OD1 ASN A 235 26.595 42.046 22.759 1.00 31.32 O
ANISOU 1661 OD1 ASN A 235 3878 4023 3996 -51 81 179 O
ATOM 1662 ND2 ASN A 235 26.762 39.948 22.018 1.00 30.15 N
ANISOU 1662 ND2 ASN A 235 3730 3882 3841 -52 85 188 N
ATOM 1663 N PHE A 236 25.780 42.998 17.570 1.00 32.83 N
ANISOU 1663 N PHE A 236 4111 4179 4181 -55 69 202 N
ATOM 1664 CA PHE A 236 26.461 43.721 16.512 1.00 34.82 C
ANISOU 1664 CA PHE A 236 4375 4422 4430 -62 70 208 C
ATOM 1665 C PHE A 236 25.513 44.267 15.446 1.00 37.64 C
ANISOU 1665 C PHE A 236 4744 4770 4787 -63 58 215 C
ATOM 1666 O PHE A 236 24.778 43.504 14.826 1.00 39.81 O
ANISOU 1666 O PHE A 236 5024 5046 5057 -63 54 218 O
ATOM 1667 CB PHE A 236 27.550 42.830 15.916 1.00 33.06 C
ANISOU 1667 CB PHE A 236 4157 4204 4200 -68 82 211 C
ATOM 1668 CG PHE A 236 28.532 42.308 16.935 1.00 32.87 C
ANISOU 1668 CG PHE A 236 4121 4187 4179 -68 91 207 C
ATOM 1669 CD1 PHE A 236 28.662 40.948 17.163 1.00 32.61 C
ANISOU 1669 CD1 PHE A 236 4081 4162 4144 -67 96 206 C
ATOM 1670 CD2 PHE A 236 29.334 43.177 17.670 1.00 33.56 C
ANISOU 1670 CD2 PHE A 236 4203 4273 4273 -69 92 204 C
ATOM 1671 CE1 PHE A 236 29.573 40.457 18.091 1.00 31.59 C
ANISOU 1671 CE1 PHE A 236 3942 4040 4021 -68 102 203 C
ATOM 1672 CE2 PHE A 236 30.246 42.693 18.604 1.00 33.38 C
ANISOU 1672 CE2 PHE A 236 4170 4257 4254 -70 99 201 C
ATOM 1673 CZ PHE A 236 30.364 41.329 18.815 1.00 32.20 C
ANISOU 1673 CZ PHE A 236 4014 4115 4103 -70 103 201 C
ATOM 1674 N ASN A 237 25.533 45.590 15.253 1.00 40.71 N
ANISOU 1674 N ASN A 237 5136 5148 5182 -64 51 217 N
ATOM 1675 CA ASN A 237 24.623 46.292 14.324 1.00 43.15 C
ANISOU 1675 CA ASN A 237 5454 5444 5493 -66 36 224 C
ATOM 1676 C ASN A 237 24.870 45.984 12.858 1.00 42.30 C
ANISOU 1676 C ASN A 237 5364 5334 5372 -76 36 235 C
ATOM 1677 O ASN A 237 24.012 46.252 12.011 1.00 42.89 O
ANISOU 1677 O ASN A 237 5448 5400 5446 -79 22 242 O
ATOM 1678 CB ASN A 237 24.682 47.816 14.531 1.00 45.85 C
ANISOU 1678 CB ASN A 237 5795 5776 5848 -66 28 224 C
ATOM 1679 CG ASN A 237 23.483 48.356 15.296 1.00 48.88 C
ANISOU 1679 CG ASN A 237 6167 6154 6249 -56 18 217 C
ATOM 1680 OD1 ASN A 237 22.330 48.160 14.896 1.00 48.49 O
ANISOU 1680 OD1 ASN A 237 6118 6100 6203 -53 7 220 O
ATOM 1681 ND2 ASN A 237 23.750 49.061 16.395 1.00 52.46 N
ANISOU 1681 ND2 ASN A 237 6610 6608 6713 -52 22 208 N
ATOM 1682 N SER A 238 26.043 45.421 12.577 1.00 41.69 N
ANISOU 1682 N SER A 238 5291 5263 5284 -83 50 234 N
ATOM 1683 CA SER A 238 26.517 45.182 11.214 1.00 40.52 C
ANISOU 1683 CA SER A 238 5160 5112 5121 -95 54 242 C
ATOM 1684 C SER A 238 27.486 43.995 11.114 1.00 40.37 C
ANISOU 1684 C SER A 238 5140 5103 5093 -99 73 238 C
ATOM 1685 O SER A 238 28.165 43.644 12.084 1.00 40.54 O
ANISOU 1685 O SER A 238 5149 5131 5122 -94 83 231 O
ATOM 1686 CB SER A 238 27.176 46.449 10.684 1.00 39.16 C
ANISOU 1686 CB SER A 238 4998 4931 4950 -104 52 248 C
ATOM 1687 OG SER A 238 28.500 46.203 10.265 1.00 40.51 O
ANISOU 1687 OG SER A 238 5173 5105 5111 -113 69 248 O
ATOM 1688 N SER A 239 27.552 43.394 9.929 1.00 40.02 N
ANISOU 1688 N SER A 239 5111 5059 5035 -109 77 242 N
ATOM 1689 CA SER A 239 28.433 42.259 9.690 1.00 39.69 C
ANISOU 1689 CA SER A 239 5067 5024 4986 -114 95 236 C
ATOM 1690 C SER A 239 29.911 42.638 9.808 1.00 37.77 C
ANISOU 1690 C SER A 239 4822 4781 4747 -120 110 234 C
ATOM 1691 O SER A 239 30.716 41.841 10.293 1.00 34.70 O
ANISOU 1691 O SER A 239 4423 4398 4363 -118 124 227 O
ATOM 1692 CB SER A 239 28.151 41.636 8.320 1.00 42.98 C
ANISOU 1692 CB SER A 239 5502 5440 5386 -125 97 240 C
ATOM 1693 OG SER A 239 28.737 42.401 7.274 1.00 47.42 O
ANISOU 1693 OG SER A 239 6082 5997 5938 -139 100 246 O
ATOM 1694 N ASN A 240 30.266 43.844 9.358 1.00 38.08 N
ANISOU 1694 N ASN A 240 4871 4813 4784 -127 107 240 N
ATOM 1695 CA ASN A 240 31.646 44.325 9.514 1.00 38.68 C
ANISOU 1695 CA ASN A 240 4943 4887 4865 -132 121 237 C
ATOM 1696 C ASN A 240 32.017 44.543 10.976 1.00 37.33 C
ANISOU 1696 C ASN A 240 4753 4719 4711 -121 120 232 C
ATOM 1697 O ASN A 240 33.127 44.196 11.404 1.00 37.70 O
ANISOU 1697 O ASN A 240 4791 4769 4765 -122 134 227 O
ATOM 1698 CB ASN A 240 31.922 45.599 8.711 1.00 39.79 C
ANISOU 1698 CB ASN A 240 5098 5018 5000 -143 117 246 C
ATOM 1699 CG ASN A 240 33.396 45.999 8.746 1.00 41.58 C
ANISOU 1699 CG ASN A 240 5321 5243 5231 -150 132 244 C
ATOM 1700 OD1 ASN A 240 34.252 45.306 8.195 1.00 43.00 O
ANISOU 1700 OD1 ASN A 240 5505 5426 5406 -158 151 240 O
ATOM 1701 ND2 ASN A 240 33.695 47.116 9.405 1.00 41.48 N
ANISOU 1701 ND2 ASN A 240 5302 5225 5230 -146 126 245 N
ATOM 1702 N ILE A 241 31.083 45.114 11.732 1.00 36.20 N
ANISOU 1702 N ILE A 241 4604 4574 4575 -111 105 232 N
ATOM 1703 CA ILE A 241 31.261 45.319 13.160 1.00 35.90 C
ANISOU 1703 CA ILE A 241 4549 4540 4551 -102 103 226 C
ATOM 1704 C ILE A 241 31.516 43.995 13.865 1.00 36.98 C
ANISOU 1704 C ILE A 241 4673 4686 4689 -97 112 220 C
ATOM 1705 O ILE A 241 32.380 43.901 14.739 1.00 37.44 O
ANISOU 1705 O ILE A 241 4720 4748 4756 -95 118 215 O
ATOM 1706 CB ILE A 241 30.052 46.024 13.783 1.00 35.59 C
ANISOU 1706 CB ILE A 241 4506 4498 4518 -93 87 225 C
ATOM 1707 CG1 ILE A 241 29.953 47.453 13.210 1.00 34.67 C
ANISOU 1707 CG1 ILE A 241 4399 4369 4403 -98 78 232 C
ATOM 1708 CG2 ILE A 241 30.141 45.981 15.312 1.00 35.04 C
ANISOU 1708 CG2 ILE A 241 4419 4434 4458 -84 87 217 C
ATOM 1709 CD1 ILE A 241 28.878 48.337 13.809 1.00 33.28 C
ANISOU 1709 CD1 ILE A 241 4218 4188 4239 -89 62 230 C
ATOM 1710 N MET A 242 30.791 42.959 13.465 1.00 36.62 N
ANISOU 1710 N MET A 242 4630 4645 4636 -95 111 220 N
ATOM 1711 CA MET A 242 31.032 41.647 14.037 1.00 37.18 C
ANISOU 1711 CA MET A 242 4690 4724 4711 -92 119 215 C
ATOM 1712 C MET A 242 32.424 41.095 13.692 1.00 37.70 C
ANISOU 1712 C MET A 242 4753 4790 4778 -99 135 213 C
ATOM 1713 O MET A 242 33.157 40.658 14.588 1.00 38.38 O
ANISOU 1713 O MET A 242 4827 4880 4876 -97 140 209 O
ATOM 1714 CB MET A 242 29.938 40.668 13.648 1.00 36.79 C
ANISOU 1714 CB MET A 242 4644 4678 4654 -89 114 215 C
ATOM 1715 CG MET A 242 30.033 39.362 14.398 1.00 38.24 C
ANISOU 1715 CG MET A 242 4815 4871 4844 -84 119 211 C
ATOM 1716 SD MET A 242 28.712 38.256 13.916 1.00 40.40 S
ANISOU 1716 SD MET A 242 5092 5148 5110 -80 113 212 S
ATOM 1717 CE MET A 242 29.174 36.795 14.835 1.00 42.16 C
ANISOU 1717 CE MET A 242 5298 5379 5341 -77 120 208 C
ATOM 1718 N LYS A 243 32.784 41.131 12.408 1.00 37.58 N
ANISOU 1718 N LYS A 243 4752 4770 4754 -109 144 215 N
ATOM 1719 CA LYS A 243 34.065 40.607 11.930 1.00 37.98 C
ANISOU 1719 CA LYS A 243 4801 4820 4809 -117 162 211 C
ATOM 1720 C LYS A 243 35.171 41.285 12.704 1.00 38.23 C
ANISOU 1720 C LYS A 243 4822 4848 4853 -117 166 210 C
ATOM 1721 O LYS A 243 36.123 40.657 13.177 1.00 37.88 O
ANISOU 1721 O LYS A 243 4765 4805 4821 -117 175 206 O
ATOM 1722 CB LYS A 243 34.220 40.886 10.430 1.00 38.82 C
ANISOU 1722 CB LYS A 243 4927 4921 4901 -130 170 214 C
ATOM 1723 CG LYS A 243 35.568 40.543 9.801 1.00 38.93 C
ANISOU 1723 CG LYS A 243 4941 4933 4917 -141 191 209 C
ATOM 1724 CD LYS A 243 35.464 40.712 8.288 1.00 41.35 C
ANISOU 1724 CD LYS A 243 5269 5237 5205 -155 198 211 C
ATOM 1725 CE LYS A 243 36.809 40.818 7.582 1.00 41.78 C
ANISOU 1725 CE LYS A 243 5326 5287 5261 -168 220 207 C
ATOM 1726 NZ LYS A 243 37.434 39.488 7.331 1.00 43.58 N
ANISOU 1726 NZ LYS A 243 5546 5517 5495 -171 239 197 N
ATOM 1727 N THR A 244 34.997 42.582 12.867 1.00 38.97 N
ANISOU 1727 N THR A 244 4920 4938 4946 -117 156 214 N
ATOM 1728 CA THR A 244 36.039 43.416 13.413 1.00 40.34 C
ANISOU 1728 CA THR A 244 5087 5107 5130 -118 159 214 C
ATOM 1729 C THR A 244 36.143 43.306 14.951 1.00 40.22 C
ANISOU 1729 C THR A 244 5056 5098 5128 -109 152 211 C
ATOM 1730 O THR A 244 37.213 43.508 15.530 1.00 40.38 O
ANISOU 1730 O THR A 244 5066 5116 5160 -111 157 209 O
ATOM 1731 CB THR A 244 35.872 44.856 12.874 1.00 39.22 C
ANISOU 1731 CB THR A 244 4958 4959 4984 -123 153 220 C
ATOM 1732 OG1 THR A 244 37.140 45.502 12.839 1.00 40.08 O
ANISOU 1732 OG1 THR A 244 5065 5063 5101 -130 162 220 O
ATOM 1733 CG2 THR A 244 34.890 45.661 13.695 1.00 39.25 C
ANISOU 1733 CG2 THR A 244 4959 4962 4990 -114 135 221 C
ATOM 1734 N CYS A 245 35.035 42.954 15.597 1.00 40.40 N
ANISOU 1734 N CYS A 245 5075 5126 5148 -101 141 210 N
ATOM 1735 CA CYS A 245 35.031 42.711 17.034 1.00 39.59 C
ANISOU 1735 CA CYS A 245 4958 5030 5054 -95 135 206 C
ATOM 1736 C CYS A 245 35.489 41.301 17.371 1.00 38.27 C
ANISOU 1736 C CYS A 245 4779 4867 4892 -94 141 205 C
ATOM 1737 O CYS A 245 36.137 41.095 18.393 1.00 39.27 O
ANISOU 1737 O CYS A 245 4893 4996 5029 -93 140 204 O
ATOM 1738 CB CYS A 245 33.646 42.953 17.626 1.00 41.69 C
ANISOU 1738 CB CYS A 245 5225 5300 5315 -87 122 205 C
ATOM 1739 SG CYS A 245 33.201 44.695 17.768 1.00 42.41 S
ANISOU 1739 SG CYS A 245 5321 5384 5407 -85 112 205 S
ATOM 1740 N LEU A 246 35.156 40.328 16.526 1.00 36.10 N
ANISOU 1740 N LEU A 246 4509 4594 4612 -95 147 205 N
ATOM 1741 CA LEU A 246 35.584 38.955 16.784 1.00 35.61 C
ANISOU 1741 CA LEU A 246 4435 4534 4558 -95 153 203 C
ATOM 1742 C LEU A 246 37.106 38.817 16.705 1.00 36.12 C
ANISOU 1742 C LEU A 246 4492 4594 4637 -101 165 201 C
ATOM 1743 O LEU A 246 37.692 37.951 17.360 1.00 36.68 O
ANISOU 1743 O LEU A 246 4549 4666 4721 -100 166 201 O
ATOM 1744 CB LEU A 246 34.896 37.954 15.848 1.00 34.09 C
ANISOU 1744 CB LEU A 246 4249 4344 4357 -95 157 202 C
ATOM 1745 CG LEU A 246 33.377 37.762 15.953 1.00 33.62 C
ANISOU 1745 CG LEU A 246 4195 4290 4287 -89 146 203 C
ATOM 1746 CD1 LEU A 246 32.913 36.640 15.040 1.00 33.46 C
ANISOU 1746 CD1 LEU A 246 4180 4271 4261 -90 151 202 C
ATOM 1747 CD2 LEU A 246 32.927 37.502 17.379 1.00 33.24 C
ANISOU 1747 CD2 LEU A 246 4135 4249 4244 -82 135 203 C
ATOM 1748 N GLN A 247 37.732 39.680 15.909 1.00 35.85 N
ANISOU 1748 N GLN A 247 4466 4552 4601 -108 173 201 N
ATOM 1749 CA GLN A 247 39.172 39.662 15.715 1.00 35.37 C
ANISOU 1749 CA GLN A 247 4398 4485 4555 -114 186 200 C
ATOM 1750 C GLN A 247 39.907 40.028 16.977 1.00 36.35 C
ANISOU 1750 C GLN A 247 4508 4609 4694 -112 179 201 C
ATOM 1751 O GLN A 247 41.039 39.591 17.183 1.00 37.03 O
ANISOU 1751 O GLN A 247 4582 4690 4797 -116 186 200 O
ATOM 1752 CB GLN A 247 39.587 40.596 14.583 1.00 35.95 C
ANISOU 1752 CB GLN A 247 4485 4552 4621 -123 196 200 C
ATOM 1753 CG GLN A 247 39.473 39.937 13.222 1.00 38.29 C
ANISOU 1753 CG GLN A 247 4793 4848 4908 -130 210 197 C
ATOM 1754 CD GLN A 247 39.517 40.912 12.071 1.00 40.02 C
ANISOU 1754 CD GLN A 247 5029 5062 5113 -139 217 199 C
ATOM 1755 OE1 GLN A 247 39.685 40.512 10.921 1.00 40.56 O
ANISOU 1755 OE1 GLN A 247 5107 5129 5173 -149 231 196 O
ATOM 1756 NE2 GLN A 247 39.357 42.197 12.368 1.00 43.50 N
ANISOU 1756 NE2 GLN A 247 5475 5501 5551 -138 206 205 N
ATOM 1757 N ASN A 248 39.266 40.820 17.831 1.00 36.02 N
ANISOU 1757 N ASN A 248 4468 4570 4645 -107 165 203 N
ATOM 1758 CA ASN A 248 39.915 41.245 19.060 1.00 35.60 C
ANISOU 1758 CA ASN A 248 4403 4517 4603 -107 157 204 C
ATOM 1759 C ASN A 248 39.569 40.395 20.274 1.00 36.00 C
ANISOU 1759 C ASN A 248 4444 4576 4658 -103 146 205 C
ATOM 1760 O ASN A 248 39.921 40.713 21.414 1.00 36.54 O
ANISOU 1760 O ASN A 248 4505 4646 4733 -103 137 206 O
ATOM 1761 CB ASN A 248 39.713 42.732 19.277 1.00 35.66 C
ANISOU 1761 CB ASN A 248 4419 4522 4605 -106 150 204 C
ATOM 1762 CG ASN A 248 40.648 43.563 18.419 1.00 36.39 C
ANISOU 1762 CG ASN A 248 4516 4605 4702 -113 160 205 C
ATOM 1763 OD1 ASN A 248 41.756 43.138 18.107 1.00 36.25 O
ANISOU 1763 OD1 ASN A 248 4492 4583 4697 -118 171 205 O
ATOM 1764 ND2 ASN A 248 40.211 44.750 18.041 1.00 37.13 N
ANISOU 1764 ND2 ASN A 248 4622 4696 4788 -114 156 206 N
ATOM 1765 N LEU A 249 38.898 39.285 19.987 1.00 35.58 N
ANISOU 1765 N LEU A 249 4390 4527 4601 -100 147 204 N
ATOM 1766 CA LEU A 249 38.783 38.161 20.900 1.00 34.83 C
ANISOU 1766 CA LEU A 249 4283 4438 4512 -98 140 206 C
ATOM 1767 C LEU A 249 40.080 37.340 20.937 1.00 35.30 C
ANISOU 1767 C LEU A 249 4328 4490 4592 -102 146 207 C
ATOM 1768 O LEU A 249 40.207 36.438 21.760 1.00 36.39 O
ANISOU 1768 O LEU A 249 4454 4631 4739 -102 138 210 O
ATOM 1769 CB LEU A 249 37.619 37.263 20.472 1.00 33.12 C
ANISOU 1769 CB LEU A 249 4071 4227 4284 -93 140 205 C
ATOM 1770 CG LEU A 249 36.275 37.247 21.200 1.00 31.77 C
ANISOU 1770 CG LEU A 249 3904 4066 4101 -88 128 206 C
ATOM 1771 CD1 LEU A 249 35.884 38.568 21.834 1.00 31.19 C
ANISOU 1771 CD1 LEU A 249 3836 3995 4020 -87 120 205 C
ATOM 1772 CD2 LEU A 249 35.204 36.769 20.240 1.00 31.85 C
ANISOU 1772 CD2 LEU A 249 3923 4078 4101 -84 131 205 C
ATOM 1773 N ALA A 250 41.027 37.641 20.043 1.00 35.60 N
ANISOU 1773 N ALA A 250 4366 4519 4639 -107 159 205 N
ATOM 1774 CA ALA A 250 42.350 36.967 20.010 1.00 35.84 C
ANISOU 1774 CA ALA A 250 4381 4540 4693 -111 167 204 C
ATOM 1775 C ALA A 250 42.923 36.761 21.407 1.00 35.65 C
ANISOU 1775 C ALA A 250 4343 4517 4685 -112 152 210 C
ATOM 1776 O ALA A 250 42.916 37.683 22.224 1.00 38.89 O
ANISOU 1776 O ALA A 250 4756 4930 5090 -113 142 212 O
ATOM 1777 CB ALA A 250 43.342 37.746 19.155 1.00 33.26 C
ANISOU 1777 CB ALA A 250 4057 4204 4373 -117 182 201 C
ATOM 1778 N GLY A 251 43.399 35.552 21.678 1.00 34.57 N
ANISOU 1778 N GLY A 251 4191 4376 4566 -113 151 212 N
ATOM 1779 CA GLY A 251 43.926 35.210 22.993 1.00 35.23 C
ANISOU 1779 CA GLY A 251 4260 4459 4664 -116 135 219 C
ATOM 1780 C GLY A 251 42.971 34.427 23.874 1.00 35.84 C
ANISOU 1780 C GLY A 251 4337 4547 4732 -113 120 223 C
ATOM 1781 O GLY A 251 43.393 33.575 24.637 1.00 37.32 O
ANISOU 1781 O GLY A 251 4510 4732 4935 -116 109 230 O
ATOM 1782 N LEU A 252 41.681 34.716 23.766 1.00 36.16 N
ANISOU 1782 N LEU A 252 4391 4598 4748 -109 119 221 N
ATOM 1783 CA LEU A 252 40.661 34.089 24.590 1.00 35.85 C
ANISOU 1783 CA LEU A 252 4352 4570 4697 -107 106 225 C
ATOM 1784 C LEU A 252 40.744 32.566 24.571 1.00 36.90 C
ANISOU 1784 C LEU A 252 4473 4701 4845 -107 104 229 C
ATOM 1785 O LEU A 252 40.971 31.952 23.530 1.00 37.45 O
ANISOU 1785 O LEU A 252 4539 4763 4924 -105 117 224 O
ATOM 1786 CB LEU A 252 39.281 34.558 24.127 1.00 34.97 C
ANISOU 1786 CB LEU A 252 4256 4467 4561 -101 109 221 C
ATOM 1787 CG LEU A 252 37.955 34.018 24.660 1.00 34.72 C
ANISOU 1787 CG LEU A 252 4229 4447 4515 -97 101 222 C
ATOM 1788 CD1 LEU A 252 37.831 34.120 26.174 1.00 35.33 C
ANISOU 1788 CD1 LEU A 252 4303 4533 4588 -102 86 227 C
ATOM 1789 CD2 LEU A 252 36.827 34.787 23.992 1.00 34.65 C
ANISOU 1789 CD2 LEU A 252 4235 4443 4487 -92 106 216 C
ATOM 1790 N HIS A 253 40.580 31.974 25.748 1.00 38.55 N
ANISOU 1790 N HIS A 253 4674 4915 5055 -110 88 236 N
ATOM 1791 CA HIS A 253 40.368 30.539 25.888 1.00 39.21 C
ANISOU 1791 CA HIS A 253 4748 4999 5150 -109 83 241 C
ATOM 1792 C HIS A 253 38.973 30.380 26.438 1.00 36.29 C
ANISOU 1792 C HIS A 253 4387 4643 4756 -107 75 243 C
ATOM 1793 O HIS A 253 38.713 30.728 27.592 1.00 35.55 O
ANISOU 1793 O HIS A 253 4295 4558 4652 -112 62 247 O
ATOM 1794 CB HIS A 253 41.433 29.937 26.812 1.00 43.65 C
ANISOU 1794 CB HIS A 253 5293 5554 5736 -117 69 250 C
ATOM 1795 CG HIS A 253 41.270 28.450 27.076 1.00 49.15 C
ANISOU 1795 CG HIS A 253 5977 6249 6446 -118 61 257 C
ATOM 1796 ND1 HIS A 253 42.016 27.515 26.451 1.00 52.04 N
ANISOU 1796 ND1 HIS A 253 6328 6602 6840 -117 67 256 N
ATOM 1797 CD2 HIS A 253 40.434 27.757 27.959 1.00 52.93 C
ANISOU 1797 CD2 HIS A 253 6456 6739 6915 -120 46 265 C
ATOM 1798 CE1 HIS A 253 41.670 26.287 26.895 1.00 52.16 C
ANISOU 1798 CE1 HIS A 253 6335 6619 6864 -118 56 264 C
ATOM 1799 NE2 HIS A 253 40.700 26.436 27.816 1.00 55.22 N
ANISOU 1799 NE2 HIS A 253 6731 7020 7227 -120 43 270 N
ATOM 1800 N VAL A 254 38.055 29.903 25.598 1.00 32.46 N
ANISOU 1800 N VAL A 254 3908 4161 4263 -101 84 238 N
ATOM 1801 CA VAL A 254 36.679 29.637 26.014 1.00 31.75 C
ANISOU 1801 CA VAL A 254 3825 4083 4154 -98 77 239 C
ATOM 1802 C VAL A 254 36.298 28.181 25.863 1.00 30.63 C
ANISOU 1802 C VAL A 254 3674 3941 4020 -97 75 243 C
ATOM 1803 O VAL A 254 36.605 27.540 24.856 1.00 30.75 O
ANISOU 1803 O VAL A 254 3686 3949 4049 -94 85 239 O
ATOM 1804 CB VAL A 254 35.611 30.452 25.230 1.00 32.60 C
ANISOU 1804 CB VAL A 254 3948 4196 4241 -92 86 231 C
ATOM 1805 CG1 VAL A 254 34.892 31.433 26.142 1.00 33.40 C
ANISOU 1805 CG1 VAL A 254 4058 4307 4324 -93 79 230 C
ATOM 1806 CG2 VAL A 254 36.182 31.118 23.986 1.00 32.45 C
ANISOU 1806 CG2 VAL A 254 3936 4168 4226 -90 101 225 C
ATOM 1807 N HIS A 255 35.592 27.670 26.855 1.00 30.35 N
ANISOU 1807 N HIS A 255 3637 3915 3976 -99 62 250 N
ATOM 1808 CA HIS A 255 35.041 26.335 26.750 1.00 31.74 C
ANISOU 1808 CA HIS A 255 3806 4092 4158 -98 59 253 C
ATOM 1809 C HIS A 255 33.798 26.371 25.905 1.00 30.57 C
ANISOU 1809 C HIS A 255 3670 3950 3995 -90 68 246 C
ATOM 1810 O HIS A 255 33.573 25.476 25.102 1.00 31.20 O
ANISOU 1810 O HIS A 255 3747 4025 4082 -86 73 245 O
ATOM 1811 CB HIS A 255 34.788 25.721 28.136 1.00 33.10 C
ANISOU 1811 CB HIS A 255 3973 4274 4330 -105 41 265 C
ATOM 1812 CG HIS A 255 34.146 24.352 28.092 1.00 34.71 C
ANISOU 1812 CG HIS A 255 4170 4478 4538 -103 37 270 C
ATOM 1813 ND1 HIS A 255 32.855 24.144 28.434 1.00 36.53 N
ANISOU 1813 ND1 HIS A 255 4406 4720 4750 -102 34 270 N
ATOM 1814 CD2 HIS A 255 34.651 23.115 27.706 1.00 35.32 C
ANISOU 1814 CD2 HIS A 255 4233 4545 4639 -103 35 273 C
ATOM 1815 CE1 HIS A 255 32.554 22.837 28.284 1.00 36.05 C
ANISOU 1815 CE1 HIS A 255 4337 4658 4701 -101 30 275 C
ATOM 1816 NE2 HIS A 255 33.651 22.210 27.836 1.00 35.78 N
ANISOU 1816 NE2 HIS A 255 4291 4611 4693 -102 30 277 N
ATOM 1817 N ARG A 256 32.983 27.406 26.052 1.00 29.93 N
ANISOU 1817 N ARG A 256 3602 3877 3893 -88 69 242 N
ATOM 1818 CA ARG A 256 31.758 27.476 25.275 1.00 30.55 C
ANISOU 1818 CA ARG A 256 3690 3959 3958 -80 75 236 C
ATOM 1819 C ARG A 256 31.495 28.873 24.737 1.00 30.61 C
ANISOU 1819 C ARG A 256 3710 3966 3952 -77 83 229 C
ATOM 1820 O ARG A 256 31.310 29.809 25.510 1.00 30.96 O
ANISOU 1820 O ARG A 256 3758 4015 3987 -79 79 228 O
ATOM 1821 CB ARG A 256 30.565 26.981 26.088 1.00 30.88 C
ANISOU 1821 CB ARG A 256 3732 4012 3989 -81 67 240 C
ATOM 1822 CG ARG A 256 29.362 26.654 25.225 1.00 32.93 C
ANISOU 1822 CG ARG A 256 3998 4273 4241 -73 71 236 C
ATOM 1823 CD ARG A 256 28.252 25.930 25.978 1.00 34.95 C
ANISOU 1823 CD ARG A 256 4250 4539 4489 -74 63 240 C
ATOM 1824 NE ARG A 256 28.767 24.833 26.798 1.00 37.04 N
ANISOU 1824 NE ARG A 256 4503 4805 4766 -80 54 250 N
ATOM 1825 CZ ARG A 256 28.669 24.777 28.127 1.00 36.71 C
ANISOU 1825 CZ ARG A 256 4457 4772 4718 -88 44 256 C
ATOM 1826 NH1 ARG A 256 28.049 25.747 28.798 1.00 35.06 N
ANISOU 1826 NH1 ARG A 256 4257 4572 4492 -89 45 252 N
ATOM 1827 NH2 ARG A 256 29.179 23.741 28.779 1.00 35.95 N
ANISOU 1827 NH2 ARG A 256 4350 4675 4633 -94 34 267 N
ATOM 1828 N LEU A 257 31.488 29.011 23.409 1.00 29.60 N
ANISOU 1828 N LEU A 257 3590 3832 3825 -73 93 224 N
ATOM 1829 CA LEU A 257 31.143 30.287 22.793 1.00 28.85 C
ANISOU 1829 CA LEU A 257 3507 3734 3717 -71 98 218 C
ATOM 1830 C LEU A 257 29.805 30.188 22.076 1.00 28.66 C
ANISOU 1830 C LEU A 257 3493 3713 3683 -65 99 215 C
ATOM 1831 O LEU A 257 29.616 29.333 21.210 1.00 27.98 O
ANISOU 1831 O LEU A 257 3407 3624 3599 -64 103 215 O
ATOM 1832 CB LEU A 257 32.242 30.754 21.834 1.00 28.84 C
ANISOU 1832 CB LEU A 257 3509 3723 3724 -73 109 215 C
ATOM 1833 CG LEU A 257 32.197 32.178 21.251 1.00 28.21 C
ANISOU 1833 CG LEU A 257 3443 3641 3635 -72 114 211 C
ATOM 1834 CD1 LEU A 257 32.336 33.252 22.313 1.00 26.79 C
ANISOU 1834 CD1 LEU A 257 3262 3464 3452 -74 107 211 C
ATOM 1835 CD2 LEU A 257 33.281 32.328 20.202 1.00 27.48 C
ANISOU 1835 CD2 LEU A 257 3353 3539 3550 -76 126 208 C
ATOM 1836 N ILE A 258 28.884 31.065 22.463 1.00 28.21 N
ANISOU 1836 N ILE A 258 3442 3661 3615 -62 94 213 N
ATOM 1837 CA ILE A 258 27.553 31.138 21.857 1.00 28.93 C
ANISOU 1837 CA ILE A 258 3541 3753 3696 -57 93 211 C
ATOM 1838 C ILE A 258 27.387 32.447 21.067 1.00 28.71 C
ANISOU 1838 C ILE A 258 3525 3719 3662 -56 96 208 C
ATOM 1839 O ILE A 258 27.483 33.544 21.625 1.00 27.72 O
ANISOU 1839 O ILE A 258 3400 3594 3535 -56 94 205 O
ATOM 1840 CB ILE A 258 26.440 30.996 22.920 1.00 28.76 C
ANISOU 1840 CB ILE A 258 3515 3741 3670 -55 86 211 C
ATOM 1841 CG1 ILE A 258 26.604 29.681 23.687 1.00 28.19 C
ANISOU 1841 CG1 ILE A 258 3431 3675 3603 -58 82 217 C
ATOM 1842 CG2 ILE A 258 25.070 31.072 22.265 1.00 28.26 C
ANISOU 1842 CG2 ILE A 258 3458 3677 3600 -49 84 209 C
ATOM 1843 CD1 ILE A 258 26.236 29.776 25.149 1.00 29.13 C
ANISOU 1843 CD1 ILE A 258 3545 3803 3717 -61 76 218 C
ATOM 1844 N LEU A 259 27.116 32.297 19.771 1.00 29.62 N
ANISOU 1844 N LEU A 259 3650 3829 3775 -55 99 207 N
ATOM 1845 CA LEU A 259 27.184 33.376 18.790 1.00 29.78 C
ANISOU 1845 CA LEU A 259 3682 3841 3790 -56 102 206 C
ATOM 1846 C LEU A 259 25.876 33.455 18.004 1.00 29.99 C
ANISOU 1846 C LEU A 259 3718 3866 3809 -52 96 206 C
ATOM 1847 O LEU A 259 25.297 32.423 17.662 1.00 30.89 O
ANISOU 1847 O LEU A 259 3832 3982 3922 -51 95 207 O
ATOM 1848 CB LEU A 259 28.326 33.058 17.833 1.00 30.13 C
ANISOU 1848 CB LEU A 259 3731 3880 3837 -62 112 205 C
ATOM 1849 CG LEU A 259 29.341 34.139 17.497 1.00 31.57 C
ANISOU 1849 CG LEU A 259 3918 4056 4020 -66 118 205 C
ATOM 1850 CD1 LEU A 259 29.934 34.747 18.761 1.00 32.12 C
ANISOU 1850 CD1 LEU A 259 3978 4128 4096 -66 115 205 C
ATOM 1851 CD2 LEU A 259 30.443 33.558 16.620 1.00 31.69 C
ANISOU 1851 CD2 LEU A 259 3934 4066 4040 -73 131 203 C
ATOM 1852 N GLY A 260 25.401 34.666 17.721 1.00 29.65 N
ANISOU 1852 N GLY A 260 3683 3818 3762 -51 91 206 N
ATOM 1853 CA GLY A 260 24.200 34.828 16.900 1.00 29.40 C
ANISOU 1853 CA GLY A 260 3661 3783 3727 -49 84 208 C
ATOM 1854 C GLY A 260 23.336 36.030 17.216 1.00 29.69 C
ANISOU 1854 C GLY A 260 3699 3816 3766 -45 75 207 C
ATOM 1855 O GLY A 260 23.754 36.928 17.928 1.00 29.58 O
ANISOU 1855 O GLY A 260 3681 3802 3756 -45 76 204 O
ATOM 1856 N GLU A 261 22.124 36.044 16.671 1.00 30.89 N
ANISOU 1856 N GLU A 261 3855 3964 3916 -42 66 208 N
ATOM 1857 CA GLU A 261 21.174 37.137 16.904 1.00 31.28 C
ANISOU 1857 CA GLU A 261 3904 4008 3972 -38 56 207 C
ATOM 1858 C GLU A 261 19.758 36.606 17.174 1.00 30.65 C
ANISOU 1858 C GLU A 261 3818 3930 3897 -32 49 206 C
ATOM 1859 O GLU A 261 19.590 35.427 17.482 1.00 30.01 O
ANISOU 1859 O GLU A 261 3731 3856 3814 -30 52 206 O
ATOM 1860 CB GLU A 261 21.207 38.154 15.754 1.00 32.55 C
ANISOU 1860 CB GLU A 261 4079 4157 4131 -42 50 212 C
ATOM 1861 CG GLU A 261 21.339 37.534 14.374 1.00 34.07 C
ANISOU 1861 CG GLU A 261 4285 4346 4313 -48 50 218 C
ATOM 1862 CD GLU A 261 21.557 38.556 13.269 1.00 36.21 C
ANISOU 1862 CD GLU A 261 4571 4606 4579 -56 45 224 C
ATOM 1863 OE1 GLU A 261 21.156 38.274 12.114 1.00 37.84 O
ANISOU 1863 OE1 GLU A 261 4791 4808 4778 -61 39 229 O
ATOM 1864 OE2 GLU A 261 22.124 39.636 13.537 1.00 35.70 O
ANISOU 1864 OE2 GLU A 261 4507 4539 4519 -57 46 223 O
ATOM 1865 N PHE A 262 18.754 37.479 17.089 1.00 30.84 N
ANISOU 1865 N PHE A 262 3841 3945 3929 -28 39 205 N
ATOM 1866 CA PHE A 262 17.386 37.136 17.474 1.00 30.11 C
ANISOU 1866 CA PHE A 262 3741 3854 3845 -22 33 203 C
ATOM 1867 C PHE A 262 16.424 37.536 16.389 1.00 30.81 C
ANISOU 1867 C PHE A 262 3838 3930 3939 -21 19 209 C
ATOM 1868 O PHE A 262 16.691 38.470 15.653 1.00 32.18 O
ANISOU 1868 O PHE A 262 4020 4093 4112 -25 13 213 O
ATOM 1869 CB PHE A 262 16.999 37.857 18.757 1.00 29.57 C
ANISOU 1869 CB PHE A 262 3660 3788 3787 -18 35 194 C
ATOM 1870 CG PHE A 262 17.819 37.461 19.953 1.00 29.19 C
ANISOU 1870 CG PHE A 262 3604 3752 3733 -20 47 189 C
ATOM 1871 CD1 PHE A 262 18.894 38.242 20.362 1.00 28.71 C
ANISOU 1871 CD1 PHE A 262 3545 3692 3671 -23 52 186 C
ATOM 1872 CD2 PHE A 262 17.514 36.312 20.675 1.00 28.56 C
ANISOU 1872 CD2 PHE A 262 3515 3683 3651 -19 51 188 C
ATOM 1873 CE1 PHE A 262 19.646 37.880 21.470 1.00 28.75 C
ANISOU 1873 CE1 PHE A 262 3543 3708 3672 -26 61 183 C
ATOM 1874 CE2 PHE A 262 18.261 35.949 21.784 1.00 28.06 C
ANISOU 1874 CE2 PHE A 262 3446 3632 3583 -22 59 185 C
ATOM 1875 CZ PHE A 262 19.329 36.734 22.182 1.00 28.05 C
ANISOU 1875 CZ PHE A 262 3447 3630 3580 -26 63 182 C
ATOM 1876 N LYS A 263 15.300 36.835 16.296 1.00 32.47 N
ANISOU 1876 N LYS A 263 4043 4140 4153 -17 12 210 N
ATOM 1877 CA LYS A 263 14.287 37.123 15.288 1.00 34.65 C
ANISOU 1877 CA LYS A 263 4326 4404 4436 -17 -2 216 C
ATOM 1878 C LYS A 263 13.798 38.546 15.423 1.00 35.27 C
ANISOU 1878 C LYS A 263 4400 4469 4529 -14 -11 214 C
ATOM 1879 O LYS A 263 13.600 39.252 14.428 1.00 35.43 O
ANISOU 1879 O LYS A 263 4432 4478 4552 -18 -24 221 O
ATOM 1880 CB LYS A 263 13.102 36.166 15.419 1.00 36.05 C
ANISOU 1880 CB LYS A 263 4495 4583 4619 -12 -7 216 C
ATOM 1881 CG LYS A 263 13.325 34.816 14.758 1.00 37.89 C
ANISOU 1881 CG LYS A 263 4735 4821 4838 -15 -5 221 C
ATOM 1882 CD LYS A 263 12.899 34.815 13.303 1.00 37.00 C
ANISOU 1882 CD LYS A 263 4637 4698 4721 -20 -20 230 C
ATOM 1883 CE LYS A 263 12.907 33.387 12.786 1.00 38.94 C
ANISOU 1883 CE LYS A 263 4888 4950 4956 -23 -17 232 C
ATOM 1884 NZ LYS A 263 11.710 33.052 11.961 1.00 39.16 N
ANISOU 1884 NZ LYS A 263 4920 4969 4988 -23 -34 238 N
ATOM 1885 N ASP A 264 13.629 38.954 16.673 1.00 36.07 N
ANISOU 1885 N ASP A 264 4488 4575 4641 -9 -3 204 N
ATOM 1886 CA ASP A 264 13.100 40.262 17.013 1.00 38.91 C
ANISOU 1886 CA ASP A 264 4840 4923 5019 -6 -9 199 C
ATOM 1887 C ASP A 264 14.183 41.320 17.229 1.00 39.97 C
ANISOU 1887 C ASP A 264 4979 5057 5151 -9 -4 196 C
ATOM 1888 O ASP A 264 13.897 42.390 17.751 1.00 41.09 O
ANISOU 1888 O ASP A 264 5113 5191 5308 -6 -6 189 O
ATOM 1889 CB ASP A 264 12.218 40.144 18.260 1.00 40.23 C
ANISOU 1889 CB ASP A 264 4989 5095 5199 0 -3 187 C
ATOM 1890 CG ASP A 264 12.877 39.354 19.383 1.00 39.60 C
ANISOU 1890 CG ASP A 264 4904 5034 5107 0 13 180 C
ATOM 1891 OD1 ASP A 264 12.513 39.589 20.553 1.00 41.23 O
ANISOU 1891 OD1 ASP A 264 5097 5245 5321 1 21 169 O
ATOM 1892 OD2 ASP A 264 13.740 38.495 19.105 1.00 38.06 O
ANISOU 1892 OD2 ASP A 264 4717 4848 4896 -5 18 186 O
ATOM 1893 N GLU A 265 15.411 41.019 16.804 1.00 41.74 N
ANISOU 1893 N GLU A 265 5213 5286 5357 -15 1 202 N
ATOM 1894 CA GLU A 265 16.577 41.875 17.011 1.00 43.82 C
ANISOU 1894 CA GLU A 265 5482 5550 5618 -19 8 200 C
ATOM 1895 C GLU A 265 17.701 41.398 16.086 1.00 45.69 C
ANISOU 1895 C GLU A 265 5732 5789 5836 -27 12 208 C
ATOM 1896 O GLU A 265 18.690 40.798 16.533 1.00 45.11 O
ANISOU 1896 O GLU A 265 5658 5727 5752 -29 24 206 O
ATOM 1897 CB GLU A 265 17.016 41.829 18.480 1.00 45.97 C
ANISOU 1897 CB GLU A 265 5741 5834 5890 -17 21 188 C
ATOM 1898 CG GLU A 265 18.276 42.625 18.799 1.00 52.27 C
ANISOU 1898 CG GLU A 265 6542 6632 6684 -21 28 186 C
ATOM 1899 CD GLU A 265 18.078 44.125 18.683 1.00 57.99 C
ANISOU 1899 CD GLU A 265 7267 7343 7423 -20 20 184 C
ATOM 1900 OE1 GLU A 265 17.366 44.696 19.539 1.00 65.42 O
ANISOU 1900 OE1 GLU A 265 8195 8281 8378 -15 21 174 O
ATOM 1901 OE2 GLU A 265 18.638 44.736 17.743 1.00 59.34 O
ANISOU 1901 OE2 GLU A 265 7449 7505 7591 -25 15 192 O
ATOM 1902 N ARG A 266 17.537 41.666 14.791 1.00 49.42 N
ANISOU 1902 N ARG A 266 6218 6251 6305 -32 1 218 N
ATOM 1903 CA ARG A 266 18.369 41.040 13.758 1.00 49.28 C
ANISOU 1903 CA ARG A 266 6217 6237 6270 -41 5 226 C
ATOM 1904 C ARG A 266 19.684 41.757 13.474 1.00 52.57 C
ANISOU 1904 C ARG A 266 6641 6652 6679 -48 12 227 C
ATOM 1905 O ARG A 266 20.660 41.536 14.193 1.00 61.47 O
ANISOU 1905 O ARG A 266 7763 7788 7803 -48 26 222 O
ATOM 1906 CB ARG A 266 17.568 40.796 12.489 1.00 48.29 C
ANISOU 1906 CB ARG A 266 6104 6103 6140 -45 -8 235 C
ATOM 1907 CG ARG A 266 16.592 39.650 12.641 1.00 47.52 C
ANISOU 1907 CG ARG A 266 5999 6010 6044 -40 -11 234 C
ATOM 1908 CD ARG A 266 16.131 39.164 11.288 1.00 49.21 C
ANISOU 1908 CD ARG A 266 6229 6219 6249 -46 -22 243 C
ATOM 1909 NE ARG A 266 14.966 39.892 10.796 1.00 48.60 N
ANISOU 1909 NE ARG A 266 6153 6127 6184 -46 -43 250 N
ATOM 1910 CZ ARG A 266 13.782 39.336 10.565 1.00 46.87 C
ANISOU 1910 CZ ARG A 266 5931 5904 5971 -42 -54 252 C
ATOM 1911 NH1 ARG A 266 13.603 38.041 10.779 1.00 46.31 N
ANISOU 1911 NH1 ARG A 266 5856 5844 5894 -39 -47 249 N
ATOM 1912 NH2 ARG A 266 12.777 40.077 10.113 1.00 48.02 N
ANISOU 1912 NH2 ARG A 266 6078 6035 6131 -42 -75 259 N
ATOM 1913 N ASN A 267 19.722 42.589 12.434 1.00 50.26 N
ANISOU 1913 N ASN A 267 6362 6348 6384 -55 2 236 N
ATOM 1914 CA ASN A 267 20.908 43.411 12.088 1.00 51.54 C
ANISOU 1914 CA ASN A 267 6533 6507 6541 -63 8 239 C
ATOM 1915 C ASN A 267 21.849 42.872 11.017 1.00 49.92 C
ANISOU 1915 C ASN A 267 6344 6305 6317 -75 17 244 C
ATOM 1916 O ASN A 267 22.267 43.626 10.140 1.00 52.21 O
ANISOU 1916 O ASN A 267 6648 6587 6601 -84 13 252 O
ATOM 1917 CB ASN A 267 21.734 43.823 13.324 1.00 52.08 C
ANISOU 1917 CB ASN A 267 6589 6581 6616 -59 20 230 C
ATOM 1918 CG ASN A 267 20.985 44.765 14.243 1.00 55.08 C
ANISOU 1918 CG ASN A 267 6956 6955 7015 -50 12 224 C
ATOM 1919 OD1 ASN A 267 20.310 45.698 13.791 1.00 59.92 O
ANISOU 1919 OD1 ASN A 267 7572 7555 7638 -50 -2 228 O
ATOM 1920 ND2 ASN A 267 21.101 44.528 15.545 1.00 53.92 N
ANISOU 1920 ND2 ASN A 267 6795 6817 6873 -44 21 213 N
ATOM 1921 N LEU A 268 22.206 41.595 11.087 1.00 49.54 N
ANISOU 1921 N LEU A 268 6294 6267 6260 -75 29 240 N
ATOM 1922 CA LEU A 268 23.195 41.057 10.142 1.00 51.82 C
ANISOU 1922 CA LEU A 268 6595 6559 6533 -86 41 242 C
ATOM 1923 C LEU A 268 22.643 40.830 8.731 1.00 53.68 C
ANISOU 1923 C LEU A 268 6851 6790 6756 -96 32 250 C
ATOM 1924 O LEU A 268 21.927 39.857 8.468 1.00 53.58 O
ANISOU 1924 O LEU A 268 6838 6779 6739 -94 28 250 O
ATOM 1925 CB LEU A 268 23.890 39.812 10.696 1.00 50.73 C
ANISOU 1925 CB LEU A 268 6448 6433 6394 -83 57 234 C
ATOM 1926 CG LEU A 268 25.256 40.067 11.336 1.00 49.78 C
ANISOU 1926 CG LEU A 268 6320 6315 6277 -84 72 229 C
ATOM 1927 CD1 LEU A 268 25.176 40.681 12.727 1.00 48.57 C
ANISOU 1927 CD1 LEU A 268 6152 6165 6138 -75 69 225 C
ATOM 1928 CD2 LEU A 268 26.002 38.753 11.403 1.00 51.87 C
ANISOU 1928 CD2 LEU A 268 6580 6589 6539 -86 87 224 C
ATOM 1929 N GLU A 269 22.976 41.760 7.840 1.00 55.45 N
ANISOU 1929 N GLU A 269 7089 7005 6972 -107 27 258 N
ATOM 1930 CA GLU A 269 22.556 41.720 6.442 1.00 56.61 C
ANISOU 1930 CA GLU A 269 7258 7147 7104 -120 17 268 C
ATOM 1931 C GLU A 269 23.115 40.473 5.761 1.00 58.06 C
ANISOU 1931 C GLU A 269 7450 7338 7271 -129 33 263 C
ATOM 1932 O GLU A 269 22.381 39.755 5.086 1.00 60.48 O
ANISOU 1932 O GLU A 269 7765 7645 7568 -132 26 266 O
ATOM 1933 CB GLU A 269 22.972 43.009 5.703 1.00 59.39 C
ANISOU 1933 CB GLU A 269 7624 7488 7451 -132 11 277 C
ATOM 1934 CG GLU A 269 24.480 43.240 5.484 1.00 61.91 C
ANISOU 1934 CG GLU A 269 7948 7811 7761 -142 31 274 C
ATOM 1935 CD GLU A 269 25.274 43.697 6.720 1.00 61.41 C
ANISOU 1935 CD GLU A 269 7867 7751 7714 -132 41 267 C
ATOM 1936 OE1 GLU A 269 24.764 43.668 7.858 1.00 61.73 O
ANISOU 1936 OE1 GLU A 269 7890 7794 7770 -117 37 261 O
ATOM 1937 OE2 GLU A 269 26.448 44.088 6.554 1.00 63.05 O
ANISOU 1937 OE2 GLU A 269 8078 7959 7917 -139 54 266 O
ATOM 1938 N ILE A 270 24.409 40.217 5.960 1.00 56.89 N
ANISOU 1938 N ILE A 270 7298 7196 7119 -132 55 256 N
ATOM 1939 CA ILE A 270 25.069 39.013 5.440 1.00 57.03 C
ANISOU 1939 CA ILE A 270 7321 7221 7126 -139 73 249 C
ATOM 1940 C ILE A 270 25.932 38.360 6.520 1.00 55.40 C
ANISOU 1940 C ILE A 270 7093 7022 6931 -129 90 238 C
ATOM 1941 O ILE A 270 26.418 39.035 7.438 1.00 54.24 O
ANISOU 1941 O ILE A 270 6935 6875 6797 -123 92 237 O
ATOM 1942 CB ILE A 270 25.889 39.265 4.138 1.00 58.98 C
ANISOU 1942 CB ILE A 270 7589 7466 7354 -158 83 252 C
ATOM 1943 CG1 ILE A 270 26.957 40.351 4.327 1.00 58.99 C
ANISOU 1943 CG1 ILE A 270 7589 7463 7359 -163 91 253 C
ATOM 1944 CG2 ILE A 270 24.970 39.626 2.972 1.00 62.42 C
ANISOU 1944 CG2 ILE A 270 8047 7894 7774 -170 65 263 C
ATOM 1945 CD1 ILE A 270 28.319 39.838 4.753 1.00 60.03 C
ANISOU 1945 CD1 ILE A 270 7710 7601 7496 -162 116 242 C
ATOM 1946 N PHE A 271 26.105 37.045 6.407 1.00 53.82 N
ANISOU 1946 N PHE A 271 6891 6829 6730 -129 102 231 N
ATOM 1947 CA PHE A 271 26.832 36.272 7.411 1.00 53.11 C
ANISOU 1947 CA PHE A 271 6781 6745 6653 -121 115 222 C
ATOM 1948 C PHE A 271 27.690 35.175 6.774 1.00 51.63 C
ANISOU 1948 C PHE A 271 6596 6560 6461 -129 135 214 C
ATOM 1949 O PHE A 271 27.297 34.004 6.725 1.00 51.36 O
ANISOU 1949 O PHE A 271 6557 6529 6427 -126 137 210 O
ATOM 1950 CB PHE A 271 25.862 35.706 8.462 1.00 50.76 C
ANISOU 1950 CB PHE A 271 6467 6451 6366 -106 104 222 C
ATOM 1951 CG PHE A 271 26.544 35.078 9.643 1.00 49.62 C
ANISOU 1951 CG PHE A 271 6302 6313 6236 -98 114 215 C
ATOM 1952 CD1 PHE A 271 26.355 33.737 9.932 1.00 49.01 C
ANISOU 1952 CD1 PHE A 271 6216 6242 6164 -93 117 211 C
ATOM 1953 CD2 PHE A 271 27.384 35.827 10.461 1.00 50.05 C
ANISOU 1953 CD2 PHE A 271 6348 6368 6300 -96 118 214 C
ATOM 1954 CE1 PHE A 271 26.980 33.151 11.020 1.00 50.53 C
ANISOU 1954 CE1 PHE A 271 6390 6439 6370 -87 124 206 C
ATOM 1955 CE2 PHE A 271 28.016 35.249 11.547 1.00 51.93 C
ANISOU 1955 CE2 PHE A 271 6567 6610 6550 -90 125 210 C
ATOM 1956 CZ PHE A 271 27.815 33.905 11.827 1.00 51.24 C
ANISOU 1956 CZ PHE A 271 6471 6528 6467 -86 127 206 C
ATOM 1957 N GLU A 272 28.858 35.584 6.282 1.00 51.56 N
ANISOU 1957 N GLU A 272 6592 6549 6448 -140 150 212 N
ATOM 1958 CA GLU A 272 29.770 34.714 5.541 1.00 53.25 C
ANISOU 1958 CA GLU A 272 6810 6763 6657 -150 172 202 C
ATOM 1959 C GLU A 272 30.924 34.253 6.432 1.00 48.62 C
ANISOU 1959 C GLU A 272 6202 6179 6091 -145 187 194 C
ATOM 1960 O GLU A 272 31.219 34.898 7.438 1.00 48.51 O
ANISOU 1960 O GLU A 272 6176 6164 6089 -136 182 197 O
ATOM 1961 CB GLU A 272 30.304 35.428 4.282 1.00 60.45 C
ANISOU 1961 CB GLU A 272 7743 7671 7552 -169 181 204 C
ATOM 1962 CG GLU A 272 29.367 35.384 3.069 1.00 70.84 C
ANISOU 1962 CG GLU A 272 9083 8985 8845 -180 171 209 C
ATOM 1963 CD GLU A 272 30.089 35.436 1.710 1.00 82.85 C
ANISOU 1963 CD GLU A 272 10626 10506 10347 -202 188 205 C
ATOM 1964 OE1 GLU A 272 29.433 35.759 0.685 1.00 78.21 O
ANISOU 1964 OE1 GLU A 272 10061 9916 9739 -214 178 213 O
ATOM 1965 OE2 GLU A 272 31.311 35.148 1.649 1.00 89.10 O
ANISOU 1965 OE2 GLU A 272 11411 11298 11145 -207 212 195 O
ATOM 1966 N PRO A 273 31.576 33.131 6.070 1.00 46.85 N
ANISOU 1966 N PRO A 273 5974 5956 5872 -149 205 184 N
ATOM 1967 CA PRO A 273 32.735 32.589 6.784 1.00 46.34 C
ANISOU 1967 CA PRO A 273 5888 5890 5828 -145 219 177 C
ATOM 1968 C PRO A 273 33.780 33.614 7.200 1.00 46.94 C
ANISOU 1968 C PRO A 273 5959 5963 5913 -147 225 178 C
ATOM 1969 O PRO A 273 34.441 33.410 8.207 1.00 47.46 O
ANISOU 1969 O PRO A 273 6005 6028 5998 -140 227 177 O
ATOM 1970 CB PRO A 273 33.365 31.649 5.760 1.00 44.38 C
ANISOU 1970 CB PRO A 273 5644 5639 5577 -157 241 165 C
ATOM 1971 CG PRO A 273 32.243 31.219 4.891 1.00 44.88 C
ANISOU 1971 CG PRO A 273 5725 5704 5621 -161 233 166 C
ATOM 1972 CD PRO A 273 31.103 32.193 5.038 1.00 46.34 C
ANISOU 1972 CD PRO A 273 5921 5891 5794 -157 210 179 C
ATOM 1973 N SER A 274 33.934 34.689 6.427 1.00 48.53 N
ANISOU 1973 N SER A 274 6177 6160 6099 -158 227 183 N
ATOM 1974 CA SER A 274 35.005 35.663 6.653 1.00 49.52 C
ANISOU 1974 CA SER A 274 6299 6282 6232 -161 234 184 C
ATOM 1975 C SER A 274 34.769 36.513 7.899 1.00 50.77 C
ANISOU 1975 C SER A 274 6446 6441 6400 -149 217 191 C
ATOM 1976 O SER A 274 35.707 37.057 8.474 1.00 53.75 O
ANISOU 1976 O SER A 274 6814 6816 6791 -148 222 191 O
ATOM 1977 CB SER A 274 35.200 36.565 5.430 1.00 50.76 C
ANISOU 1977 CB SER A 274 6479 6436 6370 -178 241 187 C
ATOM 1978 OG SER A 274 34.297 37.659 5.439 1.00 51.97 O
ANISOU 1978 OG SER A 274 6644 6588 6511 -176 220 199 O
ATOM 1979 N ILE A 275 33.513 36.634 8.305 1.00 49.38 N
ANISOU 1979 N ILE A 275 6272 6268 6219 -140 197 197 N
ATOM 1980 CA ILE A 275 33.175 37.281 9.567 1.00 51.27 C
ANISOU 1980 CA ILE A 275 6500 6509 6468 -128 182 202 C
ATOM 1981 C ILE A 275 33.707 36.471 10.760 1.00 51.34 C
ANISOU 1981 C ILE A 275 6488 6522 6497 -119 185 198 C
ATOM 1982 O ILE A 275 34.027 37.030 11.808 1.00 52.90 O
ANISOU 1982 O ILE A 275 6674 6720 6705 -114 179 199 O
ATOM 1983 CB ILE A 275 31.653 37.479 9.667 1.00 52.11 C
ANISOU 1983 CB ILE A 275 6613 6618 6566 -121 162 208 C
ATOM 1984 CG1 ILE A 275 31.204 38.482 8.604 1.00 52.87 C
ANISOU 1984 CG1 ILE A 275 6731 6709 6647 -131 156 215 C
ATOM 1985 CG2 ILE A 275 31.236 37.933 11.060 1.00 51.82 C
ANISOU 1985 CG2 ILE A 275 6563 6584 6541 -109 149 210 C
ATOM 1986 CD1 ILE A 275 29.757 38.327 8.209 1.00 55.15 C
ANISOU 1986 CD1 ILE A 275 7029 6998 6926 -128 139 220 C
ATOM 1987 N MET A 276 33.824 35.160 10.563 1.00 52.19 N
ANISOU 1987 N MET A 276 6589 6632 6609 -120 194 192 N
ATOM 1988 CA MET A 276 34.246 34.203 11.583 1.00 53.62 C
ANISOU 1988 CA MET A 276 6749 6814 6808 -113 195 189 C
ATOM 1989 C MET A 276 35.753 34.258 11.802 1.00 53.44 C
ANISOU 1989 C MET A 276 6715 6787 6803 -117 209 185 C
ATOM 1990 O MET A 276 36.289 33.591 12.687 1.00 51.93 O
ANISOU 1990 O MET A 276 6505 6595 6629 -112 208 183 O
ATOM 1991 CB MET A 276 33.894 32.796 11.100 1.00 58.96 C
ANISOU 1991 CB MET A 276 7424 7492 7484 -113 200 184 C
ATOM 1992 CG MET A 276 33.194 31.902 12.106 1.00 60.60 C
ANISOU 1992 CG MET A 276 7617 7705 7700 -102 188 186 C
ATOM 1993 SD MET A 276 31.409 32.017 11.934 1.00 61.06 S
ANISOU 1993 SD MET A 276 7689 7770 7741 -97 171 191 S
ATOM 1994 CE MET A 276 31.085 33.579 12.754 1.00 59.96 C
ANISOU 1994 CE MET A 276 7550 7630 7598 -92 157 198 C
ATOM 1995 N GLU A 277 36.419 35.051 10.972 1.00 53.48 N
ANISOU 1995 N GLU A 277 6730 6787 6802 -127 220 184 N
ATOM 1996 CA GLU A 277 37.878 35.099 10.858 1.00 53.07 C
ANISOU 1996 CA GLU A 277 6669 6728 6764 -133 237 178 C
ATOM 1997 C GLU A 277 38.695 35.219 12.149 1.00 48.87 C
ANISOU 1997 C GLU A 277 6117 6195 6254 -127 232 180 C
ATOM 1998 O GLU A 277 39.661 34.488 12.327 1.00 48.64 O
ANISOU 1998 O GLU A 277 6073 6161 6246 -129 242 175 O
ATOM 1999 CB GLU A 277 38.262 36.227 9.906 1.00 59.24 C
ANISOU 1999 CB GLU A 277 7467 7505 7533 -144 245 180 C
ATOM 2000 CG GLU A 277 38.556 35.772 8.493 1.00 66.48 C
ANISOU 2000 CG GLU A 277 8397 8420 8440 -157 265 172 C
ATOM 2001 CD GLU A 277 40.044 35.723 8.227 1.00 73.77 C
ANISOU 2001 CD GLU A 277 9311 9336 9380 -166 287 165 C
ATOM 2002 OE1 GLU A 277 40.686 36.798 8.246 1.00 74.43 O
ANISOU 2002 OE1 GLU A 277 9397 9416 9464 -170 290 168 O
ATOM 2003 OE2 GLU A 277 40.570 34.611 8.004 1.00 80.24 O
ANISOU 2003 OE2 GLU A 277 10120 10153 10212 -168 302 155 O
ATOM 2004 N GLY A 278 38.326 36.143 13.034 1.00 46.46 N
ANISOU 2004 N GLY A 278 5812 5893 5947 -121 216 187 N
ATOM 2005 CA GLY A 278 39.035 36.322 14.305 1.00 43.35 C
ANISOU 2005 CA GLY A 278 5402 5498 5571 -117 209 189 C
ATOM 2006 C GLY A 278 39.096 35.094 15.202 1.00 43.34 C
ANISOU 2006 C GLY A 278 5382 5498 5585 -111 204 189 C
ATOM 2007 O GLY A 278 39.912 35.029 16.116 1.00 41.87 O
ANISOU 2007 O GLY A 278 5181 5310 5417 -111 201 190 O
ATOM 2008 N LEU A 279 38.244 34.111 14.922 1.00 45.16 N
ANISOU 2008 N LEU A 279 5614 5733 5809 -108 203 187 N
ATOM 2009 CA LEU A 279 38.149 32.878 15.709 1.00 45.91 C
ANISOU 2009 CA LEU A 279 5694 5831 5918 -104 196 188 C
ATOM 2010 C LEU A 279 39.275 31.837 15.530 1.00 48.10 C
ANISOU 2010 C LEU A 279 5954 6100 6219 -107 209 183 C
ATOM 2011 O LEU A 279 39.240 30.795 16.177 1.00 52.65 O
ANISOU 2011 O LEU A 279 6517 6677 6809 -104 202 184 O
ATOM 2012 CB LEU A 279 36.777 32.221 15.488 1.00 45.42 C
ANISOU 2012 CB LEU A 279 5640 5776 5842 -99 189 189 C
ATOM 2013 CG LEU A 279 35.560 32.569 16.368 1.00 45.22 C
ANISOU 2013 CG LEU A 279 5617 5760 5804 -91 171 195 C
ATOM 2014 CD1 LEU A 279 35.768 33.748 17.313 1.00 43.81 C
ANISOU 2014 CD1 LEU A 279 5438 5583 5625 -90 162 199 C
ATOM 2015 CD2 LEU A 279 34.318 32.788 15.517 1.00 43.27 C
ANISOU 2015 CD2 LEU A 279 5386 5515 5536 -90 169 194 C
ATOM 2016 N CYS A 280 40.263 32.096 14.675 1.00 48.15 N
ANISOU 2016 N CYS A 280 5963 6099 6233 -115 227 177 N
ATOM 2017 CA CYS A 280 41.429 31.205 14.598 1.00 49.67 C
ANISOU 2017 CA CYS A 280 6137 6282 6453 -118 239 171 C
ATOM 2018 C CYS A 280 42.411 31.536 15.706 1.00 48.48 C
ANISOU 2018 C CYS A 280 5969 6125 6323 -118 231 176 C
ATOM 2019 O CYS A 280 43.263 30.720 16.072 1.00 48.14 O
ANISOU 2019 O CYS A 280 5907 6075 6309 -118 233 174 O
ATOM 2020 CB CYS A 280 42.142 31.335 13.261 1.00 53.92 C
ANISOU 2020 CB CYS A 280 6682 6812 6991 -128 264 160 C
ATOM 2021 SG CYS A 280 41.026 31.774 11.931 1.00 63.74 S
ANISOU 2021 SG CYS A 280 7955 8063 8199 -133 270 158 S
ATOM 2022 N ASP A 281 42.281 32.753 16.221 1.00 47.03 N
ANISOU 2022 N ASP A 281 5794 5946 6129 -117 221 182 N
ATOM 2023 CA ASP A 281 43.143 33.269 17.260 1.00 44.59 C
ANISOU 2023 CA ASP A 281 5472 5633 5835 -117 212 187 C
ATOM 2024 C ASP A 281 42.533 33.079 18.630 1.00 40.83 C
ANISOU 2024 C ASP A 281 4990 5165 5357 -111 189 196 C
ATOM 2025 O ASP A 281 43.076 33.556 19.614 1.00 40.37 O
ANISOU 2025 O ASP A 281 4924 5106 5308 -112 178 201 O
ATOM 2026 CB ASP A 281 43.415 34.747 17.012 1.00 49.19 C
ANISOU 2026 CB ASP A 281 6067 6215 6408 -120 215 188 C
ATOM 2027 CG ASP A 281 44.369 34.977 15.854 1.00 53.39 C
ANISOU 2027 CG ASP A 281 6600 6737 6946 -128 238 181 C
ATOM 2028 OD1 ASP A 281 45.351 34.205 15.742 1.00 54.35 O
ANISOU 2028 OD1 ASP A 281 6705 6849 7093 -132 249 176 O
ATOM 2029 OD2 ASP A 281 44.141 35.935 15.070 1.00 52.80 O
ANISOU 2029 OD2 ASP A 281 6542 6664 6853 -132 245 180 O
ATOM 2030 N VAL A 282 41.398 32.389 18.689 1.00 40.57 N
ANISOU 2030 N VAL A 282 4961 5140 5311 -106 183 197 N
ATOM 2031 CA VAL A 282 40.760 32.043 19.969 1.00 39.65 C
ANISOU 2031 CA VAL A 282 4840 5032 5192 -102 163 204 C
ATOM 2032 C VAL A 282 40.648 30.520 20.048 1.00 37.81 C
ANISOU 2032 C VAL A 282 4594 4797 4973 -101 161 205 C
ATOM 2033 O VAL A 282 40.402 29.876 19.027 1.00 37.09 O
ANISOU 2033 O VAL A 282 4506 4704 4881 -101 173 199 O
ATOM 2034 CB VAL A 282 39.378 32.753 20.183 1.00 39.19 C
ANISOU 2034 CB VAL A 282 4797 4985 5106 -98 154 206 C
ATOM 2035 CG1 VAL A 282 39.221 33.971 19.283 1.00 39.27 C
ANISOU 2035 CG1 VAL A 282 4824 4994 5101 -99 163 202 C
ATOM 2036 CG2 VAL A 282 38.207 31.822 19.948 1.00 39.18 C
ANISOU 2036 CG2 VAL A 282 4800 4990 5094 -93 151 206 C
ATOM 2037 N THR A 283 40.846 29.943 21.235 1.00 36.91 N
ANISOU 2037 N THR A 283 4466 4684 4872 -101 146 213 N
ATOM 2038 CA THR A 283 40.731 28.477 21.373 1.00 36.52 C
ANISOU 2038 CA THR A 283 4404 4633 4838 -100 142 215 C
ATOM 2039 C THR A 283 39.368 28.079 21.980 1.00 36.21 C
ANISOU 2039 C THR A 283 4370 4606 4779 -96 128 220 C
ATOM 2040 O THR A 283 39.062 28.402 23.137 1.00 36.05 O
ANISOU 2040 O THR A 283 4350 4594 4751 -97 113 227 O
ATOM 2041 CB THR A 283 41.967 27.805 22.068 1.00 35.17 C
ANISOU 2041 CB THR A 283 4210 4451 4700 -105 135 220 C
ATOM 2042 OG1 THR A 283 41.642 27.369 23.389 1.00 34.04 O
ANISOU 2042 OG1 THR A 283 4061 4314 4558 -106 113 231 O
ATOM 2043 CG2 THR A 283 43.178 28.743 22.123 1.00 34.74 C
ANISOU 2043 CG2 THR A 283 4152 4388 4658 -109 139 219 C
ATOM 2044 N ILE A 284 38.552 27.403 21.170 1.00 35.38 N
ANISOU 2044 N ILE A 284 4271 4503 4666 -93 135 215 N
ATOM 2045 CA ILE A 284 37.174 27.062 21.533 1.00 35.88 C
ANISOU 2045 CA ILE A 284 4342 4578 4712 -88 125 219 C
ATOM 2046 C ILE A 284 37.020 25.563 21.759 1.00 36.07 C
ANISOU 2046 C ILE A 284 4352 4600 4750 -88 119 222 C
ATOM 2047 O ILE A 284 37.404 24.763 20.911 1.00 37.23 O
ANISOU 2047 O ILE A 284 4494 4739 4913 -88 130 216 O
ATOM 2048 CB ILE A 284 36.186 27.487 20.415 1.00 36.44 C
ANISOU 2048 CB ILE A 284 4430 4653 4760 -84 135 212 C
ATOM 2049 CG1 ILE A 284 36.370 28.960 20.056 1.00 36.73 C
ANISOU 2049 CG1 ILE A 284 4480 4689 4784 -86 141 209 C
ATOM 2050 CG2 ILE A 284 34.742 27.242 20.819 1.00 35.48 C
ANISOU 2050 CG2 ILE A 284 4315 4542 4621 -80 124 215 C
ATOM 2051 CD1 ILE A 284 36.060 29.270 18.609 1.00 37.34 C
ANISOU 2051 CD1 ILE A 284 4573 4765 4850 -86 155 201 C
ATOM 2052 N ASP A 285 36.451 25.177 22.895 1.00 37.55 N
ANISOU 2052 N ASP A 285 4536 4797 4935 -88 102 231 N
ATOM 2053 CA ASP A 285 36.090 23.778 23.106 1.00 37.95 C
ANISOU 2053 CA ASP A 285 4575 4846 4996 -87 95 236 C
ATOM 2054 C ASP A 285 34.752 23.471 22.434 1.00 36.87 C
ANISOU 2054 C ASP A 285 4450 4717 4842 -82 99 232 C
ATOM 2055 O ASP A 285 34.667 22.554 21.624 1.00 37.29 O
ANISOU 2055 O ASP A 285 4499 4764 4903 -80 107 227 O
ATOM 2056 CB ASP A 285 36.058 23.408 24.596 1.00 41.29 C
ANISOU 2056 CB ASP A 285 4990 5275 5423 -92 75 249 C
ATOM 2057 CG ASP A 285 37.383 23.701 25.328 1.00 47.22 C
ANISOU 2057 CG ASP A 285 5729 6019 6193 -99 68 255 C
ATOM 2058 OD1 ASP A 285 37.386 23.613 26.579 1.00 51.84 O
ANISOU 2058 OD1 ASP A 285 6310 6610 6777 -104 50 266 O
ATOM 2059 OD2 ASP A 285 38.415 24.022 24.686 1.00 46.69 O
ANISOU 2059 OD2 ASP A 285 5657 5940 6141 -99 79 249 O
ATOM 2060 N GLU A 286 33.716 24.238 22.766 1.00 37.01 N
ANISOU 2060 N GLU A 286 4480 4745 4834 -79 95 233 N
ATOM 2061 CA GLU A 286 32.378 24.051 22.190 1.00 37.71 C
ANISOU 2061 CA GLU A 286 4581 4841 4907 -74 97 229 C
ATOM 2062 C GLU A 286 31.887 25.326 21.523 1.00 37.11 C
ANISOU 2062 C GLU A 286 4521 4767 4810 -71 104 223 C
ATOM 2063 O GLU A 286 32.001 26.426 22.080 1.00 38.60 O
ANISOU 2063 O GLU A 286 4715 4960 4991 -72 101 224 O
ATOM 2064 CB GLU A 286 31.374 23.601 23.251 1.00 41.48 C
ANISOU 2064 CB GLU A 286 5055 5328 5375 -73 83 237 C
ATOM 2065 CG GLU A 286 31.789 22.331 23.999 1.00 49.02 C
ANISOU 2065 CG GLU A 286 5993 6281 6349 -77 72 246 C
ATOM 2066 CD GLU A 286 30.804 21.886 25.079 1.00 54.32 C
ANISOU 2066 CD GLU A 286 6663 6964 7010 -79 59 255 C
ATOM 2067 OE1 GLU A 286 31.238 21.137 25.985 1.00 58.36 O
ANISOU 2067 OE1 GLU A 286 7162 7475 7535 -85 47 264 O
ATOM 2068 OE2 GLU A 286 29.607 22.269 25.033 1.00 55.84 O
ANISOU 2068 OE2 GLU A 286 6865 7165 7184 -75 59 252 O
ATOM 2069 N PHE A 287 31.339 25.184 20.328 1.00 34.02 N
ANISOU 2069 N PHE A 287 4139 4373 4411 -68 113 217 N
ATOM 2070 CA PHE A 287 30.903 26.340 19.578 1.00 33.20 C
ANISOU 2070 CA PHE A 287 4052 4270 4291 -67 118 212 C
ATOM 2071 C PHE A 287 29.431 26.243 19.188 1.00 32.60 C
ANISOU 2071 C PHE A 287 3986 4200 4200 -62 114 212 C
ATOM 2072 O PHE A 287 28.982 25.244 18.618 1.00 33.10 O
ANISOU 2072 O PHE A 287 4048 4261 4265 -61 115 210 O
ATOM 2073 CB PHE A 287 31.792 26.512 18.353 1.00 34.22 C
ANISOU 2073 CB PHE A 287 4186 4389 4424 -71 133 205 C
ATOM 2074 CG PHE A 287 31.426 27.680 17.494 1.00 36.10 C
ANISOU 2074 CG PHE A 287 4442 4628 4646 -71 138 202 C
ATOM 2075 CD1 PHE A 287 31.630 28.983 17.937 1.00 36.00 C
ANISOU 2075 CD1 PHE A 287 4434 4616 4626 -72 136 203 C
ATOM 2076 CD2 PHE A 287 30.891 27.483 16.232 1.00 37.25 C
ANISOU 2076 CD2 PHE A 287 4600 4770 4781 -72 145 197 C
ATOM 2077 CE1 PHE A 287 31.303 30.062 17.138 1.00 36.04 C
ANISOU 2077 CE1 PHE A 287 4455 4620 4618 -72 139 201 C
ATOM 2078 CE2 PHE A 287 30.566 28.564 15.427 1.00 38.27 C
ANISOU 2078 CE2 PHE A 287 4746 4898 4894 -74 147 196 C
ATOM 2079 CZ PHE A 287 30.770 29.855 15.882 1.00 36.68 C
ANISOU 2079 CZ PHE A 287 4548 4698 4689 -74 144 198 C
ATOM 2080 N ARG A 288 28.674 27.286 19.501 1.00 31.79 N
ANISOU 2080 N ARG A 288 3892 4102 4084 -60 108 212 N
ATOM 2081 CA ARG A 288 27.240 27.277 19.240 1.00 30.69 C
ANISOU 2081 CA ARG A 288 3760 3967 3933 -55 103 212 C
ATOM 2082 C ARG A 288 26.793 28.460 18.413 1.00 30.07 C
ANISOU 2082 C ARG A 288 3697 3885 3842 -54 105 210 C
ATOM 2083 O ARG A 288 27.074 29.605 18.741 1.00 30.75 O
ANISOU 2083 O ARG A 288 3785 3970 3924 -55 104 209 O
ATOM 2084 CB ARG A 288 26.453 27.197 20.548 1.00 31.35 C
ANISOU 2084 CB ARG A 288 3836 4059 4013 -53 93 217 C
ATOM 2085 CG ARG A 288 26.712 25.909 21.310 1.00 31.04 C
ANISOU 2085 CG ARG A 288 3783 4024 3985 -55 88 222 C
ATOM 2086 CD ARG A 288 25.449 25.367 21.945 1.00 32.88 C
ANISOU 2086 CD ARG A 288 4012 4265 4213 -52 80 225 C
ATOM 2087 NE ARG A 288 25.467 25.621 23.377 1.00 35.65 N
ANISOU 2087 NE ARG A 288 4358 4624 4563 -55 74 229 N
ATOM 2088 CZ ARG A 288 24.646 26.438 24.017 1.00 35.18 C
ANISOU 2088 CZ ARG A 288 4302 4572 4493 -54 71 227 C
ATOM 2089 NH1 ARG A 288 23.704 27.081 23.362 1.00 36.28 N
ANISOU 2089 NH1 ARG A 288 4449 4708 4624 -49 73 222 N
ATOM 2090 NH2 ARG A 288 24.771 26.602 25.323 1.00 36.94 N
ANISOU 2090 NH2 ARG A 288 4519 4801 4712 -60 66 229 N
ATOM 2091 N LEU A 289 26.111 28.163 17.319 1.00 30.44 N
ANISOU 2091 N LEU A 289 3754 3930 3883 -53 105 208 N
ATOM 2092 CA LEU A 289 25.530 29.183 16.485 1.00 31.15 C
ANISOU 2092 CA LEU A 289 3858 4015 3961 -54 104 207 C
ATOM 2093 C LEU A 289 24.034 29.200 16.621 1.00 30.74 C
ANISOU 2093 C LEU A 289 3808 3967 3904 -48 93 209 C
ATOM 2094 O LEU A 289 23.366 28.177 16.451 1.00 30.80 O
ANISOU 2094 O LEU A 289 3813 3975 3912 -46 90 210 O
ATOM 2095 CB LEU A 289 25.920 28.978 15.032 1.00 33.64 C
ANISOU 2095 CB LEU A 289 4186 4324 4272 -59 112 204 C
ATOM 2096 CG LEU A 289 27.125 29.855 14.699 1.00 37.07 C
ANISOU 2096 CG LEU A 289 4624 4753 4706 -65 122 202 C
ATOM 2097 CD1 LEU A 289 27.976 29.244 13.592 1.00 37.15 C
ANISOU 2097 CD1 LEU A 289 4639 4757 4716 -73 136 197 C
ATOM 2098 CD2 LEU A 289 26.650 31.264 14.353 1.00 36.54 C
ANISOU 2098 CD2 LEU A 289 4570 4683 4628 -66 116 204 C
ATOM 2099 N THR A 290 23.511 30.377 16.931 1.00 30.40 N
ANISOU 2099 N THR A 290 3769 3923 3857 -46 87 209 N
ATOM 2100 CA THR A 290 22.077 30.562 17.052 1.00 30.67 C
ANISOU 2100 CA THR A 290 3803 3958 3889 -40 77 210 C
ATOM 2101 C THR A 290 21.493 31.271 15.825 1.00 31.64 C
ANISOU 2101 C THR A 290 3942 4073 4006 -42 72 212 C
ATOM 2102 O THR A 290 22.199 31.526 14.845 1.00 31.09 O
ANISOU 2102 O THR A 290 3883 3997 3930 -48 77 212 O
ATOM 2103 CB THR A 290 21.725 31.320 18.340 1.00 30.32 C
ANISOU 2103 CB THR A 290 3751 3918 3848 -37 74 209 C
ATOM 2104 OG1 THR A 290 22.144 32.690 18.230 1.00 29.82 O
ANISOU 2104 OG1 THR A 290 3694 3850 3784 -39 74 207 O
ATOM 2105 CG2 THR A 290 22.387 30.652 19.547 1.00 28.89 C
ANISOU 2105 CG2 THR A 290 3557 3746 3672 -39 77 209 C
ATOM 2106 N TYR A 291 20.197 31.575 15.878 1.00 33.55 N
ANISOU 2106 N TYR A 291 4184 4313 4249 -37 62 213 N
ATOM 2107 CA TYR A 291 19.521 32.217 14.761 1.00 34.02 C
ANISOU 2107 CA TYR A 291 4256 4363 4304 -38 53 216 C
ATOM 2108 C TYR A 291 20.370 33.335 14.188 1.00 34.24 C
ANISOU 2108 C TYR A 291 4296 4386 4328 -44 56 217 C
ATOM 2109 O TYR A 291 20.972 34.120 14.922 1.00 33.65 O
ANISOU 2109 O TYR A 291 4216 4312 4257 -44 60 214 O
ATOM 2110 CB TYR A 291 18.157 32.770 15.182 1.00 34.43 C
ANISOU 2110 CB TYR A 291 4304 4413 4363 -32 42 216 C
ATOM 2111 CG TYR A 291 17.489 33.582 14.093 1.00 36.06 C
ANISOU 2111 CG TYR A 291 4523 4608 4568 -34 30 221 C
ATOM 2112 CD1 TYR A 291 16.808 32.955 13.048 1.00 35.23 C
ANISOU 2112 CD1 TYR A 291 4428 4499 4459 -36 22 225 C
ATOM 2113 CD2 TYR A 291 17.560 34.981 14.088 1.00 35.75 C
ANISOU 2113 CD2 TYR A 291 4488 4562 4533 -34 26 221 C
ATOM 2114 CE1 TYR A 291 16.213 33.692 12.040 1.00 35.44 C
ANISOU 2114 CE1 TYR A 291 4466 4514 4483 -40 9 231 C
ATOM 2115 CE2 TYR A 291 16.953 35.724 13.086 1.00 35.75 C
ANISOU 2115 CE2 TYR A 291 4499 4550 4532 -37 13 227 C
ATOM 2116 CZ TYR A 291 16.282 35.077 12.064 1.00 36.22 C
ANISOU 2116 CZ TYR A 291 4568 4605 4586 -40 4 232 C
ATOM 2117 OH TYR A 291 15.678 35.810 11.059 1.00 36.94 O
ANISOU 2117 OH TYR A 291 4672 4685 4677 -45 -10 240 O
ATOM 2118 N THR A 292 20.428 33.387 12.868 1.00 36.44 N
ANISOU 2118 N THR A 292 4589 4657 4596 -51 55 220 N
ATOM 2119 CA THR A 292 21.021 34.522 12.186 1.00 39.76 C
ANISOU 2119 CA THR A 292 5023 5071 5012 -58 55 222 C
ATOM 2120 C THR A 292 20.067 34.903 11.079 1.00 42.06 C
ANISOU 2120 C THR A 292 5328 5353 5297 -61 41 229 C
ATOM 2121 O THR A 292 19.323 34.059 10.573 1.00 43.26 O
ANISOU 2121 O THR A 292 5484 5506 5447 -61 36 230 O
ATOM 2122 CB THR A 292 22.420 34.224 11.614 1.00 40.67 C
ANISOU 2122 CB THR A 292 5144 5186 5119 -67 70 220 C
ATOM 2123 OG1 THR A 292 23.049 33.173 12.360 1.00 42.99 O
ANISOU 2123 OG1 THR A 292 5425 5489 5420 -64 81 215 O
ATOM 2124 CG2 THR A 292 23.283 35.456 11.712 1.00 42.26 C
ANISOU 2124 CG2 THR A 292 5348 5384 5321 -70 74 221 C
ATOM 2125 N ASN A 293 20.060 36.184 10.733 1.00 44.21 N
ANISOU 2125 N ASN A 293 5608 5617 5570 -65 34 233 N
ATOM 2126 CA ASN A 293 19.195 36.690 9.676 1.00 45.66 C
ANISOU 2126 CA ASN A 293 5807 5792 5750 -70 18 241 C
ATOM 2127 C ASN A 293 19.573 36.034 8.340 1.00 44.72 C
ANISOU 2127 C ASN A 293 5706 5672 5613 -82 22 244 C
ATOM 2128 O ASN A 293 18.770 35.318 7.748 1.00 46.82 O
ANISOU 2128 O ASN A 293 5978 5937 5874 -84 14 246 O
ATOM 2129 CB ASN A 293 19.282 38.223 9.648 1.00 48.63 C
ANISOU 2129 CB ASN A 293 6186 6158 6131 -71 10 245 C
ATOM 2130 CG ASN A 293 18.479 38.849 8.529 1.00 49.23 C
ANISOU 2130 CG ASN A 293 6278 6222 6204 -78 -8 256 C
ATOM 2131 OD1 ASN A 293 18.983 39.730 7.830 1.00 49.91 O
ANISOU 2131 OD1 ASN A 293 6377 6301 6283 -88 -11 262 O
ATOM 2132 ND2 ASN A 293 17.230 38.408 8.353 1.00 47.54 N
ANISOU 2132 ND2 ASN A 293 6062 6004 5995 -74 -22 259 N
ATOM 2133 N ASP A 294 20.813 36.247 7.907 1.00 44.87 N
ANISOU 2133 N ASP A 294 5733 5692 5622 -91 35 242 N
ATOM 2134 CA ASP A 294 21.407 35.538 6.772 1.00 44.21 C
ANISOU 2134 CA ASP A 294 5665 5609 5521 -104 46 241 C
ATOM 2135 C ASP A 294 22.228 34.376 7.317 1.00 42.37 C
ANISOU 2135 C ASP A 294 5420 5386 5292 -101 64 232 C
ATOM 2136 O ASP A 294 22.675 34.425 8.466 1.00 44.18 O
ANISOU 2136 O ASP A 294 5632 5619 5534 -92 71 227 O
ATOM 2137 CB ASP A 294 22.331 36.492 5.994 1.00 47.38 C
ANISOU 2137 CB ASP A 294 6082 6007 5912 -117 51 245 C
ATOM 2138 CG ASP A 294 22.853 35.892 4.686 1.00 49.29 C
ANISOU 2138 CG ASP A 294 6343 6249 6135 -133 62 244 C
ATOM 2139 OD1 ASP A 294 22.038 35.320 3.922 1.00 50.29 O
ANISOU 2139 OD1 ASP A 294 6481 6375 6252 -138 52 246 O
ATOM 2140 OD2 ASP A 294 24.076 36.005 4.420 1.00 47.58 O
ANISOU 2140 OD2 ASP A 294 6130 6034 5912 -142 80 239 O
ATOM 2141 N PHE A 295 22.417 33.333 6.509 1.00 39.34 N
ANISOU 2141 N PHE A 295 5044 5004 4898 -108 73 228 N
ATOM 2142 CA PHE A 295 23.341 32.241 6.848 1.00 38.03 C
ANISOU 2142 CA PHE A 295 4868 4845 4737 -107 92 218 C
ATOM 2143 C PHE A 295 23.891 31.549 5.599 1.00 38.84 C
ANISOU 2143 C PHE A 295 4984 4946 4824 -121 105 213 C
ATOM 2144 O PHE A 295 23.141 31.009 4.791 1.00 40.94 O
ANISOU 2144 O PHE A 295 5263 5212 5081 -126 98 214 O
ATOM 2145 CB PHE A 295 22.698 31.210 7.797 1.00 36.15 C
ANISOU 2145 CB PHE A 295 4611 4612 4511 -94 88 216 C
ATOM 2146 CG PHE A 295 23.671 30.200 8.351 1.00 34.46 C
ANISOU 2146 CG PHE A 295 4383 4403 4307 -92 104 207 C
ATOM 2147 CD1 PHE A 295 24.402 30.473 9.501 1.00 35.37 C
ANISOU 2147 CD1 PHE A 295 4482 4522 4435 -86 110 206 C
ATOM 2148 CD2 PHE A 295 23.853 28.971 7.728 1.00 34.45 C
ANISOU 2148 CD2 PHE A 295 4383 4402 4303 -97 113 201 C
ATOM 2149 CE1 PHE A 295 25.308 29.544 10.012 1.00 35.83 C
ANISOU 2149 CE1 PHE A 295 4525 4582 4504 -84 122 200 C
ATOM 2150 CE2 PHE A 295 24.760 28.041 8.222 1.00 34.30 C
ANISOU 2150 CE2 PHE A 295 4349 4386 4296 -95 127 194 C
ATOM 2151 CZ PHE A 295 25.488 28.326 9.366 1.00 34.87 C
ANISOU 2151 CZ PHE A 295 4405 4461 4382 -89 131 194 C
ATOM 2152 N SER A 296 25.209 31.563 5.460 1.00 40.34 N
ANISOU 2152 N SER A 296 5174 5137 5015 -128 124 207 N
ATOM 2153 CA SER A 296 25.882 30.877 4.370 1.00 40.13 C
ANISOU 2153 CA SER A 296 5159 5110 4977 -141 141 199 C
ATOM 2154 C SER A 296 26.091 29.411 4.757 1.00 40.65 C
ANISOU 2154 C SER A 296 5209 5179 5055 -135 152 189 C
ATOM 2155 O SER A 296 26.579 29.130 5.836 1.00 39.96 O
ANISOU 2155 O SER A 296 5101 5094 4986 -125 156 186 O
ATOM 2156 CB SER A 296 27.223 31.563 4.093 1.00 38.56 C
ANISOU 2156 CB SER A 296 4965 4909 4776 -151 159 195 C
ATOM 2157 OG SER A 296 28.087 30.714 3.363 1.00 39.56 O
ANISOU 2157 OG SER A 296 5094 5036 4899 -162 181 184 O
ATOM 2158 N ASP A 297 25.729 28.476 3.882 1.00 43.17 N
ANISOU 2158 N ASP A 297 5538 5498 5365 -142 155 184 N
ATOM 2159 CA ASP A 297 25.921 27.054 4.180 1.00 42.79 C
ANISOU 2159 CA ASP A 297 5475 5451 5329 -137 164 174 C
ATOM 2160 C ASP A 297 27.374 26.718 4.495 1.00 43.20 C
ANISOU 2160 C ASP A 297 5513 5503 5396 -139 186 164 C
ATOM 2161 O ASP A 297 27.645 25.934 5.402 1.00 42.52 O
ANISOU 2161 O ASP A 297 5406 5419 5331 -129 189 161 O
ATOM 2162 CB ASP A 297 25.386 26.159 3.055 1.00 43.28 C
ANISOU 2162 CB ASP A 297 5552 5513 5378 -147 166 169 C
ATOM 2163 CG ASP A 297 23.860 26.016 3.080 1.00 47.09 C
ANISOU 2163 CG ASP A 297 6040 5997 5856 -141 142 177 C
ATOM 2164 OD1 ASP A 297 23.329 25.244 2.260 1.00 46.97 O
ANISOU 2164 OD1 ASP A 297 6034 5980 5830 -147 140 174 O
ATOM 2165 OD2 ASP A 297 23.177 26.666 3.910 1.00 51.01 O
ANISOU 2165 OD2 ASP A 297 6528 6494 6359 -129 125 188 O
ATOM 2166 N ASP A 298 28.311 27.337 3.782 1.00 46.51 N
ANISOU 2166 N ASP A 298 5944 5920 5807 -151 202 160 N
ATOM 2167 CA ASP A 298 29.722 26.976 3.956 1.00 49.51 C
ANISOU 2167 CA ASP A 298 6310 6297 6203 -154 225 149 C
ATOM 2168 C ASP A 298 30.425 27.563 5.184 1.00 48.16 C
ANISOU 2168 C ASP A 298 6121 6127 6052 -144 223 154 C
ATOM 2169 O ASP A 298 31.642 27.490 5.290 1.00 48.24 O
ANISOU 2169 O ASP A 298 6120 6133 6074 -148 241 147 O
ATOM 2170 CB ASP A 298 30.545 27.155 2.665 1.00 53.00 C
ANISOU 2170 CB ASP A 298 6769 6736 6630 -173 246 140 C
ATOM 2171 CG ASP A 298 30.546 28.580 2.141 1.00 59.73 C
ANISOU 2171 CG ASP A 298 7642 7588 7463 -183 242 149 C
ATOM 2172 OD1 ASP A 298 30.505 29.534 2.942 1.00 63.58 O
ANISOU 2172 OD1 ASP A 298 8123 8076 7957 -174 230 159 O
ATOM 2173 OD2 ASP A 298 30.613 28.746 0.902 1.00 64.00 O
ANISOU 2173 OD2 ASP A 298 8205 8127 7982 -200 251 145 O
ATOM 2174 N ILE A 299 29.670 28.110 6.128 1.00 47.94 N
ANISOU 2174 N ILE A 299 6086 6102 6026 -133 203 165 N
ATOM 2175 CA ILE A 299 30.297 28.540 7.370 1.00 51.07 C
ANISOU 2175 CA ILE A 299 6464 6499 6440 -124 201 168 C
ATOM 2176 C ILE A 299 30.691 27.358 8.272 1.00 54.50 C
ANISOU 2176 C ILE A 299 6875 6934 6898 -115 205 164 C
ATOM 2177 O ILE A 299 31.641 27.450 9.052 1.00 57.28 O
ANISOU 2177 O ILE A 299 7212 7284 7267 -112 210 163 O
ATOM 2178 CB ILE A 299 29.544 29.711 8.095 1.00 51.44 C
ANISOU 2178 CB ILE A 299 6513 6548 6482 -116 182 180 C
ATOM 2179 CG1 ILE A 299 29.704 29.667 9.625 1.00 52.06 C
ANISOU 2179 CG1 ILE A 299 6570 6630 6579 -104 175 183 C
ATOM 2180 CG2 ILE A 299 28.082 29.800 7.711 1.00 50.42 C
ANISOU 2180 CG2 ILE A 299 6396 6420 6338 -114 165 186 C
ATOM 2181 CD1 ILE A 299 28.865 28.632 10.337 1.00 50.69 C
ANISOU 2181 CD1 ILE A 299 6384 6461 6413 -94 164 184 C
ATOM 2182 N VAL A 300 29.990 26.234 8.133 1.00 56.10 N
ANISOU 2182 N VAL A 300 7075 7137 7101 -112 201 161 N
ATOM 2183 CA VAL A 300 30.317 25.023 8.896 1.00 53.10 C
ANISOU 2183 CA VAL A 300 6674 6758 6745 -106 203 158 C
ATOM 2184 C VAL A 300 31.631 24.402 8.427 1.00 52.90 C
ANISOU 2184 C VAL A 300 6640 6725 6734 -113 225 146 C
ATOM 2185 O VAL A 300 32.270 23.659 9.167 1.00 53.26 O
ANISOU 2185 O VAL A 300 6665 6768 6804 -108 227 144 O
ATOM 2186 CB VAL A 300 29.188 23.953 8.846 1.00 55.56 C
ANISOU 2186 CB VAL A 300 6983 7071 7053 -101 192 158 C
ATOM 2187 CG1 VAL A 300 27.905 24.495 9.462 1.00 52.91 C
ANISOU 2187 CG1 VAL A 300 6652 6742 6708 -92 171 170 C
ATOM 2188 CG2 VAL A 300 28.948 23.428 7.427 1.00 55.08 C
ANISOU 2188 CG2 VAL A 300 6939 7007 6979 -110 202 149 C
ATOM 2189 N LYS A 301 32.024 24.719 7.197 1.00 51.45 N
ANISOU 2189 N LYS A 301 6472 6537 6536 -125 240 138 N
ATOM 2190 CA LYS A 301 33.214 24.151 6.577 1.00 50.43 C
ANISOU 2190 CA LYS A 301 6338 6401 6420 -134 265 124 C
ATOM 2191 C LYS A 301 34.455 25.024 6.838 1.00 49.39 C
ANISOU 2191 C LYS A 301 6200 6266 6299 -138 275 123 C
ATOM 2192 O LYS A 301 35.546 24.741 6.337 1.00 51.12 O
ANISOU 2192 O LYS A 301 6414 6478 6530 -146 297 112 O
ATOM 2193 CB LYS A 301 32.937 23.914 5.077 1.00 54.66 C
ANISOU 2193 CB LYS A 301 6895 6936 6934 -148 277 114 C
ATOM 2194 CG LYS A 301 34.043 24.307 4.099 1.00 62.54 C
ANISOU 2194 CG LYS A 301 7902 7929 7928 -163 303 103 C
ATOM 2195 CD LYS A 301 33.536 24.486 2.666 1.00 66.29 C
ANISOU 2195 CD LYS A 301 8407 8406 8372 -179 310 98 C
ATOM 2196 CE LYS A 301 34.072 25.758 1.998 1.00 68.21 C
ANISOU 2196 CE LYS A 301 8669 8650 8598 -192 319 100 C
ATOM 2197 NZ LYS A 301 35.528 26.036 2.197 1.00 64.63 N
ANISOU 2197 NZ LYS A 301 8202 8191 8163 -196 340 92 N
ATOM 2198 N PHE A 302 34.288 26.060 7.655 1.00 48.47 N
ANISOU 2198 N PHE A 302 6084 6154 6179 -132 261 136 N
ATOM 2199 CA PHE A 302 35.339 27.042 7.912 1.00 49.98 C
ANISOU 2199 CA PHE A 302 6270 6340 6376 -135 268 137 C
ATOM 2200 C PHE A 302 36.503 26.426 8.670 1.00 50.49 C
ANISOU 2200 C PHE A 302 6310 6400 6474 -132 276 132 C
ATOM 2201 O PHE A 302 36.315 25.817 9.724 1.00 54.53 O
ANISOU 2201 O PHE A 302 6805 6913 7002 -122 263 138 O
ATOM 2202 CB PHE A 302 34.760 28.232 8.683 1.00 54.87 C
ANISOU 2202 CB PHE A 302 6895 6966 6986 -128 248 150 C
ATOM 2203 CG PHE A 302 35.665 29.435 8.735 1.00 59.80 C
ANISOU 2203 CG PHE A 302 7521 7587 7610 -133 255 153 C
ATOM 2204 CD1 PHE A 302 36.098 30.057 7.560 1.00 59.67 C
ANISOU 2204 CD1 PHE A 302 7523 7568 7580 -146 270 148 C
ATOM 2205 CD2 PHE A 302 36.059 29.971 9.963 1.00 59.75 C
ANISOU 2205 CD2 PHE A 302 7501 7581 7618 -125 245 159 C
ATOM 2206 CE1 PHE A 302 36.923 31.171 7.611 1.00 60.33 C
ANISOU 2206 CE1 PHE A 302 7608 7648 7665 -151 275 150 C
ATOM 2207 CE2 PHE A 302 36.885 31.085 10.017 1.00 61.20 C
ANISOU 2207 CE2 PHE A 302 7687 7762 7804 -130 250 161 C
ATOM 2208 CZ PHE A 302 37.317 31.685 8.842 1.00 62.54 C
ANISOU 2208 CZ PHE A 302 7873 7928 7961 -142 265 157 C
ATOM 2209 N HIS A 303 37.704 26.596 8.124 1.00 50.79 N
ANISOU 2209 N HIS A 303 6346 6430 6522 -141 297 123 N
ATOM 2210 CA HIS A 303 38.921 25.928 8.613 1.00 50.68 C
ANISOU 2210 CA HIS A 303 6306 6407 6542 -140 308 117 C
ATOM 2211 C HIS A 303 39.263 26.206 10.059 1.00 52.72 C
ANISOU 2211 C HIS A 303 6546 6665 6819 -130 291 128 C
ATOM 2212 O HIS A 303 39.925 25.392 10.707 1.00 54.28 O
ANISOU 2212 O HIS A 303 6720 6856 7046 -127 291 126 O
ATOM 2213 CB HIS A 303 40.108 26.291 7.728 1.00 47.88 C
ANISOU 2213 CB HIS A 303 5954 6045 6193 -153 334 105 C
ATOM 2214 CG HIS A 303 40.528 27.741 7.846 1.00 47.80 C
ANISOU 2214 CG HIS A 303 5952 6036 6173 -156 333 112 C
ATOM 2215 ND1 HIS A 303 39.750 28.764 7.417 1.00 47.17 N
ANISOU 2215 ND1 HIS A 303 5896 5963 6062 -159 325 120 N
ATOM 2216 CD2 HIS A 303 41.677 28.320 8.382 1.00 45.57 C
ANISOU 2216 CD2 HIS A 303 5656 5747 5911 -156 338 114 C
ATOM 2217 CE1 HIS A 303 40.371 29.932 7.661 1.00 45.28 C
ANISOU 2217 CE1 HIS A 303 5658 5722 5823 -161 325 125 C
ATOM 2218 NE2 HIS A 303 41.551 29.660 8.250 1.00 44.32 N
ANISOU 2218 NE2 HIS A 303 5514 5592 5732 -160 333 121 N
ATOM 2219 N CYS A 304 38.829 27.349 10.582 1.00 52.44 N
ANISOU 2219 N CYS A 304 6520 6637 6768 -127 276 139 N
ATOM 2220 CA CYS A 304 39.144 27.701 11.963 1.00 54.84 C
ANISOU 2220 CA CYS A 304 6808 6940 7086 -119 261 149 C
ATOM 2221 C CYS A 304 38.209 26.996 12.962 1.00 55.20 C
ANISOU 2221 C CYS A 304 6846 6993 7133 -110 240 157 C
ATOM 2222 O CYS A 304 38.317 27.205 14.170 1.00 60.44 O
ANISOU 2222 O CYS A 304 7498 7659 7806 -104 225 166 O
ATOM 2223 CB CYS A 304 39.214 29.237 12.155 1.00 59.73 C
ANISOU 2223 CB CYS A 304 7440 7564 7691 -121 255 156 C
ATOM 2224 SG CYS A 304 40.488 30.004 11.093 1.00 67.65 S
ANISOU 2224 SG CYS A 304 8449 8558 8696 -134 280 147 S
ATOM 2225 N LEU A 305 37.321 26.136 12.452 1.00 49.14 N
ANISOU 2225 N LEU A 305 6084 6228 6357 -108 239 154 N
ATOM 2226 CA LEU A 305 36.469 25.283 13.292 1.00 45.15 C
ANISOU 2226 CA LEU A 305 5570 5728 5856 -100 222 161 C
ATOM 2227 C LEU A 305 36.925 23.825 13.266 1.00 44.70 C
ANISOU 2227 C LEU A 305 5494 5664 5824 -100 228 154 C
ATOM 2228 O LEU A 305 36.209 22.934 13.734 1.00 43.12 O
ANISOU 2228 O LEU A 305 5288 5467 5628 -94 216 159 O
ATOM 2229 CB LEU A 305 35.008 25.347 12.844 1.00 44.66 C
ANISOU 2229 CB LEU A 305 5525 5674 5767 -97 214 163 C
ATOM 2230 CG LEU A 305 34.311 26.697 12.658 1.00 45.46 C
ANISOU 2230 CG LEU A 305 5646 5782 5843 -97 207 168 C
ATOM 2231 CD1 LEU A 305 32.925 26.460 12.084 1.00 44.14 C
ANISOU 2231 CD1 LEU A 305 5494 5621 5656 -95 199 169 C
ATOM 2232 CD2 LEU A 305 34.238 27.506 13.951 1.00 44.60 C
ANISOU 2232 CD2 LEU A 305 5531 5678 5735 -92 192 178 C
ATOM 2233 N ALA A 306 38.117 23.589 12.722 1.00 43.33 N
ANISOU 2233 N ALA A 306 5312 5479 5670 -106 246 144 N
ATOM 2234 CA ALA A 306 38.646 22.244 12.563 1.00 40.53 C
ANISOU 2234 CA ALA A 306 4939 5115 5344 -107 255 136 C
ATOM 2235 C ALA A 306 38.884 21.546 13.902 1.00 39.52 C
ANISOU 2235 C ALA A 306 4788 4984 5242 -101 237 146 C
ATOM 2236 O ALA A 306 38.552 20.373 14.063 1.00 37.60 O
ANISOU 2236 O ALA A 306 4535 4739 5013 -98 231 146 O
ATOM 2237 CB ALA A 306 39.927 22.280 11.748 1.00 39.53 C
ANISOU 2237 CB ALA A 306 4807 4976 5234 -115 280 122 C
ATOM 2238 N ASN A 307 39.458 22.275 14.854 1.00 39.65 N
ANISOU 2238 N ASN A 307 4797 5000 5265 -100 227 155 N
ATOM 2239 CA ASN A 307 39.858 21.697 16.133 1.00 38.76 C
ANISOU 2239 CA ASN A 307 4662 4884 5178 -97 209 166 C
ATOM 2240 C ASN A 307 38.769 21.790 17.194 1.00 35.99 C
ANISOU 2240 C ASN A 307 4317 4547 4810 -91 185 180 C
ATOM 2241 O ASN A 307 38.959 21.358 18.325 1.00 37.27 O
ANISOU 2241 O ASN A 307 4464 4708 4988 -90 169 190 O
ATOM 2242 CB ASN A 307 41.192 22.297 16.625 1.00 41.36 C
ANISOU 2242 CB ASN A 307 4980 5205 5529 -101 211 168 C
ATOM 2243 CG ASN A 307 42.384 21.904 15.736 1.00 46.26 C
ANISOU 2243 CG ASN A 307 5589 5810 6177 -106 234 154 C
ATOM 2244 OD1 ASN A 307 42.200 21.383 14.627 1.00 45.94 O
ANISOU 2244 OD1 ASN A 307 5553 5766 6133 -108 252 140 O
ATOM 2245 ND2 ASN A 307 43.615 22.162 16.218 1.00 45.11 N
ANISOU 2245 ND2 ASN A 307 5426 5654 6059 -109 234 155 N
ATOM 2246 N VAL A 308 37.620 22.337 16.826 1.00 32.99 N
ANISOU 2246 N VAL A 308 3957 4178 4397 -89 184 180 N
ATOM 2247 CA VAL A 308 36.507 22.440 17.770 1.00 31.96 C
ANISOU 2247 CA VAL A 308 3832 4060 4251 -84 164 192 C
ATOM 2248 C VAL A 308 36.018 21.043 18.171 1.00 30.64 C
ANISOU 2248 C VAL A 308 3652 3893 4096 -81 154 196 C
ATOM 2249 O VAL A 308 35.897 20.160 17.326 1.00 30.37 O
ANISOU 2249 O VAL A 308 3615 3852 4068 -81 164 187 O
ATOM 2250 CB VAL A 308 35.367 23.332 17.208 1.00 30.19 C
ANISOU 2250 CB VAL A 308 3631 3846 3993 -82 165 190 C
ATOM 2251 CG1 VAL A 308 34.062 23.105 17.941 1.00 28.70 C
ANISOU 2251 CG1 VAL A 308 3445 3668 3789 -77 148 199 C
ATOM 2252 CG2 VAL A 308 35.775 24.788 17.302 1.00 30.02 C
ANISOU 2252 CG2 VAL A 308 3618 3826 3960 -84 167 191 C
ATOM 2253 N SER A 309 35.762 20.840 19.458 1.00 30.20 N
ANISOU 2253 N SER A 309 3588 3842 4043 -80 135 208 N
ATOM 2254 CA SER A 309 35.357 19.524 19.932 1.00 31.12 C
ANISOU 2254 CA SER A 309 3692 3959 4173 -79 124 214 C
ATOM 2255 C SER A 309 33.840 19.298 19.907 1.00 30.65 C
ANISOU 2255 C SER A 309 3644 3911 4091 -74 117 216 C
ATOM 2256 O SER A 309 33.404 18.209 19.587 1.00 32.05 O
ANISOU 2256 O SER A 309 3816 4085 4276 -72 116 215 O
ATOM 2257 CB SER A 309 35.916 19.244 21.320 1.00 31.84 C
ANISOU 2257 CB SER A 309 3767 4048 4282 -82 105 227 C
ATOM 2258 OG SER A 309 34.864 19.258 22.259 1.00 35.06 O
ANISOU 2258 OG SER A 309 4180 4470 4671 -81 89 238 O
ATOM 2259 N ALA A 310 33.042 20.304 20.265 1.00 30.16 N
ANISOU 2259 N ALA A 310 3596 3860 4002 -72 111 220 N
ATOM 2260 CA ALA A 310 31.580 20.229 20.068 1.00 29.52 C
ANISOU 2260 CA ALA A 310 3526 3788 3899 -68 107 220 C
ATOM 2261 C ALA A 310 31.073 21.355 19.177 1.00 29.48 C
ANISOU 2261 C ALA A 310 3542 3787 3872 -66 117 213 C
ATOM 2262 O ALA A 310 31.326 22.528 19.445 1.00 30.40 O
ANISOU 2262 O ALA A 310 3665 3906 3979 -67 117 214 O
ATOM 2263 CB ALA A 310 30.839 20.222 21.393 1.00 28.39 C
ANISOU 2263 CB ALA A 310 3381 3656 3748 -68 90 232 C
ATOM 2264 N MET A 311 30.365 20.986 18.116 1.00 29.55 N
ANISOU 2264 N MET A 311 3560 3794 3872 -64 123 207 N
ATOM 2265 CA MET A 311 29.814 21.940 17.164 1.00 30.94 C
ANISOU 2265 CA MET A 311 3756 3973 4027 -64 130 201 C
ATOM 2266 C MET A 311 28.291 21.928 17.247 1.00 31.20 C
ANISOU 2266 C MET A 311 3797 4013 4043 -59 119 205 C
ATOM 2267 O MET A 311 27.668 20.864 17.326 1.00 30.70 O
ANISOU 2267 O MET A 311 3728 3952 3985 -56 114 207 O
ATOM 2268 CB MET A 311 30.285 21.584 15.749 1.00 33.19 C
ANISOU 2268 CB MET A 311 4046 4248 4314 -68 146 190 C
ATOM 2269 CG MET A 311 29.687 22.410 14.620 1.00 34.78 C
ANISOU 2269 CG MET A 311 4270 4451 4493 -69 152 186 C
ATOM 2270 SD MET A 311 30.114 24.166 14.675 1.00 38.74 S
ANISOU 2270 SD MET A 311 4782 4954 4981 -72 154 187 S
ATOM 2271 CE MET A 311 31.832 24.095 15.176 1.00 36.50 C
ANISOU 2271 CE MET A 311 4482 4663 4722 -76 163 186 C
ATOM 2272 N SER A 312 27.684 23.109 17.218 1.00 31.57 N
ANISOU 2272 N SER A 312 3857 4065 4073 -57 116 206 N
ATOM 2273 CA SER A 312 26.240 23.194 17.415 1.00 31.47 C
ANISOU 2273 CA SER A 312 3849 4059 4048 -53 106 209 C
ATOM 2274 C SER A 312 25.539 24.273 16.578 1.00 30.58 C
ANISOU 2274 C SER A 312 3754 3946 3917 -52 107 207 C
ATOM 2275 O SER A 312 26.037 25.387 16.436 1.00 30.72 O
ANISOU 2275 O SER A 312 3780 3962 3930 -54 111 206 O
ATOM 2276 CB SER A 312 25.951 23.390 18.896 1.00 31.56 C
ANISOU 2276 CB SER A 312 3851 4078 4059 -51 96 216 C
ATOM 2277 OG SER A 312 24.573 23.327 19.144 1.00 33.44 O
ANISOU 2277 OG SER A 312 4092 4323 4289 -46 87 219 O
ATOM 2278 N LEU A 313 24.381 23.925 16.026 1.00 28.63 N
ANISOU 2278 N LEU A 313 3514 3700 3663 -49 101 207 N
ATOM 2279 CA LEU A 313 23.575 24.868 15.267 1.00 27.61 C
ANISOU 2279 CA LEU A 313 3401 3569 3520 -49 98 206 C
ATOM 2280 C LEU A 313 22.114 24.810 15.706 1.00 27.05 C
ANISOU 2280 C LEU A 313 3329 3503 3445 -43 86 210 C
ATOM 2281 O LEU A 313 21.513 23.745 15.718 1.00 26.93 O
ANISOU 2281 O LEU A 313 3308 3489 3434 -40 82 212 O
ATOM 2282 CB LEU A 313 23.680 24.589 13.759 1.00 28.22 C
ANISOU 2282 CB LEU A 313 3492 3640 3590 -54 105 202 C
ATOM 2283 CG LEU A 313 25.038 24.572 13.043 1.00 28.11 C
ANISOU 2283 CG LEU A 313 3481 3620 3579 -62 120 195 C
ATOM 2284 CD1 LEU A 313 24.839 24.030 11.642 1.00 28.38 C
ANISOU 2284 CD1 LEU A 313 3528 3649 3604 -67 126 190 C
ATOM 2285 CD2 LEU A 313 25.687 25.950 12.986 1.00 28.14 C
ANISOU 2285 CD2 LEU A 313 3493 3622 3576 -65 124 196 C
ATOM 2286 N ALA A 314 21.546 25.963 16.047 1.00 26.75 N
ANISOU 2286 N ALA A 314 3295 3466 3401 -40 80 212 N
ATOM 2287 CA ALA A 314 20.164 26.039 16.474 1.00 26.79 C
ANISOU 2287 CA ALA A 314 3297 3474 3405 -35 69 214 C
ATOM 2288 C ALA A 314 19.465 27.232 15.844 1.00 27.57 C
ANISOU 2288 C ALA A 314 3409 3568 3498 -34 64 215 C
ATOM 2289 O ALA A 314 19.935 28.364 15.975 1.00 27.52 O
ANISOU 2289 O ALA A 314 3407 3560 3490 -35 66 214 O
ATOM 2290 CB ALA A 314 20.087 26.129 17.991 1.00 26.92 C
ANISOU 2290 CB ALA A 314 3300 3498 3427 -32 68 216 C
ATOM 2291 N GLY A 315 18.336 26.967 15.181 1.00 27.67 N
ANISOU 2291 N GLY A 315 3427 3577 3508 -32 55 216 N
ATOM 2292 CA GLY A 315 17.497 27.989 14.553 1.00 28.00 C
ANISOU 2292 CA GLY A 315 3479 3612 3546 -31 46 218 C
ATOM 2293 C GLY A 315 18.027 28.497 13.221 1.00 30.05 C
ANISOU 2293 C GLY A 315 3756 3863 3795 -38 47 218 C
ATOM 2294 O GLY A 315 17.550 29.505 12.697 1.00 31.13 O
ANISOU 2294 O GLY A 315 3903 3994 3930 -40 39 221 O
ATOM 2295 N VAL A 316 18.987 27.773 12.654 1.00 29.99 N
ANISOU 2295 N VAL A 316 3752 3856 3784 -44 58 216 N
ATOM 2296 CA VAL A 316 19.826 28.281 11.577 1.00 30.66 C
ANISOU 2296 CA VAL A 316 3853 3936 3858 -53 64 215 C
ATOM 2297 C VAL A 316 19.284 28.005 10.155 1.00 31.42 C
ANISOU 2297 C VAL A 316 3966 4026 3943 -60 59 216 C
ATOM 2298 O VAL A 316 18.740 26.927 9.892 1.00 31.72 O
ANISOU 2298 O VAL A 316 4003 4066 3982 -59 56 215 O
ATOM 2299 CB VAL A 316 21.256 27.724 11.773 1.00 30.76 C
ANISOU 2299 CB VAL A 316 3860 3952 3875 -57 81 210 C
ATOM 2300 CG1 VAL A 316 22.133 27.986 10.560 1.00 29.72 C
ANISOU 2300 CG1 VAL A 316 3744 3815 3734 -68 91 207 C
ATOM 2301 CG2 VAL A 316 21.880 28.290 13.050 1.00 28.64 C
ANISOU 2301 CG2 VAL A 316 3578 3687 3615 -53 84 210 C
ATOM 2302 N SER A 317 19.447 28.977 9.248 1.00 32.23 N
ANISOU 2302 N SER A 317 4085 4122 4035 -68 57 219 N
ATOM 2303 CA SER A 317 18.974 28.874 7.848 1.00 33.12 C
ANISOU 2303 CA SER A 317 4218 4230 4135 -77 50 221 C
ATOM 2304 C SER A 317 19.710 27.840 7.000 1.00 33.61 C
ANISOU 2304 C SER A 317 4288 4293 4188 -86 64 215 C
ATOM 2305 O SER A 317 19.463 27.763 5.799 1.00 37.73 O
ANISOU 2305 O SER A 317 4828 4811 4695 -97 61 216 O
ATOM 2306 CB SER A 317 19.089 30.217 7.091 1.00 34.88 C
ANISOU 2306 CB SER A 317 4458 4445 4347 -86 45 227 C
ATOM 2307 OG SER A 317 18.635 31.338 7.831 1.00 39.19 O
ANISOU 2307 OG SER A 317 4997 4989 4903 -78 34 232 O
ATOM 2308 N ILE A 318 20.614 27.067 7.588 1.00 32.55 N
ANISOU 2308 N ILE A 318 4140 4163 4062 -84 80 208 N
ATOM 2309 CA ILE A 318 21.417 26.099 6.830 1.00 31.86 C
ANISOU 2309 CA ILE A 318 4057 4076 3970 -92 95 199 C
ATOM 2310 C ILE A 318 20.532 25.150 6.021 1.00 31.15 C
ANISOU 2310 C ILE A 318 3976 3985 3874 -95 88 198 C
ATOM 2311 O ILE A 318 19.562 24.632 6.548 1.00 31.73 O
ANISOU 2311 O ILE A 318 4039 4059 3955 -86 76 201 O
ATOM 2312 CB ILE A 318 22.360 25.316 7.768 1.00 31.79 C
ANISOU 2312 CB ILE A 318 4028 4071 3979 -87 109 193 C
ATOM 2313 CG1 ILE A 318 23.272 24.370 6.967 1.00 32.07 C
ANISOU 2313 CG1 ILE A 318 4067 4105 4014 -96 127 182 C
ATOM 2314 CG2 ILE A 318 21.564 24.627 8.879 1.00 30.42 C
ANISOU 2314 CG2 ILE A 318 3836 3902 3819 -74 98 196 C
ATOM 2315 CD1 ILE A 318 24.462 23.847 7.738 1.00 31.74 C
ANISOU 2315 CD1 ILE A 318 4005 4063 3990 -93 141 176 C
ATOM 2316 N LYS A 319 20.863 24.936 4.745 1.00 31.91 N
ANISOU 2316 N LYS A 319 4090 4078 3955 -109 96 193 N
ATOM 2317 CA LYS A 319 20.031 24.106 3.843 1.00 32.47 C
ANISOU 2317 CA LYS A 319 4172 4146 4016 -115 89 191 C
ATOM 2318 C LYS A 319 20.733 22.826 3.414 1.00 31.91 C
ANISOU 2318 C LYS A 319 4099 4076 3948 -120 107 178 C
ATOM 2319 O LYS A 319 20.082 21.826 3.102 1.00 30.25 O
ANISOU 2319 O LYS A 319 3890 3866 3738 -120 102 175 O
ATOM 2320 CB LYS A 319 19.628 24.875 2.572 1.00 33.19 C
ANISOU 2320 CB LYS A 319 4292 4234 4085 -129 80 196 C
ATOM 2321 CG LYS A 319 19.022 26.250 2.773 1.00 33.21 C
ANISOU 2321 CG LYS A 319 4299 4233 4086 -126 63 209 C
ATOM 2322 CD LYS A 319 17.679 26.174 3.485 1.00 35.44 C
ANISOU 2322 CD LYS A 319 4570 4515 4381 -113 42 217 C
ATOM 2323 CE LYS A 319 16.836 27.396 3.173 1.00 35.72 C
ANISOU 2323 CE LYS A 319 4616 4543 4411 -115 21 229 C
ATOM 2324 NZ LYS A 319 17.680 28.618 3.238 1.00 37.06 N
ANISOU 2324 NZ LYS A 319 4791 4712 4578 -119 27 231 N
ATOM 2325 N TYR A 320 22.061 22.884 3.365 1.00 32.34 N
ANISOU 2325 N TYR A 320 4151 4131 4005 -125 128 170 N
ATOM 2326 CA TYR A 320 22.884 21.729 3.030 1.00 33.78 C
ANISOU 2326 CA TYR A 320 4327 4312 4194 -130 148 156 C
ATOM 2327 C TYR A 320 24.099 21.689 3.925 1.00 35.60 C
ANISOU 2327 C TYR A 320 4538 4543 4445 -125 163 151 C
ATOM 2328 O TYR A 320 24.828 22.673 4.045 1.00 38.09 O
ANISOU 2328 O TYR A 320 4855 4858 4758 -127 169 153 O
ATOM 2329 CB TYR A 320 23.339 21.760 1.569 1.00 32.48 C
ANISOU 2329 CB TYR A 320 4187 4144 4009 -149 162 146 C
ATOM 2330 CG TYR A 320 22.222 21.755 0.568 1.00 32.85 C
ANISOU 2330 CG TYR A 320 4256 4190 4034 -158 147 151 C
ATOM 2331 CD1 TYR A 320 21.716 22.946 0.061 1.00 32.86 C
ANISOU 2331 CD1 TYR A 320 4278 4191 4017 -165 133 162 C
ATOM 2332 CD2 TYR A 320 21.667 20.559 0.122 1.00 33.70 C
ANISOU 2332 CD2 TYR A 320 4365 4297 4141 -160 145 144 C
ATOM 2333 CE1 TYR A 320 20.687 22.955 -0.860 1.00 33.99 C
ANISOU 2333 CE1 TYR A 320 4441 4331 4140 -174 116 167 C
ATOM 2334 CE2 TYR A 320 20.634 20.553 -0.802 1.00 34.56 C
ANISOU 2334 CE2 TYR A 320 4496 4405 4231 -169 130 148 C
ATOM 2335 CZ TYR A 320 20.153 21.759 -1.293 1.00 35.40 C
ANISOU 2335 CZ TYR A 320 4621 4509 4317 -176 115 160 C
ATOM 2336 OH TYR A 320 19.126 21.774 -2.210 1.00 37.19 O
ANISOU 2336 OH TYR A 320 4870 4733 4526 -186 97 166 O
ATOM 2337 N LEU A 321 24.305 20.544 4.560 1.00 37.63 N
ANISOU 2337 N LEU A 321 4774 4800 4722 -117 167 146 N
ATOM 2338 CA LEU A 321 25.512 20.290 5.316 1.00 39.26 C
ANISOU 2338 CA LEU A 321 4961 5005 4950 -113 181 141 C
ATOM 2339 C LEU A 321 26.215 19.154 4.591 1.00 41.91 C
ANISOU 2339 C LEU A 321 5293 5335 5294 -121 200 125 C
ATOM 2340 O LEU A 321 25.887 17.987 4.791 1.00 41.73 O
ANISOU 2340 O LEU A 321 5259 5311 5284 -116 197 121 O
ATOM 2341 CB LEU A 321 25.174 19.904 6.762 1.00 37.76 C
ANISOU 2341 CB LEU A 321 4748 4818 4780 -98 167 149 C
ATOM 2342 CG LEU A 321 26.183 20.232 7.864 1.00 37.40 C
ANISOU 2342 CG LEU A 321 4683 4772 4752 -93 172 152 C
ATOM 2343 CD1 LEU A 321 25.728 19.673 9.196 1.00 37.62 C
ANISOU 2343 CD1 LEU A 321 4691 4804 4796 -81 158 160 C
ATOM 2344 CD2 LEU A 321 27.561 19.689 7.551 1.00 38.64 C
ANISOU 2344 CD2 LEU A 321 4832 4924 4925 -99 193 140 C
ATOM 2345 N GLU A 322 27.169 19.501 3.731 1.00 46.25 N
ANISOU 2345 N GLU A 322 5854 5882 5837 -134 220 115 N
ATOM 2346 CA GLU A 322 27.816 18.503 2.884 1.00 51.33 C
ANISOU 2346 CA GLU A 322 6498 6520 6486 -143 241 97 C
ATOM 2347 C GLU A 322 29.319 18.718 2.703 1.00 53.38 C
ANISOU 2347 C GLU A 322 6751 6774 6757 -151 266 86 C
ATOM 2348 O GLU A 322 30.050 17.794 2.316 1.00 56.01 O
ANISOU 2348 O GLU A 322 7075 7101 7105 -156 285 70 O
ATOM 2349 CB GLU A 322 27.106 18.398 1.516 1.00 53.11 C
ANISOU 2349 CB GLU A 322 6750 6745 6683 -157 242 91 C
ATOM 2350 CG GLU A 322 27.126 19.668 0.668 1.00 54.07 C
ANISOU 2350 CG GLU A 322 6898 6869 6776 -170 243 95 C
ATOM 2351 CD GLU A 322 26.134 19.641 -0.490 1.00 56.65 C
ANISOU 2351 CD GLU A 322 7252 7197 7074 -182 234 96 C
ATOM 2352 OE1 GLU A 322 26.295 20.451 -1.427 1.00 59.85 O
ANISOU 2352 OE1 GLU A 322 7681 7603 7453 -198 240 96 O
ATOM 2353 OE2 GLU A 322 25.185 18.827 -0.473 1.00 56.25 O
ANISOU 2353 OE2 GLU A 322 7200 7146 7024 -177 221 97 O
ATOM 2354 N ASP A 323 29.785 19.925 2.997 1.00 53.62 N
ANISOU 2354 N ASP A 323 6784 6806 6781 -152 266 93 N
ATOM 2355 CA ASP A 323 31.167 20.295 2.659 1.00 58.87 C
ANISOU 2355 CA ASP A 323 7447 7466 7453 -161 290 83 C
ATOM 2356 C ASP A 323 32.257 19.562 3.468 1.00 51.26 C
ANISOU 2356 C ASP A 323 6453 6495 6526 -154 301 76 C
ATOM 2357 O ASP A 323 33.340 19.326 2.960 1.00 52.13 O
ANISOU 2357 O ASP A 323 6559 6599 6648 -163 325 61 O
ATOM 2358 CB ASP A 323 31.379 21.812 2.832 1.00 69.92 C
ANISOU 2358 CB ASP A 323 8857 8869 8839 -163 285 94 C
ATOM 2359 CG ASP A 323 30.203 22.654 2.333 1.00 76.91 C
ANISOU 2359 CG ASP A 323 9768 9761 9694 -167 267 106 C
ATOM 2360 OD1 ASP A 323 29.434 23.163 3.185 1.00 80.06 O
ANISOU 2360 OD1 ASP A 323 10162 10163 10093 -155 245 121 O
ATOM 2361 OD2 ASP A 323 30.062 22.823 1.099 1.00 80.37 O
ANISOU 2361 OD2 ASP A 323 10229 10198 10107 -182 275 101 O
ATOM 2362 N VAL A 324 31.932 19.191 4.704 1.00 44.86 N
ANISOU 2362 N VAL A 324 5623 5687 5735 -139 283 86 N
ATOM 2363 CA VAL A 324 32.892 19.089 5.807 1.00 40.73 C
ANISOU 2363 CA VAL A 324 5073 5159 5243 -131 284 89 C
ATOM 2364 C VAL A 324 34.184 18.334 5.520 1.00 39.99 C
ANISOU 2364 C VAL A 324 4963 5054 5177 -137 308 72 C
ATOM 2365 O VAL A 324 34.150 17.155 5.192 1.00 40.73 O
ANISOU 2365 O VAL A 324 5048 5142 5284 -138 315 61 O
ATOM 2366 CB VAL A 324 32.244 18.504 7.076 1.00 39.54 C
ANISOU 2366 CB VAL A 324 4904 5011 5107 -117 261 101 C
ATOM 2367 CG1 VAL A 324 33.065 18.866 8.294 1.00 37.46 C
ANISOU 2367 CG1 VAL A 324 4621 4746 4866 -110 256 110 C
ATOM 2368 CG2 VAL A 324 30.832 19.034 7.249 1.00 39.09 C
ANISOU 2368 CG2 VAL A 324 4862 4963 5024 -112 240 115 C
ATOM 2369 N PRO A 325 35.333 19.021 5.657 1.00 38.37 N
ANISOU 2369 N PRO A 325 4751 4844 4982 -141 321 70 N
ATOM 2370 CA PRO A 325 36.615 18.364 5.466 1.00 38.06 C
ANISOU 2370 CA PRO A 325 4693 4793 4974 -146 343 55 C
ATOM 2371 C PRO A 325 36.785 17.200 6.438 1.00 38.30 C
ANISOU 2371 C PRO A 325 4693 4816 5040 -135 333 57 C
ATOM 2372 O PRO A 325 36.467 17.315 7.617 1.00 40.89 O
ANISOU 2372 O PRO A 325 5011 5148 5375 -124 311 73 O
ATOM 2373 CB PRO A 325 37.626 19.476 5.765 1.00 36.52 C
ANISOU 2373 CB PRO A 325 4495 4596 4784 -148 350 58 C
ATOM 2374 CG PRO A 325 36.874 20.735 5.522 1.00 35.43 C
ANISOU 2374 CG PRO A 325 4383 4469 4608 -151 340 70 C
ATOM 2375 CD PRO A 325 35.500 20.443 6.003 1.00 36.65 C
ANISOU 2375 CD PRO A 325 4542 4631 4749 -141 314 82 C
ATOM 2376 N LYS A 326 37.295 16.090 5.932 1.00 38.84 N
ANISOU 2376 N LYS A 326 4750 4874 5132 -139 350 40 N
ATOM 2377 CA LYS A 326 37.383 14.857 6.689 1.00 39.06 C
ANISOU 2377 CA LYS A 326 4750 4893 5195 -130 341 40 C
ATOM 2378 C LYS A 326 38.441 14.885 7.804 1.00 37.32 C
ANISOU 2378 C LYS A 326 4502 4665 5012 -124 335 48 C
ATOM 2379 O LYS A 326 38.594 13.915 8.543 1.00 36.90 O
ANISOU 2379 O LYS A 326 4425 4603 4990 -118 324 51 O
ATOM 2380 CB LYS A 326 37.617 13.692 5.722 1.00 43.33 C
ANISOU 2380 CB LYS A 326 5286 5424 5751 -137 362 18 C
ATOM 2381 CG LYS A 326 36.631 13.652 4.552 1.00 47.67 C
ANISOU 2381 CG LYS A 326 5865 5982 6264 -145 368 10 C
ATOM 2382 CD LYS A 326 37.121 12.776 3.402 1.00 51.40 C
ANISOU 2382 CD LYS A 326 6337 6445 6748 -156 397 -15 C
ATOM 2383 CE LYS A 326 36.903 11.296 3.697 1.00 55.26 C
ANISOU 2383 CE LYS A 326 6804 6924 7267 -149 391 -21 C
ATOM 2384 NZ LYS A 326 37.603 10.404 2.727 1.00 57.53 N
ANISOU 2384 NZ LYS A 326 7084 7199 7575 -159 421 -49 N
ATOM 2385 N HIS A 327 39.149 16.003 7.946 1.00 37.26 N
ANISOU 2385 N HIS A 327 4498 4657 4999 -128 341 51 N
ATOM 2386 CA HIS A 327 40.153 16.148 9.012 1.00 36.84 C
ANISOU 2386 CA HIS A 327 4421 4597 4979 -123 333 60 C
ATOM 2387 C HIS A 327 39.664 16.900 10.233 1.00 36.10 C
ANISOU 2387 C HIS A 327 4328 4513 4872 -115 306 82 C
ATOM 2388 O HIS A 327 40.406 17.055 11.205 1.00 34.38 O
ANISOU 2388 O HIS A 327 4092 4290 4679 -112 296 91 O
ATOM 2389 CB HIS A 327 41.434 16.776 8.476 1.00 36.30 C
ANISOU 2389 CB HIS A 327 4349 4520 4922 -132 358 48 C
ATOM 2390 CG HIS A 327 41.326 18.263 8.208 1.00 36.85 C
ANISOU 2390 CG HIS A 327 4443 4600 4956 -137 360 54 C
ATOM 2391 ND1 HIS A 327 40.966 18.763 7.003 1.00 36.75 N
ANISOU 2391 ND1 HIS A 327 4457 4594 4911 -147 377 44 N
ATOM 2392 CD2 HIS A 327 41.556 19.360 9.039 1.00 36.21 C
ANISOU 2392 CD2 HIS A 327 4363 4524 4870 -133 347 69 C
ATOM 2393 CE1 HIS A 327 40.964 20.104 7.063 1.00 36.17 C
ANISOU 2393 CE1 HIS A 327 4399 4528 4814 -149 373 54 C
ATOM 2394 NE2 HIS A 327 41.325 20.469 8.311 1.00 36.82 N
ANISOU 2394 NE2 HIS A 327 4465 4609 4913 -140 355 68 N
ATOM 2395 N PHE A 328 38.421 17.378 10.188 1.00 35.76 N
ANISOU 2395 N PHE A 328 4308 4485 4794 -112 293 91 N
ATOM 2396 CA PHE A 328 37.810 18.062 11.331 1.00 36.43 C
ANISOU 2396 CA PHE A 328 4396 4581 4865 -105 267 111 C
ATOM 2397 C PHE A 328 37.682 17.121 12.540 1.00 35.19 C
ANISOU 2397 C PHE A 328 4216 4421 4733 -97 247 122 C
ATOM 2398 O PHE A 328 37.430 15.932 12.396 1.00 34.42 O
ANISOU 2398 O PHE A 328 4108 4318 4650 -95 246 118 O
ATOM 2399 CB PHE A 328 36.443 18.659 10.950 1.00 37.42 C
ANISOU 2399 CB PHE A 328 4548 4720 4950 -103 259 116 C
ATOM 2400 CG PHE A 328 36.513 19.990 10.227 1.00 38.12 C
ANISOU 2400 CG PHE A 328 4658 4813 5011 -110 269 114 C
ATOM 2401 CD1 PHE A 328 35.422 20.864 10.260 1.00 37.44 C
ANISOU 2401 CD1 PHE A 328 4593 4739 4894 -107 256 124 C
ATOM 2402 CD2 PHE A 328 37.656 20.381 9.511 1.00 38.62 C
ANISOU 2402 CD2 PHE A 328 4723 4869 5082 -119 292 103 C
ATOM 2403 CE1 PHE A 328 35.467 22.087 9.593 1.00 37.29 C
ANISOU 2403 CE1 PHE A 328 4593 4723 4851 -114 263 123 C
ATOM 2404 CE2 PHE A 328 37.704 21.605 8.843 1.00 36.70 C
ANISOU 2404 CE2 PHE A 328 4500 4630 4813 -126 300 102 C
ATOM 2405 CZ PHE A 328 36.609 22.456 8.884 1.00 36.67 C
ANISOU 2405 CZ PHE A 328 4517 4638 4779 -124 285 113 C
ATOM 2406 N LYS A 329 37.852 17.678 13.730 1.00 36.08 N
ANISOU 2406 N LYS A 329 4322 4538 4849 -93 229 137 N
ATOM 2407 CA LYS A 329 37.975 16.892 14.951 1.00 35.32 C
ANISOU 2407 CA LYS A 329 4204 4438 4778 -89 209 149 C
ATOM 2408 C LYS A 329 36.689 16.782 15.756 1.00 33.19 C
ANISOU 2408 C LYS A 329 3940 4182 4488 -83 187 164 C
ATOM 2409 O LYS A 329 36.692 16.173 16.822 1.00 33.14 O
ANISOU 2409 O LYS A 329 3918 4175 4499 -81 169 175 O
ATOM 2410 CB LYS A 329 39.056 17.491 15.853 1.00 36.81 C
ANISOU 2410 CB LYS A 329 4379 4621 4984 -91 203 157 C
ATOM 2411 CG LYS A 329 40.308 17.932 15.133 1.00 39.31 C
ANISOU 2411 CG LYS A 329 4691 4926 5316 -97 225 145 C
ATOM 2412 CD LYS A 329 41.415 16.911 15.240 1.00 41.46 C
ANISOU 2412 CD LYS A 329 4936 5181 5635 -98 230 139 C
ATOM 2413 CE LYS A 329 42.760 17.575 14.983 1.00 42.62 C
ANISOU 2413 CE LYS A 329 5074 5316 5800 -104 246 132 C
ATOM 2414 NZ LYS A 329 43.841 16.728 15.556 1.00 46.61 N
ANISOU 2414 NZ LYS A 329 5549 5804 6355 -105 242 133 N
ATOM 2415 N TRP A 330 35.601 17.369 15.258 1.00 32.47 N
ANISOU 2415 N TRP A 330 3871 4101 4362 -82 187 163 N
ATOM 2416 CA TRP A 330 34.330 17.427 16.000 1.00 30.69 C
ANISOU 2416 CA TRP A 330 3653 3889 4117 -76 168 176 C
ATOM 2417 C TRP A 330 34.030 16.137 16.682 1.00 29.63 C
ANISOU 2417 C TRP A 330 3502 3753 4002 -74 154 183 C
ATOM 2418 O TRP A 330 34.101 15.082 16.065 1.00 29.94 O
ANISOU 2418 O TRP A 330 3533 3783 4057 -74 161 174 O
ATOM 2419 CB TRP A 330 33.164 17.798 15.091 1.00 29.60 C
ANISOU 2419 CB TRP A 330 3538 3760 3948 -75 172 171 C
ATOM 2420 CG TRP A 330 33.313 19.117 14.374 1.00 29.81 C
ANISOU 2420 CG TRP A 330 3584 3789 3952 -79 183 166 C
ATOM 2421 CD1 TRP A 330 34.291 20.097 14.568 1.00 29.91 C
ANISOU 2421 CD1 TRP A 330 3596 3799 3968 -82 189 166 C
ATOM 2422 CD2 TRP A 330 32.418 19.674 13.347 1.00 30.01 C
ANISOU 2422 CD2 TRP A 330 3633 3820 3949 -80 188 161 C
ATOM 2423 NE1 TRP A 330 34.082 21.172 13.742 1.00 29.81 N
ANISOU 2423 NE1 TRP A 330 3604 3790 3932 -85 198 162 N
ATOM 2424 CE2 TRP A 330 32.980 20.983 12.979 1.00 29.68 C
ANISOU 2424 CE2 TRP A 330 3602 3778 3895 -85 197 159 C
ATOM 2425 CE3 TRP A 330 31.255 19.235 12.713 1.00 29.35 C
ANISOU 2425 CE3 TRP A 330 3560 3740 3849 -79 185 159 C
ATOM 2426 CZ2 TRP A 330 32.389 21.789 12.023 1.00 28.89 C
ANISOU 2426 CZ2 TRP A 330 3525 3681 3768 -88 202 156 C
ATOM 2427 CZ3 TRP A 330 30.678 20.058 11.745 1.00 29.04 C
ANISOU 2427 CZ3 TRP A 330 3544 3704 3783 -82 189 156 C
ATOM 2428 CH2 TRP A 330 31.231 21.302 11.409 1.00 28.86 C
ANISOU 2428 CH2 TRP A 330 3533 3681 3749 -87 197 155 C
ATOM 2429 N GLN A 331 33.727 16.217 17.972 1.00 29.44 N
ANISOU 2429 N GLN A 331 3472 3736 3977 -72 134 198 N
ATOM 2430 CA GLN A 331 33.292 15.057 18.754 1.00 29.32 C
ANISOU 2430 CA GLN A 331 3442 3721 3976 -70 118 207 C
ATOM 2431 C GLN A 331 31.767 14.960 18.887 1.00 29.05 C
ANISOU 2431 C GLN A 331 3421 3700 3917 -66 108 213 C
ATOM 2432 O GLN A 331 31.226 13.851 18.940 1.00 29.51 O
ANISOU 2432 O GLN A 331 3470 3756 3983 -64 101 215 O
ATOM 2433 CB GLN A 331 33.990 15.018 20.113 1.00 29.48 C
ANISOU 2433 CB GLN A 331 3447 3739 4013 -74 102 221 C
ATOM 2434 CG GLN A 331 35.432 14.543 20.002 1.00 30.72 C
ANISOU 2434 CG GLN A 331 3584 3879 4207 -77 107 217 C
ATOM 2435 CD GLN A 331 36.234 14.793 21.259 1.00 31.46 C
ANISOU 2435 CD GLN A 331 3665 3971 4315 -82 91 231 C
ATOM 2436 OE1 GLN A 331 36.456 13.890 22.049 1.00 32.56 O
ANISOU 2436 OE1 GLN A 331 3788 4105 4478 -84 75 242 O
ATOM 2437 NE2 GLN A 331 36.661 16.028 21.457 1.00 32.50 N
ANISOU 2437 NE2 GLN A 331 3806 4107 4434 -84 95 231 N
ATOM 2438 N SER A 332 31.073 16.099 18.943 1.00 27.93 N
ANISOU 2438 N SER A 332 3296 3569 3745 -65 107 214 N
ATOM 2439 CA SER A 332 29.628 16.073 18.767 1.00 28.50 C
ANISOU 2439 CA SER A 332 3381 3651 3796 -61 102 216 C
ATOM 2440 C SER A 332 29.142 17.131 17.783 1.00 28.90 C
ANISOU 2440 C SER A 332 3452 3705 3821 -59 113 208 C
ATOM 2441 O SER A 332 29.835 18.123 17.526 1.00 29.53 O
ANISOU 2441 O SER A 332 3539 3783 3896 -62 121 204 O
ATOM 2442 CB SER A 332 28.862 16.112 20.106 1.00 29.34 C
ANISOU 2442 CB SER A 332 3485 3769 3894 -60 84 230 C
ATOM 2443 OG SER A 332 29.130 17.288 20.840 1.00 31.03 O
ANISOU 2443 OG SER A 332 3703 3990 4097 -62 81 234 O
ATOM 2444 N LEU A 333 27.970 16.881 17.200 1.00 27.42 N
ANISOU 2444 N LEU A 333 3276 3522 3620 -56 111 205 N
ATOM 2445 CA LEU A 333 27.351 17.790 16.257 1.00 26.60 C
ANISOU 2445 CA LEU A 333 3192 3421 3492 -56 117 200 C
ATOM 2446 C LEU A 333 25.841 17.834 16.498 1.00 27.46 C
ANISOU 2446 C LEU A 333 3308 3538 3585 -51 105 205 C
ATOM 2447 O LEU A 333 25.152 16.801 16.546 1.00 26.81 O
ANISOU 2447 O LEU A 333 3220 3457 3508 -49 99 207 O
ATOM 2448 CB LEU A 333 27.675 17.403 14.807 1.00 25.60 C
ANISOU 2448 CB LEU A 333 3073 3286 3367 -59 132 187 C
ATOM 2449 CG LEU A 333 26.971 18.173 13.677 1.00 25.05 C
ANISOU 2449 CG LEU A 333 3027 3218 3272 -61 137 181 C
ATOM 2450 CD1 LEU A 333 27.222 19.676 13.761 1.00 24.83 C
ANISOU 2450 CD1 LEU A 333 3009 3193 3230 -62 139 184 C
ATOM 2451 CD2 LEU A 333 27.362 17.626 12.312 1.00 24.29 C
ANISOU 2451 CD2 LEU A 333 2937 3113 3176 -67 152 168 C
ATOM 2452 N SER A 334 25.343 19.056 16.637 1.00 28.39 N
ANISOU 2452 N SER A 334 3438 3663 3686 -50 102 208 N
ATOM 2453 CA SER A 334 23.972 19.315 17.011 1.00 27.85 C
ANISOU 2453 CA SER A 334 3374 3602 3604 -45 91 213 C
ATOM 2454 C SER A 334 23.390 20.229 15.951 1.00 27.59 C
ANISOU 2454 C SER A 334 3360 3567 3553 -45 94 208 C
ATOM 2455 O SER A 334 23.919 21.310 15.710 1.00 27.79 O
ANISOU 2455 O SER A 334 3394 3592 3573 -48 100 206 O
ATOM 2456 CB SER A 334 23.959 20.019 18.360 1.00 28.18 C
ANISOU 2456 CB SER A 334 3411 3652 3644 -45 84 220 C
ATOM 2457 OG SER A 334 23.203 19.298 19.306 1.00 29.58 O
ANISOU 2457 OG SER A 334 3578 3836 3825 -43 74 227 O
ATOM 2458 N ILE A 335 22.327 19.766 15.300 1.00 27.65 N
ANISOU 2458 N ILE A 335 3374 3574 3555 -43 89 207 N
ATOM 2459 CA ILE A 335 21.561 20.542 14.334 1.00 27.34 C
ANISOU 2459 CA ILE A 335 3353 3534 3500 -43 88 205 C
ATOM 2460 C ILE A 335 20.159 20.488 14.905 1.00 27.74 C
ANISOU 2460 C ILE A 335 3401 3590 3548 -37 74 211 C
ATOM 2461 O ILE A 335 19.529 19.425 14.911 1.00 27.21 O
ANISOU 2461 O ILE A 335 3328 3523 3486 -35 69 213 O
ATOM 2462 CB ILE A 335 21.525 19.879 12.941 1.00 27.91 C
ANISOU 2462 CB ILE A 335 3436 3600 3569 -48 93 199 C
ATOM 2463 CG1 ILE A 335 22.853 19.186 12.574 1.00 28.56 C
ANISOU 2463 CG1 ILE A 335 3512 3676 3662 -53 108 191 C
ATOM 2464 CG2 ILE A 335 21.106 20.868 11.876 1.00 27.94 C
ANISOU 2464 CG2 ILE A 335 3459 3600 3554 -52 92 197 C
ATOM 2465 CD1 ILE A 335 23.995 20.138 12.329 1.00 29.52 C
ANISOU 2465 CD1 ILE A 335 3639 3795 3781 -58 119 187 C
ATOM 2466 N ILE A 336 19.692 21.625 15.417 1.00 27.68 N
ANISOU 2466 N ILE A 336 3396 3585 3534 -35 69 214 N
ATOM 2467 CA ILE A 336 18.405 21.720 16.099 1.00 28.16 C
ANISOU 2467 CA ILE A 336 3452 3651 3594 -30 59 219 C
ATOM 2468 C ILE A 336 17.564 22.817 15.470 1.00 28.43 C
ANISOU 2468 C ILE A 336 3500 3682 3620 -28 53 218 C
ATOM 2469 O ILE A 336 18.030 23.947 15.315 1.00 28.66 O
ANISOU 2469 O ILE A 336 3537 3709 3644 -30 56 217 O
ATOM 2470 CB ILE A 336 18.587 22.030 17.604 1.00 28.28 C
ANISOU 2470 CB ILE A 336 3455 3674 3614 -28 58 222 C
ATOM 2471 CG1 ILE A 336 19.192 20.827 18.333 1.00 29.47 C
ANISOU 2471 CG1 ILE A 336 3592 3829 3776 -30 59 225 C
ATOM 2472 CG2 ILE A 336 17.268 22.454 18.245 1.00 27.23 C
ANISOU 2472 CG2 ILE A 336 3320 3546 3480 -24 50 224 C
ATOM 2473 CD1 ILE A 336 19.680 21.134 19.740 1.00 30.99 C
ANISOU 2473 CD1 ILE A 336 3774 4028 3970 -32 59 229 C
ATOM 2474 N ARG A 337 16.322 22.480 15.134 1.00 28.97 N
ANISOU 2474 N ARG A 337 3569 3748 3687 -25 44 220 N
ATOM 2475 CA ARG A 337 15.368 23.419 14.512 1.00 30.33 C
ANISOU 2475 CA ARG A 337 3752 3915 3854 -24 35 221 C
ATOM 2476 C ARG A 337 15.966 24.198 13.327 1.00 29.69 C
ANISOU 2476 C ARG A 337 3689 3827 3763 -30 38 220 C
ATOM 2477 O ARG A 337 15.831 25.425 13.231 1.00 29.76 O
ANISOU 2477 O ARG A 337 3705 3833 3769 -30 34 221 O
ATOM 2478 CB ARG A 337 14.768 24.381 15.546 1.00 31.15 C
ANISOU 2478 CB ARG A 337 3849 4022 3963 -19 31 222 C
ATOM 2479 CG ARG A 337 13.989 23.730 16.688 1.00 33.02 C
ANISOU 2479 CG ARG A 337 4071 4267 4208 -14 29 224 C
ATOM 2480 CD ARG A 337 13.865 24.681 17.879 1.00 34.04 C
ANISOU 2480 CD ARG A 337 4192 4401 4339 -13 31 222 C
ATOM 2481 NE ARG A 337 14.028 26.063 17.428 1.00 37.01 N
ANISOU 2481 NE ARG A 337 4577 4770 4712 -13 30 220 N
ATOM 2482 CZ ARG A 337 14.964 26.909 17.858 1.00 37.84 C
ANISOU 2482 CZ ARG A 337 4684 4878 4815 -15 37 217 C
ATOM 2483 NH1 ARG A 337 15.005 28.128 17.344 1.00 36.88 N
ANISOU 2483 NH1 ARG A 337 4571 4748 4691 -16 34 216 N
ATOM 2484 NH2 ARG A 337 15.833 26.557 18.808 1.00 37.34 N
ANISOU 2484 NH2 ARG A 337 4613 4823 4752 -18 44 217 N
ATOM 2485 N CYS A 338 16.632 23.481 12.430 1.00 28.83 N
ANISOU 2485 N CYS A 338 3587 3715 3649 -36 44 217 N
ATOM 2486 CA CYS A 338 17.219 24.113 11.259 1.00 28.75 C
ANISOU 2486 CA CYS A 338 3595 3699 3627 -44 48 215 C
ATOM 2487 C CYS A 338 16.400 23.817 10.009 1.00 28.73 C
ANISOU 2487 C CYS A 338 3608 3691 3617 -48 39 216 C
ATOM 2488 O CYS A 338 15.287 23.292 10.100 1.00 27.26 O
ANISOU 2488 O CYS A 338 3417 3505 3435 -43 28 219 O
ATOM 2489 CB CYS A 338 18.662 23.677 11.092 1.00 28.72 C
ANISOU 2489 CB CYS A 338 3591 3697 3624 -49 64 209 C
ATOM 2490 SG CYS A 338 19.688 24.184 12.473 1.00 29.34 S
ANISOU 2490 SG CYS A 338 3654 3780 3712 -46 72 209 S
ATOM 2491 N GLN A 339 16.954 24.147 8.846 1.00 29.74 N
ANISOU 2491 N GLN A 339 3753 3813 3731 -58 44 214 N
ATOM 2492 CA GLN A 339 16.169 24.133 7.621 1.00 31.67 C
ANISOU 2492 CA GLN A 339 4015 4052 3964 -65 33 216 C
ATOM 2493 C GLN A 339 16.720 23.241 6.521 1.00 32.16 C
ANISOU 2493 C GLN A 339 4090 4113 4017 -75 43 209 C
ATOM 2494 O GLN A 339 16.549 23.544 5.338 1.00 34.29 O
ANISOU 2494 O GLN A 339 4379 4377 4270 -86 39 210 O
ATOM 2495 CB GLN A 339 16.007 25.560 7.102 1.00 33.06 C
ANISOU 2495 CB GLN A 339 4206 4222 4131 -70 25 222 C
ATOM 2496 CG GLN A 339 14.867 26.324 7.758 1.00 34.05 C
ANISOU 2496 CG GLN A 339 4323 4345 4266 -61 8 229 C
ATOM 2497 CD GLN A 339 15.016 27.834 7.625 1.00 34.28 C
ANISOU 2497 CD GLN A 339 4361 4369 4293 -64 3 234 C
ATOM 2498 OE1 GLN A 339 15.079 28.538 8.622 1.00 34.75 O
ANISOU 2498 OE1 GLN A 339 4409 4431 4363 -56 4 234 O
ATOM 2499 NE2 GLN A 339 15.068 28.333 6.394 1.00 34.30 N
ANISOU 2499 NE2 GLN A 339 4385 4365 4281 -75 -2 238 N
ATOM 2500 N LEU A 340 17.370 22.148 6.903 1.00 32.15 N
ANISOU 2500 N LEU A 340 4076 4115 4024 -73 56 202 N
ATOM 2501 CA LEU A 340 17.994 21.239 5.937 1.00 33.34 C
ANISOU 2501 CA LEU A 340 4234 4263 4167 -83 68 193 C
ATOM 2502 C LEU A 340 17.028 20.747 4.857 1.00 33.32 C
ANISOU 2502 C LEU A 340 4248 4257 4154 -89 57 193 C
ATOM 2503 O LEU A 340 15.934 20.278 5.156 1.00 34.17 O
ANISOU 2503 O LEU A 340 4348 4364 4268 -82 43 198 O
ATOM 2504 CB LEU A 340 18.627 20.047 6.670 1.00 32.72 C
ANISOU 2504 CB LEU A 340 4136 4188 4107 -77 80 186 C
ATOM 2505 CG LEU A 340 20.101 20.031 7.092 1.00 31.26 C
ANISOU 2505 CG LEU A 340 3941 4004 3930 -78 98 180 C
ATOM 2506 CD1 LEU A 340 20.795 21.371 6.965 1.00 30.30 C
ANISOU 2506 CD1 LEU A 340 3829 3882 3801 -83 104 182 C
ATOM 2507 CD2 LEU A 340 20.191 19.510 8.516 1.00 31.69 C
ANISOU 2507 CD2 LEU A 340 3971 4063 4005 -67 96 183 C
ATOM 2508 N LYS A 341 17.434 20.871 3.602 1.00 35.16 N
ANISOU 2508 N LYS A 341 4502 4487 4369 -103 64 188 N
ATOM 2509 CA LYS A 341 16.641 20.366 2.484 1.00 37.36 C
ANISOU 2509 CA LYS A 341 4798 4762 4635 -112 55 188 C
ATOM 2510 C LYS A 341 16.956 18.902 2.212 1.00 37.23 C
ANISOU 2510 C LYS A 341 4776 4745 4623 -114 67 175 C
ATOM 2511 O LYS A 341 16.194 18.211 1.546 1.00 38.01 O
ANISOU 2511 O LYS A 341 4884 4842 4716 -118 58 174 O
ATOM 2512 CB LYS A 341 16.893 21.189 1.220 1.00 40.31 C
ANISOU 2512 CB LYS A 341 5200 5132 4984 -129 55 188 C
ATOM 2513 CG LYS A 341 16.193 22.540 1.194 1.00 44.76 C
ANISOU 2513 CG LYS A 341 5772 5692 5542 -129 36 202 C
ATOM 2514 CD LYS A 341 15.924 22.986 -0.244 1.00 51.59 C
ANISOU 2514 CD LYS A 341 6667 6553 6382 -148 27 206 C
ATOM 2515 CE LYS A 341 14.734 22.243 -0.863 1.00 55.83 C
ANISOU 2515 CE LYS A 341 7213 7086 6914 -151 9 208 C
ATOM 2516 NZ LYS A 341 14.547 22.538 -2.313 1.00 57.55 N
ANISOU 2516 NZ LYS A 341 7462 7299 7105 -172 2 211 N
ATOM 2517 N GLN A 342 18.088 18.448 2.741 1.00 37.55 N
ANISOU 2517 N GLN A 342 4801 4787 4676 -111 86 167 N
ATOM 2518 CA GLN A 342 18.607 17.104 2.516 1.00 38.38 C
ANISOU 2518 CA GLN A 342 4898 4891 4790 -114 100 154 C
ATOM 2519 C GLN A 342 19.300 16.573 3.751 1.00 37.40 C
ANISOU 2519 C GLN A 342 4747 4769 4692 -102 109 152 C
ATOM 2520 O GLN A 342 19.792 17.344 4.573 1.00 38.59 O
ANISOU 2520 O GLN A 342 4889 4923 4849 -97 111 157 O
ATOM 2521 CB GLN A 342 19.638 17.122 1.407 1.00 39.79 C
ANISOU 2521 CB GLN A 342 5093 5067 4956 -130 121 140 C
ATOM 2522 CG GLN A 342 19.133 16.617 0.075 1.00 44.46 C
ANISOU 2522 CG GLN A 342 5707 5656 5528 -144 120 133 C
ATOM 2523 CD GLN A 342 20.240 16.552 -0.957 1.00 46.43 C
ANISOU 2523 CD GLN A 342 5972 5904 5765 -161 144 118 C
ATOM 2524 OE1 GLN A 342 21.417 16.809 -0.654 1.00 45.70 O
ANISOU 2524 OE1 GLN A 342 5870 5811 5681 -162 163 112 O
ATOM 2525 NE2 GLN A 342 19.873 16.209 -2.188 1.00 47.77 N
ANISOU 2525 NE2 GLN A 342 6163 6071 5913 -177 145 111 N
ATOM 2526 N PHE A 343 19.359 15.255 3.875 1.00 35.61 N
ANISOU 2526 N PHE A 343 4508 4542 4481 -99 113 145 N
ATOM 2527 CA PHE A 343 20.086 14.662 4.976 1.00 35.13 C
ANISOU 2527 CA PHE A 343 4421 4480 4445 -90 120 143 C
ATOM 2528 C PHE A 343 21.589 14.884 4.775 1.00 34.14 C
ANISOU 2528 C PHE A 343 4294 4353 4324 -97 143 133 C
ATOM 2529 O PHE A 343 22.110 14.590 3.698 1.00 35.03 O
ANISOU 2529 O PHE A 343 4418 4461 4429 -109 158 120 O
ATOM 2530 CB PHE A 343 19.756 13.173 5.130 1.00 34.36 C
ANISOU 2530 CB PHE A 343 4309 4380 4364 -86 118 139 C
ATOM 2531 CG PHE A 343 20.159 12.610 6.456 1.00 32.80 C
ANISOU 2531 CG PHE A 343 4084 4183 4192 -75 117 144 C
ATOM 2532 CD1 PHE A 343 19.276 12.633 7.523 1.00 32.84 C
ANISOU 2532 CD1 PHE A 343 4079 4195 4204 -65 100 157 C
ATOM 2533 CD2 PHE A 343 21.430 12.087 6.645 1.00 31.93 C
ANISOU 2533 CD2 PHE A 343 3960 4069 4101 -77 134 134 C
ATOM 2534 CE1 PHE A 343 19.647 12.124 8.759 1.00 32.41 C
ANISOU 2534 CE1 PHE A 343 4001 4142 4171 -57 98 163 C
ATOM 2535 CE2 PHE A 343 21.813 11.585 7.871 1.00 32.10 C
ANISOU 2535 CE2 PHE A 343 3957 4090 4147 -69 130 141 C
ATOM 2536 CZ PHE A 343 20.920 11.601 8.933 1.00 32.61 C
ANISOU 2536 CZ PHE A 343 4013 4162 4215 -60 112 155 C
ATOM 2537 N PRO A 344 22.280 15.408 5.810 1.00 33.04 N
ANISOU 2537 N PRO A 344 4139 4215 4197 -91 145 138 N
ATOM 2538 CA PRO A 344 23.700 15.733 5.766 1.00 34.18 C
ANISOU 2538 CA PRO A 344 4280 4357 4348 -96 164 131 C
ATOM 2539 C PRO A 344 24.559 14.588 5.269 1.00 36.15 C
ANISOU 2539 C PRO A 344 4521 4599 4614 -102 183 115 C
ATOM 2540 O PRO A 344 24.275 13.418 5.554 1.00 37.46 O
ANISOU 2540 O PRO A 344 4673 4762 4797 -96 179 113 O
ATOM 2541 CB PRO A 344 24.037 16.002 7.228 1.00 32.75 C
ANISOU 2541 CB PRO A 344 4078 4179 4185 -85 158 141 C
ATOM 2542 CG PRO A 344 22.777 16.528 7.788 1.00 32.03 C
ANISOU 2542 CG PRO A 344 3990 4094 4083 -78 137 154 C
ATOM 2543 CD PRO A 344 21.700 15.735 7.123 1.00 32.42 C
ANISOU 2543 CD PRO A 344 4047 4142 4126 -79 129 153 C
ATOM 2544 N THR A 345 25.597 14.918 4.516 1.00 37.43 N
ANISOU 2544 N THR A 345 4692 4758 4773 -112 203 103 N
ATOM 2545 CA THR A 345 26.578 13.912 4.160 1.00 39.78 C
ANISOU 2545 CA THR A 345 4976 5046 5089 -117 224 86 C
ATOM 2546 C THR A 345 27.768 14.103 5.106 1.00 40.98 C
ANISOU 2546 C THR A 345 5106 5195 5266 -112 231 87 C
ATOM 2547 O THR A 345 28.438 15.141 5.082 1.00 43.48 O
ANISOU 2547 O THR A 345 5429 5513 5576 -117 239 89 O
ATOM 2548 CB THR A 345 26.951 13.943 2.654 1.00 39.51 C
ANISOU 2548 CB THR A 345 4964 5010 5038 -134 244 69 C
ATOM 2549 OG1 THR A 345 28.214 14.582 2.462 1.00 39.39 O
ANISOU 2549 OG1 THR A 345 4949 4991 5025 -142 265 61 O
ATOM 2550 CG2 THR A 345 25.890 14.666 1.841 1.00 39.85 C
ANISOU 2550 CG2 THR A 345 5036 5058 5044 -141 232 75 C
ATOM 2551 N LEU A 346 27.997 13.117 5.965 1.00 39.86 N
ANISOU 2551 N LEU A 346 4940 5049 5155 -104 227 89 N
ATOM 2552 CA LEU A 346 29.011 13.239 7.000 1.00 39.45 C
ANISOU 2552 CA LEU A 346 4866 4994 5128 -99 228 93 C
ATOM 2553 C LEU A 346 29.940 12.064 6.979 1.00 42.19 C
ANISOU 2553 C LEU A 346 5191 5329 5509 -100 242 80 C
ATOM 2554 O LEU A 346 29.496 10.911 6.907 1.00 46.09 O
ANISOU 2554 O LEU A 346 5676 5819 6015 -97 237 77 O
ATOM 2555 CB LEU A 346 28.376 13.300 8.383 1.00 37.51 C
ANISOU 2555 CB LEU A 346 4608 4755 4889 -87 204 112 C
ATOM 2556 CG LEU A 346 27.492 14.485 8.734 1.00 36.27 C
ANISOU 2556 CG LEU A 346 4466 4609 4705 -83 189 126 C
ATOM 2557 CD1 LEU A 346 26.632 14.109 9.926 1.00 33.33 C
ANISOU 2557 CD1 LEU A 346 4081 4243 4340 -73 168 141 C
ATOM 2558 CD2 LEU A 346 28.344 15.714 9.020 1.00 36.13 C
ANISOU 2558 CD2 LEU A 346 4450 4592 4683 -86 195 129 C
ATOM 2559 N ASP A 347 31.231 12.365 7.052 1.00 42.43 N
ANISOU 2559 N ASP A 347 5212 5353 5557 -104 257 74 N
ATOM 2560 CA ASP A 347 32.273 11.359 7.176 1.00 42.12 C
ANISOU 2560 CA ASP A 347 5147 5300 5556 -104 269 63 C
ATOM 2561 C ASP A 347 33.395 11.942 8.011 1.00 40.63 C
ANISOU 2561 C ASP A 347 4942 5107 5386 -102 271 69 C
ATOM 2562 O ASP A 347 34.493 12.233 7.530 1.00 43.13 O
ANISOU 2562 O ASP A 347 5256 5416 5713 -110 292 56 O
ATOM 2563 CB ASP A 347 32.739 10.844 5.812 1.00 46.94 C
ANISOU 2563 CB ASP A 347 5765 5902 6167 -116 296 38 C
ATOM 2564 CG ASP A 347 32.566 11.863 4.717 1.00 55.13 C
ANISOU 2564 CG ASP A 347 6833 6947 7167 -127 309 32 C
ATOM 2565 OD1 ASP A 347 31.694 11.637 3.839 1.00 57.13 O
ANISOU 2565 OD1 ASP A 347 7105 7203 7395 -132 309 27 O
ATOM 2566 OD2 ASP A 347 33.288 12.894 4.744 1.00 60.24 O
ANISOU 2566 OD2 ASP A 347 7484 7595 7807 -131 317 34 O
ATOM 2567 N LEU A 348 33.060 12.141 9.278 1.00 38.22 N
ANISOU 2567 N LEU A 348 4627 4807 5085 -93 248 88 N
ATOM 2568 CA LEU A 348 33.950 12.690 10.270 1.00 35.72 C
ANISOU 2568 CA LEU A 348 4297 4490 4786 -91 243 98 C
ATOM 2569 C LEU A 348 34.400 11.556 11.173 1.00 35.15 C
ANISOU 2569 C LEU A 348 4194 4406 4753 -86 233 102 C
ATOM 2570 O LEU A 348 33.573 10.808 11.695 1.00 35.84 O
ANISOU 2570 O LEU A 348 4276 4497 4843 -81 215 112 O
ATOM 2571 CB LEU A 348 33.231 13.772 11.069 1.00 35.53 C
ANISOU 2571 CB LEU A 348 4283 4479 4735 -86 224 116 C
ATOM 2572 CG LEU A 348 32.909 15.060 10.308 1.00 35.70 C
ANISOU 2572 CG LEU A 348 4332 4509 4721 -91 232 114 C
ATOM 2573 CD1 LEU A 348 32.061 15.989 11.154 1.00 34.44 C
ANISOU 2573 CD1 LEU A 348 4181 4361 4540 -85 211 131 C
ATOM 2574 CD2 LEU A 348 34.191 15.761 9.887 1.00 36.64 C
ANISOU 2574 CD2 LEU A 348 4451 4621 4847 -98 251 105 C
ATOM 2575 N PRO A 349 35.718 11.420 11.358 1.00 34.58 N
ANISOU 2575 N PRO A 349 4103 4322 4713 -89 243 97 N
ATOM 2576 CA PRO A 349 36.236 10.222 12.006 1.00 33.47 C
ANISOU 2576 CA PRO A 349 3933 4168 4615 -86 235 99 C
ATOM 2577 C PRO A 349 36.112 10.179 13.531 1.00 32.76 C
ANISOU 2577 C PRO A 349 3829 4082 4536 -80 206 122 C
ATOM 2578 O PRO A 349 36.155 9.097 14.100 1.00 32.36 O
ANISOU 2578 O PRO A 349 3757 4022 4513 -78 194 128 O
ATOM 2579 CB PRO A 349 37.699 10.190 11.569 1.00 33.73 C
ANISOU 2579 CB PRO A 349 3951 4185 4679 -92 257 84 C
ATOM 2580 CG PRO A 349 38.048 11.614 11.276 1.00 34.62 C
ANISOU 2580 CG PRO A 349 4082 4306 4766 -96 267 83 C
ATOM 2581 CD PRO A 349 36.786 12.349 10.936 1.00 34.24 C
ANISOU 2581 CD PRO A 349 4063 4275 4670 -95 262 88 C
ATOM 2582 N PHE A 350 35.938 11.323 14.188 1.00 32.94 N
ANISOU 2582 N PHE A 350 3863 4116 4534 -79 196 135 N
ATOM 2583 CA PHE A 350 35.889 11.334 15.660 1.00 32.84 C
ANISOU 2583 CA PHE A 350 3838 4108 4530 -76 171 156 C
ATOM 2584 C PHE A 350 34.556 11.772 16.258 1.00 31.68 C
ANISOU 2584 C PHE A 350 3707 3978 4349 -72 153 171 C
ATOM 2585 O PHE A 350 34.417 11.874 17.479 1.00 30.58 O
ANISOU 2585 O PHE A 350 3562 3845 4210 -71 133 188 O
ATOM 2586 CB PHE A 350 37.057 12.140 16.246 1.00 34.10 C
ANISOU 2586 CB PHE A 350 3989 4262 4702 -79 171 161 C
ATOM 2587 CG PHE A 350 38.399 11.538 15.960 1.00 34.12 C
ANISOU 2587 CG PHE A 350 3970 4246 4749 -83 183 151 C
ATOM 2588 CD1 PHE A 350 39.184 12.023 14.925 1.00 34.69 C
ANISOU 2588 CD1 PHE A 350 4046 4311 4823 -87 210 133 C
ATOM 2589 CD2 PHE A 350 38.866 10.462 16.706 1.00 34.43 C
ANISOU 2589 CD2 PHE A 350 3982 4272 4827 -82 168 158 C
ATOM 2590 CE1 PHE A 350 40.423 11.459 14.652 1.00 35.40 C
ANISOU 2590 CE1 PHE A 350 4114 4381 4955 -91 223 121 C
ATOM 2591 CE2 PHE A 350 40.101 9.889 16.439 1.00 34.52 C
ANISOU 2591 CE2 PHE A 350 3970 4262 4882 -85 180 148 C
ATOM 2592 CZ PHE A 350 40.882 10.389 15.410 1.00 35.02 C
ANISOU 2592 CZ PHE A 350 4037 4319 4949 -89 208 128 C
ATOM 2593 N LEU A 351 33.568 12.004 15.398 1.00 31.89 N
ANISOU 2593 N LEU A 351 3755 4014 4347 -71 160 164 N
ATOM 2594 CA LEU A 351 32.216 12.331 15.864 1.00 31.21 C
ANISOU 2594 CA LEU A 351 3682 3943 4230 -67 145 175 C
ATOM 2595 C LEU A 351 31.579 11.166 16.644 1.00 30.75 C
ANISOU 2595 C LEU A 351 3611 3885 4186 -64 126 186 C
ATOM 2596 O LEU A 351 31.264 10.122 16.074 1.00 29.81 O
ANISOU 2596 O LEU A 351 3487 3760 4078 -63 129 179 O
ATOM 2597 CB LEU A 351 31.341 12.750 14.684 1.00 30.29 C
ANISOU 2597 CB LEU A 351 3590 3833 4084 -67 155 165 C
ATOM 2598 CG LEU A 351 30.073 13.531 15.008 1.00 29.78 C
ANISOU 2598 CG LEU A 351 3542 3783 3987 -63 143 175 C
ATOM 2599 CD1 LEU A 351 30.421 14.985 15.282 1.00 29.23 C
ANISOU 2599 CD1 LEU A 351 3484 3720 3902 -65 145 179 C
ATOM 2600 CD2 LEU A 351 29.084 13.413 13.856 1.00 29.71 C
ANISOU 2600 CD2 LEU A 351 3552 3777 3957 -63 149 167 C
ATOM 2601 N LYS A 352 31.419 11.349 17.952 1.00 31.72 N
ANISOU 2601 N LYS A 352 3727 4015 4308 -63 107 204 N
ATOM 2602 CA LYS A 352 30.856 10.314 18.813 1.00 32.71 C
ANISOU 2602 CA LYS A 352 3840 4142 4445 -62 88 216 C
ATOM 2603 C LYS A 352 29.366 10.455 18.867 1.00 33.12 C
ANISOU 2603 C LYS A 352 3907 4208 4468 -59 81 221 C
ATOM 2604 O LYS A 352 28.649 9.457 18.971 1.00 35.49 O
ANISOU 2604 O LYS A 352 4201 4508 4774 -57 72 225 O
ATOM 2605 CB LYS A 352 31.352 10.437 20.248 1.00 34.48 C
ANISOU 2605 CB LYS A 352 4051 4368 4679 -66 71 233 C
ATOM 2606 CG LYS A 352 32.818 10.141 20.487 1.00 36.22 C
ANISOU 2606 CG LYS A 352 4253 4574 4935 -70 71 233 C
ATOM 2607 CD LYS A 352 33.038 10.041 21.986 1.00 37.08 C
ANISOU 2607 CD LYS A 352 4351 4686 5053 -75 48 254 C
ATOM 2608 CE LYS A 352 34.478 10.338 22.372 1.00 38.30 C
ANISOU 2608 CE LYS A 352 4491 4828 5232 -80 47 256 C
ATOM 2609 NZ LYS A 352 34.693 11.804 22.487 1.00 39.44 N
ANISOU 2609 NZ LYS A 352 4651 4982 5351 -81 53 254 N
ATOM 2610 N SER A 353 28.896 11.697 18.807 1.00 31.37 N
ANISOU 2610 N SER A 353 3704 3998 4217 -58 84 221 N
ATOM 2611 CA SER A 353 27.495 11.990 19.089 1.00 29.60 C
ANISOU 2611 CA SER A 353 3491 3786 3966 -54 75 227 C
ATOM 2612 C SER A 353 26.909 12.950 18.062 1.00 27.58 C
ANISOU 2612 C SER A 353 3258 3536 3685 -52 87 217 C
ATOM 2613 O SER A 353 27.466 14.008 17.823 1.00 27.18 O
ANISOU 2613 O SER A 353 3216 3485 3625 -54 95 213 O
ATOM 2614 CB SER A 353 27.383 12.553 20.511 1.00 29.70 C
ANISOU 2614 CB SER A 353 3502 3810 3971 -57 62 242 C
ATOM 2615 OG SER A 353 26.074 12.999 20.792 1.00 30.78 O
ANISOU 2615 OG SER A 353 3651 3960 4084 -54 56 246 O
ATOM 2616 N LEU A 354 25.795 12.562 17.450 1.00 26.88 N
ANISOU 2616 N LEU A 354 3177 3450 3585 -49 85 214 N
ATOM 2617 CA LEU A 354 25.129 13.384 16.436 1.00 26.59 C
ANISOU 2617 CA LEU A 354 3161 3415 3523 -48 93 206 C
ATOM 2618 C LEU A 354 23.648 13.590 16.748 1.00 27.56 C
ANISOU 2618 C LEU A 354 3292 3549 3629 -43 81 213 C
ATOM 2619 O LEU A 354 22.902 12.636 16.982 1.00 27.63 O
ANISOU 2619 O LEU A 354 3294 3559 3644 -41 72 218 O
ATOM 2620 CB LEU A 354 25.298 12.794 15.023 1.00 25.84 C
ANISOU 2620 CB LEU A 354 3073 3312 3433 -50 106 192 C
ATOM 2621 CG LEU A 354 24.418 13.357 13.886 1.00 25.36 C
ANISOU 2621 CG LEU A 354 3034 3253 3347 -50 110 186 C
ATOM 2622 CD1 LEU A 354 24.756 14.799 13.553 1.00 24.82 C
ANISOU 2622 CD1 LEU A 354 2981 3188 3261 -53 117 184 C
ATOM 2623 CD2 LEU A 354 24.499 12.505 12.630 1.00 25.51 C
ANISOU 2623 CD2 LEU A 354 3057 3264 3370 -53 121 173 C
ATOM 2624 N THR A 355 23.235 14.852 16.727 1.00 28.96 N
ANISOU 2624 N THR A 355 3484 3733 3786 -43 82 214 N
ATOM 2625 CA THR A 355 21.848 15.232 16.966 1.00 29.41 C
ANISOU 2625 CA THR A 355 3548 3798 3828 -39 72 219 C
ATOM 2626 C THR A 355 21.327 16.115 15.829 1.00 29.48 C
ANISOU 2626 C THR A 355 3576 3805 3818 -38 76 213 C
ATOM 2627 O THR A 355 21.848 17.206 15.565 1.00 28.82 O
ANISOU 2627 O THR A 355 3502 3721 3726 -40 83 210 O
ATOM 2628 CB THR A 355 21.701 15.962 18.314 1.00 29.86 C
ANISOU 2628 CB THR A 355 3600 3864 3880 -38 65 228 C
ATOM 2629 OG1 THR A 355 22.012 15.046 19.369 1.00 29.69 O
ANISOU 2629 OG1 THR A 355 3562 3844 3873 -40 58 236 O
ATOM 2630 CG2 THR A 355 20.287 16.508 18.489 1.00 29.38 C
ANISOU 2630 CG2 THR A 355 3547 3811 3804 -34 58 231 C
ATOM 2631 N LEU A 356 20.307 15.601 15.155 1.00 28.75 N
ANISOU 2631 N LEU A 356 3490 3712 3721 -36 72 211 N
ATOM 2632 CA LEU A 356 19.562 16.339 14.173 1.00 28.13 C
ANISOU 2632 CA LEU A 356 3430 3633 3626 -36 71 208 C
ATOM 2633 C LEU A 356 18.117 16.164 14.592 1.00 28.39 C
ANISOU 2633 C LEU A 356 3460 3670 3655 -31 58 214 C
ATOM 2634 O LEU A 356 17.556 15.066 14.542 1.00 29.18 O
ANISOU 2634 O LEU A 356 3554 3769 3763 -29 53 216 O
ATOM 2635 CB LEU A 356 19.799 15.746 12.795 1.00 28.35 C
ANISOU 2635 CB LEU A 356 3467 3652 3652 -41 79 198 C
ATOM 2636 CG LEU A 356 19.782 16.689 11.591 1.00 29.27 C
ANISOU 2636 CG LEU A 356 3605 3765 3750 -46 84 193 C
ATOM 2637 CD1 LEU A 356 20.303 15.933 10.379 1.00 29.75 C
ANISOU 2637 CD1 LEU A 356 3672 3818 3810 -53 95 182 C
ATOM 2638 CD2 LEU A 356 18.405 17.268 11.313 1.00 28.52 C
ANISOU 2638 CD2 LEU A 356 3521 3672 3641 -44 70 198 C
ATOM 2639 N THR A 357 17.511 17.233 15.065 1.00 28.24 N
ANISOU 2639 N THR A 357 3446 3656 3628 -28 53 218 N
ATOM 2640 CA THR A 357 16.154 17.113 15.550 1.00 28.20 C
ANISOU 2640 CA THR A 357 3436 3654 3622 -24 42 224 C
ATOM 2641 C THR A 357 15.327 18.347 15.191 1.00 28.39 C
ANISOU 2641 C THR A 357 3473 3678 3636 -22 37 224 C
ATOM 2642 O THR A 357 15.882 19.444 15.013 1.00 27.50 O
ANISOU 2642 O THR A 357 3368 3564 3516 -24 41 222 O
ATOM 2643 CB THR A 357 16.138 16.804 17.067 1.00 28.39 C
ANISOU 2643 CB THR A 357 3443 3686 3654 -22 39 230 C
ATOM 2644 OG1 THR A 357 14.806 16.450 17.478 1.00 29.46 O
ANISOU 2644 OG1 THR A 357 3575 3827 3792 -18 30 235 O
ATOM 2645 CG2 THR A 357 16.647 17.993 17.879 1.00 28.19 C
ANISOU 2645 CG2 THR A 357 3418 3666 3624 -23 42 231 C
ATOM 2646 N MET A 358 14.012 18.148 15.065 1.00 28.47 N
ANISOU 2646 N MET A 358 3482 3687 3646 -18 26 227 N
ATOM 2647 CA MET A 358 13.045 19.227 14.798 1.00 29.15 C
ANISOU 2647 CA MET A 358 3577 3771 3727 -16 19 228 C
ATOM 2648 C MET A 358 13.359 19.992 13.507 1.00 29.15 C
ANISOU 2648 C MET A 358 3595 3763 3715 -20 19 225 C
ATOM 2649 O MET A 358 13.300 21.205 13.464 1.00 29.21 O
ANISOU 2649 O MET A 358 3610 3769 3719 -20 18 225 O
ATOM 2650 CB MET A 358 12.902 20.193 16.001 1.00 29.40 C
ANISOU 2650 CB MET A 358 3600 3808 3759 -13 20 229 C
ATOM 2651 CG MET A 358 12.801 19.512 17.367 1.00 31.27 C
ANISOU 2651 CG MET A 358 3821 4055 4005 -12 21 232 C
ATOM 2652 SD MET A 358 12.655 20.632 18.786 1.00 34.38 S
ANISOU 2652 SD MET A 358 4208 4457 4398 -11 24 232 S
ATOM 2653 CE MET A 358 10.924 21.070 18.673 1.00 34.54 C
ANISOU 2653 CE MET A 358 4227 4474 4423 -5 16 231 C
ATOM 2654 N ASN A 359 13.684 19.277 12.449 1.00 30.27 N
ANISOU 2654 N ASN A 359 3747 3901 3854 -25 22 221 N
ATOM 2655 CA ASN A 359 13.974 19.932 11.185 1.00 33.41 C
ANISOU 2655 CA ASN A 359 4163 4291 4238 -31 22 219 C
ATOM 2656 C ASN A 359 12.694 20.404 10.485 1.00 35.40 C
ANISOU 2656 C ASN A 359 4426 4537 4485 -31 7 223 C
ATOM 2657 O ASN A 359 11.639 19.789 10.647 1.00 34.95 O
ANISOU 2657 O ASN A 359 4362 4479 4435 -27 -2 226 O
ATOM 2658 CB ASN A 359 14.776 18.987 10.278 1.00 32.78 C
ANISOU 2658 CB ASN A 359 4090 4209 4155 -38 32 212 C
ATOM 2659 CG ASN A 359 15.654 19.727 9.298 1.00 32.82 C
ANISOU 2659 CG ASN A 359 4112 4209 4146 -47 40 208 C
ATOM 2660 OD1 ASN A 359 15.380 19.750 8.098 1.00 33.36 O
ANISOU 2660 OD1 ASN A 359 4198 4273 4203 -55 37 206 O
ATOM 2661 ND2 ASN A 359 16.714 20.349 9.804 1.00 32.95 N
ANISOU 2661 ND2 ASN A 359 4125 4229 4164 -48 51 206 N
ATOM 2662 N LYS A 360 12.789 21.502 9.731 1.00 39.78 N
ANISOU 2662 N LYS A 360 4997 5087 5030 -36 4 224 N
ATOM 2663 CA LYS A 360 11.705 21.933 8.839 1.00 45.27 C
ANISOU 2663 CA LYS A 360 5704 5774 5720 -39 -12 229 C
ATOM 2664 C LYS A 360 11.485 20.917 7.703 1.00 46.62 C
ANISOU 2664 C LYS A 360 5888 5942 5884 -45 -15 227 C
ATOM 2665 O LYS A 360 12.436 20.429 7.090 1.00 48.65 O
ANISOU 2665 O LYS A 360 6153 6199 6132 -53 -3 221 O
ATOM 2666 CB LYS A 360 11.971 23.341 8.280 1.00 49.69 C
ANISOU 2666 CB LYS A 360 6279 6328 6270 -44 -15 232 C
ATOM 2667 CG LYS A 360 10.857 23.909 7.390 1.00 56.90 C
ANISOU 2667 CG LYS A 360 7206 7232 7181 -48 -35 239 C
ATOM 2668 CD LYS A 360 11.288 24.119 5.927 1.00 60.95 C
ANISOU 2668 CD LYS A 360 7743 7739 7674 -62 -36 239 C
ATOM 2669 CE LYS A 360 10.256 23.633 4.899 1.00 62.56 C
ANISOU 2669 CE LYS A 360 7960 7936 7873 -68 -54 244 C
ATOM 2670 NZ LYS A 360 8.836 24.052 5.119 1.00 60.82 N
ANISOU 2670 NZ LYS A 360 7734 7709 7667 -61 -75 252 N
ATOM 2671 N GLY A 361 10.224 20.589 7.449 1.00 48.54 N
ANISOU 2671 N GLY A 361 6131 6180 6131 -43 -31 232 N
ATOM 2672 CA GLY A 361 9.866 19.612 6.422 1.00 50.71 C
ANISOU 2672 CA GLY A 361 6415 6450 6399 -49 -37 230 C
ATOM 2673 C GLY A 361 10.347 18.188 6.678 1.00 52.07 C
ANISOU 2673 C GLY A 361 6578 6628 6578 -48 -25 223 C
ATOM 2674 O GLY A 361 10.847 17.854 7.761 1.00 54.36 O
ANISOU 2674 O GLY A 361 6850 6924 6878 -41 -15 221 O
ATOM 2675 N SER A 362 10.171 17.342 5.668 1.00 48.40 N
ANISOU 2675 N SER A 362 6125 6160 6105 -55 -28 219 N
ATOM 2676 CA SER A 362 10.674 15.990 5.709 1.00 44.44 C
ANISOU 2676 CA SER A 362 5614 5659 5608 -55 -17 211 C
ATOM 2677 C SER A 362 12.041 15.983 5.074 1.00 41.40 C
ANISOU 2677 C SER A 362 5240 5275 5212 -65 1 201 C
ATOM 2678 O SER A 362 12.389 16.875 4.321 1.00 41.47 O
ANISOU 2678 O SER A 362 5268 5282 5206 -74 2 201 O
ATOM 2679 CB SER A 362 9.756 15.055 4.946 1.00 45.79 C
ANISOU 2679 CB SER A 362 5792 5826 5779 -58 -29 211 C
ATOM 2680 OG SER A 362 8.444 15.125 5.470 1.00 49.64 O
ANISOU 2680 OG SER A 362 6269 6312 6278 -49 -46 220 O
ATOM 2681 N ILE A 363 12.828 14.990 5.438 1.00 39.51 N
ANISOU 2681 N ILE A 363 4988 5038 4983 -63 15 194 N
ATOM 2682 CA ILE A 363 14.058 14.651 4.750 1.00 36.46 C
ANISOU 2682 CA ILE A 363 4609 4650 4591 -73 34 182 C
ATOM 2683 C ILE A 363 14.120 13.145 4.882 1.00 34.46 C
ANISOU 2683 C ILE A 363 4343 4396 4353 -70 38 175 C
ATOM 2684 O ILE A 363 13.538 12.574 5.804 1.00 33.02 O
ANISOU 2684 O ILE A 363 4142 4216 4186 -60 30 181 O
ATOM 2685 CB ILE A 363 15.310 15.295 5.385 1.00 35.85 C
ANISOU 2685 CB ILE A 363 4525 4577 4518 -72 49 180 C
ATOM 2686 CG1 ILE A 363 15.259 15.194 6.909 1.00 35.12 C
ANISOU 2686 CG1 ILE A 363 4408 4489 4444 -59 46 187 C
ATOM 2687 CG2 ILE A 363 15.493 16.741 4.917 1.00 34.48 C
ANISOU 2687 CG2 ILE A 363 4370 4404 4328 -78 49 183 C
ATOM 2688 CD1 ILE A 363 16.556 15.576 7.583 1.00 36.09 C
ANISOU 2688 CD1 ILE A 363 4522 4616 4574 -59 61 184 C
ATOM 2689 N SER A 364 14.780 12.494 3.942 1.00 33.71 N
ANISOU 2689 N SER A 364 4257 4297 4253 -80 51 162 N
ATOM 2690 CA SER A 364 14.954 11.063 4.044 1.00 33.35 C
ANISOU 2690 CA SER A 364 4198 4249 4224 -78 57 154 C
ATOM 2691 C SER A 364 16.386 10.761 4.457 1.00 32.98 C
ANISOU 2691 C SER A 364 4137 4202 4191 -78 77 145 C
ATOM 2692 O SER A 364 17.295 11.525 4.158 1.00 33.41 O
ANISOU 2692 O SER A 364 4200 4257 4237 -85 90 140 O
ATOM 2693 CB SER A 364 14.563 10.363 2.744 1.00 32.87 C
ANISOU 2693 CB SER A 364 4154 4183 4152 -89 56 144 C
ATOM 2694 OG SER A 364 14.973 11.117 1.627 1.00 33.85 O
ANISOU 2694 OG SER A 364 4303 4306 4252 -103 64 138 O
ATOM 2695 N PHE A 365 16.566 9.665 5.181 1.00 33.32 N
ANISOU 2695 N PHE A 365 4157 4243 4257 -71 78 144 N
ATOM 2696 CA PHE A 365 17.883 9.240 5.607 1.00 34.36 C
ANISOU 2696 CA PHE A 365 4273 4372 4408 -71 95 136 C
ATOM 2697 C PHE A 365 18.777 8.918 4.411 1.00 35.93 C
ANISOU 2697 C PHE A 365 4483 4564 4602 -84 115 118 C
ATOM 2698 O PHE A 365 18.313 8.359 3.420 1.00 37.45 O
ANISOU 2698 O PHE A 365 4689 4754 4786 -90 115 109 O
ATOM 2699 CB PHE A 365 17.778 8.022 6.529 1.00 33.34 C
ANISOU 2699 CB PHE A 365 4119 4241 4306 -63 89 140 C
ATOM 2700 CG PHE A 365 19.098 7.574 7.070 1.00 32.41 C
ANISOU 2700 CG PHE A 365 3982 4119 4211 -62 103 134 C
ATOM 2701 CD1 PHE A 365 19.639 8.182 8.197 1.00 31.28 C
ANISOU 2701 CD1 PHE A 365 3827 3981 4077 -57 102 144 C
ATOM 2702 CD2 PHE A 365 19.821 6.572 6.430 1.00 31.70 C
ANISOU 2702 CD2 PHE A 365 3887 4020 4136 -67 117 118 C
ATOM 2703 CE1 PHE A 365 20.869 7.787 8.683 1.00 30.42 C
ANISOU 2703 CE1 PHE A 365 3700 3867 3990 -57 113 140 C
ATOM 2704 CE2 PHE A 365 21.052 6.176 6.916 1.00 31.40 C
ANISOU 2704 CE2 PHE A 365 3830 3976 4123 -67 129 113 C
ATOM 2705 CZ PHE A 365 21.575 6.788 8.039 1.00 30.53 C
ANISOU 2705 CZ PHE A 365 3708 3871 4021 -62 126 125 C
ATOM 2706 N LYS A 366 20.051 9.300 4.517 1.00 38.31 N
ANISOU 2706 N LYS A 366 4780 4864 4909 -87 133 111 N
ATOM 2707 CA LYS A 366 21.099 8.950 3.557 1.00 39.20 C
ANISOU 2707 CA LYS A 366 4898 4970 5024 -98 156 92 C
ATOM 2708 C LYS A 366 22.276 8.352 4.309 1.00 38.48 C
ANISOU 2708 C LYS A 366 4781 4873 4964 -94 168 87 C
ATOM 2709 O LYS A 366 22.601 8.813 5.402 1.00 38.36 O
ANISOU 2709 O LYS A 366 4752 4861 4959 -86 162 98 O
ATOM 2710 CB LYS A 366 21.576 10.199 2.811 1.00 42.63 C
ANISOU 2710 CB LYS A 366 5355 5407 5433 -109 167 88 C
ATOM 2711 CG LYS A 366 20.970 10.407 1.427 1.00 46.49 C
ANISOU 2711 CG LYS A 366 5874 5896 5892 -122 167 82 C
ATOM 2712 CD LYS A 366 21.433 11.709 0.772 1.00 49.50 C
ANISOU 2712 CD LYS A 366 6277 6281 6249 -134 175 82 C
ATOM 2713 CE LYS A 366 22.908 11.691 0.370 1.00 55.07 C
ANISOU 2713 CE LYS A 366 6981 6982 6961 -143 204 65 C
ATOM 2714 NZ LYS A 366 23.855 12.173 1.430 1.00 55.92 N
ANISOU 2714 NZ LYS A 366 7067 7089 7087 -135 210 70 N
ATOM 2715 N LYS A 367 22.899 7.322 3.727 1.00 40.28 N
ANISOU 2715 N LYS A 367 5002 5092 5208 -99 184 69 N
ATOM 2716 CA LYS A 367 24.168 6.735 4.219 1.00 39.37 C
ANISOU 2716 CA LYS A 367 4863 4969 5127 -98 198 61 C
ATOM 2717 C LYS A 367 25.091 7.761 4.910 1.00 37.30 C
ANISOU 2717 C LYS A 367 4595 4709 4868 -96 203 68 C
ATOM 2718 O LYS A 367 25.370 8.823 4.357 1.00 35.08 O
ANISOU 2718 O LYS A 367 4332 4432 4564 -103 212 65 O
ATOM 2719 CB LYS A 367 24.937 6.111 3.035 1.00 42.81 C
ANISOU 2719 CB LYS A 367 5302 5394 5567 -110 223 35 C
ATOM 2720 CG LYS A 367 25.140 4.596 3.044 1.00 45.15 C
ANISOU 2720 CG LYS A 367 5579 5680 5897 -107 228 23 C
ATOM 2721 CD LYS A 367 23.883 3.812 2.675 1.00 48.53 C
ANISOU 2721 CD LYS A 367 6014 6108 6316 -106 213 24 C
ATOM 2722 CE LYS A 367 24.193 2.338 2.436 1.00 47.78 C
ANISOU 2722 CE LYS A 367 5900 6000 6252 -107 222 8 C
ATOM 2723 NZ LYS A 367 22.994 1.471 2.626 1.00 47.86 N
ANISOU 2723 NZ LYS A 367 5908 6011 6265 -100 201 16 N
ATOM 2724 N VAL A 368 25.538 7.459 6.126 1.00 35.34 N
ANISOU 2724 N VAL A 368 4320 4458 4646 -87 196 78 N
ATOM 2725 CA VAL A 368 26.660 8.197 6.715 1.00 34.63 C
ANISOU 2725 CA VAL A 368 4222 4369 4567 -87 204 80 C
ATOM 2726 C VAL A 368 27.796 7.235 7.037 1.00 34.83 C
ANISOU 2726 C VAL A 368 4221 4381 4633 -86 214 71 C
ATOM 2727 O VAL A 368 27.595 6.023 7.102 1.00 34.87 O
ANISOU 2727 O VAL A 368 4211 4378 4659 -83 210 68 O
ATOM 2728 CB VAL A 368 26.295 9.065 7.961 1.00 34.24 C
ANISOU 2728 CB VAL A 368 4169 4329 4511 -78 185 102 C
ATOM 2729 CG1 VAL A 368 25.389 10.229 7.584 1.00 33.47 C
ANISOU 2729 CG1 VAL A 368 4097 4242 4378 -80 178 109 C
ATOM 2730 CG2 VAL A 368 25.684 8.247 9.086 1.00 34.30 C
ANISOU 2730 CG2 VAL A 368 4157 4338 4536 -69 164 116 C
ATOM 2731 N ALA A 369 29.000 7.770 7.199 1.00 35.05 N
ANISOU 2731 N ALA A 369 4241 4404 4672 -89 228 67 N
ATOM 2732 CA ALA A 369 30.135 6.950 7.606 1.00 34.47 C
ANISOU 2732 CA ALA A 369 4140 4317 4640 -88 236 61 C
ATOM 2733 C ALA A 369 30.805 7.613 8.803 1.00 34.28 C
ANISOU 2733 C ALA A 369 4101 4294 4628 -83 226 76 C
ATOM 2734 O ALA A 369 31.659 8.488 8.641 1.00 32.95 O
ANISOU 2734 O ALA A 369 3936 4125 4456 -88 239 72 O
ATOM 2735 CB ALA A 369 31.109 6.753 6.452 1.00 33.44 C
ANISOU 2735 CB ALA A 369 4011 4175 4518 -99 265 35 C
ATOM 2736 N LEU A 370 30.377 7.205 10.003 1.00 33.30 N
ANISOU 2736 N LEU A 370 3962 4173 4517 -75 203 94 N
ATOM 2737 CA LEU A 370 30.852 7.785 11.257 1.00 31.42 C
ANISOU 2737 CA LEU A 370 3712 3937 4287 -72 190 111 C
ATOM 2738 C LEU A 370 31.366 6.690 12.184 1.00 31.91 C
ANISOU 2738 C LEU A 370 3744 3988 4390 -68 179 118 C
ATOM 2739 O LEU A 370 30.666 6.275 13.105 1.00 31.94 O
ANISOU 2739 O LEU A 370 3741 3997 4396 -63 157 135 O
ATOM 2740 CB LEU A 370 29.732 8.586 11.929 1.00 30.50 C
ANISOU 2740 CB LEU A 370 3611 3838 4140 -67 171 129 C
ATOM 2741 CG LEU A 370 29.055 9.672 11.070 1.00 30.28 C
ANISOU 2741 CG LEU A 370 3611 3820 4072 -70 178 125 C
ATOM 2742 CD1 LEU A 370 27.760 10.170 11.689 1.00 28.20 C
ANISOU 2742 CD1 LEU A 370 3359 3571 3785 -64 158 141 C
ATOM 2743 CD2 LEU A 370 30.017 10.822 10.795 1.00 30.07 C
ANISOU 2743 CD2 LEU A 370 3592 3793 4038 -75 193 120 C
ATOM 2744 N PRO A 371 32.605 6.216 11.944 1.00 32.41 N
ANISOU 2744 N PRO A 371 3789 4035 4487 -72 193 106 N
ATOM 2745 CA PRO A 371 33.201 5.112 12.719 1.00 31.85 C
ANISOU 2745 CA PRO A 371 3687 3950 4461 -70 182 111 C
ATOM 2746 C PRO A 371 33.159 5.259 14.257 1.00 31.28 C
ANISOU 2746 C PRO A 371 3604 3884 4397 -66 155 137 C
ATOM 2747 O PRO A 371 32.960 4.255 14.952 1.00 32.30 O
ANISOU 2747 O PRO A 371 3715 4007 4549 -64 138 147 O
ATOM 2748 CB PRO A 371 34.650 5.064 12.215 1.00 32.04 C
ANISOU 2748 CB PRO A 371 3698 3958 4517 -75 204 94 C
ATOM 2749 CG PRO A 371 34.877 6.378 11.527 1.00 32.04 C
ANISOU 2749 CG PRO A 371 3721 3967 4485 -79 222 86 C
ATOM 2750 CD PRO A 371 33.550 6.744 10.943 1.00 31.95 C
ANISOU 2750 CD PRO A 371 3738 3972 4430 -79 220 86 C
ATOM 2751 N SER A 372 33.336 6.473 14.779 1.00 29.98 N
ANISOU 2751 N SER A 372 3449 3729 4211 -67 152 147 N
ATOM 2752 CA SER A 372 33.268 6.717 16.235 1.00 29.90 C
ANISOU 2752 CA SER A 372 3431 3726 4202 -65 128 170 C
ATOM 2753 C SER A 372 31.854 6.830 16.835 1.00 30.70 C
ANISOU 2753 C SER A 372 3545 3844 4273 -62 109 185 C
ATOM 2754 O SER A 372 31.726 6.974 18.058 1.00 32.33 O
ANISOU 2754 O SER A 372 3746 4057 4478 -62 90 204 O
ATOM 2755 CB SER A 372 34.011 7.997 16.606 1.00 28.42 C
ANISOU 2755 CB SER A 372 3249 3543 4004 -68 131 174 C
ATOM 2756 OG SER A 372 35.382 7.901 16.332 1.00 28.78 O
ANISOU 2756 OG SER A 372 3279 3572 4083 -72 144 164 O
ATOM 2757 N LEU A 373 30.811 6.781 16.000 1.00 29.48 N
ANISOU 2757 N LEU A 373 3408 3697 4094 -60 116 177 N
ATOM 2758 CA LEU A 373 29.460 7.151 16.437 1.00 28.93 C
ANISOU 2758 CA LEU A 373 3354 3644 3993 -56 102 189 C
ATOM 2759 C LEU A 373 28.843 6.210 17.469 1.00 28.40 C
ANISOU 2759 C LEU A 373 3273 3579 3938 -55 80 206 C
ATOM 2760 O LEU A 373 28.609 5.039 17.191 1.00 28.80 O
ANISOU 2760 O LEU A 373 3313 3621 4007 -54 77 203 O
ATOM 2761 CB LEU A 373 28.519 7.305 15.234 1.00 28.92 C
ANISOU 2761 CB LEU A 373 3373 3647 3965 -55 113 177 C
ATOM 2762 CG LEU A 373 27.090 7.826 15.454 1.00 28.55 C
ANISOU 2762 CG LEU A 373 3344 3616 3886 -51 101 186 C
ATOM 2763 CD1 LEU A 373 27.077 9.297 15.840 1.00 28.71 C
ANISOU 2763 CD1 LEU A 373 3378 3648 3881 -52 101 192 C
ATOM 2764 CD2 LEU A 373 26.269 7.611 14.198 1.00 28.17 C
ANISOU 2764 CD2 LEU A 373 3311 3568 3821 -51 110 174 C
ATOM 2765 N SER A 374 28.563 6.741 18.649 1.00 27.11 N
ANISOU 2765 N SER A 374 3110 3426 3762 -56 64 223 N
ATOM 2766 CA SER A 374 27.876 5.977 19.676 1.00 27.51 C
ANISOU 2766 CA SER A 374 3151 3482 3818 -56 43 240 C
ATOM 2767 C SER A 374 26.445 6.476 19.995 1.00 27.89 C
ANISOU 2767 C SER A 374 3216 3548 3833 -53 36 248 C
ATOM 2768 O SER A 374 25.613 5.701 20.456 1.00 29.42 O
ANISOU 2768 O SER A 374 3405 3745 4028 -53 23 257 O
ATOM 2769 CB SER A 374 28.716 5.935 20.952 1.00 27.38 C
ANISOU 2769 CB SER A 374 3119 3463 3820 -61 28 256 C
ATOM 2770 OG SER A 374 28.652 7.158 21.657 1.00 26.95 O
ANISOU 2770 OG SER A 374 3076 3422 3740 -64 25 264 O
ATOM 2771 N TYR A 375 26.170 7.755 19.741 1.00 27.12 N
ANISOU 2771 N TYR A 375 3137 3460 3706 -52 44 243 N
ATOM 2772 CA TYR A 375 24.909 8.389 20.128 1.00 26.55 C
ANISOU 2772 CA TYR A 375 3079 3403 3605 -50 38 250 C
ATOM 2773 C TYR A 375 24.226 9.057 18.922 1.00 26.34 C
ANISOU 2773 C TYR A 375 3072 3380 3555 -46 51 237 C
ATOM 2774 O TYR A 375 24.815 9.927 18.259 1.00 26.41 O
ANISOU 2774 O TYR A 375 3091 3386 3556 -46 63 227 O
ATOM 2775 CB TYR A 375 25.170 9.408 21.244 1.00 26.03 C
ANISOU 2775 CB TYR A 375 3015 3347 3526 -54 32 260 C
ATOM 2776 CG TYR A 375 23.938 10.110 21.737 1.00 26.35 C
ANISOU 2776 CG TYR A 375 3068 3403 3540 -52 27 265 C
ATOM 2777 CD1 TYR A 375 23.305 9.702 22.909 1.00 26.25 C
ANISOU 2777 CD1 TYR A 375 3049 3399 3524 -55 13 279 C
ATOM 2778 CD2 TYR A 375 23.394 11.192 21.027 1.00 27.08 C
ANISOU 2778 CD2 TYR A 375 3178 3500 3608 -48 37 256 C
ATOM 2779 CE1 TYR A 375 22.157 10.340 23.360 1.00 26.73 C
ANISOU 2779 CE1 TYR A 375 3120 3473 3562 -54 10 283 C
ATOM 2780 CE2 TYR A 375 22.252 11.847 21.473 1.00 27.28 C
ANISOU 2780 CE2 TYR A 375 3213 3538 3612 -46 32 260 C
ATOM 2781 CZ TYR A 375 21.635 11.416 22.639 1.00 27.12 C
ANISOU 2781 CZ TYR A 375 3186 3527 3592 -49 20 272 C
ATOM 2782 OH TYR A 375 20.502 12.062 23.080 1.00 27.13 O
ANISOU 2782 OH TYR A 375 3195 3539 3573 -48 18 275 O
ATOM 2783 N LEU A 376 22.991 8.651 18.638 1.00 25.31 N
ANISOU 2783 N LEU A 376 2947 3253 3414 -42 46 237 N
ATOM 2784 CA LEU A 376 22.287 9.149 17.447 1.00 25.16 C
ANISOU 2784 CA LEU A 376 2947 3236 3377 -39 54 226 C
ATOM 2785 C LEU A 376 20.829 9.544 17.721 1.00 25.63 C
ANISOU 2785 C LEU A 376 3015 3305 3415 -36 45 233 C
ATOM 2786 O LEU A 376 19.960 8.685 17.959 1.00 25.52 O
ANISOU 2786 O LEU A 376 2996 3294 3406 -34 36 238 O
ATOM 2787 CB LEU A 376 22.376 8.137 16.303 1.00 24.27 C
ANISOU 2787 CB LEU A 376 2832 3111 3276 -39 62 214 C
ATOM 2788 CG LEU A 376 21.957 8.569 14.896 1.00 24.28 C
ANISOU 2788 CG LEU A 376 2853 3111 3259 -39 72 201 C
ATOM 2789 CD1 LEU A 376 22.590 9.896 14.495 1.00 24.30 C
ANISOU 2789 CD1 LEU A 376 2870 3115 3246 -42 84 195 C
ATOM 2790 CD2 LEU A 376 22.301 7.491 13.878 1.00 23.95 C
ANISOU 2790 CD2 LEU A 376 2808 3057 3233 -41 81 188 C
ATOM 2791 N ASP A 377 20.583 10.854 17.708 1.00 25.87 N
ANISOU 2791 N ASP A 377 3059 3343 3425 -35 49 232 N
ATOM 2792 CA ASP A 377 19.241 11.407 17.865 1.00 25.77 C
ANISOU 2792 CA ASP A 377 3056 3340 3395 -32 42 236 C
ATOM 2793 C ASP A 377 18.811 12.053 16.551 1.00 26.13 C
ANISOU 2793 C ASP A 377 3120 3382 3425 -30 48 226 C
ATOM 2794 O ASP A 377 19.284 13.131 16.184 1.00 26.33 O
ANISOU 2794 O ASP A 377 3156 3407 3439 -32 56 221 O
ATOM 2795 CB ASP A 377 19.190 12.416 19.017 1.00 25.80 C
ANISOU 2795 CB ASP A 377 3060 3353 3388 -33 39 243 C
ATOM 2796 CG ASP A 377 17.765 12.893 19.326 1.00 26.75 C
ANISOU 2796 CG ASP A 377 3186 3482 3495 -29 32 247 C
ATOM 2797 OD1 ASP A 377 17.579 13.707 20.264 1.00 27.03 O
ANISOU 2797 OD1 ASP A 377 3221 3525 3521 -30 30 251 O
ATOM 2798 OD2 ASP A 377 16.820 12.462 18.631 1.00 26.77 O
ANISOU 2798 OD2 ASP A 377 3193 3482 3495 -26 29 245 O
ATOM 2799 N LEU A 378 17.928 11.361 15.841 1.00 26.32 N
ANISOU 2799 N LEU A 378 3148 3403 3448 -28 44 223 N
ATOM 2800 CA LEU A 378 17.313 11.867 14.609 1.00 25.94 C
ANISOU 2800 CA LEU A 378 3118 3352 3385 -28 46 216 C
ATOM 2801 C LEU A 378 15.790 11.988 14.797 1.00 25.54 C
ANISOU 2801 C LEU A 378 3071 3307 3327 -24 34 222 C
ATOM 2802 O LEU A 378 15.012 11.743 13.860 1.00 25.88 O
ANISOU 2802 O LEU A 378 3123 3345 3364 -23 30 219 O
ATOM 2803 CB LEU A 378 17.611 10.902 13.456 1.00 25.73 C
ANISOU 2803 CB LEU A 378 3094 3316 3364 -31 52 206 C
ATOM 2804 CG LEU A 378 18.867 10.950 12.581 1.00 25.43 C
ANISOU 2804 CG LEU A 378 3061 3270 3328 -37 68 194 C
ATOM 2805 CD1 LEU A 378 19.957 11.860 13.108 1.00 24.95 C
ANISOU 2805 CD1 LEU A 378 2999 3211 3268 -39 76 195 C
ATOM 2806 CD2 LEU A 378 19.376 9.535 12.361 1.00 25.24 C
ANISOU 2806 CD2 LEU A 378 3025 3238 3325 -38 72 188 C
ATOM 2807 N SER A 379 15.381 12.358 16.009 1.00 23.92 N
ANISOU 2807 N SER A 379 2857 3109 3121 -21 28 231 N
ATOM 2808 CA SER A 379 13.988 12.401 16.391 1.00 23.52 C
ANISOU 2808 CA SER A 379 2805 3063 3068 -17 18 237 C
ATOM 2809 C SER A 379 13.274 13.618 15.814 1.00 23.71 C
ANISOU 2809 C SER A 379 2843 3086 3077 -15 17 234 C
ATOM 2810 O SER A 379 13.917 14.605 15.462 1.00 23.62 O
ANISOU 2810 O SER A 379 2842 3074 3058 -17 23 230 O
ATOM 2811 CB SER A 379 13.875 12.412 17.919 1.00 23.88 C
ANISOU 2811 CB SER A 379 2836 3118 3117 -17 15 246 C
ATOM 2812 OG SER A 379 14.074 13.712 18.466 1.00 23.51 O
ANISOU 2812 OG SER A 379 2794 3076 3060 -18 19 246 O
ATOM 2813 N ARG A 380 11.944 13.540 15.713 1.00 24.09 N
ANISOU 2813 N ARG A 380 2892 3135 3125 -12 7 237 N
ATOM 2814 CA ARG A 380 11.101 14.717 15.440 1.00 24.17 C
ANISOU 2814 CA ARG A 380 2912 3144 3127 -10 3 237 C
ATOM 2815 C ARG A 380 11.428 15.443 14.115 1.00 24.99 C
ANISOU 2815 C ARG A 380 3034 3240 3219 -13 4 231 C
ATOM 2816 O ARG A 380 11.481 16.669 14.075 1.00 25.81 O
ANISOU 2816 O ARG A 380 3146 3344 3316 -13 5 231 O
ATOM 2817 CB ARG A 380 11.190 15.692 16.623 1.00 23.35 C
ANISOU 2817 CB ARG A 380 2802 3048 3021 -9 6 239 C
ATOM 2818 CG ARG A 380 10.264 15.356 17.765 1.00 23.93 C
ANISOU 2818 CG ARG A 380 2862 3129 3102 -6 2 245 C
ATOM 2819 CD ARG A 380 10.722 15.938 19.088 1.00 24.49 C
ANISOU 2819 CD ARG A 380 2925 3208 3170 -8 8 246 C
ATOM 2820 NE ARG A 380 11.693 15.019 19.673 1.00 26.67 N
ANISOU 2820 NE ARG A 380 3192 3488 3451 -13 11 250 N
ATOM 2821 CZ ARG A 380 11.572 14.378 20.833 1.00 26.26 C
ANISOU 2821 CZ ARG A 380 3128 3445 3404 -15 9 256 C
ATOM 2822 NH1 ARG A 380 10.521 14.548 21.625 1.00 24.78 N
ANISOU 2822 NH1 ARG A 380 2934 3263 3216 -15 7 259 N
ATOM 2823 NH2 ARG A 380 12.549 13.564 21.197 1.00 27.67 N
ANISOU 2823 NH2 ARG A 380 3300 3624 3589 -20 10 260 N
ATOM 2824 N ASN A 381 11.663 14.694 13.043 1.00 25.54 N
ANISOU 2824 N ASN A 381 3113 3304 3288 -16 5 227 N
ATOM 2825 CA ASN A 381 12.091 15.290 11.773 1.00 26.84 C
ANISOU 2825 CA ASN A 381 3295 3461 3438 -22 8 221 C
ATOM 2826 C ASN A 381 11.155 14.973 10.629 1.00 27.08 C
ANISOU 2826 C ASN A 381 3338 3485 3464 -24 -1 221 C
ATOM 2827 O ASN A 381 11.489 15.254 9.480 1.00 27.69 O
ANISOU 2827 O ASN A 381 3433 3558 3530 -31 0 216 O
ATOM 2828 CB ASN A 381 13.503 14.803 11.360 1.00 27.23 C
ANISOU 2828 CB ASN A 381 3347 3509 3488 -27 22 214 C
ATOM 2829 CG ASN A 381 14.605 15.363 12.238 1.00 27.61 C
ANISOU 2829 CG ASN A 381 3388 3563 3540 -27 32 214 C
ATOM 2830 OD1 ASN A 381 14.682 16.570 12.474 1.00 27.88 O
ANISOU 2830 OD1 ASN A 381 3427 3598 3566 -27 32 216 O
ATOM 2831 ND2 ASN A 381 15.474 14.482 12.723 1.00 27.45 N
ANISOU 2831 ND2 ASN A 381 3354 3542 3531 -28 39 212 N
ATOM 2832 N ALA A 382 9.998 14.382 10.920 1.00 27.21 N
ANISOU 2832 N ALA A 382 3347 3502 3489 -19 -13 226 N
ATOM 2833 CA ALA A 382 9.178 13.798 9.866 1.00 28.30 C
ANISOU 2833 CA ALA A 382 3494 3633 3624 -21 -23 225 C
ATOM 2834 C ALA A 382 10.115 13.043 8.906 1.00 29.95 C
ANISOU 2834 C ALA A 382 3712 3838 3827 -29 -14 216 C
ATOM 2835 O ALA A 382 9.899 12.998 7.686 1.00 31.39 O
ANISOU 2835 O ALA A 382 3912 4015 3999 -36 -18 212 O
ATOM 2836 CB ALA A 382 8.370 14.867 9.138 1.00 27.06 C
ANISOU 2836 CB ALA A 382 3352 3470 3458 -23 -35 228 C
ATOM 2837 N LEU A 383 11.163 12.460 9.495 1.00 30.82 N
ANISOU 2837 N LEU A 383 3810 3951 3946 -29 -1 212 N
ATOM 2838 CA LEU A 383 12.210 11.733 8.784 1.00 31.08 C
ANISOU 2838 CA LEU A 383 3848 3981 3979 -35 11 202 C
ATOM 2839 C LEU A 383 11.661 10.444 8.212 1.00 30.88 C
ANISOU 2839 C LEU A 383 3822 3951 3960 -36 5 198 C
ATOM 2840 O LEU A 383 10.860 9.767 8.834 1.00 31.82 O
ANISOU 2840 O LEU A 383 3927 4071 4091 -30 -3 204 O
ATOM 2841 CB LEU A 383 13.382 11.447 9.739 1.00 31.32 C
ANISOU 2841 CB LEU A 383 3861 4014 4022 -33 23 200 C
ATOM 2842 CG LEU A 383 14.757 10.828 9.427 1.00 30.47 C
ANISOU 2842 CG LEU A 383 3751 3903 3921 -38 39 190 C
ATOM 2843 CD1 LEU A 383 14.778 9.330 9.692 1.00 30.60 C
ANISOU 2843 CD1 LEU A 383 3751 3917 3957 -36 38 188 C
ATOM 2844 CD2 LEU A 383 15.239 11.155 8.029 1.00 30.62 C
ANISOU 2844 CD2 LEU A 383 3790 3917 3925 -48 49 179 C
ATOM 2845 N SER A 384 12.110 10.132 7.011 1.00 31.14 N
ANISOU 2845 N SER A 384 3869 3977 3983 -45 13 187 N
ATOM 2846 CA SER A 384 11.723 8.950 6.287 1.00 31.69 C
ANISOU 2846 CA SER A 384 3941 4042 4057 -48 9 181 C
ATOM 2847 C SER A 384 12.996 8.111 6.063 1.00 33.74 C
ANISOU 2847 C SER A 384 4194 4298 4326 -53 28 168 C
ATOM 2848 O SER A 384 13.974 8.565 5.470 1.00 33.70 O
ANISOU 2848 O SER A 384 4200 4292 4312 -60 42 159 O
ATOM 2849 CB SER A 384 11.003 9.375 4.997 1.00 31.42 C
ANISOU 2849 CB SER A 384 3931 4003 4002 -56 0 179 C
ATOM 2850 OG SER A 384 11.604 8.890 3.816 1.00 31.76 O
ANISOU 2850 OG SER A 384 3988 4041 4035 -68 11 166 O
ATOM 2851 N PHE A 385 12.984 6.898 6.595 1.00 34.78 N
ANISOU 2851 N PHE A 385 4307 4427 4478 -48 27 168 N
ATOM 2852 CA PHE A 385 14.146 6.040 6.604 1.00 35.52 C
ANISOU 2852 CA PHE A 385 4389 4516 4588 -50 42 157 C
ATOM 2853 C PHE A 385 13.692 4.745 5.958 1.00 35.22 C
ANISOU 2853 C PHE A 385 4351 4472 4559 -52 39 149 C
ATOM 2854 O PHE A 385 12.880 4.021 6.533 1.00 37.17 O
ANISOU 2854 O PHE A 385 4584 4719 4819 -46 25 157 O
ATOM 2855 CB PHE A 385 14.591 5.812 8.063 1.00 36.57 C
ANISOU 2855 CB PHE A 385 4497 4653 4742 -42 41 166 C
ATOM 2856 CG PHE A 385 15.962 5.182 8.223 1.00 38.34 C
ANISOU 2856 CG PHE A 385 4707 4871 4985 -44 56 157 C
ATOM 2857 CD1 PHE A 385 16.851 5.675 9.177 1.00 39.89 C
ANISOU 2857 CD1 PHE A 385 4893 5072 5191 -42 61 163 C
ATOM 2858 CD2 PHE A 385 16.364 4.090 7.454 1.00 40.27 C
ANISOU 2858 CD2 PHE A 385 4950 5108 5243 -49 65 143 C
ATOM 2859 CE1 PHE A 385 18.112 5.099 9.354 1.00 39.92 C
ANISOU 2859 CE1 PHE A 385 4882 5069 5216 -44 74 156 C
ATOM 2860 CE2 PHE A 385 17.625 3.513 7.626 1.00 41.60 C
ANISOU 2860 CE2 PHE A 385 5103 5269 5433 -51 79 134 C
ATOM 2861 CZ PHE A 385 18.497 4.013 8.582 1.00 39.65 C
ANISOU 2861 CZ PHE A 385 4844 5024 5196 -48 82 141 C
ATOM 2862 N SER A 386 14.177 4.454 4.758 1.00 34.65 N
ANISOU 2862 N SER A 386 4292 4394 4479 -62 51 133 N
ATOM 2863 CA SER A 386 13.847 3.173 4.153 1.00 36.74 C
ANISOU 2863 CA SER A 386 4554 4650 4753 -65 49 123 C
ATOM 2864 C SER A 386 15.072 2.278 4.163 1.00 37.58 C
ANISOU 2864 C SER A 386 4646 4750 4883 -67 67 109 C
ATOM 2865 O SER A 386 16.109 2.637 3.618 1.00 39.74 O
ANISOU 2865 O SER A 386 4927 5021 5150 -75 86 96 O
ATOM 2866 CB SER A 386 13.277 3.332 2.743 1.00 37.73 C
ANISOU 2866 CB SER A 386 4707 4773 4853 -76 47 115 C
ATOM 2867 OG SER A 386 14.254 3.096 1.755 1.00 37.90 O
ANISOU 2867 OG SER A 386 4739 4790 4870 -88 68 95 O
ATOM 2868 N GLY A 387 14.943 1.123 4.804 1.00 37.76 N
ANISOU 2868 N GLY A 387 4646 4767 4931 -60 61 112 N
ATOM 2869 CA GLY A 387 16.047 0.199 4.975 1.00 39.45 C
ANISOU 2869 CA GLY A 387 4841 4973 5174 -61 75 100 C
ATOM 2870 C GLY A 387 16.704 0.291 6.335 1.00 41.11 C
ANISOU 2870 C GLY A 387 5028 5185 5405 -53 73 113 C
ATOM 2871 O GLY A 387 17.921 0.367 6.421 1.00 47.13 O
ANISOU 2871 O GLY A 387 5783 5944 6180 -56 89 105 O
ATOM 2872 N CYS A 388 15.911 0.298 7.400 1.00 41.44 N
ANISOU 2872 N CYS A 388 5060 5234 5451 -45 55 132 N
ATOM 2873 CA CYS A 388 16.460 0.193 8.746 1.00 42.56 C
ANISOU 2873 CA CYS A 388 5179 5378 5614 -39 51 145 C
ATOM 2874 C CYS A 388 16.692 -1.266 9.082 1.00 41.84 C
ANISOU 2874 C CYS A 388 5065 5277 5556 -37 48 143 C
ATOM 2875 O CYS A 388 15.823 -2.100 8.851 1.00 40.68 O
ANISOU 2875 O CYS A 388 4916 5126 5414 -36 38 144 O
ATOM 2876 CB CYS A 388 15.510 0.772 9.786 1.00 46.46 C
ANISOU 2876 CB CYS A 388 5670 5883 6097 -33 34 165 C
ATOM 2877 SG CYS A 388 16.232 1.465 11.302 1.00 53.15 S
ANISOU 2877 SG CYS A 388 6504 6738 6952 -30 33 180 S
ATOM 2878 N CYS A 389 17.878 -1.599 9.577 1.00 43.26 N
ANISOU 2878 N CYS A 389 5226 5449 5760 -38 55 141 N
ATOM 2879 CA CYS A 389 19.086 -0.770 9.488 1.00 44.14 C
ANISOU 2879 CA CYS A 389 5341 5560 5869 -41 71 134 C
ATOM 2880 C CYS A 389 20.234 -1.605 9.982 1.00 42.24 C
ANISOU 2880 C CYS A 389 5074 5307 5666 -41 76 131 C
ATOM 2881 O CYS A 389 20.038 -2.548 10.748 1.00 41.53 O
ANISOU 2881 O CYS A 389 4965 5213 5600 -38 62 142 O
ATOM 2882 CB CYS A 389 19.005 0.549 10.265 1.00 48.25 C
ANISOU 2882 CB CYS A 389 5868 6094 6369 -39 66 149 C
ATOM 2883 SG CYS A 389 17.992 0.468 11.745 1.00 57.15 S
ANISOU 2883 SG CYS A 389 6984 7231 7498 -32 43 174 S
ATOM 2884 N SER A 390 21.428 -1.258 9.519 1.00 39.24 N
ANISOU 2884 N SER A 390 4695 4921 5292 -46 95 117 N
ATOM 2885 CA SER A 390 22.614 -2.028 9.787 1.00 36.40 C
ANISOU 2885 CA SER A 390 4311 4547 4970 -47 102 111 C
ATOM 2886 C SER A 390 23.822 -1.111 9.825 1.00 36.97 C
ANISOU 2886 C SER A 390 4385 4619 5043 -51 117 106 C
ATOM 2887 O SER A 390 23.718 0.104 9.599 1.00 35.39 O
ANISOU 2887 O SER A 390 4204 4429 4811 -52 122 107 O
ATOM 2888 CB SER A 390 22.797 -3.086 8.701 1.00 35.15 C
ANISOU 2888 CB SER A 390 4150 4375 4830 -51 115 88 C
ATOM 2889 OG SER A 390 22.947 -2.476 7.436 1.00 34.75 O
ANISOU 2889 OG SER A 390 4123 4325 4754 -58 135 68 O
ATOM 2890 N TYR A 391 24.973 -1.717 10.114 1.00 36.64 N
ANISOU 2890 N TYR A 391 4319 4562 5038 -52 123 100 N
ATOM 2891 CA TYR A 391 26.250 -1.034 10.110 1.00 34.27 C
ANISOU 2891 CA TYR A 391 4015 4259 4746 -55 139 94 C
ATOM 2892 C TYR A 391 26.424 -0.148 8.876 1.00 33.93 C
ANISOU 2892 C TYR A 391 3998 4220 4673 -62 162 75 C
ATOM 2893 O TYR A 391 26.871 0.986 8.999 1.00 34.40 O
ANISOU 2893 O TYR A 391 4067 4286 4715 -64 168 78 O
ATOM 2894 CB TYR A 391 27.381 -2.062 10.218 1.00 34.40 C
ANISOU 2894 CB TYR A 391 4003 4255 4811 -56 145 84 C
ATOM 2895 CG TYR A 391 28.702 -1.580 9.687 1.00 33.94 C
ANISOU 2895 CG TYR A 391 3943 4188 4764 -62 169 67 C
ATOM 2896 CD1 TYR A 391 29.557 -0.819 10.484 1.00 33.68 C
ANISOU 2896 CD1 TYR A 391 3902 4157 4738 -61 167 78 C
ATOM 2897 CD2 TYR A 391 29.095 -1.872 8.387 1.00 33.93 C
ANISOU 2897 CD2 TYR A 391 3948 4177 4765 -68 195 39 C
ATOM 2898 CE1 TYR A 391 30.767 -0.361 10.003 1.00 33.78 C
ANISOU 2898 CE1 TYR A 391 3912 4161 4762 -67 190 62 C
ATOM 2899 CE2 TYR A 391 30.306 -1.410 7.893 1.00 35.99 C
ANISOU 2899 CE2 TYR A 391 4207 4431 5036 -74 219 22 C
ATOM 2900 CZ TYR A 391 31.136 -0.655 8.711 1.00 35.14 C
ANISOU 2900 CZ TYR A 391 4090 4324 4937 -73 216 34 C
ATOM 2901 OH TYR A 391 32.345 -0.201 8.241 1.00 36.99 O
ANISOU 2901 OH TYR A 391 4320 4550 5183 -79 240 18 O
ATOM 2902 N SER A 392 26.049 -0.647 7.701 1.00 34.09 N
ANISOU 2902 N SER A 392 4031 4236 4686 -66 173 56 N
ATOM 2903 CA SER A 392 26.313 0.076 6.447 1.00 34.92 C
ANISOU 2903 CA SER A 392 4160 4344 4764 -76 196 37 C
ATOM 2904 C SER A 392 25.494 1.364 6.265 1.00 34.85 C
ANISOU 2904 C SER A 392 4179 4351 4708 -77 190 48 C
ATOM 2905 O SER A 392 25.807 2.192 5.409 1.00 34.98 O
ANISOU 2905 O SER A 392 4216 4371 4701 -85 207 37 O
ATOM 2906 CB SER A 392 26.170 -0.843 5.225 1.00 35.79 C
ANISOU 2906 CB SER A 392 4275 4444 4878 -82 211 13 C
ATOM 2907 OG SER A 392 24.820 -1.203 5.004 1.00 36.95 O
ANISOU 2907 OG SER A 392 4435 4598 5006 -80 195 19 O
ATOM 2908 N ASP A 393 24.452 1.536 7.067 1.00 34.29 N
ANISOU 2908 N ASP A 393 4110 4291 4626 -69 166 69 N
ATOM 2909 CA ASP A 393 23.770 2.814 7.101 1.00 33.63 C
ANISOU 2909 CA ASP A 393 4048 4222 4505 -69 159 81 C
ATOM 2910 C ASP A 393 24.599 3.889 7.828 1.00 32.36 C
ANISOU 2910 C ASP A 393 3885 4066 4344 -68 162 89 C
ATOM 2911 O ASP A 393 24.484 5.077 7.519 1.00 32.44 O
ANISOU 2911 O ASP A 393 3914 4084 4325 -71 165 91 O
ATOM 2912 CB ASP A 393 22.373 2.653 7.707 1.00 35.36 C
ANISOU 2912 CB ASP A 393 4269 4450 4714 -61 135 99 C
ATOM 2913 CG ASP A 393 21.471 1.738 6.864 1.00 37.69 C
ANISOU 2913 CG ASP A 393 4572 4741 5006 -63 132 90 C
ATOM 2914 OD1 ASP A 393 21.364 1.963 5.640 1.00 38.75 O
ANISOU 2914 OD1 ASP A 393 4727 4875 5120 -72 143 75 O
ATOM 2915 OD2 ASP A 393 20.859 0.794 7.415 1.00 38.22 O
ANISOU 2915 OD2 ASP A 393 4625 4807 5090 -57 117 98 O
ATOM 2916 N LEU A 394 25.466 3.466 8.751 1.00 31.30 N
ANISOU 2916 N LEU A 394 3725 3925 4242 -64 160 94 N
ATOM 2917 CA LEU A 394 26.132 4.389 9.687 1.00 30.43 C
ANISOU 2917 CA LEU A 394 3609 3820 4133 -62 157 107 C
ATOM 2918 C LEU A 394 27.664 4.374 9.692 1.00 30.90 C
ANISOU 2918 C LEU A 394 3653 3868 4220 -66 174 97 C
ATOM 2919 O LEU A 394 28.303 5.379 10.041 1.00 30.25 O
ANISOU 2919 O LEU A 394 3573 3788 4130 -67 177 101 O
ATOM 2920 CB LEU A 394 25.622 4.143 11.106 1.00 29.85 C
ANISOU 2920 CB LEU A 394 3520 3752 4069 -55 133 129 C
ATOM 2921 CG LEU A 394 24.114 4.287 11.305 1.00 29.01 C
ANISOU 2921 CG LEU A 394 3426 3657 3937 -51 116 141 C
ATOM 2922 CD1 LEU A 394 23.758 4.062 12.763 1.00 28.63 C
ANISOU 2922 CD1 LEU A 394 3363 3615 3900 -45 96 162 C
ATOM 2923 CD2 LEU A 394 23.649 5.652 10.827 1.00 28.22 C
ANISOU 2923 CD2 LEU A 394 3352 3568 3801 -52 120 141 C
ATOM 2924 N GLY A 395 28.242 3.233 9.315 1.00 31.12 N
ANISOU 2924 N GLY A 395 3664 3880 4278 -68 183 83 N
ATOM 2925 CA GLY A 395 29.686 3.049 9.307 1.00 30.25 C
ANISOU 2925 CA GLY A 395 3536 3756 4201 -72 199 72 C
ATOM 2926 C GLY A 395 30.271 2.879 10.693 1.00 30.74 C
ANISOU 2926 C GLY A 395 3572 3814 4292 -67 182 89 C
ATOM 2927 O GLY A 395 31.479 3.025 10.881 1.00 31.87 O
ANISOU 2927 O GLY A 395 3701 3947 4459 -69 192 85 O
ATOM 2928 N THR A 396 29.417 2.550 11.659 1.00 31.06 N
ANISOU 2928 N THR A 396 3607 3861 4331 -61 157 110 N
ATOM 2929 CA THR A 396 29.813 2.453 13.059 1.00 31.63 C
ANISOU 2929 CA THR A 396 3660 3933 4425 -58 138 130 C
ATOM 2930 C THR A 396 29.458 1.105 13.648 1.00 32.93 C
ANISOU 2930 C THR A 396 3804 4090 4618 -55 120 139 C
ATOM 2931 O THR A 396 28.488 0.472 13.238 1.00 34.63 O
ANISOU 2931 O THR A 396 4025 4307 4825 -53 117 136 O
ATOM 2932 CB THR A 396 29.171 3.548 13.949 1.00 30.82 C
ANISOU 2932 CB THR A 396 3570 3848 4289 -56 123 150 C
ATOM 2933 OG1 THR A 396 29.603 3.373 15.307 1.00 29.53 O
ANISOU 2933 OG1 THR A 396 3388 3684 4147 -55 104 169 O
ATOM 2934 CG2 THR A 396 27.635 3.483 13.912 1.00 30.53 C
ANISOU 2934 CG2 THR A 396 3549 3824 4224 -52 111 157 C
ATOM 2935 N ASN A 397 30.248 0.699 14.636 1.00 33.66 N
ANISOU 2935 N ASN A 397 3871 4172 4743 -55 108 151 N
ATOM 2936 CA ASN A 397 30.037 -0.534 15.378 1.00 32.49 C
ANISOU 2936 CA ASN A 397 3702 4016 4626 -53 88 163 C
ATOM 2937 C ASN A 397 29.782 -0.297 16.852 1.00 30.77 C
ANISOU 2937 C ASN A 397 3478 3807 4403 -54 62 191 C
ATOM 2938 O ASN A 397 29.596 -1.249 17.602 1.00 30.53 O
ANISOU 2938 O ASN A 397 3431 3772 4395 -54 42 205 O
ATOM 2939 CB ASN A 397 31.275 -1.420 15.257 1.00 33.22 C
ANISOU 2939 CB ASN A 397 3766 4084 4769 -56 94 153 C
ATOM 2940 CG ASN A 397 31.169 -2.408 14.135 1.00 33.67 C
ANISOU 2940 CG ASN A 397 3818 4128 4844 -55 109 131 C
ATOM 2941 OD1 ASN A 397 32.175 -2.767 13.525 1.00 35.25 O
ANISOU 2941 OD1 ASN A 397 4006 4312 5076 -58 127 112 O
ATOM 2942 ND2 ASN A 397 29.949 -2.862 13.851 1.00 33.16 N
ANISOU 2942 ND2 ASN A 397 3766 4072 4761 -52 102 132 N
ATOM 2943 N SER A 398 29.814 0.960 17.273 1.00 29.74 N
ANISOU 2943 N SER A 398 3363 3691 4244 -55 62 199 N
ATOM 2944 CA SER A 398 29.747 1.264 18.692 1.00 30.14 C
ANISOU 2944 CA SER A 398 3409 3751 4290 -57 40 223 C
ATOM 2945 C SER A 398 28.511 2.034 19.071 1.00 29.99 C
ANISOU 2945 C SER A 398 3412 3754 4228 -55 33 233 C
ATOM 2946 O SER A 398 28.490 2.666 20.121 1.00 30.41 O
ANISOU 2946 O SER A 398 3467 3817 4269 -58 20 249 O
ATOM 2947 CB SER A 398 31.007 1.994 19.195 1.00 30.16 C
ANISOU 2947 CB SER A 398 3405 3749 4305 -61 41 226 C
ATOM 2948 OG SER A 398 31.937 2.266 18.172 1.00 30.48 O
ANISOU 2948 OG SER A 398 3444 3778 4357 -61 65 205 O
ATOM 2949 N LEU A 399 27.485 1.967 18.225 1.00 29.80 N
ANISOU 2949 N LEU A 399 3403 3736 4183 -51 40 224 N
ATOM 2950 CA LEU A 399 26.245 2.691 18.459 1.00 29.72 C
ANISOU 2950 CA LEU A 399 3413 3745 4135 -49 35 231 C
ATOM 2951 C LEU A 399 25.566 2.202 19.734 1.00 29.46 C
ANISOU 2951 C LEU A 399 3371 3719 4102 -51 12 253 C
ATOM 2952 O LEU A 399 25.270 1.021 19.867 1.00 29.55 O
ANISOU 2952 O LEU A 399 3369 3723 4134 -51 2 258 O
ATOM 2953 CB LEU A 399 25.300 2.573 17.249 1.00 29.30 C
ANISOU 2953 CB LEU A 399 3374 3693 4062 -45 46 217 C
ATOM 2954 CG LEU A 399 24.152 3.605 17.246 1.00 29.51 C
ANISOU 2954 CG LEU A 399 3424 3737 4049 -43 44 221 C
ATOM 2955 CD1 LEU A 399 24.667 5.007 16.949 1.00 28.60 C
ANISOU 2955 CD1 LEU A 399 3324 3628 3914 -44 57 214 C
ATOM 2956 CD2 LEU A 399 23.011 3.235 16.303 1.00 28.93 C
ANISOU 2956 CD2 LEU A 399 3363 3665 3962 -40 47 213 C
ATOM 2957 N ARG A 400 25.336 3.112 20.672 1.00 29.76 N
ANISOU 2957 N ARG A 400 3417 3771 4118 -53 5 266 N
ATOM 2958 CA ARG A 400 24.680 2.755 21.930 1.00 31.28 C
ANISOU 2958 CA ARG A 400 3603 3972 4307 -57 -15 287 C
ATOM 2959 C ARG A 400 23.261 3.280 22.082 1.00 29.79 C
ANISOU 2959 C ARG A 400 3431 3801 4085 -55 -16 290 C
ATOM 2960 O ARG A 400 22.479 2.737 22.861 1.00 29.48 O
ANISOU 2960 O ARG A 400 3387 3768 4043 -57 -30 304 O
ATOM 2961 CB ARG A 400 25.524 3.190 23.119 1.00 33.98 C
ANISOU 2961 CB ARG A 400 3938 4317 4653 -64 -25 301 C
ATOM 2962 CG ARG A 400 26.360 2.051 23.650 1.00 38.88 C
ANISOU 2962 CG ARG A 400 4535 4922 5313 -70 -39 311 C
ATOM 2963 CD ARG A 400 27.718 2.541 24.087 1.00 43.51 C
ANISOU 2963 CD ARG A 400 5114 5502 5914 -75 -41 314 C
ATOM 2964 NE ARG A 400 28.769 1.734 23.471 1.00 50.67 N
ANISOU 2964 NE ARG A 400 6002 6388 6863 -73 -36 305 N
ATOM 2965 CZ ARG A 400 29.236 0.585 23.962 1.00 56.14 C
ANISOU 2965 CZ ARG A 400 6672 7065 7591 -77 -52 316 C
ATOM 2966 NH1 ARG A 400 28.744 0.083 25.099 1.00 56.88 N
ANISOU 2966 NH1 ARG A 400 6761 7166 7684 -84 -75 338 N
ATOM 2967 NH2 ARG A 400 30.206 -0.062 23.315 1.00 55.80 N
ANISOU 2967 NH2 ARG A 400 6611 7001 7587 -76 -46 304 N
ATOM 2968 N HIS A 401 22.936 4.316 21.310 1.00 28.34 N
ANISOU 2968 N HIS A 401 3266 3623 3876 -50 -2 278 N
ATOM 2969 CA HIS A 401 21.691 5.055 21.454 1.00 26.92 C
ANISOU 2969 CA HIS A 401 3102 3459 3666 -48 -3 280 C
ATOM 2970 C HIS A 401 21.193 5.460 20.094 1.00 26.02 C
ANISOU 2970 C HIS A 401 3004 3343 3538 -42 10 264 C
ATOM 2971 O HIS A 401 21.874 6.176 19.357 1.00 25.75 O
ANISOU 2971 O HIS A 401 2979 3306 3500 -41 23 252 O
ATOM 2972 CB HIS A 401 21.957 6.265 22.330 1.00 25.87 C
ANISOU 2972 CB HIS A 401 2975 3336 3515 -52 -3 286 C
ATOM 2973 CG HIS A 401 20.741 7.101 22.636 1.00 25.81 C
ANISOU 2973 CG HIS A 401 2983 3345 3479 -50 -4 288 C
ATOM 2974 ND1 HIS A 401 20.179 7.132 23.858 1.00 26.26 N
ANISOU 2974 ND1 HIS A 401 3037 3413 3528 -55 -14 302 N
ATOM 2975 CD2 HIS A 401 20.027 8.010 21.852 1.00 25.71 C
ANISOU 2975 CD2 HIS A 401 2986 3336 3445 -44 5 278 C
ATOM 2976 CE1 HIS A 401 19.141 7.990 23.855 1.00 25.93 C
ANISOU 2976 CE1 HIS A 401 3007 3381 3462 -52 -10 299 C
ATOM 2977 NE2 HIS A 401 19.049 8.529 22.626 1.00 25.79 N
ANISOU 2977 NE2 HIS A 401 3001 3359 3438 -45 0 285 N
ATOM 2978 N LEU A 402 20.001 4.988 19.746 1.00 25.12 N
ANISOU 2978 N LEU A 402 2894 3232 3418 -38 6 263 N
ATOM 2979 CA LEU A 402 19.358 5.353 18.496 1.00 25.08 C
ANISOU 2979 CA LEU A 402 2905 3226 3397 -34 15 250 C
ATOM 2980 C LEU A 402 17.949 5.885 18.758 1.00 26.26 C
ANISOU 2980 C LEU A 402 3064 3387 3524 -31 9 256 C
ATOM 2981 O LEU A 402 17.045 5.152 19.197 1.00 26.27 O
ANISOU 2981 O LEU A 402 3059 3392 3530 -30 -1 264 O
ATOM 2982 CB LEU A 402 19.327 4.173 17.530 1.00 24.76 C
ANISOU 2982 CB LEU A 402 2860 3174 3373 -32 17 241 C
ATOM 2983 CG LEU A 402 18.824 4.346 16.090 1.00 25.03 C
ANISOU 2983 CG LEU A 402 2910 3204 3394 -30 27 226 C
ATOM 2984 CD1 LEU A 402 19.515 5.476 15.335 1.00 24.93 C
ANISOU 2984 CD1 LEU A 402 2913 3191 3367 -32 42 215 C
ATOM 2985 CD2 LEU A 402 18.981 3.045 15.323 1.00 24.74 C
ANISOU 2985 CD2 LEU A 402 2865 3154 3378 -31 29 217 C
ATOM 2986 N ASP A 403 17.774 7.180 18.508 1.00 26.80 N
ANISOU 2986 N ASP A 403 3148 3461 3571 -30 15 251 N
ATOM 2987 CA ASP A 403 16.458 7.785 18.570 1.00 26.28 C
ANISOU 2987 CA ASP A 403 3092 3404 3487 -27 11 254 C
ATOM 2988 C ASP A 403 15.928 8.138 17.173 1.00 26.63 C
ANISOU 2988 C ASP A 403 3153 3445 3520 -23 16 243 C
ATOM 2989 O ASP A 403 16.420 9.073 16.513 1.00 26.41 O
ANISOU 2989 O ASP A 403 3137 3414 3480 -24 25 235 O
ATOM 2990 CB ASP A 403 16.465 9.008 19.472 1.00 25.93 C
ANISOU 2990 CB ASP A 403 3052 3370 3428 -28 11 259 C
ATOM 2991 CG ASP A 403 15.075 9.519 19.756 1.00 26.30 C
ANISOU 2991 CG ASP A 403 3105 3426 3462 -25 7 262 C
ATOM 2992 OD1 ASP A 403 14.947 10.499 20.520 1.00 27.69 O
ANISOU 2992 OD1 ASP A 403 3283 3610 3626 -26 8 265 O
ATOM 2993 OD2 ASP A 403 14.102 8.943 19.232 1.00 26.00 O
ANISOU 2993 OD2 ASP A 403 3068 3386 3425 -22 2 262 O
ATOM 2994 N LEU A 404 14.916 7.382 16.747 1.00 25.92 N
ANISOU 2994 N LEU A 404 3062 3351 3432 -21 9 243 N
ATOM 2995 CA LEU A 404 14.205 7.645 15.502 1.00 26.29 C
ANISOU 2995 CA LEU A 404 3125 3394 3467 -19 10 235 C
ATOM 2996 C LEU A 404 12.723 7.982 15.757 1.00 25.60 C
ANISOU 2996 C LEU A 404 3041 3314 3371 -15 0 241 C
ATOM 2997 O LEU A 404 11.864 7.771 14.899 1.00 26.50 O
ANISOU 2997 O LEU A 404 3163 3423 3481 -14 -3 238 O
ATOM 2998 CB LEU A 404 14.332 6.436 14.555 1.00 26.51 C
ANISOU 2998 CB LEU A 404 3152 3413 3507 -20 12 227 C
ATOM 2999 CG LEU A 404 15.682 6.164 13.890 1.00 26.64 C
ANISOU 2999 CG LEU A 404 3168 3420 3532 -24 24 215 C
ATOM 3000 CD1 LEU A 404 15.792 4.749 13.337 1.00 25.60 C
ANISOU 3000 CD1 LEU A 404 3028 3279 3419 -25 24 209 C
ATOM 3001 CD2 LEU A 404 15.905 7.171 12.776 1.00 27.46 C
ANISOU 3001 CD2 LEU A 404 3293 3523 3617 -27 34 205 C
ATOM 3002 N SER A 405 12.420 8.507 16.933 1.00 24.64 N
ANISOU 3002 N SER A 405 2914 3201 3247 -15 -2 250 N
ATOM 3003 CA SER A 405 11.034 8.790 17.288 1.00 24.32 C
ANISOU 3003 CA SER A 405 2873 3166 3201 -11 -10 255 C
ATOM 3004 C SER A 405 10.461 10.016 16.561 1.00 24.71 C
ANISOU 3004 C SER A 405 2938 3214 3236 -9 -9 250 C
ATOM 3005 O SER A 405 11.205 10.833 15.980 1.00 24.73 O
ANISOU 3005 O SER A 405 2952 3214 3230 -10 -2 243 O
ATOM 3006 CB SER A 405 10.882 8.932 18.813 1.00 24.00 C
ANISOU 3006 CB SER A 405 2820 3136 3162 -13 -11 264 C
ATOM 3007 OG SER A 405 11.610 10.035 19.317 1.00 22.67 O
ANISOU 3007 OG SER A 405 2656 2972 2984 -15 -4 263 O
ATOM 3008 N PHE A 406 9.129 10.119 16.584 1.00 24.62 N
ANISOU 3008 N PHE A 406 2926 3203 3223 -5 -17 253 N
ATOM 3009 CA PHE A 406 8.382 11.250 16.005 1.00 24.10 C
ANISOU 3009 CA PHE A 406 2872 3134 3148 -3 -20 250 C
ATOM 3010 C PHE A 406 8.746 11.566 14.550 1.00 24.24 C
ANISOU 3010 C PHE A 406 2909 3144 3157 -5 -19 242 C
ATOM 3011 O PHE A 406 8.879 12.729 14.198 1.00 25.04 O
ANISOU 3011 O PHE A 406 3020 3244 3248 -6 -18 240 O
ATOM 3012 CB PHE A 406 8.525 12.503 16.878 1.00 22.97 C
ANISOU 3012 CB PHE A 406 2729 2998 2999 -3 -15 251 C
ATOM 3013 CG PHE A 406 7.975 12.346 18.266 1.00 22.83 C
ANISOU 3013 CG PHE A 406 2696 2990 2986 -2 -15 257 C
ATOM 3014 CD1 PHE A 406 8.802 11.978 19.320 1.00 22.84 C
ANISOU 3014 CD1 PHE A 406 2688 2999 2990 -7 -10 261 C
ATOM 3015 CD2 PHE A 406 6.616 12.568 18.529 1.00 22.72 C
ANISOU 3015 CD2 PHE A 406 2678 2977 2977 0 -21 259 C
ATOM 3016 CE1 PHE A 406 8.294 11.835 20.609 1.00 22.42 C
ANISOU 3016 CE1 PHE A 406 2623 2955 2938 -9 -10 267 C
ATOM 3017 CE2 PHE A 406 6.102 12.424 19.820 1.00 22.19 C
ANISOU 3017 CE2 PHE A 406 2598 2919 2913 0 -19 263 C
ATOM 3018 CZ PHE A 406 6.940 12.057 20.859 1.00 22.04 C
ANISOU 3018 CZ PHE A 406 2571 2908 2892 -6 -14 267 C
ATOM 3019 N ASN A 407 8.905 10.530 13.726 1.00 24.31 N
ANISOU 3019 N ASN A 407 2920 3147 3170 -7 -21 239 N
ATOM 3020 CA ASN A 407 9.247 10.663 12.305 1.00 24.58 C
ANISOU 3020 CA ASN A 407 2971 3172 3193 -11 -19 231 C
ATOM 3021 C ASN A 407 8.184 10.030 11.400 1.00 24.56 C
ANISOU 3021 C ASN A 407 2975 3163 3192 -11 -31 231 C
ATOM 3022 O ASN A 407 7.123 9.615 11.869 1.00 24.44 O
ANISOU 3022 O ASN A 407 2950 3149 3186 -7 -41 237 O
ATOM 3023 CB ASN A 407 10.600 9.988 12.017 1.00 24.71 C
ANISOU 3023 CB ASN A 407 2987 3187 3214 -16 -7 224 C
ATOM 3024 CG ASN A 407 11.768 10.706 12.660 1.00 25.52 C
ANISOU 3024 CG ASN A 407 3087 3294 3315 -17 3 223 C
ATOM 3025 OD1 ASN A 407 12.569 10.102 13.367 1.00 25.31 O
ANISOU 3025 OD1 ASN A 407 3046 3269 3299 -18 8 224 O
ATOM 3026 ND2 ASN A 407 11.879 11.999 12.410 1.00 26.10 N
ANISOU 3026 ND2 ASN A 407 3172 3368 3374 -18 5 222 N
ATOM 3027 N GLY A 408 8.501 9.926 10.111 1.00 24.34 N
ANISOU 3027 N GLY A 408 2964 3129 3155 -17 -29 223 N
ATOM 3028 CA GLY A 408 7.616 9.337 9.124 1.00 25.18 C
ANISOU 3028 CA GLY A 408 3078 3228 3259 -19 -40 222 C
ATOM 3029 C GLY A 408 7.804 7.851 8.892 1.00 26.28 C
ANISOU 3029 C GLY A 408 3211 3364 3409 -20 -39 217 C
ATOM 3030 O GLY A 408 7.821 7.066 9.829 1.00 27.52 O
ANISOU 3030 O GLY A 408 3349 3524 3582 -16 -38 221 O
ATOM 3031 N ALA A 409 7.919 7.455 7.631 1.00 27.62 N
ANISOU 3031 N ALA A 409 3396 3526 3570 -28 -38 208 N
ATOM 3032 CA ALA A 409 7.984 6.040 7.281 1.00 28.14 C
ANISOU 3032 CA ALA A 409 3455 3587 3647 -29 -37 202 C
ATOM 3033 C ALA A 409 9.364 5.461 7.578 1.00 29.57 C
ANISOU 3033 C ALA A 409 3626 3768 3838 -31 -20 194 C
ATOM 3034 O ALA A 409 10.380 5.902 7.015 1.00 30.08 O
ANISOU 3034 O ALA A 409 3701 3832 3893 -37 -7 184 O
ATOM 3035 CB ALA A 409 7.626 5.839 5.818 1.00 27.52 C
ANISOU 3035 CB ALA A 409 3398 3501 3555 -38 -42 193 C
ATOM 3036 N ILE A 410 9.393 4.486 8.481 1.00 29.52 N
ANISOU 3036 N ILE A 410 3599 3764 3853 -26 -22 198 N
ATOM 3037 CA ILE A 410 10.599 3.718 8.753 1.00 28.85 C
ANISOU 3037 CA ILE A 410 3502 3676 3783 -27 -9 191 C
ATOM 3038 C ILE A 410 10.366 2.267 8.308 1.00 30.13 C
ANISOU 3038 C ILE A 410 3657 3831 3960 -28 -12 185 C
ATOM 3039 O ILE A 410 9.636 1.496 8.949 1.00 28.66 O
ANISOU 3039 O ILE A 410 3456 3645 3788 -23 -24 194 O
ATOM 3040 CB ILE A 410 11.036 3.846 10.229 1.00 28.27 C
ANISOU 3040 CB ILE A 410 3409 3610 3722 -22 -8 202 C
ATOM 3041 CG1 ILE A 410 11.303 5.324 10.556 1.00 28.00 C
ANISOU 3041 CG1 ILE A 410 3383 3582 3671 -22 -4 206 C
ATOM 3042 CG2 ILE A 410 12.281 3.010 10.508 1.00 27.57 C
ANISOU 3042 CG2 ILE A 410 3305 3515 3652 -24 1 196 C
ATOM 3043 CD1 ILE A 410 11.628 5.612 12.004 1.00 27.74 C
ANISOU 3043 CD1 ILE A 410 3334 3557 3647 -18 -4 216 C
ATOM 3044 N ILE A 411 10.983 1.922 7.182 1.00 31.87 N
ANISOU 3044 N ILE A 411 3888 4043 4176 -35 -2 169 N
ATOM 3045 CA ILE A 411 10.813 0.618 6.555 1.00 33.14 C
ANISOU 3045 CA ILE A 411 4045 4195 4349 -38 -3 160 C
ATOM 3046 C ILE A 411 11.892 -0.333 7.068 1.00 33.78 C
ANISOU 3046 C ILE A 411 4106 4271 4457 -36 6 155 C
ATOM 3047 O ILE A 411 13.043 -0.248 6.662 1.00 33.15 O
ANISOU 3047 O ILE A 411 4028 4187 4379 -42 23 142 O
ATOM 3048 CB ILE A 411 10.835 0.748 5.008 1.00 34.19 C
ANISOU 3048 CB ILE A 411 4203 4323 4463 -48 2 144 C
ATOM 3049 CG1 ILE A 411 9.705 1.672 4.541 1.00 35.05 C
ANISOU 3049 CG1 ILE A 411 4333 4436 4549 -49 -11 152 C
ATOM 3050 CG2 ILE A 411 10.700 -0.605 4.320 1.00 33.33 C
ANISOU 3050 CG2 ILE A 411 4092 4205 4367 -51 3 132 C
ATOM 3051 CD1 ILE A 411 9.756 2.022 3.065 1.00 36.40 C
ANISOU 3051 CD1 ILE A 411 4531 4602 4695 -62 -6 140 C
ATOM 3052 N MET A 412 11.509 -1.220 7.983 1.00 35.73 N
ANISOU 3052 N MET A 412 4331 4517 4726 -30 -3 165 N
ATOM 3053 CA MET A 412 12.422 -2.224 8.538 1.00 36.39 C
ANISOU 3053 CA MET A 412 4392 4593 4838 -29 1 163 C
ATOM 3054 C MET A 412 12.791 -3.232 7.469 1.00 38.12 C
ANISOU 3054 C MET A 412 4613 4800 5069 -34 10 144 C
ATOM 3055 O MET A 412 11.912 -3.834 6.851 1.00 40.50 O
ANISOU 3055 O MET A 412 4921 5098 5368 -35 2 140 O
ATOM 3056 CB MET A 412 11.772 -2.955 9.710 1.00 36.87 C
ANISOU 3056 CB MET A 412 4432 4656 4918 -23 -14 180 C
ATOM 3057 CG MET A 412 11.460 -2.070 10.903 1.00 37.54 C
ANISOU 3057 CG MET A 412 4514 4754 4995 -19 -21 198 C
ATOM 3058 SD MET A 412 12.886 -1.084 11.408 1.00 38.33 S
ANISOU 3058 SD MET A 412 4613 4859 5092 -21 -7 197 S
ATOM 3059 CE MET A 412 14.065 -2.380 11.794 1.00 38.54 C
ANISOU 3059 CE MET A 412 4615 4873 5154 -22 -3 194 C
ATOM 3060 N SER A 413 14.089 -3.423 7.264 1.00 38.76 N
ANISOU 3060 N SER A 413 4687 4874 5162 -38 27 131 N
ATOM 3061 CA SER A 413 14.592 -4.199 6.137 1.00 38.09 C
ANISOU 3061 CA SER A 413 4607 4778 5086 -45 40 108 C
ATOM 3062 C SER A 413 15.843 -5.033 6.492 1.00 37.71 C
ANISOU 3062 C SER A 413 4536 4719 5074 -45 51 100 C
ATOM 3063 O SER A 413 16.233 -5.953 5.758 1.00 37.17 O
ANISOU 3063 O SER A 413 4463 4638 5022 -49 61 81 O
ATOM 3064 CB SER A 413 14.848 -3.241 4.968 1.00 39.64 C
ANISOU 3064 CB SER A 413 4831 4977 5252 -54 55 94 C
ATOM 3065 OG SER A 413 16.128 -3.411 4.381 1.00 44.50 O
ANISOU 3065 OG SER A 413 5446 5584 5877 -61 77 74 O
ATOM 3066 N ALA A 414 16.454 -4.695 7.624 1.00 36.07 N
ANISOU 3066 N ALA A 414 4312 4514 4879 -41 49 113 N
ATOM 3067 CA ALA A 414 17.665 -5.337 8.113 1.00 34.30 C
ANISOU 3067 CA ALA A 414 4064 4279 4689 -40 56 109 C
ATOM 3068 C ALA A 414 17.611 -5.300 9.635 1.00 33.45 C
ANISOU 3068 C ALA A 414 3938 4177 4594 -34 40 134 C
ATOM 3069 O ALA A 414 17.342 -4.258 10.216 1.00 34.53 O
ANISOU 3069 O ALA A 414 4083 4327 4709 -32 35 147 O
ATOM 3070 CB ALA A 414 18.891 -4.596 7.600 1.00 32.24 C
ANISOU 3070 CB ALA A 414 3809 4015 4423 -46 79 94 C
ATOM 3071 N ASN A 415 17.869 -6.427 10.283 1.00 33.35 N
ANISOU 3071 N ASN A 415 3899 4154 4616 -32 31 140 N
ATOM 3072 CA ASN A 415 17.755 -6.502 11.743 1.00 33.67 C
ANISOU 3072 CA ASN A 415 3923 4200 4668 -28 13 165 C
ATOM 3073 C ASN A 415 18.986 -6.128 12.571 1.00 33.60 C
ANISOU 3073 C ASN A 415 3900 4189 4674 -30 16 171 C
ATOM 3074 O ASN A 415 19.390 -6.867 13.460 1.00 32.54 O
ANISOU 3074 O ASN A 415 3744 4049 4570 -30 5 183 O
ATOM 3075 CB ASN A 415 17.213 -7.863 12.188 1.00 34.38 C
ANISOU 3075 CB ASN A 415 3994 4282 4785 -26 -3 173 C
ATOM 3076 CG ASN A 415 17.859 -9.028 11.476 1.00 34.51 C
ANISOU 3076 CG ASN A 415 3997 4280 4836 -28 4 155 C
ATOM 3077 OD1 ASN A 415 17.325 -10.135 11.498 1.00 35.14 O
ANISOU 3077 OD1 ASN A 415 4065 4351 4935 -26 -6 157 O
ATOM 3078 ND2 ASN A 415 19.008 -8.799 10.855 1.00 34.93 N
ANISOU 3078 ND2 ASN A 415 4050 4324 4896 -31 24 136 N
ATOM 3079 N PHE A 416 19.557 -4.965 12.273 1.00 34.46 N
ANISOU 3079 N PHE A 416 4024 4305 4764 -32 30 164 N
ATOM 3080 CA PHE A 416 20.630 -4.354 13.067 1.00 34.94 C
ANISOU 3080 CA PHE A 416 4076 4367 4833 -33 32 172 C
ATOM 3081 C PHE A 416 21.941 -5.122 13.066 1.00 36.13 C
ANISOU 3081 C PHE A 416 4204 4499 5023 -36 39 163 C
ATOM 3082 O PHE A 416 22.716 -5.036 14.028 1.00 37.10 O
ANISOU 3082 O PHE A 416 4311 4619 5164 -36 33 175 O
ATOM 3083 CB PHE A 416 20.175 -4.062 14.507 1.00 34.18 C
ANISOU 3083 CB PHE A 416 3973 4282 4730 -32 13 198 C
ATOM 3084 CG PHE A 416 19.042 -3.090 14.593 1.00 34.75 C
ANISOU 3084 CG PHE A 416 4067 4372 4764 -30 9 206 C
ATOM 3085 CD1 PHE A 416 17.722 -3.541 14.604 1.00 34.82 C
ANISOU 3085 CD1 PHE A 416 4079 4386 4765 -27 -2 212 C
ATOM 3086 CD2 PHE A 416 19.286 -1.721 14.637 1.00 34.19 C
ANISOU 3086 CD2 PHE A 416 4011 4311 4668 -30 17 205 C
ATOM 3087 CE1 PHE A 416 16.666 -2.644 14.670 1.00 35.08 C
ANISOU 3087 CE1 PHE A 416 4129 4433 4766 -25 -6 219 C
ATOM 3088 CE2 PHE A 416 18.234 -0.816 14.711 1.00 34.72 C
ANISOU 3088 CE2 PHE A 416 4095 4392 4703 -28 13 212 C
ATOM 3089 CZ PHE A 416 16.920 -1.277 14.723 1.00 35.13 C
ANISOU 3089 CZ PHE A 416 4150 4449 4748 -26 1 218 C
ATOM 3090 N MET A 417 22.212 -5.864 11.995 1.00 36.24 N
ANISOU 3090 N MET A 417 4216 4499 5053 -37 53 141 N
ATOM 3091 CA MET A 417 23.496 -6.539 11.935 1.00 36.69 C
ANISOU 3091 CA MET A 417 4250 4537 5151 -39 62 130 C
ATOM 3092 C MET A 417 24.608 -5.497 11.774 1.00 36.33 C
ANISOU 3092 C MET A 417 4211 4493 5100 -43 79 122 C
ATOM 3093 O MET A 417 24.518 -4.587 10.945 1.00 35.76 O
ANISOU 3093 O MET A 417 4161 4428 4995 -45 95 109 O
ATOM 3094 CB MET A 417 23.533 -7.691 10.921 1.00 38.11 C
ANISOU 3094 CB MET A 417 4423 4701 5355 -41 72 108 C
ATOM 3095 CG MET A 417 23.252 -7.343 9.477 1.00 42.04 C
ANISOU 3095 CG MET A 417 4945 5200 5824 -45 93 83 C
ATOM 3096 SD MET A 417 21.498 -7.276 9.042 1.00 44.36 S
ANISOU 3096 SD MET A 417 5264 5509 6079 -43 81 89 S
ATOM 3097 CE MET A 417 21.711 -6.730 7.346 1.00 44.30 C
ANISOU 3097 CE MET A 417 5285 5502 6045 -51 109 59 C
ATOM 3098 N GLY A 418 25.619 -5.607 12.632 1.00 35.86 N
ANISOU 3098 N GLY A 418 4129 4425 5071 -43 74 131 N
ATOM 3099 CA GLY A 418 26.650 -4.576 12.769 1.00 35.00 C
ANISOU 3099 CA GLY A 418 4022 4317 4957 -46 86 129 C
ATOM 3100 C GLY A 418 26.427 -3.627 13.943 1.00 33.03 C
ANISOU 3100 C GLY A 418 3779 4084 4686 -45 70 153 C
ATOM 3101 O GLY A 418 27.336 -2.911 14.346 1.00 32.41 O
ANISOU 3101 O GLY A 418 3697 4005 4611 -47 74 156 O
ATOM 3102 N LEU A 419 25.216 -3.599 14.483 1.00 32.58 N
ANISOU 3102 N LEU A 419 3731 4041 4607 -42 52 170 N
ATOM 3103 CA LEU A 419 24.902 -2.656 15.559 1.00 33.80 C
ANISOU 3103 CA LEU A 419 3893 4212 4737 -42 39 191 C
ATOM 3104 C LEU A 419 24.581 -3.362 16.881 1.00 35.00 C
ANISOU 3104 C LEU A 419 4027 4365 4906 -42 14 216 C
ATOM 3105 O LEU A 419 23.750 -2.898 17.662 1.00 34.90 O
ANISOU 3105 O LEU A 419 4022 4367 4868 -42 1 233 O
ATOM 3106 CB LEU A 419 23.770 -1.699 15.144 1.00 32.25 C
ANISOU 3106 CB LEU A 419 3724 4033 4495 -40 43 191 C
ATOM 3107 CG LEU A 419 23.955 -0.868 13.864 1.00 32.25 C
ANISOU 3107 CG LEU A 419 3745 4035 4473 -41 65 170 C
ATOM 3108 CD1 LEU A 419 22.686 -0.095 13.539 1.00 32.78 C
ANISOU 3108 CD1 LEU A 419 3836 4117 4499 -39 63 173 C
ATOM 3109 CD2 LEU A 419 25.155 0.074 13.922 1.00 31.25 C
ANISOU 3109 CD2 LEU A 419 3619 3907 4346 -44 78 165 C
ATOM 3110 N GLU A 420 25.282 -4.468 17.132 1.00 36.02 N
ANISOU 3110 N GLU A 420 4131 4477 5078 -44 7 217 N
ATOM 3111 CA GLU A 420 24.989 -5.359 18.258 1.00 36.17 C
ANISOU 3111 CA GLU A 420 4132 4493 5116 -46 -17 240 C
ATOM 3112 C GLU A 420 25.283 -4.784 19.648 1.00 35.95 C
ANISOU 3112 C GLU A 420 4101 4475 5083 -50 -34 263 C
ATOM 3113 O GLU A 420 25.070 -5.449 20.647 1.00 38.41 O
ANISOU 3113 O GLU A 420 4399 4786 5408 -54 -56 284 O
ATOM 3114 CB GLU A 420 25.700 -6.698 18.065 1.00 35.79 C
ANISOU 3114 CB GLU A 420 4057 4421 5119 -46 -21 234 C
ATOM 3115 CG GLU A 420 26.751 -6.668 16.972 1.00 37.86 C
ANISOU 3115 CG GLU A 420 4316 4668 5401 -46 3 207 C
ATOM 3116 CD GLU A 420 26.221 -7.081 15.605 1.00 40.36 C
ANISOU 3116 CD GLU A 420 4643 4981 5711 -43 20 183 C
ATOM 3117 OE1 GLU A 420 25.270 -7.885 15.511 1.00 41.67 O
ANISOU 3117 OE1 GLU A 420 4808 5147 5877 -40 10 186 O
ATOM 3118 OE2 GLU A 420 26.780 -6.621 14.596 1.00 42.32 O
ANISOU 3118 OE2 GLU A 420 4899 5224 5954 -43 44 160 O
ATOM 3119 N GLU A 421 25.743 -3.541 19.700 1.00 35.23 N
ANISOU 3119 N GLU A 421 4022 4393 4970 -51 -24 261 N
ATOM 3120 CA GLU A 421 26.064 -2.867 20.947 1.00 34.27 C
ANISOU 3120 CA GLU A 421 3899 4280 4839 -57 -37 281 C
ATOM 3121 C GLU A 421 24.940 -1.960 21.459 1.00 32.37 C
ANISOU 3121 C GLU A 421 3680 4063 4554 -57 -41 291 C
ATOM 3122 O GLU A 421 25.012 -1.460 22.580 1.00 32.22 O
ANISOU 3122 O GLU A 421 3662 4054 4524 -62 -53 308 O
ATOM 3123 CB GLU A 421 27.345 -2.046 20.761 1.00 37.33 C
ANISOU 3123 CB GLU A 421 4287 4663 5234 -58 -24 272 C
ATOM 3124 CG GLU A 421 28.625 -2.871 20.704 1.00 42.41 C
ANISOU 3124 CG GLU A 421 4904 5282 5926 -60 -26 268 C
ATOM 3125 CD GLU A 421 28.987 -3.463 22.059 1.00 46.80 C
ANISOU 3125 CD GLU A 421 5441 5833 6507 -67 -53 293 C
ATOM 3126 OE1 GLU A 421 28.945 -2.708 23.059 1.00 49.87 O
ANISOU 3126 OE1 GLU A 421 5837 6236 6875 -73 -64 310 O
ATOM 3127 OE2 GLU A 421 29.290 -4.679 22.134 1.00 47.61 O
ANISOU 3127 OE2 GLU A 421 5521 5918 6650 -69 -64 296 O
ATOM 3128 N LEU A 422 23.914 -1.750 20.633 1.00 30.52 N
ANISOU 3128 N LEU A 422 3463 3837 4295 -51 -31 280 N
ATOM 3129 CA LEU A 422 22.807 -0.829 20.929 1.00 29.97 C
ANISOU 3129 CA LEU A 422 3414 3788 4186 -50 -32 286 C
ATOM 3130 C LEU A 422 22.092 -1.160 22.233 1.00 29.23 C
ANISOU 3130 C LEU A 422 3314 3704 4087 -55 -52 308 C
ATOM 3131 O LEU A 422 21.776 -2.318 22.487 1.00 28.78 O
ANISOU 3131 O LEU A 422 3244 3641 4050 -56 -65 317 O
ATOM 3132 CB LEU A 422 21.778 -0.867 19.787 1.00 29.92 C
ANISOU 3132 CB LEU A 422 3421 3783 4162 -44 -21 271 C
ATOM 3133 CG LEU A 422 21.357 0.394 19.022 1.00 29.19 C
ANISOU 3133 CG LEU A 422 3353 3701 4036 -40 -6 259 C
ATOM 3134 CD1 LEU A 422 20.030 0.152 18.331 1.00 30.10 C
ANISOU 3134 CD1 LEU A 422 3479 3820 4135 -36 -6 254 C
ATOM 3135 CD2 LEU A 422 21.243 1.609 19.913 1.00 29.20 C
ANISOU 3135 CD2 LEU A 422 3363 3717 4012 -43 -9 270 C
ATOM 3136 N GLN A 423 21.833 -0.152 23.061 1.00 30.01 N
ANISOU 3136 N GLN A 423 3423 3818 4158 -59 -55 318 N
ATOM 3137 CA GLN A 423 21.106 -0.394 24.321 1.00 30.59 C
ANISOU 3137 CA GLN A 423 3493 3903 4223 -65 -72 339 C
ATOM 3138 C GLN A 423 19.852 0.447 24.545 1.00 30.05 C
ANISOU 3138 C GLN A 423 3443 3854 4119 -64 -68 340 C
ATOM 3139 O GLN A 423 19.066 0.171 25.461 1.00 30.76 O
ANISOU 3139 O GLN A 423 3531 3954 4200 -69 -80 354 O
ATOM 3140 CB GLN A 423 22.021 -0.396 25.553 1.00 30.15 C
ANISOU 3140 CB GLN A 423 3428 3848 4179 -76 -86 356 C
ATOM 3141 CG GLN A 423 23.053 0.696 25.598 1.00 31.81 C
ANISOU 3141 CG GLN A 423 3644 4059 4383 -77 -77 350 C
ATOM 3142 CD GLN A 423 24.225 0.360 26.504 1.00 33.17 C
ANISOU 3142 CD GLN A 423 3800 4223 4580 -86 -92 365 C
ATOM 3143 OE1 GLN A 423 24.465 -0.804 26.853 1.00 33.23 O
ANISOU 3143 OE1 GLN A 423 3790 4219 4616 -91 -108 376 O
ATOM 3144 NE2 GLN A 423 24.970 1.388 26.887 1.00 33.81 N
ANISOU 3144 NE2 GLN A 423 3887 4308 4651 -90 -89 365 N
ATOM 3145 N HIS A 424 19.659 1.445 23.692 1.00 28.53 N
ANISOU 3145 N HIS A 424 3267 3665 3907 -57 -52 324 N
ATOM 3146 CA HIS A 424 18.498 2.313 23.766 1.00 27.84 C
ANISOU 3146 CA HIS A 424 3195 3592 3788 -55 -48 323 C
ATOM 3147 C HIS A 424 18.018 2.530 22.353 1.00 27.42 C
ANISOU 3147 C HIS A 424 3154 3535 3728 -46 -36 305 C
ATOM 3148 O HIS A 424 18.780 2.986 21.501 1.00 26.86 O
ANISOU 3148 O HIS A 424 3088 3457 3659 -43 -24 292 O
ATOM 3149 CB HIS A 424 18.876 3.625 24.459 1.00 27.42 C
ANISOU 3149 CB HIS A 424 3151 3551 3716 -58 -44 325 C
ATOM 3150 CG HIS A 424 17.703 4.533 24.751 1.00 28.12 C
ANISOU 3150 CG HIS A 424 3253 3654 3775 -57 -40 325 C
ATOM 3151 ND1 HIS A 424 17.079 5.255 23.789 1.00 27.98 N
ANISOU 3151 ND1 HIS A 424 3249 3638 3743 -49 -30 311 N
ATOM 3152 CD2 HIS A 424 17.053 4.836 25.950 1.00 28.72 C
ANISOU 3152 CD2 HIS A 424 3330 3745 3836 -64 -47 336 C
ATOM 3153 CE1 HIS A 424 16.077 5.969 24.336 1.00 27.64 C
ANISOU 3153 CE1 HIS A 424 3214 3608 3679 -50 -29 314 C
ATOM 3154 NE2 HIS A 424 16.061 5.718 25.658 1.00 28.70 N
ANISOU 3154 NE2 HIS A 424 3341 3751 3813 -59 -38 328 N
ATOM 3155 N LEU A 425 16.761 2.174 22.091 1.00 26.95 N
ANISOU 3155 N LEU A 425 3097 3479 3661 -42 -39 306 N
ATOM 3156 CA LEU A 425 16.169 2.287 20.760 1.00 27.34 C
ANISOU 3156 CA LEU A 425 3159 3525 3704 -35 -30 291 C
ATOM 3157 C LEU A 425 14.752 2.882 20.852 1.00 28.72 C
ANISOU 3157 C LEU A 425 3344 3711 3857 -32 -32 293 C
ATOM 3158 O LEU A 425 13.871 2.302 21.511 1.00 28.39 O
ANISOU 3158 O LEU A 425 3295 3674 3817 -33 -41 303 O
ATOM 3159 CB LEU A 425 16.176 0.922 20.061 1.00 26.59 C
ANISOU 3159 CB LEU A 425 3053 3416 3632 -33 -33 287 C
ATOM 3160 CG LEU A 425 15.612 0.719 18.648 1.00 26.66 C
ANISOU 3160 CG LEU A 425 3072 3418 3637 -27 -27 271 C
ATOM 3161 CD1 LEU A 425 16.243 1.640 17.615 1.00 27.18 C
ANISOU 3161 CD1 LEU A 425 3154 3481 3691 -26 -11 255 C
ATOM 3162 CD2 LEU A 425 15.765 -0.726 18.216 1.00 26.05 C
ANISOU 3162 CD2 LEU A 425 2982 3328 3587 -27 -31 268 C
ATOM 3163 N ASP A 426 14.546 4.044 20.213 1.00 29.27 N
ANISOU 3163 N ASP A 426 3430 3784 3907 -28 -22 283 N
ATOM 3164 CA ASP A 426 13.267 4.774 20.309 1.00 29.81 C
ANISOU 3164 CA ASP A 426 3507 3861 3956 -25 -23 284 C
ATOM 3165 C ASP A 426 12.625 5.015 18.940 1.00 30.15 C
ANISOU 3165 C ASP A 426 3564 3898 3992 -20 -20 272 C
ATOM 3166 O ASP A 426 13.208 5.681 18.080 1.00 30.28 O
ANISOU 3166 O ASP A 426 3593 3911 4001 -19 -11 262 O
ATOM 3167 CB ASP A 426 13.422 6.103 21.078 1.00 30.04 C
ANISOU 3167 CB ASP A 426 3543 3901 3969 -27 -19 286 C
ATOM 3168 CG ASP A 426 12.077 6.663 21.588 1.00 30.88 C
ANISOU 3168 CG ASP A 426 3652 4016 4061 -26 -21 290 C
ATOM 3169 OD1 ASP A 426 11.009 6.259 21.075 1.00 31.42 O
ANISOU 3169 OD1 ASP A 426 3722 4083 4131 -22 -26 289 O
ATOM 3170 OD2 ASP A 426 12.083 7.511 22.510 1.00 30.10 O
ANISOU 3170 OD2 ASP A 426 3555 3928 3952 -29 -19 293 O
ATOM 3171 N PHE A 427 11.419 4.474 18.763 1.00 29.64 N
ANISOU 3171 N PHE A 427 3499 3834 3929 -17 -27 275 N
ATOM 3172 CA PHE A 427 10.682 4.548 17.497 1.00 29.93 C
ANISOU 3172 CA PHE A 427 3548 3864 3959 -13 -27 266 C
ATOM 3173 C PHE A 427 9.305 5.172 17.697 1.00 30.34 C
ANISOU 3173 C PHE A 427 3604 3923 4001 -9 -33 269 C
ATOM 3174 O PHE A 427 8.480 5.237 16.768 1.00 30.24 O
ANISOU 3174 O PHE A 427 3600 3905 3984 -6 -36 265 O
ATOM 3175 CB PHE A 427 10.467 3.148 16.934 1.00 29.70 C
ANISOU 3175 CB PHE A 427 3511 3826 3946 -12 -33 264 C
ATOM 3176 CG PHE A 427 11.626 2.596 16.164 1.00 29.34 C
ANISOU 3176 CG PHE A 427 3466 3770 3911 -14 -26 254 C
ATOM 3177 CD1 PHE A 427 12.204 1.392 16.543 1.00 29.22 C
ANISOU 3177 CD1 PHE A 427 3434 3749 3919 -16 -29 258 C
ATOM 3178 CD2 PHE A 427 12.104 3.241 15.031 1.00 29.30 C
ANISOU 3178 CD2 PHE A 427 3476 3760 3894 -15 -16 241 C
ATOM 3179 CE1 PHE A 427 13.244 0.848 15.809 1.00 29.44 C
ANISOU 3179 CE1 PHE A 427 3459 3766 3959 -18 -21 246 C
ATOM 3180 CE2 PHE A 427 13.142 2.704 14.293 1.00 28.70 C
ANISOU 3180 CE2 PHE A 427 3399 3674 3829 -18 -7 230 C
ATOM 3181 CZ PHE A 427 13.718 1.512 14.684 1.00 29.05 C
ANISOU 3181 CZ PHE A 427 3426 3712 3898 -19 -9 232 C
ATOM 3182 N GLN A 428 9.063 5.600 18.932 1.00 30.74 N
ANISOU 3182 N GLN A 428 3647 3983 4047 -11 -33 278 N
ATOM 3183 CA GLN A 428 7.819 6.223 19.363 1.00 30.15 C
ANISOU 3183 CA GLN A 428 3573 3915 3965 -9 -36 281 C
ATOM 3184 C GLN A 428 7.201 7.129 18.293 1.00 29.33 C
ANISOU 3184 C GLN A 428 3485 3806 3852 -4 -36 273 C
ATOM 3185 O GLN A 428 7.881 7.971 17.722 1.00 28.42 O
ANISOU 3185 O GLN A 428 3381 3689 3728 -4 -30 266 O
ATOM 3186 CB GLN A 428 8.111 7.012 20.646 1.00 30.55 C
ANISOU 3186 CB GLN A 428 3620 3977 4008 -13 -31 286 C
ATOM 3187 CG GLN A 428 6.964 7.823 21.193 1.00 32.11 C
ANISOU 3187 CG GLN A 428 3819 4182 4199 -12 -30 287 C
ATOM 3188 CD GLN A 428 7.247 8.419 22.559 1.00 33.17 C
ANISOU 3188 CD GLN A 428 3948 4328 4326 -18 -25 291 C
ATOM 3189 OE1 GLN A 428 6.404 8.330 23.455 1.00 35.88 O
ANISOU 3189 OE1 GLN A 428 4284 4679 4669 -20 -25 296 O
ATOM 3190 NE2 GLN A 428 8.412 9.043 22.724 1.00 30.41 N
ANISOU 3190 NE2 GLN A 428 3603 3980 3970 -20 -19 289 N
ATOM 3191 N HIS A 429 5.909 6.938 18.027 1.00 30.06 N
ANISOU 3191 N HIS A 429 3577 3897 3948 -1 -44 274 N
ATOM 3192 CA HIS A 429 5.127 7.823 17.146 1.00 30.44 C
ANISOU 3192 CA HIS A 429 3637 3940 3989 2 -47 269 C
ATOM 3193 C HIS A 429 5.594 7.899 15.702 1.00 30.89 C
ANISOU 3193 C HIS A 429 3709 3986 4039 2 -48 261 C
ATOM 3194 O HIS A 429 5.256 8.843 15.007 1.00 33.03 O
ANISOU 3194 O HIS A 429 3994 4254 4302 3 -50 257 O
ATOM 3195 CB HIS A 429 5.045 9.239 17.728 1.00 29.49 C
ANISOU 3195 CB HIS A 429 3519 3824 3859 3 -41 268 C
ATOM 3196 CG HIS A 429 4.010 9.405 18.810 1.00 29.99 C
ANISOU 3196 CG HIS A 429 3571 3895 3927 3 -42 273 C
ATOM 3197 ND1 HIS A 429 2.698 9.556 18.540 1.00 31.06 N
ANISOU 3197 ND1 HIS A 429 3704 4026 4068 7 -49 273 N
ATOM 3198 CD2 HIS A 429 4.135 9.476 20.191 1.00 30.15 C
ANISOU 3198 CD2 HIS A 429 3581 3927 3948 0 -36 277 C
ATOM 3199 CE1 HIS A 429 2.016 9.702 19.691 1.00 30.79 C
ANISOU 3199 CE1 HIS A 429 3658 4000 4038 6 -46 276 C
ATOM 3200 NE2 HIS A 429 2.893 9.652 20.702 1.00 30.64 N
ANISOU 3200 NE2 HIS A 429 3635 3991 4014 1 -38 279 N
ATOM 3201 N SER A 430 6.379 6.938 15.236 1.00 30.56 N
ANISOU 3201 N SER A 430 3668 3941 4003 0 -46 258 N
ATOM 3202 CA SER A 430 6.778 6.907 13.836 1.00 31.49 C
ANISOU 3202 CA SER A 430 3800 4049 4113 -2 -44 249 C
ATOM 3203 C SER A 430 6.009 5.809 13.128 1.00 32.91 C
ANISOU 3203 C SER A 430 3980 4222 4302 -1 -54 248 C
ATOM 3204 O SER A 430 5.515 4.869 13.762 1.00 33.26 O
ANISOU 3204 O SER A 430 4009 4267 4359 0 -60 254 O
ATOM 3205 CB SER A 430 8.270 6.613 13.693 1.00 31.28 C
ANISOU 3205 CB SER A 430 3774 4021 4088 -6 -33 243 C
ATOM 3206 OG SER A 430 9.038 7.414 14.560 1.00 33.17 O
ANISOU 3206 OG SER A 430 4010 4267 4323 -7 -25 245 O
ATOM 3207 N THR A 431 5.933 5.906 11.809 1.00 32.91 N
ANISOU 3207 N THR A 431 3996 4214 4293 -4 -57 240 N
ATOM 3208 CA THR A 431 5.303 4.857 11.025 1.00 34.20 C
ANISOU 3208 CA THR A 431 4161 4370 4463 -5 -65 238 C
ATOM 3209 C THR A 431 6.302 3.733 10.744 1.00 34.21 C
ANISOU 3209 C THR A 431 4158 4367 4473 -8 -58 230 C
ATOM 3210 O THR A 431 6.938 3.694 9.686 1.00 32.95 O
ANISOU 3210 O THR A 431 4012 4201 4305 -14 -51 219 O
ATOM 3211 CB THR A 431 4.713 5.412 9.717 1.00 35.33 C
ANISOU 3211 CB THR A 431 4326 4506 4592 -8 -73 233 C
ATOM 3212 OG1 THR A 431 4.002 6.625 10.001 1.00 35.19 O
ANISOU 3212 OG1 THR A 431 4311 4490 4568 -5 -79 240 O
ATOM 3213 CG2 THR A 431 3.783 4.390 9.061 1.00 35.24 C
ANISOU 3213 CG2 THR A 431 4314 4487 4588 -8 -86 233 C
ATOM 3214 N LEU A 432 6.449 2.844 11.725 1.00 35.30 N
ANISOU 3214 N LEU A 432 4276 4508 4628 -6 -58 236 N
ATOM 3215 CA LEU A 432 7.213 1.611 11.562 1.00 36.10 C
ANISOU 3215 CA LEU A 432 4369 4603 4744 -8 -53 231 C
ATOM 3216 C LEU A 432 6.533 0.701 10.551 1.00 37.47 C
ANISOU 3216 C LEU A 432 4547 4767 4921 -9 -61 225 C
ATOM 3217 O LEU A 432 5.308 0.560 10.552 1.00 40.67 O
ANISOU 3217 O LEU A 432 4952 5173 5328 -6 -74 231 O
ATOM 3218 CB LEU A 432 7.317 0.868 12.889 1.00 34.87 C
ANISOU 3218 CB LEU A 432 4190 4451 4606 -6 -56 242 C
ATOM 3219 CG LEU A 432 8.548 0.966 13.772 1.00 34.42 C
ANISOU 3219 CG LEU A 432 4123 4398 4555 -8 -47 245 C
ATOM 3220 CD1 LEU A 432 8.330 0.022 14.935 1.00 34.12 C
ANISOU 3220 CD1 LEU A 432 4064 4363 4535 -7 -55 257 C
ATOM 3221 CD2 LEU A 432 9.811 0.593 13.016 1.00 34.72 C
ANISOU 3221 CD2 LEU A 432 4163 4427 4599 -11 -36 232 C
ATOM 3222 N LYS A 433 7.332 0.066 9.709 1.00 37.85 N
ANISOU 3222 N LYS A 433 4600 4808 4973 -14 -53 212 N
ATOM 3223 CA LYS A 433 6.802 -0.731 8.623 1.00 37.88 C
ANISOU 3223 CA LYS A 433 4612 4802 4977 -17 -59 204 C
ATOM 3224 C LYS A 433 7.560 -2.033 8.574 1.00 37.86 C
ANISOU 3224 C LYS A 433 4595 4792 4995 -18 -53 196 C
ATOM 3225 O LYS A 433 8.773 -2.067 8.785 1.00 39.26 O
ANISOU 3225 O LYS A 433 4768 4969 5181 -20 -40 190 O
ATOM 3226 CB LYS A 433 7.000 0.001 7.296 1.00 39.97 C
ANISOU 3226 CB LYS A 433 4902 5064 5219 -24 -54 192 C
ATOM 3227 CG LYS A 433 5.738 0.265 6.506 1.00 42.18 C
ANISOU 3227 CG LYS A 433 5197 5341 5487 -25 -68 194 C
ATOM 3228 CD LYS A 433 5.233 1.680 6.733 1.00 44.35 C
ANISOU 3228 CD LYS A 433 5481 5623 5746 -23 -74 203 C
ATOM 3229 CE LYS A 433 3.940 1.932 5.967 1.00 48.46 C
ANISOU 3229 CE LYS A 433 6015 6138 6257 -25 -91 207 C
ATOM 3230 NZ LYS A 433 3.720 3.391 5.725 1.00 50.32 N
ANISOU 3230 NZ LYS A 433 6266 6376 6475 -26 -94 211 N
ATOM 3231 N ARG A 434 6.832 -3.103 8.290 1.00 38.15 N
ANISOU 3231 N ARG A 434 4627 4822 5044 -17 -63 195 N
ATOM 3232 CA ARG A 434 7.400 -4.426 8.033 1.00 38.64 C
ANISOU 3232 CA ARG A 434 4678 4875 5128 -19 -59 186 C
ATOM 3233 C ARG A 434 8.149 -5.017 9.223 1.00 38.69 C
ANISOU 3233 C ARG A 434 4660 4881 5159 -16 -57 194 C
ATOM 3234 O ARG A 434 8.764 -6.065 9.105 1.00 40.50 O
ANISOU 3234 O ARG A 434 4876 5101 5409 -17 -53 186 O
ATOM 3235 CB ARG A 434 8.251 -4.429 6.754 1.00 38.20 C
ANISOU 3235 CB ARG A 434 4638 4812 5064 -27 -44 164 C
ATOM 3236 CG ARG A 434 7.541 -3.781 5.565 1.00 41.36 C
ANISOU 3236 CG ARG A 434 5065 5211 5436 -33 -48 158 C
ATOM 3237 CD ARG A 434 7.962 -4.364 4.226 1.00 44.59 C
ANISOU 3237 CD ARG A 434 5487 5611 5841 -42 -38 137 C
ATOM 3238 NE ARG A 434 9.415 -4.487 4.143 1.00 48.48 N
ANISOU 3238 NE ARG A 434 5976 6101 6343 -46 -17 123 N
ATOM 3239 CZ ARG A 434 10.176 -3.912 3.219 1.00 48.46 C
ANISOU 3239 CZ ARG A 434 5992 6097 6322 -55 -1 108 C
ATOM 3240 NH1 ARG A 434 9.618 -3.173 2.260 1.00 48.91 N
ANISOU 3240 NH1 ARG A 434 6076 6157 6350 -63 -5 105 N
ATOM 3241 NH2 ARG A 434 11.496 -4.088 3.256 1.00 45.15 N
ANISOU 3241 NH2 ARG A 434 5564 5674 5915 -58 17 96 N
ATOM 3242 N VAL A 435 8.056 -4.360 10.376 1.00 38.34 N
ANISOU 3242 N VAL A 435 4607 4847 5111 -12 -60 209 N
ATOM 3243 CA VAL A 435 8.671 -4.845 11.614 1.00 39.02 C
ANISOU 3243 CA VAL A 435 4672 4935 5218 -11 -61 220 C
ATOM 3244 C VAL A 435 8.074 -6.194 12.058 1.00 39.74 C
ANISOU 3244 C VAL A 435 4745 5021 5334 -9 -74 228 C
ATOM 3245 O VAL A 435 8.621 -6.888 12.911 1.00 39.63 O
ANISOU 3245 O VAL A 435 4711 5004 5340 -9 -77 236 O
ATOM 3246 CB VAL A 435 8.589 -3.766 12.735 1.00 37.79 C
ANISOU 3246 CB VAL A 435 4515 4793 5051 -9 -62 234 C
ATOM 3247 CG1 VAL A 435 7.242 -3.783 13.438 1.00 36.38 C
ANISOU 3247 CG1 VAL A 435 4331 4622 4869 -6 -76 249 C
ATOM 3248 CG2 VAL A 435 9.725 -3.916 13.740 1.00 36.68 C
ANISOU 3248 CG2 VAL A 435 4359 4654 4924 -11 -58 241 C
ATOM 3249 N THR A 436 6.954 -6.567 11.458 1.00 43.65 N
ANISOU 3249 N THR A 436 5245 5513 5825 -8 -83 227 N
ATOM 3250 CA THR A 436 6.270 -7.792 11.835 1.00 47.02 C
ANISOU 3250 CA THR A 436 5656 5935 6273 -6 -97 235 C
ATOM 3251 C THR A 436 6.606 -8.948 10.887 1.00 48.25 C
ANISOU 3251 C THR A 436 5808 6075 6446 -8 -95 220 C
ATOM 3252 O THR A 436 6.449 -10.113 11.240 1.00 50.38 O
ANISOU 3252 O THR A 436 6062 6339 6741 -7 -104 225 O
ATOM 3253 CB THR A 436 4.750 -7.568 11.934 1.00 48.70 C
ANISOU 3253 CB THR A 436 5873 6153 6476 -3 -110 245 C
ATOM 3254 OG1 THR A 436 4.146 -8.712 12.539 1.00 52.53 O
ANISOU 3254 OG1 THR A 436 6340 6636 6983 -2 -122 256 O
ATOM 3255 CG2 THR A 436 4.123 -7.316 10.555 1.00 48.84 C
ANISOU 3255 CG2 THR A 436 5911 6166 6478 -4 -111 232 C
ATOM 3256 N GLU A 437 7.097 -8.608 9.699 1.00 48.65 N
ANISOU 3256 N GLU A 437 5877 6121 6485 -11 -83 201 N
ATOM 3257 CA GLU A 437 7.441 -9.580 8.662 1.00 48.93 C
ANISOU 3257 CA GLU A 437 5914 6144 6534 -15 -78 182 C
ATOM 3258 C GLU A 437 8.678 -10.440 8.965 1.00 49.53 C
ANISOU 3258 C GLU A 437 5970 6209 6639 -16 -70 176 C
ATOM 3259 O GLU A 437 8.885 -11.447 8.295 1.00 53.37 O
ANISOU 3259 O GLU A 437 6452 6683 7144 -18 -68 162 O
ATOM 3260 CB GLU A 437 7.634 -8.873 7.313 1.00 49.70 C
ANISOU 3260 CB GLU A 437 6038 6240 6606 -21 -67 164 C
ATOM 3261 CG GLU A 437 6.412 -8.118 6.809 1.00 51.85 C
ANISOU 3261 CG GLU A 437 6329 6518 6850 -21 -77 168 C
ATOM 3262 CD GLU A 437 6.597 -7.531 5.415 1.00 55.36 C
ANISOU 3262 CD GLU A 437 6801 6960 7270 -29 -67 150 C
ATOM 3263 OE1 GLU A 437 5.729 -6.732 5.000 1.00 55.68 O
ANISOU 3263 OE1 GLU A 437 6860 7006 7287 -30 -76 155 O
ATOM 3264 OE2 GLU A 437 7.597 -7.861 4.728 1.00 56.38 O
ANISOU 3264 OE2 GLU A 437 6934 7082 7402 -35 -51 132 O
ATOM 3265 N PHE A 438 9.506 -10.037 9.936 1.00 47.45 N
ANISOU 3265 N PHE A 438 5695 5950 6382 -15 -66 186 N
ATOM 3266 CA PHE A 438 10.685 -10.832 10.367 1.00 44.48 C
ANISOU 3266 CA PHE A 438 5297 5563 6038 -16 -61 183 C
ATOM 3267 C PHE A 438 11.115 -10.526 11.806 1.00 41.75 C
ANISOU 3267 C PHE A 438 4936 5225 5700 -15 -67 204 C
ATOM 3268 O PHE A 438 10.470 -9.733 12.478 1.00 43.04 O
ANISOU 3268 O PHE A 438 5106 5403 5844 -13 -74 219 O
ATOM 3269 CB PHE A 438 11.868 -10.708 9.383 1.00 43.25 C
ANISOU 3269 CB PHE A 438 5148 5398 5884 -21 -40 159 C
ATOM 3270 CG PHE A 438 12.488 -9.335 9.312 1.00 42.94 C
ANISOU 3270 CG PHE A 438 5125 5369 5820 -23 -27 156 C
ATOM 3271 CD1 PHE A 438 13.790 -9.127 9.757 1.00 42.62 C
ANISOU 3271 CD1 PHE A 438 5073 5326 5794 -24 -16 154 C
ATOM 3272 CD2 PHE A 438 11.789 -8.253 8.773 1.00 43.00 C
ANISOU 3272 CD2 PHE A 438 5157 5387 5791 -24 -26 155 C
ATOM 3273 CE1 PHE A 438 14.383 -7.870 9.677 1.00 41.88 C
ANISOU 3273 CE1 PHE A 438 4993 5240 5678 -26 -4 151 C
ATOM 3274 CE2 PHE A 438 12.374 -6.993 8.694 1.00 42.72 C
ANISOU 3274 CE2 PHE A 438 5135 5359 5734 -26 -14 153 C
ATOM 3275 CZ PHE A 438 13.676 -6.802 9.144 1.00 42.24 C
ANISOU 3275 CZ PHE A 438 5063 5296 5687 -27 -3 151 C
ATOM 3276 N SER A 439 12.177 -11.172 12.287 1.00 39.89 N
ANISOU 3276 N SER A 439 4681 4980 5495 -16 -66 204 N
ATOM 3277 CA SER A 439 12.729 -10.831 13.601 1.00 39.64 C
ANISOU 3277 CA SER A 439 4636 4954 5469 -17 -71 223 C
ATOM 3278 C SER A 439 13.655 -9.618 13.473 1.00 38.58 C
ANISOU 3278 C SER A 439 4513 4826 5317 -19 -55 216 C
ATOM 3279 O SER A 439 14.862 -9.748 13.308 1.00 38.43 O
ANISOU 3279 O SER A 439 4486 4797 5316 -21 -45 206 O
ATOM 3280 CB SER A 439 13.433 -12.031 14.246 1.00 38.71 C
ANISOU 3280 CB SER A 439 4491 4823 5393 -18 -80 230 C
ATOM 3281 OG SER A 439 12.490 -12.963 14.748 1.00 37.48 O
ANISOU 3281 OG SER A 439 4324 4666 5250 -18 -98 245 O
ATOM 3282 N ALA A 440 13.066 -8.432 13.534 1.00 39.51 N
ANISOU 3282 N ALA A 440 4650 4959 5401 -18 -54 220 N
ATOM 3283 CA ALA A 440 13.780 -7.206 13.170 1.00 39.04 C
ANISOU 3283 CA ALA A 440 4606 4905 5322 -19 -38 211 C
ATOM 3284 C ALA A 440 14.771 -6.735 14.226 1.00 37.35 C
ANISOU 3284 C ALA A 440 4381 4694 5114 -21 -37 222 C
ATOM 3285 O ALA A 440 15.650 -5.936 13.920 1.00 37.66 O
ANISOU 3285 O ALA A 440 4428 4734 5145 -23 -23 212 O
ATOM 3286 CB ALA A 440 12.803 -6.089 12.816 1.00 39.42 C
ANISOU 3286 CB ALA A 440 4677 4966 5333 -18 -38 212 C
ATOM 3287 N PHE A 441 14.632 -7.211 15.458 1.00 34.91 N
ANISOU 3287 N PHE A 441 4055 4388 4819 -21 -53 242 N
ATOM 3288 CA PHE A 441 15.573 -6.823 16.502 1.00 34.29 C
ANISOU 3288 CA PHE A 441 3967 4313 4748 -25 -54 253 C
ATOM 3289 C PHE A 441 16.488 -7.969 16.919 1.00 34.62 C
ANISOU 3289 C PHE A 441 3984 4339 4830 -27 -61 257 C
ATOM 3290 O PHE A 441 17.005 -7.970 18.035 1.00 35.06 O
ANISOU 3290 O PHE A 441 4027 4396 4897 -31 -71 274 O
ATOM 3291 CB PHE A 441 14.838 -6.258 17.716 1.00 32.97 C
ANISOU 3291 CB PHE A 441 3802 4162 4563 -26 -66 275 C
ATOM 3292 CG PHE A 441 13.776 -5.265 17.371 1.00 32.70 C
ANISOU 3292 CG PHE A 441 3788 4141 4494 -23 -62 272 C
ATOM 3293 CD1 PHE A 441 14.106 -3.970 17.019 1.00 32.35 C
ANISOU 3293 CD1 PHE A 441 3760 4103 4426 -22 -49 264 C
ATOM 3294 CD2 PHE A 441 12.436 -5.625 17.403 1.00 32.81 C
ANISOU 3294 CD2 PHE A 441 3804 4159 4501 -21 -71 279 C
ATOM 3295 CE1 PHE A 441 13.118 -3.056 16.699 1.00 31.91 C
ANISOU 3295 CE1 PHE A 441 3723 4058 4343 -20 -47 262 C
ATOM 3296 CE2 PHE A 441 11.443 -4.713 17.088 1.00 31.26 C
ANISOU 3296 CE2 PHE A 441 3624 3973 4277 -18 -69 277 C
ATOM 3297 CZ PHE A 441 11.788 -3.428 16.736 1.00 31.16 C
ANISOU 3297 CZ PHE A 441 3628 3966 4242 -17 -57 269 C
ATOM 3298 N LEU A 442 16.699 -8.923 16.012 1.00 35.17 N
ANISOU 3298 N LEU A 442 4046 4392 4923 -26 -56 242 N
ATOM 3299 CA LEU A 442 17.395 -10.172 16.331 1.00 35.85 C
ANISOU 3299 CA LEU A 442 4106 4461 5051 -28 -65 245 C
ATOM 3300 C LEU A 442 18.816 -9.974 16.842 1.00 36.81 C
ANISOU 3300 C LEU A 442 4215 4575 5194 -31 -62 247 C
ATOM 3301 O LEU A 442 19.216 -10.650 17.785 1.00 39.87 O
ANISOU 3301 O LEU A 442 4581 4955 5609 -35 -78 263 O
ATOM 3302 CB LEU A 442 17.391 -11.134 15.137 1.00 36.44 C
ANISOU 3302 CB LEU A 442 4177 4519 5146 -26 -57 223 C
ATOM 3303 CG LEU A 442 17.942 -12.545 15.386 1.00 37.48 C
ANISOU 3303 CG LEU A 442 4282 4631 5327 -27 -67 225 C
ATOM 3304 CD1 LEU A 442 17.100 -13.335 16.382 1.00 36.62 C
ANISOU 3304 CD1 LEU A 442 4160 4525 5228 -28 -91 250 C
ATOM 3305 CD2 LEU A 442 18.071 -13.300 14.072 1.00 38.30 C
ANISOU 3305 CD2 LEU A 442 4384 4718 5447 -25 -53 198 C
ATOM 3306 N SER A 443 19.560 -9.044 16.237 1.00 35.64 N
ANISOU 3306 N SER A 443 4079 4428 5034 -31 -43 231 N
ATOM 3307 CA SER A 443 20.945 -8.766 16.623 1.00 34.79 C
ANISOU 3307 CA SER A 443 3959 4313 4945 -34 -38 231 C
ATOM 3308 C SER A 443 21.095 -8.104 17.979 1.00 34.45 C
ANISOU 3308 C SER A 443 3914 4282 4892 -38 -52 255 C
ATOM 3309 O SER A 443 22.188 -8.099 18.538 1.00 35.42 O
ANISOU 3309 O SER A 443 4022 4396 5036 -42 -55 260 O
ATOM 3310 CB SER A 443 21.609 -7.852 15.597 1.00 36.68 C
ANISOU 3310 CB SER A 443 4214 4552 5169 -34 -13 208 C
ATOM 3311 OG SER A 443 21.711 -8.475 14.330 1.00 40.38 O
ANISOU 3311 OG SER A 443 4684 5008 5650 -33 1 183 O
ATOM 3312 N LEU A 444 20.016 -7.534 18.506 1.00 33.09 N
ANISOU 3312 N LEU A 444 3756 4129 4687 -38 -60 268 N
ATOM 3313 CA LEU A 444 20.128 -6.640 19.654 1.00 33.00 C
ANISOU 3313 CA LEU A 444 3749 4131 4656 -42 -67 287 C
ATOM 3314 C LEU A 444 20.150 -7.329 21.020 1.00 33.56 C
ANISOU 3314 C LEU A 444 3802 4203 4746 -48 -90 312 C
ATOM 3315 O LEU A 444 19.306 -7.066 21.869 1.00 32.71 O
ANISOU 3315 O LEU A 444 3701 4111 4617 -51 -101 329 O
ATOM 3316 CB LEU A 444 19.068 -5.531 19.580 1.00 31.64 C
ANISOU 3316 CB LEU A 444 3601 3979 4441 -39 -62 287 C
ATOM 3317 CG LEU A 444 19.189 -4.650 18.329 1.00 32.27 C
ANISOU 3317 CG LEU A 444 3699 4060 4500 -35 -40 264 C
ATOM 3318 CD1 LEU A 444 18.131 -3.552 18.284 1.00 32.29 C
ANISOU 3318 CD1 LEU A 444 3724 4081 4463 -33 -38 266 C
ATOM 3319 CD2 LEU A 444 20.587 -4.056 18.188 1.00 31.32 C
ANISOU 3319 CD2 LEU A 444 3578 3934 4388 -37 -28 256 C
ATOM 3320 N GLU A 445 21.146 -8.193 21.227 1.00 35.82 N
ANISOU 3320 N GLU A 445 4065 4470 5072 -51 -98 315 N
ATOM 3321 CA GLU A 445 21.259 -8.988 22.461 1.00 36.62 C
ANISOU 3321 CA GLU A 445 4149 4568 5195 -59 -123 340 C
ATOM 3322 C GLU A 445 21.643 -8.166 23.692 1.00 35.10 C
ANISOU 3322 C GLU A 445 3959 4388 4987 -67 -132 360 C
ATOM 3323 O GLU A 445 21.546 -8.645 24.811 1.00 34.31 O
ANISOU 3323 O GLU A 445 3849 4290 4894 -76 -153 383 O
ATOM 3324 CB GLU A 445 22.214 -10.179 22.275 1.00 40.10 C
ANISOU 3324 CB GLU A 445 4563 4983 5688 -60 -129 338 C
ATOM 3325 CG GLU A 445 21.668 -11.297 21.379 1.00 45.19 C
ANISOU 3325 CG GLU A 445 5200 5615 6353 -54 -127 325 C
ATOM 3326 CD GLU A 445 22.519 -12.570 21.385 1.00 47.16 C
ANISOU 3326 CD GLU A 445 5421 5838 6657 -56 -138 325 C
ATOM 3327 OE1 GLU A 445 23.670 -12.551 20.894 1.00 47.77 O
ANISOU 3327 OE1 GLU A 445 5489 5901 6761 -55 -126 310 O
ATOM 3328 OE2 GLU A 445 22.024 -13.610 21.867 1.00 48.55 O
ANISOU 3328 OE2 GLU A 445 5583 6008 6852 -59 -157 340 O
ATOM 3329 N LYS A 446 22.037 -6.915 23.482 1.00 34.84 N
ANISOU 3329 N LYS A 446 3942 4364 4930 -66 -117 350 N
ATOM 3330 CA LYS A 446 22.401 -6.023 24.583 1.00 34.92 C
ANISOU 3330 CA LYS A 446 3958 4387 4923 -74 -124 365 C
ATOM 3331 C LYS A 446 21.408 -4.881 24.846 1.00 34.27 C
ANISOU 3331 C LYS A 446 3898 4328 4792 -73 -117 367 C
ATOM 3332 O LYS A 446 21.621 -4.069 25.759 1.00 33.56 O
ANISOU 3332 O LYS A 446 3815 4250 4685 -80 -121 378 O
ATOM 3333 CB LYS A 446 23.801 -5.446 24.355 1.00 35.42 C
ANISOU 3333 CB LYS A 446 4017 4440 5000 -74 -115 356 C
ATOM 3334 CG LYS A 446 24.920 -6.454 24.535 1.00 37.39 C
ANISOU 3334 CG LYS A 446 4240 4667 5299 -77 -127 361 C
ATOM 3335 CD LYS A 446 26.234 -5.858 24.077 1.00 39.13 C
ANISOU 3335 CD LYS A 446 4456 4876 5533 -76 -113 347 C
ATOM 3336 CE LYS A 446 27.417 -6.556 24.715 1.00 40.79 C
ANISOU 3336 CE LYS A 446 4641 5067 5789 -83 -130 359 C
ATOM 3337 NZ LYS A 446 28.533 -5.580 24.866 1.00 41.95 N
ANISOU 3337 NZ LYS A 446 4789 5212 5935 -85 -123 356 N
ATOM 3338 N LEU A 447 20.334 -4.808 24.058 1.00 33.07 N
ANISOU 3338 N LEU A 447 3758 4182 4622 -66 -107 355 N
ATOM 3339 CA LEU A 447 19.368 -3.718 24.207 1.00 31.68 C
ANISOU 3339 CA LEU A 447 3603 4026 4406 -64 -100 354 C
ATOM 3340 C LEU A 447 18.682 -3.703 25.579 1.00 31.67 C
ANISOU 3340 C LEU A 447 3602 4041 4390 -73 -115 377 C
ATOM 3341 O LEU A 447 18.171 -4.730 26.039 1.00 30.91 O
ANISOU 3341 O LEU A 447 3494 3942 4305 -77 -129 390 O
ATOM 3342 CB LEU A 447 18.321 -3.764 23.099 1.00 31.26 C
ANISOU 3342 CB LEU A 447 3561 3974 4340 -55 -89 339 C
ATOM 3343 CG LEU A 447 17.594 -2.438 22.870 1.00 30.76 C
ANISOU 3343 CG LEU A 447 3519 3926 4239 -51 -77 332 C
ATOM 3344 CD1 LEU A 447 18.462 -1.524 22.016 1.00 30.67 C
ANISOU 3344 CD1 LEU A 447 3518 3911 4222 -47 -60 315 C
ATOM 3345 CD2 LEU A 447 16.250 -2.683 22.196 1.00 31.07 C
ANISOU 3345 CD2 LEU A 447 3567 3970 4267 -45 -75 326 C
ATOM 3346 N LEU A 448 18.678 -2.538 26.225 1.00 30.57 N
ANISOU 3346 N LEU A 448 3475 3916 4223 -77 -111 380 N
ATOM 3347 CA LEU A 448 18.017 -2.389 27.526 1.00 30.31 C
ANISOU 3347 CA LEU A 448 3444 3899 4171 -88 -122 399 C
ATOM 3348 C LEU A 448 16.641 -1.720 27.449 1.00 31.07 C
ANISOU 3348 C LEU A 448 3557 4012 4237 -84 -113 394 C
ATOM 3349 O LEU A 448 15.784 -1.989 28.301 1.00 32.35 O
ANISOU 3349 O LEU A 448 3718 4184 4388 -91 -121 407 O
ATOM 3350 CB LEU A 448 18.905 -1.625 28.511 1.00 28.88 C
ANISOU 3350 CB LEU A 448 3266 3725 3982 -98 -126 408 C
ATOM 3351 CG LEU A 448 20.313 -2.173 28.773 1.00 28.38 C
ANISOU 3351 CG LEU A 448 3187 3646 3950 -103 -138 416 C
ATOM 3352 CD1 LEU A 448 21.141 -1.193 29.594 1.00 26.97 C
ANISOU 3352 CD1 LEU A 448 3013 3474 3758 -112 -139 422 C
ATOM 3353 CD2 LEU A 448 20.237 -3.533 29.452 1.00 28.60 C
ANISOU 3353 CD2 LEU A 448 3197 3666 4001 -112 -159 436 C
ATOM 3354 N TYR A 449 16.446 -0.871 26.431 1.00 29.74 N
ANISOU 3354 N TYR A 449 3401 3843 4054 -73 -96 375 N
ATOM 3355 CA TYR A 449 15.290 0.021 26.297 1.00 28.62 C
ANISOU 3355 CA TYR A 449 3275 3715 3884 -69 -86 368 C
ATOM 3356 C TYR A 449 14.744 0.062 24.852 1.00 28.74 C
ANISOU 3356 C TYR A 449 3297 3723 3899 -57 -76 351 C
ATOM 3357 O TYR A 449 15.471 0.395 23.904 1.00 27.88 O
ANISOU 3357 O TYR A 449 3193 3605 3794 -51 -66 337 O
ATOM 3358 CB TYR A 449 15.685 1.434 26.750 1.00 28.63 C
ANISOU 3358 CB TYR A 449 3288 3727 3863 -72 -78 365 C
ATOM 3359 CG TYR A 449 14.567 2.465 26.774 1.00 29.49 C
ANISOU 3359 CG TYR A 449 3410 3848 3944 -69 -69 359 C
ATOM 3360 CD1 TYR A 449 14.145 3.113 25.603 1.00 29.99 C
ANISOU 3360 CD1 TYR A 449 3485 3910 4000 -58 -57 342 C
ATOM 3361 CD2 TYR A 449 13.952 2.818 27.975 1.00 30.23 C
ANISOU 3361 CD2 TYR A 449 3506 3958 4022 -77 -71 369 C
ATOM 3362 CE1 TYR A 449 13.132 4.069 25.633 1.00 30.58 C
ANISOU 3362 CE1 TYR A 449 3570 3994 4052 -55 -50 337 C
ATOM 3363 CE2 TYR A 449 12.941 3.770 28.020 1.00 30.60 C
ANISOU 3363 CE2 TYR A 449 3563 4015 4047 -75 -62 362 C
ATOM 3364 CZ TYR A 449 12.532 4.394 26.849 1.00 31.12 C
ANISOU 3364 CZ TYR A 449 3639 4077 4108 -63 -52 346 C
ATOM 3365 OH TYR A 449 11.528 5.335 26.902 1.00 30.63 O
ANISOU 3365 OH TYR A 449 3585 4023 4028 -60 -44 340 O
ATOM 3366 N LEU A 450 13.460 -0.262 24.700 1.00 28.08 N
ANISOU 3366 N LEU A 450 3216 3644 3810 -54 -78 351 N
ATOM 3367 CA LEU A 450 12.809 -0.243 23.405 1.00 28.50 C
ANISOU 3367 CA LEU A 450 3277 3691 3861 -44 -71 337 C
ATOM 3368 C LEU A 450 11.429 0.394 23.479 1.00 29.53 C
ANISOU 3368 C LEU A 450 3417 3833 3971 -41 -69 336 C
ATOM 3369 O LEU A 450 10.540 -0.122 24.169 1.00 29.91 O
ANISOU 3369 O LEU A 450 3458 3886 4018 -44 -76 347 O
ATOM 3370 CB LEU A 450 12.692 -1.659 22.832 1.00 28.35 C
ANISOU 3370 CB LEU A 450 3246 3659 3866 -42 -79 337 C
ATOM 3371 CG LEU A 450 12.013 -1.781 21.459 1.00 28.03 C
ANISOU 3371 CG LEU A 450 3214 3611 3823 -33 -73 322 C
ATOM 3372 CD1 LEU A 450 12.702 -0.883 20.440 1.00 27.59 C
ANISOU 3372 CD1 LEU A 450 3172 3551 3758 -29 -59 305 C
ATOM 3373 CD2 LEU A 450 11.975 -3.221 20.961 1.00 27.24 C
ANISOU 3373 CD2 LEU A 450 3101 3497 3749 -31 -81 321 C
ATOM 3374 N ASP A 451 11.254 1.506 22.763 1.00 29.14 N
ANISOU 3374 N ASP A 451 3381 3784 3904 -35 -58 323 N
ATOM 3375 CA ASP A 451 9.950 2.146 22.647 1.00 29.04 C
ANISOU 3375 CA ASP A 451 3377 3779 3876 -31 -56 321 C
ATOM 3376 C ASP A 451 9.406 2.006 21.222 1.00 29.58 C
ANISOU 3376 C ASP A 451 3454 3838 3946 -23 -54 309 C
ATOM 3377 O ASP A 451 9.984 2.568 20.283 1.00 30.69 O
ANISOU 3377 O ASP A 451 3605 3973 4082 -20 -47 297 O
ATOM 3378 CB ASP A 451 10.027 3.624 23.050 1.00 29.32 C
ANISOU 3378 CB ASP A 451 3423 3823 3891 -32 -47 317 C
ATOM 3379 CG ASP A 451 8.647 4.233 23.340 1.00 30.34 C
ANISOU 3379 CG ASP A 451 3556 3961 4008 -30 -46 317 C
ATOM 3380 OD1 ASP A 451 7.621 3.625 22.932 1.00 29.66 O
ANISOU 3380 OD1 ASP A 451 3467 3872 3929 -26 -51 318 O
ATOM 3381 OD2 ASP A 451 8.591 5.315 23.985 1.00 29.15 O
ANISOU 3381 OD2 ASP A 451 3411 3820 3844 -32 -40 316 O
ATOM 3382 N ILE A 452 8.311 1.250 21.075 1.00 28.13 N
ANISOU 3382 N ILE A 452 3265 3652 3769 -21 -62 312 N
ATOM 3383 CA ILE A 452 7.571 1.133 19.804 1.00 27.62 C
ANISOU 3383 CA ILE A 452 3209 3580 3705 -14 -63 302 C
ATOM 3384 C ILE A 452 6.110 1.593 19.955 1.00 27.06 C
ANISOU 3384 C ILE A 452 3140 3514 3625 -11 -66 305 C
ATOM 3385 O ILE A 452 5.241 1.207 19.180 1.00 26.79 O
ANISOU 3385 O ILE A 452 3109 3474 3595 -7 -72 302 O
ATOM 3386 CB ILE A 452 7.606 -0.305 19.211 1.00 27.56 C
ANISOU 3386 CB ILE A 452 3193 3560 3716 -13 -70 302 C
ATOM 3387 CG1 ILE A 452 7.181 -1.335 20.255 1.00 27.20 C
ANISOU 3387 CG1 ILE A 452 3131 3519 3685 -18 -80 317 C
ATOM 3388 CG2 ILE A 452 8.980 -0.640 18.625 1.00 27.28 C
ANISOU 3388 CG2 ILE A 452 3158 3516 3691 -15 -64 294 C
ATOM 3389 CD1 ILE A 452 6.863 -2.696 19.674 1.00 27.77 C
ANISOU 3389 CD1 ILE A 452 3194 3579 3776 -16 -89 317 C
ATOM 3390 N SER A 453 5.852 2.414 20.967 1.00 27.19 N
ANISOU 3390 N SER A 453 3156 3542 3631 -14 -62 310 N
ATOM 3391 CA SER A 453 4.531 2.958 21.228 1.00 27.47 C
ANISOU 3391 CA SER A 453 3193 3583 3661 -12 -63 311 C
ATOM 3392 C SER A 453 4.007 3.829 20.081 1.00 28.54 C
ANISOU 3392 C SER A 453 3342 3712 3789 -5 -62 300 C
ATOM 3393 O SER A 453 4.759 4.592 19.479 1.00 28.86 O
ANISOU 3393 O SER A 453 3393 3750 3820 -4 -56 292 O
ATOM 3394 CB SER A 453 4.561 3.792 22.499 1.00 28.00 C
ANISOU 3394 CB SER A 453 3257 3663 3717 -17 -56 315 C
ATOM 3395 OG SER A 453 5.089 3.067 23.591 1.00 29.01 O
ANISOU 3395 OG SER A 453 3375 3798 3850 -26 -58 326 O
ATOM 3396 N TYR A 454 2.709 3.704 19.797 1.00 29.29 N
ANISOU 3396 N TYR A 454 3435 3804 3888 -1 -68 301 N
ATOM 3397 CA TYR A 454 2.005 4.513 18.791 1.00 29.75 C
ANISOU 3397 CA TYR A 454 3505 3856 3942 3 -71 293 C
ATOM 3398 C TYR A 454 2.686 4.469 17.436 1.00 30.78 C
ANISOU 3398 C TYR A 454 3648 3976 4068 5 -72 285 C
ATOM 3399 O TYR A 454 2.663 5.446 16.695 1.00 33.44 O
ANISOU 3399 O TYR A 454 3999 4309 4395 7 -71 278 O
ATOM 3400 CB TYR A 454 1.809 5.970 19.251 1.00 29.93 C
ANISOU 3400 CB TYR A 454 3531 3884 3953 4 -63 290 C
ATOM 3401 CG TYR A 454 1.453 6.086 20.711 1.00 31.13 C
ANISOU 3401 CG TYR A 454 3672 4049 4107 0 -58 296 C
ATOM 3402 CD1 TYR A 454 2.437 6.401 21.651 1.00 31.35 C
ANISOU 3402 CD1 TYR A 454 3698 4086 4127 -5 -49 298 C
ATOM 3403 CD2 TYR A 454 0.142 5.848 21.163 1.00 30.87 C
ANISOU 3403 CD2 TYR A 454 3628 4017 4082 1 -61 300 C
ATOM 3404 CE1 TYR A 454 2.139 6.488 22.996 1.00 32.20 C
ANISOU 3404 CE1 TYR A 454 3796 4205 4232 -11 -44 303 C
ATOM 3405 CE2 TYR A 454 -0.170 5.927 22.511 1.00 31.64 C
ANISOU 3405 CE2 TYR A 454 3715 4126 4178 -4 -54 305 C
ATOM 3406 CZ TYR A 454 0.835 6.246 23.426 1.00 33.48 C
ANISOU 3406 CZ TYR A 454 3949 4369 4401 -11 -45 306 C
ATOM 3407 OH TYR A 454 0.567 6.349 24.779 1.00 34.24 O
ANISOU 3407 OH TYR A 454 4037 4479 4494 -19 -38 311 O
ATOM 3408 N THR A 455 3.292 3.337 17.112 1.00 30.81 N
ANISOU 3408 N THR A 455 3649 3975 4080 3 -74 285 N
ATOM 3409 CA THR A 455 3.941 3.189 15.834 1.00 31.30 C
ANISOU 3409 CA THR A 455 3724 4028 4139 3 -73 275 C
ATOM 3410 C THR A 455 2.996 2.475 14.905 1.00 32.41 C
ANISOU 3410 C THR A 455 3868 4160 4287 5 -84 273 C
ATOM 3411 O THR A 455 3.313 2.214 13.741 1.00 32.81 O
ANISOU 3411 O THR A 455 3930 4202 4334 4 -85 265 O
ATOM 3412 CB THR A 455 5.253 2.407 15.948 1.00 30.92 C
ANISOU 3412 CB THR A 455 3670 3978 4098 0 -67 273 C
ATOM 3413 OG1 THR A 455 4.979 1.065 16.380 1.00 28.98 O
ANISOU 3413 OG1 THR A 455 3409 3731 3869 0 -74 280 O
ATOM 3414 CG2 THR A 455 6.181 3.116 16.915 1.00 30.35 C
ANISOU 3414 CG2 THR A 455 3596 3915 4021 -2 -58 276 C
ATOM 3415 N ASN A 456 1.830 2.143 15.439 1.00 35.00 N
ANISOU 3415 N ASN A 456 4185 4490 4623 7 -92 281 N
ATOM 3416 CA ASN A 456 0.752 1.602 14.629 1.00 36.62 C
ANISOU 3416 CA ASN A 456 4392 4686 4834 9 -104 280 C
ATOM 3417 C ASN A 456 1.026 0.188 14.144 1.00 35.45 C
ANISOU 3417 C ASN A 456 4240 4531 4698 8 -109 279 C
ATOM 3418 O ASN A 456 0.845 -0.117 12.960 1.00 36.96 O
ANISOU 3418 O ASN A 456 4442 4712 4887 7 -114 271 O
ATOM 3419 CB ASN A 456 0.499 2.511 13.425 1.00 38.31 C
ANISOU 3419 CB ASN A 456 4625 4893 5036 10 -108 273 C
ATOM 3420 CG ASN A 456 -0.807 2.205 12.758 1.00 42.78 C
ANISOU 3420 CG ASN A 456 5193 5451 5609 12 -122 275 C
ATOM 3421 OD1 ASN A 456 -0.914 2.144 11.519 1.00 42.36 O
ANISOU 3421 OD1 ASN A 456 5155 5389 5550 10 -129 268 O
ATOM 3422 ND2 ASN A 456 -1.831 1.982 13.585 1.00 46.60 N
ANISOU 3422 ND2 ASN A 456 5662 5938 6105 15 -127 283 N
ATOM 3423 N THR A 457 1.468 -0.672 15.054 1.00 33.47 N
ANISOU 3423 N THR A 457 3973 4284 4459 6 -106 285 N
ATOM 3424 CA THR A 457 1.872 -2.011 14.675 1.00 33.43 C
ANISOU 3424 CA THR A 457 3961 4270 4467 5 -110 283 C
ATOM 3425 C THR A 457 0.789 -3.016 15.032 1.00 34.26 C
ANISOU 3425 C THR A 457 4053 4373 4588 6 -121 292 C
ATOM 3426 O THR A 457 0.378 -3.140 16.186 1.00 33.79 O
ANISOU 3426 O THR A 457 3981 4323 4535 5 -123 303 O
ATOM 3427 CB THR A 457 3.237 -2.394 15.296 1.00 33.22 C
ANISOU 3427 CB THR A 457 3927 4246 4447 1 -101 284 C
ATOM 3428 OG1 THR A 457 4.221 -1.423 14.916 1.00 31.86 O
ANISOU 3428 OG1 THR A 457 3767 4075 4261 0 -90 275 O
ATOM 3429 CG2 THR A 457 3.681 -3.783 14.838 1.00 31.80 C
ANISOU 3429 CG2 THR A 457 3740 4056 4286 0 -105 280 C
ATOM 3430 N LYS A 458 0.307 -3.707 14.014 1.00 36.09 N
ANISOU 3430 N LYS A 458 4290 4596 4827 7 -130 286 N
ATOM 3431 CA LYS A 458 -0.537 -4.854 14.224 1.00 39.01 C
ANISOU 3431 CA LYS A 458 4645 4961 5214 8 -141 293 C
ATOM 3432 C LYS A 458 0.415 -6.057 14.353 1.00 40.11 C
ANISOU 3432 C LYS A 458 4774 5095 5369 5 -140 292 C
ATOM 3433 O LYS A 458 1.022 -6.496 13.360 1.00 40.01 O
ANISOU 3433 O LYS A 458 4769 5073 5358 4 -138 280 O
ATOM 3434 CB LYS A 458 -1.562 -4.985 13.082 1.00 39.96 C
ANISOU 3434 CB LYS A 458 4776 5072 5334 10 -152 288 C
ATOM 3435 CG LYS A 458 -2.058 -6.396 12.812 1.00 43.65 C
ANISOU 3435 CG LYS A 458 5233 5530 5820 10 -163 289 C
ATOM 3436 CD LYS A 458 -3.161 -6.835 13.760 1.00 43.69 C
ANISOU 3436 CD LYS A 458 5221 5539 5839 12 -171 304 C
ATOM 3437 CE LYS A 458 -4.470 -6.942 13.000 1.00 46.16 C
ANISOU 3437 CE LYS A 458 5538 5844 6155 14 -185 303 C
ATOM 3438 NZ LYS A 458 -4.347 -7.850 11.819 1.00 47.55 N
ANISOU 3438 NZ LYS A 458 5721 6007 6336 13 -192 293 N
ATOM 3439 N ILE A 459 0.568 -6.538 15.594 1.00 39.17 N
ANISOU 3439 N ILE A 459 4638 4983 5261 3 -140 305 N
ATOM 3440 CA ILE A 459 1.463 -7.649 15.937 1.00 39.11 C
ANISOU 3440 CA ILE A 459 4617 4970 5272 0 -141 308 C
ATOM 3441 C ILE A 459 0.864 -8.986 15.528 1.00 39.29 C
ANISOU 3441 C ILE A 459 4630 4982 5314 1 -153 309 C
ATOM 3442 O ILE A 459 -0.038 -9.495 16.192 1.00 39.82 O
ANISOU 3442 O ILE A 459 4686 5052 5391 1 -162 321 O
ATOM 3443 CB ILE A 459 1.720 -7.719 17.460 1.00 39.08 C
ANISOU 3443 CB ILE A 459 4598 4976 5273 -3 -141 324 C
ATOM 3444 CG1 ILE A 459 2.249 -6.385 18.003 1.00 39.14 C
ANISOU 3444 CG1 ILE A 459 4614 4995 5260 -5 -130 324 C
ATOM 3445 CG2 ILE A 459 2.627 -8.901 17.807 1.00 38.25 C
ANISOU 3445 CG2 ILE A 459 4478 4864 5190 -7 -145 329 C
ATOM 3446 CD1 ILE A 459 3.751 -6.288 18.104 1.00 39.97 C
ANISOU 3446 CD1 ILE A 459 4719 5099 5367 -8 -122 320 C
ATOM 3447 N ASP A 460 1.365 -9.554 14.440 1.00 40.27 N
ANISOU 3447 N ASP A 460 4760 5094 5446 1 -152 295 N
ATOM 3448 CA ASP A 460 0.917 -10.874 14.004 1.00 41.94 C
ANISOU 3448 CA ASP A 460 4963 5294 5678 2 -162 294 C
ATOM 3449 C ASP A 460 2.089 -11.837 13.793 1.00 42.16 C
ANISOU 3449 C ASP A 460 4981 5311 5726 0 -159 286 C
ATOM 3450 O ASP A 460 2.056 -12.705 12.922 1.00 44.32 O
ANISOU 3450 O ASP A 460 5254 5572 6012 0 -163 275 O
ATOM 3451 CB ASP A 460 -0.030 -10.805 12.785 1.00 45.57 C
ANISOU 3451 CB ASP A 460 5437 5747 6129 4 -168 283 C
ATOM 3452 CG ASP A 460 0.511 -9.946 11.622 1.00 49.12 C
ANISOU 3452 CG ASP A 460 5909 6195 6559 3 -158 266 C
ATOM 3453 OD1 ASP A 460 -0.008 -10.098 10.486 1.00 50.44 O
ANISOU 3453 OD1 ASP A 460 6089 6354 6721 3 -164 255 O
ATOM 3454 OD2 ASP A 460 1.425 -9.118 11.826 1.00 50.81 O
ANISOU 3454 OD2 ASP A 460 6129 6414 6760 2 -146 263 O
ATOM 3455 N PHE A 461 3.119 -11.679 14.619 1.00 41.01 N
ANISOU 3455 N PHE A 461 4827 5169 5584 -2 -153 292 N
ATOM 3456 CA PHE A 461 4.269 -12.562 14.598 1.00 40.46 C
ANISOU 3456 CA PHE A 461 4745 5088 5538 -4 -151 287 C
ATOM 3457 C PHE A 461 4.832 -12.749 16.012 1.00 40.24 C
ANISOU 3457 C PHE A 461 4700 5066 5522 -8 -155 305 C
ATOM 3458 O PHE A 461 5.402 -11.827 16.592 1.00 41.44 O
ANISOU 3458 O PHE A 461 4856 5228 5660 -10 -147 309 O
ATOM 3459 CB PHE A 461 5.313 -12.017 13.620 1.00 40.60 C
ANISOU 3459 CB PHE A 461 4776 5101 5547 -5 -135 266 C
ATOM 3460 CG PHE A 461 6.600 -12.790 13.602 1.00 41.87 C
ANISOU 3460 CG PHE A 461 4924 5250 5734 -7 -130 259 C
ATOM 3461 CD1 PHE A 461 7.828 -12.114 13.612 1.00 41.99 C
ANISOU 3461 CD1 PHE A 461 4943 5267 5745 -9 -117 252 C
ATOM 3462 CD2 PHE A 461 6.598 -14.184 13.570 1.00 41.64 C
ANISOU 3462 CD2 PHE A 461 4877 5207 5735 -7 -139 260 C
ATOM 3463 CE1 PHE A 461 9.025 -12.815 13.599 1.00 42.66 C
ANISOU 3463 CE1 PHE A 461 5014 5339 5857 -11 -112 245 C
ATOM 3464 CE2 PHE A 461 7.794 -14.888 13.562 1.00 43.57 C
ANISOU 3464 CE2 PHE A 461 5107 5439 6007 -9 -135 253 C
ATOM 3465 CZ PHE A 461 9.008 -14.205 13.573 1.00 43.12 C
ANISOU 3465 CZ PHE A 461 5053 5382 5946 -11 -121 245 C
ATOM 3466 N ASP A 462 4.654 -13.950 16.558 1.00 40.57 N
ANISOU 3466 N ASP A 462 4722 5101 5589 -10 -167 317 N
ATOM 3467 CA ASP A 462 5.096 -14.285 17.918 1.00 41.64 C
ANISOU 3467 CA ASP A 462 4840 5240 5737 -16 -175 337 C
ATOM 3468 C ASP A 462 6.579 -14.018 18.164 1.00 40.94 C
ANISOU 3468 C ASP A 462 4749 5149 5656 -19 -167 334 C
ATOM 3469 O ASP A 462 6.980 -13.724 19.290 1.00 41.13 O
ANISOU 3469 O ASP A 462 4767 5182 5678 -24 -170 350 O
ATOM 3470 CB ASP A 462 4.794 -15.754 18.239 1.00 42.84 C
ANISOU 3470 CB ASP A 462 4973 5382 5921 -18 -190 348 C
ATOM 3471 CG ASP A 462 3.340 -15.998 18.645 1.00 44.71 C
ANISOU 3471 CG ASP A 462 5208 5627 6153 -18 -201 361 C
ATOM 3472 OD1 ASP A 462 2.517 -15.046 18.655 1.00 43.42 O
ANISOU 3472 OD1 ASP A 462 5058 5476 5963 -16 -196 361 O
ATOM 3473 OD2 ASP A 462 3.023 -17.169 18.966 1.00 46.94 O
ANISOU 3473 OD2 ASP A 462 5475 5901 6459 -21 -214 372 O
ATOM 3474 N GLY A 463 7.388 -14.117 17.111 1.00 39.61 N
ANISOU 3474 N GLY A 463 4584 4968 5495 -16 -157 313 N
ATOM 3475 CA GLY A 463 8.829 -13.933 17.233 1.00 38.63 C
ANISOU 3475 CA GLY A 463 4455 4839 5382 -18 -149 308 C
ATOM 3476 C GLY A 463 9.331 -12.525 16.961 1.00 38.72 C
ANISOU 3476 C GLY A 463 4485 4860 5366 -17 -133 298 C
ATOM 3477 O GLY A 463 10.491 -12.343 16.580 1.00 39.10 O
ANISOU 3477 O GLY A 463 4532 4900 5421 -18 -123 286 O
ATOM 3478 N ILE A 464 8.465 -11.529 17.154 1.00 36.91 N
ANISOU 3478 N ILE A 464 4271 4647 5106 -16 -132 303 N
ATOM 3479 CA ILE A 464 8.833 -10.132 16.918 1.00 35.50 C
ANISOU 3479 CA ILE A 464 4110 4477 4900 -15 -118 295 C
ATOM 3480 C ILE A 464 9.942 -9.636 17.857 1.00 35.12 C
ANISOU 3480 C ILE A 464 4055 4433 4853 -20 -115 304 C
ATOM 3481 O ILE A 464 10.728 -8.781 17.479 1.00 34.88 O
ANISOU 3481 O ILE A 464 4034 4404 4811 -19 -102 293 O
ATOM 3482 CB ILE A 464 7.609 -9.178 16.942 1.00 34.85 C
ANISOU 3482 CB ILE A 464 4043 4409 4788 -13 -118 299 C
ATOM 3483 CG1 ILE A 464 8.012 -7.793 16.401 1.00 34.49 C
ANISOU 3483 CG1 ILE A 464 4017 4369 4717 -11 -104 287 C
ATOM 3484 CG2 ILE A 464 6.992 -9.103 18.337 1.00 34.25 C
ANISOU 3484 CG2 ILE A 464 3958 4346 4709 -16 -128 321 C
ATOM 3485 CD1 ILE A 464 6.909 -6.760 16.354 1.00 33.37 C
ANISOU 3485 CD1 ILE A 464 3889 4239 4548 -9 -104 289 C
ATOM 3486 N PHE A 465 10.016 -10.178 19.067 1.00 35.61 N
ANISOU 3486 N PHE A 465 4102 4499 4930 -25 -128 323 N
ATOM 3487 CA PHE A 465 11.016 -9.716 20.035 1.00 34.75 C
ANISOU 3487 CA PHE A 465 3987 4394 4821 -30 -127 334 C
ATOM 3488 C PHE A 465 12.133 -10.736 20.267 1.00 35.40 C
ANISOU 3488 C PHE A 465 4049 4460 4939 -34 -134 337 C
ATOM 3489 O PHE A 465 12.898 -10.623 21.223 1.00 35.47 O
ANISOU 3489 O PHE A 465 4049 4471 4955 -40 -140 350 O
ATOM 3490 CB PHE A 465 10.360 -9.301 21.358 1.00 32.66 C
ANISOU 3490 CB PHE A 465 3722 4146 4540 -36 -136 354 C
ATOM 3491 CG PHE A 465 9.345 -8.198 21.221 1.00 32.26 C
ANISOU 3491 CG PHE A 465 3689 4110 4457 -33 -128 351 C
ATOM 3492 CD1 PHE A 465 8.069 -8.331 21.778 1.00 32.34 C
ANISOU 3492 CD1 PHE A 465 3699 4130 4459 -34 -135 362 C
ATOM 3493 CD2 PHE A 465 9.651 -7.026 20.538 1.00 31.78 C
ANISOU 3493 CD2 PHE A 465 3644 4052 4376 -29 -113 336 C
ATOM 3494 CE1 PHE A 465 7.124 -7.317 21.659 1.00 31.43 C
ANISOU 3494 CE1 PHE A 465 3597 4026 4318 -31 -128 358 C
ATOM 3495 CE2 PHE A 465 8.706 -6.010 20.409 1.00 31.22 C
ANISOU 3495 CE2 PHE A 465 3589 3993 4279 -25 -108 333 C
ATOM 3496 CZ PHE A 465 7.444 -6.156 20.970 1.00 31.43 C
ANISOU 3496 CZ PHE A 465 3613 4028 4299 -26 -115 344 C
ATOM 3497 N LEU A 466 12.228 -11.723 19.382 1.00 36.12 N
ANISOU 3497 N LEU A 466 4133 4536 5055 -31 -134 325 N
ATOM 3498 CA LEU A 466 13.290 -12.714 19.441 1.00 36.97 C
ANISOU 3498 CA LEU A 466 4220 4625 5201 -33 -140 324 C
ATOM 3499 C LEU A 466 14.627 -11.972 19.376 1.00 38.00 C
ANISOU 3499 C LEU A 466 4352 4752 5332 -34 -128 316 C
ATOM 3500 O LEU A 466 14.810 -11.095 18.536 1.00 40.99 O
ANISOU 3500 O LEU A 466 4747 5135 5691 -31 -110 298 O
ATOM 3501 CB LEU A 466 13.138 -13.696 18.271 1.00 38.48 C
ANISOU 3501 CB LEU A 466 4406 4799 5413 -28 -137 306 C
ATOM 3502 CG LEU A 466 13.450 -15.209 18.328 1.00 39.71 C
ANISOU 3502 CG LEU A 466 4537 4935 5613 -30 -149 309 C
ATOM 3503 CD1 LEU A 466 13.647 -15.792 19.730 1.00 40.43 C
ANISOU 3503 CD1 LEU A 466 4609 5026 5724 -37 -170 337 C
ATOM 3504 CD2 LEU A 466 12.357 -15.977 17.590 1.00 37.71 C
ANISOU 3504 CD2 LEU A 466 4286 4677 5362 -26 -153 302 C
ATOM 3505 N GLY A 467 15.545 -12.284 20.286 1.00 36.81 N
ANISOU 3505 N GLY A 467 4184 4596 5204 -40 -138 330 N
ATOM 3506 CA GLY A 467 16.839 -11.606 20.323 1.00 34.68 C
ANISOU 3506 CA GLY A 467 3914 4323 4938 -42 -128 323 C
ATOM 3507 C GLY A 467 17.009 -10.642 21.487 1.00 34.70 C
ANISOU 3507 C GLY A 467 3922 4341 4918 -48 -133 341 C
ATOM 3508 O GLY A 467 18.143 -10.312 21.866 1.00 35.72 O
ANISOU 3508 O GLY A 467 4046 4467 5059 -52 -133 343 O
ATOM 3509 N LEU A 468 15.895 -10.203 22.071 1.00 33.15 N
ANISOU 3509 N LEU A 468 3737 4163 4692 -50 -138 354 N
ATOM 3510 CA LEU A 468 15.921 -9.113 23.047 1.00 32.53 C
ANISOU 3510 CA LEU A 468 3670 4103 4587 -55 -139 366 C
ATOM 3511 C LEU A 468 16.101 -9.606 24.481 1.00 32.64 C
ANISOU 3511 C LEU A 468 3669 4120 4612 -67 -160 393 C
ATOM 3512 O LEU A 468 15.354 -9.240 25.400 1.00 32.26 O
ANISOU 3512 O LEU A 468 3628 4089 4541 -73 -166 408 O
ATOM 3513 CB LEU A 468 14.689 -8.203 22.889 1.00 32.54 C
ANISOU 3513 CB LEU A 468 3691 4122 4550 -51 -131 363 C
ATOM 3514 CG LEU A 468 14.584 -7.417 21.564 1.00 32.83 C
ANISOU 3514 CG LEU A 468 3745 4158 4569 -42 -111 339 C
ATOM 3515 CD1 LEU A 468 13.236 -6.712 21.428 1.00 32.24 C
ANISOU 3515 CD1 LEU A 468 3687 4099 4463 -39 -107 338 C
ATOM 3516 CD2 LEU A 468 15.732 -6.429 21.379 1.00 31.54 C
ANISOU 3516 CD2 LEU A 468 3589 3995 4400 -43 -98 329 C
ATOM 3517 N THR A 469 17.139 -10.411 24.670 1.00 32.59 N
ANISOU 3517 N THR A 469 3644 4096 4642 -70 -170 398 N
ATOM 3518 CA THR A 469 17.327 -11.130 25.915 1.00 32.61 C
ANISOU 3518 CA THR A 469 3631 4097 4661 -82 -193 425 C
ATOM 3519 C THR A 469 17.809 -10.273 27.090 1.00 33.05 C
ANISOU 3519 C THR A 469 3693 4166 4698 -93 -199 441 C
ATOM 3520 O THR A 469 17.717 -10.690 28.252 1.00 34.05 O
ANISOU 3520 O THR A 469 3812 4297 4827 -106 -218 465 O
ATOM 3521 CB THR A 469 18.223 -12.367 25.717 1.00 33.36 C
ANISOU 3521 CB THR A 469 3702 4167 4806 -83 -205 426 C
ATOM 3522 OG1 THR A 469 19.447 -11.973 25.106 1.00 34.47 O
ANISOU 3522 OG1 THR A 469 3838 4295 4961 -79 -192 409 O
ATOM 3523 CG2 THR A 469 17.536 -13.401 24.811 1.00 33.42 C
ANISOU 3523 CG2 THR A 469 3702 4162 4831 -75 -204 415 C
ATOM 3524 N SER A 470 18.277 -9.060 26.812 1.00 32.20 N
ANISOU 3524 N SER A 470 3598 4065 4569 -89 -183 428 N
ATOM 3525 CA SER A 470 18.674 -8.155 27.896 1.00 32.22 C
ANISOU 3525 CA SER A 470 3609 4082 4551 -100 -187 441 C
ATOM 3526 C SER A 470 17.655 -7.056 28.191 1.00 31.65 C
ANISOU 3526 C SER A 470 3557 4033 4433 -100 -176 439 C
ATOM 3527 O SER A 470 17.807 -6.314 29.162 1.00 32.72 O
ANISOU 3527 O SER A 470 3700 4182 4548 -109 -179 450 O
ATOM 3528 CB SER A 470 20.052 -7.541 27.619 1.00 32.70 C
ANISOU 3528 CB SER A 470 3668 4133 4623 -98 -179 431 C
ATOM 3529 OG SER A 470 21.008 -8.557 27.407 1.00 33.49 O
ANISOU 3529 OG SER A 470 3745 4209 4767 -98 -189 432 O
ATOM 3530 N LEU A 471 16.614 -6.960 27.370 1.00 31.16 N
ANISOU 3530 N LEU A 471 3505 3976 4358 -90 -164 426 N
ATOM 3531 CA LEU A 471 15.631 -5.873 27.488 1.00 30.94 C
ANISOU 3531 CA LEU A 471 3496 3967 4291 -88 -152 421 C
ATOM 3532 C LEU A 471 15.054 -5.715 28.894 1.00 30.43 C
ANISOU 3532 C LEU A 471 3434 3920 4207 -102 -162 442 C
ATOM 3533 O LEU A 471 14.677 -6.702 29.512 1.00 30.76 O
ANISOU 3533 O LEU A 471 3465 3960 4261 -110 -178 459 O
ATOM 3534 CB LEU A 471 14.507 -6.059 26.456 1.00 29.67 C
ANISOU 3534 CB LEU A 471 3341 3805 4124 -77 -143 408 C
ATOM 3535 CG LEU A 471 13.634 -4.843 26.128 1.00 29.02 C
ANISOU 3535 CG LEU A 471 3278 3738 4008 -71 -128 396 C
ATOM 3536 CD1 LEU A 471 14.438 -3.722 25.478 1.00 28.11 C
ANISOU 3536 CD1 LEU A 471 3175 3622 3884 -66 -113 380 C
ATOM 3537 CD2 LEU A 471 12.466 -5.265 25.247 1.00 28.48 C
ANISOU 3537 CD2 LEU A 471 3213 3667 3940 -62 -125 387 C
ATOM 3538 N ASN A 472 15.022 -4.480 29.391 1.00 30.80 N
ANISOU 3538 N ASN A 472 3495 3982 4224 -105 -154 440 N
ATOM 3539 CA ASN A 472 14.327 -4.149 30.642 1.00 32.41 C
ANISOU 3539 CA ASN A 472 3705 4204 4404 -118 -158 455 C
ATOM 3540 C ASN A 472 13.014 -3.434 30.390 1.00 32.96 C
ANISOU 3540 C ASN A 472 3787 4287 4447 -112 -143 444 C
ATOM 3541 O ASN A 472 11.990 -3.760 30.986 1.00 33.67 O
ANISOU 3541 O ASN A 472 3877 4387 4528 -118 -147 454 O
ATOM 3542 CB ASN A 472 15.152 -3.204 31.514 1.00 32.95 C
ANISOU 3542 CB ASN A 472 3780 4282 4456 -128 -158 460 C
ATOM 3543 CG ASN A 472 16.448 -3.807 31.981 1.00 34.40 C
ANISOU 3543 CG ASN A 472 3951 4454 4665 -137 -175 473 C
ATOM 3544 OD1 ASN A 472 16.592 -5.029 32.080 1.00 35.80 O
ANISOU 3544 OD1 ASN A 472 4113 4619 4868 -141 -191 486 O
ATOM 3545 ND2 ASN A 472 17.409 -2.943 32.284 1.00 35.17 N
ANISOU 3545 ND2 ASN A 472 4054 4552 4755 -141 -172 472 N
ATOM 3546 N THR A 473 13.072 -2.422 29.531 1.00 32.45 N
ANISOU 3546 N THR A 473 3734 4222 4371 -100 -127 425 N
ATOM 3547 CA THR A 473 11.967 -1.515 29.351 1.00 32.26 C
ANISOU 3547 CA THR A 473 3723 4210 4322 -95 -114 415 C
ATOM 3548 C THR A 473 11.404 -1.652 27.952 1.00 32.51 C
ANISOU 3548 C THR A 473 3758 4233 4362 -80 -107 399 C
ATOM 3549 O THR A 473 12.071 -1.367 26.955 1.00 33.00 O
ANISOU 3549 O THR A 473 3823 4284 4429 -71 -100 385 O
ATOM 3550 CB THR A 473 12.384 -0.064 29.637 1.00 31.91 C
ANISOU 3550 CB THR A 473 3692 4176 4256 -96 -102 407 C
ATOM 3551 OG1 THR A 473 12.953 0.005 30.942 1.00 31.73 O
ANISOU 3551 OG1 THR A 473 3667 4161 4226 -112 -111 422 O
ATOM 3552 CG2 THR A 473 11.183 0.860 29.599 1.00 32.60 C
ANISOU 3552 CG2 THR A 473 3789 4275 4320 -92 -90 397 C
ATOM 3553 N LEU A 474 10.161 -2.103 27.897 1.00 31.75 N
ANISOU 3553 N LEU A 474 3659 4139 4263 -78 -108 401 N
ATOM 3554 CA LEU A 474 9.452 -2.191 26.651 1.00 31.40 C
ANISOU 3554 CA LEU A 474 3618 4087 4223 -65 -103 387 C
ATOM 3555 C LEU A 474 8.168 -1.381 26.746 1.00 30.93 C
ANISOU 3555 C LEU A 474 3568 4039 4143 -63 -95 382 C
ATOM 3556 O LEU A 474 7.236 -1.749 27.464 1.00 31.62 O
ANISOU 3556 O LEU A 474 3650 4134 4227 -68 -99 392 O
ATOM 3557 CB LEU A 474 9.191 -3.651 26.299 1.00 31.54 C
ANISOU 3557 CB LEU A 474 3624 4094 4265 -64 -114 393 C
ATOM 3558 CG LEU A 474 8.414 -4.010 25.035 1.00 32.32 C
ANISOU 3558 CG LEU A 474 3724 4183 4370 -52 -112 381 C
ATOM 3559 CD1 LEU A 474 8.878 -3.226 23.814 1.00 32.24 C
ANISOU 3559 CD1 LEU A 474 3727 4167 4355 -43 -101 361 C
ATOM 3560 CD2 LEU A 474 8.555 -5.505 24.809 1.00 33.18 C
ANISOU 3560 CD2 LEU A 474 3819 4279 4507 -53 -125 387 C
ATOM 3561 N LYS A 475 8.155 -0.254 26.042 1.00 30.63 N
ANISOU 3561 N LYS A 475 3543 4002 4093 -55 -83 368 N
ATOM 3562 CA LYS A 475 6.953 0.554 25.847 1.00 29.48 C
ANISOU 3562 CA LYS A 475 3405 3862 3932 -50 -76 360 C
ATOM 3563 C LYS A 475 6.385 0.255 24.457 1.00 29.15 C
ANISOU 3563 C LYS A 475 3366 3808 3898 -38 -77 350 C
ATOM 3564 O LYS A 475 7.063 0.461 23.443 1.00 27.94 O
ANISOU 3564 O LYS A 475 3220 3646 3747 -32 -74 339 O
ATOM 3565 CB LYS A 475 7.291 2.036 25.966 1.00 28.72 C
ANISOU 3565 CB LYS A 475 3321 3773 3818 -49 -65 351 C
ATOM 3566 CG LYS A 475 7.911 2.415 27.287 1.00 28.57 C
ANISOU 3566 CG LYS A 475 3301 3766 3789 -61 -63 360 C
ATOM 3567 CD LYS A 475 8.316 3.874 27.313 1.00 28.85 C
ANISOU 3567 CD LYS A 475 3348 3806 3807 -59 -52 350 C
ATOM 3568 CE LYS A 475 9.116 4.138 28.580 1.00 30.13 C
ANISOU 3568 CE LYS A 475 3508 3978 3960 -72 -53 359 C
ATOM 3569 NZ LYS A 475 9.289 5.579 28.910 1.00 30.07 N
ANISOU 3569 NZ LYS A 475 3511 3978 3934 -73 -42 351 N
ATOM 3570 N MET A 476 5.159 -0.264 24.423 1.00 29.40 N
ANISOU 3570 N MET A 476 3393 3840 3935 -37 -81 353 N
ATOM 3571 CA MET A 476 4.471 -0.564 23.161 1.00 30.29 C
ANISOU 3571 CA MET A 476 3510 3943 4055 -27 -84 344 C
ATOM 3572 C MET A 476 2.976 -0.216 23.249 1.00 30.65 C
ANISOU 3572 C MET A 476 3556 3993 4096 -24 -84 344 C
ATOM 3573 O MET A 476 2.105 -0.918 22.710 1.00 30.71 O
ANISOU 3573 O MET A 476 3559 3993 4114 -20 -91 344 O
ATOM 3574 CB MET A 476 4.693 -2.019 22.742 1.00 30.82 C
ANISOU 3574 CB MET A 476 3567 3999 4143 -27 -94 348 C
ATOM 3575 CG MET A 476 4.244 -3.045 23.768 1.00 32.55 C
ANISOU 3575 CG MET A 476 3771 4223 4373 -34 -103 364 C
ATOM 3576 SD MET A 476 4.664 -4.740 23.320 1.00 34.99 S
ANISOU 3576 SD MET A 476 4067 4517 4710 -34 -116 369 S
ATOM 3577 CE MET A 476 3.668 -4.942 21.841 1.00 36.88 C
ANISOU 3577 CE MET A 476 4313 4745 4953 -23 -118 356 C
ATOM 3578 N ALA A 477 2.693 0.886 23.931 1.00 30.07 N
ANISOU 3578 N ALA A 477 3486 3930 4008 -27 -75 342 N
ATOM 3579 CA ALA A 477 1.339 1.390 24.035 1.00 30.57 C
ANISOU 3579 CA ALA A 477 3549 3996 4069 -24 -73 340 C
ATOM 3580 C ALA A 477 0.789 1.811 22.661 1.00 30.80 C
ANISOU 3580 C ALA A 477 3587 4014 4100 -13 -75 329 C
ATOM 3581 O ALA A 477 1.545 2.214 21.775 1.00 30.26 O
ANISOU 3581 O ALA A 477 3530 3940 4027 -9 -74 321 O
ATOM 3582 CB ALA A 477 1.291 2.546 25.019 1.00 29.37 C
ANISOU 3582 CB ALA A 477 3399 3857 3901 -29 -62 339 C
ATOM 3583 N GLY A 478 -0.525 1.685 22.484 1.00 30.15 N
ANISOU 3583 N GLY A 478 3500 3929 4024 -10 -79 329 N
ATOM 3584 CA GLY A 478 -1.190 2.247 21.317 1.00 30.31 C
ANISOU 3584 CA GLY A 478 3530 3940 4046 -1 -83 320 C
ATOM 3585 C GLY A 478 -0.937 1.543 19.995 1.00 31.09 C
ANISOU 3585 C GLY A 478 3635 4026 4151 2 -92 316 C
ATOM 3586 O GLY A 478 -0.869 2.187 18.939 1.00 32.70 O
ANISOU 3586 O GLY A 478 3852 4222 4349 6 -94 308 O
ATOM 3587 N ASN A 479 -0.804 0.224 20.056 1.00 29.73 N
ANISOU 3587 N ASN A 479 3454 3850 3990 0 -99 323 N
ATOM 3588 CA ASN A 479 -0.687 -0.608 18.875 1.00 29.48 C
ANISOU 3588 CA ASN A 479 3427 3807 3967 3 -107 318 C
ATOM 3589 C ASN A 479 -1.867 -1.591 18.888 1.00 29.86 C
ANISOU 3589 C ASN A 479 3463 3850 4030 4 -118 325 C
ATOM 3590 O ASN A 479 -2.981 -1.209 19.259 1.00 30.78 O
ANISOU 3590 O ASN A 479 3575 3970 4149 5 -119 328 O
ATOM 3591 CB ASN A 479 0.680 -1.327 18.842 1.00 29.48 C
ANISOU 3591 CB ASN A 479 3425 3804 3970 0 -106 318 C
ATOM 3592 CG ASN A 479 1.859 -0.365 18.694 1.00 29.77 C
ANISOU 3592 CG ASN A 479 3473 3844 3993 0 -95 311 C
ATOM 3593 OD1 ASN A 479 2.011 0.294 17.667 1.00 31.33 O
ANISOU 3593 OD1 ASN A 479 3685 4036 4182 2 -93 300 O
ATOM 3594 ND2 ASN A 479 2.704 -0.294 19.714 1.00 28.86 N
ANISOU 3594 ND2 ASN A 479 3352 3737 3876 -6 -90 317 N
ATOM 3595 N SER A 480 -1.633 -2.842 18.501 1.00 30.60 N
ANISOU 3595 N SER A 480 3552 3937 4137 3 -126 326 N
ATOM 3596 CA SER A 480 -2.686 -3.870 18.464 1.00 31.31 C
ANISOU 3596 CA SER A 480 3631 4022 4243 4 -137 333 C
ATOM 3597 C SER A 480 -2.125 -5.259 18.133 1.00 30.85 C
ANISOU 3597 C SER A 480 3566 3955 4198 3 -143 334 C
ATOM 3598 O SER A 480 -0.953 -5.400 17.791 1.00 30.21 O
ANISOU 3598 O SER A 480 3490 3871 4117 2 -139 328 O
ATOM 3599 CB SER A 480 -3.792 -3.488 17.464 1.00 31.48 C
ANISOU 3599 CB SER A 480 3660 4035 4264 10 -144 327 C
ATOM 3600 OG SER A 480 -3.248 -3.211 16.179 1.00 31.66 O
ANISOU 3600 OG SER A 480 3700 4049 4279 12 -145 315 O
ATOM 3601 N PHE A 481 -2.976 -6.274 18.238 1.00 31.71 N
ANISOU 3601 N PHE A 481 3663 4060 4323 3 -153 341 N
ATOM 3602 CA PHE A 481 -2.588 -7.668 18.044 1.00 32.83 C
ANISOU 3602 CA PHE A 481 3797 4194 4483 1 -161 344 C
ATOM 3603 C PHE A 481 -3.598 -8.370 17.169 1.00 33.70 C
ANISOU 3603 C PHE A 481 3906 4293 4605 5 -173 341 C
ATOM 3604 O PHE A 481 -4.787 -8.066 17.225 1.00 35.38 O
ANISOU 3604 O PHE A 481 4118 4507 4817 7 -177 344 O
ATOM 3605 CB PHE A 481 -2.525 -8.392 19.398 1.00 33.65 C
ANISOU 3605 CB PHE A 481 3883 4305 4597 -5 -163 360 C
ATOM 3606 CG PHE A 481 -1.299 -8.067 20.208 1.00 33.60 C
ANISOU 3606 CG PHE A 481 3875 4306 4583 -10 -155 364 C
ATOM 3607 CD1 PHE A 481 -1.215 -6.877 20.926 1.00 32.79 C
ANISOU 3607 CD1 PHE A 481 3778 4216 4463 -13 -145 365 C
ATOM 3608 CD2 PHE A 481 -0.226 -8.953 20.251 1.00 32.89 C
ANISOU 3608 CD2 PHE A 481 3779 4210 4507 -13 -158 366 C
ATOM 3609 CE1 PHE A 481 -0.080 -6.574 21.669 1.00 33.07 C
ANISOU 3609 CE1 PHE A 481 3814 4259 4492 -18 -139 369 C
ATOM 3610 CE2 PHE A 481 0.906 -8.653 20.991 1.00 33.23 C
ANISOU 3610 CE2 PHE A 481 3820 4259 4545 -19 -153 370 C
ATOM 3611 CZ PHE A 481 0.980 -7.463 21.700 1.00 33.01 C
ANISOU 3611 CZ PHE A 481 3799 4244 4497 -22 -143 372 C
ATOM 3612 N LYS A 482 -3.133 -9.318 16.367 1.00 35.60 N
ANISOU 3612 N LYS A 482 4147 4522 4856 6 -179 335 N
ATOM 3613 CA LYS A 482 -4.030 -10.204 15.624 1.00 37.70 C
ANISOU 3613 CA LYS A 482 4410 4776 5135 8 -191 333 C
ATOM 3614 C LYS A 482 -5.131 -10.756 16.545 1.00 38.68 C
ANISOU 3614 C LYS A 482 4518 4905 5274 7 -199 348 C
ATOM 3615 O LYS A 482 -4.849 -11.256 17.650 1.00 38.62 O
ANISOU 3615 O LYS A 482 4496 4903 5274 2 -198 361 O
ATOM 3616 CB LYS A 482 -3.216 -11.338 15.010 1.00 39.00 C
ANISOU 3616 CB LYS A 482 4573 4930 5315 7 -194 326 C
ATOM 3617 CG LYS A 482 -4.019 -12.400 14.290 1.00 42.74 C
ANISOU 3617 CG LYS A 482 5042 5390 5804 8 -208 324 C
ATOM 3618 CD LYS A 482 -3.113 -13.550 13.885 1.00 46.52 C
ANISOU 3618 CD LYS A 482 5515 5858 6301 7 -209 317 C
ATOM 3619 CE LYS A 482 -3.868 -14.872 13.858 1.00 51.10 C
ANISOU 3619 CE LYS A 482 6081 6429 6905 7 -223 323 C
ATOM 3620 NZ LYS A 482 -2.956 -16.010 14.185 1.00 53.27 N
ANISOU 3620 NZ LYS A 482 6340 6696 7202 4 -224 324 N
ATOM 3621 N ASP A 483 -6.381 -10.635 16.099 1.00 39.07 N
ANISOU 3621 N ASP A 483 4569 4950 5325 10 -207 348 N
ATOM 3622 CA ASP A 483 -7.562 -11.081 16.868 1.00 37.77 C
ANISOU 3622 CA ASP A 483 4389 4788 5173 9 -213 361 C
ATOM 3623 C ASP A 483 -7.613 -10.519 18.285 1.00 35.97 C
ANISOU 3623 C ASP A 483 4152 4576 4939 5 -203 373 C
ATOM 3624 O ASP A 483 -8.222 -11.107 19.174 1.00 35.94 O
ANISOU 3624 O ASP A 483 4132 4575 4945 0 -206 385 O
ATOM 3625 CB ASP A 483 -7.673 -12.613 16.890 1.00 39.53 C
ANISOU 3625 CB ASP A 483 4598 5002 5418 7 -225 368 C
ATOM 3626 CG ASP A 483 -7.775 -13.218 15.491 1.00 44.72 C
ANISOU 3626 CG ASP A 483 5263 5644 6083 11 -235 356 C
ATOM 3627 OD1 ASP A 483 -8.380 -12.583 14.595 1.00 47.31 O
ANISOU 3627 OD1 ASP A 483 5604 5967 6402 15 -239 347 O
ATOM 3628 OD2 ASP A 483 -7.245 -14.334 15.282 1.00 46.63 O
ANISOU 3628 OD2 ASP A 483 5499 5878 6340 10 -240 355 O
ATOM 3629 N ASN A 484 -6.975 -9.374 18.487 1.00 35.20 N
ANISOU 3629 N ASN A 484 4064 4486 4822 4 -191 367 N
ATOM 3630 CA ASN A 484 -6.949 -8.694 19.790 1.00 36.15 C
ANISOU 3630 CA ASN A 484 4179 4622 4933 0 -180 375 C
ATOM 3631 C ASN A 484 -6.636 -9.592 20.983 1.00 36.33 C
ANISOU 3631 C ASN A 484 4187 4652 4964 -9 -180 390 C
ATOM 3632 O ASN A 484 -7.053 -9.316 22.117 1.00 35.99 O
ANISOU 3632 O ASN A 484 4136 4620 4916 -15 -174 399 O
ATOM 3633 CB ASN A 484 -8.242 -7.904 20.055 1.00 35.75 C
ANISOU 3633 CB ASN A 484 4126 4575 4881 1 -177 376 C
ATOM 3634 CG ASN A 484 -8.593 -6.937 18.937 1.00 35.21 C
ANISOU 3634 CG ASN A 484 4072 4499 4806 9 -179 363 C
ATOM 3635 OD1 ASN A 484 -9.739 -6.880 18.530 1.00 36.29 O
ANISOU 3635 OD1 ASN A 484 4207 4629 4952 12 -186 363 O
ATOM 3636 ND2 ASN A 484 -7.617 -6.180 18.439 1.00 34.33 N
ANISOU 3636 ND2 ASN A 484 3976 4388 4679 10 -173 354 N
ATOM 3637 N THR A 485 -5.911 -10.673 20.714 1.00 36.18 N
ANISOU 3637 N THR A 485 4164 4625 4958 -10 -188 392 N
ATOM 3638 CA THR A 485 -5.365 -11.510 21.771 1.00 36.13 C
ANISOU 3638 CA THR A 485 4144 4623 4959 -19 -191 407 C
ATOM 3639 C THR A 485 -3.847 -11.273 21.958 1.00 36.28 C
ANISOU 3639 C THR A 485 4168 4644 4971 -22 -185 405 C
ATOM 3640 O THR A 485 -3.079 -11.284 20.996 1.00 37.59 O
ANISOU 3640 O THR A 485 4342 4801 5139 -17 -185 393 O
ATOM 3641 CB THR A 485 -5.743 -13.019 21.616 1.00 35.98 C
ANISOU 3641 CB THR A 485 4111 4592 4964 -20 -205 415 C
ATOM 3642 OG1 THR A 485 -4.626 -13.842 21.980 1.00 36.34 O
ANISOU 3642 OG1 THR A 485 4150 4636 5022 -26 -210 422 O
ATOM 3643 CG2 THR A 485 -6.179 -13.378 20.203 1.00 33.76 C
ANISOU 3643 CG2 THR A 485 3836 4297 4693 -11 -213 402 C
ATOM 3644 N LEU A 486 -3.447 -11.012 23.202 1.00 35.95 N
ANISOU 3644 N LEU A 486 4122 4615 4921 -31 -180 416 N
ATOM 3645 CA LEU A 486 -2.047 -10.857 23.588 1.00 34.72 C
ANISOU 3645 CA LEU A 486 3969 4462 4761 -36 -177 418 C
ATOM 3646 C LEU A 486 -1.318 -12.183 23.492 1.00 35.29 C
ANISOU 3646 C LEU A 486 4029 4522 4855 -39 -189 424 C
ATOM 3647 O LEU A 486 -1.427 -13.017 24.390 1.00 35.99 O
ANISOU 3647 O LEU A 486 4105 4613 4955 -48 -197 441 O
ATOM 3648 CB LEU A 486 -1.962 -10.326 25.016 1.00 34.46 C
ANISOU 3648 CB LEU A 486 3933 4445 4713 -48 -170 430 C
ATOM 3649 CG LEU A 486 -0.585 -10.042 25.619 1.00 36.10 C
ANISOU 3649 CG LEU A 486 4143 4658 4914 -54 -168 434 C
ATOM 3650 CD1 LEU A 486 0.180 -8.995 24.820 1.00 36.50 C
ANISOU 3650 CD1 LEU A 486 4209 4707 4953 -46 -158 417 C
ATOM 3651 CD2 LEU A 486 -0.747 -9.594 27.063 1.00 35.92 C
ANISOU 3651 CD2 LEU A 486 4119 4653 4875 -68 -163 447 C
ATOM 3652 N SER A 487 -0.572 -12.369 22.405 1.00 35.34 N
ANISOU 3652 N SER A 487 4041 4515 4870 -32 -189 410 N
ATOM 3653 CA SER A 487 0.087 -13.642 22.117 1.00 36.11 C
ANISOU 3653 CA SER A 487 4126 4598 4993 -32 -200 412 C
ATOM 3654 C SER A 487 1.442 -13.828 22.823 1.00 36.82 C
ANISOU 3654 C SER A 487 4210 4688 5091 -40 -201 420 C
ATOM 3655 O SER A 487 1.974 -12.891 23.408 1.00 36.32 O
ANISOU 3655 O SER A 487 4153 4635 5009 -43 -193 422 O
ATOM 3656 CB SER A 487 0.231 -13.820 20.607 1.00 37.17 C
ANISOU 3656 CB SER A 487 4269 4718 5135 -23 -198 392 C
ATOM 3657 OG SER A 487 0.873 -12.707 20.019 1.00 39.36 O
ANISOU 3657 OG SER A 487 4562 4998 5394 -19 -186 377 O
ATOM 3658 N ASN A 488 1.985 -15.047 22.764 1.00 39.07 N
ANISOU 3658 N ASN A 488 4481 4960 5403 -42 -212 425 N
ATOM 3659 CA ASN A 488 3.237 -15.415 23.454 1.00 40.79 C
ANISOU 3659 CA ASN A 488 4688 5173 5634 -49 -218 435 C
ATOM 3660 C ASN A 488 4.483 -14.810 22.767 1.00 39.90 C
ANISOU 3660 C ASN A 488 4583 5054 5520 -44 -207 418 C
ATOM 3661 O ASN A 488 5.244 -15.509 22.093 1.00 40.97 O
ANISOU 3661 O ASN A 488 4712 5174 5680 -41 -209 409 O
ATOM 3662 CB ASN A 488 3.319 -16.956 23.638 1.00 40.79 C
ANISOU 3662 CB ASN A 488 4668 5160 5669 -53 -235 447 C
ATOM 3663 CG ASN A 488 4.692 -17.443 24.124 1.00 43.26 C
ANISOU 3663 CG ASN A 488 4968 5463 6002 -60 -243 455 C
ATOM 3664 OD1 ASN A 488 5.251 -16.935 25.104 1.00 43.75 O
ANISOU 3664 OD1 ASN A 488 5032 5536 6055 -69 -243 467 O
ATOM 3665 ND2 ASN A 488 5.235 -18.450 23.436 1.00 41.94 N
ANISOU 3665 ND2 ASN A 488 4790 5276 5868 -56 -249 447 N
ATOM 3666 N VAL A 489 4.667 -13.501 22.934 1.00 38.55 N
ANISOU 3666 N VAL A 489 4427 4897 5322 -44 -194 413 N
ATOM 3667 CA VAL A 489 5.773 -12.781 22.300 1.00 38.35 C
ANISOU 3667 CA VAL A 489 4411 4867 5291 -40 -183 397 C
ATOM 3668 C VAL A 489 6.903 -12.478 23.264 1.00 39.03 C
ANISOU 3668 C VAL A 489 4493 4958 5378 -48 -183 407 C
ATOM 3669 O VAL A 489 7.947 -11.993 22.834 1.00 40.89 O
ANISOU 3669 O VAL A 489 4733 5189 5614 -46 -175 396 O
ATOM 3670 CB VAL A 489 5.333 -11.455 21.607 1.00 39.39 C
ANISOU 3670 CB VAL A 489 4563 5008 5394 -33 -168 381 C
ATOM 3671 CG1 VAL A 489 4.359 -11.729 20.462 1.00 38.82 C
ANISOU 3671 CG1 VAL A 489 4497 4929 5322 -25 -168 369 C
ATOM 3672 CG2 VAL A 489 4.759 -10.450 22.604 1.00 37.03 C
ANISOU 3672 CG2 VAL A 489 4270 4727 5069 -38 -164 391 C
ATOM 3673 N PHE A 490 6.691 -12.763 24.552 1.00 40.25 N
ANISOU 3673 N PHE A 490 4638 5121 5532 -59 -194 429 N
ATOM 3674 CA PHE A 490 7.643 -12.405 25.610 1.00 39.87 C
ANISOU 3674 CA PHE A 490 4588 5080 5481 -69 -197 442 C
ATOM 3675 C PHE A 490 8.375 -13.586 26.233 1.00 41.12 C
ANISOU 3675 C PHE A 490 4727 5227 5670 -78 -215 459 C
ATOM 3676 O PHE A 490 8.941 -13.450 27.323 1.00 41.73 O
ANISOU 3676 O PHE A 490 4800 5310 5744 -89 -223 476 O
ATOM 3677 CB PHE A 490 6.965 -11.643 26.752 1.00 38.53 C
ANISOU 3677 CB PHE A 490 4424 4930 5282 -78 -195 455 C
ATOM 3678 CG PHE A 490 6.081 -10.520 26.312 1.00 38.17 C
ANISOU 3678 CG PHE A 490 4396 4896 5209 -71 -180 442 C
ATOM 3679 CD1 PHE A 490 6.620 -9.355 25.784 1.00 36.77 C
ANISOU 3679 CD1 PHE A 490 4232 4722 5016 -64 -165 426 C
ATOM 3680 CD2 PHE A 490 4.698 -10.617 26.464 1.00 36.83 C
ANISOU 3680 CD2 PHE A 490 4227 4734 5031 -71 -180 446 C
ATOM 3681 CE1 PHE A 490 5.790 -8.319 25.393 1.00 36.25 C
ANISOU 3681 CE1 PHE A 490 4180 4664 4926 -58 -153 414 C
ATOM 3682 CE2 PHE A 490 3.871 -9.583 26.080 1.00 36.10 C
ANISOU 3682 CE2 PHE A 490 4147 4650 4917 -64 -167 434 C
ATOM 3683 CZ PHE A 490 4.417 -8.433 25.543 1.00 35.67 C
ANISOU 3683 CZ PHE A 490 4107 4598 4848 -58 -154 418 C
ATOM 3684 N ALA A 491 8.377 -14.730 25.555 1.00 42.29 N
ANISOU 3684 N ALA A 491 4862 5356 5847 -73 -223 455 N
ATOM 3685 CA ALA A 491 9.022 -15.939 26.088 1.00 45.52 C
ANISOU 3685 CA ALA A 491 5250 5752 6291 -81 -242 471 C
ATOM 3686 C ALA A 491 10.522 -15.755 26.395 1.00 48.29 C
ANISOU 3686 C ALA A 491 5596 6095 6656 -85 -244 473 C
ATOM 3687 O ALA A 491 11.013 -16.238 27.416 1.00 50.63 O
ANISOU 3687 O ALA A 491 5880 6390 6966 -97 -261 495 O
ATOM 3688 CB ALA A 491 8.803 -17.117 25.144 1.00 43.66 C
ANISOU 3688 CB ALA A 491 5003 5497 6087 -73 -247 462 C
ATOM 3689 N ASN A 492 11.234 -15.053 25.514 1.00 50.71 N
ANISOU 3689 N ASN A 492 5911 6397 6959 -76 -228 451 N
ATOM 3690 CA ASN A 492 12.674 -14.823 25.666 1.00 53.45 C
ANISOU 3690 CA ASN A 492 6252 6736 7321 -79 -228 450 C
ATOM 3691 C ASN A 492 13.080 -13.471 26.277 1.00 50.43 C
ANISOU 3691 C ASN A 492 5883 6369 6906 -83 -219 452 C
ATOM 3692 O ASN A 492 14.261 -13.263 26.557 1.00 53.11 O
ANISOU 3692 O ASN A 492 6217 6702 7257 -87 -221 454 O
ATOM 3693 CB ASN A 492 13.396 -15.014 24.316 1.00 59.91 C
ANISOU 3693 CB ASN A 492 7067 7535 8160 -68 -215 424 C
ATOM 3694 CG ASN A 492 13.761 -16.466 24.034 1.00 65.21 C
ANISOU 3694 CG ASN A 492 7715 8182 8877 -67 -228 425 C
ATOM 3695 OD1 ASN A 492 13.012 -17.391 24.366 1.00 67.95 O
ANISOU 3695 OD1 ASN A 492 8053 8527 9236 -70 -243 438 O
ATOM 3696 ND2 ASN A 492 14.916 -16.671 23.402 1.00 66.71 N
ANISOU 3696 ND2 ASN A 492 7896 8355 9095 -63 -222 409 N
ATOM 3697 N THR A 493 12.132 -12.551 26.470 1.00 46.53 N
ANISOU 3697 N THR A 493 5408 5896 6376 -83 -210 451 N
ATOM 3698 CA THR A 493 12.474 -11.237 27.042 1.00 44.77 C
ANISOU 3698 CA THR A 493 5198 5688 6123 -87 -201 452 C
ATOM 3699 C THR A 493 12.418 -11.316 28.553 1.00 42.20 C
ANISOU 3699 C THR A 493 4869 5374 5789 -103 -216 478 C
ATOM 3700 O THR A 493 11.531 -10.756 29.190 1.00 45.73 O
ANISOU 3700 O THR A 493 5326 5839 6207 -109 -212 485 O
ATOM 3701 CB THR A 493 11.586 -10.059 26.539 1.00 43.47 C
ANISOU 3701 CB THR A 493 5054 5538 5923 -79 -182 437 C
ATOM 3702 OG1 THR A 493 10.235 -10.233 26.986 1.00 44.80 O
ANISOU 3702 OG1 THR A 493 5225 5718 6077 -82 -186 446 O
ATOM 3703 CG2 THR A 493 11.626 -9.930 25.032 1.00 40.96 C
ANISOU 3703 CG2 THR A 493 4743 5210 5610 -65 -168 412 C
ATOM 3704 N THR A 494 13.406 -11.981 29.118 1.00 40.91 N
ANISOU 3704 N THR A 494 4691 5200 5652 -112 -232 493 N
ATOM 3705 CA THR A 494 13.360 -12.447 30.500 1.00 40.71 C
ANISOU 3705 CA THR A 494 4659 5181 5627 -130 -252 521 C
ATOM 3706 C THR A 494 13.725 -11.404 31.558 1.00 39.56 C
ANISOU 3706 C THR A 494 4525 5053 5452 -142 -251 531 C
ATOM 3707 O THR A 494 13.336 -11.522 32.711 1.00 40.62 O
ANISOU 3707 O THR A 494 4660 5200 5573 -158 -262 552 O
ATOM 3708 CB THR A 494 14.217 -13.730 30.608 1.00 41.40 C
ANISOU 3708 CB THR A 494 4724 5247 5759 -135 -273 533 C
ATOM 3709 OG1 THR A 494 13.362 -14.863 30.420 1.00 40.18 O
ANISOU 3709 OG1 THR A 494 4559 5086 5622 -133 -282 539 O
ATOM 3710 CG2 THR A 494 14.968 -13.849 31.943 1.00 42.35 C
ANISOU 3710 CG2 THR A 494 4837 5368 5883 -154 -294 560 C
ATOM 3711 N ASN A 495 14.442 -10.368 31.146 1.00 39.15 N
ANISOU 3711 N ASN A 495 4483 5002 5390 -136 -237 515 N
ATOM 3712 CA ASN A 495 14.957 -9.357 32.060 1.00 39.57 C
ANISOU 3712 CA ASN A 495 4546 5069 5419 -147 -236 522 C
ATOM 3713 C ASN A 495 14.082 -8.115 32.168 1.00 38.57 C
ANISOU 3713 C ASN A 495 4439 4963 5250 -145 -217 512 C
ATOM 3714 O ASN A 495 14.529 -7.063 32.637 1.00 40.13 O
ANISOU 3714 O ASN A 495 4648 5171 5427 -149 -210 510 O
ATOM 3715 CB ASN A 495 16.372 -8.959 31.626 1.00 41.59 C
ANISOU 3715 CB ASN A 495 4799 5312 5692 -142 -233 512 C
ATOM 3716 CG ASN A 495 17.371 -10.074 31.839 1.00 41.62 C
ANISOU 3716 CG ASN A 495 4781 5295 5738 -148 -254 526 C
ATOM 3717 OD1 ASN A 495 17.743 -10.376 32.973 1.00 42.76 O
ANISOU 3717 OD1 ASN A 495 4920 5441 5886 -164 -274 550 O
ATOM 3718 ND2 ASN A 495 17.802 -10.699 30.750 1.00 40.98 N
ANISOU 3718 ND2 ASN A 495 4687 5192 5688 -135 -250 511 N
ATOM 3719 N LEU A 496 12.833 -8.252 31.740 1.00 36.60 N
ANISOU 3719 N LEU A 496 4193 4719 4991 -138 -208 505 N
ATOM 3720 CA LEU A 496 11.903 -7.145 31.638 1.00 35.41 C
ANISOU 3720 CA LEU A 496 4059 4585 4807 -133 -190 493 C
ATOM 3721 C LEU A 496 11.484 -6.642 33.017 1.00 35.80 C
ANISOU 3721 C LEU A 496 4116 4655 4828 -150 -192 507 C
ATOM 3722 O LEU A 496 11.093 -7.419 33.876 1.00 36.47 O
ANISOU 3722 O LEU A 496 4196 4745 4916 -164 -205 527 O
ATOM 3723 CB LEU A 496 10.682 -7.617 30.849 1.00 35.40 C
ANISOU 3723 CB LEU A 496 4057 4582 4809 -122 -185 484 C
ATOM 3724 CG LEU A 496 10.150 -6.867 29.626 1.00 35.51 C
ANISOU 3724 CG LEU A 496 4082 4595 4813 -105 -166 460 C
ATOM 3725 CD1 LEU A 496 11.259 -6.359 28.710 1.00 33.68 C
ANISOU 3725 CD1 LEU A 496 3854 4352 4589 -95 -158 444 C
ATOM 3726 CD2 LEU A 496 9.204 -7.795 28.872 1.00 35.55 C
ANISOU 3726 CD2 LEU A 496 4081 4592 4833 -97 -169 457 C
ATOM 3727 N THR A 497 11.576 -5.338 33.231 1.00 36.63 N
ANISOU 3727 N THR A 497 4236 4772 4907 -150 -178 497 N
ATOM 3728 CA THR A 497 11.149 -4.744 34.496 1.00 36.58 C
ANISOU 3728 CA THR A 497 4239 4786 4872 -167 -176 507 C
ATOM 3729 C THR A 497 9.965 -3.776 34.322 1.00 37.50 C
ANISOU 3729 C THR A 497 4368 4917 4963 -160 -155 492 C
ATOM 3730 O THR A 497 9.247 -3.498 35.284 1.00 39.99 O
ANISOU 3730 O THR A 497 4688 5249 5257 -173 -151 498 O
ATOM 3731 CB THR A 497 12.317 -4.034 35.212 1.00 36.29 C
ANISOU 3731 CB THR A 497 4208 4754 4826 -177 -179 512 C
ATOM 3732 OG1 THR A 497 12.902 -3.072 34.330 1.00 36.72 O
ANISOU 3732 OG1 THR A 497 4269 4803 4878 -163 -165 492 O
ATOM 3733 CG2 THR A 497 13.388 -5.035 35.629 1.00 35.61 C
ANISOU 3733 CG2 THR A 497 4109 4655 4766 -188 -202 532 C
ATOM 3734 N PHE A 498 9.761 -3.281 33.097 1.00 36.22 N
ANISOU 3734 N PHE A 498 4210 4748 4804 -141 -142 472 N
ATOM 3735 CA PHE A 498 8.689 -2.320 32.789 1.00 34.85 C
ANISOU 3735 CA PHE A 498 4046 4583 4610 -133 -125 456 C
ATOM 3736 C PHE A 498 8.047 -2.720 31.474 1.00 33.64 C
ANISOU 3736 C PHE A 498 3890 4419 4473 -116 -122 444 C
ATOM 3737 O PHE A 498 8.736 -2.813 30.465 1.00 34.39 O
ANISOU 3737 O PHE A 498 3984 4500 4582 -105 -122 435 O
ATOM 3738 CB PHE A 498 9.281 -0.914 32.675 1.00 35.60 C
ANISOU 3738 CB PHE A 498 4154 4683 4689 -129 -112 442 C
ATOM 3739 CG PHE A 498 8.277 0.171 32.377 1.00 36.03 C
ANISOU 3739 CG PHE A 498 4218 4746 4725 -122 -94 426 C
ATOM 3740 CD1 PHE A 498 7.923 1.091 33.361 1.00 36.16 C
ANISOU 3740 CD1 PHE A 498 4243 4779 4718 -132 -85 425 C
ATOM 3741 CD2 PHE A 498 7.721 0.308 31.103 1.00 35.77 C
ANISOU 3741 CD2 PHE A 498 4187 4703 4699 -104 -88 411 C
ATOM 3742 CE1 PHE A 498 7.016 2.105 33.097 1.00 35.04 C
ANISOU 3742 CE1 PHE A 498 4108 4642 4562 -124 -69 410 C
ATOM 3743 CE2 PHE A 498 6.814 1.317 30.835 1.00 35.02 C
ANISOU 3743 CE2 PHE A 498 4099 4613 4590 -98 -74 398 C
ATOM 3744 CZ PHE A 498 6.463 2.219 31.835 1.00 35.13 C
ANISOU 3744 CZ PHE A 498 4119 4642 4583 -107 -64 397 C
ATOM 3745 N LEU A 499 6.739 -2.963 31.480 1.00 32.35 N
ANISOU 3745 N LEU A 499 3725 4260 4306 -115 -119 444 N
ATOM 3746 CA LEU A 499 6.038 -3.375 30.258 1.00 32.52 C
ANISOU 3746 CA LEU A 499 3744 4270 4341 -100 -117 434 C
ATOM 3747 C LEU A 499 4.731 -2.607 30.036 1.00 32.45 C
ANISOU 3747 C LEU A 499 3741 4268 4319 -93 -105 422 C
ATOM 3748 O LEU A 499 3.761 -2.783 30.780 1.00 31.02 O
ANISOU 3748 O LEU A 499 3557 4097 4131 -101 -104 430 O
ATOM 3749 CB LEU A 499 5.793 -4.893 30.253 1.00 32.23 C
ANISOU 3749 CB LEU A 499 3692 4224 4327 -102 -133 447 C
ATOM 3750 CG LEU A 499 5.016 -5.530 29.098 1.00 31.30 C
ANISOU 3750 CG LEU A 499 3571 4095 4226 -89 -134 439 C
ATOM 3751 CD1 LEU A 499 5.628 -5.161 27.758 1.00 31.56 C
ANISOU 3751 CD1 LEU A 499 3610 4115 4264 -75 -129 421 C
ATOM 3752 CD2 LEU A 499 4.982 -7.037 29.266 1.00 31.11 C
ANISOU 3752 CD2 LEU A 499 3533 4063 4225 -94 -151 453 C
ATOM 3753 N ASP A 500 4.721 -1.759 29.006 1.00 33.04 N
ANISOU 3753 N ASP A 500 3825 4338 4390 -80 -96 405 N
ATOM 3754 CA ASP A 500 3.562 -0.921 28.705 1.00 33.21 C
ANISOU 3754 CA ASP A 500 3852 4363 4401 -73 -85 394 C
ATOM 3755 C ASP A 500 2.790 -1.428 27.495 1.00 34.39 C
ANISOU 3755 C ASP A 500 4000 4500 4565 -61 -89 387 C
ATOM 3756 O ASP A 500 3.268 -1.366 26.354 1.00 36.35 O
ANISOU 3756 O ASP A 500 4254 4738 4820 -51 -90 377 O
ATOM 3757 CB ASP A 500 3.951 0.539 28.502 1.00 33.01 C
ANISOU 3757 CB ASP A 500 3839 4341 4359 -69 -73 380 C
ATOM 3758 CG ASP A 500 2.751 1.475 28.557 1.00 34.61 C
ANISOU 3758 CG ASP A 500 4046 4550 4552 -65 -62 371 C
ATOM 3759 OD1 ASP A 500 1.589 1.007 28.518 1.00 34.63 O
ANISOU 3759 OD1 ASP A 500 4042 4552 4561 -64 -63 373 O
ATOM 3760 OD2 ASP A 500 2.966 2.695 28.652 1.00 36.99 O
ANISOU 3760 OD2 ASP A 500 4356 4856 4840 -64 -52 362 O
ATOM 3761 N LEU A 501 1.579 -1.904 27.771 1.00 32.79 N
ANISOU 3761 N LEU A 501 3790 4300 4366 -62 -91 392 N
ATOM 3762 CA LEU A 501 0.701 -2.466 26.776 1.00 31.36 C
ANISOU 3762 CA LEU A 501 3605 4108 4199 -52 -96 388 C
ATOM 3763 C LEU A 501 -0.661 -1.775 26.811 1.00 30.96 C
ANISOU 3763 C LEU A 501 3555 4062 4143 -49 -89 381 C
ATOM 3764 O LEU A 501 -1.670 -2.355 26.413 1.00 30.66 O
ANISOU 3764 O LEU A 501 3512 4019 4117 -45 -94 382 O
ATOM 3765 CB LEU A 501 0.537 -3.957 27.040 1.00 30.96 C
ANISOU 3765 CB LEU A 501 3542 4054 4166 -58 -109 402 C
ATOM 3766 CG LEU A 501 1.588 -4.892 26.470 1.00 31.57 C
ANISOU 3766 CG LEU A 501 3616 4119 4259 -56 -120 404 C
ATOM 3767 CD1 LEU A 501 1.576 -6.198 27.257 1.00 32.38 C
ANISOU 3767 CD1 LEU A 501 3704 4221 4375 -66 -132 422 C
ATOM 3768 CD2 LEU A 501 1.324 -5.142 24.992 1.00 31.58 C
ANISOU 3768 CD2 LEU A 501 3621 4105 4271 -43 -122 391 C
ATOM 3769 N SER A 502 -0.686 -0.536 27.294 1.00 30.64 N
ANISOU 3769 N SER A 502 3522 4031 4087 -51 -77 375 N
ATOM 3770 CA SER A 502 -1.919 0.248 27.340 1.00 30.75 C
ANISOU 3770 CA SER A 502 3536 4048 4098 -48 -68 367 C
ATOM 3771 C SER A 502 -2.359 0.692 25.943 1.00 31.30 C
ANISOU 3771 C SER A 502 3612 4104 4174 -33 -71 355 C
ATOM 3772 O SER A 502 -1.525 0.901 25.057 1.00 30.91 O
ANISOU 3772 O SER A 502 3573 4048 4124 -27 -74 349 O
ATOM 3773 CB SER A 502 -1.746 1.459 28.242 1.00 30.15 C
ANISOU 3773 CB SER A 502 3465 3985 4004 -54 -54 362 C
ATOM 3774 OG SER A 502 -0.773 2.336 27.710 1.00 30.23 O
ANISOU 3774 OG SER A 502 3487 3992 4007 -49 -51 353 O
ATOM 3775 N LYS A 503 -3.672 0.836 25.766 1.00 30.80 N
ANISOU 3775 N LYS A 503 3544 4038 4119 -29 -71 352 N
ATOM 3776 CA LYS A 503 -4.266 1.277 24.505 1.00 31.17 C
ANISOU 3776 CA LYS A 503 3596 4072 4172 -17 -76 342 C
ATOM 3777 C LYS A 503 -3.979 0.361 23.316 1.00 31.49 C
ANISOU 3777 C LYS A 503 3640 4100 4223 -11 -89 343 C
ATOM 3778 O LYS A 503 -3.799 0.839 22.190 1.00 31.51 O
ANISOU 3778 O LYS A 503 3654 4093 4224 -3 -93 334 O
ATOM 3779 CB LYS A 503 -3.857 2.713 24.192 1.00 31.68 C
ANISOU 3779 CB LYS A 503 3673 4136 4225 -13 -68 331 C
ATOM 3780 CG LYS A 503 -4.679 3.726 24.958 1.00 34.45 C
ANISOU 3780 CG LYS A 503 4020 4495 4574 -15 -56 325 C
ATOM 3781 CD LYS A 503 -4.057 5.109 24.968 1.00 34.59 C
ANISOU 3781 CD LYS A 503 4047 4514 4578 -13 -47 316 C
ATOM 3782 CE LYS A 503 -4.815 5.987 25.941 1.00 35.99 C
ANISOU 3782 CE LYS A 503 4219 4701 4755 -17 -33 310 C
ATOM 3783 NZ LYS A 503 -3.980 7.124 26.411 1.00 40.44 N
ANISOU 3783 NZ LYS A 503 4791 5272 5303 -20 -22 303 N
ATOM 3784 N CYS A 504 -3.962 -0.948 23.560 1.00 31.45 N
ANISOU 3784 N CYS A 504 3626 4094 4229 -15 -97 353 N
ATOM 3785 CA CYS A 504 -3.643 -1.918 22.513 1.00 31.95 C
ANISOU 3785 CA CYS A 504 3690 4144 4302 -10 -109 353 C
ATOM 3786 C CYS A 504 -4.824 -2.712 22.001 1.00 32.65 C
ANISOU 3786 C CYS A 504 3773 4225 4407 -6 -120 355 C
ATOM 3787 O CYS A 504 -4.622 -3.784 21.411 1.00 33.21 O
ANISOU 3787 O CYS A 504 3841 4287 4489 -5 -130 357 O
ATOM 3788 CB CYS A 504 -2.557 -2.886 22.992 1.00 32.67 C
ANISOU 3788 CB CYS A 504 3778 4239 4397 -17 -112 361 C
ATOM 3789 SG CYS A 504 -0.926 -2.138 22.985 1.00 32.80 S
ANISOU 3789 SG CYS A 504 3804 4257 4398 -19 -104 356 S
ATOM 3790 N GLN A 505 -6.043 -2.202 22.230 1.00 33.62 N
ANISOU 3790 N GLN A 505 3890 4349 4533 -5 -117 354 N
ATOM 3791 CA GLN A 505 -7.295 -2.848 21.795 1.00 33.24 C
ANISOU 3791 CA GLN A 505 3834 4293 4502 -1 -127 357 C
ATOM 3792 C GLN A 505 -7.397 -4.329 22.191 1.00 35.61 C
ANISOU 3792 C GLN A 505 4122 4592 4815 -6 -135 368 C
ATOM 3793 O GLN A 505 -8.093 -5.113 21.521 1.00 36.92 O
ANISOU 3793 O GLN A 505 4283 4747 4996 -2 -147 370 O
ATOM 3794 CB GLN A 505 -7.463 -2.750 20.276 1.00 31.04 C
ANISOU 3794 CB GLN A 505 3567 3999 4227 7 -138 348 C
ATOM 3795 CG GLN A 505 -7.407 -1.352 19.702 1.00 31.26 C
ANISOU 3795 CG GLN A 505 3608 4024 4244 12 -134 337 C
ATOM 3796 CD GLN A 505 -7.453 -1.362 18.183 1.00 31.15 C
ANISOU 3796 CD GLN A 505 3607 3996 4231 18 -147 330 C
ATOM 3797 OE1 GLN A 505 -8.233 -2.099 17.573 1.00 30.44 O
ANISOU 3797 OE1 GLN A 505 3514 3896 4154 20 -159 332 O
ATOM 3798 NE2 GLN A 505 -6.609 -0.548 17.565 1.00 30.64 N
ANISOU 3798 NE2 GLN A 505 3559 3930 4152 19 -143 322 N
ATOM 3799 N LEU A 506 -6.702 -4.717 23.260 1.00 36.26 N
ANISOU 3799 N LEU A 506 4198 4685 4892 -15 -130 377 N
ATOM 3800 CA LEU A 506 -6.646 -6.123 23.670 1.00 37.05 C
ANISOU 3800 CA LEU A 506 4287 4784 5005 -21 -139 390 C
ATOM 3801 C LEU A 506 -7.962 -6.611 24.262 1.00 38.86 C
ANISOU 3801 C LEU A 506 4502 5016 5246 -25 -140 398 C
ATOM 3802 O LEU A 506 -8.548 -5.943 25.116 1.00 39.61 O
ANISOU 3802 O LEU A 506 4593 5121 5334 -30 -129 399 O
ATOM 3803 CB LEU A 506 -5.529 -6.333 24.687 1.00 35.62 C
ANISOU 3803 CB LEU A 506 4103 4613 4815 -32 -135 399 C
ATOM 3804 CG LEU A 506 -4.096 -6.276 24.186 1.00 33.79 C
ANISOU 3804 CG LEU A 506 3881 4378 4579 -29 -136 394 C
ATOM 3805 CD1 LEU A 506 -3.173 -6.335 25.390 1.00 35.17 C
ANISOU 3805 CD1 LEU A 506 4052 4563 4745 -41 -132 405 C
ATOM 3806 CD2 LEU A 506 -3.817 -7.426 23.238 1.00 33.65 C
ANISOU 3806 CD2 LEU A 506 3861 4345 4579 -25 -149 394 C
ATOM 3807 N GLU A 507 -8.415 -7.777 23.812 1.00 41.39 N
ANISOU 3807 N GLU A 507 4814 5327 5584 -23 -153 404 N
ATOM 3808 CA GLU A 507 -9.620 -8.404 24.362 1.00 45.99 C
ANISOU 3808 CA GLU A 507 5382 5911 6180 -27 -156 413 C
ATOM 3809 C GLU A 507 -9.334 -9.675 25.167 1.00 50.74 C
ANISOU 3809 C GLU A 507 5972 6515 6789 -38 -162 430 C
ATOM 3810 O GLU A 507 -10.036 -9.963 26.140 1.00 52.25 O
ANISOU 3810 O GLU A 507 6152 6715 6983 -47 -158 440 O
ATOM 3811 CB GLU A 507 -10.598 -8.737 23.250 1.00 46.41 C
ANISOU 3811 CB GLU A 507 5434 5949 6250 -17 -167 408 C
ATOM 3812 CG GLU A 507 -11.359 -7.540 22.721 1.00 49.07 C
ANISOU 3812 CG GLU A 507 5776 6282 6583 -9 -163 396 C
ATOM 3813 CD GLU A 507 -12.019 -7.830 21.392 1.00 52.04 C
ANISOU 3813 CD GLU A 507 6156 6642 6973 0 -178 390 C
ATOM 3814 OE1 GLU A 507 -12.602 -8.927 21.231 1.00 52.68 O
ANISOU 3814 OE1 GLU A 507 6227 6716 7071 0 -189 397 O
ATOM 3815 OE2 GLU A 507 -11.946 -6.958 20.503 1.00 56.23 O
ANISOU 3815 OE2 GLU A 507 6700 7167 7497 6 -179 379 O
ATOM 3816 N GLN A 508 -8.309 -10.423 24.753 1.00 51.57 N
ANISOU 3816 N GLN A 508 6079 6614 6900 -37 -172 432 N
ATOM 3817 CA GLN A 508 -7.972 -11.716 25.352 1.00 51.93 C
ANISOU 3817 CA GLN A 508 6112 6658 6957 -46 -182 448 C
ATOM 3818 C GLN A 508 -6.475 -11.864 25.610 1.00 48.66 C
ANISOU 3818 C GLN A 508 5703 6246 6539 -50 -183 451 C
ATOM 3819 O GLN A 508 -5.656 -11.385 24.836 1.00 47.39 O
ANISOU 3819 O GLN A 508 5553 6080 6373 -43 -181 439 O
ATOM 3820 CB GLN A 508 -8.406 -12.858 24.431 1.00 56.15 C
ANISOU 3820 CB GLN A 508 6640 7177 7515 -39 -197 448 C
ATOM 3821 CG GLN A 508 -9.903 -13.000 24.227 1.00 60.29 C
ANISOU 3821 CG GLN A 508 7158 7698 8050 -36 -200 448 C
ATOM 3822 CD GLN A 508 -10.278 -14.311 23.552 1.00 66.32 C
ANISOU 3822 CD GLN A 508 7913 8447 8837 -32 -217 452 C
ATOM 3823 OE1 GLN A 508 -9.421 -15.157 23.258 1.00 64.95 O
ANISOU 3823 OE1 GLN A 508 7738 8266 8674 -32 -226 454 O
ATOM 3824 NE2 GLN A 508 -11.573 -14.489 23.306 1.00 70.52 N
ANISOU 3824 NE2 GLN A 508 8438 8974 9380 -29 -221 452 N
ATOM 3825 N ILE A 509 -6.129 -12.569 26.682 1.00 45.68 N
ANISOU 3825 N ILE A 509 5315 5875 6164 -64 -187 468 N
ATOM 3826 CA ILE A 509 -4.738 -12.836 27.019 1.00 43.53 C
ANISOU 3826 CA ILE A 509 5044 5602 5891 -69 -191 474 C
ATOM 3827 C ILE A 509 -4.426 -14.329 26.925 1.00 42.51 C
ANISOU 3827 C ILE A 509 4902 5461 5787 -72 -209 485 C
ATOM 3828 O ILE A 509 -5.027 -15.126 27.636 1.00 44.36 O
ANISOU 3828 O ILE A 509 5125 5698 6030 -81 -216 501 O
ATOM 3829 CB ILE A 509 -4.420 -12.312 28.434 1.00 41.91 C
ANISOU 3829 CB ILE A 509 4841 5416 5667 -85 -183 485 C
ATOM 3830 CG1 ILE A 509 -4.656 -10.802 28.484 1.00 39.01 C
ANISOU 3830 CG1 ILE A 509 4486 5059 5277 -81 -166 472 C
ATOM 3831 CG2 ILE A 509 -2.995 -12.680 28.838 1.00 42.50 C
ANISOU 3831 CG2 ILE A 509 4914 5488 5744 -92 -191 494 C
ATOM 3832 CD1 ILE A 509 -4.450 -10.175 29.839 1.00 40.13 C
ANISOU 3832 CD1 ILE A 509 4630 5219 5398 -96 -156 480 C
ATOM 3833 N SER A 510 -3.486 -14.705 26.060 1.00 41.99 N
ANISOU 3833 N SER A 510 4837 5381 5733 -65 -215 477 N
ATOM 3834 CA SER A 510 -3.096 -16.120 25.919 1.00 43.12 C
ANISOU 3834 CA SER A 510 4967 5510 5904 -67 -231 486 C
ATOM 3835 C SER A 510 -2.438 -16.710 27.170 1.00 45.52 C
ANISOU 3835 C SER A 510 5261 5820 6213 -82 -240 508 C
ATOM 3836 O SER A 510 -1.984 -15.977 28.052 1.00 47.19 O
ANISOU 3836 O SER A 510 5479 6045 6406 -91 -233 514 O
ATOM 3837 CB SER A 510 -2.235 -16.346 24.685 1.00 41.68 C
ANISOU 3837 CB SER A 510 4789 5312 5735 -56 -233 470 C
ATOM 3838 OG SER A 510 -3.072 -16.622 23.580 1.00 41.39 O
ANISOU 3838 OG SER A 510 4754 5265 5706 -45 -235 457 O
ATOM 3839 N TRP A 511 -2.378 -18.035 27.230 1.00 48.68 N
ANISOU 3839 N TRP A 511 5646 6208 6639 -86 -256 520 N
ATOM 3840 CA TRP A 511 -2.286 -18.712 28.514 1.00 52.86 C
ANISOU 3840 CA TRP A 511 6165 6744 7174 -103 -267 545 C
ATOM 3841 C TRP A 511 -1.014 -18.578 29.306 1.00 53.08 C
ANISOU 3841 C TRP A 511 6193 6775 7198 -114 -271 556 C
ATOM 3842 O TRP A 511 -1.071 -18.256 30.504 1.00 54.19 O
ANISOU 3842 O TRP A 511 6336 6931 7322 -129 -270 571 O
ATOM 3843 CB TRP A 511 -2.728 -20.175 28.432 1.00 57.08 C
ANISOU 3843 CB TRP A 511 6683 7265 7738 -105 -285 557 C
ATOM 3844 CG TRP A 511 -3.077 -20.696 29.806 1.00 62.67 C
ANISOU 3844 CG TRP A 511 7382 7983 8445 -124 -294 584 C
ATOM 3845 CD1 TRP A 511 -4.136 -20.289 30.630 1.00 63.42 C
ANISOU 3845 CD1 TRP A 511 7480 8096 8519 -134 -285 593 C
ATOM 3846 CD2 TRP A 511 -2.347 -21.697 30.590 1.00 65.45 C
ANISOU 3846 CD2 TRP A 511 7722 8330 8816 -138 -313 607 C
ATOM 3847 NE1 TRP A 511 -4.116 -20.963 31.825 1.00 68.16 N
ANISOU 3847 NE1 TRP A 511 8072 8703 9121 -154 -296 619 N
ATOM 3848 CE2 TRP A 511 -3.070 -21.828 31.868 1.00 70.23 C
ANISOU 3848 CE2 TRP A 511 8325 8952 9407 -157 -315 629 C
ATOM 3849 CE3 TRP A 511 -1.218 -22.476 30.370 1.00 71.79 C
ANISOU 3849 CE3 TRP A 511 8514 9115 9645 -138 -328 611 C
ATOM 3850 CZ2 TRP A 511 -2.658 -22.713 32.863 1.00 73.64 C
ANISOU 3850 CZ2 TRP A 511 8745 9382 9850 -176 -333 656 C
ATOM 3851 CZ3 TRP A 511 -0.810 -23.366 31.383 1.00 80.88 C
ANISOU 3851 CZ3 TRP A 511 9653 10264 10811 -155 -347 638 C
ATOM 3852 CH2 TRP A 511 -1.515 -23.480 32.598 1.00 77.04 C
ANISOU 3852 CH2 TRP A 511 9166 9793 10309 -174 -351 661 C
ATOM 3853 N GLY A 512 0.135 -18.819 28.682 1.00 48.17 N
ANISOU 3853 N GLY A 512 5569 6139 6594 -107 -276 548 N
ATOM 3854 CA GLY A 512 1.393 -18.763 29.432 1.00 47.34 C
ANISOU 3854 CA GLY A 512 5461 6034 6490 -118 -282 559 C
ATOM 3855 C GLY A 512 2.190 -17.505 29.181 1.00 46.18 C
ANISOU 3855 C GLY A 512 5329 5894 6323 -113 -267 543 C
ATOM 3856 O GLY A 512 3.399 -17.475 29.398 1.00 48.59 O
ANISOU 3856 O GLY A 512 5632 6193 6635 -116 -272 546 O
ATOM 3857 N VAL A 513 1.492 -16.457 28.756 1.00 44.23 N
ANISOU 3857 N VAL A 513 5095 5656 6051 -104 -250 527 N
ATOM 3858 CA VAL A 513 2.098 -15.268 28.167 1.00 41.23 C
ANISOU 3858 CA VAL A 513 4731 5279 5655 -95 -234 508 C
ATOM 3859 C VAL A 513 3.086 -14.489 29.063 1.00 40.59 C
ANISOU 3859 C VAL A 513 4655 5208 5557 -105 -231 515 C
ATOM 3860 O VAL A 513 4.029 -13.893 28.546 1.00 39.29 O
ANISOU 3860 O VAL A 513 4498 5040 5391 -99 -224 502 O
ATOM 3861 CB VAL A 513 1.004 -14.359 27.560 1.00 40.41 C
ANISOU 3861 CB VAL A 513 4639 5183 5531 -85 -219 492 C
ATOM 3862 CG1 VAL A 513 0.456 -13.389 28.588 1.00 39.70 C
ANISOU 3862 CG1 VAL A 513 4557 5114 5412 -94 -209 498 C
ATOM 3863 CG2 VAL A 513 1.538 -13.612 26.354 1.00 40.62 C
ANISOU 3863 CG2 VAL A 513 4678 5203 5553 -71 -208 469 C
ATOM 3864 N PHE A 514 2.883 -14.502 30.384 1.00 41.18 N
ANISOU 3864 N PHE A 514 4728 5297 5620 -122 -236 535 N
ATOM 3865 CA PHE A 514 3.764 -13.782 31.327 1.00 40.02 C
ANISOU 3865 CA PHE A 514 4588 5161 5455 -134 -234 543 C
ATOM 3866 C PHE A 514 4.660 -14.666 32.210 1.00 40.47 C
ANISOU 3866 C PHE A 514 4634 5213 5530 -150 -254 566 C
ATOM 3867 O PHE A 514 5.461 -14.143 32.992 1.00 39.56 O
ANISOU 3867 O PHE A 514 4523 5105 5402 -161 -256 574 O
ATOM 3868 CB PHE A 514 2.960 -12.863 32.252 1.00 39.06 C
ANISOU 3868 CB PHE A 514 4477 5062 5300 -144 -222 546 C
ATOM 3869 CG PHE A 514 2.142 -11.829 31.542 1.00 41.60 C
ANISOU 3869 CG PHE A 514 4810 5390 5605 -131 -202 525 C
ATOM 3870 CD1 PHE A 514 0.758 -11.782 31.718 1.00 41.17 C
ANISOU 3870 CD1 PHE A 514 4756 5344 5542 -132 -195 525 C
ATOM 3871 CD2 PHE A 514 2.743 -10.876 30.710 1.00 41.82 C
ANISOU 3871 CD2 PHE A 514 4848 5414 5626 -118 -191 505 C
ATOM 3872 CE1 PHE A 514 -0.012 -10.818 31.067 1.00 39.87 C
ANISOU 3872 CE1 PHE A 514 4600 5183 5365 -119 -179 506 C
ATOM 3873 CE2 PHE A 514 1.975 -9.913 30.060 1.00 39.52 C
ANISOU 3873 CE2 PHE A 514 4567 5127 5320 -106 -175 487 C
ATOM 3874 CZ PHE A 514 0.598 -9.885 30.245 1.00 39.43 C
ANISOU 3874 CZ PHE A 514 4555 5123 5302 -107 -170 487 C
ATOM 3875 N ASP A 515 4.539 -15.986 32.087 1.00 41.46 N
ANISOU 3875 N ASP A 515 4743 5325 5684 -151 -271 577 N
ATOM 3876 CA ASP A 515 5.137 -16.913 33.067 1.00 44.81 C
ANISOU 3876 CA ASP A 515 5155 5745 6125 -168 -294 604 C
ATOM 3877 C ASP A 515 6.653 -16.812 33.231 1.00 45.24 C
ANISOU 3877 C ASP A 515 5207 5790 6192 -172 -302 607 C
ATOM 3878 O ASP A 515 7.200 -17.169 34.276 1.00 49.43 O
ANISOU 3878 O ASP A 515 5732 6323 6726 -190 -319 630 O
ATOM 3879 CB ASP A 515 4.737 -18.353 32.752 1.00 46.67 C
ANISOU 3879 CB ASP A 515 5373 5963 6393 -167 -310 613 C
ATOM 3880 CG ASP A 515 3.261 -18.614 33.012 1.00 49.68 C
ANISOU 3880 CG ASP A 515 5755 6356 6764 -171 -307 619 C
ATOM 3881 OD1 ASP A 515 2.584 -17.739 33.615 1.00 48.84 O
ANISOU 3881 OD1 ASP A 515 5661 6270 6624 -177 -293 619 O
ATOM 3882 OD2 ASP A 515 2.776 -19.696 32.613 1.00 51.96 O
ANISOU 3882 OD2 ASP A 515 6031 6632 7078 -167 -318 623 O
ATOM 3883 N THR A 516 7.303 -16.291 32.198 1.00 42.06 N
ANISOU 3883 N THR A 516 4808 5378 5795 -156 -291 584 N
ATOM 3884 CA THR A 516 8.747 -16.194 32.093 1.00 38.69 C
ANISOU 3884 CA THR A 516 4377 4939 5385 -155 -296 582 C
ATOM 3885 C THR A 516 9.305 -14.876 32.675 1.00 38.95 C
ANISOU 3885 C THR A 516 4424 4987 5386 -161 -285 580 C
ATOM 3886 O THR A 516 10.509 -14.731 32.859 1.00 38.92 O
ANISOU 3886 O THR A 516 4417 4976 5393 -165 -292 583 O
ATOM 3887 CB THR A 516 9.111 -16.352 30.603 1.00 38.58 C
ANISOU 3887 CB THR A 516 4358 4905 5392 -135 -287 556 C
ATOM 3888 OG1 THR A 516 9.389 -17.726 30.320 1.00 36.66 O
ANISOU 3888 OG1 THR A 516 4095 4641 5190 -134 -304 563 O
ATOM 3889 CG2 THR A 516 10.283 -15.504 30.197 1.00 39.00 C
ANISOU 3889 CG2 THR A 516 4417 4955 5444 -129 -277 541 C
ATOM 3890 N LEU A 517 8.425 -13.933 32.991 1.00 38.59 N
ANISOU 3890 N LEU A 517 4394 4962 5305 -163 -270 575 N
ATOM 3891 CA LEU A 517 8.844 -12.577 33.328 1.00 38.92 C
ANISOU 3891 CA LEU A 517 4452 5018 5317 -165 -256 567 C
ATOM 3892 C LEU A 517 9.040 -12.378 34.819 1.00 40.81 C
ANISOU 3892 C LEU A 517 4696 5273 5538 -188 -266 590 C
ATOM 3893 O LEU A 517 8.324 -11.593 35.459 1.00 40.16 O
ANISOU 3893 O LEU A 517 4625 5210 5422 -196 -254 590 O
ATOM 3894 CB LEU A 517 7.833 -11.553 32.780 1.00 38.81 C
ANISOU 3894 CB LEU A 517 4452 5016 5275 -154 -233 547 C
ATOM 3895 CG LEU A 517 7.437 -11.596 31.297 1.00 36.72 C
ANISOU 3895 CG LEU A 517 4188 4740 5023 -132 -222 524 C
ATOM 3896 CD1 LEU A 517 6.419 -10.517 30.978 1.00 35.72 C
ANISOU 3896 CD1 LEU A 517 4076 4627 4868 -125 -203 508 C
ATOM 3897 CD2 LEU A 517 8.649 -11.477 30.387 1.00 36.29 C
ANISOU 3897 CD2 LEU A 517 4132 4669 4985 -122 -220 510 C
ATOM 3898 N HIS A 518 10.040 -13.065 35.363 1.00 43.94 N
ANISOU 3898 N HIS A 518 5081 5659 5955 -200 -287 608 N
ATOM 3899 CA HIS A 518 10.240 -13.099 36.813 1.00 46.15 C
ANISOU 3899 CA HIS A 518 5363 5951 6219 -225 -301 634 C
ATOM 3900 C HIS A 518 10.701 -11.815 37.459 1.00 44.94 C
ANISOU 3900 C HIS A 518 5226 5813 6033 -233 -291 631 C
ATOM 3901 O HIS A 518 10.456 -11.607 38.644 1.00 43.68 O
ANISOU 3901 O HIS A 518 5074 5670 5849 -254 -295 647 O
ATOM 3902 CB HIS A 518 11.115 -14.287 37.218 1.00 50.85 C
ANISOU 3902 CB HIS A 518 5941 6529 6850 -236 -330 657 C
ATOM 3903 CG HIS A 518 10.508 -15.647 36.884 1.00 58.51 C
ANISOU 3903 CG HIS A 518 6895 7486 7849 -233 -343 666 C
ATOM 3904 ND1 HIS A 518 11.244 -16.780 36.826 1.00 61.77 N
ANISOU 3904 ND1 HIS A 518 7289 7876 8303 -235 -367 680 N
ATOM 3905 CD2 HIS A 518 9.193 -16.021 36.575 1.00 58.30 C
ANISOU 3905 CD2 HIS A 518 6868 7464 7817 -227 -335 662 C
ATOM 3906 CE1 HIS A 518 10.446 -17.823 36.509 1.00 59.75 C
ANISOU 3906 CE1 HIS A 518 7022 7613 8067 -232 -374 684 C
ATOM 3907 NE2 HIS A 518 9.194 -17.356 36.352 1.00 60.67 N
ANISOU 3907 NE2 HIS A 518 7150 7746 8154 -227 -354 673 N
ATOM 3908 N ARG A 519 11.333 -10.919 36.698 1.00 45.19 N
ANISOU 3908 N ARG A 519 5264 5841 6064 -218 -277 609 N
ATOM 3909 CA ARG A 519 11.800 -9.637 37.266 1.00 44.98 C
ANISOU 3909 CA ARG A 519 5252 5828 6006 -225 -266 604 C
ATOM 3910 C ARG A 519 10.823 -8.460 37.049 1.00 43.45 C
ANISOU 3910 C ARG A 519 5075 5653 5779 -217 -240 584 C
ATOM 3911 O ARG A 519 11.092 -7.333 37.475 1.00 42.08 O
ANISOU 3911 O ARG A 519 4915 5491 5580 -221 -229 578 O
ATOM 3912 CB ARG A 519 13.216 -9.267 36.770 1.00 45.51 C
ANISOU 3912 CB ARG A 519 5317 5881 6091 -217 -269 596 C
ATOM 3913 CG ARG A 519 14.135 -10.439 36.426 1.00 46.48 C
ANISOU 3913 CG ARG A 519 5420 5980 6259 -215 -290 606 C
ATOM 3914 CD ARG A 519 15.574 -10.280 36.927 1.00 48.64 C
ANISOU 3914 CD ARG A 519 5689 6245 6545 -224 -304 616 C
ATOM 3915 NE ARG A 519 16.011 -8.887 37.073 1.00 50.57 N
ANISOU 3915 NE ARG A 519 5950 6502 6761 -224 -289 604 N
ATOM 3916 CZ ARG A 519 16.624 -8.170 36.127 1.00 50.10 C
ANISOU 3916 CZ ARG A 519 5893 6435 6707 -207 -274 582 C
ATOM 3917 NH1 ARG A 519 16.887 -8.704 34.936 1.00 47.44 N
ANISOU 3917 NH1 ARG A 519 5544 6078 6401 -189 -270 568 N
ATOM 3918 NH2 ARG A 519 16.970 -6.908 36.374 1.00 47.31 N
ANISOU 3918 NH2 ARG A 519 5554 6093 6327 -208 -261 573 N
ATOM 3919 N LEU A 520 9.685 -8.736 36.411 1.00 43.63 N
ANISOU 3919 N LEU A 520 5097 5676 5804 -205 -230 575 N
ATOM 3920 CA LEU A 520 8.748 -7.691 35.978 1.00 43.49 C
ANISOU 3920 CA LEU A 520 5091 5669 5762 -194 -206 554 C
ATOM 3921 C LEU A 520 8.148 -6.902 37.135 1.00 44.68 C
ANISOU 3921 C LEU A 520 5254 5844 5878 -211 -196 558 C
ATOM 3922 O LEU A 520 7.534 -7.478 38.025 1.00 45.85 O
ANISOU 3922 O LEU A 520 5399 6000 6018 -228 -203 575 O
ATOM 3923 CB LEU A 520 7.637 -8.292 35.107 1.00 42.96 C
ANISOU 3923 CB LEU A 520 5018 5596 5708 -181 -201 546 C
ATOM 3924 CG LEU A 520 6.638 -7.319 34.467 1.00 43.32 C
ANISOU 3924 CG LEU A 520 5073 5649 5735 -167 -179 524 C
ATOM 3925 CD1 LEU A 520 7.301 -6.426 33.427 1.00 43.32 C
ANISOU 3925 CD1 LEU A 520 5080 5641 5735 -150 -168 502 C
ATOM 3926 CD2 LEU A 520 5.471 -8.073 33.853 1.00 42.36 C
ANISOU 3926 CD2 LEU A 520 4944 5522 5626 -158 -179 521 C
ATOM 3927 N GLN A 521 8.326 -5.583 37.111 1.00 44.94 N
ANISOU 3927 N GLN A 521 5300 5885 5889 -207 -179 542 N
ATOM 3928 CA GLN A 521 7.886 -4.730 38.213 1.00 44.51 C
ANISOU 3928 CA GLN A 521 5257 5852 5801 -223 -168 543 C
ATOM 3929 C GLN A 521 6.618 -3.950 37.908 1.00 45.33 C
ANISOU 3929 C GLN A 521 5368 5966 5889 -214 -146 525 C
ATOM 3930 O GLN A 521 5.839 -3.654 38.815 1.00 46.54 O
ANISOU 3930 O GLN A 521 5527 6136 6020 -229 -137 527 O
ATOM 3931 CB GLN A 521 8.988 -3.756 38.604 1.00 44.43 C
ANISOU 3931 CB GLN A 521 5257 5846 5777 -229 -167 540 C
ATOM 3932 CG GLN A 521 10.070 -4.361 39.480 1.00 47.60 C
ANISOU 3932 CG GLN A 521 5655 6245 6184 -248 -190 563 C
ATOM 3933 CD GLN A 521 11.264 -3.431 39.684 1.00 49.74 C
ANISOU 3933 CD GLN A 521 5935 6516 6447 -250 -189 559 C
ATOM 3934 OE1 GLN A 521 12.406 -3.888 39.752 1.00 52.14 O
ANISOU 3934 OE1 GLN A 521 6232 6808 6769 -254 -208 571 O
ATOM 3935 NE2 GLN A 521 11.010 -2.128 39.773 1.00 46.95 N
ANISOU 3935 NE2 GLN A 521 5595 6176 6068 -248 -169 542 N
ATOM 3936 N LEU A 522 6.418 -3.621 36.633 1.00 44.52 N
ANISOU 3936 N LEU A 522 5264 5852 5797 -191 -136 506 N
ATOM 3937 CA LEU A 522 5.365 -2.704 36.211 1.00 41.16 C
ANISOU 3937 CA LEU A 522 4845 5432 5359 -180 -116 486 C
ATOM 3938 C LEU A 522 4.726 -3.206 34.915 1.00 40.49 C
ANISOU 3938 C LEU A 522 4753 5333 5295 -161 -116 477 C
ATOM 3939 O LEU A 522 5.381 -3.272 33.871 1.00 39.57 O
ANISOU 3939 O LEU A 522 4636 5202 5194 -146 -120 469 O
ATOM 3940 CB LEU A 522 5.966 -1.302 36.020 1.00 41.87 C
ANISOU 3940 CB LEU A 522 4948 5526 5434 -174 -103 470 C
ATOM 3941 CG LEU A 522 5.228 0.022 35.719 1.00 43.41 C
ANISOU 3941 CG LEU A 522 5152 5728 5614 -165 -82 449 C
ATOM 3942 CD1 LEU A 522 4.065 -0.102 34.732 1.00 43.01 C
ANISOU 3942 CD1 LEU A 522 5096 5669 5574 -148 -75 437 C
ATOM 3943 CD2 LEU A 522 4.774 0.700 37.000 1.00 44.87 C
ANISOU 3943 CD2 LEU A 522 5343 5931 5772 -183 -70 449 C
ATOM 3944 N LEU A 523 3.448 -3.570 34.999 1.00 39.57 N
ANISOU 3944 N LEU A 523 4633 5222 5180 -161 -112 478 N
ATOM 3945 CA LEU A 523 2.657 -3.920 33.827 1.00 38.73 C
ANISOU 3945 CA LEU A 523 4521 5103 5091 -143 -111 468 C
ATOM 3946 C LEU A 523 1.439 -2.968 33.700 1.00 40.77 C
ANISOU 3946 C LEU A 523 4783 5368 5336 -137 -93 452 C
ATOM 3947 O LEU A 523 0.540 -2.984 34.540 1.00 40.64 O
ANISOU 3947 O LEU A 523 4765 5364 5311 -149 -86 457 O
ATOM 3948 CB LEU A 523 2.265 -5.399 33.893 1.00 36.95 C
ANISOU 3948 CB LEU A 523 4282 4871 4885 -148 -126 484 C
ATOM 3949 CG LEU A 523 1.385 -6.127 32.871 1.00 36.86 C
ANISOU 3949 CG LEU A 523 4262 4847 4893 -134 -130 479 C
ATOM 3950 CD1 LEU A 523 1.955 -6.081 31.467 1.00 36.31 C
ANISOU 3950 CD1 LEU A 523 4195 4761 4839 -115 -132 465 C
ATOM 3951 CD2 LEU A 523 1.189 -7.573 33.304 1.00 36.88 C
ANISOU 3951 CD2 LEU A 523 4253 4847 4913 -144 -146 499 C
ATOM 3952 N ASN A 524 1.468 -2.108 32.673 1.00 41.62 N
ANISOU 3952 N ASN A 524 4898 5469 5445 -121 -85 434 N
ATOM 3953 CA ASN A 524 0.400 -1.149 32.333 1.00 42.09 C
ANISOU 3953 CA ASN A 524 4961 5531 5498 -112 -70 418 C
ATOM 3954 C ASN A 524 -0.413 -1.831 31.223 1.00 41.59 C
ANISOU 3954 C ASN A 524 4891 5454 5455 -98 -76 415 C
ATOM 3955 O ASN A 524 0.084 -2.038 30.117 1.00 41.73 O
ANISOU 3955 O ASN A 524 4911 5458 5484 -86 -83 410 O
ATOM 3956 CB ASN A 524 1.037 0.199 31.865 1.00 42.82 C
ANISOU 3956 CB ASN A 524 5066 5623 5580 -103 -60 403 C
ATOM 3957 CG ASN A 524 0.082 1.415 31.904 1.00 45.01 C
ANISOU 3957 CG ASN A 524 5347 5905 5847 -99 -44 387 C
ATOM 3958 OD1 ASN A 524 -1.076 1.334 31.574 1.00 46.17 O
ANISOU 3958 OD1 ASN A 524 5489 6049 6003 -93 -41 383 O
ATOM 3959 ND2 ASN A 524 0.570 2.531 32.274 1.00 47.69 N
ANISOU 3959 ND2 ASN A 524 5695 6252 6172 -102 -34 379 N
ATOM 3960 N MET A 525 -1.634 -2.250 31.541 1.00 40.22 N
ANISOU 3960 N MET A 525 4710 5284 5286 -101 -75 419 N
ATOM 3961 CA MET A 525 -2.548 -2.809 30.538 1.00 39.20 C
ANISOU 3961 CA MET A 525 4574 5142 5175 -89 -81 415 C
ATOM 3962 C MET A 525 -3.870 -2.066 30.556 1.00 38.29 C
ANISOU 3962 C MET A 525 4458 5031 5059 -85 -68 405 C
ATOM 3963 O MET A 525 -4.896 -2.598 30.132 1.00 38.66 O
ANISOU 3963 O MET A 525 4496 5071 5120 -80 -72 405 O
ATOM 3964 CB MET A 525 -2.814 -4.291 30.776 1.00 39.21 C
ANISOU 3964 CB MET A 525 4564 5141 5192 -95 -94 432 C
ATOM 3965 CG MET A 525 -1.625 -5.178 30.506 1.00 40.94 C
ANISOU 3965 CG MET A 525 4781 5351 5422 -96 -109 441 C
ATOM 3966 SD MET A 525 -2.128 -6.837 30.056 1.00 44.19 S
ANISOU 3966 SD MET A 525 5179 5751 5860 -94 -126 452 S
ATOM 3967 CE MET A 525 -2.879 -7.354 31.604 1.00 44.32 C
ANISOU 3967 CE MET A 525 5187 5783 5870 -114 -125 471 C
ATOM 3968 N SER A 526 -3.832 -0.835 31.057 1.00 36.58 N
ANISOU 3968 N SER A 526 4247 4823 4826 -88 -53 395 N
ATOM 3969 CA SER A 526 -4.995 0.028 31.101 1.00 35.56 C
ANISOU 3969 CA SER A 526 4117 4697 4697 -84 -40 383 C
ATOM 3970 C SER A 526 -5.456 0.371 29.685 1.00 36.29 C
ANISOU 3970 C SER A 526 4212 4773 4804 -66 -45 372 C
ATOM 3971 O SER A 526 -4.672 0.275 28.729 1.00 36.08 O
ANISOU 3971 O SER A 526 4191 4736 4779 -57 -55 370 O
ATOM 3972 CB SER A 526 -4.649 1.305 31.851 1.00 33.69 C
ANISOU 3972 CB SER A 526 3887 4471 4441 -91 -24 374 C
ATOM 3973 OG SER A 526 -3.788 2.111 31.072 1.00 33.97 O
ANISOU 3973 OG SER A 526 3934 4500 4473 -80 -25 364 O
ATOM 3974 N HIS A 527 -6.723 0.773 29.562 1.00 35.51 N
ANISOU 3974 N HIS A 527 4105 4671 4714 -61 -39 364 N
ATOM 3975 CA HIS A 527 -7.283 1.277 28.304 1.00 34.18 C
ANISOU 3975 CA HIS A 527 3940 4488 4558 -45 -44 353 C
ATOM 3976 C HIS A 527 -7.330 0.267 27.195 1.00 34.58 C
ANISOU 3976 C HIS A 527 3989 4524 4623 -37 -62 358 C
ATOM 3977 O HIS A 527 -7.118 0.604 26.029 1.00 35.48 O
ANISOU 3977 O HIS A 527 4113 4627 4741 -25 -69 351 O
ATOM 3978 CB HIS A 527 -6.546 2.527 27.841 1.00 34.06 C
ANISOU 3978 CB HIS A 527 3938 4470 4532 -39 -39 341 C
ATOM 3979 CG HIS A 527 -6.872 3.760 28.641 1.00 34.15 C
ANISOU 3979 CG HIS A 527 3949 4491 4535 -43 -22 331 C
ATOM 3980 ND1 HIS A 527 -6.049 4.246 29.594 1.00 34.45 N
ANISOU 3980 ND1 HIS A 527 3992 4541 4554 -53 -11 331 N
ATOM 3981 CD2 HIS A 527 -7.969 4.620 28.588 1.00 33.92 C
ANISOU 3981 CD2 HIS A 527 3914 4458 4516 -38 -13 320 C
ATOM 3982 CE1 HIS A 527 -6.592 5.355 30.131 1.00 34.76 C
ANISOU 3982 CE1 HIS A 527 4030 4586 4591 -55 4 319 C
ATOM 3983 NE2 HIS A 527 -7.773 5.579 29.516 1.00 34.97 N
ANISOU 3983 NE2 HIS A 527 4049 4602 4636 -46 2 312 N
ATOM 3984 N ASN A 528 -7.607 -0.983 27.547 1.00 35.58 N
ANISOU 3984 N ASN A 528 4106 4652 4758 -43 -69 371 N
ATOM 3985 CA ASN A 528 -7.879 -2.030 26.568 1.00 36.20 C
ANISOU 3985 CA ASN A 528 4182 4717 4854 -35 -85 375 C
ATOM 3986 C ASN A 528 -9.358 -2.402 26.652 1.00 37.05 C
ANISOU 3986 C ASN A 528 4276 4822 4978 -34 -86 377 C
ATOM 3987 O ASN A 528 -10.136 -1.657 27.245 1.00 38.01 O
ANISOU 3987 O ASN A 528 4393 4949 5099 -37 -73 372 O
ATOM 3988 CB ASN A 528 -6.961 -3.241 26.804 1.00 35.87 C
ANISOU 3988 CB ASN A 528 4138 4677 4813 -42 -95 388 C
ATOM 3989 CG ASN A 528 -5.568 -3.037 26.228 1.00 35.49 C
ANISOU 3989 CG ASN A 528 4102 4625 4757 -38 -98 384 C
ATOM 3990 OD1 ASN A 528 -5.377 -3.036 25.009 1.00 34.59 O
ANISOU 3990 OD1 ASN A 528 3994 4498 4648 -28 -105 376 O
ATOM 3991 ND2 ASN A 528 -4.588 -2.870 27.102 1.00 35.21 N
ANISOU 3991 ND2 ASN A 528 4069 4600 4708 -48 -92 389 N
ATOM 3992 N ASN A 529 -9.748 -3.530 26.065 1.00 39.21 N
ANISOU 3992 N ASN A 529 4543 5085 5267 -31 -100 384 N
ATOM 3993 CA ASN A 529 -11.145 -3.988 26.106 1.00 42.59 C
ANISOU 3993 CA ASN A 529 4958 5509 5713 -30 -103 387 C
ATOM 3994 C ASN A 529 -11.302 -5.366 26.765 1.00 44.31 C
ANISOU 3994 C ASN A 529 5164 5730 5939 -40 -109 402 C
ATOM 3995 O ASN A 529 -11.966 -6.256 26.219 1.00 43.37 O
ANISOU 3995 O ASN A 529 5037 5601 5838 -36 -121 407 O
ATOM 3996 CB ASN A 529 -11.763 -3.998 24.699 1.00 44.56 C
ANISOU 3996 CB ASN A 529 5210 5740 5978 -17 -117 380 C
ATOM 3997 CG ASN A 529 -11.589 -2.674 23.972 1.00 47.04 C
ANISOU 3997 CG ASN A 529 5536 6049 6285 -8 -114 366 C
ATOM 3998 OD1 ASN A 529 -12.031 -1.626 24.451 1.00 48.57 O
ANISOU 3998 OD1 ASN A 529 5729 6248 6476 -8 -101 359 O
ATOM 3999 ND2 ASN A 529 -10.939 -2.717 22.805 1.00 44.72 N
ANISOU 3999 ND2 ASN A 529 5256 5746 5989 -1 -125 362 N
ATOM 4000 N LEU A 530 -10.686 -5.534 27.936 1.00 44.44 N
ANISOU 4000 N LEU A 530 5180 5762 5943 -54 -101 411 N
ATOM 4001 CA LEU A 530 -10.717 -6.812 28.648 1.00 43.76 C
ANISOU 4001 CA LEU A 530 5084 5681 5862 -65 -107 428 C
ATOM 4002 C LEU A 530 -12.028 -6.991 29.404 1.00 45.70 C
ANISOU 4002 C LEU A 530 5316 5932 6116 -73 -99 432 C
ATOM 4003 O LEU A 530 -12.394 -6.146 30.230 1.00 46.82 O
ANISOU 4003 O LEU A 530 5456 6085 6246 -80 -81 426 O
ATOM 4004 CB LEU A 530 -9.519 -6.940 29.602 1.00 40.90 C
ANISOU 4004 CB LEU A 530 4726 5331 5483 -78 -105 437 C
ATOM 4005 CG LEU A 530 -8.136 -7.025 28.946 1.00 39.15 C
ANISOU 4005 CG LEU A 530 4514 5102 5257 -73 -114 436 C
ATOM 4006 CD1 LEU A 530 -7.026 -6.868 29.968 1.00 38.37 C
ANISOU 4006 CD1 LEU A 530 4420 5016 5140 -86 -110 444 C
ATOM 4007 CD2 LEU A 530 -7.954 -8.310 28.153 1.00 39.01 C
ANISOU 4007 CD2 LEU A 530 4491 5070 5259 -67 -133 442 C
ATOM 4008 N LEU A 531 -12.725 -8.091 29.112 1.00 46.90 N
ANISOU 4008 N LEU A 531 5456 6075 6286 -71 -111 440 N
ATOM 4009 CA LEU A 531 -14.003 -8.419 29.754 1.00 47.91 C
ANISOU 4009 CA LEU A 531 5570 6207 6425 -79 -104 445 C
ATOM 4010 C LEU A 531 -13.850 -9.040 31.153 1.00 48.77 C
ANISOU 4010 C LEU A 531 5674 6332 6524 -99 -98 461 C
ATOM 4011 O LEU A 531 -14.752 -8.940 31.993 1.00 49.75 O
ANISOU 4011 O LEU A 531 5788 6465 6648 -110 -85 463 O
ATOM 4012 CB LEU A 531 -14.857 -9.317 28.841 1.00 48.70 C
ANISOU 4012 CB LEU A 531 5660 6291 6551 -69 -120 448 C
ATOM 4013 CG LEU A 531 -15.752 -8.644 27.778 1.00 48.49 C
ANISOU 4013 CG LEU A 531 5634 6250 6539 -53 -123 434 C
ATOM 4014 CD1 LEU A 531 -16.373 -9.673 26.848 1.00 47.71 C
ANISOU 4014 CD1 LEU A 531 5528 6135 6464 -45 -142 438 C
ATOM 4015 CD2 LEU A 531 -16.841 -7.771 28.388 1.00 47.33 C
ANISOU 4015 CD2 LEU A 531 5478 6109 6395 -56 -105 426 C
ATOM 4016 N PHE A 532 -12.706 -9.678 31.391 1.00 47.84 N
ANISOU 4016 N PHE A 532 5560 6217 6398 -106 -108 473 N
ATOM 4017 CA PHE A 532 -12.361 -10.220 32.707 1.00 45.81 C
ANISOU 4017 CA PHE A 532 5301 5975 6129 -127 -106 490 C
ATOM 4018 C PHE A 532 -10.845 -10.343 32.850 1.00 44.75 C
ANISOU 4018 C PHE A 532 5177 5843 5983 -132 -114 496 C
ATOM 4019 O PHE A 532 -10.120 -10.336 31.865 1.00 46.34 O
ANISOU 4019 O PHE A 532 5384 6032 6190 -118 -125 490 O
ATOM 4020 CB PHE A 532 -13.029 -11.591 32.929 1.00 43.46 C
ANISOU 4020 CB PHE A 532 4989 5673 5849 -135 -117 507 C
ATOM 4021 CG PHE A 532 -12.742 -12.594 31.840 1.00 43.67 C
ANISOU 4021 CG PHE A 532 5012 5681 5897 -122 -140 511 C
ATOM 4022 CD1 PHE A 532 -11.542 -13.323 31.829 1.00 42.66 C
ANISOU 4022 CD1 PHE A 532 4887 5550 5770 -125 -155 522 C
ATOM 4023 CD2 PHE A 532 -13.665 -12.815 30.818 1.00 42.59 C
ANISOU 4023 CD2 PHE A 532 4869 5530 5782 -107 -146 503 C
ATOM 4024 CE1 PHE A 532 -11.267 -14.242 30.820 1.00 41.83 C
ANISOU 4024 CE1 PHE A 532 4779 5428 5687 -114 -174 523 C
ATOM 4025 CE2 PHE A 532 -13.397 -13.737 29.806 1.00 43.74 C
ANISOU 4025 CE2 PHE A 532 5013 5659 5947 -96 -166 505 C
ATOM 4026 CZ PHE A 532 -12.196 -14.452 29.807 1.00 43.48 C
ANISOU 4026 CZ PHE A 532 4982 5623 5915 -99 -179 514 C
ATOM 4027 N LEU A 533 -10.373 -10.455 34.083 1.00 46.29 N
ANISOU 4027 N LEU A 533 5374 6053 6161 -152 -110 509 N
ATOM 4028 CA LEU A 533 -9.008 -10.896 34.341 1.00 47.47 C
ANISOU 4028 CA LEU A 533 5528 6203 6304 -159 -123 521 C
ATOM 4029 C LEU A 533 -8.986 -12.370 34.757 1.00 49.87 C
ANISOU 4029 C LEU A 533 5822 6505 6622 -170 -141 544 C
ATOM 4030 O LEU A 533 -9.998 -12.919 35.196 1.00 51.17 O
ANISOU 4030 O LEU A 533 5977 6673 6793 -179 -139 552 O
ATOM 4031 CB LEU A 533 -8.355 -10.044 35.431 1.00 45.67 C
ANISOU 4031 CB LEU A 533 5311 5993 6048 -174 -110 522 C
ATOM 4032 CG LEU A 533 -8.026 -8.587 35.124 1.00 43.76 C
ANISOU 4032 CG LEU A 533 5082 5754 5791 -165 -95 501 C
ATOM 4033 CD1 LEU A 533 -7.391 -7.963 36.353 1.00 43.17 C
ANISOU 4033 CD1 LEU A 533 5015 5697 5688 -184 -85 505 C
ATOM 4034 CD2 LEU A 533 -7.121 -8.438 33.905 1.00 42.38 C
ANISOU 4034 CD2 LEU A 533 4912 5563 5625 -146 -106 493 C
ATOM 4035 N ASP A 534 -7.830 -13.006 34.597 1.00 51.96 N
ANISOU 4035 N ASP A 534 6087 6760 6892 -171 -158 554 N
ATOM 4036 CA ASP A 534 -7.604 -14.348 35.113 1.00 52.40 C
ANISOU 4036 CA ASP A 534 6133 6814 6961 -184 -177 578 C
ATOM 4037 C ASP A 534 -6.294 -14.369 35.892 1.00 54.05 C
ANISOU 4037 C ASP A 534 6349 7030 7158 -199 -184 591 C
ATOM 4038 O ASP A 534 -5.201 -14.340 35.310 1.00 53.46 O
ANISOU 4038 O ASP A 534 6277 6944 7090 -189 -193 587 O
ATOM 4039 CB ASP A 534 -7.593 -15.379 33.982 1.00 54.34 C
ANISOU 4039 CB ASP A 534 6369 7038 7237 -169 -195 578 C
ATOM 4040 CG ASP A 534 -7.511 -16.820 34.493 1.00 56.11 C
ANISOU 4040 CG ASP A 534 6581 7258 7479 -182 -215 602 C
ATOM 4041 OD1 ASP A 534 -7.785 -17.751 33.701 1.00 52.40 O
ANISOU 4041 OD1 ASP A 534 6101 6771 7036 -171 -228 603 O
ATOM 4042 OD2 ASP A 534 -7.182 -17.023 35.684 1.00 58.21 O
ANISOU 4042 OD2 ASP A 534 6847 7536 7732 -203 -217 621 O
ATOM 4043 N SER A 535 -6.429 -14.434 37.214 1.00 55.46 N
ANISOU 4043 N SER A 535 6528 7224 7318 -223 -181 606 N
ATOM 4044 CA SER A 535 -5.310 -14.330 38.167 1.00 54.20 C
ANISOU 4044 CA SER A 535 6377 7074 7142 -241 -187 620 C
ATOM 4045 C SER A 535 -4.060 -15.109 37.783 1.00 49.01 C
ANISOU 4045 C SER A 535 5714 6400 6504 -238 -211 631 C
ATOM 4046 O SER A 535 -2.953 -14.672 38.057 1.00 46.43 O
ANISOU 4046 O SER A 535 5396 6077 6168 -242 -215 633 O
ATOM 4047 CB SER A 535 -5.756 -14.800 39.554 1.00 57.78 C
ANISOU 4047 CB SER A 535 6828 7543 7580 -270 -188 642 C
ATOM 4048 OG SER A 535 -7.164 -14.716 39.694 1.00 66.42 O
ANISOU 4048 OG SER A 535 7918 8645 8672 -272 -172 636 O
ATOM 4049 N SER A 536 -4.252 -16.263 37.157 1.00 48.57 N
ANISOU 4049 N SER A 536 5645 6328 6478 -230 -228 638 N
ATOM 4050 CA SER A 536 -3.162 -17.190 36.876 1.00 49.56 C
ANISOU 4050 CA SER A 536 5763 6438 6628 -228 -252 650 C
ATOM 4051 C SER A 536 -2.252 -16.763 35.713 1.00 48.73 C
ANISOU 4051 C SER A 536 5662 6318 6535 -206 -251 631 C
ATOM 4052 O SER A 536 -1.217 -17.394 35.457 1.00 47.22 O
ANISOU 4052 O SER A 536 5464 6112 6364 -205 -268 637 O
ATOM 4053 CB SER A 536 -3.712 -18.606 36.678 1.00 51.73 C
ANISOU 4053 CB SER A 536 6022 6700 6932 -229 -269 665 C
ATOM 4054 OG SER A 536 -4.802 -18.611 35.776 1.00 53.22 O
ANISOU 4054 OG SER A 536 6207 6882 7130 -212 -260 649 O
ATOM 4055 N HIS A 537 -2.637 -15.690 35.021 1.00 48.54 N
ANISOU 4055 N HIS A 537 5646 6297 6497 -191 -232 606 N
ATOM 4056 CA HIS A 537 -1.765 -15.045 34.038 1.00 46.55 C
ANISOU 4056 CA HIS A 537 5401 6035 6248 -173 -228 587 C
ATOM 4057 C HIS A 537 -0.607 -14.386 34.731 1.00 45.76 C
ANISOU 4057 C HIS A 537 5310 5943 6132 -184 -227 591 C
ATOM 4058 O HIS A 537 0.476 -14.247 34.157 1.00 44.57 O
ANISOU 4058 O HIS A 537 5161 5781 5990 -175 -231 584 O
ATOM 4059 CB HIS A 537 -2.518 -13.984 33.233 1.00 44.97 C
ANISOU 4059 CB HIS A 537 5210 5838 6037 -157 -208 563 C
ATOM 4060 CG HIS A 537 -3.636 -14.525 32.368 1.00 44.11 C
ANISOU 4060 CG HIS A 537 5094 5719 5945 -144 -209 556 C
ATOM 4061 ND1 HIS A 537 -3.513 -15.644 31.628 1.00 43.72 N
ANISOU 4061 ND1 HIS A 537 5034 5652 5924 -136 -225 559 N
ATOM 4062 CD2 HIS A 537 -4.911 -14.021 32.109 1.00 42.40 C
ANISOU 4062 CD2 HIS A 537 4879 5507 5722 -138 -196 545 C
ATOM 4063 CE1 HIS A 537 -4.660 -15.861 30.952 1.00 41.77 C
ANISOU 4063 CE1 HIS A 537 4783 5399 5687 -126 -223 551 C
ATOM 4064 NE2 HIS A 537 -5.509 -14.866 31.244 1.00 41.40 N
ANISOU 4064 NE2 HIS A 537 4743 5366 5619 -127 -206 543 N
ATOM 4065 N TYR A 538 -0.837 -14.005 35.986 1.00 47.36 N
ANISOU 4065 N TYR A 538 5519 6165 6310 -204 -221 603 N
ATOM 4066 CA TYR A 538 0.052 -13.122 36.742 1.00 49.98 C
ANISOU 4066 CA TYR A 538 5862 6509 6619 -215 -217 605 C
ATOM 4067 C TYR A 538 0.783 -13.815 37.877 1.00 51.36 C
ANISOU 4067 C TYR A 538 6034 6687 6793 -239 -235 632 C
ATOM 4068 O TYR A 538 1.741 -13.270 38.417 1.00 51.75 O
ANISOU 4068 O TYR A 538 6091 6741 6829 -248 -237 635 O
ATOM 4069 CB TYR A 538 -0.731 -11.923 37.284 1.00 48.96 C
ANISOU 4069 CB TYR A 538 5744 6399 6457 -220 -193 593 C
ATOM 4070 CG TYR A 538 -1.677 -11.346 36.274 1.00 48.64 C
ANISOU 4070 CG TYR A 538 5705 6354 6419 -200 -177 570 C
ATOM 4071 CD1 TYR A 538 -2.978 -11.823 36.169 1.00 48.47 C
ANISOU 4071 CD1 TYR A 538 5675 6333 6405 -198 -173 571 C
ATOM 4072 CD2 TYR A 538 -1.267 -10.343 35.402 1.00 49.72 C
ANISOU 4072 CD2 TYR A 538 5850 6486 6552 -182 -166 549 C
ATOM 4073 CE1 TYR A 538 -3.849 -11.310 35.233 1.00 49.95 C
ANISOU 4073 CE1 TYR A 538 5864 6516 6598 -180 -161 551 C
ATOM 4074 CE2 TYR A 538 -2.135 -9.820 34.461 1.00 49.98 C
ANISOU 4074 CE2 TYR A 538 5885 6515 6588 -164 -154 529 C
ATOM 4075 CZ TYR A 538 -3.424 -10.308 34.386 1.00 49.43 C
ANISOU 4075 CZ TYR A 538 5807 6445 6527 -163 -152 531 C
ATOM 4076 OH TYR A 538 -4.302 -9.804 33.462 1.00 52.93 O
ANISOU 4076 OH TYR A 538 6251 6883 6976 -146 -142 513 O
ATOM 4077 N ASN A 539 0.323 -15.004 38.255 1.00 56.89 N
ANISOU 4077 N ASN A 539 6723 7384 7509 -249 -251 651 N
ATOM 4078 CA ASN A 539 1.148 -15.897 39.053 1.00 61.53 C
ANISOU 4078 CA ASN A 539 7304 7967 8107 -268 -275 678 C
ATOM 4079 C ASN A 539 2.380 -16.200 38.209 1.00 63.73 C
ANISOU 4079 C ASN A 539 7575 8224 8413 -254 -289 674 C
ATOM 4080 O ASN A 539 2.268 -16.352 36.983 1.00 70.52 O
ANISOU 4080 O ASN A 539 8430 9070 9294 -231 -285 656 O
ATOM 4081 CB ASN A 539 0.403 -17.185 39.392 1.00 64.48 C
ANISOU 4081 CB ASN A 539 7665 8337 8497 -279 -290 699 C
ATOM 4082 CG ASN A 539 1.106 -17.998 40.466 1.00 70.19 C
ANISOU 4082 CG ASN A 539 8383 9060 9224 -305 -315 731 C
ATOM 4083 OD1 ASN A 539 0.832 -19.189 40.637 1.00 74.07 O
ANISOU 4083 OD1 ASN A 539 8861 9542 9736 -312 -333 750 O
ATOM 4084 ND2 ASN A 539 2.019 -17.360 41.199 1.00 70.39 N
ANISOU 4084 ND2 ASN A 539 8419 9094 9230 -318 -317 737 N
ATOM 4085 N GLN A 540 3.544 -16.266 38.851 1.00 58.40 N
ANISOU 4085 N GLN A 540 6902 7548 7740 -267 -304 689 N
ATOM 4086 CA GLN A 540 4.835 -16.336 38.151 1.00 56.29 C
ANISOU 4086 CA GLN A 540 6628 7261 7496 -255 -314 682 C
ATOM 4087 C GLN A 540 5.440 -14.942 37.898 1.00 53.03 C
ANISOU 4087 C GLN A 540 6230 6855 7062 -246 -295 662 C
ATOM 4088 O GLN A 540 6.562 -14.833 37.401 1.00 51.72 O
ANISOU 4088 O GLN A 540 6061 6676 6912 -237 -301 655 O
ATOM 4089 CB GLN A 540 4.734 -17.133 36.842 1.00 58.26 C
ANISOU 4089 CB GLN A 540 6864 7489 7783 -232 -318 670 C
ATOM 4090 CG GLN A 540 4.336 -18.595 37.011 1.00 61.74 C
ANISOU 4090 CG GLN A 540 7288 7917 8251 -240 -339 690 C
ATOM 4091 CD GLN A 540 5.443 -19.544 36.624 1.00 64.26 C
ANISOU 4091 CD GLN A 540 7591 8213 8612 -236 -361 697 C
ATOM 4092 OE1 GLN A 540 5.389 -20.172 35.569 1.00 65.50 O
ANISOU 4092 OE1 GLN A 540 7737 8351 8798 -219 -363 685 O
ATOM 4093 NE2 GLN A 540 6.469 -19.640 37.466 1.00 70.04 N
ANISOU 4093 NE2 GLN A 540 8320 8942 9346 -252 -378 717 N
ATOM 4094 N LEU A 541 4.692 -13.887 38.231 1.00 49.64 N
ANISOU 4094 N LEU A 541 5815 6446 6598 -248 -274 651 N
ATOM 4095 CA LEU A 541 5.244 -12.530 38.275 1.00 47.81 C
ANISOU 4095 CA LEU A 541 5598 6224 6342 -245 -258 635 C
ATOM 4096 C LEU A 541 5.703 -12.187 39.695 1.00 50.17 C
ANISOU 4096 C LEU A 541 5906 6539 6617 -272 -264 654 C
ATOM 4097 O LEU A 541 5.150 -11.295 40.355 1.00 49.59 O
ANISOU 4097 O LEU A 541 5846 6485 6510 -282 -247 649 O
ATOM 4098 CB LEU A 541 4.245 -11.494 37.763 1.00 44.07 C
ANISOU 4098 CB LEU A 541 5134 5760 5848 -232 -231 611 C
ATOM 4099 CG LEU A 541 3.765 -11.652 36.318 1.00 42.38 C
ANISOU 4099 CG LEU A 541 4915 5532 5654 -206 -224 591 C
ATOM 4100 CD1 LEU A 541 2.809 -10.522 35.985 1.00 40.67 C
ANISOU 4100 CD1 LEU A 541 4710 5327 5416 -196 -200 570 C
ATOM 4101 CD2 LEU A 541 4.912 -11.718 35.319 1.00 39.93 C
ANISOU 4101 CD2 LEU A 541 4601 5203 5367 -191 -230 581 C
ATOM 4102 N TYR A 542 6.745 -12.892 40.135 1.00 50.11 N
ANISOU 4102 N TYR A 542 5890 6521 6626 -284 -289 674 N
ATOM 4103 CA TYR A 542 7.233 -12.841 41.510 1.00 51.19 C
ANISOU 4103 CA TYR A 542 6035 6671 6744 -312 -302 697 C
ATOM 4104 C TYR A 542 7.777 -11.488 41.950 1.00 49.14 C
ANISOU 4104 C TYR A 542 5791 6424 6453 -318 -288 687 C
ATOM 4105 O TYR A 542 8.041 -11.274 43.131 1.00 49.36 O
ANISOU 4105 O TYR A 542 5829 6467 6459 -343 -295 703 O
ATOM 4106 CB TYR A 542 8.307 -13.911 41.705 1.00 53.52 C
ANISOU 4106 CB TYR A 542 6315 6946 7071 -321 -334 721 C
ATOM 4107 CG TYR A 542 7.836 -15.306 41.364 1.00 58.49 C
ANISOU 4107 CG TYR A 542 6928 7562 7734 -318 -350 733 C
ATOM 4108 CD1 TYR A 542 8.258 -15.940 40.189 1.00 61.12 C
ANISOU 4108 CD1 TYR A 542 7245 7870 8107 -296 -356 723 C
ATOM 4109 CD2 TYR A 542 6.963 -15.996 42.214 1.00 58.90 C
ANISOU 4109 CD2 TYR A 542 6978 7623 7775 -338 -358 754 C
ATOM 4110 CE1 TYR A 542 7.828 -17.224 39.875 1.00 61.43 C
ANISOU 4110 CE1 TYR A 542 7267 7894 8176 -293 -371 733 C
ATOM 4111 CE2 TYR A 542 6.528 -17.276 41.909 1.00 60.01 C
ANISOU 4111 CE2 TYR A 542 7103 7751 7947 -336 -373 766 C
ATOM 4112 CZ TYR A 542 6.958 -17.885 40.742 1.00 60.88 C
ANISOU 4112 CZ TYR A 542 7196 7835 8097 -313 -380 755 C
ATOM 4113 OH TYR A 542 6.518 -19.154 40.446 1.00 59.70 O
ANISOU 4113 OH TYR A 542 7030 7671 7979 -310 -395 766 O
ATOM 4114 N SER A 543 7.932 -10.575 41.001 1.00 47.50 N
ANISOU 4114 N SER A 543 5588 6213 6245 -295 -269 660 N
ATOM 4115 CA SER A 543 8.580 -9.304 41.267 1.00 45.26 C
ANISOU 4115 CA SER A 543 5319 5939 5937 -297 -258 649 C
ATOM 4116 C SER A 543 7.702 -8.091 40.936 1.00 44.18 C
ANISOU 4116 C SER A 543 5194 5815 5774 -285 -227 623 C
ATOM 4117 O SER A 543 8.140 -6.950 41.051 1.00 45.15 O
ANISOU 4117 O SER A 543 5329 5946 5878 -284 -215 610 O
ATOM 4118 CB SER A 543 9.897 -9.252 40.505 1.00 43.61 C
ANISOU 4118 CB SER A 543 5103 5710 5754 -282 -267 643 C
ATOM 4119 OG SER A 543 10.697 -8.200 40.984 1.00 46.83 O
ANISOU 4119 OG SER A 543 5524 6127 6142 -289 -262 639 O
ATOM 4120 N LEU A 544 6.458 -8.359 40.549 1.00 44.44 N
ANISOU 4120 N LEU A 544 5224 5851 5809 -277 -216 616 N
ATOM 4121 CA LEU A 544 5.497 -7.340 40.142 1.00 43.88 C
ANISOU 4121 CA LEU A 544 5161 5790 5720 -265 -189 592 C
ATOM 4122 C LEU A 544 5.000 -6.528 41.320 1.00 44.79 C
ANISOU 4122 C LEU A 544 5290 5929 5799 -285 -175 592 C
ATOM 4123 O LEU A 544 4.519 -7.090 42.293 1.00 48.03 O
ANISOU 4123 O LEU A 544 5699 6349 6198 -307 -180 609 O
ATOM 4124 CB LEU A 544 4.303 -8.004 39.446 1.00 42.41 C
ANISOU 4124 CB LEU A 544 4966 5599 5549 -253 -185 587 C
ATOM 4125 CG LEU A 544 3.317 -7.075 38.728 1.00 41.67 C
ANISOU 4125 CG LEU A 544 4876 5508 5446 -235 -161 561 C
ATOM 4126 CD1 LEU A 544 3.906 -6.612 37.403 1.00 42.29 C
ANISOU 4126 CD1 LEU A 544 4955 5571 5539 -210 -157 542 C
ATOM 4127 CD2 LEU A 544 1.971 -7.749 38.497 1.00 41.68 C
ANISOU 4127 CD2 LEU A 544 4869 5508 5456 -232 -157 562 C
ATOM 4128 N SER A 545 5.096 -5.207 41.223 1.00 45.71 N
ANISOU 4128 N SER A 545 5417 6052 5896 -279 -156 572 N
ATOM 4129 CA SER A 545 4.618 -4.330 42.292 1.00 46.40 C
ANISOU 4129 CA SER A 545 5517 6161 5949 -297 -139 568 C
ATOM 4130 C SER A 545 3.453 -3.439 41.857 1.00 46.06 C
ANISOU 4130 C SER A 545 5478 6125 5897 -284 -112 543 C
ATOM 4131 O SER A 545 2.702 -2.943 42.689 1.00 45.68 O
ANISOU 4131 O SER A 545 5436 6094 5826 -299 -96 539 O
ATOM 4132 CB SER A 545 5.760 -3.471 42.836 1.00 45.68 C
ANISOU 4132 CB SER A 545 5439 6076 5841 -307 -141 567 C
ATOM 4133 OG SER A 545 5.876 -2.278 42.089 1.00 47.83 O
ANISOU 4133 OG SER A 545 5717 6346 6110 -287 -123 542 O
ATOM 4134 N THR A 546 3.320 -3.228 40.552 1.00 48.48 N
ANISOU 4134 N THR A 546 5779 6417 6222 -257 -107 526 N
ATOM 4135 CA THR A 546 2.248 -2.395 40.006 1.00 47.05 C
ANISOU 4135 CA THR A 546 5600 6239 6038 -242 -85 504 C
ATOM 4136 C THR A 546 1.598 -3.055 38.791 1.00 45.40 C
ANISOU 4136 C THR A 546 5380 6014 5857 -221 -89 499 C
ATOM 4137 O THR A 546 2.275 -3.426 37.826 1.00 44.46 O
ANISOU 4137 O THR A 546 5256 5879 5757 -206 -101 498 O
ATOM 4138 CB THR A 546 2.746 -0.972 39.667 1.00 47.19 C
ANISOU 4138 CB THR A 546 5628 6257 6045 -232 -71 483 C
ATOM 4139 OG1 THR A 546 3.182 -0.322 40.866 1.00 46.93 O
ANISOU 4139 OG1 THR A 546 5606 6240 5985 -253 -66 486 O
ATOM 4140 CG2 THR A 546 1.642 -0.141 39.040 1.00 49.38 C
ANISOU 4140 CG2 THR A 546 5905 6533 6322 -216 -51 461 C
ATOM 4141 N LEU A 547 0.278 -3.210 38.875 1.00 44.96 N
ANISOU 4141 N LEU A 547 5318 5963 5801 -222 -78 495 N
ATOM 4142 CA LEU A 547 -0.542 -3.729 37.786 1.00 44.04 C
ANISOU 4142 CA LEU A 547 5191 5832 5707 -203 -80 489 C
ATOM 4143 C LEU A 547 -1.678 -2.737 37.524 1.00 43.31 C
ANISOU 4143 C LEU A 547 5101 5744 5610 -193 -59 469 C
ATOM 4144 O LEU A 547 -2.513 -2.482 38.398 1.00 42.72 O
ANISOU 4144 O LEU A 547 5026 5683 5522 -207 -45 467 O
ATOM 4145 CB LEU A 547 -1.105 -5.114 38.138 1.00 44.11 C
ANISOU 4145 CB LEU A 547 5189 5840 5729 -213 -93 509 C
ATOM 4146 CG LEU A 547 -1.311 -6.153 37.025 1.00 44.55 C
ANISOU 4146 CG LEU A 547 5234 5878 5815 -196 -107 512 C
ATOM 4147 CD1 LEU A 547 -2.030 -7.385 37.557 1.00 45.59 C
ANISOU 4147 CD1 LEU A 547 5354 6011 5955 -209 -117 530 C
ATOM 4148 CD2 LEU A 547 -2.079 -5.592 35.845 1.00 43.54 C
ANISOU 4148 CD2 LEU A 547 5105 5740 5696 -174 -97 491 C
ATOM 4149 N ASP A 548 -1.687 -2.170 36.320 1.00 42.69 N
ANISOU 4149 N ASP A 548 5024 5653 5543 -171 -56 452 N
ATOM 4150 CA ASP A 548 -2.692 -1.193 35.918 1.00 41.35 C
ANISOU 4150 CA ASP A 548 4855 5483 5372 -160 -38 433 C
ATOM 4151 C ASP A 548 -3.699 -1.806 34.947 1.00 40.36 C
ANISOU 4151 C ASP A 548 4719 5345 5269 -145 -43 430 C
ATOM 4152 O ASP A 548 -3.384 -2.053 33.783 1.00 40.26 O
ANISOU 4152 O ASP A 548 4706 5317 5271 -129 -54 427 O
ATOM 4153 CB ASP A 548 -2.016 0.028 35.293 1.00 41.30 C
ANISOU 4153 CB ASP A 548 4859 5473 5360 -147 -32 416 C
ATOM 4154 CG ASP A 548 -2.903 1.263 35.306 1.00 42.03 C
ANISOU 4154 CG ASP A 548 4953 5569 5446 -143 -12 397 C
ATOM 4155 OD1 ASP A 548 -2.342 2.375 35.233 1.00 42.58 O
ANISOU 4155 OD1 ASP A 548 5032 5640 5505 -139 -4 385 O
ATOM 4156 OD2 ASP A 548 -4.145 1.132 35.390 1.00 40.31 O
ANISOU 4156 OD2 ASP A 548 4726 5351 5235 -142 -5 394 O
ATOM 4157 N CYS A 549 -4.906 -2.074 35.434 1.00 40.04 N
ANISOU 4157 N CYS A 549 4670 5310 5231 -152 -35 432 N
ATOM 4158 CA CYS A 549 -5.943 -2.652 34.590 1.00 39.64 C
ANISOU 4158 CA CYS A 549 4609 5247 5203 -139 -40 430 C
ATOM 4159 C CYS A 549 -7.170 -1.761 34.497 1.00 38.98 C
ANISOU 4159 C CYS A 549 4523 5165 5122 -133 -23 413 C
ATOM 4160 O CYS A 549 -8.276 -2.233 34.220 1.00 39.01 O
ANISOU 4160 O CYS A 549 4515 5163 5142 -129 -24 413 O
ATOM 4161 CB CYS A 549 -6.316 -4.037 35.078 1.00 41.13 C
ANISOU 4161 CB CYS A 549 4788 5438 5401 -151 -51 449 C
ATOM 4162 SG CYS A 549 -5.067 -5.263 34.668 1.00 46.06 S
ANISOU 4162 SG CYS A 549 5411 6051 6036 -150 -76 466 S
ATOM 4163 N SER A 550 -6.948 -0.469 34.715 1.00 38.11 N
ANISOU 4163 N SER A 550 4421 5061 4999 -133 -8 399 N
ATOM 4164 CA SER A 550 -7.986 0.540 34.627 1.00 38.70 C
ANISOU 4164 CA SER A 550 4492 5134 5077 -127 7 381 C
ATOM 4165 C SER A 550 -8.479 0.770 33.209 1.00 39.50 C
ANISOU 4165 C SER A 550 4590 5217 5199 -105 0 371 C
ATOM 4166 O SER A 550 -7.837 0.368 32.232 1.00 38.55 O
ANISOU 4166 O SER A 550 4474 5085 5086 -93 -16 375 O
ATOM 4167 CB SER A 550 -7.488 1.855 35.208 1.00 38.99 C
ANISOU 4167 CB SER A 550 4538 5181 5094 -132 24 368 C
ATOM 4168 OG SER A 550 -6.295 2.244 34.580 1.00 38.88 O
ANISOU 4168 OG SER A 550 4536 5161 5075 -123 14 367 O
ATOM 4169 N PHE A 551 -9.639 1.417 33.118 1.00 39.96 N
ANISOU 4169 N PHE A 551 4642 5272 5269 -99 11 359 N
ATOM 4170 CA PHE A 551 -10.251 1.768 31.844 1.00 40.73 C
ANISOU 4170 CA PHE A 551 4736 5351 5386 -80 4 349 C
ATOM 4171 C PHE A 551 -10.333 0.590 30.880 1.00 41.89 C
ANISOU 4171 C PHE A 551 4880 5485 5549 -71 -16 360 C
ATOM 4172 O PHE A 551 -10.160 0.746 29.670 1.00 42.80 O
ANISOU 4172 O PHE A 551 5001 5587 5674 -57 -28 356 O
ATOM 4173 CB PHE A 551 -9.542 2.961 31.200 1.00 40.26 C
ANISOU 4173 CB PHE A 551 4689 5286 5320 -69 5 337 C
ATOM 4174 CG PHE A 551 -9.700 4.247 31.960 1.00 41.56 C
ANISOU 4174 CG PHE A 551 4854 5459 5475 -75 25 323 C
ATOM 4175 CD1 PHE A 551 -8.700 4.683 32.833 1.00 41.26 C
ANISOU 4175 CD1 PHE A 551 4826 5436 5413 -87 35 322 C
ATOM 4176 CD2 PHE A 551 -10.843 5.034 31.798 1.00 42.68 C
ANISOU 4176 CD2 PHE A 551 4988 5594 5633 -68 35 309 C
ATOM 4177 CE1 PHE A 551 -8.837 5.876 33.530 1.00 41.98 C
ANISOU 4177 CE1 PHE A 551 4919 5534 5495 -92 54 308 C
ATOM 4178 CE2 PHE A 551 -10.988 6.230 32.494 1.00 43.12 C
ANISOU 4178 CE2 PHE A 551 5043 5656 5682 -73 55 294 C
ATOM 4179 CZ PHE A 551 -9.984 6.650 33.360 1.00 44.31 C
ANISOU 4179 CZ PHE A 551 5205 5823 5808 -85 65 293 C
ATOM 4180 N ASN A 552 -10.589 -0.595 31.422 1.00 43.62 N
ANISOU 4180 N ASN A 552 5091 5709 5772 -81 -20 374 N
ATOM 4181 CA ASN A 552 -11.031 -1.705 30.596 1.00 44.80 C
ANISOU 4181 CA ASN A 552 5233 5846 5941 -73 -38 382 C
ATOM 4182 C ASN A 552 -12.529 -1.872 30.749 1.00 47.94 C
ANISOU 4182 C ASN A 552 5616 6241 6357 -73 -32 380 C
ATOM 4183 O ASN A 552 -13.244 -0.901 30.996 1.00 50.69 O
ANISOU 4183 O ASN A 552 5961 6590 6707 -73 -17 368 O
ATOM 4184 CB ASN A 552 -10.296 -2.990 30.958 1.00 43.13 C
ANISOU 4184 CB ASN A 552 5021 5639 5726 -83 -50 400 C
ATOM 4185 CG ASN A 552 -8.922 -3.060 30.340 1.00 41.73 C
ANISOU 4185 CG ASN A 552 4856 5457 5542 -77 -61 402 C
ATOM 4186 OD1 ASN A 552 -8.741 -3.670 29.291 1.00 40.67 O
ANISOU 4186 OD1 ASN A 552 4722 5309 5420 -67 -76 403 O
ATOM 4187 ND2 ASN A 552 -7.948 -2.418 30.977 1.00 40.32 N
ANISOU 4187 ND2 ASN A 552 4686 5288 5343 -85 -53 401 N
ATOM 4188 N ARG A 553 -13.004 -3.100 30.599 1.00 52.94 N
ANISOU 4188 N ARG A 553 6240 6869 7004 -75 -44 392 N
ATOM 4189 CA ARG A 553 -14.409 -3.402 30.829 1.00 56.96 C
ANISOU 4189 CA ARG A 553 6734 7376 7531 -76 -39 393 C
ATOM 4190 C ARG A 553 -14.536 -4.658 31.710 1.00 56.55 C
ANISOU 4190 C ARG A 553 6673 7333 7479 -92 -41 410 C
ATOM 4191 O ARG A 553 -15.438 -5.489 31.534 1.00 55.73 O
ANISOU 4191 O ARG A 553 6557 7223 7394 -91 -48 417 O
ATOM 4192 CB ARG A 553 -15.143 -3.518 29.485 1.00 62.11 C
ANISOU 4192 CB ARG A 553 7382 8008 8208 -59 -54 388 C
ATOM 4193 CG ARG A 553 -15.212 -2.194 28.731 1.00 67.25 C
ANISOU 4193 CG ARG A 553 8040 8650 8861 -46 -51 371 C
ATOM 4194 CD ARG A 553 -16.052 -2.275 27.468 1.00 76.70 C
ANISOU 4194 CD ARG A 553 9232 9827 10081 -31 -67 368 C
ATOM 4195 NE ARG A 553 -15.243 -2.463 26.264 1.00 84.81 N
ANISOU 4195 NE ARG A 553 10274 10844 11105 -21 -86 368 N
ATOM 4196 CZ ARG A 553 -15.731 -2.504 25.024 1.00 90.52 C
ANISOU 4196 CZ ARG A 553 10998 11549 11843 -9 -102 365 C
ATOM 4197 NH1 ARG A 553 -17.039 -2.376 24.798 1.00 87.80 N
ANISOU 4197 NH1 ARG A 553 10642 11195 11522 -4 -104 362 N
ATOM 4198 NH2 ARG A 553 -14.904 -2.674 24.002 1.00 93.19 N
ANISOU 4198 NH2 ARG A 553 11351 11879 12175 -2 -116 365 N
ATOM 4199 N ILE A 554 -13.607 -4.769 32.661 1.00 54.51 N
ANISOU 4199 N ILE A 554 6422 7090 7198 -107 -36 418 N
ATOM 4200 CA ILE A 554 -13.500 -5.914 33.567 1.00 53.38 C
ANISOU 4200 CA ILE A 554 6273 6956 7050 -125 -40 437 C
ATOM 4201 C ILE A 554 -14.752 -6.061 34.432 1.00 51.20 C
ANISOU 4201 C ILE A 554 5984 6689 6780 -137 -25 438 C
ATOM 4202 O ILE A 554 -15.139 -5.134 35.150 1.00 45.71 O
ANISOU 4202 O ILE A 554 5289 6004 6074 -145 -3 427 O
ATOM 4203 CB ILE A 554 -12.220 -5.836 34.449 1.00 51.85 C
ANISOU 4203 CB ILE A 554 6091 6777 6831 -140 -38 445 C
ATOM 4204 CG1 ILE A 554 -10.964 -5.846 33.568 1.00 52.09 C
ANISOU 4204 CG1 ILE A 554 6133 6799 6860 -128 -54 445 C
ATOM 4205 CG2 ILE A 554 -12.154 -6.997 35.439 1.00 50.60 C
ANISOU 4205 CG2 ILE A 554 5927 6629 6668 -160 -44 467 C
ATOM 4206 CD1 ILE A 554 -9.716 -5.319 34.245 1.00 49.87 C
ANISOU 4206 CD1 ILE A 554 5864 6529 6555 -138 -50 447 C
ATOM 4207 N GLU A 555 -15.376 -7.235 34.334 1.00 52.33 N
ANISOU 4207 N GLU A 555 6115 6826 6940 -139 -36 451 N
ATOM 4208 CA GLU A 555 -16.540 -7.580 35.146 1.00 55.85 C
ANISOU 4208 CA GLU A 555 6548 7279 7392 -152 -23 455 C
ATOM 4209 C GLU A 555 -16.121 -8.288 36.438 1.00 57.78 C
ANISOU 4209 C GLU A 555 6793 7540 7617 -177 -20 473 C
ATOM 4210 O GLU A 555 -16.611 -7.931 37.508 1.00 59.41 O
ANISOU 4210 O GLU A 555 6999 7763 7812 -195 0 470 O
ATOM 4211 CB GLU A 555 -17.548 -8.402 34.339 1.00 55.64 C
ANISOU 4211 CB GLU A 555 6507 7236 7396 -141 -36 458 C
ATOM 4212 CG GLU A 555 -18.229 -7.594 33.246 1.00 57.21 C
ANISOU 4212 CG GLU A 555 6703 7419 7613 -120 -36 440 C
ATOM 4213 CD GLU A 555 -19.161 -8.409 32.372 1.00 60.73 C
ANISOU 4213 CD GLU A 555 7136 7847 8089 -108 -52 444 C
ATOM 4214 OE1 GLU A 555 -18.847 -9.569 32.048 1.00 63.59 O
ANISOU 4214 OE1 GLU A 555 7498 8204 8459 -108 -71 459 O
ATOM 4215 OE2 GLU A 555 -20.220 -7.878 31.991 1.00 64.70 O
ANISOU 4215 OE2 GLU A 555 7629 8341 8611 -100 -46 433 O
ATOM 4216 N THR A 556 -15.234 -9.285 36.328 1.00 57.57 N
ANISOU 4216 N THR A 556 6771 7512 7590 -180 -41 491 N
ATOM 4217 CA THR A 556 -14.456 -9.818 37.468 1.00 59.48 C
ANISOU 4217 CA THR A 556 7018 7769 7810 -204 -43 509 C
ATOM 4218 C THR A 556 -13.127 -10.411 37.047 1.00 57.46 C
ANISOU 4218 C THR A 556 6769 7506 7554 -199 -67 521 C
ATOM 4219 O THR A 556 -12.741 -10.351 35.885 1.00 56.72 O
ANISOU 4219 O THR A 556 6678 7397 7474 -179 -79 513 O
ATOM 4220 CB THR A 556 -15.155 -10.958 38.250 1.00 61.90 C
ANISOU 4220 CB THR A 556 7313 8081 8122 -222 -46 528 C
ATOM 4221 OG1 THR A 556 -15.673 -11.937 37.340 1.00 57.89 O
ANISOU 4221 OG1 THR A 556 6794 7556 7644 -208 -64 534 O
ATOM 4222 CG2 THR A 556 -16.239 -10.422 39.164 1.00 64.98 C
ANISOU 4222 CG2 THR A 556 7699 8486 8504 -237 -18 520 C
ATOM 4223 N SER A 557 -12.443 -10.992 38.027 1.00 58.96 N
ANISOU 4223 N SER A 557 6964 7708 7730 -221 -73 540 N
ATOM 4224 CA SER A 557 -11.289 -11.841 37.797 1.00 59.95 C
ANISOU 4224 CA SER A 557 7091 7825 7860 -220 -97 556 C
ATOM 4225 C SER A 557 -11.642 -13.271 38.189 1.00 60.24 C
ANISOU 4225 C SER A 557 7117 7860 7910 -233 -113 579 C
ATOM 4226 O SER A 557 -11.981 -13.538 39.343 1.00 62.51 O
ANISOU 4226 O SER A 557 7403 8162 8184 -257 -106 592 O
ATOM 4227 CB SER A 557 -10.085 -11.352 38.603 1.00 56.59 C
ANISOU 4227 CB SER A 557 6680 7413 7409 -235 -96 561 C
ATOM 4228 OG SER A 557 -9.112 -12.369 38.699 1.00 55.80 O
ANISOU 4228 OG SER A 557 6579 7307 7315 -242 -120 582 O
ATOM 4229 N LYS A 558 -11.565 -14.180 37.225 1.00 58.79 N
ANISOU 4229 N LYS A 558 6925 7658 7753 -218 -133 584 N
ATOM 4230 CA LYS A 558 -11.813 -15.588 37.484 1.00 64.68 C
ANISOU 4230 CA LYS A 558 7660 8400 8516 -228 -150 606 C
ATOM 4231 C LYS A 558 -10.526 -16.366 37.821 1.00 71.33 C
ANISOU 4231 C LYS A 558 8504 9239 9358 -239 -172 626 C
ATOM 4232 O LYS A 558 -9.419 -15.930 37.487 1.00 74.00 O
ANISOU 4232 O LYS A 558 8851 9574 9692 -231 -177 620 O
ATOM 4233 CB LYS A 558 -12.562 -16.225 36.304 1.00 65.57 C
ANISOU 4233 CB LYS A 558 7760 8493 8659 -208 -160 600 C
ATOM 4234 CG LYS A 558 -11.966 -15.960 34.926 1.00 64.13 C
ANISOU 4234 CG LYS A 558 7583 8294 8490 -183 -169 584 C
ATOM 4235 CD LYS A 558 -12.539 -16.908 33.874 1.00 63.82 C
ANISOU 4235 CD LYS A 558 7531 8234 8480 -168 -185 584 C
ATOM 4236 CE LYS A 558 -13.510 -16.234 32.911 1.00 60.93 C
ANISOU 4236 CE LYS A 558 7165 7860 8123 -149 -176 563 C
ATOM 4237 NZ LYS A 558 -14.706 -15.644 33.568 1.00 60.22 N
ANISOU 4237 NZ LYS A 558 7071 7783 8027 -157 -156 559 N
ATOM 4238 N GLY A 559 -10.684 -17.489 38.527 1.00 76.48 N
ANISOU 4238 N GLY A 559 9147 9892 10017 -257 -185 650 N
ATOM 4239 CA GLY A 559 -9.623 -18.493 38.691 1.00 76.15 C
ANISOU 4239 CA GLY A 559 9103 9843 9986 -264 -211 671 C
ATOM 4240 C GLY A 559 -8.588 -18.346 39.798 1.00 79.34 C
ANISOU 4240 C GLY A 559 9516 10259 10368 -287 -216 687 C
ATOM 4241 O GLY A 559 -7.396 -18.196 39.511 1.00 85.26 O
ANISOU 4241 O GLY A 559 10271 11002 11120 -281 -227 686 O
ATOM 4242 N ILE A 560 -9.038 -18.418 41.052 1.00 78.53 N
ANISOU 4242 N ILE A 560 9417 10176 10245 -314 -209 702 N
ATOM 4243 CA ILE A 560 -8.159 -18.453 42.247 1.00 79.29 C
ANISOU 4243 CA ILE A 560 9522 10285 10319 -341 -217 722 C
ATOM 4244 C ILE A 560 -7.352 -17.180 42.484 1.00 75.81 C
ANISOU 4244 C ILE A 560 9097 9854 9851 -342 -204 708 C
ATOM 4245 O ILE A 560 -6.367 -16.898 41.794 1.00 73.16 O
ANISOU 4245 O ILE A 560 8765 9507 9524 -326 -212 700 O
ATOM 4246 CB ILE A 560 -7.239 -19.708 42.286 1.00 83.23 C
ANISOU 4246 CB ILE A 560 10013 10770 10841 -348 -251 748 C
ATOM 4247 CG1 ILE A 560 -8.061 -20.978 42.553 1.00 84.96 C
ANISOU 4247 CG1 ILE A 560 10218 10984 11078 -359 -263 769 C
ATOM 4248 CG2 ILE A 560 -6.130 -19.556 43.328 1.00 82.97 C
ANISOU 4248 CG2 ILE A 560 9991 10747 10786 -372 -261 766 C
ATOM 4249 CD1 ILE A 560 -8.503 -21.178 43.989 1.00 84.37 C
ANISOU 4249 CD1 ILE A 560 10148 10930 10977 -394 -259 791 C
ATOM 4250 N LEU A 561 -7.766 -16.444 43.508 1.00 72.50 N
ANISOU 4250 N LEU A 561 8689 9457 9400 -362 -183 706 N
ATOM 4251 CA LEU A 561 -7.322 -15.079 43.733 1.00 71.51 C
ANISOU 4251 CA LEU A 561 8579 9344 9247 -362 -164 688 C
ATOM 4252 C LEU A 561 -6.077 -14.956 44.623 1.00 75.00 C
ANISOU 4252 C LEU A 561 9032 9793 9668 -383 -177 704 C
ATOM 4253 O LEU A 561 -5.563 -13.851 44.830 1.00 75.58 O
ANISOU 4253 O LEU A 561 9120 9877 9720 -384 -164 690 O
ATOM 4254 CB LEU A 561 -8.487 -14.248 44.293 1.00 70.54 C
ANISOU 4254 CB LEU A 561 8459 9238 9101 -371 -132 673 C
ATOM 4255 CG LEU A 561 -9.715 -13.867 43.436 1.00 69.35 C
ANISOU 4255 CG LEU A 561 8300 9082 8967 -349 -114 649 C
ATOM 4256 CD1 LEU A 561 -9.357 -12.847 42.365 1.00 70.75 C
ANISOU 4256 CD1 LEU A 561 8481 9249 9150 -320 -106 623 C
ATOM 4257 CD2 LEU A 561 -10.444 -15.055 42.813 1.00 68.64 C
ANISOU 4257 CD2 LEU A 561 8193 8977 8909 -339 -128 659 C
ATOM 4258 N GLN A 562 -5.595 -16.086 45.144 1.00 78.83 N
ANISOU 4258 N GLN A 562 9513 10275 10161 -401 -203 733 N
ATOM 4259 CA GLN A 562 -4.344 -16.118 45.919 1.00 78.43 C
ANISOU 4259 CA GLN A 562 9473 10229 10098 -421 -221 752 C
ATOM 4260 C GLN A 562 -3.152 -15.957 44.992 1.00 70.12 C
ANISOU 4260 C GLN A 562 8418 9158 9065 -398 -235 744 C
ATOM 4261 O GLN A 562 -2.115 -15.434 45.387 1.00 67.45 O
ANISOU 4261 O GLN A 562 8091 8824 8713 -406 -241 747 O
ATOM 4262 CB GLN A 562 -4.200 -17.439 46.679 1.00 84.16 C
ANISOU 4262 CB GLN A 562 10192 10953 10831 -446 -248 787 C
ATOM 4263 CG GLN A 562 -4.952 -17.520 47.999 1.00 88.11 C
ANISOU 4263 CG GLN A 562 10700 11476 11299 -481 -238 802 C
ATOM 4264 CD GLN A 562 -4.815 -18.882 48.669 1.00 89.98 C
ANISOU 4264 CD GLN A 562 10931 11710 11547 -505 -267 839 C
ATOM 4265 OE1 GLN A 562 -5.806 -19.477 49.093 1.00 90.46 O
ANISOU 4265 OE1 GLN A 562 10986 11778 11606 -520 -263 849 O
ATOM 4266 NE2 GLN A 562 -3.584 -19.384 48.762 1.00 88.33 N
ANISOU 4266 NE2 GLN A 562 10720 11488 11350 -511 -298 859 N
ATOM 4267 N HIS A 563 -3.341 -16.419 43.759 1.00 67.77 N
ANISOU 4267 N HIS A 563 8108 8841 8801 -370 -241 734 N
ATOM 4268 CA HIS A 563 -2.343 -16.427 42.691 1.00 68.68 C
ANISOU 4268 CA HIS A 563 8217 8935 8940 -346 -253 725 C
ATOM 4269 C HIS A 563 -1.742 -15.086 42.335 1.00 64.83 C
ANISOU 4269 C HIS A 563 7742 8451 8436 -333 -236 701 C
ATOM 4270 O HIS A 563 -0.645 -15.035 41.773 1.00 65.27 O
ANISOU 4270 O HIS A 563 7798 8494 8506 -321 -248 698 O
ATOM 4271 CB HIS A 563 -2.946 -17.083 41.444 1.00 75.56 C
ANISOU 4271 CB HIS A 563 9075 9788 9846 -320 -256 714 C
ATOM 4272 CG HIS A 563 -2.678 -18.572 41.334 1.00 81.02 C
ANISOU 4272 CG HIS A 563 9751 10463 10570 -324 -285 737 C
ATOM 4273 ND1 HIS A 563 -2.520 -19.194 40.146 1.00 81.18 N
ANISOU 4273 ND1 HIS A 563 9759 10460 10624 -300 -295 729 N
ATOM 4274 CD2 HIS A 563 -2.521 -19.554 42.316 1.00 82.35 C
ANISOU 4274 CD2 HIS A 563 9914 10633 10741 -349 -306 769 C
ATOM 4275 CE1 HIS A 563 -2.283 -20.503 40.352 1.00 80.84 C
ANISOU 4275 CE1 HIS A 563 9702 10404 10607 -310 -321 753 C
ATOM 4276 NE2 HIS A 563 -2.282 -20.723 41.680 1.00 85.90 N
ANISOU 4276 NE2 HIS A 563 10348 11060 11229 -340 -329 778 N
ATOM 4277 N PHE A 564 -2.445 -13.994 42.636 1.00 61.41 N
ANISOU 4277 N PHE A 564 7320 8035 7975 -335 -209 684 N
ATOM 4278 CA PHE A 564 -1.882 -12.658 42.458 1.00 60.39 C
ANISOU 4278 CA PHE A 564 7204 7911 7828 -326 -194 663 C
ATOM 4279 C PHE A 564 -0.653 -12.517 43.347 1.00 62.64 C
ANISOU 4279 C PHE A 564 7498 8203 8097 -346 -207 679 C
ATOM 4280 O PHE A 564 -0.687 -12.913 44.514 1.00 64.54 O
ANISOU 4280 O PHE A 564 7743 8456 8322 -375 -214 700 O
ATOM 4281 CB PHE A 564 -2.905 -11.559 42.765 1.00 61.99 C
ANISOU 4281 CB PHE A 564 7415 8132 8005 -328 -163 643 C
ATOM 4282 CG PHE A 564 -3.834 -11.251 41.618 1.00 61.77 C
ANISOU 4282 CG PHE A 564 7380 8094 7993 -301 -148 621 C
ATOM 4283 CD1 PHE A 564 -5.170 -11.645 41.661 1.00 64.47 C
ANISOU 4283 CD1 PHE A 564 7714 8439 8341 -303 -139 620 C
ATOM 4284 CD2 PHE A 564 -3.376 -10.572 40.493 1.00 60.54 C
ANISOU 4284 CD2 PHE A 564 7227 7926 7847 -275 -145 600 C
ATOM 4285 CE1 PHE A 564 -6.030 -11.369 40.605 1.00 63.27 C
ANISOU 4285 CE1 PHE A 564 7555 8277 8205 -279 -128 600 C
ATOM 4286 CE2 PHE A 564 -4.228 -10.296 39.434 1.00 60.67 C
ANISOU 4286 CE2 PHE A 564 7238 7934 7878 -252 -134 581 C
ATOM 4287 CZ PHE A 564 -5.556 -10.695 39.489 1.00 62.61 C
ANISOU 4287 CZ PHE A 564 7475 8182 8130 -254 -126 581 C
ATOM 4288 N PRO A 565 0.440 -11.958 42.791 1.00 63.65 N
ANISOU 4288 N PRO A 565 7630 8322 8231 -332 -211 669 N
ATOM 4289 CA PRO A 565 1.753 -11.949 43.436 1.00 61.68 C
ANISOU 4289 CA PRO A 565 7386 8072 7975 -348 -228 684 C
ATOM 4290 C PRO A 565 1.730 -11.299 44.812 1.00 60.99 C
ANISOU 4290 C PRO A 565 7314 8008 7848 -377 -220 692 C
ATOM 4291 O PRO A 565 1.009 -10.326 45.025 1.00 60.40 O
ANISOU 4291 O PRO A 565 7249 7949 7749 -378 -193 673 O
ATOM 4292 CB PRO A 565 2.607 -11.110 42.480 1.00 62.42 C
ANISOU 4292 CB PRO A 565 7483 8155 8076 -324 -223 663 C
ATOM 4293 CG PRO A 565 1.892 -11.153 41.175 1.00 60.43 C
ANISOU 4293 CG PRO A 565 7223 7891 7844 -296 -212 643 C
ATOM 4294 CD PRO A 565 0.446 -11.181 41.539 1.00 62.16 C
ANISOU 4294 CD PRO A 565 7441 8123 8051 -302 -196 641 C
ATOM 4295 N LYS A 566 2.521 -11.845 45.731 1.00 63.37 N
ANISOU 4295 N LYS A 566 7618 8312 8145 -402 -242 718 N
ATOM 4296 CA LYS A 566 2.613 -11.333 47.101 1.00 65.70 C
ANISOU 4296 CA LYS A 566 7929 8629 8402 -433 -238 728 C
ATOM 4297 C LYS A 566 3.158 -9.915 47.077 1.00 62.09 C
ANISOU 4297 C LYS A 566 7486 8180 7923 -427 -221 707 C
ATOM 4298 O LYS A 566 2.816 -9.079 47.917 1.00 60.59 O
ANISOU 4298 O LYS A 566 7311 8010 7698 -445 -202 700 O
ATOM 4299 CB LYS A 566 3.537 -12.221 47.943 1.00 71.33 C
ANISOU 4299 CB LYS A 566 8642 9339 9119 -459 -272 762 C
ATOM 4300 CG LYS A 566 3.451 -13.719 47.660 1.00 77.28 C
ANISOU 4300 CG LYS A 566 9378 10076 9908 -458 -298 785 C
ATOM 4301 CD LYS A 566 2.170 -14.346 48.204 1.00 81.87 C
ANISOU 4301 CD LYS A 566 9957 10669 10480 -474 -291 795 C
ATOM 4302 CE LYS A 566 1.092 -14.488 47.137 1.00 79.90 C
ANISOU 4302 CE LYS A 566 9695 10411 10249 -447 -274 775 C
ATOM 4303 NZ LYS A 566 -0.259 -14.655 47.740 1.00 81.71 N
ANISOU 4303 NZ LYS A 566 9926 10657 10460 -463 -257 777 N
ATOM 4304 N SER A 567 4.001 -9.673 46.079 1.00 60.63 N
ANISOU 4304 N SER A 567 7297 7978 7761 -402 -226 695 N
ATOM 4305 CA SER A 567 4.694 -8.413 45.877 1.00 59.50 C
ANISOU 4305 CA SER A 567 7164 7837 7605 -393 -214 676 C
ATOM 4306 C SER A 567 3.771 -7.291 45.401 1.00 58.54 C
ANISOU 4306 C SER A 567 7048 7724 7469 -376 -181 645 C
ATOM 4307 O SER A 567 4.083 -6.107 45.572 1.00 58.09 O
ANISOU 4307 O SER A 567 7004 7676 7391 -376 -166 629 O
ATOM 4308 CB SER A 567 5.817 -8.632 44.865 1.00 60.48 C
ANISOU 4308 CB SER A 567 7279 7937 7761 -371 -230 673 C
ATOM 4309 OG SER A 567 5.404 -9.557 43.870 1.00 61.68 O
ANISOU 4309 OG SER A 567 7415 8072 7946 -351 -236 673 O
ATOM 4310 N LEU A 568 2.636 -7.669 44.816 1.00 55.81 N
ANISOU 4310 N LEU A 568 6693 7375 7135 -363 -170 637 N
ATOM 4311 CA LEU A 568 1.700 -6.712 44.234 1.00 53.04 C
ANISOU 4311 CA LEU A 568 6345 7028 6778 -346 -142 608 C
ATOM 4312 C LEU A 568 1.191 -5.670 45.231 1.00 54.86 C
ANISOU 4312 C LEU A 568 6589 7281 6972 -364 -118 598 C
ATOM 4313 O LEU A 568 0.298 -5.943 46.037 1.00 54.94 O
ANISOU 4313 O LEU A 568 6600 7305 6967 -383 -109 604 O
ATOM 4314 CB LEU A 568 0.537 -7.447 43.577 1.00 49.78 C
ANISOU 4314 CB LEU A 568 5918 6608 6386 -333 -138 606 C
ATOM 4315 CG LEU A 568 -0.538 -6.604 42.904 1.00 47.60 C
ANISOU 4315 CG LEU A 568 5643 6334 6110 -314 -112 579 C
ATOM 4316 CD1 LEU A 568 0.092 -5.570 41.978 1.00 48.51 C
ANISOU 4316 CD1 LEU A 568 5763 6440 6229 -291 -105 557 C
ATOM 4317 CD2 LEU A 568 -1.495 -7.522 42.159 1.00 46.24 C
ANISOU 4317 CD2 LEU A 568 5455 6150 5963 -300 -116 580 C
ATOM 4318 N ALA A 569 1.765 -4.470 45.144 1.00 56.55 N
ANISOU 4318 N ALA A 569 6813 7498 7173 -357 -106 580 N
ATOM 4319 CA ALA A 569 1.446 -3.364 46.053 1.00 55.68 C
ANISOU 4319 CA ALA A 569 6718 7409 7029 -374 -83 567 C
ATOM 4320 C ALA A 569 0.356 -2.409 45.543 1.00 54.98 C
ANISOU 4320 C ALA A 569 6627 7322 6938 -357 -54 538 C
ATOM 4321 O ALA A 569 -0.425 -1.888 46.342 1.00 53.11 O
ANISOU 4321 O ALA A 569 6396 7102 6680 -373 -32 529 O
ATOM 4322 CB ALA A 569 2.709 -2.593 46.407 1.00 52.39 C
ANISOU 4322 CB ALA A 569 6312 6994 6596 -380 -89 567 C
ATOM 4323 N PHE A 570 0.318 -2.181 44.226 1.00 55.74 N
ANISOU 4323 N PHE A 570 6716 7401 7059 -326 -53 524 N
ATOM 4324 CA PHE A 570 -0.641 -1.260 43.598 1.00 55.15 C
ANISOU 4324 CA PHE A 570 6640 7326 6989 -308 -29 497 C
ATOM 4325 C PHE A 570 -1.366 -1.922 42.431 1.00 54.65 C
ANISOU 4325 C PHE A 570 6562 7246 6955 -285 -33 494 C
ATOM 4326 O PHE A 570 -0.805 -2.068 41.342 1.00 55.28 O
ANISOU 4326 O PHE A 570 6638 7309 7054 -264 -45 492 O
ATOM 4327 CB PHE A 570 0.057 -0.001 43.082 1.00 59.06 C
ANISOU 4327 CB PHE A 570 7143 7817 7479 -293 -21 478 C
ATOM 4328 CG PHE A 570 0.701 0.834 44.152 1.00 65.20 C
ANISOU 4328 CG PHE A 570 7934 8609 8226 -313 -13 476 C
ATOM 4329 CD1 PHE A 570 2.008 0.578 44.569 1.00 65.59 C
ANISOU 4329 CD1 PHE A 570 7990 8659 8269 -325 -33 492 C
ATOM 4330 CD2 PHE A 570 0.018 1.908 44.717 1.00 68.58 C
ANISOU 4330 CD2 PHE A 570 8370 9052 8636 -320 12 456 C
ATOM 4331 CE1 PHE A 570 2.611 1.358 45.547 1.00 68.27 C
ANISOU 4331 CE1 PHE A 570 8345 9013 8581 -344 -28 491 C
ATOM 4332 CE2 PHE A 570 0.618 2.693 45.696 1.00 70.02 C
ANISOU 4332 CE2 PHE A 570 8566 9248 8790 -340 19 453 C
ATOM 4333 CZ PHE A 570 1.915 2.417 46.110 1.00 69.51 C
ANISOU 4333 CZ PHE A 570 8509 9184 8717 -352 -1 471 C
ATOM 4334 N PHE A 571 -2.615 -2.311 42.659 1.00 52.98 N
ANISOU 4334 N PHE A 571 6342 7039 6746 -290 -23 494 N
ATOM 4335 CA PHE A 571 -3.417 -2.953 41.636 1.00 50.88 C
ANISOU 4335 CA PHE A 571 6064 6759 6509 -270 -28 492 C
ATOM 4336 C PHE A 571 -4.592 -2.053 41.284 1.00 52.52 C
ANISOU 4336 C PHE A 571 6267 6967 6719 -258 -4 468 C
ATOM 4337 O PHE A 571 -5.608 -2.075 41.967 1.00 57.58 O
ANISOU 4337 O PHE A 571 6905 7619 7354 -271 11 466 O
ATOM 4338 CB PHE A 571 -3.927 -4.303 42.148 1.00 48.35 C
ANISOU 4338 CB PHE A 571 5733 6440 6194 -285 -39 514 C
ATOM 4339 CG PHE A 571 -4.607 -5.150 41.098 1.00 46.41 C
ANISOU 4339 CG PHE A 571 5474 6179 5979 -266 -48 515 C
ATOM 4340 CD1 PHE A 571 -4.754 -4.704 39.783 1.00 45.91 C
ANISOU 4340 CD1 PHE A 571 5408 6100 5935 -238 -47 498 C
ATOM 4341 CD2 PHE A 571 -5.122 -6.393 41.437 1.00 44.04 C
ANISOU 4341 CD2 PHE A 571 5165 5879 5689 -277 -59 535 C
ATOM 4342 CE1 PHE A 571 -5.384 -5.488 38.833 1.00 44.37 C
ANISOU 4342 CE1 PHE A 571 5202 5890 5766 -222 -56 499 C
ATOM 4343 CE2 PHE A 571 -5.755 -7.181 40.490 1.00 44.17 C
ANISOU 4343 CE2 PHE A 571 5168 5879 5733 -260 -68 536 C
ATOM 4344 CZ PHE A 571 -5.886 -6.726 39.188 1.00 44.44 C
ANISOU 4344 CZ PHE A 571 5201 5899 5785 -233 -67 517 C
ATOM 4345 N ASN A 572 -4.459 -1.272 40.215 1.00 53.40 N
ANISOU 4345 N ASN A 572 6380 7066 6842 -234 -1 451 N
ATOM 4346 CA ASN A 572 -5.524 -0.357 39.797 1.00 53.40 C
ANISOU 4346 CA ASN A 572 6376 7063 6848 -221 18 428 C
ATOM 4347 C ASN A 572 -6.614 -1.048 38.985 1.00 52.52 C
ANISOU 4347 C ASN A 572 6251 6940 6763 -207 14 428 C
ATOM 4348 O ASN A 572 -6.333 -1.701 37.977 1.00 52.06 O
ANISOU 4348 O ASN A 572 6189 6866 6723 -192 -3 434 O
ATOM 4349 CB ASN A 572 -4.947 0.829 39.016 1.00 55.70 C
ANISOU 4349 CB ASN A 572 6675 7347 7140 -203 22 410 C
ATOM 4350 CG ASN A 572 -5.971 1.927 38.760 1.00 57.24 C
ANISOU 4350 CG ASN A 572 6867 7540 7339 -193 43 387 C
ATOM 4351 OD1 ASN A 572 -7.162 1.667 38.561 1.00 54.86 O
ANISOU 4351 OD1 ASN A 572 6554 7234 7053 -189 49 383 O
ATOM 4352 ND2 ASN A 572 -5.503 3.167 38.751 1.00 56.59 N
ANISOU 4352 ND2 ASN A 572 6794 7460 7247 -189 53 372 N
ATOM 4353 N LEU A 573 -7.858 -0.885 39.426 1.00 51.29 N
ANISOU 4353 N LEU A 573 6087 6790 6608 -213 32 420 N
ATOM 4354 CA LEU A 573 -9.001 -1.476 38.737 1.00 52.17 C
ANISOU 4354 CA LEU A 573 6185 6890 6745 -201 29 420 C
ATOM 4355 C LEU A 573 -10.136 -0.482 38.501 1.00 52.81 C
ANISOU 4355 C LEU A 573 6259 6968 6836 -192 49 397 C
ATOM 4356 O LEU A 573 -11.216 -0.867 38.039 1.00 55.06 O
ANISOU 4356 O LEU A 573 6532 7244 7143 -183 49 395 O
ATOM 4357 CB LEU A 573 -9.513 -2.713 39.492 1.00 52.61 C
ANISOU 4357 CB LEU A 573 6233 6954 6803 -219 25 439 C
ATOM 4358 CG LEU A 573 -8.748 -4.026 39.266 1.00 52.90 C
ANISOU 4358 CG LEU A 573 6269 6984 6846 -221 -1 462 C
ATOM 4359 CD1 LEU A 573 -9.211 -5.107 40.228 1.00 52.45 C
ANISOU 4359 CD1 LEU A 573 6205 6937 6785 -243 -4 482 C
ATOM 4360 CD2 LEU A 573 -8.867 -4.516 37.830 1.00 50.95 C
ANISOU 4360 CD2 LEU A 573 6014 6716 6627 -196 -18 461 C
ATOM 4361 N THR A 574 -9.880 0.792 38.802 1.00 51.00 N
ANISOU 4361 N THR A 574 6038 6745 6593 -192 66 381 N
ATOM 4362 CA THR A 574 -10.863 1.866 38.631 1.00 51.11 C
ANISOU 4362 CA THR A 574 6046 6755 6618 -184 86 358 C
ATOM 4363 C THR A 574 -11.278 2.035 37.170 1.00 50.72 C
ANISOU 4363 C THR A 574 5991 6684 6596 -157 74 351 C
ATOM 4364 O THR A 574 -10.554 1.621 36.267 1.00 49.82 O
ANISOU 4364 O THR A 574 5882 6560 6487 -145 54 359 O
ATOM 4365 CB THR A 574 -10.315 3.215 39.125 1.00 53.39 C
ANISOU 4365 CB THR A 574 6345 7051 6886 -188 102 342 C
ATOM 4366 OG1 THR A 574 -9.361 3.718 38.179 1.00 58.88 O
ANISOU 4366 OG1 THR A 574 7050 7736 7584 -171 89 339 O
ATOM 4367 CG2 THR A 574 -9.651 3.072 40.491 1.00 53.20 C
ANISOU 4367 CG2 THR A 574 6331 7048 6831 -215 109 350 C
ATOM 4368 N ASN A 575 -12.441 2.652 36.953 1.00 50.97 N
ANISOU 4368 N ASN A 575 6011 6708 6645 -149 88 335 N
ATOM 4369 CA ASN A 575 -13.013 2.887 35.612 1.00 50.29 C
ANISOU 4369 CA ASN A 575 5919 6601 6586 -126 77 327 C
ATOM 4370 C ASN A 575 -13.240 1.617 34.783 1.00 48.96 C
ANISOU 4370 C ASN A 575 5744 6421 6435 -117 54 343 C
ATOM 4371 O ASN A 575 -13.021 1.591 33.569 1.00 49.17 O
ANISOU 4371 O ASN A 575 5774 6432 6474 -100 37 343 O
ATOM 4372 CB ASN A 575 -12.200 3.935 34.836 1.00 50.47 C
ANISOU 4372 CB ASN A 575 5953 6616 6606 -112 72 317 C
ATOM 4373 CG ASN A 575 -12.240 5.301 35.494 1.00 51.87 C
ANISOU 4373 CG ASN A 575 6133 6801 6773 -117 94 298 C
ATOM 4374 OD1 ASN A 575 -13.170 6.074 35.273 1.00 56.31 O
ANISOU 4374 OD1 ASN A 575 6686 7355 7354 -109 105 283 O
ATOM 4375 ND2 ASN A 575 -11.229 5.608 36.303 1.00 48.67 N
ANISOU 4375 ND2 ASN A 575 5740 6410 6340 -130 101 300 N
ATOM 4376 N ASN A 576 -13.676 0.561 35.454 1.00 48.84 N
ANISOU 4376 N ASN A 576 5721 6414 6420 -131 55 356 N
ATOM 4377 CA ASN A 576 -14.068 -0.668 34.775 1.00 49.01 C
ANISOU 4377 CA ASN A 576 5735 6424 6461 -124 35 370 C
ATOM 4378 C ASN A 576 -15.577 -0.785 34.806 1.00 49.27 C
ANISOU 4378 C ASN A 576 5750 6452 6517 -123 44 364 C
ATOM 4379 O ASN A 576 -16.267 0.212 35.007 1.00 49.80 O
ANISOU 4379 O ASN A 576 5812 6519 6590 -121 62 347 O
ATOM 4380 CB ASN A 576 -13.393 -1.886 35.413 1.00 48.39 C
ANISOU 4380 CB ASN A 576 5659 6356 6369 -139 25 391 C
ATOM 4381 CG ASN A 576 -12.016 -2.154 34.833 1.00 47.01 C
ANISOU 4381 CG ASN A 576 5496 6177 6186 -133 6 399 C
ATOM 4382 OD1 ASN A 576 -10.987 -1.846 35.439 1.00 45.97 O
ANISOU 4382 OD1 ASN A 576 5376 6056 6032 -143 9 402 O
ATOM 4383 ND2 ASN A 576 -11.994 -2.705 33.643 1.00 45.24 N
ANISOU 4383 ND2 ASN A 576 5271 5936 5980 -117 -12 402 N
ATOM 4384 N SER A 577 -16.091 -1.988 34.594 1.00 49.57 N
ANISOU 4384 N SER A 577 5779 6485 6570 -123 32 378 N
ATOM 4385 CA SER A 577 -17.524 -2.214 34.657 1.00 48.83 C
ANISOU 4385 CA SER A 577 5667 6385 6499 -123 39 374 C
ATOM 4386 C SER A 577 -17.829 -3.549 35.356 1.00 47.49 C
ANISOU 4386 C SER A 577 5490 6224 6330 -139 36 393 C
ATOM 4387 O SER A 577 -18.132 -4.548 34.714 1.00 47.31 O
ANISOU 4387 O SER A 577 5460 6190 6324 -132 18 404 O
ATOM 4388 CB SER A 577 -18.150 -2.097 33.253 1.00 51.17 C
ANISOU 4388 CB SER A 577 5958 6659 6825 -100 23 368 C
ATOM 4389 OG SER A 577 -17.586 -3.014 32.328 1.00 51.47 O
ANISOU 4389 OG SER A 577 6002 6687 6866 -91 -2 381 O
ATOM 4390 N VAL A 578 -17.733 -3.540 36.686 1.00 48.70 N
ANISOU 4390 N VAL A 578 5644 6396 6461 -161 55 396 N
ATOM 4391 CA VAL A 578 -17.804 -4.750 37.522 1.00 49.82 C
ANISOU 4391 CA VAL A 578 5783 6550 6596 -181 52 416 C
ATOM 4392 C VAL A 578 -19.234 -5.250 37.724 1.00 52.75 C
ANISOU 4392 C VAL A 578 6135 6917 6989 -185 61 416 C
ATOM 4393 O VAL A 578 -20.151 -4.453 37.958 1.00 54.03 O
ANISOU 4393 O VAL A 578 6288 7080 7160 -185 82 398 O
ATOM 4394 CB VAL A 578 -17.171 -4.493 38.910 1.00 50.12 C
ANISOU 4394 CB VAL A 578 5831 6611 6600 -206 69 419 C
ATOM 4395 CG1 VAL A 578 -17.385 -5.676 39.850 1.00 50.85 C
ANISOU 4395 CG1 VAL A 578 5919 6715 6685 -229 67 439 C
ATOM 4396 CG2 VAL A 578 -15.689 -4.178 38.781 1.00 49.61 C
ANISOU 4396 CG2 VAL A 578 5784 6549 6514 -204 57 422 C
ATOM 4397 N ALA A 579 -19.410 -6.570 37.652 1.00 54.25 N
ANISOU 4397 N ALA A 579 6318 7105 7189 -189 44 435 N
ATOM 4398 CA ALA A 579 -20.714 -7.201 37.873 1.00 55.91 C
ANISOU 4398 CA ALA A 579 6510 7311 7419 -194 51 439 C
ATOM 4399 C ALA A 579 -20.908 -7.669 39.323 1.00 59.47 C
ANISOU 4399 C ALA A 579 6960 7784 7851 -224 68 449 C
ATOM 4400 O ALA A 579 -20.196 -8.554 39.809 1.00 59.71 O
ANISOU 4400 O ALA A 579 6997 7823 7866 -238 55 470 O
ATOM 4401 CB ALA A 579 -20.933 -8.348 36.894 1.00 54.58 C
ANISOU 4401 CB ALA A 579 6334 7126 7276 -181 23 452 C
ATOM 4402 N CYS A 580 -21.882 -7.063 40.000 1.00 63.51 N
ANISOU 4402 N CYS A 580 7462 8303 8366 -234 96 435 N
ATOM 4403 CA CYS A 580 -22.180 -7.364 41.406 1.00 67.17 C
ANISOU 4403 CA CYS A 580 7924 8786 8809 -264 118 441 C
ATOM 4404 C CYS A 580 -23.278 -8.436 41.584 1.00 67.66 C
ANISOU 4404 C CYS A 580 7969 8846 8892 -272 117 453 C
ATOM 4405 O CYS A 580 -24.201 -8.271 42.379 1.00 67.81 O
ANISOU 4405 O CYS A 580 7977 8874 8911 -288 144 445 O
ATOM 4406 CB CYS A 580 -22.507 -6.062 42.160 1.00 67.69 C
ANISOU 4406 CB CYS A 580 7992 8865 8862 -274 152 417 C
ATOM 4407 SG CYS A 580 -21.108 -4.908 42.193 1.00 74.14 S
ANISOU 4407 SG CYS A 580 8831 9688 9649 -271 153 406 S
ATOM 4408 N ILE A 581 -23.147 -9.535 40.839 1.00 68.24 N
ANISOU 4408 N ILE A 581 8038 8906 8982 -262 88 471 N
ATOM 4409 CA ILE A 581 -24.065 -10.682 40.910 1.00 70.72 C
ANISOU 4409 CA ILE A 581 8336 9216 9316 -268 82 486 C
ATOM 4410 C ILE A 581 -23.520 -11.803 41.816 1.00 76.75 C
ANISOU 4410 C ILE A 581 9106 9994 10059 -293 73 513 C
ATOM 4411 O ILE A 581 -22.414 -11.694 42.356 1.00 80.26 O
ANISOU 4411 O ILE A 581 9568 10452 10474 -306 69 521 O
ATOM 4412 CB ILE A 581 -24.410 -11.252 39.502 1.00 68.39 C
ANISOU 4412 CB ILE A 581 8031 8896 9057 -241 55 489 C
ATOM 4413 CG1 ILE A 581 -23.140 -11.633 38.725 1.00 64.26 C
ANISOU 4413 CG1 ILE A 581 7522 8365 8528 -228 25 500 C
ATOM 4414 CG2 ILE A 581 -25.277 -10.278 38.710 1.00 66.08 C
ANISOU 4414 CG2 ILE A 581 7728 8587 8790 -219 64 465 C
ATOM 4415 CD1 ILE A 581 -23.388 -12.504 37.511 1.00 61.60 C
ANISOU 4415 CD1 ILE A 581 7176 8006 8220 -208 -3 507 C
ATOM 4416 N CYS A 582 -24.299 -12.875 41.973 1.00 81.67 N
ANISOU 4416 N CYS A 582 9716 10615 10699 -302 67 528 N
ATOM 4417 CA CYS A 582 -23.933 -13.991 42.854 1.00 84.67 C
ANISOU 4417 CA CYS A 582 10099 11007 11062 -327 58 555 C
ATOM 4418 C CYS A 582 -22.909 -14.952 42.243 1.00 80.79 C
ANISOU 4418 C CYS A 582 9614 10505 10574 -319 21 576 C
ATOM 4419 O CYS A 582 -22.325 -15.774 42.951 1.00 79.52 O
ANISOU 4419 O CYS A 582 9459 10355 10398 -339 10 600 O
ATOM 4420 CB CYS A 582 -25.179 -14.770 43.311 1.00 92.99 C
ANISOU 4420 CB CYS A 582 11135 12062 12132 -341 68 563 C
ATOM 4421 SG CYS A 582 -26.257 -13.923 44.499 1.00106.98 S
ANISOU 4421 SG CYS A 582 12901 13853 13891 -365 115 544 S
ATOM 4422 N GLU A 583 -22.687 -14.857 40.937 1.00 79.20 N
ANISOU 4422 N GLU A 583 9411 10284 10395 -289 2 568 N
ATOM 4423 CA GLU A 583 -21.707 -15.723 40.281 1.00 82.27 C
ANISOU 4423 CA GLU A 583 9806 10662 10790 -279 -30 585 C
ATOM 4424 C GLU A 583 -20.275 -15.389 40.715 1.00 77.81 C
ANISOU 4424 C GLU A 583 9260 10108 10195 -288 -35 590 C
ATOM 4425 O GLU A 583 -19.392 -16.251 40.694 1.00 74.69 O
ANISOU 4425 O GLU A 583 8869 9710 9799 -292 -59 610 O
ATOM 4426 CB GLU A 583 -21.842 -15.645 38.754 1.00 88.49 C
ANISOU 4426 CB GLU A 583 10588 11426 11606 -247 -46 573 C
ATOM 4427 CG GLU A 583 -21.419 -16.909 38.014 1.00 95.34 C
ANISOU 4427 CG GLU A 583 11452 12278 12493 -238 -79 590 C
ATOM 4428 CD GLU A 583 -22.286 -18.118 38.354 1.00102.10 C
ANISOU 4428 CD GLU A 583 12293 13132 13368 -249 -85 608 C
ATOM 4429 OE1 GLU A 583 -23.515 -17.953 38.519 1.00104.12 O
ANISOU 4429 OE1 GLU A 583 12536 13388 13635 -251 -69 601 O
ATOM 4430 OE2 GLU A 583 -21.740 -19.240 38.455 1.00100.90 O
ANISOU 4430 OE2 GLU A 583 12140 12977 13220 -257 -107 630 O
ATOM 4431 N HIS A 584 -20.064 -14.140 41.129 1.00 72.86 N
ANISOU 4431 N HIS A 584 8644 9494 9546 -292 -12 573 N
ATOM 4432 CA HIS A 584 -18.729 -13.636 41.434 1.00 71.36 C
ANISOU 4432 CA HIS A 584 8471 9312 9329 -297 -16 574 C
ATOM 4433 C HIS A 584 -18.531 -13.306 42.892 1.00 71.71 C
ANISOU 4433 C HIS A 584 8525 9381 9339 -328 2 579 C
ATOM 4434 O HIS A 584 -17.839 -12.336 43.221 1.00 72.30 O
ANISOU 4434 O HIS A 584 8614 9465 9389 -332 13 568 O
ATOM 4435 CB HIS A 584 -18.423 -12.407 40.576 1.00 68.01 C
ANISOU 4435 CB HIS A 584 8054 8880 8906 -273 -10 549 C
ATOM 4436 CG HIS A 584 -18.691 -12.600 39.098 1.00 67.99 C
ANISOU 4436 CG HIS A 584 8043 8854 8935 -243 -27 541 C
ATOM 4437 ND1 HIS A 584 -18.199 -13.646 38.396 1.00 68.06 N
ANISOU 4437 ND1 HIS A 584 8049 8849 8959 -234 -55 556 N
ATOM 4438 CD2 HIS A 584 -19.407 -11.821 38.190 1.00 65.52 C
ANISOU 4438 CD2 HIS A 584 7724 8528 8640 -221 -19 520 C
ATOM 4439 CE1 HIS A 584 -18.596 -13.551 37.111 1.00 64.70 C
ANISOU 4439 CE1 HIS A 584 7619 8405 8559 -208 -64 544 C
ATOM 4440 NE2 HIS A 584 -19.333 -12.433 36.985 1.00 66.26 N
ANISOU 4440 NE2 HIS A 584 7814 8602 8757 -201 -44 523 N
ATOM 4441 N GLN A 585 -19.122 -14.113 43.775 1.00 69.09 N
ANISOU 4441 N GLN A 585 8187 9059 9003 -352 6 596 N
ATOM 4442 CA GLN A 585 -19.030 -13.897 45.222 1.00 68.29 C
ANISOU 4442 CA GLN A 585 8096 8982 8867 -387 25 602 C
ATOM 4443 C GLN A 585 -17.587 -13.829 45.672 1.00 67.05 C
ANISOU 4443 C GLN A 585 7957 8833 8683 -398 11 615 C
ATOM 4444 O GLN A 585 -17.223 -12.964 46.471 1.00 66.18 O
ANISOU 4444 O GLN A 585 7860 8740 8542 -414 29 606 O
ATOM 4445 CB GLN A 585 -19.688 -15.034 45.992 1.00 69.88 C
ANISOU 4445 CB GLN A 585 8289 9191 9069 -411 23 625 C
ATOM 4446 CG GLN A 585 -21.175 -15.194 45.807 1.00 72.03 C
ANISOU 4446 CG GLN A 585 8542 9457 9366 -407 40 615 C
ATOM 4447 CD GLN A 585 -21.662 -16.519 46.351 1.00 73.76 C
ANISOU 4447 CD GLN A 585 8752 9679 9591 -428 30 642 C
ATOM 4448 OE1 GLN A 585 -21.987 -17.432 45.591 1.00 77.28 O
ANISOU 4448 OE1 GLN A 585 9185 10108 10067 -413 9 652 O
ATOM 4449 NE2 GLN A 585 -21.710 -16.635 47.674 1.00 74.04 N
ANISOU 4449 NE2 GLN A 585 8796 9737 9597 -463 45 653 N
ATOM 4450 N LYS A 586 -16.780 -14.761 45.163 1.00 66.49 N
ANISOU 4450 N LYS A 586 7886 8750 8625 -390 -21 635 N
ATOM 4451 CA LYS A 586 -15.369 -14.866 45.528 1.00 70.38 C
ANISOU 4451 CA LYS A 586 8393 9247 9099 -401 -40 650 C
ATOM 4452 C LYS A 586 -14.645 -13.541 45.304 1.00 67.59 C
ANISOU 4452 C LYS A 586 8053 8896 8729 -389 -29 628 C
ATOM 4453 O LYS A 586 -14.139 -12.941 46.259 1.00 62.92 O
ANISOU 4453 O LYS A 586 7476 8323 8106 -410 -17 628 O
ATOM 4454 CB LYS A 586 -14.677 -16.021 44.779 1.00 71.06 C
ANISOU 4454 CB LYS A 586 8473 9314 9210 -388 -76 669 C
ATOM 4455 CG LYS A 586 -14.692 -17.358 45.513 1.00 72.30 C
ANISOU 4455 CG LYS A 586 8625 9474 9369 -413 -95 702 C
ATOM 4456 CD LYS A 586 -16.058 -18.040 45.457 1.00 75.69 C
ANISOU 4456 CD LYS A 586 9038 9900 9818 -414 -88 705 C
ATOM 4457 CE LYS A 586 -16.036 -19.415 46.117 1.00 75.50 C
ANISOU 4457 CE LYS A 586 9008 9878 9798 -438 -110 738 C
ATOM 4458 NZ LYS A 586 -17.320 -20.146 45.910 1.00 73.44 N
ANISOU 4458 NZ LYS A 586 8730 9610 9560 -436 -106 741 N
ATOM 4459 N PHE A 587 -14.643 -13.080 44.050 1.00 69.94 N
ANISOU 4459 N PHE A 587 8346 9178 9049 -357 -31 609 N
ATOM 4460 CA PHE A 587 -14.002 -11.820 43.659 1.00 65.85 C
ANISOU 4460 CA PHE A 587 7839 8659 8520 -342 -22 588 C
ATOM 4461 C PHE A 587 -14.460 -10.631 44.508 1.00 63.72 C
ANISOU 4461 C PHE A 587 7577 8408 8225 -356 10 569 C
ATOM 4462 O PHE A 587 -13.638 -9.854 44.999 1.00 61.57 O
ANISOU 4462 O PHE A 587 7319 8146 7927 -365 16 564 O
ATOM 4463 CB PHE A 587 -14.230 -11.533 42.167 1.00 63.84 C
ANISOU 4463 CB PHE A 587 7577 8383 8295 -307 -28 570 C
ATOM 4464 CG PHE A 587 -13.594 -10.252 41.697 1.00 65.78 C
ANISOU 4464 CG PHE A 587 7834 8628 8531 -291 -19 549 C
ATOM 4465 CD1 PHE A 587 -12.251 -10.219 41.336 1.00 64.65 C
ANISOU 4465 CD1 PHE A 587 7701 8479 8383 -284 -37 554 C
ATOM 4466 CD2 PHE A 587 -14.331 -9.071 41.636 1.00 65.45 C
ANISOU 4466 CD2 PHE A 587 7792 8589 8487 -284 6 524 C
ATOM 4467 CE1 PHE A 587 -11.659 -9.041 40.917 1.00 63.95 C
ANISOU 4467 CE1 PHE A 587 7623 8390 8286 -271 -29 535 C
ATOM 4468 CE2 PHE A 587 -13.740 -7.888 41.221 1.00 65.69 C
ANISOU 4468 CE2 PHE A 587 7832 8617 8508 -271 13 505 C
ATOM 4469 CZ PHE A 587 -12.404 -7.872 40.861 1.00 64.46 C
ANISOU 4469 CZ PHE A 587 7687 8457 8346 -264 -4 511 C
ATOM 4470 N LEU A 588 -15.773 -10.506 44.679 1.00 63.30 N
ANISOU 4470 N LEU A 588 7513 8358 8180 -359 32 558 N
ATOM 4471 CA LEU A 588 -16.366 -9.389 45.404 1.00 63.98 C
ANISOU 4471 CA LEU A 588 7602 8459 8248 -370 66 537 C
ATOM 4472 C LEU A 588 -15.978 -9.356 46.880 1.00 64.02 C
ANISOU 4472 C LEU A 588 7621 8487 8214 -407 78 547 C
ATOM 4473 O LEU A 588 -15.663 -8.291 47.414 1.00 59.79 O
ANISOU 4473 O LEU A 588 7097 7964 7655 -416 97 532 O
ATOM 4474 CB LEU A 588 -17.886 -9.401 45.229 1.00 64.35 C
ANISOU 4474 CB LEU A 588 7631 8500 8316 -365 85 524 C
ATOM 4475 CG LEU A 588 -18.357 -8.964 43.837 1.00 64.27 C
ANISOU 4475 CG LEU A 588 7610 8468 8340 -330 82 506 C
ATOM 4476 CD1 LEU A 588 -19.637 -9.672 43.413 1.00 62.94 C
ANISOU 4476 CD1 LEU A 588 7422 8289 8204 -322 81 508 C
ATOM 4477 CD2 LEU A 588 -18.526 -7.451 43.782 1.00 66.08 C
ANISOU 4477 CD2 LEU A 588 7843 8700 8564 -321 107 476 C
ATOM 4478 N GLN A 589 -15.994 -10.521 47.527 1.00 68.12 N
ANISOU 4478 N GLN A 589 8139 9014 8729 -430 64 574 N
ATOM 4479 CA GLN A 589 -15.571 -10.631 48.919 1.00 72.89 C
ANISOU 4479 CA GLN A 589 8758 9641 9296 -468 70 589 C
ATOM 4480 C GLN A 589 -14.115 -10.223 49.011 1.00 74.36 C
ANISOU 4480 C GLN A 589 8961 9829 9461 -469 54 594 C
ATOM 4481 O GLN A 589 -13.740 -9.351 49.791 1.00 82.52 O
ANISOU 4481 O GLN A 589 10009 10878 10464 -486 71 584 O
ATOM 4482 CB GLN A 589 -15.756 -12.064 49.441 1.00 76.09 C
ANISOU 4482 CB GLN A 589 9158 10048 9702 -489 52 621 C
ATOM 4483 CG GLN A 589 -15.282 -12.285 50.874 1.00 71.06 C
ANISOU 4483 CG GLN A 589 8538 9435 9026 -531 53 640 C
ATOM 4484 CD GLN A 589 -15.823 -11.248 51.840 1.00 72.51 C
ANISOU 4484 CD GLN A 589 8730 9639 9179 -553 92 619 C
ATOM 4485 OE1 GLN A 589 -15.107 -10.779 52.720 1.00 75.13 O
ANISOU 4485 OE1 GLN A 589 9081 9988 9476 -577 97 621 O
ATOM 4486 NE2 GLN A 589 -17.090 -10.880 51.677 1.00 72.58 N
ANISOU 4486 NE2 GLN A 589 8725 9647 9202 -546 121 597 N
ATOM 4487 N TRP A 590 -13.316 -10.866 48.172 1.00 71.31 N
ANISOU 4487 N TRP A 590 8572 9425 9095 -450 22 608 N
ATOM 4488 CA TRP A 590 -11.886 -10.644 48.058 1.00 69.46 C
ANISOU 4488 CA TRP A 590 8351 9189 8851 -447 2 615 C
ATOM 4489 C TRP A 590 -11.478 -9.184 47.977 1.00 67.77 C
ANISOU 4489 C TRP A 590 8148 8979 8621 -438 21 589 C
ATOM 4490 O TRP A 590 -10.467 -8.791 48.558 1.00 68.21 O
ANISOU 4490 O TRP A 590 8219 9045 8652 -452 16 594 O
ATOM 4491 CB TRP A 590 -11.418 -11.446 46.855 1.00 69.72 C
ANISOU 4491 CB TRP A 590 8373 9197 8917 -420 -27 625 C
ATOM 4492 CG TRP A 590 -10.003 -11.243 46.427 1.00 71.75 C
ANISOU 4492 CG TRP A 590 8640 9447 9175 -409 -48 628 C
ATOM 4493 CD1 TRP A 590 -8.875 -11.911 46.884 1.00 72.41 C
ANISOU 4493 CD1 TRP A 590 8730 9531 9252 -424 -74 653 C
ATOM 4494 CD2 TRP A 590 -9.514 -10.323 45.396 1.00 71.77 C
ANISOU 4494 CD2 TRP A 590 8645 9437 9187 -379 -45 606 C
ATOM 4495 NE1 TRP A 590 -7.751 -11.472 46.233 1.00 71.89 N
ANISOU 4495 NE1 TRP A 590 8669 9454 9190 -406 -86 647 N
ATOM 4496 CE2 TRP A 590 -8.062 -10.519 45.330 1.00 71.18 C
ANISOU 4496 CE2 TRP A 590 8578 9357 9109 -380 -69 619 C
ATOM 4497 CE3 TRP A 590 -10.109 -9.384 44.557 1.00 69.44 C
ANISOU 4497 CE3 TRP A 590 8345 9135 8901 -355 -26 578 C
ATOM 4498 CZ2 TRP A 590 -7.261 -9.794 44.460 1.00 71.69 C
ANISOU 4498 CZ2 TRP A 590 8646 9410 9179 -356 -72 604 C
ATOM 4499 CZ3 TRP A 590 -9.292 -8.660 43.683 1.00 68.70 C
ANISOU 4499 CZ3 TRP A 590 8257 9031 8813 -332 -31 564 C
ATOM 4500 CH2 TRP A 590 -7.902 -8.861 43.637 1.00 70.96 C
ANISOU 4500 CH2 TRP A 590 8552 9313 9096 -333 -53 576 C
ATOM 4501 N VAL A 591 -12.270 -8.368 47.281 1.00 66.32 N
ANISOU 4501 N VAL A 591 7956 8788 8451 -415 42 561 N
ATOM 4502 CA VAL A 591 -12.049 -6.918 47.214 1.00 64.59 C
ANISOU 4502 CA VAL A 591 7747 8574 8220 -407 63 534 C
ATOM 4503 C VAL A 591 -12.034 -6.268 48.611 1.00 69.46 C
ANISOU 4503 C VAL A 591 8376 9214 8798 -439 86 529 C
ATOM 4504 O VAL A 591 -11.337 -5.271 48.823 1.00 67.57 O
ANISOU 4504 O VAL A 591 8150 8981 8540 -440 94 517 O
ATOM 4505 CB VAL A 591 -13.074 -6.233 46.268 1.00 61.89 C
ANISOU 4505 CB VAL A 591 7391 8219 7904 -379 80 507 C
ATOM 4506 CG1 VAL A 591 -13.020 -4.715 46.368 1.00 62.99 C
ANISOU 4506 CG1 VAL A 591 7539 8364 8031 -374 105 479 C
ATOM 4507 CG2 VAL A 591 -12.837 -6.655 44.827 1.00 56.99 C
ANISOU 4507 CG2 VAL A 591 6762 7574 7315 -346 56 510 C
ATOM 4508 N LYS A 592 -12.773 -6.842 49.564 1.00 79.15 N
ANISOU 4508 N LYS A 592 9603 10457 10014 -467 98 539 N
ATOM 4509 CA LYS A 592 -12.817 -6.286 50.925 1.00 85.37 C
ANISOU 4509 CA LYS A 592 10404 11268 10762 -501 121 535 C
ATOM 4510 C LYS A 592 -11.521 -6.496 51.717 1.00 86.81 C
ANISOU 4510 C LYS A 592 10607 11463 10914 -526 102 556 C
ATOM 4511 O LYS A 592 -11.100 -5.595 52.443 1.00 86.07 O
ANISOU 4511 O LYS A 592 10528 11383 10790 -542 117 545 O
ATOM 4512 CB LYS A 592 -14.042 -6.762 51.734 1.00 90.59 C
ANISOU 4512 CB LYS A 592 11059 11943 11418 -526 143 537 C
ATOM 4513 CG LYS A 592 -13.747 -7.804 52.820 1.00 98.34 C
ANISOU 4513 CG LYS A 592 12050 12939 12374 -564 129 569 C
ATOM 4514 CD LYS A 592 -14.587 -7.628 54.087 1.00100.53 C
ANISOU 4514 CD LYS A 592 12333 13240 12623 -600 162 563 C
ATOM 4515 CE LYS A 592 -13.881 -6.768 55.134 1.00 97.56 C
ANISOU 4515 CE LYS A 592 11979 12884 12202 -628 175 556 C
ATOM 4516 NZ LYS A 592 -14.625 -6.709 56.422 1.00 91.80 N
ANISOU 4516 NZ LYS A 592 11257 12179 11441 -668 206 552 N
ATOM 4517 N GLU A 593 -10.893 -7.668 51.592 1.00 91.20 N
ANISOU 4517 N GLU A 593 11160 12010 11478 -529 67 587 N
ATOM 4518 CA GLU A 593 -9.669 -7.926 52.360 1.00 98.88 C
ANISOU 4518 CA GLU A 593 12150 12993 12425 -553 46 610 C
ATOM 4519 C GLU A 593 -8.418 -7.397 51.659 1.00 96.57 C
ANISOU 4519 C GLU A 593 11864 12688 12139 -531 28 606 C
ATOM 4520 O GLU A 593 -7.447 -7.013 52.316 1.00 96.93 O
ANISOU 4520 O GLU A 593 11925 12743 12158 -548 21 613 O
ATOM 4521 CB GLU A 593 -9.510 -9.403 52.755 1.00107.07 C
ANISOU 4521 CB GLU A 593 13185 14030 13467 -573 17 647 C
ATOM 4522 CG GLU A 593 -8.730 -9.572 54.063 1.00114.98 C
ANISOU 4522 CG GLU A 593 14207 15050 14430 -613 6 670 C
ATOM 4523 CD GLU A 593 -8.353 -11.009 54.397 1.00117.66 C
ANISOU 4523 CD GLU A 593 14544 15386 14776 -631 -28 709 C
ATOM 4524 OE1 GLU A 593 -8.217 -11.319 55.604 1.00117.67 O
ANISOU 4524 OE1 GLU A 593 14559 15405 14745 -671 -31 729 O
ATOM 4525 OE2 GLU A 593 -8.178 -11.828 53.468 1.00116.93 O
ANISOU 4525 OE2 GLU A 593 14436 15271 14719 -607 -52 721 O
ATOM 4526 N GLN A 594 -8.458 -7.352 50.329 1.00 92.40 N
ANISOU 4526 N GLN A 594 11322 12138 11645 -493 21 595 N
ATOM 4527 CA GLN A 594 -7.379 -6.752 49.546 1.00 87.85 C
ANISOU 4527 CA GLN A 594 10751 11550 11077 -470 8 587 C
ATOM 4528 C GLN A 594 -7.617 -5.255 49.354 1.00 84.31 C
ANISOU 4528 C GLN A 594 10307 11105 10620 -457 37 553 C
ATOM 4529 O GLN A 594 -7.374 -4.703 48.287 1.00 86.72 O
ANISOU 4529 O GLN A 594 10608 11396 10944 -427 36 538 O
ATOM 4530 CB GLN A 594 -7.228 -7.473 48.204 1.00 85.22 C
ANISOU 4530 CB GLN A 594 10402 11192 10783 -438 -14 592 C
ATOM 4531 CG GLN A 594 -7.059 -8.982 48.317 1.00 85.09 C
ANISOU 4531 CG GLN A 594 10379 11170 10781 -448 -43 624 C
ATOM 4532 CD GLN A 594 -5.781 -9.397 49.026 1.00 87.65 C
ANISOU 4532 CD GLN A 594 10714 11497 11089 -470 -68 649 C
ATOM 4533 OE1 GLN A 594 -4.780 -9.711 48.382 1.00 89.29 O
ANISOU 4533 OE1 GLN A 594 10920 11690 11316 -455 -92 658 O
ATOM 4534 NE2 GLN A 594 -5.809 -9.405 50.357 1.00 85.84 N
ANISOU 4534 NE2 GLN A 594 10497 11290 10828 -506 -62 662 N
ATOM 4535 N LYS A 595 -8.076 -4.610 50.421 1.00 86.22 N
ANISOU 4535 N LYS A 595 10559 11368 10832 -482 64 543 N
ATOM 4536 CA LYS A 595 -8.456 -3.200 50.420 1.00 88.49 C
ANISOU 4536 CA LYS A 595 10849 11660 11110 -475 95 510 C
ATOM 4537 C LYS A 595 -7.257 -2.286 50.157 1.00 84.81 C
ANISOU 4537 C LYS A 595 10396 11191 10636 -464 88 501 C
ATOM 4538 O LYS A 595 -7.330 -1.385 49.323 1.00 79.27 O
ANISOU 4538 O LYS A 595 9690 10478 9949 -438 98 478 O
ATOM 4539 CB LYS A 595 -9.087 -2.854 51.777 1.00 94.34 C
ANISOU 4539 CB LYS A 595 11600 12425 11819 -510 123 503 C
ATOM 4540 CG LYS A 595 -10.412 -2.103 51.724 1.00 94.22 C
ANISOU 4540 CG LYS A 595 11575 12413 11812 -503 160 473 C
ATOM 4541 CD LYS A 595 -11.168 -2.286 53.037 1.00 94.95 C
ANISOU 4541 CD LYS A 595 11672 12527 11877 -541 184 474 C
ATOM 4542 CE LYS A 595 -12.594 -1.750 52.985 1.00 96.72 C
ANISOU 4542 CE LYS A 595 11881 12751 12115 -535 220 446 C
ATOM 4543 NZ LYS A 595 -12.715 -0.345 53.467 1.00 91.20 N
ANISOU 4543 NZ LYS A 595 11190 12062 11398 -542 253 414 N
ATOM 4544 N GLN A 596 -6.159 -2.541 50.872 1.00 85.66 N
ANISOU 4544 N GLN A 596 10518 11307 10721 -486 70 521 N
ATOM 4545 CA GLN A 596 -4.958 -1.696 50.843 1.00 82.55 C
ANISOU 4545 CA GLN A 596 10136 10912 10314 -482 63 515 C
ATOM 4546 C GLN A 596 -4.251 -1.704 49.494 1.00 78.88 C
ANISOU 4546 C GLN A 596 9664 10425 9880 -447 43 514 C
ATOM 4547 O GLN A 596 -3.614 -0.719 49.124 1.00 72.42 O
ANISOU 4547 O GLN A 596 8852 9602 9059 -433 46 499 O
ATOM 4548 CB GLN A 596 -3.955 -2.141 51.914 1.00 83.79 C
ANISOU 4548 CB GLN A 596 10309 11082 10443 -514 43 541 C
ATOM 4549 CG GLN A 596 -4.521 -2.291 53.317 1.00 85.22 C
ANISOU 4549 CG GLN A 596 10501 11286 10590 -554 59 547 C
ATOM 4550 CD GLN A 596 -3.602 -3.084 54.229 1.00 86.67 C
ANISOU 4550 CD GLN A 596 10697 11478 10753 -586 31 581 C
ATOM 4551 OE1 GLN A 596 -2.490 -2.649 54.549 1.00 84.72 O
ANISOU 4551 OE1 GLN A 596 10464 11234 10490 -594 18 585 O
ATOM 4552 NE2 GLN A 596 -4.065 -4.254 54.659 1.00 83.81 N
ANISOU 4552 NE2 GLN A 596 10331 11121 10392 -605 20 605 N
ATOM 4553 N PHE A 597 -4.361 -2.820 48.776 1.00 79.71 N
ANISOU 4553 N PHE A 597 9756 10515 10013 -433 22 531 N
ATOM 4554 CA PHE A 597 -3.609 -3.030 47.533 1.00 79.68 C
ANISOU 4554 CA PHE A 597 9746 10489 10037 -403 0 533 C
ATOM 4555 C PHE A 597 -4.387 -2.635 46.266 1.00 76.07 C
ANISOU 4555 C PHE A 597 9277 10018 9608 -370 12 511 C
ATOM 4556 O PHE A 597 -3.860 -2.718 45.148 1.00 69.10 O
ANISOU 4556 O PHE A 597 8389 9117 8747 -345 -2 509 O
ATOM 4557 CB PHE A 597 -3.097 -4.480 47.451 1.00 83.90 C
ANISOU 4557 CB PHE A 597 10274 11015 10588 -408 -31 564 C
ATOM 4558 CG PHE A 597 -2.419 -4.965 48.714 1.00 89.94 C
ANISOU 4558 CG PHE A 597 11050 11794 11328 -443 -45 589 C
ATOM 4559 CD1 PHE A 597 -1.269 -4.336 49.200 1.00 88.92 C
ANISOU 4559 CD1 PHE A 597 10935 11670 11178 -454 -52 591 C
ATOM 4560 CD2 PHE A 597 -2.927 -6.055 49.417 1.00 89.66 C
ANISOU 4560 CD2 PHE A 597 11011 11766 11289 -466 -54 612 C
ATOM 4561 CE1 PHE A 597 -0.649 -4.778 50.358 1.00 84.80 C
ANISOU 4561 CE1 PHE A 597 10425 11161 10634 -487 -67 615 C
ATOM 4562 CE2 PHE A 597 -2.306 -6.502 50.574 1.00 88.60 C
ANISOU 4562 CE2 PHE A 597 10888 11643 11131 -500 -69 636 C
ATOM 4563 CZ PHE A 597 -1.168 -5.862 51.045 1.00 86.68 C
ANISOU 4563 CZ PHE A 597 10660 11406 10868 -511 -77 638 C
ATOM 4564 N LEU A 598 -5.634 -2.200 46.447 1.00 71.42 N
ANISOU 4564 N LEU A 598 8683 9435 9017 -371 38 494 N
ATOM 4565 CA LEU A 598 -6.478 -1.797 45.329 1.00 67.72 C
ANISOU 4565 CA LEU A 598 8203 8953 8575 -342 49 473 C
ATOM 4566 C LEU A 598 -6.642 -0.288 45.274 1.00 68.01 C
ANISOU 4566 C LEU A 598 8245 8993 8603 -334 73 445 C
ATOM 4567 O LEU A 598 -7.096 0.337 46.233 1.00 67.53 O
ANISOU 4567 O LEU A 598 8189 8948 8521 -353 96 433 O
ATOM 4568 CB LEU A 598 -7.846 -2.482 45.389 1.00 66.04 C
ANISOU 4568 CB LEU A 598 7975 8739 8374 -345 57 475 C
ATOM 4569 CG LEU A 598 -7.955 -3.985 45.110 1.00 66.38 C
ANISOU 4569 CG LEU A 598 8008 8774 8436 -345 34 500 C
ATOM 4570 CD1 LEU A 598 -9.394 -4.454 45.276 1.00 64.98 C
ANISOU 4570 CD1 LEU A 598 7818 8599 8270 -350 47 498 C
ATOM 4571 CD2 LEU A 598 -7.441 -4.347 43.724 1.00 65.12 C
ANISOU 4571 CD2 LEU A 598 7843 8592 8305 -316 11 502 C
ATOM 4572 N VAL A 599 -6.265 0.280 44.133 1.00 69.79 N
ANISOU 4572 N VAL A 599 8469 9202 8845 -306 67 433 N
ATOM 4573 CA VAL A 599 -6.252 1.726 43.925 1.00 71.49 C
ANISOU 4573 CA VAL A 599 8689 9417 9055 -296 86 407 C
ATOM 4574 C VAL A 599 -7.668 2.290 43.935 1.00 71.30 C
ANISOU 4574 C VAL A 599 8655 9393 9041 -292 112 386 C
ATOM 4575 O VAL A 599 -8.557 1.770 43.252 1.00 69.24 O
ANISOU 4575 O VAL A 599 8381 9122 8805 -278 109 386 O
ATOM 4576 CB VAL A 599 -5.531 2.098 42.603 1.00 72.93 C
ANISOU 4576 CB VAL A 599 8872 9580 9255 -267 71 401 C
ATOM 4577 CG1 VAL A 599 -5.561 3.602 42.355 1.00 71.74 C
ANISOU 4577 CG1 VAL A 599 8726 9428 9101 -256 90 375 C
ATOM 4578 CG2 VAL A 599 -4.092 1.596 42.622 1.00 72.33 C
ANISOU 4578 CG2 VAL A 599 8805 9503 9172 -271 48 420 C
ATOM 4579 N ASN A 600 -7.853 3.348 44.725 1.00 71.51 N
ANISOU 4579 N ASN A 600 8688 9433 9050 -304 136 368 N
ATOM 4580 CA ASN A 600 -9.133 4.050 44.870 1.00 73.96 C
ANISOU 4580 CA ASN A 600 8988 9743 9368 -303 164 345 C
ATOM 4581 C ASN A 600 -10.348 3.138 45.055 1.00 74.82 C
ANISOU 4581 C ASN A 600 9083 9854 9490 -309 170 351 C
ATOM 4582 O ASN A 600 -11.366 3.304 44.375 1.00 73.66 O
ANISOU 4582 O ASN A 600 8922 9694 9371 -292 178 338 O
ATOM 4583 CB ASN A 600 -9.362 5.024 43.705 1.00 74.49 C
ANISOU 4583 CB ASN A 600 9049 9792 9459 -273 167 324 C
ATOM 4584 CG ASN A 600 -8.570 6.308 43.848 1.00 73.12 C
ANISOU 4584 CG ASN A 600 8887 9622 9271 -271 175 308 C
ATOM 4585 OD1 ASN A 600 -7.341 6.304 43.819 1.00 71.87 O
ANISOU 4585 OD1 ASN A 600 8742 9465 9098 -272 160 319 O
ATOM 4586 ND2 ASN A 600 -9.278 7.420 43.988 1.00 74.69 N
ANISOU 4586 ND2 ASN A 600 9082 9821 9475 -268 200 283 N
ATOM 4587 N VAL A 601 -10.234 2.181 45.975 1.00 77.39 N
ANISOU 4587 N VAL A 601 9412 10193 9798 -335 166 371 N
ATOM 4588 CA VAL A 601 -11.360 1.316 46.341 1.00 81.69 C
ANISOU 4588 CA VAL A 601 9945 10742 10351 -346 173 378 C
ATOM 4589 C VAL A 601 -12.522 2.131 46.886 1.00 84.81 C
ANISOU 4589 C VAL A 601 10333 11144 10746 -354 209 352 C
ATOM 4590 O VAL A 601 -13.676 1.708 46.821 1.00 83.58 O
ANISOU 4590 O VAL A 601 10162 10985 10609 -353 219 350 O
ATOM 4591 CB VAL A 601 -10.985 0.251 47.395 1.00 82.97 C
ANISOU 4591 CB VAL A 601 10115 10920 10488 -377 164 404 C
ATOM 4592 CG1 VAL A 601 -10.736 -1.093 46.730 1.00 81.73 C
ANISOU 4592 CG1 VAL A 601 9951 10751 10350 -368 132 431 C
ATOM 4593 CG2 VAL A 601 -9.807 0.694 48.258 1.00 81.70 C
ANISOU 4593 CG2 VAL A 601 9974 10774 10292 -398 162 409 C
ATOM 4594 N GLU A 602 -12.197 3.309 47.411 1.00 90.05 N
ANISOU 4594 N GLU A 602 11006 11817 11391 -361 228 333 N
ATOM 4595 CA GLU A 602 -13.179 4.217 47.990 1.00 92.75 C
ANISOU 4595 CA GLU A 602 11342 12164 11733 -370 264 305 C
ATOM 4596 C GLU A 602 -14.282 4.638 47.015 1.00 89.73 C
ANISOU 4596 C GLU A 602 10938 11762 11390 -342 273 287 C
ATOM 4597 O GLU A 602 -15.405 4.899 47.442 1.00 92.25 O
ANISOU 4597 O GLU A 602 11246 12084 11719 -350 299 270 O
ATOM 4598 CB GLU A 602 -12.478 5.455 48.561 1.00 98.79 C
ANISOU 4598 CB GLU A 602 12122 12939 12473 -378 279 287 C
ATOM 4599 CG GLU A 602 -11.532 5.168 49.722 1.00105.06 C
ANISOU 4599 CG GLU A 602 12937 13756 13226 -410 275 303 C
ATOM 4600 CD GLU A 602 -12.252 4.965 51.048 1.00107.26 C
ANISOU 4600 CD GLU A 602 13218 14056 13481 -445 302 299 C
ATOM 4601 OE1 GLU A 602 -12.915 5.912 51.528 1.00108.83 O
ANISOU 4601 OE1 GLU A 602 13413 14260 13677 -452 335 271 O
ATOM 4602 OE2 GLU A 602 -12.141 3.859 51.620 1.00104.57 O
ANISOU 4602 OE2 GLU A 602 12881 13725 13124 -467 290 324 O
ATOM 4603 N GLN A 603 -13.970 4.690 45.718 1.00 84.55 N
ANISOU 4603 N GLN A 603 10279 11086 10758 -312 250 290 N
ATOM 4604 CA GLN A 603 -14.908 5.228 44.723 1.00 80.51 C
ANISOU 4604 CA GLN A 603 9750 10554 10284 -286 255 272 C
ATOM 4605 C GLN A 603 -15.384 4.235 43.654 1.00 74.65 C
ANISOU 4605 C GLN A 603 8996 9795 9572 -266 231 287 C
ATOM 4606 O GLN A 603 -16.147 4.612 42.763 1.00 72.23 O
ANISOU 4606 O GLN A 603 8676 9470 9298 -245 231 275 O
ATOM 4607 CB GLN A 603 -14.337 6.486 44.054 1.00 86.07 C
ANISOU 4607 CB GLN A 603 10460 11248 10994 -266 253 255 C
ATOM 4608 CG GLN A 603 -14.039 7.643 45.000 1.00 97.98 C
ANISOU 4608 CG GLN A 603 11978 12769 12479 -282 279 234 C
ATOM 4609 CD GLN A 603 -12.660 7.556 45.644 1.00105.33 C
ANISOU 4609 CD GLN A 603 12931 13716 13372 -299 269 248 C
ATOM 4610 OE1 GLN A 603 -11.817 6.750 45.240 1.00108.72 O
ANISOU 4610 OE1 GLN A 603 13367 14143 13796 -295 241 271 O
ATOM 4611 NE2 GLN A 603 -12.424 8.393 46.652 1.00104.89 N
ANISOU 4611 NE2 GLN A 603 12884 13675 13291 -318 291 232 N
ATOM 4612 N MET A 604 -14.949 2.978 43.739 1.00 71.36 N
ANISOU 4612 N MET A 604 8583 9383 9146 -275 211 314 N
ATOM 4613 CA MET A 604 -15.356 1.956 42.765 1.00 68.28 C
ANISOU 4613 CA MET A 604 8182 8977 8783 -258 188 329 C
ATOM 4614 C MET A 604 -16.824 1.586 42.929 1.00 71.91 C
ANISOU 4614 C MET A 604 8623 9434 9265 -261 203 323 C
ATOM 4615 O MET A 604 -17.233 1.134 44.001 1.00 75.01 O
ANISOU 4615 O MET A 604 9014 9843 9644 -286 219 328 O
ATOM 4616 CB MET A 604 -14.507 0.699 42.904 1.00 64.71 C
ANISOU 4616 CB MET A 604 7738 8530 8317 -268 163 358 C
ATOM 4617 CG MET A 604 -13.125 0.794 42.289 1.00 66.33 C
ANISOU 4617 CG MET A 604 7958 8730 8515 -256 140 366 C
ATOM 4618 SD MET A 604 -12.253 -0.785 42.335 1.00 68.64 S
ANISOU 4618 SD MET A 604 8255 9025 8800 -265 109 400 S
ATOM 4619 CE MET A 604 -13.231 -1.760 41.190 1.00 63.25 C
ANISOU 4619 CE MET A 604 7554 8322 8156 -244 93 406 C
ATOM 4620 N THR A 605 -17.601 1.771 41.863 1.00 69.52 N
ANISOU 4620 N THR A 605 8305 9110 8997 -237 198 314 N
ATOM 4621 CA THR A 605 -19.048 1.524 41.875 1.00 71.38 C
ANISOU 4621 CA THR A 605 8520 9339 9259 -236 211 307 C
ATOM 4622 C THR A 605 -19.403 0.299 41.017 1.00 71.23 C
ANISOU 4622 C THR A 605 8492 9306 9263 -224 185 327 C
ATOM 4623 O THR A 605 -18.625 -0.079 40.145 1.00 71.10 O
ANISOU 4623 O THR A 605 8484 9281 9249 -209 158 339 O
ATOM 4624 CB THR A 605 -19.823 2.760 41.364 1.00 73.19 C
ANISOU 4624 CB THR A 605 8737 9553 9515 -219 226 280 C
ATOM 4625 OG1 THR A 605 -19.441 3.042 40.012 1.00 76.57 O
ANISOU 4625 OG1 THR A 605 9168 9962 9961 -192 201 281 O
ATOM 4626 CG2 THR A 605 -19.525 3.991 42.224 1.00 70.89 C
ANISOU 4626 CG2 THR A 605 8454 9275 9204 -232 254 259 C
ATOM 4627 N CYS A 606 -20.562 -0.322 41.265 1.00 71.94 N
ANISOU 4627 N CYS A 606 8565 9395 9372 -230 194 329 N
ATOM 4628 CA CYS A 606 -21.024 -1.459 40.445 1.00 73.31 C
ANISOU 4628 CA CYS A 606 8728 9554 9570 -218 170 345 C
ATOM 4629 C CYS A 606 -21.483 -0.966 39.074 1.00 72.40 C
ANISOU 4629 C CYS A 606 8604 9414 9488 -189 157 334 C
ATOM 4630 O CYS A 606 -21.607 0.241 38.852 1.00 74.56 O
ANISOU 4630 O CYS A 606 8876 9681 9769 -179 168 314 O
ATOM 4631 CB CYS A 606 -22.185 -2.232 41.107 1.00 73.19 C
ANISOU 4631 CB CYS A 606 8697 9544 9567 -234 184 350 C
ATOM 4632 SG CYS A 606 -21.871 -3.075 42.682 1.00 73.91 S
ANISOU 4632 SG CYS A 606 8796 9663 9621 -272 196 368 S
ATOM 4633 N ALA A 607 -21.748 -1.902 38.167 1.00 71.01 N
ANISOU 4633 N ALA A 607 8422 9224 9334 -176 132 348 N
ATOM 4634 CA ALA A 607 -22.258 -1.564 36.843 1.00 70.43 C
ANISOU 4634 CA ALA A 607 8340 9126 9292 -150 116 340 C
ATOM 4635 C ALA A 607 -23.361 -2.508 36.342 1.00 70.59 C
ANISOU 4635 C ALA A 607 8343 9133 9344 -144 105 349 C
ATOM 4636 O ALA A 607 -23.793 -2.399 35.200 1.00 70.05 O
ANISOU 4636 O ALA A 607 8268 9044 9302 -124 88 346 O
ATOM 4637 CB ALA A 607 -21.113 -1.491 35.841 1.00 65.59 C
ANISOU 4637 CB ALA A 607 7743 8505 8670 -134 91 346 C
ATOM 4638 N THR A 608 -23.819 -3.434 37.179 1.00 76.67 N
ANISOU 4638 N THR A 608 9104 9913 10111 -162 113 360 N
ATOM 4639 CA THR A 608 -24.886 -4.355 36.755 1.00 82.96 C
ANISOU 4639 CA THR A 608 9883 10698 10938 -157 103 369 C
ATOM 4640 C THR A 608 -26.180 -4.331 37.623 1.00 92.00 C
ANISOU 4640 C THR A 608 11009 11848 12099 -171 131 360 C
ATOM 4641 O THR A 608 -26.376 -3.409 38.425 1.00 89.54 O
ANISOU 4641 O THR A 608 10695 11546 11779 -181 160 343 O
ATOM 4642 CB THR A 608 -24.355 -5.779 36.482 1.00 78.27 C
ANISOU 4642 CB THR A 608 9294 10103 10338 -159 76 394 C
ATOM 4643 OG1 THR A 608 -23.389 -6.127 37.476 1.00 78.41 O
ANISOU 4643 OG1 THR A 608 9326 10142 10321 -179 82 406 O
ATOM 4644 CG2 THR A 608 -23.733 -5.859 35.095 1.00 70.61 C
ANISOU 4644 CG2 THR A 608 8333 9116 9376 -136 46 397 C
ATOM 4645 N PRO A 609 -27.027 -5.377 37.506 1.00 97.06 N
ANISOU 4645 N PRO A 609 11634 12481 12761 -172 123 372 N
ATOM 4646 CA PRO A 609 -28.481 -5.326 37.608 1.00104.80 C
ANISOU 4646 CA PRO A 609 12590 13452 13776 -172 138 362 C
ATOM 4647 C PRO A 609 -29.164 -3.948 37.427 1.00112.24 C
ANISOU 4647 C PRO A 609 13521 14383 14739 -162 157 336 C
ATOM 4648 O PRO A 609 -28.569 -3.015 36.869 1.00102.36 O
ANISOU 4648 O PRO A 609 12280 13126 13483 -148 151 325 O
ATOM 4649 CB PRO A 609 -28.725 -5.920 39.005 1.00105.03 C
ANISOU 4649 CB PRO A 609 12615 13503 13786 -202 162 370 C
ATOM 4650 CG PRO A 609 -27.557 -6.855 39.222 1.00 96.02 C
ANISOU 4650 CG PRO A 609 11493 12375 12613 -212 142 393 C
ATOM 4651 CD PRO A 609 -26.573 -6.649 38.094 1.00 94.43 C
ANISOU 4651 CD PRO A 609 11306 12161 12408 -190 114 396 C
ATOM 4652 N ASN A 613 -25.960 1.023 40.941 1.00 93.56 N
ANISOU 4652 N ASN A 613 11216 12089 12241 -210 263 263 N
ATOM 4653 CA ASN A 613 -25.249 1.730 39.902 1.00 87.05 C
ANISOU 4653 CA ASN A 613 10402 11251 11421 -187 242 260 C
ATOM 4654 C ASN A 613 -24.298 2.597 40.737 1.00 88.86 C
ANISOU 4654 C ASN A 613 10649 11499 11615 -201 260 249 C
ATOM 4655 O ASN A 613 -23.477 3.351 40.213 1.00 90.89 O
ANISOU 4655 O ASN A 613 10918 11751 11863 -188 249 244 O
ATOM 4656 CB ASN A 613 -26.278 2.569 39.163 1.00 89.12 C
ANISOU 4656 CB ASN A 613 10644 11489 11726 -168 245 241 C
ATOM 4657 CG ASN A 613 -25.946 2.846 37.700 1.00 86.52 C
ANISOU 4657 CG ASN A 613 10319 11138 11414 -140 213 244 C
ATOM 4658 OD1 ASN A 613 -24.820 2.685 37.197 1.00 87.41 O
ANISOU 4658 OD1 ASN A 613 10452 11253 11505 -134 191 257 O
ATOM 4659 ND2 ASN A 613 -27.013 3.273 36.998 1.00 79.78 N
ANISOU 4659 ND2 ASN A 613 9446 10261 10603 -125 210 233 N
ATOM 4660 N THR A 614 -24.467 2.462 42.058 1.00 87.17 N
ANISOU 4660 N THR A 614 10435 11306 11378 -228 288 246 N
ATOM 4661 CA THR A 614 -23.514 2.842 43.112 1.00 83.96 C
ANISOU 4661 CA THR A 614 10048 10923 10928 -250 303 243 C
ATOM 4662 C THR A 614 -23.881 1.953 44.316 1.00 83.59 C
ANISOU 4662 C THR A 614 10000 10896 10861 -281 321 253 C
ATOM 4663 O THR A 614 -25.061 1.644 44.473 1.00 88.39 O
ANISOU 4663 O THR A 614 10588 11499 11494 -284 335 248 O
ATOM 4664 CB THR A 614 -23.598 4.339 43.461 0.00 20.00 C
ATOM 4665 OG1 THR A 614 -24.940 4.670 43.837 0.00 20.00 O
ATOM 4666 CG2 THR A 614 -23.361 5.191 42.222 0.00 20.00 C
ATOM 4667 N SER A 615 -22.940 1.494 45.153 1.00 81.78 N
ANISOU 4667 N SER A 615 9790 10689 10591 -303 319 269 N
ATOM 4668 CA SER A 615 -21.481 1.584 45.005 1.00 77.53 C
ANISOU 4668 CA SER A 615 9275 10156 10024 -301 298 281 C
ATOM 4669 C SER A 615 -20.949 0.166 44.724 1.00 78.43 C
ANISOU 4669 C SER A 615 9396 10272 10132 -303 266 314 C
ATOM 4670 O SER A 615 -21.463 -0.487 43.816 1.00 76.74 O
ANISOU 4670 O SER A 615 9169 10040 9947 -285 247 322 O
ATOM 4671 CB SER A 615 -20.860 2.207 46.266 1.00 75.64 C
ANISOU 4671 CB SER A 615 9052 9941 9744 -328 321 272 C
ATOM 4672 OG SER A 615 -19.488 1.904 46.417 1.00 66.86 O
ANISOU 4672 OG SER A 615 7962 8839 8600 -335 300 291 O
ATOM 4673 N LEU A 616 -19.956 -0.324 45.482 1.00 75.29 N
ANISOU 4673 N LEU A 616 9016 9892 9697 -324 258 331 N
ATOM 4674 CA LEU A 616 -19.323 -1.628 45.165 1.00 75.79 C
ANISOU 4674 CA LEU A 616 9085 9954 9757 -324 225 362 C
ATOM 4675 C LEU A 616 -18.919 -2.493 46.355 1.00 74.96 C
ANISOU 4675 C LEU A 616 8991 9871 9620 -357 225 384 C
ATOM 4676 O LEU A 616 -19.317 -3.654 46.441 1.00 74.42 O
ANISOU 4676 O LEU A 616 8914 9801 9559 -365 215 404 O
ATOM 4677 CB LEU A 616 -18.094 -1.451 44.267 1.00 74.14 C
ANISOU 4677 CB LEU A 616 8888 9734 9545 -304 198 369 C
ATOM 4678 CG LEU A 616 -17.303 -2.731 43.974 1.00 73.36 C
ANISOU 4678 CG LEU A 616 8795 9633 9443 -304 164 399 C
ATOM 4679 CD1 LEU A 616 -17.463 -3.147 42.523 1.00 70.76 C
ANISOU 4679 CD1 LEU A 616 8457 9281 9148 -274 140 403 C
ATOM 4680 CD2 LEU A 616 -15.836 -2.541 44.312 1.00 73.66 C
ANISOU 4680 CD2 LEU A 616 8854 9682 9452 -312 153 408 C
ATOM 4681 N VAL A 617 -18.092 -1.938 47.239 1.00 76.68 N
ANISOU 4681 N VAL A 617 9226 10106 9802 -377 235 381 N
ATOM 4682 CA VAL A 617 -17.591 -2.666 48.407 1.00 73.44 C
ANISOU 4682 CA VAL A 617 8829 9717 9357 -411 233 403 C
ATOM 4683 C VAL A 617 -18.731 -2.961 49.394 1.00 78.92 C
ANISOU 4683 C VAL A 617 9515 10424 10046 -437 261 399 C
ATOM 4684 O VAL A 617 -18.561 -3.733 50.345 1.00 80.20 O
ANISOU 4684 O VAL A 617 9686 10603 10183 -467 260 419 O
ATOM 4685 CB VAL A 617 -16.454 -1.904 49.129 1.00 69.99 C
ANISOU 4685 CB VAL A 617 8413 9294 8882 -427 237 399 C
ATOM 4686 CG1 VAL A 617 -15.269 -2.829 49.353 1.00 68.56 C
ANISOU 4686 CG1 VAL A 617 8247 9119 8682 -438 206 431 C
ATOM 4687 CG2 VAL A 617 -16.010 -0.683 48.337 1.00 67.62 C
ANISOU 4687 CG2 VAL A 617 8117 8983 8593 -400 239 377 C
ATOM 4688 N LEU A 618 -19.893 -2.350 49.144 1.00 80.83 N
ANISOU 4688 N LEU A 618 9739 10658 10312 -426 287 374 N
ATOM 4689 CA LEU A 618 -21.095 -2.533 49.961 1.00 80.11 C
ANISOU 4689 CA LEU A 618 9636 10577 10222 -448 317 366 C
ATOM 4690 C LEU A 618 -21.875 -3.818 49.640 1.00 81.53 C
ANISOU 4690 C LEU A 618 9800 10748 10427 -446 304 386 C
ATOM 4691 O LEU A 618 -22.854 -4.135 50.325 1.00 83.26 O
ANISOU 4691 O LEU A 618 10010 10976 10648 -466 327 383 O
ATOM 4692 CB LEU A 618 -22.029 -1.311 49.844 1.00 78.03 C
ANISOU 4692 CB LEU A 618 9360 10307 9981 -437 351 329 C
ATOM 4693 CG LEU A 618 -21.780 0.018 50.585 1.00 76.18 C
ANISOU 4693 CG LEU A 618 9135 10085 9722 -450 382 302 C
ATOM 4694 CD1 LEU A 618 -20.953 -0.152 51.857 1.00 77.01 C
ANISOU 4694 CD1 LEU A 618 9264 10217 9776 -487 387 313 C
ATOM 4695 CD2 LEU A 618 -21.145 1.055 49.679 1.00 73.89 C
ANISOU 4695 CD2 LEU A 618 8849 9780 9444 -420 371 287 C
ATOM 4696 N ASP A 619 -21.438 -4.551 48.612 1.00 78.25 N
ANISOU 4696 N ASP A 619 9383 10317 10031 -423 267 405 N
ATOM 4697 CA ASP A 619 -22.108 -5.780 48.165 1.00 78.21 C
ANISOU 4697 CA ASP A 619 9362 10301 10052 -417 250 424 C
ATOM 4698 C ASP A 619 -22.094 -6.891 49.223 1.00 82.80 C
ANISOU 4698 C ASP A 619 9949 10900 10610 -452 248 450 C
ATOM 4699 O ASP A 619 -21.033 -7.243 49.745 1.00 81.00 O
ANISOU 4699 O ASP A 619 9739 10684 10352 -468 232 469 O
ATOM 4700 CB ASP A 619 -21.477 -6.277 46.865 1.00 73.86 C
ANISOU 4700 CB ASP A 619 8810 9729 9522 -387 211 438 C
ATOM 4701 CG ASP A 619 -22.016 -7.628 46.428 1.00 72.45 C
ANISOU 4701 CG ASP A 619 8618 9540 9369 -383 190 460 C
ATOM 4702 OD1 ASP A 619 -23.131 -7.690 45.871 1.00 70.20 O
ANISOU 4702 OD1 ASP A 619 8314 9241 9117 -368 197 450 O
ATOM 4703 OD2 ASP A 619 -21.307 -8.634 46.625 1.00 71.74 O
ANISOU 4703 OD2 ASP A 619 8536 9454 9267 -393 166 487 O
ATOM 4704 N PHE A 620 -23.276 -7.447 49.506 1.00 90.71 N
ANISOU 4704 N PHE A 620 10935 11903 11628 -462 263 451 N
ATOM 4705 CA PHE A 620 -23.484 -8.408 50.602 1.00 93.72 C
ANISOU 4705 CA PHE A 620 11320 12302 11987 -497 268 472 C
ATOM 4706 C PHE A 620 -23.996 -9.764 50.099 1.00 89.02 C
ANISOU 4706 C PHE A 620 10709 11694 11419 -491 244 496 C
ATOM 4707 O PHE A 620 -24.733 -9.819 49.113 1.00 79.64 O
ANISOU 4707 O PHE A 620 9502 10485 10270 -463 239 488 O
ATOM 4708 CB PHE A 620 -24.486 -7.822 51.609 1.00 98.16 C
ANISOU 4708 CB PHE A 620 11877 12880 12539 -522 313 451 C
ATOM 4709 CG PHE A 620 -24.273 -8.279 53.025 1.00104.75 C
ANISOU 4709 CG PHE A 620 12726 13741 13330 -567 325 466 C
ATOM 4710 CD1 PHE A 620 -24.932 -9.403 53.517 1.00107.83 C
ANISOU 4710 CD1 PHE A 620 13110 14138 13723 -588 325 487 C
ATOM 4711 CD2 PHE A 620 -23.418 -7.580 53.876 1.00109.56 C
ANISOU 4711 CD2 PHE A 620 13360 14371 13898 -589 336 461 C
ATOM 4712 CE1 PHE A 620 -24.735 -9.827 54.826 1.00109.78 C
ANISOU 4712 CE1 PHE A 620 13372 14410 13929 -632 335 503 C
ATOM 4713 CE2 PHE A 620 -23.217 -7.997 55.188 1.00109.72 C
ANISOU 4713 CE2 PHE A 620 13395 14415 13876 -632 345 476 C
ATOM 4714 CZ PHE A 620 -23.877 -9.123 55.663 1.00109.99 C
ANISOU 4714 CZ PHE A 620 13422 14456 13911 -654 345 498 C
ATOM 4715 N ASN A 621 -23.602 -10.852 50.767 1.00 92.03 N
ANISOU 4715 N ASN A 621 11099 12087 11781 -516 228 527 N
ATOM 4716 CA ASN A 621 -24.211 -12.165 50.509 1.00 95.94 C
ANISOU 4716 CA ASN A 621 11579 12573 12301 -516 210 550 C
ATOM 4717 C ASN A 621 -25.567 -12.258 51.190 1.00104.14 C
ANISOU 4717 C ASN A 621 12603 13620 13344 -536 243 541 C
ATOM 4718 O ASN A 621 -25.659 -12.246 52.424 1.00104.35 O
ANISOU 4718 O ASN A 621 12639 13669 13337 -572 265 544 O
ATOM 4719 CB ASN A 621 -23.371 -13.341 51.021 1.00 90.78 C
ANISOU 4719 CB ASN A 621 10937 11927 11626 -538 180 587 C
ATOM 4720 CG ASN A 621 -21.911 -13.257 50.642 1.00 83.38 C
ANISOU 4720 CG ASN A 621 10016 10985 10677 -527 150 597 C
ATOM 4721 OD1 ASN A 621 -21.547 -13.034 49.487 1.00 80.78 O
ANISOU 4721 OD1 ASN A 621 9682 10637 10371 -493 133 589 O
ATOM 4722 ND2 ASN A 621 -21.065 -13.469 51.638 1.00 79.30 N
ANISOU 4722 ND2 ASN A 621 9518 10487 10124 -558 144 616 N
ATOM 4723 N ASN A 622 -26.617 -12.362 50.384 1.00108.12 N
ANISOU 4723 N ASN A 622 13084 14105 13890 -513 247 530 N
ATOM 4724 CA ASN A 622 -27.970 -12.487 50.902 1.00106.10 C
ANISOU 4724 CA ASN A 622 12811 13854 13647 -528 277 520 C
ATOM 4725 C ASN A 622 -28.711 -13.608 50.185 1.00105.19 C
ANISOU 4725 C ASN A 622 12675 13720 13570 -514 256 537 C
ATOM 4726 O ASN A 622 -28.482 -14.782 50.478 1.00105.45 O
ANISOU 4726 O ASN A 622 12711 13757 13597 -529 235 567 O
ATOM 4727 CB ASN A 622 -28.714 -11.146 50.810 1.00105.91 C
ANISOU 4727 CB ASN A 622 12776 13826 13636 -517 314 481 C
ATOM 4728 CG ASN A 622 -28.157 -10.103 51.768 1.00107.35 C
ANISOU 4728 CG ASN A 622 12979 14031 13778 -539 342 465 C
ATOM 4729 OD1 ASN A 622 -27.560 -9.113 51.347 1.00106.39 O
ANISOU 4729 OD1 ASN A 622 12865 13904 13653 -521 341 447 O
ATOM 4730 ND2 ASN A 622 -28.340 -10.330 53.066 1.00108.53 N
ANISOU 4730 ND2 ASN A 622 13136 14204 13894 -579 365 470 N
ATOM 4731 N SER A 623 -29.576 -13.246 49.241 1.00102.90 N
ANISOU 4731 N SER A 623 12365 13409 13322 -484 261 517 N
ATOM 4732 CA SER A 623 -30.335 -14.213 48.451 1.00104.18 C
ANISOU 4732 CA SER A 623 12506 13551 13524 -468 241 530 C
ATOM 4733 C SER A 623 -29.397 -15.132 47.670 1.00105.59 C
ANISOU 4733 C SER A 623 12692 13718 13707 -452 194 556 C
ATOM 4734 O SER A 623 -28.340 -14.689 47.224 1.00103.56 O
ANISOU 4734 O SER A 623 12450 13458 13438 -438 178 554 O
ATOM 4735 CB SER A 623 -31.265 -13.480 47.484 1.00103.25 C
ANISOU 4735 CB SER A 623 12369 13412 13450 -437 250 503 C
ATOM 4736 OG SER A 623 -31.888 -12.376 48.115 1.00100.14 O
ANISOU 4736 OG SER A 623 11970 13027 13051 -447 292 474 O
ATOM 4737 N THR A 624 -29.790 -16.402 47.519 1.00110.02 N
ANISOU 4737 N THR A 624 13242 14271 14287 -455 174 579 N
ATOM 4738 CA THR A 624 -29.007 -17.443 46.810 1.00111.70 C
ANISOU 4738 CA THR A 624 13459 14472 14508 -442 131 605 C
ATOM 4739 C THR A 624 -27.587 -17.598 47.354 1.00111.81 C
ANISOU 4739 C THR A 624 13497 14500 14485 -458 115 623 C
ATOM 4740 O THR A 624 -27.163 -18.697 47.720 1.00106.31 O
ANISOU 4740 O THR A 624 12804 13807 13781 -475 93 652 O
ATOM 4741 CB THR A 624 -28.926 -17.196 45.277 1.00111.21 C
ANISOU 4741 CB THR A 624 13390 14383 14480 -401 108 593 C
ATOM 4742 OG1 THR A 624 -30.240 -17.006 44.740 1.00115.87 O
ANISOU 4742 OG1 THR A 624 13958 14958 15106 -386 121 577 O
ATOM 4743 CG2 THR A 624 -28.244 -18.368 44.555 1.00101.78 C
ANISOU 4743 CG2 THR A 624 12198 13175 13298 -389 66 618 C
ATOM 4744 N CYS A 625 -26.874 -16.477 47.402 1.00115.39 N
ANISOU 4744 N CYS A 625 13965 14960 14916 -453 125 605 N
ATOM 4745 CA CYS A 625 -25.440 -16.449 47.645 1.00120.90 C
ANISOU 4745 CA CYS A 625 14685 15666 15584 -460 107 618 C
ATOM 4746 C CYS A 625 -25.077 -15.878 49.020 1.00123.79 C
ANISOU 4746 C CYS A 625 15069 16060 15906 -495 132 617 C
ATOM 4747 O CYS A 625 -24.060 -16.258 49.607 1.00117.86 O
ANISOU 4747 O CYS A 625 14334 15320 15126 -514 116 638 O
ATOM 4748 CB CYS A 625 -24.745 -15.670 46.517 1.00113.60 C
ANISOU 4748 CB CYS A 625 13765 14726 14669 -426 94 601 C
ATOM 4749 SG CYS A 625 -25.255 -13.945 46.281 1.00107.17 S
ANISOU 4749 SG CYS A 625 12949 13911 13857 -411 129 561 S
TER 4750 CYS A 625
ATOM 4751 N GLN C 21 -13.255 44.473 25.386 1.00 60.08 N
ANISOU 4751 N GLN C 21 6912 7457 8456 105 161 -1492 N
ATOM 4752 CA GLN C 21 -12.431 44.572 24.142 1.00 61.63 C
ANISOU 4752 CA GLN C 21 7148 7618 8648 148 114 -1401 C
ATOM 4753 C GLN C 21 -11.190 45.439 24.349 1.00 62.32 C
ANISOU 4753 C GLN C 21 7267 7689 8721 137 98 -1348 C
ATOM 4754 O GLN C 21 -11.291 46.605 24.734 1.00 62.39 O
ANISOU 4754 O GLN C 21 7261 7670 8771 139 83 -1392 O
ATOM 4755 CB GLN C 21 -13.258 45.096 22.962 1.00 61.73 C
ANISOU 4755 CB GLN C 21 7144 7582 8728 213 64 -1425 C
ATOM 4756 CG GLN C 21 -12.509 45.058 21.636 1.00 68.35 C
ANISOU 4756 CG GLN C 21 8022 8392 9554 253 19 -1332 C
ATOM 4757 CD GLN C 21 -13.297 45.633 20.466 1.00 72.63 C
ANISOU 4757 CD GLN C 21 8551 8884 10158 314 -36 -1350 C
ATOM 4758 OE1 GLN C 21 -13.038 46.756 20.022 1.00 74.66 O
ANISOU 4758 OE1 GLN C 21 8817 9096 10452 339 -81 -1335 O
ATOM 4759 NE2 GLN C 21 -14.252 44.860 19.952 1.00 69.92 N
ANISOU 4759 NE2 GLN C 21 8188 8548 9828 335 -36 -1380 N
ATOM 4760 N GLN C 22 -10.025 44.861 24.063 1.00 62.95 N
ANISOU 4760 N GLN C 22 7387 7783 8747 127 99 -1255 N
ATOM 4761 CA GLN C 22 -8.735 45.500 24.327 1.00 62.42 C
ANISOU 4761 CA GLN C 22 7349 7708 8656 108 89 -1197 C
ATOM 4762 C GLN C 22 -8.166 46.229 23.120 1.00 62.10 C
ANISOU 4762 C GLN C 22 7332 7622 8638 154 36 -1136 C
ATOM 4763 O GLN C 22 -7.549 47.285 23.261 1.00 61.91 O
ANISOU 4763 O GLN C 22 7319 7572 8631 151 14 -1120 O
ATOM 4764 CB GLN C 22 -7.722 44.461 24.796 1.00 63.35 C
ANISOU 4764 CB GLN C 22 7496 7871 8702 66 121 -1131 C
ATOM 4765 CG GLN C 22 -8.160 43.671 26.012 1.00 64.59 C
ANISOU 4765 CG GLN C 22 7637 8077 8828 12 172 -1177 C
ATOM 4766 CD GLN C 22 -8.325 44.543 27.234 1.00 67.75 C
ANISOU 4766 CD GLN C 22 8018 8485 9237 -26 191 -1242 C
ATOM 4767 OE1 GLN C 22 -7.474 45.388 27.535 1.00 66.20 O
ANISOU 4767 OE1 GLN C 22 7838 8274 9038 -37 177 -1218 O
ATOM 4768 NE2 GLN C 22 -9.425 44.343 27.952 1.00 69.83 N
ANISOU 4768 NE2 GLN C 22 8247 8773 9511 -48 223 -1327 N
ATOM 4769 N TRP C 23 -8.369 45.652 21.940 1.00 60.53 N
ANISOU 4769 N TRP C 23 7143 7416 8439 194 16 -1101 N
ATOM 4770 CA TRP C 23 -7.805 46.180 20.702 1.00 61.03 C
ANISOU 4770 CA TRP C 23 7231 7445 8511 234 -31 -1034 C
ATOM 4771 C TRP C 23 -8.562 45.611 19.523 1.00 60.17 C
ANISOU 4771 C TRP C 23 7118 7327 8416 279 -53 -1034 C
ATOM 4772 O TRP C 23 -9.286 44.625 19.677 1.00 57.55 O
ANISOU 4772 O TRP C 23 6768 7021 8074 276 -26 -1070 O
ATOM 4773 CB TRP C 23 -6.302 45.861 20.645 1.00 59.55 C
ANISOU 4773 CB TRP C 23 7080 7280 8266 212 -22 -942 C
ATOM 4774 CG TRP C 23 -5.627 46.253 19.357 1.00 58.15 C
ANISOU 4774 CG TRP C 23 6928 7078 8085 246 -63 -866 C
ATOM 4775 CD1 TRP C 23 -5.219 47.525 18.961 1.00 59.05 C
ANISOU 4775 CD1 TRP C 23 7053 7151 8229 258 -106 -840 C
ATOM 4776 CD2 TRP C 23 -5.273 45.371 18.240 1.00 58.45 C
ANISOU 4776 CD2 TRP C 23 6986 7135 8088 271 -68 -806 C
ATOM 4777 NE1 TRP C 23 -4.656 47.493 17.710 1.00 58.77 N
ANISOU 4777 NE1 TRP C 23 7042 7110 8175 284 -134 -766 N
ATOM 4778 CE2 TRP C 23 -4.657 46.233 17.217 1.00 59.43 C
ANISOU 4778 CE2 TRP C 23 7132 7230 8218 295 -112 -746 C
ATOM 4779 CE3 TRP C 23 -5.403 44.008 17.989 1.00 57.11 C
ANISOU 4779 CE3 TRP C 23 6817 6999 7883 276 -43 -799 C
ATOM 4780 CZ2 TRP C 23 -4.196 45.726 16.007 1.00 57.64 C
ANISOU 4780 CZ2 TRP C 23 6926 7016 7958 320 -125 -683 C
ATOM 4781 CZ3 TRP C 23 -4.937 43.511 16.766 1.00 58.82 C
ANISOU 4781 CZ3 TRP C 23 7054 7223 8070 306 -58 -739 C
ATOM 4782 CH2 TRP C 23 -4.342 44.350 15.804 1.00 59.02 C
ANISOU 4782 CH2 TRP C 23 7099 7227 8097 327 -96 -683 C
ATOM 4783 N PHE C 24 -8.439 46.252 18.356 1.00 60.74 N
ANISOU 4783 N PHE C 24 7205 7363 8509 319 -103 -995 N
ATOM 4784 CA PHE C 24 -9.033 45.751 17.106 1.00 62.60 C
ANISOU 4784 CA PHE C 24 7443 7591 8751 363 -130 -984 C
ATOM 4785 C PHE C 24 -8.473 46.428 15.850 1.00 62.34 C
ANISOU 4785 C PHE C 24 7439 7527 8719 394 -182 -914 C
ATOM 4786 O PHE C 24 -8.061 47.587 15.897 1.00 61.62 O
ANISOU 4786 O PHE C 24 7356 7403 8653 391 -211 -897 O
ATOM 4787 CB PHE C 24 -10.575 45.843 17.136 1.00 68.00 C
ANISOU 4787 CB PHE C 24 8088 8254 9493 386 -141 -1075 C
ATOM 4788 CG PHE C 24 -11.127 47.207 16.802 1.00 73.81 C
ANISOU 4788 CG PHE C 24 8810 8932 10300 415 -195 -1106 C
ATOM 4789 CD1 PHE C 24 -11.598 47.488 15.516 1.00 75.88 C
ANISOU 4789 CD1 PHE C 24 9079 9160 10591 462 -251 -1089 C
ATOM 4790 CD2 PHE C 24 -11.198 48.207 17.772 1.00 77.84 C
ANISOU 4790 CD2 PHE C 24 9303 9422 10851 396 -194 -1155 C
ATOM 4791 CE1 PHE C 24 -12.111 48.741 15.201 1.00 78.47 C
ANISOU 4791 CE1 PHE C 24 9395 9430 10989 489 -308 -1115 C
ATOM 4792 CE2 PHE C 24 -11.713 49.463 17.462 1.00 81.97 C
ANISOU 4792 CE2 PHE C 24 9812 9885 11446 425 -249 -1186 C
ATOM 4793 CZ PHE C 24 -12.170 49.730 16.176 1.00 81.14 C
ANISOU 4793 CZ PHE C 24 9713 9743 11372 471 -307 -1164 C
ATOM 4794 N CYS C 25 -8.455 45.694 14.736 1.00 62.31 N
ANISOU 4794 N CYS C 25 7451 7537 8686 421 -194 -874 N
ATOM 4795 CA CYS C 25 -8.158 46.263 13.415 1.00 63.59 C
ANISOU 4795 CA CYS C 25 7639 7675 8848 453 -245 -816 C
ATOM 4796 C CYS C 25 -9.025 45.618 12.345 1.00 62.73 C
ANISOU 4796 C CYS C 25 7526 7565 8741 492 -268 -828 C
ATOM 4797 O CYS C 25 -9.751 44.659 12.617 1.00 61.51 O
ANISOU 4797 O CYS C 25 7351 7431 8586 494 -240 -877 O
ATOM 4798 CB CYS C 25 -6.666 46.146 13.039 1.00 67.61 C
ANISOU 4798 CB CYS C 25 8182 8209 9296 436 -236 -723 C
ATOM 4799 SG CYS C 25 -5.981 44.468 12.844 1.00 78.07 S
ANISOU 4799 SG CYS C 25 9519 9596 10545 429 -186 -685 S
ATOM 4800 N ASN C 26 -8.948 46.160 11.134 1.00 64.23 N
ANISOU 4800 N ASN C 26 7737 7732 8933 520 -319 -783 N
ATOM 4801 CA ASN C 26 -9.575 45.553 9.966 1.00 70.00 C
ANISOU 4801 CA ASN C 26 8473 8467 9655 556 -345 -781 C
ATOM 4802 C ASN C 26 -8.650 45.607 8.755 1.00 73.20 C
ANISOU 4802 C ASN C 26 8917 8886 10007 565 -368 -692 C
ATOM 4803 O ASN C 26 -7.949 46.598 8.544 1.00 75.86 O
ANISOU 4803 O ASN C 26 9273 9204 10344 555 -394 -641 O
ATOM 4804 CB ASN C 26 -10.939 46.195 9.649 1.00 72.69 C
ANISOU 4804 CB ASN C 26 8790 8759 10068 588 -396 -840 C
ATOM 4805 CG ASN C 26 -10.876 47.714 9.530 1.00 74.65 C
ANISOU 4805 CG ASN C 26 9044 8953 10366 592 -451 -825 C
ATOM 4806 OD1 ASN C 26 -9.830 48.330 9.731 1.00 76.01 O
ANISOU 4806 OD1 ASN C 26 9237 9123 10519 569 -449 -772 O
ATOM 4807 ND2 ASN C 26 -12.012 48.326 9.205 1.00 76.38 N
ANISOU 4807 ND2 ASN C 26 9242 9124 10652 623 -503 -874 N
ATOM 4808 N SER C 27 -8.632 44.528 7.980 1.00 71.15 N
ANISOU 4808 N SER C 27 8669 8662 9702 581 -356 -676 N
ATOM 4809 CA SER C 27 -7.892 44.490 6.723 1.00 67.90 C
ANISOU 4809 CA SER C 27 8291 8271 9237 592 -377 -602 C
ATOM 4810 C SER C 27 -8.843 44.062 5.608 1.00 67.14 C
ANISOU 4810 C SER C 27 8196 8170 9142 630 -413 -621 C
ATOM 4811 O SER C 27 -10.034 43.852 5.858 1.00 67.10 O
ANISOU 4811 O SER C 27 8164 8144 9185 646 -423 -690 O
ATOM 4812 CB SER C 27 -6.686 43.554 6.828 1.00 64.83 C
ANISOU 4812 CB SER C 27 7915 7936 8779 572 -324 -558 C
ATOM 4813 OG SER C 27 -7.076 42.273 7.283 1.00 63.12 O
ANISOU 4813 OG SER C 27 7681 7745 8554 574 -283 -604 O
ATOM 4814 N SER C 28 -8.319 43.919 4.392 1.00 66.16 N
ANISOU 4814 N SER C 28 8102 8069 8965 641 -432 -562 N
ATOM 4815 CA SER C 28 -9.152 43.685 3.205 1.00 67.99 C
ANISOU 4815 CA SER C 28 8342 8296 9195 675 -477 -571 C
ATOM 4816 C SER C 28 -10.073 42.459 3.265 1.00 67.92 C
ANISOU 4816 C SER C 28 8311 8302 9193 695 -457 -636 C
ATOM 4817 O SER C 28 -10.930 42.296 2.395 1.00 68.66 O
ANISOU 4817 O SER C 28 8405 8386 9295 724 -497 -655 O
ATOM 4818 CB SER C 28 -8.289 43.636 1.942 1.00 68.48 C
ANISOU 4818 CB SER C 28 8441 8393 9185 677 -490 -495 C
ATOM 4819 OG SER C 28 -7.500 42.462 1.913 1.00 69.28 O
ANISOU 4819 OG SER C 28 8547 8551 9225 671 -435 -482 O
ATOM 4820 N ASP C 29 -9.900 41.605 4.277 1.00 68.22 N
ANISOU 4820 N ASP C 29 8330 8363 9227 678 -399 -668 N
ATOM 4821 CA ASP C 29 -10.755 40.421 4.446 1.00 65.79 C
ANISOU 4821 CA ASP C 29 7999 8067 8929 691 -378 -729 C
ATOM 4822 C ASP C 29 -10.971 39.960 5.894 1.00 63.63 C
ANISOU 4822 C ASP C 29 7695 7795 8683 665 -328 -780 C
ATOM 4823 O ASP C 29 -11.453 38.851 6.123 1.00 63.35 O
ANISOU 4823 O ASP C 29 7645 7777 8647 666 -303 -819 O
ATOM 4824 CB ASP C 29 -10.276 39.248 3.562 1.00 69.06 C
ANISOU 4824 CB ASP C 29 8433 8527 9279 704 -362 -703 C
ATOM 4825 CG ASP C 29 -8.814 38.854 3.812 1.00 75.06 C
ANISOU 4825 CG ASP C 29 9210 9327 9982 680 -316 -650 C
ATOM 4826 OD1 ASP C 29 -8.326 38.957 4.962 1.00 77.96 O
ANISOU 4826 OD1 ASP C 29 9566 9694 10360 650 -280 -651 O
ATOM 4827 OD2 ASP C 29 -8.152 38.416 2.843 1.00 73.49 O
ANISOU 4827 OD2 ASP C 29 9034 9162 9727 691 -315 -609 O
ATOM 4828 N ALA C 30 -10.636 40.803 6.868 1.00 61.41 N
ANISOU 4828 N ALA C 30 7406 7497 8427 638 -316 -779 N
ATOM 4829 CA ALA C 30 -10.824 40.428 8.274 1.00 62.26 C
ANISOU 4829 CA ALA C 30 7487 7612 8556 608 -269 -826 C
ATOM 4830 C ALA C 30 -11.049 41.589 9.232 1.00 62.31 C
ANISOU 4830 C ALA C 30 7475 7584 8613 590 -274 -855 C
ATOM 4831 O ALA C 30 -10.428 42.647 9.102 1.00 60.97 O
ANISOU 4831 O ALA C 30 7322 7396 8447 586 -298 -814 O
ATOM 4832 CB ALA C 30 -9.650 39.582 8.764 1.00 62.79 C
ANISOU 4832 CB ALA C 30 7568 7720 8568 580 -218 -787 C
ATOM 4833 N ILE C 31 -11.945 41.380 10.194 1.00 62.78 N
ANISOU 4833 N ILE C 31 7499 7638 8713 578 -252 -928 N
ATOM 4834 CA ILE C 31 -11.976 42.214 11.392 1.00 65.70 C
ANISOU 4834 CA ILE C 31 7849 7992 9119 550 -237 -961 C
ATOM 4835 C ILE C 31 -11.466 41.358 12.552 1.00 65.11 C
ANISOU 4835 C ILE C 31 7771 7958 9010 507 -174 -966 C
ATOM 4836 O ILE C 31 -12.007 40.284 12.846 1.00 63.93 O
ANISOU 4836 O ILE C 31 7605 7831 8854 499 -146 -1001 O
ATOM 4837 CB ILE C 31 -13.363 42.874 11.687 1.00 68.83 C
ANISOU 4837 CB ILE C 31 8206 8351 9592 565 -262 -1044 C
ATOM 4838 CG1 ILE C 31 -14.073 42.234 12.893 1.00 68.22 C
ANISOU 4838 CG1 ILE C 31 8092 8296 9532 536 -212 -1118 C
ATOM 4839 CG2 ILE C 31 -14.250 42.903 10.442 1.00 67.89 C
ANISOU 4839 CG2 ILE C 31 8086 8208 9501 611 -316 -1055 C
ATOM 4840 CD1 ILE C 31 -14.951 43.187 13.680 1.00 69.64 C
ANISOU 4840 CD1 ILE C 31 8232 8446 9781 533 -219 -1196 C
ATOM 4841 N ILE C 32 -10.391 41.824 13.175 1.00 64.36 N
ANISOU 4841 N ILE C 32 7690 7869 8892 477 -156 -926 N
ATOM 4842 CA ILE C 32 -9.758 41.105 14.272 1.00 62.63 C
ANISOU 4842 CA ILE C 32 7472 7686 8637 433 -103 -920 C
ATOM 4843 C ILE C 32 -9.891 41.946 15.537 1.00 61.70 C
ANISOU 4843 C ILE C 32 7335 7558 8550 400 -87 -963 C
ATOM 4844 O ILE C 32 -9.768 43.171 15.487 1.00 63.23 O
ANISOU 4844 O ILE C 32 7530 7719 8774 407 -116 -961 O
ATOM 4845 CB ILE C 32 -8.270 40.806 13.956 1.00 63.80 C
ANISOU 4845 CB ILE C 32 7654 7858 8727 424 -92 -835 C
ATOM 4846 CG1 ILE C 32 -8.148 40.069 12.620 1.00 62.96 C
ANISOU 4846 CG1 ILE C 32 7565 7763 8591 460 -110 -799 C
ATOM 4847 CG2 ILE C 32 -7.609 39.989 15.063 1.00 63.24 C
ANISOU 4847 CG2 ILE C 32 7584 7822 8621 380 -43 -826 C
ATOM 4848 CD1 ILE C 32 -6.736 39.975 12.095 1.00 64.43 C
ANISOU 4848 CD1 ILE C 32 7782 7971 8726 458 -106 -718 C
ATOM 4849 N SER C 33 -10.168 41.279 16.656 1.00 58.60 N
ANISOU 4849 N SER C 33 6923 7192 8149 363 -42 -1004 N
ATOM 4850 CA SER C 33 -10.214 41.910 17.973 1.00 55.94 C
ANISOU 4850 CA SER C 33 6568 6857 7827 324 -18 -1046 C
ATOM 4851 C SER C 33 -9.895 40.896 19.071 1.00 54.38 C
ANISOU 4851 C SER C 33 6370 6704 7587 274 34 -1047 C
ATOM 4852 O SER C 33 -9.997 39.687 18.856 1.00 56.99 O
ANISOU 4852 O SER C 33 6704 7057 7891 272 49 -1034 O
ATOM 4853 CB SER C 33 -11.598 42.496 18.221 1.00 54.74 C
ANISOU 4853 CB SER C 33 6376 6682 7739 337 -28 -1137 C
ATOM 4854 OG SER C 33 -12.550 41.460 18.304 1.00 55.09 O
ANISOU 4854 OG SER C 33 6397 6747 7786 335 -7 -1182 O
ATOM 4855 N TYR C 34 -9.516 41.386 20.249 1.00 53.57 N
ANISOU 4855 N TYR C 34 6263 6611 7477 231 58 -1061 N
ATOM 4856 CA TYR C 34 -9.386 40.514 21.418 1.00 53.85 C
ANISOU 4856 CA TYR C 34 6295 6689 7476 176 106 -1071 C
ATOM 4857 C TYR C 34 -9.778 41.181 22.724 1.00 54.43 C
ANISOU 4857 C TYR C 34 6344 6771 7564 135 131 -1136 C
ATOM 4858 O TYR C 34 -9.790 42.410 22.841 1.00 53.55 O
ANISOU 4858 O TYR C 34 6226 6632 7486 144 112 -1161 O
ATOM 4859 CB TYR C 34 -7.967 39.927 21.540 1.00 54.49 C
ANISOU 4859 CB TYR C 34 6410 6792 7501 154 117 -987 C
ATOM 4860 CG TYR C 34 -6.902 40.895 22.031 1.00 54.24 C
ANISOU 4860 CG TYR C 34 6395 6753 7458 133 112 -953 C
ATOM 4861 CD1 TYR C 34 -6.286 41.789 21.148 1.00 53.62 C
ANISOU 4861 CD1 TYR C 34 6334 6645 7393 167 75 -910 C
ATOM 4862 CD2 TYR C 34 -6.499 40.905 23.372 1.00 52.82 C
ANISOU 4862 CD2 TYR C 34 6215 6599 7253 77 143 -962 C
ATOM 4863 CE1 TYR C 34 -5.313 42.673 21.586 1.00 53.63 C
ANISOU 4863 CE1 TYR C 34 6349 6639 7388 147 70 -877 C
ATOM 4864 CE2 TYR C 34 -5.525 41.786 23.819 1.00 54.60 C
ANISOU 4864 CE2 TYR C 34 6456 6818 7470 57 137 -932 C
ATOM 4865 CZ TYR C 34 -4.938 42.674 22.922 1.00 56.19 C
ANISOU 4865 CZ TYR C 34 6671 6986 7689 93 100 -890 C
ATOM 4866 OH TYR C 34 -3.964 43.559 23.348 1.00 57.10 O
ANISOU 4866 OH TYR C 34 6802 7094 7800 72 92 -859 O
ATOM 4867 N SER C 35 -10.095 40.340 23.700 1.00 53.15 N
ANISOU 4867 N SER C 35 6170 6647 7374 87 173 -1163 N
ATOM 4868 CA SER C 35 -10.261 40.753 25.073 1.00 52.58 C
ANISOU 4868 CA SER C 35 6082 6599 7297 35 206 -1215 C
ATOM 4869 C SER C 35 -9.524 39.718 25.913 1.00 53.05 C
ANISOU 4869 C SER C 35 6162 6701 7292 -21 239 -1169 C
ATOM 4870 O SER C 35 -8.905 38.810 25.367 1.00 55.52 O
ANISOU 4870 O SER C 35 6498 7018 7576 -12 232 -1103 O
ATOM 4871 CB SER C 35 -11.745 40.792 25.423 1.00 51.38 C
ANISOU 4871 CB SER C 35 5884 6454 7184 32 223 -1313 C
ATOM 4872 OG SER C 35 -12.270 39.488 25.494 1.00 49.78 O
ANISOU 4872 OG SER C 35 5674 6281 6958 13 248 -1316 O
ATOM 4873 N TYR C 36 -9.568 39.851 27.230 1.00 53.96 N
ANISOU 4873 N TYR C 36 6267 6848 7385 -79 273 -1205 N
ATOM 4874 CA TYR C 36 -8.952 38.850 28.082 1.00 57.27 C
ANISOU 4874 CA TYR C 36 6706 7308 7745 -138 301 -1163 C
ATOM 4875 C TYR C 36 -9.920 37.701 28.330 1.00 60.31 C
ANISOU 4875 C TYR C 36 7073 7722 8120 -163 328 -1195 C
ATOM 4876 O TYR C 36 -11.126 37.848 28.145 1.00 64.29 O
ANISOU 4876 O TYR C 36 7542 8222 8662 -146 334 -1266 O
ATOM 4877 CB TYR C 36 -8.491 39.465 29.404 1.00 59.60 C
ANISOU 4877 CB TYR C 36 7005 7628 8012 -196 324 -1180 C
ATOM 4878 CG TYR C 36 -7.469 40.577 29.265 1.00 59.18 C
ANISOU 4878 CG TYR C 36 6970 7547 7966 -179 297 -1146 C
ATOM 4879 CD1 TYR C 36 -7.691 41.827 29.843 1.00 60.00 C
ANISOU 4879 CD1 TYR C 36 7058 7642 8095 -187 299 -1206 C
ATOM 4880 CD2 TYR C 36 -6.278 40.380 28.566 1.00 57.76 C
ANISOU 4880 CD2 TYR C 36 6824 7351 7770 -156 271 -1055 C
ATOM 4881 CE1 TYR C 36 -6.759 42.847 29.731 1.00 58.43 C
ANISOU 4881 CE1 TYR C 36 6877 7416 7906 -175 272 -1174 C
ATOM 4882 CE2 TYR C 36 -5.345 41.397 28.439 1.00 58.10 C
ANISOU 4882 CE2 TYR C 36 6884 7370 7821 -145 247 -1022 C
ATOM 4883 CZ TYR C 36 -5.589 42.626 29.027 1.00 59.07 C
ANISOU 4883 CZ TYR C 36 6991 7481 7969 -155 247 -1080 C
ATOM 4884 OH TYR C 36 -4.665 43.636 28.911 1.00 59.04 O
ANISOU 4884 OH TYR C 36 7004 7451 7975 -146 221 -1046 O
ATOM 4885 N CYS C 37 -9.382 36.552 28.724 1.00 64.62 N
ANISOU 4885 N CYS C 37 7640 8293 8618 -202 340 -1140 N
ATOM 4886 CA CYS C 37 -10.203 35.405 29.097 1.00 70.49 C
ANISOU 4886 CA CYS C 37 8368 9066 9347 -238 365 -1162 C
ATOM 4887 C CYS C 37 -11.010 35.739 30.353 1.00 72.54 C
ANISOU 4887 C CYS C 37 8599 9364 9596 -297 406 -1239 C
ATOM 4888 O CYS C 37 -10.560 36.512 31.195 1.00 77.50 O
ANISOU 4888 O CYS C 37 9232 10007 10206 -330 418 -1251 O
ATOM 4889 CB CYS C 37 -9.327 34.161 29.308 1.00 71.42 C
ANISOU 4889 CB CYS C 37 8519 9199 9418 -270 364 -1081 C
ATOM 4890 SG CYS C 37 -8.590 33.503 27.782 1.00 76.45 S
ANISOU 4890 SG CYS C 37 9182 9797 10068 -200 322 -1004 S
ATOM 4891 N ASP C 38 -12.205 35.168 30.465 1.00 75.47 N
ANISOU 4891 N ASP C 38 8940 9755 9981 -312 428 -1294 N
ATOM 4892 CA ASP C 38 -13.102 35.435 31.595 1.00 79.06 C
ANISOU 4892 CA ASP C 38 9359 10252 10426 -369 471 -1376 C
ATOM 4893 C ASP C 38 -12.474 35.137 32.959 1.00 78.77 C
ANISOU 4893 C ASP C 38 9343 10263 10322 -454 501 -1350 C
ATOM 4894 O ASP C 38 -12.794 35.793 33.949 1.00 80.83 O
ANISOU 4894 O ASP C 38 9584 10556 10568 -498 532 -1412 O
ATOM 4895 CB ASP C 38 -14.401 34.623 31.457 1.00 81.85 C
ANISOU 4895 CB ASP C 38 9678 10622 10798 -377 490 -1424 C
ATOM 4896 CG ASP C 38 -15.231 35.022 30.244 1.00 82.64 C
ANISOU 4896 CG ASP C 38 9750 10680 10969 -299 463 -1467 C
ATOM 4897 OD1 ASP C 38 -15.045 36.141 29.719 1.00 84.52 O
ANISOU 4897 OD1 ASP C 38 9985 10882 11244 -247 438 -1483 O
ATOM 4898 OD2 ASP C 38 -16.084 34.211 29.819 1.00 82.78 O
ANISOU 4898 OD2 ASP C 38 9748 10700 11005 -292 465 -1485 O
ATOM 4899 N HIS C 39 -11.579 34.152 32.993 1.00 78.99 N
ANISOU 4899 N HIS C 39 9409 10293 10308 -477 488 -1262 N
ATOM 4900 CA HIS C 39 -11.056 33.581 34.237 1.00 81.90 C
ANISOU 4900 CA HIS C 39 9800 10707 10610 -562 510 -1227 C
ATOM 4901 C HIS C 39 -9.612 33.924 34.515 1.00 81.57 C
ANISOU 4901 C HIS C 39 9798 10657 10538 -570 490 -1158 C
ATOM 4902 O HIS C 39 -9.035 33.465 35.506 1.00 82.65 O
ANISOU 4902 O HIS C 39 9957 10826 10618 -639 500 -1119 O
ATOM 4903 CB HIS C 39 -11.245 32.061 34.217 1.00 84.48 C
ANISOU 4903 CB HIS C 39 10137 11045 10915 -593 510 -1181 C
ATOM 4904 CG HIS C 39 -10.484 31.358 33.106 1.00 87.86 C
ANISOU 4904 CG HIS C 39 10594 11428 11360 -537 467 -1101 C
ATOM 4905 ND1 HIS C 39 -10.010 30.104 33.233 1.00 89.40 N
ANISOU 4905 ND1 HIS C 39 10814 11625 11525 -568 455 -1031 N
ATOM 4906 CD2 HIS C 39 -10.118 31.787 31.827 1.00 87.66 C
ANISOU 4906 CD2 HIS C 39 10574 11355 11378 -452 433 -1082 C
ATOM 4907 CE1 HIS C 39 -9.380 29.744 32.097 1.00 88.72 C
ANISOU 4907 CE1 HIS C 39 10746 11496 11465 -503 417 -977 C
ATOM 4908 NE2 HIS C 39 -9.444 30.776 31.240 1.00 88.96 N
ANISOU 4908 NE2 HIS C 39 10765 11499 11536 -434 406 -1008 N
ATOM 4909 N LEU C 40 -9.018 34.738 33.645 1.00 78.26 N
ANISOU 4909 N LEU C 40 9386 10193 10153 -502 459 -1140 N
ATOM 4910 CA LEU C 40 -7.605 35.085 33.738 1.00 75.75 C
ANISOU 4910 CA LEU C 40 9104 9863 9814 -501 436 -1071 C
ATOM 4911 C LEU C 40 -7.414 36.448 33.082 1.00 76.05 C
ANISOU 4911 C LEU C 40 9134 9863 9896 -441 416 -1095 C
ATOM 4912 O LEU C 40 -7.707 36.619 31.894 1.00 78.49 O
ANISOU 4912 O LEU C 40 9434 10134 10252 -372 393 -1099 O
ATOM 4913 CB LEU C 40 -6.758 34.011 33.036 1.00 75.04 C
ANISOU 4913 CB LEU C 40 9043 9751 9715 -479 406 -978 C
ATOM 4914 CG LEU C 40 -5.375 33.590 33.559 1.00 73.95 C
ANISOU 4914 CG LEU C 40 8942 9621 9534 -515 390 -893 C
ATOM 4915 CD1 LEU C 40 -4.281 34.523 33.059 1.00 71.35 C
ANISOU 4915 CD1 LEU C 40 8627 9261 9218 -472 364 -857 C
ATOM 4916 CD2 LEU C 40 -5.338 33.451 35.078 1.00 72.33 C
ANISOU 4916 CD2 LEU C 40 8744 9463 9273 -606 417 -901 C
ATOM 4917 N LYS C 41 -6.934 37.422 33.851 1.00 70.82 N
ANISOU 4917 N LYS C 41 8476 9210 9219 -468 422 -1112 N
ATOM 4918 CA LYS C 41 -6.932 38.806 33.380 1.00 69.73 C
ANISOU 4918 CA LYS C 41 8326 9037 9129 -419 404 -1149 C
ATOM 4919 C LYS C 41 -5.586 39.550 33.440 1.00 66.16 C
ANISOU 4919 C LYS C 41 7903 8566 8667 -415 379 -1093 C
ATOM 4920 O LYS C 41 -5.550 40.784 33.387 1.00 64.44 O
ANISOU 4920 O LYS C 41 7676 8326 8481 -394 368 -1129 O
ATOM 4921 CB LYS C 41 -8.049 39.604 34.077 1.00 74.64 C
ANISOU 4921 CB LYS C 41 8910 9678 9770 -439 434 -1259 C
ATOM 4922 CG LYS C 41 -9.444 39.330 33.521 1.00 79.77 C
ANISOU 4922 CG LYS C 41 9522 10324 10463 -408 444 -1324 C
ATOM 4923 CD LYS C 41 -10.344 40.552 33.636 1.00 83.44 C
ANISOU 4923 CD LYS C 41 9947 10777 10979 -387 451 -1426 C
ATOM 4924 CE LYS C 41 -11.326 40.654 32.473 1.00 85.30 C
ANISOU 4924 CE LYS C 41 10153 10974 11281 -317 431 -1464 C
ATOM 4925 NZ LYS C 41 -12.503 39.747 32.595 1.00 85.31 N
ANISOU 4925 NZ LYS C 41 10124 11007 11283 -336 462 -1510 N
ATOM 4926 N PHE C 42 -4.486 38.807 33.523 1.00 62.94 N
ANISOU 4926 N PHE C 42 7528 8166 8220 -435 368 -1006 N
ATOM 4927 CA PHE C 42 -3.151 39.411 33.509 1.00 60.80 C
ANISOU 4927 CA PHE C 42 7282 7878 7941 -431 342 -947 C
ATOM 4928 C PHE C 42 -2.919 40.213 32.220 1.00 58.34 C
ANISOU 4928 C PHE C 42 6969 7516 7681 -355 309 -932 C
ATOM 4929 O PHE C 42 -3.170 39.709 31.128 1.00 57.13 O
ANISOU 4929 O PHE C 42 6813 7343 7551 -306 296 -912 O
ATOM 4930 CB PHE C 42 -2.065 38.351 33.703 1.00 60.27 C
ANISOU 4930 CB PHE C 42 7244 7824 7829 -459 333 -856 C
ATOM 4931 CG PHE C 42 -2.098 37.680 35.051 1.00 63.94 C
ANISOU 4931 CG PHE C 42 7717 8337 8239 -541 358 -858 C
ATOM 4932 CD1 PHE C 42 -2.059 36.291 35.153 1.00 64.40 C
ANISOU 4932 CD1 PHE C 42 7787 8413 8269 -565 359 -813 C
ATOM 4933 CD2 PHE C 42 -2.161 38.431 36.223 1.00 65.32 C
ANISOU 4933 CD2 PHE C 42 7889 8541 8388 -595 377 -904 C
ATOM 4934 CE1 PHE C 42 -2.082 35.666 36.393 1.00 64.75 C
ANISOU 4934 CE1 PHE C 42 7842 8500 8260 -646 378 -808 C
ATOM 4935 CE2 PHE C 42 -2.182 37.813 37.466 1.00 65.69 C
ANISOU 4935 CE2 PHE C 42 7946 8636 8377 -676 399 -903 C
ATOM 4936 CZ PHE C 42 -2.144 36.429 37.550 1.00 66.84 C
ANISOU 4936 CZ PHE C 42 8104 8797 8493 -702 399 -852 C
ATOM 4937 N PRO C 43 -2.460 41.474 32.351 1.00 56.05 N
ANISOU 4937 N PRO C 43 6680 7206 7409 -349 295 -943 N
ATOM 4938 CA PRO C 43 -2.412 42.379 31.199 1.00 55.27 C
ANISOU 4938 CA PRO C 43 6577 7058 7362 -283 263 -939 C
ATOM 4939 C PRO C 43 -1.263 42.153 30.204 1.00 54.32 C
ANISOU 4939 C PRO C 43 6481 6917 7239 -248 233 -845 C
ATOM 4940 O PRO C 43 -0.138 41.852 30.604 1.00 56.24 O
ANISOU 4940 O PRO C 43 6746 7175 7447 -277 230 -783 O
ATOM 4941 CB PRO C 43 -2.310 43.765 31.849 1.00 54.19 C
ANISOU 4941 CB PRO C 43 6435 6910 7244 -299 258 -984 C
ATOM 4942 CG PRO C 43 -1.672 43.517 33.170 1.00 51.88 C
ANISOU 4942 CG PRO C 43 6156 6658 6897 -370 278 -972 C
ATOM 4943 CD PRO C 43 -2.140 42.166 33.615 1.00 53.03 C
ANISOU 4943 CD PRO C 43 6300 6845 7001 -406 308 -972 C
ATOM 4944 N ILE C 44 -1.589 42.297 28.915 1.00 53.90 N
ANISOU 4944 N ILE C 44 6423 6833 7224 -186 211 -838 N
ATOM 4945 CA ILE C 44 -0.644 42.352 27.785 1.00 52.43 C
ANISOU 4945 CA ILE C 44 6255 6623 7042 -145 182 -761 C
ATOM 4946 C ILE C 44 -1.267 43.284 26.753 1.00 51.92 C
ANISOU 4946 C ILE C 44 6178 6517 7029 -90 155 -789 C
ATOM 4947 O ILE C 44 -2.465 43.185 26.471 1.00 54.31 O
ANISOU 4947 O ILE C 44 6461 6812 7359 -67 158 -847 O
ATOM 4948 CB ILE C 44 -0.488 40.989 27.042 1.00 52.18 C
ANISOU 4948 CB ILE C 44 6231 6605 6991 -123 184 -713 C
ATOM 4949 CG1 ILE C 44 -0.874 39.796 27.910 1.00 53.19 C
ANISOU 4949 CG1 ILE C 44 6355 6767 7085 -166 213 -728 C
ATOM 4950 CG2 ILE C 44 0.886 40.810 26.405 1.00 48.10 C
ANISOU 4950 CG2 ILE C 44 5734 6084 6456 -108 166 -626 C
ATOM 4951 CD1 ILE C 44 -2.341 39.453 27.790 1.00 53.29 C
ANISOU 4951 CD1 ILE C 44 6345 6782 7119 -155 227 -799 C
ATOM 4952 N SER C 45 -0.480 44.187 26.180 1.00 50.15 N
ANISOU 4952 N SER C 45 5967 6265 6820 -69 125 -746 N
ATOM 4953 CA SER C 45 -0.945 44.895 24.991 1.00 51.55 C
ANISOU 4953 CA SER C 45 6139 6402 7042 -15 93 -752 C
ATOM 4954 C SER C 45 -0.244 44.321 23.761 1.00 50.80 C
ANISOU 4954 C SER C 45 6061 6308 6929 19 78 -674 C
ATOM 4955 O SER C 45 0.978 44.359 23.649 1.00 52.54 O
ANISOU 4955 O SER C 45 6299 6536 7126 9 72 -607 O
ATOM 4956 CB SER C 45 -0.792 46.417 25.116 1.00 52.14 C
ANISOU 4956 CB SER C 45 6213 6440 7156 -13 65 -768 C
ATOM 4957 OG SER C 45 0.445 46.871 24.611 1.00 55.50 O
ANISOU 4957 OG SER C 45 6660 6853 7571 -10 42 -690 O
ATOM 4958 N ILE C 46 -1.034 43.759 22.858 1.00 50.82 N
ANISOU 4958 N ILE C 46 6057 6306 6943 58 73 -689 N
ATOM 4959 CA ILE C 46 -0.499 43.054 21.702 1.00 50.91 C
ANISOU 4959 CA ILE C 46 6083 6326 6933 91 64 -626 C
ATOM 4960 C ILE C 46 -1.246 43.496 20.441 1.00 50.82 C
ANISOU 4960 C ILE C 46 6069 6284 6956 143 32 -639 C
ATOM 4961 O ILE C 46 -2.471 43.595 20.443 1.00 53.05 O
ANISOU 4961 O ILE C 46 6333 6552 7270 158 29 -704 O
ATOM 4962 CB ILE C 46 -0.532 41.514 21.924 1.00 50.64 C
ANISOU 4962 CB ILE C 46 6048 6327 6865 80 92 -620 C
ATOM 4963 CG1 ILE C 46 0.086 40.760 20.739 1.00 54.28 C
ANISOU 4963 CG1 ILE C 46 6521 6796 7304 115 84 -561 C
ATOM 4964 CG2 ILE C 46 -1.940 41.022 22.224 1.00 50.79 C
ANISOU 4964 CG2 ILE C 46 6047 6348 6902 81 107 -694 C
ATOM 4965 CD1 ILE C 46 0.147 39.250 20.909 1.00 53.82 C
ANISOU 4965 CD1 ILE C 46 6462 6766 7218 107 106 -552 C
ATOM 4966 N SER C 47 -0.500 43.798 19.381 1.00 50.09 N
ANISOU 4966 N SER C 47 5992 6183 6854 168 8 -576 N
ATOM 4967 CA SER C 47 -1.090 44.222 18.109 1.00 50.49 C
ANISOU 4967 CA SER C 47 6045 6208 6930 215 -25 -576 C
ATOM 4968 C SER C 47 -0.238 43.765 16.921 1.00 51.70 C
ANISOU 4968 C SER C 47 6217 6378 7047 238 -33 -504 C
ATOM 4969 O SER C 47 0.813 43.148 17.104 1.00 50.97 O
ANISOU 4969 O SER C 47 6132 6316 6917 221 -11 -457 O
ATOM 4970 CB SER C 47 -1.266 45.742 18.085 1.00 48.57 C
ANISOU 4970 CB SER C 47 5801 5921 6731 218 -61 -588 C
ATOM 4971 OG SER C 47 -0.024 46.398 17.929 1.00 47.67 O
ANISOU 4971 OG SER C 47 5705 5804 6601 203 -73 -520 O
ATOM 4972 N SER C 48 -0.691 44.069 15.708 1.00 53.99 N
ANISOU 4972 N SER C 48 6512 6650 7349 277 -65 -496 N
ATOM 4973 CA SER C 48 0.073 43.744 14.507 1.00 55.81 C
ANISOU 4973 CA SER C 48 6759 6900 7544 299 -73 -431 C
ATOM 4974 C SER C 48 0.175 44.934 13.572 1.00 57.63 C
ANISOU 4974 C SER C 48 7003 7102 7789 315 -117 -396 C
ATOM 4975 O SER C 48 -0.624 45.864 13.658 1.00 61.32 O
ANISOU 4975 O SER C 48 7466 7528 8304 322 -147 -432 O
ATOM 4976 CB SER C 48 -0.544 42.556 13.771 1.00 57.57 C
ANISOU 4976 CB SER C 48 6979 7142 7750 330 -65 -449 C
ATOM 4977 OG SER C 48 -1.743 42.930 13.113 1.00 64.77 O
ANISOU 4977 OG SER C 48 7887 8026 8696 362 -97 -489 O
ATOM 4978 N GLU C 49 1.172 44.889 12.691 1.00 59.84 N
ANISOU 4978 N GLU C 49 7300 7404 8031 319 -120 -327 N
ATOM 4979 CA GLU C 49 1.370 45.892 11.651 1.00 61.35 C
ANISOU 4979 CA GLU C 49 7508 7576 8226 331 -161 -281 C
ATOM 4980 C GLU C 49 1.817 45.191 10.366 1.00 63.26 C
ANISOU 4980 C GLU C 49 7761 7855 8417 353 -158 -236 C
ATOM 4981 O GLU C 49 2.927 44.657 10.306 1.00 64.00 O
ANISOU 4981 O GLU C 49 7857 7989 8469 341 -129 -192 O
ATOM 4982 CB GLU C 49 2.397 46.932 12.102 1.00 64.18 C
ANISOU 4982 CB GLU C 49 7873 7922 8588 296 -169 -235 C
ATOM 4983 CG GLU C 49 2.863 47.890 11.016 1.00 66.68 C
ANISOU 4983 CG GLU C 49 8209 8226 8899 300 -208 -171 C
ATOM 4984 CD GLU C 49 3.791 48.960 11.552 1.00 68.60 C
ANISOU 4984 CD GLU C 49 8458 8452 9155 263 -219 -129 C
ATOM 4985 OE1 GLU C 49 3.325 49.809 12.338 1.00 71.88 O
ANISOU 4985 OE1 GLU C 49 8867 8822 9620 252 -239 -166 O
ATOM 4986 OE2 GLU C 49 4.983 48.958 11.184 1.00 71.58 O
ANISOU 4986 OE2 GLU C 49 8843 8860 9493 245 -207 -62 O
ATOM 4987 N PRO C 50 0.944 45.165 9.339 1.00 64.62 N
ANISOU 4987 N PRO C 50 7941 8018 8594 387 -187 -249 N
ATOM 4988 CA PRO C 50 -0.403 45.732 9.342 1.00 63.37 C
ANISOU 4988 CA PRO C 50 7776 7812 8488 406 -224 -304 C
ATOM 4989 C PRO C 50 -1.403 44.777 9.987 1.00 61.89 C
ANISOU 4989 C PRO C 50 7568 7627 8321 418 -200 -379 C
ATOM 4990 O PRO C 50 -1.008 43.826 10.659 1.00 62.67 O
ANISOU 4990 O PRO C 50 7657 7756 8396 403 -156 -388 O
ATOM 4991 CB PRO C 50 -0.706 45.868 7.853 1.00 63.93 C
ANISOU 4991 CB PRO C 50 7864 7883 8541 436 -262 -274 C
ATOM 4992 CG PRO C 50 -0.010 44.699 7.246 1.00 63.78 C
ANISOU 4992 CG PRO C 50 7851 7922 8460 443 -227 -246 C
ATOM 4993 CD PRO C 50 1.239 44.483 8.063 1.00 62.81 C
ANISOU 4993 CD PRO C 50 7723 7827 8315 410 -185 -215 C
ATOM 4994 N CYS C 51 -2.688 45.031 9.780 1.00 63.43 N
ANISOU 4994 N CYS C 51 7753 7789 8558 442 -230 -432 N
ATOM 4995 CA CYS C 51 -3.725 44.115 10.223 1.00 64.85 C
ANISOU 4995 CA CYS C 51 7911 7972 8755 454 -211 -502 C
ATOM 4996 C CYS C 51 -3.592 42.797 9.466 1.00 64.04 C
ANISOU 4996 C CYS C 51 7815 7911 8605 474 -191 -490 C
ATOM 4997 O CYS C 51 -3.088 42.781 8.337 1.00 66.19 O
ANISOU 4997 O CYS C 51 8107 8200 8841 489 -206 -439 O
ATOM 4998 CB CYS C 51 -5.100 44.721 9.980 1.00 68.97 C
ANISOU 4998 CB CYS C 51 8420 8450 9335 480 -253 -557 C
ATOM 4999 SG CYS C 51 -6.397 43.912 10.932 1.00 73.43 S
ANISOU 4999 SG CYS C 51 8949 9013 9936 481 -225 -655 S
ATOM 5000 N ILE C 52 -4.026 41.698 10.084 1.00 61.97 N
ANISOU 5000 N ILE C 52 7536 7666 8343 471 -157 -535 N
ATOM 5001 CA ILE C 52 -3.858 40.376 9.473 1.00 62.27 C
ANISOU 5001 CA ILE C 52 7579 7741 8340 488 -137 -527 C
ATOM 5002 C ILE C 52 -4.855 40.133 8.349 1.00 60.18 C
ANISOU 5002 C ILE C 52 7315 7467 8082 527 -170 -551 C
ATOM 5003 O ILE C 52 -6.071 40.130 8.566 1.00 60.97 O
ANISOU 5003 O ILE C 52 7398 7543 8224 538 -183 -611 O
ATOM 5004 CB ILE C 52 -3.880 39.210 10.501 1.00 63.34 C
ANISOU 5004 CB ILE C 52 7698 7896 8470 467 -93 -559 C
ATOM 5005 CG1 ILE C 52 -2.526 39.070 11.200 1.00 62.61 C
ANISOU 5005 CG1 ILE C 52 7612 7828 8349 435 -62 -512 C
ATOM 5006 CG2 ILE C 52 -4.200 37.879 9.834 1.00 62.20 C
ANISOU 5006 CG2 ILE C 52 7553 7774 8304 493 -85 -573 C
ATOM 5007 CD1 ILE C 52 -2.506 39.653 12.592 1.00 64.69 C
ANISOU 5007 CD1 ILE C 52 7864 8076 8636 396 -47 -532 C
ATOM 5008 N ARG C 53 -4.313 39.954 7.148 1.00 56.76 N
ANISOU 5008 N ARG C 53 6902 7056 7606 547 -182 -505 N
ATOM 5009 CA ARG C 53 -5.073 39.484 6.010 1.00 57.33 C
ANISOU 5009 CA ARG C 53 6980 7132 7670 583 -208 -522 C
ATOM 5010 C ARG C 53 -4.885 37.978 5.961 1.00 54.21 C
ANISOU 5010 C ARG C 53 6579 6772 7244 590 -173 -536 C
ATOM 5011 O ARG C 53 -3.758 37.500 5.836 1.00 55.61 O
ANISOU 5011 O ARG C 53 6765 6983 7378 583 -147 -496 O
ATOM 5012 CB ARG C 53 -4.556 40.135 4.720 1.00 62.76 C
ANISOU 5012 CB ARG C 53 7694 7829 8323 596 -241 -464 C
ATOM 5013 CG ARG C 53 -5.470 39.941 3.523 1.00 67.81 C
ANISOU 5013 CG ARG C 53 8341 8464 8958 631 -281 -481 C
ATOM 5014 CD ARG C 53 -4.954 40.610 2.259 1.00 74.74 C
ANISOU 5014 CD ARG C 53 9248 9355 9794 638 -314 -419 C
ATOM 5015 NE ARG C 53 -4.026 39.765 1.510 1.00 78.86 N
ANISOU 5015 NE ARG C 53 9783 9932 10248 643 -286 -385 N
ATOM 5016 CZ ARG C 53 -2.806 40.137 1.133 1.00 84.90 C
ANISOU 5016 CZ ARG C 53 10563 10728 10966 625 -274 -321 C
ATOM 5017 NH1 ARG C 53 -2.354 41.354 1.420 1.00 88.02 N
ANISOU 5017 NH1 ARG C 53 10966 11102 11375 600 -291 -279 N
ATOM 5018 NH2 ARG C 53 -2.038 39.290 0.460 1.00 84.91 N
ANISOU 5018 NH2 ARG C 53 10570 10782 10907 632 -246 -301 N
ATOM 5019 N LEU C 54 -5.978 37.226 6.068 1.00 52.23 N
ANISOU 5019 N LEU C 54 6313 6512 7018 605 -175 -595 N
ATOM 5020 CA LEU C 54 -5.898 35.763 6.030 1.00 49.52 C
ANISOU 5020 CA LEU C 54 5964 6196 6653 612 -147 -612 C
ATOM 5021 C LEU C 54 -5.388 35.231 4.690 1.00 50.79 C
ANISOU 5021 C LEU C 54 6145 6389 6764 640 -155 -583 C
ATOM 5022 O LEU C 54 -4.897 34.112 4.619 1.00 53.15 O
ANISOU 5022 O LEU C 54 6441 6714 7036 645 -129 -582 O
ATOM 5023 CB LEU C 54 -7.236 35.113 6.405 1.00 47.92 C
ANISOU 5023 CB LEU C 54 5741 5975 6491 619 -149 -681 C
ATOM 5024 CG LEU C 54 -7.778 35.317 7.835 1.00 48.15 C
ANISOU 5024 CG LEU C 54 5745 5983 6564 587 -130 -721 C
ATOM 5025 CD1 LEU C 54 -8.856 34.299 8.173 1.00 45.25 C
ANISOU 5025 CD1 LEU C 54 5357 5612 6223 589 -121 -782 C
ATOM 5026 CD2 LEU C 54 -6.684 35.277 8.893 1.00 47.39 C
ANISOU 5026 CD2 LEU C 54 5651 5902 6451 549 -92 -690 C
ATOM 5027 N ARG C 55 -5.491 36.044 3.641 1.00 52.94 N
ANISOU 5027 N ARG C 55 6434 6658 7022 658 -192 -558 N
ATOM 5028 CA ARG C 55 -4.934 35.715 2.333 1.00 56.15 C
ANISOU 5028 CA ARG C 55 6860 7100 7372 679 -199 -525 C
ATOM 5029 C ARG C 55 -3.431 35.522 2.439 1.00 55.15 C
ANISOU 5029 C ARG C 55 6740 7012 7203 662 -162 -475 C
ATOM 5030 O ARG C 55 -2.870 34.670 1.758 1.00 56.67 O
ANISOU 5030 O ARG C 55 6936 7242 7352 677 -146 -467 O
ATOM 5031 CB ARG C 55 -5.205 36.846 1.333 1.00 63.28 C
ANISOU 5031 CB ARG C 55 7783 7992 8267 690 -248 -496 C
ATOM 5032 CG ARG C 55 -5.008 36.489 -0.142 1.00 66.27 C
ANISOU 5032 CG ARG C 55 8183 8408 8589 714 -264 -476 C
ATOM 5033 CD ARG C 55 -6.322 36.574 -0.914 1.00 71.78 C
ANISOU 5033 CD ARG C 55 8885 9082 9305 742 -314 -511 C
ATOM 5034 NE ARG C 55 -7.474 36.169 -0.100 1.00 74.09 N
ANISOU 5034 NE ARG C 55 9152 9338 9660 748 -316 -577 N
ATOM 5035 CZ ARG C 55 -8.313 35.178 -0.397 1.00 75.87 C
ANISOU 5035 CZ ARG C 55 9367 9564 9894 771 -321 -628 C
ATOM 5036 NH1 ARG C 55 -8.162 34.474 -1.519 1.00 74.28 N
ANISOU 5036 NH1 ARG C 55 9181 9397 9643 793 -327 -625 N
ATOM 5037 NH2 ARG C 55 -9.318 34.904 0.428 1.00 75.25 N
ANISOU 5037 NH2 ARG C 55 9263 9454 9873 770 -320 -685 N
ATOM 5038 N GLY C 56 -2.795 36.328 3.288 1.00 52.94 N
ANISOU 5038 N GLY C 56 6457 6720 6935 631 -150 -444 N
ATOM 5039 CA GLY C 56 -1.342 36.346 3.451 1.00 50.73 C
ANISOU 5039 CA GLY C 56 6181 6473 6620 611 -119 -392 C
ATOM 5040 C GLY C 56 -0.895 37.697 3.977 1.00 51.54 C
ANISOU 5040 C GLY C 56 6288 6555 6737 582 -128 -353 C
ATOM 5041 O GLY C 56 -1.485 38.720 3.644 1.00 52.35 O
ANISOU 5041 O GLY C 56 6401 6630 6859 584 -167 -348 O
ATOM 5042 N THR C 57 0.144 37.707 4.810 1.00 54.44 N
ANISOU 5042 N THR C 57 6649 6935 7100 554 -97 -325 N
ATOM 5043 CA THR C 57 0.648 38.942 5.427 1.00 53.23 C
ANISOU 5043 CA THR C 57 6498 6761 6963 522 -104 -289 C
ATOM 5044 C THR C 57 2.132 38.825 5.770 1.00 52.44 C
ANISOU 5044 C THR C 57 6395 6694 6834 498 -70 -241 C
ATOM 5045 O THR C 57 2.600 37.746 6.126 1.00 51.03 O
ANISOU 5045 O THR C 57 6205 6540 6644 499 -38 -251 O
ATOM 5046 CB THR C 57 -0.110 39.267 6.733 1.00 52.63 C
ANISOU 5046 CB THR C 57 6409 6644 6943 505 -105 -333 C
ATOM 5047 OG1 THR C 57 -1.471 38.829 6.631 1.00 53.09 O
ANISOU 5047 OG1 THR C 57 6460 6682 7030 528 -120 -394 O
ATOM 5048 CG2 THR C 57 -0.083 40.759 7.020 1.00 52.79 C
ANISOU 5048 CG2 THR C 57 6435 6630 6990 485 -132 -311 C
ATOM 5049 N ASN C 58 2.864 39.932 5.651 1.00 52.07 N
ANISOU 5049 N ASN C 58 6358 6647 6778 476 -81 -188 N
ATOM 5050 CA ASN C 58 4.209 40.044 6.225 1.00 53.57 C
ANISOU 5050 CA ASN C 58 6542 6859 6954 447 -53 -144 C
ATOM 5051 C ASN C 58 4.244 41.251 7.141 1.00 51.52 C
ANISOU 5051 C ASN C 58 6283 6560 6730 415 -68 -132 C
ATOM 5052 O ASN C 58 3.867 42.345 6.725 1.00 52.19 O
ANISOU 5052 O ASN C 58 6381 6618 6829 413 -104 -116 O
ATOM 5053 CB ASN C 58 5.298 40.214 5.155 1.00 58.47 C
ANISOU 5053 CB ASN C 58 7169 7524 7521 446 -46 -84 C
ATOM 5054 CG ASN C 58 4.926 39.593 3.818 1.00 65.20 C
ANISOU 5054 CG ASN C 58 8030 8405 8336 480 -52 -94 C
ATOM 5055 OD1 ASN C 58 4.609 38.402 3.725 1.00 67.47 O
ANISOU 5055 OD1 ASN C 58 8308 8708 8618 505 -36 -135 O
ATOM 5056 ND2 ASN C 58 4.974 40.406 2.766 1.00 68.07 N
ANISOU 5056 ND2 ASN C 58 8412 8778 8672 480 -79 -55 N
ATOM 5057 N GLY C 59 4.698 41.063 8.378 1.00 49.43 N
ANISOU 5057 N GLY C 59 6005 6291 6482 389 -44 -138 N
ATOM 5058 CA GLY C 59 4.796 42.173 9.319 1.00 48.44 C
ANISOU 5058 CA GLY C 59 5880 6131 6390 357 -56 -131 C
ATOM 5059 C GLY C 59 5.339 41.841 10.694 1.00 50.00 C
ANISOU 5059 C GLY C 59 6065 6331 6599 326 -27 -139 C
ATOM 5060 O GLY C 59 6.191 40.962 10.841 1.00 52.66 O
ANISOU 5060 O GLY C 59 6393 6703 6911 321 1 -121 O
ATOM 5061 N PHE C 60 4.853 42.565 11.703 1.00 48.67 N
ANISOU 5061 N PHE C 60 5895 6127 6469 304 -38 -167 N
ATOM 5062 CA PHE C 60 5.344 42.418 13.072 1.00 46.60 C
ANISOU 5062 CA PHE C 60 5623 5866 6216 269 -15 -174 C
ATOM 5063 C PHE C 60 4.206 42.310 14.077 1.00 45.61 C
ANISOU 5063 C PHE C 60 5488 5714 6124 261 -13 -242 C
ATOM 5064 O PHE C 60 3.233 43.057 14.005 1.00 45.82 O
ANISOU 5064 O PHE C 60 5517 5708 6184 270 -37 -278 O
ATOM 5065 CB PHE C 60 6.250 43.593 13.461 1.00 45.49 C
ANISOU 5065 CB PHE C 60 5487 5714 6082 236 -26 -130 C
ATOM 5066 CG PHE C 60 7.466 43.735 12.597 1.00 46.20 C
ANISOU 5066 CG PHE C 60 5581 5833 6137 235 -24 -60 C
ATOM 5067 CD1 PHE C 60 7.419 44.487 11.418 1.00 46.37 C
ANISOU 5067 CD1 PHE C 60 5616 5850 6151 249 -51 -27 C
ATOM 5068 CD2 PHE C 60 8.662 43.124 12.954 1.00 46.08 C
ANISOU 5068 CD2 PHE C 60 5556 5853 6097 217 3 -26 C
ATOM 5069 CE1 PHE C 60 8.538 44.617 10.610 1.00 44.81 C
ANISOU 5069 CE1 PHE C 60 5421 5686 5917 244 -46 36 C
ATOM 5070 CE2 PHE C 60 9.786 43.248 12.147 1.00 46.28 C
ANISOU 5070 CE2 PHE C 60 5580 5910 6091 216 9 34 C
ATOM 5071 CZ PHE C 60 9.724 43.999 10.976 1.00 45.73 C
ANISOU 5071 CZ PHE C 60 5524 5839 6010 227 -13 65 C
ATOM 5072 N VAL C 61 4.332 41.361 14.997 1.00 43.59 N
ANISOU 5072 N VAL C 61 5223 5475 5861 243 15 -261 N
ATOM 5073 CA VAL C 61 3.514 41.350 16.194 1.00 42.96 C
ANISOU 5073 CA VAL C 61 5135 5379 5806 220 23 -318 C
ATOM 5074 C VAL C 61 4.250 42.194 17.225 1.00 42.19 C
ANISOU 5074 C VAL C 61 5039 5275 5715 178 25 -300 C
ATOM 5075 O VAL C 61 5.403 41.913 17.556 1.00 39.67 O
ANISOU 5075 O VAL C 61 4721 4977 5372 157 38 -255 O
ATOM 5076 CB VAL C 61 3.285 39.926 16.741 1.00 43.51 C
ANISOU 5076 CB VAL C 61 5196 5471 5863 215 50 -342 C
ATOM 5077 CG1 VAL C 61 2.680 39.978 18.134 1.00 42.87 C
ANISOU 5077 CG1 VAL C 61 5107 5381 5798 178 63 -391 C
ATOM 5078 CG2 VAL C 61 2.380 39.131 15.813 1.00 44.74 C
ANISOU 5078 CG2 VAL C 61 5350 5628 6019 255 46 -371 C
ATOM 5079 N HIS C 62 3.581 43.242 17.699 1.00 42.29 N
ANISOU 5079 N HIS C 62 5049 5255 5762 168 8 -338 N
ATOM 5080 CA HIS C 62 4.115 44.120 18.731 1.00 40.71 C
ANISOU 5080 CA HIS C 62 4850 5044 5573 128 7 -333 C
ATOM 5081 C HIS C 62 3.604 43.620 20.040 1.00 39.20 C
ANISOU 5081 C HIS C 62 4650 4862 5383 97 32 -386 C
ATOM 5082 O HIS C 62 2.403 43.487 20.224 1.00 40.01 O
ANISOU 5082 O HIS C 62 4741 4953 5506 106 34 -449 O
ATOM 5083 CB HIS C 62 3.669 45.564 18.500 1.00 41.50 C
ANISOU 5083 CB HIS C 62 4952 5100 5712 135 -26 -349 C
ATOM 5084 CG HIS C 62 4.042 46.114 17.139 1.00 43.55 C
ANISOU 5084 CG HIS C 62 5225 5351 5971 162 -56 -295 C
ATOM 5085 ND1 HIS C 62 5.303 46.482 16.822 1.00 45.04 N
ANISOU 5085 ND1 HIS C 62 5423 5550 6138 148 -60 -225 N
ATOM 5086 CD2 HIS C 62 3.267 46.354 16.002 1.00 44.63 C
ANISOU 5086 CD2 HIS C 62 5365 5468 6122 201 -83 -303 C
ATOM 5087 CE1 HIS C 62 5.337 46.933 15.551 1.00 45.12 C
ANISOU 5087 CE1 HIS C 62 5444 5552 6147 174 -87 -189 C
ATOM 5088 NE2 HIS C 62 4.091 46.852 15.049 1.00 46.72 N
ANISOU 5088 NE2 HIS C 62 5644 5735 6370 207 -103 -235 N
ATOM 5089 N VAL C 63 4.506 43.311 20.958 1.00 38.60 N
ANISOU 5089 N VAL C 63 4575 4807 5284 58 49 -361 N
ATOM 5090 CA VAL C 63 4.108 42.821 22.268 1.00 39.69 C
ANISOU 5090 CA VAL C 63 4706 4958 5415 21 73 -404 C
ATOM 5091 C VAL C 63 4.698 43.713 23.339 1.00 40.94 C
ANISOU 5091 C VAL C 63 4867 5110 5575 -22 71 -403 C
ATOM 5092 O VAL C 63 5.876 44.079 23.275 1.00 41.28 O
ANISOU 5092 O VAL C 63 4918 5156 5607 -34 62 -345 O
ATOM 5093 CB VAL C 63 4.546 41.359 22.502 1.00 39.65 C
ANISOU 5093 CB VAL C 63 4702 4986 5376 11 95 -379 C
ATOM 5094 CG1 VAL C 63 4.211 40.909 23.919 1.00 39.92 C
ANISOU 5094 CG1 VAL C 63 4732 5035 5398 -36 116 -416 C
ATOM 5095 CG2 VAL C 63 3.877 40.435 21.499 1.00 40.03 C
ANISOU 5095 CG2 VAL C 63 4746 5038 5423 53 97 -390 C
ATOM 5096 N GLU C 64 3.867 44.058 24.319 1.00 43.21 N
ANISOU 5096 N GLU C 64 5147 5392 5878 -47 80 -468 N
ATOM 5097 CA GLU C 64 4.262 44.929 25.416 1.00 44.50 C
ANISOU 5097 CA GLU C 64 5311 5550 6043 -91 78 -481 C
ATOM 5098 C GLU C 64 3.551 44.485 26.685 1.00 42.74 C
ANISOU 5098 C GLU C 64 5080 5349 5808 -130 106 -543 C
ATOM 5099 O GLU C 64 2.346 44.686 26.815 1.00 40.12 O
ANISOU 5099 O GLU C 64 4735 5008 5500 -122 112 -614 O
ATOM 5100 CB GLU C 64 3.925 46.386 25.082 1.00 49.07 C
ANISOU 5100 CB GLU C 64 5888 6087 6668 -73 49 -506 C
ATOM 5101 CG GLU C 64 4.560 47.422 26.004 1.00 55.99 C
ANISOU 5101 CG GLU C 64 6768 6952 7551 -113 40 -508 C
ATOM 5102 CD GLU C 64 4.715 48.798 25.359 1.00 61.64 C
ANISOU 5102 CD GLU C 64 7488 7622 8309 -92 2 -496 C
ATOM 5103 OE1 GLU C 64 4.157 49.037 24.260 1.00 61.63 O
ANISOU 5103 OE1 GLU C 64 7484 7595 8334 -48 -18 -496 O
ATOM 5104 OE2 GLU C 64 5.411 49.649 25.957 1.00 65.69 O
ANISOU 5104 OE2 GLU C 64 8006 8123 8829 -122 -10 -485 O
ATOM 5105 N PHE C 65 4.299 43.866 27.600 1.00 41.98 N
ANISOU 5105 N PHE C 65 4992 5283 5673 -175 122 -515 N
ATOM 5106 CA PHE C 65 3.769 43.449 28.898 1.00 43.13 C
ANISOU 5106 CA PHE C 65 5134 5456 5797 -224 147 -564 C
ATOM 5107 C PHE C 65 4.856 43.112 29.907 1.00 43.63 C
ANISOU 5107 C PHE C 65 5211 5546 5821 -277 153 -521 C
ATOM 5108 O PHE C 65 6.039 43.246 29.619 1.00 43.99 O
ANISOU 5108 O PHE C 65 5266 5588 5860 -275 136 -455 O
ATOM 5109 CB PHE C 65 2.793 42.266 28.746 1.00 45.60 C
ANISOU 5109 CB PHE C 65 5438 5786 6102 -214 168 -593 C
ATOM 5110 CG PHE C 65 3.459 40.917 28.604 1.00 44.53 C
ANISOU 5110 CG PHE C 65 5312 5672 5932 -219 173 -532 C
ATOM 5111 CD1 PHE C 65 3.145 39.891 29.482 1.00 43.10 C
ANISOU 5111 CD1 PHE C 65 5131 5521 5721 -260 194 -545 C
ATOM 5112 CD2 PHE C 65 4.385 40.670 27.586 1.00 44.38 C
ANISOU 5112 CD2 PHE C 65 5301 5646 5915 -183 156 -464 C
ATOM 5113 CE1 PHE C 65 3.743 38.648 29.359 1.00 44.06 C
ANISOU 5113 CE1 PHE C 65 5262 5657 5820 -264 193 -490 C
ATOM 5114 CE2 PHE C 65 4.993 39.434 27.463 1.00 44.05 C
ANISOU 5114 CE2 PHE C 65 5264 5622 5849 -184 159 -415 C
ATOM 5115 CZ PHE C 65 4.669 38.420 28.353 1.00 45.69 C
ANISOU 5115 CZ PHE C 65 5473 5852 6032 -224 175 -428 C
ATOM 5116 N ILE C 66 4.426 42.659 31.084 1.00 45.85 N
ANISOU 5116 N ILE C 66 5491 5856 6074 -327 175 -558 N
ATOM 5117 CA ILE C 66 5.305 42.302 32.196 1.00 46.45 C
ANISOU 5117 CA ILE C 66 5581 5960 6108 -386 179 -524 C
ATOM 5118 C ILE C 66 4.916 40.890 32.650 1.00 47.08 C
ANISOU 5118 C ILE C 66 5662 6071 6154 -412 199 -522 C
ATOM 5119 O ILE C 66 3.916 40.709 33.340 1.00 49.05 O
ANISOU 5119 O ILE C 66 5903 6339 6391 -441 222 -583 O
ATOM 5120 CB ILE C 66 5.173 43.315 33.366 1.00 45.85 C
ANISOU 5120 CB ILE C 66 5504 5890 6026 -433 185 -577 C
ATOM 5121 CG1 ILE C 66 5.603 44.715 32.922 1.00 45.76 C
ANISOU 5121 CG1 ILE C 66 5491 5842 6052 -408 160 -576 C
ATOM 5122 CG2 ILE C 66 5.969 42.869 34.585 1.00 45.14 C
ANISOU 5122 CG2 ILE C 66 5429 5834 5886 -499 189 -545 C
ATOM 5123 CD1 ILE C 66 4.855 45.837 33.610 1.00 46.48 C
ANISOU 5123 CD1 ILE C 66 5572 5924 6164 -426 165 -660 C
ATOM 5124 N PRO C 67 5.697 39.879 32.242 1.00 48.32 N
ANISOU 5124 N PRO C 67 5828 6232 6298 -402 189 -453 N
ATOM 5125 CA PRO C 67 5.361 38.483 32.502 1.00 47.85 C
ANISOU 5125 CA PRO C 67 5771 6194 6215 -420 200 -443 C
ATOM 5126 C PRO C 67 5.195 38.121 33.972 1.00 47.78 C
ANISOU 5126 C PRO C 67 5771 6219 6164 -495 214 -460 C
ATOM 5127 O PRO C 67 5.978 38.555 34.816 1.00 46.30 O
ANISOU 5127 O PRO C 67 5594 6043 5954 -538 207 -440 O
ATOM 5128 CB PRO C 67 6.541 37.714 31.892 1.00 47.54 C
ANISOU 5128 CB PRO C 67 5739 6150 6174 -398 179 -361 C
ATOM 5129 CG PRO C 67 7.614 38.728 31.665 1.00 48.07 C
ANISOU 5129 CG PRO C 67 5809 6203 6252 -387 161 -326 C
ATOM 5130 CD PRO C 67 6.872 39.990 31.363 1.00 49.15 C
ANISOU 5130 CD PRO C 67 5937 6320 6415 -366 165 -383 C
ATOM 5131 N ARG C 68 4.171 37.312 34.240 1.00 48.46 N
ANISOU 5131 N ARG C 68 5851 6322 6237 -513 234 -496 N
ATOM 5132 CA ARG C 68 3.875 36.791 35.570 1.00 48.65 C
ANISOU 5132 CA ARG C 68 5883 6383 6216 -588 250 -510 C
ATOM 5133 C ARG C 68 4.771 35.604 35.940 1.00 46.96 C
ANISOU 5133 C ARG C 68 5689 6180 5974 -619 232 -434 C
ATOM 5134 O ARG C 68 4.649 35.042 37.032 1.00 48.35 O
ANISOU 5134 O ARG C 68 5875 6385 6108 -685 239 -431 O
ATOM 5135 CB ARG C 68 2.390 36.400 35.678 1.00 52.04 C
ANISOU 5135 CB ARG C 68 6297 6828 6647 -596 280 -579 C
ATOM 5136 CG ARG C 68 1.399 37.547 35.489 1.00 54.43 C
ANISOU 5136 CG ARG C 68 6578 7123 6980 -573 298 -664 C
ATOM 5137 CD ARG C 68 1.517 38.587 36.590 1.00 59.28 C
ANISOU 5137 CD ARG C 68 7193 7757 7573 -622 309 -705 C
ATOM 5138 NE ARG C 68 1.236 39.933 36.090 1.00 66.87 N
ANISOU 5138 NE ARG C 68 8139 8689 8579 -578 305 -755 N
ATOM 5139 CZ ARG C 68 0.419 40.816 36.670 1.00 69.58 C
ANISOU 5139 CZ ARG C 68 8464 9042 8930 -595 326 -841 C
ATOM 5140 NH1 ARG C 68 -0.214 40.523 37.805 1.00 69.23 N
ANISOU 5140 NH1 ARG C 68 8415 9043 8846 -659 357 -889 N
ATOM 5141 NH2 ARG C 68 0.249 42.011 36.115 1.00 67.90 N
ANISOU 5141 NH2 ARG C 68 8237 8793 8765 -550 313 -879 N
ATOM 5142 N GLY C 69 5.665 35.234 35.024 1.00 43.62 N
ANISOU 5142 N GLY C 69 5267 5731 5573 -571 207 -372 N
ATOM 5143 CA GLY C 69 6.671 34.197 35.265 1.00 41.80 C
ANISOU 5143 CA GLY C 69 5051 5503 5327 -590 182 -297 C
ATOM 5144 C GLY C 69 7.791 34.278 34.244 1.00 40.98 C
ANISOU 5144 C GLY C 69 4943 5373 5253 -533 158 -242 C
ATOM 5145 O GLY C 69 7.692 35.025 33.270 1.00 40.91 O
ANISOU 5145 O GLY C 69 4923 5346 5274 -479 161 -260 O
ATOM 5146 N ASN C 70 8.860 33.516 34.459 1.00 40.51 N
ANISOU 5146 N ASN C 70 4892 5313 5186 -546 132 -176 N
ATOM 5147 CA ASN C 70 9.952 33.440 33.487 1.00 39.39 C
ANISOU 5147 CA ASN C 70 4741 5151 5072 -493 112 -124 C
ATOM 5148 C ASN C 70 9.490 32.940 32.137 1.00 39.26 C
ANISOU 5148 C ASN C 70 4711 5117 5086 -425 117 -135 C
ATOM 5149 O ASN C 70 8.653 32.042 32.056 1.00 40.59 O
ANISOU 5149 O ASN C 70 4881 5285 5256 -423 123 -155 O
ATOM 5150 CB ASN C 70 11.041 32.522 33.995 1.00 39.38 C
ANISOU 5150 CB ASN C 70 4748 5152 5062 -520 82 -57 C
ATOM 5151 CG ASN C 70 11.625 33.000 35.289 1.00 40.33 C
ANISOU 5151 CG ASN C 70 4883 5291 5150 -588 72 -39 C
ATOM 5152 OD1 ASN C 70 11.741 34.206 35.529 1.00 40.36 O
ANISOU 5152 OD1 ASN C 70 4887 5300 5148 -598 80 -61 O
ATOM 5153 ND2 ASN C 70 11.996 32.060 36.142 1.00 42.35 N
ANISOU 5153 ND2 ASN C 70 5151 5555 5384 -636 50 0 N
ATOM 5154 N LEU C 71 10.046 33.515 31.078 1.00 37.19 N
ANISOU 5154 N LEU C 71 4438 4841 4849 -370 113 -120 N
ATOM 5155 CA LEU C 71 9.618 33.180 29.732 1.00 35.74 C
ANISOU 5155 CA LEU C 71 4243 4644 4691 -304 118 -133 C
ATOM 5156 C LEU C 71 10.481 32.113 29.059 1.00 36.15 C
ANISOU 5156 C LEU C 71 4288 4690 4758 -270 100 -84 C
ATOM 5157 O LEU C 71 10.418 31.937 27.838 1.00 36.83 O
ANISOU 5157 O LEU C 71 4362 4766 4862 -212 103 -88 O
ATOM 5158 CB LEU C 71 9.552 34.442 28.882 1.00 35.45 C
ANISOU 5158 CB LEU C 71 4199 4598 4671 -265 125 -152 C
ATOM 5159 CG LEU C 71 8.164 35.044 28.632 1.00 35.90 C
ANISOU 5159 CG LEU C 71 4254 4649 4737 -252 143 -219 C
ATOM 5160 CD1 LEU C 71 7.170 34.764 29.753 1.00 35.73 C
ANISOU 5160 CD1 LEU C 71 4237 4639 4697 -304 158 -264 C
ATOM 5161 CD2 LEU C 71 8.279 36.536 28.353 1.00 36.02 C
ANISOU 5161 CD2 LEU C 71 4267 4653 4764 -240 142 -232 C
ATOM 5162 N LYS C 72 11.261 31.391 29.861 1.00 34.84 N
ANISOU 5162 N LYS C 72 4126 4528 4582 -307 81 -41 N
ATOM 5163 CA LYS C 72 12.261 30.465 29.349 1.00 35.23 C
ANISOU 5163 CA LYS C 72 4165 4570 4650 -277 60 6 C
ATOM 5164 C LYS C 72 11.652 29.299 28.558 1.00 36.23 C
ANISOU 5164 C LYS C 72 4286 4684 4795 -236 60 -9 C
ATOM 5165 O LYS C 72 12.248 28.813 27.607 1.00 38.20 O
ANISOU 5165 O LYS C 72 4521 4927 5066 -186 52 8 O
ATOM 5166 CB LYS C 72 13.109 29.952 30.508 1.00 35.04 C
ANISOU 5166 CB LYS C 72 4149 4549 4613 -331 34 52 C
ATOM 5167 CG LYS C 72 14.452 29.346 30.138 1.00 34.37 C
ANISOU 5167 CG LYS C 72 4048 4457 4552 -305 9 106 C
ATOM 5168 CD LYS C 72 15.255 29.093 31.407 1.00 34.97 C
ANISOU 5168 CD LYS C 72 4135 4537 4615 -365 -19 151 C
ATOM 5169 CE LYS C 72 16.698 28.677 31.138 1.00 35.16 C
ANISOU 5169 CE LYS C 72 4138 4554 4665 -343 -47 204 C
ATOM 5170 NZ LYS C 72 16.924 27.213 31.248 1.00 34.70 N
ANISOU 5170 NZ LYS C 72 4076 4478 4628 -339 -78 229 N
ATOM 5171 N TYR C 73 10.460 28.873 28.951 1.00 36.95 N
ANISOU 5171 N TYR C 73 4387 4774 4877 -259 69 -46 N
ATOM 5172 CA TYR C 73 9.788 27.724 28.356 1.00 35.91 C
ANISOU 5172 CA TYR C 73 4251 4629 4762 -229 66 -63 C
ATOM 5173 C TYR C 73 8.376 28.128 27.912 1.00 36.03 C
ANISOU 5173 C TYR C 73 4266 4645 4776 -214 92 -125 C
ATOM 5174 O TYR C 73 7.415 27.358 28.031 1.00 37.25 O
ANISOU 5174 O TYR C 73 4424 4796 4934 -223 94 -151 O
ATOM 5175 CB TYR C 73 9.714 26.575 29.376 1.00 36.77 C
ANISOU 5175 CB TYR C 73 4372 4734 4864 -281 46 -41 C
ATOM 5176 CG TYR C 73 11.051 26.048 29.837 1.00 37.51 C
ANISOU 5176 CG TYR C 73 4465 4821 4964 -297 13 19 C
ATOM 5177 CD1 TYR C 73 11.728 26.640 30.906 1.00 37.20 C
ANISOU 5177 CD1 TYR C 73 4436 4795 4901 -351 5 49 C
ATOM 5178 CD2 TYR C 73 11.645 24.950 29.203 1.00 38.23 C
ANISOU 5178 CD2 TYR C 73 4544 4892 5088 -256 -10 45 C
ATOM 5179 CE1 TYR C 73 12.959 26.160 31.321 1.00 37.70 C
ANISOU 5179 CE1 TYR C 73 4497 4852 4974 -364 -28 106 C
ATOM 5180 CE2 TYR C 73 12.874 24.461 29.616 1.00 37.35 C
ANISOU 5180 CE2 TYR C 73 4427 4772 4988 -268 -43 99 C
ATOM 5181 CZ TYR C 73 13.523 25.071 30.670 1.00 38.30 C
ANISOU 5181 CZ TYR C 73 4559 4907 5087 -322 -53 130 C
ATOM 5182 OH TYR C 73 14.744 24.591 31.073 1.00 40.83 O
ANISOU 5182 OH TYR C 73 4872 5217 5422 -332 -89 184 O
ATOM 5183 N LEU C 74 8.244 29.347 27.411 1.00 35.66 N
ANISOU 5183 N LEU C 74 4214 4603 4729 -190 108 -147 N
ATOM 5184 CA LEU C 74 6.958 29.818 26.928 1.00 37.10 C
ANISOU 5184 CA LEU C 74 4394 4783 4917 -170 127 -206 C
ATOM 5185 C LEU C 74 6.386 28.935 25.804 1.00 38.68 C
ANISOU 5185 C LEU C 74 4587 4972 5138 -117 125 -224 C
ATOM 5186 O LEU C 74 7.104 28.561 24.865 1.00 37.92 O
ANISOU 5186 O LEU C 74 4483 4869 5054 -70 114 -199 O
ATOM 5187 CB LEU C 74 7.054 31.276 26.465 1.00 36.60 C
ANISOU 5187 CB LEU C 74 4328 4722 4857 -149 136 -219 C
ATOM 5188 CG LEU C 74 5.771 31.860 25.858 1.00 36.35 C
ANISOU 5188 CG LEU C 74 4291 4682 4837 -122 150 -278 C
ATOM 5189 CD1 LEU C 74 4.629 31.847 26.860 1.00 35.61 C
ANISOU 5189 CD1 LEU C 74 4199 4596 4734 -169 165 -327 C
ATOM 5190 CD2 LEU C 74 6.004 33.263 25.329 1.00 37.40 C
ANISOU 5190 CD2 LEU C 74 4421 4810 4976 -99 151 -281 C
ATOM 5191 N TYR C 75 5.101 28.591 25.940 1.00 38.95 N
ANISOU 5191 N TYR C 75 4621 5003 5175 -127 135 -270 N
ATOM 5192 CA TYR C 75 4.302 28.029 24.852 1.00 38.78 C
ANISOU 5192 CA TYR C 75 4591 4970 5173 -77 135 -302 C
ATOM 5193 C TYR C 75 2.827 28.449 24.927 1.00 39.52 C
ANISOU 5193 C TYR C 75 4680 5065 5270 -84 153 -365 C
ATOM 5194 O TYR C 75 2.356 28.926 25.958 1.00 39.72 O
ANISOU 5194 O TYR C 75 4708 5101 5282 -135 167 -386 O
ATOM 5195 CB TYR C 75 4.453 26.505 24.767 1.00 41.01 C
ANISOU 5195 CB TYR C 75 4874 5241 5466 -73 118 -282 C
ATOM 5196 CG TYR C 75 3.776 25.670 25.848 1.00 42.48 C
ANISOU 5196 CG TYR C 75 5066 5427 5645 -131 117 -289 C
ATOM 5197 CD1 TYR C 75 4.515 25.144 26.907 1.00 42.82 C
ANISOU 5197 CD1 TYR C 75 5120 5472 5674 -183 102 -244 C
ATOM 5198 CD2 TYR C 75 2.406 25.351 25.774 1.00 43.05 C
ANISOU 5198 CD2 TYR C 75 5135 5498 5725 -136 128 -339 C
ATOM 5199 CE1 TYR C 75 3.916 24.359 27.877 1.00 44.09 C
ANISOU 5199 CE1 TYR C 75 5289 5635 5825 -241 99 -245 C
ATOM 5200 CE2 TYR C 75 1.794 24.562 26.739 1.00 42.63 C
ANISOU 5200 CE2 TYR C 75 5087 5447 5663 -193 128 -343 C
ATOM 5201 CZ TYR C 75 2.555 24.067 27.785 1.00 45.26 C
ANISOU 5201 CZ TYR C 75 5433 5784 5978 -247 114 -295 C
ATOM 5202 OH TYR C 75 1.974 23.284 28.757 1.00 48.08 O
ANISOU 5202 OH TYR C 75 5798 6146 6324 -310 112 -293 O
ATOM 5203 N PHE C 76 2.113 28.269 23.820 1.00 40.12 N
ANISOU 5203 N PHE C 76 4748 5130 5365 -33 152 -396 N
ATOM 5204 CA PHE C 76 0.693 28.575 23.747 1.00 39.34 C
ANISOU 5204 CA PHE C 76 4640 5029 5277 -33 165 -457 C
ATOM 5205 C PHE C 76 -0.179 27.345 23.565 1.00 41.16 C
ANISOU 5205 C PHE C 76 4866 5252 5520 -30 161 -480 C
ATOM 5206 O PHE C 76 0.175 26.411 22.837 1.00 42.92 O
ANISOU 5206 O PHE C 76 5090 5464 5752 3 146 -460 O
ATOM 5207 CB PHE C 76 0.422 29.520 22.591 1.00 38.80 C
ANISOU 5207 CB PHE C 76 4566 4953 5223 22 162 -479 C
ATOM 5208 CG PHE C 76 0.762 30.938 22.886 1.00 39.76 C
ANISOU 5208 CG PHE C 76 4690 5078 5340 12 167 -478 C
ATOM 5209 CD1 PHE C 76 1.972 31.474 22.465 1.00 38.92 C
ANISOU 5209 CD1 PHE C 76 4589 4972 5225 30 158 -430 C
ATOM 5210 CD2 PHE C 76 -0.130 31.746 23.585 1.00 39.82 C
ANISOU 5210 CD2 PHE C 76 4690 5087 5352 -16 181 -526 C
ATOM 5211 CE1 PHE C 76 2.284 32.789 22.740 1.00 39.08 C
ANISOU 5211 CE1 PHE C 76 4611 4991 5243 19 159 -428 C
ATOM 5212 CE2 PHE C 76 0.182 33.064 23.863 1.00 39.20 C
ANISOU 5212 CE2 PHE C 76 4612 5007 5273 -25 182 -528 C
ATOM 5213 CZ PHE C 76 1.391 33.583 23.441 1.00 39.52 C
ANISOU 5213 CZ PHE C 76 4662 5046 5307 -7 170 -477 C
ATOM 5214 N ASN C 77 -1.322 27.354 24.239 1.00 41.11 N
ANISOU 5214 N ASN C 77 4852 5252 5514 -67 177 -525 N
ATOM 5215 CA ASN C 77 -2.405 26.454 23.912 1.00 41.44 C
ANISOU 5215 CA ASN C 77 4884 5286 5573 -59 176 -560 C
ATOM 5216 C ASN C 77 -3.452 27.288 23.193 1.00 43.25 C
ANISOU 5216 C ASN C 77 5098 5511 5822 -22 183 -618 C
ATOM 5217 O ASN C 77 -4.105 28.130 23.806 1.00 45.84 O
ANISOU 5217 O ASN C 77 5416 5850 6150 -49 200 -657 O
ATOM 5218 CB ASN C 77 -3.008 25.824 25.171 1.00 40.93 C
ANISOU 5218 CB ASN C 77 4819 5236 5496 -131 189 -571 C
ATOM 5219 CG ASN C 77 -2.083 24.817 25.839 1.00 41.38 C
ANISOU 5219 CG ASN C 77 4892 5291 5537 -168 173 -512 C
ATOM 5220 OD1 ASN C 77 -1.355 24.072 25.178 1.00 40.66 O
ANISOU 5220 OD1 ASN C 77 4807 5182 5457 -133 150 -476 O
ATOM 5221 ND2 ASN C 77 -2.121 24.783 27.171 1.00 41.31 N
ANISOU 5221 ND2 ASN C 77 4890 5303 5503 -242 185 -504 N
ATOM 5222 N LEU C 78 -3.577 27.087 21.887 1.00 43.53 N
ANISOU 5222 N LEU C 78 5131 5532 5876 39 167 -624 N
ATOM 5223 CA LEU C 78 -4.650 27.700 21.124 1.00 45.05 C
ANISOU 5223 CA LEU C 78 5309 5716 6090 76 166 -677 C
ATOM 5224 C LEU C 78 -5.857 26.766 21.093 1.00 46.06 C
ANISOU 5224 C LEU C 78 5423 5840 6236 69 167 -719 C
ATOM 5225 O LEU C 78 -5.722 25.573 20.789 1.00 48.58 O
ANISOU 5225 O LEU C 78 5748 6151 6558 77 155 -701 O
ATOM 5226 CB LEU C 78 -4.205 28.013 19.694 1.00 43.98 C
ANISOU 5226 CB LEU C 78 5179 5569 5960 144 146 -661 C
ATOM 5227 CG LEU C 78 -2.876 28.720 19.433 1.00 43.13 C
ANISOU 5227 CG LEU C 78 5086 5466 5836 159 141 -611 C
ATOM 5228 CD1 LEU C 78 -2.728 28.949 17.939 1.00 42.60 C
ANISOU 5228 CD1 LEU C 78 5021 5391 5772 223 124 -606 C
ATOM 5229 CD2 LEU C 78 -2.756 30.039 20.178 1.00 42.85 C
ANISOU 5229 CD2 LEU C 78 5049 5435 5796 130 152 -615 C
ATOM 5230 N PHE C 79 -7.025 27.310 21.430 1.00 45.49 N
ANISOU 5230 N PHE C 79 5332 5772 6180 53 181 -776 N
ATOM 5231 CA PHE C 79 -8.293 26.595 21.309 1.00 45.54 C
ANISOU 5231 CA PHE C 79 5320 5775 6208 50 183 -823 C
ATOM 5232 C PHE C 79 -9.105 27.330 20.265 1.00 45.18 C
ANISOU 5232 C PHE C 79 5259 5715 6190 105 170 -868 C
ATOM 5233 O PHE C 79 -9.637 28.407 20.527 1.00 45.27 O
ANISOU 5233 O PHE C 79 5255 5729 6214 101 180 -907 O
ATOM 5234 CB PHE C 79 -9.046 26.543 22.638 1.00 44.53 C
ANISOU 5234 CB PHE C 79 5177 5668 6074 -19 211 -856 C
ATOM 5235 CG PHE C 79 -8.260 25.929 23.760 1.00 45.86 C
ANISOU 5235 CG PHE C 79 5362 5851 6210 -81 221 -809 C
ATOM 5236 CD1 PHE C 79 -7.396 26.706 24.534 1.00 45.56 C
ANISOU 5236 CD1 PHE C 79 5336 5828 6146 -110 231 -782 C
ATOM 5237 CD2 PHE C 79 -8.382 24.576 24.050 1.00 46.75 C
ANISOU 5237 CD2 PHE C 79 5479 5963 6319 -111 215 -790 C
ATOM 5238 CE1 PHE C 79 -6.668 26.147 25.572 1.00 44.68 C
ANISOU 5238 CE1 PHE C 79 5241 5730 6004 -168 236 -737 C
ATOM 5239 CE2 PHE C 79 -7.659 24.010 25.090 1.00 48.41 C
ANISOU 5239 CE2 PHE C 79 5707 6185 6501 -170 218 -742 C
ATOM 5240 CZ PHE C 79 -6.802 24.799 25.853 1.00 47.60 C
ANISOU 5240 CZ PHE C 79 5617 6099 6371 -198 228 -716 C
ATOM 5241 N ILE C 80 -9.171 26.744 19.074 1.00 45.39 N
ANISOU 5241 N ILE C 80 5291 5727 6229 156 147 -863 N
ATOM 5242 CA ILE C 80 -9.735 27.410 17.914 1.00 45.50 C
ANISOU 5242 CA ILE C 80 5296 5725 6264 214 127 -893 C
ATOM 5243 C ILE C 80 -11.116 26.854 17.585 1.00 48.58 C
ANISOU 5243 C ILE C 80 5663 6107 6684 222 121 -949 C
ATOM 5244 O ILE C 80 -11.394 25.663 17.754 1.00 48.15 O
ANISOU 5244 O ILE C 80 5608 6054 6632 204 122 -950 O
ATOM 5245 CB ILE C 80 -8.787 27.341 16.694 1.00 44.93 C
ANISOU 5245 CB ILE C 80 5246 5646 6178 268 103 -850 C
ATOM 5246 CG1 ILE C 80 -7.373 27.785 17.103 1.00 44.49 C
ANISOU 5246 CG1 ILE C 80 5210 5601 6094 254 111 -792 C
ATOM 5247 CG2 ILE C 80 -9.325 28.187 15.545 1.00 44.45 C
ANISOU 5247 CG2 ILE C 80 5180 5572 6134 321 81 -874 C
ATOM 5248 CD1 ILE C 80 -6.329 27.713 16.012 1.00 42.75 C
ANISOU 5248 CD1 ILE C 80 5007 5379 5855 300 94 -748 C
ATOM 5249 N SER C 81 -11.977 27.752 17.126 1.00 51.92 N
ANISOU 5249 N SER C 81 6069 6522 7135 250 111 -994 N
ATOM 5250 CA SER C 81 -13.359 27.459 16.811 1.00 51.11 C
ANISOU 5250 CA SER C 81 5940 6411 7067 260 104 -1054 C
ATOM 5251 C SER C 81 -13.684 28.146 15.490 1.00 50.08 C
ANISOU 5251 C SER C 81 5810 6262 6957 325 70 -1068 C
ATOM 5252 O SER C 81 -13.320 29.302 15.272 1.00 48.01 O
ANISOU 5252 O SER C 81 5553 5993 6693 344 61 -1058 O
ATOM 5253 CB SER C 81 -14.250 27.972 17.939 1.00 51.44 C
ANISOU 5253 CB SER C 81 5950 6465 7127 213 132 -1106 C
ATOM 5254 OG SER C 81 -15.578 28.182 17.510 1.00 57.20 O
ANISOU 5254 OG SER C 81 6649 7186 7899 235 121 -1170 O
ATOM 5255 N VAL C 82 -14.321 27.407 14.591 1.00 52.13 N
ANISOU 5255 N VAL C 82 6064 6511 7231 357 48 -1087 N
ATOM 5256 CA VAL C 82 -14.752 27.953 13.307 1.00 56.09 C
ANISOU 5256 CA VAL C 82 6566 6995 7750 415 11 -1103 C
ATOM 5257 C VAL C 82 -16.254 27.706 13.224 1.00 59.33 C
ANISOU 5257 C VAL C 82 6942 7397 8204 418 3 -1170 C
ATOM 5258 O VAL C 82 -16.703 26.560 13.127 1.00 62.69 O
ANISOU 5258 O VAL C 82 7360 7822 8634 411 2 -1183 O
ATOM 5259 CB VAL C 82 -14.011 27.322 12.095 1.00 54.73 C
ANISOU 5259 CB VAL C 82 6422 6820 7550 459 -12 -1062 C
ATOM 5260 CG1 VAL C 82 -14.443 27.980 10.798 1.00 55.69 C
ANISOU 5260 CG1 VAL C 82 6547 6928 7683 514 -51 -1075 C
ATOM 5261 CG2 VAL C 82 -12.503 27.447 12.234 1.00 52.77 C
ANISOU 5261 CG2 VAL C 82 6203 6585 7261 453 0 -998 C
ATOM 5262 N ASN C 83 -17.022 28.792 13.295 1.00 60.56 N
ANISOU 5262 N ASN C 83 7073 7542 8393 426 -4 -1213 N
ATOM 5263 CA ASN C 83 -18.483 28.731 13.320 1.00 60.83 C
ANISOU 5263 CA ASN C 83 7067 7569 8475 427 -10 -1283 C
ATOM 5264 C ASN C 83 -18.973 27.701 14.344 1.00 62.53 C
ANISOU 5264 C ASN C 83 7261 7802 8692 371 24 -1306 C
ATOM 5265 O ASN C 83 -19.780 26.818 14.041 1.00 63.38 O
ANISOU 5265 O ASN C 83 7353 7907 8819 373 16 -1335 O
ATOM 5266 CB ASN C 83 -19.034 28.501 11.908 1.00 60.12 C
ANISOU 5266 CB ASN C 83 6980 7460 8402 483 -56 -1294 C
ATOM 5267 CG ASN C 83 -18.452 29.480 10.895 1.00 62.76 C
ANISOU 5267 CG ASN C 83 7340 7778 8725 531 -92 -1261 C
ATOM 5268 OD1 ASN C 83 -18.438 30.690 11.121 1.00 64.22 O
ANISOU 5268 OD1 ASN C 83 7518 7954 8926 535 -97 -1267 O
ATOM 5269 ND2 ASN C 83 -17.957 28.959 9.783 1.00 62.48 N
ANISOU 5269 ND2 ASN C 83 7334 7742 8661 567 -118 -1225 N
ATOM 5270 N SER C 84 -18.445 27.847 15.561 1.00 62.85 N
ANISOU 5270 N SER C 84 7304 7864 8712 319 63 -1292 N
ATOM 5271 CA SER C 84 -18.679 26.954 16.704 1.00 64.50 C
ANISOU 5271 CA SER C 84 7499 8095 8910 254 100 -1301 C
ATOM 5272 C SER C 84 -18.097 25.538 16.583 1.00 63.49 C
ANISOU 5272 C SER C 84 7398 7970 8755 241 98 -1253 C
ATOM 5273 O SER C 84 -18.107 24.786 17.562 1.00 67.34 O
ANISOU 5273 O SER C 84 7882 8474 9229 183 125 -1247 O
ATOM 5274 CB SER C 84 -20.156 26.915 17.117 1.00 66.45 C
ANISOU 5274 CB SER C 84 7697 8349 9200 232 113 -1377 C
ATOM 5275 OG SER C 84 -20.315 26.165 18.316 1.00 69.24 O
ANISOU 5275 OG SER C 84 8040 8731 9537 160 153 -1380 O
ATOM 5276 N ILE C 85 -17.583 25.173 15.411 1.00 60.97 N
ANISOU 5276 N ILE C 85 7104 7632 8426 293 65 -1221 N
ATOM 5277 CA ILE C 85 -16.904 23.880 15.255 1.00 61.31 C
ANISOU 5277 CA ILE C 85 7174 7674 8447 286 60 -1177 C
ATOM 5278 C ILE C 85 -15.474 24.017 15.777 1.00 58.19 C
ANISOU 5278 C ILE C 85 6809 7289 8011 268 75 -1115 C
ATOM 5279 O ILE C 85 -14.666 24.723 15.181 1.00 61.16 O
ANISOU 5279 O ILE C 85 7205 7662 8371 305 63 -1085 O
ATOM 5280 CB ILE C 85 -16.878 23.390 13.780 1.00 61.39 C
ANISOU 5280 CB ILE C 85 7197 7664 8461 349 20 -1172 C
ATOM 5281 CG1 ILE C 85 -18.239 23.575 13.080 1.00 62.66 C
ANISOU 5281 CG1 ILE C 85 7330 7813 8663 379 -2 -1233 C
ATOM 5282 CG2 ILE C 85 -16.400 21.948 13.701 1.00 58.73 C
ANISOU 5282 CG2 ILE C 85 6878 7323 8111 340 15 -1142 C
ATOM 5283 CD1 ILE C 85 -19.405 22.810 13.691 1.00 64.13 C
ANISOU 5283 CD1 ILE C 85 7483 8003 8881 338 10 -1279 C
ATOM 5284 N GLU C 86 -15.157 23.362 16.890 1.00 56.75 N
ANISOU 5284 N GLU C 86 6629 7119 7812 209 99 -1093 N
ATOM 5285 CA GLU C 86 -13.826 23.536 17.472 1.00 58.53 C
ANISOU 5285 CA GLU C 86 6882 7355 8001 188 111 -1035 C
ATOM 5286 C GLU C 86 -12.769 22.536 16.998 1.00 57.64 C
ANISOU 5286 C GLU C 86 6797 7232 7871 206 94 -981 C
ATOM 5287 O GLU C 86 -13.007 21.328 16.932 1.00 59.77 O
ANISOU 5287 O GLU C 86 7066 7491 8149 197 83 -980 O
ATOM 5288 CB GLU C 86 -13.848 23.691 19.008 1.00 64.74 C
ANISOU 5288 CB GLU C 86 7659 8164 8772 113 147 -1035 C
ATOM 5289 CG GLU C 86 -14.575 22.625 19.823 1.00 70.42 C
ANISOU 5289 CG GLU C 86 8364 8892 9497 54 161 -1050 C
ATOM 5290 CD GLU C 86 -14.936 23.113 21.232 1.00 73.01 C
ANISOU 5290 CD GLU C 86 8676 9251 9812 -16 199 -1071 C
ATOM 5291 OE1 GLU C 86 -14.809 22.336 22.209 1.00 70.88 O
ANISOU 5291 OE1 GLU C 86 8411 8995 9522 -80 214 -1047 O
ATOM 5292 OE2 GLU C 86 -15.351 24.284 21.369 1.00 72.85 O
ANISOU 5292 OE2 GLU C 86 8637 9240 9802 -8 213 -1112 O
ATOM 5293 N LEU C 87 -11.605 23.075 16.644 1.00 52.86 N
ANISOU 5293 N LEU C 87 6213 6627 7241 234 89 -939 N
ATOM 5294 CA LEU C 87 -10.455 22.285 16.233 1.00 49.53 C
ANISOU 5294 CA LEU C 87 5815 6200 6803 253 75 -889 C
ATOM 5295 C LEU C 87 -9.835 21.667 17.482 1.00 49.20 C
ANISOU 5295 C LEU C 87 5782 6165 6746 192 89 -851 C
ATOM 5296 O LEU C 87 -10.130 22.109 18.589 1.00 51.28 O
ANISOU 5296 O LEU C 87 6036 6442 7003 139 113 -859 O
ATOM 5297 CB LEU C 87 -9.438 23.176 15.509 1.00 47.54 C
ANISOU 5297 CB LEU C 87 5579 5952 6529 297 68 -858 C
ATOM 5298 CG LEU C 87 -9.723 23.652 14.077 1.00 48.99 C
ANISOU 5298 CG LEU C 87 5763 6129 6718 361 46 -877 C
ATOM 5299 CD1 LEU C 87 -10.952 24.547 13.995 1.00 52.04 C
ANISOU 5299 CD1 LEU C 87 6130 6513 7129 366 44 -929 C
ATOM 5300 CD2 LEU C 87 -8.528 24.394 13.504 1.00 49.10 C
ANISOU 5300 CD2 LEU C 87 5797 6153 6706 392 43 -834 C
ATOM 5301 N PRO C 88 -8.982 20.635 17.323 1.00 49.63 N
ANISOU 5301 N PRO C 88 5852 6208 6796 199 74 -812 N
ATOM 5302 CA PRO C 88 -8.272 20.126 18.501 1.00 48.43 C
ANISOU 5302 CA PRO C 88 5711 6061 6630 141 82 -768 C
ATOM 5303 C PRO C 88 -7.333 21.169 19.111 1.00 47.07 C
ANISOU 5303 C PRO C 88 5548 5907 6430 124 99 -735 C
ATOM 5304 O PRO C 88 -6.894 22.093 18.417 1.00 45.75 O
ANISOU 5304 O PRO C 88 5383 5743 6254 167 99 -732 O
ATOM 5305 CB PRO C 88 -7.452 18.957 17.942 1.00 48.93 C
ANISOU 5305 CB PRO C 88 5786 6103 6699 170 56 -736 C
ATOM 5306 CG PRO C 88 -8.134 18.570 16.674 1.00 48.78 C
ANISOU 5306 CG PRO C 88 5760 6071 6703 226 37 -775 C
ATOM 5307 CD PRO C 88 -8.681 19.843 16.114 1.00 49.03 C
ANISOU 5307 CD PRO C 88 5783 6116 6730 255 47 -809 C
ATOM 5308 N LYS C 89 -7.046 21.015 20.403 1.00 47.69 N
ANISOU 5308 N LYS C 89 5631 5995 6493 59 112 -709 N
ATOM 5309 CA LYS C 89 -6.060 21.844 21.106 1.00 47.60 C
ANISOU 5309 CA LYS C 89 5630 6000 6454 35 125 -672 C
ATOM 5310 C LYS C 89 -4.765 21.915 20.305 1.00 44.96 C
ANISOU 5310 C LYS C 89 5309 5658 6114 86 109 -631 C
ATOM 5311 O LYS C 89 -4.224 20.894 19.888 1.00 42.49 O
ANISOU 5311 O LYS C 89 5003 5331 5811 106 88 -607 O
ATOM 5312 CB LYS C 89 -5.805 21.283 22.512 1.00 50.91 C
ANISOU 5312 CB LYS C 89 6057 6428 6857 -40 131 -641 C
ATOM 5313 CG LYS C 89 -4.636 21.886 23.285 1.00 50.58 C
ANISOU 5313 CG LYS C 89 6030 6400 6787 -68 137 -594 C
ATOM 5314 CD LYS C 89 -4.238 20.943 24.412 1.00 51.05 C
ANISOU 5314 CD LYS C 89 6102 6460 6834 -134 129 -552 C
ATOM 5315 CE LYS C 89 -2.804 21.152 24.868 1.00 56.04 C
ANISOU 5315 CE LYS C 89 6749 7094 7446 -145 120 -493 C
ATOM 5316 NZ LYS C 89 -1.801 20.900 23.791 1.00 56.55 N
ANISOU 5316 NZ LYS C 89 6818 7141 7527 -78 98 -466 N
ATOM 5317 N ARG C 90 -4.288 23.132 20.093 1.00 44.17 N
ANISOU 5317 N ARG C 90 5210 5570 6000 105 118 -625 N
ATOM 5318 CA ARG C 90 -3.124 23.377 19.263 1.00 44.67 C
ANISOU 5318 CA ARG C 90 5283 5633 6056 152 107 -590 C
ATOM 5319 C ARG C 90 -1.987 23.947 20.124 1.00 45.93 C
ANISOU 5319 C ARG C 90 5452 5805 6194 118 115 -543 C
ATOM 5320 O ARG C 90 -2.173 24.934 20.839 1.00 49.17 O
ANISOU 5320 O ARG C 90 5861 6227 6593 86 132 -552 O
ATOM 5321 CB ARG C 90 -3.510 24.353 18.161 1.00 44.46 C
ANISOU 5321 CB ARG C 90 5252 5608 6033 204 107 -618 C
ATOM 5322 CG ARG C 90 -2.708 24.209 16.894 1.00 45.28 C
ANISOU 5322 CG ARG C 90 5361 5711 6131 264 92 -597 C
ATOM 5323 CD ARG C 90 -3.300 25.054 15.774 1.00 46.04 C
ANISOU 5323 CD ARG C 90 5454 5808 6230 310 87 -627 C
ATOM 5324 NE ARG C 90 -3.056 24.435 14.472 1.00 48.53 N
ANISOU 5324 NE ARG C 90 5771 6121 6543 365 71 -628 N
ATOM 5325 CZ ARG C 90 -1.850 24.248 13.937 1.00 49.40 C
ANISOU 5325 CZ ARG C 90 5888 6242 6638 390 68 -591 C
ATOM 5326 NH1 ARG C 90 -0.748 24.632 14.574 1.00 48.24 N
ANISOU 5326 NH1 ARG C 90 5745 6106 6478 367 78 -546 N
ATOM 5327 NH2 ARG C 90 -1.746 23.666 12.753 1.00 51.65 N
ANISOU 5327 NH2 ARG C 90 6174 6530 6921 439 55 -600 N
ATOM 5328 N LYS C 91 -0.819 23.313 20.071 1.00 44.09 N
ANISOU 5328 N LYS C 91 5225 5568 5957 126 102 -497 N
ATOM 5329 CA LYS C 91 0.317 23.721 20.903 1.00 42.55 C
ANISOU 5329 CA LYS C 91 5039 5384 5744 93 105 -449 C
ATOM 5330 C LYS C 91 1.462 24.345 20.090 1.00 42.21 C
ANISOU 5330 C LYS C 91 4996 5348 5693 137 102 -420 C
ATOM 5331 O LYS C 91 2.031 23.696 19.206 1.00 44.42 O
ANISOU 5331 O LYS C 91 5273 5623 5982 181 90 -408 O
ATOM 5332 CB LYS C 91 0.816 22.537 21.727 1.00 41.18 C
ANISOU 5332 CB LYS C 91 4871 5200 5574 54 90 -414 C
ATOM 5333 CG LYS C 91 1.904 22.890 22.721 1.00 40.82 C
ANISOU 5333 CG LYS C 91 4833 5164 5509 12 90 -365 C
ATOM 5334 CD LYS C 91 2.322 21.678 23.527 1.00 39.48 C
ANISOU 5334 CD LYS C 91 4672 4983 5346 -26 68 -329 C
ATOM 5335 CE LYS C 91 3.422 22.057 24.498 1.00 40.63 C
ANISOU 5335 CE LYS C 91 4824 5138 5472 -68 64 -280 C
ATOM 5336 NZ LYS C 91 3.491 21.116 25.653 1.00 45.19 N
ANISOU 5336 NZ LYS C 91 5414 5708 6047 -130 46 -249 N
ATOM 5337 N GLU C 92 1.779 25.605 20.386 1.00 40.05 N
ANISOU 5337 N GLU C 92 4724 5087 5404 123 115 -411 N
ATOM 5338 CA GLU C 92 2.847 26.320 19.691 1.00 39.32 C
ANISOU 5338 CA GLU C 92 4632 5004 5302 157 114 -380 C
ATOM 5339 C GLU C 92 3.937 26.734 20.676 1.00 38.13 C
ANISOU 5339 C GLU C 92 4487 4863 5138 115 116 -334 C
ATOM 5340 O GLU C 92 3.771 27.698 21.430 1.00 37.42 O
ANISOU 5340 O GLU C 92 4400 4778 5037 79 126 -339 O
ATOM 5341 CB GLU C 92 2.318 27.550 18.941 1.00 40.11 C
ANISOU 5341 CB GLU C 92 4732 5108 5400 185 121 -405 C
ATOM 5342 CG GLU C 92 1.127 27.303 18.023 1.00 43.15 C
ANISOU 5342 CG GLU C 92 5111 5483 5798 222 116 -453 C
ATOM 5343 CD GLU C 92 1.355 26.191 17.008 1.00 46.42 C
ANISOU 5343 CD GLU C 92 5523 5895 6218 268 104 -452 C
ATOM 5344 OE1 GLU C 92 2.331 26.275 16.227 1.00 48.84 O
ANISOU 5344 OE1 GLU C 92 5830 6213 6514 301 101 -423 O
ATOM 5345 OE2 GLU C 92 0.545 25.234 16.979 1.00 47.74 O
ANISOU 5345 OE2 GLU C 92 5687 6050 6400 269 98 -481 O
ATOM 5346 N VAL C 93 5.043 25.990 20.663 1.00 36.33 N
ANISOU 5346 N VAL C 93 4256 4634 4912 122 104 -294 N
ATOM 5347 CA VAL C 93 6.191 26.253 21.525 1.00 36.26 C
ANISOU 5347 CA VAL C 93 4250 4633 4893 86 100 -246 C
ATOM 5348 C VAL C 93 6.992 27.416 20.952 1.00 36.71 C
ANISOU 5348 C VAL C 93 4303 4704 4940 108 107 -226 C
ATOM 5349 O VAL C 93 7.415 27.362 19.800 1.00 38.76 O
ANISOU 5349 O VAL C 93 4554 4969 5202 158 107 -221 O
ATOM 5350 CB VAL C 93 7.096 25.009 21.640 1.00 36.12 C
ANISOU 5350 CB VAL C 93 4227 4607 4889 90 80 -211 C
ATOM 5351 CG1 VAL C 93 8.250 25.259 22.600 1.00 36.24 C
ANISOU 5351 CG1 VAL C 93 4244 4629 4896 50 72 -162 C
ATOM 5352 CG2 VAL C 93 6.291 23.802 22.088 1.00 36.00 C
ANISOU 5352 CG2 VAL C 93 4216 4573 4887 70 68 -229 C
ATOM 5353 N LEU C 94 7.178 28.471 21.739 1.00 36.34 N
ANISOU 5353 N LEU C 94 4262 4664 4880 70 114 -215 N
ATOM 5354 CA LEU C 94 7.985 29.612 21.309 1.00 37.40 C
ANISOU 5354 CA LEU C 94 4394 4809 5007 83 118 -191 C
ATOM 5355 C LEU C 94 9.416 29.572 21.870 1.00 39.49 C
ANISOU 5355 C LEU C 94 4655 5082 5267 61 110 -137 C
ATOM 5356 O LEU C 94 10.366 29.946 21.188 1.00 40.15 O
ANISOU 5356 O LEU C 94 4728 5175 5349 87 110 -108 O
ATOM 5357 CB LEU C 94 7.309 30.926 21.686 1.00 38.23 C
ANISOU 5357 CB LEU C 94 4507 4912 5106 61 127 -216 C
ATOM 5358 CG LEU C 94 6.130 31.454 20.856 1.00 38.69 C
ANISOU 5358 CG LEU C 94 4565 4962 5172 93 132 -263 C
ATOM 5359 CD1 LEU C 94 5.564 32.702 21.517 1.00 35.83 C
ANISOU 5359 CD1 LEU C 94 4208 4595 4811 63 138 -288 C
ATOM 5360 CD2 LEU C 94 6.534 31.747 19.416 1.00 38.61 C
ANISOU 5360 CD2 LEU C 94 4551 4957 5161 148 128 -249 C
ATOM 5361 N CYS C 95 9.562 29.127 23.118 1.00 40.13 N
ANISOU 5361 N CYS C 95 4741 5159 5344 11 102 -123 N
ATOM 5362 CA CYS C 95 10.869 29.003 23.752 1.00 37.84 C
ANISOU 5362 CA CYS C 95 4448 4875 5053 -13 89 -73 C
ATOM 5363 C CYS C 95 11.040 27.598 24.300 1.00 36.86 C
ANISOU 5363 C CYS C 95 4324 4740 4940 -29 71 -57 C
ATOM 5364 O CYS C 95 10.289 27.176 25.184 1.00 37.05 O
ANISOU 5364 O CYS C 95 4361 4758 4958 -70 68 -72 O
ATOM 5365 CB CYS C 95 11.029 30.035 24.872 1.00 38.81 C
ANISOU 5365 CB CYS C 95 4581 5003 5159 -69 92 -63 C
ATOM 5366 SG CYS C 95 10.572 31.722 24.401 1.00 42.19 S
ANISOU 5366 SG CYS C 95 5012 5434 5580 -58 109 -89 S
ATOM 5367 N HIS C 96 12.023 26.881 23.756 1.00 35.77 N
ANISOU 5367 N HIS C 96 4169 4600 4819 3 57 -29 N
ATOM 5368 CA HIS C 96 12.314 25.504 24.138 1.00 34.86 C
ANISOU 5368 CA HIS C 96 4052 4470 4724 -2 32 -11 C
ATOM 5369 C HIS C 96 13.277 25.437 25.279 1.00 35.58 C
ANISOU 5369 C HIS C 96 4145 4560 4813 -51 11 35 C
ATOM 5370 O HIS C 96 13.513 24.358 25.817 1.00 37.27 O
ANISOU 5370 O HIS C 96 4359 4757 5042 -67 -15 55 O
ATOM 5371 CB HIS C 96 12.869 24.719 22.954 1.00 34.08 C
ANISOU 5371 CB HIS C 96 3931 4367 4650 60 26 -12 C
ATOM 5372 CG HIS C 96 11.956 24.704 21.757 1.00 33.89 C
ANISOU 5372 CG HIS C 96 3905 4345 4625 109 43 -58 C
ATOM 5373 ND1 HIS C 96 11.178 23.646 21.449 1.00 33.93 N
ANISOU 5373 ND1 HIS C 96 3911 4332 4646 128 35 -87 N
ATOM 5374 CD2 HIS C 96 11.704 25.677 20.785 1.00 33.17 C
ANISOU 5374 CD2 HIS C 96 3812 4271 4519 142 66 -78 C
ATOM 5375 CE1 HIS C 96 10.462 23.928 20.339 1.00 33.29 C
ANISOU 5375 CE1 HIS C 96 3829 4258 4560 171 52 -126 C
ATOM 5376 NE2 HIS C 96 10.782 25.173 19.939 1.00 33.17 N
ANISOU 5376 NE2 HIS C 96 3813 4265 4525 179 70 -119 N
ATOM 5377 N GLY C 97 13.854 26.578 25.654 1.00 35.19 N
ANISOU 5377 N GLY C 97 4097 4526 4747 -74 19 55 N
ATOM 5378 CA GLY C 97 14.779 26.652 26.798 1.00 35.93 C
ANISOU 5378 CA GLY C 97 4193 4621 4835 -124 -2 100 C
ATOM 5379 C GLY C 97 16.259 26.647 26.436 1.00 36.57 C
ANISOU 5379 C GLY C 97 4250 4707 4935 -100 -15 141 C
ATOM 5380 O GLY C 97 17.122 26.854 27.289 1.00 35.56 O
ANISOU 5380 O GLY C 97 4123 4583 4806 -138 -34 180 O
ATOM 5381 N HIS C 98 16.545 26.422 25.160 1.00 37.19 N
ANISOU 5381 N HIS C 98 4307 4791 5033 -37 -5 131 N
ATOM 5382 CA HIS C 98 17.902 26.256 24.685 1.00 37.73 C
ANISOU 5382 CA HIS C 98 4345 4866 5122 -8 -15 162 C
ATOM 5383 C HIS C 98 18.032 26.960 23.369 1.00 37.08 C
ANISOU 5383 C HIS C 98 4247 4805 5034 41 13 146 C
ATOM 5384 O HIS C 98 17.333 26.633 22.408 1.00 37.27 O
ANISOU 5384 O HIS C 98 4270 4829 5059 83 28 111 O
ATOM 5385 CB HIS C 98 18.228 24.763 24.551 1.00 39.20 C
ANISOU 5385 CB HIS C 98 4516 5033 5345 17 -42 167 C
ATOM 5386 CG HIS C 98 19.539 24.472 23.857 1.00 41.07 C
ANISOU 5386 CG HIS C 98 4715 5279 5611 59 -48 187 C
ATOM 5387 ND1 HIS C 98 20.731 24.606 24.472 1.00 45.09 N
ANISOU 5387 ND1 HIS C 98 5208 5791 6133 37 -69 230 N
ATOM 5388 CD2 HIS C 98 19.813 24.027 22.565 1.00 42.99 C
ANISOU 5388 CD2 HIS C 98 4931 5531 5872 124 -35 164 C
ATOM 5389 CE1 HIS C 98 21.722 24.266 23.617 1.00 45.68 C
ANISOU 5389 CE1 HIS C 98 5243 5875 6235 86 -68 234 C
ATOM 5390 NE2 HIS C 98 21.159 23.914 22.451 1.00 45.82 N
ANISOU 5390 NE2 HIS C 98 5254 5899 6254 138 -46 193 N
ATOM 5391 N ASP C 99 18.923 27.950 23.330 1.00 36.39 N
ANISOU 5391 N ASP C 99 4149 4737 4940 32 21 174 N
ATOM 5392 CA ASP C 99 19.246 28.693 22.115 1.00 34.51 C
ANISOU 5392 CA ASP C 99 3893 4523 4693 71 47 170 C
ATOM 5393 C ASP C 99 18.012 29.104 21.307 1.00 35.48 C
ANISOU 5393 C ASP C 99 4034 4647 4797 95 69 128 C
ATOM 5394 O ASP C 99 17.906 28.822 20.110 1.00 35.84 O
ANISOU 5394 O ASP C 99 4068 4705 4844 144 83 109 O
ATOM 5395 CB ASP C 99 20.229 27.892 21.269 1.00 33.90 C
ANISOU 5395 CB ASP C 99 3780 4458 4640 118 45 179 C
ATOM 5396 CG ASP C 99 21.652 28.013 21.759 1.00 33.73 C
ANISOU 5396 CG ASP C 99 3733 4446 4635 100 31 224 C
ATOM 5397 OD1 ASP C 99 22.513 27.268 21.253 1.00 34.48 O
ANISOU 5397 OD1 ASP C 99 3793 4549 4756 134 26 230 O
ATOM 5398 OD2 ASP C 99 21.934 28.855 22.637 1.00 33.72 O
ANISOU 5398 OD2 ASP C 99 3743 4444 4622 52 24 252 O
ATOM 5399 N ASP C 100 17.073 29.764 21.979 1.00 36.34 N
ANISOU 5399 N ASP C 100 4170 4745 4890 59 71 112 N
ATOM 5400 CA ASP C 100 15.828 30.161 21.349 1.00 35.91 C
ANISOU 5400 CA ASP C 100 4132 4687 4823 78 87 70 C
ATOM 5401 C ASP C 100 15.985 31.381 20.439 1.00 35.78 C
ANISOU 5401 C ASP C 100 4113 4687 4792 96 104 75 C
ATOM 5402 O ASP C 100 16.977 32.112 20.524 1.00 35.16 O
ANISOU 5402 O ASP C 100 4025 4622 4711 82 104 111 O
ATOM 5403 CB ASP C 100 14.758 30.377 22.406 1.00 37.51 C
ANISOU 5403 CB ASP C 100 4360 4872 5017 34 84 46 C
ATOM 5404 CG ASP C 100 14.297 29.079 23.030 1.00 39.59 C
ANISOU 5404 CG ASP C 100 4630 5120 5291 22 70 34 C
ATOM 5405 OD1 ASP C 100 13.981 28.138 22.273 1.00 41.07 O
ANISOU 5405 OD1 ASP C 100 4809 5302 5491 62 70 15 O
ATOM 5406 OD2 ASP C 100 14.236 28.990 24.279 1.00 42.19 O
ANISOU 5406 OD2 ASP C 100 4971 5442 5614 -30 59 45 O
ATOM 5407 N ASP C 101 14.995 31.577 19.571 1.00 34.77 N
ANISOU 5407 N ASP C 101 3995 4558 4657 127 115 40 N
ATOM 5408 CA ASP C 101 15.036 32.563 18.493 1.00 33.99 C
ANISOU 5408 CA ASP C 101 3894 4473 4544 150 126 44 C
ATOM 5409 C ASP C 101 14.687 33.974 18.904 1.00 33.53 C
ANISOU 5409 C ASP C 101 3854 4406 4480 119 125 46 C
ATOM 5410 O ASP C 101 15.042 34.926 18.232 1.00 33.23 O
ANISOU 5410 O ASP C 101 3813 4378 4433 126 128 66 O
ATOM 5411 CB ASP C 101 14.066 32.140 17.393 1.00 34.24 C
ANISOU 5411 CB ASP C 101 3931 4506 4571 196 133 5 C
ATOM 5412 CG ASP C 101 14.587 30.983 16.595 1.00 35.85 C
ANISOU 5412 CG ASP C 101 4114 4726 4779 237 137 3 C
ATOM 5413 OD1 ASP C 101 15.680 30.474 16.924 1.00 35.80 O
ANISOU 5413 OD1 ASP C 101 4088 4728 4783 232 134 31 O
ATOM 5414 OD2 ASP C 101 13.914 30.578 15.634 1.00 37.72 O
ANISOU 5414 OD2 ASP C 101 4353 4966 5010 276 141 -27 O
ATOM 5415 N TYR C 102 13.972 34.108 20.003 1.00 34.99 N
ANISOU 5415 N TYR C 102 4054 4571 4669 83 119 25 N
ATOM 5416 CA TYR C 102 13.376 35.385 20.330 1.00 36.37 C
ANISOU 5416 CA TYR C 102 4244 4731 4842 60 117 11 C
ATOM 5417 C TYR C 102 14.013 35.922 21.586 1.00 36.11 C
ANISOU 5417 C TYR C 102 4215 4695 4810 8 109 33 C
ATOM 5418 O TYR C 102 14.242 35.173 22.539 1.00 36.16 O
ANISOU 5418 O TYR C 102 4220 4701 4816 -19 105 39 O
ATOM 5419 CB TYR C 102 11.859 35.238 20.516 1.00 36.27 C
ANISOU 5419 CB TYR C 102 4245 4701 4834 63 119 -44 C
ATOM 5420 CG TYR C 102 11.181 34.424 19.441 1.00 35.49 C
ANISOU 5420 CG TYR C 102 4143 4603 4736 111 123 -71 C
ATOM 5421 CD1 TYR C 102 10.928 33.064 19.638 1.00 36.37 C
ANISOU 5421 CD1 TYR C 102 4250 4714 4852 118 123 -86 C
ATOM 5422 CD2 TYR C 102 10.814 34.998 18.227 1.00 34.73 C
ANISOU 5422 CD2 TYR C 102 4049 4509 4636 148 123 -78 C
ATOM 5423 CE1 TYR C 102 10.315 32.299 18.660 1.00 36.63 C
ANISOU 5423 CE1 TYR C 102 4280 4748 4887 162 125 -112 C
ATOM 5424 CE2 TYR C 102 10.201 34.243 17.239 1.00 36.62 C
ANISOU 5424 CE2 TYR C 102 4286 4752 4874 191 125 -104 C
ATOM 5425 CZ TYR C 102 9.949 32.891 17.462 1.00 37.69 C
ANISOU 5425 CZ TYR C 102 4416 4886 5015 199 127 -122 C
ATOM 5426 OH TYR C 102 9.342 32.114 16.488 1.00 37.95 O
ANISOU 5426 OH TYR C 102 4448 4922 5049 241 128 -150 O
ATOM 5427 N SER C 103 14.282 37.224 21.585 1.00 35.80 N
ANISOU 5427 N SER C 103 4179 4651 4770 -7 105 48 N
ATOM 5428 CA SER C 103 14.958 37.863 22.707 1.00 36.64 C
ANISOU 5428 CA SER C 103 4289 4755 4877 -56 97 70 C
ATOM 5429 C SER C 103 14.090 37.881 23.966 1.00 37.01 C
ANISOU 5429 C SER C 103 4350 4788 4922 -96 95 30 C
ATOM 5430 O SER C 103 14.606 38.041 25.066 1.00 37.89 O
ANISOU 5430 O SER C 103 4466 4902 5029 -140 88 44 O
ATOM 5431 CB SER C 103 15.395 39.271 22.339 1.00 34.73 C
ANISOU 5431 CB SER C 103 4047 4507 4639 -62 90 92 C
ATOM 5432 OG SER C 103 14.276 40.128 22.288 1.00 34.73 O
ANISOU 5432 OG SER C 103 4063 4485 4647 -61 87 51 O
ATOM 5433 N PHE C 104 12.783 37.698 23.810 1.00 36.90 N
ANISOU 5433 N PHE C 104 4345 4764 4911 -81 103 -20 N
ATOM 5434 CA PHE C 104 11.915 37.688 24.977 1.00 38.55 C
ANISOU 5434 CA PHE C 104 4564 4965 5115 -120 106 -62 C
ATOM 5435 C PHE C 104 11.995 36.414 25.807 1.00 40.97 C
ANISOU 5435 C PHE C 104 4872 5282 5411 -145 106 -57 C
ATOM 5436 O PHE C 104 11.548 36.402 26.954 1.00 43.03 O
ANISOU 5436 O PHE C 104 5143 5545 5661 -190 109 -81 O
ATOM 5437 CB PHE C 104 10.458 38.065 24.646 1.00 37.33 C
ANISOU 5437 CB PHE C 104 4415 4796 4972 -101 113 -123 C
ATOM 5438 CG PHE C 104 9.801 37.188 23.628 1.00 35.85 C
ANISOU 5438 CG PHE C 104 4223 4609 4789 -54 118 -139 C
ATOM 5439 CD1 PHE C 104 9.653 37.627 22.317 1.00 36.10 C
ANISOU 5439 CD1 PHE C 104 4252 4635 4830 -7 115 -137 C
ATOM 5440 CD2 PHE C 104 9.289 35.942 23.981 1.00 36.48 C
ANISOU 5440 CD2 PHE C 104 4302 4694 4863 -59 125 -158 C
ATOM 5441 CE1 PHE C 104 9.025 36.835 21.364 1.00 35.77 C
ANISOU 5441 CE1 PHE C 104 4207 4594 4790 35 118 -155 C
ATOM 5442 CE2 PHE C 104 8.663 35.139 23.036 1.00 36.19 C
ANISOU 5442 CE2 PHE C 104 4261 4656 4833 -15 128 -176 C
ATOM 5443 CZ PHE C 104 8.529 35.588 21.724 1.00 36.01 C
ANISOU 5443 CZ PHE C 104 4235 4629 4818 32 125 -177 C
ATOM 5444 N CYS C 105 12.569 35.351 25.243 1.00 42.34 N
ANISOU 5444 N CYS C 105 5036 5464 5587 -118 103 -28 N
ATOM 5445 CA CYS C 105 12.713 34.081 25.969 1.00 41.77 C
ANISOU 5445 CA CYS C 105 4964 5395 5508 -140 97 -17 C
ATOM 5446 C CYS C 105 13.535 34.230 27.253 1.00 42.04 C
ANISOU 5446 C CYS C 105 5004 5436 5531 -197 84 14 C
ATOM 5447 O CYS C 105 13.253 33.565 28.260 1.00 39.99 O
ANISOU 5447 O CYS C 105 4755 5179 5260 -238 79 9 O
ATOM 5448 CB CYS C 105 13.316 33.000 25.069 1.00 42.03 C
ANISOU 5448 CB CYS C 105 4982 5432 5553 -96 92 9 C
ATOM 5449 SG CYS C 105 12.295 32.564 23.634 1.00 45.10 S
ANISOU 5449 SG CYS C 105 5367 5816 5951 -33 104 -30 S
ATOM 5450 N ARG C 106 14.534 35.113 27.220 1.00 42.62 N
ANISOU 5450 N ARG C 106 5072 5514 5607 -203 77 47 N
ATOM 5451 CA ARG C 106 15.379 35.355 28.395 1.00 45.17 C
ANISOU 5451 CA ARG C 106 5400 5843 5919 -257 62 78 C
ATOM 5452 C ARG C 106 14.755 36.282 29.455 1.00 45.42 C
ANISOU 5452 C ARG C 106 5449 5873 5934 -307 67 44 C
ATOM 5453 O ARG C 106 15.331 36.487 30.528 1.00 46.37 O
ANISOU 5453 O ARG C 106 5576 6000 6040 -357 54 63 O
ATOM 5454 CB ARG C 106 16.814 35.775 28.007 1.00 47.19 C
ANISOU 5454 CB ARG C 106 5639 6104 6185 -247 51 131 C
ATOM 5455 CG ARG C 106 16.954 36.753 26.849 1.00 51.33 C
ANISOU 5455 CG ARG C 106 6154 6627 6720 -209 61 133 C
ATOM 5456 CD ARG C 106 17.528 38.106 27.271 1.00 57.63 C
ANISOU 5456 CD ARG C 106 6955 7423 7518 -240 54 149 C
ATOM 5457 NE ARG C 106 16.855 38.687 28.439 1.00 62.02 N
ANISOU 5457 NE ARG C 106 7531 7971 8061 -288 52 114 N
ATOM 5458 CZ ARG C 106 17.463 39.006 29.582 1.00 59.62 C
ANISOU 5458 CZ ARG C 106 7234 7671 7748 -340 37 131 C
ATOM 5459 NH1 ARG C 106 18.774 38.822 29.706 1.00 60.10 N
ANISOU 5459 NH1 ARG C 106 7280 7740 7812 -350 21 185 N
ATOM 5460 NH2 ARG C 106 16.763 39.517 30.596 1.00 53.15 N
ANISOU 5460 NH2 ARG C 106 6431 6848 6913 -382 39 91 N
ATOM 5461 N ALA C 107 13.568 36.809 29.168 1.00 42.92 N
ANISOU 5461 N ALA C 107 5138 5548 5620 -294 83 -9 N
ATOM 5462 CA ALA C 107 12.867 37.666 30.110 1.00 42.93 C
ANISOU 5462 CA ALA C 107 5151 5549 5609 -336 90 -53 C
ATOM 5463 C ALA C 107 12.418 36.901 31.353 1.00 44.22 C
ANISOU 5463 C ALA C 107 5327 5728 5747 -389 92 -69 C
ATOM 5464 O ALA C 107 11.959 35.757 31.262 1.00 45.27 O
ANISOU 5464 O ALA C 107 5460 5863 5876 -382 96 -72 O
ATOM 5465 CB ALA C 107 11.676 38.325 29.442 1.00 43.69 C
ANISOU 5465 CB ALA C 107 5245 5631 5720 -304 104 -109 C
ATOM 5466 N LEU C 108 12.543 37.556 32.508 1.00 43.44 N
ANISOU 5466 N LEU C 108 5239 5637 5628 -444 90 -80 N
ATOM 5467 CA LEU C 108 12.174 36.979 33.801 1.00 41.77 C
ANISOU 5467 CA LEU C 108 5041 5446 5383 -506 92 -93 C
ATOM 5468 C LEU C 108 10.828 37.500 34.326 1.00 43.22 C
ANISOU 5468 C LEU C 108 5229 5637 5555 -529 117 -170 C
ATOM 5469 O LEU C 108 10.269 38.466 33.795 1.00 41.39 O
ANISOU 5469 O LEU C 108 4989 5391 5345 -499 128 -212 O
ATOM 5470 CB LEU C 108 13.265 37.271 34.836 1.00 38.15 C
ANISOU 5470 CB LEU C 108 4592 4998 4904 -559 72 -54 C
ATOM 5471 CG LEU C 108 14.691 36.824 34.539 1.00 36.62 C
ANISOU 5471 CG LEU C 108 4391 4800 4722 -546 45 20 C
ATOM 5472 CD1 LEU C 108 15.625 37.368 35.605 1.00 35.12 C
ANISOU 5472 CD1 LEU C 108 4210 4620 4512 -601 24 47 C
ATOM 5473 CD2 LEU C 108 14.796 35.308 34.451 1.00 36.01 C
ANISOU 5473 CD2 LEU C 108 4312 4724 4644 -540 34 52 C
ATOM 5474 N LYS C 109 10.324 36.844 35.372 1.00 44.67 N
ANISOU 5474 N LYS C 109 5423 5843 5705 -583 125 -186 N
ATOM 5475 CA LYS C 109 9.168 37.320 36.122 1.00 46.60 C
ANISOU 5475 CA LYS C 109 5670 6104 5931 -620 150 -259 C
ATOM 5476 C LYS C 109 9.363 38.785 36.551 1.00 47.25 C
ANISOU 5476 C LYS C 109 5753 6185 6016 -636 151 -290 C
ATOM 5477 O LYS C 109 10.364 39.132 37.181 1.00 47.30 O
ANISOU 5477 O LYS C 109 5768 6196 6005 -669 133 -254 O
ATOM 5478 CB LYS C 109 8.925 36.421 37.341 1.00 48.13 C
ANISOU 5478 CB LYS C 109 5878 6329 6078 -690 154 -255 C
ATOM 5479 CG LYS C 109 7.583 36.659 38.022 1.00 52.18 C
ANISOU 5479 CG LYS C 109 6389 6866 6570 -727 187 -335 C
ATOM 5480 CD LYS C 109 7.117 35.460 38.837 1.00 53.85 C
ANISOU 5480 CD LYS C 109 6610 7106 6741 -783 194 -327 C
ATOM 5481 CE LYS C 109 7.647 35.489 40.258 1.00 53.34 C
ANISOU 5481 CE LYS C 109 6567 7074 6623 -866 186 -308 C
ATOM 5482 NZ LYS C 109 7.210 34.276 40.996 1.00 52.79 N
ANISOU 5482 NZ LYS C 109 6511 7032 6515 -924 189 -293 N
ATOM 5483 N GLY C 110 8.410 39.636 36.181 1.00 47.88 N
ANISOU 5483 N GLY C 110 5820 6252 6119 -609 169 -357 N
ATOM 5484 CA GLY C 110 8.460 41.055 36.514 1.00 48.45 C
ANISOU 5484 CA GLY C 110 5891 6316 6202 -619 168 -396 C
ATOM 5485 C GLY C 110 9.278 41.926 35.573 1.00 50.20 C
ANISOU 5485 C GLY C 110 6107 6504 6462 -572 145 -361 C
ATOM 5486 O GLY C 110 9.336 43.145 35.746 1.00 53.80 O
ANISOU 5486 O GLY C 110 6562 6945 6934 -575 139 -390 O
ATOM 5487 N GLU C 111 9.916 41.318 34.579 1.00 48.13 N
ANISOU 5487 N GLU C 111 5842 6229 6214 -529 132 -299 N
ATOM 5488 CA GLU C 111 10.704 42.080 33.618 1.00 46.59 C
ANISOU 5488 CA GLU C 111 5642 6007 6052 -487 113 -261 C
ATOM 5489 C GLU C 111 9.797 42.700 32.561 1.00 45.06 C
ANISOU 5489 C GLU C 111 5437 5787 5896 -432 118 -303 C
ATOM 5490 O GLU C 111 8.886 42.061 32.056 1.00 45.42 O
ANISOU 5490 O GLU C 111 5476 5832 5946 -405 132 -330 O
ATOM 5491 CB GLU C 111 11.779 41.193 32.972 1.00 47.77 C
ANISOU 5491 CB GLU C 111 5789 6159 6200 -465 99 -182 C
ATOM 5492 CG GLU C 111 12.738 41.914 32.031 1.00 47.74 C
ANISOU 5492 CG GLU C 111 5779 6136 6223 -429 81 -136 C
ATOM 5493 CD GLU C 111 13.962 41.086 31.673 1.00 47.47 C
ANISOU 5493 CD GLU C 111 5739 6111 6185 -420 68 -61 C
ATOM 5494 OE1 GLU C 111 14.722 41.510 30.780 1.00 47.90 O
ANISOU 5494 OE1 GLU C 111 5785 6156 6259 -388 58 -22 O
ATOM 5495 OE2 GLU C 111 14.174 40.018 32.283 1.00 48.36 O
ANISOU 5495 OE2 GLU C 111 5856 6242 6276 -445 67 -42 O
ATOM 5496 N THR C 112 10.051 43.962 32.250 1.00 45.44 N
ANISOU 5496 N THR C 112 5483 5809 5971 -419 103 -308 N
ATOM 5497 CA THR C 112 9.346 44.670 31.196 1.00 44.69 C
ANISOU 5497 CA THR C 112 5380 5684 5916 -368 99 -337 C
ATOM 5498 C THR C 112 9.781 44.101 29.846 1.00 44.07 C
ANISOU 5498 C THR C 112 5298 5600 5846 -317 92 -280 C
ATOM 5499 O THR C 112 10.977 43.965 29.591 1.00 46.38 O
ANISOU 5499 O THR C 112 5591 5897 6131 -318 80 -213 O
ATOM 5500 CB THR C 112 9.668 46.176 31.278 1.00 45.02 C
ANISOU 5500 CB THR C 112 5422 5697 5986 -374 78 -346 C
ATOM 5501 OG1 THR C 112 9.312 46.656 32.581 1.00 46.26 O
ANISOU 5501 OG1 THR C 112 5581 5862 6131 -422 86 -404 O
ATOM 5502 CG2 THR C 112 8.916 46.976 30.223 1.00 45.02 C
ANISOU 5502 CG2 THR C 112 5415 5660 6030 -323 66 -375 C
ATOM 5503 N VAL C 113 8.813 43.740 29.002 1.00 42.24 N
ANISOU 5503 N VAL C 113 5059 5360 5629 -274 100 -308 N
ATOM 5504 CA VAL C 113 9.096 43.296 27.630 1.00 40.29 C
ANISOU 5504 CA VAL C 113 4809 5108 5391 -223 93 -264 C
ATOM 5505 C VAL C 113 8.467 44.260 26.626 1.00 40.02 C
ANISOU 5505 C VAL C 113 4771 5042 5391 -181 79 -286 C
ATOM 5506 O VAL C 113 7.258 44.484 26.644 1.00 39.69 O
ANISOU 5506 O VAL C 113 4724 4987 5368 -169 83 -349 O
ATOM 5507 CB VAL C 113 8.578 41.863 27.354 1.00 39.13 C
ANISOU 5507 CB VAL C 113 4658 4979 5228 -205 110 -269 C
ATOM 5508 CG1 VAL C 113 8.824 41.462 25.907 1.00 38.56 C
ANISOU 5508 CG1 VAL C 113 4583 4904 5164 -151 104 -232 C
ATOM 5509 CG2 VAL C 113 9.225 40.855 28.287 1.00 38.46 C
ANISOU 5509 CG2 VAL C 113 4579 4922 5112 -246 117 -240 C
ATOM 5510 N ASN C 114 9.298 44.846 25.774 1.00 39.91 N
ANISOU 5510 N ASN C 114 4760 5017 5388 -161 61 -233 N
ATOM 5511 CA ASN C 114 8.816 45.613 24.637 1.00 41.69 C
ANISOU 5511 CA ASN C 114 4984 5212 5641 -119 43 -238 C
ATOM 5512 C ASN C 114 9.517 45.109 23.373 1.00 43.04 C
ANISOU 5512 C ASN C 114 5155 5397 5800 -85 40 -175 C
ATOM 5513 O ASN C 114 10.699 45.409 23.145 1.00 44.33 O
ANISOU 5513 O ASN C 114 5319 5567 5955 -94 32 -115 O
ATOM 5514 CB ASN C 114 9.032 47.124 24.834 1.00 41.40 C
ANISOU 5514 CB ASN C 114 4951 5143 5634 -134 17 -241 C
ATOM 5515 CG ASN C 114 8.320 47.959 23.772 1.00 43.62 C
ANISOU 5515 CG ASN C 114 5233 5388 5950 -94 -6 -255 C
ATOM 5516 OD1 ASN C 114 7.354 47.498 23.160 1.00 45.81 O
ANISOU 5516 OD1 ASN C 114 5507 5663 6235 -60 -2 -286 O
ATOM 5517 ND2 ASN C 114 8.786 49.190 23.552 1.00 42.24 N
ANISOU 5517 ND2 ASN C 114 5063 5183 5801 -100 -35 -231 N
ATOM 5518 N THR C 115 8.809 44.316 22.570 1.00 41.04 N
ANISOU 5518 N THR C 115 4899 5149 5542 -47 48 -190 N
ATOM 5519 CA THR C 115 9.428 43.726 21.385 1.00 41.13 C
ANISOU 5519 CA THR C 115 4909 5180 5538 -14 49 -139 C
ATOM 5520 C THR C 115 8.452 43.564 20.244 1.00 41.64 C
ANISOU 5520 C THR C 115 4974 5234 5611 32 43 -162 C
ATOM 5521 O THR C 115 7.251 43.387 20.457 1.00 41.78 O
ANISOU 5521 O THR C 115 4989 5239 5643 41 46 -221 O
ATOM 5522 CB THR C 115 10.096 42.363 21.685 1.00 42.04 C
ANISOU 5522 CB THR C 115 5018 5328 5625 -21 70 -114 C
ATOM 5523 OG1 THR C 115 11.059 42.071 20.668 1.00 40.95 O
ANISOU 5523 OG1 THR C 115 4875 5210 5473 1 70 -57 O
ATOM 5524 CG2 THR C 115 9.064 41.234 21.745 1.00 42.13 C
ANISOU 5524 CG2 THR C 115 5027 5346 5632 -5 84 -160 C
ATOM 5525 N SER C 116 8.975 43.632 19.025 1.00 42.28 N
ANISOU 5525 N SER C 116 5057 5323 5682 60 35 -116 N
ATOM 5526 CA SER C 116 8.162 43.335 17.858 1.00 41.35 C
ANISOU 5526 CA SER C 116 4942 5204 5565 105 29 -132 C
ATOM 5527 C SER C 116 8.738 42.148 17.083 1.00 41.41 C
ANISOU 5527 C SER C 116 4944 5247 5541 129 46 -101 C
ATOM 5528 O SER C 116 9.929 42.098 16.779 1.00 41.34 O
ANISOU 5528 O SER C 116 4932 5261 5513 123 52 -47 O
ATOM 5529 CB SER C 116 7.908 44.578 16.990 1.00 39.78 C
ANISOU 5529 CB SER C 116 4751 4976 5384 120 -1 -120 C
ATOM 5530 OG SER C 116 9.085 45.098 16.429 1.00 39.13 O
ANISOU 5530 OG SER C 116 4674 4907 5288 111 -8 -52 O
ATOM 5531 N ILE C 117 7.868 41.187 16.795 1.00 41.55 N
ANISOU 5531 N ILE C 117 4959 5269 5557 155 55 -140 N
ATOM 5532 CA ILE C 117 8.269 39.909 16.242 1.00 41.02 C
ANISOU 5532 CA ILE C 117 4886 5234 5466 178 71 -125 C
ATOM 5533 C ILE C 117 7.847 39.793 14.789 1.00 39.74 C
ANISOU 5533 C ILE C 117 4727 5077 5294 222 63 -125 C
ATOM 5534 O ILE C 117 6.653 39.755 14.500 1.00 40.10 O
ANISOU 5534 O ILE C 117 4776 5105 5353 243 53 -170 O
ATOM 5535 CB ILE C 117 7.639 38.758 17.036 1.00 41.06 C
ANISOU 5535 CB ILE C 117 4884 5239 5474 172 86 -168 C
ATOM 5536 CG1 ILE C 117 7.908 38.950 18.529 1.00 42.59 C
ANISOU 5536 CG1 ILE C 117 5078 5428 5675 123 92 -172 C
ATOM 5537 CG2 ILE C 117 8.166 37.417 16.540 1.00 41.03 C
ANISOU 5537 CG2 ILE C 117 4873 5263 5452 194 99 -152 C
ATOM 5538 CD1 ILE C 117 6.732 38.585 19.408 1.00 44.38 C
ANISOU 5538 CD1 ILE C 117 5304 5643 5915 107 99 -232 C
ATOM 5539 N PRO C 118 8.827 39.724 13.870 1.00 40.25 N
ANISOU 5539 N PRO C 118 4789 5169 5332 236 66 -77 N
ATOM 5540 CA PRO C 118 8.520 39.586 12.450 1.00 41.13 C
ANISOU 5540 CA PRO C 118 4906 5294 5426 275 59 -74 C
ATOM 5541 C PRO C 118 7.879 38.247 12.150 1.00 41.43 C
ANISOU 5541 C PRO C 118 4939 5343 5459 306 70 -114 C
ATOM 5542 O PRO C 118 8.112 37.274 12.872 1.00 42.07 O
ANISOU 5542 O PRO C 118 5010 5431 5542 297 87 -126 O
ATOM 5543 CB PRO C 118 9.895 39.672 11.781 1.00 40.77 C
ANISOU 5543 CB PRO C 118 4854 5284 5350 273 70 -14 C
ATOM 5544 CG PRO C 118 10.856 39.267 12.840 1.00 40.62 C
ANISOU 5544 CG PRO C 118 4821 5276 5335 244 87 2 C
ATOM 5545 CD PRO C 118 10.279 39.803 14.110 1.00 39.56 C
ANISOU 5545 CD PRO C 118 4694 5106 5231 213 78 -24 C
ATOM 5546 N PHE C 119 7.081 38.209 11.089 1.00 43.63 N
ANISOU 5546 N PHE C 119 5225 5619 5731 339 57 -133 N
ATOM 5547 CA PHE C 119 6.433 36.983 10.618 1.00 46.03 C
ANISOU 5547 CA PHE C 119 5525 5933 6029 372 63 -172 C
ATOM 5548 C PHE C 119 5.953 37.138 9.183 1.00 47.64 C
ANISOU 5548 C PHE C 119 5740 6146 6214 407 47 -174 C
ATOM 5549 O PHE C 119 5.769 38.260 8.705 1.00 49.64 O
ANISOU 5549 O PHE C 119 6005 6387 6467 405 25 -155 O
ATOM 5550 CB PHE C 119 5.238 36.619 11.508 1.00 43.00 C
ANISOU 5550 CB PHE C 119 5139 5519 5678 366 60 -229 C
ATOM 5551 CG PHE C 119 4.114 37.608 11.451 1.00 42.71 C
ANISOU 5551 CG PHE C 119 5111 5449 5666 368 36 -257 C
ATOM 5552 CD1 PHE C 119 3.045 37.413 10.586 1.00 43.80 C
ANISOU 5552 CD1 PHE C 119 5253 5579 5809 402 19 -292 C
ATOM 5553 CD2 PHE C 119 4.116 38.733 12.268 1.00 41.54 C
ANISOU 5553 CD2 PHE C 119 4965 5277 5540 337 27 -253 C
ATOM 5554 CE1 PHE C 119 1.995 38.321 10.537 1.00 44.60 C
ANISOU 5554 CE1 PHE C 119 5359 5647 5940 406 -7 -320 C
ATOM 5555 CE2 PHE C 119 3.080 39.645 12.215 1.00 41.95 C
ANISOU 5555 CE2 PHE C 119 5021 5295 5622 342 2 -284 C
ATOM 5556 CZ PHE C 119 2.015 39.439 11.355 1.00 42.70 C
ANISOU 5556 CZ PHE C 119 5118 5380 5724 377 -15 -318 C
ATOM 5557 N SER C 120 5.739 36.010 8.508 1.00 48.88 N
ANISOU 5557 N SER C 120 5892 6322 6355 439 55 -197 N
ATOM 5558 CA SER C 120 5.052 36.000 7.215 1.00 50.29 C
ANISOU 5558 CA SER C 120 6082 6509 6517 474 37 -211 C
ATOM 5559 C SER C 120 4.343 34.674 6.989 1.00 50.15 C
ANISOU 5559 C SER C 120 6058 6494 6503 503 42 -261 C
ATOM 5560 O SER C 120 4.870 33.624 7.341 1.00 55.77 O
ANISOU 5560 O SER C 120 6757 7220 7213 505 63 -267 O
ATOM 5561 CB SER C 120 6.021 36.298 6.062 1.00 49.58 C
ANISOU 5561 CB SER C 120 5996 6460 6381 482 41 -163 C
ATOM 5562 OG SER C 120 6.797 35.163 5.729 1.00 50.34 O
ANISOU 5562 OG SER C 120 6078 6594 6453 498 68 -164 O
ATOM 5563 N PHE C 121 3.146 34.722 6.418 1.00 48.73 N
ANISOU 5563 N PHE C 121 5886 6296 6331 525 19 -297 N
ATOM 5564 CA PHE C 121 2.450 33.500 6.024 1.00 48.41 C
ANISOU 5564 CA PHE C 121 5841 6259 6293 555 19 -343 C
ATOM 5565 C PHE C 121 1.752 33.648 4.668 1.00 49.09 C
ANISOU 5565 C PHE C 121 5940 6352 6358 588 -5 -356 C
ATOM 5566 O PHE C 121 1.473 34.763 4.228 1.00 45.79 O
ANISOU 5566 O PHE C 121 5536 5924 5937 585 -30 -337 O
ATOM 5567 CB PHE C 121 1.495 33.009 7.124 1.00 45.95 C
ANISOU 5567 CB PHE C 121 5520 5914 6024 543 20 -390 C
ATOM 5568 CG PHE C 121 0.258 33.845 7.295 1.00 45.95 C
ANISOU 5568 CG PHE C 121 5524 5878 6054 540 -4 -420 C
ATOM 5569 CD1 PHE C 121 -0.869 33.628 6.497 1.00 46.43 C
ANISOU 5569 CD1 PHE C 121 5589 5930 6123 570 -28 -459 C
ATOM 5570 CD2 PHE C 121 0.199 34.828 8.284 1.00 46.54 C
ANISOU 5570 CD2 PHE C 121 5597 5929 6156 508 -6 -414 C
ATOM 5571 CE1 PHE C 121 -2.020 34.391 6.663 1.00 46.78 C
ANISOU 5571 CE1 PHE C 121 5632 5940 6202 570 -53 -489 C
ATOM 5572 CE2 PHE C 121 -0.952 35.596 8.457 1.00 47.35 C
ANISOU 5572 CE2 PHE C 121 5699 5998 6292 507 -29 -448 C
ATOM 5573 CZ PHE C 121 -2.061 35.378 7.646 1.00 47.29 C
ANISOU 5573 CZ PHE C 121 5693 5981 6295 539 -53 -485 C
ATOM 5574 N GLU C 122 1.481 32.515 4.024 1.00 52.73 N
ANISOU 5574 N GLU C 122 6398 6829 6806 618 -2 -388 N
ATOM 5575 CA GLU C 122 0.951 32.487 2.662 1.00 59.04 C
ANISOU 5575 CA GLU C 122 7210 7644 7578 650 -25 -400 C
ATOM 5576 C GLU C 122 -0.562 32.343 2.551 1.00 59.58 C
ANISOU 5576 C GLU C 122 7281 7679 7677 667 -53 -451 C
ATOM 5577 O GLU C 122 -1.141 32.783 1.559 1.00 68.22 O
ANISOU 5577 O GLU C 122 8389 8774 8755 686 -83 -454 O
ATOM 5578 CB GLU C 122 1.639 31.412 1.812 1.00 69.64 C
ANISOU 5578 CB GLU C 122 8548 9029 8881 676 -6 -405 C
ATOM 5579 CG GLU C 122 2.659 31.940 0.809 1.00 76.81 C
ANISOU 5579 CG GLU C 122 9464 9984 9733 677 1 -358 C
ATOM 5580 CD GLU C 122 2.016 32.570 -0.422 1.00 81.79 C
ANISOU 5580 CD GLU C 122 10117 10625 10333 693 -30 -354 C
ATOM 5581 OE1 GLU C 122 1.400 33.655 -0.298 1.00 83.69 O
ANISOU 5581 OE1 GLU C 122 10370 10834 10592 679 -60 -339 O
ATOM 5582 OE2 GLU C 122 2.139 31.984 -1.521 1.00 83.04 O
ANISOU 5582 OE2 GLU C 122 10280 10822 10449 718 -28 -366 O
ATOM 5583 N GLY C 123 -1.204 31.708 3.524 1.00 53.07 N
ANISOU 5583 N GLY C 123 6443 6827 6895 660 -47 -492 N
ATOM 5584 CA GLY C 123 -2.668 31.663 3.524 1.00 51.75 C
ANISOU 5584 CA GLY C 123 6273 6627 6762 671 -73 -542 C
ATOM 5585 C GLY C 123 -3.309 30.462 2.849 1.00 51.00 C
ANISOU 5585 C GLY C 123 6175 6538 6664 702 -80 -586 C
ATOM 5586 O GLY C 123 -3.075 30.173 1.678 1.00 51.89 O
ANISOU 5586 O GLY C 123 6298 6679 6738 729 -88 -582 O
ATOM 5587 N ILE C 124 -4.143 29.777 3.615 1.00 52.20 N
ANISOU 5587 N ILE C 124 6312 6664 6856 696 -78 -630 N
ATOM 5588 CA ILE C 124 -4.816 28.555 3.203 1.00 50.34 C
ANISOU 5588 CA ILE C 124 6071 6426 6628 719 -85 -676 C
ATOM 5589 C ILE C 124 -6.256 28.968 2.884 1.00 47.96 C
ANISOU 5589 C ILE C 124 5768 6099 6355 732 -119 -716 C
ATOM 5590 O ILE C 124 -6.578 30.146 3.019 1.00 46.32 O
ANISOU 5590 O ILE C 124 5562 5875 6160 722 -134 -705 O
ATOM 5591 CB ILE C 124 -4.695 27.521 4.363 1.00 50.16 C
ANISOU 5591 CB ILE C 124 6032 6392 6634 697 -60 -692 C
ATOM 5592 CG1 ILE C 124 -3.844 26.334 3.940 1.00 51.10 C
ANISOU 5592 CG1 ILE C 124 6151 6534 6730 715 -46 -689 C
ATOM 5593 CG2 ILE C 124 -6.030 27.166 5.003 1.00 48.91 C
ANISOU 5593 CG2 ILE C 124 5859 6202 6521 686 -69 -742 C
ATOM 5594 CD1 ILE C 124 -2.385 26.699 3.789 1.00 53.95 C
ANISOU 5594 CD1 ILE C 124 6517 6926 7054 712 -26 -637 C
ATOM 5595 N LEU C 125 -7.120 28.052 2.447 1.00 46.16 N
ANISOU 5595 N LEU C 125 5534 5864 6140 753 -134 -762 N
ATOM 5596 CA LEU C 125 -8.536 28.417 2.306 1.00 46.24 C
ANISOU 5596 CA LEU C 125 5537 5846 6186 761 -166 -803 C
ATOM 5597 C LEU C 125 -9.260 28.422 3.654 1.00 47.48 C
ANISOU 5597 C LEU C 125 5670 5973 6395 730 -153 -833 C
ATOM 5598 O LEU C 125 -9.317 27.403 4.337 1.00 48.59 O
ANISOU 5598 O LEU C 125 5798 6110 6550 714 -132 -852 O
ATOM 5599 CB LEU C 125 -9.284 27.526 1.302 1.00 43.81 C
ANISOU 5599 CB LEU C 125 5230 5540 5874 795 -191 -844 C
ATOM 5600 CG LEU C 125 -10.726 27.985 0.998 1.00 42.12 C
ANISOU 5600 CG LEU C 125 5008 5299 5696 807 -230 -884 C
ATOM 5601 CD1 LEU C 125 -10.764 29.423 0.491 1.00 40.62 C
ANISOU 5601 CD1 LEU C 125 4831 5104 5496 813 -258 -854 C
ATOM 5602 CD2 LEU C 125 -11.448 27.054 0.036 1.00 39.88 C
ANISOU 5602 CD2 LEU C 125 4725 5017 5408 839 -255 -924 C
ATOM 5603 N PHE C 126 -9.808 29.573 4.031 1.00 49.74 N
ANISOU 5603 N PHE C 126 5950 6239 6709 718 -165 -837 N
ATOM 5604 CA PHE C 126 -10.614 29.678 5.243 1.00 52.75 C
ANISOU 5604 CA PHE C 126 6306 6596 7139 689 -153 -873 C
ATOM 5605 C PHE C 126 -12.031 30.068 4.883 1.00 55.63 C
ANISOU 5605 C PHE C 126 6655 6936 7543 706 -188 -922 C
ATOM 5606 O PHE C 126 -12.229 30.858 3.959 1.00 61.70 O
ANISOU 5606 O PHE C 126 7436 7698 8306 732 -224 -912 O
ATOM 5607 CB PHE C 126 -10.068 30.762 6.172 1.00 53.31 C
ANISOU 5607 CB PHE C 126 6376 6662 7216 658 -136 -846 C
ATOM 5608 CG PHE C 126 -8.702 30.483 6.709 1.00 53.53 C
ANISOU 5608 CG PHE C 126 6414 6711 7211 635 -103 -799 C
ATOM 5609 CD1 PHE C 126 -8.530 29.657 7.809 1.00 54.53 C
ANISOU 5609 CD1 PHE C 126 6531 6842 7347 603 -71 -807 C
ATOM 5610 CD2 PHE C 126 -7.584 31.073 6.133 1.00 56.13 C
ANISOU 5610 CD2 PHE C 126 6766 7059 7502 643 -104 -745 C
ATOM 5611 CE1 PHE C 126 -7.264 29.407 8.318 1.00 57.06 C
ANISOU 5611 CE1 PHE C 126 6860 7179 7641 582 -45 -763 C
ATOM 5612 CE2 PHE C 126 -6.311 30.825 6.634 1.00 58.41 C
ANISOU 5612 CE2 PHE C 126 7059 7367 7764 623 -74 -703 C
ATOM 5613 CZ PHE C 126 -6.152 29.991 7.732 1.00 57.21 C
ANISOU 5613 CZ PHE C 126 6896 7215 7624 594 -46 -712 C
ATOM 5614 N PRO C 127 -13.025 29.522 5.607 1.00 57.67 N
ANISOU 5614 N PRO C 127 6888 7181 7844 690 -179 -973 N
ATOM 5615 CA PRO C 127 -14.339 30.186 5.688 1.00 60.94 C
ANISOU 5615 CA PRO C 127 7276 7567 8308 695 -205 -1022 C
ATOM 5616 C PRO C 127 -14.119 31.649 6.133 1.00 66.71 C
ANISOU 5616 C PRO C 127 8008 8286 9054 684 -208 -1005 C
ATOM 5617 O PRO C 127 -13.165 31.891 6.869 1.00 71.02 O
ANISOU 5617 O PRO C 127 8561 8842 9579 657 -178 -971 O
ATOM 5618 CB PRO C 127 -15.057 29.381 6.770 1.00 59.12 C
ANISOU 5618 CB PRO C 127 7017 7334 8111 663 -176 -1068 C
ATOM 5619 CG PRO C 127 -14.459 28.014 6.674 1.00 58.76 C
ANISOU 5619 CG PRO C 127 6984 7307 8035 660 -158 -1052 C
ATOM 5620 CD PRO C 127 -13.034 28.180 6.218 1.00 55.91 C
ANISOU 5620 CD PRO C 127 6655 6965 7623 670 -152 -990 C
ATOM 5621 N LYS C 128 -14.959 32.630 5.772 1.00 73.93 N
ANISOU 5621 N LYS C 128 8910 9173 10004 703 -246 -1030 N
ATOM 5622 CA LYS C 128 -16.355 32.504 5.377 1.00 72.03 C
ANISOU 5622 CA LYS C 128 8645 8913 9809 724 -278 -1087 C
ATOM 5623 C LYS C 128 -17.129 32.252 6.684 1.00 70.14 C
ANISOU 5623 C LYS C 128 8366 8668 9615 690 -245 -1143 C
ATOM 5624 O LYS C 128 -17.862 31.272 6.813 1.00 71.01 O
ANISOU 5624 O LYS C 128 8456 8782 9740 685 -237 -1183 O
ATOM 5625 CB LYS C 128 -16.541 31.409 4.317 1.00 79.28 C
ANISOU 5625 CB LYS C 128 9576 9844 10701 752 -296 -1091 C
ATOM 5626 CG LYS C 128 -17.551 31.720 3.223 1.00 87.19 C
ANISOU 5626 CG LYS C 128 10574 10826 11727 790 -353 -1117 C
ATOM 5627 CD LYS C 128 -18.887 31.046 3.495 1.00 89.31 C
ANISOU 5627 CD LYS C 128 10804 11081 12046 790 -358 -1187 C
ATOM 5628 CE LYS C 128 -19.852 31.229 2.337 1.00 85.95 C
ANISOU 5628 CE LYS C 128 10376 10637 11641 830 -418 -1211 C
ATOM 5629 NZ LYS C 128 -21.099 30.457 2.577 1.00 87.16 N
ANISOU 5629 NZ LYS C 128 10492 10781 11843 828 -420 -1278 N
ATOM 5630 N GLY C 129 -16.918 33.131 7.671 1.00 68.06 N
ANISOU 5630 N GLY C 129 8092 8398 9368 663 -225 -1145 N
ATOM 5631 CA GLY C 129 -17.586 33.013 8.979 1.00 67.22 C
ANISOU 5631 CA GLY C 129 7947 8293 9298 625 -189 -1198 C
ATOM 5632 C GLY C 129 -16.944 33.631 10.222 1.00 65.49 C
ANISOU 5632 C GLY C 129 7726 8082 9075 584 -151 -1187 C
ATOM 5633 O GLY C 129 -16.248 34.646 10.143 1.00 63.54 O
ANISOU 5633 O GLY C 129 7497 7825 8820 590 -163 -1152 O
ATOM 5634 N HIS C 130 -17.184 32.988 11.369 1.00 66.04 N
ANISOU 5634 N HIS C 130 7773 8169 9148 541 -107 -1217 N
ATOM 5635 CA HIS C 130 -16.845 33.496 12.711 1.00 68.12 C
ANISOU 5635 CA HIS C 130 8026 8442 9412 495 -69 -1224 C
ATOM 5636 C HIS C 130 -15.837 32.617 13.422 1.00 65.83 C
ANISOU 5636 C HIS C 130 7757 8181 9072 455 -28 -1179 C
ATOM 5637 O HIS C 130 -16.064 31.419 13.607 1.00 64.07 O
ANISOU 5637 O HIS C 130 7530 7973 8838 437 -11 -1186 O
ATOM 5638 CB HIS C 130 -18.136 33.635 13.538 1.00 71.98 C
ANISOU 5638 CB HIS C 130 8466 8930 9951 473 -52 -1305 C
ATOM 5639 CG HIS C 130 -17.921 33.911 15.018 1.00 75.16 C
ANISOU 5639 CG HIS C 130 8854 9352 10348 418 -5 -1322 C
ATOM 5640 ND1 HIS C 130 -18.289 35.069 15.600 1.00 80.16 N
ANISOU 5640 ND1 HIS C 130 9464 9975 11018 412 -3 -1365 N
ATOM 5641 CD2 HIS C 130 -17.388 33.115 16.035 1.00 74.54 C
ANISOU 5641 CD2 HIS C 130 8784 9306 10231 364 40 -1303 C
ATOM 5642 CE1 HIS C 130 -17.995 35.027 16.915 1.00 77.48 C
ANISOU 5642 CE1 HIS C 130 9116 9661 10658 357 43 -1375 C
ATOM 5643 NE2 HIS C 130 -17.441 33.832 17.179 1.00 76.73 N
ANISOU 5643 NE2 HIS C 130 9042 9593 10516 326 69 -1334 N
ATOM 5644 N TYR C 131 -14.733 33.224 13.858 1.00 63.39 N
ANISOU 5644 N TYR C 131 7470 7878 8736 438 -16 -1134 N
ATOM 5645 CA TYR C 131 -13.620 32.510 14.484 1.00 61.13 C
ANISOU 5645 CA TYR C 131 7206 7616 8402 403 15 -1085 C
ATOM 5646 C TYR C 131 -13.364 32.901 15.935 1.00 60.70 C
ANISOU 5646 C TYR C 131 7142 7576 8343 348 52 -1094 C
ATOM 5647 O TYR C 131 -13.286 34.082 16.265 1.00 63.04 O
ANISOU 5647 O TYR C 131 7434 7863 8656 346 49 -1104 O
ATOM 5648 CB TYR C 131 -12.347 32.765 13.696 1.00 60.53 C
ANISOU 5648 CB TYR C 131 7167 7540 8290 429 -1 -1014 C
ATOM 5649 CG TYR C 131 -12.311 32.100 12.356 1.00 61.25 C
ANISOU 5649 CG TYR C 131 7273 7629 8368 473 -28 -995 C
ATOM 5650 CD1 TYR C 131 -12.989 32.641 11.268 1.00 61.18 C
ANISOU 5650 CD1 TYR C 131 7263 7601 8382 518 -68 -1014 C
ATOM 5651 CD2 TYR C 131 -11.580 30.932 12.166 1.00 61.89 C
ANISOU 5651 CD2 TYR C 131 7372 7727 8414 471 -16 -959 C
ATOM 5652 CE1 TYR C 131 -12.946 32.027 10.029 1.00 62.68 C
ANISOU 5652 CE1 TYR C 131 7469 7793 8554 556 -93 -997 C
ATOM 5653 CE2 TYR C 131 -11.528 30.314 10.932 1.00 59.66 C
ANISOU 5653 CE2 TYR C 131 7103 7445 8117 512 -40 -947 C
ATOM 5654 CZ TYR C 131 -12.213 30.864 9.872 1.00 60.42 C
ANISOU 5654 CZ TYR C 131 7198 7526 8230 554 -77 -966 C
ATOM 5655 OH TYR C 131 -12.166 30.244 8.655 1.00 62.56 O
ANISOU 5655 OH TYR C 131 7484 7801 8482 592 -101 -956 O
ATOM 5656 N ARG C 132 -13.210 31.897 16.788 1.00 62.00 N
ANISOU 5656 N ARG C 132 7306 7764 8485 304 84 -1088 N
ATOM 5657 CA ARG C 132 -12.849 32.098 18.186 1.00 66.28 C
ANISOU 5657 CA ARG C 132 7844 8326 9011 246 120 -1089 C
ATOM 5658 C ARG C 132 -11.505 31.412 18.423 1.00 67.60 C
ANISOU 5658 C ARG C 132 8044 8508 9132 225 130 -1017 C
ATOM 5659 O ARG C 132 -11.245 30.341 17.873 1.00 68.16 O
ANISOU 5659 O ARG C 132 8128 8580 9189 239 122 -989 O
ATOM 5660 CB ARG C 132 -13.918 31.495 19.104 1.00 70.33 C
ANISOU 5660 CB ARG C 132 8326 8857 9538 201 149 -1146 C
ATOM 5661 CG ARG C 132 -13.915 31.988 20.547 1.00 78.04 C
ANISOU 5661 CG ARG C 132 9289 9856 10506 142 186 -1170 C
ATOM 5662 CD ARG C 132 -14.817 33.205 20.754 1.00 85.82 C
ANISOU 5662 CD ARG C 132 10241 10832 11535 151 186 -1241 C
ATOM 5663 NE ARG C 132 -16.199 32.968 20.323 1.00 90.22 N
ANISOU 5663 NE ARG C 132 10762 11381 12135 171 178 -1305 N
ATOM 5664 CZ ARG C 132 -17.203 32.609 21.123 1.00 91.10 C
ANISOU 5664 CZ ARG C 132 10836 11515 12260 130 208 -1365 C
ATOM 5665 NH1 ARG C 132 -17.010 32.443 22.425 1.00 95.29 N
ANISOU 5665 NH1 ARG C 132 11364 12080 12760 64 250 -1371 N
ATOM 5666 NH2 ARG C 132 -18.413 32.419 20.617 1.00 92.09 N
ANISOU 5666 NH2 ARG C 132 10929 11631 12429 154 197 -1421 N
ATOM 5667 N CYS C 133 -10.647 32.038 19.225 1.00 67.01 N
ANISOU 5667 N CYS C 133 7980 8442 9035 194 146 -990 N
ATOM 5668 CA CYS C 133 -9.357 31.458 19.578 1.00 61.37 C
ANISOU 5668 CA CYS C 133 7293 7742 8281 171 155 -924 C
ATOM 5669 C CYS C 133 -8.934 31.897 20.968 1.00 56.61 C
ANISOU 5669 C CYS C 133 6690 7158 7659 112 182 -922 C
ATOM 5670 O CYS C 133 -8.592 33.060 21.166 1.00 58.38 O
ANISOU 5670 O CYS C 133 6916 7376 7887 113 180 -922 O
ATOM 5671 CB CYS C 133 -8.282 31.863 18.558 1.00 66.48 C
ANISOU 5671 CB CYS C 133 7966 8379 8915 216 130 -869 C
ATOM 5672 SG CYS C 133 -6.584 31.439 19.045 1.00 73.77 S
ANISOU 5672 SG CYS C 133 8915 9318 9794 189 140 -790 S
ATOM 5673 N VAL C 134 -8.959 30.982 21.931 1.00 51.06 N
ANISOU 5673 N VAL C 134 5987 6476 6936 59 205 -918 N
ATOM 5674 CA VAL C 134 -8.358 31.283 23.235 1.00 51.55 C
ANISOU 5674 CA VAL C 134 6056 6559 6970 0 228 -903 C
ATOM 5675 C VAL C 134 -6.889 30.883 23.270 1.00 48.71 C
ANISOU 5675 C VAL C 134 5726 6203 6579 -5 219 -825 C
ATOM 5676 O VAL C 134 -6.556 29.698 23.270 1.00 45.01 O
ANISOU 5676 O VAL C 134 5268 5738 6096 -15 216 -791 O
ATOM 5677 CB VAL C 134 -9.124 30.710 24.459 1.00 52.39 C
ANISOU 5677 CB VAL C 134 6145 6692 7065 -65 259 -940 C
ATOM 5678 CG1 VAL C 134 -10.260 31.630 24.859 1.00 54.87 C
ANISOU 5678 CG1 VAL C 134 6427 7013 7406 -74 276 -1020 C
ATOM 5679 CG2 VAL C 134 -9.664 29.323 24.188 1.00 56.55 C
ANISOU 5679 CG2 VAL C 134 6669 7220 7596 -69 256 -939 C
ATOM 5680 N ALA C 135 -6.025 31.900 23.283 1.00 49.08 N
ANISOU 5680 N ALA C 135 5784 6245 6618 2 213 -799 N
ATOM 5681 CA ALA C 135 -4.579 31.728 23.404 1.00 45.15 C
ANISOU 5681 CA ALA C 135 5310 5751 6092 -5 207 -729 C
ATOM 5682 C ALA C 135 -4.155 31.781 24.871 1.00 44.30 C
ANISOU 5682 C ALA C 135 5209 5667 5956 -74 227 -718 C
ATOM 5683 O ALA C 135 -4.120 32.841 25.485 1.00 45.25 O
ANISOU 5683 O ALA C 135 5325 5792 6075 -96 236 -738 O
ATOM 5684 CB ALA C 135 -3.850 32.786 22.591 1.00 42.77 C
ANISOU 5684 CB ALA C 135 5017 5434 5796 37 188 -703 C
ATOM 5685 N GLU C 136 -3.843 30.619 25.425 1.00 43.54 N
ANISOU 5685 N GLU C 136 5121 5582 5838 -111 230 -687 N
ATOM 5686 CA GLU C 136 -3.404 30.517 26.799 1.00 43.77 C
ANISOU 5686 CA GLU C 136 5159 5634 5835 -180 245 -669 C
ATOM 5687 C GLU C 136 -1.868 30.401 26.824 1.00 42.07 C
ANISOU 5687 C GLU C 136 4965 5417 5601 -180 228 -595 C
ATOM 5688 O GLU C 136 -1.304 29.445 26.295 1.00 39.51 O
ANISOU 5688 O GLU C 136 4651 5084 5278 -159 211 -552 O
ATOM 5689 CB GLU C 136 -4.074 29.301 27.433 1.00 45.91 C
ANISOU 5689 CB GLU C 136 5427 5920 6095 -226 256 -679 C
ATOM 5690 CG GLU C 136 -4.191 29.351 28.943 1.00 49.97 C
ANISOU 5690 CG GLU C 136 5943 6465 6576 -308 278 -688 C
ATOM 5691 CD GLU C 136 -5.150 28.303 29.497 1.00 53.21 C
ANISOU 5691 CD GLU C 136 6345 6892 6979 -354 292 -710 C
ATOM 5692 OE1 GLU C 136 -5.013 27.108 29.143 1.00 51.48 O
ANISOU 5692 OE1 GLU C 136 6135 6660 6764 -348 275 -675 O
ATOM 5693 OE2 GLU C 136 -6.040 28.681 30.300 1.00 57.60 O
ANISOU 5693 OE2 GLU C 136 6884 7474 7525 -399 321 -765 O
ATOM 5694 N ALA C 137 -1.201 31.393 27.410 1.00 41.54 N
ANISOU 5694 N ALA C 137 4905 5358 5520 -202 231 -584 N
ATOM 5695 CA ALA C 137 0.258 31.419 27.476 1.00 39.67 C
ANISOU 5695 CA ALA C 137 4685 5120 5268 -204 216 -516 C
ATOM 5696 C ALA C 137 0.730 30.686 28.714 1.00 40.10 C
ANISOU 5696 C ALA C 137 4752 5192 5290 -271 218 -484 C
ATOM 5697 O ALA C 137 0.430 31.093 29.829 1.00 41.23 O
ANISOU 5697 O ALA C 137 4896 5356 5412 -327 234 -508 O
ATOM 5698 CB ALA C 137 0.756 32.846 27.495 1.00 39.16 C
ANISOU 5698 CB ALA C 137 4621 5051 5205 -196 215 -518 C
ATOM 5699 N ILE C 138 1.464 29.596 28.515 1.00 40.77 N
ANISOU 5699 N ILE C 138 4846 5270 5372 -265 199 -430 N
ATOM 5700 CA ILE C 138 1.892 28.754 29.625 1.00 41.58 C
ANISOU 5700 CA ILE C 138 4962 5386 5449 -328 193 -393 C
ATOM 5701 C ILE C 138 3.400 28.783 29.766 1.00 43.45 C
ANISOU 5701 C ILE C 138 5211 5619 5677 -329 171 -327 C
ATOM 5702 O ILE C 138 4.116 28.644 28.771 1.00 45.74 O
ANISOU 5702 O ILE C 138 5497 5893 5987 -274 155 -298 O
ATOM 5703 CB ILE C 138 1.413 27.291 29.465 1.00 41.20 C
ANISOU 5703 CB ILE C 138 4915 5329 5410 -330 183 -386 C
ATOM 5704 CG1 ILE C 138 -0.057 27.149 29.888 1.00 41.10 C
ANISOU 5704 CG1 ILE C 138 4892 5330 5393 -363 207 -446 C
ATOM 5705 CG2 ILE C 138 2.242 26.354 30.330 1.00 41.94 C
ANISOU 5705 CG2 ILE C 138 5024 5425 5484 -380 162 -326 C
ATOM 5706 CD1 ILE C 138 -1.071 27.406 28.798 1.00 39.23 C
ANISOU 5706 CD1 ILE C 138 4636 5081 5188 -305 216 -500 C
ATOM 5707 N ALA C 139 3.862 28.986 31.000 1.00 43.07 N
ANISOU 5707 N ALA C 139 5174 5589 5598 -393 171 -307 N
ATOM 5708 CA ALA C 139 5.268 28.834 31.360 1.00 43.83 C
ANISOU 5708 CA ALA C 139 5282 5685 5686 -407 147 -241 C
ATOM 5709 C ALA C 139 5.583 27.351 31.531 1.00 47.25 C
ANISOU 5709 C ALA C 139 5723 6108 6122 -422 122 -197 C
ATOM 5710 O ALA C 139 5.271 26.755 32.573 1.00 50.28 O
ANISOU 5710 O ALA C 139 6118 6504 6481 -486 119 -189 O
ATOM 5711 CB ALA C 139 5.572 29.590 32.643 1.00 41.95 C
ANISOU 5711 CB ALA C 139 5055 5470 5413 -474 153 -238 C
ATOM 5712 N GLY C 140 6.208 26.765 30.510 1.00 46.43 N
ANISOU 5712 N GLY C 140 5611 5981 6048 -363 102 -168 N
ATOM 5713 CA GLY C 140 6.476 25.326 30.457 1.00 47.28 C
ANISOU 5713 CA GLY C 140 5722 6071 6170 -363 74 -133 C
ATOM 5714 C GLY C 140 7.051 24.657 31.695 1.00 48.98 C
ANISOU 5714 C GLY C 140 5954 6290 6366 -431 49 -83 C
ATOM 5715 O GLY C 140 6.692 23.522 32.001 1.00 52.70 O
ANISOU 5715 O GLY C 140 6431 6750 6840 -456 32 -70 O
ATOM 5716 N ASP C 141 7.935 25.347 32.410 1.00 51.51 N
ANISOU 5716 N ASP C 141 6282 6624 6665 -463 43 -53 N
ATOM 5717 CA ASP C 141 8.630 24.756 33.570 1.00 57.00 C
ANISOU 5717 CA ASP C 141 6993 7322 7340 -527 13 0 C
ATOM 5718 C ASP C 141 7.724 24.501 34.778 1.00 60.05 C
ANISOU 5718 C ASP C 141 7398 7731 7687 -610 22 -12 C
ATOM 5719 O ASP C 141 7.747 23.414 35.359 1.00 60.69 O
ANISOU 5719 O ASP C 141 7491 7803 7763 -651 -4 22 O
ATOM 5720 CB ASP C 141 9.860 25.592 33.985 1.00 56.90 C
ANISOU 5720 CB ASP C 141 6983 7319 7317 -539 2 36 C
ATOM 5721 CG ASP C 141 9.561 27.086 34.095 1.00 57.85 C
ANISOU 5721 CG ASP C 141 7101 7461 7415 -544 36 -5 C
ATOM 5722 OD1 ASP C 141 8.701 27.598 33.342 1.00 57.11 O
ANISOU 5722 OD1 ASP C 141 6996 7368 7333 -505 65 -58 O
ATOM 5723 OD2 ASP C 141 10.204 27.756 34.933 1.00 58.45 O
ANISOU 5723 OD2 ASP C 141 7187 7554 7467 -586 30 13 O
ATOM 5724 N THR C 142 6.926 25.506 35.132 1.00 60.96 N
ANISOU 5724 N THR C 142 7513 7874 7775 -634 60 -65 N
ATOM 5725 CA THR C 142 6.067 25.465 36.309 1.00 60.04 C
ANISOU 5725 CA THR C 142 7410 7789 7614 -715 78 -88 C
ATOM 5726 C THR C 142 4.631 25.108 35.938 1.00 62.47 C
ANISOU 5726 C THR C 142 7706 8099 7929 -708 106 -143 C
ATOM 5727 O THR C 142 3.785 24.898 36.813 1.00 65.81 O
ANISOU 5727 O THR C 142 8136 8548 8318 -774 123 -165 O
ATOM 5728 CB THR C 142 6.053 26.835 37.011 1.00 58.44 C
ANISOU 5728 CB THR C 142 7209 7617 7376 -749 105 -120 C
ATOM 5729 OG1 THR C 142 5.661 27.841 36.071 1.00 55.60 O
ANISOU 5729 OG1 THR C 142 6830 7251 7042 -685 132 -174 O
ATOM 5730 CG2 THR C 142 7.429 27.179 37.571 1.00 56.94 C
ANISOU 5730 CG2 THR C 142 7031 7429 7172 -770 77 -65 C
ATOM 5731 N GLU C 143 4.362 25.067 34.635 1.00 63.87 N
ANISOU 5731 N GLU C 143 7866 8251 8149 -629 110 -168 N
ATOM 5732 CA GLU C 143 3.012 24.859 34.090 1.00 62.69 C
ANISOU 5732 CA GLU C 143 7702 8100 8014 -608 135 -226 C
ATOM 5733 C GLU C 143 1.993 25.918 34.531 1.00 58.12 C
ANISOU 5733 C GLU C 143 7114 7554 7414 -635 178 -296 C
ATOM 5734 O GLU C 143 0.788 25.701 34.428 1.00 55.94 O
ANISOU 5734 O GLU C 143 6826 7286 7142 -641 200 -345 O
ATOM 5735 CB GLU C 143 2.513 23.437 34.369 1.00 67.18 C
ANISOU 5735 CB GLU C 143 8278 8661 8585 -643 118 -206 C
ATOM 5736 CG GLU C 143 3.209 22.372 33.529 1.00 75.78 C
ANISOU 5736 CG GLU C 143 9368 9709 9715 -592 78 -160 C
ATOM 5737 CD GLU C 143 2.626 22.245 32.129 1.00 79.72 C
ANISOU 5737 CD GLU C 143 9847 10185 10256 -511 86 -201 C
ATOM 5738 OE1 GLU C 143 3.351 22.532 31.147 1.00 78.05 O
ANISOU 5738 OE1 GLU C 143 9627 9957 10071 -442 77 -192 O
ATOM 5739 OE2 GLU C 143 1.439 21.860 32.012 1.00 81.35 O
ANISOU 5739 OE2 GLU C 143 10047 10394 10467 -520 102 -241 O
ATOM 5740 N GLU C 144 2.493 27.062 35.000 1.00 57.89 N
ANISOU 5740 N GLU C 144 7087 7541 7364 -649 188 -302 N
ATOM 5741 CA GLU C 144 1.655 28.206 35.368 1.00 59.28 C
ANISOU 5741 CA GLU C 144 7253 7745 7527 -666 226 -372 C
ATOM 5742 C GLU C 144 1.147 28.926 34.131 1.00 55.95 C
ANISOU 5742 C GLU C 144 6809 7301 7147 -586 238 -421 C
ATOM 5743 O GLU C 144 1.809 28.952 33.099 1.00 58.16 O
ANISOU 5743 O GLU C 144 7087 7553 7457 -522 218 -392 O
ATOM 5744 CB GLU C 144 2.424 29.208 36.246 1.00 63.93 C
ANISOU 5744 CB GLU C 144 7853 8354 8084 -705 227 -363 C
ATOM 5745 CG GLU C 144 2.994 28.658 37.551 1.00 69.38 C
ANISOU 5745 CG GLU C 144 8567 9068 8726 -789 213 -314 C
ATOM 5746 CD GLU C 144 1.966 28.464 38.653 1.00 72.35 C
ANISOU 5746 CD GLU C 144 8944 9486 9058 -869 242 -354 C
ATOM 5747 OE1 GLU C 144 0.894 27.884 38.389 1.00 73.18 O
ANISOU 5747 OE1 GLU C 144 9038 9594 9174 -868 259 -388 O
ATOM 5748 OE2 GLU C 144 2.245 28.875 39.801 1.00 77.09 O
ANISOU 5748 OE2 GLU C 144 9559 10120 9611 -937 248 -352 O
ATOM 5749 N LYS C 145 -0.034 29.515 34.240 1.00 54.61 N
ANISOU 5749 N LYS C 145 6621 7147 6978 -593 270 -494 N
ATOM 5750 CA LYS C 145 -0.585 30.309 33.159 1.00 55.04 C
ANISOU 5750 CA LYS C 145 6656 7182 7074 -523 278 -543 C
ATOM 5751 C LYS C 145 -0.110 31.747 33.296 1.00 54.20 C
ANISOU 5751 C LYS C 145 6548 7076 6968 -513 282 -559 C
ATOM 5752 O LYS C 145 -0.263 32.359 34.357 1.00 55.78 O
ANISOU 5752 O LYS C 145 6748 7303 7139 -568 300 -589 O
ATOM 5753 CB LYS C 145 -2.114 30.242 33.170 1.00 59.14 C
ANISOU 5753 CB LYS C 145 7152 7713 7603 -530 306 -617 C
ATOM 5754 CG LYS C 145 -2.657 28.825 33.141 1.00 61.06 C
ANISOU 5754 CG LYS C 145 7397 7958 7845 -549 303 -603 C
ATOM 5755 CD LYS C 145 -4.172 28.795 33.128 1.00 62.27 C
ANISOU 5755 CD LYS C 145 7524 8125 8011 -556 331 -678 C
ATOM 5756 CE LYS C 145 -4.660 27.362 32.982 1.00 65.40 C
ANISOU 5756 CE LYS C 145 7921 8516 8411 -570 323 -659 C
ATOM 5757 NZ LYS C 145 -6.138 27.276 32.801 1.00 70.83 N
ANISOU 5757 NZ LYS C 145 8580 9214 9118 -570 348 -731 N
ATOM 5758 N LEU C 146 0.475 32.270 32.224 1.00 51.89 N
ANISOU 5758 N LEU C 146 6254 6754 6706 -447 264 -540 N
ATOM 5759 CA LEU C 146 0.980 33.643 32.189 1.00 52.18 C
ANISOU 5759 CA LEU C 146 6290 6784 6750 -432 262 -549 C
ATOM 5760 C LEU C 146 -0.118 34.623 31.834 1.00 50.61 C
ANISOU 5760 C LEU C 146 6070 6578 6581 -404 278 -626 C
ATOM 5761 O LEU C 146 -0.401 35.543 32.586 1.00 54.82 O
ANISOU 5761 O LEU C 146 6597 7124 7106 -435 293 -672 O
ATOM 5762 CB LEU C 146 2.100 33.772 31.164 1.00 51.63 C
ANISOU 5762 CB LEU C 146 6228 6688 6701 -376 235 -491 C
ATOM 5763 CG LEU C 146 3.391 33.032 31.475 1.00 51.14 C
ANISOU 5763 CG LEU C 146 6182 6629 6617 -396 214 -414 C
ATOM 5764 CD1 LEU C 146 4.083 32.683 30.170 1.00 50.14 C
ANISOU 5764 CD1 LEU C 146 6054 6479 6517 -330 193 -370 C
ATOM 5765 CD2 LEU C 146 4.278 33.878 32.371 1.00 49.98 C
ANISOU 5765 CD2 LEU C 146 6046 6494 6449 -438 210 -393 C
ATOM 5766 N PHE C 147 -0.716 34.432 30.669 1.00 48.82 N
ANISOU 5766 N PHE C 147 5830 6328 6388 -344 272 -643 N
ATOM 5767 CA PHE C 147 -1.878 35.207 30.268 1.00 49.10 C
ANISOU 5767 CA PHE C 147 5844 6355 6457 -315 283 -717 C
ATOM 5768 C PHE C 147 -2.837 34.376 29.401 1.00 49.28 C
ANISOU 5768 C PHE C 147 5853 6367 6503 -278 283 -739 C
ATOM 5769 O PHE C 147 -2.566 33.216 29.094 1.00 49.84 O
ANISOU 5769 O PHE C 147 5933 6437 6565 -273 274 -696 O
ATOM 5770 CB PHE C 147 -1.456 36.519 29.597 1.00 47.10 C
ANISOU 5770 CB PHE C 147 5589 6073 6232 -270 265 -717 C
ATOM 5771 CG PHE C 147 -0.659 36.341 28.333 1.00 46.79 C
ANISOU 5771 CG PHE C 147 5561 6010 6207 -212 238 -657 C
ATOM 5772 CD1 PHE C 147 0.727 36.403 28.358 1.00 45.32 C
ANISOU 5772 CD1 PHE C 147 5393 5823 6003 -217 223 -589 C
ATOM 5773 CD2 PHE C 147 -1.298 36.134 27.110 1.00 45.54 C
ANISOU 5773 CD2 PHE C 147 5393 5831 6078 -154 228 -672 C
ATOM 5774 CE1 PHE C 147 1.460 36.251 27.192 1.00 44.99 C
ANISOU 5774 CE1 PHE C 147 5358 5764 5972 -166 203 -538 C
ATOM 5775 CE2 PHE C 147 -0.569 35.985 25.943 1.00 43.51 C
ANISOU 5775 CE2 PHE C 147 5145 5557 5828 -104 206 -620 C
ATOM 5776 CZ PHE C 147 0.810 36.045 25.984 1.00 43.44 C
ANISOU 5776 CZ PHE C 147 5152 5551 5800 -110 195 -554 C
ATOM 5777 N CYS C 148 -3.967 34.966 29.034 1.00 51.70 N
ANISOU 5777 N CYS C 148 6136 6665 6843 -251 290 -807 N
ATOM 5778 CA CYS C 148 -4.994 34.264 28.279 1.00 53.00 C
ANISOU 5778 CA CYS C 148 6285 6821 7032 -219 290 -837 C
ATOM 5779 C CYS C 148 -5.810 35.282 27.514 1.00 51.88 C
ANISOU 5779 C CYS C 148 6122 6655 6936 -168 282 -894 C
ATOM 5780 O CYS C 148 -6.361 36.207 28.110 1.00 52.03 O
ANISOU 5780 O CYS C 148 6122 6678 6967 -185 295 -953 O
ATOM 5781 CB CYS C 148 -5.889 33.451 29.215 1.00 57.82 C
ANISOU 5781 CB CYS C 148 6882 7463 7624 -277 319 -874 C
ATOM 5782 SG CYS C 148 -7.028 32.314 28.393 1.00 63.43 S
ANISOU 5782 SG CYS C 148 7575 8165 8359 -248 317 -899 S
ATOM 5783 N LEU C 149 -5.879 35.109 26.196 1.00 51.82 N
ANISOU 5783 N LEU C 149 6115 6620 6953 -106 258 -877 N
ATOM 5784 CA LEU C 149 -6.570 36.058 25.321 1.00 52.81 C
ANISOU 5784 CA LEU C 149 6223 6716 7123 -52 240 -919 C
ATOM 5785 C LEU C 149 -7.752 35.430 24.602 1.00 55.44 C
ANISOU 5785 C LEU C 149 6537 7042 7483 -21 237 -960 C
ATOM 5786 O LEU C 149 -7.637 34.343 24.030 1.00 55.85 O
ANISOU 5786 O LEU C 149 6599 7095 7525 -6 230 -927 O
ATOM 5787 CB LEU C 149 -5.598 36.664 24.306 1.00 49.65 C
ANISOU 5787 CB LEU C 149 5843 6290 6729 -5 209 -864 C
ATOM 5788 CG LEU C 149 -4.444 37.458 24.918 1.00 48.87 C
ANISOU 5788 CG LEU C 149 5761 6194 6611 -31 207 -826 C
ATOM 5789 CD1 LEU C 149 -3.630 38.161 23.850 1.00 46.48 C
ANISOU 5789 CD1 LEU C 149 5474 5866 6320 15 177 -777 C
ATOM 5790 CD2 LEU C 149 -4.991 38.466 25.913 1.00 49.89 C
ANISOU 5790 CD2 LEU C 149 5873 6326 6754 -63 222 -890 C
ATOM 5791 N ASN C 150 -8.890 36.118 24.652 1.00 57.61 N
ANISOU 5791 N ASN C 150 6782 7309 7796 -12 240 -1035 N
ATOM 5792 CA ASN C 150 -10.085 35.695 23.929 1.00 59.00 C
ANISOU 5792 CA ASN C 150 6935 7475 8006 21 233 -1080 C
ATOM 5793 C ASN C 150 -10.141 36.440 22.601 1.00 57.37 C
ANISOU 5793 C ASN C 150 6731 7230 7835 90 193 -1074 C
ATOM 5794 O ASN C 150 -10.605 37.577 22.533 1.00 59.47 O
ANISOU 5794 O ASN C 150 6981 7476 8139 108 180 -1117 O
ATOM 5795 CB ASN C 150 -11.350 35.936 24.770 1.00 62.15 C
ANISOU 5795 CB ASN C 150 7295 7890 8428 -9 260 -1168 C
ATOM 5796 CG ASN C 150 -12.516 35.043 24.358 1.00 64.82 C
ANISOU 5796 CG ASN C 150 7609 8231 8786 1 264 -1207 C
ATOM 5797 OD1 ASN C 150 -12.769 34.844 23.169 1.00 68.64 O
ANISOU 5797 OD1 ASN C 150 8094 8689 9294 55 234 -1197 O
ATOM 5798 ND2 ASN C 150 -13.240 34.509 25.347 1.00 62.97 N
ANISOU 5798 ND2 ASN C 150 7352 8031 8541 -53 300 -1252 N
ATOM 5799 N PHE C 151 -9.625 35.796 21.557 1.00 55.14 N
ANISOU 5799 N PHE C 151 6471 6939 7540 126 171 -1018 N
ATOM 5800 CA PHE C 151 -9.575 36.371 20.219 1.00 54.64 C
ANISOU 5800 CA PHE C 151 6416 6845 7500 187 132 -1001 C
ATOM 5801 C PHE C 151 -10.852 36.091 19.433 1.00 60.31 C
ANISOU 5801 C PHE C 151 7110 7548 8254 224 116 -1051 C
ATOM 5802 O PHE C 151 -11.547 35.090 19.669 1.00 59.91 O
ANISOU 5802 O PHE C 151 7046 7513 8203 208 133 -1079 O
ATOM 5803 CB PHE C 151 -8.382 35.818 19.441 1.00 52.67 C
ANISOU 5803 CB PHE C 151 6198 6597 7214 207 119 -921 C
ATOM 5804 CG PHE C 151 -7.103 36.577 19.651 1.00 51.01 C
ANISOU 5804 CG PHE C 151 6009 6386 6983 197 116 -868 C
ATOM 5805 CD1 PHE C 151 -6.158 36.132 20.570 1.00 49.33 C
ANISOU 5805 CD1 PHE C 151 5810 6197 6734 152 139 -830 C
ATOM 5806 CD2 PHE C 151 -6.831 37.728 18.910 1.00 49.61 C
ANISOU 5806 CD2 PHE C 151 5840 6183 6824 230 86 -851 C
ATOM 5807 CE1 PHE C 151 -4.972 36.823 20.753 1.00 48.67 C
ANISOU 5807 CE1 PHE C 151 5744 6112 6633 141 135 -780 C
ATOM 5808 CE2 PHE C 151 -5.647 38.424 19.092 1.00 47.68 C
ANISOU 5808 CE2 PHE C 151 5615 5939 6562 218 82 -800 C
ATOM 5809 CZ PHE C 151 -4.716 37.970 20.014 1.00 48.63 C
ANISOU 5809 CZ PHE C 151 5745 6083 6646 174 107 -766 C
ATOM 5810 N THR C 152 -11.145 36.984 18.492 1.00 61.47 N
ANISOU 5810 N THR C 152 7255 7664 8434 272 79 -1060 N
ATOM 5811 CA THR C 152 -12.307 36.858 17.630 1.00 61.60 C
ANISOU 5811 CA THR C 152 7252 7662 8489 312 55 -1103 C
ATOM 5812 C THR C 152 -11.967 37.404 16.244 1.00 60.56 C
ANISOU 5812 C THR C 152 7142 7503 8363 366 8 -1063 C
ATOM 5813 O THR C 152 -11.552 38.555 16.103 1.00 60.29 O
ANISOU 5813 O THR C 152 7116 7448 8341 377 -12 -1046 O
ATOM 5814 CB THR C 152 -13.536 37.573 18.245 1.00 66.57 C
ANISOU 5814 CB THR C 152 7840 8281 9171 305 59 -1190 C
ATOM 5815 OG1 THR C 152 -13.873 36.954 19.495 1.00 66.54 O
ANISOU 5815 OG1 THR C 152 7816 8310 9153 250 106 -1227 O
ATOM 5816 CG2 THR C 152 -14.750 37.501 17.322 1.00 67.28 C
ANISOU 5816 CG2 THR C 152 7906 8349 9306 349 28 -1235 C
ATOM 5817 N ILE C 153 -12.119 36.556 15.230 1.00 60.43 N
ANISOU 5817 N ILE C 153 7135 7489 8335 398 -7 -1045 N
ATOM 5818 CA ILE C 153 -11.901 36.951 13.839 1.00 58.62 C
ANISOU 5818 CA ILE C 153 6926 7240 8105 447 -51 -1009 C
ATOM 5819 C ILE C 153 -13.195 36.765 13.056 1.00 57.48 C
ANISOU 5819 C ILE C 153 6761 7078 7998 483 -80 -1059 C
ATOM 5820 O ILE C 153 -13.873 35.754 13.213 1.00 57.90 O
ANISOU 5820 O ILE C 153 6798 7144 8055 476 -64 -1092 O
ATOM 5821 CB ILE C 153 -10.790 36.112 13.163 1.00 59.82 C
ANISOU 5821 CB ILE C 153 7111 7413 8202 456 -47 -940 C
ATOM 5822 CG1 ILE C 153 -9.501 36.104 13.995 1.00 63.47 C
ANISOU 5822 CG1 ILE C 153 7590 7896 8628 418 -17 -891 C
ATOM 5823 CG2 ILE C 153 -10.493 36.627 11.761 1.00 59.43 C
ANISOU 5823 CG2 ILE C 153 7084 7351 8145 500 -90 -900 C
ATOM 5824 CD1 ILE C 153 -9.296 34.855 14.828 1.00 64.32 C
ANISOU 5824 CD1 ILE C 153 7694 8030 8712 382 20 -891 C
ATOM 5825 N ILE C 154 -13.540 37.749 12.232 0.50 56.22 N
ANISOU 5825 N ILE C 154 6603 6888 7870 520 -126 -1061 N
ATOM 5826 CA ILE C 154 -14.636 37.607 11.283 0.50 57.22 C
ANISOU 5826 CA ILE C 154 6716 6996 8028 559 -164 -1096 C
ATOM 5827 C ILE C 154 -14.053 37.771 9.883 0.50 57.67 C
ANISOU 5827 C ILE C 154 6809 7047 8055 596 -205 -1036 C
ATOM 5828 O ILE C 154 -13.457 38.802 9.572 0.50 56.92 O
ANISOU 5828 O ILE C 154 6732 6935 7958 603 -229 -996 O
ATOM 5829 CB ILE C 154 -15.770 38.625 11.551 0.50 58.77 C
ANISOU 5829 CB ILE C 154 6876 7158 8295 570 -189 -1164 C
ATOM 5830 CG1 ILE C 154 -16.392 38.380 12.934 1.00 62.35 C
ANISOU 5830 CG1 ILE C 154 7290 7625 8771 530 -142 -1230 C
ATOM 5831 CG2 ILE C 154 -16.853 38.533 10.484 1.00 54.68 C
ANISOU 5831 CG2 ILE C 154 6345 6617 7811 614 -236 -1194 C
ATOM 5832 CD1 ILE C 154 -17.155 39.563 13.499 0.50 60.86 C
ANISOU 5832 CD1 ILE C 154 7066 7408 8647 531 -155 -1293 C
ATOM 5833 N HIS C 155 -14.221 36.742 9.054 1.00 59.90 N
ANISOU 5833 N HIS C 155 7101 7345 8314 617 -211 -1029 N
ATOM 5834 CA HIS C 155 -13.620 36.694 7.718 1.00 65.18 C
ANISOU 5834 CA HIS C 155 7803 8018 8942 648 -243 -973 C
ATOM 5835 C HIS C 155 -14.638 36.834 6.624 1.00 66.94 C
ANISOU 5835 C HIS C 155 8021 8219 9191 689 -295 -998 C
ATOM 5836 O HIS C 155 -15.662 36.147 6.631 1.00 65.38 O
ANISOU 5836 O HIS C 155 7799 8019 9021 697 -296 -1052 O
ATOM 5837 CB HIS C 155 -12.831 35.392 7.545 1.00 69.37 C
ANISOU 5837 CB HIS C 155 8352 8586 9417 642 -211 -941 C
ATOM 5838 CG HIS C 155 -12.006 35.325 6.271 1.00 73.38 C
ANISOU 5838 CG HIS C 155 8895 9109 9874 668 -232 -882 C
ATOM 5839 ND1 HIS C 155 -12.196 34.375 5.334 1.00 75.73 N
ANISOU 5839 ND1 HIS C 155 9202 9423 10148 694 -243 -885 N
ATOM 5840 CD2 HIS C 155 -10.956 36.124 5.811 1.00 74.99 C
ANISOU 5840 CD2 HIS C 155 9127 9319 10046 669 -243 -819 C
ATOM 5841 CE1 HIS C 155 -11.319 34.555 4.324 1.00 77.06 C
ANISOU 5841 CE1 HIS C 155 9401 9609 10268 710 -258 -830 C
ATOM 5842 NE2 HIS C 155 -10.563 35.628 4.615 1.00 76.57 N
ANISOU 5842 NE2 HIS C 155 9350 9541 10200 694 -257 -788 N
TER 5843 HIS C 155
ATOM 5844 N PRO B 27 -18.558 -37.811 -12.203 1.00114.26 N
ANISOU 5844 N PRO B 27 14453 14140 14820 114 -175 182 N
ATOM 5845 CA PRO B 27 -18.135 -37.559 -13.576 1.00113.21 C
ANISOU 5845 CA PRO B 27 14354 13993 14665 122 -188 173 C
ATOM 5846 C PRO B 27 -17.070 -36.455 -13.662 1.00110.96 C
ANISOU 5846 C PRO B 27 14076 13724 14358 137 -182 183 C
ATOM 5847 O PRO B 27 -15.873 -36.754 -13.692 1.00104.52 O
ANISOU 5847 O PRO B 27 13276 12908 13528 147 -159 198 O
ATOM 5848 CB PRO B 27 -19.438 -37.128 -14.271 1.00111.62 C
ANISOU 5848 CB PRO B 27 14151 13786 14471 112 -223 149 C
ATOM 5849 CG PRO B 27 -20.554 -37.633 -13.403 1.00110.67 C
ANISOU 5849 CG PRO B 27 14001 13668 14380 97 -226 145 C
ATOM 5850 CD PRO B 27 -19.977 -38.195 -12.129 1.00113.89 C
ANISOU 5850 CD PRO B 27 14390 14085 14797 98 -194 166 C
ATOM 5851 N CYS B 28 -17.516 -35.198 -13.691 1.00111.58 N
ANISOU 5851 N CYS B 28 14144 13818 14434 138 -202 176 N
ATOM 5852 CA CYS B 28 -16.639 -34.032 -13.796 1.00109.27 C
ANISOU 5852 CA CYS B 28 13856 13540 14121 151 -198 184 C
ATOM 5853 C CYS B 28 -16.811 -33.114 -12.589 1.00109.95 C
ANISOU 5853 C CYS B 28 13907 13652 14216 150 -195 191 C
ATOM 5854 O CYS B 28 -17.002 -33.580 -11.464 1.00113.74 O
ANISOU 5854 O CYS B 28 14362 14141 14712 143 -182 200 O
ATOM 5855 CB CYS B 28 -16.969 -33.246 -15.066 1.00111.85 C
ANISOU 5855 CB CYS B 28 14205 13859 14433 155 -225 168 C
ATOM 5856 SG CYS B 28 -16.487 -34.045 -16.607 1.00122.72 S
ANISOU 5856 SG CYS B 28 15627 15206 15791 161 -228 160 S
ATOM 5857 N ILE B 29 -16.719 -31.808 -12.836 1.00105.57 N
ANISOU 5857 N ILE B 29 13352 13109 13649 156 -207 188 N
ATOM 5858 CA ILE B 29 -17.087 -30.786 -11.860 1.00 97.86 C
ANISOU 5858 CA ILE B 29 12344 12156 12681 154 -210 191 C
ATOM 5859 C ILE B 29 -18.052 -29.809 -12.534 1.00 95.71 C
ANISOU 5859 C ILE B 29 12073 11883 12408 153 -241 173 C
ATOM 5860 O ILE B 29 -17.891 -29.465 -13.707 1.00 91.02 O
ANISOU 5860 O ILE B 29 11505 11278 11798 160 -254 165 O
ATOM 5861 CB ILE B 29 -15.864 -30.026 -11.300 1.00 96.63 C
ANISOU 5861 CB ILE B 29 12184 12018 12510 165 -190 207 C
ATOM 5862 CG1 ILE B 29 -14.762 -30.997 -10.852 1.00 96.25 C
ANISOU 5862 CG1 ILE B 29 12140 11969 12459 169 -161 224 C
ATOM 5863 CG2 ILE B 29 -16.281 -29.139 -10.133 1.00 98.68 C
ANISOU 5863 CG2 ILE B 29 12410 12302 12781 161 -191 210 C
ATOM 5864 CD1 ILE B 29 -13.409 -30.347 -10.628 1.00 94.58 C
ANISOU 5864 CD1 ILE B 29 11932 11772 12230 181 -142 239 C
ATOM 5865 N GLU B 30 -19.056 -29.373 -11.781 1.00 97.03 N
ANISOU 5865 N GLU B 30 12210 12061 12592 145 -251 169 N
ATOM 5866 CA GLU B 30 -20.108 -28.506 -12.295 1.00 98.16 C
ANISOU 5866 CA GLU B 30 12349 12205 12739 143 -280 153 C
ATOM 5867 C GLU B 30 -20.041 -27.117 -11.650 1.00103.14 C
ANISOU 5867 C GLU B 30 12961 12858 13367 147 -280 157 C
ATOM 5868 O GLU B 30 -20.409 -26.952 -10.482 1.00106.61 O
ANISOU 5868 O GLU B 30 13371 13313 13822 141 -273 162 O
ATOM 5869 CB GLU B 30 -21.465 -29.161 -12.029 1.00 97.90 C
ANISOU 5869 CB GLU B 30 12298 12166 12731 128 -294 142 C
ATOM 5870 CG GLU B 30 -22.680 -28.393 -12.526 1.00 98.40 C
ANISOU 5870 CG GLU B 30 12354 12230 12801 125 -325 126 C
ATOM 5871 CD GLU B 30 -23.937 -29.247 -12.542 1.00 97.62 C
ANISOU 5871 CD GLU B 30 12244 12121 12726 111 -340 113 C
ATOM 5872 OE1 GLU B 30 -23.822 -30.489 -12.643 1.00 96.18 O
ANISOU 5872 OE1 GLU B 30 12071 11924 12549 105 -331 114 O
ATOM 5873 OE2 GLU B 30 -25.044 -28.676 -12.457 1.00 94.76 O
ANISOU 5873 OE2 GLU B 30 11862 11764 12376 106 -361 103 O
ATOM 5874 N VAL B 31 -19.562 -26.129 -12.406 1.00100.08 N
ANISOU 5874 N VAL B 31 12592 12472 12961 158 -287 155 N
ATOM 5875 CA VAL B 31 -19.522 -24.741 -11.923 1.00 93.04 C
ANISOU 5875 CA VAL B 31 11685 11599 12066 162 -288 157 C
ATOM 5876 C VAL B 31 -20.855 -24.035 -12.122 1.00 89.51 C
ANISOU 5876 C VAL B 31 11225 11154 11630 158 -315 143 C
ATOM 5877 O VAL B 31 -21.415 -23.496 -11.173 1.00 88.55 O
ANISOU 5877 O VAL B 31 11075 11047 11522 154 -315 144 O
ATOM 5878 CB VAL B 31 -18.392 -23.891 -12.554 1.00 90.93 C
ANISOU 5878 CB VAL B 31 11440 11333 11774 176 -281 162 C
ATOM 5879 CG1 VAL B 31 -17.341 -23.543 -11.510 1.00 90.26 C
ANISOU 5879 CG1 VAL B 31 11341 11266 11685 179 -255 178 C
ATOM 5880 CG2 VAL B 31 -17.778 -24.583 -13.763 1.00 91.54 C
ANISOU 5880 CG2 VAL B 31 11554 11390 11836 182 -281 160 C
ATOM 5881 N VAL B 32 -21.349 -24.030 -13.356 1.00 88.01 N
ANISOU 5881 N VAL B 32 11057 10949 11434 161 -338 130 N
ATOM 5882 CA VAL B 32 -22.651 -23.448 -13.660 1.00 91.18 C
ANISOU 5882 CA VAL B 32 11447 11350 11845 158 -366 115 C
ATOM 5883 C VAL B 32 -23.520 -24.508 -14.333 1.00 96.34 C
ANISOU 5883 C VAL B 32 12108 11986 12508 149 -384 103 C
ATOM 5884 O VAL B 32 -23.175 -24.985 -15.416 1.00 98.63 O
ANISOU 5884 O VAL B 32 12428 12260 12784 153 -390 98 O
ATOM 5885 CB VAL B 32 -22.542 -22.204 -14.570 1.00 89.09 C
ANISOU 5885 CB VAL B 32 11200 11086 11562 170 -380 110 C
ATOM 5886 CG1 VAL B 32 -23.891 -21.500 -14.672 1.00 86.54 C
ANISOU 5886 CG1 VAL B 32 10861 10767 11251 167 -406 98 C
ATOM 5887 CG2 VAL B 32 -21.478 -21.243 -14.058 1.00 86.22 C
ANISOU 5887 CG2 VAL B 32 10835 10737 11186 178 -360 122 C
ATOM 5888 N PRO B 33 -24.643 -24.891 -13.687 1.00100.29 N
ANISOU 5888 N PRO B 33 12581 12489 13033 137 -392 97 N
ATOM 5889 CA PRO B 33 -25.541 -25.924 -14.222 1.00102.25 C
ANISOU 5889 CA PRO B 33 12833 12722 13294 127 -409 84 C
ATOM 5890 C PRO B 33 -26.023 -25.614 -15.640 1.00101.82 C
ANISOU 5890 C PRO B 33 12802 12656 13228 132 -439 69 C
ATOM 5891 O PRO B 33 -26.309 -24.455 -15.954 1.00101.81 O
ANISOU 5891 O PRO B 33 12800 12662 13220 140 -453 65 O
ATOM 5892 CB PRO B 33 -26.718 -25.910 -13.238 1.00102.23 C
ANISOU 5892 CB PRO B 33 12793 12729 13320 115 -415 82 C
ATOM 5893 CG PRO B 33 -26.126 -25.418 -11.961 1.00100.06 C
ANISOU 5893 CG PRO B 33 12497 12473 13048 117 -390 97 C
ATOM 5894 CD PRO B 33 -25.102 -24.398 -12.373 1.00100.28 C
ANISOU 5894 CD PRO B 33 12544 12506 13050 132 -384 103 C
ATOM 5895 N ASN B 34 -26.087 -26.648 -16.480 1.00103.02 N
ANISOU 5895 N ASN B 34 12976 12789 13377 128 -446 60 N
ATOM 5896 CA ASN B 34 -26.489 -26.531 -17.895 1.00107.45 C
ANISOU 5896 CA ASN B 34 13562 13337 13925 132 -474 45 C
ATOM 5897 C ASN B 34 -25.622 -25.599 -18.767 1.00104.88 C
ANISOU 5897 C ASN B 34 13267 13011 13570 150 -475 48 C
ATOM 5898 O ASN B 34 -25.942 -25.377 -19.939 1.00 98.89 O
ANISOU 5898 O ASN B 34 12530 12243 12798 155 -498 36 O
ATOM 5899 CB ASN B 34 -27.980 -26.148 -18.024 1.00110.74 C
ANISOU 5899 CB ASN B 34 13959 13757 14358 126 -505 30 C
ATOM 5900 CG ASN B 34 -28.924 -27.251 -17.563 1.00113.72 C
ANISOU 5900 CG ASN B 34 14315 14128 14764 108 -510 23 C
ATOM 5901 OD1 ASN B 34 -28.818 -28.403 -17.988 1.00116.33 O
ANISOU 5901 OD1 ASN B 34 14661 14442 15094 101 -508 18 O
ATOM 5902 ND2 ASN B 34 -29.874 -26.890 -16.705 1.00112.50 N
ANISOU 5902 ND2 ASN B 34 14125 13986 14632 101 -515 22 N
ATOM 5903 N ILE B 35 -24.534 -25.067 -18.202 1.00104.76 N
ANISOU 5903 N ILE B 35 13251 13006 13544 158 -450 63 N
ATOM 5904 CA ILE B 35 -23.723 -24.033 -18.873 1.00102.27 C
ANISOU 5904 CA ILE B 35 12959 12693 13204 174 -448 67 C
ATOM 5905 C ILE B 35 -22.199 -24.298 -18.887 1.00 98.50 C
ANISOU 5905 C ILE B 35 12503 12213 12710 182 -419 81 C
ATOM 5906 O ILE B 35 -21.591 -24.302 -19.960 1.00 96.56 O
ANISOU 5906 O ILE B 35 12290 11954 12442 192 -421 80 O
ATOM 5907 CB ILE B 35 -24.056 -22.606 -18.339 1.00106.82 C
ANISOU 5907 CB ILE B 35 13514 13288 13784 179 -453 70 C
ATOM 5908 CG1 ILE B 35 -25.479 -22.189 -18.751 1.00106.65 C
ANISOU 5908 CG1 ILE B 35 13481 13267 13772 176 -485 55 C
ATOM 5909 CG2 ILE B 35 -23.040 -21.573 -18.823 1.00107.16 C
ANISOU 5909 CG2 ILE B 35 13579 13334 13802 195 -444 77 C
ATOM 5910 CD1 ILE B 35 -25.930 -20.832 -18.239 1.00102.69 C
ANISOU 5910 CD1 ILE B 35 12957 12782 13276 181 -491 56 C
ATOM 5911 N THR B 36 -21.586 -24.512 -17.719 1.00 95.84 N
ANISOU 5911 N THR B 36 12146 11886 12380 178 -393 96 N
ATOM 5912 CA THR B 36 -20.116 -24.630 -17.628 1.00 94.38 C
ANISOU 5912 CA THR B 36 11978 11701 12180 186 -365 111 C
ATOM 5913 C THR B 36 -19.624 -25.797 -16.756 1.00 92.07 C
ANISOU 5913 C THR B 36 11675 11409 11899 178 -341 122 C
ATOM 5914 O THR B 36 -20.028 -25.931 -15.596 1.00 90.67 O
ANISOU 5914 O THR B 36 11467 11244 11740 169 -333 126 O
ATOM 5915 CB THR B 36 -19.467 -23.304 -17.159 1.00 95.64 C
ANISOU 5915 CB THR B 36 12129 11878 12331 195 -354 120 C
ATOM 5916 OG1 THR B 36 -19.960 -22.220 -17.956 1.00 93.37 O
ANISOU 5916 OG1 THR B 36 11851 11591 12034 203 -376 111 O
ATOM 5917 CG2 THR B 36 -17.943 -23.355 -17.287 1.00 93.76 C
ANISOU 5917 CG2 THR B 36 11911 11639 12075 205 -328 134 C
ATOM 5918 N TYR B 37 -18.740 -26.620 -17.326 1.00 92.82 N
ANISOU 5918 N TYR B 37 11796 11489 11980 183 -327 126 N
ATOM 5919 CA TYR B 37 -18.231 -27.832 -16.665 1.00 92.16 C
ANISOU 5919 CA TYR B 37 11708 11402 11905 177 -304 137 C
ATOM 5920 C TYR B 37 -16.707 -27.978 -16.737 1.00 90.73 C
ANISOU 5920 C TYR B 37 11546 11220 11707 188 -277 152 C
ATOM 5921 O TYR B 37 -16.079 -27.607 -17.734 1.00 86.81 O
ANISOU 5921 O TYR B 37 11078 10715 11190 199 -278 151 O
ATOM 5922 CB TYR B 37 -18.908 -29.087 -17.238 1.00 92.51 C
ANISOU 5922 CB TYR B 37 11764 11426 11958 168 -315 125 C
ATOM 5923 CG TYR B 37 -20.388 -29.184 -16.927 1.00 92.54 C
ANISOU 5923 CG TYR B 37 11744 11432 11985 155 -337 112 C
ATOM 5924 CD1 TYR B 37 -21.336 -28.553 -17.736 1.00 93.34 C
ANISOU 5924 CD1 TYR B 37 11850 11530 12084 155 -368 96 C
ATOM 5925 CD2 TYR B 37 -20.843 -29.902 -15.823 1.00 93.45 C
ANISOU 5925 CD2 TYR B 37 11831 11552 12123 143 -327 117 C
ATOM 5926 CE1 TYR B 37 -22.691 -28.631 -17.450 1.00 94.09 C
ANISOU 5926 CE1 TYR B 37 11921 11626 12200 143 -388 84 C
ATOM 5927 CE2 TYR B 37 -22.198 -29.989 -15.535 1.00 95.78 C
ANISOU 5927 CE2 TYR B 37 12103 11847 12439 131 -346 105 C
ATOM 5928 CZ TYR B 37 -23.117 -29.349 -16.350 1.00 94.29 C
ANISOU 5928 CZ TYR B 37 11918 11656 12249 131 -377 89 C
ATOM 5929 OH TYR B 37 -24.462 -29.425 -16.070 1.00 90.30 O
ANISOU 5929 OH TYR B 37 11389 11153 11767 119 -396 77 O
ATOM 5930 N GLN B 38 -16.132 -28.530 -15.668 1.00 94.64 N
ANISOU 5930 N GLN B 38 12024 11724 12210 185 -252 167 N
ATOM 5931 CA GLN B 38 -14.684 -28.738 -15.541 1.00 96.41 C
ANISOU 5931 CA GLN B 38 12260 11951 12421 194 -224 184 C
ATOM 5932 C GLN B 38 -14.309 -30.222 -15.512 1.00 97.52 C
ANISOU 5932 C GLN B 38 12410 12076 12565 191 -207 190 C
ATOM 5933 O GLN B 38 -14.629 -30.934 -14.555 1.00 97.23 O
ANISOU 5933 O GLN B 38 12352 12045 12546 182 -198 195 O
ATOM 5934 CB GLN B 38 -14.150 -28.043 -14.281 1.00 92.79 C
ANISOU 5934 CB GLN B 38 11773 11516 11966 195 -207 198 C
ATOM 5935 CG GLN B 38 -13.231 -26.862 -14.540 1.00 91.87 C
ANISOU 5935 CG GLN B 38 11665 11409 11831 207 -201 204 C
ATOM 5936 CD GLN B 38 -11.796 -27.289 -14.778 1.00 94.28 C
ANISOU 5936 CD GLN B 38 11989 11710 12120 216 -176 218 C
ATOM 5937 OE1 GLN B 38 -11.453 -27.799 -15.845 1.00 95.95 O
ANISOU 5937 OE1 GLN B 38 12232 11903 12321 222 -177 215 O
ATOM 5938 NE2 GLN B 38 -10.947 -27.079 -13.781 1.00 95.43 N
ANISOU 5938 NE2 GLN B 38 12116 11873 12266 218 -155 233 N
ATOM 5939 N CYS B 39 -13.623 -30.674 -16.560 1.00 97.71 N
ANISOU 5939 N CYS B 39 12469 12083 12572 199 -202 190 N
ATOM 5940 CA CYS B 39 -13.204 -32.070 -16.674 1.00 99.42 C
ANISOU 5940 CA CYS B 39 12700 12283 12791 198 -186 196 C
ATOM 5941 C CYS B 39 -11.698 -32.158 -16.910 1.00 94.37 C
ANISOU 5941 C CYS B 39 12080 11643 12133 211 -160 212 C
ATOM 5942 O CYS B 39 -11.240 -32.560 -17.981 1.00 97.30 O
ANISOU 5942 O CYS B 39 12484 11995 12490 218 -159 209 O
ATOM 5943 CB CYS B 39 -13.983 -32.778 -17.792 1.00106.98 C
ANISOU 5943 CB CYS B 39 13681 13216 13748 193 -206 178 C
ATOM 5944 SG CYS B 39 -15.777 -32.516 -17.749 1.00125.04 S
ANISOU 5944 SG CYS B 39 15948 15504 16054 178 -240 157 S
ATOM 5945 N MET B 40 -10.935 -31.779 -15.891 1.00 87.05 N
ANISOU 5945 N MET B 40 11131 10735 11207 215 -140 228 N
ATOM 5946 CA MET B 40 -9.484 -31.712 -15.992 1.00 86.78 C
ANISOU 5946 CA MET B 40 11111 10704 11157 227 -116 244 C
ATOM 5947 C MET B 40 -8.826 -32.836 -15.203 1.00 85.06 C
ANISOU 5947 C MET B 40 10884 10487 10946 227 -89 261 C
ATOM 5948 O MET B 40 -9.289 -33.187 -14.117 1.00 87.08 O
ANISOU 5948 O MET B 40 11112 10753 11218 219 -85 265 O
ATOM 5949 CB MET B 40 -8.995 -30.355 -15.481 1.00 89.23 C
ANISOU 5949 CB MET B 40 11404 11037 11462 232 -114 251 C
ATOM 5950 CG MET B 40 -7.554 -30.022 -15.837 1.00 89.37 C
ANISOU 5950 CG MET B 40 11438 11056 11461 246 -94 264 C
ATOM 5951 SD MET B 40 -6.974 -28.488 -15.086 1.00 90.40 S
ANISOU 5951 SD MET B 40 11545 11214 11586 250 -89 272 S
ATOM 5952 CE MET B 40 -8.068 -27.287 -15.848 1.00 85.57 C
ANISOU 5952 CE MET B 40 10939 10600 10972 247 -121 251 C
ATOM 5953 N ASP B 41 -7.748 -33.391 -15.759 1.00 84.93 N
ANISOU 5953 N ASP B 41 10893 10459 10916 237 -70 271 N
ATOM 5954 CA ASP B 41 -6.952 -34.439 -15.107 1.00 86.90 C
ANISOU 5954 CA ASP B 41 11138 10709 11170 240 -42 289 C
ATOM 5955 C ASP B 41 -7.807 -35.648 -14.689 1.00 90.85 C
ANISOU 5955 C ASP B 41 11630 11199 11688 229 -42 285 C
ATOM 5956 O ASP B 41 -7.584 -36.248 -13.632 1.00 94.40 O
ANISOU 5956 O ASP B 41 12059 11659 12150 227 -23 299 O
ATOM 5957 CB ASP B 41 -6.174 -33.855 -13.913 1.00 86.92 C
ANISOU 5957 CB ASP B 41 11111 10739 11173 244 -24 307 C
ATOM 5958 CG ASP B 41 -5.020 -34.740 -13.460 1.00 89.10 C
ANISOU 5958 CG ASP B 41 11388 11016 11446 252 6 328 C
ATOM 5959 OD1 ASP B 41 -4.643 -35.672 -14.203 1.00 91.67 O
ANISOU 5959 OD1 ASP B 41 11741 11322 11767 257 16 330 O
ATOM 5960 OD2 ASP B 41 -4.485 -34.500 -12.353 1.00 87.58 O
ANISOU 5960 OD2 ASP B 41 11170 10848 11258 254 20 342 O
ATOM 5961 N GLN B 42 -8.775 -35.999 -15.537 1.00 91.37 N
ANISOU 5961 N GLN B 42 11712 11244 11757 222 -63 267 N
ATOM 5962 CA GLN B 42 -9.723 -37.087 -15.259 1.00 91.54 C
ANISOU 5962 CA GLN B 42 11727 11254 11798 209 -66 260 C
ATOM 5963 C GLN B 42 -9.459 -38.363 -16.078 1.00 94.84 C
ANISOU 5963 C GLN B 42 12177 11644 12212 211 -56 259 C
ATOM 5964 O GLN B 42 -10.247 -39.314 -16.023 1.00 90.86 O
ANISOU 5964 O GLN B 42 11672 11126 11723 200 -59 251 O
ATOM 5965 CB GLN B 42 -11.165 -36.604 -15.462 1.00 88.87 C
ANISOU 5965 CB GLN B 42 11379 10915 11471 197 -98 239 C
ATOM 5966 CG GLN B 42 -11.614 -35.507 -14.501 1.00 90.63 C
ANISOU 5966 CG GLN B 42 11568 11164 11702 193 -107 240 C
ATOM 5967 CD GLN B 42 -12.071 -36.028 -13.145 1.00 93.74 C
ANISOU 5967 CD GLN B 42 11928 11569 12117 184 -96 247 C
ATOM 5968 OE1 GLN B 42 -13.170 -35.708 -12.684 1.00 95.93 O
ANISOU 5968 OE1 GLN B 42 12183 11854 12410 174 -113 238 O
ATOM 5969 NE2 GLN B 42 -11.230 -36.829 -12.498 1.00 93.16 N
ANISOU 5969 NE2 GLN B 42 11851 11498 12045 189 -68 266 N
ATOM 5970 N LYS B 43 -8.351 -38.367 -16.827 1.00 99.61 N
ANISOU 5970 N LYS B 43 12808 12240 12797 224 -43 266 N
ATOM 5971 CA LYS B 43 -7.873 -39.528 -17.611 1.00101.99 C
ANISOU 5971 CA LYS B 43 13143 12516 13092 229 -29 268 C
ATOM 5972 C LYS B 43 -8.847 -40.024 -18.691 1.00 97.94 C
ANISOU 5972 C LYS B 43 12654 11978 12580 220 -51 245 C
ATOM 5973 O LYS B 43 -8.808 -41.195 -19.071 1.00100.37 O
ANISOU 5973 O LYS B 43 12982 12264 12890 218 -41 244 O
ATOM 5974 CB LYS B 43 -7.459 -40.691 -16.691 1.00102.69 C
ANISOU 5974 CB LYS B 43 13220 12604 13193 228 0 285 C
ATOM 5975 CG LYS B 43 -6.355 -40.357 -15.702 1.00106.64 C
ANISOU 5975 CG LYS B 43 13699 13128 13690 238 24 309 C
ATOM 5976 CD LYS B 43 -6.399 -41.297 -14.510 1.00107.83 C
ANISOU 5976 CD LYS B 43 13826 13284 13858 234 44 323 C
ATOM 5977 CE LYS B 43 -5.637 -40.720 -13.329 1.00108.32 C
ANISOU 5977 CE LYS B 43 13859 13376 13919 240 60 343 C
ATOM 5978 NZ LYS B 43 -5.808 -41.556 -12.109 1.00107.75 N
ANISOU 5978 NZ LYS B 43 13762 13312 13865 236 77 356 N
ATOM 5979 N LEU B 44 -9.693 -39.129 -19.194 1.00 94.61 N
ANISOU 5979 N LEU B 44 12231 11558 12155 215 -81 227 N
ATOM 5980 CA LEU B 44 -10.744 -39.489 -20.152 1.00 96.20 C
ANISOU 5980 CA LEU B 44 12452 11740 12359 206 -107 204 C
ATOM 5981 C LEU B 44 -10.211 -39.801 -21.554 1.00100.04 C
ANISOU 5981 C LEU B 44 12983 12202 12824 216 -107 198 C
ATOM 5982 O LEU B 44 -9.327 -39.103 -22.066 1.00 98.39 O
ANISOU 5982 O LEU B 44 12790 11997 12595 229 -101 204 O
ATOM 5983 CB LEU B 44 -11.800 -38.380 -20.238 1.00 92.66 C
ANISOU 5983 CB LEU B 44 11987 11303 11913 200 -140 188 C
ATOM 5984 CG LEU B 44 -12.409 -37.836 -18.940 1.00 91.01 C
ANISOU 5984 CG LEU B 44 11735 11118 11724 191 -143 192 C
ATOM 5985 CD1 LEU B 44 -13.077 -36.497 -19.204 1.00 90.73 C
ANISOU 5985 CD1 LEU B 44 11692 11096 11685 191 -172 180 C
ATOM 5986 CD2 LEU B 44 -13.390 -38.816 -18.310 1.00 91.27 C
ANISOU 5986 CD2 LEU B 44 11750 11145 11782 176 -145 186 C
ATOM 5987 N SER B 45 -10.760 -40.854 -22.162 1.00102.56 N
ANISOU 5987 N SER B 45 13322 12497 13147 208 -113 184 N
ATOM 5988 CA SER B 45 -10.433 -41.235 -23.540 1.00100.83 C
ANISOU 5988 CA SER B 45 13147 12255 12909 214 -116 175 C
ATOM 5989 C SER B 45 -11.131 -40.331 -24.546 1.00101.68 C
ANISOU 5989 C SER B 45 13268 12360 13004 215 -150 155 C
ATOM 5990 O SER B 45 -10.512 -39.843 -25.497 1.00 97.99 O
ANISOU 5990 O SER B 45 12829 11886 12513 228 -151 154 O
ATOM 5991 CB SER B 45 -10.827 -42.690 -23.810 1.00 96.06 C
ANISOU 5991 CB SER B 45 12558 11625 12314 205 -111 167 C
ATOM 5992 OG SER B 45 -9.704 -43.545 -23.734 1.00 96.97 O
ANISOU 5992 OG SER B 45 12689 11729 12424 214 -77 184 O
ATOM 5993 N LYS B 46 -12.429 -40.128 -24.329 1.00102.28 N
ANISOU 5993 N LYS B 46 13324 12442 13096 200 -177 139 N
ATOM 5994 CA LYS B 46 -13.265 -39.321 -25.209 1.00100.39 C
ANISOU 5994 CA LYS B 46 13094 12202 12848 199 -212 118 C
ATOM 5995 C LYS B 46 -14.130 -38.351 -24.400 1.00 99.53 C
ANISOU 5995 C LYS B 46 12946 12116 12753 192 -231 115 C
ATOM 5996 O LYS B 46 -14.011 -38.269 -23.176 1.00 98.63 O
ANISOU 5996 O LYS B 46 12800 12020 12656 189 -216 129 O
ATOM 5997 CB LYS B 46 -14.130 -40.224 -26.103 1.00 99.69 C
ANISOU 5997 CB LYS B 46 13027 12088 12760 189 -232 96 C
ATOM 5998 CG LYS B 46 -13.386 -40.852 -27.280 1.00102.40 C
ANISOU 5998 CG LYS B 46 13417 12407 13081 198 -222 94 C
ATOM 5999 CD LYS B 46 -12.758 -42.207 -26.955 1.00100.17 C
ANISOU 5999 CD LYS B 46 13143 12109 12806 196 -191 105 C
ATOM 6000 CE LYS B 46 -11.669 -42.575 -27.956 1.00 94.67 C
ANISOU 6000 CE LYS B 46 12491 11394 12085 211 -173 110 C
ATOM 6001 NZ LYS B 46 -11.017 -43.879 -27.652 1.00 86.45 N
ANISOU 6001 NZ LYS B 46 11458 10336 11050 211 -141 122 N
ATOM 6002 N VAL B 47 -14.991 -37.617 -25.096 1.00100.13 N
ANISOU 6002 N VAL B 47 13026 12193 12824 190 -263 98 N
ATOM 6003 CA VAL B 47 -15.855 -36.616 -24.476 1.00104.78 C
ANISOU 6003 CA VAL B 47 13581 12804 13426 185 -283 93 C
ATOM 6004 C VAL B 47 -16.992 -37.283 -23.690 1.00110.11 C
ANISOU 6004 C VAL B 47 14226 13479 14129 166 -292 85 C
ATOM 6005 O VAL B 47 -17.681 -38.153 -24.231 1.00112.68 O
ANISOU 6005 O VAL B 47 14563 13786 14460 155 -305 69 O
ATOM 6006 CB VAL B 47 -16.454 -35.674 -25.544 1.00103.37 C
ANISOU 6006 CB VAL B 47 13418 12624 13231 189 -316 76 C
ATOM 6007 CG1 VAL B 47 -17.081 -34.446 -24.899 1.00104.31 C
ANISOU 6007 CG1 VAL B 47 13505 12768 13360 188 -332 76 C
ATOM 6008 CG2 VAL B 47 -15.389 -35.262 -26.552 1.00104.10 C
ANISOU 6008 CG2 VAL B 47 13548 12709 13294 207 -308 81 C
ATOM 6009 N PRO B 48 -17.183 -36.890 -22.408 1.00111.68 N
ANISOU 6009 N PRO B 48 14386 13699 14346 161 -284 96 N
ATOM 6010 CA PRO B 48 -18.335 -37.372 -21.631 1.00114.85 C
ANISOU 6010 CA PRO B 48 14757 14104 14776 144 -293 88 C
ATOM 6011 C PRO B 48 -19.641 -36.850 -22.228 1.00121.87 C
ANISOU 6011 C PRO B 48 15641 14993 15669 136 -332 66 C
ATOM 6012 O PRO B 48 -20.009 -35.695 -21.994 1.00125.28 O
ANISOU 6012 O PRO B 48 16055 15443 16102 139 -346 65 O
ATOM 6013 CB PRO B 48 -18.105 -36.773 -20.236 1.00108.02 C
ANISOU 6013 CB PRO B 48 13855 13264 13923 144 -277 106 C
ATOM 6014 CG PRO B 48 -16.658 -36.436 -20.188 1.00104.39 C
ANISOU 6014 CG PRO B 48 13408 12809 13443 160 -251 125 C
ATOM 6015 CD PRO B 48 -16.286 -36.055 -21.589 1.00106.72 C
ANISOU 6015 CD PRO B 48 13741 13092 13713 171 -264 116 C
ATOM 6016 N ASP B 49 -20.327 -37.701 -22.991 1.00129.38 N
ANISOU 6016 N ASP B 49 16609 15924 16625 126 -348 48 N
ATOM 6017 CA ASP B 49 -21.473 -37.272 -23.810 1.00134.30 C
ANISOU 6017 CA ASP B 49 17235 16544 17247 121 -386 26 C
ATOM 6018 C ASP B 49 -22.852 -37.312 -23.118 1.00136.48 C
ANISOU 6018 C ASP B 49 17474 16829 17553 104 -404 16 C
ATOM 6019 O ASP B 49 -23.880 -37.517 -23.772 1.00142.29 O
ANISOU 6019 O ASP B 49 18213 17556 18294 95 -433 -4 O
ATOM 6020 CB ASP B 49 -21.491 -38.002 -25.174 1.00132.32 C
ANISOU 6020 CB ASP B 49 17025 16268 16981 121 -398 10 C
ATOM 6021 CG ASP B 49 -21.489 -39.526 -25.045 1.00128.61 C
ANISOU 6021 CG ASP B 49 16562 15778 16524 109 -383 7 C
ATOM 6022 OD1 ASP B 49 -20.899 -40.063 -24.081 1.00125.28 O
ANISOU 6022 OD1 ASP B 49 16127 15359 16114 108 -352 25 O
ATOM 6023 OD2 ASP B 49 -22.069 -40.191 -25.932 1.00120.86 O
ANISOU 6023 OD2 ASP B 49 15601 14778 15542 101 -401 -11 O
ATOM 6024 N ASP B 50 -22.860 -37.099 -21.801 1.00129.49 N
ANISOU 6024 N ASP B 50 16553 15960 16685 101 -388 30 N
ATOM 6025 CA ASP B 50 -24.102 -36.953 -21.027 1.00122.83 C
ANISOU 6025 CA ASP B 50 15672 15127 15869 87 -403 23 C
ATOM 6026 C ASP B 50 -24.202 -35.579 -20.348 1.00117.84 C
ANISOU 6026 C ASP B 50 15013 14521 15238 94 -407 31 C
ATOM 6027 O ASP B 50 -25.181 -35.280 -19.661 1.00115.09 O
ANISOU 6027 O ASP B 50 14632 14184 14911 84 -418 27 O
ATOM 6028 CB ASP B 50 -24.268 -38.095 -20.013 1.00124.34 C
ANISOU 6028 CB ASP B 50 15842 15314 16086 73 -381 30 C
ATOM 6029 CG ASP B 50 -22.946 -38.557 -19.418 1.00125.88 C
ANISOU 6029 CG ASP B 50 16045 15509 16274 82 -342 52 C
ATOM 6030 OD1 ASP B 50 -22.020 -37.730 -19.269 1.00122.87 O
ANISOU 6030 OD1 ASP B 50 15668 15141 15875 96 -331 66 O
ATOM 6031 OD2 ASP B 50 -22.838 -39.760 -19.095 1.00126.76 O
ANISOU 6031 OD2 ASP B 50 16157 15606 16397 74 -324 55 O
ATOM 6032 N ILE B 51 -23.173 -34.759 -20.553 1.00114.28 N
ANISOU 6032 N ILE B 51 14577 14078 14764 110 -396 43 N
ATOM 6033 CA ILE B 51 -23.176 -33.338 -20.200 1.00110.29 C
ANISOU 6033 CA ILE B 51 14055 13595 14254 119 -403 49 C
ATOM 6034 C ILE B 51 -24.285 -32.627 -20.990 1.00108.42 C
ANISOU 6034 C ILE B 51 13819 1 |
