*** STRUCTURAL PROTEIN 03-JUN-07 2V26 ***
Job options:
ID = 22021014344621848
JOBID = STRUCTURAL PROTEIN 03-JUN-07 2V26
USERID = unknown
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = on
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
HEADER STRUCTURAL PROTEIN 03-JUN-07 2V26
TITLE MYOSIN VI (MD) PRE-POWERSTROKE STATE (MG.ADP.VO4)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN VI;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN MOTOR, RESIDUES 5-377,379-789;
COMPND 5 SYNONYM: UNCONVENTIONAL MYOSIN VI;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS CALMODULIN-BINDING, NUCLEOTIDE-BINDING, MYOSIN, MEMBRANE,
KEYWDS 2 VANADATE, MYOSIN VI, TRANSPORT, PRE- POWERSTROKE,
KEYWDS 3 TRANSITION STATE, PROTEIN TRANSPORT, ACTIN-BINDING, MOTOR
KEYWDS 4 PROTEIN, NUCLEAR PROTEIN, ENDOCYTOSIS, ATP-BINDING, COILED
KEYWDS 5 COIL, DOMAIN MOTOR, GOLGI APPARATUS, PHOSPHORYLATION,
KEYWDS 6 MOLECULAR MOTOR, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.MENETREY,P.LLINAS,M.MUKHERJEA,H.L.SWEENEY,A.HOUDUSSE
REVDAT 2 24-FEB-09 2V26 1 VERSN
REVDAT 1 20-NOV-07 2V26 0
JRNL AUTH J.MENETREY,P.LLINAS,M.MUKHERJEA,H.L.SWEENEY,
JRNL AUTH 2 A.HOUDUSSE
JRNL TITL THE STRUCTURAL BASIS FOR THE LARGE POWERSTROKE OF
JRNL TITL 2 MYOSIN VI.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 131 300 2007
JRNL REFN ISSN 0092-8674
JRNL PMID 17956731
JRNL DOI 10.1016/J.CELL.2007.08.027
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 81037
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 9071
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5939
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 643
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6058
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 71
REMARK 3 SOLVENT ATOMS : 536
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.20000
REMARK 3 B22 (A**2) : 0.77000
REMARK 3 B33 (A**2) : -0.57000
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): 0.128
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.122
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6252 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8429 ; 1.062 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 760 ; 5.036 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 309 ;35.161 ;24.175
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1126 ;12.493 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;14.632 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 919 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4700 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3011 ; 0.186 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4323 ; 0.299 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 461 ; 0.097 ; 0.200
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): 54 ; 0.145 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.068 ; 0.200
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): 3872 ; 0.517 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6044 ; 0.832 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2669 ; 1.355 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2376 ; 2.113 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2V26 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JUN-07.
REMARK 100 THE PDBE ID CODE IS EBI-32777.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0080
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90108
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.75
REMARK 200 RESOLUTION RANGE LOW (A) : 70.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.0
REMARK 200 R MERGE (I) : 0.11
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.0
REMARK 200 R MERGE FOR SHELL (I) : 0.41
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2BKH
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.8
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3-4% PEG 8000, 50MM MES PH 6.75,
REMARK 280 100MM SAM, 1MM TCEP
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 46.75600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.48800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.92250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.48800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.75600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.92250
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 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LEU A 34
REMARK 465 ASN A 35
REMARK 465 GLN A 36
REMARK 465 LYS A 37
REMARK 465 THR A 174
REMARK 465 GLY A 175
REMARK 465 GLN A 176
REMARK 465 ASP A 177
REMARK 465 ILE A 178
REMARK 465 ASP A 179
REMARK 465 LEU A 396
REMARK 465 THR A 397
REMARK 465 THR A 398
REMARK 465 ALA A 399
REMARK 465 GLY A 400
REMARK 465 GLY A 401
REMARK 465 ALA A 402
REMARK 465 LYS A 403
REMARK 465 GLY A 404
REMARK 465 THR A 405
REMARK 465 VAL A 406
REMARK 465 GLU A 622
REMARK 465 SER A 623
REMARK 465 SER A 624
REMARK 465 THR A 625
REMARK 465 ASN A 626
REMARK 465 ASN A 627
REMARK 465 ASN A 628
REMARK 465 LYS A 629
REMARK 465 ASP A 630
REMARK 465 THR A 631
REMARK 465 LYS A 632
REMARK 465 GLN A 633
REMARK 465 LYS A 634
REMARK 465 ALA A 635
REMARK 465 GLY A 636
REMARK 465 LYS A 637
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 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 ALA A 91 -119.72 52.75
REMARK 500 LYS A 105 -18.21 78.89
REMARK 500 ASN A 244 -176.40 -69.52
REMARK 500 SER A 467 -161.82 -122.29
REMARK 500 LEU A 522 -48.35 69.99
REMARK 500 ASP A 553 -4.66 76.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 VO4 A1791 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A1789 O2B
REMARK 620 2 VO4 A1791 O2 85.4
REMARK 620 3 VO4 A1791 O4 86.3 119.5
REMARK 620 4 VO4 A1791 O1 178.6 95.8 93.7
REMARK 620 5 VO4 A1791 O3 83.2 119.1 119.2 95.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 158 OG1
REMARK 620 2 SER A 204 OG 82.3
REMARK 620 3 ADP A1789 O1B 91.3 172.1
REMARK 620 4 VO4 A1791 O2 170.8 88.6 97.9
REMARK 620 5 HOH A2527 O 86.5 82.9 92.2 93.4
REMARK 620 6 HOH A2314 O 84.5 87.6 96.3 94.1 167.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A1789
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 A1791
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1792
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1793
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1794
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1795
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1796
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1797
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1798
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1799
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BKH RELATED DB: PDB
REMARK 900 MYOSIN VI NUCLEOTIDE-FREE (MD) CRYSTAL
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 2BKI RELATED DB: PDB
REMARK 900 MYOSIN VI NUCLEOTIDE-FREE (LONG.S1) CRYSTAL
REMARK 900 STRUCTURE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS STATE THAT THE ORIGINAL SEQUENCE (UNIPROT
REMARK 999 Q29122) OF MYOSIN VI FROM PIG WAS MOST LIKELY
REMARK 999 INCORRECT BECAUSE THE CHANGES THAT ARE IN THEIR CLONE
REMARK 999 (LYS DELETION AND THE 6 MUTATIONS) ARE CONSERVED ACROSS
REMARK 999 THE MYOSIN VI FAMILY.
DBREF 2V26 A 5 377 UNP Q29122 MYO6_PIG 5 377
DBREF 2V26 A 378 788 UNP Q29122 MYO6_PIG 379 789
SEQADV 2V26 VAL A 547 UNP Q29122 GLY 548 CONFLICT
SEQADV 2V26 ARG A 572 UNP Q29122 ALA 573 CONFLICT
SEQADV 2V26 ASP A 573 UNP Q29122 TYR 574 CONFLICT
SEQADV 2V26 LEU A 714 UNP Q29122 VAL 715 CONFLICT
SEQADV 2V26 TYR A 721 UNP Q29122 SER 722 CONFLICT
SEQADV 2V26 MET A 722 UNP Q29122 LEU 723 CONFLICT
SEQRES 1 A 784 LYS PRO VAL TRP ALA PRO HIS PRO THR ASP GLY PHE GLN
SEQRES 2 A 784 VAL GLY ASN ILE VAL ASP ILE GLY PRO ASP SER LEU THR
SEQRES 3 A 784 ILE GLU PRO LEU ASN GLN LYS GLY LYS THR PHE LEU ALA
SEQRES 4 A 784 LEU ILE ASN GLN VAL PHE PRO ALA GLU GLU ASP SER LYS
SEQRES 5 A 784 LYS ASP VAL GLU ASP ASN CYS SER LEU MET TYR LEU ASN
SEQRES 6 A 784 GLU ALA THR LEU LEU HIS ASN ILE LYS VAL ARG TYR SER
SEQRES 7 A 784 LYS ASP ARG ILE TYR THR TYR VAL ALA ASN ILE LEU ILE
SEQRES 8 A 784 ALA VAL ASN PRO TYR PHE ASP ILE PRO LYS ILE TYR SER
SEQRES 9 A 784 SER GLU THR ILE LYS SER TYR GLN GLY LYS SER LEU GLY
SEQRES 10 A 784 THR MET PRO PRO HIS VAL PHE ALA ILE ALA ASP LYS ALA
SEQRES 11 A 784 PHE ARG ASP MET LYS VAL LEU LYS LEU SER GLN SER ILE
SEQRES 12 A 784 ILE VAL SER GLY GLU SER GLY ALA GLY LYS THR GLU ASN
SEQRES 13 A 784 THR LYS PHE VAL LEU ARG TYR LEU THR GLU SER TYR GLY
SEQRES 14 A 784 THR GLY GLN ASP ILE ASP ASP ARG ILE VAL GLU ALA ASN
SEQRES 15 A 784 PRO LEU LEU GLU ALA PHE GLY ASN ALA LYS THR VAL ARG
SEQRES 16 A 784 ASN ASN ASN SER SER ARG PHE GLY LYS PHE VAL GLU ILE
SEQRES 17 A 784 HIS PHE ASN GLU LYS SER SER VAL VAL GLY GLY PHE VAL
SEQRES 18 A 784 SER HIS TYR LEU LEU GLU LYS SER ARG ILE CYS VAL GLN
SEQRES 19 A 784 GLY LYS GLU GLU ARG ASN TYR HIS ILE PHE TYR ARG LEU
SEQRES 20 A 784 CYS ALA GLY ALA SER GLU ASP ILE ARG GLU ARG LEU HIS
SEQRES 21 A 784 LEU SER SER PRO ASP ASN PHE ARG TYR LEU ASN ARG GLY
SEQRES 22 A 784 CYS THR ARG TYR PHE ALA ASN LYS GLU THR ASP LYS GLN
SEQRES 23 A 784 ILE LEU GLN ASN ARG LYS SER PRO GLU TYR LEU LYS ALA
SEQRES 24 A 784 GLY SER LEU LYS ASP PRO LEU LEU ASP ASP HIS GLY ASP
SEQRES 25 A 784 PHE ILE ARG MET CYS THR ALA MET LYS LYS ILE GLY LEU
SEQRES 26 A 784 ASP ASP GLU GLU LYS LEU ASP LEU PHE ARG VAL VAL ALA
SEQRES 27 A 784 GLY VAL LEU HIS LEU GLY ASN ILE ASP PHE GLU GLU ALA
SEQRES 28 A 784 GLY SER THR SER GLY GLY CYS ASN LEU LYS ASN LYS SER
SEQRES 29 A 784 THR GLN ALA LEU GLU TYR CYS ALA GLU LEU LEU GLY LEU
SEQRES 30 A 784 ASP GLN ASP ASP LEU ARG VAL SER LEU THR THR ARG VAL
SEQRES 31 A 784 MET LEU THR THR ALA GLY GLY ALA LYS GLY THR VAL ILE
SEQRES 32 A 784 LYS VAL PRO LEU LYS VAL GLU GLN ALA ASN ASN ALA ARG
SEQRES 33 A 784 ASP ALA LEU ALA LYS THR VAL TYR SER HIS LEU PHE ASP
SEQRES 34 A 784 HIS VAL VAL ASN ARG VAL ASN GLN CYS PHE PRO PHE GLU
SEQRES 35 A 784 THR SER SER TYR PHE ILE GLY VAL LEU ASP ILE ALA GLY
SEQRES 36 A 784 PHE GLU TYR PHE GLU HIS ASN SER PHE GLU GLN PHE CYS
SEQRES 37 A 784 ILE ASN TYR CYS ASN GLU LYS LEU GLN GLN PHE PHE ASN
SEQRES 38 A 784 GLU ARG ILE LEU LYS GLU GLU GLN GLU LEU TYR GLN LYS
SEQRES 39 A 784 GLU GLY LEU GLY VAL ASN GLU VAL HIS TYR VAL ASP ASN
SEQRES 40 A 784 GLN ASP CYS ILE ASP LEU ILE GLU ALA ARG LEU VAL GLY
SEQRES 41 A 784 ILE LEU ASP ILE LEU ASP GLU GLU ASN ARG LEU PRO GLN
SEQRES 42 A 784 PRO SER ASP GLN HIS PHE THR SER ALA VAL HIS GLN LYS
SEQRES 43 A 784 HIS LYS ASP HIS PHE ARG LEU SER ILE PRO ARG LYS SER
SEQRES 44 A 784 LYS LEU ALA ILE HIS ARG ASN ILE ARG ASP ASP GLU GLY
SEQRES 45 A 784 PHE ILE ILE ARG HIS PHE ALA GLY ALA VAL CYS TYR GLU
SEQRES 46 A 784 THR THR GLN PHE VAL GLU LYS ASN ASN ASP ALA LEU HIS
SEQRES 47 A 784 MET SER LEU GLU SER LEU ILE CYS GLU SER ARG ASP LYS
SEQRES 48 A 784 PHE ILE ARG GLU LEU PHE GLU SER SER THR ASN ASN ASN
SEQRES 49 A 784 LYS ASP THR LYS GLN LYS ALA GLY LYS LEU SER PHE ILE
SEQRES 50 A 784 SER VAL GLY ASN LYS PHE LYS THR GLN LEU ASN LEU LEU
SEQRES 51 A 784 LEU ASP LYS LEU ARG SER THR GLY ALA SER PHE ILE ARG
SEQRES 52 A 784 CYS ILE LYS PRO ASN LEU LYS MET THR SER HIS HIS PHE
SEQRES 53 A 784 GLU GLY ALA GLN ILE LEU SER GLN LEU GLN CYS SER GLY
SEQRES 54 A 784 MET VAL SER VAL LEU ASP LEU MET GLN GLY GLY PHE PRO
SEQRES 55 A 784 SER ARG ALA SER PHE HIS GLU LEU TYR ASN MET TYR LYS
SEQRES 56 A 784 LYS TYR MET PRO ASP LYS LEU ALA ARG LEU ASP PRO ARG
SEQRES 57 A 784 LEU PHE CYS LYS ALA LEU PHE LYS ALA LEU GLY LEU ASN
SEQRES 58 A 784 GLU ILE ASP TYR LYS PHE GLY LEU THR LYS VAL PHE PHE
SEQRES 59 A 784 ARG PRO GLY LYS PHE ALA GLU PHE ASP GLN ILE MET LYS
SEQRES 60 A 784 SER ASP PRO ASP HIS LEU ALA GLU LEU VAL LYS ARG VAL
SEQRES 61 A 784 ASN HIS TRP LEU
HET ADP A1789 27
HET MG A1801 1
HET VO4 A1791 5
HET EDO A1792 4
HET EDO A1793 4
HET EDO A1794 4
HET EDO A1795 4
HET EDO A1796 4
HET EDO A1797 4
HET EDO A1798 4
HET SO4 A1799 5
HET SO4 A1800 5
HETNAM VO4 VANADATE ION
HETNAM SO4 SULFATE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM MG MAGNESIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 VO4 O4 V 3-
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 ADP C10 H15 N5 O10 P2
FORMUL 5 EDO 7(C2 H6 O2)
FORMUL 6 MG MG 2+
FORMUL 7 HOH *536(H2 O1)
HELIX 1 1 ASN A 46 VAL A 48 5 3
HELIX 2 2 ASN A 62 LEU A 65 5 4
HELIX 3 3 ASN A 69 LYS A 83 1 15
HELIX 4 4 SER A 108 GLN A 116 1 9
HELIX 5 5 HIS A 126 LYS A 142 1 17
HELIX 6 6 GLY A 156 GLY A 173 1 18
HELIX 7 7 ASP A 180 ALA A 185 1 6
HELIX 8 8 ALA A 185 GLY A 193 1 9
HELIX 9 9 LYS A 232 CYS A 236 5 5
HELIX 10 10 TYR A 245 ALA A 255 1 11
HELIX 11 11 SER A 256 LEU A 263 1 8
HELIX 12 12 SER A 267 ASN A 270 5 4
HELIX 13 13 PHE A 271 ARG A 276 1 6
HELIX 14 14 ASN A 284 LYS A 289 1 6
HELIX 15 15 LEU A 292 LYS A 296 5 5
HELIX 16 16 SER A 297 GLY A 304 1 8
HELIX 17 17 ASP A 312 GLY A 328 1 17
HELIX 18 18 ASP A 330 ASN A 349 1 20
HELIX 19 19 SER A 368 GLY A 380 1 13
HELIX 20 20 ASP A 382 THR A 391 1 10
HELIX 21 21 LYS A 412 GLN A 441 1 30
HELIX 22 22 SER A 467 LEU A 489 1 23
HELIX 23 23 LYS A 490 GLU A 499 1 10
HELIX 24 24 ASN A 511 ALA A 520 1 10
HELIX 25 25 GLY A 524 LEU A 535 1 12
HELIX 26 26 SER A 539 HIS A 551 1 13
HELIX 27 27 ILE A 559 SER A 563 5 5
HELIX 28 28 LEU A 565 ARG A 569 5 5
HELIX 29 29 GLN A 592 ASN A 597 1 6
HELIX 30 30 HIS A 602 GLU A 611 1 10
HELIX 31 31 ASP A 614 PHE A 621 1 8
HELIX 32 32 SER A 642 SER A 660 1 19
HELIX 33 33 GLU A 681 SER A 692 1 12
HELIX 34 34 GLY A 693 GLN A 702 1 10
HELIX 35 35 PHE A 711 LYS A 719 1 9
HELIX 36 36 LYS A 720 MET A 722 5 3
HELIX 37 37 PRO A 723 ARG A 728 1 6
HELIX 38 38 ASP A 730 LEU A 742 1 13
HELIX 39 39 ASN A 745 ILE A 747 5 3
HELIX 40 40 LYS A 762 LYS A 771 1 10
HELIX 41 41 ASP A 773 LEU A 788 1 16
SHEET 1 AA 5 PHE A 41 LEU A 44 0
SHEET 2 AA 5 SER A 28 GLU A 32 -1 O LEU A 29 N ALA A 43
SHEET 3 AA 5 GLY A 15 ILE A 24 -1 O ASN A 20 N GLU A 32
SHEET 4 AA 5 VAL A 7 HIS A 11 -1 O VAL A 7 N GLY A 19
SHEET 5 AA 5 PHE A 49 PRO A 50 -1 O PHE A 49 N TRP A 8
SHEET 1 AB 7 TYR A 87 VAL A 90 0
SHEET 2 AB 7 ILE A 93 VAL A 97 -1 O ILE A 93 N VAL A 90
SHEET 3 AB 7 GLY A 662 ILE A 669 1 O PHE A 665 N LEU A 94
SHEET 4 AB 7 GLN A 145 SER A 150 1 O SER A 146 N SER A 664
SHEET 5 AB 7 TYR A 450 ASP A 456 1 O PHE A 451 N GLN A 145
SHEET 6 AB 7 GLY A 207 PHE A 214 -1 O LYS A 208 N ASP A 456
SHEET 7 AB 7 VAL A 220 TYR A 228 -1 N VAL A 221 O HIS A 213
SHEET 1 AC 2 ASN A 194 ALA A 195 0
SHEET 2 AC 2 SER A 203 SER A 204 -1 O SER A 203 N ALA A 195
SHEET 1 AD 2 PHE A 352 GLU A 354 0
SHEET 2 AD 2 CYS A 362 LEU A 364 -1 O ASN A 363 N GLU A 353
SHEET 1 AE 2 THR A 392 VAL A 394 0
SHEET 2 AE 2 LYS A 408 PRO A 410 -1 O VAL A 409 N ARG A 393
SHEET 1 AF 3 LEU A 557 SER A 558 0
SHEET 2 AF 3 GLY A 576 HIS A 581 -1 O ILE A 578 N SER A 558
SHEET 3 AF 3 GLY A 584 GLU A 589 -1 O GLY A 584 N HIS A 581
SHEET 1 AG 3 SER A 707 SER A 710 0
SHEET 2 AG 3 LYS A 755 PHE A 758 -1 O VAL A 756 N ALA A 709
SHEET 3 AG 3 TYR A 749 PHE A 751 -1 O LYS A 750 N PHE A 757
LINK O2 VO4 A1791 MG MG A1801 1555 1555 1.79
LINK V VO4 A1791 O2B ADP A1789 1555 1555 2.16
LINK MG MG A1801 O HOH A2527 1555 1555 2.16
LINK MG MG A1801 OG SER A 204 1555 1555 2.22
LINK MG MG A1801 O1B ADP A1789 1555 1555 2.06
LINK MG MG A1801 O HOH A2314 1555 1555 2.15
LINK MG MG A1801 OG1 THR A 158 1555 1555 2.10
SITE 1 AC1 23 ASN A 98 PRO A 99 TYR A 100 PHE A 101
SITE 2 AC1 23 ASP A 102 TYR A 107 GLY A 154 ALA A 155
SITE 3 AC1 23 GLY A 156 LYS A 157 THR A 158 GLU A 159
SITE 4 AC1 23 PHE A 163 ASN A 200 LEU A 310 VO4 A1791
SITE 5 AC1 23 MG A1801 HOH A2524 HOH A2525 HOH A2526
SITE 6 AC1 23 HOH A2527 HOH A2528 HOH A2529
SITE 1 AC2 6 THR A 158 SER A 204 ADP A1789 VO4 A1791
SITE 2 AC2 6 HOH A2314 HOH A2527
SITE 1 AC3 13 SER A 153 GLY A 154 LYS A 157 ASN A 200
SITE 2 AC3 13 SER A 203 SER A 204 ALA A 458 GLY A 459
SITE 3 AC3 13 ADP A1789 MG A1801 HOH A2314 HOH A2315
SITE 4 AC3 13 HOH A2527
SITE 1 AC4 5 HIS A 227 TYR A 228 LEU A 229 GLN A 650
SITE 2 AC4 5 HOH A2530
SITE 1 AC5 5 PHE A 206 GLY A 207 ALA A 458 CYS A 476
SITE 2 AC5 5 EDO A1798
SITE 1 AC6 7 GLU A 152 ARG A 199 GLU A 461 TYR A 462
SITE 2 AC6 7 LYS A 670 LEU A 673 HOH A2531
SITE 1 AC7 6 ASP A 84 ARG A 85 ILE A 86 TYR A 87
SITE 2 AC7 6 ILE A 106 HOH A2134
SITE 1 AC8 6 TRP A 8 HIS A 75 LYS A 78 HOH A2017
SITE 2 AC8 6 HOH A2532 HOH A2533
SITE 1 AC9 7 TYR A 462 ASN A 466 LEU A 565 HIS A 568
SITE 2 AC9 7 ALA A 585 VAL A 586 CYS A 587
SITE 1 BC1 8 ARG A 205 PHE A 206 LEU A 229 GLU A 231
SITE 2 BC1 8 ILE A 473 PHE A 647 EDO A1793 HOH A2534
SITE 1 BC2 6 LYS A 83 ARG A 85 SER A 256 GLU A 257
SITE 2 BC2 6 HOH A2535 HOH A2536
SITE 1 BC3 2 ARG A 521 LYS A 782
CRYST1 93.512 93.845 100.976 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010694 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010656 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009903 0.00000
ATOM 1 N LYS A 5 -6.475 16.224 -21.125 1.00 26.13 N
ATOM 2 CA LYS A 5 -6.945 15.269 -20.078 1.00 25.92 C
ATOM 3 C LYS A 5 -6.415 15.653 -18.698 1.00 25.29 C
ATOM 4 O LYS A 5 -5.228 15.955 -18.555 1.00 25.58 O
ATOM 5 CB LYS A 5 -6.501 13.842 -20.406 1.00 26.15 C
ATOM 6 CG LYS A 5 -7.213 13.201 -21.587 1.00 27.88 C
ATOM 7 CD LYS A 5 -6.597 11.845 -21.899 1.00 29.78 C
ATOM 8 CE LYS A 5 -7.081 11.296 -23.235 1.00 31.92 C
ATOM 9 NZ LYS A 5 -6.637 12.128 -24.398 1.00 33.33 N
ATOM 10 N PRO A 6 -7.289 15.626 -17.674 1.00 24.53 N
ATOM 11 CA PRO A 6 -6.833 15.878 -16.300 1.00 23.55 C
ATOM 12 C PRO A 6 -5.754 14.892 -15.838 1.00 22.34 C
ATOM 13 O PRO A 6 -5.743 13.733 -16.257 1.00 22.18 O
ATOM 14 CB PRO A 6 -8.109 15.715 -15.460 1.00 23.76 C
ATOM 15 CG PRO A 6 -9.073 14.980 -16.331 1.00 24.45 C
ATOM 16 CD PRO A 6 -8.741 15.378 -17.734 1.00 24.58 C
ATOM 17 N VAL A 7 -4.850 15.369 -14.985 1.00 20.79 N
ATOM 18 CA VAL A 7 -3.759 14.554 -14.445 1.00 19.11 C
ATOM 19 C VAL A 7 -3.702 14.723 -12.923 1.00 18.13 C
ATOM 20 O VAL A 7 -4.357 15.612 -12.375 1.00 17.81 O
ATOM 21 CB VAL A 7 -2.387 14.945 -15.054 1.00 19.30 C
ATOM 22 CG1 VAL A 7 -2.314 14.567 -16.538 1.00 19.20 C
ATOM 23 CG2 VAL A 7 -2.107 16.443 -14.857 1.00 18.38 C
ATOM 24 N TRP A 8 -2.934 13.862 -12.256 1.00 17.07 N
ATOM 25 CA TRP A 8 -2.675 13.992 -10.817 1.00 15.87 C
ATOM 26 C TRP A 8 -1.305 14.612 -10.579 1.00 15.69 C
ATOM 27 O TRP A 8 -0.301 14.125 -11.101 1.00 15.74 O
ATOM 28 CB TRP A 8 -2.712 12.625 -10.124 1.00 15.24 C
ATOM 29 CG TRP A 8 -4.059 11.994 -10.060 1.00 14.36 C
ATOM 30 CD1 TRP A 8 -4.476 10.875 -10.731 1.00 14.14 C
ATOM 31 CD2 TRP A 8 -5.168 12.422 -9.266 1.00 13.43 C
ATOM 32 NE1 TRP A 8 -5.778 10.592 -10.411 1.00 13.65 N
ATOM 33 CE2 TRP A 8 -6.233 11.530 -9.521 1.00 13.48 C
ATOM 34 CE3 TRP A 8 -5.372 13.486 -8.375 1.00 14.20 C
ATOM 35 CZ2 TRP A 8 -7.483 11.661 -8.909 1.00 14.00 C
ATOM 36 CZ3 TRP A 8 -6.616 13.616 -7.763 1.00 13.99 C
ATOM 37 CH2 TRP A 8 -7.655 12.706 -8.034 1.00 14.60 C
ATOM 38 N ALA A 9 -1.267 15.676 -9.780 1.00 15.27 N
ATOM 39 CA ALA A 9 -0.014 16.307 -9.382 1.00 15.22 C
ATOM 40 C ALA A 9 0.019 16.470 -7.858 1.00 15.05 C
ATOM 41 O ALA A 9 -1.037 16.471 -7.228 1.00 14.80 O
ATOM 42 CB ALA A 9 0.147 17.658 -10.082 1.00 15.11 C
ATOM 43 N PRO A 10 1.225 16.600 -7.267 1.00 15.09 N
ATOM 44 CA PRO A 10 1.363 16.645 -5.802 1.00 15.41 C
ATOM 45 C PRO A 10 0.531 17.727 -5.116 1.00 15.54 C
ATOM 46 O PRO A 10 0.382 18.840 -5.638 1.00 15.72 O
ATOM 47 CB PRO A 10 2.851 16.941 -5.595 1.00 15.63 C
ATOM 48 CG PRO A 10 3.514 16.437 -6.823 1.00 15.82 C
ATOM 49 CD PRO A 10 2.538 16.702 -7.934 1.00 15.01 C
ATOM 50 N HIS A 11 0.000 17.379 -3.948 1.00 15.33 N
ATOM 51 CA HIS A 11 -0.663 18.315 -3.056 1.00 15.46 C
ATOM 52 C HIS A 11 -0.175 17.965 -1.652 1.00 15.47 C
ATOM 53 O HIS A 11 -0.129 16.782 -1.293 1.00 15.35 O
ATOM 54 CB HIS A 11 -2.183 18.183 -3.159 1.00 15.57 C
ATOM 55 CG HIS A 11 -2.933 19.221 -2.385 1.00 16.18 C
ATOM 56 ND1 HIS A 11 -3.116 19.145 -1.021 1.00 16.25 N
ATOM 57 CD2 HIS A 11 -3.547 20.360 -2.783 1.00 16.96 C
ATOM 58 CE1 HIS A 11 -3.811 20.190 -0.612 1.00 17.69 C
ATOM 59 NE2 HIS A 11 -4.087 20.944 -1.661 1.00 17.52 N
ATOM 60 N PRO A 12 0.202 18.984 -0.855 1.00 15.72 N
ATOM 61 CA PRO A 12 0.894 18.704 0.411 1.00 15.92 C
ATOM 62 C PRO A 12 0.050 18.038 1.500 1.00 16.17 C
ATOM 63 O PRO A 12 0.611 17.401 2.393 1.00 16.47 O
ATOM 64 CB PRO A 12 1.378 20.087 0.864 1.00 16.06 C
ATOM 65 CG PRO A 12 0.448 21.048 0.229 1.00 16.17 C
ATOM 66 CD PRO A 12 0.025 20.434 -1.079 1.00 15.80 C
ATOM 67 N THR A 13 -1.271 18.177 1.440 1.00 15.98 N
ATOM 68 CA THR A 13 -2.128 17.547 2.449 1.00 16.36 C
ATOM 69 C THR A 13 -3.051 16.476 1.875 1.00 15.73 C
ATOM 70 O THR A 13 -3.452 15.554 2.590 1.00 15.49 O
ATOM 71 CB THR A 13 -2.943 18.581 3.267 1.00 16.81 C
ATOM 72 OG1 THR A 13 -3.810 19.308 2.396 1.00 18.30 O
ATOM 73 CG2 THR A 13 -2.014 19.557 3.992 1.00 17.59 C
ATOM 74 N ASP A 14 -3.387 16.605 0.594 1.00 15.01 N
ATOM 75 CA ASP A 14 -4.218 15.615 -0.095 1.00 14.78 C
ATOM 76 C ASP A 14 -3.401 14.510 -0.766 1.00 13.97 C
ATOM 77 O ASP A 14 -3.961 13.515 -1.234 1.00 13.88 O
ATOM 78 CB ASP A 14 -5.122 16.297 -1.128 1.00 15.39 C
ATOM 79 CG ASP A 14 -6.188 17.167 -0.489 1.00 17.14 C
ATOM 80 OD1 ASP A 14 -6.612 18.142 -1.138 1.00 18.36 O
ATOM 81 OD2 ASP A 14 -6.598 16.881 0.658 1.00 18.58 O
ATOM 82 N GLY A 15 -2.084 14.690 -0.813 1.00 13.43 N
ATOM 83 CA GLY A 15 -1.190 13.753 -1.487 1.00 13.12 C
ATOM 84 C GLY A 15 -1.094 14.104 -2.960 1.00 12.98 C
ATOM 85 O GLY A 15 -0.009 14.427 -3.463 1.00 12.85 O
ATOM 86 N PHE A 16 -2.239 14.043 -3.637 1.00 12.93 N
ATOM 87 CA PHE A 16 -2.368 14.468 -5.032 1.00 13.50 C
ATOM 88 C PHE A 16 -3.615 15.320 -5.243 1.00 13.94 C
ATOM 89 O PHE A 16 -4.589 15.204 -4.499 1.00 13.57 O
ATOM 90 CB PHE A 16 -2.405 13.258 -5.975 1.00 13.32 C
ATOM 91 CG PHE A 16 -1.109 12.507 -6.044 1.00 13.39 C
ATOM 92 CD1 PHE A 16 -0.913 11.362 -5.278 1.00 13.57 C
ATOM 93 CD2 PHE A 16 -0.075 12.944 -6.875 1.00 12.67 C
ATOM 94 CE1 PHE A 16 0.286 10.659 -5.342 1.00 12.95 C
ATOM 95 CE2 PHE A 16 1.131 12.253 -6.940 1.00 12.53 C
ATOM 96 CZ PHE A 16 1.316 11.105 -6.171 1.00 13.66 C
ATOM 97 N GLN A 17 -3.573 16.170 -6.271 1.00 14.50 N
ATOM 98 CA GLN A 17 -4.721 16.976 -6.684 1.00 15.71 C
ATOM 99 C GLN A 17 -4.924 16.885 -8.199 1.00 16.25 C
ATOM 100 O GLN A 17 -3.970 16.624 -8.931 1.00 16.32 O
ATOM 101 CB GLN A 17 -4.538 18.443 -6.266 1.00 15.47 C
ATOM 102 CG GLN A 17 -3.283 19.121 -6.827 1.00 15.93 C
ATOM 103 CD GLN A 17 -3.135 20.555 -6.344 1.00 16.00 C
ATOM 104 OE1 GLN A 17 -4.055 21.365 -6.486 1.00 16.97 O
ATOM 105 NE2 GLN A 17 -1.980 20.871 -5.762 1.00 16.04 N
ATOM 106 N VAL A 18 -6.162 17.108 -8.647 1.00 17.68 N
ATOM 107 CA VAL A 18 -6.517 17.100 -10.074 1.00 19.15 C
ATOM 108 C VAL A 18 -6.112 18.418 -10.717 1.00 19.38 C
ATOM 109 O VAL A 18 -6.315 19.491 -10.142 1.00 19.84 O
ATOM 110 CB VAL A 18 -8.053 16.946 -10.315 1.00 19.19 C
ATOM 111 CG1 VAL A 18 -8.357 16.845 -11.814 1.00 19.84 C
ATOM 112 CG2 VAL A 18 -8.609 15.746 -9.599 1.00 20.24 C
ATOM 113 N GLY A 19 -5.553 18.329 -11.918 1.00 20.11 N
ATOM 114 CA GLY A 19 -5.234 19.519 -12.699 1.00 20.97 C
ATOM 115 C GLY A 19 -5.059 19.222 -14.172 1.00 21.42 C
ATOM 116 O GLY A 19 -5.189 18.076 -14.603 1.00 21.25 O
ATOM 117 N ASN A 20 -4.774 20.270 -14.940 1.00 21.96 N
ATOM 118 CA ASN A 20 -4.419 20.137 -16.345 1.00 22.69 C
ATOM 119 C ASN A 20 -3.003 20.648 -16.581 1.00 22.73 C
ATOM 120 O ASN A 20 -2.592 21.647 -15.986 1.00 22.93 O
ATOM 121 CB ASN A 20 -5.407 20.907 -17.227 1.00 22.92 C
ATOM 122 CG ASN A 20 -6.789 20.281 -17.242 1.00 23.88 C
ATOM 123 OD1 ASN A 20 -7.691 20.739 -16.548 1.00 26.59 O
ATOM 124 ND2 ASN A 20 -6.957 19.226 -18.027 1.00 25.52 N
ATOM 125 N ILE A 21 -2.254 19.960 -17.438 1.00 23.11 N
ATOM 126 CA ILE A 21 -0.927 20.438 -17.823 1.00 23.28 C
ATOM 127 C ILE A 21 -1.109 21.546 -18.852 1.00 23.62 C
ATOM 128 O ILE A 21 -1.686 21.324 -19.920 1.00 23.81 O
ATOM 129 CB ILE A 21 -0.018 19.323 -18.402 1.00 23.34 C
ATOM 130 CG1 ILE A 21 0.068 18.127 -17.444 1.00 23.23 C
ATOM 131 CG2 ILE A 21 1.377 19.884 -18.679 1.00 23.20 C
ATOM 132 CD1 ILE A 21 0.513 16.824 -18.104 1.00 23.17 C
ATOM 133 N VAL A 22 -0.639 22.741 -18.518 1.00 23.86 N
ATOM 134 CA VAL A 22 -0.793 23.885 -19.415 1.00 24.23 C
ATOM 135 C VAL A 22 0.522 24.264 -20.102 1.00 24.55 C
ATOM 136 O VAL A 22 0.512 24.915 -21.155 1.00 24.68 O
ATOM 137 CB VAL A 22 -1.453 25.109 -18.712 1.00 24.20 C
ATOM 138 CG1 VAL A 22 -2.880 24.767 -18.279 1.00 24.62 C
ATOM 139 CG2 VAL A 22 -0.621 25.591 -17.526 1.00 24.14 C
ATOM 140 N ASP A 23 1.641 23.843 -19.513 1.00 24.68 N
ATOM 141 CA ASP A 23 2.966 24.147 -20.054 1.00 24.85 C
ATOM 142 C ASP A 23 4.035 23.144 -19.613 1.00 24.80 C
ATOM 143 O ASP A 23 3.843 22.379 -18.665 1.00 24.57 O
ATOM 144 CB ASP A 23 3.386 25.568 -19.667 1.00 25.07 C
ATOM 145 CG ASP A 23 4.334 26.199 -20.677 1.00 26.01 C
ATOM 146 OD1 ASP A 23 4.865 27.287 -20.372 1.00 27.16 O
ATOM 147 OD2 ASP A 23 4.549 25.618 -21.764 1.00 26.40 O
ATOM 148 N ILE A 24 5.165 23.165 -20.315 1.00 24.63 N
ATOM 149 CA ILE A 24 6.283 22.270 -20.038 1.00 24.56 C
ATOM 150 C ILE A 24 7.609 23.040 -20.039 1.00 24.94 C
ATOM 151 O ILE A 24 7.827 23.930 -20.867 1.00 24.80 O
ATOM 152 CB ILE A 24 6.299 21.059 -21.035 1.00 24.49 C
ATOM 153 CG1 ILE A 24 7.414 20.059 -20.693 1.00 24.26 C
ATOM 154 CG2 ILE A 24 6.383 21.529 -22.497 1.00 24.18 C
ATOM 155 CD1 ILE A 24 7.290 18.720 -21.415 1.00 23.97 C
ATOM 156 N GLY A 25 8.471 22.705 -19.084 1.00 25.27 N
ATOM 157 CA GLY A 25 9.803 23.296 -18.976 1.00 25.96 C
ATOM 158 C GLY A 25 10.854 22.211 -18.819 1.00 26.38 C
ATOM 159 O GLY A 25 10.512 21.027 -18.759 1.00 26.34 O
ATOM 160 N PRO A 26 12.142 22.601 -18.756 1.00 27.09 N
ATOM 161 CA PRO A 26 13.241 21.638 -18.628 1.00 27.73 C
ATOM 162 C PRO A 26 13.038 20.582 -17.536 1.00 28.59 C
ATOM 163 O PRO A 26 13.194 19.391 -17.808 1.00 28.96 O
ATOM 164 CB PRO A 26 14.447 22.529 -18.318 1.00 27.69 C
ATOM 165 CG PRO A 26 14.134 23.801 -19.011 1.00 27.25 C
ATOM 166 CD PRO A 26 12.647 23.986 -18.836 1.00 27.07 C
ATOM 167 N ASP A 27 12.677 20.998 -16.324 1.00 29.36 N
ATOM 168 CA ASP A 27 12.504 20.030 -15.237 1.00 30.12 C
ATOM 169 C ASP A 27 11.079 20.004 -14.670 1.00 29.87 C
ATOM 170 O ASP A 27 10.817 19.347 -13.659 1.00 30.23 O
ATOM 171 CB ASP A 27 13.540 20.267 -14.122 1.00 30.57 C
ATOM 172 CG ASP A 27 13.817 19.010 -13.291 1.00 31.94 C
ATOM 173 OD1 ASP A 27 13.492 17.888 -13.752 1.00 33.75 O
ATOM 174 OD2 ASP A 27 14.367 19.142 -12.173 1.00 33.69 O
ATOM 175 N SER A 28 10.154 20.695 -15.334 1.00 29.50 N
ATOM 176 CA SER A 28 8.818 20.866 -14.776 1.00 28.76 C
ATOM 177 C SER A 28 7.660 20.738 -15.763 1.00 28.24 C
ATOM 178 O SER A 28 7.825 20.872 -16.983 1.00 28.09 O
ATOM 179 CB SER A 28 8.721 22.209 -14.037 1.00 29.10 C
ATOM 180 OG SER A 28 8.651 23.297 -14.945 1.00 29.34 O
ATOM 181 N LEU A 29 6.489 20.449 -15.200 1.00 27.14 N
ATOM 182 CA LEU A 29 5.218 20.636 -15.871 1.00 26.36 C
ATOM 183 C LEU A 29 4.456 21.707 -15.103 1.00 26.16 C
ATOM 184 O LEU A 29 4.488 21.738 -13.868 1.00 26.13 O
ATOM 185 CB LEU A 29 4.411 19.335 -15.900 1.00 26.17 C
ATOM 186 CG LEU A 29 4.958 18.158 -16.714 1.00 25.79 C
ATOM 187 CD1 LEU A 29 4.064 16.942 -16.547 1.00 25.48 C
ATOM 188 CD2 LEU A 29 5.096 18.517 -18.189 1.00 25.19 C
ATOM 189 N THR A 30 3.786 22.592 -15.833 1.00 25.63 N
ATOM 190 CA THR A 30 2.955 23.608 -15.210 1.00 25.34 C
ATOM 191 C THR A 30 1.524 23.092 -15.140 1.00 25.03 C
ATOM 192 O THR A 30 0.927 22.726 -16.156 1.00 24.54 O
ATOM 193 CB THR A 30 3.038 24.960 -15.953 1.00 25.57 C
ATOM 194 OG1 THR A 30 4.398 25.401 -15.976 1.00 25.43 O
ATOM 195 CG2 THR A 30 2.208 26.012 -15.245 1.00 25.53 C
ATOM 196 N ILE A 31 1.000 23.041 -13.921 1.00 24.85 N
ATOM 197 CA ILE A 31 -0.312 22.469 -13.662 1.00 25.07 C
ATOM 198 C ILE A 31 -1.286 23.567 -13.262 1.00 25.37 C
ATOM 199 O ILE A 31 -0.988 24.384 -12.387 1.00 25.14 O
ATOM 200 CB ILE A 31 -0.264 21.383 -12.539 1.00 24.80 C
ATOM 201 CG1 ILE A 31 0.850 20.353 -12.790 1.00 24.91 C
ATOM 202 CG2 ILE A 31 -1.631 20.705 -12.366 1.00 24.59 C
ATOM 203 CD1 ILE A 31 0.712 19.534 -14.077 1.00 24.24 C
ATOM 204 N GLU A 32 -2.434 23.587 -13.930 1.00 26.01 N
ATOM 205 CA GLU A 32 -3.552 24.424 -13.528 1.00 27.04 C
ATOM 206 C GLU A 32 -4.516 23.571 -12.701 1.00 27.12 C
ATOM 207 O GLU A 32 -5.106 22.626 -13.226 1.00 27.09 O
ATOM 208 CB GLU A 32 -4.257 25.002 -14.756 1.00 26.94 C
ATOM 209 CG GLU A 32 -5.375 25.984 -14.439 1.00 27.77 C
ATOM 210 CD GLU A 32 -6.095 26.459 -15.686 1.00 28.00 C
ATOM 211 OE1 GLU A 32 -5.946 27.649 -16.036 1.00 30.33 O
ATOM 212 OE2 GLU A 32 -6.800 25.645 -16.322 1.00 29.79 O
ATOM 213 N PRO A 33 -4.676 23.901 -11.403 1.00 27.57 N
ATOM 214 CA PRO A 33 -5.554 23.150 -10.499 1.00 27.85 C
ATOM 215 C PRO A 33 -7.003 23.104 -10.983 1.00 28.05 C
ATOM 216 O PRO A 33 -7.488 24.078 -11.568 1.00 28.45 O
ATOM 217 CB PRO A 33 -5.467 23.940 -9.188 1.00 27.82 C
ATOM 218 CG PRO A 33 -4.183 24.677 -9.269 1.00 28.06 C
ATOM 219 CD PRO A 33 -4.023 25.027 -10.712 1.00 27.72 C
ATOM 220 N GLY A 38 -6.510 30.045 -14.368 1.00 33.44 N
ATOM 221 CA GLY A 38 -5.511 31.109 -14.350 1.00 33.23 C
ATOM 222 C GLY A 38 -4.356 30.862 -13.397 1.00 33.16 C
ATOM 223 O GLY A 38 -3.251 31.370 -13.609 1.00 33.36 O
ATOM 224 N LYS A 39 -4.613 30.084 -12.346 1.00 32.83 N
ATOM 225 CA LYS A 39 -3.604 29.775 -11.330 1.00 32.35 C
ATOM 226 C LYS A 39 -2.742 28.599 -11.773 1.00 31.85 C
ATOM 227 O LYS A 39 -3.220 27.704 -12.474 1.00 31.98 O
ATOM 228 CB LYS A 39 -4.262 29.467 -9.979 1.00 32.53 C
ATOM 229 CG LYS A 39 -4.841 30.684 -9.252 1.00 32.98 C
ATOM 230 CD LYS A 39 -6.276 30.981 -9.679 1.00 33.93 C
ATOM 231 CE LYS A 39 -6.785 32.282 -9.072 1.00 34.23 C
ATOM 232 NZ LYS A 39 -6.060 33.472 -9.594 1.00 34.56 N
ATOM 233 N THR A 40 -1.474 28.611 -11.366 1.00 31.01 N
ATOM 234 CA THR A 40 -0.520 27.571 -11.751 1.00 30.11 C
ATOM 235 C THR A 40 0.441 27.201 -10.623 1.00 29.25 C
ATOM 236 O THR A 40 0.759 28.025 -9.759 1.00 29.04 O
ATOM 237 CB THR A 40 0.338 27.991 -12.977 1.00 30.30 C
ATOM 238 OG1 THR A 40 1.064 29.190 -12.672 1.00 30.94 O
ATOM 239 CG2 THR A 40 -0.521 28.206 -14.227 1.00 30.50 C
ATOM 240 N PHE A 41 0.898 25.953 -10.642 1.00 28.06 N
ATOM 241 CA PHE A 41 2.022 25.523 -9.818 1.00 26.93 C
ATOM 242 C PHE A 41 2.919 24.572 -10.611 1.00 26.43 C
ATOM 243 O PHE A 41 2.479 23.956 -11.587 1.00 26.12 O
ATOM 244 CB PHE A 41 1.556 24.901 -8.489 1.00 26.89 C
ATOM 245 CG PHE A 41 0.802 23.600 -8.638 1.00 26.31 C
ATOM 246 CD1 PHE A 41 1.460 22.379 -8.490 1.00 25.86 C
ATOM 247 CD2 PHE A 41 -0.568 23.595 -8.895 1.00 25.92 C
ATOM 248 CE1 PHE A 41 0.771 21.174 -8.612 1.00 25.14 C
ATOM 249 CE2 PHE A 41 -1.266 22.394 -9.021 1.00 25.65 C
ATOM 250 CZ PHE A 41 -0.593 21.181 -8.880 1.00 26.00 C
ATOM 251 N LEU A 42 4.177 24.472 -10.195 1.00 25.84 N
ATOM 252 CA LEU A 42 5.141 23.619 -10.881 1.00 25.44 C
ATOM 253 C LEU A 42 5.262 22.249 -10.221 1.00 25.12 C
ATOM 254 O LEU A 42 5.230 22.121 -8.994 1.00 24.89 O
ATOM 255 CB LEU A 42 6.514 24.298 -10.957 1.00 25.54 C
ATOM 256 CG LEU A 42 6.616 25.627 -11.719 1.00 25.68 C
ATOM 257 CD1 LEU A 42 7.926 26.315 -11.392 1.00 26.57 C
ATOM 258 CD2 LEU A 42 6.478 25.426 -13.224 1.00 26.28 C
ATOM 259 N ALA A 43 5.395 21.227 -11.058 1.00 24.69 N
ATOM 260 CA ALA A 43 5.624 19.870 -10.593 1.00 24.54 C
ATOM 261 C ALA A 43 6.701 19.224 -11.453 1.00 24.52 C
ATOM 262 O ALA A 43 6.839 19.554 -12.631 1.00 24.43 O
ATOM 263 CB ALA A 43 4.342 19.069 -10.659 1.00 24.40 C
ATOM 264 N LEU A 44 7.468 18.316 -10.859 1.00 24.40 N
ATOM 265 CA LEU A 44 8.425 17.518 -11.613 1.00 24.60 C
ATOM 266 C LEU A 44 7.676 16.579 -12.552 1.00 24.59 C
ATOM 267 O LEU A 44 6.605 16.073 -12.206 1.00 24.27 O
ATOM 268 CB LEU A 44 9.319 16.707 -10.668 1.00 24.86 C
ATOM 269 CG LEU A 44 10.252 17.473 -9.720 1.00 25.25 C
ATOM 270 CD1 LEU A 44 10.934 16.511 -8.760 1.00 25.86 C
ATOM 271 CD2 LEU A 44 11.293 18.291 -10.483 1.00 25.92 C
ATOM 272 N ILE A 45 8.240 16.352 -13.736 1.00 24.66 N
ATOM 273 CA ILE A 45 7.620 15.473 -14.727 1.00 24.99 C
ATOM 274 C ILE A 45 7.279 14.102 -14.125 1.00 24.87 C
ATOM 275 O ILE A 45 6.178 13.589 -14.337 1.00 24.84 O
ATOM 276 CB ILE A 45 8.476 15.357 -16.021 1.00 25.08 C
ATOM 277 CG1 ILE A 45 8.582 16.726 -16.705 1.00 25.65 C
ATOM 278 CG2 ILE A 45 7.873 14.339 -16.993 1.00 25.54 C
ATOM 279 CD1 ILE A 45 9.744 16.856 -17.683 1.00 26.72 C
ATOM 280 N ASN A 46 8.196 13.540 -13.337 1.00 24.92 N
ATOM 281 CA ASN A 46 7.970 12.229 -12.713 1.00 25.08 C
ATOM 282 C ASN A 46 6.991 12.212 -11.523 1.00 24.79 C
ATOM 283 O ASN A 46 6.698 11.152 -10.968 1.00 25.12 O
ATOM 284 CB ASN A 46 9.304 11.544 -12.357 1.00 25.50 C
ATOM 285 CG ASN A 46 10.037 12.215 -11.199 1.00 26.44 C
ATOM 286 OD1 ASN A 46 9.671 13.301 -10.745 1.00 28.03 O
ATOM 287 ND2 ASN A 46 11.091 11.560 -10.718 1.00 28.30 N
ATOM 288 N GLN A 47 6.483 13.385 -11.147 1.00 24.23 N
ATOM 289 CA GLN A 47 5.527 13.501 -10.040 1.00 23.82 C
ATOM 290 C GLN A 47 4.094 13.712 -10.536 1.00 22.47 C
ATOM 291 O GLN A 47 3.172 13.908 -9.740 1.00 22.14 O
ATOM 292 CB GLN A 47 5.936 14.634 -9.094 1.00 23.95 C
ATOM 293 CG GLN A 47 7.210 14.365 -8.297 1.00 25.26 C
ATOM 294 CD GLN A 47 7.707 15.588 -7.538 1.00 25.70 C
ATOM 295 OE1 GLN A 47 7.409 16.735 -7.897 1.00 29.09 O
ATOM 296 NE2 GLN A 47 8.484 15.347 -6.488 1.00 28.31 N
ATOM 297 N VAL A 48 3.919 13.665 -11.855 1.00 21.38 N
ATOM 298 CA VAL A 48 2.615 13.853 -12.483 1.00 20.32 C
ATOM 299 C VAL A 48 2.151 12.541 -13.125 1.00 19.88 C
ATOM 300 O VAL A 48 2.887 11.926 -13.904 1.00 19.61 O
ATOM 301 CB VAL A 48 2.656 15.003 -13.526 1.00 20.50 C
ATOM 302 CG1 VAL A 48 1.296 15.222 -14.155 1.00 20.09 C
ATOM 303 CG2 VAL A 48 3.147 16.297 -12.876 1.00 20.31 C
ATOM 304 N PHE A 49 0.929 12.128 -12.791 1.00 19.02 N
ATOM 305 CA PHE A 49 0.397 10.828 -13.202 1.00 18.29 C
ATOM 306 C PHE A 49 -0.909 10.965 -13.980 1.00 18.10 C
ATOM 307 O PHE A 49 -1.693 11.878 -13.715 1.00 17.86 O
ATOM 308 CB PHE A 49 0.158 9.943 -11.966 1.00 18.18 C
ATOM 309 CG PHE A 49 1.403 9.637 -11.186 1.00 17.56 C
ATOM 310 CD1 PHE A 49 1.789 10.442 -10.119 1.00 17.35 C
ATOM 311 CD2 PHE A 49 2.194 8.538 -11.517 1.00 17.91 C
ATOM 312 CE1 PHE A 49 2.941 10.165 -9.395 1.00 16.86 C
ATOM 313 CE2 PHE A 49 3.349 8.249 -10.800 1.00 17.80 C
ATOM 314 CZ PHE A 49 3.725 9.064 -9.736 1.00 17.62 C
ATOM 315 N PRO A 50 -1.158 10.043 -14.932 1.00 17.88 N
ATOM 316 CA PRO A 50 -2.447 10.034 -15.616 1.00 17.91 C
ATOM 317 C PRO A 50 -3.551 9.680 -14.630 1.00 18.01 C
ATOM 318 O PRO A 50 -3.300 8.958 -13.657 1.00 17.81 O
ATOM 319 CB PRO A 50 -2.290 8.929 -16.666 1.00 17.69 C
ATOM 320 CG PRO A 50 -1.204 8.061 -16.154 1.00 18.15 C
ATOM 321 CD PRO A 50 -0.270 8.967 -15.410 1.00 17.74 C
ATOM 322 N ALA A 51 -4.745 10.208 -14.879 1.00 18.31 N
ATOM 323 CA ALA A 51 -5.900 9.984 -14.021 1.00 18.77 C
ATOM 324 C ALA A 51 -6.943 9.130 -14.735 1.00 19.24 C
ATOM 325 O ALA A 51 -6.987 9.096 -15.970 1.00 19.06 O
ATOM 326 CB ALA A 51 -6.503 11.315 -13.592 1.00 18.77 C
ATOM 327 N GLU A 52 -7.764 8.428 -13.955 1.00 19.60 N
ATOM 328 CA GLU A 52 -8.911 7.706 -14.498 1.00 20.35 C
ATOM 329 C GLU A 52 -9.909 8.706 -15.068 1.00 21.15 C
ATOM 330 O GLU A 52 -10.164 9.754 -14.467 1.00 20.84 O
ATOM 331 CB GLU A 52 -9.587 6.847 -13.423 1.00 20.20 C
ATOM 332 CG GLU A 52 -8.684 5.782 -12.800 1.00 20.10 C
ATOM 333 CD GLU A 52 -8.189 4.758 -13.803 1.00 19.29 C
ATOM 334 OE1 GLU A 52 -9.016 3.974 -14.316 1.00 20.74 O
ATOM 335 OE2 GLU A 52 -6.971 4.730 -14.069 1.00 19.44 O
ATOM 336 N GLU A 53 -10.466 8.371 -16.229 1.00 22.09 N
ATOM 337 CA GLU A 53 -11.370 9.268 -16.958 1.00 23.66 C
ATOM 338 C GLU A 53 -12.643 9.623 -16.182 1.00 23.46 C
ATOM 339 O GLU A 53 -13.131 10.757 -16.258 1.00 23.84 O
ATOM 340 CB GLU A 53 -11.707 8.667 -18.331 1.00 23.38 C
ATOM 341 CG GLU A 53 -10.510 8.625 -19.286 1.00 25.31 C
ATOM 342 CD GLU A 53 -10.716 7.718 -20.495 1.00 25.62 C
ATOM 343 OE1 GLU A 53 -11.484 6.731 -20.406 1.00 28.40 O
ATOM 344 OE2 GLU A 53 -10.091 7.991 -21.541 1.00 28.92 O
ATOM 345 N ASP A 54 -13.173 8.654 -15.441 1.00 23.62 N
ATOM 346 CA ASP A 54 -14.346 8.869 -14.598 1.00 23.72 C
ATOM 347 C ASP A 54 -13.868 9.020 -13.154 1.00 23.65 C
ATOM 348 O ASP A 54 -13.272 8.102 -12.581 1.00 23.64 O
ATOM 349 CB ASP A 54 -15.335 7.707 -14.753 1.00 24.00 C
ATOM 350 CG ASP A 54 -16.681 7.958 -14.066 1.00 24.97 C
ATOM 351 OD1 ASP A 54 -16.751 8.708 -13.063 1.00 24.81 O
ATOM 352 OD2 ASP A 54 -17.683 7.371 -14.531 1.00 26.37 O
ATOM 353 N SER A 55 -14.120 10.192 -12.584 1.00 23.15 N
ATOM 354 CA SER A 55 -13.605 10.537 -11.263 1.00 22.80 C
ATOM 355 C SER A 55 -14.550 10.133 -10.129 1.00 22.30 C
ATOM 356 O SER A 55 -14.165 10.181 -8.957 1.00 21.97 O
ATOM 357 CB SER A 55 -13.323 12.039 -11.188 1.00 22.83 C
ATOM 358 OG SER A 55 -14.533 12.778 -11.185 1.00 23.72 O
ATOM 359 N LYS A 56 -15.772 9.736 -10.486 1.00 21.82 N
ATOM 360 CA LYS A 56 -16.837 9.459 -9.511 1.00 21.72 C
ATOM 361 C LYS A 56 -17.085 7.968 -9.290 1.00 21.33 C
ATOM 362 O LYS A 56 -17.524 7.560 -8.207 1.00 20.99 O
ATOM 363 CB LYS A 56 -18.140 10.137 -9.941 1.00 21.93 C
ATOM 364 CG LYS A 56 -18.081 11.656 -9.928 1.00 23.24 C
ATOM 365 CD LYS A 56 -19.292 12.255 -10.623 1.00 26.12 C
ATOM 366 CE LYS A 56 -19.152 13.760 -10.772 1.00 27.58 C
ATOM 367 NZ LYS A 56 -20.246 14.319 -11.617 1.00 28.77 N
ATOM 368 N LYS A 57 -16.834 7.184 -10.339 1.00 21.02 N
ATOM 369 CA LYS A 57 -16.814 5.720 -10.301 1.00 20.60 C
ATOM 370 C LYS A 57 -15.709 5.226 -9.372 1.00 19.33 C
ATOM 371 O LYS A 57 -14.807 5.983 -9.010 1.00 19.11 O
ATOM 372 CB LYS A 57 -16.517 5.162 -11.706 1.00 20.91 C
ATOM 373 CG LYS A 57 -15.085 5.502 -12.212 1.00 22.43 C
ATOM 374 CD LYS A 57 -14.504 4.510 -13.231 1.00 22.29 C
ATOM 375 CE LYS A 57 -13.560 3.495 -12.581 1.00 24.96 C
ATOM 376 NZ LYS A 57 -12.134 3.955 -12.466 1.00 25.35 N
ATOM 377 N ASP A 58 -15.773 3.946 -9.022 1.00 17.63 N
ATOM 378 CA ASP A 58 -14.643 3.269 -8.395 1.00 16.32 C
ATOM 379 C ASP A 58 -14.554 1.823 -8.873 1.00 15.40 C
ATOM 380 O ASP A 58 -15.513 1.282 -9.438 1.00 14.98 O
ATOM 381 CB ASP A 58 -14.700 3.368 -6.858 1.00 16.45 C
ATOM 382 CG ASP A 58 -15.933 2.703 -6.258 1.00 17.36 C
ATOM 383 OD1 ASP A 58 -16.800 3.433 -5.741 1.00 19.70 O
ATOM 384 OD2 ASP A 58 -16.029 1.460 -6.280 1.00 17.86 O
ATOM 385 N VAL A 59 -13.390 1.217 -8.672 1.00 13.98 N
ATOM 386 CA VAL A 59 -13.201 -0.197 -8.974 1.00 13.39 C
ATOM 387 C VAL A 59 -12.904 -0.982 -7.702 1.00 13.10 C
ATOM 388 O VAL A 59 -12.237 -0.488 -6.787 1.00 12.76 O
ATOM 389 CB VAL A 59 -12.100 -0.441 -10.037 1.00 13.00 C
ATOM 390 CG1 VAL A 59 -12.542 0.099 -11.401 1.00 13.89 C
ATOM 391 CG2 VAL A 59 -10.758 0.172 -9.613 1.00 12.91 C
ATOM 392 N GLU A 60 -13.413 -2.205 -7.656 1.00 12.62 N
ATOM 393 CA GLU A 60 -13.237 -3.076 -6.498 1.00 12.84 C
ATOM 394 C GLU A 60 -11.812 -3.618 -6.381 1.00 12.58 C
ATOM 395 O GLU A 60 -11.326 -3.842 -5.273 1.00 12.74 O
ATOM 396 CB GLU A 60 -14.267 -4.208 -6.532 1.00 12.47 C
ATOM 397 CG GLU A 60 -15.701 -3.695 -6.334 1.00 12.65 C
ATOM 398 CD GLU A 60 -16.746 -4.789 -6.284 1.00 13.55 C
ATOM 399 OE1 GLU A 60 -16.556 -5.838 -6.931 1.00 16.17 O
ATOM 400 OE2 GLU A 60 -17.776 -4.588 -5.597 1.00 15.13 O
ATOM 401 N ASP A 61 -11.155 -3.817 -7.524 1.00 12.63 N
ATOM 402 CA ASP A 61 -9.759 -4.251 -7.571 1.00 12.77 C
ATOM 403 C ASP A 61 -8.943 -3.165 -8.255 1.00 12.94 C
ATOM 404 O ASP A 61 -9.211 -2.800 -9.411 1.00 12.43 O
ATOM 405 CB ASP A 61 -9.629 -5.589 -8.313 1.00 13.27 C
ATOM 406 CG ASP A 61 -8.180 -6.096 -8.411 1.00 13.58 C
ATOM 407 OD1 ASP A 61 -7.259 -5.528 -7.779 1.00 13.00 O
ATOM 408 OD2 ASP A 61 -7.961 -7.089 -9.143 1.00 16.71 O
ATOM 409 N ASN A 62 -7.954 -2.637 -7.541 1.00 12.44 N
ATOM 410 CA ASN A 62 -7.102 -1.589 -8.105 1.00 12.93 C
ATOM 411 C ASN A 62 -6.387 -2.026 -9.387 1.00 13.34 C
ATOM 412 O ASN A 62 -6.006 -1.192 -10.206 1.00 13.02 O
ATOM 413 CB ASN A 62 -6.122 -1.066 -7.056 1.00 12.84 C
ATOM 414 CG ASN A 62 -6.819 -0.264 -5.976 1.00 12.55 C
ATOM 415 OD1 ASN A 62 -7.321 0.839 -6.230 1.00 11.49 O
ATOM 416 ND2 ASN A 62 -6.865 -0.814 -4.764 1.00 12.50 N
ATOM 417 N CYS A 63 -6.239 -3.340 -9.569 1.00 13.75 N
ATOM 418 CA CYS A 63 -5.698 -3.894 -10.814 1.00 15.19 C
ATOM 419 C CYS A 63 -6.584 -3.616 -12.039 1.00 15.30 C
ATOM 420 O CYS A 63 -6.124 -3.760 -13.177 1.00 15.98 O
ATOM 421 CB CYS A 63 -5.444 -5.397 -10.672 1.00 15.44 C
ATOM 422 SG CYS A 63 -4.170 -5.807 -9.473 1.00 18.78 S
ATOM 423 N SER A 64 -7.833 -3.213 -11.795 1.00 15.28 N
ATOM 424 CA SER A 64 -8.807 -2.890 -12.851 1.00 15.75 C
ATOM 425 C SER A 64 -8.696 -1.452 -13.361 1.00 15.68 C
ATOM 426 O SER A 64 -9.351 -1.091 -14.347 1.00 15.94 O
ATOM 427 CB SER A 64 -10.237 -3.118 -12.361 1.00 15.52 C
ATOM 428 OG SER A 64 -10.489 -4.488 -12.117 1.00 17.39 O
ATOM 429 N LEU A 65 -7.893 -0.629 -12.685 1.00 15.51 N
ATOM 430 CA LEU A 65 -7.706 0.764 -13.101 1.00 15.54 C
ATOM 431 C LEU A 65 -7.062 0.814 -14.484 1.00 15.94 C
ATOM 432 O LEU A 65 -6.268 -0.059 -14.830 1.00 15.82 O
ATOM 433 CB LEU A 65 -6.834 1.529 -12.100 1.00 15.54 C
ATOM 434 CG LEU A 65 -7.359 1.790 -10.680 1.00 14.21 C
ATOM 435 CD1 LEU A 65 -6.202 2.140 -9.753 1.00 14.45 C
ATOM 436 CD2 LEU A 65 -8.434 2.875 -10.642 1.00 13.07 C
ATOM 437 N MET A 66 -7.412 1.826 -15.272 1.00 16.42 N
ATOM 438 CA MET A 66 -6.773 2.029 -16.573 1.00 17.53 C
ATOM 439 C MET A 66 -5.292 2.356 -16.396 1.00 16.70 C
ATOM 440 O MET A 66 -4.438 1.846 -17.124 1.00 16.58 O
ATOM 441 CB MET A 66 -7.472 3.140 -17.362 1.00 17.36 C
ATOM 442 CG MET A 66 -6.826 3.406 -18.713 1.00 19.31 C
ATOM 443 SD MET A 66 -7.654 4.689 -19.661 1.00 21.33 S
ATOM 444 CE MET A 66 -9.088 3.811 -20.279 1.00 21.79 C
ATOM 445 N TYR A 67 -5.000 3.206 -15.413 1.00 16.26 N
ATOM 446 CA TYR A 67 -3.632 3.560 -15.075 1.00 15.86 C
ATOM 447 C TYR A 67 -3.368 3.112 -13.653 1.00 15.53 C
ATOM 448 O TYR A 67 -4.087 3.511 -12.731 1.00 15.16 O
ATOM 449 CB TYR A 67 -3.416 5.068 -15.207 1.00 16.34 C
ATOM 450 CG TYR A 67 -3.889 5.624 -16.529 1.00 16.64 C
ATOM 451 CD1 TYR A 67 -3.152 5.420 -17.693 1.00 17.81 C
ATOM 452 CD2 TYR A 67 -5.080 6.351 -16.616 1.00 17.57 C
ATOM 453 CE1 TYR A 67 -3.584 5.929 -18.916 1.00 18.06 C
ATOM 454 CE2 TYR A 67 -5.520 6.865 -17.835 1.00 17.38 C
ATOM 455 CZ TYR A 67 -4.765 6.647 -18.978 1.00 17.59 C
ATOM 456 OH TYR A 67 -5.191 7.145 -20.189 1.00 18.50 O
ATOM 457 N LEU A 68 -2.363 2.255 -13.498 1.00 15.12 N
ATOM 458 CA LEU A 68 -1.947 1.764 -12.181 1.00 15.01 C
ATOM 459 C LEU A 68 -0.772 2.583 -11.669 1.00 14.36 C
ATOM 460 O LEU A 68 0.357 2.434 -12.140 1.00 14.43 O
ATOM 461 CB LEU A 68 -1.594 0.269 -12.233 1.00 14.96 C
ATOM 462 CG LEU A 68 -2.717 -0.766 -12.036 1.00 15.84 C
ATOM 463 CD1 LEU A 68 -3.718 -0.744 -13.173 1.00 15.92 C
ATOM 464 CD2 LEU A 68 -2.128 -2.157 -11.895 1.00 15.56 C
ATOM 465 N ASN A 69 -1.053 3.466 -10.711 1.00 13.81 N
ATOM 466 CA ASN A 69 -0.022 4.292 -10.084 1.00 13.29 C
ATOM 467 C ASN A 69 -0.484 4.767 -8.710 1.00 13.06 C
ATOM 468 O ASN A 69 -1.653 4.608 -8.363 1.00 12.86 O
ATOM 469 CB ASN A 69 0.375 5.477 -10.986 1.00 13.28 C
ATOM 470 CG ASN A 69 -0.767 6.450 -11.222 1.00 13.32 C
ATOM 471 OD1 ASN A 69 -1.284 7.064 -10.284 1.00 12.34 O
ATOM 472 ND2 ASN A 69 -1.155 6.610 -12.486 1.00 13.06 N
ATOM 473 N GLU A 70 0.424 5.351 -7.934 1.00 12.93 N
ATOM 474 CA GLU A 70 0.095 5.703 -6.547 1.00 13.36 C
ATOM 475 C GLU A 70 -1.047 6.716 -6.447 1.00 12.43 C
ATOM 476 O GLU A 70 -1.838 6.675 -5.500 1.00 12.31 O
ATOM 477 CB GLU A 70 1.336 6.173 -5.773 1.00 13.30 C
ATOM 478 CG GLU A 70 2.043 7.401 -6.340 1.00 14.59 C
ATOM 479 CD GLU A 70 3.260 7.810 -5.522 1.00 16.16 C
ATOM 480 OE1 GLU A 70 3.898 8.820 -5.888 1.00 21.12 O
ATOM 481 OE2 GLU A 70 3.582 7.131 -4.518 1.00 21.06 O
ATOM 482 N ALA A 71 -1.137 7.613 -7.429 1.00 11.65 N
ATOM 483 CA ALA A 71 -2.182 8.636 -7.441 1.00 11.17 C
ATOM 484 C ALA A 71 -3.572 8.054 -7.718 1.00 10.99 C
ATOM 485 O ALA A 71 -4.538 8.406 -7.048 1.00 10.71 O
ATOM 486 CB ALA A 71 -1.840 9.749 -8.429 1.00 11.38 C
ATOM 487 N THR A 72 -3.666 7.151 -8.693 1.00 10.67 N
ATOM 488 CA THR A 72 -4.951 6.525 -9.019 1.00 10.40 C
ATOM 489 C THR A 72 -5.375 5.558 -7.916 1.00 10.42 C
ATOM 490 O THR A 72 -6.562 5.431 -7.617 1.00 10.70 O
ATOM 491 CB THR A 72 -4.927 5.826 -10.394 1.00 10.49 C
ATOM 492 OG1 THR A 72 -3.842 4.893 -10.442 1.00 10.26 O
ATOM 493 CG2 THR A 72 -4.747 6.869 -11.509 1.00 11.00 C
ATOM 494 N LEU A 73 -4.391 4.898 -7.309 1.00 10.22 N
ATOM 495 CA LEU A 73 -4.616 4.025 -6.161 1.00 10.40 C
ATOM 496 C LEU A 73 -5.223 4.838 -5.019 1.00 9.95 C
ATOM 497 O LEU A 73 -6.248 4.460 -4.460 1.00 9.47 O
ATOM 498 CB LEU A 73 -3.292 3.391 -5.713 1.00 10.24 C
ATOM 499 CG LEU A 73 -3.287 2.571 -4.422 1.00 10.83 C
ATOM 500 CD1 LEU A 73 -4.214 1.368 -4.550 1.00 12.17 C
ATOM 501 CD2 LEU A 73 -1.865 2.126 -4.099 1.00 10.96 C
ATOM 502 N LEU A 74 -4.588 5.960 -4.693 1.00 9.99 N
ATOM 503 CA LEU A 74 -5.063 6.823 -3.619 1.00 9.91 C
ATOM 504 C LEU A 74 -6.489 7.297 -3.881 1.00 9.93 C
ATOM 505 O LEU A 74 -7.341 7.231 -2.999 1.00 9.98 O
ATOM 506 CB LEU A 74 -4.127 8.023 -3.446 1.00 9.72 C
ATOM 507 CG LEU A 74 -4.465 8.976 -2.297 1.00 9.58 C
ATOM 508 CD1 LEU A 74 -4.298 8.303 -0.931 1.00 10.48 C
ATOM 509 CD2 LEU A 74 -3.610 10.240 -2.394 1.00 10.23 C
ATOM 510 N HIS A 75 -6.748 7.751 -5.105 1.00 9.98 N
ATOM 511 CA HIS A 75 -8.058 8.283 -5.446 1.00 10.16 C
ATOM 512 C HIS A 75 -9.146 7.219 -5.380 1.00 9.77 C
ATOM 513 O HIS A 75 -10.237 7.483 -4.896 1.00 9.34 O
ATOM 514 CB HIS A 75 -8.047 8.922 -6.834 1.00 10.44 C
ATOM 515 CG HIS A 75 -9.385 9.441 -7.258 1.00 11.62 C
ATOM 516 ND1 HIS A 75 -9.956 10.563 -6.699 1.00 13.24 N
ATOM 517 CD2 HIS A 75 -10.270 8.985 -8.176 1.00 13.44 C
ATOM 518 CE1 HIS A 75 -11.136 10.778 -7.255 1.00 14.09 C
ATOM 519 NE2 HIS A 75 -11.349 9.835 -8.155 1.00 13.67 N
ATOM 520 N ASN A 76 -8.842 6.019 -5.866 1.00 9.66 N
ATOM 521 CA ASN A 76 -9.820 4.942 -5.889 1.00 9.93 C
ATOM 522 C ASN A 76 -10.237 4.569 -4.472 1.00 9.92 C
ATOM 523 O ASN A 76 -11.426 4.440 -4.181 1.00 9.48 O
ATOM 524 CB ASN A 76 -9.275 3.726 -6.639 1.00 10.29 C
ATOM 525 CG ASN A 76 -10.351 2.713 -6.948 1.00 10.62 C
ATOM 526 OD1 ASN A 76 -11.338 3.030 -7.618 1.00 12.01 O
ATOM 527 ND2 ASN A 76 -10.177 1.488 -6.451 1.00 10.79 N
ATOM 528 N ILE A 77 -9.242 4.414 -3.599 1.00 10.02 N
ATOM 529 C ILE A 77 -10.314 5.270 -1.551 1.00 10.37 C
ATOM 530 O ILE A 77 -11.215 5.007 -0.745 1.00 9.81 O
ATOM 531 CA AILE A 77 -9.486 4.146 -2.183 0.50 10.32 C
ATOM 532 CB AILE A 77 -8.149 3.912 -1.415 0.50 10.56 C
ATOM 533 CG1AILE A 77 -7.527 2.581 -1.850 0.50 11.16 C
ATOM 534 CG2AILE A 77 -8.364 3.929 0.097 0.50 11.31 C
ATOM 535 CD1AILE A 77 -6.055 2.438 -1.502 0.50 12.07 C
ATOM 537 CB BILE A 77 -8.099 4.017 -1.417 0.50 10.50 C
ATOM 538 CG1BILE A 77 -7.288 2.834 -1.966 0.50 11.11 C
ATOM 539 CG2BILE A 77 -8.294 3.914 0.097 0.50 11.30 C
ATOM 540 CD1BILE A 77 -8.021 1.509 -1.986 0.50 11.11 C
ATOM 541 N LYS A 78 -10.025 6.514 -1.939 1.00 10.51 N
ATOM 542 CA LYS A 78 -10.724 7.691 -1.420 1.00 10.77 C
ATOM 543 C LYS A 78 -12.197 7.719 -1.822 1.00 10.59 C
ATOM 544 O LYS A 78 -13.074 7.996 -0.997 1.00 10.46 O
ATOM 545 CB LYS A 78 -10.020 8.975 -1.880 1.00 10.73 C
ATOM 546 CG LYS A 78 -10.563 10.253 -1.239 1.00 11.43 C
ATOM 547 CD LYS A 78 -9.704 11.461 -1.622 1.00 12.70 C
ATOM 548 CE LYS A 78 -10.185 12.730 -0.949 1.00 16.29 C
ATOM 549 NZ LYS A 78 -9.244 13.866 -1.197 1.00 18.23 N
ATOM 550 N VAL A 79 -12.460 7.437 -3.094 1.00 10.77 N
ATOM 551 CA VAL A 79 -13.825 7.431 -3.601 1.00 10.87 C
ATOM 552 C VAL A 79 -14.617 6.355 -2.872 1.00 10.51 C
ATOM 553 O VAL A 79 -15.713 6.609 -2.364 1.00 11.04 O
ATOM 554 CB VAL A 79 -13.862 7.216 -5.133 1.00 10.88 C
ATOM 555 CG1 VAL A 79 -15.287 6.952 -5.596 1.00 11.22 C
ATOM 556 CG2 VAL A 79 -13.299 8.430 -5.843 1.00 11.30 C
ATOM 557 N ARG A 80 -14.033 5.164 -2.784 1.00 10.24 N
ATOM 558 CA ARG A 80 -14.667 4.054 -2.087 1.00 10.06 C
ATOM 559 C ARG A 80 -14.963 4.402 -0.626 1.00 9.99 C
ATOM 560 O ARG A 80 -16.079 4.202 -0.154 1.00 10.09 O
ATOM 561 CB ARG A 80 -13.828 2.783 -2.223 1.00 9.61 C
ATOM 562 CG ARG A 80 -13.883 2.206 -3.642 1.00 9.75 C
ATOM 563 CD ARG A 80 -13.119 0.905 -3.801 1.00 9.86 C
ATOM 564 NE ARG A 80 -13.663 -0.188 -2.990 1.00 10.12 N
ATOM 565 CZ ARG A 80 -14.781 -0.864 -3.260 1.00 11.32 C
ATOM 566 NH1 ARG A 80 -15.174 -1.842 -2.449 1.00 9.99 N
ATOM 567 NH2 ARG A 80 -15.514 -0.570 -4.334 1.00 10.88 N
ATOM 568 N TYR A 81 -13.981 4.978 0.063 1.00 10.22 N
ATOM 569 CA TYR A 81 -14.159 5.391 1.456 1.00 10.59 C
ATOM 570 C TYR A 81 -15.327 6.369 1.631 1.00 10.91 C
ATOM 571 O TYR A 81 -16.055 6.296 2.618 1.00 11.19 O
ATOM 572 CB TYR A 81 -12.879 6.024 1.982 1.00 10.56 C
ATOM 573 CG TYR A 81 -12.810 6.171 3.487 1.00 10.69 C
ATOM 574 CD1 TYR A 81 -12.698 5.046 4.308 1.00 11.84 C
ATOM 575 CD2 TYR A 81 -12.823 7.436 4.087 1.00 11.17 C
ATOM 576 CE1 TYR A 81 -12.618 5.167 5.693 1.00 11.66 C
ATOM 577 CE2 TYR A 81 -12.734 7.569 5.477 1.00 10.79 C
ATOM 578 CZ TYR A 81 -12.629 6.430 6.269 1.00 10.86 C
ATOM 579 OH TYR A 81 -12.538 6.548 7.640 1.00 10.88 O
ATOM 580 N SER A 82 -15.504 7.268 0.664 1.00 11.57 N
ATOM 581 CA SER A 82 -16.575 8.272 0.715 1.00 12.22 C
ATOM 582 C SER A 82 -17.964 7.642 0.552 1.00 12.48 C
ATOM 583 O SER A 82 -18.978 8.249 0.924 1.00 12.99 O
ATOM 584 CB SER A 82 -16.358 9.357 -0.349 1.00 12.28 C
ATOM 585 OG SER A 82 -16.683 8.887 -1.650 1.00 12.75 O
ATOM 586 N LYS A 83 -17.993 6.435 -0.011 1.00 12.43 N
ATOM 587 CA LYS A 83 -19.216 5.648 -0.170 1.00 12.64 C
ATOM 588 C LYS A 83 -19.312 4.557 0.907 1.00 12.81 C
ATOM 589 O LYS A 83 -20.083 3.602 0.778 1.00 12.93 O
ATOM 590 CB LYS A 83 -19.259 5.014 -1.564 1.00 12.77 C
ATOM 591 CG LYS A 83 -19.168 6.003 -2.716 1.00 13.32 C
ATOM 592 CD LYS A 83 -18.963 5.278 -4.037 1.00 13.87 C
ATOM 593 CE LYS A 83 -18.890 6.251 -5.208 1.00 15.43 C
ATOM 594 NZ LYS A 83 -18.524 5.567 -6.477 1.00 15.26 N
ATOM 595 N ASP A 84 -18.523 4.711 1.970 1.00 12.62 N
ATOM 596 CA ASP A 84 -18.472 3.739 3.074 1.00 12.65 C
ATOM 597 C ASP A 84 -18.078 2.336 2.617 1.00 12.35 C
ATOM 598 O ASP A 84 -18.551 1.329 3.166 1.00 12.83 O
ATOM 599 CB ASP A 84 -19.794 3.716 3.862 1.00 13.12 C
ATOM 600 CG ASP A 84 -20.053 5.016 4.596 1.00 14.58 C
ATOM 601 OD1 ASP A 84 -19.079 5.748 4.860 1.00 14.91 O
ATOM 602 OD2 ASP A 84 -21.228 5.314 4.906 1.00 15.52 O
ATOM 603 N ARG A 85 -17.217 2.283 1.605 1.00 11.49 N
ATOM 604 CA ARG A 85 -16.609 1.031 1.168 1.00 11.21 C
ATOM 605 C ARG A 85 -15.168 1.046 1.635 1.00 10.96 C
ATOM 606 O ARG A 85 -14.296 1.626 0.983 1.00 11.08 O
ATOM 607 CB ARG A 85 -16.697 0.872 -0.349 1.00 11.46 C
ATOM 608 CG ARG A 85 -18.122 0.825 -0.840 1.00 11.92 C
ATOM 609 CD ARG A 85 -18.230 1.049 -2.338 1.00 13.22 C
ATOM 610 NE ARG A 85 -19.635 1.259 -2.687 1.00 14.93 N
ATOM 611 CZ ARG A 85 -20.076 1.667 -3.874 1.00 15.14 C
ATOM 612 NH1 ARG A 85 -19.234 1.915 -4.873 1.00 13.65 N
ATOM 613 NH2 ARG A 85 -21.380 1.829 -4.053 1.00 16.66 N
ATOM 614 N ILE A 86 -14.932 0.424 2.787 1.00 10.64 N
ATOM 615 CA ILE A 86 -13.623 0.476 3.428 1.00 10.26 C
ATOM 616 C ILE A 86 -12.627 -0.554 2.893 1.00 9.83 C
ATOM 617 O ILE A 86 -11.423 -0.434 3.148 1.00 10.10 O
ATOM 618 CB ILE A 86 -13.734 0.360 4.979 1.00 9.87 C
ATOM 619 CG1 ILE A 86 -14.218 -1.032 5.410 1.00 11.07 C
ATOM 620 CG2 ILE A 86 -14.630 1.483 5.532 1.00 10.71 C
ATOM 621 CD1 ILE A 86 -14.087 -1.283 6.931 1.00 10.17 C
ATOM 622 N TYR A 87 -13.136 -1.557 2.171 1.00 9.14 N
ATOM 623 CA TYR A 87 -12.314 -2.637 1.626 1.00 8.88 C
ATOM 624 C TYR A 87 -12.134 -2.528 0.113 1.00 9.05 C
ATOM 625 O TYR A 87 -13.113 -2.350 -0.628 1.00 9.35 O
ATOM 626 CB TYR A 87 -12.931 -4.001 1.950 1.00 8.87 C
ATOM 627 CG TYR A 87 -13.122 -4.283 3.425 1.00 8.58 C
ATOM 628 CD1 TYR A 87 -14.386 -4.565 3.941 1.00 9.77 C
ATOM 629 CD2 TYR A 87 -12.039 -4.300 4.291 1.00 9.73 C
ATOM 630 CE1 TYR A 87 -14.572 -4.842 5.294 1.00 9.70 C
ATOM 631 CE2 TYR A 87 -12.207 -4.565 5.649 1.00 9.88 C
ATOM 632 CZ TYR A 87 -13.475 -4.838 6.144 1.00 9.67 C
ATOM 633 OH TYR A 87 -13.636 -5.103 7.486 1.00 8.64 O
ATOM 634 N THR A 88 -10.882 -2.654 -0.326 1.00 8.84 N
ATOM 635 CA THR A 88 -10.526 -2.654 -1.750 1.00 9.24 C
ATOM 636 C THR A 88 -9.353 -3.615 -1.973 1.00 9.39 C
ATOM 637 O THR A 88 -8.452 -3.707 -1.142 1.00 9.89 O
ATOM 638 CB THR A 88 -10.111 -1.239 -2.233 1.00 8.69 C
ATOM 639 OG1 THR A 88 -11.011 -0.251 -1.717 1.00 9.11 O
ATOM 640 CG2 THR A 88 -10.102 -1.151 -3.770 1.00 8.64 C
ATOM 641 N TYR A 89 -9.365 -4.325 -3.097 1.00 10.10 N
ATOM 642 CA TYR A 89 -8.287 -5.259 -3.419 1.00 10.56 C
ATOM 643 C TYR A 89 -7.139 -4.617 -4.191 1.00 10.89 C
ATOM 644 O TYR A 89 -7.322 -3.633 -4.909 1.00 11.55 O
ATOM 645 CB TYR A 89 -8.806 -6.419 -4.267 1.00 10.64 C
ATOM 646 CG TYR A 89 -9.784 -7.339 -3.581 1.00 10.86 C
ATOM 647 CD1 TYR A 89 -11.050 -7.544 -4.111 1.00 11.01 C
ATOM 648 CD2 TYR A 89 -9.435 -8.014 -2.408 1.00 11.02 C
ATOM 649 CE1 TYR A 89 -11.959 -8.398 -3.493 1.00 11.40 C
ATOM 650 CE2 TYR A 89 -10.329 -8.864 -1.778 1.00 11.69 C
ATOM 651 CZ TYR A 89 -11.591 -9.050 -2.327 1.00 11.30 C
ATOM 652 OH TYR A 89 -12.487 -9.883 -1.707 1.00 11.38 O
ATOM 653 N VAL A 90 -5.956 -5.193 -4.018 1.00 11.19 N
ATOM 654 CA VAL A 90 -4.925 -5.178 -5.045 1.00 11.60 C
ATOM 655 C VAL A 90 -4.697 -6.666 -5.296 1.00 11.80 C
ATOM 656 O VAL A 90 -3.985 -7.330 -4.538 1.00 11.83 O
ATOM 657 CB VAL A 90 -3.620 -4.487 -4.588 1.00 11.64 C
ATOM 658 CG1 VAL A 90 -2.550 -4.580 -5.684 1.00 12.17 C
ATOM 659 CG2 VAL A 90 -3.874 -3.025 -4.224 1.00 11.55 C
ATOM 660 N ALA A 91 -5.336 -7.186 -6.343 1.00 12.06 N
ATOM 661 CA ALA A 91 -5.417 -8.633 -6.591 1.00 12.30 C
ATOM 662 C ALA A 91 -5.944 -9.367 -5.352 1.00 12.60 C
ATOM 663 O ALA A 91 -7.058 -9.096 -4.913 1.00 12.93 O
ATOM 664 CB ALA A 91 -4.064 -9.205 -7.052 1.00 12.33 C
ATOM 665 N ASN A 92 -5.151 -10.283 -4.800 1.00 12.24 N
ATOM 666 CA ASN A 92 -5.553 -11.044 -3.605 1.00 12.47 C
ATOM 667 C ASN A 92 -5.111 -10.463 -2.254 1.00 11.97 C
ATOM 668 O ASN A 92 -5.246 -11.118 -1.211 1.00 11.70 O
ATOM 669 CB ASN A 92 -5.171 -12.536 -3.721 1.00 13.07 C
ATOM 670 CG ASN A 92 -3.699 -12.773 -4.075 1.00 15.40 C
ATOM 671 OD1 ASN A 92 -3.258 -13.926 -4.131 1.00 20.50 O
ATOM 672 ND2 ASN A 92 -2.946 -11.711 -4.319 1.00 16.09 N
ATOM 673 N ILE A 93 -4.601 -9.233 -2.275 1.00 11.07 N
ATOM 674 CA ILE A 93 -4.275 -8.516 -1.034 1.00 11.01 C
ATOM 675 C ILE A 93 -5.389 -7.510 -0.747 1.00 10.38 C
ATOM 676 O ILE A 93 -5.860 -6.839 -1.657 1.00 10.43 O
ATOM 677 CB ILE A 93 -2.904 -7.800 -1.130 1.00 10.90 C
ATOM 678 CG1 ILE A 93 -1.781 -8.836 -1.320 1.00 12.33 C
ATOM 679 CG2 ILE A 93 -2.656 -6.933 0.116 1.00 11.75 C
ATOM 680 CD1 ILE A 93 -0.508 -8.267 -1.911 1.00 14.27 C
ATOM 681 N LEU A 94 -5.826 -7.428 0.509 1.00 9.99 N
ATOM 682 CA LEU A 94 -6.916 -6.528 0.879 1.00 9.74 C
ATOM 683 C LEU A 94 -6.415 -5.271 1.582 1.00 9.60 C
ATOM 684 O LEU A 94 -5.598 -5.347 2.502 1.00 9.41 O
ATOM 685 CB LEU A 94 -7.930 -7.241 1.781 1.00 10.07 C
ATOM 686 CG LEU A 94 -9.222 -6.497 2.139 1.00 11.41 C
ATOM 687 CD1 LEU A 94 -10.132 -6.295 0.926 1.00 11.65 C
ATOM 688 CD2 LEU A 94 -9.947 -7.265 3.215 1.00 12.53 C
ATOM 689 N ILE A 95 -6.933 -4.126 1.146 1.00 9.44 N
ATOM 690 CA ILE A 95 -6.715 -2.845 1.822 1.00 9.71 C
ATOM 691 C ILE A 95 -7.980 -2.477 2.594 1.00 9.58 C
ATOM 692 O ILE A 95 -9.078 -2.481 2.031 1.00 9.37 O
ATOM 693 CB ILE A 95 -6.355 -1.731 0.818 1.00 10.11 C
ATOM 694 CG1 ILE A 95 -5.044 -2.080 0.097 1.00 10.43 C
ATOM 695 CG2 ILE A 95 -6.273 -0.366 1.514 1.00 9.39 C
ATOM 696 CD1 ILE A 95 -4.668 -1.119 -1.030 1.00 10.49 C
ATOM 697 N ALA A 96 -7.815 -2.178 3.881 1.00 9.12 N
ATOM 698 CA ALA A 96 -8.938 -1.817 4.757 1.00 9.15 C
ATOM 699 C ALA A 96 -8.711 -0.470 5.439 1.00 9.21 C
ATOM 700 O ALA A 96 -7.808 -0.340 6.273 1.00 9.33 O
ATOM 701 CB ALA A 96 -9.147 -2.903 5.817 1.00 8.97 C
ATOM 702 N VAL A 97 -9.525 0.527 5.102 1.00 9.22 N
ATOM 703 CA VAL A 97 -9.383 1.847 5.711 1.00 9.65 C
ATOM 704 C VAL A 97 -10.368 1.996 6.871 1.00 9.29 C
ATOM 705 O VAL A 97 -11.582 1.902 6.682 1.00 9.60 O
ATOM 706 CB VAL A 97 -9.600 2.993 4.697 1.00 9.86 C
ATOM 707 CG1 VAL A 97 -9.278 4.326 5.345 1.00 10.09 C
ATOM 708 CG2 VAL A 97 -8.740 2.790 3.448 1.00 9.86 C
ATOM 709 N ASN A 98 -9.836 2.224 8.069 1.00 9.21 N
ATOM 710 CA ASN A 98 -10.653 2.351 9.275 1.00 9.60 C
ATOM 711 C ASN A 98 -11.759 3.401 9.087 1.00 9.99 C
ATOM 712 O ASN A 98 -11.452 4.561 8.817 1.00 9.67 O
ATOM 713 CB ASN A 98 -9.744 2.736 10.447 1.00 9.14 C
ATOM 714 CG ASN A 98 -10.436 2.658 11.795 1.00 10.11 C
ATOM 715 OD1 ASN A 98 -11.659 2.582 11.888 1.00 9.05 O
ATOM 716 ND2 ASN A 98 -9.641 2.684 12.856 1.00 9.50 N
ATOM 717 N PRO A 99 -13.046 2.990 9.197 1.00 10.40 N
ATOM 718 CA PRO A 99 -14.166 3.946 9.074 1.00 10.72 C
ATOM 719 C PRO A 99 -14.401 4.827 10.308 1.00 10.85 C
ATOM 720 O PRO A 99 -15.027 5.891 10.193 1.00 10.83 O
ATOM 721 CB PRO A 99 -15.376 3.034 8.860 1.00 10.48 C
ATOM 722 CG PRO A 99 -15.025 1.775 9.592 1.00 11.18 C
ATOM 723 CD PRO A 99 -13.525 1.606 9.407 1.00 10.70 C
ATOM 724 N TYR A 100 -13.921 4.374 11.469 1.00 11.02 N
ATOM 725 CA TYR A 100 -14.143 5.051 12.762 1.00 11.34 C
ATOM 726 C TYR A 100 -15.631 5.266 13.114 1.00 12.04 C
ATOM 727 O TYR A 100 -15.984 6.153 13.919 1.00 12.10 O
ATOM 728 CB TYR A 100 -13.342 6.357 12.857 1.00 11.36 C
ATOM 729 CG TYR A 100 -11.900 6.171 13.298 1.00 11.22 C
ATOM 730 CD1 TYR A 100 -10.843 6.615 12.501 1.00 11.00 C
ATOM 731 CD2 TYR A 100 -11.596 5.551 14.515 1.00 10.88 C
ATOM 732 CE1 TYR A 100 -9.511 6.462 12.910 1.00 10.26 C
ATOM 733 CE2 TYR A 100 -10.269 5.384 14.932 1.00 10.84 C
ATOM 734 CZ TYR A 100 -9.238 5.837 14.123 1.00 10.84 C
ATOM 735 OH TYR A 100 -7.937 5.681 14.530 1.00 11.05 O
ATOM 736 N PHE A 101 -16.483 4.446 12.501 1.00 12.68 N
ATOM 737 CA PHE A 101 -17.886 4.292 12.896 1.00 13.61 C
ATOM 738 C PHE A 101 -18.424 2.947 12.415 1.00 13.99 C
ATOM 739 O PHE A 101 -17.822 2.298 11.553 1.00 13.62 O
ATOM 740 CB PHE A 101 -18.753 5.462 12.397 1.00 13.56 C
ATOM 741 CG PHE A 101 -19.210 5.335 10.964 1.00 14.08 C
ATOM 742 CD1 PHE A 101 -20.519 4.965 10.675 1.00 14.39 C
ATOM 743 CD2 PHE A 101 -18.340 5.605 9.909 1.00 13.70 C
ATOM 744 CE1 PHE A 101 -20.958 4.860 9.356 1.00 14.12 C
ATOM 745 CE2 PHE A 101 -18.767 5.495 8.589 1.00 14.49 C
ATOM 746 CZ PHE A 101 -20.077 5.122 8.313 1.00 14.14 C
ATOM 747 N ASP A 102 -19.552 2.526 12.981 1.00 15.00 N
ATOM 748 CA ASP A 102 -20.155 1.253 12.613 1.00 16.04 C
ATOM 749 C ASP A 102 -21.006 1.387 11.358 1.00 16.32 C
ATOM 750 O ASP A 102 -22.069 2.027 11.370 1.00 16.25 O
ATOM 751 CB ASP A 102 -20.972 0.678 13.776 1.00 16.48 C
ATOM 752 CG ASP A 102 -20.098 0.196 14.919 1.00 18.59 C
ATOM 753 OD1 ASP A 102 -20.370 0.574 16.083 1.00 21.64 O
ATOM 754 OD2 ASP A 102 -19.128 -0.547 14.654 1.00 19.95 O
ATOM 755 N ILE A 103 -20.512 0.803 10.269 1.00 16.60 N
ATOM 756 CA ILE A 103 -21.230 0.789 8.999 1.00 16.97 C
ATOM 757 C ILE A 103 -22.312 -0.281 9.088 1.00 17.46 C
ATOM 758 O ILE A 103 -22.007 -1.447 9.345 1.00 17.19 O
ATOM 759 CB ILE A 103 -20.283 0.516 7.803 1.00 16.81 C
ATOM 760 CG1 ILE A 103 -19.219 1.614 7.702 1.00 16.41 C
ATOM 761 CG2 ILE A 103 -21.076 0.418 6.488 1.00 16.74 C
ATOM 762 CD1 ILE A 103 -18.094 1.307 6.720 1.00 16.73 C
ATOM 763 N PRO A 104 -23.585 0.114 8.882 1.00 18.14 N
ATOM 764 CA PRO A 104 -24.690 -0.825 9.097 1.00 18.73 C
ATOM 765 C PRO A 104 -24.583 -2.068 8.223 1.00 18.93 C
ATOM 766 O PRO A 104 -24.219 -1.968 7.047 1.00 19.22 O
ATOM 767 CB PRO A 104 -25.929 -0.011 8.695 1.00 18.89 C
ATOM 768 CG PRO A 104 -25.522 1.407 8.838 1.00 18.96 C
ATOM 769 CD PRO A 104 -24.070 1.438 8.447 1.00 18.34 C
ATOM 770 N LYS A 105 -24.866 -3.227 8.818 1.00 19.22 N
ATOM 771 CA LYS A 105 -25.157 -4.469 8.085 1.00 19.43 C
ATOM 772 C LYS A 105 -23.956 -5.241 7.522 1.00 18.75 C
ATOM 773 O LYS A 105 -24.087 -6.428 7.212 1.00 18.49 O
ATOM 774 CB LYS A 105 -26.172 -4.219 6.950 1.00 19.98 C
ATOM 775 CG LYS A 105 -27.513 -3.635 7.383 1.00 22.64 C
ATOM 776 CD LYS A 105 -28.250 -3.071 6.177 1.00 26.04 C
ATOM 777 CE LYS A 105 -29.558 -2.404 6.569 1.00 27.60 C
ATOM 778 NZ LYS A 105 -30.422 -2.190 5.371 1.00 29.68 N
ATOM 779 N ILE A 106 -22.796 -4.594 7.394 1.00 18.11 N
ATOM 780 CA ILE A 106 -21.701 -5.196 6.614 1.00 17.38 C
ATOM 781 C ILE A 106 -21.014 -6.396 7.280 1.00 16.87 C
ATOM 782 O ILE A 106 -20.237 -7.098 6.629 1.00 16.62 O
ATOM 783 CB ILE A 106 -20.649 -4.157 6.104 1.00 17.64 C
ATOM 784 CG1 ILE A 106 -19.867 -3.528 7.262 1.00 17.30 C
ATOM 785 CG2 ILE A 106 -21.315 -3.100 5.209 1.00 17.95 C
ATOM 786 CD1 ILE A 106 -18.587 -2.792 6.825 1.00 17.25 C
ATOM 787 N TYR A 107 -21.306 -6.627 8.562 1.00 16.13 N
ATOM 788 CA TYR A 107 -20.789 -7.800 9.275 1.00 15.88 C
ATOM 789 C TYR A 107 -21.905 -8.716 9.777 1.00 16.07 C
ATOM 790 O TYR A 107 -21.674 -9.569 10.631 1.00 16.25 O
ATOM 791 CB TYR A 107 -19.868 -7.379 10.431 1.00 15.59 C
ATOM 792 CG TYR A 107 -18.756 -6.454 9.993 1.00 14.85 C
ATOM 793 CD1 TYR A 107 -18.750 -5.113 10.376 1.00 15.54 C
ATOM 794 CD2 TYR A 107 -17.723 -6.911 9.173 1.00 14.44 C
ATOM 795 CE1 TYR A 107 -17.735 -4.250 9.970 1.00 15.20 C
ATOM 796 CE2 TYR A 107 -16.701 -6.052 8.753 1.00 13.90 C
ATOM 797 CZ TYR A 107 -16.716 -4.726 9.157 1.00 14.61 C
ATOM 798 OH TYR A 107 -15.717 -3.863 8.752 1.00 14.93 O
ATOM 799 N SER A 108 -23.107 -8.548 9.223 1.00 16.25 N
ATOM 800 CA SER A 108 -24.271 -9.343 9.631 1.00 16.67 C
ATOM 801 C SER A 108 -24.116 -10.827 9.291 1.00 16.95 C
ATOM 802 O SER A 108 -23.306 -11.198 8.436 1.00 16.37 O
ATOM 803 CB SER A 108 -25.535 -8.805 8.963 1.00 16.70 C
ATOM 804 OG SER A 108 -25.518 -9.080 7.574 1.00 17.54 O
ATOM 805 N SER A 109 -24.914 -11.663 9.952 1.00 17.24 N
ATOM 806 CA SER A 109 -24.963 -13.094 9.658 1.00 17.94 C
ATOM 807 C SER A 109 -25.389 -13.361 8.209 1.00 17.99 C
ATOM 808 O SER A 109 -24.925 -14.322 7.595 1.00 18.12 O
ATOM 809 CB SER A 109 -25.903 -13.818 10.632 1.00 18.07 C
ATOM 810 OG SER A 109 -25.310 -13.948 11.913 1.00 19.59 O
ATOM 811 N GLU A 110 -26.265 -12.507 7.676 1.00 18.49 N
ATOM 812 CA GLU A 110 -26.679 -12.576 6.269 1.00 19.34 C
ATOM 813 C GLU A 110 -25.490 -12.350 5.334 1.00 18.15 C
ATOM 814 O GLU A 110 -25.307 -13.078 4.354 1.00 18.36 O
ATOM 815 CB GLU A 110 -27.780 -11.552 5.974 1.00 19.65 C
ATOM 816 CG GLU A 110 -28.318 -11.603 4.548 1.00 21.64 C
ATOM 817 CD GLU A 110 -29.508 -10.683 4.307 1.00 22.24 C
ATOM 818 OE1 GLU A 110 -30.309 -10.996 3.397 1.00 26.17 O
ATOM 819 OE2 GLU A 110 -29.645 -9.651 5.009 1.00 26.70 O
ATOM 820 N THR A 111 -24.693 -11.332 5.646 1.00 17.01 N
ATOM 821 CA THR A 111 -23.493 -11.014 4.876 1.00 15.96 C
ATOM 822 C THR A 111 -22.488 -12.168 4.942 1.00 15.34 C
ATOM 823 O THR A 111 -21.948 -12.586 3.916 1.00 14.95 O
ATOM 824 CB THR A 111 -22.867 -9.680 5.345 1.00 15.98 C
ATOM 825 OG1 THR A 111 -23.855 -8.643 5.263 1.00 16.14 O
ATOM 826 CG2 THR A 111 -21.670 -9.302 4.473 1.00 15.25 C
ATOM 827 N ILE A 112 -22.271 -12.700 6.145 1.00 14.94 N
ATOM 828 CA ILE A 112 -21.400 -13.864 6.335 1.00 14.55 C
ATOM 829 C ILE A 112 -21.803 -15.011 5.401 1.00 14.88 C
ATOM 830 O ILE A 112 -20.969 -15.557 4.680 1.00 14.67 O
ATOM 831 CB ILE A 112 -21.385 -14.347 7.819 1.00 14.40 C
ATOM 832 CG1 ILE A 112 -20.648 -13.333 8.702 1.00 13.96 C
ATOM 833 CG2 ILE A 112 -20.736 -15.722 7.932 1.00 14.04 C
ATOM 834 CD1 ILE A 112 -20.603 -13.690 10.196 1.00 14.22 C
ATOM 835 N LYS A 113 -23.089 -15.356 5.403 1.00 15.53 N
ATOM 836 CA LYS A 113 -23.597 -16.433 4.552 1.00 16.12 C
ATOM 837 C LYS A 113 -23.316 -16.178 3.070 1.00 15.78 C
ATOM 838 O LYS A 113 -22.947 -17.100 2.343 1.00 16.17 O
ATOM 839 CB LYS A 113 -25.095 -16.660 4.793 1.00 16.44 C
ATOM 840 CG LYS A 113 -25.384 -17.298 6.144 1.00 19.41 C
ATOM 841 CD LYS A 113 -26.811 -17.830 6.240 1.00 22.99 C
ATOM 842 CE LYS A 113 -27.189 -18.125 7.687 1.00 25.51 C
ATOM 843 NZ LYS A 113 -27.550 -16.882 8.430 1.00 28.22 N
ATOM 844 N SER A 114 -23.451 -14.920 2.654 1.00 15.70 N
ATOM 845 CA SER A 114 -23.307 -14.522 1.249 1.00 15.59 C
ATOM 846 C SER A 114 -21.881 -14.642 0.701 1.00 15.19 C
ATOM 847 O SER A 114 -21.689 -14.654 -0.519 1.00 15.23 O
ATOM 848 CB SER A 114 -23.840 -13.102 1.029 1.00 15.79 C
ATOM 849 OG SER A 114 -22.946 -12.120 1.531 1.00 17.04 O
ATOM 850 N TYR A 115 -20.891 -14.704 1.596 1.00 14.42 N
ATOM 851 CA TYR A 115 -19.486 -14.853 1.194 1.00 14.32 C
ATOM 852 C TYR A 115 -19.003 -16.303 1.133 1.00 14.40 C
ATOM 853 O TYR A 115 -17.919 -16.582 0.614 1.00 14.41 O
ATOM 854 CB TYR A 115 -18.563 -13.992 2.085 1.00 13.81 C
ATOM 855 CG TYR A 115 -18.509 -12.563 1.606 1.00 13.12 C
ATOM 856 CD1 TYR A 115 -17.526 -12.148 0.702 1.00 12.62 C
ATOM 857 CD2 TYR A 115 -19.467 -11.636 2.015 1.00 11.87 C
ATOM 858 CE1 TYR A 115 -17.492 -10.835 0.234 1.00 11.79 C
ATOM 859 CE2 TYR A 115 -19.450 -10.326 1.549 1.00 12.29 C
ATOM 860 CZ TYR A 115 -18.465 -9.933 0.658 1.00 12.14 C
ATOM 861 OH TYR A 115 -18.452 -8.640 0.200 1.00 13.62 O
ATOM 862 N GLN A 116 -19.805 -17.230 1.651 1.00 14.55 N
ATOM 863 CA GLN A 116 -19.370 -18.629 1.749 1.00 15.14 C
ATOM 864 C GLN A 116 -19.194 -19.301 0.382 1.00 15.08 C
ATOM 865 O GLN A 116 -20.124 -19.347 -0.427 1.00 15.06 O
ATOM 866 CB GLN A 116 -20.314 -19.427 2.654 1.00 15.13 C
ATOM 867 CG GLN A 116 -20.262 -18.974 4.108 1.00 15.70 C
ATOM 868 CD GLN A 116 -21.389 -19.525 4.972 1.00 16.47 C
ATOM 869 OE1 GLN A 116 -21.486 -19.194 6.157 1.00 18.26 O
ATOM 870 NE2 GLN A 116 -22.245 -20.356 4.387 1.00 16.60 N
ATOM 871 N GLY A 117 -17.983 -19.789 0.130 1.00 14.99 N
ATOM 872 CA GLY A 117 -17.649 -20.482 -1.116 1.00 15.16 C
ATOM 873 C GLY A 117 -17.517 -19.605 -2.351 1.00 15.33 C
ATOM 874 O GLY A 117 -17.410 -20.122 -3.469 1.00 15.84 O
ATOM 875 N LYS A 118 -17.510 -18.285 -2.167 1.00 14.78 N
ATOM 876 CA LYS A 118 -17.405 -17.362 -3.304 1.00 14.83 C
ATOM 877 C LYS A 118 -15.955 -17.020 -3.608 1.00 14.46 C
ATOM 878 O LYS A 118 -15.210 -16.592 -2.725 1.00 14.45 O
ATOM 879 CB LYS A 118 -18.203 -16.075 -3.055 1.00 14.83 C
ATOM 880 CG LYS A 118 -19.650 -16.290 -2.649 1.00 16.54 C
ATOM 881 CD LYS A 118 -20.520 -16.748 -3.812 1.00 18.75 C
ATOM 882 CE LYS A 118 -21.938 -17.034 -3.337 1.00 20.43 C
ATOM 883 NZ LYS A 118 -22.649 -15.791 -2.903 1.00 21.19 N
ATOM 884 N SER A 119 -15.560 -17.215 -4.864 1.00 13.75 N
ATOM 885 CA SER A 119 -14.233 -16.821 -5.331 1.00 13.53 C
ATOM 886 C SER A 119 -14.005 -15.320 -5.156 1.00 13.27 C
ATOM 887 O SER A 119 -14.956 -14.537 -5.157 1.00 13.03 O
ATOM 888 CB SER A 119 -14.065 -17.186 -6.806 1.00 13.51 C
ATOM 889 OG SER A 119 -14.212 -18.584 -6.999 1.00 14.14 O
ATOM 890 N LEU A 120 -12.742 -14.929 -5.009 1.00 13.59 N
ATOM 891 CA LEU A 120 -12.372 -13.513 -4.966 1.00 14.02 C
ATOM 892 C LEU A 120 -12.878 -12.819 -6.221 1.00 14.20 C
ATOM 893 O LEU A 120 -12.720 -13.340 -7.322 1.00 14.21 O
ATOM 894 CB LEU A 120 -10.850 -13.349 -4.882 1.00 13.88 C
ATOM 895 CG LEU A 120 -10.128 -13.717 -3.590 1.00 15.10 C
ATOM 896 CD1 LEU A 120 -8.629 -13.656 -3.822 1.00 15.53 C
ATOM 897 CD2 LEU A 120 -10.532 -12.784 -2.447 1.00 14.80 C
ATOM 898 N GLY A 121 -13.504 -11.658 -6.040 1.00 14.38 N
ATOM 899 CA GLY A 121 -13.996 -10.860 -7.155 1.00 14.91 C
ATOM 900 C GLY A 121 -15.438 -11.137 -7.545 1.00 15.14 C
ATOM 901 O GLY A 121 -16.024 -10.383 -8.324 1.00 15.67 O
ATOM 902 N THR A 122 -16.016 -12.213 -7.012 1.00 14.67 N
ATOM 903 CA THR A 122 -17.422 -12.554 -7.295 1.00 14.73 C
ATOM 904 C THR A 122 -18.382 -11.903 -6.290 1.00 14.62 C
ATOM 905 O THR A 122 -19.599 -11.946 -6.454 1.00 14.48 O
ATOM 906 CB THR A 122 -17.651 -14.086 -7.354 1.00 14.81 C
ATOM 907 OG1 THR A 122 -17.499 -14.660 -6.049 1.00 15.60 O
ATOM 908 CG2 THR A 122 -16.663 -14.737 -8.311 1.00 14.87 C
ATOM 909 N MET A 123 -17.801 -11.321 -5.244 1.00 14.25 N
ATOM 910 CA MET A 123 -18.502 -10.558 -4.221 1.00 13.88 C
ATOM 911 C MET A 123 -17.669 -9.291 -4.018 1.00 13.50 C
ATOM 912 O MET A 123 -16.475 -9.296 -4.340 1.00 13.73 O
ATOM 913 CB MET A 123 -18.549 -11.333 -2.899 1.00 13.96 C
ATOM 914 CG MET A 123 -19.405 -12.593 -2.894 1.00 14.50 C
ATOM 915 SD MET A 123 -21.152 -12.266 -3.201 1.00 16.34 S
ATOM 916 CE MET A 123 -21.672 -11.517 -1.657 1.00 16.24 C
ATOM 917 N PRO A 124 -18.278 -8.208 -3.487 1.00 13.10 N
ATOM 918 CA PRO A 124 -17.484 -7.009 -3.185 1.00 12.59 C
ATOM 919 C PRO A 124 -16.333 -7.301 -2.219 1.00 11.96 C
ATOM 920 O PRO A 124 -16.407 -8.259 -1.437 1.00 11.53 O
ATOM 921 CB PRO A 124 -18.505 -6.064 -2.540 1.00 12.91 C
ATOM 922 CG PRO A 124 -19.824 -6.506 -3.113 1.00 13.29 C
ATOM 923 CD PRO A 124 -19.702 -8.004 -3.163 1.00 13.12 C
ATOM 924 N PRO A 125 -15.261 -6.492 -2.282 1.00 11.23 N
ATOM 925 CA PRO A 125 -14.119 -6.706 -1.397 1.00 10.67 C
ATOM 926 C PRO A 125 -14.545 -6.715 0.066 1.00 10.19 C
ATOM 927 O PRO A 125 -15.367 -5.895 0.482 1.00 9.99 O
ATOM 928 CB PRO A 125 -13.225 -5.497 -1.685 1.00 11.02 C
ATOM 929 CG PRO A 125 -13.562 -5.125 -3.094 1.00 11.03 C
ATOM 930 CD PRO A 125 -15.049 -5.341 -3.176 1.00 11.15 C
ATOM 931 N HIS A 126 -13.989 -7.644 0.832 1.00 9.86 N
ATOM 932 CA HIS A 126 -14.375 -7.809 2.225 1.00 9.64 C
ATOM 933 C HIS A 126 -13.386 -8.717 2.936 1.00 9.59 C
ATOM 934 O HIS A 126 -12.816 -9.637 2.337 1.00 9.50 O
ATOM 935 CB HIS A 126 -15.779 -8.427 2.297 1.00 9.85 C
ATOM 936 CG HIS A 126 -16.530 -8.114 3.554 1.00 10.74 C
ATOM 937 ND1 HIS A 126 -16.164 -8.610 4.787 1.00 11.46 N
ATOM 938 CD2 HIS A 126 -17.657 -7.390 3.762 1.00 11.58 C
ATOM 939 CE1 HIS A 126 -17.017 -8.185 5.703 1.00 11.52 C
ATOM 940 NE2 HIS A 126 -17.935 -7.447 5.106 1.00 11.45 N
ATOM 941 N VAL A 127 -13.189 -8.449 4.221 1.00 9.72 N
ATOM 942 C VAL A 127 -12.918 -10.765 5.033 1.00 9.91 C
ATOM 943 O VAL A 127 -12.142 -11.710 5.099 1.00 9.78 O
ATOM 944 CA AVAL A 127 -12.403 -9.317 5.089 0.50 9.74 C
ATOM 945 CB AVAL A 127 -12.382 -8.764 6.544 0.50 9.88 C
ATOM 946 CG1AVAL A 127 -13.755 -8.852 7.206 0.50 10.19 C
ATOM 947 CG2AVAL A 127 -11.337 -9.461 7.368 0.50 9.42 C
ATOM 949 CB BVAL A 127 -12.269 -8.839 6.521 0.50 10.01 C
ATOM 950 CG1BVAL A 127 -11.201 -7.770 6.609 0.50 10.19 C
ATOM 951 CG2BVAL A 127 -13.611 -8.331 7.050 0.50 10.19 C
ATOM 952 N PHE A 128 -14.237 -10.920 4.901 1.00 10.37 N
ATOM 953 CA PHE A 128 -14.859 -12.252 4.804 1.00 10.49 C
ATOM 954 C PHE A 128 -14.341 -13.039 3.589 1.00 10.64 C
ATOM 955 O PHE A 128 -14.156 -14.259 3.658 1.00 10.36 O
ATOM 956 CB PHE A 128 -16.391 -12.155 4.726 1.00 10.70 C
ATOM 957 CG PHE A 128 -17.062 -11.612 5.976 1.00 10.87 C
ATOM 958 CD1 PHE A 128 -16.402 -11.571 7.212 1.00 11.03 C
ATOM 959 CD2 PHE A 128 -18.383 -11.175 5.917 1.00 11.70 C
ATOM 960 CE1 PHE A 128 -17.044 -11.072 8.356 1.00 11.12 C
ATOM 961 CE2 PHE A 128 -19.031 -10.680 7.048 1.00 12.06 C
ATOM 962 CZ PHE A 128 -18.360 -10.626 8.271 1.00 11.99 C
ATOM 963 N ALA A 129 -14.121 -12.334 2.482 1.00 10.69 N
ATOM 964 CA ALA A 129 -13.596 -12.947 1.265 1.00 11.07 C
ATOM 965 C ALA A 129 -12.153 -13.431 1.436 1.00 10.98 C
ATOM 966 O ALA A 129 -11.779 -14.473 0.900 1.00 11.08 O
ATOM 967 CB ALA A 129 -13.707 -11.988 0.099 1.00 11.33 C
ATOM 968 N ILE A 130 -11.347 -12.673 2.181 1.00 11.07 N
ATOM 969 CA ILE A 130 -9.980 -13.100 2.500 1.00 11.03 C
ATOM 970 C ILE A 130 -10.017 -14.362 3.368 1.00 11.33 C
ATOM 971 O ILE A 130 -9.262 -15.311 3.133 1.00 11.41 O
ATOM 972 CB ILE A 130 -9.179 -11.970 3.196 1.00 11.14 C
ATOM 973 CG1 ILE A 130 -8.993 -10.779 2.241 1.00 10.82 C
ATOM 974 CG2 ILE A 130 -7.836 -12.483 3.744 1.00 11.39 C
ATOM 975 CD1 ILE A 130 -8.213 -11.086 0.935 1.00 11.97 C
ATOM 976 N ALA A 131 -10.916 -14.363 4.351 1.00 11.38 N
ATOM 977 CA ALA A 131 -11.128 -15.512 5.234 1.00 11.79 C
ATOM 978 C ALA A 131 -11.557 -16.749 4.449 1.00 12.08 C
ATOM 979 O ALA A 131 -11.030 -17.841 4.665 1.00 11.74 O
ATOM 980 CB ALA A 131 -12.156 -15.179 6.289 1.00 12.11 C
ATOM 981 N ASP A 132 -12.507 -16.572 3.534 1.00 12.56 N
ATOM 982 CA ASP A 132 -12.987 -17.693 2.725 1.00 13.71 C
ATOM 983 C ASP A 132 -11.908 -18.217 1.772 1.00 13.86 C
ATOM 984 O ASP A 132 -11.812 -19.425 1.538 1.00 13.99 O
ATOM 985 CB ASP A 132 -14.251 -17.321 1.952 1.00 14.00 C
ATOM 986 CG ASP A 132 -15.111 -18.534 1.645 1.00 15.78 C
ATOM 987 OD1 ASP A 132 -15.792 -19.018 2.571 1.00 17.42 O
ATOM 988 OD2 ASP A 132 -15.089 -19.006 0.494 1.00 19.22 O
ATOM 989 N LYS A 133 -11.096 -17.306 1.237 1.00 14.03 N
ATOM 990 CA LYS A 133 -9.990 -17.676 0.361 1.00 14.75 C
ATOM 991 C LYS A 133 -8.960 -18.511 1.117 1.00 14.51 C
ATOM 992 O LYS A 133 -8.450 -19.495 0.585 1.00 14.63 O
ATOM 993 CB LYS A 133 -9.349 -16.429 -0.252 1.00 14.98 C
ATOM 994 CG LYS A 133 -8.104 -16.682 -1.099 1.00 17.89 C
ATOM 995 CD LYS A 133 -8.425 -17.309 -2.445 1.00 21.93 C
ATOM 996 CE LYS A 133 -7.340 -16.970 -3.472 1.00 23.28 C
ATOM 997 NZ LYS A 133 -5.947 -17.104 -2.938 1.00 24.94 N
ATOM 998 N ALA A 134 -8.671 -18.125 2.362 1.00 14.33 N
ATOM 999 CA ALA A 134 -7.770 -18.911 3.214 1.00 14.35 C
ATOM 1000 C ALA A 134 -8.320 -20.322 3.438 1.00 14.52 C
ATOM 1001 O ALA A 134 -7.589 -21.310 3.337 1.00 14.32 O
ATOM 1002 CB ALA A 134 -7.541 -18.212 4.543 1.00 14.53 C
ATOM 1003 N PHE A 135 -9.613 -20.399 3.738 1.00 14.79 N
ATOM 1004 CA PHE A 135 -10.298 -21.675 3.921 1.00 15.60 C
ATOM 1005 C PHE A 135 -10.207 -22.542 2.661 1.00 16.15 C
ATOM 1006 O PHE A 135 -9.859 -23.720 2.742 1.00 15.78 O
ATOM 1007 CB PHE A 135 -11.760 -21.441 4.326 1.00 15.74 C
ATOM 1008 CG PHE A 135 -12.533 -22.709 4.562 1.00 16.21 C
ATOM 1009 CD1 PHE A 135 -12.343 -23.451 5.726 1.00 16.23 C
ATOM 1010 CD2 PHE A 135 -13.444 -23.164 3.615 1.00 17.03 C
ATOM 1011 CE1 PHE A 135 -13.059 -24.632 5.949 1.00 16.33 C
ATOM 1012 CE2 PHE A 135 -14.161 -24.342 3.825 1.00 18.23 C
ATOM 1013 CZ PHE A 135 -13.967 -25.073 4.991 1.00 16.85 C
ATOM 1014 N ARG A 136 -10.511 -21.943 1.510 1.00 17.00 N
ATOM 1015 CA ARG A 136 -10.445 -22.622 0.209 1.00 18.52 C
ATOM 1016 C ARG A 136 -9.042 -23.146 -0.092 1.00 18.37 C
ATOM 1017 O ARG A 136 -8.878 -24.296 -0.510 1.00 18.31 O
ATOM 1018 CB ARG A 136 -10.905 -21.667 -0.899 1.00 18.35 C
ATOM 1019 CG ARG A 136 -10.879 -22.229 -2.327 1.00 20.03 C
ATOM 1020 CD ARG A 136 -11.324 -21.165 -3.342 1.00 20.78 C
ATOM 1021 NE ARG A 136 -12.606 -20.593 -2.940 1.00 25.53 N
ATOM 1022 CZ ARG A 136 -12.803 -19.339 -2.532 1.00 26.89 C
ATOM 1023 NH1 ARG A 136 -14.020 -18.966 -2.170 1.00 28.30 N
ATOM 1024 NH2 ARG A 136 -11.810 -18.454 -2.501 1.00 27.22 N
ATOM 1025 N ASP A 137 -8.033 -22.304 0.128 1.00 18.33 N
ATOM 1026 CA ASP A 137 -6.644 -22.708 -0.084 1.00 18.64 C
ATOM 1027 C ASP A 137 -6.227 -23.837 0.853 1.00 18.55 C
ATOM 1028 O ASP A 137 -5.523 -24.756 0.437 1.00 18.43 O
ATOM 1029 CB ASP A 137 -5.699 -21.516 0.061 1.00 18.82 C
ATOM 1030 CG ASP A 137 -5.795 -20.545 -1.105 1.00 20.19 C
ATOM 1031 OD1 ASP A 137 -5.362 -19.389 -0.939 1.00 22.01 O
ATOM 1032 OD2 ASP A 137 -6.305 -20.926 -2.183 1.00 22.11 O
ATOM 1033 N MET A 138 -6.676 -23.770 2.108 1.00 18.55 N
ATOM 1034 CA MET A 138 -6.402 -24.813 3.089 1.00 19.03 C
ATOM 1035 C MET A 138 -6.935 -26.160 2.596 1.00 19.69 C
ATOM 1036 O MET A 138 -6.229 -27.165 2.653 1.00 19.59 O
ATOM 1037 CB MET A 138 -7.019 -24.455 4.444 1.00 18.57 C
ATOM 1038 CG MET A 138 -6.705 -25.443 5.557 1.00 18.87 C
ATOM 1039 SD MET A 138 -7.779 -25.268 6.994 1.00 18.86 S
ATOM 1040 CE MET A 138 -9.335 -25.909 6.365 1.00 19.58 C
ATOM 1041 N LYS A 139 -8.175 -26.152 2.105 1.00 20.50 N
ATOM 1042 CA LYS A 139 -8.833 -27.339 1.541 1.00 21.76 C
ATOM 1043 C LYS A 139 -8.167 -27.861 0.268 1.00 21.81 C
ATOM 1044 O LYS A 139 -7.911 -29.062 0.145 1.00 22.20 O
ATOM 1045 CB LYS A 139 -10.294 -27.020 1.221 1.00 22.00 C
ATOM 1046 CG LYS A 139 -11.283 -27.291 2.326 1.00 24.05 C
ATOM 1047 CD LYS A 139 -12.696 -27.037 1.805 1.00 26.55 C
ATOM 1048 CE LYS A 139 -13.730 -27.853 2.554 1.00 28.39 C
ATOM 1049 NZ LYS A 139 -15.121 -27.501 2.144 1.00 30.06 N
ATOM 1050 N VAL A 140 -7.912 -26.964 -0.680 1.00 22.16 N
ATOM 1051 CA VAL A 140 -7.406 -27.346 -2.003 1.00 22.27 C
ATOM 1052 C VAL A 140 -5.927 -27.747 -1.967 1.00 22.28 C
ATOM 1053 O VAL A 140 -5.535 -28.752 -2.573 1.00 22.38 O
ATOM 1054 CB VAL A 140 -7.661 -26.231 -3.064 1.00 22.42 C
ATOM 1055 CG1 VAL A 140 -7.035 -26.586 -4.417 1.00 22.93 C
ATOM 1056 CG2 VAL A 140 -9.152 -25.986 -3.233 1.00 22.52 C
ATOM 1057 N LEU A 141 -5.116 -26.975 -1.245 1.00 21.79 N
ATOM 1058 CA LEU A 141 -3.671 -27.201 -1.215 1.00 21.75 C
ATOM 1059 C LEU A 141 -3.204 -28.107 -0.072 1.00 21.26 C
ATOM 1060 O LEU A 141 -2.046 -28.536 -0.052 1.00 21.47 O
ATOM 1061 CB LEU A 141 -2.914 -25.866 -1.191 1.00 21.91 C
ATOM 1062 CG LEU A 141 -3.165 -24.908 -2.359 1.00 23.07 C
ATOM 1063 CD1 LEU A 141 -2.581 -23.543 -2.060 1.00 23.79 C
ATOM 1064 CD2 LEU A 141 -2.604 -25.466 -3.674 1.00 24.41 C
ATOM 1065 N LYS A 142 -4.110 -28.409 0.858 1.00 20.75 N
ATOM 1066 CA LYS A 142 -3.803 -29.225 2.043 1.00 20.34 C
ATOM 1067 C LYS A 142 -2.622 -28.614 2.803 1.00 19.58 C
ATOM 1068 O LYS A 142 -1.608 -29.268 3.076 1.00 19.42 O
ATOM 1069 CB LYS A 142 -3.555 -30.695 1.663 1.00 20.89 C
ATOM 1070 CG LYS A 142 -4.545 -31.235 0.636 1.00 22.74 C
ATOM 1071 CD LYS A 142 -5.158 -32.560 1.068 1.00 26.60 C
ATOM 1072 CE LYS A 142 -6.589 -32.368 1.578 1.00 28.46 C
ATOM 1073 NZ LYS A 142 -6.699 -31.354 2.672 1.00 30.83 N
ATOM 1074 N LEU A 143 -2.775 -27.335 3.125 1.00 18.54 N
ATOM 1075 CA LEU A 143 -1.712 -26.537 3.708 1.00 17.96 C
ATOM 1076 C LEU A 143 -2.340 -25.561 4.692 1.00 16.80 C
ATOM 1077 O LEU A 143 -3.289 -24.859 4.350 1.00 15.85 O
ATOM 1078 CB LEU A 143 -0.972 -25.776 2.598 1.00 18.20 C
ATOM 1079 CG LEU A 143 0.136 -24.761 2.919 1.00 19.09 C
ATOM 1080 CD1 LEU A 143 1.333 -25.443 3.563 1.00 20.18 C
ATOM 1081 CD2 LEU A 143 0.561 -24.006 1.671 1.00 18.83 C
ATOM 1082 N SER A 144 -1.817 -25.529 5.914 1.00 16.07 N
ATOM 1083 CA SER A 144 -2.277 -24.555 6.902 1.00 15.30 C
ATOM 1084 C SER A 144 -2.039 -23.140 6.385 1.00 14.81 C
ATOM 1085 O SER A 144 -1.157 -22.916 5.548 1.00 14.86 O
ATOM 1086 CB SER A 144 -1.598 -24.783 8.248 1.00 15.60 C
ATOM 1087 OG SER A 144 -2.126 -25.945 8.868 1.00 15.34 O
ATOM 1088 N GLN A 145 -2.846 -22.200 6.871 1.00 14.18 N
ATOM 1089 CA GLN A 145 -2.867 -20.847 6.325 1.00 13.43 C
ATOM 1090 C GLN A 145 -2.721 -19.794 7.411 1.00 12.73 C
ATOM 1091 O GLN A 145 -3.187 -19.981 8.538 1.00 12.84 O
ATOM 1092 CB GLN A 145 -4.169 -20.599 5.553 1.00 13.65 C
ATOM 1093 CG GLN A 145 -4.408 -21.545 4.377 1.00 14.71 C
ATOM 1094 CD GLN A 145 -3.490 -21.281 3.208 1.00 15.50 C
ATOM 1095 OE1 GLN A 145 -3.298 -20.133 2.794 1.00 17.05 O
ATOM 1096 NE2 GLN A 145 -2.921 -22.347 2.655 1.00 17.33 N
ATOM 1097 N SER A 146 -2.068 -18.692 7.061 1.00 12.16 N
ATOM 1098 C SER A 146 -2.585 -16.309 7.276 1.00 11.97 C
ATOM 1099 O SER A 146 -2.392 -16.087 6.076 1.00 12.03 O
ATOM 1100 CA ASER A 146 -1.998 -17.541 7.949 0.50 11.97 C
ATOM 1101 CB ASER A 146 -0.560 -17.267 8.392 0.50 12.05 C
ATOM 1102 OG ASER A 146 0.240 -16.853 7.301 0.50 11.60 O
ATOM 1104 CB BSER A 146 -0.529 -17.263 8.343 0.50 12.15 C
ATOM 1105 OG BSER A 146 0.023 -18.359 9.057 0.50 12.26 O
ATOM 1106 N ILE A 147 -3.315 -15.524 8.060 1.00 11.41 N
ATOM 1107 CA ILE A 147 -3.845 -14.252 7.598 1.00 10.86 C
ATOM 1108 C ILE A 147 -3.153 -13.197 8.445 1.00 10.69 C
ATOM 1109 O ILE A 147 -3.305 -13.178 9.676 1.00 10.56 O
ATOM 1110 CB ILE A 147 -5.379 -14.181 7.732 1.00 10.99 C
ATOM 1111 CG1 ILE A 147 -6.028 -15.246 6.830 1.00 11.23 C
ATOM 1112 CG2 ILE A 147 -5.888 -12.775 7.392 1.00 11.01 C
ATOM 1113 CD1 ILE A 147 -7.492 -15.526 7.136 1.00 11.22 C
ATOM 1114 N ILE A 148 -2.368 -12.356 7.777 1.00 10.52 N
ATOM 1115 C ILE A 148 -2.277 -9.993 8.341 1.00 10.58 C
ATOM 1116 O ILE A 148 -2.500 -9.485 7.245 1.00 10.36 O
ATOM 1117 CA AILE A 148 -1.569 -11.335 8.455 0.50 10.57 C
ATOM 1118 CB AILE A 148 -0.116 -11.243 7.896 0.50 10.75 C
ATOM 1119 CG1AILE A 148 0.641 -12.558 8.099 0.50 11.34 C
ATOM 1120 CG2AILE A 148 0.663 -10.099 8.554 0.50 10.75 C
ATOM 1121 CD1AILE A 148 0.663 -13.438 6.876 0.50 12.08 C
ATOM 1123 CB BILE A 148 -0.137 -11.238 7.821 0.50 10.69 C
ATOM 1124 CG1BILE A 148 0.506 -12.628 7.674 0.50 11.21 C
ATOM 1125 CG2BILE A 148 0.756 -10.277 8.625 0.50 10.61 C
ATOM 1126 CD1BILE A 148 0.640 -13.415 8.975 0.50 11.55 C
ATOM 1127 N VAL A 149 -2.637 -9.429 9.489 1.00 10.22 N
ATOM 1128 CA VAL A 149 -3.375 -8.171 9.510 1.00 10.30 C
ATOM 1129 C VAL A 149 -2.415 -7.093 10.019 1.00 10.67 C
ATOM 1130 O VAL A 149 -2.116 -7.044 11.214 1.00 11.37 O
ATOM 1131 CB VAL A 149 -4.657 -8.281 10.365 1.00 10.48 C
ATOM 1132 CG1 VAL A 149 -5.564 -7.092 10.131 1.00 10.30 C
ATOM 1133 CG2 VAL A 149 -5.418 -9.573 10.033 1.00 11.17 C
ATOM 1134 N SER A 150 -1.926 -6.259 9.099 1.00 10.20 N
ATOM 1135 C SER A 150 -1.382 -3.848 9.421 1.00 10.14 C
ATOM 1136 O SER A 150 -2.479 -3.559 8.925 1.00 10.62 O
ATOM 1137 CA ASER A 150 -0.873 -5.284 9.408 0.50 10.33 C
ATOM 1138 CB ASER A 150 0.261 -5.394 8.390 0.50 10.26 C
ATOM 1139 OG ASER A 150 -0.174 -4.924 7.127 0.50 11.49 O
ATOM 1141 CB BSER A 150 0.294 -5.414 8.414 0.50 10.07 C
ATOM 1142 OG BSER A 150 0.830 -6.729 8.396 0.50 10.32 O
ATOM 1143 N GLY A 151 -0.567 -2.947 9.966 1.00 10.11 N
ATOM 1144 CA GLY A 151 -0.918 -1.531 10.034 1.00 10.22 C
ATOM 1145 C GLY A 151 -0.436 -0.874 11.310 1.00 10.32 C
ATOM 1146 O GLY A 151 -0.110 -1.549 12.292 1.00 10.62 O
ATOM 1147 N GLU A 152 -0.394 0.455 11.299 1.00 9.85 N
ATOM 1148 CA GLU A 152 0.034 1.212 12.469 1.00 10.25 C
ATOM 1149 C GLU A 152 -1.037 1.189 13.559 1.00 9.34 C
ATOM 1150 O GLU A 152 -2.165 0.725 13.337 1.00 8.65 O
ATOM 1151 CB GLU A 152 0.403 2.654 12.079 1.00 10.32 C
ATOM 1152 CG GLU A 152 -0.776 3.524 11.686 1.00 11.80 C
ATOM 1153 CD GLU A 152 -0.359 4.951 11.373 1.00 12.95 C
ATOM 1154 OE1 GLU A 152 -0.509 5.354 10.211 1.00 17.42 O
ATOM 1155 OE2 GLU A 152 0.140 5.660 12.280 1.00 16.26 O
ATOM 1156 N SER A 153 -0.665 1.660 14.744 1.00 8.74 N
ATOM 1157 CA SER A 153 -1.593 1.740 15.853 1.00 8.86 C
ATOM 1158 C SER A 153 -2.874 2.481 15.472 1.00 8.48 C
ATOM 1159 O SER A 153 -2.829 3.600 14.942 1.00 9.05 O
ATOM 1160 CB SER A 153 -0.925 2.396 17.062 1.00 8.59 C
ATOM 1161 OG SER A 153 -1.858 2.567 18.106 1.00 9.73 O
ATOM 1162 N GLY A 154 -4.009 1.842 15.754 1.00 8.61 N
ATOM 1163 CA GLY A 154 -5.326 2.409 15.480 1.00 8.38 C
ATOM 1164 C GLY A 154 -5.844 2.207 14.062 1.00 8.35 C
ATOM 1165 O GLY A 154 -6.890 2.747 13.712 1.00 8.90 O
ATOM 1166 N ALA A 155 -5.116 1.446 13.246 1.00 8.19 N
ATOM 1167 CA ALA A 155 -5.497 1.241 11.840 1.00 7.99 C
ATOM 1168 C ALA A 155 -6.702 0.316 11.651 1.00 8.16 C
ATOM 1169 O ALA A 155 -7.398 0.413 10.633 1.00 8.45 O
ATOM 1170 CB ALA A 155 -4.310 0.744 11.027 1.00 7.87 C
ATOM 1171 N GLY A 156 -6.923 -0.592 12.605 1.00 8.01 N
ATOM 1172 CA GLY A 156 -8.052 -1.525 12.553 1.00 7.80 C
ATOM 1173 C GLY A 156 -7.707 -3.009 12.521 1.00 7.53 C
ATOM 1174 O GLY A 156 -8.557 -3.831 12.162 1.00 7.93 O
ATOM 1175 N LYS A 157 -6.485 -3.363 12.929 1.00 7.57 N
ATOM 1176 CA LYS A 157 -6.025 -4.762 12.908 1.00 7.51 C
ATOM 1177 C LYS A 157 -6.862 -5.666 13.803 1.00 7.73 C
ATOM 1178 O LYS A 157 -7.285 -6.755 13.396 1.00 7.89 O
ATOM 1179 CB LYS A 157 -4.549 -4.867 13.316 1.00 7.38 C
ATOM 1180 CG LYS A 157 -3.591 -4.092 12.427 1.00 7.04 C
ATOM 1181 CD LYS A 157 -2.153 -4.281 12.887 1.00 7.81 C
ATOM 1182 CE LYS A 157 -1.895 -3.654 14.267 1.00 7.00 C
ATOM 1183 NZ LYS A 157 -2.134 -2.167 14.264 1.00 6.80 N
ATOM 1184 N THR A 158 -7.093 -5.217 15.028 1.00 7.60 N
ATOM 1185 CA THR A 158 -7.835 -6.015 16.004 1.00 7.72 C
ATOM 1186 C THR A 158 -9.288 -6.208 15.581 1.00 7.82 C
ATOM 1187 O THR A 158 -9.813 -7.332 15.629 1.00 7.84 O
ATOM 1188 CB THR A 158 -7.707 -5.399 17.406 1.00 7.39 C
ATOM 1189 OG1 THR A 158 -6.358 -5.586 17.852 1.00 7.44 O
ATOM 1190 CG2 THR A 158 -8.678 -6.040 18.414 1.00 8.25 C
ATOM 1191 N GLU A 159 -9.928 -5.135 15.129 1.00 8.09 N
ATOM 1192 CA GLU A 159 -11.294 -5.262 14.632 1.00 8.84 C
ATOM 1193 C GLU A 159 -11.394 -6.268 13.478 1.00 8.87 C
ATOM 1194 O GLU A 159 -12.269 -7.142 13.482 1.00 9.01 O
ATOM 1195 CB GLU A 159 -11.895 -3.901 14.267 1.00 8.95 C
ATOM 1196 CG GLU A 159 -12.180 -3.019 15.492 1.00 10.48 C
ATOM 1197 CD GLU A 159 -12.909 -3.758 16.609 1.00 12.73 C
ATOM 1198 OE1 GLU A 159 -14.055 -4.205 16.380 1.00 13.49 O
ATOM 1199 OE2 GLU A 159 -12.333 -3.901 17.716 1.00 13.44 O
ATOM 1200 N ASN A 160 -10.482 -6.170 12.511 1.00 8.99 N
ATOM 1201 CA ASN A 160 -10.508 -7.085 11.371 1.00 9.23 C
ATOM 1202 C ASN A 160 -10.165 -8.531 11.714 1.00 9.26 C
ATOM 1203 O ASN A 160 -10.728 -9.463 11.133 1.00 9.05 O
ATOM 1204 CB ASN A 160 -9.664 -6.541 10.226 1.00 9.37 C
ATOM 1205 CG ASN A 160 -10.359 -5.404 9.518 1.00 10.14 C
ATOM 1206 OD1 ASN A 160 -11.272 -5.626 8.725 1.00 11.91 O
ATOM 1207 ND2 ASN A 160 -9.964 -4.179 9.831 1.00 10.19 N
ATOM 1208 N THR A 161 -9.271 -8.712 12.683 1.00 9.04 N
ATOM 1209 CA THR A 161 -8.996 -10.040 13.237 1.00 9.78 C
ATOM 1210 C THR A 161 -10.283 -10.654 13.794 1.00 9.94 C
ATOM 1211 O THR A 161 -10.606 -11.807 13.504 1.00 10.15 O
ATOM 1212 CB THR A 161 -7.902 -9.951 14.325 1.00 9.66 C
ATOM 1213 OG1 THR A 161 -6.696 -9.481 13.717 1.00 10.77 O
ATOM 1214 CG2 THR A 161 -7.639 -11.320 14.982 1.00 10.22 C
ATOM 1215 N LYS A 162 -11.033 -9.868 14.561 1.00 10.02 N
ATOM 1216 CA LYS A 162 -12.301 -10.339 15.112 1.00 10.62 C
ATOM 1217 C LYS A 162 -13.312 -10.709 14.018 1.00 10.63 C
ATOM 1218 O LYS A 162 -14.021 -11.716 14.148 1.00 10.71 O
ATOM 1219 CB LYS A 162 -12.879 -9.324 16.099 1.00 10.98 C
ATOM 1220 CG LYS A 162 -12.119 -9.297 17.422 1.00 11.87 C
ATOM 1221 CD LYS A 162 -12.799 -8.427 18.450 1.00 15.09 C
ATOM 1222 CE LYS A 162 -12.468 -6.968 18.232 1.00 14.99 C
ATOM 1223 NZ LYS A 162 -12.805 -6.151 19.434 1.00 14.84 N
ATOM 1224 N PHE A 163 -13.354 -9.933 12.934 1.00 10.80 N
ATOM 1225 CA PHE A 163 -14.264 -10.245 11.816 1.00 11.21 C
ATOM 1226 C PHE A 163 -13.896 -11.566 11.150 1.00 11.39 C
ATOM 1227 O PHE A 163 -14.778 -12.364 10.816 1.00 11.57 O
ATOM 1228 CB PHE A 163 -14.278 -9.142 10.747 1.00 11.40 C
ATOM 1229 CG PHE A 163 -14.625 -7.774 11.264 1.00 12.18 C
ATOM 1230 CD1 PHE A 163 -13.926 -6.662 10.804 1.00 13.36 C
ATOM 1231 CD2 PHE A 163 -15.640 -7.588 12.201 1.00 13.22 C
ATOM 1232 CE1 PHE A 163 -14.221 -5.387 11.268 1.00 13.38 C
ATOM 1233 CE2 PHE A 163 -15.948 -6.308 12.671 1.00 15.19 C
ATOM 1234 CZ PHE A 163 -15.238 -5.208 12.205 1.00 14.04 C
ATOM 1235 N VAL A 164 -12.597 -11.780 10.930 1.00 11.21 N
ATOM 1236 CA VAL A 164 -12.109 -13.033 10.337 1.00 11.47 C
ATOM 1237 C VAL A 164 -12.488 -14.225 11.216 1.00 12.06 C
ATOM 1238 O VAL A 164 -12.999 -15.232 10.721 1.00 11.51 O
ATOM 1239 CB VAL A 164 -10.568 -13.017 10.093 1.00 11.39 C
ATOM 1240 CG1 VAL A 164 -10.061 -14.407 9.723 1.00 11.08 C
ATOM 1241 CG2 VAL A 164 -10.199 -12.021 9.000 1.00 10.58 C
ATOM 1242 N LEU A 165 -12.250 -14.098 12.522 1.00 12.31 N
ATOM 1243 CA LEU A 165 -12.555 -15.186 13.457 1.00 13.26 C
ATOM 1244 C LEU A 165 -14.045 -15.488 13.510 1.00 13.59 C
ATOM 1245 O LEU A 165 -14.438 -16.661 13.541 1.00 13.76 O
ATOM 1246 CB LEU A 165 -12.006 -14.882 14.854 1.00 13.03 C
ATOM 1247 CG LEU A 165 -10.480 -14.718 14.941 1.00 14.10 C
ATOM 1248 CD1 LEU A 165 -10.073 -14.219 16.324 1.00 15.64 C
ATOM 1249 CD2 LEU A 165 -9.735 -15.998 14.572 1.00 15.60 C
ATOM 1250 N ARG A 166 -14.866 -14.435 13.504 1.00 14.06 N
ATOM 1251 CA ARG A 166 -16.321 -14.585 13.493 1.00 15.36 C
ATOM 1252 C ARG A 166 -16.767 -15.280 12.213 1.00 14.81 C
ATOM 1253 O ARG A 166 -17.567 -16.212 12.261 1.00 15.00 O
ATOM 1254 CB ARG A 166 -17.026 -13.233 13.642 1.00 15.32 C
ATOM 1255 CG ARG A 166 -18.546 -13.333 13.810 1.00 17.29 C
ATOM 1256 CD ARG A 166 -19.181 -11.983 14.123 1.00 18.13 C
ATOM 1257 NE ARG A 166 -18.801 -11.454 15.438 1.00 24.21 N
ATOM 1258 CZ ARG A 166 -19.613 -11.384 16.495 1.00 25.69 C
ATOM 1259 NH1 ARG A 166 -20.866 -11.819 16.416 1.00 27.52 N
ATOM 1260 NH2 ARG A 166 -19.171 -10.877 17.640 1.00 26.24 N
ATOM 1261 N TYR A 167 -16.227 -14.841 11.078 1.00 14.18 N
ATOM 1262 CA TYR A 167 -16.583 -15.439 9.794 1.00 14.30 C
ATOM 1263 C TYR A 167 -16.320 -16.945 9.741 1.00 14.42 C
ATOM 1264 O TYR A 167 -17.190 -17.722 9.322 1.00 14.67 O
ATOM 1265 CB TYR A 167 -15.858 -14.753 8.631 1.00 13.93 C
ATOM 1266 CG TYR A 167 -16.193 -15.407 7.316 1.00 14.01 C
ATOM 1267 CD1 TYR A 167 -17.361 -15.065 6.631 1.00 14.49 C
ATOM 1268 CD2 TYR A 167 -15.381 -16.412 6.785 1.00 13.61 C
ATOM 1269 CE1 TYR A 167 -17.697 -15.685 5.431 1.00 13.84 C
ATOM 1270 CE2 TYR A 167 -15.709 -17.041 5.578 1.00 13.83 C
ATOM 1271 CZ TYR A 167 -16.870 -16.668 4.918 1.00 13.97 C
ATOM 1272 OH TYR A 167 -17.211 -17.278 3.735 1.00 15.32 O
ATOM 1273 N LEU A 168 -15.123 -17.349 10.156 1.00 14.39 N
ATOM 1274 CA LEU A 168 -14.690 -18.740 10.027 1.00 14.90 C
ATOM 1275 C LEU A 168 -15.446 -19.674 10.968 1.00 15.42 C
ATOM 1276 O LEU A 168 -15.826 -20.781 10.576 1.00 15.51 O
ATOM 1277 CB LEU A 168 -13.179 -18.865 10.242 1.00 14.80 C
ATOM 1278 CG LEU A 168 -12.251 -18.295 9.158 1.00 14.43 C
ATOM 1279 CD1 LEU A 168 -10.805 -18.231 9.639 1.00 15.79 C
ATOM 1280 CD2 LEU A 168 -12.358 -19.085 7.854 1.00 15.57 C
ATOM 1281 N THR A 169 -15.655 -19.228 12.205 1.00 16.03 N
ATOM 1282 CA THR A 169 -16.345 -20.050 13.205 1.00 16.83 C
ATOM 1283 C THR A 169 -17.850 -20.144 12.944 1.00 17.56 C
ATOM 1284 O THR A 169 -18.459 -21.185 13.196 1.00 17.83 O
ATOM 1285 CB THR A 169 -16.078 -19.561 14.641 1.00 16.67 C
ATOM 1286 OG1 THR A 169 -16.498 -18.197 14.776 1.00 16.33 O
ATOM 1287 CG2 THR A 169 -14.591 -19.672 14.963 1.00 17.09 C
ATOM 1288 N GLU A 170 -18.442 -19.067 12.432 1.00 17.83 N
ATOM 1289 CA GLU A 170 -19.865 -19.069 12.075 1.00 18.80 C
ATOM 1290 C GLU A 170 -20.135 -19.894 10.811 1.00 18.92 C
ATOM 1291 O GLU A 170 -21.156 -20.585 10.721 1.00 19.09 O
ATOM 1292 CB GLU A 170 -20.398 -17.640 11.923 1.00 18.61 C
ATOM 1293 CG GLU A 170 -21.906 -17.557 11.721 1.00 20.00 C
ATOM 1294 CD GLU A 170 -22.490 -16.185 12.023 1.00 19.81 C
ATOM 1295 OE1 GLU A 170 -23.481 -15.827 11.361 1.00 22.48 O
ATOM 1296 OE2 GLU A 170 -21.982 -15.472 12.917 1.00 21.85 O
ATOM 1297 N SER A 171 -19.214 -19.831 9.850 1.00 19.00 N
ATOM 1298 CA SER A 171 -19.387 -20.516 8.568 1.00 19.34 C
ATOM 1299 C SER A 171 -19.073 -22.008 8.626 1.00 20.15 C
ATOM 1300 O SER A 171 -19.787 -22.816 8.031 1.00 20.24 O
ATOM 1301 CB SER A 171 -18.528 -19.864 7.480 1.00 19.09 C
ATOM 1302 OG SER A 171 -18.847 -18.494 7.339 1.00 17.31 O
ATOM 1303 N TYR A 172 -18.004 -22.366 9.333 1.00 21.06 N
ATOM 1304 CA TYR A 172 -17.452 -23.719 9.236 1.00 22.27 C
ATOM 1305 C TYR A 172 -17.330 -24.447 10.576 1.00 22.85 C
ATOM 1306 O TYR A 172 -16.684 -25.496 10.671 1.00 22.92 O
ATOM 1307 CB TYR A 172 -16.127 -23.688 8.459 1.00 22.48 C
ATOM 1308 CG TYR A 172 -16.278 -23.038 7.095 1.00 23.16 C
ATOM 1309 CD1 TYR A 172 -15.590 -21.866 6.771 1.00 23.41 C
ATOM 1310 CD2 TYR A 172 -17.146 -23.577 6.142 1.00 23.54 C
ATOM 1311 CE1 TYR A 172 -15.748 -21.262 5.514 1.00 23.31 C
ATOM 1312 CE2 TYR A 172 -17.316 -22.981 4.896 1.00 23.64 C
ATOM 1313 CZ TYR A 172 -16.617 -21.830 4.586 1.00 23.55 C
ATOM 1314 OH TYR A 172 -16.796 -21.258 3.346 1.00 23.89 O
ATOM 1315 N GLY A 173 -17.988 -23.899 11.594 1.00 23.63 N
ATOM 1316 CA GLY A 173 -18.025 -24.501 12.925 1.00 24.57 C
ATOM 1317 C GLY A 173 -19.208 -25.433 13.104 1.00 25.15 C
ATOM 1318 O GLY A 173 -20.177 -25.382 12.340 1.00 26.22 O
ATOM 1319 N ASP A 180 -17.707 -20.303 18.044 1.00 28.14 N
ATOM 1320 CA ASP A 180 -18.426 -19.264 18.775 1.00 27.90 C
ATOM 1321 C ASP A 180 -17.760 -18.874 20.102 1.00 27.09 C
ATOM 1322 O ASP A 180 -17.735 -17.696 20.457 1.00 26.89 O
ATOM 1323 CB ASP A 180 -19.873 -19.682 19.015 1.00 28.50 C
ATOM 1324 CG ASP A 180 -20.719 -18.557 19.570 1.00 29.51 C
ATOM 1325 OD1 ASP A 180 -21.208 -17.721 18.777 1.00 31.71 O
ATOM 1326 OD2 ASP A 180 -20.908 -18.520 20.802 1.00 31.42 O
ATOM 1327 N ARG A 181 -17.240 -19.857 20.838 1.00 26.25 N
ATOM 1328 CA ARG A 181 -16.513 -19.568 22.077 1.00 25.45 C
ATOM 1329 C ARG A 181 -15.199 -18.841 21.796 1.00 24.90 C
ATOM 1330 O ARG A 181 -14.737 -18.047 22.617 1.00 24.35 O
ATOM 1331 CB ARG A 181 -16.272 -20.837 22.899 1.00 25.67 C
ATOM 1332 CG ARG A 181 -17.528 -21.357 23.593 1.00 26.16 C
ATOM 1333 CD ARG A 181 -17.203 -22.328 24.721 1.00 27.86 C
ATOM 1334 NE ARG A 181 -16.587 -23.557 24.229 1.00 28.86 N
ATOM 1335 CZ ARG A 181 -17.256 -24.650 23.868 1.00 29.78 C
ATOM 1336 NH1 ARG A 181 -18.582 -24.684 23.942 1.00 30.18 N
ATOM 1337 NH2 ARG A 181 -16.592 -25.713 23.433 1.00 29.95 N
ATOM 1338 N ILE A 182 -14.615 -19.113 20.629 1.00 24.14 N
ATOM 1339 CA ILE A 182 -13.441 -18.379 20.146 1.00 24.01 C
ATOM 1340 C ILE A 182 -13.764 -16.884 20.021 1.00 23.70 C
ATOM 1341 O ILE A 182 -12.957 -16.025 20.394 1.00 23.66 O
ATOM 1342 CB ILE A 182 -12.928 -18.957 18.797 1.00 23.94 C
ATOM 1343 CG1 ILE A 182 -12.264 -20.322 19.026 1.00 24.58 C
ATOM 1344 CG2 ILE A 182 -11.950 -17.990 18.130 1.00 24.40 C
ATOM 1345 CD1 ILE A 182 -12.239 -21.248 17.816 1.00 24.64 C
ATOM 1346 N VAL A 183 -14.958 -16.593 19.508 1.00 23.24 N
ATOM 1347 CA VAL A 183 -15.463 -15.228 19.384 1.00 23.07 C
ATOM 1348 C VAL A 183 -15.801 -14.648 20.760 1.00 23.00 C
ATOM 1349 O VAL A 183 -15.415 -13.524 21.087 1.00 21.99 O
ATOM 1350 CB VAL A 183 -16.722 -15.192 18.472 1.00 23.21 C
ATOM 1351 CG1 VAL A 183 -17.379 -13.810 18.473 1.00 23.46 C
ATOM 1352 CG2 VAL A 183 -16.367 -15.627 17.061 1.00 23.12 C
ATOM 1353 N GLU A 184 -16.510 -15.438 21.563 1.00 23.20 N
ATOM 1354 CA GLU A 184 -17.036 -14.978 22.848 1.00 23.68 C
ATOM 1355 C GLU A 184 -15.952 -14.683 23.886 1.00 23.15 C
ATOM 1356 O GLU A 184 -16.173 -13.895 24.802 1.00 22.97 O
ATOM 1357 CB GLU A 184 -18.050 -15.986 23.401 1.00 24.09 C
ATOM 1358 CG GLU A 184 -19.415 -15.957 22.701 1.00 26.44 C
ATOM 1359 CD GLU A 184 -20.216 -14.694 22.997 1.00 29.46 C
ATOM 1360 OE1 GLU A 184 -20.110 -14.156 24.121 1.00 31.25 O
ATOM 1361 OE2 GLU A 184 -20.961 -14.241 22.100 1.00 31.76 O
ATOM 1362 N ALA A 185 -14.785 -15.308 23.731 1.00 22.85 N
ATOM 1363 CA ALA A 185 -13.685 -15.150 24.686 1.00 22.64 C
ATOM 1364 C ALA A 185 -12.956 -13.814 24.554 1.00 22.52 C
ATOM 1365 O ALA A 185 -12.193 -13.428 25.443 1.00 22.60 O
ATOM 1366 CB ALA A 185 -12.702 -16.306 24.553 1.00 22.73 C
ATOM 1367 N ASN A 186 -13.198 -13.106 23.454 1.00 22.06 N
ATOM 1368 CA ASN A 186 -12.455 -11.880 23.149 1.00 21.92 C
ATOM 1369 C ASN A 186 -12.513 -10.744 24.192 1.00 21.05 C
ATOM 1370 O ASN A 186 -11.469 -10.154 24.501 1.00 21.03 O
ATOM 1371 CB ASN A 186 -12.811 -11.352 21.760 1.00 22.62 C
ATOM 1372 CG ASN A 186 -11.653 -10.651 21.111 1.00 24.52 C
ATOM 1373 OD1 ASN A 186 -10.744 -11.292 20.579 1.00 27.56 O
ATOM 1374 ND2 ASN A 186 -11.660 -9.325 21.166 1.00 26.40 N
ATOM 1375 N PRO A 187 -13.717 -10.419 24.724 1.00 20.02 N
ATOM 1376 CA PRO A 187 -13.814 -9.428 25.803 1.00 19.36 C
ATOM 1377 C PRO A 187 -12.884 -9.697 26.991 1.00 18.59 C
ATOM 1378 O PRO A 187 -12.441 -8.755 27.646 1.00 18.46 O
ATOM 1379 CB PRO A 187 -15.277 -9.538 26.247 1.00 19.46 C
ATOM 1380 CG PRO A 187 -15.994 -9.966 25.019 1.00 19.75 C
ATOM 1381 CD PRO A 187 -15.056 -10.912 24.332 1.00 20.01 C
ATOM 1382 N LEU A 188 -12.593 -10.967 27.259 1.00 17.69 N
ATOM 1383 CA LEU A 188 -11.697 -11.335 28.352 1.00 17.20 C
ATOM 1384 C LEU A 188 -10.244 -10.959 28.046 1.00 16.12 C
ATOM 1385 O LEU A 188 -9.559 -10.360 28.880 1.00 15.78 O
ATOM 1386 CB LEU A 188 -11.827 -12.833 28.658 1.00 17.49 C
ATOM 1387 CG LEU A 188 -11.098 -13.445 29.851 1.00 18.49 C
ATOM 1388 CD1 LEU A 188 -11.357 -12.650 31.113 1.00 20.08 C
ATOM 1389 CD2 LEU A 188 -11.529 -14.902 30.026 1.00 18.19 C
ATOM 1390 N LEU A 189 -9.778 -11.301 26.847 1.00 15.14 N
ATOM 1391 CA LEU A 189 -8.414 -10.966 26.441 1.00 14.39 C
ATOM 1392 C LEU A 189 -8.224 -9.450 26.402 1.00 13.82 C
ATOM 1393 O LEU A 189 -7.232 -8.931 26.919 1.00 13.55 O
ATOM 1394 CB LEU A 189 -8.079 -11.577 25.074 1.00 14.73 C
ATOM 1395 CG LEU A 189 -8.041 -13.105 24.973 1.00 15.77 C
ATOM 1396 CD1 LEU A 189 -7.662 -13.516 23.562 1.00 17.04 C
ATOM 1397 CD2 LEU A 189 -7.065 -13.683 25.981 1.00 16.96 C
ATOM 1398 N GLU A 190 -9.187 -8.748 25.807 1.00 13.22 N
ATOM 1399 CA GLU A 190 -9.112 -7.285 25.697 1.00 13.24 C
ATOM 1400 C GLU A 190 -9.150 -6.581 27.053 1.00 12.59 C
ATOM 1401 O GLU A 190 -8.518 -5.540 27.232 1.00 11.90 O
ATOM 1402 CB GLU A 190 -10.212 -6.741 24.772 1.00 13.76 C
ATOM 1403 CG GLU A 190 -10.077 -7.255 23.351 1.00 15.79 C
ATOM 1404 CD GLU A 190 -10.778 -6.400 22.306 1.00 18.46 C
ATOM 1405 OE1 GLU A 190 -11.519 -5.461 22.665 1.00 19.17 O
ATOM 1406 OE2 GLU A 190 -10.573 -6.683 21.107 1.00 19.76 O
ATOM 1407 N ALA A 191 -9.884 -7.147 28.010 1.00 11.89 N
ATOM 1408 CA ALA A 191 -9.924 -6.556 29.345 1.00 11.45 C
ATOM 1409 C ALA A 191 -8.526 -6.543 29.970 1.00 10.80 C
ATOM 1410 O ALA A 191 -8.133 -5.561 30.592 1.00 10.71 O
ATOM 1411 CB ALA A 191 -10.899 -7.301 30.234 1.00 11.51 C
ATOM 1412 N PHE A 192 -7.778 -7.628 29.775 1.00 10.44 N
ATOM 1413 CA PHE A 192 -6.494 -7.807 30.458 1.00 10.40 C
ATOM 1414 C PHE A 192 -5.296 -7.328 29.646 1.00 9.97 C
ATOM 1415 O PHE A 192 -4.240 -7.031 30.208 1.00 10.06 O
ATOM 1416 CB PHE A 192 -6.313 -9.267 30.891 1.00 10.51 C
ATOM 1417 CG PHE A 192 -7.174 -9.652 32.061 1.00 11.48 C
ATOM 1418 CD1 PHE A 192 -8.469 -10.131 31.859 1.00 12.19 C
ATOM 1419 CD2 PHE A 192 -6.704 -9.502 33.368 1.00 12.08 C
ATOM 1420 CE1 PHE A 192 -9.283 -10.468 32.943 1.00 11.85 C
ATOM 1421 CE2 PHE A 192 -7.515 -9.840 34.461 1.00 12.22 C
ATOM 1422 CZ PHE A 192 -8.800 -10.320 34.245 1.00 11.76 C
ATOM 1423 N GLY A 193 -5.473 -7.230 28.330 1.00 9.50 N
ATOM 1424 CA GLY A 193 -4.358 -6.906 27.439 1.00 9.58 C
ATOM 1425 C GLY A 193 -4.458 -5.646 26.600 1.00 9.45 C
ATOM 1426 O GLY A 193 -3.509 -5.320 25.881 1.00 9.60 O
ATOM 1427 N ASN A 194 -5.596 -4.950 26.670 1.00 9.39 N
ATOM 1428 CA ASN A 194 -5.813 -3.711 25.908 1.00 9.31 C
ATOM 1429 C ASN A 194 -5.910 -2.501 26.833 1.00 9.68 C
ATOM 1430 O ASN A 194 -6.321 -2.630 28.003 1.00 9.15 O
ATOM 1431 CB ASN A 194 -7.079 -3.791 25.020 1.00 9.14 C
ATOM 1432 CG ASN A 194 -6.882 -4.634 23.752 1.00 10.10 C
ATOM 1433 OD1 ASN A 194 -7.277 -4.223 22.655 1.00 11.91 O
ATOM 1434 ND2 ASN A 194 -6.298 -5.810 23.899 1.00 8.98 N
ATOM 1435 N ALA A 195 -5.533 -1.335 26.309 1.00 9.77 N
ATOM 1436 CA ALA A 195 -5.530 -0.094 27.089 1.00 9.97 C
ATOM 1437 C ALA A 195 -5.678 1.151 26.224 1.00 10.43 C
ATOM 1438 O ALA A 195 -5.351 1.136 25.042 1.00 10.08 O
ATOM 1439 CB ALA A 195 -4.256 0.001 27.921 1.00 10.44 C
ATOM 1440 N LYS A 196 -6.162 2.230 26.833 1.00 10.42 N
ATOM 1441 CA LYS A 196 -6.197 3.529 26.174 1.00 10.75 C
ATOM 1442 C LYS A 196 -4.791 4.120 26.001 1.00 10.81 C
ATOM 1443 O LYS A 196 -4.079 4.372 26.983 1.00 10.59 O
ATOM 1444 CB LYS A 196 -7.096 4.500 26.951 1.00 11.12 C
ATOM 1445 CG LYS A 196 -7.210 5.889 26.320 1.00 11.31 C
ATOM 1446 CD LYS A 196 -7.729 6.914 27.331 1.00 13.53 C
ATOM 1447 CE LYS A 196 -8.175 8.205 26.644 1.00 14.27 C
ATOM 1448 NZ LYS A 196 -7.061 8.962 26.006 1.00 15.28 N
ATOM 1449 N THR A 197 -4.395 4.313 24.745 1.00 10.66 N
ATOM 1450 CA THR A 197 -3.245 5.157 24.406 1.00 11.13 C
ATOM 1451 C THR A 197 -3.759 6.367 23.627 1.00 11.60 C
ATOM 1452 O THR A 197 -4.926 6.397 23.226 1.00 11.72 O
ATOM 1453 CB THR A 197 -2.190 4.424 23.542 1.00 11.21 C
ATOM 1454 OG1 THR A 197 -2.681 4.303 22.200 1.00 10.63 O
ATOM 1455 CG2 THR A 197 -1.859 3.042 24.114 1.00 11.82 C
ATOM 1456 N VAL A 198 -2.900 7.357 23.394 1.00 11.84 N
ATOM 1457 CA VAL A 198 -3.346 8.529 22.642 1.00 12.53 C
ATOM 1458 C VAL A 198 -3.620 8.205 21.166 1.00 11.93 C
ATOM 1459 O VAL A 198 -4.286 8.986 20.483 1.00 12.03 O
ATOM 1460 CB VAL A 198 -2.420 9.779 22.792 1.00 12.96 C
ATOM 1461 CG1 VAL A 198 -2.105 10.058 24.264 1.00 14.31 C
ATOM 1462 CG2 VAL A 198 -1.168 9.647 21.976 1.00 13.78 C
ATOM 1463 N ARG A 199 -3.117 7.063 20.683 1.00 11.24 N
ATOM 1464 CA ARG A 199 -3.372 6.639 19.292 1.00 10.84 C
ATOM 1465 C ARG A 199 -4.613 5.761 19.129 1.00 10.45 C
ATOM 1466 O ARG A 199 -5.185 5.675 18.040 1.00 10.15 O
ATOM 1467 CB ARG A 199 -2.164 5.919 18.681 1.00 11.08 C
ATOM 1468 CG ARG A 199 -0.855 6.693 18.704 1.00 11.98 C
ATOM 1469 CD ARG A 199 -0.967 8.040 18.021 1.00 12.71 C
ATOM 1470 NE ARG A 199 0.301 8.765 18.062 1.00 13.32 N
ATOM 1471 CZ ARG A 199 0.435 10.071 17.845 1.00 15.30 C
ATOM 1472 NH1 ARG A 199 1.642 10.630 17.902 1.00 15.55 N
ATOM 1473 NH2 ARG A 199 -0.629 10.824 17.573 1.00 16.06 N
ATOM 1474 N ASN A 200 -5.018 5.097 20.210 1.00 9.91 N
ATOM 1475 CA ASN A 200 -6.093 4.116 20.153 1.00 9.32 C
ATOM 1476 C ASN A 200 -6.674 3.892 21.543 1.00 9.33 C
ATOM 1477 O ASN A 200 -5.974 3.437 22.454 1.00 9.06 O
ATOM 1478 CB ASN A 200 -5.553 2.794 19.579 1.00 9.70 C
ATOM 1479 CG ASN A 200 -6.640 1.765 19.308 1.00 9.35 C
ATOM 1480 OD1 ASN A 200 -7.809 1.956 19.648 1.00 9.03 O
ATOM 1481 ND2 ASN A 200 -6.240 0.640 18.705 1.00 9.60 N
ATOM 1482 N ASN A 201 -7.955 4.220 21.692 1.00 9.45 N
ATOM 1483 CA ASN A 201 -8.683 4.012 22.945 1.00 9.51 C
ATOM 1484 C ASN A 201 -8.694 2.542 23.372 1.00 9.51 C
ATOM 1485 O ASN A 201 -8.784 2.236 24.567 1.00 9.87 O
ATOM 1486 CB ASN A 201 -10.121 4.519 22.806 1.00 9.96 C
ATOM 1487 CG ASN A 201 -10.213 6.040 22.789 1.00 10.79 C
ATOM 1488 OD1 ASN A 201 -9.405 6.730 23.405 1.00 12.47 O
ATOM 1489 ND2 ASN A 201 -11.222 6.562 22.097 1.00 13.62 N
ATOM 1490 N ASN A 202 -8.603 1.648 22.388 1.00 9.20 N
ATOM 1491 CA ASN A 202 -8.589 0.215 22.624 1.00 9.36 C
ATOM 1492 C ASN A 202 -7.298 -0.452 22.128 1.00 9.41 C
ATOM 1493 O ASN A 202 -7.333 -1.506 21.497 1.00 9.53 O
ATOM 1494 CB ASN A 202 -9.817 -0.445 21.981 1.00 9.84 C
ATOM 1495 CG ASN A 202 -10.069 -1.855 22.508 1.00 9.59 C
ATOM 1496 OD1 ASN A 202 -9.782 -2.155 23.670 1.00 11.57 O
ATOM 1497 ND2 ASN A 202 -10.607 -2.720 21.658 1.00 9.89 N
ATOM 1498 N SER A 203 -6.158 0.167 22.426 1.00 9.43 N
ATOM 1499 CA SER A 203 -4.869 -0.324 21.945 1.00 9.35 C
ATOM 1500 C SER A 203 -4.513 -1.707 22.500 1.00 9.47 C
ATOM 1501 O SER A 203 -4.582 -1.934 23.711 1.00 9.91 O
ATOM 1502 CB SER A 203 -3.763 0.683 22.288 1.00 9.34 C
ATOM 1503 OG SER A 203 -2.526 0.317 21.700 1.00 9.17 O
ATOM 1504 N SER A 204 -4.128 -2.618 21.607 1.00 9.23 N
ATOM 1505 CA SER A 204 -3.586 -3.926 22.008 1.00 9.38 C
ATOM 1506 C SER A 204 -2.157 -3.743 22.520 1.00 9.35 C
ATOM 1507 O SER A 204 -1.280 -3.263 21.783 1.00 9.46 O
ATOM 1508 CB SER A 204 -3.564 -4.908 20.828 1.00 9.75 C
ATOM 1509 OG SER A 204 -4.810 -4.979 20.157 1.00 9.77 O
ATOM 1510 N ARG A 205 -1.917 -4.132 23.772 1.00 9.13 N
ATOM 1511 CA ARG A 205 -0.568 -4.054 24.355 1.00 9.11 C
ATOM 1512 C ARG A 205 0.088 -5.437 24.471 1.00 9.15 C
ATOM 1513 O ARG A 205 0.958 -5.678 25.321 1.00 8.81 O
ATOM 1514 CB ARG A 205 -0.573 -3.310 25.700 1.00 9.04 C
ATOM 1515 CG ARG A 205 -1.375 -1.999 25.714 1.00 9.00 C
ATOM 1516 CD ARG A 205 -1.050 -1.088 24.530 1.00 8.75 C
ATOM 1517 NE ARG A 205 0.317 -0.570 24.584 1.00 10.34 N
ATOM 1518 CZ ARG A 205 0.902 0.099 23.594 1.00 10.99 C
ATOM 1519 NH1 ARG A 205 0.244 0.343 22.462 1.00 9.60 N
ATOM 1520 NH2 ARG A 205 2.147 0.532 23.738 1.00 10.51 N
ATOM 1521 N PHE A 206 -0.341 -6.331 23.588 1.00 9.16 N
ATOM 1522 CA PHE A 206 0.259 -7.645 23.415 1.00 9.59 C
ATOM 1523 C PHE A 206 -0.001 -8.071 21.980 1.00 10.12 C
ATOM 1524 O PHE A 206 -0.887 -7.521 21.312 1.00 10.39 O
ATOM 1525 CB PHE A 206 -0.339 -8.662 24.404 1.00 9.29 C
ATOM 1526 CG PHE A 206 -1.769 -9.044 24.100 1.00 9.00 C
ATOM 1527 CD1 PHE A 206 -2.076 -10.297 23.567 1.00 9.36 C
ATOM 1528 CD2 PHE A 206 -2.809 -8.145 24.340 1.00 8.33 C
ATOM 1529 CE1 PHE A 206 -3.407 -10.641 23.278 1.00 8.78 C
ATOM 1530 CE2 PHE A 206 -4.131 -8.480 24.056 1.00 10.45 C
ATOM 1531 CZ PHE A 206 -4.431 -9.726 23.527 1.00 9.14 C
ATOM 1532 N GLY A 207 0.759 -9.048 21.510 1.00 10.38 N
ATOM 1533 CA GLY A 207 0.524 -9.613 20.187 1.00 10.33 C
ATOM 1534 C GLY A 207 -0.165 -10.953 20.324 1.00 11.07 C
ATOM 1535 O GLY A 207 -0.048 -11.617 21.356 1.00 10.91 O
ATOM 1536 N LYS A 208 -0.885 -11.356 19.285 1.00 11.28 N
ATOM 1537 CA LYS A 208 -1.515 -12.667 19.289 1.00 12.09 C
ATOM 1538 C LYS A 208 -1.562 -13.313 17.910 1.00 11.92 C
ATOM 1539 O LYS A 208 -1.663 -12.635 16.882 1.00 11.23 O
ATOM 1540 CB LYS A 208 -2.917 -12.606 19.916 1.00 12.25 C
ATOM 1541 CG LYS A 208 -3.955 -11.872 19.098 1.00 13.30 C
ATOM 1542 CD LYS A 208 -5.310 -11.866 19.783 1.00 13.56 C
ATOM 1543 CE LYS A 208 -6.359 -11.323 18.835 1.00 16.13 C
ATOM 1544 NZ LYS A 208 -7.716 -11.397 19.438 1.00 20.16 N
ATOM 1545 N PHE A 209 -1.463 -14.637 17.917 1.00 12.03 N
ATOM 1546 CA PHE A 209 -1.698 -15.449 16.739 1.00 12.39 C
ATOM 1547 C PHE A 209 -2.802 -16.419 17.141 1.00 12.68 C
ATOM 1548 O PHE A 209 -2.593 -17.273 18.002 1.00 12.96 O
ATOM 1549 CB PHE A 209 -0.425 -16.196 16.339 1.00 12.54 C
ATOM 1550 CG PHE A 209 -0.507 -16.867 14.989 1.00 12.84 C
ATOM 1551 CD1 PHE A 209 -0.783 -16.126 13.844 1.00 13.83 C
ATOM 1552 CD2 PHE A 209 -0.283 -18.234 14.863 1.00 13.91 C
ATOM 1553 CE1 PHE A 209 -0.858 -16.739 12.594 1.00 13.97 C
ATOM 1554 CE2 PHE A 209 -0.349 -18.855 13.618 1.00 13.60 C
ATOM 1555 CZ PHE A 209 -0.639 -18.109 12.482 1.00 14.02 C
ATOM 1556 N VAL A 210 -3.983 -16.245 16.554 1.00 12.51 N
ATOM 1557 CA VAL A 210 -5.146 -17.068 16.889 1.00 12.96 C
ATOM 1558 C VAL A 210 -5.346 -18.125 15.806 1.00 13.40 C
ATOM 1559 O VAL A 210 -5.630 -17.795 14.647 1.00 12.99 O
ATOM 1560 CB VAL A 210 -6.439 -16.222 17.060 1.00 13.00 C
ATOM 1561 CG1 VAL A 210 -7.612 -17.100 17.501 1.00 13.07 C
ATOM 1562 CG2 VAL A 210 -6.218 -15.100 18.059 1.00 13.11 C
ATOM 1563 N GLU A 211 -5.187 -19.389 16.197 1.00 13.82 N
ATOM 1564 CA GLU A 211 -5.346 -20.516 15.280 1.00 14.78 C
ATOM 1565 C GLU A 211 -6.717 -21.164 15.424 1.00 14.78 C
ATOM 1566 O GLU A 211 -7.131 -21.513 16.533 1.00 14.52 O
ATOM 1567 CB GLU A 211 -4.266 -21.576 15.522 1.00 14.90 C
ATOM 1568 CG GLU A 211 -2.841 -21.131 15.206 1.00 15.70 C
ATOM 1569 CD GLU A 211 -1.783 -22.081 15.760 1.00 16.37 C
ATOM 1570 OE1 GLU A 211 -2.081 -23.282 15.947 1.00 18.17 O
ATOM 1571 OE2 GLU A 211 -0.646 -21.624 16.009 1.00 18.63 O
ATOM 1572 N ILE A 212 -7.416 -21.287 14.300 1.00 14.87 N
ATOM 1573 C ILE A 212 -8.301 -23.399 13.598 1.00 15.55 C
ATOM 1574 O ILE A 212 -7.815 -23.449 12.464 1.00 15.04 O
ATOM 1575 CA AILE A 212 -8.648 -22.066 14.245 0.50 15.11 C
ATOM 1576 CB AILE A 212 -9.786 -21.346 13.475 0.50 15.16 C
ATOM 1577 CG1AILE A 212 -10.184 -20.048 14.191 0.50 15.03 C
ATOM 1578 CG2AILE A 212 -11.004 -22.273 13.322 0.50 15.08 C
ATOM 1579 CD1AILE A 212 -11.127 -19.155 13.393 0.50 14.92 C
ATOM 1581 CB BILE A 212 -9.730 -21.345 13.353 0.50 15.23 C
ATOM 1582 CG1BILE A 212 -9.918 -19.882 13.786 0.50 15.27 C
ATOM 1583 CG2BILE A 212 -11.058 -22.126 13.364 0.50 15.21 C
ATOM 1584 CD1BILE A 212 -10.376 -19.696 15.218 0.50 15.09 C
ATOM 1585 N HIS A 213 -8.532 -24.475 14.341 1.00 15.86 N
ATOM 1586 CA HIS A 213 -8.129 -25.797 13.894 1.00 16.78 C
ATOM 1587 C HIS A 213 -9.278 -26.586 13.288 1.00 17.46 C
ATOM 1588 O HIS A 213 -10.411 -26.523 13.765 1.00 17.28 O
ATOM 1589 CB HIS A 213 -7.447 -26.558 15.030 1.00 16.57 C
ATOM 1590 CG HIS A 213 -6.031 -26.131 15.259 1.00 16.81 C
ATOM 1591 ND1 HIS A 213 -4.950 -26.905 14.893 1.00 16.85 N
ATOM 1592 CD2 HIS A 213 -5.518 -24.999 15.798 1.00 16.59 C
ATOM 1593 CE1 HIS A 213 -3.833 -26.273 15.205 1.00 16.94 C
ATOM 1594 NE2 HIS A 213 -4.150 -25.112 15.752 1.00 16.84 N
ATOM 1595 N PHE A 214 -8.953 -27.321 12.226 1.00 18.79 N
ATOM 1596 CA PHE A 214 -9.932 -28.040 11.421 1.00 19.88 C
ATOM 1597 C PHE A 214 -9.615 -29.526 11.347 1.00 21.04 C
ATOM 1598 O PHE A 214 -8.447 -29.925 11.409 1.00 21.42 O
ATOM 1599 CB PHE A 214 -9.955 -27.482 9.996 1.00 19.50 C
ATOM 1600 CG PHE A 214 -10.443 -26.064 9.899 1.00 18.92 C
ATOM 1601 CD1 PHE A 214 -9.581 -24.996 10.146 1.00 18.15 C
ATOM 1602 CD2 PHE A 214 -11.760 -25.797 9.548 1.00 17.91 C
ATOM 1603 CE1 PHE A 214 -10.027 -23.682 10.050 1.00 18.06 C
ATOM 1604 CE2 PHE A 214 -12.220 -24.483 9.448 1.00 18.59 C
ATOM 1605 CZ PHE A 214 -11.348 -23.423 9.702 1.00 18.39 C
ATOM 1606 N ASN A 215 -10.662 -30.333 11.194 1.00 22.54 N
ATOM 1607 CA ASN A 215 -10.502 -31.758 10.910 1.00 24.19 C
ATOM 1608 C ASN A 215 -10.375 -32.051 9.413 1.00 25.02 C
ATOM 1609 O ASN A 215 -10.284 -31.133 8.592 1.00 24.84 O
ATOM 1610 CB ASN A 215 -11.623 -32.597 11.562 1.00 24.25 C
ATOM 1611 CG ASN A 215 -13.031 -32.214 11.087 1.00 25.21 C
ATOM 1612 OD1 ASN A 215 -13.230 -31.703 9.981 1.00 25.73 O
ATOM 1613 ND2 ASN A 215 -14.020 -32.488 11.934 1.00 26.21 N
ATOM 1614 N GLU A 216 -10.367 -33.340 9.075 1.00 26.23 N
ATOM 1615 CA GLU A 216 -10.240 -33.816 7.696 1.00 27.33 C
ATOM 1616 C GLU A 216 -11.433 -33.440 6.818 1.00 27.61 C
ATOM 1617 O GLU A 216 -11.301 -33.345 5.597 1.00 27.97 O
ATOM 1618 CB GLU A 216 -10.012 -35.338 7.675 1.00 27.62 C
ATOM 1619 CG GLU A 216 -11.032 -36.174 8.479 1.00 29.42 C
ATOM 1620 CD GLU A 216 -10.901 -36.010 9.993 1.00 31.83 C
ATOM 1621 OE1 GLU A 216 -9.797 -35.670 10.477 1.00 33.28 O
ATOM 1622 OE2 GLU A 216 -11.908 -36.224 10.703 1.00 32.81 O
ATOM 1623 N LYS A 217 -12.590 -33.231 7.447 1.00 27.94 N
ATOM 1624 CA LYS A 217 -13.793 -32.766 6.758 1.00 28.25 C
ATOM 1625 C LYS A 217 -13.826 -31.239 6.652 1.00 28.06 C
ATOM 1626 O LYS A 217 -14.797 -30.667 6.148 1.00 28.19 O
ATOM 1627 CB LYS A 217 -15.056 -33.261 7.473 1.00 28.51 C
ATOM 1628 CG LYS A 217 -15.284 -34.766 7.405 1.00 29.77 C
ATOM 1629 CD LYS A 217 -16.762 -35.101 7.571 1.00 31.65 C
ATOM 1630 CE LYS A 217 -17.018 -36.603 7.478 1.00 33.15 C
ATOM 1631 NZ LYS A 217 -16.713 -37.313 8.756 1.00 33.96 N
ATOM 1632 N SER A 218 -12.761 -30.598 7.136 1.00 27.76 N
ATOM 1633 CA SER A 218 -12.629 -29.135 7.164 1.00 27.41 C
ATOM 1634 C SER A 218 -13.715 -28.463 8.008 1.00 26.84 C
ATOM 1635 O SER A 218 -14.288 -27.438 7.622 1.00 27.01 O
ATOM 1636 CB SER A 218 -12.579 -28.554 5.748 1.00 27.43 C
ATOM 1637 OG SER A 218 -11.550 -29.163 4.996 1.00 28.13 O
ATOM 1638 N SER A 219 -13.989 -29.061 9.163 1.00 26.07 N
ATOM 1639 CA SER A 219 -14.908 -28.496 10.141 1.00 25.40 C
ATOM 1640 C SER A 219 -14.119 -28.114 11.396 1.00 24.46 C
ATOM 1641 O SER A 219 -13.179 -28.814 11.777 1.00 24.38 O
ATOM 1642 CB SER A 219 -16.010 -29.505 10.477 1.00 25.56 C
ATOM 1643 OG SER A 219 -17.006 -28.922 11.296 1.00 26.79 O
ATOM 1644 N VAL A 220 -14.499 -27.002 12.021 1.00 23.71 N
ATOM 1645 CA VAL A 220 -13.797 -26.484 13.208 1.00 22.77 C
ATOM 1646 C VAL A 220 -13.875 -27.464 14.383 1.00 22.37 C
ATOM 1647 O VAL A 220 -14.966 -27.892 14.772 1.00 22.43 O
ATOM 1648 CB VAL A 220 -14.352 -25.097 13.642 1.00 23.01 C
ATOM 1649 CG1 VAL A 220 -13.652 -24.590 14.904 1.00 22.57 C
ATOM 1650 CG2 VAL A 220 -14.217 -24.081 12.511 1.00 22.50 C
ATOM 1651 N VAL A 221 -12.714 -27.815 14.934 1.00 21.51 N
ATOM 1652 CA VAL A 221 -12.637 -28.705 16.102 1.00 20.67 C
ATOM 1653 C VAL A 221 -12.261 -27.973 17.393 1.00 20.03 C
ATOM 1654 O VAL A 221 -12.550 -28.444 18.498 1.00 19.97 O
ATOM 1655 CB VAL A 221 -11.672 -29.904 15.874 1.00 20.53 C
ATOM 1656 CG1 VAL A 221 -12.183 -30.796 14.746 1.00 20.68 C
ATOM 1657 CG2 VAL A 221 -10.235 -29.437 15.608 1.00 20.64 C
ATOM 1658 N GLY A 222 -11.623 -26.814 17.247 1.00 19.12 N
ATOM 1659 CA GLY A 222 -11.168 -26.040 18.393 1.00 18.06 C
ATOM 1660 C GLY A 222 -10.266 -24.903 17.963 1.00 17.21 C
ATOM 1661 O GLY A 222 -10.171 -24.586 16.773 1.00 16.66 O
ATOM 1662 N GLY A 223 -9.604 -24.289 18.935 1.00 16.75 N
ATOM 1663 CA GLY A 223 -8.734 -23.153 18.658 1.00 16.29 C
ATOM 1664 C GLY A 223 -7.549 -23.070 19.597 1.00 16.03 C
ATOM 1665 O GLY A 223 -7.479 -23.781 20.602 1.00 15.78 O
ATOM 1666 N PHE A 224 -6.604 -22.200 19.260 1.00 15.53 N
ATOM 1667 CA PHE A 224 -5.479 -21.937 20.141 1.00 15.23 C
ATOM 1668 C PHE A 224 -4.979 -20.519 19.952 1.00 15.12 C
ATOM 1669 O PHE A 224 -4.678 -20.103 18.829 1.00 15.08 O
ATOM 1670 CB PHE A 224 -4.335 -22.918 19.908 1.00 15.32 C
ATOM 1671 CG PHE A 224 -3.286 -22.880 20.984 1.00 15.62 C
ATOM 1672 CD1 PHE A 224 -3.426 -23.651 22.136 1.00 16.97 C
ATOM 1673 CD2 PHE A 224 -2.168 -22.059 20.858 1.00 15.59 C
ATOM 1674 CE1 PHE A 224 -2.459 -23.610 23.137 1.00 16.83 C
ATOM 1675 CE2 PHE A 224 -1.198 -22.014 21.854 1.00 16.56 C
ATOM 1676 CZ PHE A 224 -1.348 -22.793 22.996 1.00 16.75 C
ATOM 1677 N VAL A 225 -4.896 -19.794 21.062 1.00 14.69 N
ATOM 1678 CA VAL A 225 -4.383 -18.432 21.064 1.00 14.49 C
ATOM 1679 C VAL A 225 -2.962 -18.432 21.620 1.00 14.61 C
ATOM 1680 O VAL A 225 -2.744 -18.813 22.775 1.00 14.36 O
ATOM 1681 CB VAL A 225 -5.262 -17.476 21.910 1.00 14.22 C
ATOM 1682 CG1 VAL A 225 -4.707 -16.042 21.852 1.00 14.38 C
ATOM 1683 CG2 VAL A 225 -6.714 -17.510 21.448 1.00 14.70 C
ATOM 1684 N SER A 226 -2.002 -18.033 20.786 1.00 14.71 N
ATOM 1685 CA SER A 226 -0.646 -17.754 21.245 1.00 14.97 C
ATOM 1686 C SER A 226 -0.558 -16.267 21.524 1.00 15.14 C
ATOM 1687 O SER A 226 -0.982 -15.453 20.703 1.00 15.04 O
ATOM 1688 CB SER A 226 0.400 -18.149 20.195 1.00 15.05 C
ATOM 1689 OG SER A 226 0.424 -19.554 19.995 1.00 16.19 O
ATOM 1690 N HIS A 227 -0.038 -15.913 22.693 1.00 15.21 N
ATOM 1691 CA HIS A 227 0.083 -14.506 23.067 1.00 15.27 C
ATOM 1692 C HIS A 227 1.541 -14.130 23.274 1.00 15.72 C
ATOM 1693 O HIS A 227 2.363 -14.964 23.689 1.00 15.97 O
ATOM 1694 CB HIS A 227 -0.742 -14.207 24.320 1.00 15.43 C
ATOM 1695 CG HIS A 227 -0.162 -14.785 25.570 1.00 15.48 C
ATOM 1696 ND1 HIS A 227 -0.209 -16.132 25.853 1.00 15.31 N
ATOM 1697 CD2 HIS A 227 0.483 -14.203 26.608 1.00 16.44 C
ATOM 1698 CE1 HIS A 227 0.384 -16.357 27.013 1.00 16.30 C
ATOM 1699 NE2 HIS A 227 0.815 -15.203 27.490 1.00 16.98 N
ATOM 1700 N TYR A 228 1.851 -12.870 22.988 1.00 15.48 N
ATOM 1701 CA TYR A 228 3.226 -12.403 22.936 1.00 15.81 C
ATOM 1702 C TYR A 228 3.415 -11.045 23.590 1.00 15.24 C
ATOM 1703 O TYR A 228 2.671 -10.101 23.325 1.00 14.73 O
ATOM 1704 CB TYR A 228 3.708 -12.316 21.480 1.00 16.64 C
ATOM 1705 CG TYR A 228 3.645 -13.620 20.724 1.00 17.92 C
ATOM 1706 CD1 TYR A 228 2.552 -13.926 19.912 1.00 18.82 C
ATOM 1707 CD2 TYR A 228 4.677 -14.558 20.823 1.00 19.12 C
ATOM 1708 CE1 TYR A 228 2.486 -15.132 19.224 1.00 19.56 C
ATOM 1709 CE2 TYR A 228 4.621 -15.764 20.132 1.00 19.76 C
ATOM 1710 CZ TYR A 228 3.525 -16.041 19.337 1.00 19.20 C
ATOM 1711 OH TYR A 228 3.460 -17.233 18.655 1.00 19.57 O
ATOM 1712 N LEU A 229 4.425 -10.966 24.449 1.00 14.49 N
ATOM 1713 CA LEU A 229 5.074 -9.701 24.778 1.00 14.06 C
ATOM 1714 C LEU A 229 4.121 -8.636 25.346 1.00 13.43 C
ATOM 1715 O LEU A 229 4.017 -7.516 24.830 1.00 13.62 O
ATOM 1716 CB LEU A 229 5.852 -9.195 23.546 1.00 14.61 C
ATOM 1717 CG LEU A 229 6.789 -10.263 22.935 1.00 15.10 C
ATOM 1718 CD1 LEU A 229 7.049 -10.054 21.433 1.00 15.86 C
ATOM 1719 CD2 LEU A 229 8.102 -10.355 23.711 1.00 15.12 C
ATOM 1720 N LEU A 230 3.411 -9.005 26.411 1.00 12.53 N
ATOM 1721 CA LEU A 230 2.591 -8.042 27.143 1.00 12.06 C
ATOM 1722 C LEU A 230 3.447 -6.867 27.622 1.00 12.29 C
ATOM 1723 O LEU A 230 4.565 -7.064 28.111 1.00 12.08 O
ATOM 1724 CB LEU A 230 1.915 -8.714 28.346 1.00 11.78 C
ATOM 1725 CG LEU A 230 0.947 -7.853 29.163 1.00 11.26 C
ATOM 1726 CD1 LEU A 230 -0.345 -7.581 28.378 1.00 10.52 C
ATOM 1727 CD2 LEU A 230 0.649 -8.540 30.495 1.00 11.40 C
ATOM 1728 N GLU A 231 2.914 -5.657 27.478 1.00 12.49 N
ATOM 1729 CA GLU A 231 3.585 -4.434 27.932 1.00 13.43 C
ATOM 1730 C GLU A 231 3.523 -4.311 29.457 1.00 13.97 C
ATOM 1731 O GLU A 231 2.514 -3.880 30.020 1.00 14.14 O
ATOM 1732 CB GLU A 231 2.949 -3.213 27.267 1.00 12.96 C
ATOM 1733 CG GLU A 231 3.693 -1.899 27.511 1.00 13.24 C
ATOM 1734 CD GLU A 231 3.080 -0.732 26.754 1.00 14.42 C
ATOM 1735 OE1 GLU A 231 1.875 -0.454 26.924 1.00 14.47 O
ATOM 1736 OE2 GLU A 231 3.814 -0.084 25.984 1.00 16.59 O
ATOM 1737 N LYS A 232 4.615 -4.678 30.122 1.00 14.94 N
ATOM 1738 CA LYS A 232 4.611 -4.757 31.587 1.00 15.60 C
ATOM 1739 C LYS A 232 4.691 -3.411 32.311 1.00 15.28 C
ATOM 1740 O LYS A 232 4.131 -3.254 33.400 1.00 15.12 O
ATOM 1741 CB LYS A 232 5.672 -5.756 32.082 1.00 15.72 C
ATOM 1742 CG LYS A 232 5.350 -7.209 31.702 1.00 15.91 C
ATOM 1743 CD LYS A 232 6.406 -8.193 32.206 1.00 17.46 C
ATOM 1744 CE LYS A 232 6.312 -9.514 31.454 1.00 19.62 C
ATOM 1745 NZ LYS A 232 7.336 -10.492 31.906 1.00 22.28 N
ATOM 1746 N SER A 233 5.351 -2.428 31.703 1.00 15.06 N
ATOM 1747 CA SER A 233 5.501 -1.111 32.323 1.00 15.25 C
ATOM 1748 C SER A 233 4.164 -0.432 32.616 1.00 14.76 C
ATOM 1749 O SER A 233 4.039 0.296 33.607 1.00 14.97 O
ATOM 1750 CB SER A 233 6.358 -0.198 31.450 1.00 15.79 C
ATOM 1751 OG SER A 233 5.747 -0.007 30.186 1.00 16.44 O
ATOM 1752 N ARG A 234 3.169 -0.693 31.761 1.00 14.02 N
ATOM 1753 CA ARG A 234 1.842 -0.078 31.870 1.00 13.41 C
ATOM 1754 C ARG A 234 1.131 -0.449 33.169 1.00 13.24 C
ATOM 1755 O ARG A 234 0.302 0.309 33.668 1.00 13.33 O
ATOM 1756 CB ARG A 234 0.966 -0.480 30.683 1.00 13.21 C
ATOM 1757 CG ARG A 234 -0.413 0.199 30.649 1.00 12.49 C
ATOM 1758 CD ARG A 234 -1.053 0.069 29.284 1.00 12.24 C
ATOM 1759 NE ARG A 234 -0.188 0.635 28.259 1.00 11.25 N
ATOM 1760 CZ ARG A 234 -0.264 1.882 27.796 1.00 11.12 C
ATOM 1761 NH1 ARG A 234 0.594 2.287 26.864 1.00 11.68 N
ATOM 1762 NH2 ARG A 234 -1.205 2.712 28.231 1.00 11.49 N
ATOM 1763 N ILE A 235 1.454 -1.626 33.694 1.00 13.19 N
ATOM 1764 CA ILE A 235 0.864 -2.113 34.942 1.00 13.45 C
ATOM 1765 C ILE A 235 1.051 -1.118 36.093 1.00 13.62 C
ATOM 1766 O ILE A 235 0.163 -0.973 36.938 1.00 13.62 O
ATOM 1767 CB ILE A 235 1.421 -3.518 35.305 1.00 13.37 C
ATOM 1768 CG1 ILE A 235 1.179 -4.492 34.136 1.00 13.39 C
ATOM 1769 CG2 ILE A 235 0.815 -4.038 36.624 1.00 13.36 C
ATOM 1770 CD1 ILE A 235 2.044 -5.731 34.158 1.00 12.52 C
ATOM 1771 N CYS A 236 2.186 -0.417 36.100 1.00 13.96 N
ATOM 1772 CA CYS A 236 2.548 0.456 37.221 1.00 14.65 C
ATOM 1773 C CYS A 236 2.405 1.957 36.956 1.00 14.91 C
ATOM 1774 O CYS A 236 2.067 2.717 37.864 1.00 15.46 O
ATOM 1775 CB CYS A 236 3.964 0.133 37.713 1.00 14.43 C
ATOM 1776 SG CYS A 236 4.195 -1.577 38.201 1.00 16.12 S
ATOM 1777 N VAL A 237 2.650 2.388 35.719 1.00 14.63 N
ATOM 1778 CA VAL A 237 2.600 3.814 35.398 1.00 15.18 C
ATOM 1779 C VAL A 237 2.122 4.081 33.967 1.00 14.95 C
ATOM 1780 O VAL A 237 2.362 3.279 33.065 1.00 14.55 O
ATOM 1781 CB VAL A 237 3.972 4.511 35.667 1.00 15.24 C
ATOM 1782 CG1 VAL A 237 5.031 4.078 34.635 1.00 16.28 C
ATOM 1783 CG2 VAL A 237 3.826 6.042 35.727 1.00 16.36 C
ATOM 1784 N GLN A 238 1.428 5.207 33.795 1.00 15.04 N
ATOM 1785 CA GLN A 238 0.957 5.674 32.488 1.00 15.70 C
ATOM 1786 C GLN A 238 1.080 7.193 32.392 1.00 16.35 C
ATOM 1787 O GLN A 238 1.160 7.882 33.413 1.00 16.97 O
ATOM 1788 CB GLN A 238 -0.511 5.283 32.249 1.00 15.38 C
ATOM 1789 CG GLN A 238 -0.924 3.882 32.740 1.00 14.10 C
ATOM 1790 CD GLN A 238 -1.163 3.825 34.244 1.00 14.59 C
ATOM 1791 OE1 GLN A 238 -1.649 4.782 34.850 1.00 13.66 O
ATOM 1792 NE2 GLN A 238 -0.821 2.694 34.850 1.00 13.95 N
ATOM 1793 N GLY A 239 1.079 7.706 31.161 1.00 17.07 N
ATOM 1794 CA GLY A 239 0.993 9.147 30.911 1.00 17.77 C
ATOM 1795 C GLY A 239 -0.414 9.661 31.176 1.00 18.08 C
ATOM 1796 O GLY A 239 -1.377 8.883 31.201 1.00 18.46 O
ATOM 1797 N LYS A 240 -0.543 10.973 31.360 1.00 18.51 N
ATOM 1798 CA LYS A 240 -1.818 11.589 31.754 1.00 18.69 C
ATOM 1799 C LYS A 240 -2.990 11.426 30.776 1.00 18.47 C
ATOM 1800 O LYS A 240 -4.150 11.563 31.171 1.00 18.14 O
ATOM 1801 CB LYS A 240 -1.624 13.070 32.084 1.00 19.28 C
ATOM 1802 CG LYS A 240 -1.073 13.299 33.466 1.00 21.38 C
ATOM 1803 CD LYS A 240 -1.591 14.602 34.049 1.00 24.45 C
ATOM 1804 CE LYS A 240 -1.238 14.727 35.528 1.00 25.90 C
ATOM 1805 NZ LYS A 240 0.229 14.624 35.761 1.00 27.91 N
ATOM 1806 N GLU A 241 -2.687 11.149 29.509 1.00 17.94 N
ATOM 1807 CA GLU A 241 -3.725 10.920 28.508 1.00 18.09 C
ATOM 1808 C GLU A 241 -3.984 9.430 28.274 1.00 17.02 C
ATOM 1809 O GLU A 241 -4.788 9.060 27.416 1.00 17.18 O
ATOM 1810 CB GLU A 241 -3.357 11.592 27.181 1.00 18.65 C
ATOM 1811 CG GLU A 241 -3.619 13.091 27.123 1.00 22.24 C
ATOM 1812 CD GLU A 241 -3.814 13.580 25.700 1.00 26.42 C
ATOM 1813 OE1 GLU A 241 -4.979 13.807 25.310 1.00 29.24 O
ATOM 1814 OE2 GLU A 241 -2.811 13.710 24.960 1.00 29.06 O
ATOM 1815 N GLU A 242 -3.304 8.578 29.032 1.00 15.69 N
ATOM 1816 CA GLU A 242 -3.400 7.133 28.815 1.00 14.55 C
ATOM 1817 C GLU A 242 -3.923 6.428 30.061 1.00 13.76 C
ATOM 1818 O GLU A 242 -4.036 7.044 31.124 1.00 13.98 O
ATOM 1819 CB GLU A 242 -2.050 6.568 28.366 1.00 14.73 C
ATOM 1820 CG GLU A 242 -1.548 7.201 27.052 1.00 15.28 C
ATOM 1821 CD GLU A 242 -0.572 6.332 26.282 1.00 17.71 C
ATOM 1822 OE1 GLU A 242 -0.131 5.282 26.814 1.00 16.28 O
ATOM 1823 OE2 GLU A 242 -0.247 6.711 25.128 1.00 17.53 O
ATOM 1824 N ARG A 243 -4.268 5.150 29.920 1.00 12.73 N
ATOM 1825 CA ARG A 243 -4.758 4.369 31.053 1.00 11.46 C
ATOM 1826 C ARG A 243 -4.017 3.055 31.201 1.00 11.00 C
ATOM 1827 O ARG A 243 -3.336 2.600 30.278 1.00 10.20 O
ATOM 1828 CB ARG A 243 -6.253 4.070 30.919 1.00 11.73 C
ATOM 1829 CG ARG A 243 -7.138 5.277 30.709 1.00 11.30 C
ATOM 1830 CD ARG A 243 -8.571 4.981 31.124 1.00 13.25 C
ATOM 1831 NE ARG A 243 -9.092 3.736 30.560 1.00 11.93 N
ATOM 1832 CZ ARG A 243 -10.358 3.342 30.658 1.00 13.18 C
ATOM 1833 NH1 ARG A 243 -11.254 4.112 31.268 1.00 11.80 N
ATOM 1834 NH2 ARG A 243 -10.735 2.183 30.135 1.00 11.83 N
ATOM 1835 N ASN A 244 -4.161 2.452 32.380 1.00 10.36 N
ATOM 1836 CA ASN A 244 -3.740 1.072 32.602 1.00 10.10 C
ATOM 1837 C ASN A 244 -4.682 0.156 31.816 1.00 9.76 C
ATOM 1838 O ASN A 244 -5.565 0.644 31.094 1.00 10.23 O
ATOM 1839 CB ASN A 244 -3.802 0.765 34.098 1.00 9.72 C
ATOM 1840 CG ASN A 244 -2.809 -0.292 34.528 1.00 9.84 C
ATOM 1841 OD1 ASN A 244 -2.543 -1.254 33.803 1.00 8.96 O
ATOM 1842 ND2 ASN A 244 -2.260 -0.124 35.735 1.00 9.66 N
ATOM 1843 N TYR A 245 -4.509 -1.156 31.947 1.00 9.68 N
ATOM 1844 CA TYR A 245 -5.385 -2.123 31.262 1.00 9.62 C
ATOM 1845 C TYR A 245 -6.861 -1.933 31.605 1.00 9.57 C
ATOM 1846 O TYR A 245 -7.201 -1.555 32.727 1.00 9.94 O
ATOM 1847 CB TYR A 245 -4.906 -3.555 31.512 1.00 9.58 C
ATOM 1848 CG TYR A 245 -3.558 -3.756 30.866 1.00 9.58 C
ATOM 1849 CD1 TYR A 245 -2.384 -3.766 31.623 1.00 9.27 C
ATOM 1850 CD2 TYR A 245 -3.456 -3.859 29.482 1.00 9.21 C
ATOM 1851 CE1 TYR A 245 -1.132 -3.913 31.001 1.00 10.61 C
ATOM 1852 CE2 TYR A 245 -2.227 -4.002 28.859 1.00 10.75 C
ATOM 1853 CZ TYR A 245 -1.071 -4.032 29.615 1.00 9.86 C
ATOM 1854 OH TYR A 245 0.132 -4.173 28.964 1.00 8.99 O
ATOM 1855 N HIS A 246 -7.728 -2.165 30.617 1.00 9.27 N
ATOM 1856 CA HIS A 246 -9.167 -1.914 30.771 1.00 9.35 C
ATOM 1857 C HIS A 246 -9.753 -2.523 32.039 1.00 9.41 C
ATOM 1858 O HIS A 246 -10.607 -1.915 32.693 1.00 9.18 O
ATOM 1859 CB HIS A 246 -9.952 -2.443 29.564 1.00 9.53 C
ATOM 1860 CG HIS A 246 -9.672 -1.726 28.279 1.00 9.92 C
ATOM 1861 ND1 HIS A 246 -9.424 -0.370 28.211 1.00 10.03 N
ATOM 1862 CD2 HIS A 246 -9.655 -2.175 27.001 1.00 9.81 C
ATOM 1863 CE1 HIS A 246 -9.232 -0.024 26.950 1.00 10.91 C
ATOM 1864 NE2 HIS A 246 -9.370 -1.100 26.196 1.00 10.01 N
ATOM 1865 N ILE A 247 -9.288 -3.722 32.384 1.00 9.51 N
ATOM 1866 CA ILE A 247 -9.864 -4.476 33.500 1.00 10.10 C
ATOM 1867 C ILE A 247 -9.956 -3.652 34.789 1.00 10.40 C
ATOM 1868 O ILE A 247 -10.964 -3.709 35.496 1.00 10.35 O
ATOM 1869 CB ILE A 247 -9.133 -5.834 33.732 1.00 10.13 C
ATOM 1870 CG1 ILE A 247 -9.802 -6.644 34.857 1.00 10.94 C
ATOM 1871 CG2 ILE A 247 -7.633 -5.629 34.005 1.00 9.78 C
ATOM 1872 CD1 ILE A 247 -11.280 -6.971 34.617 1.00 11.43 C
ATOM 1873 N PHE A 248 -8.925 -2.864 35.078 1.00 10.53 N
ATOM 1874 CA PHE A 248 -8.933 -2.023 36.277 1.00 11.04 C
ATOM 1875 C PHE A 248 -10.143 -1.086 36.297 1.00 11.55 C
ATOM 1876 O PHE A 248 -10.795 -0.927 37.329 1.00 11.80 O
ATOM 1877 CB PHE A 248 -7.628 -1.239 36.407 1.00 10.78 C
ATOM 1878 CG PHE A 248 -6.419 -2.109 36.595 1.00 10.68 C
ATOM 1879 CD1 PHE A 248 -6.142 -2.681 37.831 1.00 9.96 C
ATOM 1880 CD2 PHE A 248 -5.554 -2.360 35.534 1.00 9.95 C
ATOM 1881 CE1 PHE A 248 -5.017 -3.496 38.016 1.00 10.52 C
ATOM 1882 CE2 PHE A 248 -4.424 -3.178 35.705 1.00 10.25 C
ATOM 1883 CZ PHE A 248 -4.158 -3.745 36.953 1.00 10.43 C
ATOM 1884 N TYR A 249 -10.464 -0.512 35.139 1.00 11.86 N
ATOM 1885 CA TYR A 249 -11.527 0.489 35.033 1.00 12.47 C
ATOM 1886 C TYR A 249 -12.895 -0.170 34.921 1.00 12.94 C
ATOM 1887 O TYR A 249 -13.880 0.329 35.474 1.00 13.30 O
ATOM 1888 CB TYR A 249 -11.240 1.446 33.871 1.00 12.38 C
ATOM 1889 CG TYR A 249 -9.847 2.002 33.982 1.00 12.30 C
ATOM 1890 CD1 TYR A 249 -8.768 1.326 33.408 1.00 12.77 C
ATOM 1891 CD2 TYR A 249 -9.590 3.156 34.719 1.00 12.61 C
ATOM 1892 CE1 TYR A 249 -7.477 1.797 33.539 1.00 12.86 C
ATOM 1893 CE2 TYR A 249 -8.289 3.639 34.862 1.00 12.57 C
ATOM 1894 CZ TYR A 249 -7.245 2.951 34.263 1.00 12.77 C
ATOM 1895 OH TYR A 249 -5.958 3.400 34.370 1.00 12.22 O
ATOM 1896 N ARG A 250 -12.944 -1.307 34.232 1.00 13.07 N
ATOM 1897 CA ARG A 250 -14.172 -2.089 34.130 1.00 13.42 C
ATOM 1898 C ARG A 250 -14.599 -2.592 35.508 1.00 14.02 C
ATOM 1899 O ARG A 250 -15.769 -2.480 35.884 1.00 14.01 O
ATOM 1900 CB ARG A 250 -13.988 -3.247 33.154 1.00 13.66 C
ATOM 1901 CG ARG A 250 -13.812 -2.789 31.709 1.00 13.51 C
ATOM 1902 CD ARG A 250 -13.730 -3.975 30.761 1.00 15.71 C
ATOM 1903 NE ARG A 250 -13.407 -3.542 29.403 1.00 16.83 N
ATOM 1904 CZ ARG A 250 -13.219 -4.363 28.370 1.00 17.62 C
ATOM 1905 NH1 ARG A 250 -13.344 -5.678 28.512 1.00 17.77 N
ATOM 1906 NH2 ARG A 250 -12.920 -3.860 27.185 1.00 18.39 N
ATOM 1907 N LEU A 251 -13.635 -3.104 36.267 1.00 14.05 N
ATOM 1908 CA LEU A 251 -13.897 -3.585 37.622 1.00 14.63 C
ATOM 1909 C LEU A 251 -14.343 -2.461 38.559 1.00 15.02 C
ATOM 1910 O LEU A 251 -15.326 -2.618 39.288 1.00 15.19 O
ATOM 1911 CB LEU A 251 -12.661 -4.297 38.181 1.00 14.60 C
ATOM 1912 CG LEU A 251 -12.791 -5.009 39.530 1.00 14.27 C
ATOM 1913 CD1 LEU A 251 -13.898 -6.074 39.512 1.00 14.87 C
ATOM 1914 CD2 LEU A 251 -11.447 -5.619 39.930 1.00 15.19 C
ATOM 1915 N CYS A 252 -13.638 -1.328 38.535 1.00 15.23 N
ATOM 1916 CA CYS A 252 -13.978 -0.204 39.413 1.00 15.94 C
ATOM 1917 C CYS A 252 -15.346 0.396 39.070 1.00 16.11 C
ATOM 1918 O CYS A 252 -16.109 0.750 39.970 1.00 16.20 O
ATOM 1919 CB CYS A 252 -12.893 0.882 39.398 1.00 16.00 C
ATOM 1920 SG CYS A 252 -11.373 0.492 40.328 1.00 17.72 S
ATOM 1921 N ALA A 253 -15.656 0.490 37.778 1.00 15.77 N
ATOM 1922 CA ALA A 253 -16.927 1.072 37.322 1.00 15.93 C
ATOM 1923 C ALA A 253 -18.120 0.139 37.515 1.00 15.94 C
ATOM 1924 O ALA A 253 -19.230 0.595 37.818 1.00 16.15 O
ATOM 1925 CB ALA A 253 -16.832 1.493 35.859 1.00 15.91 C
ATOM 1926 N GLY A 254 -17.888 -1.161 37.345 1.00 15.66 N
ATOM 1927 CA GLY A 254 -18.982 -2.117 37.206 1.00 15.94 C
ATOM 1928 C GLY A 254 -19.234 -3.092 38.338 1.00 16.02 C
ATOM 1929 O GLY A 254 -20.340 -3.628 38.449 1.00 16.33 O
ATOM 1930 N ALA A 255 -18.224 -3.342 39.169 1.00 15.92 N
ATOM 1931 CA ALA A 255 -18.346 -4.325 40.247 1.00 16.02 C
ATOM 1932 C ALA A 255 -19.496 -3.970 41.179 1.00 16.01 C
ATOM 1933 O ALA A 255 -19.780 -2.793 41.406 1.00 15.92 O
ATOM 1934 CB ALA A 255 -17.053 -4.430 41.043 1.00 16.18 C
ATOM 1935 N SER A 256 -20.152 -4.998 41.705 1.00 16.14 N
ATOM 1936 CA SER A 256 -21.181 -4.812 42.726 1.00 16.39 C
ATOM 1937 C SER A 256 -20.552 -4.212 43.978 1.00 16.53 C
ATOM 1938 O SER A 256 -19.336 -4.310 44.183 1.00 16.06 O
ATOM 1939 CB SER A 256 -21.825 -6.152 43.072 1.00 16.23 C
ATOM 1940 OG SER A 256 -20.892 -7.012 43.700 1.00 16.93 O
ATOM 1941 N GLU A 257 -21.376 -3.591 44.818 1.00 16.81 N
ATOM 1942 CA GLU A 257 -20.888 -3.063 46.087 1.00 17.66 C
ATOM 1943 C GLU A 257 -20.304 -4.159 46.972 1.00 17.93 C
ATOM 1944 O GLU A 257 -19.336 -3.921 47.693 1.00 18.01 O
ATOM 1945 CB GLU A 257 -21.986 -2.293 46.823 1.00 17.74 C
ATOM 1946 CG GLU A 257 -22.184 -0.877 46.315 1.00 18.96 C
ATOM 1947 CD GLU A 257 -21.052 0.049 46.715 1.00 21.43 C
ATOM 1948 OE1 GLU A 257 -20.109 0.209 45.916 1.00 20.66 O
ATOM 1949 OE2 GLU A 257 -21.095 0.606 47.837 1.00 23.44 O
ATOM 1950 N ASP A 258 -20.881 -5.358 46.912 1.00 18.55 N
ATOM 1951 CA ASP A 258 -20.342 -6.496 47.658 1.00 19.33 C
ATOM 1952 C ASP A 258 -18.914 -6.824 47.216 1.00 19.41 C
ATOM 1953 O ASP A 258 -18.031 -7.017 48.055 1.00 19.41 O
ATOM 1954 CB ASP A 258 -21.235 -7.732 47.520 1.00 19.64 C
ATOM 1955 CG ASP A 258 -20.822 -8.853 48.459 1.00 21.16 C
ATOM 1956 OD1 ASP A 258 -20.533 -9.963 47.972 1.00 23.36 O
ATOM 1957 OD2 ASP A 258 -20.775 -8.623 49.685 1.00 23.95 O
ATOM 1958 N ILE A 259 -18.694 -6.876 45.903 1.00 19.36 N
ATOM 1959 CA ILE A 259 -17.358 -7.149 45.362 1.00 19.44 C
ATOM 1960 C ILE A 259 -16.396 -6.004 45.678 1.00 19.53 C
ATOM 1961 O ILE A 259 -15.265 -6.245 46.106 1.00 19.40 O
ATOM 1962 CB ILE A 259 -17.394 -7.457 43.843 1.00 19.39 C
ATOM 1963 CG1 ILE A 259 -17.976 -8.857 43.610 1.00 19.29 C
ATOM 1964 CG2 ILE A 259 -15.984 -7.342 43.222 1.00 19.47 C
ATOM 1965 CD1 ILE A 259 -18.349 -9.145 42.171 1.00 19.72 C
ATOM 1966 N ARG A 260 -16.854 -4.768 45.492 1.00 19.70 N
ATOM 1967 CA ARG A 260 -16.051 -3.595 45.832 1.00 20.46 C
ATOM 1968 C ARG A 260 -15.578 -3.626 47.290 1.00 20.59 C
ATOM 1969 O ARG A 260 -14.411 -3.352 47.571 1.00 20.35 O
ATOM 1970 CB ARG A 260 -16.814 -2.298 45.562 1.00 20.47 C
ATOM 1971 CG ARG A 260 -15.944 -1.060 45.736 1.00 22.36 C
ATOM 1972 CD ARG A 260 -16.743 0.197 46.003 1.00 25.36 C
ATOM 1973 NE ARG A 260 -17.676 0.061 47.122 1.00 27.92 N
ATOM 1974 CZ ARG A 260 -17.347 0.124 48.410 1.00 29.22 C
ATOM 1975 NH1 ARG A 260 -18.293 -0.005 49.329 1.00 30.15 N
ATOM 1976 NH2 ARG A 260 -16.085 0.308 48.786 1.00 30.42 N
ATOM 1977 N GLU A 261 -16.491 -3.957 48.203 1.00 20.89 N
ATOM 1978 CA GLU A 261 -16.171 -4.042 49.630 1.00 21.69 C
ATOM 1979 C GLU A 261 -15.146 -5.131 49.941 1.00 21.08 C
ATOM 1980 O GLU A 261 -14.165 -4.879 50.646 1.00 21.20 O
ATOM 1981 CB GLU A 261 -17.441 -4.262 50.467 1.00 21.65 C
ATOM 1982 CG GLU A 261 -18.327 -3.030 50.595 1.00 23.70 C
ATOM 1983 CD GLU A 261 -19.740 -3.342 51.084 1.00 23.88 C
ATOM 1984 OE1 GLU A 261 -20.117 -4.533 51.161 1.00 27.53 O
ATOM 1985 OE2 GLU A 261 -20.483 -2.383 51.382 1.00 28.00 O
ATOM 1986 N ARG A 262 -15.382 -6.334 49.419 1.00 20.78 N
ATOM 1987 CA ARG A 262 -14.504 -7.483 49.660 1.00 20.89 C
ATOM 1988 C ARG A 262 -13.094 -7.244 49.125 1.00 20.32 C
ATOM 1989 O ARG A 262 -12.118 -7.742 49.685 1.00 19.97 O
ATOM 1990 CB ARG A 262 -15.070 -8.745 49.007 1.00 21.27 C
ATOM 1991 CG ARG A 262 -16.273 -9.368 49.699 1.00 23.93 C
ATOM 1992 CD ARG A 262 -16.661 -10.634 48.956 1.00 28.17 C
ATOM 1993 NE ARG A 262 -17.871 -11.268 49.473 1.00 31.59 N
ATOM 1994 CZ ARG A 262 -18.306 -12.465 49.087 1.00 33.14 C
ATOM 1995 NH1 ARG A 262 -17.626 -13.167 48.184 1.00 34.00 N
ATOM 1996 NH2 ARG A 262 -19.419 -12.971 49.607 1.00 33.76 N
ATOM 1997 N LEU A 263 -13.004 -6.487 48.035 1.00 19.61 N
ATOM 1998 CA LEU A 263 -11.723 -6.221 47.380 1.00 19.37 C
ATOM 1999 C LEU A 263 -11.127 -4.877 47.776 1.00 19.47 C
ATOM 2000 O LEU A 263 -10.044 -4.508 47.302 1.00 18.94 O
ATOM 2001 CB LEU A 263 -11.883 -6.309 45.862 1.00 19.20 C
ATOM 2002 CG LEU A 263 -12.328 -7.666 45.306 1.00 18.79 C
ATOM 2003 CD1 LEU A 263 -12.316 -7.633 43.787 1.00 18.13 C
ATOM 2004 CD2 LEU A 263 -11.465 -8.817 45.825 1.00 18.87 C
ATOM 2005 N HIS A 264 -11.846 -4.157 48.641 1.00 19.68 N
ATOM 2006 CA HIS A 264 -11.440 -2.837 49.146 1.00 20.31 C
ATOM 2007 C HIS A 264 -11.169 -1.836 48.023 1.00 20.29 C
ATOM 2008 O HIS A 264 -10.213 -1.053 48.072 1.00 20.46 O
ATOM 2009 CB HIS A 264 -10.247 -2.963 50.102 1.00 20.56 C
ATOM 2010 CG HIS A 264 -10.400 -4.064 51.103 1.00 22.42 C
ATOM 2011 ND1 HIS A 264 -11.162 -3.930 52.245 1.00 24.16 N
ATOM 2012 CD2 HIS A 264 -9.914 -5.328 51.121 1.00 22.88 C
ATOM 2013 CE1 HIS A 264 -11.130 -5.061 52.927 1.00 24.22 C
ATOM 2014 NE2 HIS A 264 -10.374 -5.923 52.270 1.00 24.82 N
ATOM 2015 N LEU A 265 -12.030 -1.863 47.012 1.00 20.05 N
ATOM 2016 CA LEU A 265 -11.874 -0.990 45.867 1.00 20.28 C
ATOM 2017 C LEU A 265 -12.503 0.379 46.105 1.00 20.19 C
ATOM 2018 O LEU A 265 -13.295 0.567 47.040 1.00 20.33 O
ATOM 2019 CB LEU A 265 -12.413 -1.661 44.595 1.00 20.32 C
ATOM 2020 CG LEU A 265 -11.669 -2.931 44.158 1.00 21.46 C
ATOM 2021 CD1 LEU A 265 -12.351 -3.558 42.960 1.00 22.40 C
ATOM 2022 CD2 LEU A 265 -10.194 -2.656 43.857 1.00 22.51 C
ATOM 2023 N SER A 266 -12.108 1.335 45.269 1.00 20.05 N
ATOM 2024 CA SER A 266 -12.602 2.708 45.318 1.00 20.05 C
ATOM 2025 C SER A 266 -12.331 3.374 43.967 1.00 19.78 C
ATOM 2026 O SER A 266 -11.885 2.704 43.026 1.00 19.92 O
ATOM 2027 CB SER A 266 -11.965 3.489 46.481 1.00 20.18 C
ATOM 2028 OG SER A 266 -10.552 3.383 46.489 1.00 20.70 O
ATOM 2029 N SER A 267 -12.614 4.671 43.856 1.00 19.27 N
ATOM 2030 CA SER A 267 -12.356 5.410 42.617 1.00 19.25 C
ATOM 2031 C SER A 267 -10.864 5.347 42.233 1.00 18.67 C
ATOM 2032 O SER A 267 -10.007 5.300 43.113 1.00 18.67 O
ATOM 2033 CB SER A 267 -12.854 6.858 42.718 1.00 19.37 C
ATOM 2034 OG SER A 267 -12.269 7.554 43.807 1.00 20.79 O
ATOM 2035 N PRO A 268 -10.559 5.311 40.919 1.00 18.26 N
ATOM 2036 CA PRO A 268 -9.192 5.106 40.408 1.00 18.01 C
ATOM 2037 C PRO A 268 -8.122 6.063 40.941 1.00 17.72 C
ATOM 2038 O PRO A 268 -6.946 5.696 40.994 1.00 17.59 O
ATOM 2039 CB PRO A 268 -9.355 5.299 38.895 1.00 18.09 C
ATOM 2040 CG PRO A 268 -10.757 4.916 38.630 1.00 18.30 C
ATOM 2041 CD PRO A 268 -11.533 5.414 39.815 1.00 18.48 C
ATOM 2042 N ASP A 269 -8.519 7.276 41.317 1.00 17.50 N
ATOM 2043 CA ASP A 269 -7.578 8.258 41.868 1.00 17.67 C
ATOM 2044 C ASP A 269 -6.958 7.819 43.200 1.00 17.40 C
ATOM 2045 O ASP A 269 -5.977 8.411 43.650 1.00 17.82 O
ATOM 2046 CB ASP A 269 -8.251 9.622 42.028 1.00 17.98 C
ATOM 2047 CG ASP A 269 -9.465 9.566 42.924 1.00 19.01 C
ATOM 2048 OD1 ASP A 269 -9.461 10.236 43.982 1.00 20.76 O
ATOM 2049 OD2 ASP A 269 -10.421 8.839 42.581 1.00 19.93 O
ATOM 2050 N ASN A 270 -7.526 6.781 43.817 1.00 17.08 N
ATOM 2051 CA ASN A 270 -7.019 6.259 45.090 1.00 16.66 C
ATOM 2052 C ASN A 270 -5.879 5.251 44.932 1.00 16.28 C
ATOM 2053 O ASN A 270 -5.353 4.740 45.929 1.00 15.72 O
ATOM 2054 CB ASN A 270 -8.159 5.648 45.911 1.00 17.13 C
ATOM 2055 CG ASN A 270 -9.120 6.696 46.440 1.00 18.52 C
ATOM 2056 OD1 ASN A 270 -8.777 7.479 47.328 1.00 20.49 O
ATOM 2057 ND2 ASN A 270 -10.330 6.716 45.897 1.00 19.58 N
ATOM 2058 N PHE A 271 -5.491 4.980 43.685 1.00 15.46 N
ATOM 2059 CA PHE A 271 -4.474 3.969 43.398 1.00 15.23 C
ATOM 2060 C PHE A 271 -3.311 4.525 42.589 1.00 15.06 C
ATOM 2061 O PHE A 271 -3.508 5.043 41.487 1.00 14.79 O
ATOM 2062 CB PHE A 271 -5.106 2.768 42.681 1.00 15.04 C
ATOM 2063 CG PHE A 271 -6.165 2.077 43.494 1.00 15.41 C
ATOM 2064 CD1 PHE A 271 -7.516 2.344 43.274 1.00 16.32 C
ATOM 2065 CD2 PHE A 271 -5.810 1.178 44.496 1.00 15.60 C
ATOM 2066 CE1 PHE A 271 -8.499 1.714 44.035 1.00 16.32 C
ATOM 2067 CE2 PHE A 271 -6.781 0.543 45.264 1.00 15.47 C
ATOM 2068 CZ PHE A 271 -8.130 0.814 45.035 1.00 15.89 C
ATOM 2069 N ARG A 272 -2.103 4.406 43.145 1.00 14.88 N
ATOM 2070 CA ARG A 272 -0.870 4.828 42.463 1.00 15.38 C
ATOM 2071 C ARG A 272 -0.744 4.221 41.062 1.00 14.45 C
ATOM 2072 O ARG A 272 -0.314 4.897 40.124 1.00 14.47 O
ATOM 2073 CB ARG A 272 0.365 4.476 43.305 1.00 15.30 C
ATOM 2074 CG ARG A 272 1.705 4.765 42.627 1.00 16.84 C
ATOM 2075 CD ARG A 272 2.889 4.588 43.569 1.00 17.46 C
ATOM 2076 NE ARG A 272 2.985 5.697 44.517 1.00 22.63 N
ATOM 2077 CZ ARG A 272 2.581 5.650 45.784 1.00 23.98 C
ATOM 2078 NH1 ARG A 272 2.715 6.722 46.555 1.00 25.69 N
ATOM 2079 NH2 ARG A 272 2.051 4.538 46.289 1.00 24.21 N
ATOM 2080 N TYR A 273 -1.127 2.953 40.920 1.00 13.81 N
ATOM 2081 CA TYR A 273 -1.011 2.270 39.621 1.00 13.25 C
ATOM 2082 C TYR A 273 -2.025 2.761 38.580 1.00 13.21 C
ATOM 2083 O TYR A 273 -1.944 2.379 37.407 1.00 12.87 O
ATOM 2084 CB TYR A 273 -1.071 0.745 39.776 1.00 13.03 C
ATOM 2085 CG TYR A 273 0.162 0.112 40.399 1.00 12.59 C
ATOM 2086 CD1 TYR A 273 1.360 0.824 40.540 1.00 13.22 C
ATOM 2087 CD2 TYR A 273 0.138 -1.218 40.809 1.00 13.55 C
ATOM 2088 CE1 TYR A 273 2.498 0.224 41.105 1.00 12.12 C
ATOM 2089 CE2 TYR A 273 1.262 -1.822 41.369 1.00 12.57 C
ATOM 2090 CZ TYR A 273 2.436 -1.100 41.508 1.00 12.72 C
ATOM 2091 OH TYR A 273 3.523 -1.719 42.069 1.00 12.56 O
ATOM 2092 N LEU A 274 -2.954 3.615 39.007 1.00 12.90 N
ATOM 2093 CA LEU A 274 -3.933 4.221 38.107 1.00 13.40 C
ATOM 2094 C LEU A 274 -3.870 5.749 38.053 1.00 14.05 C
ATOM 2095 O LEU A 274 -4.245 6.347 37.046 1.00 14.16 O
ATOM 2096 CB LEU A 274 -5.355 3.794 38.493 1.00 13.20 C
ATOM 2097 CG LEU A 274 -5.693 2.307 38.622 1.00 12.71 C
ATOM 2098 CD1 LEU A 274 -7.155 2.132 39.016 1.00 12.70 C
ATOM 2099 CD2 LEU A 274 -5.400 1.561 37.327 1.00 12.47 C
ATOM 2100 N ASN A 275 -3.401 6.386 39.126 1.00 14.60 N
ATOM 2101 CA ASN A 275 -3.653 7.826 39.300 1.00 15.34 C
ATOM 2102 C ASN A 275 -2.661 8.816 38.654 1.00 15.94 C
ATOM 2103 O ASN A 275 -2.873 10.032 38.721 1.00 16.33 O
ATOM 2104 CB ASN A 275 -3.952 8.169 40.776 1.00 15.04 C
ATOM 2105 CG ASN A 275 -2.735 8.046 41.676 1.00 15.14 C
ATOM 2106 OD1 ASN A 275 -1.596 8.035 41.209 1.00 14.74 O
ATOM 2107 ND2 ASN A 275 -2.973 7.959 42.989 1.00 14.42 N
ATOM 2108 N ARG A 276 -1.598 8.300 38.034 1.00 16.60 N
ATOM 2109 CA ARG A 276 -0.722 9.114 37.174 1.00 17.48 C
ATOM 2110 C ARG A 276 -1.280 9.166 35.756 1.00 17.65 C
ATOM 2111 O ARG A 276 -0.950 10.066 34.976 1.00 17.81 O
ATOM 2112 CB ARG A 276 0.705 8.560 37.133 1.00 17.84 C
ATOM 2113 CG ARG A 276 1.640 9.061 38.236 1.00 20.04 C
ATOM 2114 CD ARG A 276 1.437 8.324 39.556 1.00 22.58 C
ATOM 2115 NE ARG A 276 1.595 6.873 39.432 1.00 24.22 N
ATOM 2116 CZ ARG A 276 2.762 6.232 39.444 1.00 25.16 C
ATOM 2117 NH1 ARG A 276 3.905 6.902 39.567 1.00 26.05 N
ATOM 2118 NH2 ARG A 276 2.786 4.912 39.327 1.00 25.31 N
ATOM 2119 N GLY A 277 -2.111 8.183 35.422 1.00 17.60 N
ATOM 2120 CA GLY A 277 -2.782 8.149 34.127 1.00 17.41 C
ATOM 2121 C GLY A 277 -4.107 8.882 34.158 1.00 17.48 C
ATOM 2122 O GLY A 277 -4.452 9.548 35.144 1.00 17.71 O
ATOM 2123 N CYS A 278 -4.850 8.767 33.066 1.00 17.40 N
ATOM 2124 CA CYS A 278 -6.202 9.284 33.005 1.00 17.26 C
ATOM 2125 C CYS A 278 -7.124 8.386 33.830 1.00 16.86 C
ATOM 2126 O CYS A 278 -7.151 7.168 33.636 1.00 16.73 O
ATOM 2127 CB CYS A 278 -6.674 9.341 31.555 1.00 17.42 C
ATOM 2128 SG CYS A 278 -8.350 9.951 31.382 1.00 18.94 S
ATOM 2129 N THR A 279 -7.868 8.986 34.756 1.00 16.77 N
ATOM 2130 CA THR A 279 -8.738 8.213 35.651 1.00 17.16 C
ATOM 2131 C THR A 279 -10.219 8.275 35.263 1.00 16.94 C
ATOM 2132 O THR A 279 -11.082 7.814 36.011 1.00 17.01 O
ATOM 2133 CB THR A 279 -8.582 8.650 37.129 1.00 17.26 C
ATOM 2134 OG1 THR A 279 -8.971 10.023 37.271 1.00 18.18 O
ATOM 2135 CG2 THR A 279 -7.143 8.461 37.603 1.00 17.86 C
ATOM 2136 N ARG A 280 -10.500 8.840 34.092 1.00 16.93 N
ATOM 2137 CA ARG A 280 -11.866 8.958 33.591 1.00 16.77 C
ATOM 2138 C ARG A 280 -12.328 7.645 32.957 1.00 16.58 C
ATOM 2139 O ARG A 280 -11.526 6.915 32.367 1.00 16.59 O
ATOM 2140 CB ARG A 280 -11.962 10.095 32.567 1.00 17.10 C
ATOM 2141 CG ARG A 280 -11.588 11.478 33.109 1.00 17.86 C
ATOM 2142 CD ARG A 280 -11.143 12.416 31.989 1.00 19.41 C
ATOM 2143 NE ARG A 280 -12.225 12.753 31.066 1.00 20.87 N
ATOM 2144 CZ ARG A 280 -12.072 13.445 29.938 1.00 21.21 C
ATOM 2145 NH1 ARG A 280 -13.122 13.694 29.171 1.00 22.96 N
ATOM 2146 NH2 ARG A 280 -10.875 13.882 29.569 1.00 21.77 N
ATOM 2147 N TYR A 281 -13.617 7.348 33.093 1.00 16.24 N
ATOM 2148 CA TYR A 281 -14.213 6.184 32.457 1.00 16.01 C
ATOM 2149 C TYR A 281 -14.704 6.520 31.057 1.00 16.04 C
ATOM 2150 O TYR A 281 -15.070 7.665 30.777 1.00 15.78 O
ATOM 2151 CB TYR A 281 -15.407 5.666 33.266 1.00 16.07 C
ATOM 2152 CG TYR A 281 -15.089 5.211 34.673 1.00 15.58 C
ATOM 2153 CD1 TYR A 281 -14.208 4.149 34.908 1.00 15.82 C
ATOM 2154 CD2 TYR A 281 -15.700 5.819 35.771 1.00 15.89 C
ATOM 2155 CE1 TYR A 281 -13.923 3.722 36.203 1.00 15.52 C
ATOM 2156 CE2 TYR A 281 -15.423 5.398 37.071 1.00 15.63 C
ATOM 2157 CZ TYR A 281 -14.536 4.347 37.277 1.00 15.99 C
ATOM 2158 OH TYR A 281 -14.252 3.921 38.556 1.00 15.69 O
ATOM 2159 N PHE A 282 -14.717 5.515 30.183 1.00 16.25 N
ATOM 2160 CA PHE A 282 -15.497 5.602 28.951 1.00 16.68 C
ATOM 2161 C PHE A 282 -16.954 5.387 29.332 1.00 17.14 C
ATOM 2162 O PHE A 282 -17.306 4.363 29.917 1.00 17.14 O
ATOM 2163 CB PHE A 282 -15.064 4.546 27.931 1.00 16.33 C
ATOM 2164 CG PHE A 282 -13.713 4.802 27.331 1.00 15.51 C
ATOM 2165 CD1 PHE A 282 -12.585 4.162 27.833 1.00 15.06 C
ATOM 2166 CD2 PHE A 282 -13.566 5.684 26.262 1.00 15.02 C
ATOM 2167 CE1 PHE A 282 -11.333 4.392 27.278 1.00 14.65 C
ATOM 2168 CE2 PHE A 282 -12.317 5.927 25.706 1.00 14.35 C
ATOM 2169 CZ PHE A 282 -11.194 5.279 26.221 1.00 15.58 C
ATOM 2170 N ALA A 283 -17.787 6.378 29.029 1.00 18.13 N
ATOM 2171 CA ALA A 283 -19.217 6.306 29.314 1.00 19.09 C
ATOM 2172 C ALA A 283 -19.972 7.283 28.427 1.00 19.84 C
ATOM 2173 O ALA A 283 -19.378 8.195 27.850 1.00 19.89 O
ATOM 2174 CB ALA A 283 -19.496 6.601 30.795 1.00 19.05 C
ATOM 2175 N ASN A 284 -21.275 7.064 28.296 1.00 20.99 N
ATOM 2176 CA ASN A 284 -22.152 8.054 27.679 1.00 22.28 C
ATOM 2177 C ASN A 284 -23.175 8.539 28.705 1.00 23.14 C
ATOM 2178 O ASN A 284 -23.095 8.166 29.877 1.00 22.83 O
ATOM 2179 CB ASN A 284 -22.809 7.506 26.399 1.00 22.38 C
ATOM 2180 CG ASN A 284 -23.659 6.268 26.643 1.00 22.53 C
ATOM 2181 OD1 ASN A 284 -24.276 6.110 27.698 1.00 22.63 O
ATOM 2182 ND2 ASN A 284 -23.705 5.385 25.650 1.00 22.66 N
ATOM 2183 N LYS A 285 -24.126 9.363 28.270 1.00 24.27 N
ATOM 2184 CA LYS A 285 -25.166 9.891 29.158 1.00 25.48 C
ATOM 2185 C LYS A 285 -25.866 8.806 29.975 1.00 25.75 C
ATOM 2186 O LYS A 285 -26.036 8.946 31.190 1.00 26.00 O
ATOM 2187 CB LYS A 285 -26.203 10.685 28.355 1.00 25.80 C
ATOM 2188 CG LYS A 285 -25.745 12.074 27.950 1.00 27.68 C
ATOM 2189 CD LYS A 285 -26.870 12.850 27.282 1.00 30.57 C
ATOM 2190 CE LYS A 285 -26.438 14.272 26.957 1.00 32.09 C
ATOM 2191 NZ LYS A 285 -27.502 15.024 26.230 1.00 33.16 N
ATOM 2192 N GLU A 286 -26.248 7.722 29.302 1.00 26.05 N
ATOM 2193 CA GLU A 286 -27.016 6.643 29.919 1.00 26.61 C
ATOM 2194 C GLU A 286 -26.181 5.812 30.897 1.00 25.85 C
ATOM 2195 O GLU A 286 -26.580 5.617 32.049 1.00 25.77 O
ATOM 2196 CB GLU A 286 -27.648 5.751 28.841 1.00 26.60 C
ATOM 2197 CG GLU A 286 -28.570 6.506 27.872 1.00 28.27 C
ATOM 2198 CD GLU A 286 -28.852 5.750 26.577 1.00 28.80 C
ATOM 2199 OE1 GLU A 286 -28.044 4.872 26.191 1.00 32.37 O
ATOM 2200 OE2 GLU A 286 -29.885 6.049 25.931 1.00 32.75 O
ATOM 2201 N THR A 287 -25.020 5.342 30.443 1.00 25.30 N
ATOM 2202 CA THR A 287 -24.184 4.443 31.247 1.00 24.72 C
ATOM 2203 C THR A 287 -23.519 5.128 32.443 1.00 24.61 C
ATOM 2204 O THR A 287 -23.223 4.478 33.445 1.00 24.46 O
ATOM 2205 CB THR A 287 -23.122 3.712 30.396 1.00 24.58 C
ATOM 2206 OG1 THR A 287 -22.283 4.671 29.743 1.00 23.95 O
ATOM 2207 CG2 THR A 287 -23.790 2.816 29.355 1.00 24.50 C
ATOM 2208 N ASP A 288 -23.297 6.436 32.337 1.00 24.60 N
ATOM 2209 CA ASP A 288 -22.796 7.233 33.459 1.00 24.97 C
ATOM 2210 C ASP A 288 -23.702 7.095 34.689 1.00 25.01 C
ATOM 2211 O ASP A 288 -23.220 7.024 35.820 1.00 24.75 O
ATOM 2212 CB ASP A 288 -22.650 8.704 33.055 1.00 24.96 C
ATOM 2213 CG ASP A 288 -22.396 9.619 34.245 1.00 25.85 C
ATOM 2214 OD1 ASP A 288 -23.285 10.439 34.560 1.00 26.82 O
ATOM 2215 OD2 ASP A 288 -21.324 9.506 34.875 1.00 25.89 O
ATOM 2216 N LYS A 289 -25.011 7.030 34.445 1.00 25.14 N
ATOM 2217 CA LYS A 289 -26.014 6.895 35.505 1.00 25.27 C
ATOM 2218 C LYS A 289 -25.962 5.539 36.206 1.00 25.31 C
ATOM 2219 O LYS A 289 -26.453 5.398 37.329 1.00 25.42 O
ATOM 2220 CB LYS A 289 -27.417 7.138 34.938 1.00 25.50 C
ATOM 2221 CG LYS A 289 -27.628 8.546 34.408 1.00 26.33 C
ATOM 2222 CD LYS A 289 -29.033 8.728 33.855 1.00 27.82 C
ATOM 2223 CE LYS A 289 -29.164 10.059 33.134 1.00 28.37 C
ATOM 2224 NZ LYS A 289 -30.543 10.265 32.602 1.00 29.14 N
ATOM 2225 N GLN A 290 -25.367 4.552 35.538 1.00 24.91 N
ATOM 2226 CA GLN A 290 -25.242 3.198 36.073 1.00 24.98 C
ATOM 2227 C GLN A 290 -23.993 3.029 36.940 1.00 24.38 C
ATOM 2228 O GLN A 290 -23.868 2.043 37.667 1.00 24.51 O
ATOM 2229 CB GLN A 290 -25.228 2.176 34.934 1.00 24.89 C
ATOM 2230 CG GLN A 290 -26.554 2.035 34.209 1.00 25.73 C
ATOM 2231 CD GLN A 290 -26.489 1.042 33.070 1.00 26.17 C
ATOM 2232 OE1 GLN A 290 -27.023 -0.062 33.164 1.00 28.97 O
ATOM 2233 NE2 GLN A 290 -25.826 1.427 31.985 1.00 27.42 N
ATOM 2234 N ILE A 291 -23.070 3.984 36.849 1.00 23.79 N
ATOM 2235 CA ILE A 291 -21.858 3.964 37.668 1.00 23.52 C
ATOM 2236 C ILE A 291 -22.130 4.682 38.988 1.00 23.51 C
ATOM 2237 O ILE A 291 -22.559 5.840 38.994 1.00 23.32 O
ATOM 2238 CB ILE A 291 -20.644 4.607 36.942 1.00 23.44 C
ATOM 2239 CG1 ILE A 291 -20.428 3.957 35.568 1.00 23.29 C
ATOM 2240 CG2 ILE A 291 -19.378 4.499 37.802 1.00 23.24 C
ATOM 2241 CD1 ILE A 291 -19.481 4.728 34.654 1.00 23.04 C
ATOM 2242 N LEU A 292 -21.890 3.981 40.096 1.00 23.55 N
ATOM 2243 CA LEU A 292 -22.092 4.540 41.432 1.00 23.76 C
ATOM 2244 C LEU A 292 -21.147 5.705 41.698 1.00 23.80 C
ATOM 2245 O LEU A 292 -20.013 5.725 41.213 1.00 23.83 O
ATOM 2246 CB LEU A 292 -21.923 3.468 42.512 1.00 23.76 C
ATOM 2247 CG LEU A 292 -23.018 2.404 42.644 1.00 24.43 C
ATOM 2248 CD1 LEU A 292 -22.526 1.257 43.503 1.00 24.96 C
ATOM 2249 CD2 LEU A 292 -24.314 2.988 43.214 1.00 25.86 C
ATOM 2250 N GLN A 293 -21.638 6.670 42.472 1.00 23.74 N
ATOM 2251 CA GLN A 293 -20.902 7.884 42.821 1.00 23.77 C
ATOM 2252 C GLN A 293 -19.512 7.595 43.390 1.00 22.87 C
ATOM 2253 O GLN A 293 -18.549 8.281 43.046 1.00 22.69 O
ATOM 2254 CB GLN A 293 -21.717 8.724 43.819 1.00 23.88 C
ATOM 2255 CG GLN A 293 -23.120 9.099 43.324 1.00 25.04 C
ATOM 2256 CD GLN A 293 -24.039 9.629 44.426 1.00 25.26 C
ATOM 2257 OE1 GLN A 293 -24.557 10.741 44.330 1.00 27.54 O
ATOM 2258 NE2 GLN A 293 -24.243 8.834 45.470 1.00 27.45 N
ATOM 2259 N ASN A 294 -19.418 6.570 44.243 1.00 22.18 N
ATOM 2260 CA ASN A 294 -18.166 6.222 44.928 1.00 21.59 C
ATOM 2261 C ASN A 294 -17.083 5.597 44.030 1.00 20.97 C
ATOM 2262 O ASN A 294 -16.003 5.235 44.508 1.00 20.94 O
ATOM 2263 CB ASN A 294 -18.431 5.351 46.175 1.00 21.67 C
ATOM 2264 CG ASN A 294 -18.935 3.939 45.841 1.00 22.22 C
ATOM 2265 OD1 ASN A 294 -19.055 3.548 44.678 1.00 21.88 O
ATOM 2266 ND2 ASN A 294 -19.230 3.168 46.884 1.00 22.77 N
ATOM 2267 N ARG A 295 -17.380 5.479 42.738 1.00 20.48 N
ATOM 2268 CA ARG A 295 -16.434 4.923 41.769 1.00 19.89 C
ATOM 2269 C ARG A 295 -15.777 6.017 40.932 1.00 19.84 C
ATOM 2270 O ARG A 295 -14.813 5.759 40.208 1.00 19.57 O
ATOM 2271 CB ARG A 295 -17.129 3.927 40.828 1.00 19.77 C
ATOM 2272 CG ARG A 295 -18.095 2.953 41.488 1.00 19.12 C
ATOM 2273 CD ARG A 295 -17.430 2.086 42.548 1.00 19.49 C
ATOM 2274 NE ARG A 295 -18.400 1.194 43.183 1.00 19.09 N
ATOM 2275 CZ ARG A 295 -18.700 -0.022 42.737 1.00 19.24 C
ATOM 2276 NH1 ARG A 295 -18.105 -0.502 41.650 1.00 18.89 N
ATOM 2277 NH2 ARG A 295 -19.596 -0.761 43.373 1.00 19.50 N
ATOM 2278 N LYS A 296 -16.301 7.235 41.032 1.00 19.78 N
ATOM 2279 CA LYS A 296 -15.895 8.330 40.153 1.00 19.94 C
ATOM 2280 C LYS A 296 -14.815 9.215 40.766 1.00 19.97 C
ATOM 2281 O LYS A 296 -14.931 9.653 41.914 1.00 20.09 O
ATOM 2282 CB LYS A 296 -17.118 9.151 39.737 1.00 20.00 C
ATOM 2283 CG LYS A 296 -18.133 8.331 38.928 1.00 20.42 C
ATOM 2284 CD LYS A 296 -19.462 9.041 38.752 1.00 22.96 C
ATOM 2285 CE LYS A 296 -20.390 8.183 37.905 1.00 23.50 C
ATOM 2286 NZ LYS A 296 -21.735 8.779 37.691 1.00 24.64 N
ATOM 2287 N SER A 297 -13.764 9.468 39.990 1.00 20.07 N
ATOM 2288 CA SER A 297 -12.635 10.288 40.433 1.00 20.35 C
ATOM 2289 C SER A 297 -12.960 11.778 40.304 1.00 20.69 C
ATOM 2290 O SER A 297 -13.830 12.148 39.517 1.00 20.83 O
ATOM 2291 CB SER A 297 -11.390 9.965 39.602 1.00 20.20 C
ATOM 2292 OG SER A 297 -11.530 10.443 38.276 1.00 19.89 O
ATOM 2293 N PRO A 298 -12.257 12.639 41.069 1.00 21.26 N
ATOM 2294 CA PRO A 298 -12.378 14.085 40.884 1.00 21.67 C
ATOM 2295 C PRO A 298 -12.211 14.522 39.423 1.00 22.11 C
ATOM 2296 O PRO A 298 -12.931 15.414 38.977 1.00 22.49 O
ATOM 2297 CB PRO A 298 -11.239 14.638 41.745 1.00 21.67 C
ATOM 2298 CG PRO A 298 -11.120 13.656 42.842 1.00 21.75 C
ATOM 2299 CD PRO A 298 -11.332 12.319 42.174 1.00 21.44 C
ATOM 2300 N GLU A 299 -11.280 13.893 38.699 1.00 22.41 N
ATOM 2301 CA GLU A 299 -11.044 14.185 37.277 1.00 23.02 C
ATOM 2302 C GLU A 299 -12.294 13.882 36.447 1.00 22.58 C
ATOM 2303 O GLU A 299 -12.687 14.683 35.597 1.00 23.07 O
ATOM 2304 CB GLU A 299 -9.834 13.393 36.739 1.00 22.91 C
ATOM 2305 CG GLU A 299 -9.428 13.729 35.291 1.00 24.15 C
ATOM 2306 CD GLU A 299 -8.434 12.734 34.663 1.00 24.38 C
ATOM 2307 OE1 GLU A 299 -7.989 11.776 35.334 1.00 25.94 O
ATOM 2308 OE2 GLU A 299 -8.093 12.920 33.473 1.00 27.57 O
ATOM 2309 N TYR A 300 -12.910 12.728 36.704 1.00 22.34 N
ATOM 2310 CA TYR A 300 -14.138 12.321 36.022 1.00 22.25 C
ATOM 2311 C TYR A 300 -15.298 13.275 36.318 1.00 22.42 C
ATOM 2312 O TYR A 300 -16.065 13.621 35.425 1.00 22.29 O
ATOM 2313 CB TYR A 300 -14.521 10.891 36.414 1.00 22.12 C
ATOM 2314 CG TYR A 300 -15.724 10.347 35.672 1.00 21.99 C
ATOM 2315 CD1 TYR A 300 -15.585 9.745 34.422 1.00 21.74 C
ATOM 2316 CD2 TYR A 300 -17.004 10.429 36.223 1.00 22.10 C
ATOM 2317 CE1 TYR A 300 -16.691 9.241 33.741 1.00 21.57 C
ATOM 2318 CE2 TYR A 300 -18.115 9.930 35.547 1.00 22.11 C
ATOM 2319 CZ TYR A 300 -17.951 9.336 34.309 1.00 22.14 C
ATOM 2320 OH TYR A 300 -19.049 8.839 33.639 1.00 22.44 O
ATOM 2321 N LEU A 301 -15.421 13.692 37.575 1.00 22.64 N
ATOM 2322 CA LEU A 301 -16.516 14.575 37.983 1.00 23.37 C
ATOM 2323 C LEU A 301 -16.387 15.974 37.378 1.00 23.67 C
ATOM 2324 O LEU A 301 -17.393 16.630 37.092 1.00 23.91 O
ATOM 2325 CB LEU A 301 -16.612 14.644 39.514 1.00 23.30 C
ATOM 2326 CG LEU A 301 -17.005 13.347 40.235 1.00 23.64 C
ATOM 2327 CD1 LEU A 301 -16.723 13.436 41.733 1.00 23.76 C
ATOM 2328 CD2 LEU A 301 -18.463 12.966 39.974 1.00 24.38 C
ATOM 2329 N LYS A 302 -15.148 16.407 37.164 1.00 24.00 N
ATOM 2330 CA LYS A 302 -14.862 17.723 36.597 1.00 24.37 C
ATOM 2331 C LYS A 302 -14.932 17.740 35.068 1.00 24.21 C
ATOM 2332 O LYS A 302 -15.589 18.608 34.486 1.00 24.36 O
ATOM 2333 CB LYS A 302 -13.491 18.210 37.072 1.00 24.40 C
ATOM 2334 CG LYS A 302 -13.101 19.608 36.593 1.00 25.36 C
ATOM 2335 CD LYS A 302 -11.629 19.898 36.870 1.00 25.61 C
ATOM 2336 CE LYS A 302 -11.386 20.346 38.308 1.00 28.18 C
ATOM 2337 NZ LYS A 302 -11.669 21.802 38.509 1.00 29.62 N
ATOM 2338 N ALA A 303 -14.249 16.789 34.428 1.00 23.76 N
ATOM 2339 CA ALA A 303 -14.112 16.777 32.964 1.00 23.40 C
ATOM 2340 C ALA A 303 -15.171 15.950 32.234 1.00 22.99 C
ATOM 2341 O ALA A 303 -15.351 16.097 31.023 1.00 23.18 O
ATOM 2342 CB ALA A 303 -12.708 16.324 32.565 1.00 23.54 C
ATOM 2343 N GLY A 304 -15.864 15.083 32.967 1.00 22.45 N
ATOM 2344 CA GLY A 304 -16.843 14.180 32.368 1.00 21.77 C
ATOM 2345 C GLY A 304 -16.182 12.931 31.808 1.00 21.18 C
ATOM 2346 O GLY A 304 -14.983 12.711 31.996 1.00 21.21 O
ATOM 2347 N SER A 305 -16.962 12.120 31.104 1.00 20.90 N
ATOM 2348 CA SER A 305 -16.479 10.835 30.612 1.00 20.39 C
ATOM 2349 C SER A 305 -15.622 10.956 29.357 1.00 20.14 C
ATOM 2350 O SER A 305 -15.629 11.983 28.666 1.00 19.89 O
ATOM 2351 CB SER A 305 -17.656 9.889 30.351 1.00 20.61 C
ATOM 2352 OG SER A 305 -18.432 10.334 29.253 1.00 20.76 O
ATOM 2353 N LEU A 306 -14.879 9.891 29.079 1.00 19.70 N
ATOM 2354 CA LEU A 306 -14.203 9.734 27.804 1.00 19.72 C
ATOM 2355 C LEU A 306 -15.215 9.199 26.797 1.00 19.81 C
ATOM 2356 O LEU A 306 -16.121 8.445 27.159 1.00 19.24 O
ATOM 2357 CB LEU A 306 -13.038 8.754 27.932 1.00 19.62 C
ATOM 2358 CG LEU A 306 -11.913 9.067 28.918 1.00 19.21 C
ATOM 2359 CD1 LEU A 306 -11.019 7.845 29.076 1.00 19.47 C
ATOM 2360 CD2 LEU A 306 -11.111 10.280 28.460 1.00 18.66 C
ATOM 2361 N LYS A 307 -15.057 9.600 25.538 1.00 20.15 N
ATOM 2362 CA LYS A 307 -16.019 9.253 24.499 1.00 20.47 C
ATOM 2363 C LYS A 307 -15.423 8.269 23.496 1.00 20.60 C
ATOM 2364 O LYS A 307 -14.296 8.451 23.025 1.00 20.29 O
ATOM 2365 CB LYS A 307 -16.508 10.514 23.767 1.00 20.72 C
ATOM 2366 CG LYS A 307 -16.839 11.711 24.666 1.00 21.66 C
ATOM 2367 CD LYS A 307 -18.041 11.445 25.558 1.00 23.61 C
ATOM 2368 CE LYS A 307 -18.385 12.672 26.392 1.00 24.35 C
ATOM 2369 NZ LYS A 307 -19.466 12.362 27.364 1.00 25.74 N
ATOM 2370 N ASP A 308 -16.189 7.228 23.180 1.00 20.93 N
ATOM 2371 CA ASP A 308 -15.805 6.252 22.160 1.00 21.49 C
ATOM 2372 C ASP A 308 -17.054 5.572 21.598 1.00 22.03 C
ATOM 2373 O ASP A 308 -18.024 5.367 22.334 1.00 22.25 O
ATOM 2374 CB ASP A 308 -14.855 5.201 22.751 1.00 21.28 C
ATOM 2375 CG ASP A 308 -14.157 4.369 21.681 1.00 21.48 C
ATOM 2376 OD1 ASP A 308 -14.545 3.204 21.491 1.00 22.07 O
ATOM 2377 OD2 ASP A 308 -13.235 4.884 21.018 1.00 21.07 O
ATOM 2378 N PRO A 309 -17.048 5.243 20.289 1.00 22.46 N
ATOM 2379 CA PRO A 309 -18.157 4.476 19.709 1.00 23.00 C
ATOM 2380 C PRO A 309 -18.207 3.022 20.191 1.00 23.31 C
ATOM 2381 O PRO A 309 -19.290 2.440 20.261 1.00 24.09 O
ATOM 2382 CB PRO A 309 -17.874 4.514 18.199 1.00 22.94 C
ATOM 2383 CG PRO A 309 -16.808 5.534 18.002 1.00 22.89 C
ATOM 2384 CD PRO A 309 -16.037 5.594 19.275 1.00 22.40 C
ATOM 2385 N LEU A 310 -17.050 2.444 20.511 1.00 23.35 N
ATOM 2386 CA LEU A 310 -16.977 1.040 20.926 1.00 23.03 C
ATOM 2387 C LEU A 310 -16.981 0.876 22.452 1.00 22.41 C
ATOM 2388 O LEU A 310 -17.809 0.147 23.000 1.00 22.94 O
ATOM 2389 CB LEU A 310 -15.750 0.350 20.303 1.00 23.24 C
ATOM 2390 CG LEU A 310 -15.479 -1.144 20.557 1.00 23.41 C
ATOM 2391 CD1 LEU A 310 -16.614 -2.051 20.066 1.00 24.66 C
ATOM 2392 CD2 LEU A 310 -14.152 -1.563 19.924 1.00 23.31 C
ATOM 2393 N LEU A 311 -16.074 1.578 23.126 1.00 21.34 N
ATOM 2394 CA LEU A 311 -15.777 1.328 24.538 1.00 19.81 C
ATOM 2395 C LEU A 311 -16.712 2.002 25.528 1.00 19.01 C
ATOM 2396 O LEU A 311 -17.111 3.149 25.339 1.00 18.45 O
ATOM 2397 CB LEU A 311 -14.349 1.760 24.859 1.00 19.96 C
ATOM 2398 CG LEU A 311 -13.177 1.052 24.187 1.00 20.49 C
ATOM 2399 CD1 LEU A 311 -11.900 1.707 24.667 1.00 20.78 C
ATOM 2400 CD2 LEU A 311 -13.168 -0.445 24.483 1.00 21.25 C
ATOM 2401 N ASP A 312 -17.012 1.276 26.604 1.00 17.93 N
ATOM 2402 CA ASP A 312 -17.827 1.763 27.707 1.00 17.13 C
ATOM 2403 C ASP A 312 -17.506 0.903 28.922 1.00 16.37 C
ATOM 2404 O ASP A 312 -17.855 -0.269 28.951 1.00 16.19 O
ATOM 2405 CB ASP A 312 -19.308 1.627 27.357 1.00 17.56 C
ATOM 2406 CG ASP A 312 -20.200 2.299 28.364 1.00 17.82 C
ATOM 2407 OD1 ASP A 312 -20.540 3.480 28.135 1.00 19.72 O
ATOM 2408 OD2 ASP A 312 -20.536 1.661 29.386 1.00 18.06 O
ATOM 2409 N ASP A 313 -16.848 1.479 29.925 1.00 15.82 N
ATOM 2410 CA ASP A 313 -16.309 0.671 31.027 1.00 15.01 C
ATOM 2411 C ASP A 313 -17.359 -0.152 31.781 1.00 14.93 C
ATOM 2412 O ASP A 313 -17.146 -1.339 32.046 1.00 14.76 O
ATOM 2413 CB ASP A 313 -15.455 1.520 31.974 1.00 14.79 C
ATOM 2414 CG ASP A 313 -14.181 2.031 31.309 1.00 14.28 C
ATOM 2415 OD1 ASP A 313 -13.532 1.264 30.557 1.00 13.95 O
ATOM 2416 OD2 ASP A 313 -13.820 3.198 31.545 1.00 12.74 O
ATOM 2417 N HIS A 314 -18.492 0.467 32.103 1.00 15.09 N
ATOM 2418 CA HIS A 314 -19.573 -0.233 32.802 1.00 15.32 C
ATOM 2419 C HIS A 314 -20.222 -1.309 31.922 1.00 14.98 C
ATOM 2420 O HIS A 314 -20.360 -2.465 32.343 1.00 14.97 O
ATOM 2421 CB HIS A 314 -20.624 0.758 33.320 1.00 15.67 C
ATOM 2422 CG HIS A 314 -21.625 0.134 34.238 1.00 16.68 C
ATOM 2423 ND1 HIS A 314 -22.732 -0.545 33.777 1.00 18.44 N
ATOM 2424 CD2 HIS A 314 -21.673 0.062 35.589 1.00 17.80 C
ATOM 2425 CE1 HIS A 314 -23.426 -0.998 34.806 1.00 18.56 C
ATOM 2426 NE2 HIS A 314 -22.804 -0.645 35.917 1.00 18.16 N
ATOM 2427 N GLY A 315 -20.611 -0.923 30.708 1.00 14.95 N
ATOM 2428 CA GLY A 315 -21.177 -1.849 29.728 1.00 15.10 C
ATOM 2429 C GLY A 315 -20.247 -3.006 29.399 1.00 14.94 C
ATOM 2430 O GLY A 315 -20.695 -4.144 29.279 1.00 15.23 O
ATOM 2431 N ASP A 316 -18.954 -2.711 29.256 1.00 14.95 N
ATOM 2432 CA ASP A 316 -17.943 -3.735 28.952 1.00 14.78 C
ATOM 2433 C ASP A 316 -17.689 -4.681 30.130 1.00 14.50 C
ATOM 2434 O ASP A 316 -17.408 -5.855 29.923 1.00 14.38 O
ATOM 2435 CB ASP A 316 -16.626 -3.107 28.460 1.00 15.08 C
ATOM 2436 CG ASP A 316 -16.760 -2.435 27.091 1.00 16.37 C
ATOM 2437 OD1 ASP A 316 -17.655 -2.814 26.304 1.00 16.93 O
ATOM 2438 OD2 ASP A 316 -15.960 -1.516 26.802 1.00 16.40 O
ATOM 2439 N PHE A 317 -17.791 -4.179 31.358 1.00 14.49 N
ATOM 2440 CA PHE A 317 -17.718 -5.061 32.527 1.00 14.59 C
ATOM 2441 C PHE A 317 -18.837 -6.104 32.461 1.00 14.49 C
ATOM 2442 O PHE A 317 -18.584 -7.302 32.595 1.00 13.90 O
ATOM 2443 CB PHE A 317 -17.797 -4.278 33.843 1.00 14.42 C
ATOM 2444 CG PHE A 317 -17.713 -5.153 35.073 1.00 14.76 C
ATOM 2445 CD1 PHE A 317 -16.485 -5.667 35.498 1.00 14.90 C
ATOM 2446 CD2 PHE A 317 -18.861 -5.480 35.798 1.00 15.27 C
ATOM 2447 CE1 PHE A 317 -16.399 -6.480 36.628 1.00 15.35 C
ATOM 2448 CE2 PHE A 317 -18.782 -6.295 36.937 1.00 15.21 C
ATOM 2449 CZ PHE A 317 -17.546 -6.794 37.346 1.00 14.86 C
ATOM 2450 N ILE A 318 -20.064 -5.635 32.231 1.00 15.12 N
ATOM 2451 CA ILE A 318 -21.230 -6.519 32.109 1.00 16.20 C
ATOM 2452 C ILE A 318 -21.024 -7.526 30.975 1.00 16.30 C
ATOM 2453 O ILE A 318 -21.210 -8.733 31.163 1.00 16.44 O
ATOM 2454 CB ILE A 318 -22.549 -5.713 31.898 1.00 16.22 C
ATOM 2455 CG1 ILE A 318 -22.829 -4.817 33.113 1.00 16.45 C
ATOM 2456 CG2 ILE A 318 -23.728 -6.657 31.604 1.00 17.12 C
ATOM 2457 CD1 ILE A 318 -24.025 -3.885 32.947 1.00 17.23 C
ATOM 2458 N ARG A 319 -20.622 -7.025 29.809 1.00 16.81 N
ATOM 2459 CA ARG A 319 -20.411 -7.870 28.633 1.00 17.58 C
ATOM 2460 C ARG A 319 -19.302 -8.892 28.861 1.00 17.10 C
ATOM 2461 O ARG A 319 -19.409 -10.043 28.426 1.00 17.14 O
ATOM 2462 CB ARG A 319 -20.125 -7.018 27.393 1.00 17.68 C
ATOM 2463 CG ARG A 319 -21.379 -6.443 26.743 1.00 19.00 C
ATOM 2464 CD ARG A 319 -21.049 -5.694 25.453 1.00 19.27 C
ATOM 2465 NE ARG A 319 -20.409 -4.406 25.715 1.00 22.56 N
ATOM 2466 CZ ARG A 319 -21.063 -3.259 25.896 1.00 22.86 C
ATOM 2467 NH1 ARG A 319 -22.390 -3.226 25.839 1.00 24.03 N
ATOM 2468 NH2 ARG A 319 -20.387 -2.143 26.135 1.00 22.98 N
ATOM 2469 N MET A 320 -18.249 -8.469 29.561 1.00 16.68 N
ATOM 2470 CA MET A 320 -17.136 -9.353 29.900 1.00 16.70 C
ATOM 2471 C MET A 320 -17.590 -10.484 30.820 1.00 16.40 C
ATOM 2472 O MET A 320 -17.238 -11.641 30.607 1.00 16.58 O
ATOM 2473 CB MET A 320 -16.005 -8.559 30.551 1.00 16.63 C
ATOM 2474 CG MET A 320 -14.794 -9.385 30.953 1.00 16.57 C
ATOM 2475 SD MET A 320 -13.697 -8.467 32.055 1.00 17.15 S
ATOM 2476 CE MET A 320 -14.711 -8.319 33.533 1.00 17.95 C
ATOM 2477 N CYS A 321 -18.376 -10.143 31.837 1.00 16.57 N
ATOM 2478 CA CYS A 321 -18.898 -11.139 32.774 1.00 16.90 C
ATOM 2479 C CYS A 321 -19.842 -12.132 32.097 1.00 17.25 C
ATOM 2480 O CYS A 321 -19.815 -13.329 32.409 1.00 17.06 O
ATOM 2481 CB CYS A 321 -19.572 -10.454 33.963 1.00 17.05 C
ATOM 2482 SG CYS A 321 -18.395 -9.619 35.045 1.00 17.88 S
ATOM 2483 N THR A 322 -20.653 -11.635 31.163 1.00 17.74 N
ATOM 2484 CA THR A 322 -21.518 -12.492 30.348 1.00 18.50 C
ATOM 2485 C THR A 322 -20.660 -13.442 29.511 1.00 18.63 C
ATOM 2486 O THR A 322 -20.911 -14.651 29.486 1.00 18.58 O
ATOM 2487 CB THR A 322 -22.470 -11.665 29.448 1.00 18.57 C
ATOM 2488 OG1 THR A 322 -23.304 -10.837 30.268 1.00 19.28 O
ATOM 2489 CG2 THR A 322 -23.361 -12.576 28.609 1.00 19.24 C
ATOM 2490 N ALA A 323 -19.644 -12.883 28.853 1.00 18.93 N
ATOM 2491 CA ALA A 323 -18.681 -13.648 28.059 1.00 19.53 C
ATOM 2492 C ALA A 323 -18.007 -14.752 28.875 1.00 19.98 C
ATOM 2493 O ALA A 323 -17.912 -15.890 28.416 1.00 19.86 O
ATOM 2494 CB ALA A 323 -17.632 -12.717 27.449 1.00 19.61 C
ATOM 2495 N MET A 324 -17.552 -14.411 30.083 1.00 20.55 N
ATOM 2496 CA MET A 324 -16.913 -15.381 30.978 1.00 21.61 C
ATOM 2497 C MET A 324 -17.841 -16.563 31.273 1.00 21.61 C
ATOM 2498 O MET A 324 -17.414 -17.720 31.241 1.00 21.58 O
ATOM 2499 CB MET A 324 -16.481 -14.718 32.292 1.00 21.54 C
ATOM 2500 CG MET A 324 -15.290 -13.765 32.194 1.00 22.11 C
ATOM 2501 SD MET A 324 -14.972 -13.035 33.815 1.00 23.76 S
ATOM 2502 CE MET A 324 -13.589 -11.948 33.495 1.00 23.64 C
ATOM 2503 N LYS A 325 -19.108 -16.259 31.547 1.00 22.00 N
ATOM 2504 CA LYS A 325 -20.113 -17.280 31.843 1.00 22.71 C
ATOM 2505 C LYS A 325 -20.401 -18.172 30.638 1.00 22.82 C
ATOM 2506 O LYS A 325 -20.451 -19.399 30.770 1.00 22.91 O
ATOM 2507 CB LYS A 325 -21.409 -16.638 32.346 1.00 23.04 C
ATOM 2508 CG LYS A 325 -21.361 -16.178 33.788 1.00 24.80 C
ATOM 2509 CD LYS A 325 -22.731 -15.690 34.246 1.00 28.08 C
ATOM 2510 CE LYS A 325 -22.689 -15.155 35.669 1.00 29.47 C
ATOM 2511 NZ LYS A 325 -23.900 -14.342 35.984 1.00 31.04 N
ATOM 2512 N LYS A 326 -20.572 -17.557 29.470 1.00 22.88 N
ATOM 2513 CA LYS A 326 -20.893 -18.297 28.248 1.00 23.33 C
ATOM 2514 C LYS A 326 -19.811 -19.305 27.864 1.00 23.15 C
ATOM 2515 O LYS A 326 -20.122 -20.405 27.403 1.00 23.51 O
ATOM 2516 CB LYS A 326 -21.172 -17.349 27.077 1.00 23.36 C
ATOM 2517 CG LYS A 326 -22.461 -16.551 27.211 1.00 24.98 C
ATOM 2518 CD LYS A 326 -23.282 -16.623 25.930 1.00 27.21 C
ATOM 2519 CE LYS A 326 -24.240 -15.449 25.796 1.00 27.63 C
ATOM 2520 NZ LYS A 326 -23.651 -14.362 24.973 1.00 28.62 N
ATOM 2521 N ILE A 327 -18.549 -18.932 28.070 1.00 22.81 N
ATOM 2522 CA ILE A 327 -17.418 -19.776 27.669 1.00 22.68 C
ATOM 2523 C ILE A 327 -17.034 -20.819 28.729 1.00 22.72 C
ATOM 2524 O ILE A 327 -16.171 -21.669 28.489 1.00 22.43 O
ATOM 2525 CB ILE A 327 -16.176 -18.942 27.225 1.00 22.58 C
ATOM 2526 CG1 ILE A 327 -15.519 -18.230 28.415 1.00 22.71 C
ATOM 2527 CG2 ILE A 327 -16.559 -17.969 26.107 1.00 22.48 C
ATOM 2528 CD1 ILE A 327 -14.222 -17.503 28.067 1.00 22.72 C
ATOM 2529 N GLY A 328 -17.668 -20.746 29.897 1.00 22.91 N
ATOM 2530 CA GLY A 328 -17.513 -21.787 30.913 1.00 23.21 C
ATOM 2531 C GLY A 328 -16.736 -21.444 32.174 1.00 23.55 C
ATOM 2532 O GLY A 328 -16.420 -22.337 32.963 1.00 23.48 O
ATOM 2533 N LEU A 329 -16.416 -20.167 32.377 1.00 23.79 N
ATOM 2534 CA LEU A 329 -15.779 -19.756 33.632 1.00 24.22 C
ATOM 2535 C LEU A 329 -16.831 -19.663 34.724 1.00 24.68 C
ATOM 2536 O LEU A 329 -17.852 -18.993 34.550 1.00 24.88 O
ATOM 2537 CB LEU A 329 -15.048 -18.414 33.491 1.00 24.16 C
ATOM 2538 CG LEU A 329 -13.596 -18.442 33.015 1.00 24.01 C
ATOM 2539 CD1 LEU A 329 -13.522 -18.650 31.514 1.00 24.43 C
ATOM 2540 CD2 LEU A 329 -12.883 -17.153 33.409 1.00 24.09 C
ATOM 2541 N ASP A 330 -16.592 -20.344 35.842 1.00 25.07 N
ATOM 2542 CA ASP A 330 -17.531 -20.278 36.956 1.00 25.36 C
ATOM 2543 C ASP A 330 -17.281 -19.033 37.802 1.00 25.39 C
ATOM 2544 O ASP A 330 -16.265 -18.351 37.628 1.00 25.11 O
ATOM 2545 CB ASP A 330 -17.538 -21.575 37.789 1.00 25.89 C
ATOM 2546 CG ASP A 330 -16.213 -21.864 38.476 1.00 26.71 C
ATOM 2547 OD1 ASP A 330 -15.491 -20.919 38.857 1.00 27.65 O
ATOM 2548 OD2 ASP A 330 -15.905 -23.062 38.669 1.00 28.59 O
ATOM 2549 N ASP A 331 -18.214 -18.737 38.702 1.00 25.31 N
ATOM 2550 CA ASP A 331 -18.156 -17.517 39.503 1.00 25.36 C
ATOM 2551 C ASP A 331 -16.917 -17.453 40.402 1.00 24.85 C
ATOM 2552 O ASP A 331 -16.385 -16.367 40.644 1.00 24.76 O
ATOM 2553 CB ASP A 331 -19.449 -17.333 40.310 1.00 26.01 C
ATOM 2554 CG ASP A 331 -20.658 -17.012 39.425 1.00 27.51 C
ATOM 2555 OD1 ASP A 331 -20.476 -16.712 38.221 1.00 28.93 O
ATOM 2556 OD2 ASP A 331 -21.798 -17.062 39.939 1.00 30.01 O
ATOM 2557 N GLU A 332 -16.453 -18.613 40.872 1.00 24.28 N
ATOM 2558 CA GLU A 332 -15.226 -18.691 41.673 1.00 24.11 C
ATOM 2559 C GLU A 332 -14.017 -18.210 40.872 1.00 23.17 C
ATOM 2560 O GLU A 332 -13.223 -17.404 41.364 1.00 23.07 O
ATOM 2561 CB GLU A 332 -14.983 -20.113 42.195 1.00 24.25 C
ATOM 2562 CG GLU A 332 -13.738 -20.242 43.079 1.00 25.38 C
ATOM 2563 CD GLU A 332 -13.517 -21.644 43.616 1.00 25.61 C
ATOM 2564 OE1 GLU A 332 -12.340 -22.044 43.748 1.00 27.98 O
ATOM 2565 OE2 GLU A 332 -14.507 -22.345 43.915 1.00 28.36 O
ATOM 2566 N GLU A 333 -13.901 -18.702 39.638 1.00 22.20 N
ATOM 2567 CA GLU A 333 -12.833 -18.305 38.720 1.00 21.56 C
ATOM 2568 C GLU A 333 -12.863 -16.801 38.477 1.00 20.66 C
ATOM 2569 O GLU A 333 -11.832 -16.137 38.548 1.00 20.36 O
ATOM 2570 CB GLU A 333 -12.966 -19.033 37.383 1.00 21.78 C
ATOM 2571 CG GLU A 333 -12.852 -20.541 37.456 1.00 23.41 C
ATOM 2572 CD GLU A 333 -12.718 -21.165 36.085 1.00 25.42 C
ATOM 2573 OE1 GLU A 333 -11.651 -20.975 35.468 1.00 25.87 O
ATOM 2574 OE2 GLU A 333 -13.669 -21.842 35.628 1.00 25.37 O
ATOM 2575 N LYS A 334 -14.055 -16.278 38.197 1.00 19.67 N
ATOM 2576 CA LYS A 334 -14.259 -14.844 37.993 1.00 19.12 C
ATOM 2577 C LYS A 334 -13.753 -14.023 39.186 1.00 18.47 C
ATOM 2578 O LYS A 334 -13.005 -13.055 39.018 1.00 17.67 O
ATOM 2579 CB LYS A 334 -15.741 -14.564 37.721 1.00 19.16 C
ATOM 2580 CG LYS A 334 -16.099 -13.097 37.512 1.00 19.62 C
ATOM 2581 CD LYS A 334 -17.517 -12.923 36.955 1.00 20.57 C
ATOM 2582 CE LYS A 334 -18.603 -13.366 37.938 1.00 22.59 C
ATOM 2583 NZ LYS A 334 -19.978 -13.316 37.331 1.00 23.50 N
ATOM 2584 N LEU A 335 -14.156 -14.426 40.389 1.00 17.74 N
ATOM 2585 CA LEU A 335 -13.771 -13.710 41.604 1.00 17.66 C
ATOM 2586 C LEU A 335 -12.272 -13.824 41.892 1.00 17.03 C
ATOM 2587 O LEU A 335 -11.659 -12.866 42.370 1.00 16.72 O
ATOM 2588 CB LEU A 335 -14.616 -14.161 42.802 1.00 18.07 C
ATOM 2589 CG LEU A 335 -16.118 -13.848 42.705 1.00 19.40 C
ATOM 2590 CD1 LEU A 335 -16.872 -14.333 43.937 1.00 21.14 C
ATOM 2591 CD2 LEU A 335 -16.382 -12.363 42.466 1.00 20.52 C
ATOM 2592 N ASP A 336 -11.692 -14.983 41.572 1.00 16.65 N
ATOM 2593 CA ASP A 336 -10.244 -15.188 41.677 1.00 16.34 C
ATOM 2594 C ASP A 336 -9.502 -14.167 40.812 1.00 15.60 C
ATOM 2595 O ASP A 336 -8.561 -13.520 41.272 1.00 15.65 O
ATOM 2596 CB ASP A 336 -9.849 -16.612 41.257 1.00 16.75 C
ATOM 2597 CG ASP A 336 -10.146 -17.663 42.326 1.00 18.14 C
ATOM 2598 OD1 ASP A 336 -10.402 -17.306 43.499 1.00 19.58 O
ATOM 2599 OD2 ASP A 336 -10.105 -18.866 41.983 1.00 19.62 O
ATOM 2600 N LEU A 337 -9.941 -14.017 39.564 1.00 14.71 N
ATOM 2601 CA LEU A 337 -9.337 -13.040 38.655 1.00 13.96 C
ATOM 2602 C LEU A 337 -9.410 -11.634 39.230 1.00 13.61 C
ATOM 2603 O LEU A 337 -8.405 -10.921 39.276 1.00 13.11 O
ATOM 2604 CB LEU A 337 -10.009 -13.083 37.278 1.00 13.80 C
ATOM 2605 CG LEU A 337 -9.872 -14.361 36.442 1.00 13.60 C
ATOM 2606 CD1 LEU A 337 -10.722 -14.210 35.196 1.00 14.13 C
ATOM 2607 CD2 LEU A 337 -8.421 -14.633 36.074 1.00 13.01 C
ATOM 2608 N PHE A 338 -10.600 -11.241 39.680 1.00 13.52 N
ATOM 2609 CA PHE A 338 -10.811 -9.907 40.234 1.00 13.71 C
ATOM 2610 C PHE A 338 -9.950 -9.673 41.474 1.00 13.73 C
ATOM 2611 O PHE A 338 -9.428 -8.578 41.671 1.00 13.51 O
ATOM 2612 CB PHE A 338 -12.285 -9.673 40.585 1.00 14.17 C
ATOM 2613 CG PHE A 338 -13.214 -9.660 39.394 1.00 14.33 C
ATOM 2614 CD1 PHE A 338 -14.592 -9.762 39.586 1.00 14.64 C
ATOM 2615 CD2 PHE A 338 -12.724 -9.565 38.090 1.00 14.20 C
ATOM 2616 CE1 PHE A 338 -15.464 -9.744 38.505 1.00 15.25 C
ATOM 2617 CE2 PHE A 338 -13.592 -9.552 36.997 1.00 15.30 C
ATOM 2618 CZ PHE A 338 -14.963 -9.642 37.207 1.00 15.06 C
ATOM 2619 N ARG A 339 -9.809 -10.716 42.291 1.00 13.83 N
ATOM 2620 CA ARG A 339 -9.050 -10.651 43.540 1.00 14.29 C
ATOM 2621 C ARG A 339 -7.582 -10.320 43.278 1.00 13.68 C
ATOM 2622 O ARG A 339 -7.008 -9.457 43.948 1.00 13.71 O
ATOM 2623 CB ARG A 339 -9.186 -11.969 44.309 1.00 14.42 C
ATOM 2624 CG ARG A 339 -8.448 -12.023 45.639 1.00 15.72 C
ATOM 2625 CD ARG A 339 -8.906 -13.223 46.479 1.00 15.80 C
ATOM 2626 NE ARG A 339 -8.857 -14.490 45.740 1.00 19.06 N
ATOM 2627 CZ ARG A 339 -7.757 -15.218 45.555 1.00 20.38 C
ATOM 2628 NH1 ARG A 339 -6.586 -14.814 46.045 1.00 21.62 N
ATOM 2629 NH2 ARG A 339 -7.826 -16.354 44.870 1.00 22.01 N
ATOM 2630 N VAL A 340 -6.987 -10.998 42.299 1.00 13.18 N
ATOM 2631 CA VAL A 340 -5.587 -10.751 41.933 1.00 12.75 C
ATOM 2632 C VAL A 340 -5.415 -9.325 41.371 1.00 12.18 C
ATOM 2633 O VAL A 340 -4.458 -8.636 41.706 1.00 11.77 O
ATOM 2634 CB VAL A 340 -5.037 -11.832 40.964 1.00 12.81 C
ATOM 2635 CG1 VAL A 340 -3.591 -11.527 40.555 1.00 12.96 C
ATOM 2636 CG2 VAL A 340 -5.113 -13.217 41.606 1.00 13.49 C
ATOM 2637 N VAL A 341 -6.354 -8.885 40.536 1.00 12.12 N
ATOM 2638 CA VAL A 341 -6.342 -7.517 40.010 1.00 11.79 C
ATOM 2639 C VAL A 341 -6.318 -6.487 41.155 1.00 11.82 C
ATOM 2640 O VAL A 341 -5.469 -5.586 41.181 1.00 11.37 O
ATOM 2641 CB VAL A 341 -7.542 -7.280 39.047 1.00 11.89 C
ATOM 2642 CG1 VAL A 341 -7.697 -5.807 38.705 1.00 11.18 C
ATOM 2643 CG2 VAL A 341 -7.372 -8.117 37.779 1.00 11.63 C
ATOM 2644 N ALA A 342 -7.229 -6.648 42.115 1.00 11.57 N
ATOM 2645 CA ALA A 342 -7.281 -5.777 43.284 1.00 12.07 C
ATOM 2646 C ALA A 342 -6.014 -5.884 44.147 1.00 11.73 C
ATOM 2647 O ALA A 342 -5.548 -4.880 44.696 1.00 12.41 O
ATOM 2648 CB ALA A 342 -8.524 -6.082 44.111 1.00 11.90 C
ATOM 2649 N GLY A 343 -5.461 -7.091 44.244 1.00 12.07 N
ATOM 2650 CA GLY A 343 -4.221 -7.329 44.995 1.00 11.92 C
ATOM 2651 C GLY A 343 -3.063 -6.535 44.417 1.00 11.84 C
ATOM 2652 O GLY A 343 -2.275 -5.937 45.152 1.00 11.77 O
ATOM 2653 N VAL A 344 -2.970 -6.519 43.090 1.00 11.54 N
ATOM 2654 CA VAL A 344 -1.964 -5.711 42.390 1.00 11.46 C
ATOM 2655 C VAL A 344 -2.160 -4.211 42.662 1.00 11.30 C
ATOM 2656 O VAL A 344 -1.192 -3.478 42.893 1.00 11.21 O
ATOM 2657 CB VAL A 344 -1.964 -6.021 40.868 1.00 11.21 C
ATOM 2658 CG1 VAL A 344 -1.126 -5.003 40.091 1.00 12.11 C
ATOM 2659 CG2 VAL A 344 -1.439 -7.428 40.618 1.00 11.82 C
ATOM 2660 N LEU A 345 -3.412 -3.754 42.646 1.00 11.52 N
ATOM 2661 CA LEU A 345 -3.714 -2.361 42.973 1.00 11.85 C
ATOM 2662 C LEU A 345 -3.258 -1.967 44.385 1.00 12.11 C
ATOM 2663 O LEU A 345 -2.594 -0.946 44.556 1.00 12.92 O
ATOM 2664 CB LEU A 345 -5.200 -2.050 42.781 1.00 11.64 C
ATOM 2665 CG LEU A 345 -5.683 -1.878 41.335 1.00 11.34 C
ATOM 2666 CD1 LEU A 345 -7.190 -1.630 41.302 1.00 11.19 C
ATOM 2667 CD2 LEU A 345 -4.933 -0.744 40.637 1.00 10.91 C
ATOM 2668 N HIS A 346 -3.598 -2.776 45.385 1.00 12.94 N
ATOM 2669 CA HIS A 346 -3.180 -2.482 46.760 1.00 13.31 C
ATOM 2670 C HIS A 346 -1.665 -2.566 46.949 1.00 13.41 C
ATOM 2671 O HIS A 346 -1.083 -1.783 47.704 1.00 13.73 O
ATOM 2672 CB HIS A 346 -3.934 -3.362 47.759 1.00 13.71 C
ATOM 2673 CG HIS A 346 -5.406 -3.087 47.790 1.00 13.22 C
ATOM 2674 ND1 HIS A 346 -5.923 -1.871 48.179 1.00 14.26 N
ATOM 2675 CD2 HIS A 346 -6.468 -3.866 47.476 1.00 13.61 C
ATOM 2676 CE1 HIS A 346 -7.241 -1.910 48.093 1.00 13.84 C
ATOM 2677 NE2 HIS A 346 -7.597 -3.110 47.673 1.00 12.64 N
ATOM 2678 N LEU A 347 -1.033 -3.505 46.253 1.00 13.53 N
ATOM 2679 CA LEU A 347 0.431 -3.598 46.231 1.00 13.92 C
ATOM 2680 C LEU A 347 1.065 -2.261 45.863 1.00 14.10 C
ATOM 2681 O LEU A 347 2.013 -1.823 46.517 1.00 14.37 O
ATOM 2682 CB LEU A 347 0.904 -4.692 45.269 1.00 13.78 C
ATOM 2683 CG LEU A 347 2.410 -4.945 45.128 1.00 13.70 C
ATOM 2684 CD1 LEU A 347 3.109 -5.082 46.496 1.00 14.39 C
ATOM 2685 CD2 LEU A 347 2.655 -6.180 44.278 1.00 13.93 C
ATOM 2686 N GLY A 348 0.526 -1.615 44.827 1.00 13.96 N
ATOM 2687 CA GLY A 348 1.051 -0.339 44.341 1.00 14.25 C
ATOM 2688 C GLY A 348 0.915 0.812 45.311 1.00 14.73 C
ATOM 2689 O GLY A 348 1.645 1.796 45.213 1.00 14.94 O
ATOM 2690 N ASN A 349 -0.025 0.684 46.247 1.00 14.88 N
ATOM 2691 CA ASN A 349 -0.272 1.723 47.237 1.00 15.50 C
ATOM 2692 C ASN A 349 0.687 1.684 48.427 1.00 15.89 C
ATOM 2693 O ASN A 349 0.671 2.594 49.258 1.00 16.36 O
ATOM 2694 CB ASN A 349 -1.726 1.686 47.710 1.00 15.30 C
ATOM 2695 CG ASN A 349 -2.668 2.388 46.748 1.00 15.21 C
ATOM 2696 OD1 ASN A 349 -2.235 2.988 45.764 1.00 14.70 O
ATOM 2697 ND2 ASN A 349 -3.961 2.331 47.039 1.00 14.59 N
ATOM 2698 N ILE A 350 1.508 0.637 48.503 1.00 16.14 N
ATOM 2699 CA ILE A 350 2.520 0.517 49.563 1.00 16.83 C
ATOM 2700 C ILE A 350 3.690 1.477 49.314 1.00 17.48 C
ATOM 2701 O ILE A 350 4.340 1.416 48.266 1.00 17.50 O
ATOM 2702 CB ILE A 350 3.032 -0.937 49.716 1.00 16.79 C
ATOM 2703 CG1 ILE A 350 1.886 -1.871 50.129 1.00 16.72 C
ATOM 2704 CG2 ILE A 350 4.180 -1.005 50.727 1.00 16.64 C
ATOM 2705 CD1 ILE A 350 2.234 -3.341 50.114 1.00 16.95 C
ATOM 2706 N ASP A 351 3.931 2.359 50.286 1.00 18.06 N
ATOM 2707 CA ASP A 351 4.953 3.406 50.210 1.00 18.95 C
ATOM 2708 C ASP A 351 6.062 3.138 51.216 1.00 18.92 C
ATOM 2709 O ASP A 351 5.817 2.534 52.261 1.00 18.74 O
ATOM 2710 CB ASP A 351 4.353 4.768 50.561 1.00 19.55 C
ATOM 2711 CG ASP A 351 3.356 5.262 49.536 1.00 21.91 C
ATOM 2712 OD1 ASP A 351 3.510 4.927 48.349 1.00 24.64 O
ATOM 2713 OD2 ASP A 351 2.434 6.012 49.923 1.00 25.59 O
ATOM 2714 N PHE A 352 7.262 3.635 50.917 1.00 19.01 N
ATOM 2715 CA PHE A 352 8.429 3.436 51.783 1.00 19.03 C
ATOM 2716 C PHE A 352 9.084 4.757 52.181 1.00 19.64 C
ATOM 2717 O PHE A 352 8.968 5.763 51.477 1.00 19.69 O
ATOM 2718 CB PHE A 352 9.459 2.518 51.109 1.00 18.70 C
ATOM 2719 CG PHE A 352 8.862 1.271 50.517 1.00 17.95 C
ATOM 2720 CD1 PHE A 352 8.522 1.223 49.165 1.00 18.02 C
ATOM 2721 CD2 PHE A 352 8.625 0.152 51.307 1.00 17.19 C
ATOM 2722 CE1 PHE A 352 7.960 0.075 48.612 1.00 17.00 C
ATOM 2723 CE2 PHE A 352 8.062 -1.000 50.763 1.00 17.45 C
ATOM 2724 CZ PHE A 352 7.728 -1.036 49.409 1.00 17.25 C
ATOM 2725 N GLU A 353 9.774 4.740 53.320 1.00 19.97 N
ATOM 2726 CA GLU A 353 10.480 5.919 53.815 1.00 20.72 C
ATOM 2727 C GLU A 353 11.842 5.536 54.380 1.00 20.56 C
ATOM 2728 O GLU A 353 12.053 4.393 54.770 1.00 19.81 O
ATOM 2729 CB GLU A 353 9.647 6.658 54.869 1.00 20.53 C
ATOM 2730 CG GLU A 353 9.375 5.883 56.159 1.00 21.89 C
ATOM 2731 CD GLU A 353 8.461 6.636 57.116 1.00 22.33 C
ATOM 2732 OE1 GLU A 353 8.574 6.422 58.341 1.00 24.93 O
ATOM 2733 OE2 GLU A 353 7.629 7.442 56.646 1.00 25.20 O
ATOM 2734 N GLU A 354 12.753 6.506 54.411 1.00 20.97 N
ATOM 2735 CA GLU A 354 14.081 6.332 54.998 1.00 21.51 C
ATOM 2736 C GLU A 354 13.978 5.889 56.453 1.00 20.95 C
ATOM 2737 O GLU A 354 13.230 6.480 57.236 1.00 21.18 O
ATOM 2738 CB GLU A 354 14.859 7.650 54.935 1.00 21.87 C
ATOM 2739 CG GLU A 354 14.896 8.303 53.562 1.00 24.72 C
ATOM 2740 CD GLU A 354 16.126 7.932 52.758 1.00 28.50 C
ATOM 2741 OE1 GLU A 354 16.883 8.858 52.385 1.00 30.42 O
ATOM 2742 OE2 GLU A 354 16.342 6.727 52.503 1.00 30.69 O
ATOM 2743 N ALA A 355 14.720 4.842 56.801 1.00 20.85 N
ATOM 2744 CA ALA A 355 14.771 4.356 58.179 1.00 20.70 C
ATOM 2745 C ALA A 355 15.784 5.139 59.010 1.00 20.69 C
ATOM 2746 O ALA A 355 15.688 5.185 60.239 1.00 20.59 O
ATOM 2747 CB ALA A 355 15.103 2.871 58.207 1.00 20.64 C
ATOM 2748 N GLY A 356 16.762 5.741 58.336 1.00 20.64 N
ATOM 2749 CA GLY A 356 17.870 6.393 59.026 1.00 21.09 C
ATOM 2750 C GLY A 356 18.840 5.356 59.563 1.00 21.20 C
ATOM 2751 O GLY A 356 18.929 4.251 59.034 1.00 21.51 O
ATOM 2752 N SER A 357 19.536 5.696 60.642 1.00 21.58 N
ATOM 2753 CA SER A 357 20.665 4.899 61.122 1.00 21.91 C
ATOM 2754 C SER A 357 20.309 3.605 61.865 1.00 21.83 C
ATOM 2755 O SER A 357 21.199 2.890 62.335 1.00 21.67 O
ATOM 2756 CB SER A 357 21.581 5.772 61.979 1.00 22.07 C
ATOM 2757 OG SER A 357 22.072 6.857 61.218 1.00 24.13 O
ATOM 2758 N THR A 358 19.018 3.296 61.962 1.00 21.46 N
ATOM 2759 CA THR A 358 18.582 2.043 62.585 1.00 21.31 C
ATOM 2760 C THR A 358 19.043 0.841 61.757 1.00 21.58 C
ATOM 2761 O THR A 358 19.897 0.065 62.194 1.00 21.14 O
ATOM 2762 CB THR A 358 17.053 1.996 62.778 1.00 21.22 C
ATOM 2763 OG1 THR A 358 16.405 2.241 61.520 1.00 20.81 O
ATOM 2764 CG2 THR A 358 16.613 3.037 63.797 1.00 21.09 C
ATOM 2765 N SER A 359 18.487 0.707 60.557 1.00 22.14 N
ATOM 2766 CA SER A 359 18.852 -0.374 59.645 1.00 22.58 C
ATOM 2767 C SER A 359 19.713 0.127 58.491 1.00 22.74 C
ATOM 2768 O SER A 359 20.398 -0.664 57.842 1.00 23.45 O
ATOM 2769 CB SER A 359 17.593 -1.024 59.075 1.00 22.61 C
ATOM 2770 OG SER A 359 16.866 -0.085 58.303 1.00 23.03 O
ATOM 2771 N GLY A 360 19.665 1.435 58.238 1.00 22.87 N
ATOM 2772 CA GLY A 360 20.294 2.040 57.062 1.00 22.87 C
ATOM 2773 C GLY A 360 19.451 1.911 55.800 1.00 22.86 C
ATOM 2774 O GLY A 360 19.817 2.435 54.742 1.00 23.61 O
ATOM 2775 N GLY A 361 18.320 1.217 55.914 1.00 22.18 N
ATOM 2776 CA GLY A 361 17.456 0.935 54.766 1.00 21.50 C
ATOM 2777 C GLY A 361 16.178 1.747 54.757 1.00 20.82 C
ATOM 2778 O GLY A 361 16.209 2.978 54.797 1.00 20.77 O
ATOM 2779 N CYS A 362 15.047 1.052 54.704 1.00 20.46 N
ATOM 2780 CA CYS A 362 13.748 1.712 54.654 1.00 20.28 C
ATOM 2781 C CYS A 362 12.691 0.968 55.464 1.00 20.04 C
ATOM 2782 O CYS A 362 12.850 -0.214 55.773 1.00 19.94 O
ATOM 2783 CB CYS A 362 13.285 1.878 53.201 1.00 20.11 C
ATOM 2784 SG CYS A 362 12.842 0.341 52.366 1.00 20.92 S
ATOM 2785 N ASN A 363 11.628 1.690 55.815 1.00 19.88 N
ATOM 2786 CA ASN A 363 10.435 1.122 56.431 1.00 20.05 C
ATOM 2787 C ASN A 363 9.227 1.442 55.563 1.00 20.11 C
ATOM 2788 O ASN A 363 9.263 2.385 54.771 1.00 19.84 O
ATOM 2789 CB ASN A 363 10.196 1.721 57.825 1.00 20.08 C
ATOM 2790 CG ASN A 363 11.373 1.529 58.764 1.00 20.57 C
ATOM 2791 OD1 ASN A 363 11.767 2.454 59.477 1.00 22.02 O
ATOM 2792 ND2 ASN A 363 11.935 0.330 58.774 1.00 20.23 N
ATOM 2793 N LEU A 364 8.161 0.661 55.711 1.00 20.47 N
ATOM 2794 CA LEU A 364 6.868 1.039 55.143 1.00 21.09 C
ATOM 2795 C LEU A 364 6.360 2.275 55.873 1.00 21.57 C
ATOM 2796 O LEU A 364 6.502 2.374 57.097 1.00 21.66 O
ATOM 2797 CB LEU A 364 5.849 -0.093 55.294 1.00 21.08 C
ATOM 2798 CG LEU A 364 5.655 -1.084 54.144 1.00 21.50 C
ATOM 2799 CD1 LEU A 364 6.853 -2.007 53.982 1.00 22.08 C
ATOM 2800 CD2 LEU A 364 4.391 -1.894 54.382 1.00 21.33 C
ATOM 2801 N LYS A 365 5.782 3.220 55.133 1.00 22.08 N
ATOM 2802 CA LYS A 365 5.149 4.383 55.757 1.00 22.91 C
ATOM 2803 C LYS A 365 3.967 3.912 56.601 1.00 23.24 C
ATOM 2804 O LYS A 365 3.315 2.925 56.253 1.00 23.07 O
ATOM 2805 CB LYS A 365 4.670 5.393 54.705 1.00 23.13 C
ATOM 2806 CG LYS A 365 5.774 6.022 53.866 1.00 23.79 C
ATOM 2807 CD LYS A 365 5.260 7.223 53.088 1.00 25.67 C
ATOM 2808 CE LYS A 365 6.365 7.835 52.236 1.00 26.69 C
ATOM 2809 NZ LYS A 365 5.933 9.080 51.537 1.00 27.70 N
ATOM 2810 N ASN A 366 3.698 4.606 57.709 1.00 24.00 N
ATOM 2811 CA ASN A 366 2.525 4.307 58.544 1.00 24.84 C
ATOM 2812 C ASN A 366 1.209 4.352 57.761 1.00 24.62 C
ATOM 2813 O ASN A 366 0.311 3.538 58.002 1.00 24.84 O
ATOM 2814 CB ASN A 366 2.458 5.239 59.761 1.00 25.38 C
ATOM 2815 CG ASN A 366 3.524 4.926 60.800 1.00 27.37 C
ATOM 2816 OD1 ASN A 366 3.871 3.763 61.029 1.00 29.88 O
ATOM 2817 ND2 ASN A 366 4.041 5.968 61.448 1.00 29.16 N
ATOM 2818 N LYS A 367 1.124 5.292 56.819 1.00 24.60 N
ATOM 2819 CA LYS A 367 -0.014 5.441 55.905 1.00 24.79 C
ATOM 2820 C LYS A 367 -0.322 4.180 55.093 1.00 23.99 C
ATOM 2821 O LYS A 367 -1.467 3.969 54.683 1.00 24.04 O
ATOM 2822 CB LYS A 367 0.251 6.577 54.911 1.00 24.96 C
ATOM 2823 CG LYS A 367 0.084 7.992 55.441 1.00 26.19 C
ATOM 2824 CD LYS A 367 0.443 8.999 54.345 1.00 26.33 C
ATOM 2825 CE LYS A 367 0.641 10.410 54.894 1.00 28.96 C
ATOM 2826 NZ LYS A 367 -0.649 11.117 55.155 1.00 30.29 N
ATOM 2827 N SER A 368 0.704 3.361 54.854 1.00 23.11 N
ATOM 2828 CA SER A 368 0.603 2.181 53.987 1.00 22.31 C
ATOM 2829 C SER A 368 0.139 0.906 54.694 1.00 22.06 C
ATOM 2830 O SER A 368 0.112 -0.168 54.084 1.00 21.48 O
ATOM 2831 CB SER A 368 1.949 1.918 53.300 1.00 22.15 C
ATOM 2832 OG SER A 368 2.364 3.041 52.547 1.00 21.30 O
ATOM 2833 N THR A 369 -0.218 1.023 55.974 1.00 21.87 N
ATOM 2834 CA THR A 369 -0.638 -0.130 56.771 1.00 21.86 C
ATOM 2835 C THR A 369 -1.839 -0.860 56.153 1.00 21.46 C
ATOM 2836 O THR A 369 -1.819 -2.086 56.026 1.00 21.39 O
ATOM 2837 CB THR A 369 -0.920 0.282 58.242 1.00 22.08 C
ATOM 2838 OG1 THR A 369 0.292 0.770 58.832 1.00 22.63 O
ATOM 2839 CG2 THR A 369 -1.430 -0.899 59.060 1.00 22.83 C
ATOM 2840 N GLN A 370 -2.861 -0.103 55.754 1.00 21.29 N
ATOM 2841 CA GLN A 370 -4.059 -0.682 55.139 1.00 21.42 C
ATOM 2842 C GLN A 370 -3.727 -1.381 53.823 1.00 20.29 C
ATOM 2843 O GLN A 370 -4.161 -2.509 53.588 1.00 20.06 O
ATOM 2844 CB GLN A 370 -5.123 0.387 54.905 1.00 21.60 C
ATOM 2845 CG GLN A 370 -5.875 0.822 56.157 1.00 23.58 C
ATOM 2846 CD GLN A 370 -6.914 1.892 55.865 1.00 23.66 C
ATOM 2847 OE1 GLN A 370 -7.500 1.929 54.778 1.00 27.70 O
ATOM 2848 NE2 GLN A 370 -7.147 2.770 56.835 1.00 27.11 N
ATOM 2849 N ALA A 371 -2.943 -0.706 52.982 1.00 19.35 N
ATOM 2850 CA ALA A 371 -2.522 -1.254 51.689 1.00 18.47 C
ATOM 2851 C ALA A 371 -1.790 -2.581 51.855 1.00 18.03 C
ATOM 2852 O ALA A 371 -2.018 -3.519 51.095 1.00 17.56 O
ATOM 2853 CB ALA A 371 -1.659 -0.259 50.945 1.00 18.45 C
ATOM 2854 N LEU A 372 -0.916 -2.653 52.859 1.00 17.54 N
ATOM 2855 CA LEU A 372 -0.201 -3.885 53.182 1.00 17.45 C
ATOM 2856 C LEU A 372 -1.162 -5.002 53.590 1.00 17.46 C
ATOM 2857 O LEU A 372 -1.015 -6.141 53.140 1.00 17.00 O
ATOM 2858 CB LEU A 372 0.820 -3.640 54.299 1.00 17.47 C
ATOM 2859 CG LEU A 372 1.559 -4.870 54.838 1.00 17.63 C
ATOM 2860 CD1 LEU A 372 2.584 -5.392 53.842 1.00 18.07 C
ATOM 2861 CD2 LEU A 372 2.225 -4.533 56.159 1.00 18.41 C
ATOM 2862 N GLU A 373 -2.124 -4.658 54.448 1.00 17.82 N
ATOM 2863 CA GLU A 373 -3.145 -5.591 54.926 1.00 18.69 C
ATOM 2864 C GLU A 373 -3.987 -6.138 53.773 1.00 17.84 C
ATOM 2865 O GLU A 373 -4.142 -7.350 53.637 1.00 17.70 O
ATOM 2866 CB GLU A 373 -4.053 -4.908 55.958 1.00 18.54 C
ATOM 2867 CG GLU A 373 -5.142 -5.819 56.531 1.00 20.84 C
ATOM 2868 CD GLU A 373 -6.173 -5.082 57.374 1.00 21.27 C
ATOM 2869 OE1 GLU A 373 -7.368 -5.451 57.301 1.00 24.97 O
ATOM 2870 OE2 GLU A 373 -5.800 -4.136 58.107 1.00 26.03 O
ATOM 2871 N TYR A 374 -4.511 -5.236 52.948 1.00 17.74 N
ATOM 2872 CA TYR A 374 -5.379 -5.611 51.823 1.00 17.73 C
ATOM 2873 C TYR A 374 -4.639 -6.441 50.775 1.00 17.35 C
ATOM 2874 O TYR A 374 -5.146 -7.463 50.312 1.00 16.68 O
ATOM 2875 CB TYR A 374 -5.999 -4.374 51.166 1.00 18.28 C
ATOM 2876 CG TYR A 374 -6.885 -3.530 52.064 1.00 19.27 C
ATOM 2877 CD1 TYR A 374 -7.114 -2.184 51.777 1.00 19.88 C
ATOM 2878 CD2 TYR A 374 -7.495 -4.075 53.203 1.00 20.04 C
ATOM 2879 CE1 TYR A 374 -7.935 -1.401 52.593 1.00 20.36 C
ATOM 2880 CE2 TYR A 374 -8.304 -3.300 54.026 1.00 20.24 C
ATOM 2881 CZ TYR A 374 -8.520 -1.971 53.717 1.00 20.29 C
ATOM 2882 OH TYR A 374 -9.328 -1.217 54.542 1.00 21.81 O
ATOM 2883 N CYS A 375 -3.439 -5.993 50.412 1.00 16.79 N
ATOM 2884 CA CYS A 375 -2.607 -6.709 49.448 1.00 16.32 C
ATOM 2885 C CYS A 375 -2.296 -8.121 49.929 1.00 16.34 C
ATOM 2886 O CYS A 375 -2.482 -9.089 49.192 1.00 16.23 O
ATOM 2887 CB CYS A 375 -1.309 -5.943 49.181 1.00 16.28 C
ATOM 2888 SG CYS A 375 -0.186 -6.808 48.067 1.00 16.74 S
ATOM 2889 N ALA A 376 -1.840 -8.234 51.177 1.00 16.35 N
ATOM 2890 CA ALA A 376 -1.499 -9.526 51.754 1.00 16.80 C
ATOM 2891 C ALA A 376 -2.708 -10.454 51.778 1.00 16.88 C
ATOM 2892 O ALA A 376 -2.599 -11.627 51.432 1.00 17.12 O
ATOM 2893 CB ALA A 376 -0.926 -9.354 53.153 1.00 16.58 C
ATOM 2894 N GLU A 377 -3.858 -9.915 52.173 1.00 17.41 N
ATOM 2895 CA GLU A 377 -5.079 -10.707 52.263 1.00 17.91 C
ATOM 2896 C GLU A 377 -5.433 -11.286 50.897 1.00 17.64 C
ATOM 2897 O GLU A 377 -5.646 -12.491 50.760 1.00 17.56 O
ATOM 2898 CB GLU A 377 -6.230 -9.857 52.798 1.00 18.32 C
ATOM 2899 CG GLU A 377 -7.575 -10.582 52.846 1.00 20.66 C
ATOM 2900 CD GLU A 377 -8.761 -9.629 52.784 1.00 24.35 C
ATOM 2901 OE1 GLU A 377 -9.895 -10.117 52.616 1.00 26.47 O
ATOM 2902 OE2 GLU A 377 -8.567 -8.397 52.900 1.00 26.57 O
ATOM 2903 N LEU A 378 -5.455 -10.416 49.891 1.00 17.48 N
ATOM 2904 CA LEU A 378 -5.892 -10.793 48.548 1.00 17.50 C
ATOM 2905 C LEU A 378 -4.925 -11.727 47.828 1.00 17.52 C
ATOM 2906 O LEU A 378 -5.351 -12.553 47.021 1.00 17.56 O
ATOM 2907 CB LEU A 378 -6.194 -9.547 47.710 1.00 17.58 C
ATOM 2908 CG LEU A 378 -7.320 -8.657 48.255 1.00 17.69 C
ATOM 2909 CD1 LEU A 378 -7.498 -7.419 47.397 1.00 19.02 C
ATOM 2910 CD2 LEU A 378 -8.645 -9.420 48.384 1.00 19.03 C
ATOM 2911 N LEU A 379 -3.633 -11.601 48.131 1.00 17.14 N
ATOM 2912 CA LEU A 379 -2.602 -12.422 47.502 1.00 16.95 C
ATOM 2913 C LEU A 379 -2.210 -13.676 48.301 1.00 17.01 C
ATOM 2914 O LEU A 379 -1.333 -14.430 47.879 1.00 17.03 O
ATOM 2915 CB LEU A 379 -1.366 -11.579 47.140 1.00 16.85 C
ATOM 2916 CG LEU A 379 -1.559 -10.419 46.150 1.00 16.52 C
ATOM 2917 CD1 LEU A 379 -0.233 -9.724 45.876 1.00 16.39 C
ATOM 2918 CD2 LEU A 379 -2.210 -10.868 44.829 1.00 17.13 C
ATOM 2919 N GLY A 380 -2.888 -13.909 49.426 1.00 17.35 N
ATOM 2920 CA GLY A 380 -2.656 -15.102 50.251 1.00 17.75 C
ATOM 2921 C GLY A 380 -1.296 -15.102 50.925 1.00 18.07 C
ATOM 2922 O GLY A 380 -0.667 -16.157 51.093 1.00 18.48 O
ATOM 2923 N LEU A 381 -0.845 -13.912 51.306 1.00 18.32 N
ATOM 2924 CA LEU A 381 0.479 -13.730 51.897 1.00 18.74 C
ATOM 2925 C LEU A 381 0.395 -13.279 53.347 1.00 19.09 C
ATOM 2926 O LEU A 381 -0.533 -12.570 53.738 1.00 18.98 O
ATOM 2927 CB LEU A 381 1.286 -12.698 51.100 1.00 18.38 C
ATOM 2928 CG LEU A 381 1.442 -12.862 49.586 1.00 17.83 C
ATOM 2929 CD1 LEU A 381 2.217 -11.668 49.019 1.00 17.64 C
ATOM 2930 CD2 LEU A 381 2.123 -14.181 49.224 1.00 17.43 C
ATOM 2931 N ASP A 382 1.379 -13.699 54.137 1.00 19.97 N
ATOM 2932 CA ASP A 382 1.580 -13.167 55.477 1.00 20.74 C
ATOM 2933 C ASP A 382 2.066 -11.719 55.360 1.00 20.84 C
ATOM 2934 O ASP A 382 3.007 -11.440 54.606 1.00 20.88 O
ATOM 2935 CB ASP A 382 2.617 -14.010 56.227 1.00 21.05 C
ATOM 2936 CG ASP A 382 2.892 -13.491 57.618 1.00 22.40 C
ATOM 2937 OD1 ASP A 382 3.909 -12.788 57.793 1.00 23.96 O
ATOM 2938 OD2 ASP A 382 2.087 -13.773 58.532 1.00 23.76 O
ATOM 2939 N GLN A 383 1.421 -10.815 56.099 1.00 20.89 N
ATOM 2940 CA GLN A 383 1.764 -9.388 56.099 1.00 21.45 C
ATOM 2941 C GLN A 383 3.244 -9.109 56.368 1.00 21.35 C
ATOM 2942 O GLN A 383 3.850 -8.255 55.714 1.00 21.04 O
ATOM 2943 CB GLN A 383 0.925 -8.626 57.128 1.00 21.42 C
ATOM 2944 CG GLN A 383 -0.524 -8.409 56.732 1.00 22.39 C
ATOM 2945 CD GLN A 383 -1.254 -7.471 57.672 1.00 22.65 C
ATOM 2946 OE1 GLN A 383 -2.407 -7.710 58.029 1.00 25.28 O
ATOM 2947 NE2 GLN A 383 -0.587 -6.394 58.077 1.00 25.33 N
ATOM 2948 N ASP A 384 3.813 -9.816 57.343 1.00 21.22 N
ATOM 2949 CA ASP A 384 5.217 -9.622 57.685 1.00 21.09 C
ATOM 2950 C ASP A 384 6.141 -10.152 56.589 1.00 20.51 C
ATOM 2951 O ASP A 384 7.148 -9.515 56.280 1.00 20.11 O
ATOM 2952 CB ASP A 384 5.561 -10.252 59.035 1.00 21.77 C
ATOM 2953 CG ASP A 384 6.941 -9.851 59.527 1.00 23.46 C
ATOM 2954 OD1 ASP A 384 7.148 -8.652 59.820 1.00 26.20 O
ATOM 2955 OD2 ASP A 384 7.818 -10.735 59.617 1.00 26.47 O
ATOM 2956 N ASP A 385 5.793 -11.301 56.006 1.00 19.88 N
ATOM 2957 CA ASP A 385 6.530 -11.858 54.864 1.00 19.77 C
ATOM 2958 C ASP A 385 6.594 -10.854 53.710 1.00 19.20 C
ATOM 2959 O ASP A 385 7.646 -10.664 53.098 1.00 18.67 O
ATOM 2960 CB ASP A 385 5.888 -13.161 54.369 1.00 19.81 C
ATOM 2961 CG ASP A 385 6.230 -14.368 55.234 1.00 21.18 C
ATOM 2962 OD1 ASP A 385 7.102 -14.265 56.128 1.00 21.74 O
ATOM 2963 OD2 ASP A 385 5.624 -15.437 55.001 1.00 21.97 O
ATOM 2964 N LEU A 386 5.463 -10.215 53.420 1.00 18.91 N
ATOM 2965 CA LEU A 386 5.406 -9.203 52.359 1.00 18.65 C
ATOM 2966 C LEU A 386 6.261 -7.979 52.709 1.00 18.56 C
ATOM 2967 O LEU A 386 7.045 -7.509 51.884 1.00 18.17 O
ATOM 2968 CB LEU A 386 3.956 -8.798 52.072 1.00 18.64 C
ATOM 2969 CG LEU A 386 3.694 -7.741 50.990 1.00 18.33 C
ATOM 2970 CD1 LEU A 386 4.286 -8.148 49.640 1.00 16.62 C
ATOM 2971 CD2 LEU A 386 2.210 -7.479 50.864 1.00 18.70 C
ATOM 2972 N ARG A 387 6.109 -7.482 53.934 1.00 18.55 N
ATOM 2973 CA ARG A 387 6.909 -6.363 54.445 1.00 18.98 C
ATOM 2974 C ARG A 387 8.407 -6.625 54.311 1.00 18.42 C
ATOM 2975 O ARG A 387 9.150 -5.784 53.796 1.00 18.20 O
ATOM 2976 CB ARG A 387 6.558 -6.088 55.914 1.00 18.75 C
ATOM 2977 CG ARG A 387 7.341 -4.942 56.547 1.00 20.27 C
ATOM 2978 CD ARG A 387 7.161 -4.909 58.056 1.00 20.68 C
ATOM 2979 NE ARG A 387 5.752 -4.880 58.444 1.00 24.75 N
ATOM 2980 CZ ARG A 387 5.048 -3.770 58.644 1.00 26.19 C
ATOM 2981 NH1 ARG A 387 3.773 -3.856 58.995 1.00 27.79 N
ATOM 2982 NH2 ARG A 387 5.611 -2.575 58.501 1.00 27.68 N
ATOM 2983 N VAL A 388 8.838 -7.795 54.779 1.00 18.21 N
ATOM 2984 CA VAL A 388 10.249 -8.178 54.764 1.00 18.14 C
ATOM 2985 C VAL A 388 10.774 -8.323 53.331 1.00 18.11 C
ATOM 2986 O VAL A 388 11.873 -7.856 53.011 1.00 17.92 O
ATOM 2987 CB VAL A 388 10.475 -9.482 55.579 1.00 18.30 C
ATOM 2988 CG1 VAL A 388 11.836 -10.108 55.282 1.00 18.51 C
ATOM 2989 CG2 VAL A 388 10.310 -9.205 57.074 1.00 18.75 C
ATOM 2990 N SER A 389 9.974 -8.955 52.476 1.00 17.90 N
ATOM 2991 CA SER A 389 10.361 -9.193 51.084 1.00 17.99 C
ATOM 2992 C SER A 389 10.480 -7.899 50.276 1.00 17.60 C
ATOM 2993 O SER A 389 11.232 -7.843 49.299 1.00 17.63 O
ATOM 2994 CB SER A 389 9.373 -10.146 50.413 1.00 18.02 C
ATOM 2995 OG SER A 389 9.428 -11.438 51.003 1.00 19.38 O
ATOM 2996 N LEU A 390 9.737 -6.870 50.680 1.00 17.12 N
ATOM 2997 CA LEU A 390 9.746 -5.581 49.979 1.00 17.07 C
ATOM 2998 C LEU A 390 10.841 -4.626 50.455 1.00 17.14 C
ATOM 2999 O LEU A 390 11.173 -3.669 49.760 1.00 16.84 O
ATOM 3000 CB LEU A 390 8.386 -4.885 50.092 1.00 16.83 C
ATOM 3001 CG LEU A 390 7.191 -5.487 49.345 1.00 16.73 C
ATOM 3002 CD1 LEU A 390 5.951 -4.666 49.642 1.00 16.91 C
ATOM 3003 CD2 LEU A 390 7.453 -5.559 47.842 1.00 17.82 C
ATOM 3004 N THR A 391 11.393 -4.888 51.637 1.00 17.32 N
ATOM 3005 CA THR A 391 12.315 -3.947 52.279 1.00 18.05 C
ATOM 3006 C THR A 391 13.694 -4.540 52.601 1.00 18.72 C
ATOM 3007 O THR A 391 14.580 -3.827 53.087 1.00 18.53 O
ATOM 3008 CB THR A 391 11.708 -3.368 53.581 1.00 17.74 C
ATOM 3009 OG1 THR A 391 11.413 -4.439 54.483 1.00 17.40 O
ATOM 3010 CG2 THR A 391 10.430 -2.580 53.291 1.00 17.94 C
ATOM 3011 N THR A 392 13.864 -5.836 52.344 1.00 19.98 N
ATOM 3012 CA THR A 392 15.133 -6.536 52.588 1.00 21.42 C
ATOM 3013 C THR A 392 15.393 -7.593 51.519 1.00 22.81 C
ATOM 3014 O THR A 392 14.466 -8.038 50.833 1.00 22.91 O
ATOM 3015 CB THR A 392 15.168 -7.266 53.961 1.00 21.35 C
ATOM 3016 OG1 THR A 392 14.359 -8.449 53.903 1.00 21.10 O
ATOM 3017 CG2 THR A 392 14.699 -6.368 55.108 1.00 21.12 C
ATOM 3018 N ARG A 393 16.653 -8.007 51.402 1.00 24.28 N
ATOM 3019 CA ARG A 393 17.036 -9.093 50.501 1.00 26.04 C
ATOM 3020 C ARG A 393 18.245 -9.864 51.030 1.00 26.89 C
ATOM 3021 O ARG A 393 19.246 -9.266 51.412 1.00 27.13 O
ATOM 3022 CB ARG A 393 17.325 -8.551 49.099 1.00 26.06 C
ATOM 3023 CG ARG A 393 17.597 -9.636 48.062 1.00 27.51 C
ATOM 3024 CD ARG A 393 17.379 -9.135 46.645 1.00 29.01 C
ATOM 3025 NE ARG A 393 15.981 -8.783 46.398 1.00 30.79 N
ATOM 3026 CZ ARG A 393 15.555 -7.567 46.063 1.00 31.95 C
ATOM 3027 NH1 ARG A 393 16.417 -6.564 45.915 1.00 33.36 N
ATOM 3028 NH2 ARG A 393 14.264 -7.355 45.862 1.00 31.46 N
ATOM 3029 N VAL A 394 18.134 -11.190 51.059 1.00 28.22 N
ATOM 3030 CA VAL A 394 19.270 -12.055 51.376 1.00 29.41 C
ATOM 3031 C VAL A 394 20.181 -12.091 50.149 1.00 30.17 C
ATOM 3032 O VAL A 394 19.739 -12.442 49.052 1.00 30.35 O
ATOM 3033 CB VAL A 394 18.820 -13.486 51.784 1.00 29.40 C
ATOM 3034 CG1 VAL A 394 20.026 -14.389 52.049 1.00 29.67 C
ATOM 3035 CG2 VAL A 394 17.920 -13.437 53.014 1.00 29.54 C
ATOM 3036 N MET A 395 21.441 -11.700 50.332 1.00 30.94 N
ATOM 3037 CA MET A 395 22.391 -11.614 49.220 1.00 31.99 C
ATOM 3038 C MET A 395 23.822 -11.971 49.635 1.00 31.95 C
ATOM 3039 O MET A 395 24.269 -11.633 50.734 1.00 32.21 O
ATOM 3040 CB MET A 395 22.332 -10.225 48.565 1.00 31.96 C
ATOM 3041 CG MET A 395 23.010 -9.109 49.354 1.00 32.43 C
ATOM 3042 SD MET A 395 22.553 -7.436 48.859 1.00 33.65 S
ATOM 3043 CE MET A 395 22.926 -7.456 47.100 1.00 34.43 C
ATOM 3044 N ILE A 407 23.895 -12.810 53.540 1.00 27.99 N
ATOM 3045 CA ILE A 407 23.373 -11.877 54.539 1.00 27.98 C
ATOM 3046 C ILE A 407 22.061 -11.222 54.091 1.00 27.44 C
ATOM 3047 O ILE A 407 21.914 -10.837 52.930 1.00 27.77 O
ATOM 3048 CB ILE A 407 24.426 -10.787 54.919 1.00 27.96 C
ATOM 3049 CG1 ILE A 407 23.930 -9.947 56.102 1.00 28.17 C
ATOM 3050 CG2 ILE A 407 24.797 -9.921 53.700 1.00 28.71 C
ATOM 3051 CD1 ILE A 407 24.927 -8.924 56.613 1.00 28.37 C
ATOM 3052 N LYS A 408 21.118 -11.113 55.026 1.00 27.04 N
ATOM 3053 CA LYS A 408 19.889 -10.349 54.826 1.00 26.45 C
ATOM 3054 C LYS A 408 20.183 -8.854 54.992 1.00 25.89 C
ATOM 3055 O LYS A 408 20.426 -8.376 56.108 1.00 25.70 O
ATOM 3056 CB LYS A 408 18.816 -10.816 55.814 1.00 26.48 C
ATOM 3057 CG LYS A 408 17.471 -10.116 55.702 1.00 26.66 C
ATOM 3058 CD LYS A 408 16.497 -10.701 56.719 1.00 27.01 C
ATOM 3059 CE LYS A 408 15.348 -9.757 57.014 1.00 27.69 C
ATOM 3060 NZ LYS A 408 14.484 -10.289 58.108 1.00 28.53 N
ATOM 3061 N VAL A 409 20.162 -8.137 53.869 1.00 25.22 N
ATOM 3062 CA VAL A 409 20.521 -6.715 53.804 1.00 24.77 C
ATOM 3063 C VAL A 409 19.275 -5.841 53.628 1.00 24.27 C
ATOM 3064 O VAL A 409 18.360 -6.217 52.891 1.00 24.23 O
ATOM 3065 CB VAL A 409 21.527 -6.444 52.639 1.00 24.82 C
ATOM 3066 CG1 VAL A 409 20.864 -6.624 51.288 1.00 25.13 C
ATOM 3067 CG2 VAL A 409 22.127 -5.051 52.730 1.00 25.30 C
ATOM 3068 N PRO A 410 19.227 -4.678 54.312 1.00 23.82 N
ATOM 3069 CA PRO A 410 18.123 -3.747 54.088 1.00 23.38 C
ATOM 3070 C PRO A 410 18.201 -3.090 52.716 1.00 22.91 C
ATOM 3071 O PRO A 410 19.295 -2.774 52.237 1.00 22.92 O
ATOM 3072 CB PRO A 410 18.327 -2.688 55.178 1.00 23.24 C
ATOM 3073 CG PRO A 410 19.252 -3.316 56.173 1.00 23.59 C
ATOM 3074 CD PRO A 410 20.148 -4.170 55.343 1.00 23.80 C
ATOM 3075 N LEU A 411 17.045 -2.893 52.091 1.00 22.31 N
ATOM 3076 CA LEU A 411 16.977 -2.184 50.818 1.00 21.80 C
ATOM 3077 C LEU A 411 16.756 -0.693 51.040 1.00 21.70 C
ATOM 3078 O LEU A 411 16.130 -0.289 52.021 1.00 21.43 O
ATOM 3079 CB LEU A 411 15.851 -2.749 49.941 1.00 21.60 C
ATOM 3080 CG LEU A 411 15.969 -4.209 49.480 1.00 21.40 C
ATOM 3081 CD1 LEU A 411 14.691 -4.654 48.770 1.00 21.23 C
ATOM 3082 CD2 LEU A 411 17.195 -4.421 48.589 1.00 21.85 C
ATOM 3083 N LYS A 412 17.275 0.116 50.120 1.00 21.73 N
ATOM 3084 CA LYS A 412 17.007 1.547 50.100 1.00 22.02 C
ATOM 3085 C LYS A 412 15.594 1.778 49.557 1.00 21.70 C
ATOM 3086 O LYS A 412 15.011 0.881 48.940 1.00 21.39 O
ATOM 3087 CB LYS A 412 18.035 2.275 49.221 1.00 22.42 C
ATOM 3088 CG LYS A 412 19.514 1.941 49.489 1.00 24.20 C
ATOM 3089 CD LYS A 412 19.965 2.329 50.896 1.00 26.41 C
ATOM 3090 CE LYS A 412 20.217 1.097 51.767 1.00 28.09 C
ATOM 3091 NZ LYS A 412 21.538 0.445 51.490 1.00 28.37 N
ATOM 3092 N VAL A 413 15.054 2.973 49.785 1.00 21.78 N
ATOM 3093 CA VAL A 413 13.703 3.329 49.325 1.00 21.80 C
ATOM 3094 C VAL A 413 13.494 3.018 47.836 1.00 22.04 C
ATOM 3095 O VAL A 413 12.474 2.430 47.462 1.00 21.69 O
ATOM 3096 CB VAL A 413 13.358 4.818 49.628 1.00 21.82 C
ATOM 3097 CG1 VAL A 413 12.071 5.246 48.925 1.00 21.98 C
ATOM 3098 CG2 VAL A 413 13.233 5.048 51.130 1.00 21.95 C
ATOM 3099 N GLU A 414 14.459 3.398 46.997 1.00 22.25 N
ATOM 3100 CA GLU A 414 14.349 3.168 45.550 1.00 22.85 C
ATOM 3101 C GLU A 414 14.297 1.681 45.197 1.00 22.03 C
ATOM 3102 O GLU A 414 13.548 1.277 44.301 1.00 22.14 O
ATOM 3103 CB GLU A 414 15.482 3.863 44.786 1.00 22.90 C
ATOM 3104 CG GLU A 414 15.354 5.383 44.731 1.00 24.63 C
ATOM 3105 CD GLU A 414 16.337 6.028 43.763 1.00 25.05 C
ATOM 3106 OE1 GLU A 414 16.134 5.901 42.534 1.00 29.17 O
ATOM 3107 OE2 GLU A 414 17.304 6.676 44.231 1.00 28.31 O
ATOM 3108 N GLN A 415 15.080 0.875 45.910 1.00 21.24 N
ATOM 3109 CA GLN A 415 15.112 -0.571 45.693 1.00 20.85 C
ATOM 3110 C GLN A 415 13.802 -1.210 46.155 1.00 19.99 C
ATOM 3111 O GLN A 415 13.337 -2.189 45.565 1.00 19.78 O
ATOM 3112 CB GLN A 415 16.301 -1.209 46.417 1.00 20.91 C
ATOM 3113 CG GLN A 415 17.667 -0.818 45.853 1.00 21.73 C
ATOM 3114 CD GLN A 415 18.824 -1.446 46.615 1.00 22.05 C
ATOM 3115 OE1 GLN A 415 19.687 -2.096 46.025 1.00 25.39 O
ATOM 3116 NE2 GLN A 415 18.845 -1.256 47.929 1.00 21.50 N
ATOM 3117 N ALA A 416 13.217 -0.647 47.213 1.00 19.06 N
ATOM 3118 CA ALA A 416 11.926 -1.107 47.722 1.00 18.40 C
ATOM 3119 C ALA A 416 10.823 -0.810 46.707 1.00 18.07 C
ATOM 3120 O ALA A 416 9.987 -1.675 46.416 1.00 17.66 O
ATOM 3121 CB ALA A 416 11.617 -0.458 49.053 1.00 18.14 C
ATOM 3122 N ASN A 417 10.832 0.410 46.171 1.00 18.04 N
ATOM 3123 CA ASN A 417 9.946 0.779 45.065 1.00 18.26 C
ATOM 3124 C ASN A 417 10.066 -0.206 43.907 1.00 18.07 C
ATOM 3125 O ASN A 417 9.056 -0.648 43.354 1.00 17.51 O
ATOM 3126 CB ASN A 417 10.245 2.199 44.568 1.00 18.68 C
ATOM 3127 CG ASN A 417 9.775 3.280 45.531 1.00 19.71 C
ATOM 3128 OD1 ASN A 417 8.863 3.074 46.333 1.00 20.60 O
ATOM 3129 ND2 ASN A 417 10.397 4.454 45.441 1.00 21.27 N
ATOM 3130 N ASN A 418 11.305 -0.552 43.551 1.00 17.99 N
ATOM 3131 CA ASN A 418 11.561 -1.496 42.462 1.00 17.81 C
ATOM 3132 C ASN A 418 11.069 -2.905 42.760 1.00 17.38 C
ATOM 3133 O ASN A 418 10.538 -3.573 41.877 1.00 17.26 O
ATOM 3134 CB ASN A 418 13.046 -1.508 42.081 1.00 18.35 C
ATOM 3135 CG ASN A 418 13.479 -0.231 41.384 1.00 19.46 C
ATOM 3136 OD1 ASN A 418 12.653 0.523 40.870 1.00 21.84 O
ATOM 3137 ND2 ASN A 418 14.787 0.012 41.354 1.00 21.77 N
ATOM 3138 N ALA A 419 11.240 -3.344 44.007 1.00 16.47 N
ATOM 3139 CA ALA A 419 10.767 -4.653 44.443 1.00 15.98 C
ATOM 3140 C ALA A 419 9.246 -4.744 44.338 1.00 15.47 C
ATOM 3141 O ALA A 419 8.707 -5.718 43.790 1.00 15.45 O
ATOM 3142 CB ALA A 419 11.225 -4.929 45.876 1.00 16.05 C
ATOM 3143 N ARG A 420 8.572 -3.718 44.857 1.00 15.07 N
ATOM 3144 CA ARG A 420 7.115 -3.607 44.806 1.00 14.63 C
ATOM 3145 C ARG A 420 6.634 -3.699 43.361 1.00 14.54 C
ATOM 3146 O ARG A 420 5.802 -4.547 43.031 1.00 14.49 O
ATOM 3147 CB ARG A 420 6.673 -2.290 45.448 1.00 14.54 C
ATOM 3148 CG ARG A 420 5.163 -2.004 45.424 1.00 14.46 C
ATOM 3149 CD ARG A 420 4.890 -0.524 45.664 1.00 15.43 C
ATOM 3150 NE ARG A 420 5.457 0.307 44.602 1.00 16.42 N
ATOM 3151 CZ ARG A 420 5.860 1.563 44.753 1.00 17.41 C
ATOM 3152 NH1 ARG A 420 6.370 2.214 43.716 1.00 18.52 N
ATOM 3153 NH2 ARG A 420 5.772 2.172 45.935 1.00 17.45 N
ATOM 3154 N ASP A 421 7.189 -2.846 42.504 1.00 14.27 N
ATOM 3155 CA ASP A 421 6.774 -2.781 41.098 1.00 14.29 C
ATOM 3156 C ASP A 421 7.098 -4.060 40.321 1.00 13.95 C
ATOM 3157 O ASP A 421 6.299 -4.498 39.491 1.00 13.76 O
ATOM 3158 CB ASP A 421 7.386 -1.556 40.409 1.00 14.59 C
ATOM 3159 CG ASP A 421 6.839 -0.233 40.947 1.00 15.47 C
ATOM 3160 OD1 ASP A 421 5.838 -0.225 41.697 1.00 16.58 O
ATOM 3161 OD2 ASP A 421 7.411 0.818 40.602 1.00 16.40 O
ATOM 3162 N ALA A 422 8.260 -4.659 40.596 1.00 13.62 N
ATOM 3163 CA ALA A 422 8.659 -5.913 39.951 1.00 13.44 C
ATOM 3164 C ALA A 422 7.703 -7.043 40.312 1.00 13.58 C
ATOM 3165 O ALA A 422 7.326 -7.836 39.452 1.00 13.49 O
ATOM 3166 CB ALA A 422 10.105 -6.288 40.314 1.00 13.64 C
ATOM 3167 N LEU A 423 7.309 -7.106 41.585 1.00 13.18 N
ATOM 3168 CA LEU A 423 6.319 -8.085 42.032 1.00 13.23 C
ATOM 3169 C LEU A 423 4.965 -7.845 41.348 1.00 13.11 C
ATOM 3170 O LEU A 423 4.340 -8.789 40.847 1.00 13.18 O
ATOM 3171 CB LEU A 423 6.180 -8.067 43.560 1.00 13.40 C
ATOM 3172 CG LEU A 423 5.188 -9.050 44.204 1.00 13.55 C
ATOM 3173 CD1 LEU A 423 5.549 -10.510 43.914 1.00 13.86 C
ATOM 3174 CD2 LEU A 423 5.088 -8.800 45.708 1.00 13.60 C
ATOM 3175 N ALA A 424 4.542 -6.586 41.300 1.00 12.89 N
ATOM 3176 CA ALA A 424 3.277 -6.216 40.657 1.00 12.65 C
ATOM 3177 C ALA A 424 3.239 -6.655 39.195 1.00 12.86 C
ATOM 3178 O ALA A 424 2.264 -7.266 38.747 1.00 12.51 O
ATOM 3179 CB ALA A 424 3.045 -4.727 40.772 1.00 12.78 C
ATOM 3180 N LYS A 425 4.309 -6.349 38.465 1.00 12.91 N
ATOM 3181 CA LYS A 425 4.405 -6.696 37.048 1.00 13.27 C
ATOM 3182 C LYS A 425 4.390 -8.202 36.816 1.00 13.32 C
ATOM 3183 O LYS A 425 3.692 -8.679 35.928 1.00 13.85 O
ATOM 3184 CB LYS A 425 5.648 -6.063 36.421 1.00 13.09 C
ATOM 3185 CG LYS A 425 5.552 -4.567 36.241 1.00 13.80 C
ATOM 3186 CD LYS A 425 6.900 -4.016 35.819 1.00 15.90 C
ATOM 3187 CE LYS A 425 6.928 -2.505 35.879 1.00 17.43 C
ATOM 3188 NZ LYS A 425 8.249 -2.014 35.386 1.00 19.82 N
ATOM 3189 N THR A 426 5.132 -8.949 37.631 1.00 13.40 N
ATOM 3190 CA THR A 426 5.177 -10.405 37.503 1.00 13.69 C
ATOM 3191 C THR A 426 3.823 -11.041 37.868 1.00 12.87 C
ATOM 3192 O THR A 426 3.375 -11.970 37.201 1.00 12.86 O
ATOM 3193 CB THR A 426 6.355 -11.025 38.299 1.00 14.00 C
ATOM 3194 OG1 THR A 426 7.581 -10.384 37.907 1.00 17.29 O
ATOM 3195 CG2 THR A 426 6.478 -12.514 38.019 1.00 13.76 C
ATOM 3196 N VAL A 427 3.162 -10.527 38.902 1.00 12.38 N
ATOM 3197 CA VAL A 427 1.841 -11.045 39.277 1.00 11.63 C
ATOM 3198 C VAL A 427 0.838 -10.826 38.135 1.00 11.31 C
ATOM 3199 O VAL A 427 0.186 -11.774 37.679 1.00 10.70 O
ATOM 3200 CB VAL A 427 1.328 -10.443 40.610 1.00 12.03 C
ATOM 3201 CG1 VAL A 427 -0.144 -10.793 40.831 1.00 11.66 C
ATOM 3202 CG2 VAL A 427 2.168 -10.964 41.788 1.00 11.86 C
ATOM 3203 N TYR A 428 0.748 -9.588 37.655 1.00 10.91 N
ATOM 3204 CA TYR A 428 -0.203 -9.272 36.585 1.00 11.03 C
ATOM 3205 C TYR A 428 0.110 -10.055 35.298 1.00 11.44 C
ATOM 3206 O TYR A 428 -0.797 -10.594 34.655 1.00 11.23 O
ATOM 3207 CB TYR A 428 -0.262 -7.766 36.309 1.00 10.99 C
ATOM 3208 CG TYR A 428 -1.401 -7.421 35.373 1.00 10.61 C
ATOM 3209 CD1 TYR A 428 -2.680 -7.181 35.868 1.00 10.48 C
ATOM 3210 CD2 TYR A 428 -1.208 -7.394 33.987 1.00 10.98 C
ATOM 3211 CE1 TYR A 428 -3.735 -6.892 35.013 1.00 10.11 C
ATOM 3212 CE2 TYR A 428 -2.259 -7.107 33.120 1.00 9.88 C
ATOM 3213 CZ TYR A 428 -3.521 -6.859 33.645 1.00 11.16 C
ATOM 3214 OH TYR A 428 -4.578 -6.570 32.811 1.00 10.88 O
ATOM 3215 N SER A 429 1.391 -10.128 34.941 1.00 11.87 N
ATOM 3216 CA SER A 429 1.809 -10.850 33.737 1.00 12.58 C
ATOM 3217 C SER A 429 1.448 -12.330 33.793 1.00 12.70 C
ATOM 3218 O SER A 429 0.950 -12.899 32.814 1.00 12.82 O
ATOM 3219 CB SER A 429 3.307 -10.673 33.473 1.00 12.68 C
ATOM 3220 OG SER A 429 3.638 -11.202 32.195 1.00 14.64 O
ATOM 3221 N HIS A 430 1.693 -12.959 34.940 1.00 13.08 N
ATOM 3222 CA HIS A 430 1.291 -14.354 35.124 1.00 13.18 C
ATOM 3223 C HIS A 430 -0.235 -14.529 35.147 1.00 12.80 C
ATOM 3224 O HIS A 430 -0.752 -15.568 34.726 1.00 12.68 O
ATOM 3225 CB HIS A 430 1.953 -14.953 36.368 1.00 13.69 C
ATOM 3226 CG HIS A 430 3.397 -15.287 36.165 1.00 16.02 C
ATOM 3227 ND1 HIS A 430 3.837 -16.566 35.897 1.00 18.63 N
ATOM 3228 CD2 HIS A 430 4.498 -14.501 36.151 1.00 17.49 C
ATOM 3229 CE1 HIS A 430 5.151 -16.556 35.754 1.00 19.28 C
ATOM 3230 NE2 HIS A 430 5.577 -15.314 35.901 1.00 19.14 N
ATOM 3231 N LEU A 431 -0.946 -13.507 35.624 1.00 12.23 N
ATOM 3232 CA LEU A 431 -2.408 -13.501 35.564 1.00 11.81 C
ATOM 3233 C LEU A 431 -2.878 -13.480 34.111 1.00 11.41 C
ATOM 3234 O LEU A 431 -3.797 -14.215 33.742 1.00 11.40 O
ATOM 3235 CB LEU A 431 -2.991 -12.306 36.327 1.00 11.84 C
ATOM 3236 CG LEU A 431 -4.519 -12.209 36.448 1.00 12.11 C
ATOM 3237 CD1 LEU A 431 -5.092 -13.372 37.238 1.00 13.64 C
ATOM 3238 CD2 LEU A 431 -4.892 -10.894 37.098 1.00 11.78 C
ATOM 3239 N PHE A 432 -2.242 -12.641 33.297 1.00 10.99 N
ATOM 3240 CA PHE A 432 -2.549 -12.584 31.865 1.00 11.02 C
ATOM 3241 C PHE A 432 -2.267 -13.934 31.189 1.00 11.01 C
ATOM 3242 O PHE A 432 -3.088 -14.434 30.418 1.00 10.58 O
ATOM 3243 CB PHE A 432 -1.781 -11.446 31.181 1.00 10.98 C
ATOM 3244 CG PHE A 432 -2.185 -11.222 29.740 1.00 11.11 C
ATOM 3245 CD1 PHE A 432 -1.260 -11.378 28.716 1.00 11.28 C
ATOM 3246 CD2 PHE A 432 -3.497 -10.880 29.418 1.00 12.78 C
ATOM 3247 CE1 PHE A 432 -1.630 -11.178 27.379 1.00 12.17 C
ATOM 3248 CE2 PHE A 432 -3.887 -10.682 28.075 1.00 12.28 C
ATOM 3249 CZ PHE A 432 -2.947 -10.829 27.060 1.00 11.94 C
ATOM 3250 N ASP A 433 -1.113 -14.528 31.499 1.00 11.33 N
ATOM 3251 CA ASP A 433 -0.788 -15.870 31.011 1.00 11.76 C
ATOM 3252 C ASP A 433 -1.901 -16.858 31.359 1.00 12.05 C
ATOM 3253 O ASP A 433 -2.295 -17.680 30.525 1.00 12.10 O
ATOM 3254 CB ASP A 433 0.530 -16.372 31.606 1.00 12.24 C
ATOM 3255 CG ASP A 433 1.739 -15.589 31.134 1.00 13.01 C
ATOM 3256 OD1 ASP A 433 1.645 -14.844 30.135 1.00 14.98 O
ATOM 3257 OD2 ASP A 433 2.802 -15.726 31.777 1.00 14.84 O
ATOM 3258 N HIS A 434 -2.402 -16.780 32.594 1.00 12.24 N
ATOM 3259 CA HIS A 434 -3.484 -17.657 33.033 1.00 12.37 C
ATOM 3260 C HIS A 434 -4.759 -17.419 32.231 1.00 12.02 C
ATOM 3261 O HIS A 434 -5.430 -18.369 31.845 1.00 11.80 O
ATOM 3262 CB HIS A 434 -3.802 -17.471 34.518 1.00 12.72 C
ATOM 3263 CG HIS A 434 -4.992 -18.259 34.968 1.00 14.20 C
ATOM 3264 ND1 HIS A 434 -6.246 -17.704 35.106 1.00 16.85 N
ATOM 3265 CD2 HIS A 434 -5.129 -19.573 35.264 1.00 15.97 C
ATOM 3266 CE1 HIS A 434 -7.100 -18.636 35.488 1.00 15.97 C
ATOM 3267 NE2 HIS A 434 -6.446 -19.778 35.598 1.00 16.82 N
ATOM 3268 N VAL A 435 -5.092 -16.147 32.013 1.00 11.71 N
ATOM 3269 CA VAL A 435 -6.289 -15.786 31.253 1.00 11.53 C
ATOM 3270 C VAL A 435 -6.238 -16.389 29.842 1.00 11.71 C
ATOM 3271 O VAL A 435 -7.217 -16.986 29.388 1.00 11.11 O
ATOM 3272 CB VAL A 435 -6.510 -14.249 31.232 1.00 11.55 C
ATOM 3273 CG1 VAL A 435 -7.573 -13.857 30.207 1.00 11.90 C
ATOM 3274 CG2 VAL A 435 -6.908 -13.760 32.616 1.00 11.39 C
ATOM 3275 N VAL A 436 -5.091 -16.268 29.173 1.00 11.70 N
ATOM 3276 CA VAL A 436 -4.952 -16.804 27.811 1.00 12.11 C
ATOM 3277 C VAL A 436 -5.043 -18.331 27.826 1.00 12.58 C
ATOM 3278 O VAL A 436 -5.717 -18.924 26.988 1.00 13.14 O
ATOM 3279 CB VAL A 436 -3.658 -16.333 27.109 1.00 12.05 C
ATOM 3280 CG1 VAL A 436 -3.613 -16.852 25.663 1.00 11.63 C
ATOM 3281 CG2 VAL A 436 -3.577 -14.809 27.104 1.00 11.64 C
ATOM 3282 N ASN A 437 -4.362 -18.959 28.782 1.00 13.40 N
ATOM 3283 CA ASN A 437 -4.462 -20.407 28.972 1.00 14.34 C
ATOM 3284 C ASN A 437 -5.899 -20.848 29.252 1.00 14.53 C
ATOM 3285 O ASN A 437 -6.367 -21.844 28.690 1.00 14.89 O
ATOM 3286 CB ASN A 437 -3.533 -20.872 30.101 1.00 14.66 C
ATOM 3287 CG ASN A 437 -3.477 -22.391 30.231 1.00 15.73 C
ATOM 3288 OD1 ASN A 437 -3.676 -22.937 31.321 1.00 18.59 O
ATOM 3289 ND2 ASN A 437 -3.215 -23.077 29.125 1.00 14.83 N
ATOM 3290 N ARG A 438 -6.594 -20.107 30.114 1.00 14.70 N
ATOM 3291 CA ARG A 438 -7.981 -20.430 30.465 1.00 14.97 C
ATOM 3292 C ARG A 438 -8.890 -20.342 29.238 1.00 15.17 C
ATOM 3293 O ARG A 438 -9.773 -21.179 29.048 1.00 15.51 O
ATOM 3294 CB ARG A 438 -8.491 -19.525 31.592 1.00 14.86 C
ATOM 3295 CG ARG A 438 -9.901 -19.849 32.083 1.00 14.84 C
ATOM 3296 CD ARG A 438 -10.015 -21.290 32.572 1.00 15.30 C
ATOM 3297 NE ARG A 438 -11.380 -21.640 32.963 1.00 15.81 N
ATOM 3298 CZ ARG A 438 -12.294 -22.153 32.143 1.00 15.98 C
ATOM 3299 NH1 ARG A 438 -13.501 -22.451 32.601 1.00 15.49 N
ATOM 3300 NH2 ARG A 438 -12.008 -22.371 30.866 1.00 16.07 N
ATOM 3301 N VAL A 439 -8.646 -19.338 28.401 1.00 15.46 N
ATOM 3302 CA VAL A 439 -9.372 -19.176 27.142 1.00 15.50 C
ATOM 3303 C VAL A 439 -9.152 -20.392 26.232 1.00 15.70 C
ATOM 3304 O VAL A 439 -10.115 -20.972 25.731 1.00 15.59 O
ATOM 3305 CB VAL A 439 -9.016 -17.819 26.460 1.00 15.74 C
ATOM 3306 CG1 VAL A 439 -9.367 -17.814 24.984 1.00 15.66 C
ATOM 3307 CG2 VAL A 439 -9.733 -16.679 27.173 1.00 16.07 C
ATOM 3308 N ASN A 440 -7.896 -20.803 26.062 1.00 15.66 N
ATOM 3309 CA ASN A 440 -7.563 -21.992 25.278 1.00 15.93 C
ATOM 3310 C ASN A 440 -8.246 -23.249 25.807 1.00 16.21 C
ATOM 3311 O ASN A 440 -8.606 -24.136 25.037 1.00 16.39 O
ATOM 3312 CB ASN A 440 -6.050 -22.193 25.204 1.00 15.90 C
ATOM 3313 CG ASN A 440 -5.367 -21.140 24.339 1.00 15.92 C
ATOM 3314 OD1 ASN A 440 -5.970 -20.597 23.406 1.00 14.35 O
ATOM 3315 ND2 ASN A 440 -4.112 -20.849 24.647 1.00 15.25 N
ATOM 3316 N GLN A 441 -8.449 -23.299 27.121 1.00 16.59 N
ATOM 3317 CA GLN A 441 -9.137 -24.429 27.745 1.00 16.85 C
ATOM 3318 C GLN A 441 -10.637 -24.475 27.459 1.00 17.19 C
ATOM 3319 O GLN A 441 -11.273 -25.493 27.744 1.00 17.54 O
ATOM 3320 CB GLN A 441 -8.891 -24.453 29.257 1.00 16.88 C
ATOM 3321 CG GLN A 441 -7.468 -24.832 29.641 1.00 16.73 C
ATOM 3322 CD GLN A 441 -7.215 -24.722 31.130 1.00 17.50 C
ATOM 3323 OE1 GLN A 441 -7.804 -23.885 31.818 1.00 16.87 O
ATOM 3324 NE2 GLN A 441 -6.326 -25.569 31.638 1.00 18.83 N
ATOM 3325 N CYS A 442 -11.201 -23.394 26.904 1.00 17.28 N
ATOM 3326 C CYS A 442 -12.911 -23.967 25.197 1.00 17.78 C
ATOM 3327 O CYS A 442 -14.036 -24.377 24.914 1.00 17.96 O
ATOM 3328 CA ACYS A 442 -12.625 -23.324 26.547 0.70 17.71 C
ATOM 3329 CB ACYS A 442 -13.102 -21.870 26.502 0.70 17.67 C
ATOM 3330 SG ACYS A 442 -13.002 -20.991 28.061 0.70 18.42 S
ATOM 3332 CB BCYS A 442 -13.273 -22.028 26.811 0.30 17.58 C
ATOM 3333 SG BCYS A 442 -12.992 -20.813 25.524 0.30 17.50 S
ATOM 3334 N PHE A 443 -11.887 -24.019 24.349 1.00 17.92 N
ATOM 3335 CA PHE A 443 -12.025 -24.637 23.028 1.00 18.29 C
ATOM 3336 C PHE A 443 -10.890 -25.617 22.674 1.00 18.85 C
ATOM 3337 O PHE A 443 -10.268 -25.501 21.610 1.00 18.84 O
ATOM 3338 CB PHE A 443 -12.254 -23.578 21.929 1.00 17.92 C
ATOM 3339 CG PHE A 443 -11.438 -22.323 22.093 1.00 17.48 C
ATOM 3340 CD1 PHE A 443 -10.057 -22.341 21.915 1.00 17.49 C
ATOM 3341 CD2 PHE A 443 -12.054 -21.111 22.398 1.00 18.11 C
ATOM 3342 CE1 PHE A 443 -9.296 -21.182 22.051 1.00 16.33 C
ATOM 3343 CE2 PHE A 443 -11.296 -19.941 22.538 1.00 17.64 C
ATOM 3344 CZ PHE A 443 -9.920 -19.980 22.357 1.00 16.89 C
ATOM 3345 N PRO A 444 -10.648 -26.617 23.549 1.00 19.41 N
ATOM 3346 CA PRO A 444 -9.541 -27.537 23.334 1.00 19.99 C
ATOM 3347 C PRO A 444 -9.871 -28.603 22.291 1.00 20.58 C
ATOM 3348 O PRO A 444 -11.043 -28.907 22.052 1.00 20.64 O
ATOM 3349 CB PRO A 444 -9.358 -28.184 24.710 1.00 19.90 C
ATOM 3350 CG PRO A 444 -10.712 -28.181 25.303 1.00 19.43 C
ATOM 3351 CD PRO A 444 -11.417 -26.962 24.761 1.00 19.57 C
ATOM 3352 N PHE A 445 -8.831 -29.159 21.682 1.00 21.32 N
ATOM 3353 CA PHE A 445 -8.986 -30.221 20.692 1.00 22.27 C
ATOM 3354 C PHE A 445 -7.859 -31.231 20.847 1.00 22.80 C
ATOM 3355 O PHE A 445 -6.725 -30.863 21.156 1.00 23.25 O
ATOM 3356 CB PHE A 445 -9.023 -29.644 19.266 1.00 21.91 C
ATOM 3357 CG PHE A 445 -7.797 -28.851 18.895 1.00 22.08 C
ATOM 3358 CD1 PHE A 445 -6.750 -29.449 18.197 1.00 21.50 C
ATOM 3359 CD2 PHE A 445 -7.690 -27.504 19.239 1.00 21.54 C
ATOM 3360 CE1 PHE A 445 -5.611 -28.726 17.855 1.00 22.42 C
ATOM 3361 CE2 PHE A 445 -6.555 -26.768 18.898 1.00 21.72 C
ATOM 3362 CZ PHE A 445 -5.512 -27.381 18.209 1.00 21.99 C
ATOM 3363 N GLU A 446 -8.168 -32.505 20.639 1.00 23.78 N
ATOM 3364 CA GLU A 446 -7.149 -33.542 20.746 1.00 24.76 C
ATOM 3365 C GLU A 446 -6.259 -33.573 19.504 1.00 24.49 C
ATOM 3366 O GLU A 446 -5.036 -33.674 19.612 1.00 24.78 O
ATOM 3367 CB GLU A 446 -7.785 -34.910 20.990 1.00 24.74 C
ATOM 3368 CG GLU A 446 -6.768 -36.018 21.202 1.00 26.20 C
ATOM 3369 CD GLU A 446 -7.399 -37.371 21.457 1.00 26.56 C
ATOM 3370 OE1 GLU A 446 -6.660 -38.290 21.873 1.00 29.85 O
ATOM 3371 OE2 GLU A 446 -8.622 -37.523 21.242 1.00 29.82 O
ATOM 3372 N THR A 447 -6.874 -33.479 18.329 1.00 24.33 N
ATOM 3373 CA THR A 447 -6.123 -33.536 17.077 1.00 24.00 C
ATOM 3374 C THR A 447 -6.746 -32.649 16.001 1.00 23.36 C
ATOM 3375 O THR A 447 -7.920 -32.285 16.088 1.00 23.33 O
ATOM 3376 CB THR A 447 -5.975 -35.001 16.563 1.00 24.17 C
ATOM 3377 OG1 THR A 447 -5.026 -35.047 15.490 1.00 25.64 O
ATOM 3378 CG2 THR A 447 -7.310 -35.563 16.088 1.00 24.49 C
ATOM 3379 N SER A 448 -5.946 -32.311 14.992 1.00 22.77 N
ATOM 3380 CA SER A 448 -6.404 -31.508 13.862 1.00 22.20 C
ATOM 3381 C SER A 448 -5.583 -31.812 12.613 1.00 21.98 C
ATOM 3382 O SER A 448 -4.450 -32.299 12.708 1.00 22.20 O
ATOM 3383 CB SER A 448 -6.299 -30.017 14.192 1.00 22.01 C
ATOM 3384 OG SER A 448 -4.946 -29.642 14.397 1.00 21.36 O
ATOM 3385 N SER A 449 -6.159 -31.503 11.453 1.00 21.43 N
ATOM 3386 CA SER A 449 -5.496 -31.697 10.168 1.00 21.09 C
ATOM 3387 C SER A 449 -4.735 -30.441 9.731 1.00 20.67 C
ATOM 3388 O SER A 449 -3.574 -30.518 9.319 1.00 20.31 O
ATOM 3389 CB SER A 449 -6.513 -32.105 9.097 1.00 21.42 C
ATOM 3390 OG SER A 449 -7.241 -33.262 9.487 1.00 22.53 O
ATOM 3391 N TYR A 450 -5.401 -29.290 9.824 1.00 19.95 N
ATOM 3392 CA TYR A 450 -4.807 -28.006 9.453 1.00 19.10 C
ATOM 3393 C TYR A 450 -5.405 -26.901 10.302 1.00 17.86 C
ATOM 3394 O TYR A 450 -6.411 -27.099 10.987 1.00 17.17 O
ATOM 3395 CB TYR A 450 -5.061 -27.673 7.978 1.00 20.22 C
ATOM 3396 CG TYR A 450 -4.858 -28.825 7.028 1.00 21.58 C
ATOM 3397 CD1 TYR A 450 -5.940 -29.593 6.608 1.00 23.26 C
ATOM 3398 CD2 TYR A 450 -3.589 -29.151 6.555 1.00 22.98 C
ATOM 3399 CE1 TYR A 450 -5.773 -30.660 5.745 1.00 24.28 C
ATOM 3400 CE2 TYR A 450 -3.406 -30.227 5.683 1.00 23.90 C
ATOM 3401 CZ TYR A 450 -4.507 -30.974 5.286 1.00 23.79 C
ATOM 3402 OH TYR A 450 -4.357 -32.037 4.424 1.00 24.60 O
ATOM 3403 N PHE A 451 -4.789 -25.728 10.230 1.00 16.38 N
ATOM 3404 CA PHE A 451 -5.317 -24.562 10.910 1.00 15.17 C
ATOM 3405 C PHE A 451 -5.300 -23.355 9.989 1.00 14.27 C
ATOM 3406 O PHE A 451 -4.559 -23.318 8.999 1.00 13.46 O
ATOM 3407 CB PHE A 451 -4.523 -24.268 12.194 1.00 15.59 C
ATOM 3408 CG PHE A 451 -3.107 -23.809 11.951 1.00 15.86 C
ATOM 3409 CD1 PHE A 451 -2.827 -22.467 11.693 1.00 16.40 C
ATOM 3410 CD2 PHE A 451 -2.049 -24.713 12.002 1.00 16.42 C
ATOM 3411 CE1 PHE A 451 -1.520 -22.035 11.468 1.00 16.81 C
ATOM 3412 CE2 PHE A 451 -0.736 -24.293 11.783 1.00 16.62 C
ATOM 3413 CZ PHE A 451 -0.471 -22.949 11.512 1.00 16.95 C
ATOM 3414 N ILE A 452 -6.143 -22.385 10.315 1.00 13.42 N
ATOM 3415 CA ILE A 452 -6.040 -21.044 9.759 1.00 13.04 C
ATOM 3416 C ILE A 452 -5.730 -20.148 10.947 1.00 12.61 C
ATOM 3417 O ILE A 452 -6.491 -20.116 11.917 1.00 12.87 O
ATOM 3418 CB ILE A 452 -7.341 -20.580 9.091 1.00 12.82 C
ATOM 3419 CG1 ILE A 452 -7.720 -21.515 7.937 1.00 13.02 C
ATOM 3420 CG2 ILE A 452 -7.218 -19.110 8.609 1.00 13.30 C
ATOM 3421 CD1 ILE A 452 -9.119 -21.277 7.396 1.00 12.82 C
ATOM 3422 N GLY A 453 -4.604 -19.446 10.873 1.00 12.24 N
ATOM 3423 CA GLY A 453 -4.164 -18.576 11.958 1.00 12.17 C
ATOM 3424 C GLY A 453 -4.267 -17.121 11.551 1.00 12.11 C
ATOM 3425 O GLY A 453 -4.020 -16.782 10.397 1.00 12.25 O
ATOM 3426 N VAL A 454 -4.664 -16.266 12.489 1.00 11.76 N
ATOM 3427 CA VAL A 454 -4.749 -14.830 12.228 1.00 11.76 C
ATOM 3428 C VAL A 454 -3.788 -14.098 13.155 1.00 11.60 C
ATOM 3429 O VAL A 454 -3.837 -14.272 14.380 1.00 11.14 O
ATOM 3430 CB VAL A 454 -6.180 -14.277 12.409 1.00 11.88 C
ATOM 3431 CG1 VAL A 454 -6.278 -12.880 11.813 1.00 12.78 C
ATOM 3432 CG2 VAL A 454 -7.215 -15.205 11.754 1.00 12.66 C
ATOM 3433 N LEU A 455 -2.911 -13.293 12.557 1.00 11.44 N
ATOM 3434 CA LEU A 455 -1.888 -12.577 13.305 1.00 11.52 C
ATOM 3435 C LEU A 455 -2.285 -11.128 13.526 1.00 11.51 C
ATOM 3436 O LEU A 455 -2.545 -10.391 12.567 1.00 11.39 O
ATOM 3437 CB LEU A 455 -0.530 -12.650 12.595 1.00 11.45 C
ATOM 3438 CG LEU A 455 0.630 -11.943 13.306 1.00 11.22 C
ATOM 3439 CD1 LEU A 455 0.966 -12.620 14.637 1.00 11.34 C
ATOM 3440 CD2 LEU A 455 1.853 -11.884 12.415 1.00 12.09 C
ATOM 3441 N ASP A 456 -2.295 -10.741 14.800 1.00 11.54 N
ATOM 3442 CA ASP A 456 -2.683 -9.412 15.252 1.00 11.96 C
ATOM 3443 C ASP A 456 -1.648 -8.928 16.278 1.00 12.22 C
ATOM 3444 O ASP A 456 -1.733 -9.266 17.460 1.00 12.05 O
ATOM 3445 CB ASP A 456 -4.088 -9.477 15.882 1.00 12.34 C
ATOM 3446 CG ASP A 456 -4.607 -8.117 16.329 1.00 12.90 C
ATOM 3447 OD1 ASP A 456 -5.495 -8.079 17.209 1.00 15.23 O
ATOM 3448 OD2 ASP A 456 -4.132 -7.091 15.806 1.00 15.07 O
ATOM 3449 N ILE A 457 -0.675 -8.143 15.818 1.00 12.39 N
ATOM 3450 CA ILE A 457 0.377 -7.598 16.696 1.00 13.30 C
ATOM 3451 C ILE A 457 0.060 -6.158 17.120 1.00 13.06 C
ATOM 3452 O ILE A 457 -0.843 -5.525 16.562 1.00 13.42 O
ATOM 3453 CB ILE A 457 1.793 -7.663 16.037 1.00 13.85 C
ATOM 3454 CG1 ILE A 457 1.850 -6.791 14.770 1.00 14.61 C
ATOM 3455 CG2 ILE A 457 2.201 -9.128 15.773 1.00 13.99 C
ATOM 3456 CD1 ILE A 457 3.241 -6.339 14.357 1.00 14.49 C
ATOM 3457 N ALA A 458 0.778 -5.645 18.118 1.00 12.15 N
ATOM 3458 CA ALA A 458 0.722 -4.211 18.399 1.00 11.26 C
ATOM 3459 C ALA A 458 1.420 -3.496 17.234 1.00 10.82 C
ATOM 3460 O ALA A 458 2.520 -3.879 16.841 1.00 10.86 O
ATOM 3461 CB ALA A 458 1.395 -3.886 19.724 1.00 11.07 C
ATOM 3462 N GLY A 459 0.762 -2.488 16.666 1.00 9.90 N
ATOM 3463 CA GLY A 459 1.246 -1.846 15.444 1.00 9.38 C
ATOM 3464 C GLY A 459 2.175 -0.671 15.680 1.00 9.31 C
ATOM 3465 O GLY A 459 2.268 -0.140 16.789 1.00 9.26 O
ATOM 3466 N PHE A 460 2.845 -0.263 14.608 1.00 8.77 N
ATOM 3467 CA PHE A 460 3.789 0.850 14.614 1.00 9.03 C
ATOM 3468 C PHE A 460 3.200 2.064 15.341 1.00 9.00 C
ATOM 3469 O PHE A 460 2.073 2.479 15.063 1.00 8.72 O
ATOM 3470 CB PHE A 460 4.134 1.198 13.167 1.00 9.14 C
ATOM 3471 CG PHE A 460 5.185 2.259 13.025 1.00 9.76 C
ATOM 3472 CD1 PHE A 460 6.533 1.944 13.155 1.00 11.54 C
ATOM 3473 CD2 PHE A 460 4.820 3.572 12.750 1.00 11.11 C
ATOM 3474 CE1 PHE A 460 7.512 2.936 13.019 1.00 11.86 C
ATOM 3475 CE2 PHE A 460 5.791 4.571 12.606 1.00 12.04 C
ATOM 3476 CZ PHE A 460 7.131 4.250 12.742 1.00 11.30 C
ATOM 3477 N GLU A 461 3.950 2.621 16.286 1.00 8.83 N
ATOM 3478 CA GLU A 461 3.454 3.764 17.057 1.00 9.23 C
ATOM 3479 C GLU A 461 4.593 4.691 17.457 1.00 9.82 C
ATOM 3480 O GLU A 461 5.728 4.247 17.643 1.00 9.16 O
ATOM 3481 CB GLU A 461 2.677 3.291 18.306 1.00 9.24 C
ATOM 3482 CG GLU A 461 3.516 2.526 19.360 1.00 9.21 C
ATOM 3483 CD GLU A 461 2.736 2.197 20.642 1.00 9.76 C
ATOM 3484 OE1 GLU A 461 3.348 2.197 21.741 1.00 11.67 O
ATOM 3485 OE2 GLU A 461 1.516 1.946 20.558 1.00 10.37 O
ATOM 3486 N TYR A 462 4.283 5.977 17.578 1.00 10.29 N
ATOM 3487 CA TYR A 462 5.213 6.934 18.173 1.00 11.66 C
ATOM 3488 C TYR A 462 4.461 8.103 18.801 1.00 11.61 C
ATOM 3489 O TYR A 462 3.302 8.374 18.451 1.00 11.42 O
ATOM 3490 CB TYR A 462 6.286 7.416 17.181 1.00 12.99 C
ATOM 3491 CG TYR A 462 5.790 8.302 16.051 1.00 15.13 C
ATOM 3492 CD1 TYR A 462 5.423 9.634 16.281 1.00 16.03 C
ATOM 3493 CD2 TYR A 462 5.707 7.814 14.747 1.00 17.60 C
ATOM 3494 CE1 TYR A 462 4.971 10.448 15.238 1.00 17.87 C
ATOM 3495 CE2 TYR A 462 5.262 8.622 13.698 1.00 18.29 C
ATOM 3496 CZ TYR A 462 4.896 9.934 13.951 1.00 17.04 C
ATOM 3497 OH TYR A 462 4.458 10.734 12.916 1.00 18.57 O
ATOM 3498 N PHE A 463 5.142 8.770 19.730 1.00 11.91 N
ATOM 3499 CA PHE A 463 4.574 9.821 20.568 1.00 12.80 C
ATOM 3500 C PHE A 463 5.594 10.938 20.712 1.00 13.21 C
ATOM 3501 O PHE A 463 6.683 10.870 20.139 1.00 12.99 O
ATOM 3502 CB PHE A 463 4.238 9.240 21.949 1.00 12.94 C
ATOM 3503 CG PHE A 463 3.380 8.007 21.889 1.00 13.88 C
ATOM 3504 CD1 PHE A 463 3.957 6.742 21.815 1.00 14.74 C
ATOM 3505 CD2 PHE A 463 1.989 8.113 21.868 1.00 14.17 C
ATOM 3506 CE1 PHE A 463 3.161 5.599 21.735 1.00 15.41 C
ATOM 3507 CE2 PHE A 463 1.186 6.973 21.791 1.00 14.07 C
ATOM 3508 CZ PHE A 463 1.773 5.715 21.723 1.00 14.30 C
ATOM 3509 N GLU A 464 5.249 11.961 21.492 1.00 13.95 N
ATOM 3510 CA GLU A 464 6.198 13.020 21.816 1.00 15.16 C
ATOM 3511 C GLU A 464 7.441 12.460 22.511 1.00 14.15 C
ATOM 3512 O GLU A 464 8.550 12.931 22.278 1.00 14.78 O
ATOM 3513 CB GLU A 464 5.537 14.090 22.684 1.00 15.14 C
ATOM 3514 CG GLU A 464 4.586 15.006 21.912 1.00 17.63 C
ATOM 3515 CD GLU A 464 4.161 16.226 22.711 1.00 18.61 C
ATOM 3516 OE1 GLU A 464 4.046 16.130 23.954 1.00 24.03 O
ATOM 3517 OE2 GLU A 464 3.935 17.287 22.092 1.00 24.58 O
ATOM 3518 N HIS A 465 7.243 11.443 23.344 1.00 13.34 N
ATOM 3519 CA HIS A 465 8.330 10.777 24.056 1.00 12.64 C
ATOM 3520 C HIS A 465 8.243 9.273 23.829 1.00 12.07 C
ATOM 3521 O HIS A 465 7.269 8.639 24.226 1.00 12.13 O
ATOM 3522 CB HIS A 465 8.265 11.094 25.550 1.00 13.12 C
ATOM 3523 CG HIS A 465 8.297 12.561 25.841 1.00 13.41 C
ATOM 3524 ND1 HIS A 465 9.471 13.279 25.901 1.00 14.52 N
ATOM 3525 CD2 HIS A 465 7.299 13.452 26.046 1.00 15.76 C
ATOM 3526 CE1 HIS A 465 9.196 14.548 26.145 1.00 15.80 C
ATOM 3527 NE2 HIS A 465 7.886 14.679 26.242 1.00 16.00 N
ATOM 3528 N ASN A 466 9.271 8.725 23.192 1.00 10.93 N
ATOM 3529 CA ASN A 466 9.331 7.306 22.858 1.00 10.39 C
ATOM 3530 C ASN A 466 10.383 6.568 23.662 1.00 10.07 C
ATOM 3531 O ASN A 466 11.532 7.010 23.746 1.00 10.43 O
ATOM 3532 CB ASN A 466 9.630 7.161 21.370 1.00 10.03 C
ATOM 3533 CG ASN A 466 8.596 7.841 20.521 1.00 9.98 C
ATOM 3534 OD1 ASN A 466 7.411 7.514 20.602 1.00 9.23 O
ATOM 3535 ND2 ASN A 466 9.025 8.811 19.720 1.00 9.26 N
ATOM 3536 N SER A 467 9.993 5.431 24.231 1.00 9.68 N
ATOM 3537 CA SER A 467 10.880 4.663 25.084 1.00 9.40 C
ATOM 3538 C SER A 467 11.051 3.244 24.546 1.00 9.23 C
ATOM 3539 O SER A 467 10.763 2.973 23.372 1.00 8.65 O
ATOM 3540 CB SER A 467 10.345 4.655 26.523 1.00 9.57 C
ATOM 3541 OG SER A 467 11.344 4.282 27.457 1.00 10.81 O
ATOM 3542 N PHE A 468 11.518 2.353 25.413 1.00 8.85 N
ATOM 3543 CA PHE A 468 11.866 0.983 25.027 1.00 9.04 C
ATOM 3544 C PHE A 468 10.653 0.198 24.523 1.00 8.88 C
ATOM 3545 O PHE A 468 10.777 -0.635 23.618 1.00 9.04 O
ATOM 3546 CB PHE A 468 12.534 0.263 26.198 1.00 9.67 C
ATOM 3547 CG PHE A 468 13.211 -1.030 25.819 1.00 9.72 C
ATOM 3548 CD1 PHE A 468 14.189 -1.061 24.829 1.00 11.52 C
ATOM 3549 CD2 PHE A 468 12.879 -2.214 26.472 1.00 11.67 C
ATOM 3550 CE1 PHE A 468 14.821 -2.264 24.486 1.00 12.38 C
ATOM 3551 CE2 PHE A 468 13.503 -3.415 26.138 1.00 12.33 C
ATOM 3552 CZ PHE A 468 14.480 -3.439 25.146 1.00 11.70 C
ATOM 3553 N GLU A 469 9.485 0.484 25.095 1.00 8.42 N
ATOM 3554 CA GLU A 469 8.233 -0.157 24.666 1.00 8.57 C
ATOM 3555 C GLU A 469 7.974 0.131 23.191 1.00 8.20 C
ATOM 3556 O GLU A 469 7.692 -0.782 22.415 1.00 8.16 O
ATOM 3557 CB GLU A 469 7.052 0.326 25.519 1.00 8.97 C
ATOM 3558 CG GLU A 469 7.121 -0.095 26.985 1.00 10.24 C
ATOM 3559 CD GLU A 469 7.963 0.837 27.867 1.00 12.58 C
ATOM 3560 OE1 GLU A 469 8.546 1.822 27.374 1.00 12.16 O
ATOM 3561 OE2 GLU A 469 8.038 0.574 29.083 1.00 13.39 O
ATOM 3562 N GLN A 470 8.111 1.398 22.794 1.00 7.70 N
ATOM 3563 CA GLN A 470 7.927 1.772 21.384 1.00 7.57 C
ATOM 3564 C GLN A 470 9.006 1.137 20.510 1.00 7.58 C
ATOM 3565 O GLN A 470 8.732 0.702 19.401 1.00 7.22 O
ATOM 3566 CB GLN A 470 7.941 3.292 21.204 1.00 7.80 C
ATOM 3567 CG GLN A 470 6.670 3.987 21.699 1.00 8.56 C
ATOM 3568 CD GLN A 470 6.464 3.822 23.191 1.00 10.03 C
ATOM 3569 OE1 GLN A 470 7.330 4.187 23.991 1.00 10.23 O
ATOM 3570 NE2 GLN A 470 5.318 3.268 23.575 1.00 10.30 N
ATOM 3571 N PHE A 471 10.230 1.084 21.026 1.00 7.59 N
ATOM 3572 CA PHE A 471 11.355 0.523 20.277 1.00 7.99 C
ATOM 3573 C PHE A 471 11.076 -0.947 19.960 1.00 8.11 C
ATOM 3574 O PHE A 471 11.218 -1.386 18.814 1.00 8.27 O
ATOM 3575 CB PHE A 471 12.645 0.669 21.085 1.00 8.56 C
ATOM 3576 CG PHE A 471 13.873 0.159 20.379 1.00 8.79 C
ATOM 3577 CD1 PHE A 471 14.534 0.945 19.444 1.00 10.04 C
ATOM 3578 CD2 PHE A 471 14.375 -1.105 20.669 1.00 10.78 C
ATOM 3579 CE1 PHE A 471 15.680 0.483 18.797 1.00 11.45 C
ATOM 3580 CE2 PHE A 471 15.520 -1.583 20.032 1.00 10.77 C
ATOM 3581 CZ PHE A 471 16.171 -0.788 19.090 1.00 10.67 C
ATOM 3582 N CYS A 472 10.645 -1.688 20.975 1.00 8.03 N
ATOM 3583 CA CYS A 472 10.298 -3.098 20.805 1.00 8.16 C
ATOM 3584 C CYS A 472 9.101 -3.302 19.862 1.00 7.90 C
ATOM 3585 O CYS A 472 9.151 -4.152 18.965 1.00 7.72 O
ATOM 3586 CB CYS A 472 10.060 -3.743 22.168 1.00 8.30 C
ATOM 3587 SG CYS A 472 11.566 -3.900 23.150 1.00 10.78 S
ATOM 3588 N ILE A 473 8.040 -2.515 20.045 1.00 7.29 N
ATOM 3589 CA ILE A 473 6.867 -2.594 19.164 1.00 7.56 C
ATOM 3590 C ILE A 473 7.263 -2.317 17.711 1.00 7.17 C
ATOM 3591 O ILE A 473 6.912 -3.074 16.791 1.00 7.57 O
ATOM 3592 CB ILE A 473 5.746 -1.628 19.609 1.00 7.20 C
ATOM 3593 CG1 ILE A 473 5.108 -2.131 20.910 1.00 8.06 C
ATOM 3594 CG2 ILE A 473 4.681 -1.484 18.511 1.00 7.82 C
ATOM 3595 CD1 ILE A 473 4.225 -1.117 21.596 1.00 8.53 C
ATOM 3596 N ASN A 474 8.034 -1.256 17.507 1.00 6.86 N
ATOM 3597 CA ASN A 474 8.418 -0.876 16.146 1.00 7.57 C
ATOM 3598 C ASN A 474 9.365 -1.877 15.474 1.00 7.97 C
ATOM 3599 O ASN A 474 9.273 -2.112 14.262 1.00 8.01 O
ATOM 3600 CB ASN A 474 8.908 0.574 16.117 1.00 7.52 C
ATOM 3601 CG ASN A 474 7.784 1.554 16.452 1.00 7.07 C
ATOM 3602 OD1 ASN A 474 6.605 1.210 16.343 1.00 6.97 O
ATOM 3603 ND2 ASN A 474 8.141 2.764 16.880 1.00 6.98 N
ATOM 3604 N TYR A 475 10.229 -2.495 16.277 1.00 8.03 N
ATOM 3605 CA TYR A 475 11.084 -3.592 15.822 1.00 8.85 C
ATOM 3606 C TYR A 475 10.239 -4.769 15.308 1.00 9.12 C
ATOM 3607 O TYR A 475 10.502 -5.299 14.226 1.00 9.07 O
ATOM 3608 CB TYR A 475 12.021 -4.007 16.959 1.00 9.20 C
ATOM 3609 CG TYR A 475 12.651 -5.378 16.846 1.00 9.35 C
ATOM 3610 CD1 TYR A 475 13.468 -5.715 15.762 1.00 9.34 C
ATOM 3611 CD2 TYR A 475 12.461 -6.327 17.856 1.00 10.71 C
ATOM 3612 CE1 TYR A 475 14.065 -6.981 15.677 1.00 10.37 C
ATOM 3613 CE2 TYR A 475 13.053 -7.593 17.779 1.00 10.53 C
ATOM 3614 CZ TYR A 475 13.849 -7.907 16.688 1.00 11.35 C
ATOM 3615 OH TYR A 475 14.429 -9.157 16.612 1.00 12.04 O
ATOM 3616 N CYS A 476 9.215 -5.157 16.064 1.00 9.15 N
ATOM 3617 C CYS A 476 7.673 -5.898 14.295 1.00 9.33 C
ATOM 3618 O CYS A 476 7.591 -6.742 13.399 1.00 9.04 O
ATOM 3619 CA ACYS A 476 8.327 -6.241 15.626 0.50 9.69 C
ATOM 3620 CB ACYS A 476 7.260 -6.539 16.673 0.50 9.77 C
ATOM 3621 SG ACYS A 476 7.930 -7.076 18.250 0.50 13.05 S
ATOM 3623 CB BCYS A 476 7.256 -6.475 16.703 0.50 9.48 C
ATOM 3624 SG BCYS A 476 6.047 -7.719 16.275 0.50 11.08 S
ATOM 3625 N ASN A 477 7.222 -4.652 14.162 1.00 9.40 N
ATOM 3626 CA ASN A 477 6.611 -4.196 12.915 1.00 10.15 C
ATOM 3627 C ASN A 477 7.592 -4.221 11.728 1.00 10.32 C
ATOM 3628 O ASN A 477 7.192 -4.546 10.602 1.00 10.66 O
ATOM 3629 CB ASN A 477 5.969 -2.820 13.098 1.00 10.38 C
ATOM 3630 CG ASN A 477 4.612 -2.893 13.796 1.00 11.23 C
ATOM 3631 OD1 ASN A 477 3.563 -2.795 13.148 1.00 13.62 O
ATOM 3632 ND2 ASN A 477 4.623 -3.073 15.121 1.00 10.14 N
ATOM 3633 N GLU A 478 8.866 -3.898 11.984 1.00 10.72 N
ATOM 3634 CA GLU A 478 9.940 -4.049 10.978 1.00 11.51 C
ATOM 3635 C GLU A 478 10.016 -5.491 10.496 1.00 11.88 C
ATOM 3636 O GLU A 478 10.079 -5.758 9.290 1.00 11.71 O
ATOM 3637 CB GLU A 478 11.328 -3.741 11.562 1.00 12.05 C
ATOM 3638 CG GLU A 478 11.698 -2.319 11.802 1.00 14.80 C
ATOM 3639 CD GLU A 478 11.656 -1.405 10.581 1.00 15.71 C
ATOM 3640 OE1 GLU A 478 11.325 -0.253 10.815 1.00 14.91 O
ATOM 3641 OE2 GLU A 478 11.939 -1.786 9.418 1.00 16.97 O
ATOM 3642 N LYS A 479 10.031 -6.414 11.455 1.00 11.90 N
ATOM 3643 CA LYS A 479 10.179 -7.842 11.162 1.00 12.42 C
ATOM 3644 C LYS A 479 9.010 -8.332 10.315 1.00 12.46 C
ATOM 3645 O LYS A 479 9.202 -9.076 9.346 1.00 12.63 O
ATOM 3646 CB LYS A 479 10.288 -8.655 12.457 1.00 12.79 C
ATOM 3647 CG LYS A 479 11.540 -8.355 13.296 1.00 14.42 C
ATOM 3648 CD LYS A 479 12.756 -9.172 12.861 1.00 16.99 C
ATOM 3649 CE LYS A 479 12.711 -10.602 13.403 1.00 17.12 C
ATOM 3650 NZ LYS A 479 13.926 -11.384 13.025 1.00 17.98 N
ATOM 3651 N LEU A 480 7.804 -7.899 10.669 1.00 12.12 N
ATOM 3652 CA LEU A 480 6.615 -8.308 9.917 1.00 12.60 C
ATOM 3653 C LEU A 480 6.572 -7.726 8.504 1.00 12.50 C
ATOM 3654 O LEU A 480 6.174 -8.412 7.556 1.00 11.92 O
ATOM 3655 CB LEU A 480 5.328 -8.017 10.693 1.00 13.12 C
ATOM 3656 CG LEU A 480 4.809 -9.205 11.519 1.00 14.17 C
ATOM 3657 CD1 LEU A 480 4.443 -10.382 10.609 1.00 15.27 C
ATOM 3658 CD2 LEU A 480 5.800 -9.645 12.601 1.00 15.58 C
ATOM 3659 N GLN A 481 7.004 -6.475 8.351 1.00 11.81 N
ATOM 3660 CA GLN A 481 7.115 -5.885 7.014 1.00 12.06 C
ATOM 3661 C GLN A 481 8.130 -6.643 6.162 1.00 12.02 C
ATOM 3662 O GLN A 481 7.935 -6.819 4.954 1.00 12.18 O
ATOM 3663 CB GLN A 481 7.490 -4.399 7.082 1.00 11.89 C
ATOM 3664 CG GLN A 481 7.535 -3.705 5.711 1.00 11.98 C
ATOM 3665 CD GLN A 481 6.184 -3.669 4.997 1.00 12.78 C
ATOM 3666 OE1 GLN A 481 5.137 -3.467 5.615 1.00 13.17 O
ATOM 3667 NE2 GLN A 481 6.209 -3.869 3.683 1.00 12.80 N
ATOM 3668 N GLN A 482 9.207 -7.098 6.796 1.00 12.30 N
ATOM 3669 CA GLN A 482 10.230 -7.865 6.093 1.00 12.70 C
ATOM 3670 C GLN A 482 9.661 -9.189 5.572 1.00 12.52 C
ATOM 3671 O GLN A 482 9.988 -9.617 4.460 1.00 12.34 O
ATOM 3672 CB GLN A 482 11.454 -8.073 6.999 1.00 13.12 C
ATOM 3673 CG GLN A 482 12.531 -9.057 6.499 1.00 15.38 C
ATOM 3674 CD GLN A 482 13.069 -8.761 5.111 1.00 18.23 C
ATOM 3675 OE1 GLN A 482 13.455 -9.683 4.389 1.00 19.35 O
ATOM 3676 NE2 GLN A 482 13.107 -7.486 4.728 1.00 19.64 N
ATOM 3677 N PHE A 483 8.785 -9.810 6.360 1.00 12.56 N
ATOM 3678 CA PHE A 483 8.124 -11.046 5.936 1.00 12.85 C
ATOM 3679 C PHE A 483 7.253 -10.809 4.700 1.00 12.76 C
ATOM 3680 O PHE A 483 7.254 -11.627 3.763 1.00 12.98 O
ATOM 3681 CB PHE A 483 7.306 -11.668 7.076 1.00 13.38 C
ATOM 3682 CG PHE A 483 6.501 -12.875 6.657 1.00 14.45 C
ATOM 3683 CD1 PHE A 483 5.122 -12.785 6.497 1.00 15.53 C
ATOM 3684 CD2 PHE A 483 7.126 -14.093 6.407 1.00 15.61 C
ATOM 3685 CE1 PHE A 483 4.374 -13.895 6.099 1.00 15.94 C
ATOM 3686 CE2 PHE A 483 6.381 -15.209 6.012 1.00 16.76 C
ATOM 3687 CZ PHE A 483 5.008 -15.104 5.860 1.00 15.54 C
ATOM 3688 N PHE A 484 6.518 -9.699 4.697 1.00 12.29 N
ATOM 3689 CA PHE A 484 5.736 -9.303 3.521 1.00 12.31 C
ATOM 3690 C PHE A 484 6.638 -9.078 2.312 1.00 12.38 C
ATOM 3691 O PHE A 484 6.360 -9.600 1.233 1.00 12.34 O
ATOM 3692 CB PHE A 484 4.913 -8.037 3.784 1.00 12.77 C
ATOM 3693 CG PHE A 484 4.192 -7.524 2.557 1.00 13.12 C
ATOM 3694 CD1 PHE A 484 2.951 -8.042 2.198 1.00 15.13 C
ATOM 3695 CD2 PHE A 484 4.770 -6.542 1.749 1.00 14.02 C
ATOM 3696 CE1 PHE A 484 2.281 -7.574 1.058 1.00 15.87 C
ATOM 3697 CE2 PHE A 484 4.112 -6.070 0.608 1.00 14.84 C
ATOM 3698 CZ PHE A 484 2.867 -6.591 0.264 1.00 15.67 C
ATOM 3699 N ASN A 485 7.702 -8.291 2.494 1.00 12.41 N
ATOM 3700 CA ASN A 485 8.660 -8.017 1.414 1.00 13.02 C
ATOM 3701 C ASN A 485 9.236 -9.307 0.812 1.00 13.54 C
ATOM 3702 O ASN A 485 9.331 -9.455 -0.417 1.00 13.20 O
ATOM 3703 CB ASN A 485 9.805 -7.123 1.914 1.00 13.02 C
ATOM 3704 CG ASN A 485 9.364 -5.694 2.219 1.00 13.14 C
ATOM 3705 OD1 ASN A 485 8.256 -5.276 1.891 1.00 13.56 O
ATOM 3706 ND2 ASN A 485 10.254 -4.935 2.862 1.00 14.72 N
ATOM 3707 N GLU A 486 9.598 -10.231 1.699 1.00 14.22 N
ATOM 3708 CA GLU A 486 10.172 -11.527 1.345 1.00 15.95 C
ATOM 3709 C GLU A 486 9.171 -12.384 0.568 1.00 15.68 C
ATOM 3710 O GLU A 486 9.490 -12.905 -0.503 1.00 15.23 O
ATOM 3711 CB GLU A 486 10.646 -12.224 2.630 1.00 15.93 C
ATOM 3712 CG GLU A 486 10.849 -13.747 2.583 1.00 18.37 C
ATOM 3713 CD GLU A 486 11.024 -14.344 3.983 1.00 18.92 C
ATOM 3714 OE1 GLU A 486 11.919 -13.885 4.724 1.00 23.89 O
ATOM 3715 OE2 GLU A 486 10.267 -15.269 4.349 1.00 22.52 O
ATOM 3716 N ARG A 487 7.956 -12.508 1.101 1.00 15.56 N
ATOM 3717 CA ARG A 487 6.932 -13.359 0.495 1.00 16.29 C
ATOM 3718 C ARG A 487 6.310 -12.768 -0.786 1.00 16.41 C
ATOM 3719 O ARG A 487 6.104 -13.496 -1.769 1.00 17.42 O
ATOM 3720 CB ARG A 487 5.859 -13.710 1.543 1.00 16.26 C
ATOM 3721 CG ARG A 487 4.806 -14.735 1.108 1.00 17.34 C
ATOM 3722 CD ARG A 487 5.391 -16.118 0.803 1.00 17.48 C
ATOM 3723 NE ARG A 487 5.901 -16.821 1.982 1.00 18.10 N
ATOM 3724 CZ ARG A 487 5.169 -17.589 2.789 1.00 18.95 C
ATOM 3725 NH1 ARG A 487 3.868 -17.749 2.582 1.00 18.53 N
ATOM 3726 NH2 ARG A 487 5.740 -18.189 3.824 1.00 20.15 N
ATOM 3727 N ILE A 488 6.041 -11.461 -0.788 1.00 16.38 N
ATOM 3728 CA ILE A 488 5.243 -10.825 -1.855 1.00 16.45 C
ATOM 3729 C ILE A 488 6.039 -10.072 -2.925 1.00 16.67 C
ATOM 3730 O ILE A 488 5.620 -10.018 -4.089 1.00 17.50 O
ATOM 3731 CB ILE A 488 4.133 -9.900 -1.271 1.00 16.48 C
ATOM 3732 CG1 ILE A 488 3.183 -10.704 -0.375 1.00 16.62 C
ATOM 3733 CG2 ILE A 488 3.334 -9.188 -2.378 1.00 16.60 C
ATOM 3734 CD1 ILE A 488 2.549 -11.927 -1.055 1.00 17.33 C
ATOM 3735 N LEU A 489 7.151 -9.462 -2.532 1.00 15.80 N
ATOM 3736 CA LEU A 489 7.942 -8.677 -3.476 1.00 15.79 C
ATOM 3737 C LEU A 489 9.174 -9.415 -3.982 1.00 15.89 C
ATOM 3738 O LEU A 489 9.560 -9.241 -5.143 1.00 16.53 O
ATOM 3739 CB LEU A 489 8.319 -7.311 -2.886 1.00 15.31 C
ATOM 3740 CG LEU A 489 7.174 -6.312 -2.688 1.00 15.76 C
ATOM 3741 CD1 LEU A 489 7.634 -5.111 -1.878 1.00 14.91 C
ATOM 3742 CD2 LEU A 489 6.581 -5.864 -4.028 1.00 15.89 C
ATOM 3743 N LYS A 490 9.792 -10.228 -3.125 1.00 15.75 N
ATOM 3744 CA LYS A 490 10.990 -10.975 -3.516 1.00 16.13 C
ATOM 3745 C LYS A 490 10.636 -12.329 -4.132 1.00 16.00 C
ATOM 3746 O LYS A 490 10.915 -12.571 -5.309 1.00 16.03 O
ATOM 3747 CB LYS A 490 11.942 -11.172 -2.334 1.00 16.13 C
ATOM 3748 CG LYS A 490 13.350 -11.627 -2.754 1.00 18.15 C
ATOM 3749 CD LYS A 490 14.001 -12.485 -1.680 1.00 22.09 C
ATOM 3750 CE LYS A 490 14.285 -11.692 -0.430 1.00 24.52 C
ATOM 3751 NZ LYS A 490 14.113 -12.534 0.797 1.00 27.45 N
ATOM 3752 N GLU A 491 10.018 -13.204 -3.337 1.00 16.00 N
ATOM 3753 CA GLU A 491 9.716 -14.571 -3.787 1.00 16.09 C
ATOM 3754 C GLU A 491 8.783 -14.621 -4.998 1.00 15.59 C
ATOM 3755 O GLU A 491 8.903 -15.513 -5.836 1.00 15.15 O
ATOM 3756 CB GLU A 491 9.155 -15.410 -2.638 1.00 16.12 C
ATOM 3757 CG GLU A 491 10.203 -15.807 -1.606 1.00 17.06 C
ATOM 3758 CD GLU A 491 9.612 -16.504 -0.385 1.00 17.69 C
ATOM 3759 OE1 GLU A 491 10.355 -16.689 0.604 1.00 21.26 O
ATOM 3760 OE2 GLU A 491 8.417 -16.860 -0.407 1.00 20.12 O
ATOM 3761 N GLU A 492 7.863 -13.664 -5.090 1.00 15.18 N
ATOM 3762 CA GLU A 492 6.951 -13.590 -6.226 1.00 15.49 C
ATOM 3763 C GLU A 492 7.735 -13.371 -7.522 1.00 15.31 C
ATOM 3764 O GLU A 492 7.487 -14.031 -8.534 1.00 15.14 O
ATOM 3765 CB GLU A 492 5.927 -12.471 -6.012 1.00 15.57 C
ATOM 3766 CG GLU A 492 4.819 -12.411 -7.041 1.00 17.16 C
ATOM 3767 CD GLU A 492 3.711 -13.442 -6.817 1.00 18.88 C
ATOM 3768 OE1 GLU A 492 2.730 -13.415 -7.592 1.00 20.16 O
ATOM 3769 OE2 GLU A 492 3.805 -14.262 -5.878 1.00 19.16 O
ATOM 3770 N GLN A 493 8.695 -12.450 -7.479 1.00 15.22 N
ATOM 3771 CA GLN A 493 9.500 -12.135 -8.660 1.00 15.22 C
ATOM 3772 C GLN A 493 10.491 -13.248 -8.997 1.00 15.40 C
ATOM 3773 O GLN A 493 10.771 -13.502 -10.173 1.00 15.16 O
ATOM 3774 CB GLN A 493 10.193 -10.786 -8.491 1.00 15.13 C
ATOM 3775 CG GLN A 493 9.189 -9.650 -8.324 1.00 14.41 C
ATOM 3776 CD GLN A 493 9.800 -8.282 -8.507 1.00 15.36 C
ATOM 3777 OE1 GLN A 493 10.090 -7.871 -9.626 1.00 13.40 O
ATOM 3778 NE2 GLN A 493 9.981 -7.558 -7.405 1.00 14.69 N
ATOM 3779 N GLU A 494 11.004 -13.918 -7.967 1.00 15.66 N
ATOM 3780 CA GLU A 494 11.872 -15.078 -8.158 1.00 16.30 C
ATOM 3781 C GLU A 494 11.130 -16.209 -8.865 1.00 16.49 C
ATOM 3782 O GLU A 494 11.702 -16.875 -9.734 1.00 16.16 O
ATOM 3783 CB GLU A 494 12.444 -15.559 -6.827 1.00 16.87 C
ATOM 3784 CG GLU A 494 13.482 -14.612 -6.254 1.00 18.43 C
ATOM 3785 CD GLU A 494 13.975 -15.012 -4.878 1.00 21.29 C
ATOM 3786 OE1 GLU A 494 13.397 -15.932 -4.251 1.00 22.56 O
ATOM 3787 OE2 GLU A 494 14.957 -14.392 -4.420 1.00 23.04 O
ATOM 3788 N LEU A 495 9.859 -16.404 -8.501 1.00 16.23 N
ATOM 3789 CA LEU A 495 8.996 -17.391 -9.162 1.00 16.48 C
ATOM 3790 C LEU A 495 8.801 -17.079 -10.643 1.00 16.35 C
ATOM 3791 O LEU A 495 8.969 -17.955 -11.494 1.00 16.47 O
ATOM 3792 CB LEU A 495 7.634 -17.486 -8.463 1.00 16.33 C
ATOM 3793 CG LEU A 495 6.592 -18.443 -9.063 1.00 17.44 C
ATOM 3794 CD1 LEU A 495 7.093 -19.890 -9.072 1.00 17.48 C
ATOM 3795 CD2 LEU A 495 5.276 -18.333 -8.308 1.00 16.99 C
ATOM 3796 N TYR A 496 8.445 -15.833 -10.944 1.00 16.01 N
ATOM 3797 CA TYR A 496 8.271 -15.399 -12.328 1.00 16.39 C
ATOM 3798 C TYR A 496 9.549 -15.649 -13.134 1.00 17.04 C
ATOM 3799 O TYR A 496 9.497 -16.140 -14.261 1.00 16.89 O
ATOM 3800 CB TYR A 496 7.915 -13.912 -12.396 1.00 15.82 C
ATOM 3801 CG TYR A 496 6.625 -13.477 -11.715 1.00 15.58 C
ATOM 3802 CD1 TYR A 496 6.429 -12.138 -11.388 1.00 14.72 C
ATOM 3803 CD2 TYR A 496 5.603 -14.388 -11.405 1.00 14.15 C
ATOM 3804 CE1 TYR A 496 5.258 -11.704 -10.781 1.00 15.00 C
ATOM 3805 CE2 TYR A 496 4.421 -13.963 -10.788 1.00 14.58 C
ATOM 3806 CZ TYR A 496 4.258 -12.618 -10.485 1.00 15.33 C
ATOM 3807 OH TYR A 496 3.108 -12.165 -9.879 1.00 15.79 O
ATOM 3808 N GLN A 497 10.692 -15.314 -12.536 1.00 17.79 N
ATOM 3809 CA GLN A 497 12.003 -15.493 -13.164 1.00 19.37 C
ATOM 3810 C GLN A 497 12.301 -16.968 -13.459 1.00 19.54 C
ATOM 3811 O GLN A 497 12.667 -17.320 -14.584 1.00 19.89 O
ATOM 3812 CB GLN A 497 13.091 -14.906 -12.259 1.00 19.62 C
ATOM 3813 CG GLN A 497 14.515 -15.155 -12.725 1.00 22.84 C
ATOM 3814 CD GLN A 497 15.044 -14.033 -13.583 1.00 26.67 C
ATOM 3815 OE1 GLN A 497 14.618 -13.852 -14.728 1.00 29.66 O
ATOM 3816 NE2 GLN A 497 15.986 -13.269 -13.036 1.00 27.50 N
ATOM 3817 N LYS A 498 12.142 -17.809 -12.439 1.00 19.90 N
ATOM 3818 CA LYS A 498 12.383 -19.255 -12.528 1.00 20.71 C
ATOM 3819 C LYS A 498 11.506 -19.911 -13.598 1.00 20.52 C
ATOM 3820 O LYS A 498 11.925 -20.866 -14.265 1.00 20.35 O
ATOM 3821 CB LYS A 498 12.142 -19.894 -11.155 1.00 20.83 C
ATOM 3822 CG LYS A 498 12.141 -21.420 -11.106 1.00 21.88 C
ATOM 3823 CD LYS A 498 12.070 -21.938 -9.666 1.00 22.44 C
ATOM 3824 CE LYS A 498 10.778 -21.525 -8.947 1.00 25.52 C
ATOM 3825 NZ LYS A 498 9.575 -22.259 -9.445 1.00 27.29 N
ATOM 3826 N GLU A 499 10.296 -19.384 -13.756 1.00 20.44 N
ATOM 3827 CA GLU A 499 9.329 -19.917 -14.715 1.00 20.30 C
ATOM 3828 C GLU A 499 9.479 -19.314 -16.112 1.00 20.26 C
ATOM 3829 O GLU A 499 8.817 -19.749 -17.065 1.00 19.97 O
ATOM 3830 CB GLU A 499 7.907 -19.732 -14.179 1.00 20.42 C
ATOM 3831 CG GLU A 499 7.555 -20.714 -13.069 1.00 20.69 C
ATOM 3832 CD GLU A 499 7.370 -22.139 -13.576 1.00 21.79 C
ATOM 3833 OE1 GLU A 499 6.711 -22.321 -14.623 1.00 21.59 O
ATOM 3834 OE2 GLU A 499 7.877 -23.073 -12.920 1.00 22.25 O
ATOM 3835 N GLY A 500 10.354 -18.315 -16.226 1.00 19.80 N
ATOM 3836 CA GLY A 500 10.657 -17.672 -17.505 1.00 19.47 C
ATOM 3837 C GLY A 500 9.552 -16.788 -18.055 1.00 19.38 C
ATOM 3838 O GLY A 500 9.372 -16.701 -19.272 1.00 19.21 O
ATOM 3839 N LEU A 501 8.821 -16.115 -17.165 1.00 18.85 N
ATOM 3840 CA LEU A 501 7.663 -15.308 -17.565 1.00 18.75 C
ATOM 3841 C LEU A 501 7.988 -13.938 -18.165 1.00 18.88 C
ATOM 3842 O LEU A 501 7.125 -13.319 -18.789 1.00 19.03 O
ATOM 3843 CB LEU A 501 6.685 -15.131 -16.394 1.00 18.32 C
ATOM 3844 CG LEU A 501 6.077 -16.372 -15.741 1.00 18.57 C
ATOM 3845 CD1 LEU A 501 5.060 -15.939 -14.696 1.00 16.92 C
ATOM 3846 CD2 LEU A 501 5.424 -17.309 -16.771 1.00 18.67 C
ATOM 3847 N GLY A 502 9.215 -13.462 -17.968 1.00 19.28 N
ATOM 3848 CA GLY A 502 9.617 -12.140 -18.459 1.00 19.64 C
ATOM 3849 C GLY A 502 8.805 -10.981 -17.896 1.00 20.06 C
ATOM 3850 O GLY A 502 8.449 -10.047 -18.625 1.00 20.20 O
ATOM 3851 N VAL A 503 8.503 -11.046 -16.601 1.00 20.05 N
ATOM 3852 CA VAL A 503 7.817 -9.956 -15.909 1.00 20.37 C
ATOM 3853 C VAL A 503 8.852 -8.900 -15.516 1.00 20.66 C
ATOM 3854 O VAL A 503 9.864 -9.230 -14.891 1.00 20.48 O
ATOM 3855 CB VAL A 503 7.073 -10.458 -14.642 1.00 20.24 C
ATOM 3856 CG1 VAL A 503 6.369 -9.307 -13.929 1.00 19.83 C
ATOM 3857 CG2 VAL A 503 6.074 -11.553 -15.002 1.00 20.07 C
ATOM 3858 N ASN A 504 8.599 -7.646 -15.896 1.00 21.38 N
ATOM 3859 CA ASN A 504 9.473 -6.524 -15.540 1.00 21.97 C
ATOM 3860 C ASN A 504 9.762 -6.524 -14.042 1.00 21.83 C
ATOM 3861 O ASN A 504 8.842 -6.663 -13.234 1.00 21.95 O
ATOM 3862 CB ASN A 504 8.836 -5.186 -15.942 1.00 22.56 C
ATOM 3863 CG ASN A 504 8.742 -5.002 -17.452 1.00 23.87 C
ATOM 3864 OD1 ASN A 504 9.494 -5.607 -18.217 1.00 25.67 O
ATOM 3865 ND2 ASN A 504 7.818 -4.148 -17.884 1.00 25.77 N
ATOM 3866 N GLU A 505 11.037 -6.396 -13.678 1.00 21.57 N
ATOM 3867 CA GLU A 505 11.417 -6.380 -12.266 1.00 21.27 C
ATOM 3868 C GLU A 505 11.010 -5.065 -11.616 1.00 20.33 C
ATOM 3869 O GLU A 505 11.203 -3.993 -12.184 1.00 20.33 O
ATOM 3870 CB GLU A 505 12.915 -6.643 -12.068 1.00 21.34 C
ATOM 3871 CG GLU A 505 13.316 -6.775 -10.588 1.00 22.17 C
ATOM 3872 CD GLU A 505 14.805 -6.971 -10.357 1.00 22.97 C
ATOM 3873 OE1 GLU A 505 15.209 -7.035 -9.171 1.00 24.47 O
ATOM 3874 OE2 GLU A 505 15.569 -7.060 -11.344 1.00 24.99 O
ATOM 3875 N VAL A 506 10.430 -5.168 -10.424 1.00 19.39 N
ATOM 3876 CA VAL A 506 10.087 -4.004 -9.622 1.00 18.53 C
ATOM 3877 C VAL A 506 11.089 -3.938 -8.475 1.00 18.20 C
ATOM 3878 O VAL A 506 11.194 -4.871 -7.677 1.00 17.57 O
ATOM 3879 CB VAL A 506 8.633 -4.091 -9.087 1.00 18.66 C
ATOM 3880 CG1 VAL A 506 8.366 -3.020 -8.039 1.00 18.34 C
ATOM 3881 CG2 VAL A 506 7.637 -3.971 -10.236 1.00 18.05 C
ATOM 3882 N HIS A 507 11.855 -2.854 -8.430 1.00 18.09 N
ATOM 3883 CA HIS A 507 12.797 -2.637 -7.339 1.00 18.24 C
ATOM 3884 C HIS A 507 12.102 -1.890 -6.207 1.00 18.31 C
ATOM 3885 O HIS A 507 11.186 -1.101 -6.439 1.00 17.92 O
ATOM 3886 CB HIS A 507 14.030 -1.877 -7.828 1.00 18.58 C
ATOM 3887 CG HIS A 507 14.900 -2.680 -8.746 1.00 19.23 C
ATOM 3888 ND1 HIS A 507 14.697 -2.730 -10.108 1.00 20.44 N
ATOM 3889 CD2 HIS A 507 15.968 -3.473 -8.496 1.00 20.66 C
ATOM 3890 CE1 HIS A 507 15.603 -3.519 -10.658 1.00 20.33 C
ATOM 3891 NE2 HIS A 507 16.390 -3.978 -9.702 1.00 21.45 N
ATOM 3892 N TYR A 508 12.543 -2.152 -4.984 1.00 18.29 N
ATOM 3893 CA TYR A 508 11.939 -1.567 -3.790 1.00 18.91 C
ATOM 3894 C TYR A 508 13.010 -1.438 -2.720 1.00 18.77 C
ATOM 3895 O TYR A 508 14.058 -2.082 -2.802 1.00 18.91 O
ATOM 3896 CB TYR A 508 10.785 -2.444 -3.279 1.00 19.08 C
ATOM 3897 CG TYR A 508 11.210 -3.850 -2.904 1.00 19.64 C
ATOM 3898 CD1 TYR A 508 11.343 -4.843 -3.877 1.00 19.51 C
ATOM 3899 CD2 TYR A 508 11.487 -4.186 -1.576 1.00 19.26 C
ATOM 3900 CE1 TYR A 508 11.743 -6.131 -3.538 1.00 19.73 C
ATOM 3901 CE2 TYR A 508 11.884 -5.473 -1.227 1.00 20.13 C
ATOM 3902 CZ TYR A 508 12.006 -6.439 -2.213 1.00 20.03 C
ATOM 3903 OH TYR A 508 12.402 -7.712 -1.878 1.00 21.56 O
ATOM 3904 N VAL A 509 12.744 -0.609 -1.717 1.00 18.80 N
ATOM 3905 CA VAL A 509 13.685 -0.421 -0.619 1.00 18.79 C
ATOM 3906 C VAL A 509 13.411 -1.483 0.438 1.00 18.43 C
ATOM 3907 O VAL A 509 12.344 -1.498 1.055 1.00 18.75 O
ATOM 3908 CB VAL A 509 13.593 1.003 -0.014 1.00 18.92 C
ATOM 3909 CG1 VAL A 509 14.606 1.181 1.124 1.00 19.87 C
ATOM 3910 CG2 VAL A 509 13.818 2.059 -1.094 1.00 20.13 C
ATOM 3911 N ASP A 510 14.370 -2.384 0.624 1.00 17.62 N
ATOM 3912 CA ASP A 510 14.244 -3.416 1.641 1.00 17.42 C
ATOM 3913 C ASP A 510 14.642 -2.876 3.012 1.00 16.67 C
ATOM 3914 O ASP A 510 15.380 -1.893 3.106 1.00 16.92 O
ATOM 3915 CB ASP A 510 15.084 -4.637 1.286 1.00 17.77 C
ATOM 3916 CG ASP A 510 14.758 -5.826 2.160 1.00 18.50 C
ATOM 3917 OD1 ASP A 510 13.554 -6.114 2.350 1.00 19.80 O
ATOM 3918 OD2 ASP A 510 15.702 -6.441 2.687 1.00 20.80 O
ATOM 3919 N ASN A 511 14.150 -3.516 4.069 1.00 15.56 N
ATOM 3920 CA ASN A 511 14.399 -3.037 5.426 1.00 14.82 C
ATOM 3921 C ASN A 511 15.245 -3.975 6.290 1.00 14.53 C
ATOM 3922 O ASN A 511 15.330 -3.794 7.512 1.00 13.75 O
ATOM 3923 CB ASN A 511 13.072 -2.698 6.124 1.00 14.36 C
ATOM 3924 CG ASN A 511 12.260 -3.934 6.483 1.00 14.93 C
ATOM 3925 OD1 ASN A 511 12.342 -4.970 5.818 1.00 15.08 O
ATOM 3926 ND2 ASN A 511 11.473 -3.827 7.549 1.00 13.89 N
ATOM 3927 N GLN A 512 15.882 -4.968 5.666 1.00 14.27 N
ATOM 3928 CA GLN A 512 16.723 -5.899 6.421 1.00 14.43 C
ATOM 3929 C GLN A 512 17.845 -5.186 7.177 1.00 14.14 C
ATOM 3930 O GLN A 512 18.223 -5.613 8.270 1.00 13.77 O
ATOM 3931 CB GLN A 512 17.297 -7.010 5.530 1.00 14.92 C
ATOM 3932 CG GLN A 512 18.045 -8.117 6.303 1.00 16.13 C
ATOM 3933 CD GLN A 512 17.147 -8.946 7.225 1.00 17.74 C
ATOM 3934 OE1 GLN A 512 16.072 -9.406 6.830 1.00 18.25 O
ATOM 3935 NE2 GLN A 512 17.602 -9.152 8.459 1.00 17.84 N
ATOM 3936 N ASP A 513 18.365 -4.100 6.604 1.00 13.97 N
ATOM 3937 CA ASP A 513 19.422 -3.326 7.264 1.00 14.18 C
ATOM 3938 C ASP A 513 18.953 -2.712 8.591 1.00 13.94 C
ATOM 3939 O ASP A 513 19.728 -2.605 9.546 1.00 13.56 O
ATOM 3940 CB ASP A 513 20.043 -2.270 6.322 1.00 14.71 C
ATOM 3941 CG ASP A 513 19.044 -1.216 5.840 1.00 15.84 C
ATOM 3942 OD1 ASP A 513 17.822 -1.471 5.826 1.00 17.13 O
ATOM 3943 OD2 ASP A 513 19.497 -0.114 5.451 1.00 18.88 O
ATOM 3944 N CYS A 514 17.679 -2.337 8.650 1.00 13.38 N
ATOM 3945 CA CYS A 514 17.110 -1.787 9.879 1.00 12.74 C
ATOM 3946 C CYS A 514 16.971 -2.888 10.926 1.00 12.12 C
ATOM 3947 O CYS A 514 17.292 -2.694 12.102 1.00 11.76 O
ATOM 3948 CB CYS A 514 15.769 -1.120 9.597 1.00 13.02 C
ATOM 3949 SG CYS A 514 15.177 -0.129 10.981 1.00 14.26 S
ATOM 3950 N ILE A 515 16.512 -4.054 10.482 1.00 11.34 N
ATOM 3951 CA ILE A 515 16.437 -5.230 11.343 1.00 11.33 C
ATOM 3952 C ILE A 515 17.822 -5.593 11.898 1.00 11.53 C
ATOM 3953 O ILE A 515 17.974 -5.763 13.104 1.00 11.60 O
ATOM 3954 CB ILE A 515 15.785 -6.414 10.603 1.00 11.46 C
ATOM 3955 CG1 ILE A 515 14.318 -6.077 10.309 1.00 11.05 C
ATOM 3956 CG2 ILE A 515 15.897 -7.712 11.417 1.00 11.41 C
ATOM 3957 CD1 ILE A 515 13.675 -6.972 9.285 1.00 13.29 C
ATOM 3958 N ASP A 516 18.828 -5.660 11.024 1.00 11.94 N
ATOM 3959 CA ASP A 516 20.200 -5.974 11.456 1.00 12.52 C
ATOM 3960 C ASP A 516 20.759 -4.963 12.460 1.00 11.88 C
ATOM 3961 O ASP A 516 21.415 -5.348 13.423 1.00 12.14 O
ATOM 3962 CB ASP A 516 21.144 -6.107 10.259 1.00 13.07 C
ATOM 3963 CG ASP A 516 20.792 -7.279 9.354 1.00 14.73 C
ATOM 3964 OD1 ASP A 516 19.994 -8.153 9.753 1.00 17.41 O
ATOM 3965 OD2 ASP A 516 21.331 -7.324 8.231 1.00 18.40 O
ATOM 3966 N LEU A 517 20.490 -3.676 12.242 1.00 11.60 N
ATOM 3967 CA LEU A 517 20.883 -2.643 13.208 1.00 11.33 C
ATOM 3968 C LEU A 517 20.377 -2.991 14.609 1.00 10.86 C
ATOM 3969 O LEU A 517 21.087 -2.819 15.600 1.00 10.19 O
ATOM 3970 CB LEU A 517 20.351 -1.266 12.785 1.00 11.25 C
ATOM 3971 CG LEU A 517 20.436 -0.123 13.808 1.00 12.11 C
ATOM 3972 CD1 LEU A 517 21.878 0.226 14.144 1.00 13.05 C
ATOM 3973 CD2 LEU A 517 19.707 1.115 13.305 1.00 11.82 C
ATOM 3974 N ILE A 518 19.149 -3.493 14.674 1.00 10.53 N
ATOM 3975 CA ILE A 518 18.510 -3.787 15.949 1.00 11.08 C
ATOM 3976 C ILE A 518 18.965 -5.118 16.559 1.00 11.38 C
ATOM 3977 O ILE A 518 19.291 -5.177 17.755 1.00 11.46 O
ATOM 3978 CB ILE A 518 16.959 -3.717 15.826 1.00 11.11 C
ATOM 3979 CG1 ILE A 518 16.531 -2.296 15.408 1.00 10.98 C
ATOM 3980 CG2 ILE A 518 16.291 -4.147 17.137 1.00 11.41 C
ATOM 3981 CD1 ILE A 518 15.096 -2.172 14.883 1.00 11.37 C
ATOM 3982 N GLU A 519 19.006 -6.173 15.746 1.00 11.78 N
ATOM 3983 CA GLU A 519 19.107 -7.542 16.280 1.00 12.88 C
ATOM 3984 C GLU A 519 20.408 -8.299 15.979 1.00 12.87 C
ATOM 3985 O GLU A 519 20.540 -9.463 16.366 1.00 12.98 O
ATOM 3986 CB GLU A 519 17.905 -8.390 15.827 1.00 12.89 C
ATOM 3987 CG GLU A 519 17.938 -8.724 14.345 1.00 13.99 C
ATOM 3988 CD GLU A 519 16.922 -9.773 13.918 1.00 13.91 C
ATOM 3989 OE1 GLU A 519 17.254 -10.531 12.985 1.00 16.56 O
ATOM 3990 OE2 GLU A 519 15.806 -9.834 14.479 1.00 13.79 O
ATOM 3991 N ALA A 520 21.352 -7.669 15.283 1.00 13.02 N
ATOM 3992 CA ALA A 520 22.608 -8.354 14.928 1.00 13.37 C
ATOM 3993 C ALA A 520 23.353 -8.846 16.166 1.00 13.62 C
ATOM 3994 O ALA A 520 23.351 -8.189 17.207 1.00 13.36 O
ATOM 3995 CB ALA A 520 23.502 -7.460 14.098 1.00 13.36 C
ATOM 3996 N ARG A 521 23.984 -10.012 16.047 1.00 13.98 N
ATOM 3997 CA ARG A 521 24.741 -10.574 17.162 1.00 14.61 C
ATOM 3998 C ARG A 521 25.900 -9.668 17.552 1.00 14.53 C
ATOM 3999 O ARG A 521 26.631 -9.176 16.689 1.00 15.03 O
ATOM 4000 CB ARG A 521 25.242 -11.984 16.835 1.00 14.48 C
ATOM 4001 CG ARG A 521 24.128 -13.011 16.705 1.00 15.85 C
ATOM 4002 CD ARG A 521 24.685 -14.417 16.580 1.00 16.98 C
ATOM 4003 NE ARG A 521 23.629 -15.423 16.514 1.00 19.94 N
ATOM 4004 CZ ARG A 521 23.183 -15.979 15.391 1.00 20.61 C
ATOM 4005 NH1 ARG A 521 23.696 -15.634 14.214 1.00 20.96 N
ATOM 4006 NH2 ARG A 521 22.219 -16.885 15.444 1.00 22.41 N
ATOM 4007 N LEU A 522 26.032 -9.446 18.860 1.00 14.82 N
ATOM 4008 CA LEU A 522 27.091 -8.635 19.484 1.00 14.89 C
ATOM 4009 C LEU A 522 27.011 -7.137 19.241 1.00 14.84 C
ATOM 4010 O LEU A 522 27.127 -6.351 20.181 1.00 15.14 O
ATOM 4011 CB LEU A 522 28.495 -9.140 19.109 1.00 15.21 C
ATOM 4012 CG LEU A 522 28.897 -10.540 19.563 1.00 16.06 C
ATOM 4013 CD1 LEU A 522 30.352 -10.775 19.216 1.00 17.73 C
ATOM 4014 CD2 LEU A 522 28.653 -10.756 21.058 1.00 16.74 C
ATOM 4015 N VAL A 523 26.827 -6.750 17.981 1.00 14.51 N
ATOM 4016 CA VAL A 523 26.903 -5.351 17.571 1.00 14.30 C
ATOM 4017 C VAL A 523 25.522 -4.690 17.450 1.00 14.03 C
ATOM 4018 O VAL A 523 25.422 -3.468 17.406 1.00 14.43 O
ATOM 4019 CB VAL A 523 27.693 -5.190 16.236 1.00 14.37 C
ATOM 4020 CG1 VAL A 523 29.132 -5.698 16.391 1.00 15.10 C
ATOM 4021 CG2 VAL A 523 26.997 -5.929 15.100 1.00 14.50 C
ATOM 4022 N GLY A 524 24.468 -5.500 17.379 1.00 13.49 N
ATOM 4023 CA GLY A 524 23.104 -4.977 17.287 1.00 12.96 C
ATOM 4024 C GLY A 524 22.690 -4.282 18.572 1.00 12.55 C
ATOM 4025 O GLY A 524 23.212 -4.583 19.647 1.00 12.33 O
ATOM 4026 N ILE A 525 21.737 -3.360 18.460 1.00 12.40 N
ATOM 4027 CA ILE A 525 21.294 -2.552 19.600 1.00 12.46 C
ATOM 4028 C ILE A 525 20.854 -3.403 20.799 1.00 12.19 C
ATOM 4029 O ILE A 525 21.224 -3.110 21.941 1.00 11.91 O
ATOM 4030 CB ILE A 525 20.183 -1.545 19.190 1.00 12.28 C
ATOM 4031 CG1 ILE A 525 20.727 -0.534 18.165 1.00 12.06 C
ATOM 4032 CG2 ILE A 525 19.610 -0.821 20.415 1.00 12.86 C
ATOM 4033 CD1 ILE A 525 19.665 0.394 17.563 1.00 12.75 C
ATOM 4034 N LEU A 526 20.080 -4.456 20.542 1.00 12.15 N
ATOM 4035 CA LEU A 526 19.608 -5.335 21.623 1.00 12.28 C
ATOM 4036 C LEU A 526 20.765 -5.995 22.390 1.00 12.42 C
ATOM 4037 O LEU A 526 20.734 -6.077 23.622 1.00 12.33 O
ATOM 4038 CB LEU A 526 18.642 -6.396 21.087 1.00 12.34 C
ATOM 4039 CG LEU A 526 17.331 -5.883 20.464 1.00 12.91 C
ATOM 4040 CD1 LEU A 526 16.519 -7.061 19.964 1.00 14.13 C
ATOM 4041 CD2 LEU A 526 16.524 -5.044 21.453 1.00 14.38 C
ATOM 4042 N ASP A 527 21.786 -6.441 21.662 1.00 12.56 N
ATOM 4043 CA ASP A 527 22.958 -7.066 22.286 1.00 13.02 C
ATOM 4044 C ASP A 527 23.856 -6.056 23.015 1.00 12.89 C
ATOM 4045 O ASP A 527 24.460 -6.385 24.045 1.00 13.00 O
ATOM 4046 CB ASP A 527 23.762 -7.881 21.260 1.00 13.54 C
ATOM 4047 CG ASP A 527 23.234 -9.321 21.092 1.00 14.74 C
ATOM 4048 OD1 ASP A 527 23.945 -10.147 20.477 1.00 16.60 O
ATOM 4049 OD2 ASP A 527 22.129 -9.645 21.582 1.00 17.23 O
ATOM 4050 N ILE A 528 23.937 -4.835 22.492 1.00 12.73 N
ATOM 4051 CA ILE A 528 24.672 -3.752 23.168 1.00 13.08 C
ATOM 4052 C ILE A 528 23.969 -3.392 24.481 1.00 13.39 C
ATOM 4053 O ILE A 528 24.620 -3.148 25.510 1.00 13.63 O
ATOM 4054 CB ILE A 528 24.844 -2.504 22.257 1.00 12.88 C
ATOM 4055 CG1 ILE A 528 25.725 -2.837 21.044 1.00 12.93 C
ATOM 4056 CG2 ILE A 528 25.466 -1.339 23.028 1.00 13.50 C
ATOM 4057 CD1 ILE A 528 25.788 -1.721 20.005 1.00 13.02 C
ATOM 4058 N LEU A 529 22.638 -3.379 24.445 1.00 13.23 N
ATOM 4059 CA LEU A 529 21.847 -3.151 25.650 1.00 13.57 C
ATOM 4060 C LEU A 529 22.062 -4.252 26.697 1.00 13.93 C
ATOM 4061 O LEU A 529 22.303 -3.955 27.875 1.00 14.41 O
ATOM 4062 CB LEU A 529 20.365 -3.003 25.299 1.00 13.24 C
ATOM 4063 CG LEU A 529 19.428 -2.511 26.407 1.00 12.86 C
ATOM 4064 CD1 LEU A 529 19.887 -1.184 27.022 1.00 13.61 C
ATOM 4065 CD2 LEU A 529 18.024 -2.386 25.833 1.00 13.19 C
ATOM 4066 N ASP A 530 21.985 -5.508 26.260 1.00 14.21 N
ATOM 4067 CA ASP A 530 22.292 -6.665 27.111 1.00 14.92 C
ATOM 4068 C ASP A 530 23.667 -6.523 27.758 1.00 15.52 C
ATOM 4069 O ASP A 530 23.815 -6.761 28.957 1.00 15.56 O
ATOM 4070 CB ASP A 530 22.260 -7.962 26.298 1.00 14.80 C
ATOM 4071 CG ASP A 530 20.849 -8.476 26.052 1.00 14.93 C
ATOM 4072 OD1 ASP A 530 19.866 -7.773 26.373 1.00 14.11 O
ATOM 4073 OD2 ASP A 530 20.728 -9.603 25.529 1.00 15.30 O
ATOM 4074 N GLU A 531 24.655 -6.124 26.956 1.00 16.10 N
ATOM 4075 CA GLU A 531 26.024 -5.896 27.429 1.00 17.31 C
ATOM 4076 C GLU A 531 26.044 -4.864 28.564 1.00 16.87 C
ATOM 4077 O GLU A 531 26.738 -5.048 29.570 1.00 16.62 O
ATOM 4078 CB GLU A 531 26.926 -5.467 26.260 1.00 17.30 C
ATOM 4079 CG GLU A 531 28.347 -5.041 26.648 1.00 18.98 C
ATOM 4080 CD GLU A 531 29.244 -4.726 25.448 1.00 19.83 C
ATOM 4081 OE1 GLU A 531 30.443 -4.443 25.681 1.00 24.25 O
ATOM 4082 OE2 GLU A 531 28.773 -4.758 24.283 1.00 23.51 O
ATOM 4083 N GLU A 532 25.266 -3.796 28.405 1.00 16.54 N
ATOM 4084 CA GLU A 532 25.158 -2.767 29.437 1.00 16.51 C
ATOM 4085 C GLU A 532 24.587 -3.302 30.752 1.00 16.71 C
ATOM 4086 O GLU A 532 25.110 -2.992 31.826 1.00 16.84 O
ATOM 4087 CB GLU A 532 24.324 -1.583 28.948 1.00 16.38 C
ATOM 4088 CG GLU A 532 24.505 -0.315 29.794 1.00 16.36 C
ATOM 4089 CD GLU A 532 25.907 0.265 29.705 1.00 17.27 C
ATOM 4090 OE1 GLU A 532 26.397 0.781 30.734 1.00 17.93 O
ATOM 4091 OE2 GLU A 532 26.517 0.209 28.611 1.00 16.30 O
ATOM 4092 N ASN A 533 23.527 -4.105 30.674 1.00 16.61 N
ATOM 4093 CA ASN A 533 22.928 -4.695 31.878 1.00 17.32 C
ATOM 4094 C ASN A 533 23.942 -5.509 32.678 1.00 17.78 C
ATOM 4095 O ASN A 533 23.819 -5.646 33.896 1.00 17.90 O
ATOM 4096 CB ASN A 533 21.742 -5.585 31.523 1.00 17.25 C
ATOM 4097 CG ASN A 533 20.496 -4.791 31.155 1.00 17.17 C
ATOM 4098 OD1 ASN A 533 20.214 -4.580 29.978 1.00 17.25 O
ATOM 4099 ND2 ASN A 533 19.743 -4.352 32.164 1.00 15.97 N
ATOM 4100 N ARG A 534 24.951 -6.020 31.977 1.00 18.31 N
ATOM 4101 CA ARG A 534 25.939 -6.932 32.559 1.00 19.15 C
ATOM 4102 C ARG A 534 27.217 -6.249 33.054 1.00 19.49 C
ATOM 4103 O ARG A 534 28.056 -6.888 33.695 1.00 19.74 O
ATOM 4104 CB ARG A 534 26.270 -8.047 31.562 1.00 19.18 C
ATOM 4105 CG ARG A 534 25.134 -9.045 31.400 1.00 20.39 C
ATOM 4106 CD ARG A 534 25.335 -9.952 30.209 1.00 22.85 C
ATOM 4107 NE ARG A 534 24.250 -10.924 30.114 1.00 25.27 N
ATOM 4108 CZ ARG A 534 23.780 -11.428 28.976 1.00 26.07 C
ATOM 4109 NH1 ARG A 534 22.787 -12.306 29.010 1.00 27.52 N
ATOM 4110 NH2 ARG A 534 24.291 -11.054 27.810 1.00 26.84 N
ATOM 4111 N LEU A 535 27.358 -4.958 32.764 1.00 19.86 N
ATOM 4112 CA LEU A 535 28.515 -4.182 33.212 1.00 20.43 C
ATOM 4113 C LEU A 535 28.448 -3.891 34.717 1.00 20.79 C
ATOM 4114 O LEU A 535 27.362 -3.917 35.306 1.00 20.82 O
ATOM 4115 CB LEU A 535 28.648 -2.885 32.399 1.00 20.35 C
ATOM 4116 CG LEU A 535 29.133 -3.015 30.949 1.00 20.41 C
ATOM 4117 CD1 LEU A 535 29.056 -1.678 30.230 1.00 20.88 C
ATOM 4118 CD2 LEU A 535 30.557 -3.586 30.865 1.00 21.63 C
ATOM 4119 N PRO A 536 29.613 -3.635 35.354 1.00 21.38 N
ATOM 4120 CA PRO A 536 29.635 -3.341 36.790 1.00 21.50 C
ATOM 4121 C PRO A 536 28.729 -2.170 37.178 1.00 21.54 C
ATOM 4122 O PRO A 536 28.012 -2.257 38.180 1.00 21.71 O
ATOM 4123 CB PRO A 536 31.105 -2.988 37.056 1.00 21.51 C
ATOM 4124 CG PRO A 536 31.857 -3.665 35.980 1.00 21.94 C
ATOM 4125 CD PRO A 536 30.969 -3.621 34.774 1.00 21.38 C
ATOM 4126 N GLN A 537 28.754 -1.100 36.382 1.00 21.40 N
ATOM 4127 CA GLN A 537 27.946 0.093 36.644 1.00 21.30 C
ATOM 4128 C GLN A 537 27.088 0.473 35.429 1.00 20.41 C
ATOM 4129 O GLN A 537 27.422 1.424 34.717 1.00 20.46 O
ATOM 4130 CB GLN A 537 28.843 1.274 37.049 1.00 21.69 C
ATOM 4131 CG GLN A 537 29.859 0.965 38.159 1.00 24.01 C
ATOM 4132 CD GLN A 537 29.216 0.685 39.511 1.00 26.83 C
ATOM 4133 OE1 GLN A 537 29.758 -0.077 40.318 1.00 28.88 O
ATOM 4134 NE2 GLN A 537 28.063 1.300 39.768 1.00 28.11 N
ATOM 4135 N PRO A 538 25.979 -0.262 35.191 1.00 19.69 N
ATOM 4136 CA PRO A 538 25.171 -0.031 33.981 1.00 19.12 C
ATOM 4137 C PRO A 538 24.665 1.408 33.866 1.00 18.72 C
ATOM 4138 O PRO A 538 24.260 2.009 34.867 1.00 18.47 O
ATOM 4139 CB PRO A 538 24.003 -1.004 34.147 1.00 19.15 C
ATOM 4140 CG PRO A 538 24.537 -2.082 35.031 1.00 19.49 C
ATOM 4141 CD PRO A 538 25.404 -1.340 36.016 1.00 19.45 C
ATOM 4142 N SER A 539 24.697 1.938 32.643 1.00 18.06 N
ATOM 4143 CA SER A 539 24.372 3.334 32.368 1.00 17.58 C
ATOM 4144 C SER A 539 23.685 3.486 31.010 1.00 17.34 C
ATOM 4145 O SER A 539 24.206 3.014 29.998 1.00 16.84 O
ATOM 4146 CB SER A 539 25.654 4.171 32.394 1.00 17.61 C
ATOM 4147 OG SER A 539 25.523 5.360 31.645 1.00 17.04 O
ATOM 4148 N ASP A 540 22.531 4.158 30.996 1.00 17.07 N
ATOM 4149 CA ASP A 540 21.804 4.454 29.753 1.00 17.04 C
ATOM 4150 C ASP A 540 22.677 5.248 28.774 1.00 16.98 C
ATOM 4151 O ASP A 540 22.669 4.988 27.571 1.00 16.37 O
ATOM 4152 CB ASP A 540 20.512 5.242 30.036 1.00 17.21 C
ATOM 4153 CG ASP A 540 19.486 4.447 30.842 1.00 18.75 C
ATOM 4154 OD1 ASP A 540 19.367 3.223 30.637 1.00 19.33 O
ATOM 4155 OD2 ASP A 540 18.778 5.065 31.669 1.00 18.99 O
ATOM 4156 N GLN A 541 23.427 6.214 29.301 1.00 16.75 N
ATOM 4157 CA GLN A 541 24.318 7.037 28.485 1.00 17.06 C
ATOM 4158 C GLN A 541 25.446 6.217 27.847 1.00 16.61 C
ATOM 4159 O GLN A 541 25.749 6.390 26.668 1.00 16.06 O
ATOM 4160 CB GLN A 541 24.890 8.205 29.303 1.00 17.33 C
ATOM 4161 CG GLN A 541 23.871 9.306 29.638 1.00 19.73 C
ATOM 4162 CD GLN A 541 23.048 9.050 30.906 1.00 22.04 C
ATOM 4163 OE1 GLN A 541 22.177 9.857 31.259 1.00 24.94 O
ATOM 4164 NE2 GLN A 541 23.321 7.944 31.599 1.00 22.27 N
ATOM 4165 N HIS A 542 26.058 5.327 28.630 1.00 16.52 N
ATOM 4166 CA HIS A 542 27.112 4.451 28.122 1.00 16.46 C
ATOM 4167 C HIS A 542 26.578 3.556 27.001 1.00 16.06 C
ATOM 4168 O HIS A 542 27.211 3.428 25.946 1.00 16.28 O
ATOM 4169 CB HIS A 542 27.720 3.610 29.249 1.00 17.09 C
ATOM 4170 CG HIS A 542 28.939 2.841 28.839 1.00 18.33 C
ATOM 4171 ND1 HIS A 542 28.888 1.523 28.442 1.00 19.35 N
ATOM 4172 CD2 HIS A 542 30.241 3.207 28.759 1.00 19.63 C
ATOM 4173 CE1 HIS A 542 30.106 1.107 28.141 1.00 20.30 C
ATOM 4174 NE2 HIS A 542 30.945 2.110 28.326 1.00 20.25 N
ATOM 4175 N PHE A 543 25.408 2.964 27.232 1.00 15.20 N
ATOM 4176 CA PHE A 543 24.717 2.162 26.217 1.00 14.68 C
ATOM 4177 C PHE A 543 24.497 2.976 24.945 1.00 14.22 C
ATOM 4178 O PHE A 543 24.824 2.522 23.846 1.00 13.89 O
ATOM 4179 CB PHE A 543 23.379 1.631 26.760 1.00 14.19 C
ATOM 4180 CG PHE A 543 22.351 1.348 25.691 1.00 13.81 C
ATOM 4181 CD1 PHE A 543 21.239 2.179 25.546 1.00 13.60 C
ATOM 4182 CD2 PHE A 543 22.500 0.264 24.826 1.00 13.62 C
ATOM 4183 CE1 PHE A 543 20.286 1.928 24.556 1.00 13.10 C
ATOM 4184 CE2 PHE A 543 21.552 0.006 23.829 1.00 13.93 C
ATOM 4185 CZ PHE A 543 20.443 0.841 23.697 1.00 13.26 C
ATOM 4186 N THR A 544 23.953 4.183 25.104 1.00 13.97 N
ATOM 4187 CA THR A 544 23.605 5.023 23.960 1.00 14.03 C
ATOM 4188 C THR A 544 24.848 5.434 23.171 1.00 14.45 C
ATOM 4189 O THR A 544 24.845 5.408 21.943 1.00 14.11 O
ATOM 4190 CB THR A 544 22.774 6.247 24.389 1.00 13.97 C
ATOM 4191 OG1 THR A 544 21.693 5.804 25.219 1.00 13.79 O
ATOM 4192 CG2 THR A 544 22.209 6.974 23.172 1.00 13.87 C
ATOM 4193 N SER A 545 25.911 5.788 23.887 1.00 14.90 N
ATOM 4194 CA SER A 545 27.185 6.124 23.260 1.00 15.66 C
ATOM 4195 C SER A 545 27.731 4.940 22.465 1.00 15.48 C
ATOM 4196 O SER A 545 28.206 5.113 21.342 1.00 15.92 O
ATOM 4197 CB SER A 545 28.184 6.600 24.317 1.00 15.89 C
ATOM 4198 OG SER A 545 27.755 7.838 24.862 1.00 17.80 O
ATOM 4199 N ALA A 546 27.626 3.743 23.039 1.00 15.67 N
ATOM 4200 CA ALA A 546 28.063 2.511 22.382 1.00 15.85 C
ATOM 4201 C ALA A 546 27.304 2.265 21.077 1.00 15.95 C
ATOM 4202 O ALA A 546 27.910 1.907 20.064 1.00 15.64 O
ATOM 4203 CB ALA A 546 27.929 1.323 23.322 1.00 15.91 C
ATOM 4204 N VAL A 547 25.989 2.485 21.100 1.00 15.82 N
ATOM 4205 CA VAL A 547 25.159 2.342 19.903 1.00 16.04 C
ATOM 4206 C VAL A 547 25.658 3.254 18.776 1.00 16.27 C
ATOM 4207 O VAL A 547 25.852 2.807 17.646 1.00 16.49 O
ATOM 4208 CB VAL A 547 23.656 2.604 20.212 1.00 15.89 C
ATOM 4209 CG1 VAL A 547 22.843 2.749 18.927 1.00 15.57 C
ATOM 4210 CG2 VAL A 547 23.088 1.488 21.076 1.00 16.06 C
ATOM 4211 N HIS A 548 25.881 4.528 19.080 1.00 16.52 N
ATOM 4212 CA HIS A 548 26.377 5.452 18.067 1.00 16.84 C
ATOM 4213 C HIS A 548 27.794 5.093 17.600 1.00 17.33 C
ATOM 4214 O HIS A 548 28.067 5.091 16.397 1.00 17.16 O
ATOM 4215 CB HIS A 548 26.288 6.899 18.556 1.00 16.60 C
ATOM 4216 CG HIS A 548 24.883 7.412 18.648 1.00 15.80 C
ATOM 4217 ND1 HIS A 548 24.320 7.844 19.830 1.00 16.59 N
ATOM 4218 CD2 HIS A 548 23.923 7.542 17.704 1.00 14.67 C
ATOM 4219 CE1 HIS A 548 23.075 8.226 19.607 1.00 14.29 C
ATOM 4220 NE2 HIS A 548 22.810 8.058 18.324 1.00 16.20 N
ATOM 4221 N GLN A 549 28.672 4.770 18.549 1.00 18.28 N
ATOM 4222 CA GLN A 549 30.070 4.426 18.253 1.00 19.43 C
ATOM 4223 C GLN A 549 30.185 3.175 17.380 1.00 19.76 C
ATOM 4224 O GLN A 549 30.935 3.164 16.396 1.00 19.72 O
ATOM 4225 CB GLN A 549 30.865 4.234 19.552 1.00 19.67 C
ATOM 4226 CG GLN A 549 32.303 3.735 19.360 1.00 22.26 C
ATOM 4227 CD GLN A 549 32.828 2.988 20.573 1.00 25.79 C
ATOM 4228 OE1 GLN A 549 32.235 2.939 21.704 1.00 30.69 O
ATOM 4229 NE2 GLN A 549 33.756 2.063 20.344 1.00 28.30 N
ATOM 4230 N LYS A 550 29.441 2.131 17.742 1.00 19.85 N
ATOM 4231 CA LYS A 550 29.507 0.853 17.028 1.00 20.53 C
ATOM 4232 C LYS A 550 28.786 0.883 15.677 1.00 20.40 C
ATOM 4233 O LYS A 550 28.977 -0.013 14.847 1.00 21.19 O
ATOM 4234 CB LYS A 550 28.998 -0.296 17.910 1.00 20.62 C
ATOM 4235 CG LYS A 550 30.027 -0.779 18.934 1.00 22.44 C
ATOM 4236 CD LYS A 550 29.386 -1.560 20.076 1.00 25.25 C
ATOM 4237 CE LYS A 550 30.407 -2.388 20.860 1.00 27.24 C
ATOM 4238 NZ LYS A 550 31.588 -1.605 21.331 1.00 28.92 N
ATOM 4239 N HIS A 551 27.977 1.916 15.450 1.00 20.19 N
ATOM 4240 CA HIS A 551 27.204 2.027 14.208 1.00 20.13 C
ATOM 4241 C HIS A 551 27.469 3.314 13.444 1.00 20.54 C
ATOM 4242 O HIS A 551 26.565 3.883 12.825 1.00 19.77 O
ATOM 4243 CB HIS A 551 25.711 1.861 14.487 1.00 19.68 C
ATOM 4244 CG HIS A 551 25.354 0.509 15.011 1.00 18.85 C
ATOM 4245 ND1 HIS A 551 25.251 -0.598 14.196 1.00 18.88 N
ATOM 4246 CD2 HIS A 551 25.103 0.077 16.269 1.00 18.67 C
ATOM 4247 CE1 HIS A 551 24.938 -1.651 14.928 1.00 17.59 C
ATOM 4248 NE2 HIS A 551 24.838 -1.268 16.188 1.00 18.93 N
ATOM 4249 N LYS A 552 28.725 3.756 13.486 1.00 21.42 N
ATOM 4250 CA LYS A 552 29.169 4.912 12.722 1.00 22.26 C
ATOM 4251 C LYS A 552 28.758 4.790 11.260 1.00 22.00 C
ATOM 4252 O LYS A 552 29.048 3.782 10.605 1.00 22.31 O
ATOM 4253 CB LYS A 552 30.690 5.060 12.828 1.00 22.69 C
ATOM 4254 CG LYS A 552 31.164 5.973 13.949 1.00 25.07 C
ATOM 4255 CD LYS A 552 31.486 7.378 13.426 1.00 27.74 C
ATOM 4256 CE LYS A 552 32.805 7.401 12.653 1.00 29.22 C
ATOM 4257 NZ LYS A 552 32.873 8.529 11.680 1.00 30.48 N
ATOM 4258 N ASP A 553 28.055 5.815 10.779 1.00 21.61 N
ATOM 4259 CA ASP A 553 27.640 5.950 9.377 1.00 21.28 C
ATOM 4260 C ASP A 553 26.449 5.088 8.942 1.00 20.38 C
ATOM 4261 O ASP A 553 25.987 5.218 7.811 1.00 20.38 O
ATOM 4262 CB ASP A 553 28.826 5.752 8.414 1.00 22.01 C
ATOM 4263 CG ASP A 553 29.906 6.807 8.583 1.00 23.54 C
ATOM 4264 OD1 ASP A 553 29.577 7.973 8.894 1.00 25.83 O
ATOM 4265 OD2 ASP A 553 31.092 6.463 8.389 1.00 26.46 O
ATOM 4266 N HIS A 554 25.946 4.223 9.824 1.00 19.08 N
ATOM 4267 CA HIS A 554 24.830 3.346 9.456 1.00 17.84 C
ATOM 4268 C HIS A 554 23.619 4.165 9.009 1.00 17.31 C
ATOM 4269 O HIS A 554 23.180 5.068 9.721 1.00 16.78 O
ATOM 4270 CB HIS A 554 24.444 2.417 10.612 1.00 17.51 C
ATOM 4271 CG HIS A 554 23.536 1.300 10.203 1.00 16.47 C
ATOM 4272 ND1 HIS A 554 23.905 -0.026 10.277 1.00 15.87 N
ATOM 4273 CD2 HIS A 554 22.279 1.314 9.699 1.00 14.59 C
ATOM 4274 CE1 HIS A 554 22.912 -0.780 9.841 1.00 14.31 C
ATOM 4275 NE2 HIS A 554 21.914 0.008 9.483 1.00 16.28 N
ATOM 4276 N PHE A 555 23.083 3.831 7.837 1.00 17.07 N
ATOM 4277 CA PHE A 555 21.975 4.572 7.221 1.00 17.20 C
ATOM 4278 C PHE A 555 20.702 4.636 8.075 1.00 16.63 C
ATOM 4279 O PHE A 555 19.931 5.594 7.976 1.00 16.63 O
ATOM 4280 CB PHE A 555 21.654 3.989 5.838 1.00 18.24 C
ATOM 4281 CG PHE A 555 20.408 4.551 5.208 1.00 19.63 C
ATOM 4282 CD1 PHE A 555 20.387 5.852 4.708 1.00 22.13 C
ATOM 4283 CD2 PHE A 555 19.260 3.768 5.096 1.00 21.37 C
ATOM 4284 CE1 PHE A 555 19.233 6.374 4.117 1.00 22.36 C
ATOM 4285 CE2 PHE A 555 18.100 4.277 4.506 1.00 22.74 C
ATOM 4286 CZ PHE A 555 18.087 5.585 4.018 1.00 22.10 C
ATOM 4287 N ARG A 556 20.496 3.626 8.916 1.00 15.48 N
ATOM 4288 CA ARG A 556 19.252 3.507 9.679 1.00 14.97 C
ATOM 4289 C ARG A 556 19.313 4.135 11.069 1.00 14.74 C
ATOM 4290 O ARG A 556 18.323 4.100 11.806 1.00 14.38 O
ATOM 4291 CB ARG A 556 18.829 2.040 9.787 1.00 14.80 C
ATOM 4292 CG ARG A 556 18.508 1.383 8.459 1.00 15.34 C
ATOM 4293 CD ARG A 556 17.227 1.919 7.853 1.00 16.83 C
ATOM 4294 NE ARG A 556 16.861 1.145 6.672 1.00 17.66 N
ATOM 4295 CZ ARG A 556 15.672 1.170 6.077 1.00 19.10 C
ATOM 4296 NH1 ARG A 556 14.689 1.937 6.540 1.00 19.25 N
ATOM 4297 NH2 ARG A 556 15.467 0.418 5.004 1.00 19.58 N
ATOM 4298 N LEU A 557 20.462 4.716 11.416 1.00 14.50 N
ATOM 4299 CA LEU A 557 20.648 5.319 12.737 1.00 14.48 C
ATOM 4300 C LEU A 557 21.044 6.789 12.643 1.00 14.97 C
ATOM 4301 O LEU A 557 21.867 7.160 11.805 1.00 14.63 O
ATOM 4302 CB LEU A 557 21.706 4.543 13.528 1.00 14.33 C
ATOM 4303 CG LEU A 557 21.996 4.988 14.965 1.00 13.88 C
ATOM 4304 CD1 LEU A 557 20.851 4.610 15.901 1.00 12.86 C
ATOM 4305 CD2 LEU A 557 23.311 4.397 15.462 1.00 14.63 C
ATOM 4306 N SER A 558 20.462 7.617 13.509 1.00 15.18 N
ATOM 4307 CA SER A 558 20.842 9.027 13.596 1.00 15.82 C
ATOM 4308 C SER A 558 20.840 9.525 15.048 1.00 16.17 C
ATOM 4309 O SER A 558 20.407 8.822 15.962 1.00 15.31 O
ATOM 4310 CB SER A 558 19.924 9.888 12.716 1.00 16.07 C
ATOM 4311 OG SER A 558 20.473 11.181 12.512 1.00 17.67 O
ATOM 4312 N ILE A 559 21.352 10.736 15.252 1.00 16.98 N
ATOM 4313 CA ILE A 559 21.342 11.376 16.566 1.00 17.32 C
ATOM 4314 C ILE A 559 20.135 12.321 16.659 1.00 17.78 C
ATOM 4315 O ILE A 559 19.726 12.898 15.647 1.00 17.86 O
ATOM 4316 CB ILE A 559 22.678 12.137 16.848 1.00 17.64 C
ATOM 4317 CG1 ILE A 559 23.018 13.088 15.700 1.00 17.37 C
ATOM 4318 CG2 ILE A 559 23.821 11.148 17.097 1.00 17.85 C
ATOM 4319 CD1 ILE A 559 24.224 13.989 15.959 1.00 17.29 C
ATOM 4320 N PRO A 560 19.548 12.469 17.863 1.00 17.96 N
ATOM 4321 CA PRO A 560 18.337 13.277 18.045 1.00 18.66 C
ATOM 4322 C PRO A 560 18.403 14.712 17.518 1.00 19.55 C
ATOM 4323 O PRO A 560 17.384 15.230 17.061 1.00 19.49 O
ATOM 4324 CB PRO A 560 18.151 13.289 19.563 1.00 18.50 C
ATOM 4325 CG PRO A 560 18.770 12.023 20.016 1.00 17.94 C
ATOM 4326 CD PRO A 560 19.974 11.848 19.131 1.00 17.86 C
ATOM 4327 N ARG A 561 19.569 15.352 17.583 1.00 20.61 N
ATOM 4328 CA ARG A 561 19.675 16.746 17.123 1.00 22.13 C
ATOM 4329 C ARG A 561 19.436 16.914 15.613 1.00 22.42 C
ATOM 4330 O ARG A 561 19.183 18.025 15.136 1.00 22.80 O
ATOM 4331 CB ARG A 561 20.984 17.412 17.579 1.00 22.18 C
ATOM 4332 CG ARG A 561 22.264 16.833 17.013 1.00 24.55 C
ATOM 4333 CD ARG A 561 23.402 17.846 17.145 1.00 28.60 C
ATOM 4334 NE ARG A 561 24.685 17.312 16.690 1.00 31.22 N
ATOM 4335 CZ ARG A 561 25.135 17.376 15.438 1.00 32.44 C
ATOM 4336 NH1 ARG A 561 24.410 17.958 14.485 1.00 33.75 N
ATOM 4337 NH2 ARG A 561 26.315 16.851 15.138 1.00 32.58 N
ATOM 4338 N LYS A 562 19.486 15.801 14.881 1.00 22.81 N
ATOM 4339 CA LYS A 562 19.197 15.784 13.444 1.00 23.23 C
ATOM 4340 C LYS A 562 17.724 15.486 13.138 1.00 23.17 C
ATOM 4341 O LYS A 562 17.348 15.316 11.974 1.00 23.09 O
ATOM 4342 CB LYS A 562 20.093 14.764 12.736 1.00 23.53 C
ATOM 4343 CG LYS A 562 21.550 14.825 13.162 1.00 24.99 C
ATOM 4344 CD LYS A 562 22.405 15.677 12.251 1.00 28.29 C
ATOM 4345 CE LYS A 562 23.249 14.795 11.340 1.00 29.40 C
ATOM 4346 NZ LYS A 562 24.614 15.355 11.147 1.00 30.44 N
ATOM 4347 N SER A 563 16.890 15.432 14.176 1.00 23.10 N
ATOM 4348 CA SER A 563 15.468 15.151 13.993 1.00 23.20 C
ATOM 4349 C SER A 563 14.749 16.214 13.174 1.00 23.62 C
ATOM 4350 O SER A 563 15.126 17.388 13.182 1.00 23.40 O
ATOM 4351 CB SER A 563 14.756 14.989 15.331 1.00 23.11 C
ATOM 4352 OG SER A 563 13.363 14.821 15.121 1.00 23.14 O
ATOM 4353 N LYS A 564 13.696 15.780 12.488 1.00 24.04 N
ATOM 4354 CA LYS A 564 12.836 16.668 11.718 1.00 24.56 C
ATOM 4355 C LYS A 564 11.929 17.490 12.635 1.00 24.53 C
ATOM 4356 O LYS A 564 11.442 18.555 12.248 1.00 24.65 O
ATOM 4357 CB LYS A 564 12.003 15.853 10.725 1.00 24.94 C
ATOM 4358 CG LYS A 564 12.847 15.020 9.765 1.00 26.42 C
ATOM 4359 CD LYS A 564 12.026 14.503 8.589 1.00 29.17 C
ATOM 4360 CE LYS A 564 12.931 13.918 7.515 1.00 29.85 C
ATOM 4361 NZ LYS A 564 12.235 13.806 6.198 1.00 31.23 N
ATOM 4362 N LEU A 565 11.721 16.995 13.855 1.00 24.44 N
ATOM 4363 CA LEU A 565 10.817 17.633 14.808 1.00 24.04 C
ATOM 4364 C LEU A 565 11.550 18.407 15.907 1.00 23.81 C
ATOM 4365 O LEU A 565 12.502 17.907 16.512 1.00 23.80 O
ATOM 4366 CB LEU A 565 9.859 16.602 15.419 1.00 24.23 C
ATOM 4367 CG LEU A 565 8.854 15.907 14.488 1.00 24.52 C
ATOM 4368 CD1 LEU A 565 8.117 14.812 15.235 1.00 25.21 C
ATOM 4369 CD2 LEU A 565 7.858 16.892 13.877 1.00 25.41 C
ATOM 4370 N ALA A 566 11.078 19.628 16.155 1.00 23.28 N
ATOM 4371 CA ALA A 566 11.643 20.519 17.164 1.00 22.85 C
ATOM 4372 C ALA A 566 11.786 19.862 18.538 1.00 22.42 C
ATOM 4373 O ALA A 566 12.806 20.023 19.209 1.00 22.22 O
ATOM 4374 CB ALA A 566 10.799 21.779 17.274 1.00 22.89 C
ATOM 4375 N ILE A 567 10.761 19.117 18.941 1.00 22.26 N
ATOM 4376 CA ILE A 567 10.698 18.514 20.278 1.00 22.39 C
ATOM 4377 C ILE A 567 11.914 17.630 20.613 1.00 22.21 C
ATOM 4378 O ILE A 567 12.240 17.430 21.784 1.00 21.83 O
ATOM 4379 CB ILE A 567 9.339 17.766 20.497 1.00 22.31 C
ATOM 4380 CG1 ILE A 567 9.099 17.475 21.985 1.00 22.98 C
ATOM 4381 CG2 ILE A 567 9.232 16.511 19.611 1.00 22.32 C
ATOM 4382 CD1 ILE A 567 7.636 17.317 22.372 1.00 22.98 C
ATOM 4383 N HIS A 568 12.599 17.137 19.582 1.00 22.16 N
ATOM 4384 CA HIS A 568 13.725 16.219 19.773 1.00 22.42 C
ATOM 4385 C HIS A 568 15.112 16.878 19.745 1.00 22.70 C
ATOM 4386 O HIS A 568 16.102 16.249 20.123 1.00 22.87 O
ATOM 4387 CB HIS A 568 13.659 15.087 18.743 1.00 22.46 C
ATOM 4388 CG HIS A 568 12.405 14.274 18.817 1.00 21.69 C
ATOM 4389 ND1 HIS A 568 11.654 13.962 17.705 1.00 22.47 N
ATOM 4390 CD2 HIS A 568 11.770 13.708 19.870 1.00 21.65 C
ATOM 4391 CE1 HIS A 568 10.608 13.244 18.071 1.00 20.63 C
ATOM 4392 NE2 HIS A 568 10.657 13.073 19.379 1.00 22.47 N
ATOM 4393 N ARG A 569 15.163 18.143 19.327 1.00 23.09 N
ATOM 4394 CA ARG A 569 16.419 18.857 19.029 1.00 23.55 C
ATOM 4395 C ARG A 569 17.367 19.058 20.211 1.00 23.08 C
ATOM 4396 O ARG A 569 18.563 19.265 20.007 1.00 23.50 O
ATOM 4397 CB ARG A 569 16.123 20.224 18.400 1.00 24.02 C
ATOM 4398 CG ARG A 569 15.258 20.176 17.151 1.00 26.00 C
ATOM 4399 CD ARG A 569 16.061 20.245 15.863 1.00 29.60 C
ATOM 4400 NE ARG A 569 15.176 20.462 14.719 1.00 31.99 N
ATOM 4401 CZ ARG A 569 14.665 21.643 14.373 1.00 33.44 C
ATOM 4402 NH1 ARG A 569 14.950 22.734 15.074 1.00 34.62 N
ATOM 4403 NH2 ARG A 569 13.865 21.737 13.320 1.00 34.33 N
ATOM 4404 N ASN A 570 16.834 19.027 21.431 1.00 22.42 N
ATOM 4405 CA ASN A 570 17.655 19.246 22.627 1.00 22.02 C
ATOM 4406 C ASN A 570 18.051 17.988 23.398 1.00 21.39 C
ATOM 4407 O ASN A 570 18.686 18.069 24.451 1.00 21.52 O
ATOM 4408 CB ASN A 570 17.005 20.283 23.554 1.00 22.37 C
ATOM 4409 CG ASN A 570 17.129 21.695 23.019 1.00 22.97 C
ATOM 4410 OD1 ASN A 570 18.118 22.040 22.370 1.00 24.23 O
ATOM 4411 ND2 ASN A 570 16.126 22.524 23.291 1.00 22.71 N
ATOM 4412 N ILE A 571 17.680 16.826 22.868 1.00 20.58 N
ATOM 4413 CA ILE A 571 18.148 15.553 23.409 1.00 19.76 C
ATOM 4414 C ILE A 571 19.622 15.369 23.033 1.00 19.66 C
ATOM 4415 O ILE A 571 19.993 15.492 21.863 1.00 19.54 O
ATOM 4416 CB ILE A 571 17.299 14.360 22.882 1.00 19.62 C
ATOM 4417 CG1 ILE A 571 15.806 14.584 23.162 1.00 19.54 C
ATOM 4418 CG2 ILE A 571 17.777 13.044 23.489 1.00 18.88 C
ATOM 4419 CD1 ILE A 571 14.864 13.635 22.397 1.00 19.60 C
ATOM 4420 N ARG A 572 20.458 15.094 24.030 1.00 19.67 N
ATOM 4421 CA ARG A 572 21.894 14.899 23.811 1.00 19.84 C
ATOM 4422 C ARG A 572 22.167 13.600 23.049 1.00 19.29 C
ATOM 4423 O ARG A 572 21.348 12.674 23.077 1.00 18.63 O
ATOM 4424 CB ARG A 572 22.647 14.912 25.146 1.00 20.29 C
ATOM 4425 CG ARG A 572 22.513 16.234 25.914 1.00 22.86 C
ATOM 4426 CD ARG A 572 22.966 16.113 27.360 1.00 27.14 C
ATOM 4427 NE ARG A 572 24.417 16.223 27.500 1.00 31.08 N
ATOM 4428 CZ ARG A 572 25.220 15.231 27.878 1.00 32.22 C
ATOM 4429 NH1 ARG A 572 24.725 14.033 28.171 1.00 32.52 N
ATOM 4430 NH2 ARG A 572 26.526 15.443 27.971 1.00 33.20 N
ATOM 4431 N ASP A 573 23.317 13.543 22.374 1.00 18.79 N
ATOM 4432 CA ASP A 573 23.739 12.353 21.624 1.00 18.75 C
ATOM 4433 C ASP A 573 23.692 11.054 22.442 1.00 18.12 C
ATOM 4434 O ASP A 573 23.359 9.998 21.903 1.00 18.15 O
ATOM 4435 CB ASP A 573 25.148 12.546 21.045 1.00 18.99 C
ATOM 4436 CG ASP A 573 25.186 13.528 19.879 1.00 20.44 C
ATOM 4437 OD1 ASP A 573 26.177 13.491 19.118 1.00 22.13 O
ATOM 4438 OD2 ASP A 573 24.240 14.333 19.714 1.00 20.77 O
ATOM 4439 N ASP A 574 24.027 11.129 23.730 1.00 17.56 N
ATOM 4440 CA ASP A 574 24.002 9.945 24.596 1.00 17.15 C
ATOM 4441 C ASP A 574 22.689 9.779 25.380 1.00 16.41 C
ATOM 4442 O ASP A 574 22.615 8.967 26.305 1.00 16.11 O
ATOM 4443 CB ASP A 574 25.225 9.904 25.536 1.00 17.65 C
ATOM 4444 CG ASP A 574 25.249 11.056 26.541 1.00 19.27 C
ATOM 4445 OD1 ASP A 574 26.171 11.080 27.389 1.00 21.73 O
ATOM 4446 OD2 ASP A 574 24.363 11.931 26.492 1.00 20.20 O
ATOM 4447 N GLU A 575 21.665 10.543 24.993 1.00 15.80 N
ATOM 4448 CA GLU A 575 20.348 10.483 25.634 1.00 15.84 C
ATOM 4449 C GLU A 575 19.268 9.957 24.693 1.00 14.42 C
ATOM 4450 O GLU A 575 18.109 9.833 25.082 1.00 13.88 O
ATOM 4451 CB GLU A 575 19.915 11.860 26.146 1.00 16.15 C
ATOM 4452 CG GLU A 575 20.793 12.471 27.215 1.00 18.48 C
ATOM 4453 CD GLU A 575 20.251 13.805 27.710 1.00 18.50 C
ATOM 4454 OE1 GLU A 575 20.387 14.076 28.922 1.00 23.58 O
ATOM 4455 OE2 GLU A 575 19.684 14.580 26.900 1.00 22.14 O
ATOM 4456 N GLY A 576 19.640 9.661 23.453 1.00 13.68 N
ATOM 4457 CA GLY A 576 18.669 9.147 22.502 1.00 12.81 C
ATOM 4458 C GLY A 576 19.256 8.775 21.163 1.00 12.13 C
ATOM 4459 O GLY A 576 20.418 9.054 20.880 1.00 12.01 O
ATOM 4460 N PHE A 577 18.437 8.134 20.341 1.00 11.92 N
ATOM 4461 CA PHE A 577 18.807 7.875 18.958 1.00 11.71 C
ATOM 4462 C PHE A 577 17.567 7.838 18.086 1.00 11.48 C
ATOM 4463 O PHE A 577 16.455 7.603 18.575 1.00 11.88 O
ATOM 4464 CB PHE A 577 19.655 6.595 18.803 1.00 11.84 C
ATOM 4465 CG PHE A 577 19.035 5.352 19.398 1.00 12.39 C
ATOM 4466 CD1 PHE A 577 17.873 4.803 18.862 1.00 13.22 C
ATOM 4467 CD2 PHE A 577 19.640 4.709 20.477 1.00 12.92 C
ATOM 4468 CE1 PHE A 577 17.301 3.646 19.407 1.00 13.25 C
ATOM 4469 CE2 PHE A 577 19.075 3.549 21.030 1.00 13.77 C
ATOM 4470 CZ PHE A 577 17.907 3.023 20.493 1.00 12.99 C
ATOM 4471 N ILE A 578 17.775 8.094 16.802 1.00 11.27 N
ATOM 4472 CA ILE A 578 16.734 7.979 15.796 1.00 11.20 C
ATOM 4473 C ILE A 578 16.940 6.675 15.026 1.00 10.90 C
ATOM 4474 O ILE A 578 18.063 6.353 14.618 1.00 10.93 O
ATOM 4475 CB ILE A 578 16.781 9.191 14.824 1.00 11.37 C
ATOM 4476 CG1 ILE A 578 16.390 10.478 15.557 1.00 11.27 C
ATOM 4477 CG2 ILE A 578 15.893 8.970 13.596 1.00 11.32 C
ATOM 4478 CD1 ILE A 578 16.665 11.736 14.752 1.00 11.82 C
ATOM 4479 N ILE A 579 15.852 5.931 14.838 1.00 10.89 N
ATOM 4480 CA ILE A 579 15.854 4.770 13.948 1.00 10.56 C
ATOM 4481 C ILE A 579 15.005 5.106 12.727 1.00 10.54 C
ATOM 4482 O ILE A 579 13.845 5.498 12.857 1.00 10.32 O
ATOM 4483 CB ILE A 579 15.288 3.495 14.634 1.00 10.43 C
ATOM 4484 CG1 ILE A 579 16.028 3.186 15.949 1.00 11.07 C
ATOM 4485 CG2 ILE A 579 15.277 2.301 13.648 1.00 11.00 C
ATOM 4486 CD1 ILE A 579 17.490 2.771 15.803 1.00 12.02 C
ATOM 4487 N ARG A 580 15.598 4.959 11.550 1.00 10.32 N
ATOM 4488 CA ARG A 580 14.908 5.235 10.301 1.00 11.65 C
ATOM 4489 C ARG A 580 14.107 4.000 9.909 1.00 11.29 C
ATOM 4490 O ARG A 580 14.493 3.238 9.020 1.00 11.84 O
ATOM 4491 CB ARG A 580 15.899 5.651 9.204 1.00 11.53 C
ATOM 4492 CG ARG A 580 16.620 6.972 9.487 1.00 13.58 C
ATOM 4493 CD ARG A 580 17.293 7.540 8.249 1.00 13.43 C
ATOM 4494 NE ARG A 580 17.864 8.863 8.521 1.00 17.66 N
ATOM 4495 CZ ARG A 580 19.148 9.107 8.773 1.00 18.85 C
ATOM 4496 NH1 ARG A 580 20.039 8.121 8.782 1.00 19.16 N
ATOM 4497 NH2 ARG A 580 19.546 10.353 9.013 1.00 19.71 N
ATOM 4498 N HIS A 581 13.000 3.798 10.615 1.00 11.18 N
ATOM 4499 CA HIS A 581 12.099 2.684 10.365 1.00 10.98 C
ATOM 4500 C HIS A 581 11.495 2.749 8.969 1.00 11.14 C
ATOM 4501 O HIS A 581 11.410 3.822 8.364 1.00 11.05 O
ATOM 4502 CB HIS A 581 10.985 2.667 11.408 1.00 10.94 C
ATOM 4503 CG HIS A 581 11.435 2.227 12.765 1.00 10.71 C
ATOM 4504 ND1 HIS A 581 11.544 3.090 13.833 1.00 11.63 N
ATOM 4505 CD2 HIS A 581 11.797 1.008 13.228 1.00 9.03 C
ATOM 4506 CE1 HIS A 581 11.952 2.422 14.897 1.00 8.65 C
ATOM 4507 NE2 HIS A 581 12.114 1.157 14.557 1.00 11.62 N
ATOM 4508 N PHE A 582 11.057 1.598 8.467 1.00 11.28 N
ATOM 4509 CA PHE A 582 10.414 1.550 7.151 1.00 11.99 C
ATOM 4510 C PHE A 582 9.207 2.490 7.111 1.00 12.12 C
ATOM 4511 O PHE A 582 8.896 3.067 6.066 1.00 12.70 O
ATOM 4512 CB PHE A 582 9.988 0.117 6.808 1.00 12.30 C
ATOM 4513 CG PHE A 582 8.709 -0.315 7.479 1.00 12.71 C
ATOM 4514 CD1 PHE A 582 7.501 -0.291 6.781 1.00 13.33 C
ATOM 4515 CD2 PHE A 582 8.706 -0.718 8.811 1.00 12.89 C
ATOM 4516 CE1 PHE A 582 6.310 -0.683 7.393 1.00 13.72 C
ATOM 4517 CE2 PHE A 582 7.514 -1.114 9.435 1.00 14.34 C
ATOM 4518 CZ PHE A 582 6.316 -1.094 8.718 1.00 13.76 C
ATOM 4519 N ALA A 583 8.547 2.643 8.261 1.00 12.38 N
ATOM 4520 CA ALA A 583 7.319 3.429 8.388 1.00 12.43 C
ATOM 4521 C ALA A 583 7.562 4.883 8.802 1.00 12.62 C
ATOM 4522 O ALA A 583 6.608 5.651 8.996 1.00 12.73 O
ATOM 4523 CB ALA A 583 6.359 2.747 9.369 1.00 12.49 C
ATOM 4524 N GLY A 584 8.831 5.256 8.935 1.00 12.54 N
ATOM 4525 CA GLY A 584 9.203 6.624 9.293 1.00 12.30 C
ATOM 4526 C GLY A 584 10.211 6.674 10.422 1.00 12.19 C
ATOM 4527 O GLY A 584 10.272 5.762 11.253 1.00 12.19 O
ATOM 4528 N ALA A 585 11.007 7.739 10.445 1.00 11.79 N
ATOM 4529 CA ALA A 585 11.993 7.934 11.508 1.00 11.48 C
ATOM 4530 C ALA A 585 11.294 8.150 12.848 1.00 11.52 C
ATOM 4531 O ALA A 585 10.292 8.875 12.934 1.00 11.76 O
ATOM 4532 CB ALA A 585 12.916 9.102 11.189 1.00 12.12 C
ATOM 4533 N VAL A 586 11.819 7.493 13.879 1.00 11.02 N
ATOM 4534 CA VAL A 586 11.329 7.650 15.243 1.00 10.54 C
ATOM 4535 C VAL A 586 12.512 7.958 16.149 1.00 10.86 C
ATOM 4536 O VAL A 586 13.519 7.251 16.126 1.00 10.28 O
ATOM 4537 CB VAL A 586 10.601 6.373 15.759 1.00 10.24 C
ATOM 4538 CG1 VAL A 586 10.137 6.567 17.198 1.00 10.30 C
ATOM 4539 CG2 VAL A 586 9.402 6.049 14.887 1.00 10.21 C
ATOM 4540 N CYS A 587 12.379 9.016 16.947 1.00 11.19 N
ATOM 4541 CA CYS A 587 13.416 9.388 17.905 1.00 11.03 C
ATOM 4542 C CYS A 587 13.075 8.815 19.277 1.00 10.81 C
ATOM 4543 O CYS A 587 12.001 9.090 19.820 1.00 10.32 O
ATOM 4544 CB CYS A 587 13.563 10.908 17.980 1.00 11.28 C
ATOM 4545 SG CYS A 587 14.912 11.425 19.063 1.00 13.67 S
ATOM 4546 N TYR A 588 13.986 7.999 19.802 1.00 10.51 N
ATOM 4547 CA TYR A 588 13.844 7.348 21.106 1.00 10.69 C
ATOM 4548 C TYR A 588 14.713 8.027 22.159 1.00 11.16 C
ATOM 4549 O TYR A 588 15.899 8.271 21.928 1.00 11.41 O
ATOM 4550 CB TYR A 588 14.249 5.873 21.007 1.00 10.40 C
ATOM 4551 CG TYR A 588 13.412 5.086 20.023 1.00 9.52 C
ATOM 4552 CD1 TYR A 588 13.826 4.917 18.698 1.00 9.76 C
ATOM 4553 CD2 TYR A 588 12.202 4.520 20.416 1.00 10.25 C
ATOM 4554 CE1 TYR A 588 13.043 4.202 17.785 1.00 9.21 C
ATOM 4555 CE2 TYR A 588 11.417 3.808 19.520 1.00 8.83 C
ATOM 4556 CZ TYR A 588 11.843 3.643 18.217 1.00 9.63 C
ATOM 4557 OH TYR A 588 11.063 2.932 17.342 1.00 9.74 O
ATOM 4558 N GLU A 589 14.107 8.344 23.295 1.00 11.70 N
ATOM 4559 CA GLU A 589 14.842 8.743 24.487 1.00 13.30 C
ATOM 4560 C GLU A 589 15.268 7.453 25.161 1.00 12.97 C
ATOM 4561 O GLU A 589 14.443 6.556 25.364 1.00 12.92 O
ATOM 4562 CB GLU A 589 13.950 9.557 25.426 1.00 13.26 C
ATOM 4563 CG GLU A 589 13.524 10.905 24.858 1.00 15.28 C
ATOM 4564 CD GLU A 589 12.388 11.563 25.640 1.00 15.93 C
ATOM 4565 OE1 GLU A 589 12.024 12.704 25.288 1.00 21.18 O
ATOM 4566 OE2 GLU A 589 11.856 10.951 26.591 1.00 20.36 O
ATOM 4567 N THR A 590 16.551 7.353 25.495 1.00 13.10 N
ATOM 4568 CA THR A 590 17.097 6.102 26.011 1.00 13.43 C
ATOM 4569 C THR A 590 17.155 5.992 27.543 1.00 14.28 C
ATOM 4570 O THR A 590 17.627 4.979 28.065 1.00 13.85 O
ATOM 4571 CB THR A 590 18.463 5.738 25.370 1.00 13.62 C
ATOM 4572 OG1 THR A 590 19.336 6.868 25.429 1.00 12.69 O
ATOM 4573 CG2 THR A 590 18.277 5.327 23.912 1.00 13.53 C
ATOM 4574 N THR A 591 16.676 7.016 28.260 1.00 15.14 N
ATOM 4575 C THR A 591 15.659 5.701 30.020 1.00 15.71 C
ATOM 4576 O THR A 591 14.626 5.501 29.375 1.00 16.24 O
ATOM 4577 CA ATHR A 591 16.541 6.915 29.712 0.50 15.55 C
ATOM 4578 CB ATHR A 591 15.922 8.191 30.324 0.50 15.64 C
ATOM 4579 OG1ATHR A 591 16.574 9.345 29.786 0.50 16.67 O
ATOM 4580 CG2ATHR A 591 16.070 8.194 31.841 0.50 14.69 C
ATOM 4582 CB BTHR A 591 15.915 8.164 30.392 0.50 15.78 C
ATOM 4583 OG1BTHR A 591 14.781 8.624 29.642 0.50 15.82 O
ATOM 4584 CG2BTHR A 591 16.932 9.275 30.525 0.50 16.43 C
ATOM 4585 N GLN A 592 16.080 4.894 30.988 1.00 15.98 N
ATOM 4586 CA GLN A 592 15.353 3.690 31.417 1.00 16.52 C
ATOM 4587 C GLN A 592 15.438 2.481 30.469 1.00 15.37 C
ATOM 4588 O GLN A 592 14.819 1.456 30.740 1.00 15.12 O
ATOM 4589 CB GLN A 592 13.880 3.995 31.758 1.00 16.72 C
ATOM 4590 CG GLN A 592 13.681 5.101 32.792 1.00 18.66 C
ATOM 4591 CD GLN A 592 12.220 5.355 33.104 1.00 19.00 C
ATOM 4592 OE1 GLN A 592 11.491 4.447 33.508 1.00 23.57 O
ATOM 4593 NE2 GLN A 592 11.785 6.594 32.926 1.00 23.09 N
ATOM 4594 N PHE A 593 16.201 2.580 29.379 1.00 14.75 N
ATOM 4595 CA PHE A 593 16.374 1.427 28.479 1.00 14.14 C
ATOM 4596 C PHE A 593 16.985 0.241 29.222 1.00 14.28 C
ATOM 4597 O PHE A 593 16.523 -0.889 29.078 1.00 14.02 O
ATOM 4598 CB PHE A 593 17.237 1.788 27.263 1.00 13.80 C
ATOM 4599 CG PHE A 593 16.450 2.086 26.002 1.00 13.35 C
ATOM 4600 CD1 PHE A 593 15.406 3.009 26.000 1.00 11.66 C
ATOM 4601 CD2 PHE A 593 16.782 1.452 24.799 1.00 12.90 C
ATOM 4602 CE1 PHE A 593 14.696 3.289 24.823 1.00 12.07 C
ATOM 4603 CE2 PHE A 593 16.076 1.728 23.620 1.00 12.27 C
ATOM 4604 CZ PHE A 593 15.036 2.654 23.635 1.00 12.73 C
ATOM 4605 N VAL A 594 18.012 0.508 30.030 1.00 14.54 N
ATOM 4606 CA VAL A 594 18.695 -0.547 30.788 1.00 15.32 C
ATOM 4607 C VAL A 594 17.748 -1.213 31.800 1.00 15.54 C
ATOM 4608 O VAL A 594 17.629 -2.439 31.819 1.00 15.33 O
ATOM 4609 CB VAL A 594 19.994 -0.030 31.463 1.00 15.12 C
ATOM 4610 CG1 VAL A 594 20.612 -1.097 32.376 1.00 15.73 C
ATOM 4611 CG2 VAL A 594 21.003 0.402 30.401 1.00 15.57 C
ATOM 4612 N GLU A 595 17.053 -0.419 32.615 1.00 16.27 N
ATOM 4613 CA GLU A 595 16.113 -1.021 33.572 1.00 17.70 C
ATOM 4614 C GLU A 595 14.962 -1.754 32.875 1.00 16.79 C
ATOM 4615 O GLU A 595 14.563 -2.842 33.305 1.00 16.96 O
ATOM 4616 CB GLU A 595 15.620 -0.024 34.637 1.00 17.90 C
ATOM 4617 CG GLU A 595 14.717 1.107 34.161 1.00 20.75 C
ATOM 4618 CD GLU A 595 14.130 1.920 35.317 1.00 20.84 C
ATOM 4619 OE1 GLU A 595 13.704 3.067 35.080 1.00 25.15 O
ATOM 4620 OE2 GLU A 595 14.092 1.421 36.466 1.00 26.26 O
ATOM 4621 N LYS A 596 14.466 -1.182 31.778 1.00 15.92 N
ATOM 4622 CA LYS A 596 13.361 -1.790 31.025 1.00 15.28 C
ATOM 4623 C LYS A 596 13.761 -3.055 30.257 1.00 15.22 C
ATOM 4624 O LYS A 596 12.903 -3.835 29.850 1.00 15.41 O
ATOM 4625 CB LYS A 596 12.711 -0.770 30.091 1.00 15.25 C
ATOM 4626 CG LYS A 596 11.862 0.253 30.827 1.00 14.21 C
ATOM 4627 CD LYS A 596 11.282 1.291 29.882 1.00 12.91 C
ATOM 4628 CE LYS A 596 10.314 2.209 30.622 1.00 12.20 C
ATOM 4629 NZ LYS A 596 9.680 3.213 29.704 1.00 12.68 N
ATOM 4630 N ASN A 597 15.061 -3.261 30.078 1.00 15.20 N
ATOM 4631 CA ASN A 597 15.553 -4.461 29.403 1.00 15.26 C
ATOM 4632 C ASN A 597 15.677 -5.684 30.319 1.00 15.80 C
ATOM 4633 O ASN A 597 15.946 -6.791 29.849 1.00 15.27 O
ATOM 4634 CB ASN A 597 16.888 -4.174 28.718 1.00 14.99 C
ATOM 4635 CG ASN A 597 17.310 -5.287 27.774 1.00 14.34 C
ATOM 4636 OD1 ASN A 597 16.509 -5.780 26.976 1.00 12.56 O
ATOM 4637 ND2 ASN A 597 18.573 -5.690 27.864 1.00 15.04 N
ATOM 4638 N ASN A 598 15.466 -5.478 31.618 1.00 16.32 N
ATOM 4639 CA ASN A 598 15.635 -6.540 32.609 1.00 17.49 C
ATOM 4640 C ASN A 598 14.306 -7.086 33.120 1.00 18.09 C
ATOM 4641 O ASN A 598 13.583 -6.405 33.863 1.00 18.09 O
ATOM 4642 CB ASN A 598 16.504 -6.055 33.777 1.00 17.53 C
ATOM 4643 CG ASN A 598 16.961 -7.189 34.683 1.00 18.27 C
ATOM 4644 OD1 ASN A 598 16.607 -8.351 34.478 1.00 18.32 O
ATOM 4645 ND2 ASN A 598 17.767 -6.852 35.689 1.00 20.60 N
ATOM 4646 N ASP A 599 14.008 -8.320 32.721 1.00 19.01 N
ATOM 4647 CA ASP A 599 12.758 -8.999 33.060 1.00 20.53 C
ATOM 4648 C ASP A 599 12.874 -9.880 34.313 1.00 20.72 C
ATOM 4649 O ASP A 599 11.893 -10.506 34.732 1.00 20.83 O
ATOM 4650 CB ASP A 599 12.310 -9.858 31.874 1.00 21.08 C
ATOM 4651 CG ASP A 599 10.805 -9.836 31.666 1.00 22.78 C
ATOM 4652 OD1 ASP A 599 10.141 -8.883 32.123 1.00 26.09 O
ATOM 4653 OD2 ASP A 599 10.285 -10.777 31.032 1.00 26.30 O
ATOM 4654 N ALA A 600 14.066 -9.926 34.903 1.00 21.11 N
ATOM 4655 CA ALA A 600 14.335 -10.814 36.038 1.00 21.23 C
ATOM 4656 C ALA A 600 13.561 -10.423 37.295 1.00 21.39 C
ATOM 4657 O ALA A 600 13.308 -9.243 37.544 1.00 21.13 O
ATOM 4658 CB ALA A 600 15.836 -10.881 36.333 1.00 21.27 C
ATOM 4659 N LEU A 601 13.168 -11.432 38.067 1.00 21.67 N
ATOM 4660 CA LEU A 601 12.562 -11.212 39.373 1.00 21.88 C
ATOM 4661 C LEU A 601 13.456 -11.858 40.420 1.00 22.34 C
ATOM 4662 O LEU A 601 13.841 -13.027 40.286 1.00 21.81 O
ATOM 4663 CB LEU A 601 11.143 -11.794 39.433 1.00 21.92 C
ATOM 4664 CG LEU A 601 10.311 -11.534 40.699 1.00 21.74 C
ATOM 4665 CD1 LEU A 601 9.912 -10.064 40.831 1.00 21.64 C
ATOM 4666 CD2 LEU A 601 9.073 -12.422 40.743 1.00 21.91 C
ATOM 4667 N HIS A 602 13.797 -11.085 41.448 1.00 22.81 N
ATOM 4668 CA HIS A 602 14.619 -11.580 42.544 1.00 23.79 C
ATOM 4669 C HIS A 602 13.959 -12.792 43.192 1.00 23.97 C
ATOM 4670 O HIS A 602 12.742 -12.822 43.373 1.00 23.92 O
ATOM 4671 CB HIS A 602 14.879 -10.475 43.573 1.00 23.98 C
ATOM 4672 CG HIS A 602 15.895 -9.467 43.127 1.00 25.68 C
ATOM 4673 ND1 HIS A 602 15.568 -8.167 42.808 1.00 26.93 N
ATOM 4674 CD2 HIS A 602 17.231 -9.577 42.928 1.00 26.81 C
ATOM 4675 CE1 HIS A 602 16.658 -7.517 42.440 1.00 27.05 C
ATOM 4676 NE2 HIS A 602 17.681 -8.350 42.504 1.00 27.61 N
ATOM 4677 N MET A 603 14.771 -13.791 43.525 1.00 24.64 N
ATOM 4678 CA MET A 603 14.264 -15.045 44.083 1.00 25.26 C
ATOM 4679 C MET A 603 13.425 -14.867 45.342 1.00 25.01 C
ATOM 4680 O MET A 603 12.471 -15.617 45.563 1.00 25.07 O
ATOM 4681 CB MET A 603 15.404 -16.036 44.333 1.00 26.15 C
ATOM 4682 CG MET A 603 15.451 -17.150 43.312 1.00 28.01 C
ATOM 4683 SD MET A 603 14.003 -18.223 43.441 1.00 33.99 S
ATOM 4684 CE MET A 603 14.139 -19.148 41.913 1.00 30.39 C
ATOM 4685 N SER A 604 13.779 -13.873 46.151 1.00 24.68 N
ATOM 4686 CA SER A 604 13.029 -13.538 47.364 1.00 24.62 C
ATOM 4687 C SER A 604 11.553 -13.280 47.055 1.00 24.45 C
ATOM 4688 O SER A 604 10.664 -13.775 47.756 1.00 24.09 O
ATOM 4689 CB SER A 604 13.648 -12.319 48.057 1.00 24.76 C
ATOM 4690 OG SER A 604 13.688 -11.193 47.192 1.00 25.72 O
ATOM 4691 N LEU A 605 11.310 -12.516 45.992 1.00 23.97 N
ATOM 4692 CA LEU A 605 9.957 -12.164 45.563 1.00 24.04 C
ATOM 4693 C LEU A 605 9.246 -13.326 44.867 1.00 24.17 C
ATOM 4694 O LEU A 605 8.045 -13.521 45.060 1.00 23.90 O
ATOM 4695 CB LEU A 605 9.984 -10.915 44.668 1.00 23.72 C
ATOM 4696 CG LEU A 605 10.605 -9.652 45.290 1.00 23.80 C
ATOM 4697 CD1 LEU A 605 10.885 -8.577 44.236 1.00 23.57 C
ATOM 4698 CD2 LEU A 605 9.738 -9.096 46.414 1.00 23.24 C
ATOM 4699 N GLU A 606 9.985 -14.088 44.060 1.00 24.46 N
ATOM 4700 CA GLU A 606 9.441 -15.281 43.409 1.00 25.25 C
ATOM 4701 C GLU A 606 9.009 -16.309 44.455 1.00 24.82 C
ATOM 4702 O GLU A 606 7.920 -16.874 44.360 1.00 24.84 O
ATOM 4703 CB GLU A 606 10.463 -15.891 42.444 1.00 25.14 C
ATOM 4704 CG GLU A 606 9.911 -17.019 41.574 1.00 26.50 C
ATOM 4705 CD GLU A 606 10.960 -17.645 40.664 1.00 27.12 C
ATOM 4706 OE1 GLU A 606 10.734 -18.785 40.201 1.00 29.55 O
ATOM 4707 OE2 GLU A 606 12.006 -17.007 40.405 1.00 30.23 O
ATOM 4708 N SER A 607 9.863 -16.529 45.454 1.00 24.82 N
ATOM 4709 CA SER A 607 9.578 -17.473 46.542 1.00 24.67 C
ATOM 4710 C SER A 607 8.351 -17.065 47.350 1.00 24.26 C
ATOM 4711 O SER A 607 7.537 -17.916 47.714 1.00 24.46 O
ATOM 4712 CB SER A 607 10.795 -17.628 47.461 1.00 24.81 C
ATOM 4713 OG SER A 607 11.841 -18.320 46.795 1.00 26.37 O
ATOM 4714 N LEU A 608 8.224 -15.764 47.615 1.00 23.60 N
ATOM 4715 CA LEU A 608 7.093 -15.210 48.359 1.00 23.16 C
ATOM 4716 C LEU A 608 5.755 -15.562 47.709 1.00 23.06 C
ATOM 4717 O LEU A 608 4.850 -16.087 48.364 1.00 22.93 O
ATOM 4718 CB LEU A 608 7.229 -13.685 48.473 1.00 22.89 C
ATOM 4719 CG LEU A 608 6.053 -12.880 49.044 1.00 22.71 C
ATOM 4720 CD1 LEU A 608 5.935 -13.052 50.561 1.00 22.78 C
ATOM 4721 CD2 LEU A 608 6.186 -11.415 48.684 1.00 22.96 C
ATOM 4722 N ILE A 609 5.644 -15.274 46.417 1.00 22.89 N
ATOM 4723 CA ILE A 609 4.393 -15.474 45.697 1.00 22.93 C
ATOM 4724 C ILE A 609 4.124 -16.952 45.367 1.00 23.32 C
ATOM 4725 O ILE A 609 2.977 -17.397 45.428 1.00 23.17 O
ATOM 4726 CB ILE A 609 4.294 -14.528 44.447 1.00 22.69 C
ATOM 4727 CG1 ILE A 609 2.838 -14.339 44.007 1.00 22.36 C
ATOM 4728 CG2 ILE A 609 5.221 -14.969 43.312 1.00 22.87 C
ATOM 4729 CD1 ILE A 609 2.032 -13.423 44.921 1.00 21.25 C
ATOM 4730 N CYS A 610 5.177 -17.709 45.052 1.00 23.80 N
ATOM 4731 CA CYS A 610 5.033 -19.138 44.735 1.00 24.76 C
ATOM 4732 C CYS A 610 4.558 -19.947 45.938 1.00 24.70 C
ATOM 4733 O CYS A 610 3.975 -21.021 45.777 1.00 24.90 O
ATOM 4734 CB CYS A 610 6.343 -19.725 44.204 1.00 24.86 C
ATOM 4735 SG CYS A 610 6.747 -19.214 42.528 1.00 27.47 S
ATOM 4736 N GLU A 611 4.808 -19.415 47.132 1.00 24.77 N
ATOM 4737 CA GLU A 611 4.418 -20.055 48.386 1.00 25.04 C
ATOM 4738 C GLU A 611 3.198 -19.391 49.023 1.00 24.56 C
ATOM 4739 O GLU A 611 2.976 -19.503 50.233 1.00 24.68 O
ATOM 4740 CB GLU A 611 5.597 -20.064 49.365 1.00 25.40 C
ATOM 4741 CG GLU A 611 6.688 -21.064 48.996 1.00 27.33 C
ATOM 4742 CD GLU A 611 8.041 -20.734 49.606 1.00 29.52 C
ATOM 4743 OE1 GLU A 611 8.097 -19.974 50.598 1.00 30.77 O
ATOM 4744 OE2 GLU A 611 9.058 -21.244 49.087 1.00 31.27 O
ATOM 4745 N SER A 612 2.399 -18.703 48.207 1.00 23.90 N
ATOM 4746 CA SER A 612 1.154 -18.118 48.692 1.00 23.15 C
ATOM 4747 C SER A 612 0.275 -19.215 49.277 1.00 23.14 C
ATOM 4748 O SER A 612 0.307 -20.358 48.819 1.00 22.75 O
ATOM 4749 CB SER A 612 0.406 -17.400 47.566 1.00 23.17 C
ATOM 4750 OG SER A 612 -0.918 -17.075 47.957 1.00 21.71 O
ATOM 4751 N ARG A 613 -0.507 -18.860 50.288 1.00 23.22 N
ATOM 4752 CA ARG A 613 -1.430 -19.811 50.904 1.00 23.55 C
ATOM 4753 C ARG A 613 -2.645 -20.062 50.015 1.00 23.26 C
ATOM 4754 O ARG A 613 -3.405 -21.009 50.237 1.00 23.37 O
ATOM 4755 CB ARG A 613 -1.844 -19.328 52.295 1.00 23.81 C
ATOM 4756 CG ARG A 613 -0.666 -19.251 53.262 1.00 25.61 C
ATOM 4757 CD ARG A 613 -1.101 -18.842 54.655 1.00 28.74 C
ATOM 4758 NE ARG A 613 0.038 -18.685 55.558 1.00 30.45 N
ATOM 4759 CZ ARG A 613 -0.049 -18.669 56.887 1.00 31.55 C
ATOM 4760 NH1 ARG A 613 -1.225 -18.808 57.487 1.00 30.71 N
ATOM 4761 NH2 ARG A 613 1.047 -18.518 57.620 1.00 32.25 N
ATOM 4762 N ASP A 614 -2.806 -19.219 48.998 1.00 22.71 N
ATOM 4763 CA ASP A 614 -3.918 -19.335 48.065 1.00 22.34 C
ATOM 4764 C ASP A 614 -3.546 -20.202 46.861 1.00 21.87 C
ATOM 4765 O ASP A 614 -2.570 -19.925 46.160 1.00 21.44 O
ATOM 4766 CB ASP A 614 -4.384 -17.951 47.614 1.00 22.49 C
ATOM 4767 CG ASP A 614 -5.625 -18.013 46.752 1.00 23.41 C
ATOM 4768 OD1 ASP A 614 -6.708 -18.354 47.281 1.00 24.62 O
ATOM 4769 OD2 ASP A 614 -5.516 -17.724 45.544 1.00 24.38 O
ATOM 4770 N LYS A 615 -4.340 -21.248 46.635 1.00 21.31 N
ATOM 4771 CA LYS A 615 -4.097 -22.215 45.565 1.00 21.32 C
ATOM 4772 C LYS A 615 -4.035 -21.549 44.191 1.00 20.61 C
ATOM 4773 O LYS A 615 -3.122 -21.826 43.407 1.00 20.44 O
ATOM 4774 CB LYS A 615 -5.177 -23.304 45.574 1.00 21.27 C
ATOM 4775 CG LYS A 615 -4.907 -24.483 44.651 1.00 22.27 C
ATOM 4776 CD LYS A 615 -6.039 -25.500 44.717 1.00 22.46 C
ATOM 4777 CE LYS A 615 -5.757 -26.699 43.830 1.00 25.11 C
ATOM 4778 NZ LYS A 615 -6.999 -27.466 43.521 1.00 26.80 N
ATOM 4779 N PHE A 616 -5.004 -20.678 43.914 1.00 20.19 N
ATOM 4780 CA PHE A 616 -5.091 -19.986 42.623 1.00 20.15 C
ATOM 4781 C PHE A 616 -3.807 -19.228 42.312 1.00 20.15 C
ATOM 4782 O PHE A 616 -3.273 -19.331 41.208 1.00 20.15 O
ATOM 4783 CB PHE A 616 -6.289 -19.029 42.584 1.00 19.86 C
ATOM 4784 CG PHE A 616 -6.499 -18.375 41.240 1.00 19.87 C
ATOM 4785 CD1 PHE A 616 -7.166 -19.049 40.219 1.00 19.92 C
ATOM 4786 CD2 PHE A 616 -6.027 -17.089 40.997 1.00 19.02 C
ATOM 4787 CE1 PHE A 616 -7.360 -18.448 38.970 1.00 19.90 C
ATOM 4788 CE2 PHE A 616 -6.214 -16.481 39.751 1.00 19.34 C
ATOM 4789 CZ PHE A 616 -6.882 -17.163 38.740 1.00 18.39 C
ATOM 4790 N ILE A 617 -3.312 -18.485 43.298 1.00 20.43 N
ATOM 4791 CA ILE A 617 -2.096 -17.690 43.127 1.00 20.76 C
ATOM 4792 C ILE A 617 -0.848 -18.566 42.946 1.00 21.14 C
ATOM 4793 O ILE A 617 -0.006 -18.273 42.094 1.00 20.64 O
ATOM 4794 CB ILE A 617 -1.969 -16.619 44.231 1.00 20.97 C
ATOM 4795 CG1 ILE A 617 -2.939 -15.474 43.901 1.00 21.37 C
ATOM 4796 CG2 ILE A 617 -0.536 -16.079 44.337 1.00 20.99 C
ATOM 4797 CD1 ILE A 617 -3.256 -14.563 45.028 1.00 22.76 C
ATOM 4798 N ARG A 618 -0.749 -19.650 43.715 1.00 21.51 N
ATOM 4799 CA ARG A 618 0.309 -20.640 43.501 1.00 22.21 C
ATOM 4800 C ARG A 618 0.305 -21.183 42.073 1.00 22.51 C
ATOM 4801 O ARG A 618 1.366 -21.353 41.468 1.00 22.91 O
ATOM 4802 CB ARG A 618 0.184 -21.810 44.480 1.00 22.18 C
ATOM 4803 CG ARG A 618 0.661 -21.510 45.883 1.00 22.37 C
ATOM 4804 CD ARG A 618 0.981 -22.798 46.661 1.00 22.41 C
ATOM 4805 NE ARG A 618 -0.096 -23.784 46.589 1.00 22.60 N
ATOM 4806 CZ ARG A 618 -1.206 -23.753 47.323 1.00 22.43 C
ATOM 4807 NH1 ARG A 618 -1.409 -22.783 48.208 1.00 22.05 N
ATOM 4808 NH2 ARG A 618 -2.123 -24.699 47.169 1.00 23.16 N
ATOM 4809 N GLU A 619 -0.888 -21.452 41.544 1.00 22.97 N
ATOM 4810 CA GLU A 619 -1.033 -22.065 40.219 1.00 23.72 C
ATOM 4811 C GLU A 619 -0.746 -21.104 39.057 1.00 23.67 C
ATOM 4812 O GLU A 619 -0.574 -21.536 37.914 1.00 23.78 O
ATOM 4813 CB GLU A 619 -2.405 -22.731 40.068 1.00 24.06 C
ATOM 4814 CG GLU A 619 -2.597 -23.940 40.982 1.00 26.23 C
ATOM 4815 CD GLU A 619 -3.548 -24.975 40.414 1.00 29.61 C
ATOM 4816 OE1 GLU A 619 -3.318 -25.442 39.274 1.00 31.64 O
ATOM 4817 OE2 GLU A 619 -4.516 -25.338 41.116 1.00 30.90 O
ATOM 4818 N LEU A 620 -0.686 -19.806 39.354 1.00 23.71 N
ATOM 4819 CA LEU A 620 -0.227 -18.818 38.376 1.00 23.74 C
ATOM 4820 C LEU A 620 1.265 -19.001 38.104 1.00 24.20 C
ATOM 4821 O LEU A 620 1.761 -18.634 37.035 1.00 24.00 O
ATOM 4822 CB LEU A 620 -0.488 -17.391 38.868 1.00 23.53 C
ATOM 4823 CG LEU A 620 -1.925 -16.911 39.098 1.00 23.07 C
ATOM 4824 CD1 LEU A 620 -1.912 -15.490 39.624 1.00 21.99 C
ATOM 4825 CD2 LEU A 620 -2.755 -16.993 37.825 1.00 23.23 C
ATOM 4826 N PHE A 621 1.956 -19.584 39.086 1.00 24.80 N
ATOM 4827 CA PHE A 621 3.402 -19.775 39.069 1.00 25.34 C
ATOM 4828 C PHE A 621 3.753 -21.258 39.155 1.00 25.67 C
ATOM 4829 O PHE A 621 4.014 -21.904 38.142 1.00 26.55 O
ATOM 4830 CB PHE A 621 4.033 -19.039 40.251 1.00 25.26 C
ATOM 4831 CG PHE A 621 3.904 -17.544 40.176 1.00 25.25 C
ATOM 4832 CD1 PHE A 621 2.765 -16.901 40.654 1.00 24.72 C
ATOM 4833 CD2 PHE A 621 4.926 -16.778 39.629 1.00 25.09 C
ATOM 4834 CE1 PHE A 621 2.644 -15.516 40.577 1.00 24.73 C
ATOM 4835 CE2 PHE A 621 4.816 -15.394 39.553 1.00 24.91 C
ATOM 4836 CZ PHE A 621 3.672 -14.761 40.025 1.00 25.00 C
ATOM 4837 N LEU A 638 24.388 -12.777 38.547 1.00 26.06 N
ATOM 4838 CA LEU A 638 23.635 -11.566 38.228 1.00 25.78 C
ATOM 4839 C LEU A 638 22.171 -11.889 37.942 1.00 25.32 C
ATOM 4840 O LEU A 638 21.863 -12.835 37.211 1.00 25.73 O
ATOM 4841 CB LEU A 638 24.268 -10.838 37.033 1.00 25.95 C
ATOM 4842 CG LEU A 638 23.588 -9.582 36.464 1.00 25.96 C
ATOM 4843 CD1 LEU A 638 23.681 -8.390 37.421 1.00 26.56 C
ATOM 4844 CD2 LEU A 638 24.178 -9.232 35.106 1.00 26.01 C
ATOM 4845 N SER A 639 21.273 -11.105 38.529 1.00 24.64 N
ATOM 4846 CA SER A 639 19.846 -11.260 38.279 1.00 23.59 C
ATOM 4847 C SER A 639 19.468 -10.445 37.038 1.00 22.84 C
ATOM 4848 O SER A 639 19.133 -9.261 37.143 1.00 22.90 O
ATOM 4849 CB SER A 639 19.042 -10.816 39.505 1.00 23.91 C
ATOM 4850 OG SER A 639 17.651 -10.807 39.244 1.00 24.08 O
ATOM 4851 N PHE A 640 19.554 -11.084 35.870 1.00 21.78 N
ATOM 4852 CA PHE A 640 19.247 -10.436 34.587 1.00 20.54 C
ATOM 4853 C PHE A 640 18.663 -11.394 33.550 1.00 19.95 C
ATOM 4854 O PHE A 640 19.234 -12.457 33.271 1.00 19.81 O
ATOM 4855 CB PHE A 640 20.491 -9.735 34.010 1.00 20.41 C
ATOM 4856 CG PHE A 640 20.311 -9.237 32.591 1.00 19.85 C
ATOM 4857 CD1 PHE A 640 19.374 -8.245 32.296 1.00 18.84 C
ATOM 4858 CD2 PHE A 640 21.082 -9.756 31.557 1.00 19.33 C
ATOM 4859 CE1 PHE A 640 19.204 -7.791 30.985 1.00 18.40 C
ATOM 4860 CE2 PHE A 640 20.926 -9.302 30.246 1.00 19.26 C
ATOM 4861 CZ PHE A 640 19.985 -8.316 29.962 1.00 18.16 C
ATOM 4862 N ILE A 641 17.526 -10.997 32.980 1.00 18.87 N
ATOM 4863 CA ILE A 641 16.908 -11.698 31.856 1.00 18.13 C
ATOM 4864 C ILE A 641 16.554 -10.648 30.799 1.00 17.15 C
ATOM 4865 O ILE A 641 15.816 -9.701 31.079 1.00 17.12 O
ATOM 4866 CB ILE A 641 15.652 -12.514 32.283 1.00 18.18 C
ATOM 4867 CG1 ILE A 641 16.043 -13.639 33.257 1.00 18.83 C
ATOM 4868 CG2 ILE A 641 14.945 -13.108 31.067 1.00 18.26 C
ATOM 4869 CD1 ILE A 641 14.877 -14.431 33.809 1.00 18.73 C
ATOM 4870 N SER A 642 17.095 -10.817 29.596 1.00 16.12 N
ATOM 4871 CA SER A 642 16.931 -9.835 28.518 1.00 15.24 C
ATOM 4872 C SER A 642 15.515 -9.754 27.949 1.00 15.11 C
ATOM 4873 O SER A 642 14.992 -10.733 27.414 1.00 14.94 O
ATOM 4874 CB SER A 642 17.907 -10.124 27.376 1.00 14.81 C
ATOM 4875 OG SER A 642 17.661 -9.246 26.286 1.00 13.89 O
ATOM 4876 N VAL A 643 14.915 -8.571 28.035 1.00 15.07 N
ATOM 4877 CA VAL A 643 13.622 -8.325 27.405 1.00 15.20 C
ATOM 4878 C VAL A 643 13.771 -8.313 25.876 1.00 15.13 C
ATOM 4879 O VAL A 643 12.951 -8.899 25.172 1.00 15.68 O
ATOM 4880 CB VAL A 643 12.961 -7.020 27.927 1.00 14.94 C
ATOM 4881 CG1 VAL A 643 11.748 -6.633 27.075 1.00 15.40 C
ATOM 4882 CG2 VAL A 643 12.542 -7.190 29.376 1.00 15.11 C
ATOM 4883 N GLY A 644 14.827 -7.672 25.379 1.00 15.59 N
ATOM 4884 CA GLY A 644 15.080 -7.580 23.933 1.00 15.76 C
ATOM 4885 C GLY A 644 15.257 -8.946 23.293 1.00 16.34 C
ATOM 4886 O GLY A 644 14.715 -9.222 22.219 1.00 15.91 O
ATOM 4887 N ASN A 645 16.010 -9.808 23.963 1.00 16.69 N
ATOM 4888 CA ASN A 645 16.204 -11.172 23.489 1.00 17.94 C
ATOM 4889 C ASN A 645 14.891 -11.965 23.504 1.00 18.17 C
ATOM 4890 O ASN A 645 14.703 -12.863 22.683 1.00 18.21 O
ATOM 4891 CB ASN A 645 17.294 -11.879 24.303 1.00 18.33 C
ATOM 4892 CG ASN A 645 17.440 -13.348 23.940 1.00 20.74 C
ATOM 4893 OD1 ASN A 645 17.150 -14.235 24.754 1.00 23.68 O
ATOM 4894 ND2 ASN A 645 17.879 -13.614 22.712 1.00 21.81 N
ATOM 4895 N LYS A 646 13.979 -11.612 24.415 1.00 18.38 N
ATOM 4896 CA LYS A 646 12.620 -12.187 24.391 1.00 18.85 C
ATOM 4897 C LYS A 646 11.824 -11.716 23.181 1.00 18.18 C
ATOM 4898 O LYS A 646 11.115 -12.506 22.566 1.00 18.76 O
ATOM 4899 CB LYS A 646 11.831 -11.895 25.677 1.00 19.10 C
ATOM 4900 CG LYS A 646 12.450 -12.427 26.960 1.00 20.67 C
ATOM 4901 CD LYS A 646 13.384 -13.612 26.719 1.00 22.51 C
ATOM 4902 CE LYS A 646 14.459 -13.656 27.794 1.00 22.84 C
ATOM 4903 NZ LYS A 646 15.831 -13.511 27.234 1.00 21.79 N
ATOM 4904 N PHE A 647 11.926 -10.434 22.839 1.00 18.01 N
ATOM 4905 CA PHE A 647 11.266 -9.946 21.635 1.00 17.28 C
ATOM 4906 C PHE A 647 11.794 -10.702 20.416 1.00 16.85 C
ATOM 4907 O PHE A 647 11.012 -11.186 19.597 1.00 16.88 O
ATOM 4908 CB PHE A 647 11.393 -8.419 21.480 1.00 17.73 C
ATOM 4909 CG PHE A 647 10.299 -7.656 22.179 1.00 17.69 C
ATOM 4910 CD1 PHE A 647 10.419 -7.308 23.522 1.00 18.15 C
ATOM 4911 CD2 PHE A 647 9.131 -7.308 21.499 1.00 17.67 C
ATOM 4912 CE1 PHE A 647 9.388 -6.613 24.182 1.00 18.40 C
ATOM 4913 CE2 PHE A 647 8.092 -6.620 22.147 1.00 17.47 C
ATOM 4914 CZ PHE A 647 8.221 -6.271 23.490 1.00 17.74 C
ATOM 4915 N LYS A 648 13.113 -10.855 20.331 1.00 15.56 N
ATOM 4916 CA LYS A 648 13.724 -11.464 19.154 1.00 15.04 C
ATOM 4917 C LYS A 648 13.387 -12.950 19.041 1.00 14.94 C
ATOM 4918 O LYS A 648 12.965 -13.419 17.981 1.00 14.65 O
ATOM 4919 CB LYS A 648 15.241 -11.255 19.168 1.00 14.55 C
ATOM 4920 CG LYS A 648 15.949 -11.840 17.956 1.00 14.56 C
ATOM 4921 CD LYS A 648 17.450 -11.696 18.097 1.00 15.88 C
ATOM 4922 CE LYS A 648 18.169 -12.163 16.849 1.00 17.65 C
ATOM 4923 NZ LYS A 648 19.644 -12.081 17.044 1.00 19.56 N
ATOM 4924 N THR A 649 13.575 -13.680 20.137 1.00 15.14 N
ATOM 4925 CA THR A 649 13.356 -15.121 20.149 1.00 15.78 C
ATOM 4926 C THR A 649 11.903 -15.470 19.821 1.00 15.88 C
ATOM 4927 O THR A 649 11.655 -16.358 19.002 1.00 15.87 O
ATOM 4928 CB THR A 649 13.804 -15.741 21.491 1.00 16.09 C
ATOM 4929 OG1 THR A 649 15.203 -15.488 21.675 1.00 16.53 O
ATOM 4930 CG2 THR A 649 13.569 -17.256 21.503 1.00 16.74 C
ATOM 4931 N GLN A 650 10.962 -14.742 20.428 1.00 15.80 N
ATOM 4932 CA GLN A 650 9.524 -14.993 20.230 1.00 16.49 C
ATOM 4933 C GLN A 650 9.083 -14.701 18.799 1.00 16.17 C
ATOM 4934 O GLN A 650 8.336 -15.484 18.198 1.00 16.51 O
ATOM 4935 CB GLN A 650 8.679 -14.177 21.222 1.00 16.68 C
ATOM 4936 CG GLN A 650 8.734 -14.683 22.665 1.00 19.07 C
ATOM 4937 CD GLN A 650 8.256 -16.119 22.800 1.00 21.65 C
ATOM 4938 OE1 GLN A 650 8.933 -16.954 23.401 1.00 23.82 O
ATOM 4939 NE2 GLN A 650 7.096 -16.416 22.224 1.00 23.02 N
ATOM 4940 N LEU A 651 9.549 -13.577 18.258 1.00 15.81 N
ATOM 4941 CA LEU A 651 9.235 -13.190 16.885 1.00 15.54 C
ATOM 4942 C LEU A 651 9.798 -14.182 15.883 1.00 15.22 C
ATOM 4943 O LEU A 651 9.157 -14.486 14.880 1.00 14.70 O
ATOM 4944 CB LEU A 651 9.791 -11.804 16.565 1.00 16.04 C
ATOM 4945 CG LEU A 651 9.070 -10.598 17.150 1.00 17.74 C
ATOM 4946 CD1 LEU A 651 9.915 -9.363 16.912 1.00 19.26 C
ATOM 4947 CD2 LEU A 651 7.688 -10.462 16.535 1.00 19.82 C
ATOM 4948 N ASN A 652 11.004 -14.677 16.148 1.00 14.93 N
ATOM 4949 CA ASN A 652 11.617 -15.638 15.240 1.00 15.58 C
ATOM 4950 C ASN A 652 10.880 -16.973 15.230 1.00 16.03 C
ATOM 4951 O ASN A 652 10.758 -17.598 14.182 1.00 16.43 O
ATOM 4952 CB ASN A 652 13.109 -15.793 15.530 1.00 15.57 C
ATOM 4953 CG ASN A 652 13.925 -14.653 14.950 1.00 15.20 C
ATOM 4954 OD1 ASN A 652 13.475 -13.950 14.034 1.00 16.16 O
ATOM 4955 ND2 ASN A 652 15.131 -14.466 15.467 1.00 15.45 N
ATOM 4956 N LEU A 653 10.359 -17.377 16.388 1.00 16.74 N
ATOM 4957 CA LEU A 653 9.509 -18.572 16.484 1.00 17.30 C
ATOM 4958 C LEU A 653 8.209 -18.374 15.706 1.00 17.35 C
ATOM 4959 O LEU A 653 7.779 -19.254 14.945 1.00 17.62 O
ATOM 4960 CB LEU A 653 9.208 -18.912 17.946 1.00 17.80 C
ATOM 4961 CG LEU A 653 10.366 -19.462 18.790 1.00 18.95 C
ATOM 4962 CD1 LEU A 653 9.938 -19.578 20.253 1.00 20.54 C
ATOM 4963 CD2 LEU A 653 10.882 -20.801 18.266 1.00 20.83 C
ATOM 4964 N LEU A 654 7.599 -17.209 15.899 1.00 17.17 N
ATOM 4965 CA LEU A 654 6.400 -16.817 15.165 1.00 17.10 C
ATOM 4966 C LEU A 654 6.643 -16.805 13.658 1.00 17.25 C
ATOM 4967 O LEU A 654 5.830 -17.324 12.890 1.00 16.84 O
ATOM 4968 CB LEU A 654 5.907 -15.448 15.639 1.00 17.15 C
ATOM 4969 CG LEU A 654 4.651 -14.874 14.980 1.00 17.29 C
ATOM 4970 CD1 LEU A 654 3.469 -15.853 15.058 1.00 17.78 C
ATOM 4971 CD2 LEU A 654 4.305 -13.552 15.628 1.00 17.07 C
ATOM 4972 N LEU A 655 7.764 -16.220 13.239 1.00 17.08 N
ATOM 4973 CA LEU A 655 8.093 -16.146 11.817 1.00 17.54 C
ATOM 4974 C LEU A 655 8.329 -17.527 11.201 1.00 18.07 C
ATOM 4975 O LEU A 655 7.949 -17.766 10.055 1.00 17.78 O
ATOM 4976 CB LEU A 655 9.276 -15.208 11.573 1.00 17.43 C
ATOM 4977 CG LEU A 655 8.925 -13.716 11.658 1.00 18.05 C
ATOM 4978 CD1 LEU A 655 10.169 -12.880 11.897 1.00 18.70 C
ATOM 4979 CD2 LEU A 655 8.192 -13.239 10.404 1.00 18.99 C
ATOM 4980 N ASP A 656 8.934 -18.432 11.972 1.00 18.69 N
ATOM 4981 CA ASP A 656 9.088 -19.833 11.557 1.00 20.01 C
ATOM 4982 C ASP A 656 7.733 -20.459 11.229 1.00 20.06 C
ATOM 4983 O ASP A 656 7.588 -21.147 10.217 1.00 20.47 O
ATOM 4984 CB ASP A 656 9.752 -20.661 12.660 1.00 20.32 C
ATOM 4985 CG ASP A 656 11.245 -20.439 12.753 1.00 22.13 C
ATOM 4986 OD1 ASP A 656 11.813 -20.805 13.806 1.00 25.09 O
ATOM 4987 OD2 ASP A 656 11.856 -19.917 11.793 1.00 23.56 O
ATOM 4988 N LYS A 657 6.754 -20.221 12.098 1.00 20.23 N
ATOM 4989 CA LYS A 657 5.401 -20.748 11.917 1.00 20.77 C
ATOM 4990 C LYS A 657 4.743 -20.151 10.672 1.00 20.14 C
ATOM 4991 O LYS A 657 4.122 -20.871 9.886 1.00 19.83 O
ATOM 4992 CB LYS A 657 4.549 -20.483 13.159 1.00 20.73 C
ATOM 4993 CG LYS A 657 3.262 -21.312 13.227 1.00 22.03 C
ATOM 4994 CD LYS A 657 2.490 -21.045 14.515 1.00 22.68 C
ATOM 4995 CE LYS A 657 3.249 -21.528 15.751 1.00 25.50 C
ATOM 4996 NZ LYS A 657 2.800 -20.833 16.985 1.00 26.98 N
ATOM 4997 N LEU A 658 4.897 -18.838 10.491 1.00 19.48 N
ATOM 4998 CA LEU A 658 4.333 -18.154 9.326 1.00 19.51 C
ATOM 4999 C LEU A 658 4.934 -18.657 8.016 1.00 19.68 C
ATOM 5000 O LEU A 658 4.225 -18.810 7.024 1.00 19.47 O
ATOM 5001 CB LEU A 658 4.509 -16.634 9.436 1.00 19.39 C
ATOM 5002 CG LEU A 658 3.829 -15.917 10.608 1.00 19.25 C
ATOM 5003 CD1 LEU A 658 4.112 -14.423 10.549 1.00 19.27 C
ATOM 5004 CD2 LEU A 658 2.322 -16.180 10.651 1.00 20.20 C
ATOM 5005 N ARG A 659 6.239 -18.919 8.023 1.00 19.94 N
ATOM 5006 CA ARG A 659 6.935 -19.370 6.818 1.00 20.54 C
ATOM 5007 C ARG A 659 6.479 -20.750 6.356 1.00 20.34 C
ATOM 5008 O ARG A 659 6.563 -21.063 5.164 1.00 20.73 O
ATOM 5009 CB ARG A 659 8.450 -19.355 7.024 1.00 20.72 C
ATOM 5010 CG ARG A 659 9.057 -17.967 6.934 1.00 22.64 C
ATOM 5011 CD ARG A 659 10.570 -18.009 7.062 1.00 25.34 C
ATOM 5012 NE ARG A 659 11.112 -16.690 7.380 1.00 27.41 N
ATOM 5013 CZ ARG A 659 11.579 -16.328 8.574 1.00 28.31 C
ATOM 5014 NH1 ARG A 659 11.596 -17.190 9.586 1.00 28.72 N
ATOM 5015 NH2 ARG A 659 12.047 -15.101 8.753 1.00 28.85 N
ATOM 5016 N SER A 660 5.987 -21.558 7.295 1.00 20.16 N
ATOM 5017 CA SER A 660 5.496 -22.907 6.993 1.00 20.06 C
ATOM 5018 C SER A 660 4.064 -22.924 6.442 1.00 19.66 C
ATOM 5019 O SER A 660 3.563 -23.979 6.038 1.00 19.75 O
ATOM 5020 CB SER A 660 5.605 -23.815 8.222 1.00 20.31 C
ATOM 5021 OG SER A 660 4.637 -23.488 9.206 1.00 21.72 O
ATOM 5022 N THR A 661 3.417 -21.759 6.415 1.00 18.67 N
ATOM 5023 CA THR A 661 2.021 -21.660 5.989 1.00 17.87 C
ATOM 5024 C THR A 661 1.871 -20.863 4.695 1.00 17.16 C
ATOM 5025 O THR A 661 2.778 -20.135 4.287 1.00 17.01 O
ATOM 5026 CB THR A 661 1.144 -20.968 7.064 1.00 17.98 C
ATOM 5027 OG1 THR A 661 1.566 -19.605 7.210 1.00 17.82 O
ATOM 5028 CG2 THR A 661 1.231 -21.688 8.412 1.00 18.43 C
ATOM 5029 N GLY A 662 0.712 -21.007 4.057 1.00 16.40 N
ATOM 5030 CA GLY A 662 0.315 -20.109 2.978 1.00 15.70 C
ATOM 5031 C GLY A 662 -0.133 -18.812 3.621 1.00 15.19 C
ATOM 5032 O GLY A 662 -0.844 -18.833 4.623 1.00 15.80 O
ATOM 5033 N ALA A 663 0.287 -17.683 3.066 1.00 14.33 N
ATOM 5034 CA ALA A 663 0.008 -16.400 3.712 1.00 13.78 C
ATOM 5035 C ALA A 663 -0.924 -15.527 2.888 1.00 13.37 C
ATOM 5036 O ALA A 663 -0.789 -15.452 1.668 1.00 13.84 O
ATOM 5037 CB ALA A 663 1.304 -15.666 4.011 1.00 13.92 C
ATOM 5038 N SER A 664 -1.875 -14.889 3.572 1.00 12.62 N
ATOM 5039 CA SER A 664 -2.758 -13.876 2.989 1.00 12.19 C
ATOM 5040 C SER A 664 -2.561 -12.597 3.788 1.00 11.73 C
ATOM 5041 O SER A 664 -2.234 -12.657 4.979 1.00 12.17 O
ATOM 5042 CB SER A 664 -4.226 -14.308 3.079 1.00 12.52 C
ATOM 5043 OG SER A 664 -4.454 -15.524 2.386 1.00 13.75 O
ATOM 5044 N PHE A 665 -2.767 -11.447 3.149 1.00 11.02 N
ATOM 5045 CA PHE A 665 -2.453 -10.167 3.780 1.00 10.38 C
ATOM 5046 C PHE A 665 -3.609 -9.180 3.748 1.00 9.82 C
ATOM 5047 O PHE A 665 -4.233 -8.964 2.704 1.00 9.74 O
ATOM 5048 CB PHE A 665 -1.219 -9.529 3.128 1.00 10.77 C
ATOM 5049 CG PHE A 665 0.039 -10.327 3.300 1.00 11.01 C
ATOM 5050 CD1 PHE A 665 0.858 -10.121 4.409 1.00 11.85 C
ATOM 5051 CD2 PHE A 665 0.413 -11.280 2.353 1.00 12.63 C
ATOM 5052 CE1 PHE A 665 2.026 -10.853 4.578 1.00 13.16 C
ATOM 5053 CE2 PHE A 665 1.577 -12.028 2.517 1.00 13.04 C
ATOM 5054 CZ PHE A 665 2.386 -11.813 3.637 1.00 12.62 C
ATOM 5055 N ILE A 666 -3.884 -8.593 4.911 1.00 8.86 N
ATOM 5056 CA ILE A 666 -4.813 -7.477 5.030 1.00 8.95 C
ATOM 5057 C ILE A 666 -4.005 -6.267 5.510 1.00 8.83 C
ATOM 5058 O ILE A 666 -3.384 -6.312 6.581 1.00 8.76 O
ATOM 5059 CB ILE A 666 -5.960 -7.790 6.023 1.00 8.26 C
ATOM 5060 CG1 ILE A 666 -6.739 -9.025 5.552 1.00 8.92 C
ATOM 5061 CG2 ILE A 666 -6.890 -6.574 6.200 1.00 9.06 C
ATOM 5062 CD1 ILE A 666 -7.772 -9.519 6.539 1.00 9.72 C
ATOM 5063 N ARG A 667 -4.013 -5.207 4.707 1.00 8.58 N
ATOM 5064 CA ARG A 667 -3.291 -3.975 5.024 1.00 8.69 C
ATOM 5065 C ARG A 667 -4.270 -2.939 5.560 1.00 8.29 C
ATOM 5066 O ARG A 667 -5.032 -2.326 4.806 1.00 7.77 O
ATOM 5067 CB ARG A 667 -2.514 -3.456 3.798 1.00 8.89 C
ATOM 5068 CG ARG A 667 -2.029 -1.996 3.829 1.00 12.46 C
ATOM 5069 CD ARG A 667 -1.481 -1.507 5.178 1.00 16.86 C
ATOM 5070 NE ARG A 667 -0.346 -2.277 5.682 1.00 19.83 N
ATOM 5071 CZ ARG A 667 0.573 -1.787 6.513 1.00 21.46 C
ATOM 5072 NH1 ARG A 667 0.515 -0.516 6.912 1.00 23.15 N
ATOM 5073 NH2 ARG A 667 1.570 -2.555 6.921 1.00 20.62 N
ATOM 5074 N CYS A 668 -4.250 -2.758 6.875 1.00 7.78 N
ATOM 5075 CA CYS A 668 -5.126 -1.780 7.508 1.00 7.99 C
ATOM 5076 C CYS A 668 -4.496 -0.399 7.453 1.00 7.78 C
ATOM 5077 O CYS A 668 -3.292 -0.240 7.698 1.00 8.04 O
ATOM 5078 CB CYS A 668 -5.432 -2.152 8.956 1.00 7.73 C
ATOM 5079 SG CYS A 668 -6.351 -3.677 9.116 1.00 9.95 S
ATOM 5080 N ILE A 669 -5.341 0.583 7.156 1.00 7.73 N
ATOM 5081 CA ILE A 669 -4.934 1.974 6.967 1.00 8.34 C
ATOM 5082 C ILE A 669 -5.690 2.893 7.923 1.00 8.22 C
ATOM 5083 O ILE A 669 -6.920 2.817 8.025 1.00 7.87 O
ATOM 5084 CB ILE A 669 -5.226 2.435 5.514 1.00 8.32 C
ATOM 5085 CG1 ILE A 669 -4.478 1.571 4.485 1.00 9.70 C
ATOM 5086 CG2 ILE A 669 -4.957 3.940 5.350 1.00 8.60 C
ATOM 5087 CD1 ILE A 669 -2.966 1.692 4.497 1.00 11.16 C
ATOM 5088 N LYS A 670 -4.955 3.760 8.619 1.00 8.50 N
ATOM 5089 CA LYS A 670 -5.573 4.730 9.528 1.00 8.98 C
ATOM 5090 C LYS A 670 -5.789 6.074 8.813 1.00 9.17 C
ATOM 5091 O LYS A 670 -4.824 6.688 8.341 1.00 9.10 O
ATOM 5092 CB LYS A 670 -4.725 4.906 10.790 1.00 9.09 C
ATOM 5093 CG LYS A 670 -5.393 5.764 11.866 1.00 9.19 C
ATOM 5094 CD LYS A 670 -4.617 5.741 13.197 1.00 9.97 C
ATOM 5095 CE LYS A 670 -3.285 6.463 13.096 1.00 12.45 C
ATOM 5096 NZ LYS A 670 -2.532 6.387 14.386 1.00 13.39 N
ATOM 5097 N PRO A 671 -7.058 6.526 8.718 1.00 9.13 N
ATOM 5098 CA PRO A 671 -7.377 7.663 7.840 1.00 9.37 C
ATOM 5099 C PRO A 671 -6.959 9.038 8.359 1.00 9.72 C
ATOM 5100 O PRO A 671 -6.813 9.967 7.565 1.00 9.69 O
ATOM 5101 CB PRO A 671 -8.902 7.588 7.719 1.00 9.50 C
ATOM 5102 CG PRO A 671 -9.341 7.005 9.028 1.00 9.18 C
ATOM 5103 CD PRO A 671 -8.268 5.984 9.369 1.00 9.19 C
ATOM 5104 N ASN A 672 -6.777 9.164 9.672 1.00 9.93 N
ATOM 5105 CA ASN A 672 -6.449 10.448 10.302 1.00 10.44 C
ATOM 5106 C ASN A 672 -5.978 10.207 11.730 1.00 11.03 C
ATOM 5107 O ASN A 672 -6.029 9.079 12.222 1.00 10.33 O
ATOM 5108 CB ASN A 672 -7.659 11.393 10.283 1.00 10.33 C
ATOM 5109 CG ASN A 672 -8.842 10.844 11.060 1.00 9.99 C
ATOM 5110 OD1 ASN A 672 -8.838 10.840 12.294 1.00 11.29 O
ATOM 5111 ND2 ASN A 672 -9.867 10.391 10.343 1.00 10.58 N
ATOM 5112 N LEU A 673 -5.530 11.270 12.392 1.00 12.12 N
ATOM 5113 CA LEU A 673 -4.973 11.150 13.737 1.00 13.54 C
ATOM 5114 C LEU A 673 -5.956 11.580 14.833 1.00 14.17 C
ATOM 5115 O LEU A 673 -5.565 11.729 15.998 1.00 14.91 O
ATOM 5116 CB LEU A 673 -3.662 11.944 13.833 1.00 14.01 C
ATOM 5117 CG LEU A 673 -2.549 11.574 12.837 1.00 14.91 C
ATOM 5118 CD1 LEU A 673 -1.328 12.462 13.054 1.00 17.64 C
ATOM 5119 CD2 LEU A 673 -2.161 10.098 12.936 1.00 17.01 C
ATOM 5120 N LYS A 674 -7.224 11.750 14.460 1.00 14.26 N
ATOM 5121 CA LYS A 674 -8.251 12.293 15.361 1.00 15.14 C
ATOM 5122 C LYS A 674 -9.393 11.324 15.695 1.00 14.58 C
ATOM 5123 O LYS A 674 -10.364 11.704 16.366 1.00 14.30 O
ATOM 5124 CB LYS A 674 -8.820 13.595 14.784 1.00 15.30 C
ATOM 5125 CG LYS A 674 -7.767 14.653 14.481 1.00 16.17 C
ATOM 5126 CD LYS A 674 -8.365 15.873 13.784 1.00 17.54 C
ATOM 5127 CE LYS A 674 -8.764 16.958 14.770 1.00 21.43 C
ATOM 5128 NZ LYS A 674 -9.214 18.199 14.069 1.00 23.98 N
ATOM 5129 N MET A 675 -9.273 10.078 15.234 1.00 14.12 N
ATOM 5130 CA MET A 675 -10.301 9.039 15.449 1.00 14.19 C
ATOM 5131 C MET A 675 -11.683 9.448 14.934 1.00 13.94 C
ATOM 5132 O MET A 675 -12.709 9.085 15.516 1.00 14.23 O
ATOM 5133 CB MET A 675 -10.393 8.652 16.930 1.00 14.27 C
ATOM 5134 CG MET A 675 -9.067 8.286 17.557 1.00 14.22 C
ATOM 5135 SD MET A 675 -9.280 7.919 19.305 1.00 15.37 S
ATOM 5136 CE MET A 675 -7.576 7.627 19.747 1.00 15.36 C
ATOM 5137 N THR A 676 -11.700 10.215 13.851 1.00 13.81 N
ATOM 5138 CA THR A 676 -12.944 10.731 13.293 1.00 13.99 C
ATOM 5139 C THR A 676 -13.349 9.964 12.037 1.00 14.08 C
ATOM 5140 O THR A 676 -12.488 9.450 11.311 1.00 13.33 O
ATOM 5141 CB THR A 676 -12.827 12.228 12.960 1.00 14.25 C
ATOM 5142 OG1 THR A 676 -11.717 12.437 12.081 1.00 14.37 O
ATOM 5143 CG2 THR A 676 -12.616 13.047 14.229 1.00 14.14 C
ATOM 5144 N SER A 677 -14.657 9.897 11.793 1.00 13.88 N
ATOM 5145 CA SER A 677 -15.199 9.306 10.567 1.00 14.09 C
ATOM 5146 C SER A 677 -15.227 10.331 9.429 1.00 14.25 C
ATOM 5147 O SER A 677 -15.257 11.537 9.676 1.00 14.38 O
ATOM 5148 CB SER A 677 -16.607 8.750 10.815 1.00 14.12 C
ATOM 5149 OG SER A 677 -17.483 9.766 11.289 1.00 14.38 O
ATOM 5150 N HIS A 678 -15.220 9.833 8.192 1.00 14.50 N
ATOM 5151 CA HIS A 678 -15.272 10.663 6.977 1.00 15.09 C
ATOM 5152 C HIS A 678 -14.281 11.826 6.980 1.00 14.82 C
ATOM 5153 O HIS A 678 -14.630 12.955 6.617 1.00 14.86 O
ATOM 5154 CB HIS A 678 -16.702 11.155 6.719 1.00 15.53 C
ATOM 5155 CG HIS A 678 -17.718 10.057 6.694 1.00 17.18 C
ATOM 5156 ND1 HIS A 678 -17.736 9.082 5.720 1.00 19.72 N
ATOM 5157 CD2 HIS A 678 -18.741 9.771 7.531 1.00 18.35 C
ATOM 5158 CE1 HIS A 678 -18.734 8.249 5.954 1.00 18.92 C
ATOM 5159 NE2 HIS A 678 -19.355 8.641 7.051 1.00 19.74 N
ATOM 5160 N HIS A 679 -13.053 11.535 7.406 1.00 14.36 N
ATOM 5161 CA HIS A 679 -11.943 12.478 7.358 1.00 14.51 C
ATOM 5162 C HIS A 679 -10.730 11.774 6.758 1.00 13.95 C
ATOM 5163 O HIS A 679 -9.831 11.335 7.473 1.00 13.51 O
ATOM 5164 CB HIS A 679 -11.638 13.043 8.749 1.00 15.05 C
ATOM 5165 CG HIS A 679 -12.515 14.191 9.136 1.00 17.80 C
ATOM 5166 ND1 HIS A 679 -12.226 15.495 8.793 1.00 20.39 N
ATOM 5167 CD2 HIS A 679 -13.679 14.233 9.827 1.00 19.95 C
ATOM 5168 CE1 HIS A 679 -13.171 16.291 9.262 1.00 20.79 C
ATOM 5169 NE2 HIS A 679 -14.064 15.551 9.894 1.00 21.29 N
ATOM 5170 N PHE A 680 -10.745 11.653 5.433 1.00 12.86 N
ATOM 5171 CA PHE A 680 -9.697 10.985 4.664 1.00 12.56 C
ATOM 5172 C PHE A 680 -8.515 11.942 4.504 1.00 12.49 C
ATOM 5173 O PHE A 680 -8.600 12.915 3.745 1.00 12.75 O
ATOM 5174 CB PHE A 680 -10.286 10.595 3.300 1.00 12.24 C
ATOM 5175 CG PHE A 680 -9.402 9.719 2.455 1.00 11.48 C
ATOM 5176 CD1 PHE A 680 -9.607 8.338 2.410 1.00 10.98 C
ATOM 5177 CD2 PHE A 680 -8.403 10.274 1.658 1.00 10.84 C
ATOM 5178 CE1 PHE A 680 -8.804 7.529 1.606 1.00 11.32 C
ATOM 5179 CE2 PHE A 680 -7.592 9.471 0.847 1.00 10.63 C
ATOM 5180 CZ PHE A 680 -7.794 8.096 0.822 1.00 11.11 C
ATOM 5181 N GLU A 681 -7.429 11.690 5.239 1.00 12.12 N
ATOM 5182 CA GLU A 681 -6.225 12.524 5.135 1.00 11.89 C
ATOM 5183 C GLU A 681 -5.301 11.966 4.058 1.00 11.28 C
ATOM 5184 O GLU A 681 -4.542 11.023 4.297 1.00 10.78 O
ATOM 5185 CB GLU A 681 -5.505 12.652 6.482 1.00 12.22 C
ATOM 5186 CG GLU A 681 -6.265 13.477 7.526 1.00 13.94 C
ATOM 5187 CD GLU A 681 -6.256 14.981 7.248 1.00 17.91 C
ATOM 5188 OE1 GLU A 681 -7.074 15.698 7.867 1.00 20.52 O
ATOM 5189 OE2 GLU A 681 -5.442 15.451 6.423 1.00 18.95 O
ATOM 5190 N GLY A 682 -5.398 12.551 2.864 1.00 11.09 N
ATOM 5191 CA GLY A 682 -4.723 12.031 1.678 1.00 11.00 C
ATOM 5192 C GLY A 682 -3.242 11.757 1.811 1.00 10.95 C
ATOM 5193 O GLY A 682 -2.779 10.664 1.465 1.00 10.66 O
ATOM 5194 N ALA A 683 -2.497 12.749 2.303 1.00 10.58 N
ATOM 5195 CA ALA A 683 -1.048 12.625 2.450 1.00 10.64 C
ATOM 5196 C ALA A 683 -0.686 11.531 3.459 1.00 10.22 C
ATOM 5197 O ALA A 683 0.214 10.727 3.212 1.00 10.43 O
ATOM 5198 CB ALA A 683 -0.427 13.969 2.845 1.00 10.38 C
ATOM 5199 N GLN A 684 -1.412 11.498 4.576 1.00 10.19 N
ATOM 5200 CA GLN A 684 -1.227 10.480 5.612 1.00 10.48 C
ATOM 5201 C GLN A 684 -1.452 9.068 5.077 1.00 10.11 C
ATOM 5202 O GLN A 684 -0.666 8.152 5.356 1.00 10.19 O
ATOM 5203 CB GLN A 684 -2.162 10.747 6.791 1.00 10.34 C
ATOM 5204 CG GLN A 684 -1.788 11.993 7.598 1.00 11.18 C
ATOM 5205 CD GLN A 684 -2.788 12.325 8.698 1.00 11.13 C
ATOM 5206 OE1 GLN A 684 -2.934 13.491 9.086 1.00 13.33 O
ATOM 5207 NE2 GLN A 684 -3.476 11.311 9.209 1.00 10.86 N
ATOM 5208 N ILE A 685 -2.522 8.905 4.301 1.00 9.60 N
ATOM 5209 CA ILE A 685 -2.883 7.605 3.731 1.00 9.30 C
ATOM 5210 C ILE A 685 -1.898 7.200 2.635 1.00 9.42 C
ATOM 5211 O ILE A 685 -1.457 6.052 2.590 1.00 9.14 O
ATOM 5212 CB ILE A 685 -4.355 7.594 3.246 1.00 8.98 C
ATOM 5213 CG1 ILE A 685 -5.281 7.668 4.466 1.00 9.31 C
ATOM 5214 CG2 ILE A 685 -4.667 6.341 2.394 1.00 9.13 C
ATOM 5215 CD1 ILE A 685 -6.693 8.022 4.157 1.00 9.80 C
ATOM 5216 N LEU A 686 -1.529 8.153 1.780 1.00 9.59 N
ATOM 5217 CA LEU A 686 -0.502 7.897 0.762 1.00 10.01 C
ATOM 5218 C LEU A 686 0.796 7.364 1.370 1.00 10.00 C
ATOM 5219 O LEU A 686 1.385 6.424 0.838 1.00 9.39 O
ATOM 5220 CB LEU A 686 -0.208 9.150 -0.068 1.00 10.19 C
ATOM 5221 CG LEU A 686 0.861 9.015 -1.162 1.00 9.96 C
ATOM 5222 CD1 LEU A 686 0.499 7.963 -2.226 1.00 11.99 C
ATOM 5223 CD2 LEU A 686 1.131 10.374 -1.808 1.00 10.58 C
ATOM 5224 N SER A 687 1.231 7.974 2.475 1.00 10.55 N
ATOM 5225 CA SER A 687 2.439 7.557 3.180 1.00 11.18 C
ATOM 5226 C SER A 687 2.369 6.090 3.600 1.00 10.96 C
ATOM 5227 O SER A 687 3.340 5.343 3.440 1.00 11.29 O
ATOM 5228 CB SER A 687 2.691 8.448 4.402 1.00 11.53 C
ATOM 5229 OG SER A 687 3.938 8.124 4.996 1.00 13.73 O
ATOM 5230 N GLN A 688 1.213 5.685 4.123 1.00 10.73 N
ATOM 5231 CA GLN A 688 0.985 4.299 4.517 1.00 10.44 C
ATOM 5232 C GLN A 688 0.982 3.353 3.314 1.00 10.55 C
ATOM 5233 O GLN A 688 1.537 2.263 3.386 1.00 10.47 O
ATOM 5234 CB GLN A 688 -0.324 4.172 5.299 1.00 10.36 C
ATOM 5235 CG GLN A 688 -0.267 4.810 6.677 1.00 10.12 C
ATOM 5236 CD GLN A 688 -1.636 4.919 7.288 1.00 10.40 C
ATOM 5237 OE1 GLN A 688 -2.181 3.933 7.792 1.00 10.11 O
ATOM 5238 NE2 GLN A 688 -2.218 6.112 7.227 1.00 8.69 N
ATOM 5239 N LEU A 689 0.375 3.778 2.209 1.00 10.48 N
ATOM 5240 CA LEU A 689 0.317 2.936 1.015 1.00 10.74 C
ATOM 5241 C LEU A 689 1.724 2.708 0.465 1.00 10.91 C
ATOM 5242 O LEU A 689 2.045 1.628 -0.033 1.00 10.89 O
ATOM 5243 CB LEU A 689 -0.603 3.551 -0.047 1.00 10.50 C
ATOM 5244 CG LEU A 689 -2.102 3.643 0.266 1.00 11.03 C
ATOM 5245 CD1 LEU A 689 -2.799 4.517 -0.778 1.00 11.42 C
ATOM 5246 CD2 LEU A 689 -2.778 2.259 0.349 1.00 11.39 C
ATOM 5247 N GLN A 690 2.565 3.733 0.589 1.00 11.42 N
ATOM 5248 CA GLN A 690 3.960 3.650 0.177 1.00 12.24 C
ATOM 5249 C GLN A 690 4.795 2.736 1.081 1.00 12.55 C
ATOM 5250 O GLN A 690 5.366 1.752 0.604 1.00 12.36 O
ATOM 5251 CB GLN A 690 4.579 5.049 0.092 1.00 11.93 C
ATOM 5252 CG GLN A 690 4.015 5.918 -1.029 1.00 12.66 C
ATOM 5253 CD GLN A 690 4.436 7.373 -0.894 1.00 13.46 C
ATOM 5254 OE1 GLN A 690 4.784 7.828 0.198 1.00 16.00 O
ATOM 5255 NE2 GLN A 690 4.393 8.113 -2.001 1.00 15.46 N
ATOM 5256 N CYS A 691 4.855 3.036 2.382 1.00 12.81 N
ATOM 5257 CA CYS A 691 5.743 2.279 3.268 1.00 13.40 C
ATOM 5258 C CYS A 691 5.287 0.840 3.520 1.00 12.90 C
ATOM 5259 O CYS A 691 6.104 -0.021 3.844 1.00 13.48 O
ATOM 5260 CB CYS A 691 6.018 3.019 4.579 1.00 13.40 C
ATOM 5261 SG CYS A 691 4.648 3.097 5.695 1.00 15.68 S
ATOM 5262 N SER A 692 3.994 0.574 3.343 1.00 12.69 N
ATOM 5263 CA SER A 692 3.464 -0.782 3.494 1.00 12.20 C
ATOM 5264 C SER A 692 3.850 -1.671 2.312 1.00 12.27 C
ATOM 5265 O SER A 692 3.716 -2.894 2.380 1.00 11.59 O
ATOM 5266 CB SER A 692 1.941 -0.755 3.618 1.00 12.39 C
ATOM 5267 OG SER A 692 1.340 -0.336 2.403 1.00 11.97 O
ATOM 5268 N GLY A 693 4.303 -1.043 1.229 1.00 12.05 N
ATOM 5269 CA GLY A 693 4.685 -1.763 0.020 1.00 12.48 C
ATOM 5270 C GLY A 693 3.572 -1.902 -1.006 1.00 12.76 C
ATOM 5271 O GLY A 693 3.776 -2.509 -2.062 1.00 12.78 O
ATOM 5272 N MET A 694 2.403 -1.334 -0.714 1.00 12.72 N
ATOM 5273 CA MET A 694 1.241 -1.472 -1.609 1.00 13.19 C
ATOM 5274 C MET A 694 1.444 -0.821 -2.977 1.00 12.87 C
ATOM 5275 O MET A 694 0.956 -1.333 -3.991 1.00 12.68 O
ATOM 5276 CB MET A 694 -0.055 -0.980 -0.954 1.00 13.76 C
ATOM 5277 CG MET A 694 -0.623 -1.919 0.131 1.00 15.62 C
ATOM 5278 SD MET A 694 -0.469 -3.692 -0.202 1.00 20.79 S
ATOM 5279 CE MET A 694 -1.550 -3.892 -1.617 1.00 20.35 C
ATOM 5280 N VAL A 695 2.161 0.301 -3.008 1.00 12.59 N
ATOM 5281 CA VAL A 695 2.480 0.958 -4.281 1.00 12.82 C
ATOM 5282 C VAL A 695 3.416 0.070 -5.115 1.00 12.96 C
ATOM 5283 O VAL A 695 3.225 -0.074 -6.334 1.00 13.23 O
ATOM 5284 CB VAL A 695 3.042 2.387 -4.069 1.00 12.58 C
ATOM 5285 CG1 VAL A 695 3.536 3.000 -5.397 1.00 13.05 C
ATOM 5286 CG2 VAL A 695 1.964 3.274 -3.453 1.00 11.95 C
ATOM 5287 N SER A 696 4.398 -0.548 -4.455 1.00 13.06 N
ATOM 5288 CA SER A 696 5.301 -1.494 -5.120 1.00 13.64 C
ATOM 5289 C SER A 696 4.557 -2.714 -5.665 1.00 13.89 C
ATOM 5290 O SER A 696 4.819 -3.157 -6.783 1.00 14.14 O
ATOM 5291 CB SER A 696 6.417 -1.942 -4.181 1.00 13.58 C
ATOM 5292 OG SER A 696 7.262 -0.856 -3.842 1.00 13.74 O
ATOM 5293 N VAL A 697 3.633 -3.250 -4.870 1.00 13.96 N
ATOM 5294 CA VAL A 697 2.844 -4.415 -5.273 1.00 14.53 C
ATOM 5295 C VAL A 697 1.954 -4.100 -6.473 1.00 14.70 C
ATOM 5296 O VAL A 697 1.843 -4.913 -7.398 1.00 14.68 O
ATOM 5297 CB VAL A 697 2.006 -4.961 -4.096 1.00 14.55 C
ATOM 5298 CG1 VAL A 697 0.965 -5.980 -4.579 1.00 15.44 C
ATOM 5299 CG2 VAL A 697 2.929 -5.570 -3.057 1.00 15.10 C
ATOM 5300 N LEU A 698 1.337 -2.918 -6.463 1.00 15.02 N
ATOM 5301 CA LEU A 698 0.481 -2.496 -7.574 1.00 15.46 C
ATOM 5302 C LEU A 698 1.293 -2.402 -8.864 1.00 16.02 C
ATOM 5303 O LEU A 698 0.823 -2.808 -9.928 1.00 16.50 O
ATOM 5304 CB LEU A 698 -0.219 -1.167 -7.268 1.00 15.41 C
ATOM 5305 CG LEU A 698 -1.299 -0.713 -8.263 1.00 15.15 C
ATOM 5306 CD1 LEU A 698 -2.527 -1.632 -8.249 1.00 16.16 C
ATOM 5307 CD2 LEU A 698 -1.697 0.730 -7.990 1.00 15.51 C
ATOM 5308 N ASP A 699 2.513 -1.882 -8.748 1.00 16.53 N
ATOM 5309 CA ASP A 699 3.458 -1.794 -9.864 1.00 17.32 C
ATOM 5310 C ASP A 699 3.720 -3.188 -10.437 1.00 17.60 C
ATOM 5311 O ASP A 699 3.620 -3.398 -11.652 1.00 17.84 O
ATOM 5312 CB ASP A 699 4.759 -1.133 -9.386 1.00 17.26 C
ATOM 5313 CG ASP A 699 5.740 -0.832 -10.513 1.00 18.54 C
ATOM 5314 OD1 ASP A 699 6.817 -0.282 -10.202 1.00 20.00 O
ATOM 5315 OD2 ASP A 699 5.462 -1.134 -11.692 1.00 19.78 O
ATOM 5316 N LEU A 700 4.025 -4.137 -9.558 1.00 18.37 N
ATOM 5317 CA LEU A 700 4.307 -5.510 -9.966 1.00 19.08 C
ATOM 5318 C LEU A 700 3.102 -6.172 -10.640 1.00 19.97 C
ATOM 5319 O LEU A 700 3.265 -6.927 -11.605 1.00 19.52 O
ATOM 5320 CB LEU A 700 4.782 -6.339 -8.773 1.00 19.08 C
ATOM 5321 CG LEU A 700 5.269 -7.769 -9.030 1.00 18.92 C
ATOM 5322 CD1 LEU A 700 6.406 -7.809 -10.060 1.00 18.57 C
ATOM 5323 CD2 LEU A 700 5.696 -8.410 -7.721 1.00 18.98 C
ATOM 5324 N MET A 701 1.905 -5.870 -10.134 1.00 20.66 N
ATOM 5325 CA MET A 701 0.653 -6.418 -10.673 1.00 21.71 C
ATOM 5326 C MET A 701 0.290 -5.950 -12.083 1.00 21.90 C
ATOM 5327 O MET A 701 -0.552 -6.569 -12.740 1.00 22.17 O
ATOM 5328 CB MET A 701 -0.525 -6.168 -9.720 1.00 22.27 C
ATOM 5329 CG MET A 701 -0.651 -7.137 -8.526 1.00 24.38 C
ATOM 5330 SD MET A 701 -0.360 -8.920 -8.781 1.00 29.62 S
ATOM 5331 CE MET A 701 -0.930 -9.207 -10.445 1.00 29.50 C
ATOM 5332 N GLN A 702 0.920 -4.871 -12.555 1.00 21.96 N
ATOM 5333 CA GLN A 702 0.730 -4.421 -13.941 1.00 21.92 C
ATOM 5334 C GLN A 702 0.971 -5.569 -14.919 1.00 21.73 C
ATOM 5335 O GLN A 702 0.287 -5.678 -15.945 1.00 22.07 O
ATOM 5336 CB GLN A 702 1.653 -3.249 -14.276 1.00 21.59 C
ATOM 5337 CG GLN A 702 1.162 -1.906 -13.761 1.00 22.06 C
ATOM 5338 CD GLN A 702 2.065 -0.758 -14.171 1.00 22.21 C
ATOM 5339 OE1 GLN A 702 1.636 0.171 -14.865 1.00 23.08 O
ATOM 5340 NE2 GLN A 702 3.325 -0.817 -13.751 1.00 21.16 N
ATOM 5341 N GLY A 703 1.935 -6.425 -14.584 1.00 21.32 N
ATOM 5342 CA GLY A 703 2.263 -7.589 -15.403 1.00 20.84 C
ATOM 5343 C GLY A 703 2.421 -8.896 -14.646 1.00 20.28 C
ATOM 5344 O GLY A 703 2.978 -9.853 -15.181 1.00 20.67 O
ATOM 5345 N GLY A 704 1.924 -8.949 -13.411 1.00 19.53 N
ATOM 5346 CA GLY A 704 2.051 -10.149 -12.581 1.00 18.67 C
ATOM 5347 C GLY A 704 0.895 -11.137 -12.674 1.00 18.08 C
ATOM 5348 O GLY A 704 -0.080 -10.908 -13.395 1.00 17.78 O
ATOM 5349 N PHE A 705 1.010 -12.236 -11.931 1.00 17.50 N
ATOM 5350 CA PHE A 705 0.066 -13.354 -12.021 1.00 17.48 C
ATOM 5351 C PHE A 705 -0.162 -13.968 -10.639 1.00 17.36 C
ATOM 5352 O PHE A 705 0.631 -14.805 -10.200 1.00 17.41 O
ATOM 5353 CB PHE A 705 0.605 -14.443 -12.959 1.00 17.54 C
ATOM 5354 CG PHE A 705 0.903 -13.972 -14.358 1.00 17.80 C
ATOM 5355 CD1 PHE A 705 2.163 -13.469 -14.686 1.00 18.10 C
ATOM 5356 CD2 PHE A 705 -0.066 -14.065 -15.360 1.00 17.76 C
ATOM 5357 CE1 PHE A 705 2.449 -13.042 -15.985 1.00 18.23 C
ATOM 5358 CE2 PHE A 705 0.213 -13.649 -16.665 1.00 17.77 C
ATOM 5359 CZ PHE A 705 1.476 -13.134 -16.975 1.00 18.47 C
ATOM 5360 N PRO A 706 -1.243 -13.561 -9.947 1.00 17.24 N
ATOM 5361 CA PRO A 706 -1.446 -14.018 -8.563 1.00 17.34 C
ATOM 5362 C PRO A 706 -1.883 -15.481 -8.420 1.00 17.29 C
ATOM 5363 O PRO A 706 -1.724 -16.063 -7.342 1.00 17.73 O
ATOM 5364 CB PRO A 706 -2.527 -13.066 -8.034 1.00 17.63 C
ATOM 5365 CG PRO A 706 -3.269 -12.613 -9.235 1.00 17.26 C
ATOM 5366 CD PRO A 706 -2.312 -12.650 -10.398 1.00 17.27 C
ATOM 5367 N SER A 707 -2.415 -16.070 -9.491 1.00 17.05 N
ATOM 5368 CA SER A 707 -2.862 -17.467 -9.472 1.00 16.97 C
ATOM 5369 C SER A 707 -2.008 -18.338 -10.389 1.00 16.91 C
ATOM 5370 O SER A 707 -1.646 -17.913 -11.485 1.00 16.91 O
ATOM 5371 CB SER A 707 -4.327 -17.565 -9.903 1.00 16.98 C
ATOM 5372 OG SER A 707 -5.174 -16.874 -9.003 1.00 17.50 O
ATOM 5373 N ARG A 708 -1.686 -19.549 -9.933 1.00 16.94 N
ATOM 5374 CA ARG A 708 -0.900 -20.500 -10.732 1.00 17.25 C
ATOM 5375 C ARG A 708 -1.014 -21.942 -10.263 1.00 17.34 C
ATOM 5376 O ARG A 708 -1.283 -22.210 -9.092 1.00 17.20 O
ATOM 5377 CB ARG A 708 0.583 -20.104 -10.795 1.00 17.20 C
ATOM 5378 CG ARG A 708 1.273 -19.922 -9.453 1.00 17.99 C
ATOM 5379 CD ARG A 708 1.147 -18.483 -8.994 1.00 18.57 C
ATOM 5380 NE ARG A 708 1.832 -18.231 -7.733 1.00 19.53 N
ATOM 5381 CZ ARG A 708 2.148 -17.017 -7.296 1.00 18.56 C
ATOM 5382 NH1 ARG A 708 2.775 -16.871 -6.135 1.00 20.14 N
ATOM 5383 NH2 ARG A 708 1.843 -15.952 -8.022 1.00 19.29 N
ATOM 5384 N ALA A 709 -0.795 -22.861 -11.200 1.00 17.66 N
ATOM 5385 CA ALA A 709 -0.737 -24.290 -10.912 1.00 18.16 C
ATOM 5386 C ALA A 709 0.153 -24.984 -11.938 1.00 18.52 C
ATOM 5387 O ALA A 709 0.347 -24.476 -13.041 1.00 18.74 O
ATOM 5388 CB ALA A 709 -2.140 -24.894 -10.934 1.00 18.12 C
ATOM 5389 N SER A 710 0.698 -26.137 -11.566 1.00 19.01 N
ATOM 5390 CA SER A 710 1.419 -26.988 -12.513 1.00 19.38 C
ATOM 5391 C SER A 710 0.465 -27.453 -13.609 1.00 19.54 C
ATOM 5392 O SER A 710 -0.589 -28.021 -13.311 1.00 19.53 O
ATOM 5393 CB SER A 710 2.008 -28.198 -11.791 1.00 19.27 C
ATOM 5394 OG SER A 710 2.230 -29.271 -12.693 1.00 19.58 O
ATOM 5395 N PHE A 711 0.821 -27.212 -14.870 1.00 20.06 N
ATOM 5396 CA PHE A 711 -0.046 -27.642 -15.970 1.00 20.81 C
ATOM 5397 C PHE A 711 -0.010 -29.158 -16.196 1.00 21.17 C
ATOM 5398 O PHE A 711 -0.962 -29.725 -16.723 1.00 21.44 O
ATOM 5399 CB PHE A 711 0.191 -26.851 -17.272 1.00 20.79 C
ATOM 5400 CG PHE A 711 1.620 -26.836 -17.750 1.00 21.28 C
ATOM 5401 CD1 PHE A 711 2.178 -27.952 -18.377 1.00 21.73 C
ATOM 5402 CD2 PHE A 711 2.393 -25.684 -17.623 1.00 20.52 C
ATOM 5403 CE1 PHE A 711 3.493 -27.929 -18.834 1.00 21.96 C
ATOM 5404 CE2 PHE A 711 3.713 -25.652 -18.081 1.00 21.67 C
ATOM 5405 CZ PHE A 711 4.262 -26.778 -18.688 1.00 21.60 C
ATOM 5406 N HIS A 712 1.078 -29.807 -15.787 1.00 21.78 N
ATOM 5407 CA HIS A 712 1.135 -31.272 -15.815 1.00 22.33 C
ATOM 5408 C HIS A 712 0.185 -31.877 -14.785 1.00 22.33 C
ATOM 5409 O HIS A 712 -0.502 -32.855 -15.075 1.00 22.01 O
ATOM 5410 CB HIS A 712 2.561 -31.791 -15.609 1.00 22.76 C
ATOM 5411 CG HIS A 712 3.411 -31.716 -16.839 1.00 24.21 C
ATOM 5412 ND1 HIS A 712 4.469 -30.841 -16.960 1.00 26.35 N
ATOM 5413 CD2 HIS A 712 3.357 -32.404 -18.004 1.00 25.68 C
ATOM 5414 CE1 HIS A 712 5.032 -30.995 -18.145 1.00 26.57 C
ATOM 5415 NE2 HIS A 712 4.375 -31.936 -18.799 1.00 26.55 N
ATOM 5416 N GLU A 713 0.140 -31.287 -13.590 1.00 22.43 N
ATOM 5417 CA GLU A 713 -0.779 -31.742 -12.544 1.00 22.90 C
ATOM 5418 C GLU A 713 -2.242 -31.518 -12.927 1.00 22.47 C
ATOM 5419 O GLU A 713 -3.099 -32.363 -12.642 1.00 22.39 O
ATOM 5420 CB GLU A 713 -0.461 -31.076 -11.206 1.00 22.85 C
ATOM 5421 CG GLU A 713 0.854 -31.544 -10.592 1.00 23.98 C
ATOM 5422 CD GLU A 713 1.201 -30.822 -9.302 1.00 24.42 C
ATOM 5423 OE1 GLU A 713 0.353 -30.061 -8.783 1.00 26.90 O
ATOM 5424 OE2 GLU A 713 2.330 -31.024 -8.804 1.00 27.56 O
ATOM 5425 N LEU A 714 -2.524 -30.389 -13.576 1.00 22.20 N
ATOM 5426 CA LEU A 714 -3.870 -30.110 -14.087 1.00 22.04 C
ATOM 5427 C LEU A 714 -4.300 -31.162 -15.109 1.00 21.95 C
ATOM 5428 O LEU A 714 -5.373 -31.755 -14.987 1.00 21.79 O
ATOM 5429 CB LEU A 714 -3.951 -28.706 -14.693 1.00 21.85 C
ATOM 5430 CG LEU A 714 -4.048 -27.518 -13.731 1.00 21.86 C
ATOM 5431 CD1 LEU A 714 -4.028 -26.216 -14.517 1.00 21.48 C
ATOM 5432 CD2 LEU A 714 -5.299 -27.592 -12.839 1.00 21.11 C
ATOM 5433 N TYR A 715 -3.446 -31.401 -16.101 1.00 21.97 N
ATOM 5434 CA TYR A 715 -3.679 -32.439 -17.100 1.00 22.05 C
ATOM 5435 C TYR A 715 -3.905 -33.795 -16.430 1.00 21.97 C
ATOM 5436 O TYR A 715 -4.867 -34.488 -16.757 1.00 21.68 O
ATOM 5437 CB TYR A 715 -2.511 -32.494 -18.088 1.00 22.32 C
ATOM 5438 CG TYR A 715 -2.540 -33.654 -19.063 1.00 23.15 C
ATOM 5439 CD1 TYR A 715 -2.031 -34.903 -18.705 1.00 23.74 C
ATOM 5440 CD2 TYR A 715 -3.052 -33.495 -20.349 1.00 23.66 C
ATOM 5441 CE1 TYR A 715 -2.043 -35.971 -19.599 1.00 24.25 C
ATOM 5442 CE2 TYR A 715 -3.064 -34.558 -21.255 1.00 24.44 C
ATOM 5443 CZ TYR A 715 -2.560 -35.789 -20.871 1.00 23.82 C
ATOM 5444 OH TYR A 715 -2.572 -36.846 -21.756 1.00 24.23 O
ATOM 5445 N ASN A 716 -3.027 -34.152 -15.488 1.00 22.00 N
ATOM 5446 CA ASN A 716 -3.132 -35.409 -14.738 1.00 22.28 C
ATOM 5447 C ASN A 716 -4.474 -35.571 -14.030 1.00 22.07 C
ATOM 5448 O ASN A 716 -5.008 -36.677 -13.942 1.00 21.99 O
ATOM 5449 CB ASN A 716 -2.004 -35.530 -13.706 1.00 22.42 C
ATOM 5450 CG ASN A 716 -0.651 -35.875 -14.328 1.00 23.69 C
ATOM 5451 OD1 ASN A 716 0.349 -35.981 -13.614 1.00 26.21 O
ATOM 5452 ND2 ASN A 716 -0.610 -36.045 -15.647 1.00 24.36 N
ATOM 5453 N MET A 717 -5.010 -34.460 -13.528 1.00 21.85 N
ATOM 5454 CA MET A 717 -6.276 -34.467 -12.802 1.00 21.86 C
ATOM 5455 C MET A 717 -7.469 -34.745 -13.719 1.00 21.87 C
ATOM 5456 O MET A 717 -8.397 -35.472 -13.342 1.00 21.88 O
ATOM 5457 CB MET A 717 -6.460 -33.140 -12.059 1.00 21.82 C
ATOM 5458 CG MET A 717 -7.664 -33.105 -11.144 1.00 21.61 C
ATOM 5459 SD MET A 717 -7.645 -31.677 -10.053 1.00 21.69 S
ATOM 5460 CE MET A 717 -7.918 -30.318 -11.189 1.00 21.23 C
ATOM 5461 N TYR A 718 -7.436 -34.171 -14.920 1.00 21.78 N
ATOM 5462 CA TYR A 718 -8.533 -34.310 -15.878 1.00 22.09 C
ATOM 5463 C TYR A 718 -8.396 -35.538 -16.783 1.00 23.05 C
ATOM 5464 O TYR A 718 -9.339 -35.886 -17.502 1.00 22.87 O
ATOM 5465 CB TYR A 718 -8.653 -33.048 -16.740 1.00 21.39 C
ATOM 5466 CG TYR A 718 -9.224 -31.842 -16.018 1.00 20.68 C
ATOM 5467 CD1 TYR A 718 -8.392 -30.946 -15.341 1.00 20.01 C
ATOM 5468 CD2 TYR A 718 -10.595 -31.590 -16.021 1.00 19.53 C
ATOM 5469 CE1 TYR A 718 -8.917 -29.835 -14.679 1.00 19.52 C
ATOM 5470 CE2 TYR A 718 -11.128 -30.482 -15.366 1.00 19.17 C
ATOM 5471 CZ TYR A 718 -10.286 -29.611 -14.696 1.00 19.80 C
ATOM 5472 OH TYR A 718 -10.821 -28.519 -14.042 1.00 19.27 O
ATOM 5473 N LYS A 719 -7.232 -36.187 -16.731 1.00 24.15 N
ATOM 5474 CA LYS A 719 -6.857 -37.240 -17.686 1.00 25.79 C
ATOM 5475 C LYS A 719 -7.894 -38.356 -17.859 1.00 26.50 C
ATOM 5476 O LYS A 719 -8.224 -38.721 -18.988 1.00 26.57 O
ATOM 5477 CB LYS A 719 -5.470 -37.812 -17.351 1.00 25.77 C
ATOM 5478 CG LYS A 719 -4.970 -38.893 -18.317 1.00 27.33 C
ATOM 5479 CD LYS A 719 -3.443 -38.971 -18.370 1.00 29.63 C
ATOM 5480 CE LYS A 719 -2.820 -39.314 -17.017 1.00 30.70 C
ATOM 5481 NZ LYS A 719 -1.370 -38.955 -16.982 1.00 32.41 N
ATOM 5482 N LYS A 720 -8.415 -38.876 -16.749 1.00 27.63 N
ATOM 5483 CA LYS A 720 -9.337 -40.024 -16.795 1.00 28.89 C
ATOM 5484 C LYS A 720 -10.668 -39.747 -17.512 1.00 29.36 C
ATOM 5485 O LYS A 720 -11.366 -40.682 -17.911 1.00 29.42 O
ATOM 5486 CB LYS A 720 -9.582 -40.605 -15.394 1.00 28.81 C
ATOM 5487 CG LYS A 720 -10.171 -39.637 -14.371 1.00 29.30 C
ATOM 5488 CD LYS A 720 -10.714 -40.372 -13.144 1.00 29.70 C
ATOM 5489 CE LYS A 720 -9.605 -40.959 -12.275 1.00 31.67 C
ATOM 5490 NZ LYS A 720 -10.155 -41.726 -11.117 1.00 33.22 N
ATOM 5491 N TYR A 721 -11.005 -38.470 -17.678 1.00 30.09 N
ATOM 5492 CA TYR A 721 -12.254 -38.075 -18.327 1.00 30.99 C
ATOM 5493 C TYR A 721 -12.063 -37.617 -19.774 1.00 31.66 C
ATOM 5494 O TYR A 721 -13.041 -37.416 -20.500 1.00 31.49 O
ATOM 5495 CB TYR A 721 -12.962 -36.985 -17.510 1.00 31.05 C
ATOM 5496 CG TYR A 721 -13.342 -37.431 -16.115 1.00 31.31 C
ATOM 5497 CD1 TYR A 721 -14.383 -38.337 -15.910 1.00 31.56 C
ATOM 5498 CD2 TYR A 721 -12.655 -36.954 -15.000 1.00 31.61 C
ATOM 5499 CE1 TYR A 721 -14.732 -38.756 -14.629 1.00 31.80 C
ATOM 5500 CE2 TYR A 721 -12.997 -37.367 -13.713 1.00 31.76 C
ATOM 5501 CZ TYR A 721 -14.035 -38.267 -13.538 1.00 31.54 C
ATOM 5502 OH TYR A 721 -14.377 -38.679 -12.271 1.00 32.04 O
ATOM 5503 N MET A 722 -10.807 -37.466 -20.186 1.00 32.43 N
ATOM 5504 CA MET A 722 -10.480 -36.876 -21.484 1.00 33.51 C
ATOM 5505 C MET A 722 -10.822 -37.769 -22.669 1.00 34.17 C
ATOM 5506 O MET A 722 -10.612 -38.984 -22.611 1.00 34.14 O
ATOM 5507 CB MET A 722 -8.995 -36.528 -21.555 1.00 33.51 C
ATOM 5508 CG MET A 722 -8.614 -35.247 -20.852 1.00 33.78 C
ATOM 5509 SD MET A 722 -6.932 -34.760 -21.278 1.00 33.78 S
ATOM 5510 CE MET A 722 -6.016 -36.214 -20.790 1.00 34.64 C
ATOM 5511 N PRO A 723 -11.345 -37.165 -23.754 1.00 34.93 N
ATOM 5512 CA PRO A 723 -11.468 -37.913 -25.000 1.00 35.58 C
ATOM 5513 C PRO A 723 -10.094 -38.044 -25.656 1.00 36.08 C
ATOM 5514 O PRO A 723 -9.232 -37.180 -25.465 1.00 36.06 O
ATOM 5515 CB PRO A 723 -12.388 -37.033 -25.849 1.00 35.61 C
ATOM 5516 CG PRO A 723 -12.152 -35.665 -25.359 1.00 35.34 C
ATOM 5517 CD PRO A 723 -11.840 -35.781 -23.889 1.00 35.08 C
ATOM 5518 N ASP A 724 -9.904 -39.122 -26.414 1.00 36.72 N
ATOM 5519 CA ASP A 724 -8.629 -39.416 -27.070 1.00 37.20 C
ATOM 5520 C ASP A 724 -8.043 -38.225 -27.839 1.00 37.17 C
ATOM 5521 O ASP A 724 -6.823 -38.048 -27.870 1.00 37.25 O
ATOM 5522 CB ASP A 724 -8.783 -40.634 -27.989 1.00 37.54 C
ATOM 5523 CG ASP A 724 -7.493 -41.004 -28.697 1.00 38.49 C
ATOM 5524 OD1 ASP A 724 -6.724 -41.824 -28.148 1.00 39.77 O
ATOM 5525 OD2 ASP A 724 -7.245 -40.469 -29.800 1.00 40.24 O
ATOM 5526 N LYS A 725 -8.912 -37.411 -28.438 1.00 37.19 N
ATOM 5527 CA LYS A 725 -8.476 -36.293 -29.287 1.00 37.27 C
ATOM 5528 C LYS A 725 -7.711 -35.183 -28.550 1.00 37.05 C
ATOM 5529 O LYS A 725 -6.873 -34.509 -29.157 1.00 37.11 O
ATOM 5530 CB LYS A 725 -9.647 -35.724 -30.108 1.00 37.29 C
ATOM 5531 CG LYS A 725 -10.754 -35.051 -29.300 1.00 37.64 C
ATOM 5532 CD LYS A 725 -11.979 -34.721 -30.157 1.00 37.74 C
ATOM 5533 CE LYS A 725 -11.794 -33.459 -31.003 1.00 38.60 C
ATOM 5534 NZ LYS A 725 -11.016 -33.702 -32.253 1.00 39.23 N
ATOM 5535 N LEU A 726 -7.998 -34.993 -27.261 1.00 36.79 N
ATOM 5536 CA LEU A 726 -7.228 -34.052 -26.433 1.00 36.52 C
ATOM 5537 C LEU A 726 -6.180 -34.750 -25.571 1.00 36.14 C
ATOM 5538 O LEU A 726 -5.147 -34.161 -25.250 1.00 36.13 O
ATOM 5539 CB LEU A 726 -8.128 -33.195 -25.535 1.00 36.70 C
ATOM 5540 CG LEU A 726 -9.187 -32.288 -26.155 1.00 36.90 C
ATOM 5541 CD1 LEU A 726 -10.542 -32.721 -25.663 1.00 37.38 C
ATOM 5542 CD2 LEU A 726 -8.939 -30.850 -25.751 1.00 37.76 C
ATOM 5543 N ALA A 727 -6.458 -35.995 -25.187 1.00 35.79 N
ATOM 5544 CA ALA A 727 -5.522 -36.793 -24.390 1.00 35.49 C
ATOM 5545 C ALA A 727 -4.187 -36.997 -25.108 1.00 35.26 C
ATOM 5546 O ALA A 727 -3.134 -37.059 -24.470 1.00 35.29 O
ATOM 5547 CB ALA A 727 -6.141 -38.136 -24.027 1.00 35.53 C
ATOM 5548 N ARG A 728 -4.245 -37.085 -26.435 1.00 34.91 N
ATOM 5549 CA ARG A 728 -3.065 -37.319 -27.266 1.00 34.82 C
ATOM 5550 C ARG A 728 -2.164 -36.094 -27.429 1.00 34.12 C
ATOM 5551 O ARG A 728 -0.980 -36.227 -27.752 1.00 34.25 O
ATOM 5552 CB ARG A 728 -3.485 -37.832 -28.645 1.00 34.84 C
ATOM 5553 CG ARG A 728 -3.742 -39.327 -28.691 1.00 35.60 C
ATOM 5554 CD ARG A 728 -3.982 -39.792 -30.120 1.00 35.82 C
ATOM 5555 NE ARG A 728 -3.598 -41.193 -30.304 1.00 38.31 N
ATOM 5556 CZ ARG A 728 -3.563 -41.820 -31.479 1.00 39.41 C
ATOM 5557 NH1 ARG A 728 -3.894 -41.181 -32.597 1.00 39.94 N
ATOM 5558 NH2 ARG A 728 -3.195 -43.095 -31.538 1.00 39.96 N
ATOM 5559 N LEU A 729 -2.725 -34.908 -27.206 1.00 33.26 N
ATOM 5560 CA LEU A 729 -1.996 -33.662 -27.431 1.00 32.20 C
ATOM 5561 C LEU A 729 -1.213 -33.213 -26.202 1.00 31.36 C
ATOM 5562 O LEU A 729 -1.468 -33.673 -25.085 1.00 31.36 O
ATOM 5563 CB LEU A 729 -2.949 -32.552 -27.891 1.00 32.32 C
ATOM 5564 CG LEU A 729 -3.835 -32.801 -29.119 1.00 32.42 C
ATOM 5565 CD1 LEU A 729 -4.792 -31.638 -29.306 1.00 32.86 C
ATOM 5566 CD2 LEU A 729 -3.012 -33.035 -30.386 1.00 32.45 C
ATOM 5567 N ASP A 730 -0.254 -32.316 -26.431 1.00 30.27 N
ATOM 5568 CA ASP A 730 0.539 -31.691 -25.372 1.00 29.30 C
ATOM 5569 C ASP A 730 -0.375 -31.212 -24.239 1.00 28.32 C
ATOM 5570 O ASP A 730 -1.432 -30.641 -24.509 1.00 28.20 O
ATOM 5571 CB ASP A 730 1.339 -30.524 -25.964 1.00 29.57 C
ATOM 5572 CG ASP A 730 2.282 -29.883 -24.963 1.00 30.47 C
ATOM 5573 OD1 ASP A 730 3.484 -30.226 -24.962 1.00 31.49 O
ATOM 5574 OD2 ASP A 730 1.821 -29.034 -24.176 1.00 31.30 O
ATOM 5575 N PRO A 731 0.019 -31.459 -22.970 1.00 27.42 N
ATOM 5576 CA PRO A 731 -0.811 -31.094 -21.813 1.00 26.65 C
ATOM 5577 C PRO A 731 -1.233 -29.624 -21.787 1.00 25.78 C
ATOM 5578 O PRO A 731 -2.284 -29.297 -21.233 1.00 25.55 O
ATOM 5579 CB PRO A 731 0.095 -31.411 -20.619 1.00 26.78 C
ATOM 5580 CG PRO A 731 0.988 -32.489 -21.117 1.00 27.38 C
ATOM 5581 CD PRO A 731 1.269 -32.118 -22.544 1.00 27.37 C
ATOM 5582 N ARG A 732 -0.428 -28.752 -22.392 1.00 24.78 N
ATOM 5583 CA ARG A 732 -0.763 -27.332 -22.480 1.00 23.88 C
ATOM 5584 C ARG A 732 -1.929 -27.073 -23.429 1.00 23.10 C
ATOM 5585 O ARG A 732 -2.659 -26.098 -23.263 1.00 22.57 O
ATOM 5586 CB ARG A 732 0.454 -26.511 -22.905 1.00 24.25 C
ATOM 5587 CG ARG A 732 1.603 -26.561 -21.913 1.00 25.12 C
ATOM 5588 CD ARG A 732 2.796 -25.780 -22.428 1.00 28.40 C
ATOM 5589 NE ARG A 732 3.433 -26.435 -23.568 1.00 30.33 N
ATOM 5590 CZ ARG A 732 4.442 -27.298 -23.477 1.00 32.08 C
ATOM 5591 NH1 ARG A 732 4.942 -27.627 -22.290 1.00 33.22 N
ATOM 5592 NH2 ARG A 732 4.954 -27.835 -24.579 1.00 32.37 N
ATOM 5593 N LEU A 733 -2.097 -27.949 -24.419 1.00 22.30 N
ATOM 5594 CA LEU A 733 -3.189 -27.821 -25.384 1.00 21.66 C
ATOM 5595 C LEU A 733 -4.550 -28.140 -24.779 1.00 21.00 C
ATOM 5596 O LEU A 733 -5.525 -27.441 -25.054 1.00 20.56 O
ATOM 5597 CB LEU A 733 -2.942 -28.673 -26.628 1.00 21.96 C
ATOM 5598 CG LEU A 733 -2.013 -28.055 -27.671 1.00 22.65 C
ATOM 5599 CD1 LEU A 733 -1.759 -29.060 -28.787 1.00 23.51 C
ATOM 5600 CD2 LEU A 733 -2.583 -26.750 -28.226 1.00 22.59 C
ATOM 5601 N PHE A 734 -4.618 -29.188 -23.958 1.00 20.15 N
ATOM 5602 CA PHE A 734 -5.844 -29.444 -23.212 1.00 19.49 C
ATOM 5603 C PHE A 734 -6.164 -28.242 -22.328 1.00 18.90 C
ATOM 5604 O PHE A 734 -7.306 -27.787 -22.288 1.00 18.53 O
ATOM 5605 CB PHE A 734 -5.777 -30.708 -22.348 1.00 19.64 C
ATOM 5606 CG PHE A 734 -6.890 -30.779 -21.334 1.00 19.99 C
ATOM 5607 CD1 PHE A 734 -8.179 -31.125 -21.724 1.00 21.02 C
ATOM 5608 CD2 PHE A 734 -6.664 -30.426 -20.004 1.00 20.95 C
ATOM 5609 CE1 PHE A 734 -9.223 -31.152 -20.804 1.00 21.08 C
ATOM 5610 CE2 PHE A 734 -7.700 -30.454 -19.075 1.00 20.39 C
ATOM 5611 CZ PHE A 734 -8.981 -30.818 -19.475 1.00 20.18 C
ATOM 5612 N CYS A 735 -5.150 -27.739 -21.623 1.00 18.40 N
ATOM 5613 CA CYS A 735 -5.326 -26.581 -20.747 1.00 18.08 C
ATOM 5614 C CYS A 735 -5.891 -25.400 -21.525 1.00 17.27 C
ATOM 5615 O CYS A 735 -6.854 -24.781 -21.088 1.00 16.59 O
ATOM 5616 CB CYS A 735 -4.011 -26.198 -20.058 1.00 18.24 C
ATOM 5617 SG CYS A 735 -3.438 -27.402 -18.829 1.00 20.27 S
ATOM 5618 N LYS A 736 -5.309 -25.110 -22.689 1.00 16.94 N
ATOM 5619 CA LYS A 736 -5.785 -24.010 -23.529 1.00 16.93 C
ATOM 5620 C LYS A 736 -7.249 -24.193 -23.939 1.00 16.66 C
ATOM 5621 O LYS A 736 -8.031 -23.245 -23.901 1.00 16.39 O
ATOM 5622 CB LYS A 736 -4.896 -23.836 -24.763 1.00 17.37 C
ATOM 5623 CG LYS A 736 -3.562 -23.179 -24.459 1.00 18.71 C
ATOM 5624 CD LYS A 736 -2.709 -23.034 -25.711 1.00 21.17 C
ATOM 5625 CE LYS A 736 -1.379 -22.365 -25.378 1.00 23.05 C
ATOM 5626 NZ LYS A 736 -0.499 -22.233 -26.578 1.00 25.00 N
ATOM 5627 N ALA A 737 -7.609 -25.419 -24.315 1.00 16.31 N
ATOM 5628 CA ALA A 737 -8.983 -25.748 -24.675 1.00 16.27 C
ATOM 5629 C ALA A 737 -9.926 -25.510 -23.497 1.00 16.25 C
ATOM 5630 O ALA A 737 -10.975 -24.889 -23.656 1.00 16.31 O
ATOM 5631 CB ALA A 737 -9.075 -27.192 -25.163 1.00 16.42 C
ATOM 5632 N LEU A 738 -9.530 -25.987 -22.316 1.00 16.26 N
ATOM 5633 CA LEU A 738 -10.294 -25.763 -21.088 1.00 16.49 C
ATOM 5634 C LEU A 738 -10.500 -24.273 -20.809 1.00 16.51 C
ATOM 5635 O LEU A 738 -11.624 -23.837 -20.547 1.00 16.08 O
ATOM 5636 CB LEU A 738 -9.611 -26.441 -19.893 1.00 16.53 C
ATOM 5637 CG LEU A 738 -10.296 -26.345 -18.520 1.00 16.87 C
ATOM 5638 CD1 LEU A 738 -11.711 -26.924 -18.555 1.00 17.93 C
ATOM 5639 CD2 LEU A 738 -9.463 -27.035 -17.463 1.00 16.88 C
ATOM 5640 N PHE A 739 -9.415 -23.499 -20.878 1.00 16.87 N
ATOM 5641 CA PHE A 739 -9.478 -22.059 -20.603 1.00 17.07 C
ATOM 5642 C PHE A 739 -10.450 -21.359 -21.543 1.00 17.61 C
ATOM 5643 O PHE A 739 -11.276 -20.552 -21.107 1.00 17.61 O
ATOM 5644 CB PHE A 739 -8.095 -21.396 -20.703 1.00 16.99 C
ATOM 5645 CG PHE A 739 -7.037 -22.007 -19.811 1.00 16.34 C
ATOM 5646 CD1 PHE A 739 -5.692 -21.743 -20.053 1.00 16.37 C
ATOM 5647 CD2 PHE A 739 -7.372 -22.834 -18.739 1.00 16.30 C
ATOM 5648 CE1 PHE A 739 -4.701 -22.291 -19.254 1.00 15.93 C
ATOM 5649 CE2 PHE A 739 -6.385 -23.391 -17.930 1.00 16.26 C
ATOM 5650 CZ PHE A 739 -5.045 -23.118 -18.190 1.00 16.77 C
ATOM 5651 N LYS A 740 -10.353 -21.680 -22.832 1.00 17.97 N
ATOM 5652 CA LYS A 740 -11.196 -21.055 -23.849 1.00 18.58 C
ATOM 5653 C LYS A 740 -12.670 -21.412 -23.689 1.00 18.77 C
ATOM 5654 O LYS A 740 -13.538 -20.555 -23.868 1.00 18.80 O
ATOM 5655 CB LYS A 740 -10.707 -21.405 -25.255 1.00 18.63 C
ATOM 5656 CG LYS A 740 -9.353 -20.808 -25.595 1.00 19.62 C
ATOM 5657 CD LYS A 740 -9.019 -21.003 -27.059 1.00 20.19 C
ATOM 5658 CE LYS A 740 -7.669 -20.383 -27.400 1.00 21.23 C
ATOM 5659 NZ LYS A 740 -7.480 -20.291 -28.868 1.00 21.21 N
ATOM 5660 N ALA A 741 -12.933 -22.676 -23.352 1.00 19.03 N
ATOM 5661 CA ALA A 741 -14.281 -23.165 -23.061 1.00 19.58 C
ATOM 5662 C ALA A 741 -14.876 -22.476 -21.838 1.00 19.86 C
ATOM 5663 O ALA A 741 -16.097 -22.338 -21.732 1.00 20.14 O
ATOM 5664 CB ALA A 741 -14.272 -24.682 -22.874 1.00 19.48 C
ATOM 5665 N LEU A 742 -14.007 -22.044 -20.922 1.00 20.25 N
ATOM 5666 CA LEU A 742 -14.423 -21.290 -19.739 1.00 20.67 C
ATOM 5667 C LEU A 742 -14.480 -19.781 -19.994 1.00 20.86 C
ATOM 5668 O LEU A 742 -14.780 -18.998 -19.087 1.00 21.07 O
ATOM 5669 CB LEU A 742 -13.512 -21.609 -18.544 1.00 20.70 C
ATOM 5670 CG LEU A 742 -13.589 -23.034 -17.984 1.00 21.27 C
ATOM 5671 CD1 LEU A 742 -12.442 -23.276 -17.029 1.00 21.94 C
ATOM 5672 CD2 LEU A 742 -14.927 -23.312 -17.297 1.00 23.02 C
ATOM 5673 N GLY A 743 -14.192 -19.382 -21.231 1.00 20.95 N
ATOM 5674 CA GLY A 743 -14.338 -17.994 -21.658 1.00 21.30 C
ATOM 5675 C GLY A 743 -13.140 -17.101 -21.391 1.00 21.31 C
ATOM 5676 O GLY A 743 -13.240 -15.880 -21.518 1.00 21.46 O
ATOM 5677 N LEU A 744 -12.011 -17.705 -21.024 1.00 21.40 N
ATOM 5678 CA LEU A 744 -10.764 -16.961 -20.818 1.00 21.55 C
ATOM 5679 C LEU A 744 -10.146 -16.534 -22.139 1.00 21.85 C
ATOM 5680 O LEU A 744 -10.150 -17.296 -23.111 1.00 21.74 O
ATOM 5681 CB LEU A 744 -9.748 -17.781 -20.013 1.00 21.37 C
ATOM 5682 CG LEU A 744 -10.004 -17.989 -18.515 1.00 20.93 C
ATOM 5683 CD1 LEU A 744 -8.939 -18.884 -17.905 1.00 21.30 C
ATOM 5684 CD2 LEU A 744 -10.060 -16.648 -17.781 1.00 21.43 C
ATOM 5685 N ASN A 745 -9.623 -15.309 -22.160 1.00 22.23 N
ATOM 5686 CA ASN A 745 -8.919 -14.767 -23.320 1.00 22.88 C
ATOM 5687 C ASN A 745 -7.415 -15.009 -23.207 1.00 22.89 C
ATOM 5688 O ASN A 745 -6.897 -15.230 -22.108 1.00 22.72 O
ATOM 5689 CB ASN A 745 -9.212 -13.268 -23.476 1.00 23.03 C
ATOM 5690 CG ASN A 745 -10.702 -12.962 -23.568 1.00 24.20 C
ATOM 5691 OD1 ASN A 745 -11.396 -13.420 -24.482 1.00 25.69 O
ATOM 5692 ND2 ASN A 745 -11.199 -12.173 -22.620 1.00 25.57 N
ATOM 5693 N GLU A 746 -6.715 -14.967 -24.341 1.00 23.01 N
ATOM 5694 CA GLU A 746 -5.279 -15.263 -24.383 1.00 23.46 C
ATOM 5695 C GLU A 746 -4.449 -14.408 -23.422 1.00 22.88 C
ATOM 5696 O GLU A 746 -3.453 -14.873 -22.870 1.00 23.08 O
ATOM 5697 CB GLU A 746 -4.734 -15.129 -25.809 1.00 23.78 C
ATOM 5698 CG GLU A 746 -5.397 -16.067 -26.800 1.00 26.24 C
ATOM 5699 CD GLU A 746 -4.493 -16.467 -27.955 1.00 29.27 C
ATOM 5700 OE1 GLU A 746 -3.436 -15.825 -28.172 1.00 29.93 O
ATOM 5701 OE2 GLU A 746 -4.857 -17.437 -28.652 1.00 30.71 O
ATOM 5702 N ILE A 747 -4.874 -13.167 -23.215 1.00 22.49 N
ATOM 5703 CA ILE A 747 -4.155 -12.251 -22.330 1.00 22.41 C
ATOM 5704 C ILE A 747 -4.332 -12.567 -20.837 1.00 21.79 C
ATOM 5705 O ILE A 747 -3.584 -12.056 -19.999 1.00 21.83 O
ATOM 5706 CB ILE A 747 -4.515 -10.767 -22.602 1.00 22.63 C
ATOM 5707 CG1 ILE A 747 -6.001 -10.498 -22.339 1.00 23.31 C
ATOM 5708 CG2 ILE A 747 -4.099 -10.368 -24.023 1.00 23.76 C
ATOM 5709 CD1 ILE A 747 -6.316 -9.041 -22.049 1.00 25.48 C
ATOM 5710 N ASP A 748 -5.306 -13.422 -20.523 1.00 20.96 N
ATOM 5711 CA ASP A 748 -5.658 -13.758 -19.135 1.00 20.10 C
ATOM 5712 C ASP A 748 -4.711 -14.756 -18.475 1.00 19.72 C
ATOM 5713 O ASP A 748 -4.680 -14.867 -17.246 1.00 19.04 O
ATOM 5714 CB ASP A 748 -7.086 -14.314 -19.066 1.00 19.99 C
ATOM 5715 CG ASP A 748 -8.136 -13.305 -19.490 1.00 20.77 C
ATOM 5716 OD1 ASP A 748 -9.240 -13.741 -19.881 1.00 22.18 O
ATOM 5717 OD2 ASP A 748 -7.874 -12.082 -19.423 1.00 20.56 O
ATOM 5718 N TYR A 749 -3.956 -15.489 -19.289 1.00 19.31 N
ATOM 5719 CA TYR A 749 -3.076 -16.544 -18.784 1.00 19.46 C
ATOM 5720 C TYR A 749 -1.746 -16.607 -19.534 1.00 19.39 C
ATOM 5721 O TYR A 749 -1.610 -16.059 -20.635 1.00 19.55 O
ATOM 5722 CB TYR A 749 -3.784 -17.911 -18.826 1.00 19.53 C
ATOM 5723 CG TYR A 749 -4.318 -18.283 -20.193 1.00 19.72 C
ATOM 5724 CD1 TYR A 749 -3.525 -18.976 -21.109 1.00 20.19 C
ATOM 5725 CD2 TYR A 749 -5.615 -17.939 -20.574 1.00 19.84 C
ATOM 5726 CE1 TYR A 749 -4.014 -19.318 -22.374 1.00 20.05 C
ATOM 5727 CE2 TYR A 749 -6.109 -18.272 -21.833 1.00 20.60 C
ATOM 5728 CZ TYR A 749 -5.302 -18.957 -22.726 1.00 20.40 C
ATOM 5729 OH TYR A 749 -5.796 -19.285 -23.968 1.00 20.91 O
ATOM 5730 N LYS A 750 -0.774 -17.281 -18.925 1.00 19.45 N
ATOM 5731 CA LYS A 750 0.550 -17.458 -19.512 1.00 19.66 C
ATOM 5732 C LYS A 750 1.194 -18.742 -19.012 1.00 19.53 C
ATOM 5733 O LYS A 750 1.227 -19.002 -17.808 1.00 18.99 O
ATOM 5734 CB LYS A 750 1.450 -16.258 -19.191 1.00 20.19 C
ATOM 5735 CG LYS A 750 2.738 -16.231 -19.994 1.00 21.75 C
ATOM 5736 CD LYS A 750 3.347 -14.840 -20.007 1.00 24.39 C
ATOM 5737 CE LYS A 750 4.465 -14.732 -21.036 1.00 25.98 C
ATOM 5738 NZ LYS A 750 5.646 -15.558 -20.663 1.00 27.20 N
ATOM 5739 N PHE A 751 1.702 -19.543 -19.946 1.00 19.17 N
ATOM 5740 CA PHE A 751 2.424 -20.758 -19.601 1.00 19.31 C
ATOM 5741 C PHE A 751 3.896 -20.478 -19.328 1.00 19.56 C
ATOM 5742 O PHE A 751 4.602 -19.929 -20.176 1.00 19.67 O
ATOM 5743 CB PHE A 751 2.273 -21.813 -20.703 1.00 19.34 C
ATOM 5744 CG PHE A 751 0.889 -22.363 -20.815 1.00 18.90 C
ATOM 5745 CD1 PHE A 751 0.529 -23.516 -20.123 1.00 18.78 C
ATOM 5746 CD2 PHE A 751 -0.068 -21.720 -21.592 1.00 19.05 C
ATOM 5747 CE1 PHE A 751 -0.760 -24.026 -20.212 1.00 18.90 C
ATOM 5748 CE2 PHE A 751 -1.366 -22.226 -21.689 1.00 19.48 C
ATOM 5749 CZ PHE A 751 -1.709 -23.382 -20.992 1.00 18.74 C
ATOM 5750 N GLY A 752 4.340 -20.842 -18.129 1.00 19.72 N
ATOM 5751 CA GLY A 752 5.758 -20.827 -17.788 1.00 20.44 C
ATOM 5752 C GLY A 752 6.373 -22.175 -18.106 1.00 20.77 C
ATOM 5753 O GLY A 752 5.781 -22.976 -18.835 1.00 20.89 O
ATOM 5754 N LEU A 753 7.551 -22.431 -17.544 1.00 21.16 N
ATOM 5755 CA LEU A 753 8.266 -23.688 -17.768 1.00 21.62 C
ATOM 5756 C LEU A 753 7.562 -24.918 -17.189 1.00 21.53 C
ATOM 5757 O LEU A 753 7.591 -25.990 -17.800 1.00 21.73 O
ATOM 5758 CB LEU A 753 9.701 -23.599 -17.233 1.00 21.74 C
ATOM 5759 CG LEU A 753 10.672 -22.703 -18.013 1.00 22.86 C
ATOM 5760 CD1 LEU A 753 11.992 -22.561 -17.267 1.00 24.25 C
ATOM 5761 CD2 LEU A 753 10.910 -23.226 -19.431 1.00 24.04 C
ATOM 5762 N THR A 754 6.944 -24.773 -16.017 1.00 21.26 N
ATOM 5763 CA THR A 754 6.239 -25.899 -15.378 1.00 21.28 C
ATOM 5764 C THR A 754 4.819 -25.533 -14.938 1.00 20.91 C
ATOM 5765 O THR A 754 3.961 -26.406 -14.789 1.00 20.73 O
ATOM 5766 CB THR A 754 7.007 -26.477 -14.156 1.00 21.36 C
ATOM 5767 OG1 THR A 754 6.995 -25.535 -13.075 1.00 21.85 O
ATOM 5768 CG2 THR A 754 8.455 -26.838 -14.511 1.00 21.93 C
ATOM 5769 N LYS A 755 4.581 -24.240 -14.739 1.00 20.48 N
ATOM 5770 CA LYS A 755 3.307 -23.760 -14.216 1.00 20.26 C
ATOM 5771 C LYS A 755 2.572 -22.867 -15.212 1.00 19.36 C
ATOM 5772 O LYS A 755 3.192 -22.153 -16.008 1.00 19.06 O
ATOM 5773 CB LYS A 755 3.525 -23.004 -12.898 1.00 20.27 C
ATOM 5774 CG LYS A 755 4.142 -23.847 -11.785 1.00 21.30 C
ATOM 5775 CD LYS A 755 4.383 -23.026 -10.531 1.00 21.97 C
ATOM 5776 CE LYS A 755 4.988 -23.887 -9.430 1.00 24.23 C
ATOM 5777 NZ LYS A 755 5.060 -23.154 -8.131 1.00 26.81 N
ATOM 5778 N VAL A 756 1.244 -22.917 -15.168 1.00 18.57 N
ATOM 5779 CA VAL A 756 0.423 -21.959 -15.897 1.00 17.80 C
ATOM 5780 C VAL A 756 -0.039 -20.874 -14.917 1.00 17.62 C
ATOM 5781 O VAL A 756 -0.430 -21.176 -13.787 1.00 17.72 O
ATOM 5782 CB VAL A 756 -0.769 -22.641 -16.647 1.00 17.89 C
ATOM 5783 CG1 VAL A 756 -1.693 -23.387 -15.684 1.00 17.32 C
ATOM 5784 CG2 VAL A 756 -1.541 -21.625 -17.476 1.00 17.32 C
ATOM 5785 N PHE A 757 0.028 -19.624 -15.365 1.00 17.24 N
ATOM 5786 CA PHE A 757 -0.229 -18.455 -14.529 1.00 16.73 C
ATOM 5787 C PHE A 757 -1.449 -17.701 -15.022 1.00 16.59 C
ATOM 5788 O PHE A 757 -1.689 -17.623 -16.224 1.00 16.58 O
ATOM 5789 CB PHE A 757 0.980 -17.516 -14.575 1.00 16.61 C
ATOM 5790 CG PHE A 757 2.178 -18.029 -13.834 1.00 16.24 C
ATOM 5791 CD1 PHE A 757 3.036 -18.956 -14.420 1.00 16.38 C
ATOM 5792 CD2 PHE A 757 2.460 -17.574 -12.550 1.00 16.28 C
ATOM 5793 CE1 PHE A 757 4.152 -19.430 -13.731 1.00 16.16 C
ATOM 5794 CE2 PHE A 757 3.567 -18.044 -11.852 1.00 15.91 C
ATOM 5795 CZ PHE A 757 4.418 -18.971 -12.441 1.00 16.68 C
ATOM 5796 N PHE A 758 -2.200 -17.121 -14.091 1.00 16.34 N
ATOM 5797 CA PHE A 758 -3.418 -16.403 -14.423 1.00 16.08 C
ATOM 5798 C PHE A 758 -3.351 -14.985 -13.877 1.00 16.28 C
ATOM 5799 O PHE A 758 -2.830 -14.757 -12.784 1.00 16.16 O
ATOM 5800 CB PHE A 758 -4.641 -17.141 -13.871 1.00 16.17 C
ATOM 5801 CG PHE A 758 -4.761 -18.561 -14.362 1.00 15.85 C
ATOM 5802 CD1 PHE A 758 -4.050 -19.587 -13.746 1.00 16.47 C
ATOM 5803 CD2 PHE A 758 -5.577 -18.868 -15.446 1.00 16.25 C
ATOM 5804 CE1 PHE A 758 -4.142 -20.899 -14.200 1.00 16.00 C
ATOM 5805 CE2 PHE A 758 -5.686 -20.180 -15.904 1.00 15.66 C
ATOM 5806 CZ PHE A 758 -4.965 -21.195 -15.283 1.00 15.59 C
ATOM 5807 N ARG A 759 -3.891 -14.047 -14.646 1.00 16.60 N
ATOM 5808 CA ARG A 759 -3.846 -12.624 -14.314 1.00 17.00 C
ATOM 5809 C ARG A 759 -4.832 -12.278 -13.193 1.00 17.21 C
ATOM 5810 O ARG A 759 -5.712 -13.083 -12.871 1.00 16.88 O
ATOM 5811 CB ARG A 759 -4.132 -11.790 -15.572 1.00 17.26 C
ATOM 5812 CG ARG A 759 -3.011 -11.808 -16.610 1.00 18.65 C
ATOM 5813 CD ARG A 759 -1.930 -10.786 -16.285 1.00 20.66 C
ATOM 5814 NE ARG A 759 -2.405 -9.417 -16.478 1.00 22.66 N
ATOM 5815 CZ ARG A 759 -1.943 -8.354 -15.821 1.00 23.14 C
ATOM 5816 NH1 ARG A 759 -2.448 -7.152 -16.075 1.00 23.96 N
ATOM 5817 NH2 ARG A 759 -0.986 -8.485 -14.909 1.00 22.76 N
ATOM 5818 N PRO A 760 -4.693 -11.077 -12.588 1.00 17.31 N
ATOM 5819 CA PRO A 760 -5.702 -10.664 -11.607 1.00 17.43 C
ATOM 5820 C PRO A 760 -7.088 -10.633 -12.244 1.00 17.18 C
ATOM 5821 O PRO A 760 -7.206 -10.450 -13.461 1.00 17.85 O
ATOM 5822 CB PRO A 760 -5.276 -9.239 -11.228 1.00 17.41 C
ATOM 5823 CG PRO A 760 -3.845 -9.152 -11.586 1.00 17.60 C
ATOM 5824 CD PRO A 760 -3.646 -10.054 -12.768 1.00 17.30 C
ATOM 5825 N GLY A 761 -8.121 -10.828 -11.431 1.00 17.30 N
ATOM 5826 CA GLY A 761 -9.503 -10.766 -11.904 1.00 17.20 C
ATOM 5827 C GLY A 761 -9.990 -12.072 -12.505 1.00 17.08 C
ATOM 5828 O GLY A 761 -11.113 -12.148 -13.014 1.00 17.35 O
ATOM 5829 N LYS A 762 -9.144 -13.098 -12.452 1.00 16.92 N
ATOM 5830 CA LYS A 762 -9.483 -14.405 -13.023 1.00 16.88 C
ATOM 5831 C LYS A 762 -9.505 -15.507 -11.965 1.00 16.42 C
ATOM 5832 O LYS A 762 -9.336 -16.685 -12.285 1.00 15.76 O
ATOM 5833 CB LYS A 762 -8.527 -14.762 -14.169 1.00 16.92 C
ATOM 5834 CG LYS A 762 -8.443 -13.704 -15.275 1.00 19.03 C
ATOM 5835 CD LYS A 762 -9.793 -13.485 -15.947 1.00 21.79 C
ATOM 5836 CE LYS A 762 -9.866 -12.129 -16.638 1.00 24.18 C
ATOM 5837 NZ LYS A 762 -11.214 -11.904 -17.230 1.00 26.02 N
ATOM 5838 N PHE A 763 -9.726 -15.116 -10.709 1.00 16.11 N
ATOM 5839 CA PHE A 763 -9.795 -16.067 -9.599 1.00 15.90 C
ATOM 5840 C PHE A 763 -10.975 -17.025 -9.721 1.00 15.84 C
ATOM 5841 O PHE A 763 -10.858 -18.201 -9.363 1.00 15.94 O
ATOM 5842 CB PHE A 763 -9.852 -15.335 -8.253 1.00 15.85 C
ATOM 5843 CG PHE A 763 -8.576 -14.615 -7.902 1.00 15.72 C
ATOM 5844 CD1 PHE A 763 -8.420 -13.266 -8.200 1.00 16.02 C
ATOM 5845 CD2 PHE A 763 -7.527 -15.291 -7.278 1.00 16.52 C
ATOM 5846 CE1 PHE A 763 -7.238 -12.593 -7.879 1.00 16.18 C
ATOM 5847 CE2 PHE A 763 -6.343 -14.630 -6.948 1.00 16.54 C
ATOM 5848 CZ PHE A 763 -6.200 -13.280 -7.252 1.00 15.53 C
ATOM 5849 N ALA A 764 -12.106 -16.527 -10.217 1.00 15.73 N
ATOM 5850 CA ALA A 764 -13.295 -17.367 -10.393 1.00 15.59 C
ATOM 5851 C ALA A 764 -13.013 -18.540 -11.327 1.00 15.45 C
ATOM 5852 O ALA A 764 -13.223 -19.701 -10.961 1.00 15.29 O
ATOM 5853 CB ALA A 764 -14.471 -16.544 -10.894 1.00 15.85 C
ATOM 5854 N GLU A 765 -12.517 -18.230 -12.525 1.00 15.08 N
ATOM 5855 CA GLU A 765 -12.164 -19.256 -13.503 1.00 15.02 C
ATOM 5856 C GLU A 765 -11.073 -20.187 -12.970 1.00 14.78 C
ATOM 5857 O GLU A 765 -11.173 -21.408 -13.111 1.00 14.57 O
ATOM 5858 CB GLU A 765 -11.731 -18.612 -14.822 1.00 15.38 C
ATOM 5859 CG GLU A 765 -12.840 -17.849 -15.535 1.00 16.19 C
ATOM 5860 CD GLU A 765 -12.975 -16.392 -15.097 1.00 17.96 C
ATOM 5861 OE1 GLU A 765 -13.775 -15.671 -15.733 1.00 20.41 O
ATOM 5862 OE2 GLU A 765 -12.300 -15.961 -14.130 1.00 18.14 O
ATOM 5863 N PHE A 766 -10.047 -19.611 -12.342 1.00 14.50 N
ATOM 5864 CA PHE A 766 -8.986 -20.406 -11.727 1.00 14.41 C
ATOM 5865 C PHE A 766 -9.560 -21.407 -10.721 1.00 14.28 C
ATOM 5866 O PHE A 766 -9.220 -22.587 -10.759 1.00 14.30 O
ATOM 5867 CB PHE A 766 -7.928 -19.510 -11.061 1.00 14.56 C
ATOM 5868 CG PHE A 766 -6.811 -20.277 -10.393 1.00 14.27 C
ATOM 5869 CD1 PHE A 766 -6.743 -20.369 -9.002 1.00 14.97 C
ATOM 5870 CD2 PHE A 766 -5.829 -20.911 -11.155 1.00 14.89 C
ATOM 5871 CE1 PHE A 766 -5.712 -21.081 -8.385 1.00 15.18 C
ATOM 5872 CE2 PHE A 766 -4.796 -21.620 -10.547 1.00 15.77 C
ATOM 5873 CZ PHE A 766 -4.738 -21.708 -9.159 1.00 15.41 C
ATOM 5874 N ASP A 767 -10.442 -20.935 -9.839 1.00 14.43 N
ATOM 5875 CA ASP A 767 -11.052 -21.796 -8.815 1.00 14.70 C
ATOM 5876 C ASP A 767 -11.855 -22.942 -9.420 1.00 15.04 C
ATOM 5877 O ASP A 767 -11.850 -24.061 -8.891 1.00 14.97 O
ATOM 5878 CB ASP A 767 -11.918 -20.975 -7.863 1.00 14.57 C
ATOM 5879 CG ASP A 767 -11.089 -20.103 -6.927 1.00 15.27 C
ATOM 5880 OD1 ASP A 767 -9.862 -20.333 -6.803 1.00 16.71 O
ATOM 5881 OD2 ASP A 767 -11.670 -19.184 -6.316 1.00 16.03 O
ATOM 5882 N GLN A 768 -12.527 -22.661 -10.534 1.00 15.50 N
ATOM 5883 CA GLN A 768 -13.282 -23.684 -11.268 1.00 16.11 C
ATOM 5884 C GLN A 768 -12.357 -24.753 -11.844 1.00 15.96 C
ATOM 5885 O GLN A 768 -12.623 -25.950 -11.712 1.00 15.73 O
ATOM 5886 CB GLN A 768 -14.136 -23.048 -12.374 1.00 16.45 C
ATOM 5887 CG GLN A 768 -15.314 -22.230 -11.853 1.00 18.93 C
ATOM 5888 CD GLN A 768 -16.333 -23.079 -11.114 1.00 22.36 C
ATOM 5889 OE1 GLN A 768 -16.987 -23.938 -11.705 1.00 24.85 O
ATOM 5890 NE2 GLN A 768 -16.472 -22.841 -9.813 1.00 24.89 N
ATOM 5891 N ILE A 769 -11.269 -24.308 -12.472 1.00 16.02 N
ATOM 5892 CA ILE A 769 -10.250 -25.195 -13.043 1.00 16.31 C
ATOM 5893 C ILE A 769 -9.625 -26.106 -11.979 1.00 16.63 C
ATOM 5894 O ILE A 769 -9.317 -27.274 -12.246 1.00 16.61 O
ATOM 5895 CB ILE A 769 -9.145 -24.365 -13.763 1.00 16.32 C
ATOM 5896 CG1 ILE A 769 -9.742 -23.609 -14.957 1.00 16.21 C
ATOM 5897 CG2 ILE A 769 -7.979 -25.242 -14.210 1.00 16.71 C
ATOM 5898 CD1 ILE A 769 -8.925 -22.413 -15.414 1.00 16.10 C
ATOM 5899 N MET A 770 -9.466 -25.571 -10.772 1.00 16.65 N
ATOM 5900 CA MET A 770 -8.761 -26.268 -9.698 1.00 17.50 C
ATOM 5901 C MET A 770 -9.592 -27.307 -8.932 1.00 17.68 C
ATOM 5902 O MET A 770 -9.027 -28.120 -8.201 1.00 17.59 O
ATOM 5903 CB MET A 770 -8.154 -25.254 -8.722 1.00 17.59 C
ATOM 5904 CG MET A 770 -7.014 -24.440 -9.320 1.00 18.10 C
ATOM 5905 SD MET A 770 -5.506 -25.402 -9.535 1.00 21.11 S
ATOM 5906 CE MET A 770 -4.962 -25.557 -7.834 1.00 21.10 C
ATOM 5907 N LYS A 771 -10.916 -27.280 -9.094 1.00 18.36 N
ATOM 5908 CA LYS A 771 -11.793 -28.215 -8.371 1.00 19.06 C
ATOM 5909 C LYS A 771 -11.492 -29.664 -8.749 1.00 19.08 C
ATOM 5910 O LYS A 771 -11.456 -30.009 -9.933 1.00 18.80 O
ATOM 5911 CB LYS A 771 -13.272 -27.896 -8.607 1.00 19.71 C
ATOM 5912 CG LYS A 771 -13.737 -26.593 -7.981 1.00 21.13 C
ATOM 5913 CD LYS A 771 -15.249 -26.516 -7.910 1.00 24.88 C
ATOM 5914 CE LYS A 771 -15.695 -25.185 -7.325 1.00 26.46 C
ATOM 5915 NZ LYS A 771 -17.004 -25.309 -6.617 1.00 29.02 N
ATOM 5916 N SER A 772 -11.272 -30.504 -7.737 1.00 19.18 N
ATOM 5917 CA SER A 772 -10.824 -31.885 -7.956 1.00 19.68 C
ATOM 5918 C SER A 772 -11.948 -32.918 -7.816 1.00 19.95 C
ATOM 5919 O SER A 772 -11.722 -34.118 -7.981 1.00 20.18 O
ATOM 5920 CB SER A 772 -9.674 -32.225 -7.002 1.00 19.59 C
ATOM 5921 OG SER A 772 -10.098 -32.120 -5.656 1.00 20.20 O
ATOM 5922 N ASP A 773 -13.142 -32.426 -7.497 1.00 20.32 N
ATOM 5923 CA ASP A 773 -14.382 -33.201 -7.399 1.00 20.63 C
ATOM 5924 C ASP A 773 -14.696 -33.952 -8.713 1.00 19.77 C
ATOM 5925 O ASP A 773 -14.728 -33.333 -9.773 1.00 19.42 O
ATOM 5926 CB ASP A 773 -15.492 -32.202 -7.039 1.00 21.32 C
ATOM 5927 CG ASP A 773 -16.880 -32.787 -7.115 1.00 23.43 C
ATOM 5928 OD1 ASP A 773 -17.234 -33.633 -6.263 1.00 27.37 O
ATOM 5929 OD2 ASP A 773 -17.637 -32.361 -8.007 1.00 25.38 O
ATOM 5930 N PRO A 774 -14.903 -35.291 -8.651 1.00 19.50 N
ATOM 5931 CA PRO A 774 -15.166 -36.060 -9.882 1.00 19.13 C
ATOM 5932 C PRO A 774 -16.296 -35.488 -10.747 1.00 18.68 C
ATOM 5933 O PRO A 774 -16.134 -35.370 -11.968 1.00 18.47 O
ATOM 5934 CB PRO A 774 -15.526 -37.455 -9.355 1.00 19.42 C
ATOM 5935 CG PRO A 774 -14.785 -37.552 -8.072 1.00 19.76 C
ATOM 5936 CD PRO A 774 -14.871 -36.174 -7.468 1.00 19.54 C
ATOM 5937 N ASP A 775 -17.415 -35.126 -10.124 1.00 18.12 N
ATOM 5938 CA ASP A 775 -18.529 -34.506 -10.837 1.00 18.17 C
ATOM 5939 C ASP A 775 -18.097 -33.252 -11.598 1.00 17.70 C
ATOM 5940 O ASP A 775 -18.463 -33.073 -12.763 1.00 17.36 O
ATOM 5941 CB ASP A 775 -19.667 -34.147 -9.872 1.00 18.46 C
ATOM 5942 CG ASP A 775 -20.477 -35.359 -9.422 1.00 20.08 C
ATOM 5943 OD1 ASP A 775 -20.145 -36.503 -9.806 1.00 21.63 O
ATOM 5944 OD2 ASP A 775 -21.456 -35.154 -8.670 1.00 21.40 O
ATOM 5945 N HIS A 776 -17.322 -32.390 -10.937 1.00 17.30 N
ATOM 5946 CA HIS A 776 -16.911 -31.122 -11.547 1.00 17.28 C
ATOM 5947 C HIS A 776 -15.892 -31.313 -12.670 1.00 16.95 C
ATOM 5948 O HIS A 776 -15.951 -30.614 -13.681 1.00 16.91 O
ATOM 5949 CB HIS A 776 -16.383 -30.133 -10.500 1.00 17.49 C
ATOM 5950 CG HIS A 776 -16.428 -28.705 -10.954 1.00 18.06 C
ATOM 5951 ND1 HIS A 776 -15.369 -28.089 -11.587 1.00 18.70 N
ATOM 5952 CD2 HIS A 776 -17.416 -27.779 -10.890 1.00 19.37 C
ATOM 5953 CE1 HIS A 776 -15.695 -26.843 -11.877 1.00 18.49 C
ATOM 5954 NE2 HIS A 776 -16.931 -26.630 -11.464 1.00 19.00 N
ATOM 5955 N LEU A 777 -14.969 -32.258 -12.495 1.00 16.74 N
ATOM 5956 CA LEU A 777 -14.001 -32.589 -13.549 1.00 16.60 C
ATOM 5957 C LEU A 777 -14.715 -33.069 -14.813 1.00 16.70 C
ATOM 5958 O LEU A 777 -14.420 -32.607 -15.925 1.00 16.33 O
ATOM 5959 CB LEU A 777 -13.011 -33.652 -13.067 1.00 16.57 C
ATOM 5960 CG LEU A 777 -12.098 -33.274 -11.896 1.00 16.64 C
ATOM 5961 CD1 LEU A 777 -11.424 -34.514 -11.322 1.00 17.78 C
ATOM 5962 CD2 LEU A 777 -11.070 -32.239 -12.326 1.00 17.69 C
ATOM 5963 N ALA A 778 -15.668 -33.982 -14.628 1.00 16.59 N
ATOM 5964 CA ALA A 778 -16.491 -34.481 -15.724 1.00 16.66 C
ATOM 5965 C ALA A 778 -17.289 -33.359 -16.375 1.00 16.72 C
ATOM 5966 O ALA A 778 -17.398 -33.303 -17.603 1.00 16.66 O
ATOM 5967 CB ALA A 778 -17.418 -35.585 -15.231 1.00 16.40 C
ATOM 5968 N GLU A 779 -17.833 -32.461 -15.555 1.00 16.91 N
ATOM 5969 CA GLU A 779 -18.596 -31.323 -16.061 1.00 17.50 C
ATOM 5970 C GLU A 779 -17.773 -30.451 -17.006 1.00 17.53 C
ATOM 5971 O GLU A 779 -18.246 -30.078 -18.081 1.00 17.51 O
ATOM 5972 CB GLU A 779 -19.165 -30.461 -14.927 1.00 17.38 C
ATOM 5973 CG GLU A 779 -20.160 -29.423 -15.440 1.00 18.21 C
ATOM 5974 CD GLU A 779 -20.741 -28.517 -14.369 1.00 18.56 C
ATOM 5975 OE1 GLU A 779 -21.510 -27.608 -14.743 1.00 22.17 O
ATOM 5976 OE2 GLU A 779 -20.443 -28.696 -13.169 1.00 20.72 O
ATOM 5977 N LEU A 780 -16.547 -30.128 -16.601 1.00 17.66 N
ATOM 5978 CA LEU A 780 -15.708 -29.241 -17.404 1.00 18.10 C
ATOM 5979 C LEU A 780 -15.215 -29.904 -18.687 1.00 18.31 C
ATOM 5980 O LEU A 780 -15.177 -29.265 -19.735 1.00 18.31 O
ATOM 5981 CB LEU A 780 -14.545 -28.668 -16.586 1.00 17.97 C
ATOM 5982 CG LEU A 780 -14.884 -27.781 -15.379 1.00 18.83 C
ATOM 5983 CD1 LEU A 780 -13.678 -26.909 -15.033 1.00 17.91 C
ATOM 5984 CD2 LEU A 780 -16.130 -26.911 -15.574 1.00 20.17 C
ATOM 5985 N VAL A 781 -14.863 -31.185 -18.609 1.00 18.70 N
ATOM 5986 CA VAL A 781 -14.472 -31.928 -19.807 1.00 19.27 C
ATOM 5987 C VAL A 781 -15.637 -31.966 -20.807 1.00 19.71 C
ATOM 5988 O VAL A 781 -15.435 -31.754 -22.004 1.00 19.57 O
ATOM 5989 CB VAL A 781 -13.920 -33.337 -19.478 1.00 19.31 C
ATOM 5990 CG1 VAL A 781 -13.690 -34.153 -20.752 1.00 19.12 C
ATOM 5991 CG2 VAL A 781 -12.612 -33.224 -18.691 1.00 19.60 C
ATOM 5992 N LYS A 782 -16.853 -32.197 -20.310 1.00 19.99 N
ATOM 5993 CA LYS A 782 -18.032 -32.171 -21.173 1.00 20.53 C
ATOM 5994 C LYS A 782 -18.194 -30.809 -21.861 1.00 21.00 C
ATOM 5995 O LYS A 782 -18.575 -30.745 -23.034 1.00 20.86 O
ATOM 5996 CB LYS A 782 -19.300 -32.563 -20.405 1.00 20.61 C
ATOM 5997 CG LYS A 782 -20.484 -32.861 -21.323 1.00 20.88 C
ATOM 5998 CD LYS A 782 -21.669 -33.455 -20.578 1.00 20.59 C
ATOM 5999 CE LYS A 782 -22.820 -33.717 -21.542 1.00 21.24 C
ATOM 6000 NZ LYS A 782 -24.004 -34.321 -20.867 1.00 20.86 N
ATOM 6001 N ARG A 783 -17.883 -29.733 -21.136 1.00 21.43 N
ATOM 6002 CA ARG A 783 -17.915 -28.382 -21.700 1.00 22.09 C
ATOM 6003 C ARG A 783 -16.881 -28.224 -22.815 1.00 22.16 C
ATOM 6004 O ARG A 783 -17.176 -27.639 -23.861 1.00 22.37 O
ATOM 6005 CB ARG A 783 -17.686 -27.321 -20.624 1.00 22.32 C
ATOM 6006 CG ARG A 783 -18.835 -27.149 -19.651 1.00 23.67 C
ATOM 6007 CD ARG A 783 -18.635 -25.900 -18.816 1.00 25.80 C
ATOM 6008 NE ARG A 783 -19.395 -25.936 -17.567 1.00 28.39 N
ATOM 6009 CZ ARG A 783 -19.263 -25.041 -16.590 1.00 29.31 C
ATOM 6010 NH1 ARG A 783 -19.987 -25.149 -15.483 1.00 30.11 N
ATOM 6011 NH2 ARG A 783 -18.404 -24.036 -16.719 1.00 28.78 N
ATOM 6012 N VAL A 784 -15.679 -28.749 -22.580 1.00 22.33 N
ATOM 6013 CA VAL A 784 -14.609 -28.765 -23.585 1.00 22.60 C
ATOM 6014 C VAL A 784 -15.066 -29.524 -24.833 1.00 23.28 C
ATOM 6015 O VAL A 784 -14.921 -29.029 -25.952 1.00 22.76 O
ATOM 6016 CB VAL A 784 -13.296 -29.366 -23.020 1.00 22.52 C
ATOM 6017 CG1 VAL A 784 -12.224 -29.495 -24.103 1.00 22.41 C
ATOM 6018 CG2 VAL A 784 -12.779 -28.512 -21.866 1.00 22.33 C
ATOM 6019 N ASN A 785 -15.641 -30.709 -24.626 1.00 23.98 N
ATOM 6020 CA ASN A 785 -16.190 -31.512 -25.725 1.00 25.02 C
ATOM 6021 C ASN A 785 -17.217 -30.761 -26.571 1.00 25.65 C
ATOM 6022 O ASN A 785 -17.191 -30.841 -27.800 1.00 26.10 O
ATOM 6023 CB ASN A 785 -16.793 -32.814 -25.191 1.00 24.90 C
ATOM 6024 CG ASN A 785 -15.743 -33.780 -24.677 1.00 24.83 C
ATOM 6025 OD1 ASN A 785 -14.578 -33.732 -25.081 1.00 25.23 O
ATOM 6026 ND2 ASN A 785 -16.153 -34.676 -23.788 1.00 24.18 N
ATOM 6027 N HIS A 786 -18.109 -30.027 -25.912 1.00 26.35 N
ATOM 6028 CA HIS A 786 -19.113 -29.227 -26.610 1.00 27.04 C
ATOM 6029 C HIS A 786 -18.489 -28.035 -27.341 1.00 26.95 C
ATOM 6030 O HIS A 786 -18.968 -27.630 -28.403 1.00 27.25 O
ATOM 6031 CB HIS A 786 -20.196 -28.750 -25.641 1.00 27.39 C
ATOM 6032 CG HIS A 786 -21.392 -28.162 -26.321 1.00 28.95 C
ATOM 6033 ND1 HIS A 786 -21.609 -26.803 -26.402 1.00 30.26 N
ATOM 6034 CD2 HIS A 786 -22.428 -28.748 -26.967 1.00 30.19 C
ATOM 6035 CE1 HIS A 786 -22.733 -26.578 -27.060 1.00 30.47 C
ATOM 6036 NE2 HIS A 786 -23.249 -27.742 -27.414 1.00 30.96 N
ATOM 6037 N TRP A 787 -17.423 -27.485 -26.763 1.00 26.66 N
ATOM 6038 CA TRP A 787 -16.694 -26.360 -27.347 1.00 26.27 C
ATOM 6039 C TRP A 787 -15.968 -26.774 -28.627 1.00 26.54 C
ATOM 6040 O TRP A 787 -15.937 -26.019 -29.598 1.00 26.46 O
ATOM 6041 CB TRP A 787 -15.717 -25.781 -26.321 1.00 25.76 C
ATOM 6042 CG TRP A 787 -14.824 -24.690 -26.834 1.00 25.03 C
ATOM 6043 CD1 TRP A 787 -15.140 -23.369 -26.990 1.00 24.48 C
ATOM 6044 CD2 TRP A 787 -13.459 -24.827 -27.242 1.00 24.24 C
ATOM 6045 NE1 TRP A 787 -14.055 -22.676 -27.477 1.00 24.58 N
ATOM 6046 CE2 TRP A 787 -13.009 -23.548 -27.637 1.00 24.28 C
ATOM 6047 CE3 TRP A 787 -12.571 -25.908 -27.314 1.00 24.25 C
ATOM 6048 CZ2 TRP A 787 -11.710 -23.323 -28.102 1.00 24.62 C
ATOM 6049 CZ3 TRP A 787 -11.280 -25.682 -27.771 1.00 24.38 C
ATOM 6050 CH2 TRP A 787 -10.862 -24.399 -28.158 1.00 24.71 C
ATOM 6051 N LEU A 788 -15.394 -27.976 -28.620 1.00 26.98 N
ATOM 6052 CA LEU A 788 -14.727 -28.527 -29.798 1.00 27.57 C
ATOM 6053 C LEU A 788 -15.723 -28.862 -30.906 1.00 27.81 C
ATOM 6054 O LEU A 788 -16.751 -29.497 -30.660 1.00 28.32 O
ATOM 6055 CB LEU A 788 -13.913 -29.771 -29.428 1.00 27.75 C
ATOM 6056 CG LEU A 788 -12.570 -29.576 -28.719 1.00 28.30 C
ATOM 6057 CD1 LEU A 788 -12.063 -30.912 -28.218 1.00 29.42 C
ATOM 6058 CD2 LEU A 788 -11.536 -28.918 -29.629 1.00 29.03 C
TER 6059 LEU A 788
HETATM 6060 PB ADP A1789 -5.417 -1.654 15.916 1.00 8.11 P
HETATM 6061 O1B ADP A1789 -5.708 -3.034 16.472 1.00 6.94 O
HETATM 6062 O2B ADP A1789 -4.532 -0.835 16.806 1.00 9.16 O
HETATM 6063 O3B ADP A1789 -4.962 -1.639 14.474 1.00 7.97 O
HETATM 6064 PA ADP A1789 -8.272 -1.380 16.276 1.00 8.83 P
HETATM 6065 O1A ADP A1789 -8.635 -2.580 15.453 1.00 7.95 O
HETATM 6066 O2A ADP A1789 -8.306 -1.475 17.784 1.00 8.06 O
HETATM 6067 O3A ADP A1789 -6.810 -0.822 15.871 1.00 8.13 O
HETATM 6068 O5' ADP A1789 -9.208 -0.152 15.829 1.00 8.81 O
HETATM 6069 C5' ADP A1789 -9.158 1.081 16.536 1.00 8.88 C
HETATM 6070 C4' ADP A1789 -10.581 1.609 16.646 1.00 9.91 C
HETATM 6071 O4' ADP A1789 -11.035 1.956 15.342 1.00 9.72 O
HETATM 6072 C3' ADP A1789 -11.605 0.597 17.144 1.00 10.20 C
HETATM 6073 O3' ADP A1789 -11.667 0.516 18.571 1.00 11.35 O
HETATM 6074 C2' ADP A1789 -12.907 1.091 16.547 1.00 10.14 C
HETATM 6075 O2' ADP A1789 -13.377 2.241 17.274 1.00 9.54 O
HETATM 6076 C1' ADP A1789 -12.420 1.607 15.210 1.00 10.33 C
HETATM 6077 N9 ADP A1789 -12.542 0.634 14.095 1.00 10.32 N
HETATM 6078 C8 ADP A1789 -11.530 0.004 13.463 1.00 10.50 C
HETATM 6079 N7 ADP A1789 -11.984 -0.767 12.442 1.00 10.34 N
HETATM 6080 C5 ADP A1789 -13.320 -0.622 12.411 1.00 10.23 C
HETATM 6081 C6 ADP A1789 -14.433 -1.153 11.591 1.00 10.50 C
HETATM 6082 N6 ADP A1789 -14.205 -2.014 10.570 1.00 10.90 N
HETATM 6083 N1 ADP A1789 -15.688 -0.743 11.901 1.00 11.06 N
HETATM 6084 C2 ADP A1789 -15.941 0.111 12.911 1.00 10.82 C
HETATM 6085 N3 ADP A1789 -14.984 0.636 13.695 1.00 11.45 N
HETATM 6086 C4 ADP A1789 -13.679 0.308 13.495 1.00 10.43 C
HETATM 6087 V VO4 A1791 -2.938 -1.236 18.203 1.00 9.06 V
HETATM 6088 O1 VO4 A1791 -1.500 -1.550 19.454 1.00 8.51 O
HETATM 6089 O2 VO4 A1791 -4.023 -2.639 18.806 1.00 9.30 O
HETATM 6090 O3 VO4 A1791 -3.305 0.516 18.780 1.00 10.09 O
HETATM 6091 O4 VO4 A1791 -1.839 -1.495 16.688 1.00 11.10 O
HETATM 6092 C1 EDO A1792 5.052 -14.764 26.556 1.00 32.24 C
HETATM 6093 O1 EDO A1792 3.809 -14.105 26.285 1.00 31.99 O
HETATM 6094 C2 EDO A1792 5.919 -14.731 25.307 1.00 32.14 C
HETATM 6095 O2 EDO A1792 6.044 -13.379 24.856 1.00 31.75 O
HETATM 6096 C1 EDO A1793 4.205 -7.310 19.613 1.00 16.80 C
HETATM 6097 O1 EDO A1793 2.787 -7.207 19.800 1.00 16.33 O
HETATM 6098 C2 EDO A1793 4.751 -5.907 19.359 1.00 16.71 C
HETATM 6099 O2 EDO A1793 4.441 -5.543 18.013 1.00 16.46 O
HETATM 6100 C1 EDO A1794 2.119 7.738 15.298 1.00 19.16 C
HETATM 6101 O1 EDO A1794 1.616 6.779 16.241 1.00 17.35 O
HETATM 6102 C2 EDO A1794 0.978 8.572 14.712 1.00 20.12 C
HETATM 6103 O2 EDO A1794 -0.016 7.699 14.168 1.00 20.24 O
HETATM 6104 C1 EDO A1795 -16.979 -2.906 2.404 1.00 18.23 C
HETATM 6105 O1 EDO A1795 -16.030 -2.135 1.653 1.00 16.05 O
HETATM 6106 C2 EDO A1795 -17.976 -2.017 3.136 1.00 17.97 C
HETATM 6107 O2 EDO A1795 -17.309 -0.985 3.874 1.00 17.67 O
HETATM 6108 C1 EDO A1796 -10.497 14.477 -5.689 1.00 35.22 C
HETATM 6109 O1 EDO A1796 -9.171 14.960 -5.916 1.00 36.03 O
HETATM 6110 C2 EDO A1796 -10.452 13.325 -4.696 1.00 34.41 C
HETATM 6111 O2 EDO A1796 -9.307 12.496 -4.943 1.00 32.89 O
HETATM 6112 C1 EDO A1797 8.292 11.158 15.662 1.00 27.06 C
HETATM 6113 O1 EDO A1797 8.683 10.347 14.519 1.00 28.42 O
HETATM 6114 C2 EDO A1797 8.802 10.474 16.935 1.00 25.89 C
HETATM 6115 O2 EDO A1797 10.235 10.507 16.922 1.00 24.78 O
HETATM 6116 C1 EDO A1798 3.235 -4.816 22.868 1.00 21.35 C
HETATM 6117 O1 EDO A1798 3.473 -6.203 22.584 1.00 21.00 O
HETATM 6118 C2 EDO A1798 4.283 -4.202 23.807 1.00 22.81 C
HETATM 6119 O2 EDO A1798 5.015 -5.184 24.559 1.00 23.39 O
HETATM 6120 S SO4 A1799 -25.008 -3.728 43.326 1.00 22.55 S
HETATM 6121 O1 SO4 A1799 -24.299 -3.568 42.060 1.00 24.72 O
HETATM 6122 O2 SO4 A1799 -26.306 -3.066 43.243 1.00 23.92 O
HETATM 6123 O3 SO4 A1799 -25.237 -5.146 43.561 1.00 23.86 O
HETATM 6124 O4 SO4 A1799 -24.204 -3.202 44.422 1.00 22.90 O
HETATM 6125 S SO4 A1800 21.317 -15.780 19.377 0.50 26.97 S
HETATM 6126 O1 SO4 A1800 21.257 -16.782 18.317 0.50 27.10 O
HETATM 6127 O2 SO4 A1800 20.034 -15.092 19.481 0.50 27.08 O
HETATM 6128 O3 SO4 A1800 21.618 -16.437 20.645 0.50 26.94 O
HETATM 6129 O4 SO4 A1800 22.359 -14.808 19.069 0.50 27.05 O
HETATM 6130 MG MG A1801 -5.139 -3.919 18.238 1.00 7.52 MG
HETATM 6131 O HOH A2001 -3.690 18.125 -18.929 1.00 28.06 O
HETATM 6132 O HOH A2002 -4.717 11.654 -17.552 1.00 25.09 O
HETATM 6133 O HOH A2003 -7.853 8.629 -11.031 1.00 15.38 O
HETATM 6134 O HOH A2004 2.052 13.737 0.177 1.00 25.60 O
HETATM 6135 O HOH A2005 4.232 21.807 -1.178 1.00 30.15 O
HETATM 6136 O HOH A2006 2.325 21.017 -5.102 1.00 30.12 O
HETATM 6137 O HOH A2007 -0.711 15.461 6.168 1.00 37.08 O
HETATM 6138 O HOH A2008 3.420 17.336 -1.808 1.00 27.82 O
HETATM 6139 O HOH A2009 0.157 23.669 -1.946 1.00 36.89 O
HETATM 6140 O HOH A2010 2.780 15.713 1.990 1.00 28.21 O
HETATM 6141 O HOH A2011 3.143 19.794 -2.697 1.00 26.65 O
HETATM 6142 O HOH A2012 -3.045 14.661 5.118 1.00 18.18 O
HETATM 6143 O HOH A2013 -7.151 14.538 1.760 1.00 21.27 O
HETATM 6144 O HOH A2014 -6.442 12.427 -1.617 1.00 15.98 O
HETATM 6145 O HOH A2015 -11.316 13.847 -8.807 1.00 24.00 O
HETATM 6146 O HOH A2016 2.473 14.538 -2.409 1.00 27.71 O
HETATM 6147 O HOH A2017 -7.128 16.255 -4.005 1.00 25.67 O
HETATM 6148 O HOH A2018 -6.534 21.159 -7.635 1.00 26.49 O
HETATM 6149 O HOH A2019 -1.340 23.401 -4.626 1.00 33.76 O
HETATM 6150 O HOH A2020 -7.972 26.893 -8.119 1.00 32.96 O
HETATM 6151 O HOH A2021 -16.338 12.992 0.548 1.00 31.44 O
HETATM 6152 O HOH A2022 -1.763 19.809 -22.543 1.00 36.02 O
HETATM 6153 O HOH A2023 -10.057 12.708 -10.871 1.00 31.73 O
HETATM 6154 O HOH A2024 -20.687 9.182 -7.070 1.00 28.05 O
HETATM 6155 O HOH A2025 -20.138 -2.384 -2.389 1.00 26.09 O
HETATM 6156 O HOH A2026 -11.958 -7.984 -11.811 1.00 28.23 O
HETATM 6157 O HOH A2027 -10.263 -9.617 -6.831 1.00 33.97 O
HETATM 6158 O HOH A2028 -13.163 -6.858 -9.589 1.00 19.91 O
HETATM 6159 O HOH A2029 6.694 24.010 -16.932 1.00 25.71 O
HETATM 6160 O HOH A2030 3.912 4.657 -11.501 1.00 27.53 O
HETATM 6161 O HOH A2031 -9.294 27.013 -11.380 1.00 38.50 O
HETATM 6162 O HOH A2032 -7.061 28.333 -11.957 1.00 44.42 O
HETATM 6163 O HOH A2033 -14.672 10.512 3.365 1.00 20.35 O
HETATM 6164 O HOH A2034 -17.111 11.697 2.848 1.00 24.38 O
HETATM 6165 O HOH A2035 -23.178 1.268 3.472 1.00 30.17 O
HETATM 6166 O HOH A2036 -23.486 -2.909 0.827 1.00 29.70 O
HETATM 6167 O HOH A2037 4.199 19.992 -7.345 1.00 22.80 O
HETATM 6168 O HOH A2038 5.076 26.135 -8.016 1.00 31.87 O
HETATM 6169 O HOH A2039 4.493 12.881 -16.390 1.00 38.23 O
HETATM 6170 O HOH A2040 6.338 9.043 -12.628 1.00 35.79 O
HETATM 6171 O HOH A2041 10.956 14.432 -13.378 1.00 30.91 O
HETATM 6172 O HOH A2042 -20.289 6.826 16.002 1.00 22.30 O
HETATM 6173 O HOH A2043 -16.040 8.784 17.379 1.00 27.48 O
HETATM 6174 O HOH A2044 -18.689 -4.413 14.332 1.00 36.12 O
HETATM 6175 O HOH A2045 -23.862 -2.097 13.181 1.00 30.71 O
HETATM 6176 O HOH A2046 -25.209 -9.516 47.759 1.00 32.81 O
HETATM 6177 O HOH A2047 1.570 11.590 -17.219 1.00 35.53 O
HETATM 6178 O HOH A2048 -7.285 10.439 -18.385 1.00 23.36 O
HETATM 6179 O HOH A2049 -26.466 -16.150 0.898 1.00 30.15 O
HETATM 6180 O HOH A2050 -20.834 -5.674 3.029 1.00 28.89 O
HETATM 6181 O HOH A2051 -10.151 10.107 -11.707 1.00 16.97 O
HETATM 6182 O HOH A2052 -10.749 4.471 -16.362 1.00 34.43 O
HETATM 6183 O HOH A2053 -19.467 -3.909 -0.213 1.00 19.44 O
HETATM 6184 O HOH A2054 -9.553 6.071 -17.746 1.00 28.73 O
HETATM 6185 O HOH A2055 -24.996 -11.961 -2.841 1.00 35.95 O
HETATM 6186 O HOH A2056 -20.078 8.522 -13.084 1.00 34.41 O
HETATM 6187 O HOH A2057 -18.871 -17.001 -10.391 1.00 34.52 O
HETATM 6188 O HOH A2058 -12.262 -7.620 -7.162 1.00 19.71 O
HETATM 6189 O HOH A2059 -14.686 11.823 -6.968 1.00 34.15 O
HETATM 6190 O HOH A2060 -17.816 9.651 -6.172 1.00 23.66 O
HETATM 6191 O HOH A2061 -12.591 7.369 -9.979 1.00 19.81 O
HETATM 6192 O HOH A2062 -18.016 0.042 -7.506 1.00 24.58 O
HETATM 6193 O HOH A2063 -3.531 -22.061 -5.578 1.00 31.68 O
HETATM 6194 O HOH A2064 -15.075 -3.008 -9.927 1.00 18.75 O
HETATM 6195 O HOH A2065 -17.727 -2.408 -3.863 1.00 17.29 O
HETATM 6196 O HOH A2066 -18.428 -8.080 -6.814 1.00 24.55 O
HETATM 6197 O HOH A2067 -9.025 -7.223 -11.706 1.00 25.52 O
HETATM 6198 O HOH A2068 -8.184 -9.599 -8.813 1.00 26.16 O
HETATM 6199 O HOH A2069 -1.745 -28.320 12.813 1.00 32.49 O
HETATM 6200 O HOH A2070 -12.497 -4.333 -10.168 1.00 19.01 O
HETATM 6201 O HOH A2071 -5.520 -2.433 -15.772 1.00 29.36 O
HETATM 6202 O HOH A2072 -7.264 8.763 -20.547 1.00 24.76 O
HETATM 6203 O HOH A2073 2.458 1.287 -10.909 1.00 26.64 O
HETATM 6204 O HOH A2074 0.353 5.167 -14.560 1.00 20.04 O
HETATM 6205 O HOH A2075 5.235 5.793 -7.425 1.00 25.52 O
HETATM 6206 O HOH A2076 3.137 4.796 -8.793 1.00 17.16 O
HETATM 6207 O HOH A2077 -5.070 10.989 -6.073 1.00 14.52 O
HETATM 6208 O HOH A2078 -8.318 6.498 -9.532 1.00 10.45 O
HETATM 6209 O HOH A2079 -10.934 5.290 -9.324 1.00 14.23 O
HETATM 6210 O HOH A2080 -13.127 9.799 1.232 1.00 17.66 O
HETATM 6211 O HOH A2081 -13.907 11.382 -3.192 1.00 40.04 O
HETATM 6212 O HOH A2082 -19.417 10.392 2.571 1.00 30.58 O
HETATM 6213 O HOH A2083 -22.158 2.714 -0.802 1.00 23.01 O
HETATM 6214 O HOH A2084 -16.242 5.654 5.515 1.00 18.27 O
HETATM 6215 O HOH A2085 -22.188 7.601 5.764 1.00 28.60 O
HETATM 6216 O HOH A2086 -20.963 0.067 2.217 1.00 27.60 O
HETATM 6217 O HOH A2087 -21.376 -0.350 -0.999 1.00 27.49 O
HETATM 6218 O HOH A2088 -11.678 2.741 1.104 1.00 12.32 O
HETATM 6219 O HOH A2089 -10.018 0.445 0.745 1.00 9.92 O
HETATM 6220 O HOH A2090 2.139 -19.695 23.356 1.00 41.98 O
HETATM 6221 O HOH A2091 -0.880 -20.368 26.669 1.00 21.82 O
HETATM 6222 O HOH A2092 -14.410 -10.884 -3.242 1.00 12.70 O
HETATM 6223 O HOH A2093 -0.354 -11.668 -3.600 1.00 33.06 O
HETATM 6224 O HOH A2094 -3.909 -16.439 -4.735 1.00 30.18 O
HETATM 6225 O HOH A2095 -6.159 -13.717 -0.668 1.00 25.16 O
HETATM 6226 O HOH A2096 -15.738 7.125 7.859 1.00 12.28 O
HETATM 6227 O HOH A2097 -7.575 4.593 16.987 1.00 9.31 O
HETATM 6228 O HOH A2098 -17.894 7.577 15.185 1.00 22.02 O
HETATM 6229 O HOH A2099 -19.069 -9.586 38.704 1.00 30.48 O
HETATM 6230 O HOH A2100 -24.273 -8.319 45.286 1.00 21.82 O
HETATM 6231 O HOH A2101 -20.833 4.208 15.083 1.00 22.54 O
HETATM 6232 O HOH A2102 -17.541 -1.717 16.479 1.00 31.11 O
HETATM 6233 O HOH A2103 -19.302 -2.397 12.729 1.00 31.69 O
HETATM 6234 O HOH A2104 -24.680 4.865 8.515 1.00 37.72 O
HETATM 6235 O HOH A2105 -21.914 -2.883 11.618 1.00 22.91 O
HETATM 6236 O HOH A2106 -24.601 -0.455 4.999 1.00 31.40 O
HETATM 6237 O HOH A2107 -25.792 -3.439 11.581 1.00 28.99 O
HETATM 6238 O HOH A2108 -22.854 -5.349 10.636 1.00 19.88 O
HETATM 6239 O HOH A2109 -27.499 -7.682 6.486 1.00 26.11 O
HETATM 6240 O HOH A2110 -26.446 -10.433 12.296 1.00 28.42 O
HETATM 6241 O HOH A2111 -27.169 -14.219 2.855 1.00 26.11 O
HETATM 6242 O HOH A2112 -28.128 -11.168 9.304 1.00 25.42 O
HETATM 6243 O HOH A2113 -20.255 8.263 23.077 1.00 26.92 O
HETATM 6244 O HOH A2114 -23.440 -6.241 3.562 1.00 33.97 O
HETATM 6245 O HOH A2115 -22.652 -18.076 -0.180 1.00 22.21 O
HETATM 6246 O HOH A2116 -23.631 -9.509 0.817 1.00 26.81 O
HETATM 6247 O HOH A2117 -15.407 4.112 48.504 1.00 38.54 O
HETATM 6248 O HOH A2118 -21.386 11.200 41.251 1.00 40.43 O
HETATM 6249 O HOH A2119 -20.213 -6.647 0.705 1.00 23.14 O
HETATM 6250 O HOH A2120 -15.845 -15.100 -0.472 1.00 13.28 O
HETATM 6251 O HOH A2121 -7.681 13.668 41.994 1.00 32.70 O
HETATM 6252 O HOH A2122 -23.273 -19.634 8.326 1.00 28.85 O
HETATM 6253 O HOH A2123 -20.112 -22.856 0.545 1.00 35.60 O
HETATM 6254 O HOH A2124 -22.241 12.113 29.802 1.00 40.54 O
HETATM 6255 O HOH A2125 -23.324 -14.659 -5.281 1.00 27.58 O
HETATM 6256 O HOH A2126 -15.389 -19.848 -9.027 1.00 23.67 O
HETATM 6257 O HOH A2127 -17.513 -18.048 -6.752 1.00 19.04 O
HETATM 6258 O HOH A2128 -15.581 -13.245 -2.619 1.00 13.57 O
HETATM 6259 O HOH A2129 -11.636 -12.774 -9.842 1.00 22.34 O
HETATM 6260 O HOH A2130 -19.705 -16.937 -7.784 1.00 25.34 O
HETATM 6261 O HOH A2131 -21.146 -14.147 -6.951 1.00 30.35 O
HETATM 6262 O HOH A2132 -14.764 -7.698 -5.731 1.00 16.88 O
HETATM 6263 O HOH A2133 -19.710 -8.836 24.079 1.00 36.83 O
HETATM 6264 O HOH A2134 -16.631 -3.761 -0.563 1.00 14.90 O
HETATM 6265 O HOH A2135 -12.731 -15.440 -1.491 1.00 18.78 O
HETATM 6266 O HOH A2136 -8.508 -21.939 38.376 1.00 35.52 O
HETATM 6267 O HOH A2137 -4.211 -15.432 -1.233 1.00 36.66 O
HETATM 6268 O HOH A2138 -6.408 -22.541 -4.538 1.00 35.80 O
HETATM 6269 O HOH A2139 -0.298 -27.279 10.366 1.00 30.85 O
HETATM 6270 O HOH A2140 0.285 -27.388 6.578 1.00 22.41 O
HETATM 6271 O HOH A2141 -1.543 -21.318 0.188 1.00 29.26 O
HETATM 6272 O HOH A2142 -0.473 -8.189 12.866 1.00 16.60 O
HETATM 6273 O HOH A2143 -0.439 -7.643 6.161 1.00 14.47 O
HETATM 6274 O HOH A2144 -0.018 -5.307 4.560 1.00 24.45 O
HETATM 6275 O HOH A2145 1.821 -7.328 11.047 1.00 24.77 O
HETATM 6276 O HOH A2146 14.595 -13.011 55.021 1.00 36.98 O
HETATM 6277 O HOH A2147 2.708 6.570 11.279 1.00 31.37 O
HETATM 6278 O HOH A2148 -0.571 7.868 9.808 1.00 15.98 O
HETATM 6279 O HOH A2149 2.103 3.402 8.985 1.00 28.84 O
HETATM 6280 O HOH A2150 -0.917 3.193 20.524 1.00 15.46 O
HETATM 6281 O HOH A2151 -8.702 -1.040 8.817 1.00 11.69 O
HETATM 6282 O HOH A2152 -15.733 -5.021 18.342 1.00 33.31 O
HETATM 6283 O HOH A2153 -16.155 -3.075 14.901 1.00 32.26 O
HETATM 6284 O HOH A2154 17.651 -4.070 43.463 1.00 40.11 O
HETATM 6285 O HOH A2155 -14.474 -12.411 16.824 1.00 19.57 O
HETATM 6286 O HOH A2156 -1.116 -20.234 33.400 1.00 24.95 O
HETATM 6287 O HOH A2157 -0.797 -24.559 26.204 1.00 25.68 O
HETATM 6288 O HOH A2158 -19.094 -17.749 15.794 1.00 23.51 O
HETATM 6289 O HOH A2159 -3.648 -27.644 22.174 1.00 41.05 O
HETATM 6290 O HOH A2160 -24.092 -16.858 9.109 1.00 31.74 O
HETATM 6291 O HOH A2161 -20.255 -15.516 15.812 1.00 37.81 O
HETATM 6292 O HOH A2162 -17.580 -23.156 1.544 1.00 36.01 O
HETATM 6293 O HOH A2163 -18.952 -27.275 9.351 1.00 34.23 O
HETATM 6294 O HOH A2164 -21.447 -14.478 18.462 1.00 35.85 O
HETATM 6295 O HOH A2165 -15.435 -21.296 18.923 1.00 30.51 O
HETATM 6296 O HOH A2166 -17.965 -22.821 20.520 1.00 36.74 O
HETATM 6297 O HOH A2167 5.745 17.251 18.065 1.00 35.17 O
HETATM 6298 O HOH A2168 2.280 -15.703 -1.993 1.00 30.85 O
HETATM 6299 O HOH A2169 13.264 -8.691 -5.327 1.00 30.33 O
HETATM 6300 O HOH A2170 -6.175 -6.927 21.470 1.00 17.34 O
HETATM 6301 O HOH A2171 13.373 0.596 -11.351 1.00 36.19 O
HETATM 6302 O HOH A2172 9.684 2.142 -4.034 1.00 33.22 O
HETATM 6303 O HOH A2173 -3.401 10.245 17.331 1.00 19.87 O
HETATM 6304 O HOH A2174 -4.579 7.634 16.272 1.00 14.42 O
HETATM 6305 O HOH A2175 -10.332 9.512 23.872 1.00 35.10 O
HETATM 6306 O HOH A2176 -9.505 4.631 19.049 1.00 12.15 O
HETATM 6307 O HOH A2177 -7.069 8.008 23.444 1.00 13.29 O
HETATM 6308 O HOH A2178 31.238 0.910 24.622 1.00 37.76 O
HETATM 6309 O HOH A2179 -2.902 -8.509 20.027 1.00 29.15 O
HETATM 6310 O HOH A2180 -9.141 -13.679 20.071 1.00 31.48 O
HETATM 6311 O HOH A2181 -8.632 -9.267 17.609 1.00 26.91 O
HETATM 6312 O HOH A2182 28.227 11.648 23.315 1.00 33.05 O
HETATM 6313 O HOH A2183 24.754 7.849 15.015 1.00 21.65 O
HETATM 6314 O HOH A2184 -12.553 -34.805 14.216 1.00 36.25 O
HETATM 6315 O HOH A2185 15.463 11.618 10.815 1.00 25.67 O
HETATM 6316 O HOH A2186 14.797 17.685 25.468 1.00 35.85 O
HETATM 6317 O HOH A2187 -17.050 -27.003 7.016 1.00 30.60 O
HETATM 6318 O HOH A2188 13.054 8.593 7.420 1.00 33.14 O
HETATM 6319 O HOH A2189 -14.100 -30.548 19.139 1.00 37.73 O
HETATM 6320 O HOH A2190 15.362 12.317 27.729 1.00 38.63 O
HETATM 6321 O HOH A2191 -1.362 -19.893 18.136 1.00 21.48 O
HETATM 6322 O HOH A2192 -0.725 -18.578 24.686 1.00 18.01 O
HETATM 6323 O HOH A2193 3.761 -17.571 23.042 1.00 41.96 O
HETATM 6324 O HOH A2194 9.698 -3.367 25.898 1.00 15.15 O
HETATM 6325 O HOH A2195 16.456 -15.086 37.142 1.00 33.45 O
HETATM 6326 O HOH A2196 6.573 -8.817 27.737 1.00 21.78 O
HETATM 6327 O HOH A2197 4.113 2.724 26.184 1.00 17.58 O
HETATM 6328 O HOH A2198 7.070 -3.601 29.043 1.00 26.79 O
HETATM 6329 O HOH A2199 4.058 2.222 29.155 1.00 42.61 O
HETATM 6330 O HOH A2200 -5.800 -22.259 38.585 1.00 30.22 O
HETATM 6331 O HOH A2201 1.952 4.017 24.548 1.00 28.37 O
HETATM 6332 O HOH A2202 1.969 3.049 30.421 1.00 30.24 O
HETATM 6333 O HOH A2203 -0.789 5.536 37.248 1.00 16.32 O
HETATM 6334 O HOH A2204 -0.139 10.713 28.041 1.00 23.36 O
HETATM 6335 O HOH A2205 1.313 5.520 29.016 1.00 22.75 O
HETATM 6336 O HOH A2206 -7.596 1.501 29.396 1.00 9.66 O
HETATM 6337 O HOH A2207 -14.130 -6.040 25.600 1.00 33.59 O
HETATM 6338 O HOH A2208 -12.133 -3.676 24.632 1.00 28.52 O
HETATM 6339 O HOH A2209 -3.574 15.809 12.649 1.00 34.49 O
HETATM 6340 O HOH A2210 -20.897 1.148 40.010 1.00 24.36 O
HETATM 6341 O HOH A2211 -22.020 -5.887 38.575 1.00 32.79 O
HETATM 6342 O HOH A2212 -22.102 -1.336 40.753 1.00 28.53 O
HETATM 6343 O HOH A2213 -20.490 -7.545 40.015 1.00 21.04 O
HETATM 6344 O HOH A2214 -22.018 -9.542 41.474 1.00 32.31 O
HETATM 6345 O HOH A2215 -22.037 -9.378 44.135 1.00 26.44 O
HETATM 6346 O HOH A2216 1.923 10.963 7.676 1.00 31.53 O
HETATM 6347 O HOH A2217 -24.042 -5.341 48.721 1.00 21.45 O
HETATM 6348 O HOH A2218 6.591 3.059 -3.211 1.00 27.51 O
HETATM 6349 O HOH A2219 8.236 4.257 -0.914 1.00 30.95 O
HETATM 6350 O HOH A2220 -1.330 -26.397 -6.931 1.00 30.26 O
HETATM 6351 O HOH A2221 -9.510 1.475 48.476 1.00 25.68 O
HETATM 6352 O HOH A2222 -11.951 10.477 45.297 1.00 27.95 O
HETATM 6353 O HOH A2223 -12.678 8.027 47.069 1.00 26.32 O
HETATM 6354 O HOH A2224 -15.465 -20.608 -14.851 1.00 39.39 O
HETATM 6355 O HOH A2225 -5.401 5.783 35.001 1.00 27.02 O
HETATM 6356 O HOH A2226 -3.571 8.022 46.398 1.00 36.54 O
HETATM 6357 O HOH A2227 0.807 8.270 42.751 1.00 36.37 O
HETATM 6358 O HOH A2228 -5.352 10.836 39.675 1.00 28.32 O
HETATM 6359 O HOH A2229 -13.345 7.839 37.483 1.00 17.76 O
HETATM 6360 O HOH A2230 -7.116 11.838 37.951 1.00 30.06 O
HETATM 6361 O HOH A2231 -15.534 -13.128 -11.816 1.00 30.12 O
HETATM 6362 O HOH A2232 -12.283 -26.302 -4.687 1.00 26.45 O
HETATM 6363 O HOH A2233 -18.507 7.111 25.450 1.00 27.44 O
HETATM 6364 O HOH A2234 -13.197 -36.016 -4.506 1.00 28.46 O
HETATM 6365 O HOH A2235 -25.274 11.209 32.702 1.00 31.37 O
HETATM 6366 O HOH A2236 -25.887 3.203 25.950 1.00 32.96 O
HETATM 6367 O HOH A2237 -30.109 8.182 30.086 1.00 38.75 O
HETATM 6368 O HOH A2238 -23.952 -0.405 31.133 1.00 30.90 O
HETATM 6369 O HOH A2239 -24.534 7.077 40.081 1.00 30.63 O
HETATM 6370 O HOH A2240 -14.234 5.903 46.341 1.00 27.02 O
HETATM 6371 O HOH A2241 -22.893 9.485 40.007 1.00 31.64 O
HETATM 6372 O HOH A2242 -15.241 8.478 44.510 1.00 35.70 O
HETATM 6373 O HOH A2243 -14.060 11.404 43.861 1.00 30.41 O
HETATM 6374 O HOH A2244 -14.041 17.285 40.599 1.00 30.27 O
HETATM 6375 O HOH A2245 -8.803 12.526 39.800 1.00 24.58 O
HETATM 6376 O HOH A2246 -19.145 13.935 35.256 1.00 43.01 O
HETATM 6377 O HOH A2247 -19.864 12.751 31.091 1.00 23.22 O
HETATM 6378 O HOH A2248 -16.539 14.511 28.837 1.00 30.40 O
HETATM 6379 O HOH A2249 -13.246 11.756 25.000 1.00 28.68 O
HETATM 6380 O HOH A2250 -13.175 8.843 19.986 1.00 33.36 O
HETATM 6381 O HOH A2251 -17.365 -2.391 23.685 1.00 28.83 O
HETATM 6382 O HOH A2252 -19.179 4.723 26.059 1.00 23.14 O
HETATM 6383 O HOH A2253 -19.381 3.121 31.355 1.00 17.65 O
HETATM 6384 O HOH A2254 -13.676 -0.784 28.654 1.00 20.46 O
HETATM 6385 O HOH A2255 -17.266 -5.952 25.396 1.00 37.28 O
HETATM 6386 O HOH A2256 -22.947 -9.872 33.176 1.00 22.61 O
HETATM 6387 O HOH A2257 -20.375 -10.644 25.963 1.00 29.94 O
HETATM 6388 O HOH A2258 -23.326 -0.168 26.984 1.00 48.27 O
HETATM 6389 O HOH A2259 -20.011 -20.689 33.276 1.00 36.65 O
HETATM 6390 O HOH A2260 -14.550 -23.321 30.026 1.00 24.12 O
HETATM 6391 O HOH A2261 -12.816 -22.558 39.989 1.00 38.23 O
HETATM 6392 O HOH A2262 -20.611 -20.173 38.611 1.00 33.23 O
HETATM 6393 O HOH A2263 -18.115 -21.335 41.280 1.00 35.75 O
HETATM 6394 O HOH A2264 -9.460 -22.769 36.014 1.00 38.03 O
HETATM 6395 O HOH A2265 -10.215 -20.340 39.793 1.00 27.67 O
HETATM 6396 O HOH A2266 -13.088 -17.103 44.219 1.00 24.98 O
HETATM 6397 O HOH A2267 -1.858 1.305 43.330 1.00 11.81 O
HETATM 6398 O HOH A2268 -4.743 0.558 49.189 1.00 18.52 O
HETATM 6399 O HOH A2269 7.620 4.848 48.288 1.00 21.02 O
HETATM 6400 O HOH A2270 11.752 8.942 52.903 1.00 27.77 O
HETATM 6401 O HOH A2271 17.875 5.534 55.534 1.00 26.95 O
HETATM 6402 O HOH A2272 22.784 9.358 61.430 1.00 33.55 O
HETATM 6403 O HOH A2273 13.642 1.827 61.840 1.00 28.60 O
HETATM 6404 O HOH A2274 14.349 -0.866 58.526 1.00 30.09 O
HETATM 6405 O HOH A2275 22.654 -1.640 56.693 1.00 17.75 O
HETATM 6406 O HOH A2276 10.757 -2.136 58.326 1.00 32.61 O
HETATM 6407 O HOH A2277 8.234 -1.416 57.642 1.00 23.30 O
HETATM 6408 O HOH A2278 5.128 6.946 58.268 1.00 27.37 O
HETATM 6409 O HOH A2279 2.896 7.633 56.923 1.00 26.05 O
HETATM 6410 O HOH A2280 -2.716 2.190 53.098 1.00 23.29 O
HETATM 6411 O HOH A2281 -3.684 -9.071 55.722 1.00 24.09 O
HETATM 6412 O HOH A2282 -5.549 -14.454 52.632 1.00 28.82 O
HETATM 6413 O HOH A2283 -2.839 -11.556 55.273 1.00 28.39 O
HETATM 6414 O HOH A2284 8.926 -12.503 57.808 1.00 37.20 O
HETATM 6415 O HOH A2285 7.830 -16.671 57.247 1.00 32.98 O
HETATM 6416 O HOH A2286 3.489 -15.315 53.241 1.00 23.70 O
HETATM 6417 O HOH A2287 13.480 -8.699 48.233 1.00 27.62 O
HETATM 6418 O HOH A2288 11.989 -4.199 57.139 1.00 32.55 O
HETATM 6419 O HOH A2289 14.969 -1.990 55.176 1.00 18.36 O
HETATM 6420 O HOH A2290 14.932 -10.916 53.005 1.00 32.57 O
HETATM 6421 O HOH A2291 24.201 -14.942 55.239 1.00 37.48 O
HETATM 6422 O HOH A2292 19.931 -9.483 58.909 1.00 27.73 O
HETATM 6423 O HOH A2293 12.147 -10.339 60.198 1.00 34.43 O
HETATM 6424 O HOH A2294 13.445 -12.953 57.411 1.00 33.49 O
HETATM 6425 O HOH A2295 16.566 5.443 47.654 1.00 24.83 O
HETATM 6426 O HOH A2296 14.600 -4.343 44.521 1.00 27.68 O
HETATM 6427 O HOH A2297 20.882 -1.879 49.536 1.00 27.92 O
HETATM 6428 O HOH A2298 11.198 -2.863 39.319 1.00 30.24 O
HETATM 6429 O HOH A2299 16.578 -2.136 42.466 1.00 30.72 O
HETATM 6430 O HOH A2300 2.162 -12.003 29.857 1.00 16.73 O
HETATM 6431 O HOH A2301 0.291 -18.045 34.788 1.00 27.30 O
HETATM 6432 O HOH A2302 3.094 -18.183 32.926 1.00 30.39 O
HETATM 6433 O HOH A2303 4.471 -13.860 32.812 1.00 26.11 O
HETATM 6434 O HOH A2304 -0.360 -18.992 28.978 1.00 17.99 O
HETATM 6435 O HOH A2305 -2.557 -22.492 26.590 1.00 18.17 O
HETATM 6436 O HOH A2306 -6.943 -24.909 23.114 1.00 17.86 O
HETATM 6437 O HOH A2307 -5.450 -26.357 26.506 1.00 40.56 O
HETATM 6438 O HOH A2308 -13.736 -26.040 28.780 1.00 28.52 O
HETATM 6439 O HOH A2309 -7.428 -23.335 34.384 1.00 36.75 O
HETATM 6440 O HOH A2310 -13.202 -27.311 21.259 1.00 28.19 O
HETATM 6441 O HOH A2311 -6.198 -27.888 22.741 1.00 19.29 O
HETATM 6442 O HOH A2312 -10.367 -33.513 17.955 1.00 36.66 O
HETATM 6443 O HOH A2313 -3.068 -30.654 16.090 1.00 28.88 O
HETATM 6444 O HOH A2314 -3.568 -5.132 17.401 1.00 10.12 O
HETATM 6445 O HOH A2315 0.912 -0.389 19.082 1.00 11.50 O
HETATM 6446 O HOH A2316 7.178 13.077 17.991 1.00 28.81 O
HETATM 6447 O HOH A2317 4.799 19.257 20.244 1.00 40.32 O
HETATM 6448 O HOH A2318 2.318 12.191 22.113 1.00 21.22 O
HETATM 6449 O HOH A2319 6.187 16.809 26.109 1.00 23.82 O
HETATM 6450 O HOH A2320 4.705 11.313 24.803 1.00 19.41 O
HETATM 6451 O HOH A2321 6.666 3.889 26.952 1.00 38.00 O
HETATM 6452 O HOH A2322 13.054 -0.731 16.946 1.00 24.68 O
HETATM 6453 O HOH A2323 3.062 -1.038 10.842 1.00 34.93 O
HETATM 6454 O HOH A2324 4.330 -4.306 9.768 1.00 16.88 O
HETATM 6455 O HOH A2325 1.807 -4.146 11.408 1.00 17.91 O
HETATM 6456 O HOH A2326 13.378 -11.680 10.351 1.00 26.52 O
HETATM 6457 O HOH A2327 11.070 -11.113 9.026 1.00 20.77 O
HETATM 6458 O HOH A2328 13.509 -10.306 2.033 1.00 36.96 O
HETATM 6459 O HOH A2329 8.050 -2.615 0.896 1.00 21.82 O
HETATM 6460 O HOH A2330 10.960 -13.012 6.964 1.00 32.92 O
HETATM 6461 O HOH A2331 8.722 -16.689 2.802 1.00 27.85 O
HETATM 6462 O HOH A2332 4.659 -15.061 -3.402 1.00 32.76 O
HETATM 6463 O HOH A2333 1.928 -17.750 0.575 1.00 26.82 O
HETATM 6464 O HOH A2334 13.278 -10.915 -6.776 1.00 30.67 O
HETATM 6465 O HOH A2335 9.606 -18.142 -5.261 1.00 28.88 O
HETATM 6466 O HOH A2336 10.809 -11.660 -12.321 1.00 21.22 O
HETATM 6467 O HOH A2337 13.756 -11.938 -9.166 1.00 29.94 O
HETATM 6468 O HOH A2338 9.348 -9.522 -11.777 1.00 18.17 O
HETATM 6469 O HOH A2339 14.597 -16.928 -9.797 1.00 26.90 O
HETATM 6470 O HOH A2340 12.082 -18.355 -4.363 1.00 30.02 O
HETATM 6471 O HOH A2341 13.550 -16.079 -16.739 1.00 32.14 O
HETATM 6472 O HOH A2342 8.613 -19.969 -19.973 1.00 32.02 O
HETATM 6473 O HOH A2343 11.737 -13.934 -16.672 1.00 28.99 O
HETATM 6474 O HOH A2344 10.008 -12.869 -14.805 1.00 18.33 O
HETATM 6475 O HOH A2345 6.118 -5.786 -13.404 1.00 32.71 O
HETATM 6476 O HOH A2346 9.206 -2.343 -13.498 1.00 33.06 O
HETATM 6477 O HOH A2347 13.510 -6.342 -6.914 1.00 25.16 O
HETATM 6478 O HOH A2348 11.200 -0.472 -10.126 1.00 21.04 O
HETATM 6479 O HOH A2349 14.696 -4.386 -5.068 1.00 20.29 O
HETATM 6480 O HOH A2350 11.011 -1.964 3.386 1.00 24.92 O
HETATM 6481 O HOH A2351 10.414 0.727 -1.748 1.00 25.80 O
HETATM 6482 O HOH A2352 16.987 -1.841 -0.577 1.00 30.19 O
HETATM 6483 O HOH A2353 12.908 -8.203 0.778 1.00 36.73 O
HETATM 6484 O HOH A2354 18.183 -3.831 3.587 1.00 24.28 O
HETATM 6485 O HOH A2355 22.242 0.068 5.100 1.00 24.98 O
HETATM 6486 O HOH A2356 22.890 -3.507 9.007 1.00 30.37 O
HETATM 6487 O HOH A2357 21.411 -9.702 7.151 1.00 32.43 O
HETATM 6488 O HOH A2358 19.769 -10.059 11.756 1.00 28.99 O
HETATM 6489 O HOH A2359 24.078 -4.205 14.165 1.00 21.59 O
HETATM 6490 O HOH A2360 17.072 -13.125 13.515 1.00 22.19 O
HETATM 6491 O HOH A2361 16.338 -11.120 10.383 1.00 24.71 O
HETATM 6492 O HOH A2362 21.270 -7.479 18.909 1.00 13.49 O
HETATM 6493 O HOH A2363 24.221 -14.940 11.073 1.00 32.14 O
HETATM 6494 O HOH A2364 26.790 -9.629 13.893 1.00 26.00 O
HETATM 6495 O HOH A2365 24.497 -11.016 13.327 1.00 23.54 O
HETATM 6496 O HOH A2366 17.975 -6.152 24.499 1.00 15.41 O
HETATM 6497 O HOH A2367 25.131 -8.990 24.693 1.00 32.44 O
HETATM 6498 O HOH A2368 22.975 -10.825 24.584 1.00 30.24 O
HETATM 6499 O HOH A2369 20.785 -12.201 26.800 1.00 32.00 O
HETATM 6500 O HOH A2370 27.983 -6.922 22.875 1.00 33.69 O
HETATM 6501 O HOH A2371 29.366 -1.441 25.515 1.00 29.63 O
HETATM 6502 O HOH A2372 26.798 -1.346 26.224 1.00 19.57 O
HETATM 6503 O HOH A2373 28.636 1.606 31.963 1.00 21.86 O
HETATM 6504 O HOH A2374 21.145 -5.050 34.866 1.00 26.50 O
HETATM 6505 O HOH A2375 26.487 -9.371 26.933 1.00 28.50 O
HETATM 6506 O HOH A2376 23.962 -12.310 32.713 1.00 36.98 O
HETATM 6507 O HOH A2377 25.569 -5.677 36.006 1.00 22.89 O
HETATM 6508 O HOH A2378 30.556 -0.194 34.336 1.00 32.08 O
HETATM 6509 O HOH A2379 19.773 9.320 29.596 1.00 35.23 O
HETATM 6510 O HOH A2380 30.013 3.792 25.474 1.00 23.07 O
HETATM 6511 O HOH A2381 28.187 9.290 27.077 1.00 34.23 O
HETATM 6512 O HOH A2382 27.182 9.503 21.209 1.00 34.11 O
HETATM 6513 O HOH A2383 24.908 6.394 12.704 1.00 31.01 O
HETATM 6514 O HOH A2384 24.424 6.838 6.812 1.00 26.01 O
HETATM 6515 O HOH A2385 31.977 3.597 7.176 1.00 29.95 O
HETATM 6516 O HOH A2386 33.426 7.591 8.047 1.00 27.40 O
HETATM 6517 O HOH A2387 12.654 0.595 4.506 1.00 22.66 O
HETATM 6518 O HOH A2388 22.411 11.077 10.155 1.00 36.99 O
HETATM 6519 O HOH A2389 24.295 10.367 13.541 1.00 29.18 O
HETATM 6520 O HOH A2390 12.642 12.126 14.563 1.00 32.11 O
HETATM 6521 O HOH A2391 13.461 12.787 12.206 1.00 29.59 O
HETATM 6522 O HOH A2392 8.323 20.430 14.900 1.00 31.70 O
HETATM 6523 O HOH A2393 8.181 19.049 17.474 1.00 25.41 O
HETATM 6524 O HOH A2394 14.444 18.382 22.892 1.00 25.65 O
HETATM 6525 O HOH A2395 11.527 15.674 23.749 1.00 25.56 O
HETATM 6526 O HOH A2396 20.974 18.094 21.269 1.00 28.83 O
HETATM 6527 O HOH A2397 21.549 14.622 19.760 1.00 19.21 O
HETATM 6528 O HOH A2398 25.269 15.585 22.624 1.00 26.59 O
HETATM 6529 O HOH A2399 20.729 7.817 27.767 1.00 20.62 O
HETATM 6530 O HOH A2400 26.139 13.352 24.378 1.00 30.30 O
HETATM 6531 O HOH A2401 15.242 10.409 8.438 1.00 31.52 O
HETATM 6532 O HOH A2402 22.959 8.012 9.087 1.00 26.95 O
HETATM 6533 O HOH A2403 3.845 5.305 9.160 1.00 28.80 O
HETATM 6534 O HOH A2404 10.811 9.791 8.311 1.00 28.73 O
HETATM 6535 O HOH A2405 8.549 10.082 11.173 1.00 35.09 O
HETATM 6536 O HOH A2406 11.464 10.426 22.187 1.00 16.27 O
HETATM 6537 O HOH A2407 13.172 15.427 25.830 1.00 30.03 O
HETATM 6538 O HOH A2408 11.272 13.101 22.748 1.00 21.33 O
HETATM 6539 O HOH A2409 10.981 8.463 27.548 1.00 32.63 O
HETATM 6540 O HOH A2410 13.007 6.297 27.492 1.00 20.25 O
HETATM 6541 O HOH A2411 16.843 9.972 27.379 1.00 19.89 O
HETATM 6542 O HOH A2412 17.792 2.329 33.149 1.00 17.79 O
HETATM 6543 O HOH A2413 16.658 4.176 34.753 1.00 34.05 O
HETATM 6544 O HOH A2414 7.503 3.813 31.654 1.00 28.98 O
HETATM 6545 O HOH A2415 10.488 -3.467 28.676 1.00 25.78 O
HETATM 6546 O HOH A2416 13.699 -14.280 36.960 1.00 36.29 O
HETATM 6547 O HOH A2417 13.213 -8.089 41.135 1.00 25.90 O
HETATM 6548 O HOH A2418 13.406 -6.042 42.612 1.00 36.34 O
HETATM 6549 O HOH A2419 18.354 -13.181 43.271 1.00 31.15 O
HETATM 6550 O HOH A2420 16.434 -12.510 46.099 1.00 29.08 O
HETATM 6551 O HOH A2421 4.544 -16.569 50.944 1.00 27.58 O
HETATM 6552 O HOH A2422 1.881 -22.822 50.558 1.00 33.94 O
HETATM 6553 O HOH A2423 2.375 -17.997 53.706 1.00 42.83 O
HETATM 6554 O HOH A2424 -3.502 -20.029 56.390 1.00 32.89 O
HETATM 6555 O HOH A2425 -2.857 -22.960 52.235 1.00 37.48 O
HETATM 6556 O HOH A2426 -6.103 -22.322 48.644 1.00 26.03 O
HETATM 6557 O HOH A2427 -7.557 -20.608 45.477 1.00 23.33 O
HETATM 6558 O HOH A2428 -4.197 -19.969 38.666 1.00 28.73 O
HETATM 6559 O HOH A2429 -8.012 -22.866 42.447 1.00 42.51 O
HETATM 6560 O HOH A2430 -4.145 -24.371 49.073 1.00 29.81 O
HETATM 6561 O HOH A2431 -2.163 -26.894 45.498 1.00 38.03 O
HETATM 6562 O HOH A2432 21.894 -9.052 40.597 1.00 32.78 O
HETATM 6563 O HOH A2433 18.943 -12.984 28.940 1.00 20.76 O
HETATM 6564 O HOH A2434 20.517 -13.473 14.860 1.00 34.48 O
HETATM 6565 O HOH A2435 13.563 -18.141 18.144 1.00 22.02 O
HETATM 6566 O HOH A2436 11.898 -16.073 24.697 1.00 33.77 O
HETATM 6567 O HOH A2437 15.960 -16.573 17.288 1.00 26.76 O
HETATM 6568 O HOH A2438 7.782 -21.936 15.553 1.00 29.52 O
HETATM 6569 O HOH A2439 13.495 -19.497 15.424 1.00 32.48 O
HETATM 6570 O HOH A2440 10.514 -23.050 15.097 1.00 33.70 O
HETATM 6571 O HOH A2441 4.279 -21.953 1.824 1.00 46.88 O
HETATM 6572 O HOH A2442 -0.975 -13.132 -0.823 1.00 32.54 O
HETATM 6573 O HOH A2443 1.816 -15.320 0.536 1.00 32.93 O
HETATM 6574 O HOH A2444 -3.938 -17.520 3.947 1.00 16.25 O
HETATM 6575 O HOH A2445 -7.017 -14.988 1.489 1.00 19.55 O
HETATM 6576 O HOH A2446 -3.005 -11.803 0.404 1.00 17.14 O
HETATM 6577 O HOH A2447 2.415 0.858 9.142 1.00 28.17 O
HETATM 6578 O HOH A2448 2.361 -4.488 5.123 1.00 26.95 O
HETATM 6579 O HOH A2449 -3.297 8.564 9.707 1.00 12.85 O
HETATM 6580 O HOH A2450 -6.909 8.322 14.643 1.00 12.67 O
HETATM 6581 O HOH A2451 -5.158 13.898 11.260 1.00 19.11 O
HETATM 6582 O HOH A2452 -6.996 11.533 18.735 1.00 38.53 O
HETATM 6583 O HOH A2453 -12.834 11.703 17.664 1.00 28.53 O
HETATM 6584 O HOH A2454 -13.937 7.085 17.083 1.00 22.42 O
HETATM 6585 O HOH A2455 -16.179 11.331 13.986 1.00 23.07 O
HETATM 6586 O HOH A2456 -18.787 11.722 9.750 1.00 31.17 O
HETATM 6587 O HOH A2457 -18.638 9.707 13.665 1.00 29.19 O
HETATM 6588 O HOH A2458 -21.363 8.753 10.313 1.00 43.96 O
HETATM 6589 O HOH A2459 -14.152 15.151 4.563 1.00 30.68 O
HETATM 6590 O HOH A2460 -12.094 9.196 8.557 1.00 11.37 O
HETATM 6591 O HOH A2461 -12.905 12.772 3.915 1.00 19.87 O
HETATM 6592 O HOH A2462 -7.628 15.125 10.540 1.00 24.72 O
HETATM 6593 O HOH A2463 2.385 11.624 1.708 1.00 22.85 O
HETATM 6594 O HOH A2464 0.898 8.453 7.572 1.00 16.61 O
HETATM 6595 O HOH A2465 1.549 12.782 5.707 1.00 32.80 O
HETATM 6596 O HOH A2466 3.023 6.501 7.012 1.00 24.19 O
HETATM 6597 O HOH A2467 -1.243 1.443 8.635 1.00 10.66 O
HETATM 6598 O HOH A2468 4.528 10.198 1.170 1.00 27.97 O
HETATM 6599 O HOH A2469 5.278 0.757 -1.992 1.00 13.31 O
HETATM 6600 O HOH A2470 8.496 -0.912 2.926 1.00 21.50 O
HETATM 6601 O HOH A2471 7.973 4.367 1.806 1.00 25.83 O
HETATM 6602 O HOH A2472 2.346 1.774 -8.436 1.00 18.96 O
HETATM 6603 O HOH A2473 8.820 -0.030 -5.766 1.00 20.38 O
HETATM 6604 O HOH A2474 8.120 -0.882 -1.210 1.00 21.77 O
HETATM 6605 O HOH A2475 6.416 -3.137 -13.449 1.00 25.30 O
HETATM 6606 O HOH A2476 7.172 0.582 -7.777 1.00 22.98 O
HETATM 6607 O HOH A2477 9.010 -0.161 -11.704 1.00 24.87 O
HETATM 6608 O HOH A2478 3.593 -9.930 -17.905 1.00 39.62 O
HETATM 6609 O HOH A2479 -0.766 -15.064 -5.032 1.00 24.43 O
HETATM 6610 O HOH A2480 -5.332 -18.022 -6.562 1.00 23.59 O
HETATM 6611 O HOH A2481 -1.821 -23.660 -6.816 1.00 23.26 O
HETATM 6612 O HOH A2482 -2.623 -19.870 -7.078 1.00 24.26 O
HETATM 6613 O HOH A2483 3.620 -19.642 -5.081 1.00 42.77 O
HETATM 6614 O HOH A2484 0.461 -27.066 -8.839 1.00 38.19 O
HETATM 6615 O HOH A2485 -2.871 -34.057 -10.622 1.00 30.64 O
HETATM 6616 O HOH A2486 -7.058 -38.409 -14.192 1.00 27.02 O
HETATM 6617 O HOH A2487 -11.102 -38.182 -10.420 1.00 37.47 O
HETATM 6618 O HOH A2488 -16.500 -19.399 -17.036 1.00 34.94 O
HETATM 6619 O HOH A2489 -8.182 -17.753 -24.797 1.00 27.90 O
HETATM 6620 O HOH A2490 -1.605 -16.721 -23.488 1.00 27.81 O
HETATM 6621 O HOH A2491 -8.140 -14.095 -26.869 1.00 32.42 O
HETATM 6622 O HOH A2492 -9.558 -10.453 -20.827 1.00 28.06 O
HETATM 6623 O HOH A2493 -6.274 -10.147 -18.142 1.00 33.58 O
HETATM 6624 O HOH A2494 -4.035 -19.800 -26.044 1.00 31.73 O
HETATM 6625 O HOH A2495 1.646 -18.741 -22.738 1.00 21.42 O
HETATM 6626 O HOH A2496 5.406 -23.650 -21.573 1.00 29.12 O
HETATM 6627 O HOH A2497 8.094 -26.236 -20.470 1.00 38.19 O
HETATM 6628 O HOH A2498 4.086 -28.858 -14.929 1.00 24.66 O
HETATM 6629 O HOH A2499 -6.134 -14.836 -10.719 1.00 26.67 O
HETATM 6630 O HOH A2500 -12.897 -14.008 -12.304 1.00 27.11 O
HETATM 6631 O HOH A2501 -11.911 -9.970 -14.695 1.00 40.37 O
HETATM 6632 O HOH A2502 -10.839 -17.131 -4.932 1.00 16.40 O
HETATM 6633 O HOH A2503 -11.197 -24.285 -6.288 1.00 22.67 O
HETATM 6634 O HOH A2504 -8.154 -18.456 -5.983 1.00 29.62 O
HETATM 6635 O HOH A2505 -8.745 -22.720 -5.915 1.00 31.64 O
HETATM 6636 O HOH A2506 -17.465 -19.487 -10.686 1.00 26.09 O
HETATM 6637 O HOH A2507 -6.781 -29.177 -6.995 1.00 28.96 O
HETATM 6638 O HOH A2508 -11.680 -28.943 -4.927 1.00 30.69 O
HETATM 6639 O HOH A2509 -12.017 -33.673 -4.044 1.00 30.50 O
HETATM 6640 O HOH A2510 -18.169 -35.705 -7.260 1.00 25.00 O
HETATM 6641 O HOH A2511 -21.107 -33.498 -13.429 1.00 18.78 O
HETATM 6642 O HOH A2512 -18.900 -38.563 -11.294 1.00 29.38 O
HETATM 6643 O HOH A2513 -12.989 -29.265 -12.264 1.00 19.12 O
HETATM 6644 O HOH A2514 -20.272 -30.541 -11.257 1.00 28.72 O
HETATM 6645 O HOH A2515 -21.900 -27.572 -17.582 1.00 31.75 O
HETATM 6646 O HOH A2516 -21.057 -30.022 -18.787 1.00 23.66 O
HETATM 6647 O HOH A2517 -18.180 -22.593 -19.419 1.00 37.36 O
HETATM 6648 O HOH A2518 -19.003 -25.619 -24.066 1.00 31.33 O
HETATM 6649 O HOH A2519 -17.486 -22.856 -14.422 1.00 33.43 O
HETATM 6650 O HOH A2520 -16.009 -32.747 -29.181 1.00 32.84 O
HETATM 6651 O HOH A2521 -14.814 -37.058 -22.801 1.00 27.41 O
HETATM 6652 O HOH A2522 -19.185 -34.831 -24.186 1.00 27.11 O
HETATM 6653 O HOH A2523 -17.213 -23.701 -30.071 1.00 27.35 O
HETATM 6654 O HOH A2524 -18.060 -0.661 10.576 1.00 19.30 O
HETATM 6655 O HOH A2525 -10.727 -2.004 18.871 1.00 10.44 O
HETATM 6656 O HOH A2526 -11.449 2.634 20.135 1.00 21.36 O
HETATM 6657 O HOH A2527 -6.830 -3.092 19.292 1.00 10.05 O
HETATM 6658 O HOH A2528 -11.300 -1.535 9.750 1.00 11.19 O
HETATM 6659 O HOH A2529 -15.954 2.556 15.323 1.00 19.93 O
HETATM 6660 O HOH A2530 3.495 -11.683 27.593 1.00 18.73 O
HETATM 6661 O HOH A2531 0.477 4.919 14.847 1.00 19.86 O
HETATM 6662 O HOH A2532 -8.070 17.184 -6.637 1.00 23.11 O
HETATM 6663 O HOH A2533 -6.966 11.286 -4.073 1.00 15.71 O
HETATM 6664 O HOH A2534 7.004 -3.753 26.349 1.00 17.17 O
HETATM 6665 O HOH A2535 -23.759 -5.742 46.058 1.00 15.79 O
HETATM 6666 O HOH A2536 -28.224 -2.630 41.375 1.00 20.14 O
CONECT 1189 6130
CONECT 1509 6130
CONECT 6060 6061 6062 6063 6067
CONECT 6061 6060 6130
CONECT 6062 6060 6087
CONECT 6063 6060
CONECT 6064 6065 6066 6067 6068
CONECT 6065 6064
CONECT 6066 6064
CONECT 6067 6060 6064
CONECT 6068 6064 6069
CONECT 6069 6068 6070
CONECT 6070 6069 6071 6072
CONECT 6071 6070 6076
CONECT 6072 6070 6073 6074
CONECT 6073 6072
CONECT 6074 6072 6075 6076
CONECT 6075 6074
CONECT 6076 6071 6074 6077
CONECT 6077 6076 6078 6086
CONECT 6078 6077 6079
CONECT 6079 6078 6080
CONECT 6080 6079 6081 6086
CONECT 6081 6080 6082 6083
CONECT 6082 6081
CONECT 6083 6081 6084
CONECT 6084 6083 6085
CONECT 6085 6084 6086
CONECT 6086 6077 6080 6085
CONECT 6087 6062 6088 6089 6090
CONECT 6087 6091
CONECT 6088 6087
CONECT 6089 6087 6130
CONECT 6090 6087
CONECT 6091 6087
CONECT 6092 6093 6094
CONECT 6093 6092
CONECT 6094 6092 6095
CONECT 6095 6094
CONECT 6096 6097 6098
CONECT 6097 6096
CONECT 6098 6096 6099
CONECT 6099 6098
CONECT 6100 6101 6102
CONECT 6101 6100
CONECT 6102 6100 6103
CONECT 6103 6102
CONECT 6104 6105 6106
CONECT 6105 6104
CONECT 6106 6104 6107
CONECT 6107 6106
CONECT 6108 6109 6110
CONECT 6109 6108
CONECT 6110 6108 6111
CONECT 6111 6110
CONECT 6112 6113 6114
CONECT 6113 6112
CONECT 6114 6112 6115
CONECT 6115 6114
CONECT 6116 6117 6118
CONECT 6117 6116
CONECT 6118 6116 6119
CONECT 6119 6118
CONECT 6120 6121 6122 6123 6124
CONECT 6121 6120
CONECT 6122 6120
CONECT 6123 6120
CONECT 6124 6120
CONECT 6125 6126 6127 6128 6129
CONECT 6126 6125
CONECT 6127 6125
CONECT 6128 6125
CONECT 6129 6125
CONECT 6130 1189 1509 6061 6089
CONECT 6130 6444 6657
CONECT 6444 6130
CONECT 6657 6130
MASTER 396 0 12 41 24 0 29 6 6665 1 77 61
END
A second structure was input as follows:
HEADER MOTOR PROTEIN 22-MAY-17 5O2L
TITLE MYOSIN VI MOTOR DOMAIN IN THE PRE-TRANSITION STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCONVENTIONAL MYOSIN-VI;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: MYO6;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS MYOSIN, MOTOR DOMAIN, PRE-TRANSITION STATE, MOTOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.ISABET,H.BENISTY,A.HOUDUSSE
REVDAT 3 20-JUN-18 5O2L 1 JRNL
REVDAT 2 13-JUN-18 5O2L 1 JRNL
REVDAT 1 23-MAY-18 5O2L 0
JRNL AUTH F.BLANC,T.ISABET,H.BENISTY,H.L.SWEENEY,M.CECCHINI,A.HOUDUSSE
JRNL TITL AN INTERMEDIATE ALONG THE RECOVERY STROKE OF MYOSIN VI
JRNL TITL 2 REVEALED BY X-RAY CRYSTALLOGRAPHY AND MOLECULAR DYNAMICS.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 6213 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 29844196
JRNL DOI 10.1073/PNAS.1711512115
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 55469
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2769
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.26
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.78
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4037
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2635
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3835
REMARK 3 BIN R VALUE (WORKING SET) : 0.2605
REMARK 3 BIN FREE R VALUE : 0.3194
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 202
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6045
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 239
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.08720
REMARK 3 B22 (A**2) : -5.60200
REMARK 3 B33 (A**2) : 7.68920
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.367
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.186
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.168
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.185
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.169
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6265 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8457 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2926 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 165 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 919 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6265 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 801 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 7456 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.19
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.01
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|5 - A|704 A|995 - A|1006 S|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5110 31.9703 24.9344
REMARK 3 T TENSOR
REMARK 3 T11: -0.0660 T22: -0.0329
REMARK 3 T33: -0.2999 T12: -0.0615
REMARK 3 T13: 0.0453 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 1.4788 L22: 0.6633
REMARK 3 L33: 1.7810 L12: -0.3459
REMARK 3 L13: 0.4638 L23: 0.0649
REMARK 3 S TENSOR
REMARK 3 S11: -0.0407 S12: -0.1833 S13: 0.1246
REMARK 3 S21: -0.1564 S22: 0.0390 S23: -0.0518
REMARK 3 S31: -0.3194 S32: -0.0250 S33: 0.0017
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|705 - A|789 T|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4716 64.0577 34.9460
REMARK 3 T TENSOR
REMARK 3 T11: -0.2960 T22: 0.1920
REMARK 3 T33: -0.1732 T12: -0.1009
REMARK 3 T13: -0.0408 T23: -0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 8.3155 L22: 8.3154
REMARK 3 L33: 3.4091 L12: 2.9104
REMARK 3 L13: -0.3144 L23: 2.9104
REMARK 3 S TENSOR
REMARK 3 S11: -0.0202 S12: -0.0147 S13: -0.5442
REMARK 3 S21: -0.5308 S22: -0.2461 S23: 0.5072
REMARK 3 S31: -0.3337 S32: -0.4617 S33: 0.2663
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5O2L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1200003012.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55469
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
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 : 1.290
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2V26
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% POLYETHYLENE GLYCOL [PEG] 8000, 50
REMARK 280 MM TRIS, PH 7.5, 1 MM TCEP, 15% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
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 36.17000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.83000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.91500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.83000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.17000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.91500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 356
REMARK 465 SER A 357
REMARK 465 THR A 358
REMARK 465 SER A 359
REMARK 465 GLY A 360
REMARK 465 THR A 397
REMARK 465 THR A 398
REMARK 465 ALA A 399
REMARK 465 GLY A 400
REMARK 465 GLY A 401
REMARK 465 ALA A 402
REMARK 465 LYS A 403
REMARK 465 GLY A 404
REMARK 465 THR A 405
REMARK 465 SER A 624
REMARK 465 THR A 625
REMARK 465 ASN A 626
REMARK 465 ASN A 627
REMARK 465 ASN A 628
REMARK 465 LYS A 629
REMARK 465 ASP A 630
REMARK 465 THR A 631
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 5 CG CD CE NZ
REMARK 470 LYS A 37 CG CD CE NZ
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 GLU A 110 CD OE1 OE2
REMARK 470 GLN A 176 CG CD OE1 NE2
REMARK 470 ILE A 178 CG1 CG2 CD1
REMARK 470 GLU A 184 CG CD OE1 OE2
REMARK 470 GLU A 216 CG CD OE1 OE2
REMARK 470 LYS A 217 CD CE NZ
REMARK 470 LYS A 240 CD CE NZ
REMARK 470 GLU A 261 CG CD OE1 OE2
REMARK 470 LYS A 285 CD CE NZ
REMARK 470 LYS A 289 CD CE NZ
REMARK 470 LYS A 325 CD CE NZ
REMARK 470 GLU A 354 CG CD OE1 OE2
REMARK 470 VAL A 406 CG1 CG2
REMARK 470 LYS A 408 CD CE NZ
REMARK 470 GLU A 446 CG CD OE1 OE2
REMARK 470 LYS A 564 CE NZ
REMARK 470 LYS A 615 CE NZ
REMARK 470 GLU A 622 CD OE1 OE2
REMARK 470 LYS A 632 CG CD CE NZ
REMARK 470 GLN A 633 CG CD OE1 NE2
REMARK 470 LYS A 634 CG CD CE NZ
REMARK 470 LYS A 637 CG CD CE NZ
REMARK 470 ARG A 728 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 746 CD OE1 OE2
REMARK 470 LYS A 755 CG CD CE NZ
REMARK 470 LYS A 762 CD CE NZ
REMARK 470 GLN A 768 CG CD OE1 NE2
REMARK 470 LYS A 771 CG CD CE NZ
REMARK 470 LYS A 782 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 MG MG A 802 F2 BEF A 803 1.66
REMARK 500 NH1 ARG A 393 SD MET A 395 2.11
REMARK 500 NH1 ARG A 393 CE MET A 395 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 THR A 392 C ARG A 393 N -0.296
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR A 392 CA - C - N ANGL. DEV. = -15.0 DEGREES
REMARK 500 THR A 392 O - C - N ANGL. DEV. = 11.2 DEGREES
REMARK 500 ARG A 393 C - N - CA ANGL. DEV. = -16.2 DEGREES
REMARK 500 ARG A 393 CA - C - N ANGL. DEV. = 20.9 DEGREES
REMARK 500 ARG A 393 O - C - N ANGL. DEV. = -21.0 DEGREES
REMARK 500 VAL A 394 C - N - CA ANGL. DEV. = 18.3 DEGREES
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 ALA A 91 -114.96 60.16
REMARK 500 LYS A 105 -2.31 58.46
REMARK 500 ASP A 177 -5.67 -55.22
REMARK 500 PHE A 443 59.72 -140.50
REMARK 500 SER A 467 -166.94 -117.91
REMARK 500 LEU A 522 -54.14 70.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 158 OG1
REMARK 620 2 SER A 204 OG 89.0
REMARK 620 3 ADP A 801 O1B 82.9 171.9
REMARK 620 4 HOH A 937 O 89.3 85.3 94.5
REMARK 620 5 HOH A 902 O 85.7 93.9 85.6 175.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BEF A 803 BE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 801 O3B
REMARK 620 2 BEF A 803 F1 87.3
REMARK 620 3 BEF A 803 F2 85.7 109.4
REMARK 620 4 BEF A 803 F3 150.2 110.0 109.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEF A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 811
DBREF 5O2L A 5 789 UNP F1RQI7 F1RQI7_PIG 5 789
SEQRES 1 A 785 LYS PRO VAL TRP ALA PRO HIS PRO THR ASP GLY PHE GLN
SEQRES 2 A 785 VAL GLY ASN ILE VAL ASP ILE GLY PRO ASP SER LEU THR
SEQRES 3 A 785 ILE GLU PRO LEU ASN GLN LYS GLY LYS THR PHE LEU ALA
SEQRES 4 A 785 LEU ILE ASN GLN VAL PHE PRO ALA GLU GLU ASP SER LYS
SEQRES 5 A 785 LYS ASP VAL GLU ASP ASN CYS SER LEU MET TYR LEU ASN
SEQRES 6 A 785 GLU ALA THR LEU LEU HIS ASN ILE LYS VAL ARG TYR SER
SEQRES 7 A 785 LYS ASP ARG ILE TYR THR TYR VAL ALA ASN ILE LEU ILE
SEQRES 8 A 785 ALA VAL ASN PRO TYR PHE ASP ILE PRO LYS ILE TYR SER
SEQRES 9 A 785 SER GLU THR ILE LYS SER TYR GLN GLY LYS SER LEU GLY
SEQRES 10 A 785 THR MET PRO PRO HIS VAL PHE ALA ILE ALA ASP LYS ALA
SEQRES 11 A 785 PHE ARG ASP MET LYS VAL LEU LYS LEU SER GLN SER ILE
SEQRES 12 A 785 ILE VAL SER GLY GLU SER GLY ALA GLY LYS THR GLU ASN
SEQRES 13 A 785 THR LYS PHE VAL LEU ARG TYR LEU THR GLU SER TYR GLY
SEQRES 14 A 785 THR GLY GLN ASP ILE ASP ASP ARG ILE VAL GLU ALA ASN
SEQRES 15 A 785 PRO LEU LEU GLU ALA PHE GLY ASN ALA LYS THR VAL ARG
SEQRES 16 A 785 ASN ASN ASN SER SER ARG PHE GLY LYS PHE VAL GLU ILE
SEQRES 17 A 785 HIS PHE ASN GLU LYS SER SER VAL VAL GLY GLY PHE VAL
SEQRES 18 A 785 SER HIS TYR LEU LEU GLU LYS SER ARG ILE CYS VAL GLN
SEQRES 19 A 785 GLY LYS GLU GLU ARG ASN TYR HIS ILE PHE TYR ARG LEU
SEQRES 20 A 785 CYS ALA GLY ALA SER GLU ASP ILE ARG GLU ARG LEU HIS
SEQRES 21 A 785 LEU SER SER PRO ASP ASN PHE ARG TYR LEU ASN ARG GLY
SEQRES 22 A 785 CYS THR ARG TYR PHE ALA ASN LYS GLU THR ASP LYS GLN
SEQRES 23 A 785 ILE LEU GLN ASN ARG LYS SER PRO GLU TYR LEU LYS ALA
SEQRES 24 A 785 GLY SER LEU LYS ASP PRO LEU LEU ASP ASP HIS GLY ASP
SEQRES 25 A 785 PHE ILE ARG MET CYS THR ALA MET LYS LYS ILE GLY LEU
SEQRES 26 A 785 ASP ASP GLU GLU LYS LEU ASP LEU PHE ARG VAL VAL ALA
SEQRES 27 A 785 GLY VAL LEU HIS LEU GLY ASN ILE ASP PHE GLU GLU ALA
SEQRES 28 A 785 GLY SER THR SER GLY GLY CYS ASN LEU LYS ASN LYS SER
SEQRES 29 A 785 THR GLN ALA LEU GLU TYR CYS ALA GLU LEU LEU GLY LEU
SEQRES 30 A 785 ASP GLN ASP ASP LEU ARG VAL SER LEU THR THR ARG VAL
SEQRES 31 A 785 MET LEU THR THR ALA GLY GLY ALA LYS GLY THR VAL ILE
SEQRES 32 A 785 LYS VAL PRO LEU LYS VAL GLU GLN ALA ASN ASN ALA ARG
SEQRES 33 A 785 ASP ALA LEU ALA LYS THR VAL TYR SER HIS LEU PHE ASP
SEQRES 34 A 785 HIS VAL VAL ASN ARG VAL ASN GLN CYS PHE PRO PHE GLU
SEQRES 35 A 785 THR SER SER TYR PHE ILE GLY VAL LEU ASP ILE ALA GLY
SEQRES 36 A 785 PHE GLU TYR PHE GLU HIS ASN SER PHE GLU GLN PHE CYS
SEQRES 37 A 785 ILE ASN TYR CYS ASN GLU LYS LEU GLN GLN PHE PHE ASN
SEQRES 38 A 785 GLU ARG ILE LEU LYS GLU GLU GLN GLU LEU TYR GLN LYS
SEQRES 39 A 785 GLU GLY LEU GLY VAL ASN GLU VAL HIS TYR VAL ASP ASN
SEQRES 40 A 785 GLN ASP CYS ILE ASP LEU ILE GLU ALA ARG LEU VAL GLY
SEQRES 41 A 785 ILE LEU ASP ILE LEU ASP GLU GLU ASN ARG LEU PRO GLN
SEQRES 42 A 785 PRO SER ASP GLN HIS PHE THR SER ALA VAL HIS GLN LYS
SEQRES 43 A 785 HIS LYS ASP HIS PHE ARG LEU SER ILE PRO ARG LYS SER
SEQRES 44 A 785 LYS LEU ALA ILE HIS ARG ASN ILE ARG ASP ASP GLU GLY
SEQRES 45 A 785 PHE ILE ILE ARG HIS PHE ALA GLY ALA VAL CYS TYR GLU
SEQRES 46 A 785 THR THR GLN PHE VAL GLU LYS ASN ASN ASP ALA LEU HIS
SEQRES 47 A 785 MET SER LEU GLU SER LEU ILE CYS GLU SER ARG ASP LYS
SEQRES 48 A 785 PHE ILE ARG GLU LEU PHE GLU SER SER THR ASN ASN ASN
SEQRES 49 A 785 LYS ASP THR LYS GLN LYS ALA GLY LYS LEU SER PHE ILE
SEQRES 50 A 785 SER VAL GLY ASN LYS PHE LYS THR GLN LEU ASN LEU LEU
SEQRES 51 A 785 LEU ASP LYS LEU ARG SER THR GLY ALA SER PHE ILE ARG
SEQRES 52 A 785 CYS ILE LYS PRO ASN LEU LYS MET THR SER HIS HIS PHE
SEQRES 53 A 785 GLU GLY ALA GLN ILE LEU SER GLN LEU GLN CYS SER GLY
SEQRES 54 A 785 MET VAL SER VAL LEU ASP LEU MET GLN GLY GLY PHE PRO
SEQRES 55 A 785 SER ARG ALA SER PHE HIS GLU LEU TYR ASN MET TYR LYS
SEQRES 56 A 785 LYS TYR MET PRO ASP LYS LEU ALA ARG LEU ASP PRO ARG
SEQRES 57 A 785 LEU PHE CYS LYS ALA LEU PHE LYS ALA LEU GLY LEU ASN
SEQRES 58 A 785 GLU ILE ASP TYR LYS PHE GLY LEU THR LYS VAL PHE PHE
SEQRES 59 A 785 ARG PRO GLY LYS PHE ALA GLU PHE ASP GLN ILE MET LYS
SEQRES 60 A 785 SER ASP PRO ASP HIS LEU ALA GLU LEU VAL LYS ARG VAL
SEQRES 61 A 785 ASN HIS TRP LEU ILE
HET ADP A 801 27
HET MG A 802 1
HET BEF A 803 4
HET GOL A 804 6
HET GOL A 805 6
HET GOL A 806 6
HET GOL A 807 6
HET GOL A 808 6
HET GOL A 809 6
HET GOL A 810 6
HET GOL A 811 6
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM BEF BERYLLIUM TRIFLUORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 MG MG 2+
FORMUL 4 BEF BE F3 1-
FORMUL 5 GOL 8(C3 H8 O3)
FORMUL 13 HOH *239(H2 O)
HELIX 1 AA1 ASN A 46 VAL A 48 5 3
HELIX 2 AA2 ASP A 61 LEU A 65 5 5
HELIX 3 AA3 ASN A 69 LYS A 83 1 15
HELIX 4 AA4 SER A 108 TYR A 115 1 8
HELIX 5 AA5 HIS A 126 LYS A 142 1 17
HELIX 6 AA6 GLY A 156 GLY A 173 1 18
HELIX 7 AA7 GLN A 176 ILE A 178 5 3
HELIX 8 AA8 ASP A 179 ALA A 185 1 7
HELIX 9 AA9 ALA A 185 GLY A 193 1 9
HELIX 10 AB1 LYS A 232 CYS A 236 5 5
HELIX 11 AB2 TYR A 245 ALA A 255 1 11
HELIX 12 AB3 SER A 256 LEU A 263 1 8
HELIX 13 AB4 SER A 267 ASN A 270 5 4
HELIX 14 AB5 PHE A 271 ARG A 276 1 6
HELIX 15 AB6 ASN A 284 ILE A 291 1 8
HELIX 16 AB7 LEU A 292 LYS A 296 5 5
HELIX 17 AB8 SER A 297 GLY A 304 1 8
HELIX 18 AB9 ASP A 312 ILE A 327 1 16
HELIX 19 AC1 ASP A 330 ASN A 349 1 20
HELIX 20 AC2 SER A 368 GLY A 380 1 13
HELIX 21 AC3 ASP A 382 THR A 391 1 10
HELIX 22 AC4 LYS A 412 CYS A 442 1 31
HELIX 23 AC5 SER A 467 LEU A 489 1 23
HELIX 24 AC6 LEU A 489 GLY A 500 1 12
HELIX 25 AC7 ASN A 511 ALA A 520 1 10
HELIX 26 AC8 GLY A 524 ARG A 534 1 11
HELIX 27 AC9 SER A 539 HIS A 551 1 13
HELIX 28 AD1 ILE A 559 SER A 563 5 5
HELIX 29 AD2 LEU A 565 ARG A 569 5 5
HELIX 30 AD3 ARG A 572 ASP A 574 5 3
HELIX 31 AD4 GLN A 592 ASN A 597 1 6
HELIX 32 AD5 HIS A 602 GLU A 611 1 10
HELIX 33 AD6 ASP A 614 PHE A 621 1 8
HELIX 34 AD7 SER A 642 THR A 661 1 20
HELIX 35 AD8 GLU A 681 SER A 692 1 12
HELIX 36 AD9 GLY A 693 GLY A 704 1 12
HELIX 37 AE1 PHE A 711 LYS A 719 1 9
HELIX 38 AE2 LYS A 720 MET A 722 5 3
HELIX 39 AE3 PRO A 723 ALA A 727 5 5
HELIX 40 AE4 ASP A 730 GLY A 743 1 14
HELIX 41 AE5 LYS A 762 LYS A 771 1 10
HELIX 42 AE6 ASP A 773 ASN A 785 1 13
HELIX 43 AE7 HIS A 786 ILE A 789 5 4
SHEET 1 AA1 5 PHE A 41 LEU A 44 0
SHEET 2 AA1 5 SER A 28 PRO A 33 -1 N LEU A 29 O ALA A 43
SHEET 3 AA1 5 GLY A 15 ILE A 24 -1 N VAL A 22 O THR A 30
SHEET 4 AA1 5 VAL A 7 HIS A 11 -1 N VAL A 7 O GLY A 19
SHEET 5 AA1 5 PHE A 49 PRO A 50 -1 O PHE A 49 N TRP A 8
SHEET 1 AA2 7 TYR A 87 VAL A 90 0
SHEET 2 AA2 7 ILE A 93 VAL A 97 -1 O ILE A 95 N THR A 88
SHEET 3 AA2 7 GLY A 662 ILE A 669 1 O ARG A 667 N LEU A 94
SHEET 4 AA2 7 GLN A 145 SER A 150 1 N SER A 150 O CYS A 668
SHEET 5 AA2 7 TYR A 450 ASP A 456 1 O PHE A 451 N GLN A 145
SHEET 6 AA2 7 GLY A 207 PHE A 214 -1 N LYS A 208 O ASP A 456
SHEET 7 AA2 7 VAL A 220 TYR A 228 -1 O GLY A 222 N HIS A 213
SHEET 1 AA3 2 ASN A 194 THR A 197 0
SHEET 2 AA3 2 ASN A 200 SER A 204 -1 O ASN A 200 N THR A 197
SHEET 1 AA4 2 PHE A 352 GLU A 353 0
SHEET 2 AA4 2 ASN A 363 LEU A 364 -1 O ASN A 363 N GLU A 353
SHEET 1 AA5 2 THR A 392 MET A 395 0
SHEET 2 AA5 2 ILE A 407 PRO A 410 -1 O VAL A 409 N ARG A 393
SHEET 1 AA6 3 LEU A 557 SER A 558 0
SHEET 2 AA6 3 GLY A 576 HIS A 581 -1 O ILE A 578 N SER A 558
SHEET 3 AA6 3 GLY A 584 GLU A 589 -1 O TYR A 588 N PHE A 577
SHEET 1 AA7 3 SER A 707 SER A 710 0
SHEET 2 AA7 3 LYS A 755 PHE A 758 -1 O PHE A 758 N SER A 707
SHEET 3 AA7 3 TYR A 749 PHE A 751 -1 N LYS A 750 O PHE A 757
LINK OG1 THR A 158 MG MG A 802 1555 1555 1.98
LINK OG SER A 204 MG MG A 802 1555 1555 2.08
LINK O1B ADP A 801 MG MG A 802 1555 1555 2.22
LINK O3B ADP A 801 BE BEF A 803 1555 1555 2.11
LINK MG MG A 802 O HOH A 937 1555 1555 2.15
LINK MG MG A 802 O HOH A 902 1555 1555 2.06
CISPEP 1 GLN A 36 LYS A 37 0 -3.50
SITE 1 AC1 22 ASN A 98 PRO A 99 TYR A 100 PHE A 101
SITE 2 AC1 22 TYR A 107 GLU A 152 GLY A 154 ALA A 155
SITE 3 AC1 22 GLY A 156 LYS A 157 THR A 158 GLU A 159
SITE 4 AC1 22 PHE A 163 ASN A 200 LEU A 310 MG A 802
SITE 5 AC1 22 BEF A 803 HOH A 902 HOH A 933 HOH A 937
SITE 6 AC1 22 HOH A1024 HOH A1028
SITE 1 AC2 6 THR A 158 SER A 204 ADP A 801 BEF A 803
SITE 2 AC2 6 HOH A 902 HOH A 937
SITE 1 AC3 10 SER A 153 THR A 158 ASN A 200 SER A 203
SITE 2 AC3 10 SER A 204 ADP A 801 MG A 802 HOH A 902
SITE 3 AC3 10 HOH A 937 HOH A1066
SITE 1 AC4 5 ILE A 148 ASN A 477 GLN A 481 ARG A 667
SITE 2 AC4 5 GOL A 805
SITE 1 AC5 9 ILE A 148 SER A 150 PHE A 484 PHE A 665
SITE 2 AC5 9 ILE A 666 ARG A 667 SER A 692 MET A 694
SITE 3 AC5 9 GOL A 804
SITE 1 AC6 5 LYS A 196 ASN A 201 LEU A 306 LYS A 307
SITE 2 AC6 5 HOH A1074
SITE 1 AC7 3 ASP A 385 ASP A 527 LYS A 648
SITE 1 AC8 2 HIS A 507 TYR A 508
SITE 1 AC9 3 GLU A 211 LYS A 657 HOH A1027
SITE 1 AD1 2 LYS A 674 GLU A 681
SITE 1 AD2 5 SER A 563 LYS A 564 LEU A 565 ALA A 566
SITE 2 AD2 5 ARG A 569
CRYST1 72.340 83.830 177.660 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013824 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011929 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005629 0.00000
ATOM 1 N LYS A 5 21.704 41.564 59.723 1.00 89.53 N
ANISOU 1 N LYS A 5 9494 16264 8260 -892 -1446 -3624 N
ATOM 2 CA LYS A 5 21.550 40.190 60.206 1.00 88.09 C
ANISOU 2 CA LYS A 5 9207 16327 7935 -713 -1385 -3449 C
ATOM 3 C LYS A 5 20.409 39.396 59.456 1.00 87.63 C
ANISOU 3 C LYS A 5 9244 16160 7893 -621 -1240 -3218 C
ATOM 4 O LYS A 5 20.701 38.266 59.053 1.00 84.10 O
ANISOU 4 O LYS A 5 8716 15783 7454 -598 -1160 -3027 O
ATOM 5 CB LYS A 5 21.341 40.160 61.727 1.00 91.90 C
ANISOU 5 CB LYS A 5 9634 17080 8203 -530 -1478 -3564 C
ATOM 6 N PRO A 6 19.162 39.943 59.226 1.00 83.91 N
ANISOU 6 N PRO A 6 8934 15518 7431 -571 -1208 -3232 N
ATOM 7 CA PRO A 6 18.105 39.163 58.530 1.00 80.56 C
ANISOU 7 CA PRO A 6 8583 15006 7022 -493 -1076 -3015 C
ATOM 8 C PRO A 6 18.384 38.690 57.100 1.00 78.79 C
ANISOU 8 C PRO A 6 8374 14599 6965 -625 -974 -2849 C
ATOM 9 O PRO A 6 18.972 39.397 56.268 1.00 78.72 O
ANISOU 9 O PRO A 6 8398 14407 7106 -806 -984 -2910 O
ATOM 10 CB PRO A 6 16.919 40.134 58.498 1.00 82.44 C
ANISOU 10 CB PRO A 6 8986 15076 7262 -450 -1086 -3115 C
ATOM 11 CG PRO A 6 17.116 40.985 59.691 1.00 89.24 C
ANISOU 11 CG PRO A 6 9832 16060 8014 -397 -1219 -3353 C
ATOM 12 CD PRO A 6 18.605 41.234 59.694 1.00 86.62 C
ANISOU 12 CD PRO A 6 9396 15762 7755 -559 -1296 -3451 C
ATOM 13 N VAL A 7 17.904 37.469 56.809 1.00 71.00 N
ANISOU 13 N VAL A 7 7367 13662 5947 -530 -873 -2631 N
ATOM 14 CA VAL A 7 18.030 36.846 55.489 1.00 68.72 C
ANISOU 14 CA VAL A 7 7095 13222 5794 -617 -770 -2458 C
ATOM 15 C VAL A 7 16.670 36.252 55.029 1.00 69.93 C
ANISOU 15 C VAL A 7 7348 13289 5935 -515 -671 -2292 C
ATOM 16 O VAL A 7 15.705 36.204 55.798 1.00 70.00 O
ANISOU 16 O VAL A 7 7388 13386 5822 -376 -679 -2296 O
ATOM 17 CB VAL A 7 19.165 35.779 55.437 1.00 72.31 C
ANISOU 17 CB VAL A 7 7394 13833 6247 -627 -755 -2355 C
ATOM 18 CG1 VAL A 7 20.536 36.416 55.676 1.00 73.52 C
ANISOU 18 CG1 VAL A 7 7443 14057 6435 -754 -846 -2516 C
ATOM 19 CG2 VAL A 7 18.917 34.636 56.423 1.00 71.82 C
ANISOU 19 CG2 VAL A 7 7252 14014 6024 -438 -752 -2243 C
ATOM 20 N TRP A 8 16.620 35.803 53.779 1.00 63.45 N
ANISOU 20 N TRP A 8 6567 12305 5237 -590 -581 -2152 N
ATOM 21 CA TRP A 8 15.484 35.125 53.196 1.00 61.80 C
ANISOU 21 CA TRP A 8 6437 12008 5038 -518 -488 -1984 C
ATOM 22 C TRP A 8 15.831 33.664 53.014 1.00 66.74 C
ANISOU 22 C TRP A 8 6974 12734 5651 -468 -430 -1796 C
ATOM 23 O TRP A 8 16.853 33.350 52.403 1.00 65.75 O
ANISOU 23 O TRP A 8 6786 12590 5607 -556 -417 -1767 O
ATOM 24 CB TRP A 8 15.105 35.745 51.850 1.00 58.85 C
ANISOU 24 CB TRP A 8 6190 11357 4814 -638 -436 -1973 C
ATOM 25 CG TRP A 8 14.416 37.073 51.938 1.00 59.38 C
ANISOU 25 CG TRP A 8 6379 11288 4893 -656 -482 -2124 C
ATOM 26 CD1 TRP A 8 14.842 38.254 51.407 1.00 62.61 C
ANISOU 26 CD1 TRP A 8 6860 11517 5412 -802 -522 -2252 C
ATOM 27 CD2 TRP A 8 13.125 37.325 52.497 1.00 58.64 C
ANISOU 27 CD2 TRP A 8 6361 11212 4709 -522 -487 -2149 C
ATOM 28 NE1 TRP A 8 13.896 39.228 51.605 1.00 62.09 N
ANISOU 28 NE1 TRP A 8 6919 11340 5330 -758 -558 -2360 N
ATOM 29 CE2 TRP A 8 12.835 38.688 52.282 1.00 63.13 C
ANISOU 29 CE2 TRP A 8 7049 11601 5337 -581 -537 -2305 C
ATOM 30 CE3 TRP A 8 12.145 36.512 53.090 1.00 59.32 C
ANISOU 30 CE3 TRP A 8 6425 11441 4674 -362 -449 -2042 C
ATOM 31 CZ2 TRP A 8 11.632 39.269 52.694 1.00 63.33 C
ANISOU 31 CZ2 TRP A 8 7167 11600 5295 -465 -556 -2374 C
ATOM 32 CZ3 TRP A 8 10.961 37.088 53.510 1.00 61.34 C
ANISOU 32 CZ3 TRP A 8 6760 11688 4860 -259 -461 -2104 C
ATOM 33 CH2 TRP A 8 10.706 38.449 53.300 1.00 62.85 C
ANISOU 33 CH2 TRP A 8 7065 11708 5105 -302 -514 -2273 C
ATOM 34 N ALA A 9 15.012 32.778 53.578 1.00 63.18 N
ANISOU 34 N ALA A 9 6513 12398 5094 -325 -401 -1671 N
ATOM 35 CA ALA A 9 15.232 31.340 53.515 1.00 61.87 C
ANISOU 35 CA ALA A 9 6278 12320 4909 -260 -356 -1485 C
ATOM 36 C ALA A 9 13.962 30.705 53.029 1.00 66.38 C
ANISOU 36 C ALA A 9 6934 12793 5492 -207 -276 -1326 C
ATOM 37 O ALA A 9 12.909 31.327 53.190 1.00 66.07 O
ANISOU 37 O ALA A 9 6974 12709 5422 -178 -271 -1370 O
ATOM 38 CB ALA A 9 15.624 30.814 54.886 1.00 63.44 C
ANISOU 38 CB ALA A 9 6366 12788 4952 -140 -415 -1483 C
ATOM 39 N PRO A 10 14.003 29.494 52.421 1.00 63.26 N
ANISOU 39 N PRO A 10 6528 12363 5144 -190 -218 -1147 N
ATOM 40 CA PRO A 10 12.776 28.947 51.801 1.00 61.95 C
ANISOU 40 CA PRO A 10 6450 12077 5011 -163 -145 -1004 C
ATOM 41 C PRO A 10 11.612 28.709 52.752 1.00 64.57 C
ANISOU 41 C PRO A 10 6788 12533 5211 -47 -142 -942 C
ATOM 42 O PRO A 10 11.785 28.580 53.955 1.00 63.80 O
ANISOU 42 O PRO A 10 6618 12642 4981 38 -188 -962 O
ATOM 43 CB PRO A 10 13.251 27.638 51.167 1.00 62.73 C
ANISOU 43 CB PRO A 10 6521 12141 5173 -159 -104 -843 C
ATOM 44 CG PRO A 10 14.707 27.872 50.913 1.00 67.24 C
ANISOU 44 CG PRO A 10 7018 12734 5797 -228 -137 -934 C
ATOM 45 CD PRO A 10 15.175 28.651 52.102 1.00 63.93 C
ANISOU 45 CD PRO A 10 6529 12488 5274 -206 -217 -1082 C
ATOM 46 N HIS A 11 10.404 28.720 52.163 1.00 60.91 N
ANISOU 46 N HIS A 11 6412 11946 4784 -49 -86 -873 N
ATOM 47 CA HIS A 11 9.101 28.509 52.808 1.00 59.23 C
ANISOU 47 CA HIS A 11 6212 11827 4468 44 -65 -798 C
ATOM 48 C HIS A 11 8.202 27.845 51.765 1.00 61.71 C
ANISOU 48 C HIS A 11 6593 11981 4872 16 8 -646 C
ATOM 49 O HIS A 11 8.135 28.338 50.635 1.00 58.19 O
ANISOU 49 O HIS A 11 6224 11337 4547 -68 31 -689 O
ATOM 50 CB HIS A 11 8.509 29.829 53.322 1.00 59.52 C
ANISOU 50 CB HIS A 11 6283 11893 4438 72 -97 -969 C
ATOM 51 CG HIS A 11 7.256 29.644 54.113 1.00 63.24 C
ANISOU 51 CG HIS A 11 6742 12507 4778 181 -76 -904 C
ATOM 52 ND1 HIS A 11 6.041 29.386 53.498 1.00 63.89 N
ANISOU 52 ND1 HIS A 11 6881 12499 4897 184 -14 -798 N
ATOM 53 CD2 HIS A 11 7.067 29.688 55.453 1.00 66.02 C
ANISOU 53 CD2 HIS A 11 7025 13101 4960 289 -109 -930 C
ATOM 54 CE1 HIS A 11 5.160 29.278 54.478 1.00 63.53 C
ANISOU 54 CE1 HIS A 11 6790 12643 4705 287 -7 -760 C
ATOM 55 NE2 HIS A 11 5.727 29.468 55.671 1.00 65.44 N
ANISOU 55 NE2 HIS A 11 6960 13089 4815 357 -61 -837 N
ATOM 56 N PRO A 12 7.512 26.731 52.111 1.00 60.37 N
ANISOU 56 N PRO A 12 6398 11892 4647 78 40 -466 N
ATOM 57 CA PRO A 12 6.739 25.989 51.093 1.00 59.30 C
ANISOU 57 CA PRO A 12 6323 11600 4608 39 100 -319 C
ATOM 58 C PRO A 12 5.556 26.727 50.461 1.00 64.11 C
ANISOU 58 C PRO A 12 7011 12091 5257 14 132 -362 C
ATOM 59 O PRO A 12 5.200 26.390 49.338 1.00 62.61 O
ANISOU 59 O PRO A 12 6883 11728 5179 -44 170 -295 O
ATOM 60 CB PRO A 12 6.246 24.756 51.852 1.00 61.56 C
ANISOU 60 CB PRO A 12 6558 12026 4808 110 115 -129 C
ATOM 61 CG PRO A 12 6.291 25.149 53.298 1.00 67.33 C
ANISOU 61 CG PRO A 12 7213 12999 5369 198 77 -189 C
ATOM 62 CD PRO A 12 7.519 26.010 53.397 1.00 63.42 C
ANISOU 62 CD PRO A 12 6699 12510 4886 176 21 -375 C
ATOM 63 N THR A 13 4.922 27.687 51.153 1.00 62.97 N
ANISOU 63 N THR A 13 6866 12042 5019 67 115 -471 N
ATOM 64 CA THR A 13 3.769 28.365 50.536 1.00 62.21 C
ANISOU 64 CA THR A 13 6842 11836 4957 59 143 -508 C
ATOM 65 C THR A 13 4.055 29.844 50.256 1.00 62.67 C
ANISOU 65 C THR A 13 6967 11792 5053 31 106 -716 C
ATOM 66 O THR A 13 3.403 30.428 49.392 1.00 61.11 O
ANISOU 66 O THR A 13 6852 11440 4927 2 124 -750 O
ATOM 67 CB THR A 13 2.486 28.202 51.381 1.00 71.99 C
ANISOU 67 CB THR A 13 8039 13248 6068 153 164 -442 C
ATOM 68 OG1 THR A 13 2.562 28.996 52.562 1.00 74.33 O
ANISOU 68 OG1 THR A 13 8291 13726 6226 237 121 -576 O
ATOM 69 CG2 THR A 13 2.181 26.753 51.724 1.00 70.62 C
ANISOU 69 CG2 THR A 13 7803 13173 5856 168 198 -223 C
ATOM 70 N ASP A 14 4.996 30.456 51.002 1.00 58.08 N
ANISOU 70 N ASP A 14 6351 11297 4421 40 48 -853 N
ATOM 71 CA ASP A 14 5.338 31.859 50.791 1.00 56.92 C
ANISOU 71 CA ASP A 14 6269 11044 4314 2 1 -1053 C
ATOM 72 C ASP A 14 6.528 32.031 49.836 1.00 57.17 C
ANISOU 72 C ASP A 14 6333 10906 4484 -126 -6 -1091 C
ATOM 73 O ASP A 14 6.772 33.145 49.389 1.00 56.54 O
ANISOU 73 O ASP A 14 6325 10688 4468 -188 -35 -1227 O
ATOM 74 CB ASP A 14 5.622 32.548 52.130 1.00 60.23 C
ANISOU 74 CB ASP A 14 6636 11647 4600 79 -66 -1202 C
ATOM 75 CG ASP A 14 4.439 32.567 53.088 1.00 68.92 C
ANISOU 75 CG ASP A 14 7706 12931 5551 214 -60 -1192 C
ATOM 76 OD1 ASP A 14 3.304 32.288 52.645 1.00 68.44 O
ANISOU 76 OD1 ASP A 14 7675 12830 5500 239 -6 -1096 O
ATOM 77 OD2 ASP A 14 4.650 32.843 54.274 1.00 76.05 O
ANISOU 77 OD2 ASP A 14 8548 14028 6320 294 -107 -1280 O
ATOM 78 N GLY A 15 7.232 30.943 49.519 1.00 52.76 N
ANISOU 78 N GLY A 15 5722 10358 3967 -163 20 -968 N
ATOM 79 CA GLY A 15 8.426 30.976 48.683 1.00 53.59 C
ANISOU 79 CA GLY A 15 5831 10347 4185 -273 18 -993 C
ATOM 80 C GLY A 15 9.624 31.239 49.577 1.00 60.74 C
ANISOU 80 C GLY A 15 6649 11392 5036 -277 -45 -1099 C
ATOM 81 O GLY A 15 10.538 30.418 49.675 1.00 63.21 O
ANISOU 81 O GLY A 15 6882 11781 5353 -284 -46 -1037 O
ATOM 82 N PHE A 16 9.588 32.356 50.301 1.00 56.32 N
ANISOU 82 N PHE A 16 6100 10880 4418 -260 -104 -1264 N
ATOM 83 CA PHE A 16 10.630 32.734 51.252 1.00 56.10 C
ANISOU 83 CA PHE A 16 5991 10998 4327 -260 -178 -1389 C
ATOM 84 C PHE A 16 10.036 33.218 52.566 1.00 61.51 C
ANISOU 84 C PHE A 16 6657 11850 4863 -145 -229 -1484 C
ATOM 85 O PHE A 16 8.895 33.672 52.594 1.00 61.11 O
ANISOU 85 O PHE A 16 6677 11758 4783 -90 -216 -1507 O
ATOM 86 CB PHE A 16 11.537 33.811 50.654 1.00 56.90 C
ANISOU 86 CB PHE A 16 6128 10957 4536 -398 -215 -1536 C
ATOM 87 CG PHE A 16 12.372 33.281 49.522 1.00 56.69 C
ANISOU 87 CG PHE A 16 6085 10825 4631 -505 -168 -1450 C
ATOM 88 CD1 PHE A 16 13.491 32.496 49.769 1.00 59.42 C
ANISOU 88 CD1 PHE A 16 6312 11300 4963 -511 -179 -1409 C
ATOM 89 CD2 PHE A 16 12.040 33.557 48.205 1.00 56.25 C
ANISOU 89 CD2 PHE A 16 6129 10551 4694 -590 -114 -1410 C
ATOM 90 CE1 PHE A 16 14.263 32.006 48.717 1.00 58.63 C
ANISOU 90 CE1 PHE A 16 6192 11118 4969 -597 -134 -1338 C
ATOM 91 CE2 PHE A 16 12.826 33.077 47.158 1.00 57.82 C
ANISOU 91 CE2 PHE A 16 6307 10668 4991 -682 -69 -1337 C
ATOM 92 CZ PHE A 16 13.919 32.291 47.422 1.00 55.90 C
ANISOU 92 CZ PHE A 16 5943 10561 4734 -681 -77 -1302 C
ATOM 93 N GLN A 17 10.811 33.091 53.660 1.00 58.96 N
ANISOU 93 N GLN A 17 6233 11732 4438 -99 -288 -1541 N
ATOM 94 CA GLN A 17 10.451 33.580 54.982 1.00 59.82 C
ANISOU 94 CA GLN A 17 6310 12029 4389 13 -348 -1653 C
ATOM 95 C GLN A 17 11.674 34.282 55.549 1.00 65.52 C
ANISOU 95 C GLN A 17 6979 12819 5098 -36 -441 -1834 C
ATOM 96 O GLN A 17 12.782 34.027 55.072 1.00 64.32 O
ANISOU 96 O GLN A 17 6778 12627 5032 -134 -448 -1821 O
ATOM 97 CB GLN A 17 9.925 32.459 55.913 1.00 60.88 C
ANISOU 97 CB GLN A 17 6364 12394 4372 149 -320 -1500 C
ATOM 98 CG GLN A 17 10.960 31.393 56.275 1.00 71.59 C
ANISOU 98 CG GLN A 17 7613 13891 5699 157 -332 -1399 C
ATOM 99 CD GLN A 17 10.405 30.248 57.079 1.00 79.84 C
ANISOU 99 CD GLN A 17 8596 15128 6611 278 -300 -1219 C
ATOM 100 OE1 GLN A 17 9.888 30.417 58.194 1.00 74.07 O
ANISOU 100 OE1 GLN A 17 7831 14594 5717 388 -324 -1251 O
ATOM 101 NE2 GLN A 17 10.544 29.041 56.541 1.00 68.37 N
ANISOU 101 NE2 GLN A 17 7130 13628 5221 260 -248 -1024 N
ATOM 102 N VAL A 18 11.470 35.199 56.512 1.00 64.58 N
ANISOU 102 N VAL A 18 6867 12797 4874 30 -516 -2011 N
ATOM 103 CA VAL A 18 12.551 35.930 57.180 1.00 66.23 C
ANISOU 103 CA VAL A 18 7023 13083 5056 -10 -620 -2205 C
ATOM 104 C VAL A 18 13.155 35.018 58.223 1.00 74.18 C
ANISOU 104 C VAL A 18 7892 14369 5924 79 -646 -2144 C
ATOM 105 O VAL A 18 12.439 34.446 59.043 1.00 74.26 O
ANISOU 105 O VAL A 18 7868 14564 5785 221 -626 -2060 O
ATOM 106 CB VAL A 18 12.107 37.272 57.832 1.00 71.66 C
ANISOU 106 CB VAL A 18 7781 13761 5685 34 -702 -2436 C
ATOM 107 CG1 VAL A 18 13.298 38.026 58.415 1.00 73.43 C
ANISOU 107 CG1 VAL A 18 7957 14037 5907 -37 -817 -2641 C
ATOM 108 CG2 VAL A 18 11.367 38.158 56.856 1.00 71.09 C
ANISOU 108 CG2 VAL A 18 7859 13415 5736 -26 -677 -2481 C
ATOM 109 N GLY A 19 14.469 34.927 58.209 1.00 73.61 N
ANISOU 109 N GLY A 19 7737 14335 5897 -5 -692 -2186 N
ATOM 110 CA GLY A 19 15.215 34.132 59.165 1.00 74.85 C
ANISOU 110 CA GLY A 19 7759 14752 5930 74 -732 -2145 C
ATOM 111 C GLY A 19 16.538 34.783 59.478 1.00 81.83 C
ANISOU 111 C GLY A 19 8566 15689 6836 -14 -833 -2327 C
ATOM 112 O GLY A 19 16.867 35.848 58.939 1.00 82.60 O
ANISOU 112 O GLY A 19 8720 15611 7054 -150 -869 -2476 O
ATOM 113 N ASN A 20 17.281 34.157 60.383 1.00 79.13 N
ANISOU 113 N ASN A 20 8096 15595 6375 62 -884 -2313 N
ATOM 114 CA ASN A 20 18.626 34.555 60.777 1.00 79.93 C
ANISOU 114 CA ASN A 20 8092 15800 6480 -8 -984 -2464 C
ATOM 115 C ASN A 20 19.518 33.360 60.594 1.00 83.05 C
ANISOU 115 C ASN A 20 8370 16298 6887 3 -957 -2306 C
ATOM 116 O ASN A 20 19.057 32.236 60.836 1.00 82.09 O
ANISOU 116 O ASN A 20 8233 16275 6684 128 -903 -2114 O
ATOM 117 CB ASN A 20 18.670 35.035 62.232 1.00 81.11 C
ANISOU 117 CB ASN A 20 8188 16187 6443 101 -1092 -2631 C
ATOM 118 CG ASN A 20 17.834 36.250 62.533 1.00110.93 C
ANISOU 118 CG ASN A 20 12077 19881 10192 114 -1134 -2814 C
ATOM 119 OD1 ASN A 20 18.336 37.379 62.607 1.00105.03 O
ANISOU 119 OD1 ASN A 20 11352 19052 9503 12 -1223 -3033 O
ATOM 120 ND2 ASN A 20 16.550 36.030 62.791 1.00105.75 N
ANISOU 120 ND2 ASN A 20 11486 19257 9435 248 -1077 -2732 N
ATOM 121 N ILE A 21 20.778 33.573 60.147 1.00 79.20 N
ANISOU 121 N ILE A 21 7801 15786 6503 -127 -995 -2379 N
ATOM 122 CA ILE A 21 21.738 32.474 60.023 1.00 78.19 C
ANISOU 122 CA ILE A 21 7548 15777 6381 -104 -983 -2252 C
ATOM 123 C ILE A 21 22.260 32.201 61.434 1.00 84.36 C
ANISOU 123 C ILE A 21 8206 16868 6979 24 -1082 -2310 C
ATOM 124 O ILE A 21 22.719 33.137 62.103 1.00 85.04 O
ANISOU 124 O ILE A 21 8248 17043 7019 -16 -1185 -2521 O
ATOM 125 CB ILE A 21 22.891 32.763 59.013 1.00 80.76 C
ANISOU 125 CB ILE A 21 7819 15989 6879 -285 -979 -2303 C
ATOM 126 CG1 ILE A 21 22.349 33.022 57.593 1.00 80.18 C
ANISOU 126 CG1 ILE A 21 7874 15617 6974 -403 -877 -2233 C
ATOM 127 CG2 ILE A 21 23.903 31.603 58.998 1.00 79.78 C
ANISOU 127 CG2 ILE A 21 7550 16022 6740 -231 -976 -2188 C
ATOM 128 CD1 ILE A 21 23.210 33.935 56.769 1.00 87.93 C
ANISOU 128 CD1 ILE A 21 8841 16460 8108 -610 -891 -2354 C
ATOM 129 N VAL A 22 22.164 30.950 61.905 1.00 82.50 N
ANISOU 129 N VAL A 22 7922 16791 6633 180 -1056 -2126 N
ATOM 130 CA VAL A 22 22.691 30.626 63.242 1.00 85.73 C
ANISOU 130 CA VAL A 22 8212 17506 6854 313 -1151 -2163 C
ATOM 131 C VAL A 22 23.958 29.762 63.087 1.00 92.70 C
ANISOU 131 C VAL A 22 8955 18505 7762 326 -1174 -2090 C
ATOM 132 O VAL A 22 24.851 29.843 63.928 1.00 94.43 O
ANISOU 132 O VAL A 22 9048 18954 7877 372 -1275 -2190 O
ATOM 133 CB VAL A 22 21.664 30.026 64.244 1.00 89.45 C
ANISOU 133 CB VAL A 22 8720 18134 7135 500 -1133 -2040 C
ATOM 134 CG1 VAL A 22 20.609 31.059 64.613 1.00 89.80 C
ANISOU 134 CG1 VAL A 22 8866 18131 7123 504 -1140 -2172 C
ATOM 135 CG2 VAL A 22 21.008 28.753 63.721 1.00 87.31 C
ANISOU 135 CG2 VAL A 22 8503 17778 6893 567 -1023 -1761 C
ATOM 136 N ASP A 23 24.052 28.994 61.986 1.00 89.26 N
ANISOU 136 N ASP A 23 8540 17911 7463 286 -1085 -1931 N
ATOM 137 CA ASP A 23 25.209 28.163 61.705 1.00 90.24 C
ANISOU 137 CA ASP A 23 8541 18122 7624 306 -1096 -1858 C
ATOM 138 C ASP A 23 25.427 28.020 60.195 1.00 92.05 C
ANISOU 138 C ASP A 23 8806 18114 8055 179 -1006 -1796 C
ATOM 139 O ASP A 23 24.509 27.655 59.457 1.00 90.05 O
ANISOU 139 O ASP A 23 8677 17666 7871 177 -910 -1660 O
ATOM 140 CB ASP A 23 25.072 26.781 62.372 1.00 93.15 C
ANISOU 140 CB ASP A 23 8883 18650 7861 507 -1092 -1652 C
ATOM 141 CG ASP A 23 26.321 25.921 62.264 1.00110.28 C
ANISOU 141 CG ASP A 23 10915 20946 10040 566 -1126 -1591 C
ATOM 142 OD1 ASP A 23 27.297 26.195 62.999 1.00112.77 O
ANISOU 142 OD1 ASP A 23 11092 21484 10272 589 -1229 -1719 O
ATOM 143 OD2 ASP A 23 26.326 24.978 61.433 1.00118.19 O
ANISOU 143 OD2 ASP A 23 11947 21828 11130 595 -1055 -1421 O
ATOM 144 N ILE A 24 26.649 28.342 59.743 1.00 88.32 N
ANISOU 144 N ILE A 24 8217 17671 7669 68 -1040 -1902 N
ATOM 145 CA ILE A 24 27.070 28.193 58.348 1.00 86.54 C
ANISOU 145 CA ILE A 24 7994 17270 7618 -48 -960 -1854 C
ATOM 146 C ILE A 24 27.810 26.863 58.267 1.00 90.37 C
ANISOU 146 C ILE A 24 8378 17877 8083 81 -953 -1711 C
ATOM 147 O ILE A 24 28.637 26.571 59.127 1.00 90.72 O
ANISOU 147 O ILE A 24 8284 18161 8024 170 -1040 -1750 O
ATOM 148 CB ILE A 24 27.927 29.386 57.801 1.00 90.06 C
ANISOU 148 CB ILE A 24 8373 17669 8178 -262 -990 -2046 C
ATOM 149 CG1 ILE A 24 27.370 30.764 58.243 1.00 90.70 C
ANISOU 149 CG1 ILE A 24 8534 17679 8247 -364 -1042 -2224 C
ATOM 150 CG2 ILE A 24 28.074 29.300 56.266 1.00 89.77 C
ANISOU 150 CG2 ILE A 24 8372 17423 8315 -386 -886 -1977 C
ATOM 151 CD1 ILE A 24 28.267 31.984 57.999 1.00 97.46 C
ANISOU 151 CD1 ILE A 24 9317 18520 9194 -572 -1102 -2427 C
ATOM 152 N GLY A 25 27.485 26.068 57.261 1.00 86.95 N
ANISOU 152 N GLY A 25 8017 17277 7742 101 -857 -1552 N
ATOM 153 CA GLY A 25 28.116 24.779 57.037 1.00 87.61 C
ANISOU 153 CA GLY A 25 8029 17433 7825 229 -845 -1414 C
ATOM 154 C GLY A 25 28.629 24.617 55.620 1.00 93.45 C
ANISOU 154 C GLY A 25 8754 18033 8720 137 -769 -1393 C
ATOM 155 O GLY A 25 28.237 25.370 54.721 1.00 91.79 O
ANISOU 155 O GLY A 25 8624 17630 8621 -21 -707 -1441 O
ATOM 156 N PRO A 26 29.485 23.601 55.381 1.00 92.39 N
ANISOU 156 N PRO A 26 8522 17991 8590 246 -772 -1314 N
ATOM 157 CA PRO A 26 30.012 23.382 54.028 1.00 91.90 C
ANISOU 157 CA PRO A 26 8435 17820 8662 176 -698 -1297 C
ATOM 158 C PRO A 26 28.951 23.238 52.943 1.00 95.96 C
ANISOU 158 C PRO A 26 9128 18052 9280 124 -591 -1196 C
ATOM 159 O PRO A 26 29.184 23.712 51.833 1.00 97.14 O
ANISOU 159 O PRO A 26 9280 18087 9543 -13 -528 -1243 O
ATOM 160 CB PRO A 26 30.794 22.079 54.178 1.00 94.39 C
ANISOU 160 CB PRO A 26 8653 18277 8933 367 -727 -1198 C
ATOM 161 CG PRO A 26 31.227 22.074 55.594 1.00 99.88 C
ANISOU 161 CG PRO A 26 9243 19223 9482 470 -839 -1244 C
ATOM 162 CD PRO A 26 30.070 22.640 56.340 1.00 95.03 C
ANISOU 162 CD PRO A 26 8757 18548 8801 443 -850 -1246 C
ATOM 163 N ASP A 27 27.810 22.595 53.227 1.00 91.22 N
ANISOU 163 N ASP A 27 8672 17347 8643 226 -570 -1058 N
ATOM 164 CA ASP A 27 26.803 22.407 52.184 1.00 89.20 C
ANISOU 164 CA ASP A 27 8577 16831 8485 179 -474 -964 C
ATOM 165 C ASP A 27 25.436 23.058 52.479 1.00 88.43 C
ANISOU 165 C ASP A 27 8625 16607 8369 120 -453 -960 C
ATOM 166 O ASP A 27 24.639 23.225 51.553 1.00 86.12 O
ANISOU 166 O ASP A 27 8454 16101 8165 42 -378 -923 O
ATOM 167 CB ASP A 27 26.616 20.917 51.896 1.00 91.74 C
ANISOU 167 CB ASP A 27 8950 17092 8815 340 -449 -784 C
ATOM 168 CG ASP A 27 27.709 20.367 51.009 1.00109.22 C
ANISOU 168 CG ASP A 27 11070 19332 11098 369 -430 -789 C
ATOM 169 OD1 ASP A 27 28.874 20.324 51.462 1.00112.43 O
ANISOU 169 OD1 ASP A 27 11313 19949 11456 418 -491 -858 O
ATOM 170 OD2 ASP A 27 27.405 20.002 49.848 1.00115.88 O
ANISOU 170 OD2 ASP A 27 11998 19994 12039 348 -355 -729 O
ATOM 171 N SER A 28 25.173 23.448 53.736 1.00 84.07 N
ANISOU 171 N SER A 28 8055 16193 7696 161 -521 -1006 N
ATOM 172 CA SER A 28 23.888 24.047 54.092 1.00 81.74 C
ANISOU 172 CA SER A 28 7885 15806 7367 129 -505 -1009 C
ATOM 173 C SER A 28 24.020 25.081 55.204 1.00 84.24 C
ANISOU 173 C SER A 28 8146 16281 7582 102 -585 -1166 C
ATOM 174 O SER A 28 25.046 25.144 55.885 1.00 85.70 O
ANISOU 174 O SER A 28 8193 16670 7700 134 -663 -1249 O
ATOM 175 CB SER A 28 22.908 22.957 54.515 1.00 84.47 C
ANISOU 175 CB SER A 28 8318 16128 7647 271 -485 -817 C
ATOM 176 OG SER A 28 23.423 22.229 55.620 1.00 96.28 O
ANISOU 176 OG SER A 28 9723 17844 9016 418 -557 -765 O
ATOM 177 N LEU A 29 22.975 25.903 55.371 1.00 77.70 N
ANISOU 177 N LEU A 29 7425 15360 6740 48 -571 -1216 N
ATOM 178 CA LEU A 29 22.885 26.916 56.426 1.00 77.47 C
ANISOU 178 CA LEU A 29 7371 15455 6608 35 -647 -1371 C
ATOM 179 C LEU A 29 21.828 26.479 57.425 1.00 76.39 C
ANISOU 179 C LEU A 29 7291 15404 6330 176 -652 -1274 C
ATOM 180 O LEU A 29 20.926 25.718 57.066 1.00 73.76 O
ANISOU 180 O LEU A 29 7051 14960 6015 227 -583 -1106 O
ATOM 181 CB LEU A 29 22.526 28.288 55.813 1.00 77.46 C
ANISOU 181 CB LEU A 29 7451 15277 6701 -132 -630 -1520 C
ATOM 182 CG LEU A 29 23.680 29.212 55.361 1.00 83.31 C
ANISOU 182 CG LEU A 29 8110 16008 7535 -295 -667 -1688 C
ATOM 183 CD1 LEU A 29 24.580 28.556 54.339 1.00 83.51 C
ANISOU 183 CD1 LEU A 29 8067 15997 7666 -338 -617 -1613 C
ATOM 184 CD2 LEU A 29 23.144 30.470 54.745 1.00 84.33 C
ANISOU 184 CD2 LEU A 29 8352 15932 7758 -447 -646 -1798 C
ATOM 185 N THR A 30 21.951 26.910 58.672 1.00 73.25 N
ANISOU 185 N THR A 30 6832 15211 5787 239 -735 -1372 N
ATOM 186 CA THR A 30 20.958 26.610 59.699 1.00 73.01 C
ANISOU 186 CA THR A 30 6846 15293 5603 371 -740 -1291 C
ATOM 187 C THR A 30 20.190 27.899 59.933 1.00 76.69 C
ANISOU 187 C THR A 30 7386 15707 6047 310 -752 -1450 C
ATOM 188 O THR A 30 20.756 28.919 60.345 1.00 77.19 O
ANISOU 188 O THR A 30 7400 15842 6087 253 -830 -1656 O
ATOM 189 CB THR A 30 21.572 25.997 60.966 1.00 82.61 C
ANISOU 189 CB THR A 30 7945 16794 6647 517 -820 -1260 C
ATOM 190 OG1 THR A 30 22.314 24.842 60.591 1.00 82.90 O
ANISOU 190 OG1 THR A 30 7926 16844 6728 571 -810 -1118 O
ATOM 191 CG2 THR A 30 20.504 25.572 61.979 1.00 82.05 C
ANISOU 191 CG2 THR A 30 7920 16847 6409 654 -812 -1142 C
ATOM 192 N ILE A 31 18.908 27.862 59.602 1.00 72.41 N
ANISOU 192 N ILE A 31 6963 15026 5522 317 -677 -1361 N
ATOM 193 CA ILE A 31 18.063 29.037 59.734 1.00 72.39 C
ANISOU 193 CA ILE A 31 7043 14957 5506 276 -682 -1502 C
ATOM 194 C ILE A 31 17.129 28.884 60.920 1.00 78.11 C
ANISOU 194 C ILE A 31 7774 15863 6041 420 -693 -1461 C
ATOM 195 O ILE A 31 16.490 27.848 61.102 1.00 77.37 O
ANISOU 195 O ILE A 31 7693 15818 5888 513 -640 -1257 O
ATOM 196 CB ILE A 31 17.273 29.327 58.427 1.00 73.28 C
ANISOU 196 CB ILE A 31 7284 14782 5779 172 -594 -1464 C
ATOM 197 CG1 ILE A 31 18.182 29.285 57.151 1.00 71.57 C
ANISOU 197 CG1 ILE A 31 7056 14395 5741 37 -567 -1466 C
ATOM 198 CG2 ILE A 31 16.461 30.642 58.525 1.00 74.57 C
ANISOU 198 CG2 ILE A 31 7536 14862 5934 134 -610 -1628 C
ATOM 199 CD1 ILE A 31 19.289 30.317 57.056 1.00 67.31 C
ANISOU 199 CD1 ILE A 31 6457 13859 5259 -85 -637 -1671 C
ATOM 200 N GLU A 32 17.064 29.933 61.716 1.00 77.03 N
ANISOU 200 N GLU A 32 7629 15829 5811 436 -764 -1658 N
ATOM 201 CA GLU A 32 16.137 30.072 62.819 1.00 78.83 C
ANISOU 201 CA GLU A 32 7867 16232 5853 566 -777 -1667 C
ATOM 202 C GLU A 32 15.057 31.031 62.321 1.00 84.89 C
ANISOU 202 C GLU A 32 8756 16818 6681 519 -738 -1756 C
ATOM 203 O GLU A 32 15.368 32.215 62.154 1.00 85.07 O
ANISOU 203 O GLU A 32 8810 16746 6765 435 -795 -1971 O
ATOM 204 CB GLU A 32 16.870 30.593 64.055 1.00 82.03 C
ANISOU 204 CB GLU A 32 8178 16885 6106 630 -894 -1846 C
ATOM 205 CG GLU A 32 15.961 31.059 65.176 1.00 91.38 C
ANISOU 205 CG GLU A 32 9378 18248 7096 757 -919 -1921 C
ATOM 206 CD GLU A 32 16.719 31.539 66.393 1.00112.11 C
ANISOU 206 CD GLU A 32 11909 21127 9561 826 -1041 -2105 C
ATOM 207 OE1 GLU A 32 17.409 30.709 67.029 1.00105.27 O
ANISOU 207 OE1 GLU A 32 10940 20472 8586 908 -1075 -2012 O
ATOM 208 OE2 GLU A 32 16.655 32.754 66.690 1.00107.09 O
ANISOU 208 OE2 GLU A 32 11306 20473 8912 800 -1111 -2347 O
ATOM 209 N PRO A 33 13.814 30.570 62.016 1.00 83.53 N
ANISOU 209 N PRO A 33 8654 16579 6504 562 -647 -1596 N
ATOM 210 CA PRO A 33 12.794 31.511 61.490 1.00 84.23 C
ANISOU 210 CA PRO A 33 8855 16494 6653 524 -614 -1687 C
ATOM 211 C PRO A 33 12.509 32.638 62.477 1.00 93.90 C
ANISOU 211 C PRO A 33 10084 17851 7742 598 -691 -1908 C
ATOM 212 O PRO A 33 12.754 32.474 63.675 1.00 95.07 O
ANISOU 212 O PRO A 33 10149 18263 7710 710 -744 -1936 O
ATOM 213 CB PRO A 33 11.557 30.633 61.235 1.00 84.51 C
ANISOU 213 CB PRO A 33 8931 16507 6672 579 -511 -1461 C
ATOM 214 CG PRO A 33 12.043 29.233 61.260 1.00 88.36 C
ANISOU 214 CG PRO A 33 9352 17075 7148 605 -484 -1244 C
ATOM 215 CD PRO A 33 13.272 29.204 62.142 1.00 84.94 C
ANISOU 215 CD PRO A 33 8814 16837 6624 643 -575 -1331 C
ATOM 216 N LEU A 34 12.063 33.800 61.974 1.00 94.57 N
ANISOU 216 N LEU A 34 10268 17753 7913 539 -705 -2074 N
ATOM 217 CA LEU A 34 11.857 34.969 62.818 1.00 99.05 C
ANISOU 217 CA LEU A 34 10855 18407 8372 604 -791 -2316 C
ATOM 218 C LEU A 34 10.722 34.800 63.835 1.00109.99 C
ANISOU 218 C LEU A 34 12223 20020 9548 784 -769 -2283 C
ATOM 219 O LEU A 34 9.609 34.388 63.492 1.00109.02 O
ANISOU 219 O LEU A 34 12141 19859 9423 825 -679 -2138 O
ATOM 220 CB LEU A 34 11.640 36.249 61.998 1.00 98.93 C
ANISOU 220 CB LEU A 34 10964 18117 8506 502 -816 -2492 C
ATOM 221 CG LEU A 34 12.233 37.517 62.645 1.00105.05 C
ANISOU 221 CG LEU A 34 11748 18914 9251 486 -947 -2783 C
ATOM 222 CD1 LEU A 34 13.680 37.731 62.227 1.00104.83 C
ANISOU 222 CD1 LEU A 34 11680 18790 9360 319 -1003 -2850 C
ATOM 223 CD2 LEU A 34 11.419 38.737 62.294 1.00107.88 C
ANISOU 223 CD2 LEU A 34 12244 19081 9664 485 -969 -2948 C
ATOM 224 N ASN A 35 11.056 35.131 65.097 1.00113.45 N
ANISOU 224 N ASN A 35 12592 20709 9805 888 -856 -2423 N
ATOM 225 CA ASN A 35 10.220 35.136 66.306 1.00116.99 C
ANISOU 225 CA ASN A 35 13002 21435 10015 1071 -862 -2446 C
ATOM 226 C ASN A 35 9.439 33.796 66.490 1.00125.62 C
ANISOU 226 C ASN A 35 14038 22688 11002 1156 -755 -2150 C
ATOM 227 O ASN A 35 8.224 33.799 66.754 1.00125.88 O
ANISOU 227 O ASN A 35 14078 22842 10910 1268 -704 -2109 O
ATOM 228 CB ASN A 35 9.271 36.365 66.309 1.00116.35 C
ANISOU 228 CB ASN A 35 13021 21269 9920 1125 -879 -2637 C
ATOM 229 CG ASN A 35 9.960 37.717 66.177 1.00121.27 C
ANISOU 229 CG ASN A 35 13712 21729 10635 1050 -995 -2933 C
ATOM 230 OD1 ASN A 35 11.079 37.945 66.676 1.00102.19 O
ANISOU 230 OD1 ASN A 35 11241 19390 8197 1014 -1095 -3068 O
ATOM 231 ND2 ASN A 35 9.294 38.653 65.497 1.00111.31 N
ANISOU 231 ND2 ASN A 35 12575 20236 9480 1023 -989 -3040 N
ATOM 232 N GLN A 36 10.160 32.654 66.361 1.00123.92 N
ANISOU 232 N GLN A 36 13765 22481 10837 1104 -724 -1946 N
ATOM 233 CA GLN A 36 9.579 31.321 66.547 1.00123.81 C
ANISOU 233 CA GLN A 36 13703 22601 10736 1170 -635 -1658 C
ATOM 234 C GLN A 36 9.808 30.822 68.008 1.00131.39 C
ANISOU 234 C GLN A 36 14555 23926 11441 1318 -679 -1630 C
ATOM 235 O GLN A 36 8.808 30.573 68.689 1.00132.72 O
ANISOU 235 O GLN A 36 14700 24288 11439 1433 -631 -1545 O
ATOM 236 CB GLN A 36 10.079 30.313 65.486 1.00123.03 C
ANISOU 236 CB GLN A 36 13612 22319 10816 1057 -580 -1446 C
ATOM 237 CG GLN A 36 8.997 29.855 64.505 1.00125.95 C
ANISOU 237 CG GLN A 36 14055 22493 11307 1002 -470 -1271 C
ATOM 238 CD GLN A 36 8.178 30.995 63.932 1.00139.74 C
ANISOU 238 CD GLN A 36 15896 24062 13136 966 -458 -1432 C
ATOM 239 OE1 GLN A 36 7.061 31.272 64.383 1.00135.92 O
ANISOU 239 OE1 GLN A 36 15426 23664 12552 1049 -418 -1426 O
ATOM 240 NE2 GLN A 36 8.722 31.703 62.950 1.00126.38 N
ANISOU 240 NE2 GLN A 36 14268 22130 11619 847 -494 -1579 N
ATOM 241 N LYS A 37 11.059 30.733 68.544 1.00128.40 N
ANISOU 241 N LYS A 37 14106 23665 11017 1325 -771 -1707 N
ATOM 242 CA LYS A 37 12.374 30.981 67.938 1.00127.26 C
ANISOU 242 CA LYS A 37 13955 23357 11041 1199 -836 -1811 C
ATOM 243 C LYS A 37 13.220 29.708 67.942 1.00129.16 C
ANISOU 243 C LYS A 37 14121 23664 11291 1197 -830 -1603 C
ATOM 244 O LYS A 37 14.020 29.516 67.030 1.00128.07 O
ANISOU 244 O LYS A 37 13986 23343 11332 1081 -837 -1597 O
ATOM 245 CB LYS A 37 13.110 32.113 68.672 1.00131.57 C
ANISOU 245 CB LYS A 37 14470 24004 11514 1215 -967 -2115 C
ATOM 246 N GLY A 38 13.008 28.847 68.945 1.00124.60 N
ANISOU 246 N GLY A 38 13478 23344 10520 1328 -815 -1432 N
ATOM 247 CA GLY A 38 13.702 27.574 69.137 1.00123.32 C
ANISOU 247 CA GLY A 38 13250 23273 10334 1361 -815 -1219 C
ATOM 248 C GLY A 38 13.716 26.616 67.955 1.00122.39 C
ANISOU 248 C GLY A 38 13179 22905 10418 1264 -737 -1006 C
ATOM 249 O GLY A 38 14.585 25.741 67.893 1.00122.49 O
ANISOU 249 O GLY A 38 13144 22932 10464 1268 -761 -897 O
ATOM 250 N LYS A 39 12.760 26.769 67.006 1.00114.19 N
ANISOU 250 N LYS A 39 12234 21642 9511 1186 -649 -953 N
ATOM 251 CA LYS A 39 12.650 25.954 65.791 1.00110.84 C
ANISOU 251 CA LYS A 39 11867 20964 9282 1091 -573 -770 C
ATOM 252 C LYS A 39 13.749 26.345 64.783 1.00110.50 C
ANISOU 252 C LYS A 39 11834 20714 9438 968 -610 -901 C
ATOM 253 O LYS A 39 14.008 27.539 64.611 1.00111.78 O
ANISOU 253 O LYS A 39 12010 20817 9645 908 -656 -1137 O
ATOM 254 CB LYS A 39 11.255 26.122 65.157 1.00111.94 C
ANISOU 254 CB LYS A 39 12096 20949 9488 1049 -479 -704 C
ATOM 255 N THR A 40 14.435 25.350 64.169 1.00100.51 N
ANISOU 255 N THR A 40 10556 19352 8282 937 -595 -752 N
ATOM 256 CA THR A 40 15.492 25.596 63.173 1.00 96.46 C
ANISOU 256 CA THR A 40 10038 18662 7950 825 -618 -851 C
ATOM 257 C THR A 40 15.379 24.607 62.022 1.00 92.81 C
ANISOU 257 C THR A 40 9631 17981 7650 771 -542 -658 C
ATOM 258 O THR A 40 14.954 23.468 62.221 1.00 93.04 O
ANISOU 258 O THR A 40 9671 18046 7636 841 -506 -435 O
ATOM 259 CB THR A 40 16.934 25.559 63.749 1.00100.17 C
ANISOU 259 CB THR A 40 10392 19304 8365 861 -715 -941 C
ATOM 260 OG1 THR A 40 17.360 24.208 63.943 1.00 95.30 O
ANISOU 260 OG1 THR A 40 9733 18763 7715 946 -713 -729 O
ATOM 261 CG2 THR A 40 17.124 26.400 65.003 1.00101.22 C
ANISOU 261 CG2 THR A 40 10459 19684 8316 931 -804 -1126 C
ATOM 262 N PHE A 41 15.785 25.029 60.830 1.00 82.70 N
ANISOU 262 N PHE A 41 8389 16479 6554 646 -523 -743 N
ATOM 263 CA PHE A 41 15.738 24.162 59.663 1.00 79.22 C
ANISOU 263 CA PHE A 41 8003 15828 6269 595 -457 -587 C
ATOM 264 C PHE A 41 16.986 24.360 58.817 1.00 83.37 C
ANISOU 264 C PHE A 41 8490 16255 6932 509 -480 -688 C
ATOM 265 O PHE A 41 17.679 25.377 58.943 1.00 82.49 O
ANISOU 265 O PHE A 41 8330 16186 6825 450 -534 -889 O
ATOM 266 CB PHE A 41 14.456 24.400 58.845 1.00 77.91 C
ANISOU 266 CB PHE A 41 7952 15461 6191 528 -374 -543 C
ATOM 267 CG PHE A 41 14.327 25.760 58.205 1.00 77.16 C
ANISOU 267 CG PHE A 41 7907 15225 6185 418 -372 -745 C
ATOM 268 CD1 PHE A 41 13.911 26.861 58.946 1.00 79.92 C
ANISOU 268 CD1 PHE A 41 8259 15672 6435 437 -408 -906 C
ATOM 269 CD2 PHE A 41 14.589 25.935 56.852 1.00 76.96 C
ANISOU 269 CD2 PHE A 41 7935 14967 6340 301 -334 -770 C
ATOM 270 CE1 PHE A 41 13.788 28.115 58.352 1.00 80.00 C
ANISOU 270 CE1 PHE A 41 8331 15532 6535 338 -414 -1088 C
ATOM 271 CE2 PHE A 41 14.456 27.189 56.256 1.00 78.97 C
ANISOU 271 CE2 PHE A 41 8246 15083 6677 196 -333 -941 C
ATOM 272 CZ PHE A 41 14.054 28.269 57.009 1.00 77.79 C
ANISOU 272 CZ PHE A 41 8106 15014 6437 215 -375 -1096 C
ATOM 273 N LEU A 42 17.273 23.381 57.962 1.00 80.37 N
ANISOU 273 N LEU A 42 8128 15747 6662 501 -441 -549 N
ATOM 274 CA LEU A 42 18.440 23.461 57.098 1.00 80.44 C
ANISOU 274 CA LEU A 42 8091 15675 6797 427 -451 -629 C
ATOM 275 C LEU A 42 18.024 23.924 55.725 1.00 83.18 C
ANISOU 275 C LEU A 42 8532 15765 7307 298 -381 -659 C
ATOM 276 O LEU A 42 17.009 23.457 55.203 1.00 83.74 O
ANISOU 276 O LEU A 42 8700 15695 7423 297 -316 -531 O
ATOM 277 CB LEU A 42 19.184 22.106 57.011 1.00 80.99 C
ANISOU 277 CB LEU A 42 8112 15783 6879 517 -463 -480 C
ATOM 278 CG LEU A 42 19.685 21.436 58.318 1.00 86.79 C
ANISOU 278 CG LEU A 42 8756 16769 7451 665 -535 -412 C
ATOM 279 CD1 LEU A 42 20.425 20.144 58.009 1.00 87.43 C
ANISOU 279 CD1 LEU A 42 8808 16839 7574 751 -545 -269 C
ATOM 280 CD2 LEU A 42 20.601 22.347 59.118 1.00 88.73 C
ANISOU 280 CD2 LEU A 42 8884 17222 7608 663 -621 -610 C
ATOM 281 N ALA A 43 18.789 24.856 55.141 1.00 78.74 N
ANISOU 281 N ALA A 43 7941 15146 6832 183 -394 -825 N
ATOM 282 CA ALA A 43 18.552 25.362 53.783 1.00 76.71 C
ANISOU 282 CA ALA A 43 7766 14652 6727 52 -331 -861 C
ATOM 283 C ALA A 43 19.844 25.397 52.992 1.00 80.80 C
ANISOU 283 C ALA A 43 8209 15147 7345 -23 -334 -923 C
ATOM 284 O ALA A 43 20.894 25.706 53.544 1.00 82.65 O
ANISOU 284 O ALA A 43 8326 15541 7534 -24 -399 -1027 O
ATOM 285 CB ALA A 43 17.944 26.746 53.835 1.00 77.33 C
ANISOU 285 CB ALA A 43 7906 14668 6809 -35 -337 -1013 C
ATOM 286 N LEU A 44 19.769 25.106 51.699 1.00 76.59 N
ANISOU 286 N LEU A 44 7735 14427 6940 -87 -265 -866 N
ATOM 287 CA LEU A 44 20.919 25.114 50.806 1.00 75.61 C
ANISOU 287 CA LEU A 44 7541 14278 6909 -160 -253 -915 C
ATOM 288 C LEU A 44 21.485 26.517 50.676 1.00 77.60 C
ANISOU 288 C LEU A 44 7757 14529 7200 -309 -278 -1101 C
ATOM 289 O LEU A 44 20.757 27.492 50.836 1.00 77.50 O
ANISOU 289 O LEU A 44 7824 14440 7184 -373 -282 -1179 O
ATOM 290 CB LEU A 44 20.534 24.561 49.429 1.00 74.66 C
ANISOU 290 CB LEU A 44 7509 13954 6905 -189 -169 -813 C
ATOM 291 CG LEU A 44 20.143 23.084 49.378 1.00 79.04 C
ANISOU 291 CG LEU A 44 8098 14485 7449 -56 -149 -632 C
ATOM 292 CD1 LEU A 44 19.496 22.753 48.062 1.00 76.75 C
ANISOU 292 CD1 LEU A 44 7919 13974 7268 -99 -73 -555 C
ATOM 293 CD2 LEU A 44 21.351 22.164 49.638 1.00 84.62 C
ANISOU 293 CD2 LEU A 44 8683 15339 8129 44 -189 -601 C
ATOM 294 N ILE A 45 22.798 26.604 50.427 1.00 72.89 N
ANISOU 294 N ILE A 45 7035 14021 6637 -362 -299 -1172 N
ATOM 295 CA ILE A 45 23.587 27.832 50.275 1.00 72.71 C
ANISOU 295 CA ILE A 45 6951 14016 6661 -520 -329 -1342 C
ATOM 296 C ILE A 45 22.953 28.782 49.239 1.00 73.06 C
ANISOU 296 C ILE A 45 7123 13825 6811 -669 -270 -1377 C
ATOM 297 O ILE A 45 22.867 29.986 49.466 1.00 73.23 O
ANISOU 297 O ILE A 45 7175 13807 6844 -776 -306 -1508 O
ATOM 298 CB ILE A 45 25.039 27.412 49.872 1.00 76.93 C
ANISOU 298 CB ILE A 45 7329 14671 7231 -540 -332 -1357 C
ATOM 299 CG1 ILE A 45 25.792 26.841 51.089 1.00 79.48 C
ANISOU 299 CG1 ILE A 45 7509 15251 7439 -411 -418 -1371 C
ATOM 300 CG2 ILE A 45 25.839 28.549 49.191 1.00 78.17 C
ANISOU 300 CG2 ILE A 45 7433 14789 7479 -743 -326 -1489 C
ATOM 301 CD1 ILE A 45 26.939 25.900 50.738 1.00 91.04 C
ANISOU 301 CD1 ILE A 45 8841 16833 8917 -344 -411 -1319 C
ATOM 302 N ASN A 46 22.505 28.216 48.121 1.00 66.93 N
ANISOU 302 N ASN A 46 6428 12893 6110 -668 -185 -1261 N
ATOM 303 CA ASN A 46 21.940 28.903 46.977 1.00 66.27 C
ANISOU 303 CA ASN A 46 6464 12589 6126 -792 -120 -1265 C
ATOM 304 C ASN A 46 20.441 29.203 47.128 1.00 70.38 C
ANISOU 304 C ASN A 46 7140 12971 6629 -759 -107 -1233 C
ATOM 305 O ASN A 46 19.843 29.739 46.188 1.00 69.77 O
ANISOU 305 O ASN A 46 7175 12704 6628 -843 -56 -1226 O
ATOM 306 CB ASN A 46 22.179 28.036 45.731 1.00 71.49 C
ANISOU 306 CB ASN A 46 7129 13172 6860 -784 -40 -1155 C
ATOM 307 CG ASN A 46 21.896 26.564 45.962 1.00 98.51 C
ANISOU 307 CG ASN A 46 10546 16646 10237 -610 -32 -1016 C
ATOM 308 OD1 ASN A 46 22.643 25.854 46.663 1.00 99.17 O
ANISOU 308 OD1 ASN A 46 10514 16906 10260 -512 -78 -1004 O
ATOM 309 ND2 ASN A 46 20.806 26.079 45.394 1.00 83.67 N
ANISOU 309 ND2 ASN A 46 8795 14611 8386 -567 20 -908 N
ATOM 310 N GLN A 47 19.834 28.887 48.297 1.00 67.20 N
ANISOU 310 N GLN A 47 6739 12674 6119 -636 -153 -1215 N
ATOM 311 CA GLN A 47 18.410 29.114 48.552 1.00 65.77 C
ANISOU 311 CA GLN A 47 6683 12402 5904 -589 -141 -1184 C
ATOM 312 C GLN A 47 18.201 30.164 49.648 1.00 70.54 C
ANISOU 312 C GLN A 47 7286 13086 6429 -592 -215 -1327 C
ATOM 313 O GLN A 47 17.072 30.523 49.976 1.00 71.75 O
ANISOU 313 O GLN A 47 7530 13190 6541 -549 -214 -1331 O
ATOM 314 CB GLN A 47 17.735 27.791 48.917 1.00 66.74 C
ANISOU 314 CB GLN A 47 6817 12579 5964 -439 -120 -1021 C
ATOM 315 CG GLN A 47 17.753 26.781 47.765 1.00 81.53 C
ANISOU 315 CG GLN A 47 8720 14337 7922 -431 -52 -887 C
ATOM 316 CD GLN A 47 16.844 25.602 47.982 1.00102.35 C
ANISOU 316 CD GLN A 47 11403 16967 10519 -310 -30 -723 C
ATOM 317 OE1 GLN A 47 16.760 25.017 49.075 1.00 99.00 O
ANISOU 317 OE1 GLN A 47 10930 16692 9993 -203 -70 -670 O
ATOM 318 NE2 GLN A 47 16.165 25.207 46.919 1.00 98.81 N
ANISOU 318 NE2 GLN A 47 11048 16345 10150 -330 31 -635 N
ATOM 319 N VAL A 48 19.306 30.674 50.186 1.00 65.91 N
ANISOU 319 N VAL A 48 6594 12627 5823 -642 -282 -1453 N
ATOM 320 CA VAL A 48 19.341 31.697 51.222 1.00 64.80 C
ANISOU 320 CA VAL A 48 6440 12571 5611 -654 -367 -1616 C
ATOM 321 C VAL A 48 19.908 32.952 50.572 1.00 66.79 C
ANISOU 321 C VAL A 48 6716 12691 5971 -838 -384 -1755 C
ATOM 322 O VAL A 48 20.905 32.893 49.844 1.00 65.50 O
ANISOU 322 O VAL A 48 6484 12513 5890 -942 -362 -1752 O
ATOM 323 CB VAL A 48 20.114 31.240 52.477 1.00 67.93 C
ANISOU 323 CB VAL A 48 6694 13231 5885 -558 -444 -1650 C
ATOM 324 CG1 VAL A 48 20.043 32.287 53.594 1.00 68.40 C
ANISOU 324 CG1 VAL A 48 6749 13384 5857 -554 -537 -1827 C
ATOM 325 CG2 VAL A 48 19.577 29.900 52.967 1.00 66.67 C
ANISOU 325 CG2 VAL A 48 6522 13175 5634 -388 -416 -1477 C
ATOM 326 N PHE A 49 19.197 34.068 50.768 1.00 61.60 N
ANISOU 326 N PHE A 49 6165 11924 5315 -875 -416 -1866 N
ATOM 327 CA PHE A 49 19.475 35.331 50.119 1.00 60.06 C
ANISOU 327 CA PHE A 49 6034 11556 5229 -1048 -432 -1984 C
ATOM 328 C PHE A 49 19.508 36.451 51.096 1.00 65.93 C
ANISOU 328 C PHE A 49 6791 12335 5925 -1069 -537 -2176 C
ATOM 329 O PHE A 49 18.778 36.401 52.088 1.00 68.55 O
ANISOU 329 O PHE A 49 7143 12763 6139 -930 -576 -2209 O
ATOM 330 CB PHE A 49 18.377 35.601 49.074 1.00 59.37 C
ANISOU 330 CB PHE A 49 6111 11227 5219 -1073 -358 -1910 C
ATOM 331 CG PHE A 49 18.326 34.590 47.952 1.00 58.37 C
ANISOU 331 CG PHE A 49 5987 11038 5153 -1068 -257 -1734 C
ATOM 332 CD1 PHE A 49 19.132 34.731 46.830 1.00 59.39 C
ANISOU 332 CD1 PHE A 49 6097 11078 5391 -1211 -212 -1712 C
ATOM 333 CD2 PHE A 49 17.482 33.488 48.025 1.00 57.48 C
ANISOU 333 CD2 PHE A 49 5894 10963 4984 -923 -209 -1591 C
ATOM 334 CE1 PHE A 49 19.100 33.784 45.806 1.00 58.13 C
ANISOU 334 CE1 PHE A 49 5939 10872 5278 -1193 -123 -1562 C
ATOM 335 CE2 PHE A 49 17.456 32.540 47.004 1.00 57.59 C
ANISOU 335 CE2 PHE A 49 5915 10913 5055 -916 -126 -1441 C
ATOM 336 CZ PHE A 49 18.257 32.699 45.897 1.00 55.28 C
ANISOU 336 CZ PHE A 49 5606 10534 4865 -1044 -85 -1434 C
ATOM 337 N PRO A 50 20.322 37.502 50.857 1.00 62.41 N
ANISOU 337 N PRO A 50 6337 11814 5564 -1241 -589 -2311 N
ATOM 338 CA PRO A 50 20.284 38.655 51.780 1.00 62.29 C
ANISOU 338 CA PRO A 50 6354 11802 5510 -1263 -701 -2513 C
ATOM 339 C PRO A 50 18.957 39.400 51.616 1.00 65.91 C
ANISOU 339 C PRO A 50 7001 12062 5981 -1222 -695 -2544 C
ATOM 340 O PRO A 50 18.385 39.414 50.529 1.00 65.30 O
ANISOU 340 O PRO A 50 7028 11794 5990 -1261 -614 -2440 O
ATOM 341 CB PRO A 50 21.487 39.504 51.360 1.00 65.02 C
ANISOU 341 CB PRO A 50 6649 12087 5968 -1482 -747 -2620 C
ATOM 342 CG PRO A 50 21.852 39.063 49.995 1.00 68.14 C
ANISOU 342 CG PRO A 50 7034 12380 6475 -1586 -641 -2472 C
ATOM 343 CD PRO A 50 21.226 37.739 49.704 1.00 62.61 C
ANISOU 343 CD PRO A 50 6333 11732 5724 -1429 -546 -2284 C
ATOM 344 N ALA A 51 18.441 39.939 52.699 1.00 65.05 N
ANISOU 344 N ALA A 51 6926 12017 5773 -1124 -778 -2681 N
ATOM 345 CA ALA A 51 17.171 40.663 52.759 1.00 64.72 C
ANISOU 345 CA ALA A 51 7047 11828 5716 -1049 -787 -2736 C
ATOM 346 C ALA A 51 17.409 42.126 52.941 1.00 71.94 C
ANISOU 346 C ALA A 51 8046 12599 6690 -1159 -891 -2946 C
ATOM 347 O ALA A 51 18.401 42.511 53.570 1.00 75.10 O
ANISOU 347 O ALA A 51 8358 13094 7082 -1237 -982 -3083 O
ATOM 348 CB ALA A 51 16.337 40.142 53.926 1.00 64.80 C
ANISOU 348 CB ALA A 51 7031 12042 5550 -831 -803 -2736 C
ATOM 349 N GLU A 52 16.473 42.945 52.456 1.00 67.40 N
ANISOU 349 N GLU A 52 7643 11797 6168 -1155 -888 -2980 N
ATOM 350 CA GLU A 52 16.498 44.392 52.651 1.00 69.24 C
ANISOU 350 CA GLU A 52 7991 11858 6457 -1234 -995 -3184 C
ATOM 351 C GLU A 52 16.409 44.712 54.117 1.00 77.12 C
ANISOU 351 C GLU A 52 8951 13038 7313 -1105 -1107 -3371 C
ATOM 352 O GLU A 52 15.697 44.031 54.861 1.00 77.22 O
ANISOU 352 O GLU A 52 8922 13241 7176 -907 -1085 -3332 O
ATOM 353 CB GLU A 52 15.339 45.069 51.915 1.00 69.83 C
ANISOU 353 CB GLU A 52 8263 11674 6596 -1206 -966 -3167 C
ATOM 354 CG GLU A 52 15.445 44.949 50.407 1.00 74.72 C
ANISOU 354 CG GLU A 52 8939 12089 7361 -1351 -869 -3005 C
ATOM 355 CD GLU A 52 16.674 45.635 49.855 1.00 86.14 C
ANISOU 355 CD GLU A 52 10372 13414 8943 -1596 -907 -3058 C
ATOM 356 OE1 GLU A 52 16.762 46.879 49.967 1.00 77.09 O
ANISOU 356 OE1 GLU A 52 9336 12093 7862 -1685 -1004 -3216 O
ATOM 357 OE2 GLU A 52 17.582 44.918 49.381 1.00 79.95 O
ANISOU 357 OE2 GLU A 52 9459 12725 8195 -1697 -848 -2948 O
ATOM 358 N GLU A 53 17.147 45.739 54.535 1.00 77.04 N
ANISOU 358 N GLU A 53 8950 12976 7347 -1222 -1228 -3570 N
ATOM 359 CA GLU A 53 17.205 46.253 55.902 1.00 79.51 C
ANISOU 359 CA GLU A 53 9237 13437 7538 -1125 -1358 -3789 C
ATOM 360 C GLU A 53 15.788 46.687 56.347 1.00 83.48 C
ANISOU 360 C GLU A 53 9878 13894 7949 -923 -1373 -3860 C
ATOM 361 O GLU A 53 15.284 46.198 57.360 1.00 84.06 O
ANISOU 361 O GLU A 53 9886 14205 7846 -725 -1377 -3876 O
ATOM 362 CB GLU A 53 18.255 47.404 56.006 1.00 83.44 C
ANISOU 362 CB GLU A 53 9750 13812 8141 -1328 -1489 -3992 C
ATOM 363 CG GLU A 53 18.160 48.565 54.996 1.00 97.74 C
ANISOU 363 CG GLU A 53 11743 15257 10137 -1501 -1509 -4033 C
ATOM 364 CD GLU A 53 17.819 48.288 53.532 1.00111.33 C
ANISOU 364 CD GLU A 53 13541 16776 11982 -1584 -1374 -3815 C
ATOM 365 OE1 GLU A 53 18.722 47.885 52.759 1.00 96.94 O
ANISOU 365 OE1 GLU A 53 11629 14950 10254 -1755 -1312 -3692 O
ATOM 366 OE2 GLU A 53 16.632 48.464 53.166 1.00 91.09 O
ANISOU 366 OE2 GLU A 53 11124 14073 9414 -1467 -1332 -3770 O
ATOM 367 N ASP A 54 15.126 47.522 55.535 1.00 79.12 N
ANISOU 367 N ASP A 54 9505 13046 7509 -968 -1368 -3877 N
ATOM 368 CA ASP A 54 13.774 48.014 55.763 1.00 78.77 C
ANISOU 368 CA ASP A 54 9601 12926 7401 -786 -1378 -3940 C
ATOM 369 C ASP A 54 12.801 47.096 55.004 1.00 79.47 C
ANISOU 369 C ASP A 54 9702 13015 7479 -694 -1229 -3701 C
ATOM 370 O ASP A 54 12.760 47.116 53.769 1.00 77.10 O
ANISOU 370 O ASP A 54 9473 12502 7317 -814 -1157 -3569 O
ATOM 371 CB ASP A 54 13.692 49.485 55.298 1.00 82.25 C
ANISOU 371 CB ASP A 54 10237 13034 7980 -890 -1469 -4099 C
ATOM 372 CG ASP A 54 12.386 50.231 55.519 1.00 89.32 C
ANISOU 372 CG ASP A 54 11295 13818 8824 -704 -1507 -4207 C
ATOM 373 OD1 ASP A 54 11.315 49.578 55.518 1.00 87.90 O
ANISOU 373 OD1 ASP A 54 11104 13752 8542 -521 -1418 -4091 O
ATOM 374 OD2 ASP A 54 12.422 51.480 55.569 1.00 94.05 O
ANISOU 374 OD2 ASP A 54 12042 14194 9500 -753 -1621 -4395 O
ATOM 375 N SER A 55 12.063 46.251 55.758 1.00 75.61 N
ANISOU 375 N SER A 55 9133 12776 6818 -487 -1183 -3640 N
ATOM 376 CA SER A 55 11.094 45.284 55.224 1.00 73.05 C
ANISOU 376 CA SER A 55 8800 12494 6461 -386 -1051 -3420 C
ATOM 377 C SER A 55 9.723 45.928 54.988 1.00 76.91 C
ANISOU 377 C SER A 55 9441 12842 6941 -258 -1045 -3458 C
ATOM 378 O SER A 55 8.856 45.319 54.359 1.00 73.78 O
ANISOU 378 O SER A 55 9060 12428 6546 -196 -942 -3287 O
ATOM 379 CB SER A 55 10.953 44.093 56.161 1.00 75.39 C
ANISOU 379 CB SER A 55 8937 13127 6581 -239 -1009 -3327 C
ATOM 380 OG SER A 55 10.640 44.528 57.471 1.00 86.41 O
ANISOU 380 OG SER A 55 10316 14700 7815 -81 -1096 -3507 O
ATOM 381 N LYS A 56 9.527 47.158 55.487 1.00 76.85 N
ANISOU 381 N LYS A 56 9541 12734 6923 -212 -1159 -3688 N
ATOM 382 CA LYS A 56 8.268 47.884 55.290 1.00 76.96 C
ANISOU 382 CA LYS A 56 9705 12607 6930 -77 -1168 -3748 C
ATOM 383 C LYS A 56 8.240 48.604 53.921 1.00 79.40 C
ANISOU 383 C LYS A 56 10180 12553 7438 -226 -1159 -3710 C
ATOM 384 O LYS A 56 7.202 48.592 53.256 1.00 78.72 O
ANISOU 384 O LYS A 56 10178 12361 7370 -147 -1098 -3620 O
ATOM 385 CB LYS A 56 8.022 48.884 56.434 1.00 81.23 C
ANISOU 385 CB LYS A 56 10299 13203 7363 66 -1299 -4019 C
ATOM 386 CG LYS A 56 7.447 48.248 57.698 1.00103.44 C
ANISOU 386 CG LYS A 56 12983 16376 9945 287 -1286 -4039 C
ATOM 387 CD LYS A 56 5.962 47.866 57.539 1.00115.39 C
ANISOU 387 CD LYS A 56 14519 17954 11369 482 -1201 -3944 C
ATOM 388 CE LYS A 56 5.395 47.172 58.756 1.00127.99 C
ANISOU 388 CE LYS A 56 15970 19925 12734 680 -1169 -3922 C
ATOM 389 NZ LYS A 56 5.172 48.115 59.884 1.00137.32 N
ANISOU 389 NZ LYS A 56 17178 21222 13775 844 -1287 -4189 N
ATOM 390 N LYS A 57 9.375 49.214 53.509 1.00 75.29 N
ANISOU 390 N LYS A 57 9697 11852 7058 -442 -1220 -3773 N
ATOM 391 CA LYS A 57 9.510 49.988 52.273 1.00 75.18 C
ANISOU 391 CA LYS A 57 9840 11495 7231 -606 -1223 -3743 C
ATOM 392 C LYS A 57 9.387 49.150 50.987 1.00 77.02 C
ANISOU 392 C LYS A 57 10057 11663 7545 -690 -1082 -3481 C
ATOM 393 O LYS A 57 9.431 47.914 50.989 1.00 76.07 O
ANISOU 393 O LYS A 57 9792 11749 7361 -661 -985 -3321 O
ATOM 394 CB LYS A 57 10.851 50.749 52.258 1.00 79.44 C
ANISOU 394 CB LYS A 57 10393 11901 7888 -833 -1319 -3863 C
ATOM 395 CG LYS A 57 12.089 49.884 51.986 1.00 96.48 C
ANISOU 395 CG LYS A 57 12384 14186 10089 -1013 -1259 -3733 C
ATOM 396 CD LYS A 57 12.776 50.239 50.667 1.00107.85 C
ANISOU 396 CD LYS A 57 13890 15369 11717 -1261 -1223 -3629 C
ATOM 397 CE LYS A 57 14.228 49.804 50.621 1.00122.42 C
ANISOU 397 CE LYS A 57 15577 17325 13612 -1459 -1214 -3590 C
ATOM 398 NZ LYS A 57 14.383 48.330 50.462 1.00128.40 N
ANISOU 398 NZ LYS A 57 16163 18322 14300 -1412 -1092 -3395 N
ATOM 399 N ASP A 58 9.251 49.863 49.880 1.00 72.53 N
ANISOU 399 N ASP A 58 9645 10796 7119 -795 -1077 -3445 N
ATOM 400 CA ASP A 58 9.212 49.300 48.551 1.00 69.93 C
ANISOU 400 CA ASP A 58 9328 10360 6882 -895 -961 -3223 C
ATOM 401 C ASP A 58 9.878 50.277 47.591 1.00 69.69 C
ANISOU 401 C ASP A 58 9431 10022 7024 -1112 -998 -3236 C
ATOM 402 O ASP A 58 9.914 51.486 47.835 1.00 70.17 O
ANISOU 402 O ASP A 58 9627 9898 7136 -1137 -1112 -3406 O
ATOM 403 CB ASP A 58 7.774 48.927 48.107 1.00 71.60 C
ANISOU 403 CB ASP A 58 9596 10565 7043 -718 -885 -3111 C
ATOM 404 CG ASP A 58 6.826 50.098 47.868 1.00 87.81 C
ANISOU 404 CG ASP A 58 11851 12379 9133 -630 -949 -3212 C
ATOM 405 OD1 ASP A 58 6.872 50.691 46.756 1.00 88.11 O
ANISOU 405 OD1 ASP A 58 12026 12148 9306 -754 -943 -3153 O
ATOM 406 OD2 ASP A 58 5.982 50.366 48.750 1.00 96.43 O
ANISOU 406 OD2 ASP A 58 12962 13563 10113 -426 -998 -3335 O
ATOM 407 N VAL A 59 10.420 49.745 46.516 1.00 62.51 N
ANISOU 407 N VAL A 59 8487 9063 6202 -1267 -904 -3055 N
ATOM 408 CA VAL A 59 11.058 50.536 45.474 1.00 62.28 C
ANISOU 408 CA VAL A 59 8569 8763 6330 -1487 -915 -3023 C
ATOM 409 C VAL A 59 10.259 50.317 44.194 1.00 63.42 C
ANISOU 409 C VAL A 59 8812 8766 6519 -1463 -817 -2842 C
ATOM 410 O VAL A 59 9.780 49.202 43.941 1.00 60.73 O
ANISOU 410 O VAL A 59 8381 8580 6112 -1366 -716 -2699 O
ATOM 411 CB VAL A 59 12.586 50.248 45.323 1.00 65.95 C
ANISOU 411 CB VAL A 59 8896 9303 6859 -1716 -899 -2988 C
ATOM 412 CG1 VAL A 59 13.355 50.744 46.542 1.00 66.93 C
ANISOU 412 CG1 VAL A 59 8955 9518 6956 -1754 -1023 -3196 C
ATOM 413 CG2 VAL A 59 12.880 48.763 45.070 1.00 63.73 C
ANISOU 413 CG2 VAL A 59 8430 9264 6520 -1697 -776 -2813 C
ATOM 414 N GLU A 60 10.075 51.386 43.406 1.00 60.21 N
ANISOU 414 N GLU A 60 8596 8060 6222 -1545 -855 -2850 N
ATOM 415 CA GLU A 60 9.321 51.335 42.139 1.00 57.19 C
ANISOU 415 CA GLU A 60 8326 7520 5883 -1526 -776 -2687 C
ATOM 416 C GLU A 60 10.046 50.494 41.111 1.00 61.78 C
ANISOU 416 C GLU A 60 8809 8153 6510 -1682 -656 -2489 C
ATOM 417 O GLU A 60 9.425 49.867 40.220 1.00 59.72 O
ANISOU 417 O GLU A 60 8562 7892 6239 -1627 -561 -2330 O
ATOM 418 CB GLU A 60 9.073 52.751 41.606 1.00 59.39 C
ANISOU 418 CB GLU A 60 8837 7460 6267 -1585 -857 -2747 C
ATOM 419 CG GLU A 60 8.012 53.500 42.406 1.00 65.01 C
ANISOU 419 CG GLU A 60 9670 8109 6923 -1371 -962 -2923 C
ATOM 420 CD GLU A 60 7.510 54.841 41.898 1.00 83.56 C
ANISOU 420 CD GLU A 60 12268 10120 9362 -1367 -1046 -2979 C
ATOM 421 OE1 GLU A 60 8.246 55.541 41.162 1.00 80.17 O
ANISOU 421 OE1 GLU A 60 11941 9458 9062 -1582 -1065 -2933 O
ATOM 422 OE2 GLU A 60 6.381 55.216 42.292 1.00 70.61 O
ANISOU 422 OE2 GLU A 60 10719 8452 7658 -1143 -1097 -3073 O
ATOM 423 N ASP A 61 11.369 50.480 41.230 1.00 60.36 N
ANISOU 423 N ASP A 61 8526 8028 6379 -1874 -665 -2507 N
ATOM 424 CA ASP A 61 12.252 49.718 40.340 1.00 60.14 C
ANISOU 424 CA ASP A 61 8385 8074 6393 -2032 -558 -2341 C
ATOM 425 C ASP A 61 13.088 48.804 41.219 1.00 66.16 C
ANISOU 425 C ASP A 61 8927 9124 7087 -2034 -548 -2375 C
ATOM 426 O ASP A 61 13.789 49.279 42.104 1.00 66.34 O
ANISOU 426 O ASP A 61 8902 9190 7116 -2102 -638 -2522 O
ATOM 427 CB ASP A 61 13.118 50.663 39.488 1.00 62.38 C
ANISOU 427 CB ASP A 61 8758 8134 6811 -2285 -573 -2312 C
ATOM 428 CG ASP A 61 13.905 50.012 38.372 1.00 76.95 C
ANISOU 428 CG ASP A 61 10511 10030 8696 -2441 -454 -2131 C
ATOM 429 OD1 ASP A 61 14.342 48.838 38.547 1.00 75.82 O
ANISOU 429 OD1 ASP A 61 10181 10136 8492 -2411 -386 -2075 O
ATOM 430 OD2 ASP A 61 14.110 50.678 37.326 1.00 86.57 O
ANISOU 430 OD2 ASP A 61 11845 11042 10005 -2593 -432 -2045 O
ATOM 431 N ASN A 62 13.007 47.498 40.971 1.00 63.01 N
ANISOU 431 N ASN A 62 8399 8916 6625 -1958 -446 -2241 N
ATOM 432 CA ASN A 62 13.716 46.475 41.728 1.00 63.06 C
ANISOU 432 CA ASN A 62 8200 9201 6559 -1933 -428 -2244 C
ATOM 433 C ASN A 62 15.247 46.629 41.670 1.00 72.43 C
ANISOU 433 C ASN A 62 9272 10438 7810 -2149 -439 -2266 C
ATOM 434 O ASN A 62 15.918 46.135 42.567 1.00 73.31 O
ANISOU 434 O ASN A 62 9225 10764 7865 -2133 -465 -2326 O
ATOM 435 CB ASN A 62 13.287 45.105 41.243 1.00 61.41 C
ANISOU 435 CB ASN A 62 7910 9129 6293 -1824 -315 -2077 C
ATOM 436 CG ASN A 62 11.885 44.786 41.684 1.00 68.71 C
ANISOU 436 CG ASN A 62 8887 10091 7129 -1602 -316 -2077 C
ATOM 437 OD1 ASN A 62 11.618 44.566 42.870 1.00 59.81 O
ANISOU 437 OD1 ASN A 62 7694 9124 5908 -1473 -365 -2167 O
ATOM 438 ND2 ASN A 62 10.961 44.732 40.742 1.00 57.45 N
ANISOU 438 ND2 ASN A 62 7569 8536 5722 -1550 -260 -1972 N
ATOM 439 N CYS A 63 15.796 47.355 40.669 1.00 72.16 N
ANISOU 439 N CYS A 63 9313 10213 7890 -2351 -424 -2221 N
ATOM 440 CA CYS A 63 17.228 47.657 40.566 1.00 74.44 C
ANISOU 440 CA CYS A 63 9498 10538 8249 -2579 -438 -2245 C
ATOM 441 C CYS A 63 17.698 48.565 41.717 1.00 77.34 C
ANISOU 441 C CYS A 63 9861 10897 8628 -2636 -578 -2452 C
ATOM 442 O CYS A 63 18.898 48.606 41.995 1.00 77.77 O
ANISOU 442 O CYS A 63 9777 11062 8710 -2788 -605 -2500 O
ATOM 443 CB CYS A 63 17.549 48.282 39.218 1.00 76.72 C
ANISOU 443 CB CYS A 63 9883 10617 8649 -2777 -386 -2135 C
ATOM 444 SG CYS A 63 17.316 47.154 37.830 1.00 79.78 S
ANISOU 444 SG CYS A 63 10233 11062 9019 -2743 -222 -1901 S
ATOM 445 N SER A 64 16.749 49.260 42.395 1.00 72.34 N
ANISOU 445 N SER A 64 9370 10149 7968 -2505 -669 -2580 N
ATOM 446 CA SER A 64 16.991 50.160 43.533 1.00 72.65 C
ANISOU 446 CA SER A 64 9433 10165 8006 -2521 -814 -2798 C
ATOM 447 C SER A 64 17.179 49.385 44.838 1.00 74.16 C
ANISOU 447 C SER A 64 9452 10658 8069 -2378 -848 -2891 C
ATOM 448 O SER A 64 17.534 49.985 45.858 1.00 74.14 O
ANISOU 448 O SER A 64 9433 10691 8047 -2387 -968 -3078 O
ATOM 449 CB SER A 64 15.846 51.155 43.690 1.00 76.48 C
ANISOU 449 CB SER A 64 10141 10418 8501 -2408 -893 -2898 C
ATOM 450 OG SER A 64 15.533 51.796 42.465 1.00 90.96 O
ANISOU 450 OG SER A 64 12148 11976 10437 -2499 -856 -2792 O
ATOM 451 N LEU A 65 16.934 48.058 44.819 1.00 67.77 N
ANISOU 451 N LEU A 65 8520 10062 7169 -2242 -748 -2761 N
ATOM 452 CA LEU A 65 17.125 47.225 46.011 1.00 66.31 C
ANISOU 452 CA LEU A 65 8169 10170 6855 -2103 -772 -2819 C
ATOM 453 C LEU A 65 18.619 47.162 46.402 1.00 71.77 C
ANISOU 453 C LEU A 65 8686 11014 7568 -2265 -814 -2882 C
ATOM 454 O LEU A 65 19.494 47.256 45.524 1.00 71.52 O
ANISOU 454 O LEU A 65 8613 10925 7637 -2465 -769 -2805 O
ATOM 455 CB LEU A 65 16.570 45.806 45.755 1.00 63.19 C
ANISOU 455 CB LEU A 65 7695 9936 6376 -1944 -653 -2643 C
ATOM 456 CG LEU A 65 15.035 45.659 45.690 1.00 65.47 C
ANISOU 456 CG LEU A 65 8110 10159 6607 -1744 -622 -2597 C
ATOM 457 CD1 LEU A 65 14.643 44.272 45.237 1.00 63.16 C
ANISOU 457 CD1 LEU A 65 7740 9997 6262 -1640 -504 -2408 C
ATOM 458 CD2 LEU A 65 14.380 45.942 47.036 1.00 68.90 C
ANISOU 458 CD2 LEU A 65 8559 10692 6928 -1570 -714 -2755 C
ATOM 459 N MET A 66 18.913 47.010 47.706 1.00 69.74 N
ANISOU 459 N MET A 66 8322 10964 7213 -2177 -899 -3019 N
ATOM 460 CA MET A 66 20.296 46.867 48.183 1.00 71.49 C
ANISOU 460 CA MET A 66 8359 11368 7437 -2305 -946 -3086 C
ATOM 461 C MET A 66 20.847 45.533 47.677 1.00 73.10 C
ANISOU 461 C MET A 66 8396 11761 7617 -2297 -828 -2905 C
ATOM 462 O MET A 66 21.987 45.445 47.222 1.00 73.29 O
ANISOU 462 O MET A 66 8305 11834 7710 -2471 -806 -2869 O
ATOM 463 CB MET A 66 20.379 46.953 49.712 1.00 75.89 C
ANISOU 463 CB MET A 66 8845 12116 7873 -2182 -1064 -3271 C
ATOM 464 CG MET A 66 21.798 47.151 50.201 1.00 83.07 C
ANISOU 464 CG MET A 66 9595 13163 8806 -2342 -1146 -3383 C
ATOM 465 SD MET A 66 22.016 46.976 51.984 1.00 90.49 S
ANISOU 465 SD MET A 66 10409 14394 9578 -2183 -1274 -3574 S
ATOM 466 CE MET A 66 23.773 47.397 52.117 1.00 89.79 C
ANISOU 466 CE MET A 66 10148 14398 9572 -2445 -1359 -3683 C
ATOM 467 N TYR A 67 19.999 44.505 47.722 1.00 67.34 N
ANISOU 467 N TYR A 67 7661 11131 6795 -2093 -753 -2787 N
ATOM 468 CA TYR A 67 20.289 43.175 47.218 1.00 65.38 C
ANISOU 468 CA TYR A 67 7289 11034 6519 -2046 -642 -2610 C
ATOM 469 C TYR A 67 19.240 42.832 46.215 1.00 68.43 C
ANISOU 469 C TYR A 67 7802 11267 6931 -1979 -540 -2456 C
ATOM 470 O TYR A 67 18.056 42.825 46.537 1.00 67.42 O
ANISOU 470 O TYR A 67 7777 11096 6743 -1822 -544 -2459 O
ATOM 471 CB TYR A 67 20.319 42.154 48.362 1.00 66.13 C
ANISOU 471 CB TYR A 67 7246 11411 6469 -1859 -663 -2616 C
ATOM 472 CG TYR A 67 21.198 42.590 49.514 1.00 66.55 C
ANISOU 472 CG TYR A 67 7187 11624 6475 -1896 -784 -2793 C
ATOM 473 CD1 TYR A 67 22.584 42.570 49.404 1.00 68.74 C
ANISOU 473 CD1 TYR A 67 7309 12008 6801 -2052 -803 -2818 C
ATOM 474 CD2 TYR A 67 20.642 43.068 50.694 1.00 67.68 C
ANISOU 474 CD2 TYR A 67 7377 11813 6524 -1779 -883 -2946 C
ATOM 475 CE1 TYR A 67 23.397 43.011 50.441 1.00 71.20 C
ANISOU 475 CE1 TYR A 67 7514 12465 7072 -2096 -922 -2990 C
ATOM 476 CE2 TYR A 67 21.446 43.488 51.752 1.00 70.45 C
ANISOU 476 CE2 TYR A 67 7628 12312 6827 -1811 -1003 -3122 C
ATOM 477 CZ TYR A 67 22.824 43.455 51.622 1.00 77.62 C
ANISOU 477 CZ TYR A 67 8382 13321 7789 -1974 -1025 -3143 C
ATOM 478 OH TYR A 67 23.631 43.866 52.651 1.00 81.36 O
ANISOU 478 OH TYR A 67 8749 13947 8217 -2013 -1149 -3321 O
ATOM 479 N LEU A 68 19.649 42.630 44.975 1.00 65.92 N
ANISOU 479 N LEU A 68 7481 10864 6702 -2103 -451 -2330 N
ATOM 480 CA LEU A 68 18.691 42.282 43.958 1.00 63.51 C
ANISOU 480 CA LEU A 68 7293 10420 6419 -2042 -356 -2185 C
ATOM 481 C LEU A 68 18.788 40.799 43.729 1.00 66.28 C
ANISOU 481 C LEU A 68 7526 10943 6716 -1937 -268 -2039 C
ATOM 482 O LEU A 68 19.787 40.322 43.204 1.00 68.23 O
ANISOU 482 O LEU A 68 7653 11275 6995 -2029 -222 -1980 O
ATOM 483 CB LEU A 68 18.908 43.099 42.683 1.00 63.82 C
ANISOU 483 CB LEU A 68 7438 10227 6583 -2230 -317 -2138 C
ATOM 484 CG LEU A 68 18.012 42.746 41.504 1.00 67.57 C
ANISOU 484 CG LEU A 68 8029 10565 7081 -2178 -218 -1983 C
ATOM 485 CD1 LEU A 68 16.526 42.942 41.831 1.00 66.89 C
ANISOU 485 CD1 LEU A 68 8090 10381 6946 -2006 -242 -2003 C
ATOM 486 CD2 LEU A 68 18.427 43.518 40.273 1.00 69.79 C
ANISOU 486 CD2 LEU A 68 8390 10652 7474 -2377 -178 -1928 C
ATOM 487 N ASN A 69 17.779 40.065 44.200 1.00 59.94 N
ANISOU 487 N ASN A 69 6746 10202 5825 -1742 -252 -1989 N
ATOM 488 CA ASN A 69 17.697 38.618 44.077 1.00 57.22 C
ANISOU 488 CA ASN A 69 6313 10003 5426 -1621 -180 -1850 C
ATOM 489 C ASN A 69 16.210 38.216 44.076 1.00 60.54 C
ANISOU 489 C ASN A 69 6842 10364 5797 -1460 -148 -1776 C
ATOM 490 O ASN A 69 15.340 39.064 44.310 1.00 59.81 O
ANISOU 490 O ASN A 69 6873 10153 5700 -1431 -188 -1848 O
ATOM 491 CB ASN A 69 18.515 37.927 45.194 1.00 53.16 C
ANISOU 491 CB ASN A 69 5624 9748 4826 -1555 -227 -1892 C
ATOM 492 CG ASN A 69 17.953 38.108 46.562 1.00 64.82 C
ANISOU 492 CG ASN A 69 7105 11327 6197 -1426 -308 -1992 C
ATOM 493 OD1 ASN A 69 16.850 37.645 46.850 1.00 58.24 O
ANISOU 493 OD1 ASN A 69 6331 10501 5298 -1277 -288 -1934 O
ATOM 494 ND2 ASN A 69 18.703 38.733 47.455 1.00 59.50 N
ANISOU 494 ND2 ASN A 69 6358 10753 5497 -1475 -402 -2142 N
ATOM 495 N GLU A 70 15.922 36.939 43.782 1.00 55.79 N
ANISOU 495 N GLU A 70 6195 9839 5161 -1359 -79 -1634 N
ATOM 496 CA GLU A 70 14.561 36.438 43.662 1.00 55.03 C
ANISOU 496 CA GLU A 70 6186 9695 5028 -1225 -41 -1544 C
ATOM 497 C GLU A 70 13.754 36.621 44.947 1.00 58.70 C
ANISOU 497 C GLU A 70 6661 10252 5389 -1092 -103 -1618 C
ATOM 498 O GLU A 70 12.550 36.854 44.844 1.00 60.37 O
ANISOU 498 O GLU A 70 6978 10376 5586 -1019 -92 -1601 O
ATOM 499 CB GLU A 70 14.535 34.963 43.199 1.00 55.08 C
ANISOU 499 CB GLU A 70 6129 9775 5021 -1152 32 -1385 C
ATOM 500 CG GLU A 70 15.237 34.006 44.149 1.00 64.76 C
ANISOU 500 CG GLU A 70 7206 11227 6173 -1076 7 -1371 C
ATOM 501 CD GLU A 70 15.712 32.721 43.511 1.00 81.10 C
ANISOU 501 CD GLU A 70 9205 13347 8264 -1052 68 -1240 C
ATOM 502 OE1 GLU A 70 16.801 32.738 42.895 1.00 92.24 O
ANISOU 502 OE1 GLU A 70 10552 14765 9731 -1151 88 -1250 O
ATOM 503 OE2 GLU A 70 15.035 31.684 43.688 1.00 62.65 O
ANISOU 503 OE2 GLU A 70 6869 11053 5883 -932 92 -1132 O
ATOM 504 N ALA A 71 14.387 36.514 46.135 1.00 53.32 N
ANISOU 504 N ALA A 71 5869 9760 4631 -1054 -166 -1697 N
ATOM 505 CA ALA A 71 13.686 36.676 47.401 1.00 52.52 C
ANISOU 505 CA ALA A 71 5766 9776 4414 -922 -224 -1771 C
ATOM 506 C ALA A 71 13.389 38.136 47.710 1.00 57.58 C
ANISOU 506 C ALA A 71 6506 10303 5067 -958 -296 -1942 C
ATOM 507 O ALA A 71 12.339 38.426 48.300 1.00 57.41 O
ANISOU 507 O ALA A 71 6546 10294 4971 -840 -320 -1985 O
ATOM 508 CB ALA A 71 14.482 36.062 48.523 1.00 53.93 C
ANISOU 508 CB ALA A 71 5795 10198 4499 -866 -269 -1796 C
ATOM 509 N THR A 72 14.288 39.062 47.316 1.00 56.40 N
ANISOU 509 N THR A 72 6376 10045 5010 -1119 -335 -2040 N
ATOM 510 CA THR A 72 14.063 40.498 47.573 1.00 58.88 C
ANISOU 510 CA THR A 72 6801 10221 5349 -1163 -416 -2209 C
ATOM 511 C THR A 72 13.049 41.049 46.562 1.00 63.55 C
ANISOU 511 C THR A 72 7562 10571 6014 -1173 -375 -2163 C
ATOM 512 O THR A 72 12.227 41.889 46.924 1.00 65.02 O
ANISOU 512 O THR A 72 7856 10672 6177 -1104 -426 -2263 O
ATOM 513 CB THR A 72 15.353 41.316 47.585 1.00 59.19 C
ANISOU 513 CB THR A 72 6803 10225 5461 -1340 -482 -2333 C
ATOM 514 OG1 THR A 72 16.089 41.035 46.398 1.00 61.28 O
ANISOU 514 OG1 THR A 72 7044 10406 5833 -1489 -411 -2224 O
ATOM 515 CG2 THR A 72 16.180 41.055 48.805 1.00 58.69 C
ANISOU 515 CG2 THR A 72 6588 10402 5309 -1308 -552 -2425 C
ATOM 516 N LEU A 73 13.097 40.568 45.324 1.00 58.73 N
ANISOU 516 N LEU A 73 6972 9861 5484 -1244 -287 -2018 N
ATOM 517 CA LEU A 73 12.136 40.936 44.287 1.00 58.81 C
ANISOU 517 CA LEU A 73 7133 9660 5554 -1243 -243 -1953 C
ATOM 518 C LEU A 73 10.719 40.488 44.708 1.00 59.95 C
ANISOU 518 C LEU A 73 7312 9862 5606 -1050 -226 -1912 C
ATOM 519 O LEU A 73 9.791 41.285 44.655 1.00 61.42 O
ANISOU 519 O LEU A 73 7621 9922 5793 -996 -254 -1970 O
ATOM 520 CB LEU A 73 12.542 40.300 42.945 1.00 58.57 C
ANISOU 520 CB LEU A 73 7094 9557 5605 -1340 -148 -1798 C
ATOM 521 CG LEU A 73 11.455 40.177 41.882 1.00 63.77 C
ANISOU 521 CG LEU A 73 7872 10062 6294 -1297 -84 -1688 C
ATOM 522 CD1 LEU A 73 11.298 41.451 41.145 1.00 65.40 C
ANISOU 522 CD1 LEU A 73 8233 10030 6587 -1397 -108 -1737 C
ATOM 523 CD2 LEU A 73 11.809 39.111 40.882 1.00 69.14 C
ANISOU 523 CD2 LEU A 73 8499 10764 7007 -1332 8 -1531 C
ATOM 524 N LEU A 74 10.577 39.222 45.139 1.00 53.41 N
ANISOU 524 N LEU A 74 6370 9225 4698 -950 -183 -1811 N
ATOM 525 CA LEU A 74 9.317 38.630 45.587 1.00 52.09 C
ANISOU 525 CA LEU A 74 6207 9147 4439 -783 -159 -1749 C
ATOM 526 C LEU A 74 8.695 39.445 46.725 1.00 54.79 C
ANISOU 526 C LEU A 74 6580 9548 4690 -673 -237 -1900 C
ATOM 527 O LEU A 74 7.503 39.718 46.683 1.00 56.13 O
ANISOU 527 O LEU A 74 6829 9669 4830 -574 -231 -1901 O
ATOM 528 CB LEU A 74 9.530 37.176 46.042 1.00 51.22 C
ANISOU 528 CB LEU A 74 5959 9244 4259 -716 -118 -1625 C
ATOM 529 CG LEU A 74 8.285 36.383 46.409 1.00 54.29 C
ANISOU 529 CG LEU A 74 6336 9732 4561 -568 -81 -1526 C
ATOM 530 CD1 LEU A 74 7.468 36.013 45.167 1.00 52.82 C
ANISOU 530 CD1 LEU A 74 6228 9396 4443 -578 -10 -1397 C
ATOM 531 CD2 LEU A 74 8.653 35.171 47.227 1.00 55.03 C
ANISOU 531 CD2 LEU A 74 6293 10047 4568 -502 -71 -1441 C
ATOM 532 N HIS A 75 9.484 39.831 47.721 1.00 50.84 N
ANISOU 532 N HIS A 75 6014 9161 4141 -685 -311 -2031 N
ATOM 533 CA HIS A 75 9.021 40.636 48.846 1.00 50.04 C
ANISOU 533 CA HIS A 75 5938 9128 3947 -580 -394 -2197 C
ATOM 534 C HIS A 75 8.574 42.017 48.374 1.00 58.16 C
ANISOU 534 C HIS A 75 7131 9916 5050 -613 -443 -2318 C
ATOM 535 O HIS A 75 7.488 42.447 48.723 1.00 58.41 O
ANISOU 535 O HIS A 75 7231 9943 5021 -480 -463 -2375 O
ATOM 536 CB HIS A 75 10.111 40.776 49.903 1.00 51.20 C
ANISOU 536 CB HIS A 75 5982 9431 4040 -608 -471 -2320 C
ATOM 537 CG HIS A 75 9.744 41.718 51.021 1.00 55.26 C
ANISOU 537 CG HIS A 75 6531 10001 4463 -510 -569 -2519 C
ATOM 538 ND1 HIS A 75 8.829 41.363 51.992 1.00 56.73 N
ANISOU 538 ND1 HIS A 75 6679 10381 4497 -323 -569 -2525 N
ATOM 539 CD2 HIS A 75 10.145 42.995 51.248 1.00 58.23 C
ANISOU 539 CD2 HIS A 75 6986 10255 4883 -576 -667 -2714 C
ATOM 540 CE1 HIS A 75 8.741 42.408 52.806 1.00 57.86 C
ANISOU 540 CE1 HIS A 75 6869 10529 4585 -268 -668 -2732 C
ATOM 541 NE2 HIS A 75 9.512 43.416 52.396 1.00 59.01 N
ANISOU 541 NE2 HIS A 75 7091 10478 4850 -416 -734 -2855 N
ATOM 542 N ASN A 76 9.420 42.711 47.605 1.00 59.16 N
ANISOU 542 N ASN A 76 7320 9853 5306 -786 -463 -2355 N
ATOM 543 CA ASN A 76 9.155 44.041 47.063 1.00 60.46 C
ANISOU 543 CA ASN A 76 7653 9759 5560 -844 -514 -2455 C
ATOM 544 C ASN A 76 7.817 44.083 46.333 1.00 61.99 C
ANISOU 544 C ASN A 76 7960 9832 5762 -745 -464 -2372 C
ATOM 545 O ASN A 76 6.970 44.910 46.682 1.00 62.17 O
ANISOU 545 O ASN A 76 8082 9788 5750 -636 -520 -2484 O
ATOM 546 CB ASN A 76 10.284 44.489 46.110 1.00 59.49 C
ANISOU 546 CB ASN A 76 7562 9461 5582 -1069 -511 -2437 C
ATOM 547 CG ASN A 76 10.224 45.962 45.812 1.00 67.74 C
ANISOU 547 CG ASN A 76 8775 10249 6714 -1145 -590 -2566 C
ATOM 548 OD1 ASN A 76 10.204 46.799 46.721 1.00 62.77 O
ANISOU 548 OD1 ASN A 76 8183 9616 6050 -1102 -694 -2749 O
ATOM 549 ND2 ASN A 76 10.104 46.302 44.546 1.00 50.28 N
ANISOU 549 ND2 ASN A 76 6678 7816 4611 -1242 -547 -2474 N
ATOM 550 N ILE A 77 7.609 43.165 45.365 1.00 57.20 N
ANISOU 550 N ILE A 77 7332 9208 5192 -773 -364 -2185 N
ATOM 551 CA ILE A 77 6.361 43.131 44.591 1.00 55.33 C
ANISOU 551 CA ILE A 77 7191 8866 4965 -688 -316 -2097 C
ATOM 552 C ILE A 77 5.163 42.704 45.496 1.00 56.86 C
ANISOU 552 C ILE A 77 7337 9244 5023 -481 -314 -2105 C
ATOM 553 O ILE A 77 4.055 43.150 45.221 1.00 56.42 O
ANISOU 553 O ILE A 77 7375 9105 4956 -382 -317 -2117 O
ATOM 554 CB ILE A 77 6.414 42.327 43.258 1.00 56.46 C
ANISOU 554 CB ILE A 77 7334 8936 5184 -771 -218 -1908 C
ATOM 555 CG1 ILE A 77 6.624 40.814 43.501 1.00 55.82 C
ANISOU 555 CG1 ILE A 77 7095 9069 5046 -743 -151 -1778 C
ATOM 556 CG2 ILE A 77 7.424 42.915 42.265 1.00 56.23 C
ANISOU 556 CG2 ILE A 77 7371 8713 5281 -965 -216 -1900 C
ATOM 557 CD1 ILE A 77 6.251 39.853 42.224 1.00 52.72 C
ANISOU 557 CD1 ILE A 77 6708 8622 4702 -764 -53 -1587 C
ATOM 558 N LYS A 78 5.397 41.924 46.589 1.00 52.76 N
ANISOU 558 N LYS A 78 6674 8977 4397 -415 -313 -2104 N
ATOM 559 CA LYS A 78 4.362 41.509 47.559 1.00 54.09 C
ANISOU 559 CA LYS A 78 6779 9352 4422 -229 -308 -2106 C
ATOM 560 C LYS A 78 3.824 42.713 48.339 1.00 59.94 C
ANISOU 560 C LYS A 78 7595 10079 5100 -116 -398 -2305 C
ATOM 561 O LYS A 78 2.621 42.903 48.421 1.00 59.74 O
ANISOU 561 O LYS A 78 7608 10076 5015 24 -391 -2314 O
ATOM 562 CB LYS A 78 4.928 40.456 48.538 1.00 56.60 C
ANISOU 562 CB LYS A 78 6932 9933 4641 -203 -293 -2054 C
ATOM 563 CG LYS A 78 4.009 40.039 49.660 1.00 57.26 C
ANISOU 563 CG LYS A 78 6937 10257 4563 -25 -291 -2056 C
ATOM 564 CD LYS A 78 4.774 39.243 50.747 1.00 73.61 C
ANISOU 564 CD LYS A 78 8860 12575 6534 -8 -300 -2036 C
ATOM 565 CE LYS A 78 5.752 40.064 51.576 1.00 82.60 C
ANISOU 565 CE LYS A 78 9985 13755 7643 -33 -398 -2230 C
ATOM 566 NZ LYS A 78 6.910 39.255 52.084 1.00 79.34 N
ANISOU 566 NZ LYS A 78 9443 13497 7204 -92 -401 -2184 N
ATOM 567 N VAL A 79 4.727 43.512 48.898 1.00 59.20 N
ANISOU 567 N VAL A 79 7520 9954 5020 -176 -484 -2469 N
ATOM 568 CA VAL A 79 4.441 44.727 49.673 1.00 60.57 C
ANISOU 568 CA VAL A 79 7774 10094 5145 -84 -588 -2688 C
ATOM 569 C VAL A 79 3.690 45.711 48.768 1.00 63.66 C
ANISOU 569 C VAL A 79 8345 10216 5627 -72 -607 -2723 C
ATOM 570 O VAL A 79 2.669 46.280 49.185 1.00 63.80 O
ANISOU 570 O VAL A 79 8422 10246 5572 95 -644 -2821 O
ATOM 571 CB VAL A 79 5.761 45.332 50.247 1.00 65.15 C
ANISOU 571 CB VAL A 79 8340 10662 5754 -198 -681 -2843 C
ATOM 572 CG1 VAL A 79 5.548 46.719 50.841 1.00 66.50 C
ANISOU 572 CG1 VAL A 79 8628 10732 5909 -129 -801 -3082 C
ATOM 573 CG2 VAL A 79 6.366 44.409 51.283 1.00 65.08 C
ANISOU 573 CG2 VAL A 79 8154 10946 5629 -168 -673 -2823 C
ATOM 574 N ARG A 80 4.166 45.863 47.510 1.00 57.37 N
ANISOU 574 N ARG A 80 7628 9189 4979 -237 -577 -2633 N
ATOM 575 CA ARG A 80 3.520 46.775 46.586 1.00 56.59 C
ANISOU 575 CA ARG A 80 7705 8828 4968 -233 -595 -2648 C
ATOM 576 C ARG A 80 2.101 46.313 46.287 1.00 58.98 C
ANISOU 576 C ARG A 80 8010 9193 5208 -71 -533 -2549 C
ATOM 577 O ARG A 80 1.171 47.113 46.390 1.00 57.38 O
ANISOU 577 O ARG A 80 7907 8917 4977 66 -581 -2646 O
ATOM 578 CB ARG A 80 4.347 46.916 45.318 1.00 56.66 C
ANISOU 578 CB ARG A 80 7784 8613 5132 -445 -565 -2551 C
ATOM 579 CG ARG A 80 5.572 47.793 45.550 1.00 55.54 C
ANISOU 579 CG ARG A 80 7682 8354 5068 -603 -651 -2685 C
ATOM 580 CD ARG A 80 6.456 47.917 44.321 1.00 53.93 C
ANISOU 580 CD ARG A 80 7528 7954 5008 -826 -614 -2582 C
ATOM 581 NE ARG A 80 5.754 48.580 43.217 1.00 55.72 N
ANISOU 581 NE ARG A 80 7929 7929 5315 -828 -605 -2528 N
ATOM 582 CZ ARG A 80 5.600 49.897 43.120 1.00 70.08 C
ANISOU 582 CZ ARG A 80 9920 9512 7196 -837 -697 -2650 C
ATOM 583 NH1 ARG A 80 6.096 50.701 44.052 1.00 59.84 N
ANISOU 583 NH1 ARG A 80 8648 8193 5897 -852 -806 -2841 N
ATOM 584 NH2 ARG A 80 4.932 50.418 42.104 1.00 55.37 N
ANISOU 584 NH2 ARG A 80 8211 7431 5396 -825 -685 -2584 N
ATOM 585 N TYR A 81 1.923 44.999 46.034 1.00 55.95 N
ANISOU 585 N TYR A 81 7503 8964 4792 -75 -433 -2367 N
ATOM 586 CA TYR A 81 0.619 44.409 45.704 1.00 55.17 C
ANISOU 586 CA TYR A 81 7384 8938 4640 53 -368 -2252 C
ATOM 587 C TYR A 81 -0.383 44.620 46.828 1.00 57.36 C
ANISOU 587 C TYR A 81 7622 9400 4773 262 -402 -2358 C
ATOM 588 O TYR A 81 -1.523 44.971 46.550 1.00 57.17 O
ANISOU 588 O TYR A 81 7659 9335 4727 385 -402 -2367 O
ATOM 589 CB TYR A 81 0.749 42.912 45.353 1.00 54.12 C
ANISOU 589 CB TYR A 81 7120 8942 4501 -4 -267 -2049 C
ATOM 590 CG TYR A 81 -0.525 42.251 44.870 1.00 54.35 C
ANISOU 590 CG TYR A 81 7128 9023 4497 92 -202 -1918 C
ATOM 591 CD1 TYR A 81 -0.967 42.423 43.561 1.00 55.57 C
ANISOU 591 CD1 TYR A 81 7386 8982 4745 51 -174 -1839 C
ATOM 592 CD2 TYR A 81 -1.214 41.347 45.674 1.00 55.32 C
ANISOU 592 CD2 TYR A 81 7118 9401 4499 205 -162 -1854 C
ATOM 593 CE1 TYR A 81 -2.078 41.741 43.076 1.00 53.57 C
ANISOU 593 CE1 TYR A 81 7104 8785 4467 124 -117 -1716 C
ATOM 594 CE2 TYR A 81 -2.351 40.679 45.205 1.00 55.21 C
ANISOU 594 CE2 TYR A 81 7073 9440 4463 270 -102 -1724 C
ATOM 595 CZ TYR A 81 -2.771 40.877 43.903 1.00 59.60 C
ANISOU 595 CZ TYR A 81 7731 9798 5117 229 -82 -1661 C
ATOM 596 OH TYR A 81 -3.871 40.223 43.407 1.00 61.49 O
ANISOU 596 OH TYR A 81 7935 10090 5338 286 -30 -1540 O
ATOM 597 N SER A 82 0.050 44.461 48.087 1.00 55.61 N
ANISOU 597 N SER A 82 7298 9385 4446 309 -435 -2447 N
ATOM 598 CA SER A 82 -0.787 44.665 49.272 1.00 55.60 C
ANISOU 598 CA SER A 82 7246 9592 4287 511 -468 -2560 C
ATOM 599 C SER A 82 -1.294 46.137 49.377 1.00 59.44 C
ANISOU 599 C SER A 82 7886 9918 4780 621 -565 -2765 C
ATOM 600 O SER A 82 -2.264 46.367 50.084 1.00 56.79 O
ANISOU 600 O SER A 82 7528 9730 4321 814 -582 -2847 O
ATOM 601 CB SER A 82 -0.032 44.267 50.540 1.00 57.80 C
ANISOU 601 CB SER A 82 7397 10108 4458 522 -492 -2620 C
ATOM 602 OG SER A 82 0.857 45.286 50.975 1.00 62.62 O
ANISOU 602 OG SER A 82 8078 10614 5100 472 -596 -2816 O
ATOM 603 N LYS A 83 -0.655 47.101 48.646 1.00 56.97 N
ANISOU 603 N LYS A 83 7729 9306 4610 498 -626 -2839 N
ATOM 604 CA LYS A 83 -0.979 48.543 48.620 1.00 58.27 C
ANISOU 604 CA LYS A 83 8069 9260 4812 575 -730 -3028 C
ATOM 605 C LYS A 83 -1.563 48.954 47.249 1.00 62.33 C
ANISOU 605 C LYS A 83 8729 9512 5444 549 -710 -2941 C
ATOM 606 O LYS A 83 -1.593 50.142 46.896 1.00 62.50 O
ANISOU 606 O LYS A 83 8924 9278 5544 552 -794 -3057 O
ATOM 607 CB LYS A 83 0.269 49.377 48.940 1.00 61.48 C
ANISOU 607 CB LYS A 83 8546 9521 5292 442 -829 -3184 C
ATOM 608 CG LYS A 83 0.777 49.195 50.364 1.00 69.48 C
ANISOU 608 CG LYS A 83 9437 10784 6180 494 -874 -3311 C
ATOM 609 CD LYS A 83 2.098 49.895 50.582 1.00 77.64 C
ANISOU 609 CD LYS A 83 10519 11681 7298 329 -967 -3444 C
ATOM 610 CE LYS A 83 2.542 49.793 52.023 1.00 82.49 C
ANISOU 610 CE LYS A 83 11018 12549 7776 400 -1025 -3589 C
ATOM 611 NZ LYS A 83 3.979 50.158 52.179 1.00 94.30 N
ANISOU 611 NZ LYS A 83 12513 13959 9357 205 -1096 -3676 N
ATOM 612 N ASP A 84 -2.067 47.945 46.508 1.00 57.03 N
ANISOU 612 N ASP A 84 7983 8908 4777 530 -604 -2735 N
ATOM 613 CA ASP A 84 -2.693 48.032 45.195 1.00 56.91 C
ANISOU 613 CA ASP A 84 8067 8707 4850 511 -565 -2615 C
ATOM 614 C ASP A 84 -1.777 48.685 44.158 1.00 60.69 C
ANISOU 614 C ASP A 84 8693 8876 5491 317 -592 -2596 C
ATOM 615 O ASP A 84 -2.239 49.419 43.280 1.00 60.56 O
ANISOU 615 O ASP A 84 8829 8634 5547 333 -617 -2591 O
ATOM 616 CB ASP A 84 -4.068 48.727 45.278 1.00 59.96 C
ANISOU 616 CB ASP A 84 8529 9079 5175 733 -604 -2701 C
ATOM 617 CG ASP A 84 -5.093 47.919 46.056 1.00 65.24 C
ANISOU 617 CG ASP A 84 9033 10069 5685 909 -551 -2669 C
ATOM 618 OD1 ASP A 84 -4.839 46.714 46.306 1.00 62.88 O
ANISOU 618 OD1 ASP A 84 8574 9976 5340 846 -472 -2537 O
ATOM 619 OD2 ASP A 84 -6.162 48.481 46.393 1.00 72.08 O
ANISOU 619 OD2 ASP A 84 9931 10983 6474 1111 -589 -2768 O
ATOM 620 N ARG A 85 -0.470 48.378 44.260 1.00 56.81 N
ANISOU 620 N ARG A 85 8145 8388 5050 134 -583 -2578 N
ATOM 621 CA ARG A 85 0.582 48.755 43.307 1.00 56.07 C
ANISOU 621 CA ARG A 85 8144 8058 5103 -85 -587 -2528 C
ATOM 622 C ARG A 85 0.921 47.471 42.608 1.00 56.51 C
ANISOU 622 C ARG A 85 8083 8210 5177 -191 -473 -2323 C
ATOM 623 O ARG A 85 1.623 46.627 43.164 1.00 56.49 O
ANISOU 623 O ARG A 85 7932 8396 5134 -244 -438 -2290 O
ATOM 624 CB ARG A 85 1.788 49.395 44.025 1.00 57.71 C
ANISOU 624 CB ARG A 85 8359 8224 5344 -201 -669 -2677 C
ATOM 625 CG ARG A 85 1.765 50.914 44.057 1.00 63.54 C
ANISOU 625 CG ARG A 85 9290 8703 6149 -194 -788 -2848 C
ATOM 626 CD ARG A 85 0.708 51.428 45.008 1.00 69.02 C
ANISOU 626 CD ARG A 85 10016 9477 6732 53 -859 -3013 C
ATOM 627 NE ARG A 85 0.978 52.792 45.454 1.00 78.42 N
ANISOU 627 NE ARG A 85 11359 10470 7968 59 -994 -3224 N
ATOM 628 CZ ARG A 85 0.072 53.574 46.029 1.00 86.29 C
ANISOU 628 CZ ARG A 85 12447 11441 8901 269 -1077 -3388 C
ATOM 629 NH1 ARG A 85 -1.167 53.140 46.211 1.00 60.14 N
ANISOU 629 NH1 ARG A 85 9077 8300 5473 486 -1031 -3358 N
ATOM 630 NH2 ARG A 85 0.399 54.797 46.428 1.00 75.64 N
ANISOU 630 NH2 ARG A 85 11244 9895 7602 265 -1209 -3587 N
ATOM 631 N ILE A 86 0.258 47.236 41.483 1.00 51.90 N
ANISOU 631 N ILE A 86 7557 7530 4635 -186 -416 -2188 N
ATOM 632 CA ILE A 86 0.347 45.986 40.745 1.00 49.92 C
ANISOU 632 CA ILE A 86 7207 7366 4394 -256 -311 -1996 C
ATOM 633 C ILE A 86 1.488 45.999 39.739 1.00 52.57 C
ANISOU 633 C ILE A 86 7582 7546 4845 -469 -280 -1913 C
ATOM 634 O ILE A 86 1.876 44.929 39.261 1.00 47.96 O
ANISOU 634 O ILE A 86 6902 7050 4272 -546 -200 -1776 O
ATOM 635 CB ILE A 86 -1.004 45.635 40.070 1.00 52.03 C
ANISOU 635 CB ILE A 86 7497 7640 4634 -132 -268 -1897 C
ATOM 636 CG1 ILE A 86 -1.411 46.665 38.954 1.00 51.63 C
ANISOU 636 CG1 ILE A 86 7640 7313 4666 -139 -300 -1894 C
ATOM 637 CG2 ILE A 86 -2.098 45.443 41.143 1.00 53.25 C
ANISOU 637 CG2 ILE A 86 7570 8005 4659 74 -283 -1963 C
ATOM 638 CD1 ILE A 86 -2.438 46.155 37.954 1.00 46.20 C
ANISOU 638 CD1 ILE A 86 6965 6619 3971 -70 -244 -1759 C
ATOM 639 N TYR A 87 2.056 47.192 39.477 1.00 50.33 N
ANISOU 639 N TYR A 87 7436 7042 4646 -565 -346 -1999 N
ATOM 640 CA TYR A 87 3.147 47.386 38.522 1.00 50.38 C
ANISOU 640 CA TYR A 87 7490 6892 4762 -778 -321 -1926 C
ATOM 641 C TYR A 87 4.460 47.757 39.217 1.00 55.70 C
ANISOU 641 C TYR A 87 8116 7578 5469 -918 -370 -2029 C
ATOM 642 O TYR A 87 4.484 48.659 40.059 1.00 55.55 O
ANISOU 642 O TYR A 87 8154 7510 5443 -880 -466 -2194 O
ATOM 643 CB TYR A 87 2.773 48.484 37.511 1.00 52.51 C
ANISOU 643 CB TYR A 87 7964 6876 5112 -805 -355 -1914 C
ATOM 644 CG TYR A 87 1.543 48.186 36.675 1.00 52.40 C
ANISOU 644 CG TYR A 87 8002 6836 5072 -680 -311 -1808 C
ATOM 645 CD1 TYR A 87 1.536 47.140 35.759 1.00 52.70 C
ANISOU 645 CD1 TYR A 87 7970 6942 5111 -728 -213 -1639 C
ATOM 646 CD2 TYR A 87 0.416 49.004 36.735 1.00 53.76 C
ANISOU 646 CD2 TYR A 87 8301 6902 5222 -518 -375 -1881 C
ATOM 647 CE1 TYR A 87 0.415 46.868 34.975 1.00 52.07 C
ANISOU 647 CE1 TYR A 87 7936 6841 5009 -621 -180 -1548 C
ATOM 648 CE2 TYR A 87 -0.710 48.747 35.949 1.00 53.64 C
ANISOU 648 CE2 TYR A 87 8326 6872 5183 -404 -340 -1786 C
ATOM 649 CZ TYR A 87 -0.696 47.688 35.053 1.00 57.03 C
ANISOU 649 CZ TYR A 87 8681 7375 5614 -464 -243 -1618 C
ATOM 650 OH TYR A 87 -1.774 47.419 34.243 1.00 53.86 O
ANISOU 650 OH TYR A 87 8313 6961 5189 -362 -214 -1527 O
ATOM 651 N THR A 88 5.558 47.061 38.853 1.00 52.52 N
ANISOU 651 N THR A 88 7606 7248 5102 -1076 -307 -1937 N
ATOM 652 CA THR A 88 6.924 47.295 39.350 1.00 53.55 C
ANISOU 652 CA THR A 88 7668 7409 5271 -1234 -342 -2012 C
ATOM 653 C THR A 88 7.914 47.041 38.230 1.00 59.15 C
ANISOU 653 C THR A 88 8355 8055 6063 -1432 -271 -1882 C
ATOM 654 O THR A 88 7.745 46.065 37.500 1.00 58.76 O
ANISOU 654 O THR A 88 8249 8080 6000 -1419 -179 -1736 O
ATOM 655 CB THR A 88 7.253 46.393 40.572 1.00 60.81 C
ANISOU 655 CB THR A 88 8401 8609 6094 -1165 -342 -2060 C
ATOM 656 OG1 THR A 88 6.142 46.318 41.455 1.00 59.98 O
ANISOU 656 OG1 THR A 88 8293 8610 5887 -956 -375 -2133 O
ATOM 657 CG2 THR A 88 8.456 46.872 41.348 1.00 57.82 C
ANISOU 657 CG2 THR A 88 7966 8263 5739 -1286 -412 -2188 C
ATOM 658 N TYR A 89 8.964 47.868 38.108 1.00 58.58 N
ANISOU 658 N TYR A 89 8319 7861 6076 -1618 -313 -1935 N
ATOM 659 CA TYR A 89 9.995 47.632 37.093 1.00 58.79 C
ANISOU 659 CA TYR A 89 8306 7857 6175 -1817 -242 -1814 C
ATOM 660 C TYR A 89 11.117 46.723 37.560 1.00 65.32 C
ANISOU 660 C TYR A 89 8927 8916 6977 -1890 -206 -1805 C
ATOM 661 O TYR A 89 11.388 46.591 38.758 1.00 66.89 O
ANISOU 661 O TYR A 89 9029 9262 7124 -1840 -262 -1922 O
ATOM 662 CB TYR A 89 10.655 48.943 36.636 1.00 61.18 C
ANISOU 662 CB TYR A 89 8737 7920 6587 -2010 -296 -1852 C
ATOM 663 CG TYR A 89 9.725 49.931 35.980 1.00 62.18 C
ANISOU 663 CG TYR A 89 9086 7781 6757 -1968 -333 -1842 C
ATOM 664 CD1 TYR A 89 9.026 49.601 34.819 1.00 61.54 C
ANISOU 664 CD1 TYR A 89 9078 7632 6674 -1922 -256 -1689 C
ATOM 665 CD2 TYR A 89 9.574 51.215 36.490 1.00 64.47 C
ANISOU 665 CD2 TYR A 89 9522 7881 7095 -1975 -452 -1987 C
ATOM 666 CE1 TYR A 89 8.161 50.508 34.213 1.00 60.67 C
ANISOU 666 CE1 TYR A 89 9172 7282 6598 -1872 -295 -1676 C
ATOM 667 CE2 TYR A 89 8.742 52.144 35.872 1.00 66.30 C
ANISOU 667 CE2 TYR A 89 9966 7855 7368 -1929 -493 -1976 C
ATOM 668 CZ TYR A 89 8.023 51.781 34.743 1.00 69.67 C
ANISOU 668 CZ TYR A 89 10457 8230 7785 -1873 -413 -1817 C
ATOM 669 OH TYR A 89 7.169 52.684 34.163 1.00 69.86 O
ANISOU 669 OH TYR A 89 10690 8010 7843 -1809 -460 -1807 O
ATOM 670 N VAL A 90 11.801 46.143 36.575 1.00 62.35 N
ANISOU 670 N VAL A 90 8487 8569 6634 -2008 -114 -1669 N
ATOM 671 CA VAL A 90 13.058 45.391 36.644 1.00 62.31 C
ANISOU 671 CA VAL A 90 8299 8747 6628 -2116 -68 -1635 C
ATOM 672 C VAL A 90 13.829 45.991 35.478 1.00 65.72 C
ANISOU 672 C VAL A 90 8783 9035 7152 -2328 -26 -1555 C
ATOM 673 O VAL A 90 13.791 45.466 34.372 1.00 62.22 O
ANISOU 673 O VAL A 90 8341 8586 6712 -2347 66 -1414 O
ATOM 674 CB VAL A 90 12.937 43.842 36.617 1.00 64.76 C
ANISOU 674 CB VAL A 90 8467 9274 6863 -1996 13 -1537 C
ATOM 675 CG1 VAL A 90 14.316 43.185 36.667 1.00 64.64 C
ANISOU 675 CG1 VAL A 90 8271 9436 6853 -2105 51 -1516 C
ATOM 676 CG2 VAL A 90 12.071 43.338 37.767 1.00 64.27 C
ANISOU 676 CG2 VAL A 90 8370 9340 6709 -1794 -28 -1602 C
ATOM 677 N ALA A 91 14.424 47.183 35.716 1.00 65.15 N
ANISOU 677 N ALA A 91 8773 8827 7153 -2484 -103 -1648 N
ATOM 678 CA ALA A 91 15.075 48.005 34.703 1.00 66.20 C
ANISOU 678 CA ALA A 91 8983 8788 7381 -2702 -82 -1580 C
ATOM 679 C ALA A 91 13.995 48.361 33.643 1.00 68.93 C
ANISOU 679 C ALA A 91 9523 8927 7742 -2643 -48 -1474 C
ATOM 680 O ALA A 91 12.997 48.994 34.009 1.00 69.14 O
ANISOU 680 O ALA A 91 9697 8807 7765 -2527 -121 -1546 O
ATOM 681 CB ALA A 91 16.297 47.298 34.104 1.00 66.87 C
ANISOU 681 CB ALA A 91 8895 9037 7475 -2849 10 -1484 C
ATOM 682 N ASN A 92 14.124 47.895 32.392 1.00 63.34 N
ANISOU 682 N ASN A 92 8807 8225 7035 -2696 58 -1313 N
ATOM 683 CA ASN A 92 13.134 48.191 31.355 1.00 62.07 C
ANISOU 683 CA ASN A 92 8821 7884 6878 -2638 88 -1210 C
ATOM 684 C ASN A 92 11.992 47.150 31.297 1.00 62.03 C
ANISOU 684 C ASN A 92 8805 7977 6788 -2403 127 -1169 C
ATOM 685 O ASN A 92 11.079 47.286 30.468 1.00 62.20 O
ANISOU 685 O ASN A 92 8960 7873 6801 -2329 148 -1090 O
ATOM 686 CB ASN A 92 13.819 48.292 29.997 1.00 63.80 C
ANISOU 686 CB ASN A 92 9049 8058 7134 -2814 179 -1056 C
ATOM 687 CG ASN A 92 14.790 49.441 29.886 1.00 90.92 C
ANISOU 687 CG ASN A 92 12529 11353 10662 -3060 142 -1070 C
ATOM 688 OD1 ASN A 92 14.512 50.591 30.272 1.00 80.15 O
ANISOU 688 OD1 ASN A 92 11318 9778 9359 -3096 43 -1152 O
ATOM 689 ND2 ASN A 92 15.955 49.145 29.336 1.00 87.13 N
ANISOU 689 ND2 ASN A 92 11919 10990 10197 -3235 220 -990 N
ATOM 690 N ILE A 93 12.049 46.112 32.148 1.00 55.22 N
ANISOU 690 N ILE A 93 7783 7336 5861 -2293 135 -1216 N
ATOM 691 CA ILE A 93 11.016 45.065 32.178 1.00 53.33 C
ANISOU 691 CA ILE A 93 7516 7202 5544 -2087 169 -1174 C
ATOM 692 C ILE A 93 9.940 45.456 33.192 1.00 56.69 C
ANISOU 692 C ILE A 93 8012 7593 5935 -1922 81 -1289 C
ATOM 693 O ILE A 93 10.277 45.987 34.250 1.00 58.21 O
ANISOU 693 O ILE A 93 8183 7800 6133 -1938 3 -1422 O
ATOM 694 CB ILE A 93 11.658 43.677 32.475 1.00 55.32 C
ANISOU 694 CB ILE A 93 7564 7708 5747 -2059 229 -1142 C
ATOM 695 CG1 ILE A 93 12.505 43.215 31.247 1.00 56.86 C
ANISOU 695 CG1 ILE A 93 7704 7937 5964 -2187 327 -1016 C
ATOM 696 CG2 ILE A 93 10.591 42.624 32.813 1.00 53.21 C
ANISOU 696 CG2 ILE A 93 7262 7552 5404 -1853 245 -1116 C
ATOM 697 CD1 ILE A 93 13.610 42.248 31.565 1.00 69.27 C
ANISOU 697 CD1 ILE A 93 9075 9731 7512 -2219 369 -1011 C
ATOM 698 N LEU A 94 8.651 45.204 32.869 1.00 51.58 N
ANISOU 698 N LEU A 94 7443 6908 5247 -1762 93 -1244 N
ATOM 699 CA LEU A 94 7.543 45.498 33.768 1.00 50.49 C
ANISOU 699 CA LEU A 94 7358 6765 5063 -1588 21 -1344 C
ATOM 700 C LEU A 94 6.923 44.234 34.339 1.00 53.33 C
ANISOU 700 C LEU A 94 7589 7339 5336 -1430 54 -1321 C
ATOM 701 O LEU A 94 6.485 43.377 33.579 1.00 52.56 O
ANISOU 701 O LEU A 94 7468 7284 5218 -1386 123 -1203 O
ATOM 702 CB LEU A 94 6.452 46.335 33.060 1.00 50.57 C
ANISOU 702 CB LEU A 94 7560 6564 5091 -1519 -6 -1323 C
ATOM 703 CG LEU A 94 5.249 46.812 33.931 1.00 54.69 C
ANISOU 703 CG LEU A 94 8148 7070 5564 -1326 -86 -1437 C
ATOM 704 CD1 LEU A 94 5.652 47.923 34.881 1.00 56.04 C
ANISOU 704 CD1 LEU A 94 8371 7158 5763 -1359 -188 -1602 C
ATOM 705 CD2 LEU A 94 4.131 47.317 33.073 1.00 57.17 C
ANISOU 705 CD2 LEU A 94 8620 7218 5884 -1235 -94 -1387 C
ATOM 706 N ILE A 95 6.832 44.154 35.676 1.00 50.52 N
ANISOU 706 N ILE A 95 7158 7111 4925 -1342 0 -1433 N
ATOM 707 CA ILE A 95 6.142 43.084 36.401 1.00 49.48 C
ANISOU 707 CA ILE A 95 6916 7180 4705 -1184 19 -1417 C
ATOM 708 C ILE A 95 4.766 43.638 36.754 1.00 52.62 C
ANISOU 708 C ILE A 95 7409 7525 5059 -1021 -31 -1477 C
ATOM 709 O ILE A 95 4.669 44.681 37.403 1.00 54.30 O
ANISOU 709 O ILE A 95 7695 7663 5273 -995 -112 -1611 O
ATOM 710 CB ILE A 95 6.905 42.529 37.643 1.00 53.51 C
ANISOU 710 CB ILE A 95 7267 7898 5165 -1181 -1 -1483 C
ATOM 711 CG1 ILE A 95 8.265 41.911 37.236 1.00 54.18 C
ANISOU 711 CG1 ILE A 95 7246 8049 5291 -1330 51 -1420 C
ATOM 712 CG2 ILE A 95 6.019 41.487 38.407 1.00 53.50 C
ANISOU 712 CG2 ILE A 95 7169 8092 5065 -1010 17 -1452 C
ATOM 713 CD1 ILE A 95 9.027 41.238 38.431 1.00 60.29 C
ANISOU 713 CD1 ILE A 95 7853 9044 6010 -1315 33 -1471 C
ATOM 714 N ALA A 96 3.720 42.952 36.288 1.00 47.64 N
ANISOU 714 N ALA A 96 6778 6933 4392 -913 14 -1383 N
ATOM 715 CA ALA A 96 2.303 43.282 36.434 1.00 47.07 C
ANISOU 715 CA ALA A 96 6775 6838 4273 -749 -16 -1411 C
ATOM 716 C ALA A 96 1.616 42.139 37.143 1.00 52.92 C
ANISOU 716 C ALA A 96 7378 7804 4923 -624 15 -1371 C
ATOM 717 O ALA A 96 1.535 41.037 36.581 1.00 52.55 O
ANISOU 717 O ALA A 96 7264 7827 4876 -638 82 -1244 O
ATOM 718 CB ALA A 96 1.684 43.514 35.054 1.00 46.40 C
ANISOU 718 CB ALA A 96 6812 6587 4232 -754 13 -1316 C
ATOM 719 N VAL A 97 1.195 42.355 38.399 1.00 50.50 N
ANISOU 719 N VAL A 97 7026 7620 4540 -509 -35 -1478 N
ATOM 720 CA VAL A 97 0.560 41.296 39.181 1.00 49.80 C
ANISOU 720 CA VAL A 97 6802 7761 4358 -397 -6 -1434 C
ATOM 721 C VAL A 97 -0.929 41.521 39.083 1.00 54.87 C
ANISOU 721 C VAL A 97 7490 8404 4953 -246 -15 -1434 C
ATOM 722 O VAL A 97 -1.394 42.632 39.338 1.00 57.74 O
ANISOU 722 O VAL A 97 7949 8684 5306 -168 -77 -1551 O
ATOM 723 CB VAL A 97 1.082 41.206 40.636 1.00 54.58 C
ANISOU 723 CB VAL A 97 7302 8546 4890 -364 -42 -1531 C
ATOM 724 CG1 VAL A 97 0.617 39.911 41.312 1.00 54.36 C
ANISOU 724 CG1 VAL A 97 7125 8756 4772 -283 3 -1441 C
ATOM 725 CG2 VAL A 97 2.599 41.317 40.686 1.00 53.88 C
ANISOU 725 CG2 VAL A 97 7190 8424 4859 -518 -54 -1564 C
ATOM 726 N ASN A 98 -1.677 40.498 38.640 1.00 48.00 N
ANISOU 726 N ASN A 98 6559 7618 4063 -207 43 -1304 N
ATOM 727 CA ASN A 98 -3.121 40.622 38.430 1.00 47.21 C
ANISOU 727 CA ASN A 98 6487 7531 3922 -73 39 -1290 C
ATOM 728 C ASN A 98 -3.854 40.960 39.736 1.00 50.70 C
ANISOU 728 C ASN A 98 6874 8135 4256 82 -1 -1396 C
ATOM 729 O ASN A 98 -3.819 40.158 40.665 1.00 49.24 O
ANISOU 729 O ASN A 98 6555 8158 3998 111 21 -1372 O
ATOM 730 CB ASN A 98 -3.696 39.342 37.782 1.00 45.95 C
ANISOU 730 CB ASN A 98 6251 7446 3761 -80 105 -1130 C
ATOM 731 CG ASN A 98 -5.162 39.394 37.435 1.00 53.62 C
ANISOU 731 CG ASN A 98 7238 8438 4697 42 103 -1104 C
ATOM 732 OD1 ASN A 98 -5.920 40.310 37.804 1.00 46.36 O
ANISOU 732 OD1 ASN A 98 6368 7512 3734 164 56 -1203 O
ATOM 733 ND2 ASN A 98 -5.615 38.386 36.738 1.00 43.33 N
ANISOU 733 ND2 ASN A 98 5887 7168 3409 17 151 -974 N
ATOM 734 N PRO A 99 -4.531 42.142 39.824 1.00 47.80 N
ANISOU 734 N PRO A 99 6610 7679 3873 192 -62 -1514 N
ATOM 735 CA PRO A 99 -5.234 42.491 41.075 1.00 47.50 C
ANISOU 735 CA PRO A 99 6517 7810 3720 357 -101 -1629 C
ATOM 736 C PRO A 99 -6.539 41.726 41.285 1.00 52.08 C
ANISOU 736 C PRO A 99 6985 8591 4213 479 -58 -1549 C
ATOM 737 O PRO A 99 -6.986 41.626 42.422 1.00 52.75 O
ANISOU 737 O PRO A 99 6971 8885 4185 593 -65 -1604 O
ATOM 738 CB PRO A 99 -5.530 43.980 40.903 1.00 50.08 C
ANISOU 738 CB PRO A 99 7008 7946 4074 434 -181 -1773 C
ATOM 739 CG PRO A 99 -5.651 44.176 39.439 1.00 52.80 C
ANISOU 739 CG PRO A 99 7471 8071 4519 362 -166 -1684 C
ATOM 740 CD PRO A 99 -4.667 43.216 38.814 1.00 48.04 C
ANISOU 740 CD PRO A 99 6815 7454 3982 178 -100 -1548 C
ATOM 741 N TYR A 100 -7.168 41.229 40.194 1.00 48.23 N
ANISOU 741 N TYR A 100 6509 8046 3770 456 -17 -1423 N
ATOM 742 CA TYR A 100 -8.437 40.493 40.215 1.00 47.66 C
ANISOU 742 CA TYR A 100 6331 8145 3632 549 21 -1335 C
ATOM 743 C TYR A 100 -9.636 41.369 40.733 1.00 55.67 C
ANISOU 743 C TYR A 100 7355 9238 4558 750 -24 -1451 C
ATOM 744 O TYR A 100 -10.644 40.834 41.207 1.00 57.63 O
ANISOU 744 O TYR A 100 7478 9703 4716 847 4 -1410 O
ATOM 745 CB TYR A 100 -8.318 39.159 40.992 1.00 46.47 C
ANISOU 745 CB TYR A 100 6007 8229 3421 512 78 -1231 C
ATOM 746 CG TYR A 100 -7.819 38.020 40.118 1.00 45.44 C
ANISOU 746 CG TYR A 100 5852 8041 3373 361 132 -1072 C
ATOM 747 CD1 TYR A 100 -8.494 37.661 38.951 1.00 45.92 C
ANISOU 747 CD1 TYR A 100 5943 8017 3488 339 154 -977 C
ATOM 748 CD2 TYR A 100 -6.737 37.237 40.510 1.00 44.93 C
ANISOU 748 CD2 TYR A 100 5722 8028 3321 257 158 -1019 C
ATOM 749 CE1 TYR A 100 -8.067 36.589 38.163 1.00 45.67 C
ANISOU 749 CE1 TYR A 100 5890 7938 3526 214 198 -843 C
ATOM 750 CE2 TYR A 100 -6.326 36.136 39.753 1.00 44.81 C
ANISOU 750 CE2 TYR A 100 5682 7970 3376 139 204 -880 C
ATOM 751 CZ TYR A 100 -6.989 35.823 38.572 1.00 51.31 C
ANISOU 751 CZ TYR A 100 6544 8696 4254 117 223 -796 C
ATOM 752 OH TYR A 100 -6.607 34.744 37.816 1.00 47.54 O
ANISOU 752 OH TYR A 100 6047 8174 3841 11 262 -672 O
ATOM 753 N PHE A 101 -9.536 42.699 40.563 1.00 51.27 N
ANISOU 753 N PHE A 101 6951 8499 4032 808 -94 -1588 N
ATOM 754 CA PHE A 101 -10.566 43.688 40.843 1.00 52.87 C
ANISOU 754 CA PHE A 101 7201 8717 4171 1003 -150 -1713 C
ATOM 755 C PHE A 101 -10.175 45.001 40.149 1.00 60.29 C
ANISOU 755 C PHE A 101 8352 9353 5200 998 -224 -1812 C
ATOM 756 O PHE A 101 -9.042 45.130 39.685 1.00 58.87 O
ANISOU 756 O PHE A 101 8258 8992 5116 836 -227 -1794 O
ATOM 757 CB PHE A 101 -10.842 43.868 42.354 1.00 55.88 C
ANISOU 757 CB PHE A 101 7480 9335 4417 1143 -169 -1833 C
ATOM 758 CG PHE A 101 -9.923 44.802 43.094 1.00 58.38 C
ANISOU 758 CG PHE A 101 7884 9564 4734 1149 -240 -2005 C
ATOM 759 CD1 PHE A 101 -8.625 44.420 43.409 1.00 58.52 C
ANISOU 759 CD1 PHE A 101 7879 9566 4788 992 -229 -1991 C
ATOM 760 CD2 PHE A 101 -10.371 46.051 43.519 1.00 62.50 C
ANISOU 760 CD2 PHE A 101 8505 10028 5215 1318 -323 -2189 C
ATOM 761 CE1 PHE A 101 -7.777 45.290 44.087 1.00 61.45 C
ANISOU 761 CE1 PHE A 101 8326 9860 5162 988 -302 -2156 C
ATOM 762 CE2 PHE A 101 -9.517 46.921 44.198 1.00 65.65 C
ANISOU 762 CE2 PHE A 101 8992 10332 5621 1315 -399 -2358 C
ATOM 763 CZ PHE A 101 -8.228 46.534 44.482 1.00 62.91 C
ANISOU 763 CZ PHE A 101 8617 9971 5313 1145 -388 -2340 C
ATOM 764 N ASP A 102 -11.118 45.957 40.049 1.00 60.33 N
ANISOU 764 N ASP A 102 8443 9304 5177 1172 -282 -1909 N
ATOM 765 CA ASP A 102 -10.849 47.220 39.382 1.00 60.94 C
ANISOU 765 CA ASP A 102 8734 9080 5341 1176 -359 -1994 C
ATOM 766 C ASP A 102 -10.254 48.228 40.339 1.00 64.43 C
ANISOU 766 C ASP A 102 9255 9457 5770 1221 -439 -2184 C
ATOM 767 O ASP A 102 -10.902 48.663 41.283 1.00 64.79 O
ANISOU 767 O ASP A 102 9263 9641 5713 1406 -480 -2318 O
ATOM 768 CB ASP A 102 -12.108 47.774 38.703 1.00 64.04 C
ANISOU 768 CB ASP A 102 9200 9411 5721 1341 -392 -2000 C
ATOM 769 CG ASP A 102 -12.545 46.894 37.555 1.00 84.11 C
ANISOU 769 CG ASP A 102 11699 11958 8300 1265 -327 -1817 C
ATOM 770 OD1 ASP A 102 -11.913 46.974 36.467 1.00 85.68 O
ANISOU 770 OD1 ASP A 102 12014 11937 8603 1120 -321 -1736 O
ATOM 771 OD2 ASP A 102 -13.445 46.049 37.767 1.00 92.82 O
ANISOU 771 OD2 ASP A 102 12640 13298 9327 1333 -279 -1750 O
ATOM 772 N ILE A 103 -9.002 48.595 40.083 1.00 60.92 N
ANISOU 772 N ILE A 103 8916 8807 5426 1048 -462 -2197 N
ATOM 773 CA ILE A 103 -8.297 49.590 40.874 1.00 61.96 C
ANISOU 773 CA ILE A 103 9140 8835 5569 1054 -549 -2378 C
ATOM 774 C ILE A 103 -8.758 50.924 40.318 1.00 68.59 C
ANISOU 774 C ILE A 103 10192 9408 6463 1154 -640 -2469 C
ATOM 775 O ILE A 103 -8.631 51.158 39.106 1.00 69.62 O
ANISOU 775 O ILE A 103 10444 9314 6694 1058 -635 -2369 O
ATOM 776 CB ILE A 103 -6.760 49.407 40.922 1.00 63.61 C
ANISOU 776 CB ILE A 103 9349 8963 5856 823 -539 -2359 C
ATOM 777 CG1 ILE A 103 -6.395 47.924 41.261 1.00 60.43 C
ANISOU 777 CG1 ILE A 103 8738 8818 5405 731 -440 -2229 C
ATOM 778 CG2 ILE A 103 -6.164 50.398 41.967 1.00 65.40 C
ANISOU 778 CG2 ILE A 103 9645 9133 6072 854 -639 -2571 C
ATOM 779 CD1 ILE A 103 -5.028 47.586 41.130 1.00 54.21 C
ANISOU 779 CD1 ILE A 103 7935 7970 4693 517 -416 -2179 C
ATOM 780 N PRO A 104 -9.443 51.718 41.172 1.00 65.55 N
ANISOU 780 N PRO A 104 9838 9070 5997 1372 -718 -2648 N
ATOM 781 CA PRO A 104 -10.045 52.969 40.705 1.00 67.08 C
ANISOU 781 CA PRO A 104 10233 9023 6231 1509 -813 -2743 C
ATOM 782 C PRO A 104 -9.105 53.947 40.020 1.00 73.97 C
ANISOU 782 C PRO A 104 11329 9526 7252 1354 -882 -2763 C
ATOM 783 O PRO A 104 -8.011 54.250 40.516 1.00 75.64 O
ANISOU 783 O PRO A 104 11571 9658 7511 1217 -917 -2840 O
ATOM 784 CB PRO A 104 -10.582 53.604 41.998 1.00 69.90 C
ANISOU 784 CB PRO A 104 10575 9510 6475 1741 -890 -2965 C
ATOM 785 CG PRO A 104 -10.818 52.464 42.905 1.00 72.83 C
ANISOU 785 CG PRO A 104 10698 10259 6713 1778 -806 -2929 C
ATOM 786 CD PRO A 104 -9.705 51.516 42.618 1.00 67.28 C
ANISOU 786 CD PRO A 104 9914 9573 6076 1514 -726 -2776 C
ATOM 787 N LYS A 105 -9.599 54.492 38.901 1.00 69.28 N
ANISOU 787 N LYS A 105 10890 8711 6723 1388 -908 -2699 N
ATOM 788 CA LYS A 105 -9.016 55.558 38.087 1.00 70.72 C
ANISOU 788 CA LYS A 105 11313 8519 7040 1281 -981 -2700 C
ATOM 789 C LYS A 105 -7.609 55.269 37.525 1.00 74.06 C
ANISOU 789 C LYS A 105 11754 8813 7574 973 -935 -2585 C
ATOM 790 O LYS A 105 -7.113 56.098 36.755 1.00 75.16 O
ANISOU 790 O LYS A 105 12085 8647 7825 863 -984 -2559 O
ATOM 791 CB LYS A 105 -8.960 56.907 38.867 1.00 76.24 C
ANISOU 791 CB LYS A 105 12178 9039 7753 1403 -1122 -2931 C
ATOM 792 CG LYS A 105 -9.983 57.133 40.004 1.00 99.68 C
ANISOU 792 CG LYS A 105 15076 12215 10583 1698 -1173 -3117 C
ATOM 793 CD LYS A 105 -11.431 57.304 39.524 1.00115.46 C
ANISOU 793 CD LYS A 105 17098 14249 12520 1946 -1184 -3098 C
ATOM 794 CE LYS A 105 -12.407 57.317 40.678 1.00128.05 C
ANISOU 794 CE LYS A 105 18571 16122 13960 2222 -1208 -3263 C
ATOM 795 NZ LYS A 105 -13.814 57.411 40.207 1.00137.09 N
ANISOU 795 NZ LYS A 105 19709 17341 15039 2461 -1210 -3240 N
ATOM 796 N ILE A 106 -6.983 54.113 37.836 1.00 67.71 N
ANISOU 796 N ILE A 106 10754 8230 6741 836 -840 -2505 N
ATOM 797 CA ILE A 106 -5.600 53.891 37.406 1.00 66.64 C
ANISOU 797 CA ILE A 106 10627 7989 6706 558 -802 -2417 C
ATOM 798 C ILE A 106 -5.472 53.679 35.878 1.00 68.71 C
ANISOU 798 C ILE A 106 10964 8095 7047 424 -742 -2218 C
ATOM 799 O ILE A 106 -4.344 53.710 35.394 1.00 68.03 O
ANISOU 799 O ILE A 106 10915 7882 7050 200 -720 -2149 O
ATOM 800 CB ILE A 106 -4.837 52.801 38.205 1.00 68.55 C
ANISOU 800 CB ILE A 106 10654 8491 6900 450 -731 -2401 C
ATOM 801 CG1 ILE A 106 -5.322 51.380 37.902 1.00 66.42 C
ANISOU 801 CG1 ILE A 106 10202 8470 6566 462 -614 -2238 C
ATOM 802 CG2 ILE A 106 -4.875 53.115 39.721 1.00 69.38 C
ANISOU 802 CG2 ILE A 106 10699 8742 6921 578 -799 -2605 C
ATOM 803 CD1 ILE A 106 -4.265 50.336 38.222 1.00 72.78 C
ANISOU 803 CD1 ILE A 106 10841 9442 7369 291 -539 -2170 C
ATOM 804 N TYR A 107 -6.598 53.563 35.123 1.00 64.37 N
ANISOU 804 N TYR A 107 10443 7550 6464 562 -723 -2135 N
ATOM 805 CA TYR A 107 -6.573 53.482 33.657 1.00 63.40 C
ANISOU 805 CA TYR A 107 10409 7274 6404 461 -679 -1958 C
ATOM 806 C TYR A 107 -7.414 54.612 33.031 1.00 69.25 C
ANISOU 806 C TYR A 107 11364 7780 7170 606 -765 -1983 C
ATOM 807 O TYR A 107 -7.650 54.591 31.831 1.00 67.98 O
ANISOU 807 O TYR A 107 11281 7511 7038 575 -737 -1842 O
ATOM 808 CB TYR A 107 -7.029 52.105 33.128 1.00 61.62 C
ANISOU 808 CB TYR A 107 10015 7276 6123 459 -568 -1803 C
ATOM 809 CG TYR A 107 -6.278 50.948 33.743 1.00 61.57 C
ANISOU 809 CG TYR A 107 9805 7497 6090 336 -488 -1773 C
ATOM 810 CD1 TYR A 107 -4.980 50.641 33.342 1.00 61.45 C
ANISOU 810 CD1 TYR A 107 9778 7423 6148 101 -440 -1695 C
ATOM 811 CD2 TYR A 107 -6.844 50.189 34.765 1.00 62.55 C
ANISOU 811 CD2 TYR A 107 9751 7901 6115 459 -465 -1824 C
ATOM 812 CE1 TYR A 107 -4.262 49.614 33.949 1.00 58.31 C
ANISOU 812 CE1 TYR A 107 9199 7230 5725 4 -376 -1675 C
ATOM 813 CE2 TYR A 107 -6.148 49.132 35.351 1.00 61.79 C
ANISOU 813 CE2 TYR A 107 9479 8005 5994 353 -398 -1790 C
ATOM 814 CZ TYR A 107 -4.860 48.848 34.937 1.00 61.78 C
ANISOU 814 CZ TYR A 107 9474 7932 6068 132 -357 -1718 C
ATOM 815 OH TYR A 107 -4.186 47.802 35.507 1.00 59.31 O
ANISOU 815 OH TYR A 107 8990 7818 5728 46 -297 -1686 O
ATOM 816 N SER A 108 -7.816 55.616 33.832 1.00 68.75 N
ANISOU 816 N SER A 108 11400 7628 7093 766 -874 -2163 N
ATOM 817 CA SER A 108 -8.615 56.772 33.396 1.00 70.94 C
ANISOU 817 CA SER A 108 11888 7674 7391 934 -973 -2213 C
ATOM 818 C SER A 108 -7.908 57.606 32.310 1.00 78.14 C
ANISOU 818 C SER A 108 13025 8238 8428 762 -1007 -2118 C
ATOM 819 O SER A 108 -6.705 57.443 32.084 1.00 77.48 O
ANISOU 819 O SER A 108 12936 8085 8418 510 -966 -2050 O
ATOM 820 CB SER A 108 -8.934 57.670 34.589 1.00 74.73 C
ANISOU 820 CB SER A 108 12429 8125 7839 1118 -1088 -2447 C
ATOM 821 OG SER A 108 -7.814 58.450 34.986 1.00 79.09 O
ANISOU 821 OG SER A 108 13098 8469 8483 964 -1157 -2543 O
ATOM 822 N SER A 109 -8.661 58.517 31.665 1.00 77.46 N
ANISOU 822 N SER A 109 13132 7939 8360 906 -1084 -2113 N
ATOM 823 CA SER A 109 -8.171 59.423 30.618 1.00 78.93 C
ANISOU 823 CA SER A 109 13558 7778 8655 779 -1128 -2016 C
ATOM 824 C SER A 109 -7.136 60.401 31.180 1.00 83.43 C
ANISOU 824 C SER A 109 14265 8108 9325 639 -1215 -2132 C
ATOM 825 O SER A 109 -6.142 60.696 30.506 1.00 83.11 O
ANISOU 825 O SER A 109 14323 7872 9383 394 -1200 -2024 O
ATOM 826 CB SER A 109 -9.333 60.182 29.986 1.00 84.94 C
ANISOU 826 CB SER A 109 14489 8387 9397 1011 -1207 -2010 C
ATOM 827 OG SER A 109 -10.104 59.293 29.193 1.00 97.08 O
ANISOU 827 OG SER A 109 15912 10114 10860 1082 -1122 -1868 O
ATOM 828 N GLU A 110 -7.364 60.873 32.429 1.00 80.46 N
ANISOU 828 N GLU A 110 13885 7767 8919 790 -1304 -2354 N
ATOM 829 CA GLU A 110 -6.456 61.744 33.177 1.00 81.56 C
ANISOU 829 CA GLU A 110 14130 7716 9141 680 -1400 -2504 C
ATOM 830 C GLU A 110 -5.118 61.023 33.375 1.00 82.00 C
ANISOU 830 C GLU A 110 14031 7892 9233 391 -1313 -2448 C
ATOM 831 O GLU A 110 -4.070 61.615 33.123 1.00 82.62 O
ANISOU 831 O GLU A 110 14222 7745 9426 161 -1344 -2424 O
ATOM 832 CB GLU A 110 -7.082 62.133 34.530 1.00 84.30 C
ANISOU 832 CB GLU A 110 14458 8159 9415 930 -1496 -2758 C
ATOM 833 CG GLU A 110 -6.332 63.225 35.273 1.00 98.13 C
ANISOU 833 CG GLU A 110 16361 9669 11253 859 -1626 -2942 C
ATOM 834 N THR A 111 -5.168 59.725 33.765 1.00 74.76 N
ANISOU 834 N THR A 111 12856 7329 8222 399 -1202 -2413 N
ATOM 835 CA THR A 111 -4.002 58.859 33.977 1.00 72.37 C
ANISOU 835 CA THR A 111 12378 7186 7935 159 -1112 -2354 C
ATOM 836 C THR A 111 -3.232 58.731 32.664 1.00 74.73 C
ANISOU 836 C THR A 111 12733 7341 8320 -87 -1039 -2141 C
ATOM 837 O THR A 111 -2.034 59.015 32.663 1.00 75.87 O
ANISOU 837 O THR A 111 12903 7373 8552 -324 -1044 -2132 O
ATOM 838 CB THR A 111 -4.429 57.511 34.572 1.00 77.50 C
ANISOU 838 CB THR A 111 12763 8223 8460 255 -1015 -2345 C
ATOM 839 OG1 THR A 111 -5.232 57.771 35.726 1.00 74.07 O
ANISOU 839 OG1 THR A 111 12296 7908 7938 495 -1088 -2540 O
ATOM 840 CG2 THR A 111 -3.241 56.640 34.963 1.00 76.57 C
ANISOU 840 CG2 THR A 111 12466 8276 8352 37 -936 -2306 C
ATOM 841 N ILE A 112 -3.929 58.394 31.537 1.00 68.53 N
ANISOU 841 N ILE A 112 11979 6551 7510 -27 -981 -1978 N
ATOM 842 CA ILE A 112 -3.350 58.330 30.196 1.00 66.77 C
ANISOU 842 CA ILE A 112 11826 6194 7351 -226 -915 -1771 C
ATOM 843 C ILE A 112 -2.589 59.650 29.939 1.00 73.03 C
ANISOU 843 C ILE A 112 12848 6632 8269 -384 -1006 -1786 C
ATOM 844 O ILE A 112 -1.415 59.597 29.603 1.00 73.85 O
ANISOU 844 O ILE A 112 12934 6684 8443 -646 -959 -1701 O
ATOM 845 CB ILE A 112 -4.463 58.027 29.124 1.00 68.63 C
ANISOU 845 CB ILE A 112 12098 6450 7528 -72 -878 -1637 C
ATOM 846 CG1 ILE A 112 -4.745 56.520 29.035 1.00 66.01 C
ANISOU 846 CG1 ILE A 112 11525 6451 7105 -46 -756 -1553 C
ATOM 847 CG2 ILE A 112 -4.135 58.582 27.726 1.00 69.10 C
ANISOU 847 CG2 ILE A 112 12343 6254 7657 -207 -869 -1461 C
ATOM 848 CD1 ILE A 112 -6.170 56.144 28.805 1.00 71.84 C
ANISOU 848 CD1 ILE A 112 12226 7319 7751 204 -755 -1544 C
ATOM 849 N LYS A 113 -3.225 60.810 30.174 1.00 71.26 N
ANISOU 849 N LYS A 113 12828 6174 8074 -228 -1138 -1903 N
ATOM 850 CA LYS A 113 -2.621 62.139 29.974 1.00 74.08 C
ANISOU 850 CA LYS A 113 13428 6161 8556 -361 -1243 -1926 C
ATOM 851 C LYS A 113 -1.321 62.335 30.773 1.00 79.18 C
ANISOU 851 C LYS A 113 14024 6781 9278 -590 -1269 -2026 C
ATOM 852 O LYS A 113 -0.322 62.760 30.189 1.00 80.38 O
ANISOU 852 O LYS A 113 14265 6742 9534 -850 -1264 -1926 O
ATOM 853 CB LYS A 113 -3.615 63.266 30.328 1.00 78.34 C
ANISOU 853 CB LYS A 113 14178 6485 9101 -106 -1393 -2076 C
ATOM 854 CG LYS A 113 -4.352 63.860 29.134 1.00 96.10 C
ANISOU 854 CG LYS A 113 16637 8509 11368 -12 -1422 -1938 C
ATOM 855 CD LYS A 113 -3.529 64.916 28.390 1.00111.01 C
ANISOU 855 CD LYS A 113 18767 10017 13394 -239 -1479 -1839 C
ATOM 856 CE LYS A 113 -4.033 65.110 26.977 1.00124.82 C
ANISOU 856 CE LYS A 113 20662 11622 15140 -212 -1453 -1626 C
ATOM 857 NZ LYS A 113 -3.181 66.047 26.200 1.00136.27 N
ANISOU 857 NZ LYS A 113 22330 12730 16718 -462 -1488 -1493 N
ATOM 858 N SER A 114 -1.322 61.998 32.089 1.00 74.72 N
ANISOU 858 N SER A 114 13310 6423 8658 -498 -1294 -2216 N
ATOM 859 CA SER A 114 -0.169 62.145 32.998 1.00 74.60 C
ANISOU 859 CA SER A 114 13228 6419 8697 -683 -1331 -2340 C
ATOM 860 C SER A 114 1.053 61.296 32.592 1.00 76.64 C
ANISOU 860 C SER A 114 13314 6824 8982 -970 -1206 -2192 C
ATOM 861 O SER A 114 2.175 61.628 32.977 1.00 77.66 O
ANISOU 861 O SER A 114 13430 6887 9189 -1185 -1239 -2247 O
ATOM 862 CB SER A 114 -0.564 61.815 34.437 1.00 76.41 C
ANISOU 862 CB SER A 114 13317 6884 8830 -488 -1373 -2559 C
ATOM 863 OG SER A 114 -0.794 60.432 34.641 1.00 78.69 O
ANISOU 863 OG SER A 114 13355 7541 9002 -417 -1249 -2499 O
ATOM 864 N TYR A 115 0.843 60.216 31.831 1.00 70.84 N
ANISOU 864 N TYR A 115 12445 6290 8183 -970 -1070 -2015 N
ATOM 865 CA TYR A 115 1.934 59.337 31.404 1.00 69.35 C
ANISOU 865 CA TYR A 115 12085 6259 8006 -1211 -947 -1876 C
ATOM 866 C TYR A 115 2.518 59.706 30.031 1.00 76.47 C
ANISOU 866 C TYR A 115 13107 6959 8990 -1427 -899 -1670 C
ATOM 867 O TYR A 115 3.497 59.076 29.617 1.00 75.93 O
ANISOU 867 O TYR A 115 12907 7010 8935 -1636 -798 -1554 O
ATOM 868 CB TYR A 115 1.454 57.874 31.400 1.00 66.41 C
ANISOU 868 CB TYR A 115 11488 6231 7514 -1093 -827 -1809 C
ATOM 869 CG TYR A 115 1.649 57.230 32.748 1.00 67.10 C
ANISOU 869 CG TYR A 115 11379 6578 7537 -1033 -831 -1960 C
ATOM 870 CD1 TYR A 115 2.846 56.598 33.073 1.00 67.31 C
ANISOU 870 CD1 TYR A 115 11236 6759 7579 -1229 -773 -1947 C
ATOM 871 CD2 TYR A 115 0.685 57.352 33.744 1.00 68.93 C
ANISOU 871 CD2 TYR A 115 11602 6896 7692 -781 -900 -2125 C
ATOM 872 CE1 TYR A 115 3.062 56.071 34.340 1.00 65.08 C
ANISOU 872 CE1 TYR A 115 10784 6707 7235 -1173 -786 -2085 C
ATOM 873 CE2 TYR A 115 0.893 56.832 35.019 1.00 69.50 C
ANISOU 873 CE2 TYR A 115 11503 7207 7698 -728 -908 -2263 C
ATOM 874 CZ TYR A 115 2.085 56.196 35.311 1.00 73.05 C
ANISOU 874 CZ TYR A 115 11793 7800 8164 -925 -853 -2241 C
ATOM 875 OH TYR A 115 2.263 55.641 36.547 1.00 74.57 O
ANISOU 875 OH TYR A 115 11816 8237 8280 -862 -860 -2365 O
ATOM 876 N GLN A 116 1.947 60.730 29.347 1.00 75.21 N
ANISOU 876 N GLN A 116 13195 6502 8880 -1375 -972 -1627 N
ATOM 877 CA GLN A 116 2.346 61.146 27.998 1.00 76.30 C
ANISOU 877 CA GLN A 116 13470 6439 9082 -1555 -930 -1418 C
ATOM 878 C GLN A 116 3.655 61.942 27.961 1.00 83.44 C
ANISOU 878 C GLN A 116 14450 7140 10114 -1860 -967 -1403 C
ATOM 879 O GLN A 116 3.754 63.041 28.518 1.00 85.81 O
ANISOU 879 O GLN A 116 14912 7194 10498 -1877 -1101 -1533 O
ATOM 880 CB GLN A 116 1.227 61.944 27.313 1.00 78.73 C
ANISOU 880 CB GLN A 116 14017 6509 9390 -1372 -1000 -1372 C
ATOM 881 CG GLN A 116 0.065 61.063 26.849 1.00 86.98 C
ANISOU 881 CG GLN A 116 14981 7755 10313 -1140 -929 -1299 C
ATOM 882 CD GLN A 116 -1.153 61.838 26.408 1.00104.21 C
ANISOU 882 CD GLN A 116 17376 9737 12481 -909 -1018 -1300 C
ATOM 883 OE1 GLN A 116 -1.088 63.013 26.026 1.00103.75 O
ANISOU 883 OE1 GLN A 116 17560 9353 12508 -954 -1109 -1277 O
ATOM 884 NE2 GLN A 116 -2.292 61.170 26.400 1.00 91.36 N
ANISOU 884 NE2 GLN A 116 15663 8303 10746 -659 -992 -1315 N
ATOM 885 N GLY A 117 4.633 61.365 27.269 1.00 80.12 N
ANISOU 885 N GLY A 117 13908 6829 9705 -2097 -848 -1242 N
ATOM 886 CA GLY A 117 5.954 61.942 27.054 1.00 82.33 C
ANISOU 886 CA GLY A 117 14217 6969 10095 -2419 -852 -1185 C
ATOM 887 C GLY A 117 6.863 61.922 28.259 1.00 88.83 C
ANISOU 887 C GLY A 117 14904 7886 10961 -2540 -898 -1359 C
ATOM 888 O GLY A 117 7.828 62.691 28.301 1.00 91.50 O
ANISOU 888 O GLY A 117 15306 8049 11409 -2788 -947 -1363 O
ATOM 889 N LYS A 118 6.569 61.046 29.243 1.00 84.14 N
ANISOU 889 N LYS A 118 14119 7571 10279 -2374 -883 -1500 N
ATOM 890 CA LYS A 118 7.336 60.938 30.489 1.00 84.89 C
ANISOU 890 CA LYS A 118 14070 7792 10391 -2450 -932 -1680 C
ATOM 891 C LYS A 118 8.211 59.680 30.481 1.00 90.14 C
ANISOU 891 C LYS A 118 14456 8789 11003 -2571 -797 -1607 C
ATOM 892 O LYS A 118 7.721 58.569 30.233 1.00 87.49 O
ANISOU 892 O LYS A 118 13986 8690 10565 -2430 -696 -1536 O
ATOM 893 CB LYS A 118 6.417 60.966 31.727 1.00 85.98 C
ANISOU 893 CB LYS A 118 14206 7997 10463 -2170 -1029 -1906 C
ATOM 894 CG LYS A 118 5.510 62.191 31.788 1.00 92.18 C
ANISOU 894 CG LYS A 118 15263 8467 11292 -2016 -1169 -2000 C
ATOM 895 CD LYS A 118 5.508 62.850 33.142 1.00 96.57 C
ANISOU 895 CD LYS A 118 15857 8966 11868 -1937 -1315 -2264 C
ATOM 896 CE LYS A 118 4.643 64.085 33.138 1.00110.46 C
ANISOU 896 CE LYS A 118 17896 10397 13675 -1779 -1458 -2358 C
ATOM 897 NZ LYS A 118 3.420 63.921 33.972 1.00119.16 N
ANISOU 897 NZ LYS A 118 18982 11630 14664 -1429 -1506 -2523 N
ATOM 898 N SER A 119 9.516 59.874 30.757 1.00 89.62 N
ANISOU 898 N SER A 119 14305 8735 11012 -2833 -803 -1626 N
ATOM 899 CA SER A 119 10.537 58.822 30.781 1.00 88.52 C
ANISOU 899 CA SER A 119 13905 8890 10838 -2974 -690 -1568 C
ATOM 900 C SER A 119 10.343 57.881 31.971 1.00 91.23 C
ANISOU 900 C SER A 119 14051 9527 11085 -2798 -691 -1719 C
ATOM 901 O SER A 119 9.763 58.301 32.978 1.00 91.91 O
ANISOU 901 O SER A 119 14197 9567 11157 -2643 -803 -1904 O
ATOM 902 CB SER A 119 11.926 59.451 30.835 1.00 94.02 C
ANISOU 902 CB SER A 119 14576 9502 11646 -3294 -719 -1572 C
ATOM 903 OG SER A 119 12.107 60.386 29.783 1.00103.79 O
ANISOU 903 OG SER A 119 16008 10452 12977 -3469 -726 -1430 O
ATOM 904 N LEU A 120 10.826 56.612 31.863 1.00 84.91 N
ANISOU 904 N LEU A 120 13019 9028 10214 -2815 -569 -1640 N
ATOM 905 CA LEU A 120 10.719 55.628 32.956 1.00 82.58 C
ANISOU 905 CA LEU A 120 12529 9024 9825 -2660 -562 -1757 C
ATOM 906 C LEU A 120 11.349 56.189 34.235 1.00 87.58 C
ANISOU 906 C LEU A 120 13125 9658 10494 -2722 -680 -1963 C
ATOM 907 O LEU A 120 12.451 56.755 34.192 1.00 89.26 O
ANISOU 907 O LEU A 120 13330 9788 10798 -2968 -711 -1974 O
ATOM 908 CB LEU A 120 11.363 54.268 32.597 1.00 80.55 C
ANISOU 908 CB LEU A 120 12038 9059 9508 -2711 -424 -1636 C
ATOM 909 CG LEU A 120 10.735 53.407 31.476 1.00 82.61 C
ANISOU 909 CG LEU A 120 12291 9390 9708 -2618 -303 -1454 C
ATOM 910 CD1 LEU A 120 11.421 52.077 31.387 1.00 81.09 C
ANISOU 910 CD1 LEU A 120 11866 9487 9460 -2652 -191 -1379 C
ATOM 911 CD2 LEU A 120 9.272 53.132 31.722 1.00 82.78 C
ANISOU 911 CD2 LEU A 120 12377 9425 9652 -2338 -324 -1491 C
ATOM 912 N GLY A 121 10.606 56.105 35.331 1.00 82.48 N
ANISOU 912 N GLY A 121 12468 9094 9776 -2501 -752 -2127 N
ATOM 913 CA GLY A 121 11.056 56.620 36.617 1.00 83.54 C
ANISOU 913 CA GLY A 121 12573 9245 9924 -2518 -873 -2343 C
ATOM 914 C GLY A 121 10.532 58.001 36.955 1.00 88.77 C
ANISOU 914 C GLY A 121 13471 9607 10649 -2469 -1022 -2490 C
ATOM 915 O GLY A 121 10.574 58.392 38.124 1.00 89.49 O
ANISOU 915 O GLY A 121 13556 9725 10723 -2400 -1133 -2698 O
ATOM 916 N THR A 122 10.035 58.757 35.940 1.00 85.42 N
ANISOU 916 N THR A 122 13263 8896 10296 -2494 -1030 -2388 N
ATOM 917 CA THR A 122 9.469 60.107 36.133 1.00 86.54 C
ANISOU 917 CA THR A 122 13659 8717 10506 -2433 -1176 -2514 C
ATOM 918 C THR A 122 8.092 59.965 36.788 1.00 86.07 C
ANISOU 918 C THR A 122 13637 8729 10335 -2090 -1217 -2632 C
ATOM 919 O THR A 122 7.699 60.781 37.629 1.00 87.68 O
ANISOU 919 O THR A 122 13957 8811 10545 -1972 -1352 -2833 O
ATOM 920 CB THR A 122 9.399 60.879 34.792 1.00 95.82 C
ANISOU 920 CB THR A 122 15045 9577 11783 -2564 -1164 -2344 C
ATOM 921 OG1 THR A 122 10.670 60.819 34.146 1.00 96.19 O
ANISOU 921 OG1 THR A 122 15012 9627 11909 -2876 -1096 -2206 O
ATOM 922 CG2 THR A 122 8.987 62.341 34.962 1.00 98.07 C
ANISOU 922 CG2 THR A 122 15606 9493 12162 -2541 -1327 -2468 C
ATOM 923 N MET A 123 7.389 58.898 36.406 1.00 77.12 N
ANISOU 923 N MET A 123 12396 7806 9099 -1935 -1098 -2510 N
ATOM 924 CA MET A 123 6.054 58.534 36.845 1.00 74.53 C
ANISOU 924 CA MET A 123 12065 7597 8654 -1623 -1101 -2571 C
ATOM 925 C MET A 123 6.070 57.176 37.543 1.00 75.34 C
ANISOU 925 C MET A 123 11909 8083 8633 -1530 -1015 -2573 C
ATOM 926 O MET A 123 7.001 56.406 37.294 1.00 73.86 O
ANISOU 926 O MET A 123 11562 8047 8454 -1698 -926 -2470 O
ATOM 927 CB MET A 123 5.146 58.462 35.610 1.00 75.63 C
ANISOU 927 CB MET A 123 12319 7627 8790 -1536 -1035 -2394 C
ATOM 928 CG MET A 123 4.702 59.800 35.087 1.00 81.44 C
ANISOU 928 CG MET A 123 13333 7997 9612 -1519 -1138 -2413 C
ATOM 929 SD MET A 123 3.781 60.779 36.300 1.00 87.53 S
ANISOU 929 SD MET A 123 14245 8661 10353 -1252 -1308 -2688 S
ATOM 930 CE MET A 123 2.204 59.983 36.279 1.00 82.31 C
ANISOU 930 CE MET A 123 13515 8217 9542 -917 -1241 -2652 C
ATOM 931 N PRO A 124 5.047 56.805 38.360 1.00 70.27 N
ANISOU 931 N PRO A 124 11216 7610 7873 -1263 -1031 -2673 N
ATOM 932 CA PRO A 124 5.052 55.463 38.969 1.00 68.34 C
ANISOU 932 CA PRO A 124 10731 7724 7512 -1184 -944 -2648 C
ATOM 933 C PRO A 124 5.071 54.352 37.921 1.00 70.71 C
ANISOU 933 C PRO A 124 10930 8138 7799 -1242 -797 -2418 C
ATOM 934 O PRO A 124 4.704 54.610 36.764 1.00 69.45 O
ANISOU 934 O PRO A 124 10895 7805 7690 -1267 -763 -2288 O
ATOM 935 CB PRO A 124 3.735 55.433 39.750 1.00 69.84 C
ANISOU 935 CB PRO A 124 10930 8021 7587 -885 -984 -2762 C
ATOM 936 CG PRO A 124 3.443 56.873 40.045 1.00 75.89 C
ANISOU 936 CG PRO A 124 11910 8517 8408 -828 -1129 -2935 C
ATOM 937 CD PRO A 124 3.848 57.562 38.777 1.00 72.26 C
ANISOU 937 CD PRO A 124 11619 7749 8086 -1018 -1128 -2809 C
ATOM 938 N PRO A 125 5.484 53.103 38.260 1.00 66.20 N
ANISOU 938 N PRO A 125 10140 7853 7159 -1257 -711 -2360 N
ATOM 939 CA PRO A 125 5.440 52.044 37.241 1.00 63.68 C
ANISOU 939 CA PRO A 125 9737 7629 6828 -1294 -580 -2153 C
ATOM 940 C PRO A 125 4.012 51.860 36.729 1.00 67.13 C
ANISOU 940 C PRO A 125 10247 8047 7212 -1094 -552 -2086 C
ATOM 941 O PRO A 125 3.058 51.932 37.513 1.00 67.83 O
ANISOU 941 O PRO A 125 10339 8212 7222 -888 -599 -2191 O
ATOM 942 CB PRO A 125 5.967 50.806 37.973 1.00 63.76 C
ANISOU 942 CB PRO A 125 9515 7948 6762 -1292 -521 -2144 C
ATOM 943 CG PRO A 125 6.660 51.324 39.176 1.00 69.12 C
ANISOU 943 CG PRO A 125 10156 8665 7441 -1334 -615 -2325 C
ATOM 944 CD PRO A 125 5.951 52.577 39.558 1.00 66.65 C
ANISOU 944 CD PRO A 125 10025 8158 7143 -1225 -732 -2477 C
ATOM 945 N HIS A 126 3.869 51.724 35.408 1.00 61.30 N
ANISOU 945 N HIS A 126 9575 7201 6516 -1158 -484 -1920 N
ATOM 946 CA HIS A 126 2.581 51.558 34.741 1.00 60.06 C
ANISOU 946 CA HIS A 126 9487 7015 6317 -991 -457 -1840 C
ATOM 947 C HIS A 126 2.762 51.024 33.375 1.00 62.75 C
ANISOU 947 C HIS A 126 9831 7324 6687 -1095 -360 -1647 C
ATOM 948 O HIS A 126 3.730 51.382 32.706 1.00 62.51 O
ANISOU 948 O HIS A 126 9847 7169 6736 -1296 -341 -1581 O
ATOM 949 CB HIS A 126 1.841 52.899 34.620 1.00 62.58 C
ANISOU 949 CB HIS A 126 10027 7078 6672 -895 -559 -1924 C
ATOM 950 CG HIS A 126 0.358 52.767 34.555 1.00 64.96 C
ANISOU 950 CG HIS A 126 10360 7424 6896 -651 -564 -1922 C
ATOM 951 ND1 HIS A 126 -0.274 52.206 33.455 1.00 64.80 N
ANISOU 951 ND1 HIS A 126 10347 7414 6860 -616 -489 -1761 N
ATOM 952 CD2 HIS A 126 -0.576 53.128 35.463 1.00 66.79 C
ANISOU 952 CD2 HIS A 126 10611 7705 7062 -435 -636 -2067 C
ATOM 953 CE1 HIS A 126 -1.566 52.225 33.741 1.00 63.89 C
ANISOU 953 CE1 HIS A 126 10246 7357 6672 -387 -518 -1810 C
ATOM 954 NE2 HIS A 126 -1.794 52.753 34.946 1.00 65.45 N
ANISOU 954 NE2 HIS A 126 10445 7588 6833 -269 -602 -1991 N
ATOM 955 N VAL A 127 1.759 50.257 32.911 1.00 59.83 N
ANISOU 955 N VAL A 127 9424 7056 6253 -955 -303 -1557 N
ATOM 956 CA VAL A 127 1.665 49.677 31.566 1.00 58.26 C
ANISOU 956 CA VAL A 127 9232 6841 6062 -1008 -215 -1379 C
ATOM 957 C VAL A 127 1.677 50.827 30.524 1.00 62.06 C
ANISOU 957 C VAL A 127 9928 7035 6618 -1083 -249 -1325 C
ATOM 958 O VAL A 127 2.231 50.646 29.449 1.00 61.62 O
ANISOU 958 O VAL A 127 9889 6927 6597 -1225 -183 -1190 O
ATOM 959 CB VAL A 127 0.436 48.715 31.453 1.00 60.85 C
ANISOU 959 CB VAL A 127 9484 7332 6304 -821 -173 -1325 C
ATOM 960 CG1 VAL A 127 -0.893 49.413 31.730 1.00 61.87 C
ANISOU 960 CG1 VAL A 127 9718 7393 6396 -614 -249 -1407 C
ATOM 961 CG2 VAL A 127 0.398 47.984 30.125 1.00 59.54 C
ANISOU 961 CG2 VAL A 127 9310 7173 6141 -876 -86 -1155 C
ATOM 962 N PHE A 128 1.174 52.030 30.900 1.00 59.99 N
ANISOU 962 N PHE A 128 9826 6587 6381 -997 -355 -1436 N
ATOM 963 CA PHE A 128 1.150 53.241 30.074 1.00 61.18 C
ANISOU 963 CA PHE A 128 10199 6440 6606 -1055 -407 -1398 C
ATOM 964 C PHE A 128 2.569 53.797 29.823 1.00 65.47 C
ANISOU 964 C PHE A 128 10781 6848 7246 -1323 -406 -1370 C
ATOM 965 O PHE A 128 2.803 54.418 28.783 1.00 64.71 O
ANISOU 965 O PHE A 128 10827 6553 7207 -1436 -399 -1258 O
ATOM 966 CB PHE A 128 0.286 54.331 30.743 1.00 64.39 C
ANISOU 966 CB PHE A 128 10757 6695 7014 -880 -533 -1551 C
ATOM 967 CG PHE A 128 -1.200 54.068 30.861 1.00 65.29 C
ANISOU 967 CG PHE A 128 10866 6901 7039 -611 -547 -1578 C
ATOM 968 CD1 PHE A 128 -1.789 52.978 30.225 1.00 66.40 C
ANISOU 968 CD1 PHE A 128 10899 7216 7115 -547 -456 -1452 C
ATOM 969 CD2 PHE A 128 -2.018 54.924 31.584 1.00 69.00 C
ANISOU 969 CD2 PHE A 128 11439 7286 7492 -422 -656 -1733 C
ATOM 970 CE1 PHE A 128 -3.164 52.743 30.331 1.00 66.49 C
ANISOU 970 CE1 PHE A 128 10893 7322 7046 -312 -472 -1476 C
ATOM 971 CE2 PHE A 128 -3.397 54.696 31.671 1.00 70.96 C
ANISOU 971 CE2 PHE A 128 11670 7639 7654 -173 -666 -1756 C
ATOM 972 CZ PHE A 128 -3.958 53.607 31.044 1.00 66.32 C
ANISOU 972 CZ PHE A 128 10964 7230 7005 -127 -573 -1624 C
ATOM 973 N ALA A 129 3.496 53.623 30.793 1.00 61.62 N
ANISOU 973 N ALA A 129 10170 6470 6774 -1423 -419 -1470 N
ATOM 974 CA ALA A 129 4.873 54.112 30.646 1.00 61.78 C
ANISOU 974 CA ALA A 129 10200 6388 6884 -1684 -420 -1452 C
ATOM 975 C ALA A 129 5.632 53.256 29.628 1.00 65.75 C
ANISOU 975 C ALA A 129 10595 7002 7386 -1842 -292 -1273 C
ATOM 976 O ALA A 129 6.355 53.796 28.791 1.00 67.28 O
ANISOU 976 O ALA A 129 10868 7047 7648 -2034 -271 -1174 O
ATOM 977 CB ALA A 129 5.581 54.105 31.986 1.00 62.43 C
ANISOU 977 CB ALA A 129 10167 6582 6972 -1729 -474 -1617 C
ATOM 978 N ILE A 130 5.439 51.923 29.680 1.00 60.35 N
ANISOU 978 N ILE A 130 9732 6576 6620 -1757 -207 -1228 N
ATOM 979 CA ILE A 130 6.025 50.953 28.751 1.00 58.97 C
ANISOU 979 CA ILE A 130 9445 6534 6428 -1861 -86 -1073 C
ATOM 980 C ILE A 130 5.551 51.270 27.314 1.00 63.78 C
ANISOU 980 C ILE A 130 10203 6986 7044 -1871 -48 -920 C
ATOM 981 O ILE A 130 6.361 51.219 26.377 1.00 65.53 O
ANISOU 981 O ILE A 130 10417 7189 7291 -2042 23 -796 O
ATOM 982 CB ILE A 130 5.645 49.501 29.195 1.00 59.39 C
ANISOU 982 CB ILE A 130 9308 6865 6391 -1721 -26 -1073 C
ATOM 983 CG1 ILE A 130 6.403 49.088 30.498 1.00 59.43 C
ANISOU 983 CG1 ILE A 130 9147 7048 6385 -1748 -47 -1194 C
ATOM 984 CG2 ILE A 130 5.802 48.466 28.065 1.00 56.92 C
ANISOU 984 CG2 ILE A 130 8919 6661 6047 -1760 89 -912 C
ATOM 985 CD1 ILE A 130 7.986 48.858 30.362 1.00 66.57 C
ANISOU 985 CD1 ILE A 130 9926 8035 7332 -1972 5 -1159 C
ATOM 986 N ALA A 131 4.249 51.629 27.162 1.00 58.47 N
ANISOU 986 N ALA A 131 9663 6211 6343 -1684 -99 -933 N
ATOM 987 CA ALA A 131 3.620 51.995 25.884 1.00 57.07 C
ANISOU 987 CA ALA A 131 9641 5883 6162 -1655 -82 -802 C
ATOM 988 C ALA A 131 4.178 53.304 25.369 1.00 65.68 C
ANISOU 988 C ALA A 131 10914 6702 7338 -1821 -125 -758 C
ATOM 989 O ALA A 131 4.406 53.415 24.174 1.00 67.68 O
ANISOU 989 O ALA A 131 11234 6885 7597 -1920 -67 -604 O
ATOM 990 CB ALA A 131 2.120 52.099 26.040 1.00 56.52 C
ANISOU 990 CB ALA A 131 9651 5783 6040 -1405 -140 -851 C
ATOM 991 N ASP A 132 4.421 54.285 26.264 1.00 65.12 N
ANISOU 991 N ASP A 132 10926 6483 7335 -1856 -228 -891 N
ATOM 992 CA ASP A 132 4.966 55.595 25.899 1.00 67.72 C
ANISOU 992 CA ASP A 132 11440 6528 7761 -2024 -287 -863 C
ATOM 993 C ASP A 132 6.430 55.494 25.505 1.00 72.66 C
ANISOU 993 C ASP A 132 11978 7191 8438 -2309 -214 -772 C
ATOM 994 O ASP A 132 6.839 56.182 24.576 1.00 73.51 O
ANISOU 994 O ASP A 132 12214 7121 8596 -2465 -200 -644 O
ATOM 995 CB ASP A 132 4.808 56.610 27.032 1.00 70.81 C
ANISOU 995 CB ASP A 132 11935 6758 8210 -1976 -427 -1052 C
ATOM 996 CG ASP A 132 4.798 58.033 26.515 1.00 87.19 C
ANISOU 996 CG ASP A 132 14271 8482 10374 -2050 -514 -1018 C
ATOM 997 OD1 ASP A 132 3.767 58.449 25.949 1.00 89.96 O
ANISOU 997 OD1 ASP A 132 14781 8697 10702 -1887 -548 -974 O
ATOM 998 OD2 ASP A 132 5.839 58.713 26.626 1.00 91.85 O
ANISOU 998 OD2 ASP A 132 14906 8932 11059 -2276 -548 -1027 O
ATOM 999 N LYS A 133 7.222 54.641 26.205 1.00 68.26 N
ANISOU 999 N LYS A 133 11200 6872 7864 -2376 -167 -833 N
ATOM 1000 CA LYS A 133 8.642 54.449 25.889 1.00 68.33 C
ANISOU 1000 CA LYS A 133 11092 6958 7911 -2635 -94 -757 C
ATOM 1001 C LYS A 133 8.748 53.862 24.487 1.00 69.51 C
ANISOU 1001 C LYS A 133 11221 7176 8014 -2684 29 -557 C
ATOM 1002 O LYS A 133 9.603 54.284 23.718 1.00 70.09 O
ANISOU 1002 O LYS A 133 11326 7173 8130 -2897 73 -440 O
ATOM 1003 CB LYS A 133 9.360 53.570 26.938 1.00 69.65 C
ANISOU 1003 CB LYS A 133 11021 7388 8056 -2655 -73 -867 C
ATOM 1004 CG LYS A 133 10.846 53.314 26.634 1.00 77.35 C
ANISOU 1004 CG LYS A 133 11848 8479 9063 -2907 6 -794 C
ATOM 1005 CD LYS A 133 11.481 52.344 27.623 1.00 85.38 C
ANISOU 1005 CD LYS A 133 12626 9769 10045 -2895 26 -895 C
ATOM 1006 CE LYS A 133 12.759 51.719 27.120 1.00 95.07 C
ANISOU 1006 CE LYS A 133 13675 11174 11271 -3083 129 -802 C
ATOM 1007 NZ LYS A 133 13.892 52.681 27.146 1.00111.59 N
ANISOU 1007 NZ LYS A 133 15784 13155 13459 -3349 97 -808 N
ATOM 1008 N ALA A 134 7.840 52.929 24.148 1.00 64.43 N
ANISOU 1008 N ALA A 134 10531 6670 7280 -2488 79 -520 N
ATOM 1009 CA ALA A 134 7.737 52.304 22.827 1.00 62.36 C
ANISOU 1009 CA ALA A 134 10258 6480 6957 -2490 185 -349 C
ATOM 1010 C ALA A 134 7.462 53.363 21.762 1.00 66.90 C
ANISOU 1010 C ALA A 134 11058 6801 7560 -2550 167 -223 C
ATOM 1011 O ALA A 134 8.220 53.446 20.796 1.00 66.55 O
ANISOU 1011 O ALA A 134 11016 6752 7519 -2724 244 -80 O
ATOM 1012 CB ALA A 134 6.647 51.251 22.830 1.00 60.80 C
ANISOU 1012 CB ALA A 134 9994 6438 6668 -2252 209 -362 C
ATOM 1013 N PHE A 135 6.443 54.225 21.976 1.00 65.68 N
ANISOU 1013 N PHE A 135 11093 6436 7428 -2413 62 -278 N
ATOM 1014 CA PHE A 135 6.131 55.309 21.037 1.00 68.09 C
ANISOU 1014 CA PHE A 135 11633 6474 7764 -2452 28 -163 C
ATOM 1015 C PHE A 135 7.296 56.308 20.905 1.00 74.21 C
ANISOU 1015 C PHE A 135 12485 7074 8640 -2731 13 -111 C
ATOM 1016 O PHE A 135 7.584 56.767 19.797 1.00 75.77 O
ANISOU 1016 O PHE A 135 12790 7157 8843 -2858 56 58 O
ATOM 1017 CB PHE A 135 4.845 56.057 21.437 1.00 70.67 C
ANISOU 1017 CB PHE A 135 12140 6612 8099 -2234 -96 -257 C
ATOM 1018 CG PHE A 135 4.542 57.204 20.498 1.00 74.58 C
ANISOU 1018 CG PHE A 135 12891 6817 8631 -2267 -142 -136 C
ATOM 1019 CD1 PHE A 135 3.915 56.978 19.276 1.00 77.19 C
ANISOU 1019 CD1 PHE A 135 13292 7150 8886 -2184 -90 18 C
ATOM 1020 CD2 PHE A 135 4.947 58.502 20.803 1.00 78.84 C
ANISOU 1020 CD2 PHE A 135 13600 7079 9278 -2395 -237 -169 C
ATOM 1021 CE1 PHE A 135 3.682 58.032 18.387 1.00 80.19 C
ANISOU 1021 CE1 PHE A 135 13910 7266 9293 -2218 -131 144 C
ATOM 1022 CE2 PHE A 135 4.728 59.550 19.906 1.00 83.78 C
ANISOU 1022 CE2 PHE A 135 14468 7425 9940 -2439 -279 -40 C
ATOM 1023 CZ PHE A 135 4.085 59.311 18.712 1.00 81.31 C
ANISOU 1023 CZ PHE A 135 14224 7125 9546 -2344 -225 119 C
ATOM 1024 N ARG A 136 7.940 56.660 22.022 1.00 71.18 N
ANISOU 1024 N ARG A 136 12046 6668 8330 -2826 -50 -254 N
ATOM 1025 CA ARG A 136 9.043 57.618 22.003 1.00 73.30 C
ANISOU 1025 CA ARG A 136 12377 6770 8705 -3103 -77 -222 C
ATOM 1026 C ARG A 136 10.280 57.036 21.300 1.00 77.62 C
ANISOU 1026 C ARG A 136 12757 7500 9235 -3332 57 -83 C
ATOM 1027 O ARG A 136 10.880 57.748 20.501 1.00 79.74 O
ANISOU 1027 O ARG A 136 13122 7627 9549 -3538 83 61 O
ATOM 1028 CB ARG A 136 9.403 58.094 23.412 1.00 72.65 C
ANISOU 1028 CB ARG A 136 12265 6639 8701 -3138 -187 -428 C
ATOM 1029 CG ARG A 136 8.341 58.957 24.099 1.00 76.72 C
ANISOU 1029 CG ARG A 136 12974 6928 9248 -2946 -334 -572 C
ATOM 1030 CD ARG A 136 8.844 59.574 25.402 1.00 79.51 C
ANISOU 1030 CD ARG A 136 13317 7210 9684 -3011 -450 -774 C
ATOM 1031 NE ARG A 136 9.851 58.757 26.091 1.00 80.69 N
ANISOU 1031 NE ARG A 136 13210 7629 9822 -3126 -395 -842 N
ATOM 1032 CZ ARG A 136 9.587 57.890 27.064 1.00 94.26 C
ANISOU 1032 CZ ARG A 136 14758 9584 11471 -2963 -395 -982 C
ATOM 1033 NH1 ARG A 136 10.567 57.191 27.625 1.00 78.94 N
ANISOU 1033 NH1 ARG A 136 12594 7877 9522 -3077 -348 -1028 N
ATOM 1034 NH2 ARG A 136 8.341 57.717 27.489 1.00 82.20 N
ANISOU 1034 NH2 ARG A 136 13281 8072 9881 -2685 -442 -1072 N
ATOM 1035 N ASP A 137 10.652 55.760 21.574 1.00 71.49 N
ANISOU 1035 N ASP A 137 11735 7037 8391 -3292 143 -120 N
ATOM 1036 CA ASP A 137 11.810 55.114 20.942 1.00 71.42 C
ANISOU 1036 CA ASP A 137 11547 7235 8353 -3476 273 -5 C
ATOM 1037 C ASP A 137 11.572 54.977 19.450 1.00 76.78 C
ANISOU 1037 C ASP A 137 12301 7909 8964 -3480 367 198 C
ATOM 1038 O ASP A 137 12.504 55.154 18.672 1.00 77.81 O
ANISOU 1038 O ASP A 137 12396 8067 9099 -3693 448 336 O
ATOM 1039 CB ASP A 137 12.112 53.734 21.552 1.00 71.28 C
ANISOU 1039 CB ASP A 137 11272 7540 8270 -3383 332 -94 C
ATOM 1040 CG ASP A 137 12.661 53.723 22.971 1.00 86.98 C
ANISOU 1040 CG ASP A 137 13137 9600 10311 -3419 263 -276 C
ATOM 1041 OD1 ASP A 137 13.169 54.778 23.426 1.00 91.02 O
ANISOU 1041 OD1 ASP A 137 13727 9937 10920 -3581 182 -330 O
ATOM 1042 OD2 ASP A 137 12.608 52.649 23.619 1.00 90.81 O
ANISOU 1042 OD2 ASP A 137 13447 10317 10739 -3290 286 -362 O
ATOM 1043 N MET A 138 10.313 54.689 19.055 1.00 72.49 N
ANISOU 1043 N MET A 138 11857 7334 8351 -3244 355 217 N
ATOM 1044 CA MET A 138 9.887 54.564 17.661 1.00 72.03 C
ANISOU 1044 CA MET A 138 11888 7265 8215 -3206 428 396 C
ATOM 1045 C MET A 138 10.077 55.885 16.914 1.00 80.28 C
ANISOU 1045 C MET A 138 13153 8034 9318 -3369 399 535 C
ATOM 1046 O MET A 138 10.565 55.882 15.789 1.00 81.43 O
ANISOU 1046 O MET A 138 13306 8214 9419 -3496 493 713 O
ATOM 1047 CB MET A 138 8.414 54.144 17.611 1.00 71.96 C
ANISOU 1047 CB MET A 138 11948 7257 8137 -2913 388 353 C
ATOM 1048 CG MET A 138 7.907 53.850 16.215 1.00 74.35 C
ANISOU 1048 CG MET A 138 12319 7587 8344 -2843 458 517 C
ATOM 1049 SD MET A 138 6.127 54.106 16.072 1.00 76.99 S
ANISOU 1049 SD MET A 138 12841 7772 8639 -2551 361 487 S
ATOM 1050 CE MET A 138 6.023 55.913 16.274 1.00 76.65 C
ANISOU 1050 CE MET A 138 13071 7343 8709 -2641 237 499 C
ATOM 1051 N LYS A 139 9.682 57.003 17.550 1.00 78.70 N
ANISOU 1051 N LYS A 139 13133 7559 9212 -3360 267 454 N
ATOM 1052 CA LYS A 139 9.734 58.351 16.998 1.00 81.39 C
ANISOU 1052 CA LYS A 139 13714 7588 9623 -3495 211 568 C
ATOM 1053 C LYS A 139 11.174 58.853 16.863 1.00 88.50 C
ANISOU 1053 C LYS A 139 14562 8463 10600 -3832 253 650 C
ATOM 1054 O LYS A 139 11.495 59.491 15.864 1.00 90.82 O
ANISOU 1054 O LYS A 139 14976 8631 10901 -3991 292 839 O
ATOM 1055 CB LYS A 139 8.913 59.296 17.900 1.00 84.68 C
ANISOU 1055 CB LYS A 139 14318 7734 10121 -3365 46 418 C
ATOM 1056 CG LYS A 139 8.683 60.704 17.345 1.00 96.34 C
ANISOU 1056 CG LYS A 139 16085 8848 11672 -3444 -38 525 C
ATOM 1057 CD LYS A 139 7.640 61.447 18.172 1.00105.82 C
ANISOU 1057 CD LYS A 139 17466 9816 12924 -3234 -198 363 C
ATOM 1058 CE LYS A 139 7.107 62.678 17.479 1.00117.91 C
ANISOU 1058 CE LYS A 139 19303 10995 14504 -3230 -283 477 C
ATOM 1059 NZ LYS A 139 5.845 63.159 18.104 1.00125.61 N
ANISOU 1059 NZ LYS A 139 20437 11800 15489 -2948 -424 325 N
ATOM 1060 N VAL A 140 12.026 58.592 17.871 1.00 84.77 N
ANISOU 1060 N VAL A 140 13911 8114 10183 -3941 244 512 N
ATOM 1061 CA VAL A 140 13.414 59.071 17.929 1.00 85.90 C
ANISOU 1061 CA VAL A 140 13977 8251 10410 -4264 269 557 C
ATOM 1062 C VAL A 140 14.344 58.156 17.109 1.00 88.58 C
ANISOU 1062 C VAL A 140 14099 8893 10663 -4391 438 694 C
ATOM 1063 O VAL A 140 15.039 58.662 16.235 1.00 90.44 O
ANISOU 1063 O VAL A 140 14374 9078 10909 -4612 502 874 O
ATOM 1064 CB VAL A 140 13.903 59.237 19.403 1.00 89.93 C
ANISOU 1064 CB VAL A 140 14390 8766 11012 -4314 173 336 C
ATOM 1065 CG1 VAL A 140 15.383 59.609 19.472 1.00 91.78 C
ANISOU 1065 CG1 VAL A 140 14506 9039 11326 -4652 204 375 C
ATOM 1066 CG2 VAL A 140 13.067 60.275 20.149 1.00 90.76 C
ANISOU 1066 CG2 VAL A 140 14727 8553 11203 -4206 3 203 C
ATOM 1067 N LEU A 141 14.357 56.831 17.376 1.00 82.44 N
ANISOU 1067 N LEU A 141 13097 8426 9799 -4249 508 613 N
ATOM 1068 CA LEU A 141 15.245 55.889 16.675 1.00 81.91 C
ANISOU 1068 CA LEU A 141 12812 8662 9647 -4339 662 716 C
ATOM 1069 C LEU A 141 14.737 55.485 15.260 1.00 83.74 C
ANISOU 1069 C LEU A 141 13108 8951 9759 -4246 762 896 C
ATOM 1070 O LEU A 141 15.430 54.734 14.562 1.00 82.64 O
ANISOU 1070 O LEU A 141 12805 9059 9537 -4309 891 989 O
ATOM 1071 CB LEU A 141 15.487 54.622 17.519 1.00 80.05 C
ANISOU 1071 CB LEU A 141 12325 8722 9368 -4215 690 560 C
ATOM 1072 CG LEU A 141 16.219 54.803 18.850 1.00 86.45 C
ANISOU 1072 CG LEU A 141 13012 9564 10271 -4320 618 391 C
ATOM 1073 CD1 LEU A 141 15.596 53.937 19.928 1.00 84.76 C
ANISOU 1073 CD1 LEU A 141 12701 9478 10025 -4075 567 205 C
ATOM 1074 CD2 LEU A 141 17.708 54.502 18.711 1.00 90.81 C
ANISOU 1074 CD2 LEU A 141 13340 10338 10827 -4558 713 441 C
ATOM 1075 N LYS A 142 13.541 55.975 14.848 1.00 79.56 N
ANISOU 1075 N LYS A 142 12811 8205 9213 -4087 698 939 N
ATOM 1076 CA LYS A 142 12.892 55.717 13.547 1.00 79.17 C
ANISOU 1076 CA LYS A 142 12853 8178 9049 -3976 768 1099 C
ATOM 1077 C LYS A 142 12.851 54.190 13.226 1.00 83.31 C
ANISOU 1077 C LYS A 142 13168 9037 9447 -3825 874 1078 C
ATOM 1078 O LYS A 142 13.030 53.774 12.080 1.00 84.53 O
ANISOU 1078 O LYS A 142 13293 9326 9500 -3840 982 1222 O
ATOM 1079 CB LYS A 142 13.577 56.530 12.427 1.00 82.85 C
ANISOU 1079 CB LYS A 142 13416 8551 9512 -4218 834 1325 C
ATOM 1080 CG LYS A 142 13.334 58.042 12.538 1.00 86.94 C
ANISOU 1080 CG LYS A 142 14193 8693 10146 -4330 718 1371 C
ATOM 1081 CD LYS A 142 14.282 58.858 11.676 1.00 96.97 C
ANISOU 1081 CD LYS A 142 15520 9885 11438 -4631 784 1585 C
ATOM 1082 CE LYS A 142 15.495 59.317 12.452 1.00111.35 C
ANISOU 1082 CE LYS A 142 17231 11694 13382 -4911 767 1531 C
ATOM 1083 NZ LYS A 142 16.320 60.285 11.674 1.00122.26 N
ANISOU 1083 NZ LYS A 142 18701 12946 14805 -5220 810 1746 N
ATOM 1084 N LEU A 143 12.566 53.379 14.253 1.00 78.14 N
ANISOU 1084 N LEU A 143 12382 8507 8800 -3670 836 895 N
ATOM 1085 CA LEU A 143 12.535 51.918 14.196 1.00 76.15 C
ANISOU 1085 CA LEU A 143 11934 8549 8453 -3525 914 847 C
ATOM 1086 C LEU A 143 11.270 51.393 14.880 1.00 76.90 C
ANISOU 1086 C LEU A 143 12055 8631 8531 -3251 833 709 C
ATOM 1087 O LEU A 143 10.927 51.854 15.970 1.00 76.66 O
ANISOU 1087 O LEU A 143 12068 8479 8580 -3207 729 576 O
ATOM 1088 CB LEU A 143 13.821 51.395 14.881 1.00 76.70 C
ANISOU 1088 CB LEU A 143 11762 8826 8554 -3668 962 772 C
ATOM 1089 CG LEU A 143 13.859 50.015 15.536 1.00 79.28 C
ANISOU 1089 CG LEU A 143 11879 9409 8836 -3514 988 643 C
ATOM 1090 CD1 LEU A 143 14.457 48.993 14.598 1.00 79.10 C
ANISOU 1090 CD1 LEU A 143 11706 9643 8707 -3516 1121 731 C
ATOM 1091 CD2 LEU A 143 14.705 50.053 16.815 1.00 81.41 C
ANISOU 1091 CD2 LEU A 143 12001 9742 9189 -3617 946 505 C
ATOM 1092 N SER A 144 10.582 50.425 14.234 1.00 70.71 N
ANISOU 1092 N SER A 144 11242 7982 7643 -3071 881 739 N
ATOM 1093 CA SER A 144 9.357 49.814 14.753 1.00 67.87 C
ANISOU 1093 CA SER A 144 10891 7640 7258 -2818 818 627 C
ATOM 1094 C SER A 144 9.594 49.174 16.105 1.00 69.33 C
ANISOU 1094 C SER A 144 10909 7947 7486 -2774 785 459 C
ATOM 1095 O SER A 144 10.733 48.868 16.480 1.00 67.95 O
ANISOU 1095 O SER A 144 10573 7909 7334 -2911 834 433 O
ATOM 1096 CB SER A 144 8.781 48.793 13.778 1.00 69.55 C
ANISOU 1096 CB SER A 144 11069 8004 7353 -2669 884 690 C
ATOM 1097 OG SER A 144 8.013 49.450 12.784 1.00 80.59 O
ANISOU 1097 OG SER A 144 12665 9246 8710 -2616 864 803 O
ATOM 1098 N GLN A 145 8.513 49.019 16.862 1.00 63.98 N
ANISOU 1098 N GLN A 145 10268 7223 6816 -2584 700 346 N
ATOM 1099 CA GLN A 145 8.616 48.520 18.209 1.00 61.83 C
ANISOU 1099 CA GLN A 145 9860 7052 6581 -2532 658 191 C
ATOM 1100 C GLN A 145 7.632 47.413 18.465 1.00 62.76 C
ANISOU 1100 C GLN A 145 9907 7301 6639 -2309 650 128 C
ATOM 1101 O GLN A 145 6.577 47.340 17.829 1.00 61.08 O
ANISOU 1101 O GLN A 145 9794 7036 6377 -2169 635 171 O
ATOM 1102 CB GLN A 145 8.384 49.673 19.199 1.00 63.65 C
ANISOU 1102 CB GLN A 145 10204 7080 6900 -2553 544 91 C
ATOM 1103 CG GLN A 145 9.378 50.842 19.071 1.00 64.76 C
ANISOU 1103 CG GLN A 145 10422 7065 7120 -2795 534 141 C
ATOM 1104 CD GLN A 145 10.742 50.507 19.616 1.00 78.29 C
ANISOU 1104 CD GLN A 145 11944 8935 8868 -2968 578 99 C
ATOM 1105 OE1 GLN A 145 10.916 50.200 20.799 1.00 75.31 O
ANISOU 1105 OE1 GLN A 145 11455 8643 8516 -2930 533 -43 O
ATOM 1106 NE2 GLN A 145 11.749 50.587 18.772 1.00 68.92 N
ANISOU 1106 NE2 GLN A 145 10714 7797 7677 -3162 665 222 N
ATOM 1107 N BSER A 146 7.976 46.552 19.418 1.00 58.23 N
ANISOU 1107 N BSER A 146 9159 6899 6069 -2278 656 28 N
ATOM 1108 CA BSER A 146 7.082 45.484 19.836 1.00 56.35 C
ANISOU 1108 CA BSER A 146 8844 6783 5783 -2081 642 -34 C
ATOM 1109 C BSER A 146 7.074 45.401 21.362 1.00 57.97 C
ANISOU 1109 C BSER A 146 8964 7035 6027 -2035 576 -177 C
ATOM 1110 O BSER A 146 8.095 45.644 22.015 1.00 58.81 O
ANISOU 1110 O BSER A 146 8991 7174 6179 -2163 574 -228 O
ATOM 1111 CB BSER A 146 7.434 44.152 19.173 1.00 58.09 C
ANISOU 1111 CB BSER A 146 8928 7204 5939 -2056 733 21 C
ATOM 1112 OG BSER A 146 8.687 43.664 19.616 1.00 68.59 O
ANISOU 1112 OG BSER A 146 10091 8684 7285 -2164 780 -9 O
ATOM 1113 N ILE A 147 5.886 45.146 21.918 1.00 51.22 N
ANISOU 1113 N ILE A 147 8131 6181 5150 -1852 519 -242 N
ATOM 1114 CA ILE A 147 5.643 44.983 23.344 1.00 50.26 C
ANISOU 1114 CA ILE A 147 7932 6123 5042 -1770 457 -372 C
ATOM 1115 C ILE A 147 5.133 43.534 23.531 1.00 53.26 C
ANISOU 1115 C ILE A 147 8178 6695 5364 -1634 489 -375 C
ATOM 1116 O ILE A 147 4.091 43.194 22.987 1.00 50.38 O
ANISOU 1116 O ILE A 147 7861 6321 4958 -1512 487 -335 O
ATOM 1117 CB ILE A 147 4.646 46.079 23.858 1.00 52.95 C
ANISOU 1117 CB ILE A 147 8425 6291 5403 -1673 357 -445 C
ATOM 1118 CG1 ILE A 147 5.187 47.503 23.591 1.00 55.09 C
ANISOU 1118 CG1 ILE A 147 8846 6344 5741 -1818 320 -433 C
ATOM 1119 CG2 ILE A 147 4.313 45.879 25.334 1.00 50.72 C
ANISOU 1119 CG2 ILE A 147 8057 6098 5115 -1569 297 -582 C
ATOM 1120 CD1 ILE A 147 4.148 48.596 23.621 1.00 63.62 C
ANISOU 1120 CD1 ILE A 147 10118 7218 6836 -1712 231 -464 C
ATOM 1121 N ILE A 148 5.906 42.676 24.232 1.00 51.08 N
ANISOU 1121 N ILE A 148 7734 6587 5085 -1664 517 -415 N
ATOM 1122 CA ILE A 148 5.551 41.271 24.453 1.00 49.66 C
ANISOU 1122 CA ILE A 148 7429 6579 4860 -1553 544 -411 C
ATOM 1123 C ILE A 148 4.999 41.172 25.860 1.00 54.04 C
ANISOU 1123 C ILE A 148 7930 7193 5409 -1449 479 -513 C
ATOM 1124 O ILE A 148 5.698 41.470 26.829 1.00 53.80 O
ANISOU 1124 O ILE A 148 7840 7199 5401 -1504 452 -591 O
ATOM 1125 CB ILE A 148 6.750 40.315 24.167 1.00 52.83 C
ANISOU 1125 CB ILE A 148 7688 7129 5255 -1638 619 -373 C
ATOM 1126 CG1 ILE A 148 7.077 40.313 22.666 1.00 55.57 C
ANISOU 1126 CG1 ILE A 148 8089 7439 5586 -1710 689 -266 C
ATOM 1127 CG2 ILE A 148 6.480 38.872 24.608 1.00 48.91 C
ANISOU 1127 CG2 ILE A 148 7064 6796 4724 -1526 633 -380 C
ATOM 1128 CD1 ILE A 148 8.480 40.687 22.328 1.00 69.00 C
ANISOU 1128 CD1 ILE A 148 9749 9156 7313 -1886 738 -240 C
ATOM 1129 N VAL A 149 3.702 40.845 25.946 1.00 50.30 N
ANISOU 1129 N VAL A 149 7483 6729 4900 -1299 452 -513 N
ATOM 1130 CA VAL A 149 2.952 40.731 27.198 1.00 50.22 C
ANISOU 1130 CA VAL A 149 7425 6789 4866 -1178 397 -597 C
ATOM 1131 C VAL A 149 2.787 39.236 27.489 1.00 53.21 C
ANISOU 1131 C VAL A 149 7662 7346 5209 -1113 431 -564 C
ATOM 1132 O VAL A 149 1.968 38.572 26.860 1.00 51.68 O
ANISOU 1132 O VAL A 149 7475 7169 4990 -1039 448 -504 O
ATOM 1133 CB VAL A 149 1.597 41.493 27.118 1.00 53.12 C
ANISOU 1133 CB VAL A 149 7917 7048 5217 -1056 340 -618 C
ATOM 1134 CG1 VAL A 149 0.907 41.507 28.472 1.00 51.73 C
ANISOU 1134 CG1 VAL A 149 7689 6957 5010 -936 284 -715 C
ATOM 1135 CG2 VAL A 149 1.797 42.919 26.603 1.00 54.06 C
ANISOU 1135 CG2 VAL A 149 8201 6963 5379 -1126 308 -626 C
ATOM 1136 N SER A 150 3.590 38.703 28.408 1.00 50.29 N
ANISOU 1136 N SER A 150 7167 7103 4839 -1144 437 -602 N
ATOM 1137 CA SER A 150 3.573 37.274 28.637 1.00 49.61 C
ANISOU 1137 CA SER A 150 6957 7168 4726 -1093 468 -560 C
ATOM 1138 C SER A 150 3.122 36.907 30.040 1.00 52.09 C
ANISOU 1138 C SER A 150 7185 7602 5004 -1001 429 -615 C
ATOM 1139 O SER A 150 3.001 37.762 30.912 1.00 52.09 O
ANISOU 1139 O SER A 150 7208 7588 4996 -980 379 -700 O
ATOM 1140 CB SER A 150 4.939 36.666 28.321 1.00 54.51 C
ANISOU 1140 CB SER A 150 7490 7856 5364 -1194 521 -530 C
ATOM 1141 OG SER A 150 5.957 37.158 29.170 1.00 64.22 O
ANISOU 1141 OG SER A 150 8664 9124 6611 -1270 502 -601 O
ATOM 1142 N GLY A 151 2.789 35.640 30.198 1.00 45.61 N
ANISOU 1142 N GLY A 151 6275 6895 4158 -940 449 -561 N
ATOM 1143 CA GLY A 151 2.314 35.096 31.445 1.00 45.01 C
ANISOU 1143 CA GLY A 151 6110 6953 4041 -854 422 -583 C
ATOM 1144 C GLY A 151 1.352 33.952 31.232 1.00 48.97 C
ANISOU 1144 C GLY A 151 6572 7513 4521 -777 436 -502 C
ATOM 1145 O GLY A 151 0.886 33.698 30.107 1.00 46.63 O
ANISOU 1145 O GLY A 151 6333 7144 4242 -777 456 -444 O
ATOM 1146 N GLU A 152 1.071 33.252 32.340 1.00 42.95 N
ANISOU 1146 N GLU A 152 5710 6888 3719 -717 422 -497 N
ATOM 1147 CA GLU A 152 0.184 32.117 32.434 1.00 42.42 C
ANISOU 1147 CA GLU A 152 5587 6898 3632 -654 428 -419 C
ATOM 1148 C GLU A 152 -1.218 32.508 32.066 1.00 46.70 C
ANISOU 1148 C GLU A 152 6189 7396 4157 -587 410 -412 C
ATOM 1149 O GLU A 152 -1.529 33.703 32.020 1.00 49.04 O
ANISOU 1149 O GLU A 152 6564 7621 4447 -567 385 -479 O
ATOM 1150 CB GLU A 152 0.161 31.663 33.920 1.00 45.30 C
ANISOU 1150 CB GLU A 152 5843 7424 3945 -604 410 -426 C
ATOM 1151 CG GLU A 152 1.206 30.623 34.240 1.00 62.14 C
ANISOU 1151 CG GLU A 152 7889 9633 6087 -639 428 -385 C
ATOM 1152 CD GLU A 152 1.069 30.082 35.646 1.00 81.79 C
ANISOU 1152 CD GLU A 152 10277 12285 8516 -582 410 -372 C
ATOM 1153 OE1 GLU A 152 0.474 30.777 36.503 1.00 70.45 O
ANISOU 1153 OE1 GLU A 152 8833 10910 7024 -526 384 -429 O
ATOM 1154 OE2 GLU A 152 1.579 28.966 35.894 1.00 81.38 O
ANISOU 1154 OE2 GLU A 152 10153 12300 8466 -586 420 -306 O
ATOM 1155 N SER A 153 -2.104 31.510 31.912 1.00 40.34 N
ANISOU 1155 N SER A 153 5342 6642 3345 -547 415 -335 N
ATOM 1156 CA SER A 153 -3.515 31.792 31.719 1.00 40.08 C
ANISOU 1156 CA SER A 153 5336 6606 3287 -476 394 -328 C
ATOM 1157 C SER A 153 -4.075 32.450 33.019 1.00 45.10 C
ANISOU 1157 C SER A 153 5930 7348 3859 -395 366 -392 C
ATOM 1158 O SER A 153 -3.882 31.926 34.116 1.00 43.96 O
ANISOU 1158 O SER A 153 5689 7337 3678 -380 367 -381 O
ATOM 1159 CB SER A 153 -4.266 30.513 31.369 1.00 40.75 C
ANISOU 1159 CB SER A 153 5368 6735 3380 -467 402 -231 C
ATOM 1160 OG SER A 153 -5.657 30.780 31.357 1.00 45.74 O
ANISOU 1160 OG SER A 153 5999 7400 3981 -396 379 -227 O
ATOM 1161 N GLY A 154 -4.765 33.584 32.868 1.00 42.67 N
ANISOU 1161 N GLY A 154 5697 6983 3534 -336 337 -458 N
ATOM 1162 CA GLY A 154 -5.320 34.314 34.000 1.00 42.49 C
ANISOU 1162 CA GLY A 154 5646 7052 3445 -243 306 -537 C
ATOM 1163 C GLY A 154 -4.384 35.386 34.518 1.00 47.76 C
ANISOU 1163 C GLY A 154 6367 7666 4115 -262 282 -647 C
ATOM 1164 O GLY A 154 -4.763 36.128 35.418 1.00 47.25 O
ANISOU 1164 O GLY A 154 6297 7659 3997 -179 248 -735 O
ATOM 1165 N ALA A 155 -3.149 35.504 33.943 1.00 44.19 N
ANISOU 1165 N ALA A 155 5963 7103 3723 -372 297 -649 N
ATOM 1166 CA ALA A 155 -2.163 36.469 34.451 1.00 43.26 C
ANISOU 1166 CA ALA A 155 5884 6936 3616 -415 272 -750 C
ATOM 1167 C ALA A 155 -2.517 37.942 34.172 1.00 48.58 C
ANISOU 1167 C ALA A 155 6692 7464 4301 -380 226 -840 C
ATOM 1168 O ALA A 155 -2.068 38.809 34.925 1.00 50.73 O
ANISOU 1168 O ALA A 155 6989 7722 4565 -377 186 -947 O
ATOM 1169 CB ALA A 155 -0.791 36.156 33.911 1.00 42.80 C
ANISOU 1169 CB ALA A 155 5826 6819 3617 -545 304 -718 C
ATOM 1170 N GLY A 156 -3.247 38.219 33.090 1.00 44.06 N
ANISOU 1170 N GLY A 156 6211 6778 3752 -357 227 -800 N
ATOM 1171 CA GLY A 156 -3.615 39.586 32.731 1.00 43.95 C
ANISOU 1171 CA GLY A 156 6338 6608 3752 -316 180 -872 C
ATOM 1172 C GLY A 156 -3.026 40.085 31.421 1.00 46.62 C
ANISOU 1172 C GLY A 156 6801 6753 4158 -419 193 -830 C
ATOM 1173 O GLY A 156 -3.022 41.306 31.171 1.00 44.08 O
ANISOU 1173 O GLY A 156 6612 6277 3862 -417 151 -888 O
ATOM 1174 N LYS A 157 -2.560 39.139 30.540 1.00 41.64 N
ANISOU 1174 N LYS A 157 6136 6130 3555 -506 251 -726 N
ATOM 1175 CA LYS A 157 -1.950 39.496 29.262 1.00 40.72 C
ANISOU 1175 CA LYS A 157 6122 5861 3489 -606 275 -675 C
ATOM 1176 C LYS A 157 -2.912 40.251 28.400 1.00 44.87 C
ANISOU 1176 C LYS A 157 6779 6258 4013 -538 246 -660 C
ATOM 1177 O LYS A 157 -2.551 41.304 27.881 1.00 45.93 O
ANISOU 1177 O LYS A 157 7041 6230 4181 -587 227 -675 O
ATOM 1178 CB LYS A 157 -1.421 38.287 28.466 1.00 42.56 C
ANISOU 1178 CB LYS A 157 6290 6143 3736 -681 339 -575 C
ATOM 1179 CG LYS A 157 -0.485 37.322 29.183 1.00 42.32 C
ANISOU 1179 CG LYS A 157 6124 6248 3707 -736 370 -570 C
ATOM 1180 CD LYS A 157 -0.102 36.225 28.188 1.00 40.06 C
ANISOU 1180 CD LYS A 157 5802 5982 3436 -788 425 -477 C
ATOM 1181 CE LYS A 157 -1.243 35.256 27.941 1.00 39.82 C
ANISOU 1181 CE LYS A 157 5735 6015 3381 -702 425 -419 C
ATOM 1182 NZ LYS A 157 -1.596 34.524 29.197 1.00 40.04 N
ANISOU 1182 NZ LYS A 157 5644 6191 3379 -642 411 -430 N
ATOM 1183 N THR A 158 -4.125 39.705 28.220 1.00 41.00 N
ANISOU 1183 N THR A 158 6255 5839 3483 -429 241 -626 N
ATOM 1184 CA THR A 158 -5.209 40.275 27.402 1.00 40.83 C
ANISOU 1184 CA THR A 158 6339 5728 3448 -339 209 -608 C
ATOM 1185 C THR A 158 -5.613 41.655 27.938 1.00 47.12 C
ANISOU 1185 C THR A 158 7236 6428 4237 -254 142 -707 C
ATOM 1186 O THR A 158 -5.648 42.595 27.157 1.00 46.64 O
ANISOU 1186 O THR A 158 7323 6199 4200 -256 116 -700 O
ATOM 1187 CB THR A 158 -6.375 39.275 27.335 1.00 44.95 C
ANISOU 1187 CB THR A 158 6766 6386 3927 -247 214 -562 C
ATOM 1188 OG1 THR A 158 -5.935 38.115 26.614 1.00 44.27 O
ANISOU 1188 OG1 THR A 158 6625 6338 3859 -331 266 -473 O
ATOM 1189 CG2 THR A 158 -7.607 39.833 26.683 1.00 42.56 C
ANISOU 1189 CG2 THR A 158 6544 6028 3599 -131 172 -559 C
ATOM 1190 N GLU A 159 -5.839 41.798 29.272 1.00 46.58 N
ANISOU 1190 N GLU A 159 7096 6464 4137 -181 112 -800 N
ATOM 1191 CA GLU A 159 -6.214 43.091 29.857 1.00 47.47 C
ANISOU 1191 CA GLU A 159 7304 6493 4240 -85 41 -913 C
ATOM 1192 C GLU A 159 -5.103 44.145 29.647 1.00 51.07 C
ANISOU 1192 C GLU A 159 7894 6749 4761 -199 18 -952 C
ATOM 1193 O GLU A 159 -5.394 45.245 29.186 1.00 51.48 O
ANISOU 1193 O GLU A 159 8101 6626 4835 -160 -33 -978 O
ATOM 1194 CB GLU A 159 -6.585 42.954 31.349 1.00 49.46 C
ANISOU 1194 CB GLU A 159 7440 6920 4433 13 19 -1008 C
ATOM 1195 CG GLU A 159 -7.945 42.307 31.585 1.00 55.73 C
ANISOU 1195 CG GLU A 159 8132 7887 5157 155 22 -985 C
ATOM 1196 CD GLU A 159 -9.079 42.741 30.668 1.00 71.82 C
ANISOU 1196 CD GLU A 159 10255 9848 7184 262 -7 -961 C
ATOM 1197 OE1 GLU A 159 -9.381 43.957 30.603 1.00 68.35 O
ANISOU 1197 OE1 GLU A 159 9949 9272 6750 346 -69 -1038 O
ATOM 1198 OE2 GLU A 159 -9.660 41.855 30.001 1.00 55.35 O
ANISOU 1198 OE2 GLU A 159 8108 7835 5088 262 26 -865 O
ATOM 1199 N ASN A 160 -3.842 43.784 29.888 1.00 47.14 N
ANISOU 1199 N ASN A 160 7339 6275 4298 -346 55 -943 N
ATOM 1200 CA ASN A 160 -2.725 44.706 29.698 1.00 48.86 C
ANISOU 1200 CA ASN A 160 7660 6323 4581 -480 38 -972 C
ATOM 1201 C ASN A 160 -2.475 45.057 28.237 1.00 52.39 C
ANISOU 1201 C ASN A 160 8233 6600 5072 -569 62 -869 C
ATOM 1202 O ASN A 160 -2.045 46.176 27.965 1.00 52.99 O
ANISOU 1202 O ASN A 160 8449 6487 5197 -633 24 -892 O
ATOM 1203 CB ASN A 160 -1.466 44.180 30.351 1.00 50.37 C
ANISOU 1203 CB ASN A 160 7735 6613 4790 -608 71 -989 C
ATOM 1204 CG ASN A 160 -1.490 44.476 31.814 1.00 63.60 C
ANISOU 1204 CG ASN A 160 9352 8380 6432 -537 19 -1122 C
ATOM 1205 OD1 ASN A 160 -1.333 45.624 32.236 1.00 61.98 O
ANISOU 1205 OD1 ASN A 160 9246 8053 6250 -530 -50 -1227 O
ATOM 1206 ND2 ASN A 160 -1.757 43.462 32.610 1.00 49.57 N
ANISOU 1206 ND2 ASN A 160 7420 6817 4596 -475 45 -1120 N
ATOM 1207 N THR A 161 -2.785 44.138 27.293 1.00 49.33 N
ANISOU 1207 N THR A 161 7805 6275 4664 -569 119 -757 N
ATOM 1208 CA THR A 161 -2.696 44.392 25.845 1.00 48.64 C
ANISOU 1208 CA THR A 161 7832 6052 4597 -629 145 -653 C
ATOM 1209 C THR A 161 -3.707 45.515 25.511 1.00 53.86 C
ANISOU 1209 C THR A 161 8655 6559 5252 -508 74 -676 C
ATOM 1210 O THR A 161 -3.337 46.512 24.876 1.00 54.22 O
ANISOU 1210 O THR A 161 8854 6412 5337 -574 53 -650 O
ATOM 1211 CB THR A 161 -2.914 43.092 25.081 1.00 57.05 C
ANISOU 1211 CB THR A 161 8804 7242 5631 -631 210 -554 C
ATOM 1212 OG1 THR A 161 -1.835 42.212 25.389 1.00 55.23 O
ANISOU 1212 OG1 THR A 161 8448 7122 5415 -744 267 -539 O
ATOM 1213 CG2 THR A 161 -3.003 43.288 23.575 1.00 57.89 C
ANISOU 1213 CG2 THR A 161 9021 7237 5736 -663 233 -451 C
ATOM 1214 N LYS A 162 -4.952 45.386 26.023 1.00 50.77 N
ANISOU 1214 N LYS A 162 8226 6254 4810 -332 33 -729 N
ATOM 1215 CA LYS A 162 -6.014 46.392 25.876 1.00 52.28 C
ANISOU 1215 CA LYS A 162 8550 6328 4985 -181 -42 -770 C
ATOM 1216 C LYS A 162 -5.576 47.757 26.411 1.00 58.39 C
ANISOU 1216 C LYS A 162 9461 6919 5807 -197 -112 -865 C
ATOM 1217 O LYS A 162 -5.839 48.773 25.764 1.00 60.72 O
ANISOU 1217 O LYS A 162 9931 7017 6124 -166 -161 -850 O
ATOM 1218 CB LYS A 162 -7.284 45.962 26.616 1.00 54.40 C
ANISOU 1218 CB LYS A 162 8715 6768 5188 5 -70 -830 C
ATOM 1219 CG LYS A 162 -8.013 44.792 25.986 1.00 71.07 C
ANISOU 1219 CG LYS A 162 10718 9029 7256 43 -24 -740 C
ATOM 1220 CD LYS A 162 -9.433 44.833 26.473 1.00 80.38 C
ANISOU 1220 CD LYS A 162 11848 10318 8374 239 -71 -794 C
ATOM 1221 CE LYS A 162 -10.142 43.539 26.261 1.00 81.52 C
ANISOU 1221 CE LYS A 162 11844 10651 8477 267 -30 -725 C
ATOM 1222 NZ LYS A 162 -9.883 42.590 27.371 1.00 68.93 N
ANISOU 1222 NZ LYS A 162 10075 9249 6866 230 9 -745 N
ATOM 1223 N PHE A 163 -4.889 47.786 27.575 1.00 52.44 N
ANISOU 1223 N PHE A 163 8634 6223 5068 -246 -121 -963 N
ATOM 1224 CA PHE A 163 -4.440 49.047 28.179 1.00 52.46 C
ANISOU 1224 CA PHE A 163 8757 6056 5118 -267 -197 -1073 C
ATOM 1225 C PHE A 163 -3.417 49.719 27.284 1.00 55.32 C
ANISOU 1225 C PHE A 163 9256 6205 5558 -451 -188 -998 C
ATOM 1226 O PHE A 163 -3.489 50.934 27.090 1.00 56.70 O
ANISOU 1226 O PHE A 163 9611 6157 5774 -438 -259 -1028 O
ATOM 1227 CB PHE A 163 -3.880 48.855 29.601 1.00 53.01 C
ANISOU 1227 CB PHE A 163 8705 6257 5180 -290 -207 -1192 C
ATOM 1228 CG PHE A 163 -4.820 48.203 30.585 1.00 53.36 C
ANISOU 1228 CG PHE A 163 8607 6529 5139 -118 -212 -1261 C
ATOM 1229 CD1 PHE A 163 -6.171 48.526 30.603 1.00 56.30 C
ANISOU 1229 CD1 PHE A 163 9019 6914 5459 84 -257 -1297 C
ATOM 1230 CD2 PHE A 163 -4.348 47.282 31.513 1.00 54.00 C
ANISOU 1230 CD2 PHE A 163 8511 6820 5188 -157 -171 -1284 C
ATOM 1231 CE1 PHE A 163 -7.039 47.915 31.514 1.00 57.34 C
ANISOU 1231 CE1 PHE A 163 9004 7277 5506 234 -254 -1351 C
ATOM 1232 CE2 PHE A 163 -5.216 46.652 32.401 1.00 56.18 C
ANISOU 1232 CE2 PHE A 163 8652 7314 5380 -9 -168 -1327 C
ATOM 1233 CZ PHE A 163 -6.555 46.985 32.412 1.00 55.18 C
ANISOU 1233 CZ PHE A 163 8558 7207 5201 182 -207 -1361 C
ATOM 1234 N VAL A 164 -2.495 48.926 26.724 1.00 50.99 N
ANISOU 1234 N VAL A 164 8622 5727 5025 -617 -101 -896 N
ATOM 1235 CA VAL A 164 -1.477 49.389 25.770 1.00 52.57 C
ANISOU 1235 CA VAL A 164 8919 5770 5286 -809 -70 -800 C
ATOM 1236 C VAL A 164 -2.150 50.000 24.560 1.00 56.61 C
ANISOU 1236 C VAL A 164 9600 6114 5794 -757 -87 -705 C
ATOM 1237 O VAL A 164 -1.862 51.157 24.233 1.00 57.75 O
ANISOU 1237 O VAL A 164 9918 6032 5993 -820 -136 -696 O
ATOM 1238 CB VAL A 164 -0.454 48.296 25.351 1.00 55.46 C
ANISOU 1238 CB VAL A 164 9141 6281 5651 -966 34 -708 C
ATOM 1239 CG1 VAL A 164 0.442 48.782 24.209 1.00 55.76 C
ANISOU 1239 CG1 VAL A 164 9278 6176 5734 -1145 75 -591 C
ATOM 1240 CG2 VAL A 164 0.406 47.881 26.543 1.00 55.03 C
ANISOU 1240 CG2 VAL A 164 8940 6359 5611 -1039 40 -801 C
ATOM 1241 N LEU A 165 -3.053 49.248 23.917 1.00 53.68 N
ANISOU 1241 N LEU A 165 9186 5850 5360 -642 -55 -637 N
ATOM 1242 CA LEU A 165 -3.739 49.706 22.711 1.00 55.51 C
ANISOU 1242 CA LEU A 165 9566 5950 5573 -581 -71 -541 C
ATOM 1243 C LEU A 165 -4.551 50.975 22.969 1.00 61.86 C
ANISOU 1243 C LEU A 165 10542 6569 6392 -439 -179 -616 C
ATOM 1244 O LEU A 165 -4.372 51.954 22.242 1.00 62.06 O
ANISOU 1244 O LEU A 165 10751 6374 6454 -488 -211 -554 O
ATOM 1245 CB LEU A 165 -4.635 48.603 22.115 1.00 54.84 C
ANISOU 1245 CB LEU A 165 9385 6038 5415 -471 -29 -477 C
ATOM 1246 CG LEU A 165 -3.937 47.312 21.651 1.00 58.77 C
ANISOU 1246 CG LEU A 165 9736 6699 5895 -590 72 -393 C
ATOM 1247 CD1 LEU A 165 -4.958 46.274 21.244 1.00 59.07 C
ANISOU 1247 CD1 LEU A 165 9686 6890 5866 -465 90 -357 C
ATOM 1248 CD2 LEU A 165 -2.994 47.573 20.473 1.00 59.66 C
ANISOU 1248 CD2 LEU A 165 9938 6702 6027 -756 126 -271 C
ATOM 1249 N ARG A 166 -5.381 50.982 24.041 1.00 59.80 N
ANISOU 1249 N ARG A 166 10223 6396 6101 -268 -236 -748 N
ATOM 1250 CA ARG A 166 -6.232 52.111 24.438 1.00 61.51 C
ANISOU 1250 CA ARG A 166 10582 6468 6321 -96 -344 -846 C
ATOM 1251 C ARG A 166 -5.382 53.346 24.746 1.00 68.75 C
ANISOU 1251 C ARG A 166 11657 7141 7323 -205 -406 -902 C
ATOM 1252 O ARG A 166 -5.752 54.450 24.335 1.00 70.12 O
ANISOU 1252 O ARG A 166 12030 7086 7524 -142 -483 -900 O
ATOM 1253 CB ARG A 166 -7.116 51.732 25.636 1.00 63.13 C
ANISOU 1253 CB ARG A 166 10653 6865 6466 92 -375 -982 C
ATOM 1254 CG ARG A 166 -8.130 52.802 26.036 1.00 85.28 C
ANISOU 1254 CG ARG A 166 13588 9558 9257 308 -485 -1093 C
ATOM 1255 CD ARG A 166 -9.144 52.269 27.036 1.00102.60 C
ANISOU 1255 CD ARG A 166 15624 11990 11368 506 -498 -1200 C
ATOM 1256 NE ARG A 166 -9.885 53.355 27.681 1.00112.64 N
ANISOU 1256 NE ARG A 166 17006 13165 12628 704 -606 -1344 N
ATOM 1257 CZ ARG A 166 -9.684 53.762 28.930 1.00122.62 C
ANISOU 1257 CZ ARG A 166 18251 14447 13893 747 -655 -1502 C
ATOM 1258 NH1 ARG A 166 -10.397 54.764 29.430 1.00110.35 N
ANISOU 1258 NH1 ARG A 166 16809 12797 12324 944 -758 -1637 N
ATOM 1259 NH2 ARG A 166 -8.778 53.162 29.695 1.00100.54 N
ANISOU 1259 NH2 ARG A 166 15322 11772 11105 606 -605 -1532 N
ATOM 1260 N TYR A 167 -4.240 53.157 25.456 1.00 64.24 N
ANISOU 1260 N TYR A 167 10999 6614 6795 -371 -378 -950 N
ATOM 1261 CA TYR A 167 -3.325 54.251 25.751 1.00 64.33 C
ANISOU 1261 CA TYR A 167 11142 6405 6895 -508 -436 -1003 C
ATOM 1262 C TYR A 167 -2.781 54.876 24.451 1.00 65.43 C
ANISOU 1262 C TYR A 167 11450 6321 7090 -664 -419 -849 C
ATOM 1263 O TYR A 167 -2.866 56.090 24.289 1.00 65.23 O
ANISOU 1263 O TYR A 167 11629 6035 7118 -654 -505 -864 O
ATOM 1264 CB TYR A 167 -2.163 53.784 26.648 1.00 64.40 C
ANISOU 1264 CB TYR A 167 10998 6540 6932 -669 -399 -1069 C
ATOM 1265 CG TYR A 167 -1.132 54.869 26.866 1.00 67.53 C
ANISOU 1265 CG TYR A 167 11520 6713 7427 -842 -457 -1115 C
ATOM 1266 CD1 TYR A 167 -1.298 55.824 27.864 1.00 70.44 C
ANISOU 1266 CD1 TYR A 167 11981 6956 7827 -763 -572 -1285 C
ATOM 1267 CD2 TYR A 167 -0.029 54.991 26.022 1.00 68.80 C
ANISOU 1267 CD2 TYR A 167 11717 6777 7648 -1084 -401 -985 C
ATOM 1268 CE1 TYR A 167 -0.372 56.843 28.048 1.00 72.76 C
ANISOU 1268 CE1 TYR A 167 12399 7026 8220 -931 -636 -1331 C
ATOM 1269 CE2 TYR A 167 0.903 56.009 26.195 1.00 71.94 C
ANISOU 1269 CE2 TYR A 167 12228 6964 8142 -1261 -457 -1018 C
ATOM 1270 CZ TYR A 167 0.730 56.928 27.216 1.00 81.02 C
ANISOU 1270 CZ TYR A 167 13471 7981 9333 -1188 -578 -1193 C
ATOM 1271 OH TYR A 167 1.636 57.935 27.398 1.00 86.25 O
ANISOU 1271 OH TYR A 167 14249 8423 10098 -1371 -643 -1232 O
ATOM 1272 N LEU A 168 -2.206 54.047 23.555 1.00 61.25 N
ANISOU 1272 N LEU A 168 10834 5896 6544 -805 -311 -701 N
ATOM 1273 CA LEU A 168 -1.603 54.468 22.277 1.00 62.89 C
ANISOU 1273 CA LEU A 168 11168 5944 6784 -967 -273 -535 C
ATOM 1274 C LEU A 168 -2.592 55.130 21.317 1.00 70.70 C
ANISOU 1274 C LEU A 168 12348 6767 7748 -832 -321 -453 C
ATOM 1275 O LEU A 168 -2.212 56.106 20.675 1.00 74.00 O
ANISOU 1275 O LEU A 168 12950 6947 8219 -935 -350 -370 O
ATOM 1276 CB LEU A 168 -0.911 53.305 21.550 1.00 61.08 C
ANISOU 1276 CB LEU A 168 10783 5905 6517 -1104 -143 -409 C
ATOM 1277 CG LEU A 168 0.353 52.715 22.210 1.00 64.52 C
ANISOU 1277 CG LEU A 168 11050 6478 6986 -1287 -83 -446 C
ATOM 1278 CD1 LEU A 168 0.757 51.407 21.527 1.00 62.27 C
ANISOU 1278 CD1 LEU A 168 10602 6411 6646 -1352 37 -340 C
ATOM 1279 CD2 LEU A 168 1.529 53.723 22.226 1.00 65.65 C
ANISOU 1279 CD2 LEU A 168 11295 6427 7224 -1512 -105 -431 C
ATOM 1280 N THR A 169 -3.830 54.620 21.195 1.00 66.84 N
ANISOU 1280 N THR A 169 11816 6401 7180 -613 -330 -466 N
ATOM 1281 CA THR A 169 -4.825 55.234 20.294 1.00 67.78 C
ANISOU 1281 CA THR A 169 12108 6379 7267 -465 -383 -393 C
ATOM 1282 C THR A 169 -5.356 56.544 20.884 1.00 74.68 C
ANISOU 1282 C THR A 169 13167 7021 8188 -335 -516 -505 C
ATOM 1283 O THR A 169 -5.527 57.508 20.143 1.00 77.22 O
ANISOU 1283 O THR A 169 13702 7103 8536 -325 -571 -427 O
ATOM 1284 CB THR A 169 -6.000 54.280 19.950 1.00 71.44 C
ANISOU 1284 CB THR A 169 12459 7055 7632 -272 -358 -376 C
ATOM 1285 OG1 THR A 169 -6.756 53.964 21.126 1.00 73.27 O
ANISOU 1285 OG1 THR A 169 12570 7434 7836 -103 -399 -533 O
ATOM 1286 CG2 THR A 169 -5.552 53.014 19.231 1.00 63.23 C
ANISOU 1286 CG2 THR A 169 11264 6216 6545 -386 -239 -263 C
ATOM 1287 N GLU A 170 -5.607 56.588 22.209 1.00 70.89 N
ANISOU 1287 N GLU A 170 12611 6610 7714 -231 -570 -687 N
ATOM 1288 CA GLU A 170 -6.135 57.777 22.875 1.00 72.79 C
ANISOU 1288 CA GLU A 170 13015 6651 7992 -84 -701 -822 C
ATOM 1289 C GLU A 170 -5.069 58.875 23.029 1.00 79.29 C
ANISOU 1289 C GLU A 170 14004 7194 8928 -276 -755 -836 C
ATOM 1290 O GLU A 170 -5.424 60.047 23.192 1.00 81.85 O
ANISOU 1290 O GLU A 170 14530 7269 9299 -181 -872 -904 O
ATOM 1291 CB GLU A 170 -6.706 57.399 24.241 1.00 73.58 C
ANISOU 1291 CB GLU A 170 12963 6946 8048 85 -733 -1012 C
ATOM 1292 CG GLU A 170 -7.863 58.250 24.723 1.00 84.88 C
ANISOU 1292 CG GLU A 170 14510 8284 9457 356 -854 -1146 C
ATOM 1293 CD GLU A 170 -8.522 57.675 25.960 1.00109.27 C
ANISOU 1293 CD GLU A 170 17413 11630 12475 528 -861 -1310 C
ATOM 1294 OE1 GLU A 170 -9.089 56.562 25.872 1.00106.76 O
ANISOU 1294 OE1 GLU A 170 16906 11582 12077 592 -786 -1268 O
ATOM 1295 OE2 GLU A 170 -8.456 58.331 27.023 1.00105.27 O
ANISOU 1295 OE2 GLU A 170 16950 11057 11992 595 -943 -1481 O
ATOM 1296 N SER A 171 -3.777 58.507 22.969 1.00 75.33 N
ANISOU 1296 N SER A 171 13419 6729 8473 -542 -676 -772 N
ATOM 1297 CA SER A 171 -2.676 59.461 23.122 1.00 77.13 C
ANISOU 1297 CA SER A 171 13776 6719 8813 -758 -719 -779 C
ATOM 1298 C SER A 171 -2.083 59.933 21.796 1.00 83.27 C
ANISOU 1298 C SER A 171 14702 7304 9632 -949 -682 -572 C
ATOM 1299 O SER A 171 -1.721 61.101 21.701 1.00 85.42 O
ANISOU 1299 O SER A 171 15178 7283 9994 -1042 -762 -562 O
ATOM 1300 CB SER A 171 -1.553 58.865 23.968 1.00 79.00 C
ANISOU 1300 CB SER A 171 13821 7119 9078 -940 -665 -853 C
ATOM 1301 OG SER A 171 -1.966 58.580 25.294 1.00 86.45 O
ANISOU 1301 OG SER A 171 14647 8212 9988 -784 -711 -1049 O
ATOM 1302 N TYR A 172 -1.918 59.039 20.806 1.00 79.48 N
ANISOU 1302 N TYR A 172 14122 6987 9090 -1020 -562 -407 N
ATOM 1303 CA TYR A 172 -1.265 59.413 19.551 1.00 81.31 C
ANISOU 1303 CA TYR A 172 14473 7075 9346 -1212 -512 -202 C
ATOM 1304 C TYR A 172 -2.156 59.179 18.318 1.00 88.17 C
ANISOU 1304 C TYR A 172 15410 7964 10125 -1076 -483 -55 C
ATOM 1305 O TYR A 172 -1.651 59.058 17.202 1.00 87.72 O
ANISOU 1305 O TYR A 172 15384 7898 10048 -1219 -405 127 O
ATOM 1306 CB TYR A 172 0.099 58.697 19.444 1.00 81.22 C
ANISOU 1306 CB TYR A 172 14288 7222 9351 -1481 -392 -134 C
ATOM 1307 CG TYR A 172 0.970 59.063 20.627 1.00 83.18 C
ANISOU 1307 CG TYR A 172 14487 7427 9689 -1617 -437 -278 C
ATOM 1308 CD1 TYR A 172 1.397 60.374 20.820 1.00 87.63 C
ANISOU 1308 CD1 TYR A 172 15248 7685 10361 -1732 -534 -301 C
ATOM 1309 CD2 TYR A 172 1.232 58.140 21.638 1.00 81.63 C
ANISOU 1309 CD2 TYR A 172 14062 7483 9469 -1600 -402 -411 C
ATOM 1310 CE1 TYR A 172 2.122 60.743 21.951 1.00 89.44 C
ANISOU 1310 CE1 TYR A 172 15438 7871 10673 -1840 -593 -456 C
ATOM 1311 CE2 TYR A 172 1.961 58.498 22.776 1.00 83.09 C
ANISOU 1311 CE2 TYR A 172 14204 7637 9728 -1701 -456 -559 C
ATOM 1312 CZ TYR A 172 2.407 59.803 22.926 1.00 92.04 C
ANISOU 1312 CZ TYR A 172 15529 8472 10969 -1822 -553 -586 C
ATOM 1313 OH TYR A 172 3.130 60.198 24.029 1.00 90.97 O
ANISOU 1313 OH TYR A 172 15357 8298 10907 -1927 -617 -741 O
ATOM 1314 N GLY A 173 -3.471 59.230 18.530 1.00 87.34 N
ANISOU 1314 N GLY A 173 15342 7877 9969 -799 -555 -137 N
ATOM 1315 CA GLY A 173 -4.473 59.113 17.480 1.00 88.28 C
ANISOU 1315 CA GLY A 173 15532 8007 10002 -632 -555 -27 C
ATOM 1316 C GLY A 173 -4.743 60.454 16.826 1.00 99.30 C
ANISOU 1316 C GLY A 173 17219 9073 11439 -601 -649 59 C
ATOM 1317 O GLY A 173 -4.171 61.476 17.223 1.00100.89 O
ANISOU 1317 O GLY A 173 17568 9025 11742 -708 -720 24 O
ATOM 1318 N THR A 174 -5.613 60.456 15.807 1.00 99.52 N
ANISOU 1318 N THR A 174 17332 9093 11387 -456 -656 174 N
ATOM 1319 CA THR A 174 -5.975 61.655 15.043 1.00103.11 C
ANISOU 1319 CA THR A 174 18069 9247 11863 -400 -744 282 C
ATOM 1320 C THR A 174 -7.055 62.479 15.770 1.00111.70 C
ANISOU 1320 C THR A 174 19285 10186 12972 -129 -894 124 C
ATOM 1321 O THR A 174 -7.193 63.676 15.507 1.00113.42 O
ANISOU 1321 O THR A 174 19757 10094 13243 -94 -995 163 O
ATOM 1322 CB THR A 174 -6.408 61.274 13.611 1.00108.05 C
ANISOU 1322 CB THR A 174 18725 9947 12382 -356 -687 475 C
ATOM 1323 OG1 THR A 174 -7.152 60.047 13.628 1.00100.98 O
ANISOU 1323 OG1 THR A 174 17615 9369 11385 -202 -636 420 O
ATOM 1324 CG2 THR A 174 -5.217 61.151 12.657 1.00106.45 C
ANISOU 1324 CG2 THR A 174 18529 9736 12181 -644 -575 673 C
ATOM 1325 N GLY A 175 -7.767 61.841 16.697 1.00109.78 N
ANISOU 1325 N GLY A 175 18866 10161 12685 55 -906 -52 N
ATOM 1326 CA GLY A 175 -8.837 62.461 17.471 1.00112.06 C
ANISOU 1326 CA GLY A 175 19229 10375 12974 334 -1035 -222 C
ATOM 1327 C GLY A 175 -10.204 61.974 17.040 1.00118.14 C
ANISOU 1327 C GLY A 175 19940 11319 13629 608 -1049 -217 C
ATOM 1328 O GLY A 175 -11.096 61.804 17.880 1.00117.21 O
ANISOU 1328 O GLY A 175 19733 11327 13475 833 -1102 -382 O
ATOM 1329 N GLN A 176 -10.369 61.740 15.714 1.00116.72 N
ANISOU 1329 N GLN A 176 19802 11160 13385 587 -1000 -26 N
ATOM 1330 CA GLN A 176 -11.599 61.231 15.103 1.00116.87 C
ANISOU 1330 CA GLN A 176 19764 11352 13291 819 -1008 4 C
ATOM 1331 C GLN A 176 -11.875 59.806 15.583 1.00120.64 C
ANISOU 1331 C GLN A 176 19936 12201 13702 844 -920 -75 C
ATOM 1332 O GLN A 176 -10.935 59.071 15.899 1.00118.84 O
ANISOU 1332 O GLN A 176 19558 12097 13499 633 -821 -73 O
ATOM 1333 CB GLN A 176 -11.506 61.276 13.571 1.00118.80 C
ANISOU 1333 CB GLN A 176 20127 11531 13483 754 -972 231 C
ATOM 1334 N ASP A 177 -13.165 59.420 15.619 1.00118.55 N
ANISOU 1334 N ASP A 177 19578 12112 13352 1099 -958 -141 N
ATOM 1335 CA ASP A 177 -13.677 58.125 16.089 1.00116.82 C
ANISOU 1335 CA ASP A 177 19080 12239 13068 1159 -895 -219 C
ATOM 1336 C ASP A 177 -13.053 56.889 15.387 1.00119.13 C
ANISOU 1336 C ASP A 177 19215 12726 13325 961 -763 -99 C
ATOM 1337 O ASP A 177 -13.317 55.762 15.821 1.00117.46 O
ANISOU 1337 O ASP A 177 18773 12781 13074 973 -706 -159 O
ATOM 1338 CB ASP A 177 -15.207 58.082 15.957 1.00119.30 C
ANISOU 1338 CB ASP A 177 19358 12677 13295 1458 -967 -269 C
ATOM 1339 CG ASP A 177 -15.922 59.020 16.909 1.00132.39 C
ANISOU 1339 CG ASP A 177 21093 14238 14971 1689 -1085 -434 C
ATOM 1340 OD1 ASP A 177 -15.976 58.708 18.121 1.00132.74 O
ANISOU 1340 OD1 ASP A 177 20988 14423 15025 1723 -1078 -589 O
ATOM 1341 OD2 ASP A 177 -16.437 60.061 16.442 1.00139.54 O
ANISOU 1341 OD2 ASP A 177 22208 14936 15873 1849 -1188 -410 O
ATOM 1342 N ILE A 178 -12.204 57.092 14.349 1.00115.37 N
ANISOU 1342 N ILE A 178 18858 12118 12861 778 -715 67 N
ATOM 1343 CA ILE A 178 -11.497 56.015 13.640 1.00113.07 C
ANISOU 1343 CA ILE A 178 18437 11991 12534 588 -591 179 C
ATOM 1344 C ILE A 178 -10.459 55.330 14.569 1.00114.04 C
ANISOU 1344 C ILE A 178 18389 12226 12716 396 -509 105 C
ATOM 1345 O ILE A 178 -10.139 54.154 14.357 1.00111.51 O
ANISOU 1345 O ILE A 178 17891 12118 12359 302 -415 136 O
ATOM 1346 CB ILE A 178 -10.824 56.561 12.363 1.00117.51 C
ANISOU 1346 CB ILE A 178 19184 12375 13090 448 -564 371 C
ATOM 1347 N ASP A 179 -9.948 56.074 15.596 1.00110.14 N
ANISOU 1347 N ASP A 179 17953 11584 12310 346 -552 4 N
ATOM 1348 CA ASP A 179 -8.973 55.601 16.596 1.00107.97 C
ANISOU 1348 CA ASP A 179 17534 11396 12095 179 -493 -81 C
ATOM 1349 C ASP A 179 -9.623 54.626 17.584 1.00107.24 C
ANISOU 1349 C ASP A 179 17214 11569 11964 303 -482 -218 C
ATOM 1350 O ASP A 179 -8.937 53.767 18.147 1.00105.96 O
ANISOU 1350 O ASP A 179 16879 11565 11816 175 -407 -253 O
ATOM 1351 CB ASP A 179 -8.353 56.777 17.383 1.00111.59 C
ANISOU 1351 CB ASP A 179 18135 11610 12653 110 -563 -160 C
ATOM 1352 CG ASP A 179 -7.878 57.976 16.579 1.00122.75 C
ANISOU 1352 CG ASP A 179 19806 12713 14119 14 -605 -40 C
ATOM 1353 OD1 ASP A 179 -7.231 57.772 15.523 1.00122.08 O
ANISOU 1353 OD1 ASP A 179 19750 12616 14019 -150 -528 128 O
ATOM 1354 OD2 ASP A 179 -8.074 59.113 17.050 1.00131.56 O
ANISOU 1354 OD2 ASP A 179 21095 13598 15296 90 -713 -115 O
ATOM 1355 N ASP A 180 -10.946 54.787 17.810 1.00100.66 N
ANISOU 1355 N ASP A 180 16382 10785 11081 553 -558 -294 N
ATOM 1356 CA ASP A 180 -11.744 53.951 18.702 1.00 97.31 C
ANISOU 1356 CA ASP A 180 15750 10614 10609 692 -555 -413 C
ATOM 1357 C ASP A 180 -11.868 52.515 18.184 1.00 93.73 C
ANISOU 1357 C ASP A 180 15104 10412 10096 641 -464 -340 C
ATOM 1358 O ASP A 180 -11.999 51.618 19.002 1.00 92.09 O
ANISOU 1358 O ASP A 180 14700 10416 9873 650 -428 -415 O
ATOM 1359 CB ASP A 180 -13.162 54.542 18.896 1.00100.46 C
ANISOU 1359 CB ASP A 180 16205 11005 10962 976 -660 -494 C
ATOM 1360 CG ASP A 180 -13.248 55.954 19.462 1.00115.90 C
ANISOU 1360 CG ASP A 180 18351 12719 12969 1079 -768 -593 C
ATOM 1361 OD1 ASP A 180 -12.239 56.434 20.034 1.00117.01 O
ANISOU 1361 OD1 ASP A 180 18549 12722 13186 934 -769 -638 O
ATOM 1362 OD2 ASP A 180 -14.334 56.565 19.367 1.00124.55 O
ANISOU 1362 OD2 ASP A 180 19531 13766 14026 1313 -858 -635 O
ATOM 1363 N ARG A 181 -11.833 52.301 16.847 1.00 85.98 N
ANISOU 1363 N ARG A 181 14183 9408 9079 592 -431 -196 N
ATOM 1364 CA ARG A 181 -12.019 51.001 16.180 1.00 81.91 C
ANISOU 1364 CA ARG A 181 13513 9106 8502 559 -359 -126 C
ATOM 1365 C ARG A 181 -10.989 49.932 16.546 1.00 81.11 C
ANISOU 1365 C ARG A 181 13247 9144 8428 367 -259 -125 C
ATOM 1366 O ARG A 181 -11.365 48.763 16.639 1.00 78.25 O
ANISOU 1366 O ARG A 181 12708 8995 8028 387 -221 -138 O
ATOM 1367 CB ARG A 181 -12.050 51.159 14.668 1.00 79.97 C
ANISOU 1367 CB ARG A 181 13394 8781 8210 539 -351 23 C
ATOM 1368 CG ARG A 181 -13.332 51.790 14.196 1.00 81.66 C
ANISOU 1368 CG ARG A 181 13711 8947 8370 765 -446 26 C
ATOM 1369 CD ARG A 181 -13.529 51.560 12.726 1.00 80.11 C
ANISOU 1369 CD ARG A 181 13574 8763 8100 766 -430 163 C
ATOM 1370 NE ARG A 181 -14.752 52.215 12.284 1.00 80.53 N
ANISOU 1370 NE ARG A 181 13731 8767 8099 993 -530 166 N
ATOM 1371 CZ ARG A 181 -15.185 52.240 11.031 1.00 83.26 C
ANISOU 1371 CZ ARG A 181 14156 9108 8369 1052 -548 274 C
ATOM 1372 NH1 ARG A 181 -14.505 51.620 10.073 1.00 64.54 N
ANISOU 1372 NH1 ARG A 181 11772 6786 5962 902 -469 387 N
ATOM 1373 NH2 ARG A 181 -16.312 52.869 10.727 1.00 63.35 N
ANISOU 1373 NH2 ARG A 181 11724 6545 5800 1272 -647 266 N
ATOM 1374 N ILE A 182 -9.713 50.309 16.747 1.00 77.40 N
ANISOU 1374 N ILE A 182 12829 8556 8023 184 -220 -108 N
ATOM 1375 CA ILE A 182 -8.656 49.369 17.162 1.00 75.92 C
ANISOU 1375 CA ILE A 182 12487 8496 7863 8 -130 -113 C
ATOM 1376 C ILE A 182 -9.028 48.808 18.574 1.00 77.42 C
ANISOU 1376 C ILE A 182 12506 8848 8060 82 -142 -250 C
ATOM 1377 O ILE A 182 -8.829 47.612 18.852 1.00 75.72 O
ANISOU 1377 O ILE A 182 12114 8823 7832 29 -81 -256 O
ATOM 1378 CB ILE A 182 -7.238 50.045 17.138 1.00 80.13 C
ANISOU 1378 CB ILE A 182 13118 8862 8467 -196 -99 -74 C
ATOM 1379 CG1 ILE A 182 -6.875 50.613 15.742 1.00 81.42 C
ANISOU 1379 CG1 ILE A 182 13449 8875 8614 -276 -81 78 C
ATOM 1380 CG2 ILE A 182 -6.130 49.106 17.649 1.00 79.79 C
ANISOU 1380 CG2 ILE A 182 12907 8958 8452 -365 -13 -91 C
ATOM 1381 CD1 ILE A 182 -7.146 52.130 15.576 1.00 89.81 C
ANISOU 1381 CD1 ILE A 182 14747 9668 9709 -218 -173 94 C
ATOM 1382 N VAL A 183 -9.629 49.679 19.423 1.00 72.31 N
ANISOU 1382 N VAL A 183 11919 8127 7427 218 -226 -357 N
ATOM 1383 CA VAL A 183 -10.081 49.353 20.778 1.00 70.52 C
ANISOU 1383 CA VAL A 183 11552 8050 7194 313 -247 -490 C
ATOM 1384 C VAL A 183 -11.409 48.590 20.696 1.00 73.37 C
ANISOU 1384 C VAL A 183 11791 8606 7482 479 -257 -497 C
ATOM 1385 O VAL A 183 -11.508 47.495 21.249 1.00 72.73 O
ANISOU 1385 O VAL A 183 11523 8731 7382 460 -210 -517 O
ATOM 1386 CB VAL A 183 -10.205 50.638 21.648 1.00 74.99 C
ANISOU 1386 CB VAL A 183 12240 8458 7794 404 -336 -608 C
ATOM 1387 CG1 VAL A 183 -10.846 50.346 22.995 1.00 74.82 C
ANISOU 1387 CG1 VAL A 183 12075 8612 7742 539 -362 -747 C
ATOM 1388 CG2 VAL A 183 -8.857 51.315 21.831 1.00 75.17 C
ANISOU 1388 CG2 VAL A 183 12362 8301 7897 217 -328 -609 C
ATOM 1389 N GLU A 184 -12.405 49.156 19.981 1.00 69.35 N
ANISOU 1389 N GLU A 184 11386 8031 6934 634 -320 -473 N
ATOM 1390 CA GLU A 184 -13.763 48.629 19.815 1.00 69.28 C
ANISOU 1390 CA GLU A 184 11277 8190 6855 806 -347 -482 C
ATOM 1391 C GLU A 184 -13.833 47.282 19.103 1.00 74.15 C
ANISOU 1391 C GLU A 184 11759 8975 7440 729 -281 -395 C
ATOM 1392 O GLU A 184 -14.904 46.687 19.107 1.00 75.01 O
ANISOU 1392 O GLU A 184 11754 9249 7498 845 -299 -408 O
ATOM 1393 CB GLU A 184 -14.647 49.633 19.064 1.00 72.14 C
ANISOU 1393 CB GLU A 184 11807 8417 7187 974 -432 -464 C
ATOM 1394 N ALA A 185 -12.732 46.796 18.502 1.00 70.67 N
ANISOU 1394 N ALA A 185 11327 8500 7027 539 -208 -312 N
ATOM 1395 CA ALA A 185 -12.719 45.509 17.797 1.00 69.83 C
ANISOU 1395 CA ALA A 185 11105 8536 6892 466 -149 -238 C
ATOM 1396 C ALA A 185 -12.481 44.341 18.744 1.00 72.80 C
ANISOU 1396 C ALA A 185 11280 9098 7284 399 -98 -282 C
ATOM 1397 O ALA A 185 -12.865 43.215 18.411 1.00 71.05 O
ANISOU 1397 O ALA A 185 10938 9021 7036 387 -72 -248 O
ATOM 1398 CB ALA A 185 -11.663 45.510 16.702 1.00 70.76 C
ANISOU 1398 CB ALA A 185 11321 8544 7021 311 -95 -133 C
ATOM 1399 N ASN A 186 -11.847 44.593 19.911 1.00 70.30 N
ANISOU 1399 N ASN A 186 10931 8772 7008 354 -87 -354 N
ATOM 1400 CA ASN A 186 -11.561 43.566 20.928 1.00 69.67 C
ANISOU 1400 CA ASN A 186 10669 8862 6940 295 -42 -394 C
ATOM 1401 C ASN A 186 -12.816 42.809 21.404 1.00 73.06 C
ANISOU 1401 C ASN A 186 10943 9491 7323 417 -62 -424 C
ATOM 1402 O ASN A 186 -12.743 41.585 21.412 1.00 71.86 O
ANISOU 1402 O ASN A 186 10659 9474 7171 348 -17 -387 O
ATOM 1403 CB ASN A 186 -10.815 44.139 22.141 1.00 71.48 C
ANISOU 1403 CB ASN A 186 10903 9049 7208 257 -45 -478 C
ATOM 1404 CG ASN A 186 -9.326 44.000 21.980 1.00 99.60 C
ANISOU 1404 CG ASN A 186 14489 12534 10819 67 14 -438 C
ATOM 1405 OD1 ASN A 186 -8.662 44.841 21.365 1.00 99.85 O
ANISOU 1405 OD1 ASN A 186 14669 12388 10880 -2 10 -404 O
ATOM 1406 ND2 ASN A 186 -8.783 42.887 22.450 1.00 90.41 N
ANISOU 1406 ND2 ASN A 186 13178 11509 9664 -24 72 -429 N
ATOM 1407 N PRO A 187 -13.967 43.441 21.763 1.00 70.96 N
ANISOU 1407 N PRO A 187 10686 9257 7020 592 -128 -485 N
ATOM 1408 CA PRO A 187 -15.127 42.640 22.204 1.00 70.07 C
ANISOU 1408 CA PRO A 187 10402 9361 6862 689 -138 -503 C
ATOM 1409 C PRO A 187 -15.583 41.643 21.156 1.00 69.85 C
ANISOU 1409 C PRO A 187 10315 9407 6816 654 -123 -418 C
ATOM 1410 O PRO A 187 -16.142 40.598 21.503 1.00 68.83 O
ANISOU 1410 O PRO A 187 10021 9456 6673 645 -106 -408 O
ATOM 1411 CB PRO A 187 -16.219 43.694 22.452 1.00 73.65 C
ANISOU 1411 CB PRO A 187 10910 9802 7272 892 -216 -575 C
ATOM 1412 CG PRO A 187 -15.471 44.937 22.755 1.00 79.34 C
ANISOU 1412 CG PRO A 187 11795 10324 8028 892 -242 -629 C
ATOM 1413 CD PRO A 187 -14.267 44.889 21.860 1.00 74.74 C
ANISOU 1413 CD PRO A 187 11319 9584 7496 714 -197 -545 C
ATOM 1414 N LEU A 188 -15.325 41.964 19.874 1.00 64.02 N
ANISOU 1414 N LEU A 188 9715 8531 6078 628 -131 -355 N
ATOM 1415 CA LEU A 188 -15.700 41.127 18.754 1.00 61.81 C
ANISOU 1415 CA LEU A 188 9406 8303 5775 601 -126 -283 C
ATOM 1416 C LEU A 188 -14.791 39.895 18.655 1.00 58.16 C
ANISOU 1416 C LEU A 188 8860 7890 5347 433 -55 -237 C
ATOM 1417 O LEU A 188 -15.315 38.788 18.598 1.00 56.65 O
ANISOU 1417 O LEU A 188 8540 7838 5148 419 -51 -220 O
ATOM 1418 CB LEU A 188 -15.715 41.932 17.452 1.00 63.66 C
ANISOU 1418 CB LEU A 188 9820 8381 5985 638 -157 -231 C
ATOM 1419 CG LEU A 188 -16.588 41.331 16.363 1.00 70.46 C
ANISOU 1419 CG LEU A 188 10650 9322 6798 686 -186 -183 C
ATOM 1420 CD1 LEU A 188 -18.015 41.156 16.861 1.00 71.83 C
ANISOU 1420 CD1 LEU A 188 10695 9660 6937 830 -242 -234 C
ATOM 1421 CD2 LEU A 188 -16.527 42.154 15.068 1.00 73.37 C
ANISOU 1421 CD2 LEU A 188 11205 9541 7132 725 -216 -123 C
ATOM 1422 N LEU A 189 -13.457 40.065 18.701 1.00 51.04 N
ANISOU 1422 N LEU A 189 8023 6883 4485 308 -4 -222 N
ATOM 1423 CA LEU A 189 -12.525 38.923 18.673 1.00 49.28 C
ANISOU 1423 CA LEU A 189 7719 6711 4293 164 62 -187 C
ATOM 1424 C LEU A 189 -12.710 38.002 19.887 1.00 51.13 C
ANISOU 1424 C LEU A 189 7779 7101 4545 149 78 -222 C
ATOM 1425 O LEU A 189 -12.603 36.775 19.766 1.00 49.44 O
ANISOU 1425 O LEU A 189 7466 6974 4344 80 105 -189 O
ATOM 1426 CB LEU A 189 -11.070 39.400 18.615 1.00 49.36 C
ANISOU 1426 CB LEU A 189 7820 6595 4340 43 111 -172 C
ATOM 1427 CG LEU A 189 -10.689 40.275 17.404 1.00 54.61 C
ANISOU 1427 CG LEU A 189 8659 7103 4989 26 109 -117 C
ATOM 1428 CD1 LEU A 189 -9.345 40.959 17.632 1.00 55.74 C
ANISOU 1428 CD1 LEU A 189 8880 7124 5173 -91 149 -113 C
ATOM 1429 CD2 LEU A 189 -10.679 39.491 16.136 1.00 51.69 C
ANISOU 1429 CD2 LEU A 189 8291 6764 4585 -8 130 -49 C
ATOM 1430 N GLU A 190 -12.992 38.609 21.054 1.00 46.26 N
ANISOU 1430 N GLU A 190 7133 6518 3926 218 57 -287 N
ATOM 1431 CA GLU A 190 -13.239 37.925 22.327 1.00 44.65 C
ANISOU 1431 CA GLU A 190 6769 6472 3723 223 69 -319 C
ATOM 1432 C GLU A 190 -14.561 37.165 22.324 1.00 48.44 C
ANISOU 1432 C GLU A 190 7124 7109 4171 294 42 -303 C
ATOM 1433 O GLU A 190 -14.628 36.096 22.915 1.00 48.14 O
ANISOU 1433 O GLU A 190 6949 7198 4143 241 67 -282 O
ATOM 1434 CB GLU A 190 -13.214 38.906 23.496 1.00 45.74 C
ANISOU 1434 CB GLU A 190 6921 6607 3853 293 50 -402 C
ATOM 1435 CG GLU A 190 -11.827 39.478 23.724 1.00 56.25 C
ANISOU 1435 CG GLU A 190 8339 7808 5225 195 78 -423 C
ATOM 1436 CD GLU A 190 -11.605 40.127 25.076 1.00 76.82 C
ANISOU 1436 CD GLU A 190 10926 10436 7826 236 63 -514 C
ATOM 1437 OE1 GLU A 190 -12.542 40.140 25.907 1.00 60.37 O
ANISOU 1437 OE1 GLU A 190 8755 8482 5700 351 37 -563 O
ATOM 1438 OE2 GLU A 190 -10.478 40.614 25.310 1.00 68.76 O
ANISOU 1438 OE2 GLU A 190 9971 9311 6842 150 78 -538 O
ATOM 1439 N ALA A 191 -15.598 37.683 21.663 1.00 45.60 N
ANISOU 1439 N ALA A 191 6808 6743 3774 407 -11 -308 N
ATOM 1440 CA ALA A 191 -16.844 36.923 21.579 1.00 47.13 C
ANISOU 1440 CA ALA A 191 6871 7096 3939 460 -39 -291 C
ATOM 1441 C ALA A 191 -16.623 35.552 20.861 1.00 51.25 C
ANISOU 1441 C ALA A 191 7334 7647 4491 337 -15 -223 C
ATOM 1442 O ALA A 191 -17.176 34.544 21.290 1.00 52.36 O
ANISOU 1442 O ALA A 191 7328 7929 4638 307 -13 -202 O
ATOM 1443 CB ALA A 191 -17.900 37.727 20.839 1.00 48.50 C
ANISOU 1443 CB ALA A 191 7111 7250 4067 601 -104 -306 C
ATOM 1444 N PHE A 192 -15.773 35.529 19.820 1.00 44.25 N
ANISOU 1444 N PHE A 192 6563 6629 3623 264 3 -190 N
ATOM 1445 CA PHE A 192 -15.533 34.362 18.968 1.00 42.64 C
ANISOU 1445 CA PHE A 192 6334 6430 3439 170 17 -140 C
ATOM 1446 C PHE A 192 -14.302 33.529 19.307 1.00 45.17 C
ANISOU 1446 C PHE A 192 6624 6731 3807 39 77 -120 C
ATOM 1447 O PHE A 192 -14.262 32.380 18.886 1.00 42.60 O
ANISOU 1447 O PHE A 192 6244 6438 3502 -26 81 -89 O
ATOM 1448 CB PHE A 192 -15.415 34.825 17.491 1.00 44.38 C
ANISOU 1448 CB PHE A 192 6697 6535 3630 187 0 -117 C
ATOM 1449 CG PHE A 192 -16.722 35.317 16.923 1.00 45.65 C
ANISOU 1449 CG PHE A 192 6872 6732 3740 314 -70 -126 C
ATOM 1450 CD1 PHE A 192 -17.625 34.429 16.346 1.00 48.57 C
ANISOU 1450 CD1 PHE A 192 7157 7201 4096 321 -110 -112 C
ATOM 1451 CD2 PHE A 192 -17.076 36.660 17.013 1.00 48.03 C
ANISOU 1451 CD2 PHE A 192 7268 6972 4009 430 -102 -152 C
ATOM 1452 CE1 PHE A 192 -18.858 34.880 15.842 1.00 50.26 C
ANISOU 1452 CE1 PHE A 192 7370 7467 4258 443 -180 -124 C
ATOM 1453 CE2 PHE A 192 -18.313 37.110 16.539 1.00 52.09 C
ANISOU 1453 CE2 PHE A 192 7788 7531 4472 564 -171 -163 C
ATOM 1454 CZ PHE A 192 -19.189 36.218 15.935 1.00 50.69 C
ANISOU 1454 CZ PHE A 192 7517 7467 4276 570 -208 -148 C
ATOM 1455 N GLY A 193 -13.311 34.106 20.010 1.00 42.03 N
ANISOU 1455 N GLY A 193 6265 6276 3428 6 117 -141 N
ATOM 1456 CA GLY A 193 -12.056 33.429 20.331 1.00 40.33 C
ANISOU 1456 CA GLY A 193 6025 6045 3255 -109 172 -125 C
ATOM 1457 C GLY A 193 -11.754 33.204 21.799 1.00 44.71 C
ANISOU 1457 C GLY A 193 6479 6682 3829 -130 195 -146 C
ATOM 1458 O GLY A 193 -10.772 32.529 22.120 1.00 43.71 O
ANISOU 1458 O GLY A 193 6315 6557 3734 -216 235 -131 O
ATOM 1459 N ASN A 194 -12.600 33.735 22.701 1.00 41.21 N
ANISOU 1459 N ASN A 194 5983 6317 3358 -42 167 -182 N
ATOM 1460 CA ASN A 194 -12.452 33.561 24.140 1.00 40.83 C
ANISOU 1460 CA ASN A 194 5834 6372 3309 -44 185 -204 C
ATOM 1461 C ASN A 194 -13.507 32.634 24.709 1.00 43.49 C
ANISOU 1461 C ASN A 194 6022 6872 3632 -22 171 -173 C
ATOM 1462 O ASN A 194 -14.632 32.551 24.190 1.00 45.05 O
ANISOU 1462 O ASN A 194 6194 7116 3808 33 133 -162 O
ATOM 1463 CB ASN A 194 -12.473 34.894 24.887 1.00 42.87 C
ANISOU 1463 CB ASN A 194 6143 6607 3540 38 169 -278 C
ATOM 1464 CG ASN A 194 -11.229 35.724 24.669 1.00 56.06 C
ANISOU 1464 CG ASN A 194 7938 8126 5236 -17 188 -305 C
ATOM 1465 OD1 ASN A 194 -10.575 35.663 23.625 1.00 42.47 O
ANISOU 1465 OD1 ASN A 194 6300 6297 3538 -86 207 -269 O
ATOM 1466 ND2 ASN A 194 -10.874 36.520 25.649 1.00 48.05 N
ANISOU 1466 ND2 ASN A 194 6936 7108 4214 10 183 -371 N
ATOM 1467 N ALA A 195 -13.130 31.914 25.767 1.00 37.94 N
ANISOU 1467 N ALA A 195 5216 6262 2939 -72 199 -154 N
ATOM 1468 CA ALA A 195 -14.035 30.982 26.418 1.00 39.64 C
ANISOU 1468 CA ALA A 195 5284 6637 3142 -71 193 -108 C
ATOM 1469 C ALA A 195 -13.708 30.808 27.889 1.00 44.18 C
ANISOU 1469 C ALA A 195 5764 7326 3696 -76 221 -109 C
ATOM 1470 O ALA A 195 -12.564 31.025 28.288 1.00 42.26 O
ANISOU 1470 O ALA A 195 5562 7028 3465 -112 247 -134 O
ATOM 1471 CB ALA A 195 -13.981 29.637 25.725 1.00 39.73 C
ANISOU 1471 CB ALA A 195 5263 6631 3203 -166 193 -36 C
ATOM 1472 N LYS A 196 -14.712 30.385 28.685 1.00 39.57 N
ANISOU 1472 N LYS A 196 5046 6914 3074 -43 216 -79 N
ATOM 1473 CA LYS A 196 -14.513 30.042 30.082 1.00 39.88 C
ANISOU 1473 CA LYS A 196 4980 7090 3082 -50 244 -60 C
ATOM 1474 C LYS A 196 -13.711 28.735 30.216 1.00 46.32 C
ANISOU 1474 C LYS A 196 5759 7889 3951 -171 269 23 C
ATOM 1475 O LYS A 196 -14.183 27.670 29.789 1.00 47.17 O
ANISOU 1475 O LYS A 196 5815 8011 4095 -235 259 101 O
ATOM 1476 CB LYS A 196 -15.861 29.910 30.808 1.00 42.30 C
ANISOU 1476 CB LYS A 196 5145 7600 3326 14 236 -37 C
ATOM 1477 CG LYS A 196 -15.744 29.747 32.326 1.00 43.57 C
ANISOU 1477 CG LYS A 196 5196 7927 3430 28 266 -23 C
ATOM 1478 CD LYS A 196 -16.999 29.112 32.881 1.00 34.75 C
ANISOU 1478 CD LYS A 196 3917 7017 2269 35 270 51 C
ATOM 1479 CE LYS A 196 -17.085 29.064 34.398 1.00 38.50 C
ANISOU 1479 CE LYS A 196 4272 7696 2660 75 302 64 C
ATOM 1480 NZ LYS A 196 -16.076 28.141 34.983 1.00 41.47 N
ANISOU 1480 NZ LYS A 196 4631 8061 3063 -25 331 137 N
ATOM 1481 N THR A 197 -12.484 28.831 30.780 1.00 42.51 N
ANISOU 1481 N THR A 197 5308 7369 3475 -200 295 1 N
ATOM 1482 CA THR A 197 -11.652 27.681 31.148 1.00 42.04 C
ANISOU 1482 CA THR A 197 5207 7312 3453 -289 317 73 C
ATOM 1483 C THR A 197 -11.593 27.655 32.683 1.00 47.36 C
ANISOU 1483 C THR A 197 5780 8149 4065 -261 336 83 C
ATOM 1484 O THR A 197 -11.945 28.660 33.294 1.00 46.98 O
ANISOU 1484 O THR A 197 5722 8177 3953 -173 333 11 O
ATOM 1485 CB THR A 197 -10.279 27.732 30.549 1.00 44.69 C
ANISOU 1485 CB THR A 197 5642 7499 3839 -341 330 45 C
ATOM 1486 OG1 THR A 197 -9.598 28.820 31.175 1.00 45.54 O
ANISOU 1486 OG1 THR A 197 5785 7606 3911 -301 341 -38 O
ATOM 1487 CG2 THR A 197 -10.283 27.839 28.993 1.00 40.83 C
ANISOU 1487 CG2 THR A 197 5259 6860 3396 -363 316 31 C
ATOM 1488 N VAL A 198 -11.088 26.573 33.305 1.00 45.35 N
ANISOU 1488 N VAL A 198 5463 7942 3826 -324 353 164 N
ATOM 1489 CA VAL A 198 -11.003 26.512 34.777 1.00 47.16 C
ANISOU 1489 CA VAL A 198 5595 8337 3984 -294 371 183 C
ATOM 1490 C VAL A 198 -10.046 27.593 35.338 1.00 50.45 C
ANISOU 1490 C VAL A 198 6063 8742 4363 -244 376 73 C
ATOM 1491 O VAL A 198 -10.314 28.097 36.410 1.00 49.70 O
ANISOU 1491 O VAL A 198 5907 8790 4186 -176 380 37 O
ATOM 1492 CB VAL A 198 -10.636 25.109 35.321 1.00 52.77 C
ANISOU 1492 CB VAL A 198 6236 9095 4717 -370 383 305 C
ATOM 1493 CG1 VAL A 198 -11.762 24.117 35.073 1.00 52.54 C
ANISOU 1493 CG1 VAL A 198 6135 9113 4712 -420 373 417 C
ATOM 1494 CG2 VAL A 198 -9.325 24.593 34.726 1.00 52.84 C
ANISOU 1494 CG2 VAL A 198 6325 8950 4803 -432 383 308 C
ATOM 1495 N ARG A 199 -9.000 28.014 34.576 1.00 48.05 N
ANISOU 1495 N ARG A 199 5868 8275 4114 -276 374 13 N
ATOM 1496 CA ARG A 199 -8.014 29.009 35.041 1.00 46.37 C
ANISOU 1496 CA ARG A 199 5703 8036 3878 -252 374 -90 C
ATOM 1497 C ARG A 199 -8.358 30.457 34.668 1.00 48.99 C
ANISOU 1497 C ARG A 199 6122 8298 4194 -186 352 -202 C
ATOM 1498 O ARG A 199 -7.739 31.370 35.201 1.00 49.57 O
ANISOU 1498 O ARG A 199 6231 8362 4242 -158 343 -295 O
ATOM 1499 CB ARG A 199 -6.633 28.675 34.500 1.00 41.23 C
ANISOU 1499 CB ARG A 199 5109 7264 3294 -332 385 -89 C
ATOM 1500 CG ARG A 199 -5.966 27.473 35.151 1.00 48.86 C
ANISOU 1500 CG ARG A 199 5998 8299 4266 -375 399 -7 C
ATOM 1501 CD ARG A 199 -4.894 26.955 34.196 1.00 57.34 C
ANISOU 1501 CD ARG A 199 7132 9237 5418 -447 409 8 C
ATOM 1502 NE ARG A 199 -3.942 26.007 34.784 1.00 63.92 N
ANISOU 1502 NE ARG A 199 7911 10115 6260 -476 417 59 N
ATOM 1503 CZ ARG A 199 -4.188 24.717 35.006 1.00 89.44 C
ANISOU 1503 CZ ARG A 199 11087 13388 9508 -493 414 167 C
ATOM 1504 NH1 ARG A 199 -5.385 24.204 34.741 1.00 92.26 N
ANISOU 1504 NH1 ARG A 199 11424 13759 9872 -496 406 237 N
ATOM 1505 NH2 ARG A 199 -3.240 23.930 35.502 1.00 72.05 N
ANISOU 1505 NH2 ARG A 199 8849 11213 7315 -508 416 209 N
ATOM 1506 N ASN A 200 -9.300 30.679 33.747 1.00 44.35 N
ANISOU 1506 N ASN A 200 5576 7653 3622 -160 339 -195 N
ATOM 1507 CA ASN A 200 -9.666 32.042 33.345 1.00 43.69 C
ANISOU 1507 CA ASN A 200 5587 7490 3524 -87 312 -293 C
ATOM 1508 C ASN A 200 -11.061 32.047 32.723 1.00 48.06 C
ANISOU 1508 C ASN A 200 6128 8067 4065 -30 294 -266 C
ATOM 1509 O ASN A 200 -11.332 31.306 31.781 1.00 47.95 O
ANISOU 1509 O ASN A 200 6121 8000 4097 -84 296 -196 O
ATOM 1510 CB ASN A 200 -8.607 32.643 32.385 1.00 40.34 C
ANISOU 1510 CB ASN A 200 5298 6869 3163 -147 311 -335 C
ATOM 1511 CG ASN A 200 -8.811 34.088 32.005 1.00 52.65 C
ANISOU 1511 CG ASN A 200 6972 8317 4714 -84 280 -428 C
ATOM 1512 OD1 ASN A 200 -9.840 34.686 32.314 1.00 39.48 O
ANISOU 1512 OD1 ASN A 200 5296 6708 2997 22 252 -471 O
ATOM 1513 ND2 ASN A 200 -7.885 34.655 31.221 1.00 37.42 N
ANISOU 1513 ND2 ASN A 200 5159 6222 2836 -148 282 -453 N
ATOM 1514 N ASN A 201 -11.951 32.872 33.271 1.00 44.84 N
ANISOU 1514 N ASN A 201 5697 7748 3590 86 272 -330 N
ATOM 1515 CA ASN A 201 -13.330 32.992 32.821 1.00 44.31 C
ANISOU 1515 CA ASN A 201 5602 7736 3499 161 250 -318 C
ATOM 1516 C ASN A 201 -13.393 33.559 31.432 1.00 47.68 C
ANISOU 1516 C ASN A 201 6161 7980 3973 164 225 -338 C
ATOM 1517 O ASN A 201 -14.318 33.229 30.696 1.00 47.70 O
ANISOU 1517 O ASN A 201 6144 7999 3981 179 209 -295 O
ATOM 1518 CB ASN A 201 -14.145 33.865 33.767 1.00 41.49 C
ANISOU 1518 CB ASN A 201 5195 7517 3051 304 232 -400 C
ATOM 1519 CG ASN A 201 -14.488 33.194 35.052 1.00 51.24 C
ANISOU 1519 CG ASN A 201 6272 8982 4217 318 259 -359 C
ATOM 1520 OD1 ASN A 201 -14.447 31.977 35.185 1.00 52.52 O
ANISOU 1520 OD1 ASN A 201 6344 9213 4397 225 288 -248 O
ATOM 1521 ND2 ASN A 201 -14.815 33.980 36.028 1.00 41.45 N
ANISOU 1521 ND2 ASN A 201 4998 7860 2891 437 249 -448 N
ATOM 1522 N ASN A 202 -12.423 34.424 31.087 1.00 42.76 N
ANISOU 1522 N ASN A 202 5672 7193 3381 147 218 -401 N
ATOM 1523 CA ASN A 202 -12.309 35.047 29.780 1.00 41.69 C
ANISOU 1523 CA ASN A 202 5679 6875 3287 140 198 -413 C
ATOM 1524 C ASN A 202 -11.040 34.578 29.044 1.00 43.33 C
ANISOU 1524 C ASN A 202 5952 6951 3561 7 228 -369 C
ATOM 1525 O ASN A 202 -10.321 35.396 28.461 1.00 43.15 O
ANISOU 1525 O ASN A 202 6055 6774 3566 -19 224 -404 O
ATOM 1526 CB ASN A 202 -12.324 36.572 29.919 1.00 42.59 C
ANISOU 1526 CB ASN A 202 5906 6898 3380 236 160 -519 C
ATOM 1527 CG ASN A 202 -12.499 37.231 28.592 1.00 51.75 C
ANISOU 1527 CG ASN A 202 7207 7889 4568 251 133 -515 C
ATOM 1528 OD1 ASN A 202 -13.085 36.644 27.670 1.00 44.27 O
ANISOU 1528 OD1 ASN A 202 6248 6945 3629 241 132 -449 O
ATOM 1529 ND2 ASN A 202 -11.877 38.385 28.420 1.00 44.04 N
ANISOU 1529 ND2 ASN A 202 6370 6752 3610 257 112 -577 N
ATOM 1530 N SER A 203 -10.779 33.268 29.030 1.00 37.94 N
ANISOU 1530 N SER A 203 5184 6327 2904 -77 258 -291 N
ATOM 1531 CA SER A 203 -9.544 32.791 28.439 1.00 38.31 C
ANISOU 1531 CA SER A 203 5279 6272 3006 -187 288 -259 C
ATOM 1532 C SER A 203 -9.497 32.953 26.937 1.00 43.66 C
ANISOU 1532 C SER A 203 6066 6811 3713 -213 283 -239 C
ATOM 1533 O SER A 203 -10.443 32.572 26.263 1.00 43.89 O
ANISOU 1533 O SER A 203 6084 6856 3737 -184 263 -204 O
ATOM 1534 CB SER A 203 -9.294 31.330 28.792 1.00 40.52 C
ANISOU 1534 CB SER A 203 5451 6638 3306 -255 313 -184 C
ATOM 1535 OG SER A 203 -8.043 30.941 28.244 1.00 40.64 O
ANISOU 1535 OG SER A 203 5512 6561 3368 -343 340 -168 O
ATOM 1536 N SER A 204 -8.368 33.478 26.416 1.00 41.52 N
ANISOU 1536 N SER A 204 5892 6415 3471 -274 303 -257 N
ATOM 1537 CA SER A 204 -8.097 33.601 24.978 1.00 41.71 C
ANISOU 1537 CA SER A 204 6020 6315 3515 -311 310 -229 C
ATOM 1538 C SER A 204 -7.695 32.239 24.452 1.00 45.90 C
ANISOU 1538 C SER A 204 6499 6869 4073 -381 336 -168 C
ATOM 1539 O SER A 204 -6.674 31.690 24.870 1.00 43.60 O
ANISOU 1539 O SER A 204 6162 6599 3804 -446 369 -161 O
ATOM 1540 CB SER A 204 -6.975 34.605 24.698 1.00 44.62 C
ANISOU 1540 CB SER A 204 6494 6559 3899 -365 328 -260 C
ATOM 1541 OG SER A 204 -7.092 35.784 25.469 1.00 50.92 O
ANISOU 1541 OG SER A 204 7332 7331 4683 -315 300 -330 O
ATOM 1542 N ARG A 205 -8.466 31.708 23.521 1.00 45.34 N
ANISOU 1542 N ARG A 205 6437 6791 3998 -363 318 -132 N
ATOM 1543 CA ARG A 205 -8.185 30.404 22.916 1.00 43.87 C
ANISOU 1543 CA ARG A 205 6215 6613 3839 -419 330 -85 C
ATOM 1544 C ARG A 205 -7.493 30.571 21.559 1.00 46.62 C
ANISOU 1544 C ARG A 205 6668 6858 4189 -455 351 -78 C
ATOM 1545 O ARG A 205 -7.416 29.630 20.766 1.00 46.94 O
ANISOU 1545 O ARG A 205 6705 6890 4241 -480 352 -51 O
ATOM 1546 CB ARG A 205 -9.469 29.553 22.844 1.00 42.70 C
ANISOU 1546 CB ARG A 205 5996 6538 3689 -387 290 -52 C
ATOM 1547 CG ARG A 205 -10.303 29.533 24.150 1.00 47.34 C
ANISOU 1547 CG ARG A 205 6477 7251 4260 -344 274 -51 C
ATOM 1548 CD ARG A 205 -9.550 29.247 25.452 1.00 42.32 C
ANISOU 1548 CD ARG A 205 5767 6682 3632 -374 303 -50 C
ATOM 1549 NE ARG A 205 -8.794 27.990 25.396 1.00 43.00 N
ANISOU 1549 NE ARG A 205 5814 6763 3761 -448 322 -5 N
ATOM 1550 CZ ARG A 205 -7.691 27.739 26.090 1.00 55.44 C
ANISOU 1550 CZ ARG A 205 7363 8351 5350 -487 352 -6 C
ATOM 1551 NH1 ARG A 205 -7.191 28.656 26.911 1.00 43.66 N
ANISOU 1551 NH1 ARG A 205 5875 6881 3834 -470 367 -53 N
ATOM 1552 NH2 ARG A 205 -7.054 26.584 25.941 1.00 34.84 N
ANISOU 1552 NH2 ARG A 205 4727 5730 2780 -538 362 34 N
ATOM 1553 N PHE A 206 -6.878 31.752 21.352 1.00 40.68 N
ANISOU 1553 N PHE A 206 6006 6027 3425 -465 370 -102 N
ATOM 1554 CA PHE A 206 -6.054 32.101 20.194 1.00 38.69 C
ANISOU 1554 CA PHE A 206 5850 5685 3166 -512 401 -87 C
ATOM 1555 C PHE A 206 -5.001 33.123 20.634 1.00 44.35 C
ANISOU 1555 C PHE A 206 6610 6348 3892 -564 432 -112 C
ATOM 1556 O PHE A 206 -5.239 33.909 21.567 1.00 45.47 O
ANISOU 1556 O PHE A 206 6752 6489 4037 -535 411 -151 O
ATOM 1557 CB PHE A 206 -6.910 32.680 19.024 1.00 39.91 C
ANISOU 1557 CB PHE A 206 6106 5776 3281 -457 371 -71 C
ATOM 1558 CG PHE A 206 -7.464 34.072 19.278 1.00 41.44 C
ANISOU 1558 CG PHE A 206 6377 5912 3457 -399 340 -94 C
ATOM 1559 CD1 PHE A 206 -8.510 34.273 20.178 1.00 43.01 C
ANISOU 1559 CD1 PHE A 206 6522 6170 3650 -318 296 -126 C
ATOM 1560 CD2 PHE A 206 -6.903 35.184 18.661 1.00 42.83 C
ANISOU 1560 CD2 PHE A 206 6679 5975 3622 -423 355 -85 C
ATOM 1561 CE1 PHE A 206 -8.997 35.557 20.438 1.00 43.96 C
ANISOU 1561 CE1 PHE A 206 6717 6234 3752 -247 263 -159 C
ATOM 1562 CE2 PHE A 206 -7.412 36.466 18.900 1.00 45.85 C
ANISOU 1562 CE2 PHE A 206 7145 6282 3993 -363 317 -109 C
ATOM 1563 CZ PHE A 206 -8.459 36.644 19.788 1.00 43.01 C
ANISOU 1563 CZ PHE A 206 6735 5979 3627 -267 269 -152 C
ATOM 1564 N GLY A 207 -3.876 33.159 19.939 1.00 41.08 N
ANISOU 1564 N GLY A 207 6235 5893 3482 -639 480 -94 N
ATOM 1565 CA GLY A 207 -2.860 34.159 20.239 1.00 41.09 C
ANISOU 1565 CA GLY A 207 6278 5837 3496 -707 507 -112 C
ATOM 1566 C GLY A 207 -2.956 35.278 19.237 1.00 44.85 C
ANISOU 1566 C GLY A 207 6894 6199 3949 -713 505 -86 C
ATOM 1567 O GLY A 207 -3.463 35.063 18.133 1.00 41.82 O
ANISOU 1567 O GLY A 207 6562 5796 3531 -679 501 -47 O
ATOM 1568 N LYS A 208 -2.543 36.493 19.607 1.00 44.21 N
ANISOU 1568 N LYS A 208 6880 6033 3883 -751 501 -106 N
ATOM 1569 CA LYS A 208 -2.622 37.563 18.604 1.00 45.62 C
ANISOU 1569 CA LYS A 208 7204 6087 4042 -763 498 -65 C
ATOM 1570 C LYS A 208 -1.441 38.516 18.669 1.00 52.22 C
ANISOU 1570 C LYS A 208 8095 6841 4906 -880 528 -61 C
ATOM 1571 O LYS A 208 -0.835 38.680 19.727 1.00 52.24 O
ANISOU 1571 O LYS A 208 8036 6865 4946 -927 528 -113 O
ATOM 1572 CB LYS A 208 -3.950 38.367 18.665 1.00 47.24 C
ANISOU 1572 CB LYS A 208 7495 6225 4230 -648 428 -82 C
ATOM 1573 CG LYS A 208 -4.195 39.169 19.929 1.00 57.14 C
ANISOU 1573 CG LYS A 208 8750 7449 5512 -611 382 -156 C
ATOM 1574 CD LYS A 208 -5.583 39.826 19.915 1.00 64.29 C
ANISOU 1574 CD LYS A 208 9726 8310 6391 -472 313 -176 C
ATOM 1575 CE LYS A 208 -5.876 40.579 21.198 1.00 87.31 C
ANISOU 1575 CE LYS A 208 12637 11214 9324 -412 265 -263 C
ATOM 1576 NZ LYS A 208 -6.131 39.669 22.364 1.00101.29 N
ANISOU 1576 NZ LYS A 208 14247 13146 11093 -380 267 -311 N
ATOM 1577 N PHE A 209 -1.137 39.141 17.512 1.00 48.44 N
ANISOU 1577 N PHE A 209 7727 6273 4404 -931 553 7 N
ATOM 1578 CA PHE A 209 -0.152 40.203 17.389 1.00 49.17 C
ANISOU 1578 CA PHE A 209 7896 6264 4523 -1053 578 31 C
ATOM 1579 C PHE A 209 -0.900 41.410 16.841 1.00 55.60 C
ANISOU 1579 C PHE A 209 8881 6921 5325 -1008 529 67 C
ATOM 1580 O PHE A 209 -1.423 41.330 15.746 1.00 55.23 O
ANISOU 1580 O PHE A 209 8901 6859 5225 -960 533 131 O
ATOM 1581 CB PHE A 209 1.047 39.804 16.511 1.00 50.13 C
ANISOU 1581 CB PHE A 209 7983 6438 4624 -1172 662 96 C
ATOM 1582 CG PHE A 209 2.215 40.764 16.603 1.00 52.17 C
ANISOU 1582 CG PHE A 209 8277 6624 4920 -1325 693 116 C
ATOM 1583 CD1 PHE A 209 2.787 41.078 17.834 1.00 55.52 C
ANISOU 1583 CD1 PHE A 209 8639 7050 5405 -1384 674 42 C
ATOM 1584 CD2 PHE A 209 2.778 41.314 15.455 1.00 54.83 C
ANISOU 1584 CD2 PHE A 209 8703 6902 5228 -1417 741 212 C
ATOM 1585 CE1 PHE A 209 3.863 41.969 17.919 1.00 57.76 C
ANISOU 1585 CE1 PHE A 209 8951 7265 5729 -1538 695 57 C
ATOM 1586 CE2 PHE A 209 3.860 42.190 15.540 1.00 58.92 C
ANISOU 1586 CE2 PHE A 209 9246 7355 5785 -1576 770 239 C
ATOM 1587 CZ PHE A 209 4.411 42.496 16.769 1.00 57.06 C
ANISOU 1587 CZ PHE A 209 8946 7115 5619 -1641 745 159 C
ATOM 1588 N VAL A 210 -1.102 42.454 17.658 1.00 52.93 N
ANISOU 1588 N VAL A 210 8610 6472 5029 -995 472 14 N
ATOM 1589 CA VAL A 210 -1.852 43.616 17.192 1.00 52.93 C
ANISOU 1589 CA VAL A 210 8782 6309 5021 -934 414 41 C
ATOM 1590 C VAL A 210 -0.890 44.731 16.932 1.00 57.22 C
ANISOU 1590 C VAL A 210 9436 6702 5602 -1077 428 87 C
ATOM 1591 O VAL A 210 -0.235 45.240 17.853 1.00 55.56 O
ANISOU 1591 O VAL A 210 9210 6449 5452 -1158 414 25 O
ATOM 1592 CB VAL A 210 -2.993 44.063 18.125 1.00 56.20 C
ANISOU 1592 CB VAL A 210 9217 6690 5446 -785 327 -50 C
ATOM 1593 CG1 VAL A 210 -3.771 45.218 17.504 1.00 56.63 C
ANISOU 1593 CG1 VAL A 210 9457 6572 5488 -707 265 -17 C
ATOM 1594 CG2 VAL A 210 -3.925 42.907 18.426 1.00 54.81 C
ANISOU 1594 CG2 VAL A 210 8916 6678 5233 -662 318 -83 C
ATOM 1595 N GLU A 211 -0.798 45.101 15.654 1.00 55.58 N
ANISOU 1595 N GLU A 211 9340 6421 5356 -1115 455 198 N
ATOM 1596 CA GLU A 211 0.075 46.182 15.216 1.00 57.34 C
ANISOU 1596 CA GLU A 211 9681 6495 5609 -1265 474 272 C
ATOM 1597 C GLU A 211 -0.683 47.491 15.043 1.00 63.02 C
ANISOU 1597 C GLU A 211 10602 7000 6344 -1199 391 292 C
ATOM 1598 O GLU A 211 -1.742 47.502 14.421 1.00 63.61 O
ANISOU 1598 O GLU A 211 10751 7053 6364 -1060 355 325 O
ATOM 1599 CB GLU A 211 0.739 45.819 13.888 1.00 58.65 C
ANISOU 1599 CB GLU A 211 9848 6720 5714 -1357 563 398 C
ATOM 1600 CG GLU A 211 1.685 44.642 13.970 1.00 62.57 C
ANISOU 1600 CG GLU A 211 10161 7412 6199 -1438 648 384 C
ATOM 1601 CD GLU A 211 2.120 44.186 12.597 1.00 71.70 C
ANISOU 1601 CD GLU A 211 11316 8651 7276 -1485 730 495 C
ATOM 1602 OE1 GLU A 211 2.328 45.057 11.727 1.00 65.10 O
ANISOU 1602 OE1 GLU A 211 10608 7709 6418 -1563 749 603 O
ATOM 1603 OE2 GLU A 211 2.218 42.959 12.378 1.00 66.38 O
ANISOU 1603 OE2 GLU A 211 10517 8145 6558 -1440 773 474 O
ATOM 1604 N ILE A 212 -0.133 48.586 15.576 1.00 59.97 N
ANISOU 1604 N ILE A 212 10303 6452 6032 -1298 356 270 N
ATOM 1605 CA ILE A 212 -0.669 49.931 15.373 1.00 61.43 C
ANISOU 1605 CA ILE A 212 10699 6399 6242 -1257 275 298 C
ATOM 1606 C ILE A 212 0.344 50.598 14.459 1.00 64.94 C
ANISOU 1606 C ILE A 212 11244 6731 6699 -1452 327 437 C
ATOM 1607 O ILE A 212 1.512 50.687 14.828 1.00 64.48 O
ANISOU 1607 O ILE A 212 11122 6681 6694 -1633 368 431 O
ATOM 1608 CB ILE A 212 -0.949 50.738 16.684 1.00 65.45 C
ANISOU 1608 CB ILE A 212 11256 6784 6827 -1204 177 159 C
ATOM 1609 CG1 ILE A 212 -2.063 50.075 17.543 1.00 64.41 C
ANISOU 1609 CG1 ILE A 212 11022 6785 6666 -996 129 33 C
ATOM 1610 CG2 ILE A 212 -1.319 52.195 16.328 1.00 68.17 C
ANISOU 1610 CG2 ILE A 212 11844 6853 7207 -1185 94 203 C
ATOM 1611 CD1 ILE A 212 -2.500 50.888 18.812 1.00 71.86 C
ANISOU 1611 CD1 ILE A 212 12017 7624 7663 -904 28 -112 C
ATOM 1612 N HIS A 213 -0.074 50.988 13.254 1.00 61.86 N
ANISOU 1612 N HIS A 213 10994 6259 6251 -1419 330 567 N
ATOM 1613 CA HIS A 213 0.818 51.589 12.268 1.00 63.63 C
ANISOU 1613 CA HIS A 213 11315 6390 6469 -1601 387 723 C
ATOM 1614 C HIS A 213 0.714 53.102 12.300 1.00 69.77 C
ANISOU 1614 C HIS A 213 12317 6877 7314 -1640 303 763 C
ATOM 1615 O HIS A 213 -0.353 53.649 12.605 1.00 69.78 O
ANISOU 1615 O HIS A 213 12436 6749 7327 -1467 201 704 O
ATOM 1616 CB HIS A 213 0.535 51.032 10.871 1.00 64.07 C
ANISOU 1616 CB HIS A 213 11383 6550 6408 -1554 449 853 C
ATOM 1617 CG HIS A 213 0.903 49.586 10.748 1.00 65.53 C
ANISOU 1617 CG HIS A 213 11357 7004 6537 -1559 539 825 C
ATOM 1618 ND1 HIS A 213 2.008 49.184 10.028 1.00 67.65 N
ANISOU 1618 ND1 HIS A 213 11551 7387 6765 -1718 649 919 N
ATOM 1619 CD2 HIS A 213 0.313 48.496 11.286 1.00 64.60 C
ANISOU 1619 CD2 HIS A 213 11093 7050 6400 -1424 530 711 C
ATOM 1620 CE1 HIS A 213 2.050 47.865 10.143 1.00 64.82 C
ANISOU 1620 CE1 HIS A 213 11014 7250 6367 -1662 697 853 C
ATOM 1621 NE2 HIS A 213 1.041 47.409 10.876 1.00 63.58 N
ANISOU 1621 NE2 HIS A 213 10812 7121 6224 -1493 627 733 N
ATOM 1622 N PHE A 214 1.846 53.765 12.010 1.00 67.62 N
ANISOU 1622 N PHE A 214 12099 6504 7089 -1869 345 860 N
ATOM 1623 CA PHE A 214 2.009 55.220 12.028 1.00 70.18 C
ANISOU 1623 CA PHE A 214 12638 6532 7494 -1961 271 913 C
ATOM 1624 C PHE A 214 2.672 55.729 10.733 1.00 79.97 C
ANISOU 1624 C PHE A 214 13988 7699 8698 -2133 340 1130 C
ATOM 1625 O PHE A 214 3.310 54.948 10.009 1.00 79.23 O
ANISOU 1625 O PHE A 214 13767 7807 8530 -2224 457 1217 O
ATOM 1626 CB PHE A 214 2.889 55.630 13.229 1.00 71.81 C
ANISOU 1626 CB PHE A 214 12792 6672 7822 -2117 242 799 C
ATOM 1627 CG PHE A 214 2.424 55.215 14.606 1.00 71.00 C
ANISOU 1627 CG PHE A 214 12576 6645 7755 -1978 179 587 C
ATOM 1628 CD1 PHE A 214 2.634 53.922 15.070 1.00 70.61 C
ANISOU 1628 CD1 PHE A 214 12289 6871 7666 -1949 246 505 C
ATOM 1629 CD2 PHE A 214 1.846 56.139 15.469 1.00 73.46 C
ANISOU 1629 CD2 PHE A 214 13019 6753 8139 -1882 51 469 C
ATOM 1630 CE1 PHE A 214 2.215 53.544 16.340 1.00 70.22 C
ANISOU 1630 CE1 PHE A 214 12138 6901 7643 -1826 191 325 C
ATOM 1631 CE2 PHE A 214 1.433 55.762 16.750 1.00 74.36 C
ANISOU 1631 CE2 PHE A 214 13022 6958 8273 -1752 -2 276 C
ATOM 1632 CZ PHE A 214 1.627 54.472 17.180 1.00 70.21 C
ANISOU 1632 CZ PHE A 214 12261 6714 7703 -1730 70 212 C
ATOM 1633 N ASN A 215 2.556 57.055 10.467 1.00 80.21 N
ANISOU 1633 N ASN A 215 14256 7439 8781 -2179 266 1217 N
ATOM 1634 CA ASN A 215 3.190 57.702 9.315 1.00 82.41 C
ANISOU 1634 CA ASN A 215 14661 7615 9035 -2361 322 1438 C
ATOM 1635 C ASN A 215 4.576 58.249 9.746 1.00 89.44 C
ANISOU 1635 C ASN A 215 15520 8428 10035 -2660 353 1459 C
ATOM 1636 O ASN A 215 5.104 57.815 10.777 1.00 88.15 O
ANISOU 1636 O ASN A 215 15188 8372 9933 -2716 359 1309 O
ATOM 1637 CB ASN A 215 2.282 58.807 8.726 1.00 83.08 C
ANISOU 1637 CB ASN A 215 15028 7425 9116 -2247 223 1538 C
ATOM 1638 CG ASN A 215 1.659 59.769 9.722 1.00101.45 C
ANISOU 1638 CG ASN A 215 17509 9484 11555 -2144 70 1404 C
ATOM 1639 OD1 ASN A 215 2.125 59.948 10.855 1.00 91.50 O
ANISOU 1639 OD1 ASN A 215 16189 8176 10402 -2226 31 1261 O
ATOM 1640 ND2 ASN A 215 0.583 60.426 9.307 1.00 92.96 N
ANISOU 1640 ND2 ASN A 215 16638 8231 10453 -1952 -25 1444 N
ATOM 1641 N GLU A 216 5.174 59.170 8.960 1.00 88.66 N
ANISOU 1641 N GLU A 216 15574 8155 9956 -2856 372 1648 N
ATOM 1642 CA GLU A 216 6.465 59.764 9.301 1.00 90.15 C
ANISOU 1642 CA GLU A 216 15741 8260 10252 -3157 396 1683 C
ATOM 1643 C GLU A 216 6.303 60.720 10.488 1.00 95.27 C
ANISOU 1643 C GLU A 216 16512 8634 11053 -3162 249 1534 C
ATOM 1644 O GLU A 216 7.217 60.841 11.304 1.00 94.89 O
ANISOU 1644 O GLU A 216 16363 8588 11102 -3344 247 1448 O
ATOM 1645 CB GLU A 216 7.064 60.491 8.090 1.00 94.17 C
ANISOU 1645 CB GLU A 216 16385 8662 10733 -3365 458 1944 C
ATOM 1646 N LYS A 217 5.109 61.351 10.600 1.00 93.19 N
ANISOU 1646 N LYS A 217 16457 8147 10803 -2945 123 1492 N
ATOM 1647 CA LYS A 217 4.714 62.321 11.630 1.00 94.65 C
ANISOU 1647 CA LYS A 217 16796 8050 11115 -2888 -34 1345 C
ATOM 1648 C LYS A 217 4.378 61.641 12.970 1.00 98.45 C
ANISOU 1648 C LYS A 217 17104 8684 11619 -2733 -76 1083 C
ATOM 1649 O LYS A 217 4.013 62.332 13.932 1.00 99.05 O
ANISOU 1649 O LYS A 217 17281 8569 11787 -2656 -205 928 O
ATOM 1650 CB LYS A 217 3.505 63.146 11.141 1.00 98.29 C
ANISOU 1650 CB LYS A 217 17531 8255 11560 -2677 -145 1401 C
ATOM 1651 CG LYS A 217 3.834 64.138 10.021 1.00112.48 C
ANISOU 1651 CG LYS A 217 19556 9816 13366 -2840 -140 1653 C
ATOM 1652 N SER A 218 4.518 60.288 13.025 1.00 93.13 N
ANISOU 1652 N SER A 218 16174 8355 10858 -2688 31 1038 N
ATOM 1653 CA SER A 218 4.261 59.407 14.166 1.00 90.74 C
ANISOU 1653 CA SER A 218 15672 8256 10550 -2550 20 824 C
ATOM 1654 C SER A 218 2.834 59.616 14.722 1.00 94.67 C
ANISOU 1654 C SER A 218 16273 8660 11038 -2248 -102 686 C
ATOM 1655 O SER A 218 2.635 60.003 15.877 1.00 94.91 O
ANISOU 1655 O SER A 218 16323 8595 11143 -2185 -201 510 O
ATOM 1656 CB SER A 218 5.334 59.572 15.240 1.00 94.31 C
ANISOU 1656 CB SER A 218 16012 8713 11107 -2746 8 705 C
ATOM 1657 OG SER A 218 6.575 59.065 14.773 1.00101.69 O
ANISOU 1657 OG SER A 218 16788 9825 12025 -2985 137 814 O
ATOM 1658 N SER A 219 1.849 59.384 13.851 1.00 90.83 N
ANISOU 1658 N SER A 219 15853 8204 10453 -2062 -94 772 N
ATOM 1659 CA SER A 219 0.420 59.460 14.131 1.00 90.64 C
ANISOU 1659 CA SER A 219 15908 8138 10393 -1760 -191 673 C
ATOM 1660 C SER A 219 -0.262 58.262 13.477 1.00 93.61 C
ANISOU 1660 C SER A 219 16148 8782 10636 -1604 -115 714 C
ATOM 1661 O SER A 219 0.038 57.938 12.330 1.00 93.25 O
ANISOU 1661 O SER A 219 16098 8813 10520 -1685 -25 882 O
ATOM 1662 CB SER A 219 -0.171 60.775 13.636 1.00 96.96 C
ANISOU 1662 CB SER A 219 17004 8610 11227 -1694 -299 754 C
ATOM 1663 OG SER A 219 -0.033 60.911 12.232 1.00108.75 O
ANISOU 1663 OG SER A 219 18595 10070 12655 -1770 -235 983 O
ATOM 1664 N VAL A 220 -1.145 57.588 14.227 1.00 89.86 N
ANISOU 1664 N VAL A 220 15556 8460 10129 -1389 -148 557 N
ATOM 1665 CA VAL A 220 -1.862 56.365 13.835 1.00 87.96 C
ANISOU 1665 CA VAL A 220 15163 8481 9776 -1234 -91 558 C
ATOM 1666 C VAL A 220 -2.499 56.516 12.446 1.00 93.02 C
ANISOU 1666 C VAL A 220 15935 9080 10327 -1150 -84 722 C
ATOM 1667 O VAL A 220 -3.173 57.512 12.177 1.00 94.92 O
ANISOU 1667 O VAL A 220 16386 9101 10579 -1044 -177 756 O
ATOM 1668 CB VAL A 220 -2.915 55.947 14.900 1.00 90.55 C
ANISOU 1668 CB VAL A 220 15397 8914 10094 -1001 -160 370 C
ATOM 1669 CG1 VAL A 220 -3.598 54.628 14.532 1.00 88.47 C
ANISOU 1669 CG1 VAL A 220 14965 8923 9727 -868 -101 371 C
ATOM 1670 CG2 VAL A 220 -2.288 55.847 16.283 1.00 89.81 C
ANISOU 1670 CG2 VAL A 220 15183 8863 10077 -1078 -171 211 C
ATOM 1671 N VAL A 221 -2.232 55.532 11.565 1.00 88.18 N
ANISOU 1671 N VAL A 221 15203 8677 9625 -1198 25 821 N
ATOM 1672 CA VAL A 221 -2.757 55.457 10.193 1.00 87.84 C
ANISOU 1672 CA VAL A 221 15247 8652 9474 -1123 47 974 C
ATOM 1673 C VAL A 221 -3.708 54.245 10.075 1.00 88.16 C
ANISOU 1673 C VAL A 221 15134 8942 9421 -929 61 907 C
ATOM 1674 O VAL A 221 -4.484 54.142 9.122 1.00 87.62 O
ANISOU 1674 O VAL A 221 15130 8902 9261 -800 48 987 O
ATOM 1675 CB VAL A 221 -1.635 55.432 9.111 1.00 92.46 C
ANISOU 1675 CB VAL A 221 15849 9261 10022 -1347 158 1160 C
ATOM 1676 CG1 VAL A 221 -0.810 56.715 9.146 1.00 94.78 C
ANISOU 1676 CG1 VAL A 221 16314 9289 10409 -1541 133 1246 C
ATOM 1677 CG2 VAL A 221 -0.740 54.199 9.226 1.00 90.35 C
ANISOU 1677 CG2 VAL A 221 15338 9260 9731 -1473 279 1131 C
ATOM 1678 N GLY A 222 -3.631 53.359 11.065 1.00 82.41 N
ANISOU 1678 N GLY A 222 14205 8387 8719 -915 83 763 N
ATOM 1679 CA GLY A 222 -4.440 52.149 11.149 1.00 79.19 C
ANISOU 1679 CA GLY A 222 13632 8213 8244 -760 95 688 C
ATOM 1680 C GLY A 222 -3.737 51.048 11.907 1.00 77.69 C
ANISOU 1680 C GLY A 222 13217 8223 8079 -851 167 598 C
ATOM 1681 O GLY A 222 -2.709 51.290 12.545 1.00 76.96 O
ANISOU 1681 O GLY A 222 13090 8091 8061 -1012 194 569 O
ATOM 1682 N GLY A 223 -4.289 49.843 11.817 1.00 70.34 N
ANISOU 1682 N GLY A 223 12136 7505 7087 -750 193 557 N
ATOM 1683 CA GLY A 223 -3.756 48.668 12.492 1.00 67.14 C
ANISOU 1683 CA GLY A 223 11516 7297 6697 -810 255 477 C
ATOM 1684 C GLY A 223 -3.924 47.367 11.732 1.00 67.35 C
ANISOU 1684 C GLY A 223 11420 7528 6641 -777 316 509 C
ATOM 1685 O GLY A 223 -4.597 47.320 10.702 1.00 66.80 O
ANISOU 1685 O GLY A 223 11420 7468 6494 -689 303 581 O
ATOM 1686 N PHE A 224 -3.326 46.287 12.264 1.00 60.55 N
ANISOU 1686 N PHE A 224 10377 6832 5796 -841 374 450 N
ATOM 1687 CA PHE A 224 -3.383 44.948 11.680 1.00 55.89 C
ANISOU 1687 CA PHE A 224 9660 6434 5143 -818 428 461 C
ATOM 1688 C PHE A 224 -3.252 43.869 12.769 1.00 55.98 C
ANISOU 1688 C PHE A 224 9481 6593 5194 -813 441 351 C
ATOM 1689 O PHE A 224 -2.301 43.894 13.540 1.00 54.66 O
ANISOU 1689 O PHE A 224 9250 6432 5086 -924 472 313 O
ATOM 1690 CB PHE A 224 -2.278 44.785 10.627 1.00 56.54 C
ANISOU 1690 CB PHE A 224 9749 6553 5181 -960 522 568 C
ATOM 1691 CG PHE A 224 -2.424 43.516 9.837 1.00 55.34 C
ANISOU 1691 CG PHE A 224 9500 6577 4950 -913 566 580 C
ATOM 1692 CD1 PHE A 224 -3.220 43.479 8.692 1.00 58.60 C
ANISOU 1692 CD1 PHE A 224 9995 6998 5273 -814 544 644 C
ATOM 1693 CD2 PHE A 224 -1.784 42.351 10.241 1.00 53.58 C
ANISOU 1693 CD2 PHE A 224 9107 6509 4742 -961 620 523 C
ATOM 1694 CE1 PHE A 224 -3.377 42.296 7.968 1.00 58.31 C
ANISOU 1694 CE1 PHE A 224 9872 7120 5164 -768 575 640 C
ATOM 1695 CE2 PHE A 224 -1.972 41.160 9.544 1.00 56.16 C
ANISOU 1695 CE2 PHE A 224 9353 6981 5002 -908 647 520 C
ATOM 1696 CZ PHE A 224 -2.742 41.146 8.393 1.00 55.67 C
ANISOU 1696 CZ PHE A 224 9375 6924 4852 -817 625 576 C
ATOM 1697 N VAL A 225 -4.158 42.876 12.746 1.00 51.86 N
ANISOU 1697 N VAL A 225 8869 6198 4636 -693 420 310 N
ATOM 1698 CA VAL A 225 -4.247 41.753 13.684 1.00 50.31 C
ANISOU 1698 CA VAL A 225 8500 6146 4468 -670 425 222 C
ATOM 1699 C VAL A 225 -3.873 40.433 12.991 1.00 53.76 C
ANISOU 1699 C VAL A 225 8837 6727 4864 -698 484 246 C
ATOM 1700 O VAL A 225 -4.505 40.026 12.005 1.00 52.98 O
ANISOU 1700 O VAL A 225 8765 6665 4701 -628 472 283 O
ATOM 1701 CB VAL A 225 -5.667 41.644 14.310 1.00 54.04 C
ANISOU 1701 CB VAL A 225 8944 6650 4941 -511 345 152 C
ATOM 1702 CG1 VAL A 225 -5.739 40.525 15.358 1.00 52.59 C
ANISOU 1702 CG1 VAL A 225 8583 6611 4788 -501 352 75 C
ATOM 1703 CG2 VAL A 225 -6.127 42.975 14.907 1.00 55.15 C
ANISOU 1703 CG2 VAL A 225 9196 6647 5111 -451 278 119 C
ATOM 1704 N SER A 226 -2.846 39.764 13.538 1.00 50.20 N
ANISOU 1704 N SER A 226 8270 6357 4448 -795 540 219 N
ATOM 1705 CA SER A 226 -2.416 38.420 13.151 1.00 49.16 C
ANISOU 1705 CA SER A 226 8025 6362 4291 -813 590 218 C
ATOM 1706 C SER A 226 -2.918 37.491 14.256 1.00 52.77 C
ANISOU 1706 C SER A 226 8352 6910 4789 -754 557 138 C
ATOM 1707 O SER A 226 -2.692 37.762 15.435 1.00 52.04 O
ANISOU 1707 O SER A 226 8213 6810 4751 -777 545 88 O
ATOM 1708 CB SER A 226 -0.899 38.327 12.979 1.00 52.25 C
ANISOU 1708 CB SER A 226 8375 6788 4689 -951 674 247 C
ATOM 1709 OG SER A 226 -0.354 39.372 12.199 1.00 63.45 O
ANISOU 1709 OG SER A 226 9911 8115 6083 -1031 707 327 O
ATOM 1710 N HIS A 227 -3.696 36.482 13.894 1.00 49.75 N
ANISOU 1710 N HIS A 227 7919 6606 4379 -675 533 127 N
ATOM 1711 CA HIS A 227 -4.255 35.547 14.857 1.00 48.99 C
ANISOU 1711 CA HIS A 227 7702 6595 4319 -626 501 69 C
ATOM 1712 C HIS A 227 -3.542 34.211 14.683 1.00 51.26 C
ANISOU 1712 C HIS A 227 7889 6977 4610 -667 544 64 C
ATOM 1713 O HIS A 227 -3.053 33.913 13.593 1.00 50.74 O
ANISOU 1713 O HIS A 227 7853 6924 4501 -692 582 96 O
ATOM 1714 CB HIS A 227 -5.789 35.435 14.715 1.00 50.05 C
ANISOU 1714 CB HIS A 227 7846 6741 4430 -508 429 58 C
ATOM 1715 CG HIS A 227 -6.264 34.844 13.417 1.00 53.52 C
ANISOU 1715 CG HIS A 227 8315 7208 4812 -468 418 88 C
ATOM 1716 ND1 HIS A 227 -6.129 35.527 12.206 1.00 56.47 N
ANISOU 1716 ND1 HIS A 227 8812 7519 5126 -467 431 143 N
ATOM 1717 CD2 HIS A 227 -6.888 33.666 13.184 1.00 54.50 C
ANISOU 1717 CD2 HIS A 227 8364 7413 4930 -428 391 70 C
ATOM 1718 CE1 HIS A 227 -6.663 34.738 11.285 1.00 55.30 C
ANISOU 1718 CE1 HIS A 227 8654 7427 4929 -419 410 148 C
ATOM 1719 NE2 HIS A 227 -7.124 33.604 11.823 1.00 54.87 N
ANISOU 1719 NE2 HIS A 227 8485 7454 4911 -398 383 101 N
ATOM 1720 N TYR A 228 -3.456 33.431 15.772 1.00 45.78 N
ANISOU 1720 N TYR A 228 7079 6353 3964 -669 538 22 N
ATOM 1721 CA TYR A 228 -2.753 32.167 15.783 1.00 44.48 C
ANISOU 1721 CA TYR A 228 6821 6267 3813 -700 570 12 C
ATOM 1722 C TYR A 228 -3.501 31.112 16.532 1.00 49.38 C
ANISOU 1722 C TYR A 228 7346 6950 4465 -651 526 -13 C
ATOM 1723 O TYR A 228 -3.993 31.364 17.628 1.00 48.11 O
ANISOU 1723 O TYR A 228 7143 6803 4332 -630 497 -33 O
ATOM 1724 CB TYR A 228 -1.379 32.328 16.457 1.00 45.45 C
ANISOU 1724 CB TYR A 228 6892 6410 3967 -786 624 1 C
ATOM 1725 CG TYR A 228 -0.558 33.470 15.904 1.00 48.17 C
ANISOU 1725 CG TYR A 228 7319 6693 4292 -861 669 32 C
ATOM 1726 CD1 TYR A 228 0.151 33.332 14.720 1.00 49.69 C
ANISOU 1726 CD1 TYR A 228 7543 6899 4437 -899 723 71 C
ATOM 1727 CD2 TYR A 228 -0.451 34.674 16.592 1.00 49.19 C
ANISOU 1727 CD2 TYR A 228 7492 6752 4448 -898 658 22 C
ATOM 1728 CE1 TYR A 228 0.905 34.379 14.203 1.00 52.49 C
ANISOU 1728 CE1 TYR A 228 7970 7203 4772 -981 769 115 C
ATOM 1729 CE2 TYR A 228 0.309 35.726 16.091 1.00 51.18 C
ANISOU 1729 CE2 TYR A 228 7823 6932 4690 -984 695 59 C
ATOM 1730 CZ TYR A 228 0.968 35.582 14.881 1.00 56.00 C
ANISOU 1730 CZ TYR A 228 8464 7561 5254 -1030 753 113 C
ATOM 1731 OH TYR A 228 1.699 36.621 14.348 1.00 52.36 O
ANISOU 1731 OH TYR A 228 8079 7035 4779 -1126 794 166 O
ATOM 1732 N LEU A 229 -3.483 29.898 15.992 1.00 46.70 N
ANISOU 1732 N LEU A 229 6969 6652 4123 -639 524 -14 N
ATOM 1733 CA LEU A 229 -3.994 28.688 16.618 1.00 46.48 C
ANISOU 1733 CA LEU A 229 6849 6676 4133 -614 487 -27 C
ATOM 1734 C LEU A 229 -5.305 28.818 17.389 1.00 45.08 C
ANISOU 1734 C LEU A 229 6639 6517 3972 -568 429 -29 C
ATOM 1735 O LEU A 229 -5.330 28.555 18.586 1.00 43.69 O
ANISOU 1735 O LEU A 229 6382 6386 3831 -575 424 -34 O
ATOM 1736 CB LEU A 229 -2.938 28.137 17.600 1.00 47.33 C
ANISOU 1736 CB LEU A 229 6869 6830 4284 -657 520 -38 C
ATOM 1737 CG LEU A 229 -1.669 27.544 17.041 1.00 54.97 C
ANISOU 1737 CG LEU A 229 7823 7816 5246 -690 570 -44 C
ATOM 1738 CD1 LEU A 229 -0.626 27.505 18.120 1.00 57.30 C
ANISOU 1738 CD1 LEU A 229 8041 8156 5575 -731 602 -55 C
ATOM 1739 CD2 LEU A 229 -1.907 26.132 16.447 1.00 56.55 C
ANISOU 1739 CD2 LEU A 229 8004 8029 5453 -653 541 -53 C
ATOM 1740 N LEU A 230 -6.387 29.134 16.725 1.00 40.16 N
ANISOU 1740 N LEU A 230 6066 5876 3318 -516 387 -23 N
ATOM 1741 CA LEU A 230 -7.687 29.068 17.385 1.00 38.55 C
ANISOU 1741 CA LEU A 230 5808 5714 3125 -468 331 -25 C
ATOM 1742 C LEU A 230 -7.905 27.608 17.843 1.00 42.10 C
ANISOU 1742 C LEU A 230 6155 6221 3619 -489 310 -18 C
ATOM 1743 O LEU A 230 -7.654 26.693 17.056 1.00 42.54 O
ANISOU 1743 O LEU A 230 6221 6263 3682 -505 305 -18 O
ATOM 1744 CB LEU A 230 -8.805 29.495 16.409 1.00 38.46 C
ANISOU 1744 CB LEU A 230 5861 5684 3069 -405 283 -22 C
ATOM 1745 CG LEU A 230 -10.211 29.395 17.004 1.00 43.01 C
ANISOU 1745 CG LEU A 230 6365 6325 3650 -351 225 -25 C
ATOM 1746 CD1 LEU A 230 -10.473 30.495 18.085 1.00 41.98 C
ANISOU 1746 CD1 LEU A 230 6225 6210 3517 -312 227 -40 C
ATOM 1747 CD2 LEU A 230 -11.253 29.284 15.950 1.00 43.59 C
ANISOU 1747 CD2 LEU A 230 6469 6403 3688 -299 169 -24 C
ATOM 1748 N GLU A 231 -8.300 27.386 19.101 1.00 38.18 N
ANISOU 1748 N GLU A 231 5569 5787 3151 -489 299 -10 N
ATOM 1749 CA GLU A 231 -8.530 26.026 19.618 1.00 37.74 C
ANISOU 1749 CA GLU A 231 5420 5779 3141 -518 277 14 C
ATOM 1750 C GLU A 231 -9.814 25.432 19.015 1.00 43.87 C
ANISOU 1750 C GLU A 231 6178 6572 3919 -500 214 24 C
ATOM 1751 O GLU A 231 -10.913 25.937 19.213 1.00 44.47 O
ANISOU 1751 O GLU A 231 6228 6693 3973 -460 182 27 O
ATOM 1752 CB GLU A 231 -8.602 26.045 21.145 1.00 38.38 C
ANISOU 1752 CB GLU A 231 5410 5935 3237 -523 286 30 C
ATOM 1753 CG GLU A 231 -8.734 24.667 21.761 1.00 39.53 C
ANISOU 1753 CG GLU A 231 5465 6126 3430 -560 267 72 C
ATOM 1754 CD GLU A 231 -8.794 24.746 23.268 1.00 55.28 C
ANISOU 1754 CD GLU A 231 7371 8210 5424 -561 281 95 C
ATOM 1755 OE1 GLU A 231 -9.581 25.583 23.755 1.00 43.49 O
ANISOU 1755 OE1 GLU A 231 5853 6777 3894 -518 272 84 O
ATOM 1756 OE2 GLU A 231 -7.930 24.136 23.941 1.00 60.37 O
ANISOU 1756 OE2 GLU A 231 7977 8867 6092 -592 303 114 O
ATOM 1757 N LYS A 232 -9.666 24.351 18.307 1.00 40.10 N
ANISOU 1757 N LYS A 232 5709 6061 3468 -526 193 25 N
ATOM 1758 CA LYS A 232 -10.763 23.714 17.596 1.00 39.43 C
ANISOU 1758 CA LYS A 232 5613 5980 3388 -521 127 25 C
ATOM 1759 C LYS A 232 -11.496 22.681 18.427 1.00 45.21 C
ANISOU 1759 C LYS A 232 6239 6764 4176 -563 87 64 C
ATOM 1760 O LYS A 232 -12.685 22.494 18.207 1.00 44.54 O
ANISOU 1760 O LYS A 232 6115 6717 4091 -560 32 72 O
ATOM 1761 CB LYS A 232 -10.219 23.045 16.324 1.00 39.51 C
ANISOU 1761 CB LYS A 232 5694 5922 3396 -527 115 -6 C
ATOM 1762 CG LYS A 232 -9.881 23.988 15.191 1.00 44.29 C
ANISOU 1762 CG LYS A 232 6404 6491 3931 -485 139 -35 C
ATOM 1763 CD LYS A 232 -9.614 23.096 13.968 1.00 63.20 C
ANISOU 1763 CD LYS A 232 8850 8846 6318 -484 114 -69 C
ATOM 1764 CE LYS A 232 -9.828 23.724 12.617 1.00 74.92 C
ANISOU 1764 CE LYS A 232 10425 10317 7724 -435 102 -92 C
ATOM 1765 NZ LYS A 232 -9.939 22.663 11.582 1.00 81.15 N
ANISOU 1765 NZ LYS A 232 11239 11085 8509 -429 53 -135 N
ATOM 1766 N SER A 233 -10.791 21.968 19.327 1.00 45.10 N
ANISOU 1766 N SER A 233 6177 6751 4207 -606 110 95 N
ATOM 1767 CA SER A 233 -11.379 20.929 20.194 1.00 47.06 C
ANISOU 1767 CA SER A 233 6328 7042 4510 -657 76 151 C
ATOM 1768 C SER A 233 -12.514 21.477 21.062 1.00 52.32 C
ANISOU 1768 C SER A 233 6905 7822 5152 -646 69 185 C
ATOM 1769 O SER A 233 -13.528 20.788 21.237 1.00 55.78 O
ANISOU 1769 O SER A 233 7268 8306 5619 -685 22 225 O
ATOM 1770 CB SER A 233 -10.322 20.287 21.080 1.00 50.62 C
ANISOU 1770 CB SER A 233 6754 7481 5000 -688 109 183 C
ATOM 1771 OG SER A 233 -9.510 21.285 21.673 1.00 64.00 O
ANISOU 1771 OG SER A 233 8456 9206 6655 -657 171 167 O
ATOM 1772 N ARG A 234 -12.393 22.748 21.479 1.00 45.19 N
ANISOU 1772 N ARG A 234 6013 6963 4195 -590 110 161 N
ATOM 1773 CA ARG A 234 -13.388 23.492 22.259 1.00 44.94 C
ANISOU 1773 CA ARG A 234 5907 7045 4123 -549 108 172 C
ATOM 1774 C ARG A 234 -14.756 23.650 21.560 1.00 46.93 C
ANISOU 1774 C ARG A 234 6138 7338 4355 -520 52 162 C
ATOM 1775 O ARG A 234 -15.756 23.843 22.241 1.00 47.16 O
ANISOU 1775 O ARG A 234 6071 7486 4363 -501 39 185 O
ATOM 1776 CB ARG A 234 -12.868 24.920 22.548 1.00 44.57 C
ANISOU 1776 CB ARG A 234 5916 6996 4024 -482 151 124 C
ATOM 1777 CG ARG A 234 -13.861 25.731 23.405 1.00 49.23 C
ANISOU 1777 CG ARG A 234 6437 7703 4564 -417 145 118 C
ATOM 1778 CD ARG A 234 -13.239 26.752 24.292 1.00 48.00 C
ANISOU 1778 CD ARG A 234 6295 7568 4374 -373 186 84 C
ATOM 1779 NE ARG A 234 -12.058 26.213 24.941 1.00 45.23 N
ANISOU 1779 NE ARG A 234 5934 7199 4053 -431 224 104 N
ATOM 1780 CZ ARG A 234 -12.017 25.731 26.172 1.00 52.05 C
ANISOU 1780 CZ ARG A 234 6701 8159 4916 -451 240 143 C
ATOM 1781 NH1 ARG A 234 -10.896 25.228 26.648 1.00 53.40 N
ANISOU 1781 NH1 ARG A 234 6871 8306 5113 -495 268 160 N
ATOM 1782 NH2 ARG A 234 -13.093 25.789 26.955 1.00 41.82 N
ANISOU 1782 NH2 ARG A 234 5305 6998 3586 -419 228 167 N
ATOM 1783 N ILE A 235 -14.787 23.628 20.223 1.00 40.98 N
ANISOU 1783 N ILE A 235 5469 6503 3598 -509 21 126 N
ATOM 1784 CA ILE A 235 -15.994 23.901 19.455 1.00 41.01 C
ANISOU 1784 CA ILE A 235 5464 6545 3572 -469 -35 107 C
ATOM 1785 C ILE A 235 -17.068 22.802 19.680 1.00 44.87 C
ANISOU 1785 C ILE A 235 5834 7110 4105 -535 -91 152 C
ATOM 1786 O ILE A 235 -18.248 23.120 19.729 1.00 44.05 O
ANISOU 1786 O ILE A 235 5657 7108 3974 -503 -125 154 O
ATOM 1787 CB ILE A 235 -15.642 24.143 17.935 1.00 42.61 C
ANISOU 1787 CB ILE A 235 5795 6644 3750 -439 -54 59 C
ATOM 1788 CG1 ILE A 235 -14.581 25.247 17.813 1.00 41.51 C
ANISOU 1788 CG1 ILE A 235 5764 6436 3572 -394 7 33 C
ATOM 1789 CG2 ILE A 235 -16.881 24.521 17.107 1.00 44.24 C
ANISOU 1789 CG2 ILE A 235 5999 6897 3914 -381 -116 36 C
ATOM 1790 CD1 ILE A 235 -13.849 25.494 16.354 1.00 31.98 C
ANISOU 1790 CD1 ILE A 235 4694 5125 2331 -377 13 -1 C
ATOM 1791 N CYS A 236 -16.665 21.561 19.892 1.00 43.94 N
ANISOU 1791 N CYS A 236 5693 6948 4055 -626 -99 189 N
ATOM 1792 CA CYS A 236 -17.625 20.459 19.993 1.00 46.44 C
ANISOU 1792 CA CYS A 236 5911 7309 4424 -708 -158 236 C
ATOM 1793 C CYS A 236 -17.848 19.934 21.418 1.00 51.07 C
ANISOU 1793 C CYS A 236 6375 7990 5039 -770 -135 322 C
ATOM 1794 O CYS A 236 -18.970 19.545 21.754 1.00 51.50 O
ANISOU 1794 O CYS A 236 6314 8148 5106 -817 -170 369 O
ATOM 1795 CB CYS A 236 -17.215 19.331 19.054 1.00 47.16 C
ANISOU 1795 CB CYS A 236 6070 7272 4578 -770 -207 218 C
ATOM 1796 SG CYS A 236 -17.052 19.857 17.332 1.00 52.17 S
ANISOU 1796 SG CYS A 236 6838 7823 5163 -697 -238 122 S
ATOM 1797 N VAL A 237 -16.801 19.874 22.229 1.00 46.62 N
ANISOU 1797 N VAL A 237 5830 7399 4483 -775 -78 347 N
ATOM 1798 CA VAL A 237 -16.955 19.338 23.578 1.00 46.51 C
ANISOU 1798 CA VAL A 237 5706 7479 4488 -830 -56 437 C
ATOM 1799 C VAL A 237 -16.061 20.112 24.534 1.00 51.90 C
ANISOU 1799 C VAL A 237 6400 8197 5123 -772 16 430 C
ATOM 1800 O VAL A 237 -14.975 20.533 24.145 1.00 52.52 O
ANISOU 1800 O VAL A 237 6582 8179 5194 -733 44 375 O
ATOM 1801 CB VAL A 237 -16.675 17.807 23.602 1.00 49.61 C
ANISOU 1801 CB VAL A 237 6096 7780 4971 -940 -92 501 C
ATOM 1802 CG1 VAL A 237 -15.190 17.480 23.349 1.00 48.82 C
ANISOU 1802 CG1 VAL A 237 6110 7538 4900 -927 -69 471 C
ATOM 1803 CG2 VAL A 237 -17.200 17.154 24.872 1.00 49.35 C
ANISOU 1803 CG2 VAL A 237 5936 7858 4958 -1015 -84 616 C
ATOM 1804 N GLN A 238 -16.536 20.315 25.773 1.00 49.06 N
ANISOU 1804 N GLN A 238 5928 7985 4725 -767 45 484 N
ATOM 1805 CA GLN A 238 -15.815 20.992 26.852 1.00 48.20 C
ANISOU 1805 CA GLN A 238 5811 7937 4565 -714 106 479 C
ATOM 1806 C GLN A 238 -15.970 20.178 28.122 1.00 54.09 C
ANISOU 1806 C GLN A 238 6444 8791 5317 -775 123 586 C
ATOM 1807 O GLN A 238 -16.898 19.364 28.211 1.00 55.51 O
ANISOU 1807 O GLN A 238 6536 9029 5526 -849 92 663 O
ATOM 1808 CB GLN A 238 -16.353 22.418 27.093 1.00 49.04 C
ANISOU 1808 CB GLN A 238 5900 8146 4586 -606 126 413 C
ATOM 1809 CG GLN A 238 -16.516 23.306 25.866 1.00 49.65 C
ANISOU 1809 CG GLN A 238 6076 8142 4648 -539 101 325 C
ATOM 1810 CD GLN A 238 -17.801 22.975 25.112 1.00 59.19 C
ANISOU 1810 CD GLN A 238 7233 9391 5867 -556 44 337 C
ATOM 1811 OE1 GLN A 238 -18.825 22.612 25.696 1.00 47.76 O
ANISOU 1811 OE1 GLN A 238 5653 8085 4408 -581 32 392 O
ATOM 1812 NE2 GLN A 238 -17.743 22.960 23.798 1.00 49.86 N
ANISOU 1812 NE2 GLN A 238 6145 8092 4709 -556 7 294 N
ATOM 1813 N GLY A 239 -15.088 20.417 29.100 1.00 48.85 N
ANISOU 1813 N GLY A 239 5779 8159 4621 -748 170 594 N
ATOM 1814 CA GLY A 239 -15.186 19.827 30.431 1.00 47.26 C
ANISOU 1814 CA GLY A 239 5473 8083 4402 -786 193 696 C
ATOM 1815 C GLY A 239 -16.345 20.490 31.143 1.00 51.87 C
ANISOU 1815 C GLY A 239 5936 8869 4902 -740 210 706 C
ATOM 1816 O GLY A 239 -16.726 21.595 30.762 1.00 50.39 O
ANISOU 1816 O GLY A 239 5770 8708 4667 -652 210 613 O
ATOM 1817 N LYS A 240 -16.918 19.848 32.185 1.00 52.55 N
ANISOU 1817 N LYS A 240 5896 9106 4966 -792 224 820 N
ATOM 1818 CA LYS A 240 -18.111 20.346 32.893 1.00 53.55 C
ANISOU 1818 CA LYS A 240 5882 9456 5007 -752 243 842 C
ATOM 1819 C LYS A 240 -17.950 21.758 33.577 1.00 56.89 C
ANISOU 1819 C LYS A 240 6301 9993 5321 -608 282 740 C
ATOM 1820 O LYS A 240 -18.973 22.370 33.923 1.00 58.50 O
ANISOU 1820 O LYS A 240 6408 10368 5450 -543 290 721 O
ATOM 1821 CB LYS A 240 -18.610 19.308 33.922 1.00 58.26 C
ANISOU 1821 CB LYS A 240 6346 10194 5595 -846 258 1000 C
ATOM 1822 CG LYS A 240 -17.836 19.267 35.245 1.00 74.37 C
ANISOU 1822 CG LYS A 240 8361 12325 7573 -819 307 1048 C
ATOM 1823 N GLU A 241 -16.716 22.256 33.789 1.00 50.70 N
ANISOU 1823 N GLU A 241 5613 9122 4527 -559 302 673 N
ATOM 1824 CA GLU A 241 -16.540 23.581 34.396 1.00 50.72 C
ANISOU 1824 CA GLU A 241 5624 9211 4437 -432 328 568 C
ATOM 1825 C GLU A 241 -16.075 24.606 33.363 1.00 51.83 C
ANISOU 1825 C GLU A 241 5906 9186 4600 -368 309 436 C
ATOM 1826 O GLU A 241 -15.713 25.741 33.700 1.00 51.37 O
ANISOU 1826 O GLU A 241 5892 9138 4487 -272 320 336 O
ATOM 1827 CB GLU A 241 -15.559 23.527 35.584 1.00 52.93 C
ANISOU 1827 CB GLU A 241 5892 9549 4672 -420 363 585 C
ATOM 1828 CG GLU A 241 -16.050 22.722 36.790 1.00 66.72 C
ANISOU 1828 CG GLU A 241 7494 11492 6365 -461 389 717 C
ATOM 1829 CD GLU A 241 -17.354 23.113 37.478 1.00112.98 C
ANISOU 1829 CD GLU A 241 13210 17597 12122 -401 409 733 C
ATOM 1830 OE1 GLU A 241 -17.851 22.289 38.284 1.00121.17 O
ANISOU 1830 OE1 GLU A 241 14123 18790 13124 -460 432 865 O
ATOM 1831 OE2 GLU A 241 -17.877 24.226 37.228 1.00112.97 O
ANISOU 1831 OE2 GLU A 241 13216 17636 12073 -294 402 619 O
ATOM 1832 N GLU A 242 -16.076 24.190 32.098 1.00 45.73 N
ANISOU 1832 N GLU A 242 5207 8258 3908 -424 276 439 N
ATOM 1833 CA GLU A 242 -15.620 24.996 30.992 1.00 44.27 C
ANISOU 1833 CA GLU A 242 5160 7913 3748 -380 259 338 C
ATOM 1834 C GLU A 242 -16.753 25.278 30.026 1.00 48.19 C
ANISOU 1834 C GLU A 242 5656 8408 4247 -351 221 314 C
ATOM 1835 O GLU A 242 -17.811 24.645 30.094 1.00 48.95 O
ANISOU 1835 O GLU A 242 5642 8612 4343 -387 203 381 O
ATOM 1836 CB GLU A 242 -14.467 24.289 30.296 1.00 45.28 C
ANISOU 1836 CB GLU A 242 5386 7861 3956 -458 257 351 C
ATOM 1837 CG GLU A 242 -13.248 24.130 31.200 1.00 52.96 C
ANISOU 1837 CG GLU A 242 6365 8834 4922 -473 291 361 C
ATOM 1838 CD GLU A 242 -11.896 24.205 30.529 1.00 57.52 C
ANISOU 1838 CD GLU A 242 7060 9246 5547 -494 299 313 C
ATOM 1839 OE1 GLU A 242 -11.858 24.166 29.278 1.00 49.76 O
ANISOU 1839 OE1 GLU A 242 6161 8137 4610 -512 279 288 O
ATOM 1840 OE2 GLU A 242 -10.876 24.352 31.247 1.00 50.67 O
ANISOU 1840 OE2 GLU A 242 6199 8387 4665 -489 325 297 O
ATOM 1841 N ARG A 243 -16.572 26.270 29.168 1.00 43.03 N
ANISOU 1841 N ARG A 243 5116 7644 3588 -284 205 223 N
ATOM 1842 CA ARG A 243 -17.607 26.572 28.196 1.00 42.52 C
ANISOU 1842 CA ARG A 243 5061 7576 3520 -243 163 199 C
ATOM 1843 C ARG A 243 -17.035 26.629 26.817 1.00 45.58 C
ANISOU 1843 C ARG A 243 5588 7772 3957 -266 141 165 C
ATOM 1844 O ARG A 243 -15.813 26.689 26.656 1.00 44.86 O
ANISOU 1844 O ARG A 243 5592 7559 3894 -296 166 147 O
ATOM 1845 CB ARG A 243 -18.289 27.904 28.523 1.00 41.43 C
ANISOU 1845 CB ARG A 243 4915 7526 3302 -102 158 120 C
ATOM 1846 CG ARG A 243 -19.132 27.900 29.802 1.00 44.86 C
ANISOU 1846 CG ARG A 243 5190 8189 3667 -56 176 145 C
ATOM 1847 CD ARG A 243 -20.058 29.101 29.868 1.00 44.69 C
ANISOU 1847 CD ARG A 243 5151 8261 3569 97 155 63 C
ATOM 1848 NE ARG A 243 -19.512 30.338 29.282 1.00 42.84 N
ANISOU 1848 NE ARG A 243 5080 7868 3329 187 138 -39 N
ATOM 1849 CZ ARG A 243 -20.196 31.482 29.234 1.00 60.14 C
ANISOU 1849 CZ ARG A 243 7292 10096 5462 333 110 -120 C
ATOM 1850 NH1 ARG A 243 -21.404 31.560 29.769 1.00 44.93 N
ANISOU 1850 NH1 ARG A 243 5225 8376 3471 414 101 -120 N
ATOM 1851 NH2 ARG A 243 -19.669 32.557 28.660 1.00 45.45 N
ANISOU 1851 NH2 ARG A 243 5594 8069 3607 401 90 -199 N
ATOM 1852 N ASN A 244 -17.928 26.673 25.796 1.00 43.23 N
ANISOU 1852 N ASN A 244 5301 7463 3661 -245 95 154 N
ATOM 1853 CA ASN A 244 -17.525 26.886 24.403 1.00 42.42 C
ANISOU 1853 CA ASN A 244 5335 7198 3583 -244 72 116 C
ATOM 1854 C ASN A 244 -17.193 28.393 24.262 1.00 43.92 C
ANISOU 1854 C ASN A 244 5635 7328 3726 -137 82 38 C
ATOM 1855 O ASN A 244 -17.219 29.133 25.245 1.00 43.20 O
ANISOU 1855 O ASN A 244 5514 7308 3592 -72 102 8 O
ATOM 1856 CB ASN A 244 -18.692 26.455 23.465 1.00 41.06 C
ANISOU 1856 CB ASN A 244 5125 7058 3418 -249 12 128 C
ATOM 1857 CG ASN A 244 -18.290 26.025 22.091 1.00 46.53 C
ANISOU 1857 CG ASN A 244 5923 7607 4149 -293 -16 117 C
ATOM 1858 OD1 ASN A 244 -17.362 26.552 21.485 1.00 46.29 O
ANISOU 1858 OD1 ASN A 244 6023 7450 4114 -274 3 80 O
ATOM 1859 ND2 ASN A 244 -18.994 25.052 21.565 1.00 37.49 N
ANISOU 1859 ND2 ASN A 244 4719 6486 3038 -355 -64 148 N
ATOM 1860 N TYR A 245 -16.978 28.858 23.054 1.00 41.93 N
ANISOU 1860 N TYR A 245 5507 6951 3475 -114 62 7 N
ATOM 1861 CA TYR A 245 -16.748 30.267 22.777 1.00 41.28 C
ANISOU 1861 CA TYR A 245 5542 6791 3353 -21 62 -53 C
ATOM 1862 C TYR A 245 -17.927 31.163 23.307 1.00 47.13 C
ANISOU 1862 C TYR A 245 6226 7647 4032 109 32 -92 C
ATOM 1863 O TYR A 245 -19.095 30.746 23.308 1.00 46.20 O
ANISOU 1863 O TYR A 245 5999 7656 3898 133 -1 -72 O
ATOM 1864 CB TYR A 245 -16.473 30.434 21.288 1.00 40.46 C
ANISOU 1864 CB TYR A 245 5568 6552 3254 -26 42 -59 C
ATOM 1865 CG TYR A 245 -15.106 29.858 21.000 1.00 41.36 C
ANISOU 1865 CG TYR A 245 5741 6561 3413 -128 85 -40 C
ATOM 1866 CD1 TYR A 245 -13.957 30.432 21.552 1.00 42.87 C
ANISOU 1866 CD1 TYR A 245 5987 6690 3611 -147 132 -60 C
ATOM 1867 CD2 TYR A 245 -14.960 28.664 20.282 1.00 40.23 C
ANISOU 1867 CD2 TYR A 245 5584 6395 3307 -206 75 -8 C
ATOM 1868 CE1 TYR A 245 -12.694 29.879 21.337 1.00 43.05 C
ANISOU 1868 CE1 TYR A 245 6046 6640 3671 -236 173 -45 C
ATOM 1869 CE2 TYR A 245 -13.695 28.121 20.029 1.00 39.59 C
ANISOU 1869 CE2 TYR A 245 5552 6230 3261 -283 113 2 C
ATOM 1870 CZ TYR A 245 -12.566 28.721 20.588 1.00 47.95 C
ANISOU 1870 CZ TYR A 245 6655 7242 4322 -297 165 -14 C
ATOM 1871 OH TYR A 245 -11.296 28.217 20.434 1.00 46.81 O
ANISOU 1871 OH TYR A 245 6542 7036 4208 -366 205 -6 O
ATOM 1872 N HIS A 246 -17.573 32.359 23.843 1.00 44.15 N
ANISOU 1872 N HIS A 246 5919 7232 3625 189 44 -150 N
ATOM 1873 CA HIS A 246 -18.522 33.292 24.477 1.00 45.22 C
ANISOU 1873 CA HIS A 246 6013 7469 3699 330 17 -203 C
ATOM 1874 C HIS A 246 -19.763 33.574 23.627 1.00 50.36 C
ANISOU 1874 C HIS A 246 6657 8160 4316 424 -41 -210 C
ATOM 1875 O HIS A 246 -20.859 33.615 24.176 1.00 52.67 O
ANISOU 1875 O HIS A 246 6826 8621 4566 504 -61 -222 O
ATOM 1876 CB HIS A 246 -17.837 34.625 24.853 1.00 45.86 C
ANISOU 1876 CB HIS A 246 6219 7443 3764 401 23 -276 C
ATOM 1877 CG HIS A 246 -16.835 34.537 25.968 1.00 48.20 C
ANISOU 1877 CG HIS A 246 6493 7748 4075 341 69 -290 C
ATOM 1878 ND1 HIS A 246 -17.012 33.672 27.043 1.00 49.16 N
ANISOU 1878 ND1 HIS A 246 6459 8034 4186 301 98 -257 N
ATOM 1879 CD2 HIS A 246 -15.707 35.264 26.177 1.00 48.73 C
ANISOU 1879 CD2 HIS A 246 6670 7687 4159 321 87 -334 C
ATOM 1880 CE1 HIS A 246 -15.943 33.841 27.814 1.00 47.58 C
ANISOU 1880 CE1 HIS A 246 6282 7799 3995 260 131 -282 C
ATOM 1881 NE2 HIS A 246 -15.161 34.821 27.365 1.00 47.62 N
ANISOU 1881 NE2 HIS A 246 6440 7635 4017 272 123 -335 N
ATOM 1882 N ILE A 247 -19.591 33.736 22.297 1.00 46.37 N
ANISOU 1882 N ILE A 247 6275 7519 3825 416 -66 -201 N
ATOM 1883 CA ILE A 247 -20.635 34.052 21.327 1.00 45.27 C
ANISOU 1883 CA ILE A 247 6154 7396 3651 507 -128 -208 C
ATOM 1884 C ILE A 247 -21.849 33.132 21.483 1.00 51.37 C
ANISOU 1884 C ILE A 247 6743 8362 4413 499 -155 -179 C
ATOM 1885 O ILE A 247 -22.975 33.617 21.396 1.00 52.23 O
ANISOU 1885 O ILE A 247 6801 8573 4472 621 -202 -207 O
ATOM 1886 CB ILE A 247 -20.108 34.031 19.849 1.00 46.32 C
ANISOU 1886 CB ILE A 247 6432 7368 3800 462 -142 -183 C
ATOM 1887 CG1 ILE A 247 -21.189 34.515 18.829 1.00 46.12 C
ANISOU 1887 CG1 ILE A 247 6441 7358 3725 578 -213 -194 C
ATOM 1888 CG2 ILE A 247 -19.497 32.669 19.428 1.00 43.88 C
ANISOU 1888 CG2 ILE A 247 6089 7040 3544 306 -116 -131 C
ATOM 1889 CD1 ILE A 247 -21.778 35.940 19.099 1.00 47.90 C
ANISOU 1889 CD1 ILE A 247 6725 7578 3896 757 -250 -249 C
ATOM 1890 N PHE A 248 -21.630 31.823 21.731 1.00 46.54 N
ANISOU 1890 N PHE A 248 6032 7802 3850 358 -129 -124 N
ATOM 1891 CA PHE A 248 -22.746 30.877 21.876 1.00 46.12 C
ANISOU 1891 CA PHE A 248 5803 7923 3798 323 -157 -85 C
ATOM 1892 C PHE A 248 -23.662 31.240 23.030 1.00 52.58 C
ANISOU 1892 C PHE A 248 6475 8940 4561 413 -152 -102 C
ATOM 1893 O PHE A 248 -24.874 31.117 22.907 1.00 55.77 O
ANISOU 1893 O PHE A 248 6763 9494 4934 465 -193 -101 O
ATOM 1894 CB PHE A 248 -22.234 29.449 22.052 1.00 45.12 C
ANISOU 1894 CB PHE A 248 5614 7789 3739 152 -130 -18 C
ATOM 1895 CG PHE A 248 -21.566 28.909 20.815 1.00 44.10 C
ANISOU 1895 CG PHE A 248 5600 7498 3656 72 -146 -8 C
ATOM 1896 CD1 PHE A 248 -22.313 28.553 19.701 1.00 45.91 C
ANISOU 1896 CD1 PHE A 248 5824 7734 3885 69 -209 -9 C
ATOM 1897 CD2 PHE A 248 -20.185 28.745 20.765 1.00 44.54 C
ANISOU 1897 CD2 PHE A 248 5765 7410 3750 3 -99 -2 C
ATOM 1898 CE1 PHE A 248 -21.694 28.055 18.545 1.00 45.80 C
ANISOU 1898 CE1 PHE A 248 5918 7581 3901 6 -225 -8 C
ATOM 1899 CE2 PHE A 248 -19.568 28.234 19.621 1.00 47.13 C
ANISOU 1899 CE2 PHE A 248 6191 7608 4109 -59 -110 2 C
ATOM 1900 CZ PHE A 248 -20.328 27.910 18.505 1.00 45.03 C
ANISOU 1900 CZ PHE A 248 5926 7346 3835 -54 -173 -3 C
ATOM 1901 N TYR A 249 -23.096 31.725 24.126 1.00 49.12 N
ANISOU 1901 N TYR A 249 6041 8515 4106 441 -104 -125 N
ATOM 1902 CA TYR A 249 -23.844 32.057 25.338 1.00 49.44 C
ANISOU 1902 CA TYR A 249 5942 8758 4085 531 -90 -146 C
ATOM 1903 C TYR A 249 -24.392 33.474 25.267 1.00 54.56 C
ANISOU 1903 C TYR A 249 6652 9411 4666 728 -127 -235 C
ATOM 1904 O TYR A 249 -25.494 33.703 25.734 1.00 54.42 O
ANISOU 1904 O TYR A 249 6504 9587 4588 833 -145 -257 O
ATOM 1905 CB TYR A 249 -22.958 31.836 26.578 1.00 48.67 C
ANISOU 1905 CB TYR A 249 5817 8681 3992 472 -27 -132 C
ATOM 1906 CG TYR A 249 -22.341 30.454 26.574 1.00 47.02 C
ANISOU 1906 CG TYR A 249 5572 8438 3855 288 2 -41 C
ATOM 1907 CD1 TYR A 249 -21.129 30.222 25.941 1.00 47.79 C
ANISOU 1907 CD1 TYR A 249 5812 8332 4016 201 15 -34 C
ATOM 1908 CD2 TYR A 249 -23.044 29.348 27.066 1.00 47.08 C
ANISOU 1908 CD2 TYR A 249 5405 8612 3870 201 10 40 C
ATOM 1909 CE1 TYR A 249 -20.599 28.946 25.834 1.00 46.27 C
ANISOU 1909 CE1 TYR A 249 5593 8097 3888 50 32 41 C
ATOM 1910 CE2 TYR A 249 -22.521 28.056 26.958 1.00 46.29 C
ANISOU 1910 CE2 TYR A 249 5289 8455 3845 36 23 124 C
ATOM 1911 CZ TYR A 249 -21.297 27.869 26.331 1.00 49.00 C
ANISOU 1911 CZ TYR A 249 5782 8589 4248 -30 32 118 C
ATOM 1912 OH TYR A 249 -20.707 26.646 26.174 1.00 53.34 O
ANISOU 1912 OH TYR A 249 6331 9065 4870 -172 40 187 O
ATOM 1913 N ARG A 250 -23.637 34.412 24.670 1.00 52.74 N
ANISOU 1913 N ARG A 250 6620 8973 4447 778 -140 -284 N
ATOM 1914 CA ARG A 250 -24.082 35.790 24.470 1.00 53.96 C
ANISOU 1914 CA ARG A 250 6868 9085 4548 965 -185 -366 C
ATOM 1915 C ARG A 250 -25.319 35.811 23.587 1.00 61.79 C
ANISOU 1915 C ARG A 250 7810 10161 5508 1051 -249 -363 C
ATOM 1916 O ARG A 250 -26.258 36.547 23.879 1.00 64.49 O
ANISOU 1916 O ARG A 250 8100 10618 5784 1220 -285 -419 O
ATOM 1917 CB ARG A 250 -22.965 36.637 23.859 1.00 50.88 C
ANISOU 1917 CB ARG A 250 6707 8435 4190 963 -188 -392 C
ATOM 1918 CG ARG A 250 -21.877 36.915 24.864 1.00 44.33 C
ANISOU 1918 CG ARG A 250 5923 7544 3377 923 -140 -425 C
ATOM 1919 CD ARG A 250 -20.666 37.576 24.223 1.00 54.54 C
ANISOU 1919 CD ARG A 250 7423 8583 4715 872 -134 -432 C
ATOM 1920 NE ARG A 250 -19.564 37.617 25.185 1.00 64.52 N
ANISOU 1920 NE ARG A 250 8703 9808 6003 800 -86 -454 N
ATOM 1921 CZ ARG A 250 -18.458 38.340 25.057 1.00 72.09 C
ANISOU 1921 CZ ARG A 250 9818 10578 6995 765 -77 -481 C
ATOM 1922 NH1 ARG A 250 -18.281 39.114 23.997 1.00 57.44 N
ANISOU 1922 NH1 ARG A 250 8129 8545 5152 792 -109 -479 N
ATOM 1923 NH2 ARG A 250 -17.536 38.322 26.009 1.00 56.78 N
ANISOU 1923 NH2 ARG A 250 7868 8633 5073 702 -39 -508 N
ATOM 1924 N LEU A 251 -25.348 34.941 22.557 1.00 56.64 N
ANISOU 1924 N LEU A 251 7158 9467 4897 938 -266 -301 N
ATOM 1925 CA LEU A 251 -26.447 34.805 21.620 1.00 57.52 C
ANISOU 1925 CA LEU A 251 7217 9656 4983 994 -331 -294 C
ATOM 1926 C LEU A 251 -27.654 34.136 22.284 1.00 60.89 C
ANISOU 1926 C LEU A 251 7401 10355 5380 996 -337 -276 C
ATOM 1927 O LEU A 251 -28.765 34.649 22.155 1.00 60.13 O
ANISOU 1927 O LEU A 251 7230 10391 5224 1140 -388 -313 O
ATOM 1928 CB LEU A 251 -25.963 34.008 20.383 1.00 57.09 C
ANISOU 1928 CB LEU A 251 7241 9470 4982 858 -345 -242 C
ATOM 1929 CG LEU A 251 -26.737 34.034 19.092 1.00 63.23 C
ANISOU 1929 CG LEU A 251 8041 10249 5734 912 -419 -242 C
ATOM 1930 CD1 LEU A 251 -26.935 35.444 18.582 1.00 64.65 C
ANISOU 1930 CD1 LEU A 251 8367 10341 5857 1099 -464 -293 C
ATOM 1931 CD2 LEU A 251 -26.002 33.217 18.047 1.00 64.59 C
ANISOU 1931 CD2 LEU A 251 8302 10282 5957 768 -418 -199 C
ATOM 1932 N CYS A 252 -27.459 33.016 23.003 1.00 57.49 N
ANISOU 1932 N CYS A 252 6841 10014 4989 841 -288 -215 N
ATOM 1933 CA CYS A 252 -28.596 32.357 23.671 1.00 57.99 C
ANISOU 1933 CA CYS A 252 6666 10345 5024 826 -288 -182 C
ATOM 1934 C CYS A 252 -29.179 33.266 24.778 1.00 62.42 C
ANISOU 1934 C CYS A 252 7140 11079 5498 999 -272 -243 C
ATOM 1935 O CYS A 252 -30.395 33.361 24.881 1.00 63.32 O
ANISOU 1935 O CYS A 252 7102 11402 5555 1092 -303 -258 O
ATOM 1936 CB CYS A 252 -28.212 30.981 24.212 1.00 57.44 C
ANISOU 1936 CB CYS A 252 6491 10316 5016 619 -240 -91 C
ATOM 1937 SG CYS A 252 -27.890 29.740 22.924 1.00 60.67 S
ANISOU 1937 SG CYS A 252 6955 10577 5520 432 -278 -31 S
ATOM 1938 N ALA A 253 -28.334 34.005 25.512 1.00 57.34 N
ANISOU 1938 N ALA A 253 6599 10347 4839 1055 -231 -290 N
ATOM 1939 CA ALA A 253 -28.809 34.896 26.569 1.00 59.26 C
ANISOU 1939 CA ALA A 253 6777 10744 4996 1230 -220 -364 C
ATOM 1940 C ALA A 253 -29.393 36.224 26.071 1.00 67.47 C
ANISOU 1940 C ALA A 253 7908 11748 5979 1458 -287 -461 C
ATOM 1941 O ALA A 253 -30.334 36.703 26.709 1.00 69.74 O
ANISOU 1941 O ALA A 253 8069 12244 6184 1616 -299 -515 O
ATOM 1942 CB ALA A 253 -27.692 35.200 27.556 1.00 59.01 C
ANISOU 1942 CB ALA A 253 6825 10627 4968 1212 -164 -392 C
ATOM 1943 N GLY A 254 -28.819 36.815 24.999 1.00 62.21 N
ANISOU 1943 N GLY A 254 7458 10829 5352 1478 -327 -481 N
ATOM 1944 CA GLY A 254 -29.174 38.150 24.527 1.00 61.79 C
ANISOU 1944 CA GLY A 254 7536 10687 5252 1690 -392 -565 C
ATOM 1945 C GLY A 254 -30.021 38.328 23.286 1.00 66.84 C
ANISOU 1945 C GLY A 254 8195 11326 5875 1773 -469 -561 C
ATOM 1946 O GLY A 254 -30.717 39.340 23.175 1.00 66.80 O
ANISOU 1946 O GLY A 254 8220 11352 5808 1986 -526 -632 O
ATOM 1947 N ALA A 255 -29.953 37.392 22.324 1.00 63.30 N
ANISOU 1947 N ALA A 255 7741 10832 5476 1621 -479 -485 N
ATOM 1948 CA ALA A 255 -30.711 37.506 21.074 1.00 64.22 C
ANISOU 1948 CA ALA A 255 7881 10947 5572 1693 -558 -480 C
ATOM 1949 C ALA A 255 -32.194 37.782 21.338 1.00 70.07 C
ANISOU 1949 C ALA A 255 8438 11953 6234 1865 -607 -524 C
ATOM 1950 O ALA A 255 -32.754 37.266 22.298 1.00 71.09 O
ANISOU 1950 O ALA A 255 8356 12315 6340 1842 -571 -519 O
ATOM 1951 CB ALA A 255 -30.559 36.245 20.243 1.00 63.98 C
ANISOU 1951 CB ALA A 255 7814 10895 5600 1492 -559 -401 C
ATOM 1952 N SER A 256 -32.796 38.649 20.530 1.00 66.40 N
ANISOU 1952 N SER A 256 8053 11454 5720 2047 -687 -566 N
ATOM 1953 CA SER A 256 -34.211 38.977 20.602 1.00 68.53 C
ANISOU 1953 CA SER A 256 8159 11967 5910 2233 -747 -613 C
ATOM 1954 C SER A 256 -35.045 37.712 20.311 1.00 76.91 C
ANISOU 1954 C SER A 256 8988 13252 6981 2096 -758 -554 C
ATOM 1955 O SER A 256 -34.536 36.797 19.650 1.00 76.91 O
ANISOU 1955 O SER A 256 9023 13150 7048 1898 -750 -488 O
ATOM 1956 CB SER A 256 -34.527 40.065 19.575 1.00 72.49 C
ANISOU 1956 CB SER A 256 8832 12343 6370 2435 -838 -655 C
ATOM 1957 OG SER A 256 -34.403 39.601 18.236 1.00 78.61 O
ANISOU 1957 OG SER A 256 9686 13011 7172 2340 -880 -597 O
ATOM 1958 N GLU A 257 -36.325 37.669 20.733 1.00 75.51 N
ANISOU 1958 N GLU A 257 8579 13372 6737 2205 -784 -582 N
ATOM 1959 CA GLU A 257 -37.191 36.522 20.436 1.00 76.34 C
ANISOU 1959 CA GLU A 257 8456 13695 6855 2072 -805 -527 C
ATOM 1960 C GLU A 257 -37.338 36.298 18.908 1.00 81.52 C
ANISOU 1960 C GLU A 257 9202 14240 7532 2039 -890 -508 C
ATOM 1961 O GLU A 257 -37.592 35.171 18.463 1.00 80.34 O
ANISOU 1961 O GLU A 257 8937 14161 7428 1856 -904 -453 O
ATOM 1962 CB GLU A 257 -38.565 36.688 21.094 1.00 79.47 C
ANISOU 1962 CB GLU A 257 8592 14439 7165 2218 -823 -567 C
ATOM 1963 CG GLU A 257 -38.639 36.046 22.468 1.00 87.38 C
ANISOU 1963 CG GLU A 257 9388 15649 8164 2110 -732 -531 C
ATOM 1964 CD GLU A 257 -38.423 34.545 22.509 1.00107.50 C
ANISOU 1964 CD GLU A 257 11818 18231 10796 1808 -691 -422 C
ATOM 1965 OE1 GLU A 257 -38.996 33.826 21.657 1.00108.81 O
ANISOU 1965 OE1 GLU A 257 11893 18458 10991 1707 -748 -385 O
ATOM 1966 OE2 GLU A 257 -37.670 34.086 23.395 1.00104.35 O
ANISOU 1966 OE2 GLU A 257 11421 17794 10434 1675 -607 -376 O
ATOM 1967 N ASP A 258 -37.112 37.366 18.116 1.00 79.41 N
ANISOU 1967 N ASP A 258 9152 13788 7232 2211 -946 -551 N
ATOM 1968 CA ASP A 258 -37.158 37.301 16.663 1.00 79.53 C
ANISOU 1968 CA ASP A 258 9282 13688 7250 2205 -1025 -534 C
ATOM 1969 C ASP A 258 -35.919 36.565 16.149 1.00 81.19 C
ANISOU 1969 C ASP A 258 9643 13662 7545 1975 -981 -472 C
ATOM 1970 O ASP A 258 -36.049 35.682 15.288 1.00 80.94 O
ANISOU 1970 O ASP A 258 9571 13640 7543 1839 -1016 -437 O
ATOM 1971 CB ASP A 258 -37.278 38.704 16.029 1.00 82.79 C
ANISOU 1971 CB ASP A 258 9889 13973 7595 2463 -1094 -586 C
ATOM 1972 CG ASP A 258 -37.186 38.689 14.510 1.00 98.36 C
ANISOU 1972 CG ASP A 258 12009 15805 9559 2460 -1169 -558 C
ATOM 1973 OD1 ASP A 258 -37.993 37.965 13.871 1.00101.96 O
ANISOU 1973 OD1 ASP A 258 12319 16423 10000 2416 -1230 -549 O
ATOM 1974 OD2 ASP A 258 -36.284 39.370 13.960 1.00102.32 O
ANISOU 1974 OD2 ASP A 258 12770 16040 10067 2492 -1166 -544 O
ATOM 1975 N ILE A 259 -34.726 36.922 16.680 1.00 74.49 N
ANISOU 1975 N ILE A 259 8958 12610 6734 1935 -907 -465 N
ATOM 1976 CA ILE A 259 -33.468 36.297 16.276 1.00 71.74 C
ANISOU 1976 CA ILE A 259 8753 12042 6462 1734 -857 -411 C
ATOM 1977 C ILE A 259 -33.466 34.819 16.758 1.00 72.36 C
ANISOU 1977 C ILE A 259 8646 12242 6607 1502 -813 -361 C
ATOM 1978 O ILE A 259 -33.094 33.932 15.978 1.00 71.57 O
ANISOU 1978 O ILE A 259 8579 12058 6556 1344 -823 -322 O
ATOM 1979 CB ILE A 259 -32.234 37.130 16.748 1.00 73.63 C
ANISOU 1979 CB ILE A 259 9198 12055 6721 1757 -794 -422 C
ATOM 1980 CG1 ILE A 259 -32.182 38.475 15.964 1.00 74.81 C
ANISOU 1980 CG1 ILE A 259 9565 12041 6820 1954 -853 -452 C
ATOM 1981 CG2 ILE A 259 -30.917 36.360 16.538 1.00 71.87 C
ANISOU 1981 CG2 ILE A 259 9080 11649 6579 1537 -730 -366 C
ATOM 1982 CD1 ILE A 259 -31.153 39.534 16.472 1.00 81.10 C
ANISOU 1982 CD1 ILE A 259 10565 12618 7631 2007 -809 -474 C
ATOM 1983 N ARG A 260 -33.982 34.564 17.979 1.00 67.04 N
ANISOU 1983 N ARG A 260 7772 11775 5926 1495 -772 -362 N
ATOM 1984 CA ARG A 260 -34.083 33.237 18.602 1.00 66.04 C
ANISOU 1984 CA ARG A 260 7457 11778 5856 1286 -729 -303 C
ATOM 1985 C ARG A 260 -34.879 32.263 17.717 1.00 71.95 C
ANISOU 1985 C ARG A 260 8081 12632 6626 1182 -800 -277 C
ATOM 1986 O ARG A 260 -34.395 31.170 17.429 1.00 70.92 O
ANISOU 1986 O ARG A 260 7953 12421 6571 979 -790 -227 O
ATOM 1987 CB ARG A 260 -34.734 33.344 20.005 1.00 65.42 C
ANISOU 1987 CB ARG A 260 7176 11943 5737 1340 -682 -309 C
ATOM 1988 CG ARG A 260 -34.688 32.051 20.824 1.00 71.62 C
ANISOU 1988 CG ARG A 260 7788 12844 6580 1120 -623 -230 C
ATOM 1989 CD ARG A 260 -35.922 31.786 21.683 1.00 76.38 C
ANISOU 1989 CD ARG A 260 8108 13780 7132 1142 -615 -216 C
ATOM 1990 NE ARG A 260 -37.174 31.842 20.926 1.00 93.81 N
ANISOU 1990 NE ARG A 260 10189 16158 9298 1225 -702 -243 N
ATOM 1991 CZ ARG A 260 -37.682 30.842 20.211 1.00115.18 C
ANISOU 1991 CZ ARG A 260 12793 18920 12052 1074 -756 -201 C
ATOM 1992 NH1 ARG A 260 -38.826 31.001 19.557 1.00111.55 N
ANISOU 1992 NH1 ARG A 260 12213 18627 11543 1167 -840 -236 N
ATOM 1993 NH2 ARG A 260 -37.044 29.680 20.132 1.00 99.14 N
ANISOU 1993 NH2 ARG A 260 10780 16772 10117 833 -734 -129 N
ATOM 1994 N GLU A 261 -36.081 32.675 17.271 1.00 71.09 N
ANISOU 1994 N GLU A 261 7866 12695 6449 1327 -879 -317 N
ATOM 1995 CA GLU A 261 -36.997 31.875 16.451 1.00 72.08 C
ANISOU 1995 CA GLU A 261 7854 12950 6583 1250 -961 -307 C
ATOM 1996 C GLU A 261 -36.442 31.631 15.046 1.00 73.30 C
ANISOU 1996 C GLU A 261 8196 12891 6765 1194 -1015 -308 C
ATOM 1997 O GLU A 261 -36.477 30.498 14.570 1.00 71.42 O
ANISOU 1997 O GLU A 261 7904 12646 6588 1009 -1042 -279 O
ATOM 1998 CB GLU A 261 -38.384 32.545 16.371 1.00 75.45 C
ANISOU 1998 CB GLU A 261 8128 13621 6917 1452 -1032 -359 C
ATOM 1999 N ARG A 262 -35.912 32.687 14.409 1.00 69.56 N
ANISOU 1999 N ARG A 262 7946 12240 6244 1350 -1030 -341 N
ATOM 2000 CA ARG A 262 -35.319 32.657 13.074 1.00 68.94 C
ANISOU 2000 CA ARG A 262 8065 11961 6167 1329 -1074 -341 C
ATOM 2001 C ARG A 262 -34.100 31.699 13.039 1.00 69.98 C
ANISOU 2001 C ARG A 262 8288 11911 6389 1107 -1011 -297 C
ATOM 2002 O ARG A 262 -33.973 30.927 12.090 1.00 69.82 O
ANISOU 2002 O ARG A 262 8300 11834 6394 1000 -1056 -292 O
ATOM 2003 CB ARG A 262 -34.915 34.093 12.682 1.00 72.40 C
ANISOU 2003 CB ARG A 262 8726 12244 6540 1536 -1080 -366 C
ATOM 2004 CG ARG A 262 -34.449 34.302 11.248 1.00 86.32 C
ANISOU 2004 CG ARG A 262 10691 13833 8273 1560 -1131 -361 C
ATOM 2005 CD ARG A 262 -33.805 35.669 11.100 1.00 98.37 C
ANISOU 2005 CD ARG A 262 12451 15170 9755 1719 -1112 -363 C
ATOM 2006 NE ARG A 262 -34.566 36.554 10.215 1.00110.67 N
ANISOU 2006 NE ARG A 262 14076 16754 11221 1928 -1207 -385 N
ATOM 2007 CZ ARG A 262 -35.073 37.729 10.578 1.00125.17 C
ANISOU 2007 CZ ARG A 262 15940 18618 13000 2147 -1234 -416 C
ATOM 2008 NH1 ARG A 262 -34.910 38.176 11.817 1.00104.65 N
ANISOU 2008 NH1 ARG A 262 13307 16031 10424 2186 -1173 -437 N
ATOM 2009 NH2 ARG A 262 -35.740 38.469 9.701 1.00119.94 N
ANISOU 2009 NH2 ARG A 262 15347 17971 12254 2337 -1327 -430 N
ATOM 2010 N LEU A 263 -33.239 31.725 14.086 1.00 63.31 N
ANISOU 2010 N LEU A 263 7476 10990 5589 1045 -914 -271 N
ATOM 2011 CA LEU A 263 -32.050 30.875 14.187 1.00 61.36 C
ANISOU 2011 CA LEU A 263 7308 10580 5424 853 -850 -230 C
ATOM 2012 C LEU A 263 -32.319 29.547 14.925 1.00 67.22 C
ANISOU 2012 C LEU A 263 7854 11444 6241 662 -830 -188 C
ATOM 2013 O LEU A 263 -31.396 28.742 15.089 1.00 66.39 O
ANISOU 2013 O LEU A 263 7800 11216 6209 503 -783 -152 O
ATOM 2014 CB LEU A 263 -30.903 31.631 14.880 1.00 60.01 C
ANISOU 2014 CB LEU A 263 7288 10251 5262 886 -762 -224 C
ATOM 2015 CG LEU A 263 -30.383 32.900 14.201 1.00 64.65 C
ANISOU 2015 CG LEU A 263 8098 10673 5795 1038 -770 -250 C
ATOM 2016 CD1 LEU A 263 -29.215 33.464 14.963 1.00 64.13 C
ANISOU 2016 CD1 LEU A 263 8154 10458 5753 1029 -684 -243 C
ATOM 2017 CD2 LEU A 263 -29.968 32.639 12.766 1.00 66.91 C
ANISOU 2017 CD2 LEU A 263 8526 10823 6073 1001 -812 -242 C
ATOM 2018 N HIS A 264 -33.575 29.331 15.377 1.00 65.57 N
ANISOU 2018 N HIS A 264 7423 11478 6013 678 -865 -187 N
ATOM 2019 CA HIS A 264 -34.067 28.145 16.093 1.00 65.91 C
ANISOU 2019 CA HIS A 264 7255 11671 6118 501 -853 -135 C
ATOM 2020 C HIS A 264 -33.204 27.841 17.337 1.00 66.53 C
ANISOU 2020 C HIS A 264 7335 11699 6246 404 -748 -82 C
ATOM 2021 O HIS A 264 -32.886 26.687 17.617 1.00 66.09 O
ANISOU 2021 O HIS A 264 7230 11610 6270 211 -729 -25 O
ATOM 2022 CB HIS A 264 -34.171 26.924 15.153 1.00 67.61 C
ANISOU 2022 CB HIS A 264 7452 11838 6400 329 -923 -124 C
ATOM 2023 CG HIS A 264 -35.061 27.159 13.969 1.00 72.63 C
ANISOU 2023 CG HIS A 264 8070 12544 6982 419 -1033 -179 C
ATOM 2024 ND1 HIS A 264 -36.440 27.111 14.083 1.00 76.43 N
ANISOU 2024 ND1 HIS A 264 8332 13279 7431 451 -1093 -188 N
ATOM 2025 CD2 HIS A 264 -34.740 27.477 12.692 1.00 74.39 C
ANISOU 2025 CD2 HIS A 264 8466 12629 7171 488 -1089 -224 C
ATOM 2026 CE1 HIS A 264 -36.911 27.379 12.874 1.00 76.52 C
ANISOU 2026 CE1 HIS A 264 8390 13293 7393 539 -1190 -243 C
ATOM 2027 NE2 HIS A 264 -35.928 27.602 12.003 1.00 75.85 N
ANISOU 2027 NE2 HIS A 264 8542 12976 7303 565 -1190 -264 N
ATOM 2028 N LEU A 265 -32.843 28.890 18.079 1.00 61.00 N
ANISOU 2028 N LEU A 265 6693 10991 5494 542 -688 -103 N
ATOM 2029 CA LEU A 265 -32.059 28.781 19.297 1.00 60.52 C
ANISOU 2029 CA LEU A 265 6632 10902 5460 482 -593 -64 C
ATOM 2030 C LEU A 265 -32.967 28.464 20.494 1.00 67.18 C
ANISOU 2030 C LEU A 265 7229 12013 6282 458 -563 -24 C
ATOM 2031 O LEU A 265 -34.183 28.635 20.413 1.00 67.96 O
ANISOU 2031 O LEU A 265 7171 12319 6331 532 -610 -42 O
ATOM 2032 CB LEU A 265 -31.283 30.078 19.551 1.00 60.14 C
ANISOU 2032 CB LEU A 265 6758 10727 5364 641 -551 -115 C
ATOM 2033 CG LEU A 265 -30.237 30.494 18.491 1.00 64.69 C
ANISOU 2033 CG LEU A 265 7585 11038 5958 656 -562 -140 C
ATOM 2034 CD1 LEU A 265 -29.891 31.949 18.637 1.00 66.12 C
ANISOU 2034 CD1 LEU A 265 7910 11133 6080 840 -546 -195 C
ATOM 2035 CD2 LEU A 265 -28.949 29.668 18.589 1.00 62.21 C
ANISOU 2035 CD2 LEU A 265 7359 10555 5724 481 -506 -95 C
ATOM 2036 N SER A 266 -32.375 27.981 21.598 1.00 63.73 N
ANISOU 2036 N SER A 266 6753 11582 5878 353 -484 34 N
ATOM 2037 CA SER A 266 -33.052 27.673 22.865 1.00 63.93 C
ANISOU 2037 CA SER A 266 6558 11857 5876 320 -437 87 C
ATOM 2038 C SER A 266 -32.016 27.717 23.968 1.00 67.56 C
ANISOU 2038 C SER A 266 7077 12251 6341 292 -346 116 C
ATOM 2039 O SER A 266 -30.966 28.325 23.766 1.00 68.66 O
ANISOU 2039 O SER A 266 7416 12184 6488 349 -327 70 O
ATOM 2040 CB SER A 266 -33.781 26.330 22.814 1.00 66.93 C
ANISOU 2040 CB SER A 266 6755 12357 6317 120 -466 173 C
ATOM 2041 OG SER A 266 -32.993 25.289 22.266 1.00 74.94 O
ANISOU 2041 OG SER A 266 7876 13161 7435 -63 -480 217 O
ATOM 2042 N SER A 267 -32.291 27.112 25.135 1.00 62.24 N
ANISOU 2042 N SER A 267 6231 11759 5660 207 -291 193 N
ATOM 2043 CA SER A 267 -31.337 27.106 26.232 1.00 60.02 C
ANISOU 2043 CA SER A 267 5993 11438 5375 182 -209 223 C
ATOM 2044 C SER A 267 -30.123 26.214 25.862 1.00 60.16 C
ANISOU 2044 C SER A 267 6158 11203 5499 13 -200 273 C
ATOM 2045 O SER A 267 -30.276 25.259 25.092 1.00 59.86 O
ANISOU 2045 O SER A 267 6113 11094 5538 -127 -248 315 O
ATOM 2046 CB SER A 267 -32.003 26.681 27.543 1.00 62.84 C
ANISOU 2046 CB SER A 267 6121 12072 5683 138 -154 301 C
ATOM 2047 OG SER A 267 -32.842 25.549 27.409 1.00 69.63 O
ANISOU 2047 OG SER A 267 6806 13060 6588 -28 -180 396 O
ATOM 2048 N PRO A 268 -28.914 26.544 26.360 1.00 54.68 N
ANISOU 2048 N PRO A 268 5599 10369 4807 33 -145 257 N
ATOM 2049 CA PRO A 268 -27.703 25.800 25.962 1.00 54.21 C
ANISOU 2049 CA PRO A 268 5685 10073 4840 -102 -138 291 C
ATOM 2050 C PRO A 268 -27.715 24.274 26.139 1.00 58.74 C
ANISOU 2050 C PRO A 268 6170 10650 5497 -310 -140 406 C
ATOM 2051 O PRO A 268 -26.998 23.592 25.417 1.00 59.15 O
ANISOU 2051 O PRO A 268 6338 10506 5631 -410 -164 417 O
ATOM 2052 CB PRO A 268 -26.619 26.414 26.858 1.00 54.65 C
ANISOU 2052 CB PRO A 268 5830 10069 4865 -41 -71 266 C
ATOM 2053 CG PRO A 268 -27.072 27.813 27.064 1.00 58.75 C
ANISOU 2053 CG PRO A 268 6357 10677 5290 161 -72 170 C
ATOM 2054 CD PRO A 268 -28.562 27.676 27.245 1.00 55.85 C
ANISOU 2054 CD PRO A 268 5784 10564 4873 191 -96 193 C
ATOM 2055 N ASP A 269 -28.465 23.749 27.106 1.00 54.28 N
ANISOU 2055 N ASP A 269 5412 10302 4910 -374 -113 491 N
ATOM 2056 CA ASP A 269 -28.593 22.317 27.382 1.00 53.63 C
ANISOU 2056 CA ASP A 269 5235 10235 4905 -578 -117 616 C
ATOM 2057 C ASP A 269 -29.210 21.538 26.186 1.00 56.87 C
ANISOU 2057 C ASP A 269 5632 10581 5396 -688 -204 624 C
ATOM 2058 O ASP A 269 -29.098 20.315 26.148 1.00 56.09 O
ANISOU 2058 O ASP A 269 5512 10412 5386 -865 -225 711 O
ATOM 2059 CB ASP A 269 -29.449 22.110 28.650 1.00 56.51 C
ANISOU 2059 CB ASP A 269 5377 10885 5207 -605 -69 707 C
ATOM 2060 CG ASP A 269 -30.853 22.703 28.540 1.00 66.64 C
ANISOU 2060 CG ASP A 269 6497 12408 6415 -511 -94 670 C
ATOM 2061 OD1 ASP A 269 -30.960 23.937 28.346 1.00 63.89 O
ANISOU 2061 OD1 ASP A 269 6199 12087 5989 -316 -97 556 O
ATOM 2062 OD2 ASP A 269 -31.851 21.929 28.693 1.00 72.49 O
ANISOU 2062 OD2 ASP A 269 7054 13316 7174 -633 -113 758 O
ATOM 2063 N ASN A 270 -29.835 22.245 25.203 1.00 53.80 N
ANISOU 2063 N ASN A 270 5261 10206 4974 -580 -261 530 N
ATOM 2064 CA ASN A 270 -30.443 21.624 24.028 1.00 53.63 C
ANISOU 2064 CA ASN A 270 5229 10133 5013 -664 -352 517 C
ATOM 2065 C ASN A 270 -29.429 21.420 22.900 1.00 57.13 C
ANISOU 2065 C ASN A 270 5891 10294 5520 -682 -389 460 C
ATOM 2066 O ASN A 270 -29.796 20.888 21.842 1.00 57.48 O
ANISOU 2066 O ASN A 270 5955 10274 5613 -744 -470 435 O
ATOM 2067 CB ASN A 270 -31.638 22.449 23.550 1.00 57.18 C
ANISOU 2067 CB ASN A 270 5583 10756 5387 -532 -398 448 C
ATOM 2068 CG ASN A 270 -32.736 22.516 24.596 1.00 75.33 C
ANISOU 2068 CG ASN A 270 7640 13360 7621 -522 -366 505 C
ATOM 2069 OD1 ASN A 270 -33.323 21.505 24.981 1.00 69.48 O
ANISOU 2069 OD1 ASN A 270 6739 12735 6925 -689 -373 604 O
ATOM 2070 ND2 ASN A 270 -32.919 23.676 25.198 1.00 66.14 N
ANISOU 2070 ND2 ASN A 270 6451 12329 6351 -333 -321 450 N
ATOM 2071 N PHE A 271 -28.136 21.769 23.136 1.00 51.53 N
ANISOU 2071 N PHE A 271 5341 9427 4811 -636 -332 441 N
ATOM 2072 CA PHE A 271 -27.122 21.625 22.092 1.00 50.13 C
ANISOU 2072 CA PHE A 271 5362 9003 4682 -645 -358 387 C
ATOM 2073 C PHE A 271 -25.961 20.779 22.569 1.00 53.77 C
ANISOU 2073 C PHE A 271 5895 9321 5214 -755 -318 445 C
ATOM 2074 O PHE A 271 -25.300 21.124 23.551 1.00 52.92 O
ANISOU 2074 O PHE A 271 5797 9230 5079 -721 -245 470 O
ATOM 2075 CB PHE A 271 -26.644 23.008 21.585 1.00 50.59 C
ANISOU 2075 CB PHE A 271 5565 8989 4668 -466 -341 290 C
ATOM 2076 CG PHE A 271 -27.790 23.877 21.098 1.00 52.29 C
ANISOU 2076 CG PHE A 271 5720 9340 4810 -339 -389 233 C
ATOM 2077 CD1 PHE A 271 -28.309 23.723 19.815 1.00 55.25 C
ANISOU 2077 CD1 PHE A 271 6125 9675 5193 -336 -472 189 C
ATOM 2078 CD2 PHE A 271 -28.382 24.811 21.939 1.00 55.03 C
ANISOU 2078 CD2 PHE A 271 5969 9866 5076 -215 -355 221 C
ATOM 2079 CE1 PHE A 271 -29.381 24.511 19.374 1.00 56.87 C
ANISOU 2079 CE1 PHE A 271 6268 10013 5326 -210 -521 139 C
ATOM 2080 CE2 PHE A 271 -29.450 25.602 21.496 1.00 58.82 C
ANISOU 2080 CE2 PHE A 271 6388 10474 5486 -83 -404 166 C
ATOM 2081 CZ PHE A 271 -29.935 25.455 20.212 1.00 56.12 C
ANISOU 2081 CZ PHE A 271 6081 10088 5155 -80 -487 128 C
ATOM 2082 N ARG A 272 -25.677 19.684 21.834 1.00 49.56 N
ANISOU 2082 N ARG A 272 5420 8642 4770 -875 -372 457 N
ATOM 2083 CA ARG A 272 -24.555 18.796 22.136 1.00 48.15 C
ANISOU 2083 CA ARG A 272 5322 8307 4665 -970 -347 504 C
ATOM 2084 C ARG A 272 -23.229 19.573 22.205 1.00 50.84 C
ANISOU 2084 C ARG A 272 5813 8534 4970 -868 -282 453 C
ATOM 2085 O ARG A 272 -22.390 19.283 23.059 1.00 52.65 O
ANISOU 2085 O ARG A 272 6057 8729 5218 -900 -229 502 O
ATOM 2086 CB ARG A 272 -24.470 17.681 21.100 1.00 49.00 C
ANISOU 2086 CB ARG A 272 5495 8259 4862 -1077 -428 490 C
ATOM 2087 CG ARG A 272 -23.356 16.668 21.333 1.00 62.56 C
ANISOU 2087 CG ARG A 272 7298 9810 6663 -1168 -416 535 C
ATOM 2088 CD ARG A 272 -22.914 16.043 20.032 1.00 73.48 C
ANISOU 2088 CD ARG A 272 8814 11004 8101 -1192 -485 462 C
ATOM 2089 NE ARG A 272 -23.300 14.634 19.912 1.00 89.35 N
ANISOU 2089 NE ARG A 272 10788 12943 10216 -1348 -562 512 N
ATOM 2090 CZ ARG A 272 -24.464 14.188 19.438 1.00105.44 C
ANISOU 2090 CZ ARG A 272 12736 15040 12286 -1428 -646 512 C
ATOM 2091 NH1 ARG A 272 -24.690 12.885 19.338 1.00 97.56 N
ANISOU 2091 NH1 ARG A 272 11724 13949 11395 -1579 -719 555 N
ATOM 2092 NH2 ARG A 272 -25.412 15.044 19.064 1.00 84.44 N
ANISOU 2092 NH2 ARG A 272 9999 12530 9553 -1358 -661 468 N
ATOM 2093 N TYR A 273 -23.071 20.597 21.376 1.00 45.31 N
ANISOU 2093 N TYR A 273 5213 7788 4214 -747 -287 361 N
ATOM 2094 CA TYR A 273 -21.837 21.388 21.325 1.00 44.02 C
ANISOU 2094 CA TYR A 273 5192 7513 4019 -662 -230 312 C
ATOM 2095 C TYR A 273 -21.677 22.305 22.537 1.00 48.31 C
ANISOU 2095 C TYR A 273 5693 8162 4501 -584 -160 321 C
ATOM 2096 O TYR A 273 -20.637 22.947 22.688 1.00 47.78 O
ANISOU 2096 O TYR A 273 5730 8012 4414 -529 -111 287 O
ATOM 2097 CB TYR A 273 -21.768 22.170 20.005 1.00 43.94 C
ANISOU 2097 CB TYR A 273 5307 7420 3969 -569 -261 223 C
ATOM 2098 CG TYR A 273 -21.418 21.292 18.820 1.00 43.81 C
ANISOU 2098 CG TYR A 273 5378 7264 4006 -634 -315 198 C
ATOM 2099 CD1 TYR A 273 -21.092 19.943 18.996 1.00 44.79 C
ANISOU 2099 CD1 TYR A 273 5483 7320 4216 -760 -333 244 C
ATOM 2100 CD2 TYR A 273 -21.352 21.817 17.535 1.00 44.57 C
ANISOU 2100 CD2 TYR A 273 5584 7288 4060 -562 -348 127 C
ATOM 2101 CE1 TYR A 273 -20.725 19.142 17.924 1.00 43.62 C
ANISOU 2101 CE1 TYR A 273 5423 7038 4114 -805 -386 206 C
ATOM 2102 CE2 TYR A 273 -21.030 21.011 16.441 1.00 46.63 C
ANISOU 2102 CE2 TYR A 273 5925 7435 4358 -610 -398 93 C
ATOM 2103 CZ TYR A 273 -20.691 19.680 16.650 1.00 49.43 C
ANISOU 2103 CZ TYR A 273 6260 7722 4800 -729 -417 126 C
ATOM 2104 OH TYR A 273 -20.402 18.875 15.604 1.00 41.32 O
ANISOU 2104 OH TYR A 273 5311 6582 3807 -766 -473 81 O
ATOM 2105 N LEU A 274 -22.673 22.308 23.435 1.00 46.18 N
ANISOU 2105 N LEU A 274 5263 8080 4201 -586 -154 369 N
ATOM 2106 CA LEU A 274 -22.610 23.099 24.661 1.00 45.71 C
ANISOU 2106 CA LEU A 274 5147 8145 4075 -507 -91 374 C
ATOM 2107 C LEU A 274 -22.930 22.308 25.901 1.00 49.44 C
ANISOU 2107 C LEU A 274 5471 8758 4557 -595 -62 476 C
ATOM 2108 O LEU A 274 -22.473 22.686 26.957 1.00 50.01 O
ANISOU 2108 O LEU A 274 5524 8891 4588 -556 -4 488 O
ATOM 2109 CB LEU A 274 -23.612 24.282 24.607 1.00 46.30 C
ANISOU 2109 CB LEU A 274 5171 8356 4064 -366 -105 313 C
ATOM 2110 CG LEU A 274 -23.661 25.192 23.373 1.00 48.80 C
ANISOU 2110 CG LEU A 274 5614 8573 4355 -261 -146 223 C
ATOM 2111 CD1 LEU A 274 -24.823 26.137 23.468 1.00 49.08 C
ANISOU 2111 CD1 LEU A 274 5565 8769 4311 -130 -170 182 C
ATOM 2112 CD2 LEU A 274 -22.373 25.976 23.195 1.00 47.40 C
ANISOU 2112 CD2 LEU A 274 5610 8232 4167 -201 -108 169 C
ATOM 2113 N ASN A 275 -23.767 21.268 25.824 1.00 47.73 N
ANISOU 2113 N ASN A 275 5141 8607 4389 -713 -101 551 N
ATOM 2114 CA ASN A 275 -24.297 20.633 27.033 1.00 47.76 C
ANISOU 2114 CA ASN A 275 4981 8782 4386 -793 -71 662 C
ATOM 2115 C ASN A 275 -23.341 19.644 27.737 1.00 52.85 C
ANISOU 2115 C ASN A 275 5653 9338 5088 -902 -40 753 C
ATOM 2116 O ASN A 275 -23.744 19.073 28.757 1.00 51.44 O
ANISOU 2116 O ASN A 275 5345 9299 4901 -976 -14 862 O
ATOM 2117 CB ASN A 275 -25.666 19.971 26.763 1.00 48.21 C
ANISOU 2117 CB ASN A 275 4886 8964 4468 -886 -125 718 C
ATOM 2118 CG ASN A 275 -25.716 18.871 25.754 1.00 62.43 C
ANISOU 2118 CG ASN A 275 6735 10611 6375 -1018 -201 735 C
ATOM 2119 OD1 ASN A 275 -24.726 18.169 25.492 1.00 56.12 O
ANISOU 2119 OD1 ASN A 275 6059 9615 5648 -1083 -209 745 O
ATOM 2120 ND2 ASN A 275 -26.908 18.676 25.181 1.00 53.87 N
ANISOU 2120 ND2 ASN A 275 5548 9620 5299 -1057 -263 731 N
ATOM 2121 N ARG A 276 -22.087 19.462 27.257 1.00 51.72 N
ANISOU 2121 N ARG A 276 5671 8984 4995 -906 -40 716 N
ATOM 2122 CA ARG A 276 -21.133 18.643 28.037 1.00 52.04 C
ANISOU 2122 CA ARG A 276 5737 8960 5078 -980 -8 796 C
ATOM 2123 C ARG A 276 -20.339 19.569 28.948 1.00 55.45 C
ANISOU 2123 C ARG A 276 6194 9445 5431 -874 62 761 C
ATOM 2124 O ARG A 276 -19.791 19.130 29.972 1.00 56.52 O
ANISOU 2124 O ARG A 276 6299 9615 5561 -908 100 836 O
ATOM 2125 CB ARG A 276 -20.209 17.790 27.164 1.00 51.65 C
ANISOU 2125 CB ARG A 276 5825 8676 5125 -1046 -47 784 C
ATOM 2126 CG ARG A 276 -20.815 16.435 26.769 1.00 58.09 C
ANISOU 2126 CG ARG A 276 6598 9437 6035 -1194 -114 862 C
ATOM 2127 CD ARG A 276 -21.818 16.501 25.620 1.00 56.35 C
ANISOU 2127 CD ARG A 276 6361 9218 5831 -1206 -184 804 C
ATOM 2128 NE ARG A 276 -21.264 17.129 24.408 1.00 65.15 N
ANISOU 2128 NE ARG A 276 7621 10200 6934 -1113 -202 676 N
ATOM 2129 CZ ARG A 276 -20.553 16.492 23.481 1.00 73.07 C
ANISOU 2129 CZ ARG A 276 8750 11011 8003 -1143 -244 634 C
ATOM 2130 NH1 ARG A 276 -20.113 17.140 22.414 1.00 55.50 N
ANISOU 2130 NH1 ARG A 276 6642 8696 5749 -1054 -252 527 N
ATOM 2131 NH2 ARG A 276 -20.287 15.197 23.608 1.00 65.61 N
ANISOU 2131 NH2 ARG A 276 7816 9964 7150 -1259 -279 701 N
ATOM 2132 N GLY A 277 -20.300 20.848 28.567 1.00 49.99 N
ANISOU 2132 N GLY A 277 5560 8756 4678 -745 72 649 N
ATOM 2133 CA GLY A 277 -19.681 21.914 29.343 1.00 48.36 C
ANISOU 2133 CA GLY A 277 5380 8599 4394 -635 126 592 C
ATOM 2134 C GLY A 277 -20.670 22.528 30.315 1.00 53.54 C
ANISOU 2134 C GLY A 277 5893 9493 4957 -564 151 602 C
ATOM 2135 O GLY A 277 -21.782 22.020 30.502 1.00 53.84 O
ANISOU 2135 O GLY A 277 5795 9673 4990 -616 137 673 O
ATOM 2136 N CYS A 278 -20.260 23.623 30.947 1.00 50.70 N
ANISOU 2136 N CYS A 278 5561 9182 4520 -446 188 529 N
ATOM 2137 CA CYS A 278 -21.056 24.417 31.871 1.00 50.90 C
ANISOU 2137 CA CYS A 278 5472 9426 4440 -341 213 505 C
ATOM 2138 C CYS A 278 -22.119 25.217 31.071 1.00 51.88 C
ANISOU 2138 C CYS A 278 5584 9591 4535 -246 173 429 C
ATOM 2139 O CYS A 278 -21.763 25.982 30.177 1.00 49.31 O
ANISOU 2139 O CYS A 278 5395 9116 4223 -178 148 336 O
ATOM 2140 CB CYS A 278 -20.138 25.339 32.664 1.00 52.11 C
ANISOU 2140 CB CYS A 278 5690 9575 4534 -244 251 429 C
ATOM 2141 SG CYS A 278 -21.005 26.351 33.877 1.00 58.41 S
ANISOU 2141 SG CYS A 278 6361 10641 5192 -91 279 377 S
ATOM 2142 N THR A 279 -23.402 25.011 31.354 1.00 49.90 N
ANISOU 2142 N THR A 279 5172 9544 4244 -245 166 475 N
ATOM 2143 CA THR A 279 -24.458 25.674 30.581 1.00 52.06 C
ANISOU 2143 CA THR A 279 5419 9871 4490 -153 122 409 C
ATOM 2144 C THR A 279 -25.011 26.928 31.284 1.00 57.91 C
ANISOU 2144 C THR A 279 6106 10783 5115 30 140 322 C
ATOM 2145 O THR A 279 -26.019 27.491 30.842 1.00 59.30 O
ANISOU 2145 O THR A 279 6229 11053 5250 126 105 273 O
ATOM 2146 CB THR A 279 -25.579 24.686 30.235 1.00 61.34 C
ANISOU 2146 CB THR A 279 6449 11156 5700 -264 89 499 C
ATOM 2147 OG1 THR A 279 -26.110 24.123 31.432 1.00 63.55 O
ANISOU 2147 OG1 THR A 279 6548 11663 5934 -318 133 599 O
ATOM 2148 CG2 THR A 279 -25.121 23.599 29.273 1.00 60.52 C
ANISOU 2148 CG2 THR A 279 6428 10852 5716 -420 49 550 C
ATOM 2149 N ARG A 280 -24.319 27.395 32.323 1.00 53.28 N
ANISOU 2149 N ARG A 280 5540 10229 4473 90 186 293 N
ATOM 2150 CA ARG A 280 -24.713 28.577 33.086 1.00 53.13 C
ANISOU 2150 CA ARG A 280 5483 10362 4342 270 201 198 C
ATOM 2151 C ARG A 280 -24.169 29.838 32.440 1.00 56.84 C
ANISOU 2151 C ARG A 280 6140 10642 4815 398 169 62 C
ATOM 2152 O ARG A 280 -23.142 29.798 31.765 1.00 55.06 O
ANISOU 2152 O ARG A 280 6073 10182 4664 335 159 49 O
ATOM 2153 CB ARG A 280 -24.230 28.471 34.531 1.00 51.77 C
ANISOU 2153 CB ARG A 280 5243 10323 4103 274 260 226 C
ATOM 2154 CG ARG A 280 -24.883 27.345 35.318 1.00 53.45 C
ANISOU 2154 CG ARG A 280 5258 10761 4290 165 297 370 C
ATOM 2155 CD ARG A 280 -24.011 26.913 36.479 1.00 52.63 C
ANISOU 2155 CD ARG A 280 5140 10699 4158 113 349 429 C
ATOM 2156 NE ARG A 280 -23.940 27.918 37.525 1.00 56.39 N
ANISOU 2156 NE ARG A 280 5592 11322 4511 274 377 334 N
ATOM 2157 CZ ARG A 280 -23.060 27.899 38.518 1.00 67.03 C
ANISOU 2157 CZ ARG A 280 6957 12695 5816 276 413 338 C
ATOM 2158 NH1 ARG A 280 -23.091 28.835 39.455 1.00 61.45 N
ANISOU 2158 NH1 ARG A 280 6223 12135 4990 432 430 237 N
ATOM 2159 NH2 ARG A 280 -22.149 26.940 38.589 1.00 47.34 N
ANISOU 2159 NH2 ARG A 280 4508 10087 3394 131 427 436 N
ATOM 2160 N TYR A 281 -24.888 30.954 32.622 1.00 55.66 N
ANISOU 2160 N TYR A 281 5970 10596 4581 579 150 -37 N
ATOM 2161 CA TYR A 281 -24.496 32.265 32.094 1.00 54.28 C
ANISOU 2161 CA TYR A 281 5974 10248 4402 715 113 -166 C
ATOM 2162 C TYR A 281 -23.819 33.085 33.149 1.00 56.59 C
ANISOU 2162 C TYR A 281 6316 10549 4636 808 137 -251 C
ATOM 2163 O TYR A 281 -24.151 32.947 34.324 1.00 56.37 O
ANISOU 2163 O TYR A 281 6149 10741 4528 844 174 -240 O
ATOM 2164 CB TYR A 281 -25.722 33.084 31.635 1.00 55.95 C
ANISOU 2164 CB TYR A 281 6150 10552 4557 883 63 -237 C
ATOM 2165 CG TYR A 281 -26.577 32.482 30.552 1.00 58.91 C
ANISOU 2165 CG TYR A 281 6469 10942 4973 826 24 -177 C
ATOM 2166 CD1 TYR A 281 -26.069 32.274 29.273 1.00 58.47 C
ANISOU 2166 CD1 TYR A 281 6558 10651 5005 743 -10 -161 C
ATOM 2167 CD2 TYR A 281 -27.935 32.237 30.765 1.00 61.36 C
ANISOU 2167 CD2 TYR A 281 6579 11510 5225 871 16 -150 C
ATOM 2168 CE1 TYR A 281 -26.861 31.747 28.259 1.00 60.13 C
ANISOU 2168 CE1 TYR A 281 6720 10879 5247 697 -55 -119 C
ATOM 2169 CE2 TYR A 281 -28.750 31.747 29.742 1.00 62.24 C
ANISOU 2169 CE2 TYR A 281 6636 11639 5373 822 -31 -108 C
ATOM 2170 CZ TYR A 281 -28.207 31.516 28.489 1.00 64.33 C
ANISOU 2170 CZ TYR A 281 7055 11661 5726 738 -69 -97 C
ATOM 2171 OH TYR A 281 -28.968 30.986 27.492 1.00 58.37 O
ANISOU 2171 OH TYR A 281 6247 10925 5005 685 -120 -60 O
ATOM 2172 N PHE A 282 -22.993 34.041 32.724 1.00 51.99 N
ANISOU 2172 N PHE A 282 5926 9744 4082 864 110 -344 N
ATOM 2173 CA PHE A 282 -22.437 35.044 33.613 1.00 51.33 C
ANISOU 2173 CA PHE A 282 5910 9649 3946 975 113 -455 C
ATOM 2174 C PHE A 282 -23.502 36.127 33.723 1.00 58.64 C
ANISOU 2174 C PHE A 282 6815 10679 4788 1189 72 -561 C
ATOM 2175 O PHE A 282 -23.894 36.716 32.719 1.00 57.88 O
ANISOU 2175 O PHE A 282 6814 10461 4716 1260 21 -598 O
ATOM 2176 CB PHE A 282 -21.113 35.603 33.101 1.00 51.15 C
ANISOU 2176 CB PHE A 282 6098 9342 3997 927 99 -504 C
ATOM 2177 CG PHE A 282 -19.965 34.631 33.126 1.00 51.28 C
ANISOU 2177 CG PHE A 282 6131 9270 4084 741 140 -418 C
ATOM 2178 CD1 PHE A 282 -19.213 34.445 34.287 1.00 53.48 C
ANISOU 2178 CD1 PHE A 282 6369 9617 4333 707 177 -424 C
ATOM 2179 CD2 PHE A 282 -19.582 33.952 31.969 1.00 51.86 C
ANISOU 2179 CD2 PHE A 282 6270 9186 4248 611 137 -342 C
ATOM 2180 CE1 PHE A 282 -18.150 33.539 34.309 1.00 52.90 C
ANISOU 2180 CE1 PHE A 282 6311 9466 4324 549 210 -346 C
ATOM 2181 CE2 PHE A 282 -18.509 33.056 31.988 1.00 52.79 C
ANISOU 2181 CE2 PHE A 282 6405 9224 4429 455 171 -272 C
ATOM 2182 CZ PHE A 282 -17.801 32.855 33.153 1.00 50.89 C
ANISOU 2182 CZ PHE A 282 6118 9056 4162 426 207 -272 C
ATOM 2183 N ALA A 283 -24.050 36.300 34.923 1.00 58.25 N
ANISOU 2183 N ALA A 283 6627 10873 4633 1296 94 -600 N
ATOM 2184 CA ALA A 283 -25.096 37.280 35.236 1.00 59.25 C
ANISOU 2184 CA ALA A 283 6706 11144 4661 1522 60 -710 C
ATOM 2185 C ALA A 283 -25.008 37.684 36.693 1.00 64.86 C
ANISOU 2185 C ALA A 283 7344 12036 5264 1629 86 -790 C
ATOM 2186 O ALA A 283 -24.337 37.022 37.477 1.00 64.35 O
ANISOU 2186 O ALA A 283 7226 12033 5192 1517 137 -734 O
ATOM 2187 CB ALA A 283 -26.475 36.690 34.944 1.00 60.72 C
ANISOU 2187 CB ALA A 283 6705 11553 4810 1540 61 -639 C
ATOM 2188 N ASN A 284 -25.641 38.797 37.031 1.00 64.51 N
ANISOU 2188 N ASN A 284 7309 12068 5134 1855 47 -928 N
ATOM 2189 CA ASN A 284 -25.823 39.296 38.384 1.00 66.53 C
ANISOU 2189 CA ASN A 284 7479 12537 5262 2006 62 -1028 C
ATOM 2190 C ASN A 284 -27.339 39.330 38.618 1.00 75.17 C
ANISOU 2190 C ASN A 284 8376 13939 6247 2163 65 -1038 C
ATOM 2191 O ASN A 284 -28.095 38.929 37.710 1.00 75.52 O
ANISOU 2191 O ASN A 284 8365 14000 6330 2129 52 -962 O
ATOM 2192 CB ASN A 284 -25.134 40.662 38.599 1.00 66.48 C
ANISOU 2192 CB ASN A 284 7676 12330 5254 2145 3 -1206 C
ATOM 2193 CG ASN A 284 -25.510 41.765 37.639 1.00 75.35 C
ANISOU 2193 CG ASN A 284 8962 13252 6414 2291 -80 -1302 C
ATOM 2194 OD1 ASN A 284 -26.651 41.904 37.196 1.00 73.49 O
ANISOU 2194 OD1 ASN A 284 8652 13127 6143 2410 -104 -1303 O
ATOM 2195 ND2 ASN A 284 -24.558 42.624 37.358 1.00 64.62 N
ANISOU 2195 ND2 ASN A 284 7828 11600 5124 2294 -129 -1390 N
ATOM 2196 N LYS A 285 -27.790 39.797 39.806 1.00 73.97 N
ANISOU 2196 N LYS A 285 8114 14038 5953 2337 80 -1134 N
ATOM 2197 CA LYS A 285 -29.204 39.880 40.178 1.00 75.56 C
ANISOU 2197 CA LYS A 285 8109 14572 6029 2507 90 -1157 C
ATOM 2198 C LYS A 285 -29.999 40.669 39.135 1.00 79.82 C
ANISOU 2198 C LYS A 285 8722 15013 6594 2662 14 -1230 C
ATOM 2199 O LYS A 285 -31.100 40.256 38.762 1.00 81.44 O
ANISOU 2199 O LYS A 285 8763 15409 6772 2680 20 -1164 O
ATOM 2200 CB LYS A 285 -29.343 40.521 41.572 1.00 79.66 C
ANISOU 2200 CB LYS A 285 8558 15317 6392 2703 104 -1292 C
ATOM 2201 CG LYS A 285 -30.665 40.228 42.264 1.00 97.82 C
ANISOU 2201 CG LYS A 285 10580 18048 8539 2820 153 -1268 C
ATOM 2202 N GLU A 286 -29.411 41.767 38.632 1.00 75.64 N
ANISOU 2202 N GLU A 286 8440 14176 6123 2759 -62 -1356 N
ATOM 2203 CA GLU A 286 -29.999 42.662 37.625 1.00 76.20 C
ANISOU 2203 CA GLU A 286 8630 14100 6223 2919 -146 -1434 C
ATOM 2204 C GLU A 286 -30.088 42.013 36.234 1.00 79.04 C
ANISOU 2204 C GLU A 286 9025 14306 6699 2755 -159 -1298 C
ATOM 2205 O GLU A 286 -31.157 42.052 35.619 1.00 80.69 O
ANISOU 2205 O GLU A 286 9152 14620 6885 2850 -191 -1288 O
ATOM 2206 CB GLU A 286 -29.193 43.982 37.522 1.00 78.06 C
ANISOU 2206 CB GLU A 286 9142 14020 6499 3038 -222 -1590 C
ATOM 2207 CG GLU A 286 -29.046 44.776 38.821 1.00 94.36 C
ANISOU 2207 CG GLU A 286 11205 16193 8454 3219 -231 -1755 C
ATOM 2208 CD GLU A 286 -27.835 44.464 39.689 1.00119.25 C
ANISOU 2208 CD GLU A 286 14399 19290 11620 3072 -188 -1754 C
ATOM 2209 OE1 GLU A 286 -28.030 43.896 40.788 1.00123.85 O
ANISOU 2209 OE1 GLU A 286 14791 20169 12098 3064 -121 -1732 O
ATOM 2210 OE2 GLU A 286 -26.702 44.834 39.303 1.00104.92 O
ANISOU 2210 OE2 GLU A 286 12804 17149 9913 2974 -223 -1779 O
ATOM 2211 N THR A 287 -28.978 41.442 35.719 1.00 72.94 N
ANISOU 2211 N THR A 287 8374 13295 6046 2520 -138 -1203 N
ATOM 2212 CA THR A 287 -28.973 40.897 34.349 1.00 71.26 C
ANISOU 2212 CA THR A 287 8218 12916 5940 2374 -156 -1091 C
ATOM 2213 C THR A 287 -29.741 39.565 34.221 1.00 74.31 C
ANISOU 2213 C THR A 287 8371 13543 6322 2234 -107 -944 C
ATOM 2214 O THR A 287 -30.306 39.315 33.156 1.00 73.67 O
ANISOU 2214 O THR A 287 8282 13427 6285 2205 -141 -890 O
ATOM 2215 CB THR A 287 -27.564 40.793 33.805 1.00 76.11 C
ANISOU 2215 CB THR A 287 9041 13201 6675 2193 -153 -1052 C
ATOM 2216 OG1 THR A 287 -26.758 40.074 34.732 1.00 75.63 O
ANISOU 2216 OG1 THR A 287 8918 13203 6615 2046 -85 -1004 O
ATOM 2217 CG2 THR A 287 -26.950 42.168 33.546 1.00 72.96 C
ANISOU 2217 CG2 THR A 287 8893 12523 6304 2317 -220 -1181 C
ATOM 2218 N ASP A 288 -29.830 38.766 35.312 1.00 70.79 N
ANISOU 2218 N ASP A 288 7734 13348 5816 2156 -33 -882 N
ATOM 2219 CA ASP A 288 -30.588 37.509 35.373 1.00 69.41 C
ANISOU 2219 CA ASP A 288 7324 13418 5630 2017 15 -738 C
ATOM 2220 C ASP A 288 -32.050 37.778 35.017 1.00 74.72 C
ANISOU 2220 C ASP A 288 7849 14305 6235 2173 -21 -766 C
ATOM 2221 O ASP A 288 -32.651 36.993 34.272 1.00 75.43 O
ANISOU 2221 O ASP A 288 7843 14445 6371 2060 -30 -665 O
ATOM 2222 CB ASP A 288 -30.459 36.859 36.772 1.00 71.17 C
ANISOU 2222 CB ASP A 288 7379 13888 5776 1952 98 -683 C
ATOM 2223 CG ASP A 288 -31.559 35.862 37.095 1.00 81.95 C
ANISOU 2223 CG ASP A 288 8466 15584 7087 1877 145 -559 C
ATOM 2224 OD1 ASP A 288 -31.501 34.727 36.568 1.00 82.72 O
ANISOU 2224 OD1 ASP A 288 8517 15637 7274 1656 161 -413 O
ATOM 2225 OD2 ASP A 288 -32.527 36.245 37.817 1.00 82.17 O
ANISOU 2225 OD2 ASP A 288 8320 15915 6984 2046 159 -611 O
ATOM 2226 N LYS A 289 -32.608 38.912 35.529 1.00 71.45 N
ANISOU 2226 N LYS A 289 7426 14011 5713 2441 -51 -913 N
ATOM 2227 CA LYS A 289 -33.974 39.379 35.265 1.00 72.07 C
ANISOU 2227 CA LYS A 289 7373 14299 5711 2641 -94 -969 C
ATOM 2228 C LYS A 289 -34.191 39.653 33.758 1.00 76.00 C
ANISOU 2228 C LYS A 289 8006 14574 6296 2653 -175 -967 C
ATOM 2229 O LYS A 289 -35.292 39.433 33.255 1.00 76.96 O
ANISOU 2229 O LYS A 289 7979 14870 6391 2696 -201 -938 O
ATOM 2230 CB LYS A 289 -34.274 40.646 36.077 1.00 75.79 C
ANISOU 2230 CB LYS A 289 7867 14870 6061 2941 -120 -1149 C
ATOM 2231 CG LYS A 289 -34.216 40.453 37.595 1.00 80.55 C
ANISOU 2231 CG LYS A 289 8319 15740 6547 2969 -44 -1169 C
ATOM 2232 N GLN A 290 -33.138 40.109 33.044 1.00 70.79 N
ANISOU 2232 N GLN A 290 7619 13543 5735 2607 -214 -993 N
ATOM 2233 CA GLN A 290 -33.194 40.431 31.612 1.00 70.12 C
ANISOU 2233 CA GLN A 290 7691 13225 5726 2619 -290 -988 C
ATOM 2234 C GLN A 290 -33.194 39.173 30.714 1.00 72.22 C
ANISOU 2234 C GLN A 290 7897 13461 6081 2370 -275 -837 C
ATOM 2235 O GLN A 290 -33.581 39.267 29.550 1.00 72.01 O
ANISOU 2235 O GLN A 290 7926 13344 6091 2389 -336 -823 O
ATOM 2236 CB GLN A 290 -32.025 41.355 31.220 1.00 70.59 C
ANISOU 2236 CB GLN A 290 8059 12910 5854 2646 -329 -1059 C
ATOM 2237 CG GLN A 290 -32.106 42.758 31.831 1.00 83.94 C
ANISOU 2237 CG GLN A 290 9851 14573 7471 2916 -375 -1226 C
ATOM 2238 CD GLN A 290 -33.233 43.586 31.236 1.00 93.73 C
ANISOU 2238 CD GLN A 290 11088 15872 8655 3164 -459 -1301 C
ATOM 2239 OE1 GLN A 290 -33.250 43.880 30.041 1.00 86.70 O
ANISOU 2239 OE1 GLN A 290 10340 14780 7822 3174 -521 -1278 O
ATOM 2240 NE2 GLN A 290 -34.194 43.994 32.058 1.00 83.07 N
ANISOU 2240 NE2 GLN A 290 9574 14805 7184 3381 -463 -1393 N
ATOM 2241 N ILE A 291 -32.768 38.008 31.245 1.00 67.76 N
ANISOU 2241 N ILE A 291 7225 12971 5551 2146 -200 -727 N
ATOM 2242 CA ILE A 291 -32.724 36.752 30.491 1.00 66.49 C
ANISOU 2242 CA ILE A 291 7010 12776 5479 1906 -189 -589 C
ATOM 2243 C ILE A 291 -34.078 35.987 30.610 1.00 72.31 C
ANISOU 2243 C ILE A 291 7461 13848 6165 1883 -182 -523 C
ATOM 2244 O ILE A 291 -34.494 35.615 31.696 1.00 73.20 O
ANISOU 2244 O ILE A 291 7378 14231 6206 1880 -124 -495 O
ATOM 2245 CB ILE A 291 -31.506 35.870 30.918 1.00 67.96 C
ANISOU 2245 CB ILE A 291 7244 12839 5738 1674 -122 -501 C
ATOM 2246 CG1 ILE A 291 -30.176 36.644 30.826 1.00 66.12 C
ANISOU 2246 CG1 ILE A 291 7274 12295 5554 1689 -129 -568 C
ATOM 2247 CG2 ILE A 291 -31.435 34.592 30.077 1.00 68.79 C
ANISOU 2247 CG2 ILE A 291 7308 12887 5940 1437 -121 -370 C
ATOM 2248 CD1 ILE A 291 -29.069 36.076 31.649 1.00 70.43 C
ANISOU 2248 CD1 ILE A 291 7838 12792 6129 1539 -62 -522 C
ATOM 2249 N LEU A 292 -34.741 35.744 29.476 1.00 70.93 N
ANISOU 2249 N LEU A 292 7263 13660 6026 1860 -242 -494 N
ATOM 2250 CA LEU A 292 -36.005 35.001 29.406 1.00 72.00 C
ANISOU 2250 CA LEU A 292 7136 14090 6132 1814 -248 -428 C
ATOM 2251 C LEU A 292 -35.855 33.544 29.871 1.00 76.78 C
ANISOU 2251 C LEU A 292 7592 14793 6789 1542 -184 -283 C
ATOM 2252 O LEU A 292 -34.840 32.903 29.582 1.00 75.40 O
ANISOU 2252 O LEU A 292 7547 14387 6713 1355 -167 -218 O
ATOM 2253 CB LEU A 292 -36.549 35.022 27.985 1.00 71.83 C
ANISOU 2253 CB LEU A 292 7158 13983 6153 1826 -336 -432 C
ATOM 2254 CG LEU A 292 -36.920 36.400 27.431 1.00 77.03 C
ANISOU 2254 CG LEU A 292 7934 14580 6753 2101 -412 -557 C
ATOM 2255 CD1 LEU A 292 -37.240 36.323 25.945 1.00 76.25 C
ANISOU 2255 CD1 LEU A 292 7910 14356 6705 2081 -498 -543 C
ATOM 2256 CD2 LEU A 292 -38.070 37.030 28.224 1.00 79.88 C
ANISOU 2256 CD2 LEU A 292 8091 15274 6985 2328 -414 -631 C
ATOM 2257 N GLN A 293 -36.892 33.025 30.562 1.00 74.19 N
ANISOU 2257 N GLN A 293 6986 14810 6394 1523 -151 -228 N
ATOM 2258 CA GLN A 293 -36.977 31.661 31.101 1.00 73.13 C
ANISOU 2258 CA GLN A 293 6673 14817 6294 1275 -92 -78 C
ATOM 2259 C GLN A 293 -36.642 30.569 30.039 1.00 71.59 C
ANISOU 2259 C GLN A 293 6546 14413 6240 1028 -130 18 C
ATOM 2260 O GLN A 293 -36.002 29.553 30.372 1.00 69.01 O
ANISOU 2260 O GLN A 293 6223 14012 5983 813 -85 127 O
ATOM 2261 CB GLN A 293 -38.393 31.443 31.666 1.00 77.07 C
ANISOU 2261 CB GLN A 293 6860 15727 6697 1318 -74 -45 C
ATOM 2262 CG GLN A 293 -38.642 30.103 32.378 1.00 96.94 C
ANISOU 2262 CG GLN A 293 9161 18442 9230 1073 -8 121 C
ATOM 2263 CD GLN A 293 -37.875 29.888 33.668 1.00106.53 C
ANISOU 2263 CD GLN A 293 10381 19689 10407 1023 85 173 C
ATOM 2264 OE1 GLN A 293 -37.432 30.829 34.345 1.00 99.94 O
ANISOU 2264 OE1 GLN A 293 9631 18851 9489 1210 113 71 O
ATOM 2265 NE2 GLN A 293 -37.748 28.625 34.055 1.00 95.13 N
ANISOU 2265 NE2 GLN A 293 8838 18287 9020 770 130 334 N
ATOM 2266 N ASN A 294 -37.040 30.803 28.769 1.00 65.57 N
ANISOU 2266 N ASN A 294 5851 13550 5515 1073 -216 -30 N
ATOM 2267 CA ASN A 294 -36.796 29.861 27.685 1.00 64.53 C
ANISOU 2267 CA ASN A 294 5785 13230 5502 869 -264 36 C
ATOM 2268 C ASN A 294 -35.304 29.818 27.278 1.00 65.46 C
ANISOU 2268 C ASN A 294 6179 12986 5708 793 -256 32 C
ATOM 2269 O ASN A 294 -34.937 28.969 26.463 1.00 63.79 O
ANISOU 2269 O ASN A 294 6035 12607 5595 620 -287 85 O
ATOM 2270 CB ASN A 294 -37.701 30.152 26.476 1.00 66.72 C
ANISOU 2270 CB ASN A 294 6039 13536 5775 954 -361 -18 C
ATOM 2271 CG ASN A 294 -37.485 31.447 25.715 1.00 79.96 C
ANISOU 2271 CG ASN A 294 7924 15039 7419 1181 -418 -142 C
ATOM 2272 OD1 ASN A 294 -36.614 32.266 26.010 1.00 74.10 O
ANISOU 2272 OD1 ASN A 294 7366 14129 6659 1292 -391 -202 O
ATOM 2273 ND2 ASN A 294 -38.316 31.665 24.717 1.00 67.12 N
ANISOU 2273 ND2 ASN A 294 6266 13455 5779 1256 -504 -180 N
ATOM 2274 N ARG A 295 -34.449 30.708 27.866 1.00 61.59 N
ANISOU 2274 N ARG A 295 5837 12384 5180 918 -215 -35 N
ATOM 2275 CA ARG A 295 -33.000 30.749 27.590 1.00 59.91 C
ANISOU 2275 CA ARG A 295 5869 11854 5041 850 -200 -41 C
ATOM 2276 C ARG A 295 -32.200 30.053 28.670 1.00 63.50 C
ANISOU 2276 C ARG A 295 6295 12315 5518 710 -119 37 C
ATOM 2277 O ARG A 295 -31.036 29.695 28.441 1.00 61.97 O
ANISOU 2277 O ARG A 295 6258 11885 5401 596 -104 63 O
ATOM 2278 CB ARG A 295 -32.474 32.191 27.451 1.00 58.00 C
ANISOU 2278 CB ARG A 295 5827 11454 4756 1060 -215 -164 C
ATOM 2279 CG ARG A 295 -33.283 33.093 26.523 1.00 63.91 C
ANISOU 2279 CG ARG A 295 6616 12206 5462 1247 -296 -249 C
ATOM 2280 CD ARG A 295 -33.384 32.608 25.086 1.00 58.33 C
ANISOU 2280 CD ARG A 295 5975 11364 4823 1157 -362 -220 C
ATOM 2281 NE ARG A 295 -34.227 33.525 24.324 1.00 62.89 N
ANISOU 2281 NE ARG A 295 6574 11978 5342 1357 -440 -297 N
ATOM 2282 CZ ARG A 295 -33.786 34.627 23.727 1.00 75.35 C
ANISOU 2282 CZ ARG A 295 8369 13355 6907 1506 -478 -372 C
ATOM 2283 NH1 ARG A 295 -32.491 34.927 23.739 1.00 60.69 N
ANISOU 2283 NH1 ARG A 295 6722 11243 5096 1463 -444 -379 N
ATOM 2284 NH2 ARG A 295 -34.633 35.443 23.121 1.00 60.49 N
ANISOU 2284 NH2 ARG A 295 6492 11526 4964 1700 -551 -435 N
ATOM 2285 N LYS A 296 -32.801 29.875 29.846 1.00 60.46 N
ANISOU 2285 N LYS A 296 5708 12206 5058 725 -68 75 N
ATOM 2286 CA LYS A 296 -32.101 29.325 31.008 1.00 60.58 C
ANISOU 2286 CA LYS A 296 5688 12261 5069 622 10 149 C
ATOM 2287 C LYS A 296 -32.139 27.798 31.056 1.00 66.50 C
ANISOU 2287 C LYS A 296 6333 13035 5900 367 27 302 C
ATOM 2288 O LYS A 296 -33.217 27.197 30.989 1.00 69.63 O
ANISOU 2288 O LYS A 296 6538 13626 6293 294 12 369 O
ATOM 2289 CB LYS A 296 -32.673 29.907 32.301 1.00 62.86 C
ANISOU 2289 CB LYS A 296 5818 12843 5223 770 61 117 C
ATOM 2290 CG LYS A 296 -32.650 31.432 32.329 1.00 72.41 C
ANISOU 2290 CG LYS A 296 7138 14022 6354 1035 36 -45 C
ATOM 2291 CD LYS A 296 -33.539 31.954 33.416 1.00 76.98 C
ANISOU 2291 CD LYS A 296 7528 14930 6791 1200 71 -88 C
ATOM 2292 CE LYS A 296 -33.102 33.298 33.926 1.00 90.96 C
ANISOU 2292 CE LYS A 296 9433 16640 8487 1428 68 -239 C
ATOM 2293 NZ LYS A 296 -33.698 33.557 35.266 1.00107.87 N
ANISOU 2293 NZ LYS A 296 11389 19110 10487 1554 122 -265 N
ATOM 2294 N SER A 297 -30.953 27.181 31.174 1.00 59.37 N
ANISOU 2294 N SER A 297 5556 11928 5073 233 54 356 N
ATOM 2295 CA SER A 297 -30.788 25.731 31.280 1.00 58.61 C
ANISOU 2295 CA SER A 297 5398 11808 5064 -4 66 501 C
ATOM 2296 C SER A 297 -31.246 25.229 32.660 1.00 62.13 C
ANISOU 2296 C SER A 297 5636 12530 5439 -59 135 608 C
ATOM 2297 O SER A 297 -31.197 26.019 33.597 1.00 62.27 O
ANISOU 2297 O SER A 297 5622 12688 5350 87 184 556 O
ATOM 2298 CB SER A 297 -29.315 25.376 31.081 1.00 60.25 C
ANISOU 2298 CB SER A 297 5810 11726 5358 -92 76 511 C
ATOM 2299 OG SER A 297 -28.524 25.843 32.162 1.00 63.46 O
ANISOU 2299 OG SER A 297 6254 12154 5705 -25 139 494 O
ATOM 2300 N PRO A 298 -31.589 23.929 32.849 1.00 59.24 N
ANISOU 2300 N PRO A 298 5142 12234 5131 -268 142 759 N
ATOM 2301 CA PRO A 298 -31.925 23.441 34.206 1.00 60.54 C
ANISOU 2301 CA PRO A 298 5121 12658 5224 -328 216 881 C
ATOM 2302 C PRO A 298 -30.764 23.655 35.198 1.00 64.81 C
ANISOU 2302 C PRO A 298 5761 13142 5722 -284 279 880 C
ATOM 2303 O PRO A 298 -31.017 24.046 36.329 1.00 64.73 O
ANISOU 2303 O PRO A 298 5634 13371 5590 -192 339 887 O
ATOM 2304 CB PRO A 298 -32.226 21.953 33.982 1.00 62.02 C
ANISOU 2304 CB PRO A 298 5225 12821 5520 -587 196 1044 C
ATOM 2305 CG PRO A 298 -32.647 21.877 32.555 1.00 65.90 C
ANISOU 2305 CG PRO A 298 5770 13172 6099 -616 106 982 C
ATOM 2306 CD PRO A 298 -31.711 22.839 31.864 1.00 60.44 C
ANISOU 2306 CD PRO A 298 5314 12236 5414 -460 81 829 C
ATOM 2307 N GLU A 299 -29.493 23.485 34.755 1.00 62.08 N
ANISOU 2307 N GLU A 299 5629 12492 5468 -330 261 857 N
ATOM 2308 CA GLU A 299 -28.278 23.747 35.567 1.00 61.92 C
ANISOU 2308 CA GLU A 299 5721 12389 5416 -284 309 838 C
ATOM 2309 C GLU A 299 -28.284 25.215 36.078 1.00 65.91 C
ANISOU 2309 C GLU A 299 6246 13002 5797 -47 330 687 C
ATOM 2310 O GLU A 299 -27.957 25.452 37.224 1.00 65.46 O
ANISOU 2310 O GLU A 299 6148 13076 5649 12 384 692 O
ATOM 2311 CB GLU A 299 -27.000 23.460 34.735 1.00 62.10 C
ANISOU 2311 CB GLU A 299 5969 12064 5561 -353 274 809 C
ATOM 2312 CG GLU A 299 -25.643 23.609 35.441 1.00 73.60 C
ANISOU 2312 CG GLU A 299 7547 13411 7007 -330 313 794 C
ATOM 2313 CD GLU A 299 -24.376 23.587 34.578 1.00 94.20 C
ANISOU 2313 CD GLU A 299 10373 15700 9718 -363 282 739 C
ATOM 2314 OE1 GLU A 299 -24.453 23.198 33.388 1.00 77.14 O
ANISOU 2314 OE1 GLU A 299 8279 13378 7654 -437 230 738 O
ATOM 2315 OE2 GLU A 299 -23.290 23.929 35.106 1.00 85.50 O
ANISOU 2315 OE2 GLU A 299 9367 14520 8597 -317 309 698 O
ATOM 2316 N TYR A 300 -28.659 26.188 35.217 1.00 63.65 N
ANISOU 2316 N TYR A 300 6027 12655 5504 91 281 553 N
ATOM 2317 CA TYR A 300 -28.721 27.611 35.580 1.00 61.95 C
ANISOU 2317 CA TYR A 300 5847 12509 5181 323 285 402 C
ATOM 2318 C TYR A 300 -29.805 27.862 36.632 1.00 63.46 C
ANISOU 2318 C TYR A 300 5813 13066 5232 423 328 414 C
ATOM 2319 O TYR A 300 -29.600 28.668 37.528 1.00 62.36 O
ANISOU 2319 O TYR A 300 5673 13032 4987 573 360 333 O
ATOM 2320 CB TYR A 300 -28.979 28.483 34.329 1.00 61.67 C
ANISOU 2320 CB TYR A 300 5932 12322 5178 438 216 278 C
ATOM 2321 CG TYR A 300 -28.922 29.968 34.622 1.00 62.19 C
ANISOU 2321 CG TYR A 300 6075 12402 5153 674 208 118 C
ATOM 2322 CD1 TYR A 300 -27.719 30.657 34.576 1.00 62.00 C
ANISOU 2322 CD1 TYR A 300 6258 12144 5154 724 203 30 C
ATOM 2323 CD2 TYR A 300 -30.072 30.681 34.967 1.00 64.66 C
ANISOU 2323 CD2 TYR A 300 6250 12964 5354 849 203 52 C
ATOM 2324 CE1 TYR A 300 -27.659 32.022 34.842 1.00 62.64 C
ANISOU 2324 CE1 TYR A 300 6423 12215 5163 932 186 -119 C
ATOM 2325 CE2 TYR A 300 -30.013 32.039 35.283 1.00 65.35 C
ANISOU 2325 CE2 TYR A 300 6419 13052 5360 1076 188 -102 C
ATOM 2326 CZ TYR A 300 -28.803 32.707 35.207 1.00 65.35 C
ANISOU 2326 CZ TYR A 300 6640 12793 5397 1112 176 -187 C
ATOM 2327 OH TYR A 300 -28.703 34.044 35.482 1.00 63.27 O
ANISOU 2327 OH TYR A 300 6474 12501 5067 1324 152 -341 O
ATOM 2328 N LEU A 301 -30.965 27.209 36.489 1.00 61.60 N
ANISOU 2328 N LEU A 301 5386 13027 4992 345 326 506 N
ATOM 2329 CA LEU A 301 -32.099 27.328 37.409 1.00 63.27 C
ANISOU 2329 CA LEU A 301 5355 13617 5070 423 370 534 C
ATOM 2330 C LEU A 301 -31.759 26.723 38.764 1.00 67.47 C
ANISOU 2330 C LEU A 301 5786 14315 5533 346 450 649 C
ATOM 2331 O LEU A 301 -32.046 27.324 39.804 1.00 68.09 O
ANISOU 2331 O LEU A 301 5763 14641 5468 494 498 603 O
ATOM 2332 CB LEU A 301 -33.348 26.646 36.801 1.00 64.57 C
ANISOU 2332 CB LEU A 301 5339 13928 5268 318 342 619 C
ATOM 2333 CG LEU A 301 -33.914 27.266 35.521 1.00 68.35 C
ANISOU 2333 CG LEU A 301 5877 14307 5787 415 260 507 C
ATOM 2334 CD1 LEU A 301 -35.011 26.393 34.936 1.00 69.65 C
ANISOU 2334 CD1 LEU A 301 5866 14596 6002 269 227 606 C
ATOM 2335 CD2 LEU A 301 -34.443 28.669 35.757 1.00 70.02 C
ANISOU 2335 CD2 LEU A 301 6070 14664 5871 699 252 346 C
ATOM 2336 N LYS A 302 -31.076 25.572 38.753 1.00 64.08 N
ANISOU 2336 N LYS A 302 5403 13738 5205 130 461 789 N
ATOM 2337 CA LYS A 302 -30.643 24.885 39.966 1.00 64.68 C
ANISOU 2337 CA LYS A 302 5408 13939 5230 39 530 919 C
ATOM 2338 C LYS A 302 -29.470 25.624 40.693 1.00 68.17 C
ANISOU 2338 C LYS A 302 5995 14295 5610 168 555 818 C
ATOM 2339 O LYS A 302 -29.577 25.903 41.890 1.00 66.97 O
ANISOU 2339 O LYS A 302 5739 14387 5319 258 612 821 O
ATOM 2340 CB LYS A 302 -30.241 23.426 39.627 1.00 66.35 C
ANISOU 2340 CB LYS A 302 5645 13982 5581 -225 520 1096 C
ATOM 2341 CG LYS A 302 -30.179 22.518 40.858 1.00 86.42 C
ANISOU 2341 CG LYS A 302 8060 16709 8068 -346 589 1277 C
ATOM 2342 CD LYS A 302 -29.521 21.164 40.561 1.00 92.71 C
ANISOU 2342 CD LYS A 302 8937 17278 9010 -582 570 1435 C
ATOM 2343 CE LYS A 302 -29.123 20.409 41.820 1.00 94.36 C
ANISOU 2343 CE LYS A 302 9080 17611 9160 -669 634 1599 C
ATOM 2344 NZ LYS A 302 -30.289 19.914 42.606 1.00 89.96 N
ANISOU 2344 NZ LYS A 302 8269 17403 8509 -743 690 1753 N
ATOM 2345 N ALA A 303 -28.362 25.926 39.972 1.00 65.04 N
ANISOU 2345 N ALA A 303 5831 13567 5314 174 510 729 N
ATOM 2346 CA ALA A 303 -27.131 26.496 40.563 1.00 63.60 C
ANISOU 2346 CA ALA A 303 5793 13275 5099 257 526 644 C
ATOM 2347 C ALA A 303 -27.012 28.041 40.512 1.00 65.94 C
ANISOU 2347 C ALA A 303 6188 13540 5326 490 500 432 C
ATOM 2348 O ALA A 303 -26.170 28.617 41.214 1.00 63.60 O
ANISOU 2348 O ALA A 303 5973 13218 4974 577 514 351 O
ATOM 2349 CB ALA A 303 -25.909 25.876 39.886 1.00 62.59 C
ANISOU 2349 CB ALA A 303 5849 12816 5117 115 498 680 C
ATOM 2350 N GLY A 304 -27.820 28.678 39.673 1.00 64.62 N
ANISOU 2350 N GLY A 304 6022 13362 5168 586 455 344 N
ATOM 2351 CA GLY A 304 -27.802 30.124 39.502 1.00 64.64 C
ANISOU 2351 CA GLY A 304 6132 13310 5120 806 419 149 C
ATOM 2352 C GLY A 304 -26.747 30.551 38.509 1.00 67.58 C
ANISOU 2352 C GLY A 304 6751 13315 5609 789 367 69 C
ATOM 2353 O GLY A 304 -26.171 29.721 37.791 1.00 64.87 O
ANISOU 2353 O GLY A 304 6486 12772 5387 616 357 156 O
ATOM 2354 N SER A 305 -26.449 31.849 38.503 1.00 64.85 N
ANISOU 2354 N SER A 305 6534 12881 5227 968 335 -99 N
ATOM 2355 CA SER A 305 -25.474 32.374 37.562 1.00 62.81 C
ANISOU 2355 CA SER A 305 6509 12284 5071 956 288 -175 C
ATOM 2356 C SER A 305 -24.048 32.126 37.991 1.00 63.39 C
ANISOU 2356 C SER A 305 6693 12205 5187 861 311 -162 C
ATOM 2357 O SER A 305 -23.764 31.786 39.139 1.00 62.52 O
ANISOU 2357 O SER A 305 6498 12248 5007 847 356 -128 O
ATOM 2358 CB SER A 305 -25.682 33.870 37.348 1.00 66.02 C
ANISOU 2358 CB SER A 305 7023 12628 5432 1173 238 -351 C
ATOM 2359 OG SER A 305 -25.174 34.606 38.444 1.00 71.59 O
ANISOU 2359 OG SER A 305 7753 13397 6051 1289 253 -453 O
ATOM 2360 N LEU A 306 -23.151 32.299 37.011 1.00 56.96 N
ANISOU 2360 N LEU A 306 6067 11092 4484 797 278 -190 N
ATOM 2361 CA LEU A 306 -21.713 32.302 37.168 1.00 53.23 C
ANISOU 2361 CA LEU A 306 5728 10434 4063 723 287 -207 C
ATOM 2362 C LEU A 306 -21.341 33.736 37.518 1.00 58.08 C
ANISOU 2362 C LEU A 306 6458 10985 4627 886 258 -376 C
ATOM 2363 O LEU A 306 -21.968 34.679 37.014 1.00 59.56 O
ANISOU 2363 O LEU A 306 6698 11135 4796 1020 215 -471 O
ATOM 2364 CB LEU A 306 -21.054 31.857 35.861 1.00 50.44 C
ANISOU 2364 CB LEU A 306 5510 9812 3844 588 265 -161 C
ATOM 2365 CG LEU A 306 -21.147 30.400 35.476 1.00 51.90 C
ANISOU 2365 CG LEU A 306 5619 10001 4099 413 283 -6 C
ATOM 2366 CD1 LEU A 306 -20.603 30.189 34.024 1.00 48.65 C
ANISOU 2366 CD1 LEU A 306 5356 9322 3806 324 250 2 C
ATOM 2367 CD2 LEU A 306 -20.380 29.528 36.481 1.00 52.28 C
ANISOU 2367 CD2 LEU A 306 5609 10115 4140 313 329 81 C
ATOM 2368 N LYS A 307 -20.352 33.916 38.365 1.00 53.57 N
ANISOU 2368 N LYS A 307 5927 10396 4032 878 275 -417 N
ATOM 2369 CA LYS A 307 -19.968 35.252 38.777 1.00 53.75 C
ANISOU 2369 CA LYS A 307 6058 10356 4009 1023 240 -585 C
ATOM 2370 C LYS A 307 -18.623 35.632 38.217 1.00 58.02 C
ANISOU 2370 C LYS A 307 6788 10609 4648 943 217 -630 C
ATOM 2371 O LYS A 307 -17.667 34.841 38.255 1.00 57.03 O
ANISOU 2371 O LYS A 307 6673 10417 4579 796 245 -551 O
ATOM 2372 CB LYS A 307 -19.955 35.403 40.333 1.00 55.65 C
ANISOU 2372 CB LYS A 307 6189 10836 4119 1113 267 -634 C
ATOM 2373 CG LYS A 307 -21.296 35.126 41.050 1.00 64.29 C
ANISOU 2373 CG LYS A 307 7077 12261 5090 1209 298 -596 C
ATOM 2374 CD LYS A 307 -22.482 35.995 40.581 1.00 74.89 C
ANISOU 2374 CD LYS A 307 8411 13652 6391 1384 258 -689 C
ATOM 2375 CE LYS A 307 -23.784 35.755 41.343 1.00 79.41 C
ANISOU 2375 CE LYS A 307 8761 14580 6829 1486 293 -659 C
ATOM 2376 NZ LYS A 307 -24.315 34.356 41.237 1.00 71.63 N
ANISOU 2376 NZ LYS A 307 7610 13742 5865 1323 345 -463 N
ATOM 2377 N ASP A 308 -18.545 36.881 37.743 1.00 54.49 N
ANISOU 2377 N ASP A 308 6490 9996 4217 1047 164 -759 N
ATOM 2378 CA ASP A 308 -17.327 37.512 37.267 1.00 53.05 C
ANISOU 2378 CA ASP A 308 6494 9545 4117 989 137 -822 C
ATOM 2379 C ASP A 308 -17.436 39.038 37.408 1.00 58.18 C
ANISOU 2379 C ASP A 308 7267 10103 4735 1154 75 -991 C
ATOM 2380 O ASP A 308 -18.540 39.574 37.247 1.00 56.26 O
ANISOU 2380 O ASP A 308 7006 9928 4443 1302 46 -1038 O
ATOM 2381 CB ASP A 308 -17.052 37.129 35.794 1.00 53.93 C
ANISOU 2381 CB ASP A 308 6703 9445 4344 868 133 -738 C
ATOM 2382 CG ASP A 308 -15.659 37.507 35.325 1.00 59.06 C
ANISOU 2382 CG ASP A 308 7516 9846 5079 768 123 -768 C
ATOM 2383 OD1 ASP A 308 -14.691 36.826 35.734 1.00 56.95 O
ANISOU 2383 OD1 ASP A 308 7220 9581 4836 650 157 -723 O
ATOM 2384 OD2 ASP A 308 -15.522 38.564 34.669 1.00 66.39 O
ANISOU 2384 OD2 ASP A 308 8597 10587 6041 818 78 -843 O
ATOM 2385 N PRO A 309 -16.319 39.766 37.693 1.00 58.18 N
ANISOU 2385 N PRO A 309 7394 9944 4765 1132 49 -1085 N
ATOM 2386 CA PRO A 309 -16.400 41.243 37.740 1.00 61.08 C
ANISOU 2386 CA PRO A 309 7904 10186 5120 1278 -21 -1246 C
ATOM 2387 C PRO A 309 -16.811 41.909 36.398 1.00 69.87 C
ANISOU 2387 C PRO A 309 9162 11085 6300 1315 -65 -1246 C
ATOM 2388 O PRO A 309 -17.516 42.919 36.428 1.00 71.50 O
ANISOU 2388 O PRO A 309 9427 11273 6465 1490 -121 -1352 O
ATOM 2389 CB PRO A 309 -14.970 41.655 38.118 1.00 62.20 C
ANISOU 2389 CB PRO A 309 8149 10175 5308 1186 -35 -1313 C
ATOM 2390 CG PRO A 309 -14.365 40.435 38.750 1.00 63.97 C
ANISOU 2390 CG PRO A 309 8236 10551 5518 1055 29 -1216 C
ATOM 2391 CD PRO A 309 -14.941 39.307 37.973 1.00 57.91 C
ANISOU 2391 CD PRO A 309 7384 9837 4783 975 76 -1055 C
ATOM 2392 N LEU A 310 -16.396 41.358 35.233 1.00 67.33 N
ANISOU 2392 N LEU A 310 8898 10611 6073 1164 -44 -1131 N
ATOM 2393 CA LEU A 310 -16.695 41.958 33.907 1.00 68.14 C
ANISOU 2393 CA LEU A 310 9146 10511 6235 1187 -84 -1118 C
ATOM 2394 C LEU A 310 -17.672 41.154 33.027 1.00 70.21 C
ANISOU 2394 C LEU A 310 9323 10856 6497 1179 -66 -1005 C
ATOM 2395 O LEU A 310 -18.647 41.738 32.541 1.00 70.56 O
ANISOU 2395 O LEU A 310 9403 10891 6517 1316 -111 -1036 O
ATOM 2396 CB LEU A 310 -15.427 42.258 33.066 1.00 67.58 C
ANISOU 2396 CB LEU A 310 9246 10165 6268 1037 -87 -1094 C
ATOM 2397 CG LEU A 310 -14.308 41.207 33.023 1.00 71.30 C
ANISOU 2397 CG LEU A 310 9667 10631 6794 834 -25 -997 C
ATOM 2398 CD1 LEU A 310 -13.634 41.129 31.609 1.00 69.60 C
ANISOU 2398 CD1 LEU A 310 9581 10194 6670 703 -16 -918 C
ATOM 2399 CD2 LEU A 310 -13.300 41.474 34.113 1.00 74.83 C
ANISOU 2399 CD2 LEU A 310 10107 11093 7233 793 -21 -1073 C
ATOM 2400 N LEU A 311 -17.404 39.854 32.787 1.00 63.55 N
ANISOU 2400 N LEU A 311 8380 10081 5686 1025 -9 -879 N
ATOM 2401 CA LEU A 311 -18.277 39.054 31.921 1.00 62.48 C
ANISOU 2401 CA LEU A 311 8170 10010 5560 1002 -1 -778 C
ATOM 2402 C LEU A 311 -19.712 39.021 32.399 1.00 65.35 C
ANISOU 2402 C LEU A 311 8384 10611 5834 1150 -13 -796 C
ATOM 2403 O LEU A 311 -19.986 38.788 33.577 1.00 65.56 O
ANISOU 2403 O LEU A 311 8275 10846 5789 1195 12 -817 O
ATOM 2404 CB LEU A 311 -17.786 37.607 31.779 1.00 61.55 C
ANISOU 2404 CB LEU A 311 7961 9937 5488 819 56 -651 C
ATOM 2405 CG LEU A 311 -16.482 37.343 31.050 1.00 64.80 C
ANISOU 2405 CG LEU A 311 8491 10141 5989 662 75 -608 C
ATOM 2406 CD1 LEU A 311 -16.142 35.891 31.157 1.00 63.67 C
ANISOU 2406 CD1 LEU A 311 8236 10080 5876 518 125 -499 C
ATOM 2407 CD2 LEU A 311 -16.586 37.727 29.568 1.00 67.43 C
ANISOU 2407 CD2 LEU A 311 8960 10291 6370 657 44 -586 C
ATOM 2408 N ASP A 312 -20.610 39.280 31.462 1.00 60.91 N
ANISOU 2408 N ASP A 312 7848 10025 5272 1227 -52 -786 N
ATOM 2409 CA ASP A 312 -22.050 39.224 31.570 1.00 61.65 C
ANISOU 2409 CA ASP A 312 7802 10329 5291 1360 -70 -791 C
ATOM 2410 C ASP A 312 -22.565 38.835 30.231 1.00 62.92 C
ANISOU 2410 C ASP A 312 7984 10426 5496 1320 -93 -715 C
ATOM 2411 O ASP A 312 -22.521 39.660 29.329 1.00 64.39 O
ANISOU 2411 O ASP A 312 8331 10429 5708 1383 -142 -750 O
ATOM 2412 CB ASP A 312 -22.645 40.563 32.010 1.00 66.00 C
ANISOU 2412 CB ASP A 312 8403 10903 5771 1590 -124 -930 C
ATOM 2413 CG ASP A 312 -24.065 40.370 32.478 1.00 75.72 C
ANISOU 2413 CG ASP A 312 9439 12424 6906 1727 -126 -938 C
ATOM 2414 OD1 ASP A 312 -24.963 40.230 31.613 1.00 73.67 O
ANISOU 2414 OD1 ASP A 312 9145 12199 6648 1767 -155 -898 O
ATOM 2415 OD2 ASP A 312 -24.266 40.239 33.704 1.00 87.44 O
ANISOU 2415 OD2 ASP A 312 10789 14122 8312 1780 -94 -973 O
ATOM 2416 N ASP A 313 -23.067 37.613 30.073 1.00 56.33 N
ANISOU 2416 N ASP A 313 6996 9738 4670 1216 -64 -611 N
ATOM 2417 CA ASP A 313 -23.474 37.123 28.759 1.00 55.68 C
ANISOU 2417 CA ASP A 313 6933 9590 4634 1157 -89 -540 C
ATOM 2418 C ASP A 313 -24.571 37.969 28.088 1.00 62.31 C
ANISOU 2418 C ASP A 313 7801 10445 5429 1335 -157 -595 C
ATOM 2419 O ASP A 313 -24.502 38.204 26.867 1.00 61.87 O
ANISOU 2419 O ASP A 313 7875 10220 5411 1331 -196 -580 O
ATOM 2420 CB ASP A 313 -23.873 35.659 28.841 1.00 56.53 C
ANISOU 2420 CB ASP A 313 6860 9860 4758 1016 -55 -430 C
ATOM 2421 CG ASP A 313 -22.707 34.756 29.216 1.00 59.54 C
ANISOU 2421 CG ASP A 313 7246 10181 5197 835 1 -363 C
ATOM 2422 OD1 ASP A 313 -21.572 35.012 28.748 1.00 58.15 O
ANISOU 2422 OD1 ASP A 313 7229 9787 5078 771 6 -374 O
ATOM 2423 OD2 ASP A 313 -22.936 33.776 29.905 1.00 64.97 O
ANISOU 2423 OD2 ASP A 313 7777 11035 5875 755 38 -294 O
ATOM 2424 N HIS A 314 -25.532 38.473 28.879 1.00 59.68 N
ANISOU 2424 N HIS A 314 7354 10312 5009 1504 -171 -662 N
ATOM 2425 CA HIS A 314 -26.589 39.325 28.356 1.00 59.96 C
ANISOU 2425 CA HIS A 314 7407 10382 4994 1701 -239 -725 C
ATOM 2426 C HIS A 314 -26.033 40.699 27.943 1.00 62.68 C
ANISOU 2426 C HIS A 314 7995 10468 5353 1817 -291 -813 C
ATOM 2427 O HIS A 314 -26.260 41.116 26.812 1.00 59.73 O
ANISOU 2427 O HIS A 314 7737 9958 4999 1864 -343 -804 O
ATOM 2428 CB HIS A 314 -27.751 39.484 29.344 1.00 61.67 C
ANISOU 2428 CB HIS A 314 7428 10898 5107 1860 -238 -779 C
ATOM 2429 CG HIS A 314 -28.914 40.196 28.725 1.00 66.57 C
ANISOU 2429 CG HIS A 314 8037 11581 5674 2059 -309 -832 C
ATOM 2430 ND1 HIS A 314 -29.014 41.576 28.754 1.00 69.52 |
