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1oy6.pdb
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1oy6.pdb
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HEADER MEMBRANE PROTEIN 03-APR-03 1OY6
TITLE STRUCTURAL BASIS OF THE MULTIPLE BINDING CAPACITY OF THE ACRB
TITLE 2 MULTIDRUG EFFLUX PUMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACRIFLAVINE RESISTANCE PROTEIN B;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ACRB OR ACRE OR B0462;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.W.YU,G.MCDERMOTT,H.I.ZGURSKAYA,H.NIKAIDO,D.E.KOSHLAND JR.
REVDAT 3 13-JUL-11 1OY6 1 VERSN
REVDAT 2 24-FEB-09 1OY6 1 VERSN
REVDAT 1 13-MAY-03 1OY6 0
JRNL AUTH E.W.YU,G.MCDERMOTT,H.I.ZGURSKAYA,H.NIKAIDO,D.E.KOSHLAND
JRNL TITL STRUCTURAL BASIS OF MULTIPLE DRUG-BINDING CAPACITY OF THE
JRNL TITL 2 ACRB MULTIDRUG EFFLUX PUMP.
JRNL REF SCIENCE V. 300 976 2003
JRNL REFN ISSN 0036-8075
JRNL PMID 12738864
JRNL DOI 10.1126/SCIENCE.1083137
REMARK 2
REMARK 2 RESOLUTION. 3.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 34832
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.275
REMARK 3 R VALUE (WORKING SET) : 0.272
REMARK 3 FREE R VALUE : 0.330
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1741
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7639
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OY6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-03.
REMARK 100 THE RCSB ID CODE IS RCSB018793.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34832
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.700
REMARK 200 RESOLUTION RANGE LOW (A) : 46.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 71.77850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.44134
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 173.21233
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 71.77850
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 41.44134
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 173.21233
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 71.77850
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 41.44134
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 173.21233
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 71.77850
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 41.44134
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 173.21233
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 71.77850
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 41.44134
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 173.21233
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 71.77850
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 41.44134
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 173.21233
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 82.88267
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 346.42467
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 82.88267
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 346.42467
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 82.88267
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 346.42467
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 82.88267
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 346.42467
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 82.88267
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 346.42467
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 82.88267
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 346.42467
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 19040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 112260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 143.55700
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 71.77850
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 124.32401
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 ASN A 3
REMARK 465 PHE A 4
REMARK 465 PHE A 5
REMARK 465 ILE A 6
REMARK 465 PRO A 499
REMARK 465 ILE A 500
REMARK 465 ALA A 501
REMARK 465 LYS A 502
REMARK 465 GLY A 503
REMARK 465 ASP A 504
REMARK 465 HIS A 505
REMARK 465 GLY A 506
REMARK 465 GLU A 507
REMARK 465 GLY A 508
REMARK 465 LYS A 509
REMARK 465 LYS A 510
REMARK 465 GLY A 511
REMARK 465 PHE A 512
REMARK 465 ASP A 711
REMARK 465 THR A 860
REMARK 465 GLY A 861
REMARK 465 MET A 862
REMARK 465 SER A 863
REMARK 465 TYR A 864
REMARK 465 GLN A 865
REMARK 465 GLU A 866
REMARK 465 ARG A 867
REMARK 465 LEU A 868
REMARK 465 ASN A 1037
REMARK 465 GLU A 1038
REMARK 465 ASP A 1039
REMARK 465 ILE A 1040
REMARK 465 GLU A 1041
REMARK 465 HIS A 1042
REMARK 465 SER A 1043
REMARK 465 HIS A 1044
REMARK 465 THR A 1045
REMARK 465 VAL A 1046
REMARK 465 ASP A 1047
REMARK 465 HIS A 1048
REMARK 465 HIS A 1049
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 ASP A 407 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 795 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 858 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A1032 NE - CZ - NH1 ANGL. DEV. = 3.1 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 PRO A 9 -110.67 -64.73
REMARK 500 ILE A 10 -82.91 13.95
REMARK 500 LEU A 21 -70.07 -80.55
REMARK 500 LYS A 29 48.84 -160.23
REMARK 500 ALA A 33 175.81 -57.08
REMARK 500 GLN A 34 -163.14 -72.95
REMARK 500 TYR A 35 149.46 -28.04
REMARK 500 ALA A 47 134.97 -170.63
REMARK 500 TYR A 49 86.77 -156.84
REMARK 500 ALA A 52 125.89 -38.47
REMARK 500 ASN A 68 30.23 -92.43
REMARK 500 ASN A 74 120.90 62.67
REMARK 500 LEU A 75 115.34 -177.54
REMARK 500 ASN A 109 48.36 -109.03
REMARK 500 LYS A 110 -42.18 -164.55
REMARK 500 LEU A 117 40.88 -101.70
REMARK 500 SER A 133 3.79 -152.70
REMARK 500 SER A 134 42.87 26.79
REMARK 500 SER A 135 124.94 -172.31
REMARK 500 LEU A 137 -74.62 -138.94
REMARK 500 THR A 145 -55.97 -122.76
REMARK 500 ASP A 146 -81.36 -81.84
REMARK 500 GLU A 152 -40.96 178.98
REMARK 500 ASN A 161 -51.32 -168.11
REMARK 500 SER A 167 3.80 -69.56
REMARK 500 ARG A 168 -52.89 -125.67
REMARK 500 SER A 170 70.71 37.21
REMARK 500 ASP A 174 105.00 -163.05
REMARK 500 MET A 184 96.37 -58.40
REMARK 500 GLN A 197 83.06 66.44
REMARK 500 LYS A 208 57.15 -93.63
REMARK 500 ALA A 209 -54.90 -176.39
REMARK 500 GLN A 218 145.97 -171.37
REMARK 500 LYS A 226 107.90 -54.45
REMARK 500 ALA A 236 -146.87 -115.02
REMARK 500 LYS A 248 43.22 -102.38
REMARK 500 GLN A 255 -51.86 -9.43
REMARK 500 ASP A 256 35.46 -87.67
REMARK 500 THR A 295 101.61 -11.32
REMARK 500 ALA A 299 -94.74 60.98
REMARK 500 TYR A 327 89.22 7.90
REMARK 500 THR A 365 48.04 -90.24
REMARK 500 LEU A 366 -41.15 -138.57
REMARK 500 SER A 389 -168.76 -114.29
REMARK 500 MET A 420 36.43 -92.07
REMARK 500 ALA A 421 -50.42 -166.97
REMARK 500 PRO A 427 174.84 -40.73
REMARK 500 PHE A 459 158.93 -22.34
REMARK 500 THR A 463 37.19 -89.15
REMARK 500 ILE A 466 -71.19 -49.61
REMARK 500
REMARK 500 THIS ENTRY HAS 105 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ILE A 10 24.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IWG RELATED DB: PDB
REMARK 900 THE SAME PROTEIN
DBREF 1OY6 A 1 1049 UNP P31224 ACRB_ECOLI 1 1049
SEQRES 1 A 1049 MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES 2 A 1049 VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES 3 A 1049 ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES 4 A 1049 PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES 5 A 1049 ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES 6 A 1049 GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES 7 A 1049 SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES 8 A 1049 LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES 9 A 1049 VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES 10 A 1049 LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES 11 A 1049 LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES 12 A 1049 ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES 13 A 1049 TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES 14 A 1049 SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES 15 A 1049 ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES 16 A 1049 PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES 17 A 1049 ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES 18 A 1049 THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES 19 A 1049 ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES 20 A 1049 LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES 21 A 1049 LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES 22 A 1049 ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES 23 A 1049 SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES 24 A 1049 LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES 25 A 1049 MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES 26 A 1049 PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES 27 A 1049 GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES 28 A 1049 PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES 29 A 1049 THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES 30 A 1049 GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES 31 A 1049 ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES 32 A 1049 LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES 33 A 1049 GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES 34 A 1049 ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES 35 A 1049 VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES 36 A 1049 MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES 37 A 1049 GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES 38 A 1049 VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES 39 A 1049 THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES 40 A 1049 GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES 41 A 1049 GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES 42 A 1049 ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES 43 A 1049 ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES 44 A 1049 PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES 45 A 1049 MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES 46 A 1049 ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES 47 A 1049 LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES 48 A 1049 VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES 49 A 1049 GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES 50 A 1049 PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES 51 A 1049 ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES 52 A 1049 PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES 53 A 1049 ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES 54 A 1049 LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES 55 A 1049 LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES 56 A 1049 VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES 57 A 1049 ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES 58 A 1049 SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES 59 A 1049 GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES 60 A 1049 VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES 61 A 1049 MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES 62 A 1049 ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES 63 A 1049 SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES 64 A 1049 ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES 65 A 1049 PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES 66 A 1049 GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES 67 A 1049 TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES 68 A 1049 GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES 69 A 1049 PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES 70 A 1049 PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES 71 A 1049 GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES 72 A 1049 ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES 73 A 1049 LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES 74 A 1049 LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES 75 A 1049 ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES 76 A 1049 LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES 77 A 1049 LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES 78 A 1049 ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES 79 A 1049 THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES 80 A 1049 VAL VAL ARG ARG ARG PHE SER ARG LYS ASN GLU ASP ILE
SEQRES 81 A 1049 GLU HIS SER HIS THR VAL ASP HIS HIS
HELIX 1 1 PRO A 9 ILE A 27 1 19
HELIX 2 2 ASP A 53 VAL A 61 1 9
HELIX 3 3 VAL A 61 ASN A 68 1 8
HELIX 4 4 ASP A 99 GLN A 112 1 14
HELIX 5 5 ALA A 114 LEU A 118 5 5
HELIX 6 6 PRO A 119 GLN A 124 1 6
HELIX 7 7 GLU A 152 ALA A 160 1 9
HELIX 8 8 MET A 162 SER A 167 1 6
HELIX 9 9 ASN A 189 PHE A 196 1 8
HELIX 10 10 THR A 199 ASN A 211 1 13
HELIX 11 11 SER A 242 LYS A 248 1 7
HELIX 12 12 LEU A 262 VAL A 265 1 4
HELIX 13 13 ALA A 299 LYS A 312 1 14
HELIX 14 14 MET A 313 PHE A 317 5 5
HELIX 15 15 THR A 329 LEU A 359 1 31
HELIX 16 16 ALA A 371 ALA A 385 1 15
HELIX 17 17 ASN A 391 GLU A 423 1 33
HELIX 18 18 PRO A 427 VAL A 454 1 28
HELIX 19 19 GLY A 460 SER A 462 5 3
HELIX 20 20 THR A 463 ALA A 485 1 23
HELIX 21 21 ILE A 487 MET A 496 1 10
HELIX 22 22 PHE A 513 HIS A 525 1 13
HELIX 23 23 HIS A 525 SER A 537 1 13
HELIX 24 24 THR A 538 ARG A 558 1 21
HELIX 25 25 THR A 583 LYS A 601 1 19
HELIX 26 26 LYS A 643 ILE A 658 1 16
HELIX 27 27 GLY A 691 HIS A 709 1 19
HELIX 28 28 ASP A 732 GLY A 740 1 9
HELIX 29 29 SER A 742 GLY A 755 1 14
HELIX 30 30 GLU A 776 ARG A 780 5 5
HELIX 31 31 LEU A 782 GLY A 787 5 6
HELIX 32 32 PHE A 801 SER A 805 1 5
HELIX 33 33 TYR A 819 LEU A 822 5 4
HELIX 34 34 SER A 836 SER A 849 1 14
HELIX 35 35 ASN A 871 LEU A 888 1 18
HELIX 36 36 SER A 896 VAL A 901 1 6
HELIX 37 37 LEU A 903 ARG A 919 1 17
HELIX 38 38 ASP A 924 LEU A 952 1 29
HELIX 39 39 ILE A 961 MET A 970 1 10
HELIX 40 40 ARG A 971 VAL A 986 1 16
HELIX 41 41 VAL A 986 ILE A 991 1 6
HELIX 42 42 GLY A 998 ILE A 1019 1 22
HELIX 43 43 PHE A 1025 PHE A 1033 1 9
SHEET 1 A 4 TYR A 77 SER A 79 0
SHEET 2 A 4 THR A 87 THR A 93 -1 O THR A 91 N SER A 79
SHEET 3 A 4 ALA A 42 SER A 48 -1 N ILE A 45 O ILE A 90
SHEET 4 A 4 SER A 128 LYS A 131 -1 O GLU A 130 N THR A 44
SHEET 1 B 2 ASN A 81 ASP A 83 0
SHEET 2 B 2 ARG A 815 GLU A 817 -1 O LEU A 816 N SER A 82
SHEET 1 C 4 VAL A 172 ASP A 174 0
SHEET 2 C 4 LEU A 289 LEU A 293 -1 O LYS A 292 N ASP A 174
SHEET 3 C 4 PHE A 136 ASN A 144 -1 N VAL A 140 O LEU A 289
SHEET 4 C 4 LEU A 321 VAL A 324 -1 O VAL A 324 N GLY A 141
SHEET 1 D 4 ALA A 266 GLY A 272 0
SHEET 2 D 4 TYR A 182 MET A 188 -1 N TRP A 187 O LYS A 267
SHEET 3 D 4 ARG A 767 VAL A 773 1 O LYS A 770 N MET A 184
SHEET 4 D 4 TYR A 758 ASP A 764 -1 N PHE A 762 O LYS A 769
SHEET 1 E 2 GLN A 218 LEU A 219 0
SHEET 2 E 2 ALA A 232 SER A 233 -1 O ALA A 232 N LEU A 219
SHEET 1 F 2 LEU A 250 ASN A 254 0
SHEET 2 F 2 SER A 258 LEU A 261 -1 O VAL A 260 N LYS A 252
SHEET 1 G 6 GLN A 284 ALA A 286 0
SHEET 2 G 6 ILE A 278 PHE A 281 -1 N ALA A 279 O ALA A 286
SHEET 3 G 6 ALA A 611 ASN A 613 -1 O ASN A 613 N ILE A 278
SHEET 4 G 6 THR A 624 PHE A 628 -1 O ILE A 626 N VAL A 612
SHEET 5 G 6 PHE A 572 GLN A 577 -1 N VAL A 576 O GLY A 625
SHEET 6 G 6 MET A 662 VAL A 663 -1 O MET A 662 N GLN A 577
SHEET 1 H 6 GLN A 284 ALA A 286 0
SHEET 2 H 6 ILE A 278 PHE A 281 -1 N ALA A 279 O ALA A 286
SHEET 3 H 6 ALA A 611 ASN A 613 -1 O ASN A 613 N ILE A 278
SHEET 4 H 6 THR A 624 PHE A 628 -1 O ILE A 626 N VAL A 612
SHEET 5 H 6 PHE A 572 GLN A 577 -1 N VAL A 576 O GLY A 625
SHEET 6 H 6 PHE A 666 ASN A 667 -1 O PHE A 666 N MET A 573
SHEET 1 I 2 VAL A 606 SER A 608 0
SHEET 2 I 2 SER A 630 LEU A 631 -1 O SER A 630 N SER A 608
SHEET 1 J 3 PHE A 682 ILE A 685 0
SHEET 2 J 3 SER A 824 GLN A 830 -1 O ILE A 827 N PHE A 682
SHEET 3 J 3 SER A 715 PRO A 718 -1 N SER A 715 O GLN A 830
SHEET 1 K 2 PRO A 725 ILE A 729 0
SHEET 2 K 2 SER A 807 TYR A 811 -1 O ARG A 808 N LYS A 728
SHEET 1 L 2 TYR A 790 ALA A 793 0
SHEET 2 L 2 GLN A 797 PRO A 800 -1 O VAL A 799 N VAL A 791
CRYST1 143.557 143.557 519.637 90.00 90.00 120.00 H 3 2 18
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 0.006966 0.004022 0.000000 0.00000
SCALE2 0.000000 0.008043 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001924 0.00000
ATOM 1 N ASP A 7 57.329 31.943 10.791 1.00112.06 N
ATOM 2 CA ASP A 7 58.429 31.535 9.869 1.00120.11 C
ATOM 3 C ASP A 7 58.777 30.064 10.078 1.00122.63 C
ATOM 4 O ASP A 7 58.762 29.274 9.132 1.00120.27 O
ATOM 5 CB ASP A 7 59.673 32.408 10.088 1.00119.27 C
ATOM 6 CG ASP A 7 59.329 33.822 10.525 1.00124.93 C
ATOM 7 OD1 ASP A 7 60.092 34.397 11.330 1.00102.00 O
ATOM 8 OD2 ASP A 7 58.320 34.436 10.118 1.00112.53 O
ATOM 9 N ARG A 8 59.094 29.714 11.323 1.00126.95 N
ATOM 10 CA ARG A 8 59.424 28.340 11.699 1.00129.10 C
ATOM 11 C ARG A 8 58.642 27.943 12.959 1.00126.38 C
ATOM 12 O ARG A 8 58.611 28.709 13.924 1.00123.57 O
ATOM 13 CB ARG A 8 60.929 28.202 11.951 1.00129.21 C
ATOM 14 CG ARG A 8 61.805 28.664 10.789 1.00132.20 C
ATOM 15 CD ARG A 8 63.297 28.646 11.088 1.00136.16 C
ATOM 16 NE ARG A 8 63.713 29.801 11.884 1.00133.69 N
ATOM 17 CZ ARG A 8 64.973 30.093 12.201 1.00133.48 C
ATOM 18 NH1 ARG A 8 65.976 29.316 11.797 1.00122.72 N
ATOM 19 NH2 ARG A 8 65.237 31.172 12.931 1.00119.51 N
ATOM 20 N PRO A 9 58.001 26.770 12.951 1.00120.97 N
ATOM 21 CA PRO A 9 57.288 26.266 14.139 1.00119.22 C
ATOM 22 C PRO A 9 58.227 25.967 15.331 1.00116.43 C
ATOM 23 O PRO A 9 58.751 26.908 15.922 1.00118.19 O
ATOM 24 CB PRO A 9 56.574 24.996 13.617 1.00120.40 C
ATOM 25 CG PRO A 9 56.706 25.012 12.139 1.00120.30 C
ATOM 26 CD PRO A 9 57.880 25.852 11.803 1.00120.93 C
ATOM 27 N ILE A 10 58.407 24.691 15.677 1.00109.64 N
ATOM 28 CA ILE A 10 59.435 24.199 16.611 1.00103.81 C
ATOM 29 C ILE A 10 60.200 25.178 17.519 1.00101.75 C
ATOM 30 O ILE A 10 59.831 25.321 18.678 1.00 96.79 O
ATOM 31 CB ILE A 10 60.411 23.185 15.904 1.00102.47 C
ATOM 32 CG1 ILE A 10 61.113 23.719 14.627 1.00101.32 C
ATOM 33 CG2 ILE A 10 59.664 21.880 15.598 1.00 97.26 C
ATOM 34 CD1 ILE A 10 60.605 24.961 13.930 1.00 95.72 C
ATOM 35 N PHE A 11 61.254 25.827 17.020 1.00104.00 N
ATOM 36 CA PHE A 11 62.106 26.694 17.853 1.00106.87 C
ATOM 37 C PHE A 11 61.287 27.713 18.649 1.00105.83 C
ATOM 38 O PHE A 11 61.524 27.916 19.840 1.00100.34 O
ATOM 39 CB PHE A 11 63.160 27.446 17.018 1.00108.56 C
ATOM 40 CG PHE A 11 63.842 26.608 15.960 1.00114.35 C
ATOM 41 CD1 PHE A 11 64.251 27.191 14.767 1.00119.49 C
ATOM 42 CD2 PHE A 11 64.085 25.251 16.153 1.00107.00 C
ATOM 43 CE1 PHE A 11 64.881 26.440 13.783 1.00117.43 C
ATOM 44 CE2 PHE A 11 64.711 24.493 15.169 1.00112.38 C
ATOM 45 CZ PHE A 11 65.112 25.090 13.986 1.00118.31 C
ATOM 46 N ALA A 12 60.344 28.362 17.969 1.00107.15 N
ATOM 47 CA ALA A 12 59.391 29.272 18.608 1.00107.32 C
ATOM 48 C ALA A 12 58.482 28.543 19.602 1.00104.87 C
ATOM 49 O ALA A 12 58.261 29.023 20.715 1.00105.71 O
ATOM 50 CB ALA A 12 58.550 29.979 17.549 1.00109.73 C
ATOM 51 N TRP A 13 57.954 27.394 19.185 1.00104.99 N
ATOM 52 CA TRP A 13 57.096 26.558 20.037 1.00107.55 C
ATOM 53 C TRP A 13 57.826 25.948 21.242 1.00107.92 C
ATOM 54 O TRP A 13 57.190 25.588 22.233 1.00100.99 O
ATOM 55 CB TRP A 13 56.457 25.430 19.211 1.00105.17 C
ATOM 56 CG TRP A 13 55.038 25.699 18.821 1.00112.02 C
ATOM 57 CD1 TRP A 13 54.585 26.698 18.010 1.00132.77 C
ATOM 58 CD2 TRP A 13 53.883 24.956 19.224 1.00109.11 C
ATOM 59 NE1 TRP A 13 53.218 26.624 17.884 1.00136.93 N
ATOM 60 CE2 TRP A 13 52.761 25.561 18.620 1.00127.79 C
ATOM 61 CE3 TRP A 13 53.680 23.833 20.038 1.00100.17 C
ATOM 62 CZ2 TRP A 13 51.458 25.086 18.806 1.00115.11 C
ATOM 63 CZ3 TRP A 13 52.387 23.361 20.220 1.00106.80 C
ATOM 64 CH2 TRP A 13 51.295 23.987 19.605 1.00118.13 C
ATOM 65 N VAL A 14 59.149 25.835 21.149 1.00106.89 N
ATOM 66 CA VAL A 14 59.969 25.220 22.192 1.00104.19 C
ATOM 67 C VAL A 14 60.316 26.271 23.251 1.00102.81 C
ATOM 68 O VAL A 14 60.539 25.935 24.415 1.00 97.42 O
ATOM 69 CB VAL A 14 61.247 24.568 21.586 1.00103.83 C
ATOM 70 CG1 VAL A 14 62.295 24.260 22.656 1.00105.85 C
ATOM 71 CG2 VAL A 14 60.882 23.294 20.821 1.00 92.78 C
ATOM 72 N ILE A 15 60.354 27.538 22.840 1.00102.25 N
ATOM 73 CA ILE A 15 60.481 28.658 23.773 1.00104.18 C
ATOM 74 C ILE A 15 59.190 28.809 24.582 1.00103.77 C
ATOM 75 O ILE A 15 59.220 29.243 25.735 1.00105.19 O
ATOM 76 CB ILE A 15 60.849 29.976 23.012 1.00103.07 C
ATOM 77 CG1 ILE A 15 62.368 30.189 23.044 1.00110.56 C
ATOM 78 CG2 ILE A 15 60.115 31.201 23.591 1.00103.13 C
ATOM 79 CD1 ILE A 15 62.837 31.482 22.399 1.00108.58 C
ATOM 80 N ALA A 16 58.062 28.450 23.971 1.00103.53 N
ATOM 81 CA ALA A 16 56.774 28.455 24.659 1.00103.32 C
ATOM 82 C ALA A 16 56.727 27.373 25.737 1.00105.09 C
ATOM 83 O ALA A 16 56.132 27.580 26.791 1.00105.17 O
ATOM 84 CB ALA A 16 55.632 28.264 23.664 1.00101.82 C
ATOM 85 N ILE A 17 57.363 26.231 25.467 1.00106.33 N
ATOM 86 CA ILE A 17 57.406 25.110 26.411 1.00108.03 C
ATOM 87 C ILE A 17 58.397 25.366 27.556 1.00105.28 C
ATOM 88 O ILE A 17 58.270 24.776 28.630 1.00 97.28 O
ATOM 89 CB ILE A 17 57.728 23.783 25.670 1.00110.87 C
ATOM 90 CG1 ILE A 17 56.609 23.443 24.678 1.00107.88 C
ATOM 91 CG2 ILE A 17 57.897 22.623 26.655 1.00109.78 C
ATOM 92 CD1 ILE A 17 57.063 22.602 23.502 1.00105.15 C
ATOM 93 N ILE A 18 59.375 26.243 27.329 1.00105.63 N
ATOM 94 CA ILE A 18 60.241 26.723 28.408 1.00107.62 C
ATOM 95 C ILE A 18 59.390 27.486 29.420 1.00106.10 C
ATOM 96 O ILE A 18 59.575 27.348 30.627 1.00103.55 O
ATOM 97 CB ILE A 18 61.382 27.628 27.855 1.00108.17 C
ATOM 98 CG1 ILE A 18 62.543 26.771 27.343 1.00107.61 C
ATOM 99 CG2 ILE A 18 61.886 28.618 28.919 1.00105.62 C
ATOM 100 CD1 ILE A 18 63.506 27.516 26.435 1.00109.15 C
ATOM 101 N ILE A 19 58.455 28.285 28.911 1.00103.03 N
ATOM 102 CA ILE A 19 57.565 29.085 29.748 1.00101.25 C
ATOM 103 C ILE A 19 56.447 28.235 30.373 1.00 99.92 C
ATOM 104 O ILE A 19 55.847 28.639 31.369 1.00 96.01 O
ATOM 105 CB ILE A 19 56.983 30.270 28.928 1.00100.78 C
ATOM 106 CG1 ILE A 19 58.112 31.192 28.448 1.00 98.81 C
ATOM 107 CG2 ILE A 19 55.991 31.073 29.756 1.00100.50 C
ATOM 108 CD1 ILE A 19 57.762 32.005 27.220 1.00 88.81 C
ATOM 109 N MET A 20 56.172 27.063 29.798 1.00102.86 N
ATOM 110 CA MET A 20 55.218 26.124 30.391 1.00107.16 C
ATOM 111 C MET A 20 55.759 25.582 31.712 1.00104.73 C
ATOM 112 O MET A 20 54.997 25.356 32.654 1.00106.28 O
ATOM 113 CB MET A 20 54.910 24.957 29.445 1.00110.24 C
ATOM 114 CG MET A 20 54.157 25.339 28.176 1.00110.62 C
ATOM 115 SD MET A 20 52.450 25.859 28.454 1.00121.82 S
ATOM 116 CE MET A 20 51.606 24.286 28.439 1.00115.19 C
ATOM 117 N LEU A 21 57.074 25.377 31.772 1.00101.79 N
ATOM 118 CA LEU A 21 57.727 24.915 32.992 1.00 99.49 C
ATOM 119 C LEU A 21 57.948 26.080 33.952 1.00 99.45 C
ATOM 120 O LEU A 21 57.272 26.162 34.967 1.00 98.99 O
ATOM 121 CB LEU A 21 59.048 24.202 32.675 1.00100.32 C
ATOM 122 CG LEU A 21 58.999 23.043 31.670 1.00 97.94 C
ATOM 123 CD1 LEU A 21 60.218 22.150 31.847 1.00 85.26 C
ATOM 124 CD2 LEU A 21 57.714 22.223 31.786 1.00 98.23 C
ATOM 125 N ALA A 22 58.861 26.991 33.613 1.00 99.42 N
ATOM 126 CA ALA A 22 59.218 28.135 34.467 1.00 98.52 C
ATOM 127 C ALA A 22 58.032 28.817 35.163 1.00101.86 C
ATOM 128 O ALA A 22 58.181 29.345 36.265 1.00104.84 O
ATOM 129 CB ALA A 22 60.008 29.167 33.660 1.00 97.48 C
ATOM 130 N GLY A 23 56.872 28.819 34.510 1.00104.69 N
ATOM 131 CA GLY A 23 55.652 29.348 35.095 1.00105.31 C
ATOM 132 C GLY A 23 54.992 28.393 36.070 1.00105.19 C
ATOM 133 O GLY A 23 54.765 28.743 37.228 1.00104.99 O
ATOM 134 N GLY A 24 54.680 27.189 35.594 1.00105.67 N
ATOM 135 CA GLY A 24 54.097 26.145 36.425 1.00104.55 C
ATOM 136 C GLY A 24 55.078 25.460 37.369 1.00100.05 C
ATOM 137 O GLY A 24 54.693 24.563 38.117 1.00 94.02 O
ATOM 138 N LEU A 25 56.342 25.876 37.319 1.00 99.26 N
ATOM 139 CA LEU A 25 57.385 25.420 38.237 1.00102.46 C
ATOM 140 C LEU A 25 57.508 26.456 39.350 1.00102.47 C
ATOM 141 O LEU A 25 57.751 26.114 40.508 1.00 97.56 O
ATOM 142 CB LEU A 25 58.716 25.260 37.487 1.00104.13 C
ATOM 143 CG LEU A 25 60.033 24.999 38.237 1.00105.04 C
ATOM 144 CD1 LEU A 25 60.627 26.287 38.828 1.00110.25 C
ATOM 145 CD2 LEU A 25 59.879 23.923 39.311 1.00102.04 C
ATOM 146 N ALA A 26 57.341 27.726 38.984 1.00104.25 N
ATOM 147 CA ALA A 26 57.268 28.815 39.951 1.00106.34 C
ATOM 148 C ALA A 26 55.998 28.724 40.798 1.00105.72 C
ATOM 149 O ALA A 26 55.969 29.229 41.912 1.00107.03 O
ATOM 150 CB ALA A 26 57.333 30.163 39.240 1.00101.06 C
ATOM 151 N ILE A 27 54.957 28.078 40.272 1.00101.19 N
ATOM 152 CA ILE A 27 53.702 27.906 41.009 1.00 95.82 C
ATOM 153 C ILE A 27 53.847 26.862 42.125 1.00 98.12 C
ATOM 154 O ILE A 27 53.122 26.909 43.122 1.00 92.68 O
ATOM 155 CB ILE A 27 52.528 27.555 40.034 1.00 92.22 C
ATOM 156 CG1 ILE A 27 51.273 28.352 40.399 1.00 86.62 C
ATOM 157 CG2 ILE A 27 52.220 26.056 40.017 1.00 84.78 C
ATOM 158 CD1 ILE A 27 51.336 29.805 39.977 1.00 86.81 C
ATOM 159 N LEU A 28 54.787 25.933 41.949 1.00101.82 N
ATOM 160 CA LEU A 28 55.101 24.918 42.958 1.00104.56 C
ATOM 161 C LEU A 28 56.315 25.327 43.806 1.00103.74 C
ATOM 162 O LEU A 28 56.956 24.480 44.431 1.00101.52 O
ATOM 163 CB LEU A 28 55.373 23.564 42.288 1.00108.01 C
ATOM 164 CG LEU A 28 54.453 23.141 41.135 1.00118.11 C
ATOM 165 CD1 LEU A 28 55.055 21.979 40.356 1.00130.95 C
ATOM 166 CD2 LEU A 28 53.062 22.787 41.640 1.00117.93 C
ATOM 167 N LYS A 29 56.621 26.624 43.821 1.00104.10 N
ATOM 168 CA LYS A 29 57.777 27.158 44.540 1.00105.30 C
ATOM 169 C LYS A 29 57.588 28.663 44.780 1.00108.16 C
ATOM 170 O LYS A 29 58.483 29.471 44.513 1.00106.97 O
ATOM 171 CB LYS A 29 59.058 26.889 43.739 1.00102.44 C
ATOM 172 CG LYS A 29 60.349 26.988 44.547 1.00 99.50 C
ATOM 173 CD LYS A 29 61.568 27.141 43.639 1.00105.91 C
ATOM 174 CE LYS A 29 61.793 28.587 43.202 1.00110.30 C
ATOM 175 NZ LYS A 29 61.018 28.942 41.978 1.00111.91 N
ATOM 176 N LEU A 30 56.411 29.026 45.289 1.00107.37 N
ATOM 177 CA LEU A 30 56.034 30.428 45.466 1.00107.09 C
ATOM 178 C LEU A 30 54.856 30.553 46.440 1.00106.68 C
ATOM 179 O LEU A 30 53.876 29.814 46.315 1.00104.80 O
ATOM 180 CB LEU A 30 55.656 31.030 44.113 1.00107.28 C
ATOM 181 CG LEU A 30 55.521 32.550 43.995 1.00107.23 C
ATOM 182 CD1 LEU A 30 56.791 33.176 43.442 1.00102.98 C
ATOM 183 CD2 LEU A 30 54.333 32.905 43.116 1.00104.83 C
ATOM 184 N PRO A 31 54.941 31.475 47.403 1.00104.64 N
ATOM 185 CA PRO A 31 53.876 31.641 48.404 1.00106.62 C
ATOM 186 C PRO A 31 52.483 31.887 47.809 1.00105.81 C
ATOM 187 O PRO A 31 52.257 32.907 47.163 1.00101.41 O
ATOM 188 CB PRO A 31 54.331 32.867 49.214 1.00108.43 C
ATOM 189 CG PRO A 31 55.785 32.992 48.975 1.00103.29 C
ATOM 190 CD PRO A 31 56.057 32.412 47.630 1.00101.99 C
ATOM 191 N VAL A 32 51.562 30.954 48.042 1.00104.85 N
ATOM 192 CA VAL A 32 50.149 31.140 47.674 1.00104.62 C
ATOM 193 C VAL A 32 49.382 32.000 48.708 1.00104.79 C
ATOM 194 O VAL A 32 48.139 32.019 48.721 1.00 93.68 O
ATOM 195 CB VAL A 32 49.407 29.776 47.421 1.00105.14 C
ATOM 196 CG1 VAL A 32 49.557 29.348 45.966 1.00 99.53 C
ATOM 197 CG2 VAL A 32 49.895 28.662 48.350 1.00110.22 C
ATOM 198 N ALA A 33 50.139 32.716 49.554 1.00112.99 N
ATOM 199 CA ALA A 33 49.595 33.629 50.573 1.00118.71 C
ATOM 200 C ALA A 33 48.680 34.746 50.047 1.00122.37 C
ATOM 201 O ALA A 33 48.496 34.906 48.841 1.00116.96 O
ATOM 202 CB ALA A 33 50.758 34.247 51.363 1.00118.20 C
ATOM 203 N GLN A 34 48.120 35.517 50.981 1.00120.45 N
ATOM 204 CA GLN A 34 47.278 36.677 50.670 1.00116.99 C
ATOM 205 C GLN A 34 48.108 37.853 50.142 1.00113.65 C
ATOM 206 O GLN A 34 49.240 37.668 49.693 1.00104.48 O
ATOM 207 CB GLN A 34 46.513 37.123 51.930 1.00118.78 C
ATOM 208 CG GLN A 34 45.567 36.096 52.514 1.00122.13 C
ATOM 209 CD GLN A 34 44.339 35.878 51.650 1.00127.60 C
ATOM 210 OE1 GLN A 34 44.424 35.265 50.586 1.00116.15 O
ATOM 211 NE2 GLN A 34 43.198 36.382 52.101 1.00117.81 N
ATOM 212 N TYR A 35 47.511 39.048 50.160 1.00112.04 N
ATOM 213 CA TYR A 35 48.216 40.328 49.980 1.00117.74 C
ATOM 214 C TYR A 35 49.683 40.291 50.435 1.00119.20 C
ATOM 215 O TYR A 35 50.024 39.582 51.386 1.00119.44 O
ATOM 216 CB TYR A 35 47.520 41.466 50.759 1.00117.91 C
ATOM 217 CG TYR A 35 46.011 41.371 50.902 1.00124.24 C
ATOM 218 CD1 TYR A 35 45.433 40.604 51.915 1.00120.33 C
ATOM 219 CD2 TYR A 35 45.164 42.075 50.045 1.00129.89 C
ATOM 220 CE1 TYR A 35 44.054 40.519 52.054 1.00131.29 C
ATOM 221 CE2 TYR A 35 43.781 42.000 50.179 1.00134.02 C
ATOM 222 CZ TYR A 35 43.234 41.220 51.185 1.00141.92 C
ATOM 223 OH TYR A 35 41.867 41.141 51.322 1.00140.82 O
ATOM 224 N PRO A 36 50.541 41.086 49.794 1.00117.83 N
ATOM 225 CA PRO A 36 51.959 41.149 50.171 1.00113.80 C
ATOM 226 C PRO A 36 52.167 41.859 51.509 1.00109.56 C
ATOM 227 O PRO A 36 51.194 42.262 52.145 1.00 97.74 O
ATOM 228 CB PRO A 36 52.572 41.973 49.036 1.00116.05 C
ATOM 229 CG PRO A 36 51.469 42.865 48.618 1.00111.38 C
ATOM 230 CD PRO A 36 50.239 42.004 48.679 1.00117.33 C
ATOM 231 N THR A 37 53.421 42.001 51.931 1.00109.01 N
ATOM 232 CA THR A 37 53.747 42.786 53.119 1.00110.04 C
ATOM 233 C THR A 37 53.645 44.271 52.766 1.00106.77 C
ATOM 234 O THR A 37 54.333 44.740 51.855 1.00 97.82 O
ATOM 235 CB THR A 37 55.164 42.440 53.629 1.00109.64 C
ATOM 236 OG1 THR A 37 55.162 41.133 54.225 1.00107.82 O
ATOM 237 CG2 THR A 37 55.587 43.368 54.773 1.00107.78 C
ATOM 238 N ILE A 38 52.790 45.001 53.485 1.00104.06 N
ATOM 239 CA ILE A 38 52.497 46.399 53.161 1.00106.08 C
ATOM 240 C ILE A 38 52.991 47.358 54.240 1.00108.75 C
ATOM 241 O ILE A 38 53.839 48.213 53.978 1.00112.46 O
ATOM 242 CB ILE A 38 50.971 46.621 52.958 1.00104.04 C
ATOM 243 CG1 ILE A 38 50.322 45.441 52.220 1.00103.57 C
ATOM 244 CG2 ILE A 38 50.725 47.929 52.214 1.00105.42 C
ATOM 245 CD1 ILE A 38 49.543 44.513 53.136 1.00102.73 C
ATOM 246 N ALA A 39 52.450 47.209 55.448 1.00104.47 N
ATOM 247 CA ALA A 39 52.631 48.195 56.512 1.00101.25 C
ATOM 248 C ALA A 39 54.100 48.363 56.900 1.00 95.95 C
ATOM 249 O ALA A 39 54.853 47.386 56.901 1.00 89.14 O
ATOM 250 CB ALA A 39 51.807 47.811 57.733 1.00105.08 C
ATOM 251 N PRO A 40 54.508 49.595 57.217 1.00 95.45 N
ATOM 252 CA PRO A 40 55.881 49.864 57.665 1.00101.05 C
ATOM 253 C PRO A 40 56.288 48.970 58.847 1.00105.09 C
ATOM 254 O PRO A 40 55.679 49.079 59.914 1.00104.43 O
ATOM 255 CB PRO A 40 55.833 51.342 58.076 1.00101.21 C
ATOM 256 CG PRO A 40 54.713 51.919 57.300 1.00105.59 C
ATOM 257 CD PRO A 40 53.702 50.829 57.159 1.00 97.65 C
ATOM 258 N PRO A 41 57.275 48.091 58.651 1.00105.81 N
ATOM 259 CA PRO A 41 57.667 47.103 59.667 1.00 98.74 C
ATOM 260 C PRO A 41 57.919 47.672 61.065 1.00 93.23 C
ATOM 261 O PRO A 41 58.677 48.630 61.194 1.00 88.84 O
ATOM 262 CB PRO A 41 58.965 46.523 59.092 1.00100.59 C
ATOM 263 CG PRO A 41 58.801 46.653 57.631 1.00100.21 C
ATOM 264 CD PRO A 41 58.089 47.954 57.428 1.00110.78 C
ATOM 265 N ALA A 42 57.296 47.082 62.085 1.00 88.84 N
ATOM 266 CA ALA A 42 57.422 47.564 63.462 1.00 92.91 C
ATOM 267 C ALA A 42 57.836 46.469 64.450 1.00 89.40 C
ATOM 268 O ALA A 42 57.602 45.280 64.222 1.00 85.47 O
ATOM 269 CB ALA A 42 56.117 48.209 63.910 1.00 94.81 C
ATOM 270 N VAL A 43 58.453 46.903 65.548 1.00 87.45 N
ATOM 271 CA VAL A 43 58.893 46.036 66.640 1.00 87.77 C
ATOM 272 C VAL A 43 58.153 46.463 67.910 1.00 91.73 C
ATOM 273 O VAL A 43 57.777 47.625 68.047 1.00 99.93 O
ATOM 274 CB VAL A 43 60.421 46.170 66.856 1.00 85.27 C
ATOM 275 CG1 VAL A 43 60.919 45.225 67.946 1.00 88.56 C
ATOM 276 CG2 VAL A 43 61.171 45.918 65.550 1.00 75.07 C
ATOM 277 N THR A 44 57.937 45.526 68.832 1.00 89.88 N
ATOM 278 CA THR A 44 57.206 45.819 70.065 1.00 89.85 C
ATOM 279 C THR A 44 57.899 45.252 71.301 1.00 91.01 C
ATOM 280 O THR A 44 58.136 44.048 71.402 1.00 93.02 O
ATOM 281 CB THR A 44 55.765 45.281 69.983 1.00 88.50 C
ATOM 282 OG1 THR A 44 55.194 45.615 68.711 1.00 84.02 O
ATOM 283 CG2 THR A 44 54.860 45.998 70.978 1.00 87.37 C
ATOM 284 N ILE A 45 58.206 46.145 72.237 1.00 89.35 N
ATOM 285 CA ILE A 45 58.801 45.791 73.519 1.00 87.74 C
ATOM 286 C ILE A 45 57.680 45.620 74.539 1.00 92.96 C
ATOM 287 O ILE A 45 56.662 46.303 74.461 1.00103.80 O
ATOM 288 CB ILE A 45 59.782 46.895 73.979 1.00 84.75 C
ATOM 289 CG1 ILE A 45 60.696 47.310 72.815 1.00 82.43 C
ATOM 290 CG2 ILE A 45 60.597 46.415 75.176 1.00 81.71 C
ATOM 291 CD1 ILE A 45 61.799 48.263 73.188 1.00 80.51 C
ATOM 292 N SER A 46 57.869 44.700 75.483 1.00 95.05 N
ATOM 293 CA SER A 46 56.898 44.465 76.553 1.00101.02 C
ATOM 294 C SER A 46 57.602 44.275 77.897 1.00102.59 C
ATOM 295 O SER A 46 58.803 44.003 77.951 1.00 98.20 O
ATOM 296 CB SER A 46 56.029 43.242 76.239 1.00103.90 C
ATOM 297 OG SER A 46 55.669 43.201 74.866 1.00110.58 O
ATOM 298 N ALA A 47 56.840 44.419 78.977 1.00105.27 N
ATOM 299 CA ALA A 47 57.375 44.305 80.334 1.00103.71 C
ATOM 300 C ALA A 47 56.245 44.285 81.360 1.00102.28 C
ATOM 301 O ALA A 47 55.315 45.086 81.276 1.00101.98 O
ATOM 302 CB ALA A 47 58.331 45.457 80.628 1.00103.54 C
ATOM 303 N SER A 48 56.330 43.373 82.325 1.00 97.44 N
ATOM 304 CA SER A 48 55.329 43.266 83.385 1.00 96.02 C
ATOM 305 C SER A 48 55.931 43.619 84.746 1.00 96.75 C
ATOM 306 O SER A 48 57.149 43.577 84.929 1.00103.42 O
ATOM 307 CB SER A 48 54.731 41.858 83.409 1.00 92.23 C
ATOM 308 OG SER A 48 53.548 41.813 84.189 1.00 84.74 O
ATOM 309 N TYR A 49 55.061 43.958 85.694 1.00 95.46 N
ATOM 310 CA TYR A 49 55.465 44.422 87.020 1.00 91.62 C
ATOM 311 C TYR A 49 54.308 44.165 87.995 1.00 91.70 C
ATOM 312 O TYR A 49 53.466 45.040 88.204 1.00 86.82 O
ATOM 313 CB TYR A 49 55.832 45.916 86.976 1.00 91.43 C
ATOM 314 CG TYR A 49 56.557 46.466 88.202 1.00 83.14 C
ATOM 315 CD1 TYR A 49 56.739 47.840 88.357 1.00 93.37 C
ATOM 316 CD2 TYR A 49 57.070 45.625 89.197 1.00 74.50 C
ATOM 317 CE1 TYR A 49 57.397 48.362 89.465 1.00 90.88 C
ATOM 318 CE2 TYR A 49 57.730 46.144 90.307 1.00 82.78 C
ATOM 319 CZ TYR A 49 57.890 47.510 90.434 1.00 90.48 C
ATOM 320 OH TYR A 49 58.543 48.027 91.529 1.00 91.27 O
ATOM 321 N PRO A 50 54.260 42.961 88.570 1.00 94.58 N
ATOM 322 CA PRO A 50 53.113 42.514 89.380 1.00 93.60 C
ATOM 323 C PRO A 50 52.621 43.528 90.419 1.00 94.71 C
ATOM 324 O PRO A 50 53.358 43.854 91.350 1.00 98.23 O
ATOM 325 CB PRO A 50 53.633 41.247 90.086 1.00 88.80 C
ATOM 326 CG PRO A 50 54.888 40.843 89.394 1.00 93.30 C
ATOM 327 CD PRO A 50 55.303 41.926 88.465 1.00 93.45 C
ATOM 328 N GLY A 51 51.394 44.019 90.242 1.00 95.65 N
ATOM 329 CA GLY A 51 50.757 44.903 91.208 1.00 94.20 C
ATOM 330 C GLY A 51 50.868 46.380 90.876 1.00 93.07 C
ATOM 331 O GLY A 51 49.894 47.122 91.022 1.00 95.20 O
ATOM 332 N ALA A 52 52.056 46.803 90.444 1.00 89.64 N
ATOM 333 CA ALA A 52 52.337 48.201 90.101 1.00 93.74 C
ATOM 334 C ALA A 52 51.176 48.900 89.392 1.00 96.41 C
ATOM 335 O ALA A 52 50.678 48.417 88.374 1.00101.07 O
ATOM 336 CB ALA A 52 53.589 48.281 89.237 1.00 93.61 C
ATOM 337 N ASP A 53 50.755 50.039 89.940 1.00 95.06 N
ATOM 338 CA ASP A 53 49.695 50.850 89.338 1.00 93.57 C
ATOM 339 C ASP A 53 50.200 51.568 88.082 1.00 89.23 C
ATOM 340 O ASP A 53 51.384 51.499 87.757 1.00 87.02 O
ATOM 341 CB ASP A 53 49.126 51.850 90.357 1.00 92.79 C
ATOM 342 CG ASP A 53 50.088 52.980 90.683 1.00 97.08 C
ATOM 343 OD1 ASP A 53 51.106 52.729 91.360 1.00 94.20 O
ATOM 344 OD2 ASP A 53 49.895 54.157 90.319 1.00100.40 O
ATOM 345 N ALA A 54 49.296 52.258 87.388 1.00 87.31 N
ATOM 346 CA ALA A 54 49.598 52.859 86.083 1.00 87.30 C
ATOM 347 C ALA A 54 50.698 53.922 86.111 1.00 85.04 C