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PDBsum entry 2dpy

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Hydrolase PDB id
2dpy
Jmol
Contents
Protein chains
422 a.a.
Ligands
ADP
Waters ×133
HEADER    HYDROLASE                               18-MAY-06   2DPY
TITLE     CRYSTAL STRUCTURE OF THE FLAGELLAR TYPE III ATPASE FLII
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: FLAGELLUM-SPECIFIC ATP SYNTHASE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: RESIDUES 19-456;
COMPND   5 SYNONYM: FLII;
COMPND   6 EC: 3.6.3.14;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE   3 ORGANISM_TAXID: 602;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET19B
KEYWDS    BETA BARREL, ALPHA-BETA STRUCTURE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.IMADA,K.NAMBA,T.MINAMINO
REVDAT   3   24-FEB-09 2DPY    1       VERSN
REVDAT   2   23-JAN-07 2DPY    1       JRNL
REVDAT   1   26-DEC-06 2DPY    0
JRNL        AUTH   K.IMADA,T.MINAMINO,A.TAHARA,K.NAMBA
JRNL        TITL   STRUCTURAL SIMILARITY BETWEEN THE FLAGELLAR TYPE
JRNL        TITL 2 III ATPASE FLII AND F1-ATPASE SUBUNITS
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 104   485 2007
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   17202259
JRNL        DOI    10.1073/PNAS.0608090104
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.98
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1468462.990
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4
REMARK   3   NUMBER OF REFLECTIONS             : 33945
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 SET) : 0.244
REMARK   3   FREE R VALUE                     : 0.295
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 1680
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.80
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5312
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960
REMARK   3   BIN FREE R VALUE                    : 0.3610
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 262
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 6444
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 27
REMARK   3   SOLVENT ATOMS            : 133
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 32.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.20
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 11.64000
REMARK   3    B22 (A**2) : -7.70000
REMARK   3    B33 (A**2) : -3.94000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 4.90000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.35
REMARK   3   ESD FROM SIGMAA              (A) : 0.31
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.45
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.41
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.00
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.20
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.660 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.800 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.100 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.120 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.31
REMARK   3   BSOL        : 36.89
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ADP.PARAM
REMARK   3  PARAMETER FILE  4  : CIS_PEPTIDE.PARAM
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : ADP.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2DPY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-06.
REMARK 100 THE RCSB ID CODE IS RCSB025703.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL41XU
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33960
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.130
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.06800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.23800
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 8000, 0.1M CALCIUM ACETATE,
REMARK 280  3% MPD, 0.1M IMIDAZOLE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       36.37500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: MONOMER OR HEXAMER IN SOLUTION.
REMARK 300 THE PRECISE HEXAMERIC STRUCTURE IS NOT KNOWN.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A    19
REMARK 465     ALA A    20
REMARK 465     LEU A    21
REMARK 465     LEU A    22
REMARK 465     PRO A    23
REMARK 465     ALA A    24
REMARK 465     ASN A    98
REMARK 465     GLY A    99
REMARK 465     HIS A   100
REMARK 465     GLY A   101
REMARK 465     ASP A   102
REMARK 465     GLY A   103
REMARK 465     LEU A   104
REMARK 465     GLN A   105
REMARK 465     SER A   106
REMARK 465     GLY A   107
REMARK 465     MET B    19
REMARK 465     ALA B    20
REMARK 465     LEU B    21
REMARK 465     LEU B    22
REMARK 465     ASN B    98
REMARK 465     GLY B    99
REMARK 465     HIS B   100
REMARK 465     GLY B   101
REMARK 465     ASP B   102
REMARK 465     GLY B   103
REMARK 465     LEU B   104
REMARK 465     GLN B   105
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    SER A 273   N   -  CA  -  CB  ANGL. DEV. =  13.7 DEGREES
REMARK 500    GLY A 318   N   -  CA  -  C   ANGL. DEV. = -22.6 DEGREES
REMARK 500    SER B 273   N   -  CA  -  CB  ANGL. DEV. =  11.3 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    ASN A  73      132.56    -38.98
REMARK 500    GLN A  75      -30.02   -162.94
REMARK 500    ARG A  76      175.82    167.48
REMARK 500    THR A 136     -103.97    -56.25
REMARK 500    LEU A 137       -0.29     90.47
REMARK 500    ILE A 143      -86.33    -86.00
REMARK 500    THR A 144      116.73     53.22
REMARK 500    PRO A 149       35.60    -65.27
REMARK 500    LEU A 170       50.62   -148.50
REMARK 500    THR A 294     -118.31   -119.44
REMARK 500    LYS A 295       43.38    -68.05
REMARK 500    ASN A 314      151.62    -41.70
REMARK 500    ASP A 333      101.44     74.00
REMARK 500    ALA A 365       47.25    -78.93
REMARK 500    SER A 406       34.17    -82.19
REMARK 500    VAL A 407      -37.02   -134.52
REMARK 500    ASP A 415       67.86     35.10
REMARK 500    ALA A 421      -62.99    -97.10
REMARK 500    PHE A 453      -75.97   -114.44
REMARK 500    PRO A 454     -155.20   -117.66
REMARK 500    ALA B  34     -101.88    -63.37
REMARK 500    THR B  35      129.21    -13.21
REMARK 500    PRO B  60       25.90    -77.33
REMARK 500    SER B  67     -147.68   -146.29
REMARK 500    GLN B  75       45.86   -106.13
REMARK 500    GLU B  83     -131.97   -152.21
REMARK 500    GLU B  86      -40.68   -135.43
REMARK 500    ALA B  96     -137.09    -50.17
REMARK 500    LYS B 108      173.53    -58.98
REMARK 500    GLU B 156        7.47   -152.33
REMARK 500    LEU B 170       39.58   -143.41
REMARK 500    THR B 171      119.92    -38.23
REMARK 500    ALA B 237       82.24   -160.71
REMARK 500    ALA B 293      -84.92    -79.04
REMARK 500    LYS B 295       65.64     32.52
REMARK 500    ILE B 316      -88.42    -52.05
REMARK 500    HIS B 317     -111.28   -100.67
REMARK 500    GLU B 331       -1.19    -53.00
REMARK 500    ASP B 333       -3.38     68.09
REMARK 500    GLN B 335      -66.83   -102.15
REMARK 500    GLN B 336       69.58    -57.74
REMARK 500    ASP B 348       35.48    -87.56
REMARK 500    ALA B 365       44.53    -80.19
REMARK 500    LYS B 412       84.23    -52.65
REMARK 500    ASP B 450        5.51    -69.25
REMARK 500    PHE B 453      -81.51   -124.47
REMARK 500    PRO B 454      145.77    -22.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ASP A  272     SER A  273                   59.99
REMARK 500 ASP B  272     SER B  273                   50.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    ASP A 272         24.23
REMARK 500    ASP B 272         21.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 600
DBREF  2DPY A   19   456  UNP    P26465   FLII_SALTY      19    456
DBREF  2DPY B   19   456  UNP    P26465   FLII_SALTY      19    456
SEQRES   1 A  438  MET ALA LEU LEU PRO ALA VAL ARG ARG TYR GLY ARG LEU
SEQRES   2 A  438  THR ARG ALA THR GLY LEU VAL LEU GLU ALA THR GLY LEU
SEQRES   3 A  438  GLN LEU PRO LEU GLY ALA THR CYS ILE ILE GLU ARG GLN
SEQRES   4 A  438  ASP GLY PRO GLU THR LYS GLU VAL GLU SER GLU VAL VAL
SEQRES   5 A  438  GLY PHE ASN GLY GLN ARG LEU PHE LEU MET PRO LEU GLU
SEQRES   6 A  438  GLU VAL GLU GLY ILE LEU PRO GLY ALA ARG VAL TYR ALA
SEQRES   7 A  438  ARG ASN GLY HIS GLY ASP GLY LEU GLN SER GLY LYS GLN
SEQRES   8 A  438  LEU PRO LEU GLY PRO ALA LEU LEU GLY ARG VAL LEU ASP
SEQRES   9 A  438  GLY GLY GLY LYS PRO LEU ASP GLY LEU PRO ALA PRO ASP
SEQRES  10 A  438  THR LEU GLU THR GLY ALA LEU ILE THR PRO PRO PHE ASN
SEQRES  11 A  438  PRO LEU GLN ARG THR PRO ILE GLU HIS VAL LEU ASP THR
SEQRES  12 A  438  GLY VAL ARG ALA ILE ASN ALA LEU LEU THR VAL GLY ARG
SEQRES  13 A  438  GLY GLN ARG MET GLY LEU PHE ALA GLY SER GLY VAL GLY
SEQRES  14 A  438  LYS SER VAL LEU LEU GLY MET MET ALA ARG TYR THR ARG
SEQRES  15 A  438  ALA ASP VAL ILE VAL VAL GLY LEU ILE GLY GLU ARG GLY
SEQRES  16 A  438  ARG GLU VAL LYS ASP PHE ILE GLU ASN ILE LEU GLY PRO
SEQRES  17 A  438  ASP GLY ARG ALA ARG SER VAL VAL ILE ALA ALA PRO ALA
SEQRES  18 A  438  ASP VAL SER PRO LEU LEU ARG MET GLN GLY ALA ALA TYR
SEQRES  19 A  438  ALA THR ARG ILE ALA GLU ASP PHE ARG ASP ARG GLY GLN
SEQRES  20 A  438  HIS VAL LEU LEU ILE MET ASP SER LEU THR ARG TYR ALA
SEQRES  21 A  438  MET ALA GLN ARG GLU ILE ALA LEU ALA ILE GLY GLU PRO
SEQRES  22 A  438  PRO ALA THR LYS GLY TYR PRO PRO SER VAL PHE ALA LYS
SEQRES  23 A  438  LEU PRO ALA LEU VAL GLU ARG ALA GLY ASN GLY ILE HIS
SEQRES  24 A  438  GLY GLY GLY SER ILE THR ALA PHE TYR THR VAL LEU THR
SEQRES  25 A  438  GLU GLY ASP ASP GLN GLN ASP PRO ILE ALA ASP SER ALA
SEQRES  26 A  438  ARG ALA ILE LEU ASP GLY HIS ILE VAL LEU SER ARG ARG
SEQRES  27 A  438  LEU ALA GLU ALA GLY HIS TYR PRO ALA ILE ASP ILE GLU
SEQRES  28 A  438  ALA SER ILE SER ARG ALA MET THR ALA LEU ILE THR GLU
SEQRES  29 A  438  GLN HIS TYR ALA ARG VAL ARG LEU PHE LYS GLN LEU LEU
SEQRES  30 A  438  SER SER PHE GLN ARG ASN ARG ASP LEU VAL SER VAL GLY
SEQRES  31 A  438  ALA TYR ALA LYS GLY SER ASP PRO MET LEU ASP LYS ALA
SEQRES  32 A  438  ILE THR LEU TRP PRO GLN LEU GLU ALA PHE LEU GLN GLN
SEQRES  33 A  438  GLY ILE PHE GLU ARG ALA ASP TRP GLU ASP SER LEU GLN
SEQRES  34 A  438  ALA LEU ASP LEU ILE PHE PRO THR VAL
SEQRES   1 B  438  MET ALA LEU LEU PRO ALA VAL ARG ARG TYR GLY ARG LEU
SEQRES   2 B  438  THR ARG ALA THR GLY LEU VAL LEU GLU ALA THR GLY LEU
SEQRES   3 B  438  GLN LEU PRO LEU GLY ALA THR CYS ILE ILE GLU ARG GLN
SEQRES   4 B  438  ASP GLY PRO GLU THR LYS GLU VAL GLU SER GLU VAL VAL
SEQRES   5 B  438  GLY PHE ASN GLY GLN ARG LEU PHE LEU MET PRO LEU GLU
SEQRES   6 B  438  GLU VAL GLU GLY ILE LEU PRO GLY ALA ARG VAL TYR ALA
SEQRES   7 B  438  ARG ASN GLY HIS GLY ASP GLY LEU GLN SER GLY LYS GLN
SEQRES   8 B  438  LEU PRO LEU GLY PRO ALA LEU LEU GLY ARG VAL LEU ASP
SEQRES   9 B  438  GLY GLY GLY LYS PRO LEU ASP GLY LEU PRO ALA PRO ASP
SEQRES  10 B  438  THR LEU GLU THR GLY ALA LEU ILE THR PRO PRO PHE ASN
SEQRES  11 B  438  PRO LEU GLN ARG THR PRO ILE GLU HIS VAL LEU ASP THR
SEQRES  12 B  438  GLY VAL ARG ALA ILE ASN ALA LEU LEU THR VAL GLY ARG
SEQRES  13 B  438  GLY GLN ARG MET GLY LEU PHE ALA GLY SER GLY VAL GLY
SEQRES  14 B  438  LYS SER VAL LEU LEU GLY MET MET ALA ARG TYR THR ARG
SEQRES  15 B  438  ALA ASP VAL ILE VAL VAL GLY LEU ILE GLY GLU ARG GLY
SEQRES  16 B  438  ARG GLU VAL LYS ASP PHE ILE GLU ASN ILE LEU GLY PRO
SEQRES  17 B  438  ASP GLY ARG ALA ARG SER VAL VAL ILE ALA ALA PRO ALA
SEQRES  18 B  438  ASP VAL SER PRO LEU LEU ARG MET GLN GLY ALA ALA TYR
SEQRES  19 B  438  ALA THR ARG ILE ALA GLU ASP PHE ARG ASP ARG GLY GLN
SEQRES  20 B  438  HIS VAL LEU LEU ILE MET ASP SER LEU THR ARG TYR ALA
SEQRES  21 B  438  MET ALA GLN ARG GLU ILE ALA LEU ALA ILE GLY GLU PRO
SEQRES  22 B  438  PRO ALA THR LYS GLY TYR PRO PRO SER VAL PHE ALA LYS
SEQRES  23 B  438  LEU PRO ALA LEU VAL GLU ARG ALA GLY ASN GLY ILE HIS
SEQRES  24 B  438  GLY GLY GLY SER ILE THR ALA PHE TYR THR VAL LEU THR
SEQRES  25 B  438  GLU GLY ASP ASP GLN GLN ASP PRO ILE ALA ASP SER ALA
SEQRES  26 B  438  ARG ALA ILE LEU ASP GLY HIS ILE VAL LEU SER ARG ARG
SEQRES  27 B  438  LEU ALA GLU ALA GLY HIS TYR PRO ALA ILE ASP ILE GLU
SEQRES  28 B  438  ALA SER ILE SER ARG ALA MET THR ALA LEU ILE THR GLU
SEQRES  29 B  438  GLN HIS TYR ALA ARG VAL ARG LEU PHE LYS GLN LEU LEU
SEQRES  30 B  438  SER SER PHE GLN ARG ASN ARG ASP LEU VAL SER VAL GLY
SEQRES  31 B  438  ALA TYR ALA LYS GLY SER ASP PRO MET LEU ASP LYS ALA
SEQRES  32 B  438  ILE THR LEU TRP PRO GLN LEU GLU ALA PHE LEU GLN GLN
SEQRES  33 B  438  GLY ILE PHE GLU ARG ALA ASP TRP GLU ASP SER LEU GLN
SEQRES  34 B  438  ALA LEU ASP LEU ILE PHE PRO THR VAL
HET    ADP  B 600      27
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL   3  ADP    C10 H15 N5 O10 P2
FORMUL   4  HOH   *133(H2 O)
HELIX    1   1 GLY A  113  LEU A  117  5                                   5
HELIX    2   2 VAL A  163  LEU A  170  1                                   8
HELIX    3   3 GLY A  187  THR A  199  1                                  13
HELIX    4   4 ARG A  212  ASN A  222  1                                  11
HELIX    5   5 LEU A  224  ARG A  231  1                                   8
HELIX    6   6 SER A  242  ASP A  262  1                                  21
HELIX    7   7 SER A  273  ILE A  288  1                                  16
HELIX    8   8 SER A  300  GLU A  310  1                                  11
HELIX    9   9 ASP A  337  LEU A  347  1                                  11
HELIX   10  10 SER A  354  ALA A  360  1                                   7
HELIX   11  11 ALA A  375  ILE A  380  1                                   6
HELIX   12  12 THR A  381  ASN A  401  1                                  21
HELIX   13  13 ARG A  402  LEU A  404  5                                   3
HELIX   14  14 ASP A  415  THR A  423  1                                   9
HELIX   15  15 LEU A  424  GLN A  433  1                                  10
HELIX   16  16 ASP A  441  PHE A  453  1                                  13
HELIX   17  17 GLY B  113  LEU B  117  5                                   5
HELIX   18  18 VAL B  163  LEU B  170  1                                   8
HELIX   19  19 GLY B  187  THR B  199  1                                  13
HELIX   20  20 ARG B  212  ILE B  223  1                                  12
HELIX   21  21 LEU B  224  ARG B  231  1                                   8
HELIX   22  22 SER B  242  ARG B  263  1                                  22
HELIX   23  23 SER B  273  ILE B  288  1                                  16
HELIX   24  24 PRO B  298  GLU B  310  1                                  13
HELIX   25  25 ASP B  337  LEU B  347  1                                  11
HELIX   26  26 SER B  354  ALA B  360  1                                   7
HELIX   27  27 ALA B  375  ILE B  380  1                                   6
HELIX   28  28 THR B  381  VAL B  407  1                                  27
HELIX   29  29 ASP B  415  GLN B  433  1                                  19
HELIX   30  30 ASP B  441  PHE B  453  1                                  13
SHEET    1   A 7 GLY A  29  ARG A  33  0
SHEET    2   A 7 LEU A  39  THR A  42 -1  O  THR A  42   N  ARG A  30
SHEET    3   A 7 LEU A  77  PRO A  81 -1  O  LEU A  79   N  LEU A  39
SHEET    4   A 7 LYS A  63  GLY A  71 -1  N  GLY A  71   O  PHE A  78
SHEET    5   A 7 THR A  51  ARG A  56 -1  N  ILE A  54   O  VAL A  65
SHEET    6   A 7 ALA A  92  ALA A  96 -1  O  TYR A  95   N  ILE A  53
SHEET    7   A 7 GLY A  29  ARG A  33 -1  N  LEU A  31   O  ALA A  92
SHEET    1   B 2 GLN A 109  PRO A 111  0
SHEET    2   B 2 THR A 139  ALA A 141 -1  O  GLY A 140   N  LEU A 110
SHEET    1   C 8 ARG A 119  LEU A 121  0
SHEET    2   C 8 SER A 232  ALA A 237  1  O  ALA A 236   N  LEU A 121
SHEET    3   C 8 VAL A 203  ILE A 209  1  N  VAL A 206   O  VAL A 233
SHEET    4   C 8 HIS A 266  ASP A 272  1  O  ILE A 270   N  GLY A 207
SHEET    5   C 8 SER A 321  LEU A 329  1  O  THR A 323   N  LEU A 269
SHEET    6   C 8 ARG A 177  ALA A 182  1  N  MET A 178   O  ALA A 324
SHEET    7   C 8 GLY A 349  LEU A 353  1  O  LEU A 353   N  PHE A 181
SHEET    8   C 8 ILE A 366  SER A 373 -1  O  ILE A 372   N  HIS A 350
SHEET    1   D 7 THR B  62  GLU B  66  0
SHEET    2   D 7 ILE B  53  GLN B  57 -1  N  ARG B  56   O  LYS B  63
SHEET    3   D 7 ARG B  93  TYR B  95 -1  O  ARG B  93   N  GLU B  55
SHEET    4   D 7 TYR B  28  ARG B  33 -1  N  GLY B  29   O  VAL B  94
SHEET    5   D 7 LEU B  39  THR B  42 -1  O  GLU B  40   N  THR B  32
SHEET    6   D 7 LEU B  77  LEU B  79 -1  O  LEU B  79   N  LEU B  39
SHEET    7   D 7 VAL B  69  PHE B  72 -1  N  GLY B  71   O  PHE B  78
SHEET    1   E 2 GLN B 109  PRO B 111  0
SHEET    2   E 2 THR B 139  ALA B 141 -1  O  GLY B 140   N  LEU B 110
SHEET    1   F 6 VAL B 120  LEU B 121  0
SHEET    2   F 6 SER B 232  ALA B 237  1  O  ALA B 236   N  LEU B 121
SHEET    3   F 6 VAL B 203  ILE B 209  1  N  LEU B 208   O  ILE B 235
SHEET    4   F 6 HIS B 266  ASP B 272  1  O  ILE B 270   N  GLY B 207
SHEET    5   F 6 SER B 321  LEU B 329  1  O  THR B 323   N  LEU B 269
SHEET    6   F 6 GLY B 313  ASN B 314 -1  N  GLY B 313   O  ILE B 322
SHEET    1   G 8 VAL B 120  LEU B 121  0
SHEET    2   G 8 SER B 232  ALA B 237  1  O  ALA B 236   N  LEU B 121
SHEET    3   G 8 VAL B 203  ILE B 209  1  N  LEU B 208   O  ILE B 235
SHEET    4   G 8 HIS B 266  ASP B 272  1  O  ILE B 270   N  GLY B 207
SHEET    5   G 8 SER B 321  LEU B 329  1  O  THR B 323   N  LEU B 269
SHEET    6   G 8 ARG B 177  ALA B 182  1  N  MET B 178   O  ALA B 324
SHEET    7   G 8 GLY B 349  LEU B 353  1  O  LEU B 353   N  PHE B 181
SHEET    8   G 8 ILE B 366  SER B 373 -1  O  ASP B 367   N  VAL B 352
CISPEP   1 TYR A  363    PRO A  364          0        -3.74
CISPEP   2 TYR B  363    PRO B  364          0        -3.18
SITE     1 AC1  9 GLY B 185  GLY B 187  LYS B 188  SER B 189
SITE     2 AC1  9 VAL B 190  MET B 194  TYR B 363  ILE B 436
SITE     3 AC1  9 HOH B 642
CRYST1   48.160   72.750  125.740  90.00  94.13  90.00 P 1 21 1      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      0.020764  0.000000  0.001499        0.00000
SCALE2      0.000000  0.013746  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007974        0.00000
      
PROCHECK
Go to PROCHECK summary
 References