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PDBsum entry 1dim

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Glycosidase PDB id
1dim
Jmol
Contents
Protein chain
381 a.a.
Ligands
EQP
Metals
__K
Waters ×219
HEADER    GLYCOSIDASE                             23-APR-96   1DIM
TITLE     SIALIDASE FROM SALMONELLA TYPHIMURIUM COMPLEXED WITH EPANA INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.18;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE   3 ORGANISM_TAXID: 99287;
SOURCE   4 STRAIN: LT2;
SOURCE   5 VARIANT: TA263, PROTOTROPH;
SOURCE   6 GENE: NANH;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PSX62;
SOURCE  11 EXPRESSION_SYSTEM_GENE: NANH;
SOURCE  12 OTHER_DETAILS: RESIDUE MET 1 WAS EXCISED BY ESCHERICHIA COLI
KEYWDS    GLYCOSIDASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.F.GARMAN,S.C.CRENNELL,E.R.VIMR,W.G.LAVER,G.L.TAYLOR
REVDAT   3   13-JUL-11 1DIM    1       VERSN
REVDAT   2   24-FEB-09 1DIM    1       VERSN
REVDAT   1   07-DEC-96 1DIM    0
JRNL        AUTH   S.J.CRENNELL,E.F.GARMAN,C.PHILIPPON,A.VASELLA,W.G.LAVER,
JRNL        AUTH 2 E.R.VIMR,G.L.TAYLOR
JRNL        TITL   THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 NEURAMINIDASE
JRNL        TITL 2 AND ITS COMPLEXES WITH THREE INHIBITORS AT HIGH RESOLUTION.
JRNL        REF    J.MOL.BIOL.                   V. 259   264 1996
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   8656428
JRNL        DOI    10.1006/JMBI.1996.0318
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.J.CRENNELL,E.F.GARMAN,W.G.LAVER,E.R.VIMR,G.L.TAYLOR
REMARK   1  TITL   CRYSTAL STRUCTURE OF A BACTERIAL SIALIDASE (FROM SALMONELLA
REMARK   1  TITL 2 TYPHIMURIUM LT2) SHOWS THE SAME FOLD AS AN INFLUENZA VIRUS
REMARK   1  TITL 3 NEURAMINIDASE
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  90  9852 1993
REMARK   1  REFN                   ISSN 0027-8424
REMARK   1 REFERENCE 2
REMARK   1  AUTH   G.TAYLOR,E.VIMR,E.GARMAN,G.LAVER
REMARK   1  TITL   PURIFICATION, CRYSTALLIZATION AND PRELIMINARY
REMARK   1  TITL 2 CRYSTALLOGRAPHIC STUDY OF NEURAMINIDASE FROM VIBRIO CHOLERAE
REMARK   1  TITL 3 AND SALMONELLA TYPHIMURIUM LT2
REMARK   1  REF    J.MOL.BIOL.                   V. 226  1287 1992
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 3
REMARK   1  AUTH   K.WALLIMANN,A.VASELLA
REMARK   1  TITL   PHOSPHONIC-ACID ANALOGUES OF THE N-ACETYL-2-DEOXYNEURAMINIC
REMARK   1  TITL 2 ACIDS: SYNTHESIS AND INHIBITION OF VIBRIO CHOLERAE SIALIDASE
REMARK   1  REF    HELV.CHIM.ACTA                V.  73  1359 1990
REMARK   1  REFN                   ISSN 0018-019X
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 42613
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.180
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
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            : 2954
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 22
REMARK   3   SOLVENT ATOMS            : 219
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.42
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.79
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500
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  : STNA_EPANA.PAR
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : STNA_EPANA.TOP
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1DIM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-92
REMARK 200  TEMPERATURE           (KELVIN) : 289
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12091
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.6
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : 0.05400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.07800
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE MAP
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 2SIM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       23.70000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.85000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.15000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.85000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.70000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.15000
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 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 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    ARG A  37   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A  37   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    ARG A  90   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A  90   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A 251   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A 251   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    VAL A 280   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES
REMARK 500    VAL A 358   CB  -  CA  -  C   ANGL. DEV. = -14.7 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    ASP A 100       69.87     60.41
REMARK 500    ASN A 122      -50.18   -131.46
REMARK 500    VAL A 178      126.10     83.33
REMARK 500    SER A 208     -151.79   -169.10
REMARK 500    PHE A 228     -128.56     53.07
REMARK 500    SER A 230      -36.58     52.10
REMARK 500    ASN A 238     -126.21     63.56
REMARK 500    ARG A 276     -158.48     59.07
REMARK 500    HIS A 278      -26.39     72.74
REMARK 500    ARG A 309       60.79     38.57
REMARK 500    VAL A 351     -103.80     54.66
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    SER A 230        23.4      L          L   OUTSIDE RANGE
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 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 801        DISTANCE =  6.93 ANGSTROMS
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                               K A 690   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  62   OD2
REMARK 620 2 EQP A   1   O2P  89.0
REMARK 620 3 EQP A   1   O6   86.2  61.5
REMARK 620 4 EQP A   1   O7   79.4 121.8  61.0
REMARK 620 5 HOH A 691   O    52.2 141.2 111.5  59.8
REMARK 620 6 HOH A 692   O   154.9  66.6  76.9 107.5 152.1
REMARK 620 7 HOH A 697   O   112.4 156.1 127.8  74.6  60.7  92.7
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 690
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EQP A 1
DBREF  1DIM A    2   382  UNP    P29768   NANH_SALTY       1    381
SEQADV 1DIM ASP A  329  UNP  P29768    ALA   328 CONFLICT
SEQRES   1 A  381  THR VAL GLU LYS SER VAL VAL PHE LYS ALA GLU GLY GLU
SEQRES   2 A  381  HIS PHE THR ASP GLN LYS GLY ASN THR ILE VAL GLY SER
SEQRES   3 A  381  GLY SER GLY GLY THR THR LYS TYR PHE ARG ILE PRO ALA
SEQRES   4 A  381  MET CYS THR THR SER LYS GLY THR ILE VAL VAL PHE ALA
SEQRES   5 A  381  ASP ALA ARG HIS ASN THR ALA SER ASP GLN SER PHE ILE
SEQRES   6 A  381  ASP THR ALA ALA ALA ARG SER THR ASP GLY GLY LYS THR
SEQRES   7 A  381  TRP ASN LYS LYS ILE ALA ILE TYR ASN ASP ARG VAL ASN
SEQRES   8 A  381  SER LYS LEU SER ARG VAL MET ASP PRO THR CYS ILE VAL
SEQRES   9 A  381  ALA ASN ILE GLN GLY ARG GLU THR ILE LEU VAL MET VAL
SEQRES  10 A  381  GLY LYS TRP ASN ASN ASN ASP LYS THR TRP GLY ALA TYR
SEQRES  11 A  381  ARG ASP LYS ALA PRO ASP THR ASP TRP ASP LEU VAL LEU
SEQRES  12 A  381  TYR LYS SER THR ASP ASP GLY VAL THR PHE SER LYS VAL
SEQRES  13 A  381  GLU THR ASN ILE HIS ASP ILE VAL THR LYS ASN GLY THR
SEQRES  14 A  381  ILE SER ALA MET LEU GLY GLY VAL GLY SER GLY LEU GLN
SEQRES  15 A  381  LEU ASN ASP GLY LYS LEU VAL PHE PRO VAL GLN MET VAL
SEQRES  16 A  381  ARG THR LYS ASN ILE THR THR VAL LEU ASN THR SER PHE
SEQRES  17 A  381  ILE TYR SER THR ASP GLY ILE THR TRP SER LEU PRO SER
SEQRES  18 A  381  GLY TYR CYS GLU GLY PHE GLY SER GLU ASN ASN ILE ILE
SEQRES  19 A  381  GLU PHE ASN ALA SER LEU VAL ASN ASN ILE ARG ASN SER
SEQRES  20 A  381  GLY LEU ARG ARG SER PHE GLU THR LYS ASP PHE GLY LYS
SEQRES  21 A  381  THR TRP THR GLU PHE PRO PRO MET ASP LYS LYS VAL ASP
SEQRES  22 A  381  ASN ARG ASN HIS GLY VAL GLN GLY SER THR ILE THR ILE
SEQRES  23 A  381  PRO SER GLY ASN LYS LEU VAL ALA ALA HIS SER SER ALA
SEQRES  24 A  381  GLN ASN LYS ASN ASN ASP TYR THR ARG SER ASP ILE SER
SEQRES  25 A  381  LEU TYR ALA HIS ASN LEU TYR SER GLY GLU VAL LYS LEU
SEQRES  26 A  381  ILE ASP ASP PHE TYR PRO LYS VAL GLY ASN ALA SER GLY
SEQRES  27 A  381  ALA GLY TYR SER CYS LEU SER TYR ARG LYS ASN VAL ASP
SEQRES  28 A  381  LYS GLU THR LEU TYR VAL VAL TYR GLU ALA ASN GLY SER
SEQRES  29 A  381  ILE GLU PHE GLN ASP LEU SER ARG HIS LEU PRO VAL ILE
SEQRES  30 A  381  LYS SER TYR ASN
HET      K  A 690       1
HET    EQP  A   1      21
HETNAM       K POTASSIUM ION
HETNAM     EQP (4-ACETAMIDO-2,4-DIDEOXY-D-GLYCERO-ALPHA-D-GALACTO-1-
HETNAM   2 EQP  OCTOPYRANOSYL)PHOSPHONIC ACID
FORMUL   2    K    K 1+
FORMUL   3  EQP    C10 H20 N O9 P
FORMUL   4  HOH   *219(H2 O)
HELIX    1   1 SER A   29  GLY A   31  5                                   3
HELIX    2   2 TRP A  128  ALA A  130  5                                   3
HELIX    3   3 ILE A  161  ASN A  168  1                                   8
HELIX    4   4 SER A  372  SER A  380  5                                   9
SHEET    1   A 4 TYR A  35  ARG A  37  0
SHEET    2   A 4 ILE A  49  ARG A  56 -1  N  ARG A  56   O  TYR A  35
SHEET    3   A 4 ILE A  66  SER A  73 -1  N  SER A  73   O  ILE A  49
SHEET    4   A 4 ASN A  81  ILE A  86 -1  N  ILE A  86   O  THR A  68
SHEET    1   B 2 ALA A  40  THR A  43  0
SHEET    2   B 2 ILE A  49  PHE A  52 -1  N  PHE A  52   O  ALA A  40
SHEET    1   C 3 ARG A  97  MET A  99  0
SHEET    2   C 3 ILE A 114  TRP A 121 -1  N  TRP A 121   O  ARG A  97
SHEET    3   C 3 ASP A 141  SER A 147 -1  N  SER A 147   O  ILE A 114
SHEET    1   D 2 THR A 102  ILE A 108  0
SHEET    2   D 2 ARG A 111  MET A 117 -1  N  MET A 117   O  THR A 102
SHEET    1   E 4 TRP A 218  LEU A 220  0
SHEET    2   E 4 LEU A 205  SER A 212 -1  N  TYR A 211   O  SER A 219
SHEET    3   E 4 LEU A 189  ARG A 197 -1  N  MET A 195   O  ASN A 206
SHEET    4   E 4 ILE A 171  GLY A 176 -1  N  LEU A 175   O  GLN A 194
SHEET    1   F 2 ASN A 232  PHE A 237  0
SHEET    2   F 2 SER A 240  ILE A 245 -1  N  ASN A 244   O  ASN A 233
SHEET    1   G 4 SER A 283  SER A 289  0
SHEET    2   G 4 LYS A 292  ALA A 300 -1  N  SER A 298   O  SER A 283
SHEET    3   G 4 ILE A 312  HIS A 317 -1  N  HIS A 317   O  ALA A 295
SHEET    4   G 4 VAL A 324  ASP A 328 -1  N  ASP A 328   O  LEU A 314
SHEET    1   H 4 SER A 343  ASN A 350  0
SHEET    2   H 4 LYS A 353  ALA A 362 -1  N  VAL A 359   O  CYS A 344
SHEET    3   H 4 SER A 365  ASP A 370 -1  N  GLN A 369   O  VAL A 358
SHEET    4   H 4 LYS A   5  PHE A   9 -1  N  PHE A   9   O  ILE A 366
SSBOND   1 CYS A   42    CYS A  103                          1555   1555  2.05
LINK         K     K A 690                 OD2 ASP A  62     1555   1555  2.77
LINK         K     K A 690                 O2P EQP A   1     1555   1555  2.91
LINK         K     K A 690                 O6  EQP A   1     1555   1555  2.83
LINK         K     K A 690                 O7  EQP A   1     1555   1555  2.77
LINK         K     K A 690                 O   HOH A 691     1555   1555  3.38
LINK         K     K A 690                 O   HOH A 692     1555   1555  3.33
LINK         K     K A 690                 O   HOH A 697     1555   1555  2.90
CISPEP   1 ALA A  135    PRO A  136          0        -0.20
SITE     1 ACT 13 ARG A  37  ARG A  56  ASP A  62  MET A  99
SITE     2 ACT 13 ASP A 100  TRP A 121  TRP A 128  LEU A 175
SITE     3 ACT 13 GLU A 231  ARG A 246  ARG A 309  TYR A 342
SITE     4 ACT 13 GLU A 361
SITE     1 AC1  3 EQP A   1  ASP A  62  HOH A 697
SITE     1 AC2 20 ARG A  37  ILE A  38  ARG A  56  ASP A  62
SITE     2 AC2 20 ASP A 100  THR A 127  TRP A 128  LEU A 175
SITE     3 AC2 20 ARG A 246  ARG A 309  TYR A 342  HOH A 664
SITE     4 AC2 20 HOH A 688  HOH A 689    K A 690  HOH A 692
SITE     5 AC2 20 HOH A 693  HOH A 694  HOH A 695  HOH A 696
CRYST1   47.400   82.300   91.700  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      0.021097  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012151  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010905        0.00000
      
PROCHECK
Go to PROCHECK summary
 References