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PDBsum entry 2sim

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Hydrolase PDB id
2sim
Jmol
Contents
Protein chain
381 a.a.
Ligands
DAN
Waters ×242
HEADER    HYDROLASE                               15-JUL-94   2SIM
TITLE     THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 NEURAMINIDASE
TITLE    2 AND ITS COMPLEX WITH A TRANSITION STATE ANALOGUE AT 1.6
TITLE    3 ANGSTROMS RESOLUTION
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: 602;
SOURCE   4 GENE: PSX62;
SOURCE   5 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PSX62
KEYWDS    HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.L.TAYLOR,S.J.CRENNELL,E.F.GARMAN,E.R.VIMR,W.G.LAVER
REVDAT   2   24-FEB-09 2SIM    1       VERSN
REVDAT   1   30-NOV-94 2SIM    0
SPRSDE     30-NOV-94 2SIM      1SIM
JRNL        AUTH   S.J.CRENNELL,E.F.GARMAN,C.PHILIPPON,A.VASELLA,
JRNL        AUTH 2 W.G.LAVER,E.R.VIMR,G.L.TAYLOR
JRNL        TITL   THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2
JRNL        TITL 2 NEURAMINIDASE AND ITS COMPLEXES WITH THREE
JRNL        TITL 3 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,
REMARK   1  AUTH 2 G.L.TAYLOR
REMARK   1  TITL   CRYSTAL STRUCTURE OF A BACTERIAL SIALIDASE (FROM
REMARK   1  TITL 2 SALMONELLA TYPHIMURIUM LT2) SHOWS THE SAME FOLD AS
REMARK   1  TITL 3 AN INFLUENZA VIRUS 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.L.TAYLOR,E.R.VIMR,E.F.GARMAN,W.G.LAVER
REMARK   1  TITL   PURIFICATION, CRYSTALLISATION AND PRELIMINARY
REMARK   1  TITL 2 CRYSTALLOGRAPHIC STUDY OF NEURAMINIDASE FROM
REMARK   1  TITL 3 VIBRIO CHOLERAE AND SALMONELLA TYPHIMURIUM
REMARK   1  REF    J.MOL.BIOL.                   V. 226  1287 1992
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS
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   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 41098
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185
REMARK   3   R VALUE            (WORKING SET) : NULL
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
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 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          : 20
REMARK   3   SOLVENT ATOMS            : 242
REMARK   3
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT
REMARK   3   BOND LENGTHS                 (A) : 0.016 ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : 3.080 ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : NULL
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2SIM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
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        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
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 : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 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) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
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       23.80000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.95000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.25000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.95000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.80000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.25000
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 LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    HIS A  57   NE2   HIS A  57   CD2    -0.088
REMARK 500    HIS A 162   NE2   HIS A 162   CD2    -0.068
REMARK 500    HIS A 297   NE2   HIS A 297   CD2    -0.079
REMARK 500    HIS A 317   NE2   HIS A 317   CD2    -0.069
REMARK 500    HIS A 374   NE2   HIS A 374   CD2    -0.069
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A  37   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES
REMARK 500    ARG A  37   NE  -  CZ  -  NH1 ANGL. DEV. =  10.3 DEGREES
REMARK 500    ARG A  37   NE  -  CZ  -  NH2 ANGL. DEV. = -10.7 DEGREES
REMARK 500    ARG A  72   NE  -  CZ  -  NH1 ANGL. DEV. =   9.2 DEGREES
REMARK 500    ARG A  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.0 DEGREES
REMARK 500    TRP A  80   CD1 -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES
REMARK 500    TRP A  80   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES
REMARK 500    ARG A  90   CG  -  CD  -  NE  ANGL. DEV. = -18.5 DEGREES
REMARK 500    ARG A  90   NE  -  CZ  -  NH1 ANGL. DEV. =  14.7 DEGREES
REMARK 500    ARG A  90   NE  -  CZ  -  NH2 ANGL. DEV. = -12.9 DEGREES
REMARK 500    ARG A 111   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ARG A 111   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    TRP A 121   CD1 -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    TRP A 121   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES
REMARK 500    TRP A 128   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP A 128   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES
REMARK 500    TRP A 140   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    THR A 159   N   -  CA  -  CB  ANGL. DEV. = -17.3 DEGREES
REMARK 500    LEU A 182   CA  -  CB  -  CG  ANGL. DEV. =  18.3 DEGREES
REMARK 500    TRP A 218   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP A 218   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES
REMARK 500    ARG A 251   CD  -  NE  -  CZ  ANGL. DEV. =  11.2 DEGREES
REMARK 500    ARG A 251   NE  -  CZ  -  NH1 ANGL. DEV. =  13.5 DEGREES
REMARK 500    ARG A 251   NE  -  CZ  -  NH2 ANGL. DEV. = -14.9 DEGREES
REMARK 500    TRP A 263   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP A 263   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    VAL A 280   CB  -  CA  -  C   ANGL. DEV. = -15.5 DEGREES
REMARK 500    VAL A 280   CG1 -  CB  -  CG2 ANGL. DEV. =  10.2 DEGREES
REMARK 500    TYR A 331   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    TYR A 347   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A 348   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    VAL A 358   CB  -  CA  -  C   ANGL. DEV. = -17.5 DEGREES
REMARK 500    VAL A 358   N   -  CA  -  CB  ANGL. DEV. =  13.9 DEGREES
REMARK 500    VAL A 358   CG1 -  CB  -  CG2 ANGL. DEV. =  10.6 DEGREES
REMARK 500    VAL A 359   CG1 -  CB  -  CG2 ANGL. DEV. =  12.5 DEGREES
REMARK 500    ARG A 373   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG A 373   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 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    ILE A  38       70.26     58.98
REMARK 500    ASP A 100       69.40     63.47
REMARK 500    VAL A 178      127.90     82.53
REMARK 500    SER A 208     -155.46   -166.86
REMARK 500    PHE A 228     -122.58     48.64
REMARK 500    SER A 230      -28.58     43.61
REMARK 500    ALA A 239       38.84     36.05
REMARK 500    ARG A 276     -152.36     59.48
REMARK 500    HIS A 278      -30.61     74.93
REMARK 500    ASP A 306     -158.93   -160.77
REMARK 500    VAL A 351     -101.84     55.29
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 ALA A  239     SER A  240                  143.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A  90         0.11    SIDE_CHAIN
REMARK 500    ARG A 251         0.10    SIDE_CHAIN
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 580        DISTANCE =  7.13 ANGSTROMS
REMARK 525    HOH A 621        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH A 640        DISTANCE =  5.05 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 RESIDUE DAN IS THE INHIBITOR, 2,3-DEHYDRO-2-DEOXY-N-ACETYL
REMARK 600 NEURAMINIC ACID.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A 800
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 SEQUENCE ADVISORY NOTICE
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.
REMARK 999
REMARK 999      SWISS-PROT ENTRY NAME: NANH_SALTY
REMARK 999
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES
REMARK 999
REMARK 999        NAME   NUMBER         NAME   CHAIN  SEQ/INSERT CODE
REMARK 999        ALA      328          ASP            329
DBREF  2SIM A    2   382  UNP    P29768   NANH_SALTY       1    381
SEQADV 2SIM 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    DAN  A 800      20
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
FORMUL   2  DAN    C11 H17 N O8
FORMUL   3  HOH   *242(H2 O)
HELIX    1   1 SER A   29  GLY A   31  5                                   3
HELIX    2   2 THR A  127  TYR A  131  5                                   5
HELIX    3   3 ASN A  160  GLY A  169  1                                  10
HELIX    4   4 HIS A  374  SER A  380  1                                   7
SHEET    1   A 4 LYS A   5  PHE A   9  0
SHEET    2   A 4 SER A 365  ASP A 370 -1  O  ILE A 366   N  VAL A   8
SHEET    3   A 4 LYS A 353  ALA A 362 -1  O  VAL A 358   N  GLN A 369
SHEET    4   A 4 SER A 343  ASN A 350 -1  N  CYS A 344   O  VAL A 359
SHEET    1   B 2 PHE A  16  THR A  17  0
SHEET    2   B 2 THR A  23  ILE A  24 -1  N  ILE A  24   O  PHE A  16
SHEET    1   C 4 TYR A  35  THR A  43  0
SHEET    2   C 4 ILE A  49  ARG A  56 -1  N  VAL A  50   O  CYS A  42
SHEET    3   C 4 ILE A  66  SER A  73 -1  O  ASP A  67   N  ALA A  55
SHEET    4   C 4 ASN A  81  ILE A  86 -1  N  ASN A  81   O  ARG A  72
SHEET    1   D 5 SER A 155  LYS A 156  0
SHEET    2   D 5 ASP A 141  SER A 147 -1  N  LYS A 146   O  SER A 155
SHEET    3   D 5 ARG A 111  TRP A 121 -1  N  ILE A 114   O  SER A 147
SHEET    4   D 5 ARG A  97  ILE A 108 -1  N  ARG A  97   O  TRP A 121
SHEET    5   D 5 GLY A 179  SER A 180  1  O  GLY A 179   N  CYS A 103
SHEET    1   E 4 CYS A 225  GLU A 226  0
SHEET    2   E 4 LEU A 205  SER A 212 -1  O  THR A 207   N  CYS A 225
SHEET    3   E 4 LEU A 189  ARG A 197 -1  N  LEU A 189   O  SER A 212
SHEET    4   E 4 ILE A 171  GLY A 176 -1  N  SER A 172   O  VAL A 196
SHEET    1   F 4 CYS A 225  GLU A 226  0
SHEET    2   F 4 LEU A 205  SER A 212 -1  O  THR A 207   N  CYS A 225
SHEET    3   F 4 LEU A 189  ARG A 197 -1  N  LEU A 189   O  SER A 212
SHEET    4   F 4 LEU A 182  GLN A 183 -1  O  LEU A 182   N  VAL A 190
SHEET    1   G 4 ASN A 232  PHE A 237  0
SHEET    2   G 4 SER A 240  ILE A 245 -1  O  SER A 240   N  PHE A 237
SHEET    3   G 4 PHE A 254  THR A 256 -1  O  PHE A 254   N  ASN A 243
SHEET    4   G 4 THR A 264  GLU A 265 -1  O  THR A 264   N  GLU A 255
SHEET    1   H 4 SER A 283  SER A 289  0
SHEET    2   H 4 LYS A 292  ALA A 300 -1  O  LYS A 292   N  SER A 289
SHEET    3   H 4 ILE A 312  HIS A 317 -1  N  SER A 313   O  SER A 299
SHEET    4   H 4 VAL A 324  TYR A 331 -1  O  LYS A 325   N  ALA A 316
SSBOND   1 CYS A   42    CYS A  103                          1555   1555  2.06
CISPEP   1 ALA A  135    PRO A  136          0        -6.67
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 19 ARG A  37  ILE A  38  ARG A  56  ASP A  62
SITE     2 AC1 19 MET A  99  ASP A 100  THR A 127  TRP A 128
SITE     3 AC1 19 ARG A 246  ARG A 309  TYR A 342  HOH A 664
SITE     4 AC1 19 HOH A 688  HOH A 689  HOH A 690  HOH A 692
SITE     5 AC1 19 HOH A 694  HOH A 695  HOH A 696
CRYST1   47.600   82.500   91.900  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      0.021008  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012121  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010881        0.00000
      
PROCHECK
Go to PROCHECK summary
 References