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PDBsum entry 2dq8

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Hydrolase PDB id
2dq8
Jmol
Contents
Protein chain
286 a.a.
HEADER    HYDROLASE                               23-MAY-06   2DQ8
TITLE     PROTEIN MODEL FOR NEURAMINIDASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 82-367;
COMPND   5 EC: 3.2.1.18
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_COMMON: VIRUS;
SOURCE   4 OTHER_DETAILS: PHEASANT
KEYWDS    CPH
EXPDTA    THEORETICAL MODEL
AUTHOR    S.PRADEEP,M.SONIASAREE
REVDAT   1   13-JUN-06 2DQ8    0
JRNL        AUTH   S.PRADEEP,M.SONIASAREE
JRNL        TITL   PROTEIN MODEL FOR NEURAMINIDASE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.C.PEITSCH
REMARK   1  TITL   PROMOD AND SWISS-MODEL: INTERNET-BASED TOOLS FOR
REMARK   1  TITL 2 AUTOMATED COMPARATIVE PROTEIN MODELLING
REMARK   1  REF    BIOCHEM.SOC.TRANS.            V.  24   274 1996
REMARK   1  REFN   ASTM BCSTB5  UK ISSN 0300-5127
REMARK   1 REFERENCE 2
REMARK   1  AUTH   N.GUEX,M.C.PEITSCH
REMARK   1  TITL   SWISS-MODEL AND THE SWISS-PDBVIEWER: AN
REMARK   1  TITL 2 ENVIRONMENT FOR COMPARATIVE PROTEIN MODELING
REMARK   1  REF    ELECTROPHORESIS               V.  18  2714 1997
REMARK   1  REFN                GE ISSN 0173-0835
REMARK   1 REFERENCE 3
REMARK   1  AUTH   T.SCHWEDE,J.KOPP,N.GUEX,M.C.PEITSCH
REMARK   1  TITL   SWISS-MODEL: AN AUTOMATED PROTEIN
REMARK   1  TITL 2 HOMOLOGY-MODELING SERVER
REMARK   1  REF    NUCLEIC ACIDS RES.            V.  31  3381 2003
REMARK   1  REFN   ASTM NARHAD  UK ISSN 0305-1048
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : NULL
REMARK   3   AUTHORS     : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HOMOLOGY MODELLING
REMARK   4
REMARK   4 2DQ8 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-2006.
REMARK 100 THE RCSB ID CODE IS RCSB025713.
REMARK 220
REMARK 220 EXPERIMENTAL DETAILS
REMARK 220  EXPERIMENT TYPE                : THEORETICAL MODELLING
REMARK 220
REMARK 220 REMARK: NULL
REMARK 225
REMARK 225 THEORETICAL MODEL
REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE.
REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND
REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE
REMARK 225 RECORDS ARE MEANINGLESS.
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    PHE A 239   CE1   PHE A 239   CZ    -0.203
REMARK 500    ILE A 255   CA    ILE A 255   C      0.096
REMARK 500    ILE A 255   C     ILE A 255   O     -0.188
REMARK 500    PHE A 306   CD1   PHE A 306   CE1    0.110
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 118   C   -  N   -  CA  ANGL. DEV. = 16.4 DEGREES
REMARK 500    ILE A 255   CA  -  CB  -  CG2 ANGL. DEV. =-40.6 DEGREES
REMARK 500    ILE A 255   CA  -  C   -  N   ANGL. DEV. =-16.8 DEGREES
REMARK 500    ASP A 324   N   -  CA  -  CB  ANGL. DEV. =-18.2 DEGREES
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  M RES CSSEQI        PSI       PHI
REMARK 500    VAL A 357     -117.65     69.35
DBREF  2DQ8 A   82   367  UNP    Q807U4   Q807U4_9INFA    82    367
SEQRES   1 A  286  SER VAL THR LEU ALA GLY ASN SER SER LEU CYS PRO ILE
SEQRES   2 A  286  SER GLY TRP ALA VAL TYR SER LYS ASP ASN GLY ILE ARG
SEQRES   3 A  286  ILE GLY SER LYS GLY ASP VAL PHE VAL ILE ARG GLU PRO
SEQRES   4 A  286  PHE ILE SER CYS SER HIS LEU GLU CYS ARG THR PHE PHE
SEQRES   5 A  286  LEU THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN
SEQRES   6 A  286  GLY THR VAL LYS ASP ARG SER PRO TYR ARG THR LEU MET
SEQRES   7 A  286  SER CYS PRO VAL GLY GLU ALA PRO SER PRO TYR ASN SER
SEQRES   8 A  286  ARG PHE GLU SER VAL ALA TRP SER ALA SER ALA CYS HIS
SEQRES   9 A  286  ASP GLY THR SER TRP LEU THR ILE GLY ILE SER GLY PRO
SEQRES  10 A  286  ASP ASN GLY ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE
SEQRES  11 A  286  ILE THR ASP THR ILE LYS SER TRP ARG ASN ASN ILE LEU
SEQRES  12 A  286  ARG THR GLN GLU SER GLU CYS ALA CYS VAL ASN GLY SER
SEQRES  13 A  286  CYS PHE THR VAL MET THR ASP GLY PRO SER ASN GLY GLN
SEQRES  14 A  286  ALA SER TYR LYS ILE PHE LYS ILE GLU LYS GLY LYS VAL
SEQRES  15 A  286  VAL LYS SER VAL GLU LEU ASN ALA PRO ASN TYR HIS TYR
SEQRES  16 A  286  GLU GLU CYS SER CYS TYR PRO ASP ALA GLY GLU ILE THR
SEQRES  17 A  286  CYS VAL CYS ARG ASP ASN TRP HIS GLY SER ASN ARG PRO
SEQRES  18 A  286  TRP VAL SER PHE ASN GLN ASN LEU GLU TYR GLN ILE GLY
SEQRES  19 A  286  TYR ILE CYS SER GLY VAL PHE GLY ASP ASN PRO ARG PRO
SEQRES  20 A  286  ASN ASP GLY THR GLY SER CYS GLY PRO VAL SER PRO ASN
SEQRES  21 A  286  GLY ALA TYR GLY ILE LYS GLY PHE SER PHE LYS TYR GLY
SEQRES  22 A  286  ASN GLY VAL TRP ILE GLY ARG THR LYS SER THR ASN SER
HELIX    1   1 ASN A  104  SER A  110  1                                   7
HELIX    2   2 ASP A  142  ASN A  146  5                                   5
SHEET    1   A 4 PHE A 121  SER A 125  0
SHEET    2   A 4 GLU A 128  LEU A 134 -1  O  GLU A 128   N  SER A 125
SHEET    3   A 4 THR A 157  PRO A 162 -1  O  CYS A 161   N  THR A 131
SHEET    4   A 4 ARG A 173  VAL A 177 -1  O  GLU A 175   N  LEU A 158
SHEET    1   B 4 ALA A 181  HIS A 185  0
SHEET    2   B 4 TRP A 190  SER A 196 -1  O  LEU A 191   N  CYS A 184
SHEET    3   B 4 VAL A 203  TYR A 208 -1  O  LYS A 207   N  THR A 192
SHEET    4   B 4 ILE A 212  LYS A 217 -1  O  ASP A 214   N  LEU A 206
SHEET    1   C 4 ALA A 232  VAL A 234  0
SHEET    2   C 4 SER A 237  ASP A 244 -1  O  SER A 237   N  VAL A 234
SHEET    3   C 4 SER A 252  GLU A 259 -1  O  SER A 252   N  ASP A 244
SHEET    4   C 4 LYS A 262  LYS A 265 -1  O  VAL A 264   N  LYS A 257
SHEET    1   D 4 SER A 280  ASP A 284  0
SHEET    2   D 4 GLU A 287  VAL A 291 -1  O  THR A 289   N  TYR A 282
SHEET    3   D 4 PRO A 302  ASN A 307 -1  O  PHE A 306   N  ILE A 288
SHEET    4   D 4 TYR A 312  ILE A 317 -1  O  TYR A 312   N  ASN A 307
SHEET    1   E 2 LYS A 352  GLY A 354  0
SHEET    2   E 2 ARG A 361  LYS A 363 -1  O  ARG A 361   N  GLY A 354
SSBOND   1 CYS A  124    CYS A  129
SSBOND   2 CYS A  184    CYS A  231
SSBOND   3 CYS A  233    CYS A  238
SSBOND   4 CYS A  279    CYS A  292
SSBOND   5 CYS A  281    CYS A  290
CISPEP   1 PRO A  326    ARG A  327          0        -6.06
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1
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      1.000000  0.000000  0.000000        0.00000
SCALE2      0.000000  1.000000  0.000000        0.00000
SCALE3      0.000000  0.000000  1.000000        0.00000
      
PROCHECK
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