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PDBsum entry 2ht8

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Hydrolase PDB id
2ht8
Jmol
Contents
Protein chain
387 a.a.
Ligands
G39
Waters ×91
HEADER    HYDROLASE                               25-JUL-06   2HT8
TITLE     N8 NEURAMINIDASE IN COMPLEX WITH OSELTAMIVIR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.18
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_TAXID: 11320
KEYWDS    N8, NEURAMINIDASE, OSELTAMIVIR, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.J.RUSSELL,L.F.HAIRE,D.J.STEVENS,P.J.COLLINS,Y.P.LIN,G.M.BLACKBURN,
AUTHOR   2 A.J.HAY,S.J.GAMBLIN,J.J.SKEHEL
REVDAT   4   13-JUL-11 2HT8    1       VERSN
REVDAT   3   24-FEB-09 2HT8    1       VERSN
REVDAT   2   19-SEP-06 2HT8    1       JRNL
REVDAT   1   05-SEP-06 2HT8    0
JRNL        AUTH   R.J.RUSSELL,L.F.HAIRE,D.J.STEVENS,P.J.COLLINS,Y.P.LIN,
JRNL        AUTH 2 G.M.BLACKBURN,A.J.HAY,S.J.GAMBLIN,J.J.SKEHEL
JRNL        TITL   THE STRUCTURE OF H5N1 AVIAN INFLUENZA NEURAMINIDASE SUGGESTS
JRNL        TITL 2 NEW OPPORTUNITIES FOR DRUG DESIGN.
JRNL        REF    NATURE                        V. 443    45 2006
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   16915235
JRNL        DOI    10.1038/NATURE05114
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 : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
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             : 16124
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) : 0.252
REMARK   3   FREE R VALUE                     : 0.273
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 728
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            : 2998
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 20
REMARK   3   SOLVENT ATOMS            : 91
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 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) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
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  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 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  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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: WATERS PICKED AT LEVEL GREATER THAN 3
REMARK   4
REMARK   4 2HT8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-06.
REMARK 100 THE RCSB ID CODE IS RCSB038733.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16124
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.09600
REMARK 200   FOR THE DATA SET  : 7.6000
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) : 2.50
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.7
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: IMIDAZOLE, MPD, PH 8, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2
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        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  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       45.21500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.21500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       54.85500
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       45.21500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.21500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       54.85500
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       45.21500
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       45.21500
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       54.85500
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       45.21500
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       45.21500
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       54.85500
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 16280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 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 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  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     ASP A   469
REMARK 465     LYS A   470
REMARK 465     MET A   471
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    CYS A 337   CA  -  CB  -  SG  ANGL. DEV. =  10.2 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 117     -159.28   -140.71
REMARK 500    ARG A 118      165.82    171.59
REMARK 500    PRO A 126       35.00    -76.35
REMARK 500    ILE A 127      -26.23   -150.71
REMARK 500    ASN A 146     -118.21    -26.94
REMARK 500    THR A 148       18.22    -61.61
REMARK 500    ASP A 151      -71.73     80.41
REMARK 500    VAL A 163      160.86    -43.05
REMARK 500    GLU A 174      -81.78    -93.72
REMARK 500    SER A 179      115.61    179.19
REMARK 500    CYS A 183      144.99   -173.83
REMARK 500    LYS A 187      -72.90   -139.91
REMARK 500    LYS A 200       22.70   -156.32
REMARK 500    VAL A 210      138.94   -172.30
REMARK 500    ALA A 219       25.95   -142.51
REMARK 500    ILE A 222       89.56     53.81
REMARK 500    ASN A 247      -99.81    -87.11
REMARK 500    ARG A 248     -171.18    -59.94
REMARK 500    GLN A 249      162.68    -36.83
REMARK 500    ASN A 258       89.20   -154.01
REMARK 500    GLN A 259       66.24     80.65
REMARK 500    PHE A 270       55.75   -161.81
REMARK 500    GLU A 277       70.37     35.90
REMARK 500    ASP A 284       46.95     72.17
REMARK 500    CYS A 291     -159.50    -96.88
REMARK 500    TRP A 295      -91.06    -78.83
REMARK 500    LEU A 303      114.03   -162.34
REMARK 500    LEU A 310        3.71     59.95
REMARK 500    CYS A 318      -72.16    -45.74
REMARK 500    ALA A 319      132.08     -3.10
REMARK 500    GLN A 330B      33.39    -91.55
REMARK 500    TYR A 347     -142.83   -120.39
REMARK 500    ASN A 381       20.45     42.81
REMARK 500    THR A 386       32.14    -65.66
REMARK 500    LYS A 388       29.67   -144.13
REMARK 500    ASN A 400        6.96    -67.34
REMARK 500    SER A 404     -136.37   -109.44
REMARK 500    LEU A  12D     -52.15   -124.52
REMARK 500    LYS A 415     -172.70    -68.06
REMARK 500    VAL A 449      140.61     98.20
REMARK 500    TRP A 456     -177.09   -174.50
REMARK 500    TRP A 458       57.25   -118.02
REMARK 500    ASP A 460      -78.55    -39.73
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    GLN A 226        23.4      L          L   OUTSIDE RANGE
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 G39 A 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2H25   RELATED DB: PDB
REMARK 900 RELATED ID: 2H27   RELATED DB: PDB
DBREF  2HT8 A   83   471  UNP    Q07599   NRAM_IADU3      81    470
SEQRES   1 A  390  THR TYR MET ASN ASN THR GLU ALA ILE CYS ASP ALA LYS
SEQRES   2 A  390  GLY PHE ALA PRO PHE SER LYS ASP ASN GLY ILE ARG ILE
SEQRES   3 A  390  GLY SER ARG GLY HIS ILE PHE VAL ILE ARG GLU PRO PHE
SEQRES   4 A  390  VAL SER CYS SER PRO ILE GLU CYS ARG THR PHE PHE LEU
SEQRES   5 A  390  THR GLN GLY SER LEU LEU ASN ASP LYS HIS SER ASN GLY
SEQRES   6 A  390  THR VAL LYS ASP ARG SER PRO PHE ARG THR LEU MET SER
SEQRES   7 A  390  VAL GLU VAL GLY GLN SER PRO ASN VAL TYR GLN ALA ARG
SEQRES   8 A  390  PHE GLU ALA VAL ALA TRP SER ALA THR ALA CYS HIS ASP
SEQRES   9 A  390  GLY LYS LYS TRP MET THR VAL GLY VAL THR GLY PRO ASP
SEQRES  10 A  390  SER LYS ALA VAL ALA VAL ILE HIS TYR GLY GLY VAL PRO
SEQRES  11 A  390  THR ASP VAL VAL ASN SER TRP ALA GLY ASP ILE LEU ARG
SEQRES  12 A  390  THR GLN GLU SER SER CYS THR CYS ILE GLN GLY ASP CYS
SEQRES  13 A  390  TYR TRP VAL MET THR ASP GLY PRO ALA ASN ARG GLN ALA
SEQRES  14 A  390  GLN TYR ARG ILE TYR LYS ALA ASN GLN GLY ARG ILE ILE
SEQRES  15 A  390  GLY GLN THR ASP ILE SER PHE ASN GLY GLY HIS ILE GLU
SEQRES  16 A  390  GLU CYS SER CYS TYR PRO ASN ASP GLY LYS VAL GLU CYS
SEQRES  17 A  390  VAL CYS ARG ASP GLY TRP THR GLY THR ASN ARG PRO VAL
SEQRES  18 A  390  LEU VAL ILE SER PRO ASP LEU SER TYR ARG VAL GLY TYR
SEQRES  19 A  390  LEU CYS ALA GLY ILE PRO SER ASP THR PRO ARG GLY GLU
SEQRES  20 A  390  ASP THR GLN PHE THR GLY SER CYS THR SER PRO MET GLY
SEQRES  21 A  390  ASN GLN GLY TYR GLY VAL LYS GLY PHE GLY PHE ARG GLN
SEQRES  22 A  390  GLY THR ASP VAL TRP MET GLY ARG THR ILE SER ARG THR
SEQRES  23 A  390  SER ARG SER GLY PHE GLU ILE LEU ARG ILE LYS ASN GLY
SEQRES  24 A  390  TRP THR GLN THR SER LYS GLU GLN ILE ARG LYS GLN VAL
SEQRES  25 A  390  VAL VAL ASP ASN LEU ASN TRP SER GLY TYR SER GLY SER
SEQRES  26 A  390  PHE THR LEU PRO VAL GLU LEU SER GLY LYS ASP CYS LEU
SEQRES  27 A  390  VAL PRO CYS PHE TRP VAL GLU MET ILE ARG GLY LYS PRO
SEQRES  28 A  390  GLU GLU LYS THR ILE TRP THR SER SER SER SER ILE VAL
SEQRES  29 A  390  MET CYS GLY VAL ASP TYR GLU VAL ALA ASP TRP SER TRP
SEQRES  30 A  390  HIS ASP GLY ALA ILE LEU PRO PHE ASP ILE ASP LYS MET
HET    G39  A 800      20
HETNAM     G39 (3R,4R,5S)-4-(ACETYLAMINO)-5-AMINO-3-(PENTAN-3-YLOXY)
HETNAM   2 G39  CYCLOHEX-1-ENE-1-CARBOXYLIC ACID
HETSYN     G39 OSELTAMIVIR CARBOXYLATE
FORMUL   2  G39    C14 H24 N2 O4
FORMUL   3  HOH   *91(H2 O)
HELIX    1   1 ASN A  104  SER A  110  1                                   7
HELIX    2   2 ASP A  142  ASN A  146  5                                   5
HELIX    3   3 ASN A  168  ALA A  171  5                                   5
HELIX    4   4 PRO A   12A GLY A  414  1                                   6
SHEET    1   A 4 ALA A  98  LYS A 102  0
SHEET    2   A 4 THR A 439  CYS A 447 -1  O  VAL A 445   N  PHE A 100
SHEET    3   A 4 VAL A 419  GLY A 429 -1  N  MET A 426   O  SER A 442
SHEET    4   A 4 SER A 407  LEU A 412 -1  N  PHE A 410   O  CYS A 421
SHEET    1   B 4 PHE A 115  CYS A 124  0
SHEET    2   B 4 CYS A 129  LEU A 139 -1  O  PHE A 132   N  PHE A 121
SHEET    3   B 4 LEU A 158  GLU A 162 -1  O  VAL A 161   N  THR A 131
SHEET    4   B 4 ARG A 172  ALA A 175 -1  O  ALA A 175   N  LEU A 158
SHEET    1   C 4 ALA A 180  HIS A 184  0
SHEET    2   C 4 TRP A 189  THR A 195 -1  O  MET A 190   N  CYS A 183
SHEET    3   C 4 VAL A 202  TYR A 207 -1  O  HIS A 206   N  THR A 191
SHEET    4   C 4 PRO A 211  ASN A 216 -1  O  VAL A 215   N  ALA A 203
SHEET    1   D 3 ARG A 224  THR A 225  0
SHEET    2   D 3 ASP A 236  ASP A 243 -1  O  THR A 242   N  ARG A 224
SHEET    3   D 3 THR A 231  ILE A 233 -1  N  THR A 231   O  TYR A 238
SHEET    1   E 4 ARG A 224  THR A 225  0
SHEET    2   E 4 ASP A 236  ASP A 243 -1  O  THR A 242   N  ARG A 224
SHEET    3   E 4 GLN A 251  ALA A 257 -1  O  TYR A 255   N  TRP A 239
SHEET    4   E 4 ILE A 262  ILE A 268 -1  O  ILE A 263   N  LYS A 256
SHEET    1   F 4 SER A 279  PRO A 282  0
SHEET    2   F 4 VAL A 287  VAL A 290 -1  O  VAL A 290   N  SER A 279
SHEET    3   F 4 PRO A 301  ILE A 305 -1  O  ILE A 305   N  VAL A 287
SHEET    4   F 4 TYR A 312  TYR A 316 -1  O  GLY A 315   N  VAL A 302
SHEET    1   G 4 GLY A 353  GLN A 356  0
SHEET    2   G 4 ASP A 359  ARG A 364 -1  O  ASP A 359   N  GLN A 356
SHEET    3   G 4 SER A 372  ILE A 379 -1  O  LEU A 377   N  MET A 362
SHEET    4   G 4 GLN A 390  TRP A 403 -1  O  ASN A 402   N  GLY A 373
SSBOND   1 CYS A   92    CYS A  417                          1555   1555  2.02
SSBOND   2 CYS A  124    CYS A  129                          1555   1555  2.03
SSBOND   3 CYS A  183    CYS A  230                          1555   1555  2.04
SSBOND   4 CYS A  232    CYS A  237                          1555   1555  2.03
SSBOND   5 CYS A  278    CYS A  291                          1555   1555  2.03
SSBOND   6 CYS A  280    CYS A  289                          1555   1555  2.03
SSBOND   7 CYS A  318    CYS A  337                          1555   1555  2.02
SSBOND   8 CYS A  421    CYS A  447                          1555   1555  2.04
CISPEP   1 THR A  325    PRO A  326          0         0.27
CISPEP   2 LYS A  430    PRO A  431          0         0.02
CISPEP   3 LEU A  464    PRO A  465          0        -0.13
SITE     1 AC1 13 ARG A 118  GLU A 119  ASP A 151  ARG A 152
SITE     2 AC1 13 ILE A 222  ARG A 224  ALA A 246  GLU A 276
SITE     3 AC1 13 GLU A 277  ARG A 292  TYR A 347  ARG A 371
SITE     4 AC1 13 TYR A 406
CRYST1   90.430   90.430  109.710  90.00  90.00  90.00 I 4           8
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      0.011058  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011058  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009115        0.00000
      
PROCHECK
Go to PROCHECK summary
 References