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PDBsum entry 1e8t

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1e8t
Jmol
Contents
Protein chains
447 a.a. *
Ligands
GOL ×3
NAG
NAG-NAG ×2
Metals
_CA
Waters ×211
* Residue conservation analysis
HEADER    HYDROLASE                               01-OCT-00   1E8T
TITLE     STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS
TITLE    2 HEMAGGLUTININ-NEURAMINIDASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HEMAGGLUTININ-NEURAMINIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: HEAD DOMAIN, RESIDUES 124-577;
COMPND   5 SYNONYM: HN;
COMPND   6 EC: 3.2.1.18
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: NEWCASTLE DISEASE VIRUS;
SOURCE   3 ORGANISM_TAXID: 332244;
SOURCE   4 STRAIN: KANSAS
KEYWDS    SIALIDASE, NEURAMINIDASE, HYDROLASE, HEMAGGLUTININ
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.CRENNELL,T.TAKIMOTO,A.PORTNER,G.TAYLOR
REVDAT   4   19-OCT-11 1E8T    1       HEADER COMPND SOURCE KEYWDS
REVDAT   4 2                           REMARK DBREF  HETSYN FORMUL
REVDAT   4 3                           SITE   ATOM   TER    VERSN
REVDAT   3   24-FEB-09 1E8T    1       VERSN
REVDAT   2   18-JUL-03 1E8T    1       REMARK
REVDAT   1   03-APR-01 1E8T    0
JRNL        AUTH   S.CRENNELL,T.TAKIMOTO,A.PORTNER,G.TAYLOR
JRNL        TITL   CRYSTAL STRUCTURE OF THE MULTIFUNCTIONAL
JRNL        TITL 2 PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE
JRNL        REF    NAT.STRUCT.BIOL.              V.   7  1068 2000
JRNL        REFN                   ISSN 1072-8368
JRNL        PMID   11062565
JRNL        DOI    10.1038/81002
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   T.TAKIMOTO,G.L.TAYLOR,S.J.CRENNELL,R.A.SCROGGS,
REMARK   1  AUTH 2 A.PORTNER
REMARK   1  TITL   CRYSTALLIZATION OF NEWCASTLE DISEASE VIRUS
REMARK   1  TITL 2 HEMAGGLUTININ-NEURAMINIDASE GLYCOPROTEIN
REMARK   1  REF    VIROLOGY                      V. 270   208 2000
REMARK   1  REFN                   ISSN 0042-6822
REMARK   1  PMID   10772993
REMARK   1  DOI    10.1006/VIRO.2000.0263
REMARK   2
REMARK   2 RESOLUTION.    2.5  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
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) : 2.5
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.0
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97
REMARK   3   NUMBER OF REFLECTIONS             : 38111
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) : 0.222
REMARK   3   FREE R VALUE                     : 0.276
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 3848
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            : 6914
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 89
REMARK   3   SOLVENT ATOMS            : 211
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.38
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  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1E8T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  02-OCT-00.
REMARK 100 THE PDBE ID CODE IS EBI-5407.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 4.60
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
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) : 0.992
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   : 38168
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0
REMARK 200  DATA REDUNDANCY                : 11.000
REMARK 200  R MERGE                    (I) : 0.03100
REMARK 200  R SYM                      (I) : 0.03100
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
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   (%): 55.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
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       35.85500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.08000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.95500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       99.08000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.85500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.95500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     VAL A   571
REMARK 465     ARG A   572
REMARK 465     GLU A   573
REMARK 465     ALA A   574
REMARK 465     ARG A   575
REMARK 465     SER A   576
REMARK 465     GLY A   577
REMARK 465     ALA B   574
REMARK 465     ARG B   575
REMARK 465     SER B   576
REMARK 465     GLY B   577
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLY A 570    CA   C    O
REMARK 470     GLU B 573    CA   C    O    CB   CG   CD   OE1  OE2
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    ALA A 125      117.13    -36.33
REMARK 500    ILE A 127      136.19     64.84
REMARK 500    HIS A 128     -109.00    -63.05
REMARK 500    ALA A 145      -67.23    -94.15
REMARK 500    PHE A 156       85.55    -62.36
REMARK 500    GLN A 157      -56.94    -28.87
REMARK 500    ASP A 198       -5.54    -58.33
REMARK 500    ASN A 234       79.23   -106.86
REMARK 500    VAL A 302      -41.91     71.75
REMARK 500    ASP A 309       55.65     38.53
REMARK 500    TYR A 340      -76.78    -42.52
REMARK 500    ASN A 393       11.67    -68.74
REMARK 500    SER A 419     -145.78   -100.71
REMARK 500    ASN A 433       77.69     44.24
REMARK 500    LYS A 434       -8.12     66.48
REMARK 500    THR A 467     -146.39   -150.11
REMARK 500    HIS A 482        5.04     84.21
REMARK 500    ARG A 485      -28.67   -142.53
REMARK 500    ASP A 493       62.63    -64.52
REMARK 500    ASP A 507     -167.25   -123.36
REMARK 500    SER A 518     -151.16   -151.21
REMARK 500    THR A 551      -83.61    -21.80
REMARK 500    ASN A 568       35.86    -77.34
REMARK 500    PRO B 130      -33.01    -36.89
REMARK 500    ALA B 145      -71.18    -78.38
REMARK 500    SER B 154     -158.90    -84.65
REMARK 500    PHE B 156      107.86    -58.27
REMARK 500    GLU B 158       84.44    -11.62
REMARK 500    HIS B 159      102.17    -57.67
REMARK 500    ASN B 161       35.16   -142.63
REMARK 500    CYS B 196       21.39   -146.83
REMARK 500    ASP B 231     -160.53    -79.70
REMARK 500    VAL B 302      -38.05     74.98
REMARK 500    ASP B 342       65.65   -172.37
REMARK 500    ASN B 393        7.24    -67.41
REMARK 500    SER B 419     -149.31    -95.92
REMARK 500    ASN B 433     -121.53     56.71
REMARK 500    THR B 467     -145.07   -138.33
REMARK 500    THR B 471       89.07   -150.93
REMARK 500    HIS B 482       -1.03     68.50
REMARK 500    ASN B 500       68.62     68.33
REMARK 500    ASP B 507     -154.23   -103.19
REMARK 500    SER B 518     -143.18   -155.72
REMARK 500
REMARK 500 REMARK: NULL
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                              CA A1001  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 266   O
REMARK 620 2 VAL A 296   O    78.9
REMARK 620 3 ASP A 261   O   132.8  73.9
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800   ASN A 341 RESIDUES 1570 TO 1570
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800   ASN A 481 RESIDUES 1571 TO 1572
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO
REMARK 800   ASN B 481 RESIDUES 1573 TO 1574
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E8U   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS
REMARK 900  HEMAGGLUTININ-NEURAMINIDASE
REMARK 900 RELATED ID: 1E8V   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS
REMARK 900  HEMAGGLUTININ-NEURAMINIDASE
DBREF  1E8T A  124   577  UNP    Q9Q2W5   HN_NDVK        124    577
DBREF  1E8T B  124   577  UNP    Q9Q2W5   HN_NDVK        124    577
SEQRES   1 A  454  GLY ALA PRO ILE HIS ASP PRO ASP PHE ILE GLY GLY ILE
SEQRES   2 A  454  GLY LYS GLU LEU ILE VAL ASP ASN ALA SER ASP VAL THR
SEQRES   3 A  454  SER PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE
SEQRES   4 A  454  ILE PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE
SEQRES   5 A  454  PRO SER PHE ASP MET SER ALA THR HIS TYR CYS TYR THR
SEQRES   6 A  454  HIS ASN VAL ILE LEU SER GLY CYS ARG ASP HIS SER HIS
SEQRES   7 A  454  SER HIS GLN TYR LEU ALA LEU GLY VAL LEU ARG THR THR
SEQRES   8 A  454  ALA THR GLY ARG ILE PHE PHE SER THR LEU ARG SER ILE
SEQRES   9 A  454  SER LEU ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL
SEQRES  10 A  454  SER ALA THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS
SEQRES  11 A  454  VAL THR GLU THR GLU GLU GLU ASP TYR ASN SER ALA VAL
SEQRES  12 A  454  PRO THR LEU MET ALA HIS GLY ARG LEU GLY PHE ASP GLY
SEQRES  13 A  454  GLN TYR HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE
SEQRES  14 A  454  GLU ASP TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY
SEQRES  15 A  454  SER PHE ILE ASP GLY ARG VAL TRP PHE SER VAL TYR GLY
SEQRES  16 A  454  GLY LEU LYS PRO ASN SER PRO SER ASP THR VAL GLN GLU
SEQRES  17 A  454  GLY LYS TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS
SEQRES  18 A  454  PRO ASP GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER
SEQRES  19 A  454  SER TYR LYS PRO GLY ARG PHE GLY GLY LYS ARG ILE GLN
SEQRES  20 A  454  GLN ALA ILE LEU SER ILE LYS VAL SER THR SER LEU GLY
SEQRES  21 A  454  GLU ASP PRO VAL LEU THR VAL PRO PRO ASN THR VAL THR
SEQRES  22 A  454  LEU MET GLY ALA GLU GLY ARG ILE LEU THR VAL GLY THR
SEQRES  23 A  454  SER HIS PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER
SEQRES  24 A  454  PRO ALA LEU LEU TYR PRO MET THR VAL SER ASN LYS THR
SEQRES  25 A  454  ALA THR LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR
SEQRES  26 A  454  ARG PRO GLY SER ILE PRO CYS GLN ALA SER ALA ARG CYS
SEQRES  27 A  454  PRO ASN SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR
SEQRES  28 A  454  PRO LEU ILE PHE TYR ARG ASN HIS THR LEU ARG GLY VAL
SEQRES  29 A  454  PHE GLY THR MET LEU ASP SER GLU GLN ALA ARG LEU ASN
SEQRES  30 A  454  PRO ALA SER ALA VAL PHE ASP SER THR SER ARG SER ARG
SEQRES  31 A  454  ILE THR ARG VAL SER SER SER SER THR LYS ALA ALA TYR
SEQRES  32 A  454  THR THR SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS
SEQRES  33 A  454  THR TYR CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU
SEQRES  34 A  454  PHE GLY GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE
SEQRES  35 A  454  LEU LYS ASN ASP GLY VAL ARG GLU ALA ARG SER GLY
SEQRES   1 B  454  GLY ALA PRO ILE HIS ASP PRO ASP PHE ILE GLY GLY ILE
SEQRES   2 B  454  GLY LYS GLU LEU ILE VAL ASP ASN ALA SER ASP VAL THR
SEQRES   3 B  454  SER PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE
SEQRES   4 B  454  ILE PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE
SEQRES   5 B  454  PRO SER PHE ASP MET SER ALA THR HIS TYR CYS TYR THR
SEQRES   6 B  454  HIS ASN VAL ILE LEU SER GLY CYS ARG ASP HIS SER HIS
SEQRES   7 B  454  SER HIS GLN TYR LEU ALA LEU GLY VAL LEU ARG THR THR
SEQRES   8 B  454  ALA THR GLY ARG ILE PHE PHE SER THR LEU ARG SER ILE
SEQRES   9 B  454  SER LEU ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL
SEQRES  10 B  454  SER ALA THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS
SEQRES  11 B  454  VAL THR GLU THR GLU GLU GLU ASP TYR ASN SER ALA VAL
SEQRES  12 B  454  PRO THR LEU MET ALA HIS GLY ARG LEU GLY PHE ASP GLY
SEQRES  13 B  454  GLN TYR HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE
SEQRES  14 B  454  GLU ASP TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY
SEQRES  15 B  454  SER PHE ILE ASP GLY ARG VAL TRP PHE SER VAL TYR GLY
SEQRES  16 B  454  GLY LEU LYS PRO ASN SER PRO SER ASP THR VAL GLN GLU
SEQRES  17 B  454  GLY LYS TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS
SEQRES  18 B  454  PRO ASP GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER
SEQRES  19 B  454  SER TYR LYS PRO GLY ARG PHE GLY GLY LYS ARG ILE GLN
SEQRES  20 B  454  GLN ALA ILE LEU SER ILE LYS VAL SER THR SER LEU GLY
SEQRES  21 B  454  GLU ASP PRO VAL LEU THR VAL PRO PRO ASN THR VAL THR
SEQRES  22 B  454  LEU MET GLY ALA GLU GLY ARG ILE LEU THR VAL GLY THR
SEQRES  23 B  454  SER HIS PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER
SEQRES  24 B  454  PRO ALA LEU LEU TYR PRO MET THR VAL SER ASN LYS THR
SEQRES  25 B  454  ALA THR LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR
SEQRES  26 B  454  ARG PRO GLY SER ILE PRO CYS GLN ALA SER ALA ARG CYS
SEQRES  27 B  454  PRO ASN SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR
SEQRES  28 B  454  PRO LEU ILE PHE TYR ARG ASN HIS THR LEU ARG GLY VAL
SEQRES  29 B  454  PHE GLY THR MET LEU ASP SER GLU GLN ALA ARG LEU ASN
SEQRES  30 B  454  PRO ALA SER ALA VAL PHE ASP SER THR SER ARG SER ARG
SEQRES  31 B  454  ILE THR ARG VAL SER SER SER SER THR LYS ALA ALA TYR
SEQRES  32 B  454  THR THR SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS
SEQRES  33 B  454  THR TYR CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU
SEQRES  34 B  454  PHE GLY GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE
SEQRES  35 B  454  LEU LYS ASN ASP GLY VAL ARG GLU ALA ARG SER GLY
HET    NAG  A1570      14
HET    NAG  A1571      14
HET    NAG  A1572      14
HET    NAG  B1573      14
HET    NAG  B1574      14
HET     CA  A1001       1
HET    GOL  A1002       6
HET    GOL  A1003       6
HET    GOL  B1004       6
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      CA CALCIUM ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3  NAG    5(C8 H15 N O6)
FORMUL   4   CA    CA 2+
FORMUL   5  GOL    3(C3 H8 O3)
FORMUL   6  HOH   *211(H2 O)
HELIX    1   1 ASP A  129  ILE A  133  5                                   5
HELIX    2   2 ASP A  147  THR A  149  5                                   3
HELIX    3   3 THR A  257  SER A  264  1                                   8
HELIX    4   4 ASP A  287  PHE A  292  1                                   6
HELIX    5   5 SER A  324  GLU A  331  1                                   8
HELIX    6   6 GLU A  347  TYR A  359  1                                  13
HELIX    7   7 PRO A  361  GLY A  365  5                                   5
HELIX    8   8 ASN A  550  GLY A  554  5                                   5
HELIX    9   9 THR B  257  TYR B  262  1                                   6
HELIX   10  10 ASP B  287  PHE B  292  1                                   6
HELIX   11  11 SER B  324  GLN B  330  1                                   7
HELIX   12  12 GLU B  347  TYR B  359  1                                  13
HELIX   13  13 PRO B  361  GLY B  365  5                                   5
SHEET    1   A 2 PHE A 151  PRO A 153  0
SHEET    2   A 2 ILE A 565  LYS A 567 -1  N  LEU A 566   O  TYR A 152
SHEET    1   B 4 CYS A 172  ARG A 174  0
SHEET    2   B 4 TYR A 185  ILE A 192 -1  N  ILE A 192   O  CYS A 172
SHEET    3   B 4 SER A 202  THR A 213 -1  N  GLY A 209   O  TYR A 185
SHEET    4   B 4 ILE A 219  LEU A 229 -1  N  LEU A 229   O  GLN A 204
SHEET    1   C 2 SER A 177  SER A 181  0
SHEET    2   C 2 HIS A 184  THR A 188 -1  N  THR A 188   O  SER A 177
SHEET    1   D 4 SER A 239  THR A 243  0
SHEET    2   D 4 GLY A 246  LYS A 253 -1  N  LEU A 250   O  SER A 239
SHEET    3   D 4 LEU A 269  GLY A 276 -1  N  LEU A 275   O  CYS A 247
SHEET    4   D 4 TYR A 281  ASP A 285 -1  N  LYS A 284   O  HIS A 272
SHEET    1   E 4 SER A 306  ILE A 308  0
SHEET    2   E 4 ARG A 311  GLY A 319 -1  N  TRP A 313   O  SER A 306
SHEET    3   E 4 ILE A 369  LYS A 377 -1  N  ILE A 376   O  VAL A 312
SHEET    4   E 4 VAL A 387  THR A 389 -1  N  THR A 389   O  ILE A 373
SHEET    1   F 4 GLY A 402  VAL A 407  0
SHEET    2   F 4 SER A 410  GLN A 415 -1  N  TYR A 414   O  ARG A 403
SHEET    3   F 4 ALA A 424  MET A 429 -1  N  MET A 429   O  HIS A 411
SHEET    4   F 4 TYR A 442  PHE A 444 -1  N  PHE A 444   O  ALA A 424
SHEET    1   G 2 MET A 429  SER A 432  0
SHEET    2   G 2 THR A 435  LEU A 438 -1  N  THR A 437   O  THR A 430
SHEET    1   H 3 PRO A 501  PHE A 506  0
SHEET    2   H 3 GLY A 486  LEU A 492 -1  N  MET A 491   O  ALA A 502
SHEET    3   H 3 PRO A 473  ILE A 477 -1  N  ILE A 477   O  GLY A 486
SHEET    1   I 3 ARG A 557  GLU A 564  0
SHEET    2   I 3 LYS A 539  SER A 549 -1  N  ILE A 548   O  ARG A 557
SHEET    3   I 3 LYS A 523  VAL A 534 -1  N  VAL A 534   O  LYS A 539
SHEET    1   J 2 TRP A 295  PRO A 300  0
SHEET    2   J 2 VAL A 316  LEU A 320 -1  N  GLY A 319   O  VAL A 296
SHEET    1   K 2 PHE B 151  PRO B 153  0
SHEET    2   K 2 ILE B 565  LYS B 567 -1  N  LEU B 566   O  TYR B 152
SHEET    1   L 4 CYS B 172  ARG B 174  0
SHEET    2   L 4 TYR B 185  ILE B 192 -1  N  ILE B 192   O  CYS B 172
SHEET    3   L 4 HIS B 203  THR B 213 -1  N  GLY B 209   O  TYR B 185
SHEET    4   L 4 ILE B 219  LEU B 229 -1  N  LEU B 229   O  GLN B 204
SHEET    1   M 2 SER B 177  MET B 180  0
SHEET    2   M 2 TYR B 185  THR B 188 -1  N  THR B 188   O  SER B 177
SHEET    1   N 4 SER B 239  THR B 243  0
SHEET    2   N 4 GLY B 246  LYS B 253 -1  N  LEU B 250   O  SER B 239
SHEET    3   N 4 LEU B 269  GLY B 276 -1  N  LEU B 275   O  CYS B 247
SHEET    4   N 4 TYR B 281  ASP B 285 -1  N  LYS B 284   O  HIS B 272
SHEET    1   O 4 SER B 306  ILE B 308  0
SHEET    2   O 4 ARG B 311  GLY B 319 -1  N  TRP B 313   O  SER B 306
SHEET    3   O 4 ILE B 369  LYS B 377 -1  N  ILE B 376   O  VAL B 312
SHEET    4   O 4 VAL B 387  THR B 389 -1  N  THR B 389   O  ILE B 373
SHEET    1   P 4 GLY B 402  VAL B 407  0
SHEET    2   P 4 SER B 410  GLN B 415 -1  N  TYR B 414   O  ARG B 403
SHEET    3   P 4 ALA B 424  MET B 429 -1  N  MET B 429   O  HIS B 411
SHEET    4   P 4 TYR B 442  PHE B 444 -1  N  PHE B 444   O  ALA B 424
SHEET    1   Q 2 MET B 429  SER B 432  0
SHEET    2   Q 2 THR B 435  LEU B 438 -1  N  THR B 437   O  THR B 430
SHEET    1   R 3 PRO B 501  PHE B 506  0
SHEET    2   R 3 GLY B 486  LEU B 492 -1  N  MET B 491   O  ALA B 502
SHEET    3   R 3 TYR B 474  ILE B 477 -1  N  ILE B 477   O  GLY B 486
SHEET    1   S 3 ARG B 557  GLU B 564  0
SHEET    2   S 3 LYS B 539  SER B 549 -1  N  ILE B 548   O  ARG B 557
SHEET    3   S 3 LYS B 523  VAL B 534 -1  N  VAL B 534   O  LYS B 539
SHEET    1   T 2 TRP B 295  PRO B 300  0
SHEET    2   T 2 VAL B 316  LEU B 320 -1  N  GLY B 319   O  VAL B 296
SSBOND   1 CYS A  172    CYS A  196                          1555   1555  2.03
SSBOND   2 CYS A  186    CYS A  247                          1555   1555  2.04
SSBOND   3 CYS A  238    CYS A  251                          1555   1555  2.03
SSBOND   4 CYS A  344    CYS A  461                          1555   1555  2.04
SSBOND   5 CYS A  455    CYS A  465                          1555   1555  2.03
SSBOND   6 CYS A  531    CYS A  542                          1555   1555  2.03
SSBOND   7 CYS B  172    CYS B  196                          1555   1555  2.03
SSBOND   8 CYS B  186    CYS B  247                          1555   1555  2.03
SSBOND   9 CYS B  238    CYS B  251                          1555   1555  2.03
SSBOND  10 CYS B  344    CYS B  461                          1555   1555  2.03
SSBOND  11 CYS B  455    CYS B  465                          1555   1555  2.03
SSBOND  12 CYS B  531    CYS B  542                          1555   1555  2.03
LINK         ND2 ASN A 341                 C1  NAG A1570     1555   1555  1.45
LINK         ND2 ASN A 481                 C1  NAG A1571     1555   1555  1.45
LINK        CA    CA A1001                 O   ASP A 261     1555   1555  2.69
LINK        CA    CA A1001                 O   VAL A 266     1555   1555  2.42
LINK        CA    CA A1001                 O   VAL A 296     1555   1555  2.36
LINK         O4  NAG A1571                 C1  NAG A1572     1555   1555  1.38
LINK         ND2 ASN B 481                 C1  NAG B1573     1555   1555  1.45
LINK         O4  NAG B1573                 C1  NAG B1574     1555   1555  1.39
CISPEP   1 ILE A  453    PRO A  454          0         0.13
CISPEP   2 ILE B  453    PRO B  454          0         0.58
SITE     1 AC1  4 ASP A 261  SER A 264  VAL A 266  VAL A 296
SITE     1 AC2  8 ALA A 125  SER A 181  THR A 183  HIS A 184
SITE     2 AC2  8 THR A 243  PRO A 244  PRO A 325  HOH A2140
SITE     1 AC3  6 PRO A 361  GLY A 362  ARG A 363  SER A 464
SITE     2 AC3  6 CYS A 465  VAL A 466
SITE     1 AC4  2 HIS B 439  SER B 440
SITE     1 AC5  2 TYR A 340  ASN A 341
SITE     1 AC6  2 ASN A 481  THR A 483
SITE     1 AC7  3 TYR B 479  ASN B 481  THR B 483
CRYST1   71.710   77.910  198.160  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      0.013945  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012835  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005046        0.00000
MTRIX1   1 -0.988300  0.147500 -0.038900       35.58000    1
MTRIX2   1  0.120900  0.913100  0.389400      -12.26000    1
MTRIX3   1  0.093000  0.380200 -0.920200       49.01000    1
      
PROCHECK
Go to PROCHECK summary
 References