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PDBsum entry 1usx

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
1usx
Jmol
Contents
Protein chains
447 a.a. *
Ligands
DAN ×3
SIA-WIA ×3
* Residue conservation analysis
HEADER    HYDROLASE                               01-DEC-03   1USX
TITLE     CRYSTAL STRUCTURE OF THE NEWCASTLE DISEASE VIRUS
TITLE    2 HEMAGGLUTININ-NEURAMINIDASE COMPLEXED WITH THIOSIALOSIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HEMAGGLUTININ-NEURAMINIDASE GLYCOPROTEIN;
COMPND   3 CHAIN: A, B, C;
COMPND   4 FRAGMENT: HEAD DOMAIN, RESIDUES 124-577;
COMPND   5 EC: 3.2.1.18
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: NEWCASTLE DISEASE VIRUS;
SOURCE   3 ORGANISM_TAXID: 11176;
SOURCE   4 STRAIN: KANSAS
KEYWDS    HYDROLASE, NEURAMINIDASE, HEMAGGLUTININ, SIALIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.ZAITSEV,M.VON ITZSTEIN,D.GROVES,M.KIEFEL,T.TAKIMOTO,
AUTHOR   2 A.PORTNER,G.TAYLOR
REVDAT   4   20-NOV-13 1USX    1       KEYWDS REMARK VERSN  SITE
REVDAT   3   24-FEB-09 1USX    1       VERSN
REVDAT   2   26-MAR-04 1USX    1       AUTHOR
REVDAT   1   19-MAR-04 1USX    0
JRNL        AUTH   V.ZAITSEV,M.VON ITZSTEIN,D.GROVES,M.KIEFEL,
JRNL        AUTH 2 T.TAKIMOTO,A.PORTNER,G.TAYLOR
JRNL        TITL   SECOND SIALIC ACID BINDING SITE IN NEWCASTLE
JRNL        TITL 2 DISEASE VIRUS HEMAGGLUTININ-NEURAMINIDASE:
JRNL        TITL 3 IMPLICATIONS FOR FUSION
JRNL        REF    J.VIROL.                      V.  78  3733 2004
JRNL        REFN                   ISSN 0022-538X
JRNL        PMID   15016893
JRNL        DOI    10.1128/JVI.78.7.3733-3741.2004
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.CRENNELL,T.TAKIMOTO,A.PORTNER,G.TAYLOR
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE MULTIFUNCTIONAL
REMARK   1  TITL 2 PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   7  1068 2000
REMARK   1  REFN                   ISSN 1072-8368
REMARK   1  PMID   11062565
REMARK   1  DOI    10.1038/81002
REMARK   1 REFERENCE 2
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.    2.7  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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.7
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.0
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000.
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 79.6
REMARK   3   NUMBER OF REFLECTIONS             : 41877
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) : 0.225
REMARK   3   FREE R VALUE                     : 0.289
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 2095
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            : 10338
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 159
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 49.3
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.3
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.070
REMARK   3    B22 (A**2) : 2.070
REMARK   3    B33 (A**2) : -4.14
REMARK   3    B12 (A**2) : 0.0
REMARK   3    B13 (A**2) : 0.0
REMARK   3    B23 (A**2) : 0.0
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) : 1.46
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK   3   KSOL        : 0.378
REMARK   3   BSOL        : 25.8
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 1USX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  01-DEC-03.
REMARK 100 THE PDBE ID CODE IS EBI-14087.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-03
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)
REMARK 200  OPTICS                         : TOROIDAL MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43065
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 81.5
REMARK 200  DATA REDUNDANCY                : 10.200
REMARK 200  R MERGE                    (I) : 0.07800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1E8V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.4
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-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      141.98000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       57.53500
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       57.53500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       70.99000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       57.53500
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       57.53500
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      212.97000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       57.53500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.53500
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       70.99000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       57.53500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.53500
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      212.97000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      141.98000
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      141.98000
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     VAL B   571
REMARK 465     ARG B   572
REMARK 465     GLU B   573
REMARK 465     ALA B   574
REMARK 465     ARG B   575
REMARK 465     SER B   576
REMARK 465     GLY B   577
REMARK 465     VAL C   571
REMARK 465     ARG C   572
REMARK 465     GLU C   573
REMARK 465     ALA C   574
REMARK 465     ARG C   575
REMARK 465     SER C   576
REMARK 465     GLY C   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     GLY B 570    CA   C    O
REMARK 470     GLY C 570    CA   C    O
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 251   CA  -  CB  -  SG  ANGL. DEV. =   8.4 DEGREES
REMARK 500    CYS C 251   CA  -  CB  -  SG  ANGL. DEV. =   8.7 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    ILE A 127      146.84   -173.53
REMARK 500    SER A 146      138.65    -37.44
REMARK 500    LEU A 160       96.21    -64.20
REMARK 500    ASN A 161      100.26    -58.39
REMARK 500    ILE A 175       65.48     66.69
REMARK 500    SER A 200      -86.30    -39.07
REMARK 500    ASP A 231     -148.14   -147.85
REMARK 500    VAL A 302      -21.07     71.91
REMARK 500    ASN A 323       -7.87     85.35
REMARK 500    ASN A 341      -70.21    -76.66
REMARK 500    ASP A 342      164.57    -41.09
REMARK 500    PRO A 345      -72.24    -62.84
REMARK 500    ASP A 346      145.92     -6.10
REMARK 500    ASN A 393        6.59    -57.48
REMARK 500    SER A 419     -160.56   -109.11
REMARK 500    ASN A 433     -108.38     72.03
REMARK 500    PHE A 444       75.80   -119.37
REMARK 500    ASN A 445      -14.78    -47.93
REMARK 500    ILE A 453      132.38    -38.45
REMARK 500    CYS A 455       46.23   -106.61
REMARK 500    ALA A 459      139.57    -32.88
REMARK 500    THR A 467     -141.80   -137.89
REMARK 500    PRO A 475      102.82    -50.25
REMARK 500    HIS A 482       -1.59     65.69
REMARK 500    GLN A 496      -58.17   -132.52
REMARK 500    ASN A 500       95.98     45.40
REMARK 500    ALA A 502      118.77   -169.74
REMARK 500    ALA A 504      164.42    164.32
REMARK 500    ASP A 507     -166.25   -100.07
REMARK 500    ALA A 525     -124.51   -155.71
REMARK 500    LYS A 536      -78.34    -46.00
REMARK 500    LEU A 552      -54.33     63.64
REMARK 500    ALA B 145      -95.44    -75.16
REMARK 500    SER B 146      155.15    -26.25
REMARK 500    VAL B 148      -52.95    -21.20
REMARK 500    SER B 200      -82.06    -70.30
REMARK 500    SER B 202      158.58    156.54
REMARK 500    THR B 232      -60.39    -18.08
REMARK 500    THR B 255      -57.42   -121.07
REMARK 500    ASP B 287       72.88    -69.00
REMARK 500    ASP B 294       21.58    -74.03
REMARK 500    ASN B 298       98.56   -161.05
REMARK 500    VAL B 302      -33.57     67.40
REMARK 500    ASP B 309       75.96     54.56
REMARK 500    VAL B 335      138.18   -175.54
REMARK 500    PRO B 345      -73.05    -53.51
REMARK 500    ASP B 346      122.45    -15.55
REMARK 500    GLU B 347      156.18    -36.56
REMARK 500    SER B 358        1.47    -61.74
REMARK 500    ALA B 372      154.06    178.10
REMARK 500
REMARK 500 THIS ENTRY HAS     100 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A1570
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B1572
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN C1572
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUES
REMARK 800  SIA A1571  AND WIA A1572
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUES
REMARK 800  SIA B1570  AND WIA B1571
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUES
REMARK 800  SIA C1570  AND WIA C1571
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E8T   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS
REMARK 900  HEMAGGLUTININ-NEURAMINIDASE
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
REMARK 900 RELATED ID: 1USR   RELATED DB: PDB
REMARK 900  NEWCASTLE DISEASE VIRUS HEMAGGLUTININ-
REMARK 900  NEURAMINIDASE COMPLEXED WITH THIOSIALOSIDE
DBREF  1USX A  124   577  UNP    P32884   HEMA_NDVB      124    577
DBREF  1USX B  124   577  UNP    P32884   HEMA_NDVB      124    577
DBREF  1USX C  124   577  UNP    P32884   HEMA_NDVB      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
SEQRES   1 C  454  GLY ALA PRO ILE HIS ASP PRO ASP PHE ILE GLY GLY ILE
SEQRES   2 C  454  GLY LYS GLU LEU ILE VAL ASP ASN ALA SER ASP VAL THR
SEQRES   3 C  454  SER PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE
SEQRES   4 C  454  ILE PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE
SEQRES   5 C  454  PRO SER PHE ASP MET SER ALA THR HIS TYR CYS TYR THR
SEQRES   6 C  454  HIS ASN VAL ILE LEU SER GLY CYS ARG ASP HIS SER HIS
SEQRES   7 C  454  SER HIS GLN TYR LEU ALA LEU GLY VAL LEU ARG THR THR
SEQRES   8 C  454  ALA THR GLY ARG ILE PHE PHE SER THR LEU ARG SER ILE
SEQRES   9 C  454  SER LEU ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL
SEQRES  10 C  454  SER ALA THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS
SEQRES  11 C  454  VAL THR GLU THR GLU GLU GLU ASP TYR ASN SER ALA VAL
SEQRES  12 C  454  PRO THR LEU MET ALA HIS GLY ARG LEU GLY PHE ASP GLY
SEQRES  13 C  454  GLN TYR HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE
SEQRES  14 C  454  GLU ASP TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY
SEQRES  15 C  454  SER PHE ILE ASP GLY ARG VAL TRP PHE SER VAL TYR GLY
SEQRES  16 C  454  GLY LEU LYS PRO ASN SER PRO SER ASP THR VAL GLN GLU
SEQRES  17 C  454  GLY LYS TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS
SEQRES  18 C  454  PRO ASP GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER
SEQRES  19 C  454  SER TYR LYS PRO GLY ARG PHE GLY GLY LYS ARG ILE GLN
SEQRES  20 C  454  GLN ALA ILE LEU SER ILE LYS VAL SER THR SER LEU GLY
SEQRES  21 C  454  GLU ASP PRO VAL LEU THR VAL PRO PRO ASN THR VAL THR
SEQRES  22 C  454  LEU MET GLY ALA GLU GLY ARG ILE LEU THR VAL GLY THR
SEQRES  23 C  454  SER HIS PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER
SEQRES  24 C  454  PRO ALA LEU LEU TYR PRO MET THR VAL SER ASN LYS THR
SEQRES  25 C  454  ALA THR LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR
SEQRES  26 C  454  ARG PRO GLY SER ILE PRO CYS GLN ALA SER ALA ARG CYS
SEQRES  27 C  454  PRO ASN SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR
SEQRES  28 C  454  PRO LEU ILE PHE TYR ARG ASN HIS THR LEU ARG GLY VAL
SEQRES  29 C  454  PHE GLY THR MET LEU ASP SER GLU GLN ALA ARG LEU ASN
SEQRES  30 C  454  PRO ALA SER ALA VAL PHE ASP SER THR SER ARG SER ARG
SEQRES  31 C  454  ILE THR ARG VAL SER SER SER SER THR LYS ALA ALA TYR
SEQRES  32 C  454  THR THR SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS
SEQRES  33 C  454  THR TYR CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU
SEQRES  34 C  454  PHE GLY GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE
SEQRES  35 C  454  LEU LYS ASN ASP GLY VAL ARG GLU ALA ARG SER GLY
HET    SIA  A1571      20
HET    SIA  B1570      20
HET    SIA  C1570      20
HET    DAN  A1570      20
HET    WIA  A1572      13
HET    WIA  B1571      13
HET    DAN  B1572      20
HET    WIA  C1571      13
HET    DAN  C1572      20
HETNAM     SIA O-SIALIC ACID
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
HETNAM     WIA METHYL(6S)-1-THIO-L-MANNO-HEXODIALDO-6,2-
HETNAM   2 WIA  PYRANOSIDE
FORMUL   4  SIA    3(C11 H19 N O9)
FORMUL   7  DAN    3(C11 H17 N O8)
FORMUL   8  WIA    3(C7 H12 O5 S)
HELIX    1   1 ASP A  147  THR A  149  5                                   3
HELIX    2   2 THR A  257  TYR A  262  1                                   6
HELIX    3   3 ASP A  287  PHE A  292  1                                   6
HELIX    4   4 SER A  324  VAL A  329  1                                   6
HELIX    5   5 GLU A  347  SER A  357  1                                  11
HELIX    6   6 SER A  358  LYS A  360  5                                   3
HELIX    7   7 PRO A  361  GLY A  365  5                                   5
HELIX    8   8 ASP B  147  THR B  149  5                                   3
HELIX    9   9 THR B  257  ASN B  263  1                                   7
HELIX   10  10 ASP B  287  PHE B  292  1                                   6
HELIX   11  11 SER B  324  GLU B  331  1                                   8
HELIX   12  12 GLU B  347  SER B  358  1                                  12
HELIX   13  13 PRO B  361  GLY B  365  5                                   5
HELIX   14  14 ASP C  129  ILE C  133  5                                   5
HELIX   15  15 ASP C  147  THR C  149  5                                   3
HELIX   16  16 THR C  257  TYR C  262  1                                   6
HELIX   17  17 ASP C  287  PHE C  292  1                                   6
HELIX   18  18 SER C  324  GLN C  330  1                                   7
HELIX   19  19 GLU C  347  SER C  358  1                                  12
HELIX   20  20 PRO C  361  GLY C  365  5                                   5
SHEET    1  AA 4 ILE A 141  VAL A 142  0
SHEET    2  AA 4 PRO A 473  PHE A 478  1  O  LEU A 476   N  ILE A 141
SHEET    3  AA 4 LEU A 484  THR A 490 -1  N  ARG A 485   O  ILE A 477
SHEET    4  AA 4 SER A 503  PHE A 506 -1  O  ALA A 504   N  GLY A 489
SHEET    1  AB 4 PHE A 151  PRO A 153  0
SHEET    2  AB 4 PHE A 556  LYS A 567 -1  O  LEU A 566   N  TYR A 152
SHEET    3  AB 4 LYS A 539  SER A 549 -1  O  THR A 540   N  ILE A 565
SHEET    4  AB 4 ALA A 524  VAL A 534 -1  N  ALA A 525   O  GLU A 547
SHEET    1  AC 4 CYS A 172  MET A 180  0
SHEET    2  AC 4 TYR A 185  ILE A 192 -1  O  CYS A 186   N  ASP A 179
SHEET    3  AC 4 HIS A 203  THR A 213 -1  O  HIS A 203   N  VAL A 191
SHEET    4  AC 4 ILE A 219  LEU A 229 -1  O  PHE A 220   N  ARG A 212
SHEET    1  AD 4 ARG A 235  THR A 243  0
SHEET    2  AD 4 GLY A 246  LYS A 253 -1  O  GLY A 246   N  THR A 243
SHEET    3  AD 4 MET A 270  GLY A 276 -1  O  ALA A 271   N  CYS A 251
SHEET    4  AD 4 TYR A 281  ASP A 285 -1  O  HIS A 282   N  ARG A 274
SHEET    1  AE 3 TRP A 295  PRO A 300  0
SHEET    2  AE 3 ARG A 311  LEU A 320 -1  O  TYR A 317   N  TYR A 299
SHEET    3  AE 3 SER A 306  ILE A 308 -1  O  SER A 306   N  TRP A 313
SHEET    1  AF 4 TRP A 295  PRO A 300  0
SHEET    2  AF 4 ARG A 311  LEU A 320 -1  O  TYR A 317   N  TYR A 299
SHEET    3  AF 4 ARG A 368  LYS A 377 -1  O  ARG A 368   N  LEU A 320
SHEET    4  AF 4 VAL A 387  THR A 389 -1  O  VAL A 387   N  SER A 375
SHEET    1  AG 4 GLY A 402  VAL A 407  0
SHEET    2  AG 4 SER A 410  GLN A 415 -1  O  SER A 410   N  VAL A 407
SHEET    3  AG 4 ALA A 424  SER A 432 -1  O  LEU A 425   N  GLN A 415
SHEET    4  AG 4 TYR A 442  PHE A 444 -1  O  TYR A 442   N  LEU A 426
SHEET    1  AH 4 GLY A 402  VAL A 407  0
SHEET    2  AH 4 SER A 410  GLN A 415 -1  O  SER A 410   N  VAL A 407
SHEET    3  AH 4 ALA A 424  SER A 432 -1  O  LEU A 425   N  GLN A 415
SHEET    4  AH 4 THR A 435  LEU A 438 -1  O  THR A 435   N  SER A 432
SHEET    1  BA 5 ILE B 141  VAL B 142  0
SHEET    2  BA 5 TYR B 474  PHE B 478  1  O  LEU B 476   N  ILE B 141
SHEET    3  BA 5 LEU B 484  LEU B 492 -1  N  ARG B 485   O  ILE B 477
SHEET    4  BA 5 PRO B 501  PHE B 506 -1  O  ALA B 502   N  MET B 491
SHEET    5  BA 5 THR B 515  ARG B 516 -1  O  THR B 515   N  SER B 503
SHEET    1  BB 4 PHE B 151  PRO B 153  0
SHEET    2  BB 4 PHE B 556  LYS B 567 -1  O  LEU B 566   N  TYR B 152
SHEET    3  BB 4 LYS B 539  SER B 549 -1  O  THR B 540   N  ILE B 565
SHEET    4  BB 4 ALA B 524  VAL B 534 -1  N  ALA B 525   O  GLU B 547
SHEET    1  BC 4 CYS B 172  MET B 180  0
SHEET    2  BC 4 TYR B 185  ILE B 192 -1  O  CYS B 186   N  ASP B 179
SHEET    3  BC 4 HIS B 203  THR B 213 -1  O  HIS B 203   N  VAL B 191
SHEET    4  BC 4 ILE B 219  LEU B 229 -1  O  PHE B 220   N  ARG B 212
SHEET    1  BD 4 ARG B 235  ALA B 242  0
SHEET    2  BD 4 GLY B 246  LYS B 253 -1  O  ASP B 248   N  SER B 241
SHEET    3  BD 4 LEU B 269  GLY B 276 -1  O  LEU B 269   N  LYS B 253
SHEET    4  BD 4 TYR B 281  LEU B 286 -1  O  HIS B 282   N  ARG B 274
SHEET    1  BE 3 TRP B 295  PRO B 300  0
SHEET    2  BE 3 ARG B 311  LEU B 320 -1  O  TYR B 317   N  TYR B 299
SHEET    3  BE 3 SER B 306  ILE B 308 -1  O  SER B 306   N  TRP B 313
SHEET    1  BF 4 TRP B 295  PRO B 300  0
SHEET    2  BF 4 ARG B 311  LEU B 320 -1  O  TYR B 317   N  TYR B 299
SHEET    3  BF 4 ARG B 368  LYS B 377 -1  O  ARG B 368   N  LEU B 320
SHEET    4  BF 4 GLU B 384  THR B 389 -1  O  GLU B 384   N  LYS B 377
SHEET    1  BG 7 GLY B 402  VAL B 407  0
SHEET    2  BG 7 SER B 410  GLN B 415 -1  O  SER B 410   N  VAL B 407
SHEET    3  BG 7 ALA B 424  SER B 432 -1  N  LEU B 425   O  GLN B 415
SHEET    4  BG 7 THR B 435  LEU B 438 -1  O  THR B 435   N  SER B 432
SHEET    5  BG 7 ALA B 424  SER B 432 -1  O  THR B 430   N  THR B 437
SHEET    6  BG 7 TYR B 442  PHE B 444 -1  O  TYR B 442   N  LEU B 426
SHEET    7  BG 7 ALA B 424  SER B 432 -1  O  ALA B 424   N  PHE B 444
SHEET    1  CA 5 ILE C 141  VAL C 142  0
SHEET    2  CA 5 TYR C 474  PHE C 478  1  O  LEU C 476   N  ILE C 141
SHEET    3  CA 5 LEU C 484  LEU C 492 -1  N  ARG C 485   O  ILE C 477
SHEET    4  CA 5 PRO C 501  ASP C 507 -1  O  ALA C 502   N  MET C 491
SHEET    5  CA 5 ARG C 511  ARG C 516 -1  N  SER C 512   O  VAL C 505
SHEET    1  CB 4 PHE C 151  PRO C 153  0
SHEET    2  CB 4 PHE C 556  LYS C 567 -1  O  LEU C 566   N  TYR C 152
SHEET    3  CB 4 LYS C 539  SER C 549 -1  O  THR C 540   N  ILE C 565
SHEET    4  CB 4 ALA C 524  VAL C 534 -1  N  ALA C 525   O  GLU C 547
SHEET    1  CC 4 CYS C 172  MET C 180  0
SHEET    2  CC 4 TYR C 185  ILE C 192 -1  O  CYS C 186   N  ASP C 179
SHEET    3  CC 4 HIS C 203  THR C 213 -1  O  HIS C 203   N  VAL C 191
SHEET    4  CC 4 ILE C 219  LEU C 229 -1  O  PHE C 220   N  ARG C 212
SHEET    1  CD 4 ARG C 235  THR C 243  0
SHEET    2  CD 4 GLY C 246  LYS C 253 -1  O  GLY C 246   N  THR C 243
SHEET    3  CD 4 LEU C 269  LEU C 275 -1  O  LEU C 269   N  LYS C 253
SHEET    4  CD 4 TYR C 281  ASP C 285 -1  O  HIS C 282   N  ARG C 274
SHEET    1  CE 7 TRP C 295  PRO C 300  0
SHEET    2  CE 7 ARG C 311  LEU C 320 -1  O  TYR C 317   N  TYR C 299
SHEET    3  CE 7 SER C 306  ILE C 308 -1  O  SER C 306   N  TRP C 313
SHEET    4  CE 7 ARG C 311  LEU C 320 -1  O  ARG C 311   N  ILE C 308
SHEET    5  CE 7 GLU C 384  THR C 389
SHEET    6  CE 7 ARG C 368  LYS C 377 -1  O  ILE C 373   N  THR C 389
SHEET    7  CE 7 ARG C 311  LEU C 320 -1  O  VAL C 312   N  ILE C 376
SHEET    1  CF 7 GLY C 402  VAL C 407  0
SHEET    2  CF 7 SER C 410  GLN C 415 -1  O  SER C 410   N  VAL C 407
SHEET    3  CF 7 ALA C 424  THR C 430 -1  O  TYR C 427   N  LEU C 413
SHEET    4  CF 7 THR C 437  LEU C 438 -1  O  THR C 437   N  THR C 430
SHEET    5  CF 7 ALA C 424  THR C 430 -1  O  THR C 430   N  THR C 437
SHEET    6  CF 7 TYR C 442  PHE C 444 -1  O  TYR C 442   N  LEU C 426
SHEET    7  CF 7 ALA C 424  THR C 430 -1  O  ALA C 424   N  PHE C 444
SSBOND   1 CYS A  172    CYS A  196                          1555   1555  2.04
SSBOND   2 CYS A  186    CYS A  247                          1555   1555  2.04
SSBOND   3 CYS A  238    CYS A  251                          1555   1555  2.04
SSBOND   4 CYS A  344    CYS A  461                          1555   1555  2.04
SSBOND   5 CYS A  455    CYS A  465                          1555   1555  2.04
SSBOND   6 CYS A  531    CYS A  542                          1555   1555  2.03
SSBOND   7 CYS B  172    CYS B  196                          1555   1555  2.04
SSBOND   8 CYS B  186    CYS B  247                          1555   1555  2.04
SSBOND   9 CYS B  238    CYS B  251                          1555   1555  2.05
SSBOND  10 CYS B  344    CYS B  461                          1555   1555  2.04
SSBOND  11 CYS B  455    CYS B  465                          1555   1555  2.03
SSBOND  12 CYS B  531    CYS B  542                          1555   1555  2.04
SSBOND  13 CYS C  172    CYS C  196                          1555   1555  2.04
SSBOND  14 CYS C  186    CYS C  247                          1555   1555  2.04
SSBOND  15 CYS C  238    CYS C  251                          1555   1555  2.05
SSBOND  16 CYS C  344    CYS C  461                          1555   1555  2.04
SSBOND  17 CYS C  455    CYS C  465                          1555   1555  2.05
SSBOND  18 CYS C  531    CYS C  542                          1555   1555  2.04
LINK         C2  SIA A1571                 S1  WIA A1572     1555   1555  1.78
LINK         C2  SIA B1570                 S1  WIA B1571     1555   1555  1.82
LINK         C2  SIA C1570                 S1  WIA C1571     1555   1555  1.79
CISPEP   1 ILE A  453    PRO A  454          0         0.55
CISPEP   2 ILE B  453    PRO B  454          0        -0.06
CISPEP   3 ILE C  453    PRO C  454          0         0.06
SITE     1 AC1 10 ARG A 174  GLU A 258  TYR A 299  TYR A 317
SITE     2 AC1 10 ARG A 363  GLU A 401  ARG A 416  VAL A 466
SITE     3 AC1 10 ARG A 498  TYR A 526
SITE     1 AC2  8 ARG B 174  ILE B 175  GLU B 258  TYR B 317
SITE     2 AC2  8 GLU B 401  ARG B 416  ARG B 498  TYR B 526
SITE     1 AC3  7 ARG C 174  GLU C 258  TYR C 317  GLU C 401
SITE     2 AC3  7 ARG C 416  ARG C 498  TYR C 526
SITE     1 AC4  7 PHE A 156  THR A 515  ARG A 516  VAL A 517
SITE     2 AC4  7 SER A 519  THR B 168  GLY B 169
SITE     1 AC5  8 THR A 168  GLY A 169  PHE B 156  THR B 515
SITE     2 AC5  8 ARG B 516  VAL B 517  SER B 518  SER B 519
SITE     1 AC6  7 PHE C 156  GLY C 169  THR C 515  ARG C 516
SITE     2 AC6  7 VAL C 517  SER C 518  SER C 519
CRYST1  115.070  115.070  283.960  90.00  90.00  90.00 P 41 21 2    24
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      0.008690  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008690  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003522        0.00000
MTRIX1   1  0.702240  0.704600  0.102020       -0.20411    1
MTRIX2   1  0.703150 -0.708860  0.055680        0.26087    1
MTRIX3   1  0.111550  0.032640 -0.993220        0.62620    1
      
PROCHECK
Go to PROCHECK summary
 References