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PDBsum entry 1e8v

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1e8v
Jmol
Contents
Protein chains
447 a.a. *
Ligands
DAN ×2
NAG ×3
NAG-NAG
Metals
_CA ×2
Waters ×239
* Residue conservation analysis
HEADER    HYDROLASE                               01-OCT-00   1E8V
TITLE     STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS
TITLE    2 HEMAGGLUTININ-NEURAMINIDASE
CAVEAT     1E8V    NAG A1572 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT     1E8V    NAG B1571 HAS WRONG CHIRALITY AT ATOM C1
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: 11176;
SOURCE   4 STRAIN: KANSAS
KEYWDS    SIALIDASE, NEURAMINIDASE, HEMAGGLUTININ, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.CRENNELL,T.TAKIMOTO,A.PORTNER,G.TAYLOR
REVDAT   4   09-NOV-11 1E8V    1       HEADER CAVEAT COMPND KEYWDS
REVDAT   4 2                           REMARK HET    HETNAM FORMUL
REVDAT   4 3                           HETSYN LINK   SITE   HETATM
REVDAT   4 4                           VERSN
REVDAT   3   24-FEB-09 1E8V    1       VERSN
REVDAT   2   18-JUL-03 1E8V    1       REMARK
REVDAT   1   03-APR-01 1E8V    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.    2.0  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) : 2.0
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             : 75779
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) : 0.232
REMARK   3   FREE R VALUE                     : 0.267
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 3840
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            : 6896
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 112
REMARK   3   SOLVENT ATOMS            : 239
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 1E8V 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-5409.
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                             : 6.50
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) : 0.909
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   : 38673
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
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     (%) : 94.0
REMARK 200  DATA REDUNDANCY                : 12.900
REMARK 200  R MERGE                    (I) : 0.05200
REMARK 200  R SYM                      (I) : 0.05200
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: MOLECULAR REPLACEMENT
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   (%): 61.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+5/6
REMARK 290       6555   X-Y,X,Z+1/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.86667
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       77.73333
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       58.30000
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       97.16667
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       19.43333
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: 6090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.1 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     GLY B   570
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH A  2036     O    HOH A  2037              1.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 449   CD  -  NE  -  CZ  ANGL. DEV. =  11.3 DEGREES
REMARK 500    ARG A 449   NE  -  CZ  -  NH1 ANGL. DEV. =   7.8 DEGREES
REMARK 500    ARG A 449   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.6 DEGREES
REMARK 500    ARG B 449   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES
REMARK 500    ARG B 449   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ARG B 449   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 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 175       68.51     63.66
REMARK 500    ASP A 231     -153.30   -133.64
REMARK 500    VAL A 302      -37.22     64.17
REMARK 500    VAL A 335      141.84   -175.76
REMARK 500    ARG A 363      -40.09    -24.59
REMARK 500    SER A 419     -148.66    -96.12
REMARK 500    ASN A 433     -116.79     67.45
REMARK 500    CYS A 455       42.61   -100.87
REMARK 500    THR A 467     -138.37   -141.65
REMARK 500    PRO A 475      109.13    -54.48
REMARK 500    HIS A 482        5.02     85.49
REMARK 500    ASN A 500       90.06     49.27
REMARK 500    ALA A 525     -136.05   -143.76
REMARK 500    TYR A 526      153.39    -46.42
REMARK 500    LEU A 552      -54.79     72.21
REMARK 500    ILE B 175       67.75     64.10
REMARK 500    ASP B 231     -154.14   -134.76
REMARK 500    VAL B 302      -38.32     65.00
REMARK 500    VAL B 335      141.59   -175.46
REMARK 500    ASP B 346      150.83    -49.20
REMARK 500    ARG B 363      -39.79    -24.16
REMARK 500    SER B 419     -147.08    -95.11
REMARK 500    ASN B 433     -116.58     67.86
REMARK 500    CYS B 455       42.98   -101.69
REMARK 500    THR B 467     -139.79   -143.09
REMARK 500    PRO B 475      109.37    -55.30
REMARK 500    HIS B 482        5.49     86.00
REMARK 500    ASN B 500       89.75     48.85
REMARK 500    ALA B 525     -136.05   -143.54
REMARK 500    TYR B 526      153.90    -47.42
REMARK 500    LEU B 552      -54.28     73.65
REMARK 500    ASN B 568      -75.02    -40.64
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 SER A 264   O
REMARK 620 2 SER A 264   OG   72.3
REMARK 620 3 VAL A 266   O    85.2 131.2
REMARK 620 4 VAL A 296   O    82.7 142.3  72.0
REMARK 620 5 ASP A 261   OD1 149.5  92.0 123.6  96.0
REMARK 620 6 ASP A 261   O    74.3  69.4 144.7  77.1  75.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B1002  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 266   O
REMARK 620 2 VAL B 296   O    71.6
REMARK 620 3 ASP B 261   O   137.6  71.7
REMARK 620 4 ASP B 261   OD1 128.8  95.6  75.2
REMARK 620 5 SER B 264   O    82.0  77.4  70.0 145.0
REMARK 620 6 SER B 264   OG  131.6 133.7  67.1  93.5  69.5
REMARK 620 N                    1     2     3     4     5
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  CA B1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A1571
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B1570
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 1572 TO 1572
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 1573 TO 1573
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 341 RESIDUES  841 TO  841
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO
REMARK 800   ASN B 481 RESIDUES 1571 TO 1572
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
DBREF  1E8V A  124   577  UNP    Q9Q2W5   Q9Q2W5         124    577
DBREF  1E8V B  124   577  UNP    Q9Q2W5   Q9Q2W5         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  A1572      14
HET    NAG  A1573      14
HET    NAG  B 841      14
HET    NAG  B1571      14
HET    NAG  B1572      14
HET     CA  A1001       1
HET     CA  B1002       1
HET    DAN  A1571      20
HET    DAN  B1570      20
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      CA CALCIUM ION
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
FORMUL   3  NAG    5(C8 H15 N O6)
FORMUL   4   CA    2(CA 2+)
FORMUL   5  DAN    2(C11 H17 N O8)
FORMUL   6  HOH   *239(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 ASP B  129  ILE B  133  5                                   5
HELIX    8   8 ASP B  147  THR B  149  5                                   3
HELIX    9   9 THR B  257  SER B  264  1                                   8
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  TYR B  359  1                                  13
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 HIS A 203  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  MET A 180  0
SHEET    2   C 2 TYR A 185  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  LEU A 320 -1  N  TRP A 313   O  SER A 306
SHEET    3   E 4 ARG A 368  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 THR A 527  VAL A 534  0
SHEET    2   I 3 LYS A 539  SER A 549 -1  N  ILE A 545   O  THR A 528
SHEET    3   I 3 PHE A 556  GLU A 564 -1  N  VAL A 563   O  CYS A 542
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  LEU B 320 -1  N  TRP B 313   O  SER B 306
SHEET    3   O 4 ARG B 368  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 PRO B 473  ILE B 477 -1  N  ILE B 477   O  GLY B 486
SHEET    1   S 3 THR B 527  VAL B 534  0
SHEET    2   S 3 LYS B 539  SER B 549 -1  N  ILE B 545   O  THR B 528
SHEET    3   S 3 PHE B 556  GLU B 564 -1  N  VAL B 563   O  CYS B 542
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  2.03
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  2.04
SSBOND   8 CYS B  186    CYS B  247                          1555   1555  2.04
SSBOND   9 CYS B  238    CYS B  251                          1555   1555  2.02
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  2.02
LINK         ND2 ASN A 341                 C1  NAG A1572     1555   1555  1.47
LINK         ND2 ASN A 481                 C1  NAG A1573     1555   1555  1.45
LINK        CA    CA A1001                 O   SER A 264     1555   1555  2.36
LINK        CA    CA A1001                 OG  SER A 264     1555   1555  2.66
LINK        CA    CA A1001                 O   VAL A 266     1555   1555  2.22
LINK        CA    CA A1001                 O   VAL A 296     1555   1555  2.43
LINK        CA    CA A1001                 OD1 ASP A 261     1555   1555  2.50
LINK        CA    CA A1001                 O   ASP A 261     1555   1555  2.46
LINK         ND2 ASN B 341                 C1  NAG B 841     1555   1555  1.46
LINK         ND2 ASN B 481                 C1  NAG B1571     1555   1555  1.45
LINK        CA    CA B1002                 O   VAL B 266     1555   1555  2.19
LINK        CA    CA B1002                 OD1 ASP B 261     1555   1555  2.42
LINK        CA    CA B1002                 O   VAL B 296     1555   1555  2.52
LINK        CA    CA B1002                 O   ASP B 261     1555   1555  2.58
LINK        CA    CA B1002                 O   SER B 264     1555   1555  2.48
LINK        CA    CA B1002                 OG  SER B 264     1555   1555  2.69
LINK         O4  NAG B1571                 C1  NAG B1572     1555   1555  1.38
CISPEP   1 ILE A  453    PRO A  454          0         0.25
CISPEP   2 ILE B  453    PRO B  454          0         0.08
SITE     1 AC1  4 ASP A 261  SER A 264  VAL A 266  VAL A 296
SITE     1 AC2  5 GLU B 256  ASP B 261  SER B 264  VAL B 266
SITE     2 AC2  5 VAL B 296
SITE     1 AC3 11 ARG A 174  GLU A 258  TYR A 299  TYR A 317
SITE     2 AC3 11 ARG A 363  GLU A 401  ARG A 416  ARG A 498
SITE     3 AC3 11 TYR A 526  HOH A2128  HOH A2129
SITE     1 AC4 11 ARG B 174  GLU B 258  TYR B 299  TYR B 317
SITE     2 AC4 11 GLU B 401  ARG B 416  ARG B 498  TYR B 526
SITE     3 AC4 11 HOH B2108  HOH B2109  HOH B2110
SITE     1 AC5  2 TYR A 340  ASN A 341
SITE     1 AC6  2 ASN A 481  THR A 483
SITE     1 AC7  2 TYR B 340  ASN B 341
SITE     1 AC8  3 TYR B 479  ASN B 481  THR B 483
CRYST1  137.460  137.460  116.600  90.00  90.00 120.00 P 61          6
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      0.007275  0.004200  0.000000        0.00000
SCALE2      0.000000  0.008400  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008576        0.00000
MTRIX1   1 -0.161500  0.986900  0.009000        0.02500    1
MTRIX2   1  0.986900  0.161500  0.005800       -0.33000    1
MTRIX3   1  0.005600  0.001900 -1.000000       35.34000    1
      
PROCHECK
Go to PROCHECK summary
 References