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PDBsum entry 1z50

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Hydrolase PDB id
1z50
Jmol
Contents
Protein chain
448 a.a.
Ligands
NDG
NAG-NAG ×2
DAN
Metals
_CA
Waters ×196
HEADER    HYDROLASE                               16-MAR-05   1Z50
TITLE     PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ-NEURAMINIDASE (HN) WITH
TITLE    2 LIGAND DANA (SOAKED WITH SIALIC ACID, PH 8.0)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HEMAGGLUTININ-NEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SIMIAN VIRUS 5;
SOURCE   3 ORGANISM_TAXID: 11207;
SOURCE   4 STRAIN: W3;
SOURCE   5 GENE: HN;
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PBACGUS-3
KEYWDS    HEMAGGLUTININ,NEURAMINIDASE,FUSION,TETRAMER, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.YUAN,T.B.THOMPSON,B.A.WURZBURG,R.G.PATERSON,R.A.LAMB,T.S.JARDETZKY
REVDAT   3   13-JUL-11 1Z50    1       VERSN
REVDAT   2   24-FEB-09 1Z50    1       VERSN
REVDAT   1   24-MAY-05 1Z50    0
JRNL        AUTH   P.YUAN,T.B.THOMPSON,B.A.WURZBURG,R.G.PATERSON,R.A.LAMB,
JRNL        AUTH 2 T.S.JARDETZKY
JRNL        TITL   STRUCTURAL STUDIES OF THE PARAINFLUENZA VIRUS 5
JRNL        TITL 2 HEMAGGLUTININ-NEURAMINIDASE TETRAMER IN COMPLEX WITH ITS
JRNL        TITL 3 RECEPTOR, SIALYLLACTOSE.
JRNL        REF    STRUCTURE                     V.  13   803 2005
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   15893670
JRNL        DOI    10.1016/J.STR.2005.02.019
REMARK   2
REMARK   2 RESOLUTION.    2.80 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) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 26093
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.199
REMARK   3   FREE R VALUE                     : 0.224
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 725
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            : 3492
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 91
REMARK   3   SOLVENT ATOMS            : 196
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.60
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.74100
REMARK   3    B22 (A**2) : -2.74100
REMARK   3    B33 (A**2) : 5.48100
REMARK   3    B12 (A**2) : -3.50500
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
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) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 33.54
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  : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:CARBOHYDRATE.PARAM
REMARK   3  PARAMETER FILE  3  : DAN_XPLOR_PAR.TXT
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:WATER.PARAM
REMARK   3  PARAMETER FILE  5  : CNS_TOPPAR:ION.PARAM
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1Z50 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-05.
REMARK 100 THE RCSB ID CODE IS RCSB032305.
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
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 32-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9918
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26160
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.11900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.39400
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: PDB ENTRY 1E8T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 71.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000 MME, NACL, TRIS, PH 8.0,
REMARK 280  HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
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       7555   Y,X,-Z+1/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+2/3
REMARK 290      10555   -Y,-X,-Z+5/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-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       61.63900
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      123.27800
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       92.45850
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      154.09750
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       30.81950
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       61.63900
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      123.27800
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      154.09750
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       92.45850
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       30.81950
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2  0.500000 -0.866025  0.000000       68.83050
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000     -119.21792
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000       30.81950
REMARK 350   BIOMT1   3 -0.500000 -0.866025  0.000000      206.49150
REMARK 350   BIOMT2   3 -0.866025  0.500000  0.000000      119.21792
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000     -246.55600
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000      275.32200
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000     -277.37550
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      275.32200
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000     -277.37550
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     SER A    34
REMARK 465     PRO A    35
REMARK 465     SER A    36
REMARK 465     GLU A    37
REMARK 465     SER A    38
REMARK 465     LEU A    39
REMARK 465     ILE A    40
REMARK 465     THR A    41
REMARK 465     GLN A    42
REMARK 465     LYS A    43
REMARK 465     GLN A    44
REMARK 465     ILE A    45
REMARK 465     MET A    46
REMARK 465     SER A    47
REMARK 465     GLN A    48
REMARK 465     ALA A    49
REMARK 465     GLY A    50
REMARK 465     SER A    51
REMARK 465     THR A    52
REMARK 465     GLY A    53
REMARK 465     SER A    54
REMARK 465     ASN A    55
REMARK 465     SER A    56
REMARK 465     GLY A    57
REMARK 465     LEU A    58
REMARK 465     GLY A    59
REMARK 465     SER A    60
REMARK 465     ILE A    61
REMARK 465     THR A    62
REMARK 465     ASP A    63
REMARK 465     LEU A    64
REMARK 465     LEU A    65
REMARK 465     ASN A    66
REMARK 465     ASN A    67
REMARK 465     ILE A    68
REMARK 465     LEU A    69
REMARK 465     SER A    70
REMARK 465     VAL A    71
REMARK 465     ALA A    72
REMARK 465     ASN A    73
REMARK 465     GLN A    74
REMARK 465     ILE A    75
REMARK 465     ILE A    76
REMARK 465     TYR A    77
REMARK 465     ASN A    78
REMARK 465     SER A    79
REMARK 465     ALA A    80
REMARK 465     VAL A    81
REMARK 465     ALA A    82
REMARK 465     LEU A    83
REMARK 465     PRO A    84
REMARK 465     LEU A    85
REMARK 465     GLN A    86
REMARK 465     LEU A    87
REMARK 465     ASP A    88
REMARK 465     THR A    89
REMARK 465     LEU A    90
REMARK 465     GLU A    91
REMARK 465     SER A    92
REMARK 465     THR A    93
REMARK 465     LEU A    94
REMARK 465     LEU A    95
REMARK 465     THR A    96
REMARK 465     ALA A    97
REMARK 465     ILE A    98
REMARK 465     LYS A    99
REMARK 465     SER A   100
REMARK 465     LEU A   101
REMARK 465     GLN A   102
REMARK 465     THR A   103
REMARK 465     SER A   104
REMARK 465     ASP A   105
REMARK 465     LYS A   106
REMARK 465     LEU A   107
REMARK 465     GLU A   108
REMARK 465     GLN A   109
REMARK 465     ASN A   110
REMARK 465     CYS A   111
REMARK 465     SER A   112
REMARK 465     TRP A   113
REMARK 465     SER A   114
REMARK 465     ALA A   115
REMARK 465     ALA A   116
REMARK 465     LEU A   117
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 164       72.83     58.69
REMARK 500    ASP A 187      124.40   -174.96
REMARK 500    VAL A 189      -47.57   -130.69
REMARK 500    ASP A 220        9.08   -150.29
REMARK 500    THR A 291      -26.29     68.62
REMARK 500    PHE A 353       66.37   -104.57
REMARK 500    THR A 372      -73.08   -141.77
REMARK 500    SER A 408     -150.67   -111.26
REMARK 500    VAL A 440       92.00     73.39
REMARK 500    ARG A 453       -3.96   -145.01
REMARK 500    LEU A 459       62.05   -151.95
REMARK 500    ALA A 464       84.91   -154.96
REMARK 500    PHE A 478      122.65    -39.15
REMARK 500    SER A 510      135.71   -170.29
REMARK 500    ALA A 522     -112.21   -136.71
REMARK 500    LEU A 549      -76.26    -84.55
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 A 600  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 250   O
REMARK 620 2 SER A 253   OG   89.0
REMARK 620 3 ALA A 255   O   171.0  85.8
REMARK 620 4 HOH A 640   O   103.1  67.5  68.1
REMARK 620 5 ALA A 285   O    96.4 172.8  89.5 115.6
REMARK 620 6 SER A 253   O    88.4  75.9  97.4 141.2  99.3
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 NDG A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z4V   RELATED DB: PDB
REMARK 900 RELATED ID: 1Z4X   RELATED DB: PDB
REMARK 900 RELATED ID: 1Z4W   RELATED DB: PDB
REMARK 900 RELATED ID: 1Z4Z   RELATED DB: PDB
REMARK 900 RELATED ID: 1Z4Y   RELATED DB: PDB
DBREF  1Z50 A   37   565  UNP    P04850   HEMA_SV5        37    565
SEQADV 1Z50 SER A   34  UNP  P04850              CLONING ARTIFACT
SEQADV 1Z50 PRO A   35  UNP  P04850              CLONING ARTIFACT
SEQADV 1Z50 SER A   36  UNP  P04850              CLONING ARTIFACT
SEQRES   1 A  532  SER PRO SER GLU SER LEU ILE THR GLN LYS GLN ILE MET
SEQRES   2 A  532  SER GLN ALA GLY SER THR GLY SER ASN SER GLY LEU GLY
SEQRES   3 A  532  SER ILE THR ASP LEU LEU ASN ASN ILE LEU SER VAL ALA
SEQRES   4 A  532  ASN GLN ILE ILE TYR ASN SER ALA VAL ALA LEU PRO LEU
SEQRES   5 A  532  GLN LEU ASP THR LEU GLU SER THR LEU LEU THR ALA ILE
SEQRES   6 A  532  LYS SER LEU GLN THR SER ASP LYS LEU GLU GLN ASN CYS
SEQRES   7 A  532  SER TRP SER ALA ALA LEU ILE ASN ASP ASN ARG TYR ILE
SEQRES   8 A  532  ASN GLY ILE ASN GLN PHE TYR PHE SER ILE ALA GLU GLY
SEQRES   9 A  532  ARG ASN LEU THR LEU GLY PRO LEU LEU ASN MET PRO SER
SEQRES  10 A  532  PHE ILE PRO THR ALA THR THR PRO GLU GLY CYS THR ARG
SEQRES  11 A  532  ILE PRO SER PHE SER LEU THR LYS THR HIS TRP CYS TYR
SEQRES  12 A  532  THR HIS ASN VAL ILE LEU ASN GLY CYS GLN ASP HIS VAL
SEQRES  13 A  532  SER SER ASN GLN PHE VAL SER MET GLY ILE ILE GLU PRO
SEQRES  14 A  532  THR SER ALA GLY PHE PRO PHE PHE ARG THR LEU LYS THR
SEQRES  15 A  532  LEU TYR LEU SER ASP GLY VAL ASN ARG LYS SER CYS SER
SEQRES  16 A  532  ILE SER THR VAL PRO GLY GLY CYS MET MET TYR CYS PHE
SEQRES  17 A  532  VAL SER THR GLN PRO GLU ARG ASP ASP TYR PHE SER ALA
SEQRES  18 A  532  ALA PRO PRO GLU GLN ARG ILE ILE ILE MET TYR TYR ASN
SEQRES  19 A  532  ASP THR ILE VAL GLU ARG ILE ILE ASN PRO PRO GLY VAL
SEQRES  20 A  532  LEU ASP VAL TRP ALA THR LEU ASN PRO GLY THR GLY SER
SEQRES  21 A  532  GLY VAL TYR TYR LEU GLY TRP VAL LEU PHE PRO ILE TYR
SEQRES  22 A  532  GLY GLY VAL ILE LYS GLY THR SER LEU TRP ASN ASN GLN
SEQRES  23 A  532  ALA ASN LYS TYR PHE ILE PRO GLN MET VAL ALA ALA LEU
SEQRES  24 A  532  CYS SER GLN ASN GLN ALA THR GLN VAL GLN ASN ALA LYS
SEQRES  25 A  532  SER SER TYR TYR SER SER TRP PHE GLY ASN ARG MET ILE
SEQRES  26 A  532  GLN SER GLY ILE LEU ALA CYS PRO LEU ARG GLN ASP LEU
SEQRES  27 A  532  THR ASN GLU CYS LEU VAL LEU PRO PHE SER ASN ASP GLN
SEQRES  28 A  532  VAL LEU MET GLY ALA GLU GLY ARG LEU TYR MET TYR GLY
SEQRES  29 A  532  ASP SER VAL TYR TYR TYR GLN ARG SER ASN SER TRP TRP
SEQRES  30 A  532  PRO MET THR MET LEU TYR LYS VAL THR ILE THR PHE THR
SEQRES  31 A  532  ASN GLY GLN PRO SER ALA ILE SER ALA GLN ASN VAL PRO
SEQRES  32 A  532  THR GLN GLN VAL PRO ARG PRO GLY THR GLY ASP CYS SER
SEQRES  33 A  532  ALA THR ASN ARG CYS PRO GLY PHE CYS LEU THR GLY VAL
SEQRES  34 A  532  TYR ALA ASP ALA TRP LEU LEU THR ASN PRO SER SER THR
SEQRES  35 A  532  SER THR PHE GLY SER GLU ALA THR PHE THR GLY SER TYR
SEQRES  36 A  532  LEU ASN THR ALA THR GLN ARG ILE ASN PRO THR MET TYR
SEQRES  37 A  532  ILE ALA ASN ASN THR GLN ILE ILE SER SER GLN GLN PHE
SEQRES  38 A  532  GLY SER SER GLY GLN GLU ALA ALA TYR GLY HIS THR THR
SEQRES  39 A  532  CYS PHE ARG ASP THR GLY SER VAL MET VAL TYR CYS ILE
SEQRES  40 A  532  TYR ILE ILE GLU LEU SER SER SER LEU LEU GLY GLN PHE
SEQRES  41 A  532  GLN ILE VAL PRO PHE ILE ARG GLN VAL THR LEU SER
MODRES 1Z50 ASN A  139  ASN  GLYCOSYLATION SITE
MODRES 1Z50 ASN A  267  ASN  GLYCOSYLATION SITE
MODRES 1Z50 ASN A  504  ASN  GLYCOSYLATION SITE
HET    NDG  A   1      14
HET    NAG  A   2      14
HET    NAG  A   3      14
HET    NAG  A   4      14
HET    NAG  A   5      14
HET     CA  A 600       1
HET    DAN  A 601      20
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      CA CALCIUM ION
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
FORMUL   2  NDG    C8 H15 N O6
FORMUL   3  NAG    4(C8 H15 N O6)
FORMUL   5   CA    CA 2+
FORMUL   6  DAN    C11 H17 N O8
FORMUL   7  HOH   *196(H2 O)
HELIX    1   1 SER A  133  ARG A  138  1                                   6
HELIX    2   2 PRO A  246  SER A  253  1                                   8
HELIX    3   3 THR A  313  ALA A  320  1                                   8
HELIX    4   4 VAL A  329  CYS A  333  5                                   5
HELIX    5   5 ASN A  336  SER A  347  1                                  12
HELIX    6   6 THR A  445  SER A  449  5                                   5
HELIX    7   7 ASN A  471  THR A  475  5                                   5
SHEET    1   A 4 LEU A 140  LEU A 146  0
SHEET    2   A 4 PHE A 553  LEU A 564 -1  O  GLN A 561   N  GLY A 143
SHEET    3   A 4 MET A 536  SER A 546 -1  N  TYR A 541   O  PHE A 558
SHEET    4   A 4 ALA A 521  ASP A 531 -1  N  THR A 527   O  ILE A 540
SHEET    1   B 4 CYS A 161  LEU A 169  0
SHEET    2   B 4 TRP A 174  ILE A 181 -1  O  ILE A 181   N  CYS A 161
SHEET    3   B 4 ASN A 192  PRO A 202 -1  O  ASN A 192   N  VAL A 180
SHEET    4   B 4 PRO A 208  LEU A 218 -1  O  LEU A 216   N  VAL A 195
SHEET    1   C 4 ARG A 224  VAL A 232  0
SHEET    2   C 4 GLY A 235  VAL A 242 -1  O  TYR A 239   N  SER A 228
SHEET    3   C 4 GLU A 258  TYR A 265 -1  O  ILE A 262   N  MET A 238
SHEET    4   C 4 ILE A 270  ILE A 275 -1  O  VAL A 271   N  ILE A 263
SHEET    1   D 4 TRP A 284  PRO A 289  0
SHEET    2   D 4 TRP A 300  VAL A 309 -1  O  TYR A 306   N  ASN A 288
SHEET    3   D 4 ARG A 356  PRO A 366 -1  O  CYS A 365   N  VAL A 301
SHEET    4   D 4 TYR A 349  SER A 350 -1  N  SER A 350   O  ARG A 356
SHEET    1   E 4 VAL A 295  TYR A 297  0
SHEET    2   E 4 TRP A 300  VAL A 309 -1  O  LEU A 302   N  VAL A 295
SHEET    3   E 4 ARG A 356  PRO A 366 -1  O  CYS A 365   N  VAL A 301
SHEET    4   E 4 LEU A 376  PRO A 379 -1  O  LEU A 378   N  ILE A 362
SHEET    1   F 4 GLY A 391  TYR A 396  0
SHEET    2   F 4 SER A 399  GLN A 404 -1  O  TYR A 403   N  ARG A 392
SHEET    3   F 4 MET A 414  PHE A 422 -1  O  TYR A 416   N  TYR A 402
SHEET    4   F 4 PRO A 427  ASN A 434 -1  O  SER A 428   N  THR A 421
SHEET    1   G 4 ALA A 466  LEU A 468  0
SHEET    2   G 4 THR A 483  LEU A 489 -1  O  THR A 485   N  TRP A 467
SHEET    3   G 4 PRO A 498  ASN A 504 -1  O  ALA A 503   N  PHE A 484
SHEET    4   G 4 ILE A 508  GLN A 513 -1  O  GLN A 512   N  MET A 500
SSBOND   1 CYS A  161    CYS A  185                          1555   1555  2.04
SSBOND   2 CYS A  175    CYS A  236                          1555   1555  2.04
SSBOND   3 CYS A  227    CYS A  240                          1555   1555  2.05
SSBOND   4 CYS A  365    CYS A  375                          1555   1555  2.05
SSBOND   5 CYS A  448    CYS A  458                          1555   1555  2.04
SSBOND   6 CYS A  528    CYS A  539                          1555   1555  2.04
LINK         ND2 ASN A 139                 C1  NDG A   1     1555   1555  1.45
LINK         ND2 ASN A 267                 C1  NAG A   2     1555   1555  1.46
LINK         ND2 ASN A 504                 C1  NAG A   4     1555   1555  1.46
LINK         O4  NAG A   2                 C1  NAG A   3     1555   1555  1.40
LINK         O4  NAG A   4                 C1  NAG A   5     1555   1555  1.39
LINK        CA    CA A 600                 O   ASP A 250     1555   1555  2.25
LINK        CA    CA A 600                 OG  SER A 253     1555   1555  2.33
LINK        CA    CA A 600                 O   ALA A 255     1555   1555  2.30
LINK        CA    CA A 600                 O   HOH A 640     1555   1555  3.34
LINK        CA    CA A 600                 O   ALA A 285     1555   1555  2.18
LINK        CA    CA A 600                 O   SER A 253     1555   1555  2.49
SITE     1 AC1  2 ASN A 139  LEU A 564
SITE     1 AC2  4 NAG A   3  ASN A 267  THR A 269  GLN A 369
SITE     1 AC3  2 NAG A   2  GLN A 369
SITE     1 AC4  6 NAG A   5  ASN A 504  ASN A 505  THR A 506
SITE     2 AC4  6 GLN A 507  ILE A 509
SITE     1 AC5  2 NAG A   4  GLN A 507
SITE     1 AC6  4 ASP A 250  SER A 253  ALA A 255  ALA A 285
SITE     1 AC7 11 ARG A 163  GLU A 247  ASN A 288  TYR A 306
SITE     2 AC7 11 GLU A 390  ARG A 405  ARG A 495  TYR A 523
SITE     3 AC7 11 HOH A 616  HOH A 644  HOH A 737
CRYST1  137.661  137.661  184.917  90.00  90.00 120.00 P 61 2 2     12
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      0.007264  0.004194  0.000000        0.00000
SCALE2      0.000000  0.008388  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005408        0.00000
      
PROCHECK
Go to PROCHECK summary
 References