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PDBsum entry 1kit

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Hydrolase PDB id
1kit
Jmol
Contents
Protein chain
757 a.a.
Metals
_CA ×2
Waters ×699
HEADER    HYDROLASE                               21-JUN-96   1KIT
TITLE     VIBRIO CHOLERAE NEURAMINIDASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: NEURAMINIDASE;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE   3 ORGANISM_TAXID: 666;
SOURCE   4 STRAIN: CLASSICAL OGAWA 395;
SOURCE   5 GENE: NANH;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PCVD364;
SOURCE   9 EXPRESSION_SYSTEM_GENE: NANH
KEYWDS    HYDROLASE, GLYCOSIDASE, SIGNAL, REPEAT, CALCIUM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.L.TAYLOR,S.J.CRENNELL,E.F.GARMAN,E.R.VIMR,W.G.LAVER
REVDAT   2   24-FEB-09 1KIT    1       VERSN
REVDAT   1   05-JUN-97 1KIT    0
JRNL        AUTH   S.CRENNELL,E.GARMAN,G.LAVER,E.VIMR,G.TAYLOR
JRNL        TITL   CRYSTAL STRUCTURE OF VIBRIO CHOLERAE NEURAMINIDASE
JRNL        TITL 2 REVEALS DUAL LECTIN-LIKE DOMAINS IN ADDITION TO
JRNL        TITL 3 THE CATALYTIC DOMAIN.
JRNL        REF    STRUCTURE                     V.   2   535 1994
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   7922030
JRNL        DOI    10.1016/S0969-2126(00)00053-8
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   G.TAYLOR,E.VIMR,E.GARMAN,G.LAVER
REMARK   1  TITL   PURIFICATION, CRYSTALLIZATION AND PRELIMINARY
REMARK   1  TITL 2 CRYSTALLOGRAPHIC STUDY OF NEURAMINIDASE FROM
REMARK   1  TITL 3 VIBRIO CHOLERAE AND SALMONELLA TYPHIMURIUM LT2
REMARK   1  REF    J.MOL.BIOL.                   V. 226  1287 1992
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT V. 5-C
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0
REMARK   3   NUMBER OF REFLECTIONS             : 40555
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.170
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1700
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5859
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 699
REMARK   3
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT
REMARK   3   BOND LENGTHS                 (A) : 0.014 ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : 1.392 ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : 0.012 ; 5.000 ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : 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  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : NULL
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1KIT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 1993
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
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) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40491
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0
REMARK 200  DATA REDUNDANCY                : 9.150
REMARK 200  R MERGE                    (I) : 0.09800
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) : 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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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   (%): 56.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.15000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.25000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.45000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.25000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.15000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.45000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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    ASP A 637   N   -  CA  -  C   ANGL. DEV. =  17.9 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    THR A  35      -91.93    -72.73
REMARK 500    GLN A  43       34.24    -80.17
REMARK 500    ASN A  51      131.44      2.04
REMARK 500    ASN A  52      -29.73     74.08
REMARK 500    VAL A  56      148.01   -170.86
REMARK 500    ASN A  59       48.61   -143.36
REMARK 500    SER A 104      159.11    179.51
REMARK 500    ASN A 165       79.37   -108.49
REMARK 500    PRO A 166     -171.68    -67.05
REMARK 500    SER A 167      173.30    171.36
REMARK 500    ILE A 177      -64.73    -99.30
REMARK 500    ASN A 180       24.46     82.16
REMARK 500    MET A 190      169.95    170.07
REMARK 500    GLN A 214     -107.49    -36.43
REMARK 500    ILE A 225       47.62     74.59
REMARK 500    SER A 255       49.62   -102.57
REMARK 500    ASP A 273     -179.89    -68.49
REMARK 500    ASN A 283       73.26   -112.61
REMARK 500    ASP A 292       73.34     49.20
REMARK 500    ASN A 302       60.49     60.11
REMARK 500    ALA A 316     -152.92   -159.59
REMARK 500    PRO A 324      -12.12    -49.70
REMARK 500    PRO A 327       30.33    -78.53
REMARK 500    SER A 376       -4.60    -50.25
REMARK 500    GLU A 433      105.98    -57.78
REMARK 500    HIS A 434      -36.58    -35.58
REMARK 500    LEU A 450      -75.38    -27.06
REMARK 500    ASP A 459       70.84     54.66
REMARK 500    ILE A 463      -73.71    -98.95
REMARK 500    GLN A 499       75.42     30.14
REMARK 500    ARG A 577      -58.40   -160.90
REMARK 500    SER A 618     -103.35   -121.97
REMARK 500    SER A 648     -154.96    -53.45
REMARK 500    ASN A 669     -157.69   -137.62
REMARK 500    ALA A 683     -166.32   -119.82
REMARK 500    ASN A 701      151.20    178.11
REMARK 500    ALA A 707      116.22    -30.21
REMARK 500    ALA A 739     -116.97   -123.31
REMARK 500    SER A 748      -25.62    -36.22
REMARK 500    THR A 757     -113.10   -136.08
REMARK 500    SER A 760       -4.18     72.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 857        DISTANCE =  5.48 ANGSTROMS
REMARK 525    HOH A 858        DISTANCE =  6.22 ANGSTROMS
REMARK 525    HOH A1050        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH A1233        DISTANCE =  8.64 ANGSTROMS
REMARK 525    HOH A1319        DISTANCE =  6.50 ANGSTROMS
REMARK 525    HOH A1352        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH A1356        DISTANCE =  7.66 ANGSTROMS
REMARK 525    HOH A1359        DISTANCE =  6.90 ANGSTROMS
REMARK 525    HOH A1373        DISTANCE =  6.28 ANGSTROMS
REMARK 525    HOH A1405        DISTANCE =  5.49 ANGSTROMS
REMARK 525    HOH A1429        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH A1450        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH A1471        DISTANCE =  7.27 ANGSTROMS
REMARK 525    HOH A1511        DISTANCE =  9.08 ANGSTROMS
REMARK 525    HOH A1532        DISTANCE =  9.53 ANGSTROMS
REMARK 525    HOH A1536        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH A1539        DISTANCE =  8.64 ANGSTROMS
REMARK 525    HOH A1540        DISTANCE =  6.56 ANGSTROMS
REMARK 525    HOH A1543        DISTANCE =  7.27 ANGSTROMS
REMARK 525    HOH A1545        DISTANCE =  8.92 ANGSTROMS
REMARK 525    HOH A1546        DISTANCE =  7.93 ANGSTROMS
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 802  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 256   OD1
REMARK 620 2 ASP A 289   OD2  77.1
REMARK 620 3 THR A 313   OG1 145.2 114.3
REMARK 620 4 ALA A 253   O    86.0 126.0 108.7
REMARK 620 5 ASP A 289   OD1  80.0  48.7  84.3 165.8
REMARK 620 6 THR A 313   O   136.4  88.1  78.1  70.0 119.6
REMARK 620 7 ASN A 256   O    76.9 130.1  71.0  93.6  85.2 138.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 803  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 683   O
REMARK 620 2 ASP A 682   OD2  77.6
REMARK 620 3 ASP A 621   OD1  81.0 137.2
REMARK 620 4 ASP A 621   OD2  99.3 169.1  51.2
REMARK 620 5 HOH A 931   O    76.2  84.4 125.6  84.7
REMARK 620 6 ASP A 682   OD1  91.4  50.5  93.9 140.4 134.9
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE.
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 802
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 803
DBREF  1KIT A   25   781  UNP    P37060   NANH_VIBCH      25    781
SEQRES   1 A  757  ALA LEU PHE ASP TYR ASN ALA THR GLY ASP THR GLU PHE
SEQRES   2 A  757  ASP SER PRO ALA LYS GLN GLY TRP MET GLN ASP ASN THR
SEQRES   3 A  757  ASN ASN GLY SER GLY VAL LEU THR ASN ALA ASP GLY MET
SEQRES   4 A  757  PRO ALA TRP LEU VAL GLN GLY ILE GLY GLY ARG ALA GLN
SEQRES   5 A  757  TRP THR TYR SER LEU SER THR ASN GLN HIS ALA GLN ALA
SEQRES   6 A  757  SER SER PHE GLY TRP ARG MET THR THR GLU MET LYS VAL
SEQRES   7 A  757  LEU SER GLY GLY MET ILE THR ASN TYR TYR ALA ASN GLY
SEQRES   8 A  757  THR GLN ARG VAL LEU PRO ILE ILE SER LEU ASP SER SER
SEQRES   9 A  757  GLY ASN LEU VAL VAL GLU PHE GLU GLY GLN THR GLY ARG
SEQRES  10 A  757  THR VAL LEU ALA THR GLY THR ALA ALA THR GLU TYR HIS
SEQRES  11 A  757  LYS PHE GLU LEU VAL PHE LEU PRO GLY SER ASN PRO SER
SEQRES  12 A  757  ALA SER PHE TYR PHE ASP GLY LYS LEU ILE ARG ASP ASN
SEQRES  13 A  757  ILE GLN PRO THR ALA SER LYS GLN ASN MET ILE VAL TRP
SEQRES  14 A  757  GLY ASN GLY SER SER ASN THR ASP GLY VAL ALA ALA TYR
SEQRES  15 A  757  ARG ASP ILE LYS PHE GLU ILE GLN GLY ASP VAL ILE PHE
SEQRES  16 A  757  ARG GLY PRO ASP ARG ILE PRO SER ILE VAL ALA SER SER
SEQRES  17 A  757  VAL THR PRO GLY VAL VAL THR ALA PHE ALA GLU LYS ARG
SEQRES  18 A  757  VAL GLY GLY GLY ASP PRO GLY ALA LEU SER ASN THR ASN
SEQRES  19 A  757  ASP ILE ILE THR ARG THR SER ARG ASP GLY GLY ILE THR
SEQRES  20 A  757  TRP ASP THR GLU LEU ASN LEU THR GLU GLN ILE ASN VAL
SEQRES  21 A  757  SER ASP GLU PHE ASP PHE SER ASP PRO ARG PRO ILE TYR
SEQRES  22 A  757  ASP PRO SER SER ASN THR VAL LEU VAL SER TYR ALA ARG
SEQRES  23 A  757  TRP PRO THR ASP ALA ALA GLN ASN GLY ASP ARG ILE LYS
SEQRES  24 A  757  PRO TRP MET PRO ASN GLY ILE PHE TYR SER VAL TYR ASP
SEQRES  25 A  757  VAL ALA SER GLY ASN TRP GLN ALA PRO ILE ASP VAL THR
SEQRES  26 A  757  ASP GLN VAL LYS GLU ARG SER PHE GLN ILE ALA GLY TRP
SEQRES  27 A  757  GLY GLY SER GLU LEU TYR ARG ARG ASN THR SER LEU ASN
SEQRES  28 A  757  SER GLN GLN ASP TRP GLN SER ASN ALA LYS ILE ARG ILE
SEQRES  29 A  757  VAL ASP GLY ALA ALA ASN GLN ILE GLN VAL ALA ASP GLY
SEQRES  30 A  757  SER ARG LYS TYR VAL VAL THR LEU SER ILE ASP GLU SER
SEQRES  31 A  757  GLY GLY LEU VAL ALA ASN LEU ASN GLY VAL SER ALA PRO
SEQRES  32 A  757  ILE ILE LEU GLN SER GLU HIS ALA LYS VAL HIS SER PHE
SEQRES  33 A  757  HIS ASP TYR GLU LEU GLN TYR SER ALA LEU ASN HIS THR
SEQRES  34 A  757  THR THR LEU PHE VAL ASP GLY GLN GLN ILE THR THR TRP
SEQRES  35 A  757  ALA GLY GLU VAL SER GLN GLU ASN ASN ILE GLN PHE GLY
SEQRES  36 A  757  ASN ALA ASP ALA GLN ILE ASP GLY ARG LEU HIS VAL GLN
SEQRES  37 A  757  LYS ILE VAL LEU THR GLN GLN GLY HIS ASN LEU VAL GLU
SEQRES  38 A  757  PHE ASP ALA PHE TYR LEU ALA GLN GLN THR PRO GLU VAL
SEQRES  39 A  757  GLU LYS ASP LEU GLU LYS LEU GLY TRP THR LYS ILE LYS
SEQRES  40 A  757  THR GLY ASN THR MET SER LEU TYR GLY ASN ALA SER VAL
SEQRES  41 A  757  ASN PRO GLY PRO GLY HIS GLY ILE THR LEU THR ARG GLN
SEQRES  42 A  757  GLN ASN ILE SER GLY SER GLN ASN GLY ARG LEU ILE TYR
SEQRES  43 A  757  PRO ALA ILE VAL LEU ASP ARG PHE PHE LEU ASN VAL MET
SEQRES  44 A  757  SER ILE TYR SER ASP ASP GLY GLY SER ASN TRP GLN THR
SEQRES  45 A  757  GLY SER THR LEU PRO ILE PRO PHE ARG TRP LYS SER SER
SEQRES  46 A  757  SER ILE LEU GLU THR LEU GLU PRO SER GLU ALA ASP MET
SEQRES  47 A  757  VAL GLU LEU GLN ASN GLY ASP LEU LEU LEU THR ALA ARG
SEQRES  48 A  757  LEU ASP PHE ASN GLN ILE VAL ASN GLY VAL ASN TYR SER
SEQRES  49 A  757  PRO ARG GLN GLN PHE LEU SER LYS ASP GLY GLY ILE THR
SEQRES  50 A  757  TRP SER LEU LEU GLU ALA ASN ASN ALA ASN VAL PHE SER
SEQRES  51 A  757  ASN ILE SER THR GLY THR VAL ASP ALA SER ILE THR ARG
SEQRES  52 A  757  PHE GLU GLN SER ASP GLY SER HIS PHE LEU LEU PHE THR
SEQRES  53 A  757  ASN PRO GLN GLY ASN PRO ALA GLY THR ASN GLY ARG GLN
SEQRES  54 A  757  ASN LEU GLY LEU TRP PHE SER PHE ASP GLU GLY VAL THR
SEQRES  55 A  757  TRP LYS GLY PRO ILE GLN LEU VAL ASN GLY ALA SER ALA
SEQRES  56 A  757  TYR SER ASP ILE TYR GLN LEU ASP SER GLU ASN ALA ILE
SEQRES  57 A  757  VAL ILE VAL GLU THR ASP ASN SER ASN MET ARG ILE LEU
SEQRES  58 A  757  ARG MET PRO ILE THR LEU LEU LYS GLN LYS LEU THR LEU
SEQRES  59 A  757  SER GLN ASN
HET     CA  A 802       1
HET     CA  A 803       1
HETNAM      CA CALCIUM ION
FORMUL   2   CA    2(CA 2+)
FORMUL   4  HOH   *699(H2 O)
HELIX    1   1 ALA A   60  GLY A   62  5                                   3
HELIX    2   2 THR A   83  PHE A   92  1                                  10
HELIX    3   3 ASN A  318  ASP A  320  5                                   3
HELIX    4   4 THR A  349  VAL A  352  1                                   4
HELIX    5   5 HIS A  434  VAL A  437  1                                   4
HELIX    6   6 ALA A  508  ALA A  512  1                                   5
HELIX    7   7 LEU A  522  LEU A  525  1                                   4
HELIX    8   8 ALA A  670  VAL A  672  5                                   3
HELIX    9   9 ASP A  758  SER A  760  5                                   3
HELIX   10  10 ILE A  769  THR A  777  1                                   9
SHEET    1   A 6 LEU A  26  ASN A  30  0
SHEET    2   A 6 ALA A 204  ILE A 213 -1  N  PHE A 211   O  PHE A  27
SHEET    3   A 6 TRP A  94  VAL A 102 -1  N  LYS A 101   O  ALA A 205
SHEET    4   A 6 HIS A 154  LEU A 161 -1  N  PHE A 160   O  TRP A  94
SHEET    5   A 6 SER A 167  PHE A 172 -1  N  TYR A 171   O  GLU A 157
SHEET    6   A 6 ARG A 178  ILE A 181 -1  N  ILE A 181   O  ALA A 168
SHEET    1   B 3 SER A  54  ALA A  60  0
SHEET    2   B 3 MET A  63  GLY A  70 -1  N  GLN A  69   O  SER A  54
SHEET    3   B 3 GLY A 202  TYR A 206 -1  N  TYR A 206   O  TRP A  66
SHEET    1   C 4 ALA A  75  TYR A  79  0
SHEET    2   C 4 MET A 190  ASN A 195 -1  N  ASN A 195   O  ALA A  75
SHEET    3   C 4 TYR A 111  ASN A 114 -1  N  ALA A 113   O  MET A 190
SHEET    4   C 4 GLN A 117  VAL A 119 -1  N  VAL A 119   O  TYR A 112
SHEET    1   D 3 PRO A 121  LEU A 125  0
SHEET    2   D 3 LEU A 131  PHE A 135 -1  N  GLU A 134   O  ILE A 122
SHEET    3   D 3 ARG A 141  ALA A 145 -1  N  ALA A 145   O  LEU A 131
SHEET    1   E 3 SER A 227  ALA A 230  0
SHEET    2   E 3 VAL A 238  VAL A 246 -1  N  PHE A 241   O  SER A 227
SHEET    3   E 3 THR A 257  SER A 265 -1  N  SER A 265   O  VAL A 238
SHEET    1   F 4 PHE A 288  SER A 291  0
SHEET    2   F 4 THR A 303  PRO A 312 -1  N  TRP A 311   O  ASP A 289
SHEET    3   F 4 GLY A 329  ASP A 336 -1  N  TYR A 335   O  VAL A 304
SHEET    4   F 4 ASN A 341  GLN A 343 -1  N  GLN A 343   O  VAL A 334
SHEET    1   G 2 ARG A 294  ASP A 298  0
SHEET    2   G 2 THR A 303  SER A 307 -1  N  SER A 307   O  ARG A 294
SHEET    1   H 6 MET A 536  TYR A 539  0
SHEET    2   H 6 PHE A 357  ALA A 360 -1  N  ALA A 360   O  MET A 536
SHEET    3   H 6 ARG A 488  GLN A 498 -1  N  VAL A 491   O  PHE A 357
SHEET    4   H 6 TRP A 380  ILE A 388 -1  N  ARG A 387   O  HIS A 490
SHEET    5   H 6 HIS A 441  SER A 448 -1  N  TYR A 447   O  TRP A 380
SHEET    6   H 6 THR A 453  VAL A 458 -1  N  PHE A 457   O  GLU A 444
SHEET    1   I 7 THR A 528  GLY A 533  0
SHEET    2   I 7 GLY A 364  ASN A 371 -1  N  ARG A 369   O  THR A 528
SHEET    3   I 7 ASN A 474  ASN A 480 -1  N  ASN A 480   O  GLU A 366
SHEET    4   I 7 ASN A 394  ASP A 400 -1  N  ALA A 399   O  ASN A 475
SHEET    5   I 7 LYS A 404  ILE A 411 -1  N  LEU A 409   O  ASN A 394
SHEET    6   I 7 LEU A 417  LEU A 421 -1  N  ASN A 420   O  THR A 408
SHEET    7   I 7 ILE A 428  GLN A 431 -1  N  GLN A 431   O  LEU A 417
SHEET    1   J 3 SER A 543  ASN A 545  0
SHEET    2   J 3 LEU A 568  LEU A 575 -1  N  LEU A 575   O  SER A 543
SHEET    3   J 3 LEU A 580  SER A 587 -1  N  SER A 587   O  LEU A 568
SHEET    1   K 3 ALA A 620  GLU A 624  0
SHEET    2   K 3 LEU A 630  ARG A 635 -1  N  THR A 633   O  ASP A 621
SHEET    3   K 3 ARG A 650  SER A 655 -1  N  SER A 655   O  LEU A 630
SHEET    1   L 3 SER A 684  GLU A 689  0
SHEET    2   L 3 HIS A 695  ASN A 701 -1  N  THR A 700   O  SER A 684
SHEET    3   L 3 GLY A 716  SER A 720 -1  N  SER A 720   O  LEU A 697
SHEET    1   M 4 ASP A 216  PHE A 219  0
SHEET    2   M 4 MET A 762  PRO A 768 -1  N  ILE A 764   O  ASP A 216
SHEET    3   M 4 ASN A 750  GLU A 756 -1  N  VAL A 755   O  ARG A 763
SHEET    4   M 4 SER A 741  ASP A 747 -1  N  ASP A 747   O  ASN A 750
SHEET    1   N 2 LYS A 493  GLN A 498  0
SHEET    2   N 2 HIS A 501  ASP A 507 -1  N  PHE A 506   O  ILE A 494
SHEET    1   O 2 ARG A 605  SER A 608  0
SHEET    2   O 2 ILE A 611  GLU A 613 -1  N  GLU A 613   O  ARG A 605
LINK        CA    CA A 802                 OD1 ASN A 256     1555   1555  2.18
LINK        CA    CA A 802                 OD2 ASP A 289     1555   1555  2.34
LINK        CA    CA A 802                 OG1 THR A 313     1555   1555  2.25
LINK        CA    CA A 803                 O   ALA A 683     1555   1555  2.40
LINK        CA    CA A 802                 O   ALA A 253     1555   1555  2.40
LINK        CA    CA A 802                 OD1 ASP A 289     1555   1555  2.82
LINK        CA    CA A 802                 O   THR A 313     1555   1555  2.48
LINK        CA    CA A 802                 O   ASN A 256     1555   1555  2.51
LINK        CA    CA A 803                 OD2 ASP A 682     1555   1555  2.51
LINK        CA    CA A 803                 OD1 ASP A 621     1555   1555  2.50
LINK        CA    CA A 803                 OD2 ASP A 621     1555   1555  2.56
LINK        CA    CA A 803                 O   HOH A 931     1555   1555  2.65
LINK        CA    CA A 803                 OD1 ASP A 682     1555   1555  2.61
CISPEP   1 GLY A  221    PRO A  222          0         4.67
SITE     1 ACT 12 ARG A 224  ARG A 245  ASP A 250  ASP A 292
SITE     2 ACT 12 TRP A 311  ASN A 318  GLU A 619  ARG A 635
SITE     3 ACT 12 ASP A 637  ARG A 712  TYR A 740  GLU A 756
SITE     1 AC1  4 ALA A 253  ASN A 256  ASP A 289  THR A 313
SITE     1 AC2  5 GLY A 549  ASP A 621  ASP A 682  ALA A 683
SITE     2 AC2  5 HOH A 931
CRYST1   72.300   78.900  164.500  90.00  90.00  90.00 P 21 21 21    4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013831  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012674  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006079        0.00000
      
PROCHECK
Go to PROCHECK summary
 References