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PDBsum entry 1eut

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Hydrolase PDB id
1eut
Jmol
Contents
Protein chain
601 a.a.
Metals
_NA
HEADER    HYDROLASE                               21-JUN-96   1EUT
TITLE     SIALIDASE, LARGE 68KD FORM, COMPLEXED WITH GALACTOSE
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 OTHER_DETAILS: LARGE 68KD FORM
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MICROMONOSPORA VIRIDIFACIENS;
SOURCE   3 ORGANISM_TAXID: 1881;
SOURCE   4 ATCC: 31146
KEYWDS    HYDROLASE, GLYCOSIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.GASKELL,S.J.CRENNELL,G.L.TAYLOR
REVDAT   2   24-FEB-09 1EUT    1       VERSN
REVDAT   1   11-JAN-97 1EUT    0
JRNL        AUTH   A.GASKELL,S.CRENNELL,G.TAYLOR
JRNL        TITL   THE THREE DOMAINS OF A BACTERIAL SIALIDASE: A
JRNL        TITL 2 BETA-PROPELLER, AN IMMUNOGLOBULIN MODULE AND A
JRNL        TITL 3 GALACTOSE-BINDING JELLY-ROLL.
JRNL        REF    STRUCTURE                     V.   3  1197 1995
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   8591030
JRNL        DOI    10.1016/S0969-2126(01)00255-6
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   G.TAYLOR,L.DINELEY,M.GLOWKA,G.LAVER
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC
REMARK   1  TITL 2 STUDY OF NEURAMINIDASE FROM MICROMONOSPORA
REMARK   1  TITL 3 VIRIDIFACIENS
REMARK   1  REF    J.MOL.BIOL.                   V. 225  1135 1992
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
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)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 18632
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) : 0.214
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   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            : 4536
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.70
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) : 0.25
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) : 0.016
REMARK   3   BOND ANGLES            (DEGREES) : 2.57
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  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  : PARAM19X.PRO
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1EUT 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        : MAY-95
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
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                       : X11
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.993
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   : 20112
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     (%) : 79.2
REMARK 200  DATA REDUNDANCY                : 2.500
REMARK 200  R MERGE                    (I) : 0.03900
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: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       58.65000
REMARK 290   SMTRY3   2  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 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    43
REMARK 465     PRO A    44
REMARK 465     PRO A    45
REMARK 465     GLY A    46
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    GLY A  86   N   -  CA  -  C   ANGL. DEV. = -16.1 DEGREES
REMARK 500    GLY A 478   N   -  CA  -  C   ANGL. DEV. =  20.7 DEGREES
REMARK 500    ALA A 526   N   -  CA  -  C   ANGL. DEV. = -18.0 DEGREES
REMARK 500    TYR A 550   N   -  CA  -  C   ANGL. DEV. =  22.4 DEGREES
REMARK 500    PRO A 551   C   -  N   -  CA  ANGL. DEV. = -13.5 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    TYR A  51      109.56   -169.98
REMARK 500    ILE A  69       75.56     57.07
REMARK 500    ASP A  92     -155.92    -83.53
REMARK 500    PRO A  96       42.56    -60.70
REMARK 500    ASP A 131       75.94     55.75
REMARK 500    GLN A 151      -81.89   -129.86
REMARK 500    THR A 194       66.02   -119.92
REMARK 500    TRP A 199       91.16    -66.31
REMARK 500    ASP A 259     -163.13   -177.75
REMARK 500    GLU A 260      116.17    -37.99
REMARK 500    ARG A 280       73.01     29.81
REMARK 500    HIS A 294      114.68      3.54
REMARK 500    LEU A 305       74.28   -112.54
REMARK 500    THR A 309       72.09     69.71
REMARK 500    ASN A 335     -177.55   -174.09
REMARK 500    SER A 369      -98.82   -106.21
REMARK 500    ILE A 404      111.91     30.90
REMARK 500    SER A 431     -114.29    -38.14
REMARK 500    PRO A 459      124.81    -39.46
REMARK 500    ARG A 479       76.00     62.45
REMARK 500    THR A 519       13.40   -140.95
REMARK 500    ALA A 520      -63.86   -105.96
REMARK 500    SER A 527      -15.93    141.85
REMARK 500    GLU A 541      100.53    -44.86
REMARK 500    SER A 543      174.57    -33.74
REMARK 500    ALA A 545      102.79    140.47
REMARK 500    SER A 565       27.76   -141.28
REMARK 500    ASN A 574       45.34   -109.08
REMARK 500    SER A 575      136.85   -171.52
REMARK 500    ALA A 581      -90.56   -113.28
REMARK 500    ALA A 616      144.53    -36.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR A 381         0.07    SIDE_CHAIN
REMARK 500    TYR A 393         0.07    SIDE_CHAIN
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                              NA A   1  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 528   O
REMARK 620 2 ASN A 533   O   157.6
REMARK 620 3 THR A 536   O   115.4  86.8
REMARK 620 4 THR A 536   OG1 102.3  82.1  83.4
REMARK 620 5 ALA A 639   O    78.7 105.7  75.9 157.2
REMARK 620 6 GLU A 640   OE2  78.4  81.4 145.5 126.4  76.3
REMARK 620 7 ASP A 531   OD1  71.9  89.1 155.0  71.7 128.8  57.5
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE. SITE INCLUDES TWO CONTACTS WITH
REMARK 800  SYMMETRY-RELATED MOLECULES.
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1
DBREF  1EUT A   43   647  UNP    Q02834   NANH_MICVI      43    647
SEQRES   1 A  605  VAL PRO PRO GLY GLY GLU PRO LEU TYR THR GLU GLN ASP
SEQRES   2 A  605  LEU ALA VAL ASN GLY ARG GLU GLY PHE PRO ASN TYR ARG
SEQRES   3 A  605  ILE PRO ALA LEU THR VAL THR PRO ASP GLY ASP LEU LEU
SEQRES   4 A  605  ALA SER TYR ASP GLY ARG PRO THR GLY ILE ASP ALA PRO
SEQRES   5 A  605  GLY PRO ASN SER ILE LEU GLN ARG ARG SER THR ASP GLY
SEQRES   6 A  605  GLY ARG THR TRP GLY GLU GLN GLN VAL VAL SER ALA GLY
SEQRES   7 A  605  GLN THR THR ALA PRO ILE LYS GLY PHE SER ASP PRO SER
SEQRES   8 A  605  TYR LEU VAL ASP ARG GLU THR GLY THR ILE PHE ASN PHE
SEQRES   9 A  605  HIS VAL TYR SER GLN ARG GLN GLY PHE ALA GLY SER ARG
SEQRES  10 A  605  PRO GLY THR ASP PRO ALA ASP PRO ASN VAL LEU HIS ALA
SEQRES  11 A  605  ASN VAL ALA THR SER THR ASP GLY GLY LEU THR TRP SER
SEQRES  12 A  605  HIS ARG THR ILE THR ALA ASP ILE THR PRO ASP PRO GLY
SEQRES  13 A  605  TRP ARG SER ARG PHE ALA ALA SER GLY GLU GLY ILE GLN
SEQRES  14 A  605  LEU ARG TYR GLY PRO HIS ALA GLY ARG LEU ILE GLN GLN
SEQRES  15 A  605  TYR THR ILE ILE ASN ALA ALA GLY ALA PHE GLN ALA VAL
SEQRES  16 A  605  SER VAL TYR SER ASP ASP HIS GLY ARG THR TRP ARG ALA
SEQRES  17 A  605  GLY GLU ALA VAL GLY VAL GLY MET ASP GLU ASN LYS THR
SEQRES  18 A  605  VAL GLU LEU SER ASP GLY ARG VAL LEU LEU ASN SER ARG
SEQRES  19 A  605  ASP SER ALA ARG SER GLY TYR ARG LYS VAL ALA VAL SER
SEQRES  20 A  605  THR ASP GLY GLY HIS SER TYR GLY PRO VAL THR ILE ASP
SEQRES  21 A  605  ARG ASP LEU PRO ASP PRO THR ASN ASN ALA SER ILE ILE
SEQRES  22 A  605  ARG ALA PHE PRO ASP ALA PRO ALA GLY SER ALA ARG ALA
SEQRES  23 A  605  LYS VAL LEU LEU PHE SER ASN ALA ALA SER GLN THR SER
SEQRES  24 A  605  ARG SER GLN GLY THR ILE ARG MET SER CYS ASP ASP GLY
SEQRES  25 A  605  GLN THR TRP PRO VAL SER LYS VAL PHE GLN PRO GLY SER
SEQRES  26 A  605  MET SER TYR SER THR LEU THR ALA LEU PRO ASP GLY THR
SEQRES  27 A  605  TYR GLY LEU LEU TYR GLU PRO GLY THR GLY ILE ARG TYR
SEQRES  28 A  605  ALA ASN PHE ASN LEU ALA TRP LEU GLY GLY ILE CYS ALA
SEQRES  29 A  605  PRO PHE THR ILE PRO ASP VAL ALA LEU GLU PRO GLY GLN
SEQRES  30 A  605  GLN VAL THR VAL PRO VAL ALA VAL THR ASN GLN SER GLY
SEQRES  31 A  605  ILE ALA VAL PRO LYS PRO SER LEU GLN LEU ASP ALA SER
SEQRES  32 A  605  PRO ASP TRP GLN VAL GLN GLY SER VAL GLU PRO LEU MET
SEQRES  33 A  605  PRO GLY ARG GLN ALA LYS GLY GLN VAL THR ILE THR VAL
SEQRES  34 A  605  PRO ALA GLY THR THR PRO GLY ARG TYR ARG VAL GLY ALA
SEQRES  35 A  605  THR LEU ARG THR SER ALA GLY ASN ALA SER THR THR PHE
SEQRES  36 A  605  THR VAL THR VAL GLY LEU LEU ASP GLN ALA ARG MET SER
SEQRES  37 A  605  ILE ALA ASP VAL ASP SER GLU GLU THR ALA ARG GLU ASP
SEQRES  38 A  605  GLY ARG ALA SER ASN VAL ILE ASP GLY ASN PRO SER THR
SEQRES  39 A  605  PHE TRP HIS THR GLU TRP SER ARG ALA ASP ALA PRO GLY
SEQRES  40 A  605  TYR PRO HIS ARG ILE SER LEU ASP LEU GLY GLY THR HIS
SEQRES  41 A  605  THR ILE SER GLY LEU GLN TYR THR ARG ARG GLN ASN SER
SEQRES  42 A  605  ALA ASN GLU GLN VAL ALA ASP TYR GLU ILE TYR THR SER
SEQRES  43 A  605  LEU ASN GLY THR THR TRP ASP GLY PRO VAL ALA SER GLY
SEQRES  44 A  605  ARG PHE THR THR SER LEU ALA PRO GLN ARG ALA VAL PHE
SEQRES  45 A  605  PRO ALA ARG ASP ALA ARG TYR ILE ARG LEU VAL ALA LEU
SEQRES  46 A  605  SER GLU GLN THR GLY HIS LYS TYR ALA ALA VAL ALA GLU
SEQRES  47 A  605  LEU GLU VAL GLU GLY GLN ARG
HET     NA  A   1       1
HETNAM      NA SODIUM ION
FORMUL   2   NA    NA 1+
HELIX    1   1 ARG A   61  GLY A   63  5                                   3
HELIX    2   2 GLY A  215  HIS A  217  5                                   3
HELIX    3   3 ARG A  327  LYS A  329  5                                   3
HELIX    4   4 LEU A  398  TRP A  400  5                                   3
HELIX    5   5 GLN A  506  ARG A  508  5                                   3
SHEET    1   A 4 ALA A  71  VAL A  74  0
SHEET    2   A 4 LEU A  80  GLY A  86 -1  N  SER A  83   O  ALA A  71
SHEET    3   A 4 SER A  98  SER A 104 -1  N  SER A 104   O  LEU A  80
SHEET    4   A 4 GLN A 115  SER A 118 -1  N  SER A 118   O  ILE A  99
SHEET    1   B 4 GLY A 128  SER A 130  0
SHEET    2   B 4 ILE A 143  SER A 150 -1  N  SER A 150   O  GLY A 128
SHEET    3   B 4 HIS A 171  SER A 177 -1  N  SER A 177   O  ILE A 143
SHEET    4   B 4 SER A 185  THR A 188 -1  N  ARG A 187   O  VAL A 174
SHEET    1   C 2 SER A 133  VAL A 136  0
SHEET    2   C 2 ILE A 143  PHE A 146 -1  N  PHE A 146   O  SER A 133
SHEET    1   D 3 SER A 201  ALA A 204  0
SHEET    2   D 3 LEU A 221  ILE A 228 -1  N  ILE A 228   O  SER A 201
SHEET    3   D 3 PHE A 234  SER A 241 -1  N  SER A 241   O  LEU A 221
SHEET    1   E 4 ASN A 261  GLU A 265  0
SHEET    2   E 4 VAL A 271  SER A 275 -1  N  ASN A 274   O  LYS A 262
SHEET    3   E 4 TYR A 283  SER A 289 -1  N  SER A 289   O  VAL A 271
SHEET    4   E 4 THR A 300  PRO A 306 -1  N  LEU A 305   O  ARG A 284
SHEET    1   F 4 SER A 313  ARG A 316  0
SHEET    2   F 4 LEU A 331  ALA A 336 -1  N  SER A 334   O  SER A 313
SHEET    3   F 4 GLY A 345  SER A 350 -1  N  SER A 350   O  LEU A 331
SHEET    4   F 4 VAL A 359  GLN A 364 -1  N  GLN A 364   O  GLY A 345
SHEET    1   G 4 SER A 371  ALA A 375  0
SHEET    2   G 4 TYR A 381  TYR A 385 -1  N  LEU A 384   O  THR A 372
SHEET    3   G 4 GLY A 390  PHE A 396 -1  N  PHE A 396   O  TYR A 381
SHEET    4   G 4 TYR A  51  VAL A  58 -1  N  ALA A  57   O  ILE A 391
SHEET    1   H 4 PHE A 408  ILE A 410  0
SHEET    2   H 4 GLN A 419  THR A 428 -1  N  ALA A 426   O  THR A 409
SHEET    3   H 4 GLN A 462  VAL A 471 -1  N  VAL A 471   O  GLN A 419
SHEET    4   H 4 TRP A 448  VAL A 454 -1  N  SER A 453   O  GLN A 466
SHEET    1   I 4 VAL A 413  LEU A 415  0
SHEET    2   I 4 GLY A 491  VAL A 501  1  N  THR A 500   O  VAL A 413
SHEET    3   I 4 TYR A 480  THR A 488 -1  N  THR A 488   O  GLY A 491
SHEET    4   I 4 SER A 439  ASP A 443 -1  N  ASP A 443   O  GLY A 483
SHEET    1   J 5 ALA A 599  ARG A 602  0
SHEET    2   J 5 ASP A 582  SER A 588 -1  N  ILE A 585   O  ALA A 599
SHEET    3   J 5 TYR A 621  ALA A 626 -1  N  VAL A 625   O  GLU A 584
SHEET    4   J 5 HIS A 552  ASP A 557 -1  N  LEU A 556   O  ILE A 622
SHEET    5   J 5 SER A 510  VAL A 514 -1  N  ASP A 513   O  SER A 555
SHEET    1   K 3 ARG A 617  ALA A 619  0
SHEET    2   K 3 HIS A 562  THR A 570 -1  N  ILE A 564   O  ARG A 617
SHEET    3   K 3 GLU A 640  GLY A 645 -1  N  GLU A 644   O  SER A 565
SHEET    1   L 2 GLY A 566  TYR A 569  0
SHEET    2   L 2 GLN A 610  VAL A 613 -1  N  ALA A 612   O  LEU A 567
SSBOND   1 CYS A  351    CYS A  405                          1555   1555  2.27
LINK        NA    NA A   1                 O   ASN A 528     1555   1555  2.19
LINK        NA    NA A   1                 O   ASN A 533     1555   1555  2.20
LINK        NA    NA A   1                 O   THR A 536     1555   1555  2.25
LINK        NA    NA A   1                 OG1 THR A 536     1555   1555  2.28
LINK        NA    NA A   1                 O   ALA A 639     1555   1555  2.24
LINK        NA    NA A   1                 OE2 GLU A 640     1555   1555  2.56
LINK         OD1 ASP A 531                NA    NA A   1     1555   1555  2.77
CISPEP   1 ALA A   93    PRO A   94          0         0.52
CISPEP   2 ALA A  124    PRO A  125          0        -0.08
CISPEP   3 GLY A  596    PRO A  597          0         0.08
SITE     1 ACT  9 GLN A 224  GLY A 245  ALA A 250  GLY A 292
SITE     2 ACT  9 ASN A 311  PHE A 318  ALA A 619  TYR A 635
SITE     3 ACT  9 ALA A 637
SITE     1 AC1  6 ASN A 528  ASP A 531  ASN A 533  THR A 536
SITE     2 AC1  6 ALA A 639  GLU A 640
CRYST1   51.280  117.300   60.240  90.00  96.17  90.00 P 1 21 1      2
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      0.019501  0.000000  0.002108        0.00000
SCALE2      0.000000  0.008525  0.000000        0.00000
SCALE3      0.000000  0.000000  0.016697        0.00000
      
PROCHECK
Go to PROCHECK summary
 References