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PDBsum entry 1eur

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Hydrolase PDB id
1eur
Jmol
Contents
Protein chain
361 a.a.
Waters ×268
HEADER    HYDROLASE                               21-JUN-96   1EUR
TITLE     SIALIDASE
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: 41KD FORM
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MICROMONOSPORA VIRIDIFACIENS;
SOURCE   3 ORGANISM_TAXID: 1881;
SOURCE   4 ATCC: 31146
KEYWDS    NEURAMINIDASE, SIALIDASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.GASKELL,S.J.CRENNELL,G.L.TAYLOR
REVDAT   2   24-FEB-09 1EUR    1       VERSN
REVDAT   1   11-JAN-97 1EUR    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.    1.82 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) : 1.82
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             : 28814
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) : 0.173
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            : 2701
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 270
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.20
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) : 0.15
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 1EUR 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                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29469
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     (%) : 93.4
REMARK 200  DATA REDUNDANCY                : 5.600
REMARK 200  R MERGE                    (I) : 0.05500
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   (%): 38.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
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       24.07000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.37500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.36500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.37500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.07000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.36500
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE NANH_MICVI SEQUENCE REPRESENTS A 68KD PROTEIN.  THE
REMARK 400 42KD NEURAMINIDASE GIVEN HERE BELONGS TO THE SAME GENE AS
REMARK 400 THE 68KD PROTEIN BUT IS SECRETED UNDER CERTAIN
REMARK 400 CIRCUMSTANCES.
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. = -18.4 DEGREES
REMARK 500    ARG A 202   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    GLY A 292   N   -  CA  -  C   ANGL. DEV. = -15.6 DEGREES
REMARK 500    GLY A 293   N   -  CA  -  C   ANGL. DEV. = -18.3 DEGREES
REMARK 500    ARG A 303   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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  69       88.41     71.65
REMARK 500    PRO A  94       25.35    -77.86
REMARK 500    ASP A 131       74.95     56.94
REMARK 500    GLN A 151      -88.85   -131.75
REMARK 500    ASP A 259     -154.91   -168.23
REMARK 500    ASP A 291     -167.58   -125.70
REMARK 500    HIS A 294      123.41    -24.65
REMARK 500    THR A 309       81.64     72.21
REMARK 500    MET A 368      108.54   -162.96
REMARK 500    SER A 369     -105.98    -96.82
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 641        DISTANCE =  9.12 ANGSTROMS
REMARK 525    HOH A 661        DISTANCE =  6.69 ANGSTROMS
REMARK 525    HOH A 670        DISTANCE =  6.07 ANGSTROMS
REMARK 525    HOH A 688        DISTANCE =  7.72 ANGSTROMS
REMARK 525    HOH A 691        DISTANCE =  6.16 ANGSTROMS
REMARK 525    HOH A 700        DISTANCE =  6.95 ANGSTROMS
REMARK 525    HOH A 708        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH A 712        DISTANCE =  6.20 ANGSTROMS
REMARK 525    HOH A 713        DISTANCE =  7.68 ANGSTROMS
REMARK 525    HOH A 715        DISTANCE =  8.20 ANGSTROMS
REMARK 525    HOH A 718        DISTANCE =  5.96 ANGSTROMS
REMARK 525    HOH A 726        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH A 759        DISTANCE =  7.36 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE.
DBREF  1EUR A   43   407  UNP    Q02834   NANH_MICVI      43    407
SEQRES   1 A  365  VAL PRO PRO GLY GLY GLU PRO LEU TYR THR GLU GLN ASP
SEQRES   2 A  365  LEU ALA VAL ASN GLY ARG GLU GLY PHE PRO ASN TYR ARG
SEQRES   3 A  365  ILE PRO ALA LEU THR VAL THR PRO ASP GLY ASP LEU LEU
SEQRES   4 A  365  ALA SER TYR ASP GLY ARG PRO THR GLY ILE ASP ALA PRO
SEQRES   5 A  365  GLY PRO ASN SER ILE LEU GLN ARG ARG SER THR ASP GLY
SEQRES   6 A  365  GLY ARG THR TRP GLY GLU GLN GLN VAL VAL SER ALA GLY
SEQRES   7 A  365  GLN THR THR ALA PRO ILE LYS GLY PHE SER ASP PRO SER
SEQRES   8 A  365  TYR LEU VAL ASP ARG GLU THR GLY THR ILE PHE ASN PHE
SEQRES   9 A  365  HIS VAL TYR SER GLN ARG GLN GLY PHE ALA GLY SER ARG
SEQRES  10 A  365  PRO GLY THR ASP PRO ALA ASP PRO ASN VAL LEU HIS ALA
SEQRES  11 A  365  ASN VAL ALA THR SER THR ASP GLY GLY LEU THR TRP SER
SEQRES  12 A  365  HIS ARG THR ILE THR ALA ASP ILE THR PRO ASP PRO GLY
SEQRES  13 A  365  TRP ARG SER ARG PHE ALA ALA SER GLY GLU GLY ILE GLN
SEQRES  14 A  365  LEU ARG TYR GLY PRO HIS ALA GLY ARG LEU ILE GLN GLN
SEQRES  15 A  365  TYR THR ILE ILE ASN ALA ALA GLY ALA PHE GLN ALA VAL
SEQRES  16 A  365  SER VAL TYR SER ASP ASP HIS GLY ARG THR TRP ARG ALA
SEQRES  17 A  365  GLY GLU ALA VAL GLY VAL GLY MET ASP GLU ASN LYS THR
SEQRES  18 A  365  VAL GLU LEU SER ASP GLY ARG VAL LEU LEU ASN SER ARG
SEQRES  19 A  365  ASP SER ALA ARG SER GLY TYR ARG LYS VAL ALA VAL SER
SEQRES  20 A  365  THR ASP GLY GLY HIS SER TYR GLY PRO VAL THR ILE ASP
SEQRES  21 A  365  ARG ASP LEU PRO ASP PRO THR ASN ASN ALA SER ILE ILE
SEQRES  22 A  365  ARG ALA PHE PRO ASP ALA PRO ALA GLY SER ALA ARG ALA
SEQRES  23 A  365  LYS VAL LEU LEU PHE SER ASN ALA ALA SER GLN THR SER
SEQRES  24 A  365  ARG SER GLN GLY THR ILE ARG MET SER CYS ASP ASP GLY
SEQRES  25 A  365  GLN THR TRP PRO VAL SER LYS VAL PHE GLN PRO GLY SER
SEQRES  26 A  365  MET SER TYR SER THR LEU THR ALA LEU PRO ASP GLY THR
SEQRES  27 A  365  TYR GLY LEU LEU TYR GLU PRO GLY THR GLY ILE ARG TYR
SEQRES  28 A  365  ALA ASN PHE ASN LEU ALA TRP LEU GLY GLY ILE CYS ALA
SEQRES  29 A  365  PRO
FORMUL   2  HOH   *268(H2 O)
HELIX    1   1 ALA A  191  ILE A  193  5                                   3
HELIX    2   2 ARG A  327  LYS A  329  5                                   3
HELIX    3   3 LEU A  398  LEU A  401  1                                   4
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  ASP A 137  0
SHEET    2   C 2 THR A 142  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
CISPEP   1 ALA A   93    PRO A   94          0        -1.58
CISPEP   2 ALA A  124    PRO A  125          0        -0.18
CISPEP   3 ALA A  406    PRO A  407          0         0.22
SITE     1 ACT 14 ARG A  68  ARG A  87  ASP A  92  ASP A 131
SITE     2 ACT 14 VAL A 148  PHE A 155  LEU A 170  PHE A 203
SITE     3 ACT 14 ASP A 259  GLU A 260  ARG A 276  ARG A 342
SITE     4 ACT 14 TYR A 370  GLU A 386
CRYST1   48.140   82.730   84.750  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      0.020773  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012088  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011799        0.00000
      
PROCHECK
Go to PROCHECK summary
 References