spacer
spacer

PDBsum entry 1inh

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase (o-glycosyl) PDB id
1inh
Jmol
Contents
Protein chains
388 a.a. *
Ligands
NAG-NAG ×4
NAG-NAG-BMA-FUL
NAG-MAN ×2
BMA-MAN-BMA
NAG-NAG-BMA-FUC
NAG
NAG-BMA-MAN-MAN
ST6 ×2
Metals
_CA ×2
* Residue conservation analysis
HEADER    HYDROLASE (O-GLYCOSYL)                  07-JUL-95   1INH
TITLE     INFLUENZA A SUBTYPE N2 NEURAMINIDASE COMPLEXED WITH AROMATIC BANA111
TITLE    2 INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: INFLUENZA A SUBTYPE N2 NEURAMINIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: SIALIDASE;
COMPND   5 EC: 3.2.1.18
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_TAXID: 11320;
SOURCE   4 STRAIN: A/TOKYO/3/67
KEYWDS    NEURAMINIDASE, SIALIDASE, HYDROLASE, O-GLYCOSYL, HYDROLASE (O-
KEYWDS   2 GLYCOSYL)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.J.JEDRZEJAS,M.LUO
REVDAT   4   26-OCT-11 1INH    1       LINK
REVDAT   3   13-JUL-11 1INH    1       VERSN
REVDAT   2   24-FEB-09 1INH    1       VERSN
REVDAT   1   17-AUG-96 1INH    0
JRNL        AUTH   S.SINGH,M.J.JEDRZEJAS,G.M.AIR,M.LUO,W.G.LAVER,
JRNL        AUTH 2 W.J.BROUILLETTE
JRNL        TITL   STRUCTURE-BASED INHIBITORS OF INFLUENZA VIRUS SIALIDASE. A
JRNL        TITL 2 BENZOIC ACID LEAD WITH NOVEL INTERACTION.
JRNL        REF    J.MED.CHEM.                   V.  38  3217 1995
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   7650674
JRNL        DOI    10.1021/JM00017A005
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.LUO,M.J.JEDRZEJAS,S.SINGH,C.L.WHITE,W.J.BROUILLETTE,
REMARK   1  AUTH 2 G.M.AIR,W.G.LAVER
REMARK   1  TITL   BENZOIC ACID INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  51   504 1995
REMARK   1  REFN                   ISSN 0907-4449
REMARK   1 REFERENCE 2
REMARK   1  AUTH   S.SINGH,M.J.JEDRZEJAS,G.M.AIR,M.LUO,W.G.LAVER,
REMARK   1  AUTH 2 W.J.BROUILLETTE
REMARK   1  TITL   STRUCTURE-BASED INHIBITORS OF INFLUENZA VIRAL NEURAMINIDASE.
REMARK   1  TITL 2 A BENZOIC ACID LEAD WITH NOVEL INTERACTION
REMARK   1  REF    J.MED.CHEM.                   V.  38  3217 1995
REMARK   1  REFN                   ISSN 0022-2623
REMARK   1 REFERENCE 3
REMARK   1  AUTH   M.J.JEDRZEJAS,S.SINGH,W.J.BROUILLETTE,W.G.LAVER,G.M.AIR,
REMARK   1  AUTH 2 M.LUO
REMARK   1  TITL   STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS
REMARK   1  TITL 2 NEURAMINIDASE
REMARK   1  REF    BIOCHEMISTRY                  V.  34  3144 1995
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 4
REMARK   1  AUTH   J.N.VARGHESE,P.M.COLMAN
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF THE NEURAMINIDASE OF
REMARK   1  TITL 2 INFLUENZA VIRUS A/TOKYO/3/67 AT 2.2 A RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V. 221   473 1991
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    2.40 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) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000
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             : 19238
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) : 0.184
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            : 6044
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 392
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) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.012
REMARK   3   BOND ANGLES            (DEGREES) : 1.96
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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  THE REFINED MODEL COORDINATES DEPOSITED CONTAIN THE FULL
REMARK   3  PROTEIN SEQUENCE FROM VAL 82 TO ILE 469.  THE CALCIUM
REMARK   3  RESIDUE, CA 470, STABILIZES A LOOP NEAR THE NEURAMINIDASE
REMARK   3  ACTIVE SITE.  THE BANA111 INHIBITOR IS RESIDUE ST1 471.
REMARK   4
REMARK   4 1INH 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        : 13-JUN-94
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 6.8
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 : XENGEN
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21384
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     (%) : NULL
REMARK 200  DATA REDUNDANCY                : 5.000
REMARK 200  R MERGE                    (I) : 0.11700
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   (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.89000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.89000
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        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       59.87000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       70.51000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.87000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       70.51000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       70.89000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       59.87000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       70.51000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       70.89000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       59.87000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       70.51000
REMARK 290   SMTRY3   8  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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   CB   ASN B   393     HO3  BMA B   482              0.26
REMARK 500   CG   GLN B   391     H61  MAN B   481              0.32
REMARK 500   O    ASN B   393     H1   BMA B   482              0.72
REMARK 500   N    ARG B   394     C1   BMA B   482              0.73
REMARK 500   N    ARG B   394     O2   MAN B   481              0.84
REMARK 500   CA   ASN B   393     O2   BMA B   482              0.84
REMARK 500   CB   ASN B   393     O3   BMA B   482              0.86
REMARK 500   C    ASN B   393     H1   BMA B   482              0.90
REMARK 500   C    ASN B   393     C1   BMA B   482              0.90
REMARK 500   H    ASN B   393     HO2  BMA B   482              0.93
REMARK 500   N    ASN B   393     O2   BMA B   482              0.93
REMARK 500   CA   ARG B   394     O2   MAN B   481              0.99
REMARK 500   CB   GLN B   391     O6   MAN B   481              1.01
REMARK 500   OE1  GLN B   391     H4   MAN B   481              1.06
REMARK 500  HD22  ASN B   393     H3   BMA B   482              1.10
REMARK 500   CB   ARG B   394     H2   MAN B   481              1.16
REMARK 500   OH   TYR B   453     H4   BMA B   482              1.18
REMARK 500   CA   ASN B   393     C2   BMA B   482              1.20
REMARK 500   N    ASN B   393     HO2  BMA B   482              1.24
REMARK 500   H    ARG B   394     O2   MAN B   481              1.25
REMARK 500   CG   GLN B   391     C6   MAN B   481              1.26
REMARK 500   CB   GLN B   391     C6   MAN B   481              1.28
REMARK 500   CB   GLN B   391     H61  MAN B   481              1.28
REMARK 500   O    GLN B   391     H62  MAN B   481              1.32
REMARK 500   CG   ASN B   393     HO3  BMA B   482              1.34
REMARK 500   C    ASN B   393     C2   BMA B   482              1.36
REMARK 500   CE1  TYR B   453     H82  NAG A   478              1.39
REMARK 500   CD1  TYR B   453     H83  NAG A   478              1.39
REMARK 500   O    ASN B   393     HO6  BMA B   482              1.40
REMARK 500  HD22  ASN A   146     C1   NAG A   474              1.43
REMARK 500  HD22  ASN B   146     C1   NAG B   474              1.43
REMARK 500   H    ASN B   393     O2   BMA B   482              1.44
REMARK 500   CG   GLN B   395     H5   BMA B   482              1.45
REMARK 500   C    GLN B   391     H62  MAN B   481              1.55
REMARK 500   CA   GLN B   391     O6   MAN B   481              1.57
REMARK 500   CB   PHE B   377     H3   MAN B   481              1.60
REMARK 500   CB   ARG B   394     O2   MAN B   481              1.62
REMARK 500   C    ARG B   394     O5   BMA B   482              1.65
REMARK 500   O    ASN B   393     C1   BMA B   482              1.65
REMARK 500   CA   ARG B   394     C1   BMA B   482              1.67
REMARK 500   OE1  GLN B   391     C4   MAN B   481              1.68
REMARK 500   N    ARG B   394     C2   BMA B   482              1.69
REMARK 500   CD1  TYR B   453     C8   NAG A   478              1.73
REMARK 500   CB   ASN B   393     C3   BMA B   482              1.75
REMARK 500   CB   ARG B   394     C2   MAN B   481              1.75
REMARK 500   CA   ASN B   393     C3   BMA B   482              1.80
REMARK 500   N    ARG B   394     O5   BMA B   482              1.86
REMARK 500   CA   ARG B   394     O5   BMA B   482              1.87
REMARK 500   CG   ASN B   393     O3   BMA B   482              1.88
REMARK 500   C    ASN B   393     O2   BMA B   482              1.89
REMARK 500
REMARK 500 THIS ENTRY HAS      67 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   CB   ASN A   393     HO3  MAN B   485     4555     0.26
REMARK 500   CG   GLN A   391     H61  MAN B   484     4555     0.32
REMARK 500   O    ASN A   393     H1   MAN B   485     4555     0.72
REMARK 500   NH2  ARG B   331     CG2  THR B   434     3654     0.72
REMARK 500   N    ARG A   394     C1   MAN B   485     4555     0.73
REMARK 500   N    ARG A   394     O2   MAN B   484     4555     0.84
REMARK 500   CA   ASN A   393     O2   MAN B   485     4555     0.84
REMARK 500   CB   ASN A   393     O3   MAN B   485     4555     0.86
REMARK 500   C    ASN A   393     H1   MAN B   485     4555     0.90
REMARK 500   C    ASN A   393     C1   MAN B   485     4555     0.90
REMARK 500   H    ASN A   393     HO2  MAN B   485     4555     0.93
REMARK 500   N    ASN A   393     O2   MAN B   485     4555     0.93
REMARK 500   CA   ARG A   394     O2   MAN B   484     4555     0.99
REMARK 500   CB   GLN A   391     O6   MAN B   484     4555     1.01
REMARK 500  HH21  ARG B   331     CB   THR B   434     3654     1.03
REMARK 500  HH21  ARG B   331     CG2  THR B   434     3654     1.06
REMARK 500   OE1  GLN A   391     H4   MAN B   484     4555     1.06
REMARK 500  HD22  ASN A   393     H3   MAN B   485     4555     1.10
REMARK 500   CZ   ARG B   331     CG2  THR B   434     3654     1.12
REMARK 500   CB   ARG A   394     H2   MAN B   484     4555     1.16
REMARK 500   OH   TYR A   453     H4   MAN B   485     4555     1.18
REMARK 500   CA   ASN A   393     C2   MAN B   485     4555     1.20
REMARK 500   N    ASN A   393     HO2  MAN B   485     4555     1.24
REMARK 500   H    ARG A   394     O2   MAN B   484     4555     1.25
REMARK 500   CG   GLN A   391     C6   MAN B   484     4555     1.26
REMARK 500   CB   GLN A   391     C6   MAN B   484     4555     1.28
REMARK 500   CB   GLN A   391     H61  MAN B   484     4555     1.28
REMARK 500   O    GLN A   391     H62  MAN B   484     4555     1.32
REMARK 500   NH2  ARG B   331     CB   THR B   434     3654     1.33
REMARK 500   CG   ASN A   393     HO3  MAN B   485     4555     1.34
REMARK 500   C    ASN A   393     C2   MAN B   485     4555     1.36
REMARK 500   CE1  TYR A   453     H82  NAG B   478     4555     1.39
REMARK 500   CD1  TYR A   453     H83  NAG B   478     4555     1.39
REMARK 500   O    ASN A   393     HO6  MAN B   485     4555     1.40
REMARK 500   H    ASN A   393     O2   MAN B   485     4555     1.44
REMARK 500   CG   GLN A   395     H5   MAN B   485     4555     1.45
REMARK 500  HH22  ARG B   331     CB   THR B   434     3654     1.49
REMARK 500   C    GLN A   391     H62  MAN B   484     4555     1.55
REMARK 500   CA   GLN A   391     O6   MAN B   484     4555     1.57
REMARK 500   CB   PHE A   377     H3   MAN B   484     4555     1.60
REMARK 500   CB   ARG A   394     O2   MAN B   484     4555     1.62
REMARK 500   C    ARG A   394     O5   MAN B   485     4555     1.65
REMARK 500   O    ASN A   393     C1   MAN B   485     4555     1.65
REMARK 500   CA   ARG A   394     C1   MAN B   485     4555     1.67
REMARK 500   OE1  GLN A   391     C4   MAN B   484     4555     1.68
REMARK 500   N    ARG A   394     C2   MAN B   485     4555     1.69
REMARK 500   CD1  TYR A   453     C8   NAG B   478     4555     1.73
REMARK 500   CB   ASN A   393     C3   MAN B   485     4555     1.75
REMARK 500   CB   ARG A   394     C2   MAN B   484     4555     1.75
REMARK 500   NE   ARG B   331     CG2  THR B   434     3654     1.80
REMARK 500
REMARK 500 THIS ENTRY HAS      72 SYMMETRY CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    CYS A 183   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES
REMARK 500    GLY A 248   N   -  CA  -  C   ANGL. DEV. = -15.6 DEGREES
REMARK 500    CYS B 183   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES
REMARK 500    GLY B 248   N   -  CA  -  C   ANGL. DEV. = -15.6 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    ASN A  86      -20.74   -157.72
REMARK 500    SER A  88       46.80    -86.56
REMARK 500    ASN A 104       33.35     39.12
REMARK 500    THR A 117     -157.77   -134.74
REMARK 500    ARG A 118      174.16    168.52
REMARK 500    TYR A 121      166.21    176.01
REMARK 500    ASP A 147       39.23     72.27
REMARK 500    LEU A 169       -3.30    -56.69
REMARK 500    CYS A 175      171.65    179.19
REMARK 500    ALA A 177      148.79   -170.77
REMARK 500    SER A 219        5.29   -164.81
REMARK 500    GLN A 220       19.57     59.61
REMARK 500    ILE A 222       62.47     37.15
REMARK 500    GLN A 226      -39.62    -30.36
REMARK 500    ASN A 234       61.03     39.89
REMARK 500    SER A 247       75.33   -114.27
REMARK 500    GLU A 259       26.95     80.23
REMARK 500    HIS A 264      157.80    170.82
REMARK 500    HIS A 274      106.64   -161.00
REMARK 500    GLU A 277       58.45     29.05
REMARK 500    PRO A 285       49.42   -104.73
REMARK 500    CYS A 291     -145.62   -103.71
REMARK 500    ASP A 309      -20.88   -142.10
REMARK 500    SER A 315     -163.73   -168.83
REMARK 500    SER A 319      112.26    -30.78
REMARK 500    VAL A 322      127.73      3.99
REMARK 500    ASP A 324     -160.16   -128.58
REMARK 500    ASP A 329      151.78    177.67
REMARK 500    THR A 346      154.40    -49.68
REMARK 500    GLN A 347      173.24     58.60
REMARK 500    ARG A 371       73.27   -101.97
REMARK 500    ASN A 393       74.24     67.74
REMARK 500    SER A 404     -131.06   -140.67
REMARK 500    SER A 407      147.49   -179.45
REMARK 500    SER A 416      -39.47   -148.99
REMARK 500    ARG A 430      150.55    -45.35
REMARK 500    LYS A 431      -78.66     98.58
REMARK 500    SER A 457      101.67   -162.37
REMARK 500    PRO A 459     -165.65   -101.08
REMARK 500    ASP A 460      -82.33    -58.00
REMARK 500    ASN B  86      -20.74   -157.72
REMARK 500    SER B  88       46.80    -86.56
REMARK 500    ASN B 104       33.35     39.12
REMARK 500    THR B 117     -157.77   -134.74
REMARK 500    ARG B 118      174.16    168.52
REMARK 500    TYR B 121      166.21    176.01
REMARK 500    ASP B 147       39.23     72.27
REMARK 500    LEU B 169       -3.30    -56.69
REMARK 500    CYS B 175      171.65    179.19
REMARK 500    ALA B 177      148.79   -170.77
REMARK 500
REMARK 500 THIS ENTRY HAS      80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    GLN A 226        24.3      L          L   OUTSIDE RANGE
REMARK 500    ARG A 430        24.0      L          L   OUTSIDE RANGE
REMARK 500    GLN B 226        24.3      L          L   OUTSIDE RANGE
REMARK 500    ARG B 430        24.0      L          L   OUTSIDE RANGE
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 470  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 345   O
REMARK 620 2 GLN A 347   O   102.7
REMARK 620 3 ASP A 293   O   103.8 108.1
REMARK 620 4 GLY A 297   O    79.1 177.5  69.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 488  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 345   O
REMARK 620 2 GLN B 347   O   102.7
REMARK 620 3 ASP B 293   O   103.8 108.1
REMARK 620 4 GLY B 297   O    79.1 177.5  69.7
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: SUBSTRATE (SIALIC ACID) BINDING RESIDUES
REMARK 800  CATALYTIC SITE IN CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: SUBSTRATE (SIALIC ACID) BINDING RESIDUES
REMARK 800  CATALYTIC SITE IN CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUL A 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 484
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 485
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 483
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 484
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 485
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 487
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 488
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ST6 A 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ST6 B 489
DBREF  1INH A   82   469  UNP    P06820   NRAM_IATOK      82    469
DBREF  1INH B   82   469  UNP    P06820   NRAM_IATOK      82    469
SEQADV 1INH ASP A  339  UNP  P06820    ASN   339 CONFLICT
SEQADV 1INH ASP B  339  UNP  P06820    ASN   339 CONFLICT
SEQRES   1 A  388  VAL GLU TYR ARG ASN TRP SER LYS PRO GLN CYS GLN ILE
SEQRES   2 A  388  THR GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE ARG
SEQRES   3 A  388  LEU SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU PRO
SEQRES   4 A  388  TYR VAL SER CYS ASP PRO VAL LYS CYS TYR GLN PHE ALA
SEQRES   5 A  388  LEU GLY GLN GLY THR THR LEU ASP ASN LYS HIS SER ASN
SEQRES   6 A  388  ASP THR VAL HIS ASP ARG ILE PRO HIS ARG THR LEU LEU
SEQRES   7 A  388  MET ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR ARG
SEQRES   8 A  388  GLN VAL CYS ILE ALA TRP SER SER SER SER CYS HIS ASP
SEQRES   9 A  388  GLY LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASP ASP
SEQRES  10 A  388  LYS ASN ALA THR ALA SER PHE ILE TYR ASP GLY ARG LEU
SEQRES  11 A  388  VAL ASP SER ILE GLY SER TRP SER GLN ASN ILE LEU ARG
SEQRES  12 A  388  THR GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR CYS
SEQRES  13 A  388  THR VAL VAL MET THR ASP GLY SER ALA SER GLY ARG ALA
SEQRES  14 A  388  ASP THR ARG ILE LEU PHE ILE GLU GLU GLY LYS ILE VAL
SEQRES  15 A  388  HIS ILE SER PRO LEU ALA GLY SER ALA GLN HIS VAL GLU
SEQRES  16 A  388  GLU CYS SER CYS TYR PRO ARG TYR PRO GLY VAL ARG CYS
SEQRES  17 A  388  ILE CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO VAL
SEQRES  18 A  388  VAL ASP ILE ASN MET GLU ASP TYR SER ILE ASP SER SER
SEQRES  19 A  388  TYR VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG ASN
SEQRES  20 A  388  ASP ASP ARG SER SER ASN SER ASN CYS ARG ASP PRO ASN
SEQRES  21 A  388  ASN GLU ARG GLY THR GLN GLY VAL LYS GLY TRP ALA PHE
SEQRES  22 A  388  ASP ASN GLY ASN ASP LEU TRP MET GLY ARG THR ILE SER
SEQRES  23 A  388  LYS ASP LEU ARG SER GLY TYR GLU THR PHE LYS VAL ILE
SEQRES  24 A  388  GLY GLY TRP SER THR PRO ASN SER LYS SER GLN ILE ASN
SEQRES  25 A  388  ARG GLN VAL ILE VAL ASP SER ASP ASN ARG SER GLY TYR
SEQRES  26 A  388  SER GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE ASN
SEQRES  27 A  388  ARG CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS GLN
SEQRES  28 A  388  GLU THR ARG VAL TRP TRP THR SER ASN SER ILE VAL VAL
SEQRES  29 A  388  PHE CYS GLY THR SER GLY THR TYR GLY THR GLY SER TRP
SEQRES  30 A  388  PRO ASP GLY ALA ASN ILE ASN PHE MET PRO ILE
SEQRES   1 B  388  VAL GLU TYR ARG ASN TRP SER LYS PRO GLN CYS GLN ILE
SEQRES   2 B  388  THR GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE ARG
SEQRES   3 B  388  LEU SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU PRO
SEQRES   4 B  388  TYR VAL SER CYS ASP PRO VAL LYS CYS TYR GLN PHE ALA
SEQRES   5 B  388  LEU GLY GLN GLY THR THR LEU ASP ASN LYS HIS SER ASN
SEQRES   6 B  388  ASP THR VAL HIS ASP ARG ILE PRO HIS ARG THR LEU LEU
SEQRES   7 B  388  MET ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR ARG
SEQRES   8 B  388  GLN VAL CYS ILE ALA TRP SER SER SER SER CYS HIS ASP
SEQRES   9 B  388  GLY LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASP ASP
SEQRES  10 B  388  LYS ASN ALA THR ALA SER PHE ILE TYR ASP GLY ARG LEU
SEQRES  11 B  388  VAL ASP SER ILE GLY SER TRP SER GLN ASN ILE LEU ARG
SEQRES  12 B  388  THR GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR CYS
SEQRES  13 B  388  THR VAL VAL MET THR ASP GLY SER ALA SER GLY ARG ALA
SEQRES  14 B  388  ASP THR ARG ILE LEU PHE ILE GLU GLU GLY LYS ILE VAL
SEQRES  15 B  388  HIS ILE SER PRO LEU ALA GLY SER ALA GLN HIS VAL GLU
SEQRES  16 B  388  GLU CYS SER CYS TYR PRO ARG TYR PRO GLY VAL ARG CYS
SEQRES  17 B  388  ILE CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO VAL
SEQRES  18 B  388  VAL ASP ILE ASN MET GLU ASP TYR SER ILE ASP SER SER
SEQRES  19 B  388  TYR VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG ASN
SEQRES  20 B  388  ASP ASP ARG SER SER ASN SER ASN CYS ARG ASP PRO ASN
SEQRES  21 B  388  ASN GLU ARG GLY THR GLN GLY VAL LYS GLY TRP ALA PHE
SEQRES  22 B  388  ASP ASN GLY ASN ASP LEU TRP MET GLY ARG THR ILE SER
SEQRES  23 B  388  LYS ASP LEU ARG SER GLY TYR GLU THR PHE LYS VAL ILE
SEQRES  24 B  388  GLY GLY TRP SER THR PRO ASN SER LYS SER GLN ILE ASN
SEQRES  25 B  388  ARG GLN VAL ILE VAL ASP SER ASP ASN ARG SER GLY TYR
SEQRES  26 B  388  SER GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE ASN
SEQRES  27 B  388  ARG CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS GLN
SEQRES  28 B  388  GLU THR ARG VAL TRP TRP THR SER ASN SER ILE VAL VAL
SEQRES  29 B  388  PHE CYS GLY THR SER GLY THR TYR GLY THR GLY SER TRP
SEQRES  30 B  388  PRO ASP GLY ALA ASN ILE ASN PHE MET PRO ILE
MODRES 1INH ASN A  234  ASN  GLYCOSYLATION SITE
MODRES 1INH ASN B  234  ASN  GLYCOSYLATION SITE
MODRES 1INH ASN A   86  ASN  GLYCOSYLATION SITE
MODRES 1INH ASN B   86  ASN  GLYCOSYLATION SITE
MODRES 1INH ASN A  146  ASN  GLYCOSYLATION SITE
MODRES 1INH ASN B  146  ASN  GLYCOSYLATION SITE
MODRES 1INH ASN A  200  ASN  GLYCOSYLATION SITE
MODRES 1INH ASN B  200  ASN  GLYCOSYLATION SITE
HET    NAG  A 472      27
HET    NAG  A 473      28
HET    NAG  A 474      26
HET    NAG  A 475      27
HET    BMA  A 476      22
HET    FUL  A 477      21
HET    NAG  A 478      26
HET    MAN  A 483      22
HET    NAG  B 479      27
HET    BMA  B 480      21
HET    MAN  B 481      21
HET    BMA  B 482      22
HET    NAG  A 484      27
HET    NAG  A 485      28
HET    NAG  B 472      27
HET    NAG  B 473      28
HET    NAG  B 474      26
HET    NAG  B 475      27
HET    BMA  B 476      22
HET    FUC  B 477      21
HET    NAG  B 478      26
HET    MAN  B 483      22
HET    NAG  B 470      27
HET    BMA  B 471      21
HET    MAN  B 484      21
HET    MAN  B 485      22
HET    NAG  B 486      27
HET    NAG  B 487      28
HET     CA  A 470       1
HET     CA  B 488       1
HET    ST6  A 471      25
HET    ST6  B 489      25
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     FUL BETA-L-FUCOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM      CA CALCIUM ION
HETNAM     ST6 4-(ACETYLAMINO)-3-[(AMINOACETYL)AMINO]BENZOIC ACID
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL   3  NAG    16(C8 H15 N O6)
FORMUL   4  BMA    5(C6 H12 O6)
FORMUL   4  FUL    C6 H12 O5
FORMUL   5  MAN    5(C6 H12 O6)
FORMUL  10  FUC    C6 H12 O5
FORMUL  15   CA    2(CA 2+)
FORMUL  17  ST6    2(C11 H14 N3 O4 1+)
HELIX    1   1 SER A  105  ALA A  110  1                                   6
HELIX    2   2 SER B  105  ALA B  110  1                                   6
SHEET    1   A 3 TYR A 121  CYS A 124  0
SHEET    2   A 3 CYS A 129  GLY A 135 -1  N  PHE A 132   O  TYR A 121
SHEET    3   A 3 THR A 157  GLU A 162 -1  N  ASN A 161   O  GLN A 131
SHEET    1   B 4 SER A 179  HIS A 184  0
SHEET    2   B 4 TRP A 189  GLY A 196 -1  N  ILE A 194   O  SER A 179
SHEET    3   B 4 ALA A 201  TYR A 207 -1  N  ILE A 206   O  HIS A 191
SHEET    4   B 4 ARG A 210  GLY A 216 -1  N  ILE A 215   O  ALA A 203
SHEET    1   C 4 VAL A 231  ILE A 233  0
SHEET    2   C 4 THR A 236  GLY A 244 -1  N  THR A 238   O  VAL A 231
SHEET    3   C 4 ALA A 250  ILE A 257 -1  N  LEU A 255   O  VAL A 239
SHEET    4   C 4 ILE A 262  PRO A 267 -1  N  SER A 266   O  ILE A 254
SHEET    1   D 4 SER A 279  ARG A 283  0
SHEET    2   D 4 GLY A 286  ILE A 290 -1  N  ILE A 290   O  SER A 279
SHEET    3   D 4 PRO A 301  ASN A 306 -1  N  ILE A 305   O  VAL A 287
SHEET    4   D 4 SER A 311  TYR A 316 -1  N  SER A 315   O  VAL A 302
SHEET    1   E 4 ALA A 353  ASN A 356  0
SHEET    2   E 4 ASP A 359  ARG A 364 -1  N  TRP A 361   O  PHE A 354
SHEET    3   E 4 GLU A 375  ILE A 380 -1  N  VAL A 379   O  LEU A 360
SHEET    4   E 4 SER A 390  ILE A 392 -1  N  ILE A 392   O  LYS A 378
SHEET    1   F 4 SER A 407  GLU A 413  0
SHEET    2   F 4 ILE A 418  GLY A 429 -1  N  TYR A 423   O  GLY A 408
SHEET    3   F 4 THR A 439  THR A 449 -1  N  PHE A 446   O  PHE A 422
SHEET    4   F 4 GLY A  96  LYS A 102 -1  N  SER A 101   O  VAL A 445
SHEET    1   G 3 TYR B 121  CYS B 124  0
SHEET    2   G 3 CYS B 129  GLY B 135 -1  N  PHE B 132   O  TYR B 121
SHEET    3   G 3 THR B 157  GLU B 162 -1  N  ASN B 161   O  GLN B 131
SHEET    1   H 4 SER B 179  HIS B 184  0
SHEET    2   H 4 TRP B 189  GLY B 196 -1  N  ILE B 194   O  SER B 179
SHEET    3   H 4 ALA B 201  TYR B 207 -1  N  ILE B 206   O  HIS B 191
SHEET    4   H 4 ARG B 210  GLY B 216 -1  N  ILE B 215   O  ALA B 203
SHEET    1   I 4 VAL B 231  ILE B 233  0
SHEET    2   I 4 THR B 236  GLY B 244 -1  N  THR B 238   O  VAL B 231
SHEET    3   I 4 ALA B 250  ILE B 257 -1  N  LEU B 255   O  VAL B 239
SHEET    4   I 4 ILE B 262  PRO B 267 -1  N  SER B 266   O  ILE B 254
SHEET    1   J 4 SER B 279  ARG B 283  0
SHEET    2   J 4 GLY B 286  ILE B 290 -1  N  ILE B 290   O  SER B 279
SHEET    3   J 4 PRO B 301  ASN B 306 -1  N  ILE B 305   O  VAL B 287
SHEET    4   J 4 SER B 311  TYR B 316 -1  N  SER B 315   O  VAL B 302
SHEET    1   K 4 ALA B 353  ASN B 356  0
SHEET    2   K 4 ASP B 359  ARG B 364 -1  N  TRP B 361   O  PHE B 354
SHEET    3   K 4 GLU B 375  ILE B 380 -1  N  VAL B 379   O  LEU B 360
SHEET    4   K 4 SER B 390  ILE B 392 -1  N  ILE B 392   O  LYS B 378
SHEET    1   L 4 SER B 407  GLU B 413  0
SHEET    2   L 4 ILE B 418  GLY B 429 -1  N  TYR B 423   O  GLY B 408
SHEET    3   L 4 THR B 439  THR B 449 -1  N  PHE B 446   O  PHE B 422
SHEET    4   L 4 GLY B  96  LYS B 102 -1  N  SER B 101   O  VAL B 445
SHEET    1   M 2 TYR A 374  THR A 376  0
SHEET    2   M 2 GLN A 395  VAL A 398 -1  N  VAL A 398   O  TYR A 374
SHEET    1   N 2 TYR B 374  THR B 376  0
SHEET    2   N 2 GLN B 395  VAL B 398 -1  N  VAL B 398   O  TYR B 374
SSBOND   1 CYS A   92    CYS A  417                          1555   1555  2.04
SSBOND   2 CYS A  124    CYS A  129                          1555   1555  2.02
SSBOND   3 CYS A  175    CYS A  193                          1555   1555  2.03
SSBOND   4 CYS A  183    CYS A  230                          1555   1555  2.04
SSBOND   5 CYS A  232    CYS A  237                          1555   1555  2.03
SSBOND   6 CYS A  278    CYS A  291                          1555   1555  2.01
SSBOND   7 CYS A  280    CYS A  289                          1555   1555  2.03
SSBOND   8 CYS A  318    CYS A  337                          1555   1555  2.03
SSBOND   9 CYS A  421    CYS A  447                          1555   1555  2.02
SSBOND  10 CYS B   92    CYS B  417                          1555   1555  2.04
SSBOND  11 CYS B  124    CYS B  129                          1555   1555  2.02
SSBOND  12 CYS B  175    CYS B  193                          1555   1555  2.03
SSBOND  13 CYS B  183    CYS B  230                          1555   1555  2.04
SSBOND  14 CYS B  232    CYS B  237                          1555   1555  2.03
SSBOND  15 CYS B  278    CYS B  291                          1555   1555  2.01
SSBOND  16 CYS B  280    CYS B  289                          1555   1555  2.03
SSBOND  17 CYS B  318    CYS B  337                          1555   1555  2.03
SSBOND  18 CYS B  421    CYS B  447                          1555   1555  2.02
LINK         O4  NAG B 472                 C1  NAG B 473     1555   1555  1.37
LINK         O4  NAG A 472                 C1  NAG A 473     1555   1555  1.37
LINK         O4  NAG A 484                 C1  NAG A 485     1555   1555  1.43
LINK         O4  NAG B 486                 C1  NAG B 487     1555   1555  1.43
LINK         O2  MAN B 481                 C1  BMA B 482     1555   1555  1.44
LINK         O2  MAN B 484                 C1  MAN B 485     1555   1555  1.44
LINK         ND2 ASN A 234                 C1  NAG A 484     1555   1555  1.45
LINK         ND2 ASN B 234                 C1  NAG B 486     1555   1555  1.45
LINK         O3  BMA B 480                 C1  MAN B 481     1555   1555  1.46
LINK         O3  BMA B 471                 C1  MAN B 484     1555   1555  1.46
LINK         ND2 ASN A  86                 C1  NAG A 472     1555   1555  1.46
LINK         ND2 ASN B  86                 C1  NAG B 472     1555   1555  1.46
LINK         O4  NAG A 474                 C1  NAG A 475     1555   1555  1.46
LINK         O4  NAG B 474                 C1  NAG B 475     1555   1555  1.46
LINK         O4  NAG A 475                 C1  BMA A 476     1555   1555  1.47
LINK         O4  NAG B 475                 C1  BMA B 476     1555   1555  1.47
LINK         ND2 ASN A 146                 C1  NAG A 474     1555   1555  1.49
LINK         ND2 ASN B 146                 C1  NAG B 474     1555   1555  1.49
LINK         ND2 ASN A 200                 C1  NAG A 478     1555   1555  1.50
LINK         ND2 ASN B 200                 C1  NAG B 478     1555   1555  1.50
LINK         O6  NAG A 474                 C1  FUL A 477     1555   1555  1.52
LINK         O6  NAG B 474                 C1  FUC B 477     1555   1555  1.52
LINK         O6  NAG A 478                 C1  MAN A 483     1555   1555  1.55
LINK         O6  NAG B 478                 C1  MAN B 483     1555   1555  1.55
LINK         O4  NAG B 479                 C1  BMA B 480     1555   1555  1.55
LINK         O4  NAG B 470                 C1  BMA B 471     1555   1555  1.55
LINK         O4  NAG A 478                 C1  NAG B 479     1555   1555  1.60
LINK         O4  NAG B 478                 C1  NAG B 470     1555   1555  1.60
LINK         O   GLY A 345                CA    CA A 470     1555   1555  1.92
LINK         O   GLY B 345                CA    CA B 488     1555   1555  1.92
LINK         O   GLN A 347                CA    CA A 470     1555   1555  1.98
LINK         O   GLN B 347                CA    CA B 488     1555   1555  1.98
LINK         O   ASP A 293                CA    CA A 470     1555   1555  2.57
LINK         O   ASP B 293                CA    CA B 488     1555   1555  2.57
LINK         O   GLY A 297                CA    CA A 470     1555   1555  2.92
LINK         O   GLY B 297                CA    CA B 488     1555   1555  2.92
CISPEP   1 TYR A  284    PRO A  285          0         0.31
CISPEP   2 THR A  325    PRO A  326          0        -0.76
CISPEP   3 TYR B  284    PRO B  285          0         0.31
CISPEP   4 THR B  325    PRO B  326          0        -0.76
SITE     1 CAA 11 ARG A 118  GLU A 119  ASP A 151  ARG A 152
SITE     2 CAA 11 TRP A 178  ILE A 222  ARG A 224  GLU A 276
SITE     3 CAA 11 ARG A 292  ARG A 371  TYR A 406
SITE     1 CAB 11 ARG B 118  GLU B 119  ASP B 151  ARG B 152
SITE     2 CAB 11 TRP B 178  ILE B 222  ARG B 224  GLU B 276
SITE     3 CAB 11 ARG B 292  ARG B 371  TYR B 406
SITE     1 AC1  7 GLU A  83  ASN A  86  SER A  88  TYR A 284
SITE     2 AC1  7 NAG A 473  NAG A 484  NAG A 485
SITE     1 AC2  2 LYS A  89  NAG A 472
SITE     1 AC3  5 ASN A 146  ASP A 147  TRP A 437  NAG A 475
SITE     2 AC3  5 FUL A 477
SITE     1 AC4  3 TRP A 437  NAG A 474  BMA A 476
SITE     1 AC5  1 NAG A 475
SITE     1 AC6  4 ASN A 146  ASP A 147  NAG A 474  PHE B 466
SITE     1 AC7  6 ASN A 200  MAN A 483  TYR B 453  GLY B 454
SITE     2 AC7  6 THR B 455  NAG B 479
SITE     1 AC8  3 NAG A 478  THR B 455  NAG B 479
SITE     1 AC9  6 NAG A 478  MAN A 483  ASN B 393  BMA B 480
SITE     2 AC9  6 MAN B 481  BMA B 482
SITE     1 BC1  4 GLN B 391  ARG B 394  NAG B 479  MAN B 481
SITE     1 BC2 10 PHE B 377  LYS B 378  GLN B 391  ILE B 392
SITE     2 BC2 10 ASN B 393  ARG B 394  GLN B 395  NAG B 479
SITE     3 BC2 10 BMA B 480  BMA B 482
SITE     1 BC3 10 TRP B 361  THR B 376  PHE B 377  ILE B 392
SITE     2 BC3 10 ASN B 393  ARG B 394  GLN B 395  TYR B 453
SITE     3 BC3 10 NAG B 479  MAN B 481
SITE     1 BC4  6 ASN A 234  TYR A 284  PRO A 285  GLU A 308
SITE     2 BC4  6 NAG A 472  NAG A 485
SITE     1 BC5  2 NAG A 472  NAG A 484
SITE     1 BC6  7 GLU B  83  ASN B  86  SER B  88  TYR B 284
SITE     2 BC6  7 NAG B 473  NAG B 486  NAG B 487
SITE     1 BC7  2 LYS B  89  NAG B 472
SITE     1 BC8  5 ASN B 146  ASP B 147  TRP B 437  NAG B 475
SITE     2 BC8  5 FUC B 477
SITE     1 BC9  3 TRP B 437  NAG B 474  BMA B 476
SITE     1 CC1  1 NAG B 475
SITE     1 CC2  4 PHE A 466  ASN B 146  ASP B 147  NAG B 474
SITE     1 CC3  6 TYR A 453  GLY A 454  THR A 455  ASN B 200
SITE     2 CC3  6 NAG B 470  MAN B 483
SITE     1 CC4  3 THR A 455  NAG B 470  NAG B 478
SITE     1 CC5  6 ASN A 393  BMA B 471  NAG B 478  MAN B 483
SITE     2 CC5  6 MAN B 484  MAN B 485
SITE     1 CC6  4 GLN A 391  ARG A 394  NAG B 470  MAN B 484
SITE     1 CC7 10 PHE A 377  LYS A 378  GLN A 391  ILE A 392
SITE     2 CC7 10 ASN A 393  ARG A 394  GLN A 395  NAG B 470
SITE     3 CC7 10 BMA B 471  MAN B 485
SITE     1 CC8 10 TRP A 361  THR A 376  PHE A 377  ILE A 392
SITE     2 CC8 10 ASN A 393  ARG A 394  GLN A 395  TYR A 453
SITE     3 CC8 10 NAG B 470  MAN B 484
SITE     1 CC9  6 ASN B 234  TYR B 284  PRO B 285  GLU B 308
SITE     2 CC9  6 NAG B 472  NAG B 487
SITE     1 DC1  2 NAG B 472  NAG B 486
SITE     1 DC2  6 ASP A 293  GLY A 297  ASP A 324  GLY A 345
SITE     2 DC2  6 THR A 346  GLN A 347
SITE     1 DC3  6 ASP B 293  GLY B 297  ASP B 324  GLY B 345
SITE     2 DC3  6 THR B 346  GLN B 347
SITE     1 DC4  9 ARG A 118  GLU A 119  ASP A 151  ARG A 152
SITE     2 DC4  9 TRP A 178  GLU A 276  GLU A 277  ARG A 371
SITE     3 DC4  9 TYR A 406
SITE     1 DC5  9 ARG B 118  GLU B 119  ASP B 151  ARG B 152
SITE     2 DC5  9 TRP B 178  GLU B 276  GLU B 277  ARG B 371
SITE     3 DC5  9 TYR B 406
CRYST1  119.740  141.020  141.780  90.00  90.00  90.00 C 2 2 21     16
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      0.008351  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007091  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007053        0.00000
      
PROCHECK
Go to PROCHECK summary
 References