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PDBsum entry 1ing

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Hydrolase (o-glycosyl) PDB id
1ing
Jmol
Contents
Protein chains
388 a.a. *
Ligands
NAG-NAG ×4
NAG-NAG-BMA-FUL
NAG-NAG-BMA-MAN-
MAN-MAN
×2
ST5 ×2
NAG-NAG-BMA-FUC
Metals
_CA ×2
Waters ×750
* Residue conservation analysis
HEADER    HYDROLASE (O-GLYCOSYL)                  07-JUL-95   1ING
TITLE     INFLUENZA A SUBTYPE N2 NEURAMINIDASE COMPLEXED WITH AROMATIC BANA109
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   3   13-JUL-11 1ING    1       VERSN
REVDAT   2   24-FEB-09 1ING    1       VERSN
REVDAT   1   17-AUG-96 1ING    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             : 19746
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) : 0.163
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            : 250
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) : 2.02
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 BANA109 INHIBITOR IS RESIDUE ST1 471.
REMARK   4
REMARK   4 1ING 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        : 20-NOV-93
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 11.8
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   : 21824
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) : 0.10600
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): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 11.8
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       69.81000
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       69.81000
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       59.71000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       69.53000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.71000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       69.53000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       69.81000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       59.71000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.53000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       69.81000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       59.71000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       69.53000
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   CA   GLY B   170     H2   HOH B   486              0.76
REMARK 500   CA   GLY B   170     O    HOH B   486              0.79
REMARK 500   O    GLY B   456     HO3  MAN A   483              0.80
REMARK 500   OG1  THR B   455     H61  NAG A   478              0.81
REMARK 500   C    GLY B   170     H2   HOH B   486              0.97
REMARK 500   N    ARG B   394     H2   HOH B   489              0.99
REMARK 500  HH21  ARG A   210     H1   HOH A   607              1.03
REMARK 500   H    ARG B   394     H2   HOH B   489              1.05
REMARK 500   CA   ARG B   394     O    HOH B   489              1.06
REMARK 500   CA   ARG B   394     H2   HOH B   489              1.20
REMARK 500   N    ARG B   394     O    HOH B   489              1.21
REMARK 500   HE   ARG B   327    HH21  ARG B   364              1.23
REMARK 500   HE   ARG A   327    HH21  ARG A   364              1.23
REMARK 500  HH12  ARG A    85     H2   HOH A   503              1.27
REMARK 500  HH12  ARG B    85     H2   HOH B   512              1.27
REMARK 500   CB   THR B   455     H61  NAG A   478              1.34
REMARK 500   CA   GLY B   170     H1   HOH B   486              1.34
REMARK 500   HE   ARG A   430     H1   HOH A   496              1.35
REMARK 500   HE   ARG B   430     H1   HOH B   505              1.35
REMARK 500  HH11  ARG A   283     HE   ARG A   288              1.42
REMARK 500  HH11  ARG B   283     HE   ARG B   288              1.42
REMARK 500  HH12  ARG A   283    HH21  ARG A   288              1.42
REMARK 500  HH12  ARG B   283    HH21  ARG B   288              1.42
REMARK 500   CA   ARG B   394     H1   HOH B   489              1.48
REMARK 500   O    LEU B   163     H1   HOH B   494              1.51
REMARK 500  HH11  ARG A   210     H2   HOH A   508              1.51
REMARK 500  HH11  ARG B   210     H2   HOH B   520              1.51
REMARK 500   CG2  THR B   455     H1   NAG A   478              1.53
REMARK 500   C    ARG B   394     H1   HOH B   489              1.53
REMARK 500   C    ARG B   394     O    HOH B   489              1.57
REMARK 500   C    GLY B   170     O    HOH B   486              1.59
REMARK 500   C    GLY B   170     H1   HOH B   486              1.59
REMARK 500   H    GLN A   173     O    GLY B   164              1.60
REMARK 500   O    ARG B   394     O    HOH B   489              1.94
REMARK 500   CB   ARG B   394     O    HOH B   489              1.95
REMARK 500   N    GLY B   170     O    HOH B   486              2.09
REMARK 500   OG1  THR B   455     C5   NAG A   478              2.13
REMARK 500   CB   THR B   455     C6   NAG A   478              2.15
REMARK 500   O    GLY B   170     O    HOH B   486              2.17
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   H3   FUL A   477     H4   MAN A   481     3654     0.40
REMARK 500   HZ1  LYS B   368     H1   HOH B   613     3654     0.46
REMARK 500   C4   FUL A   477     H61  MAN A   481     3654     0.59
REMARK 500   CA   GLY A   170     H2   HOH A   602     4555     0.76
REMARK 500   CA   GLY A   170     O    HOH A   602     4555     0.79
REMARK 500   O    GLY A   456     HO3  MAN B   483     4555     0.80
REMARK 500   OG1  THR A   455     H61  NAG B   478     4555     0.81
REMARK 500   O    ASN B   328     H2   HOH B   576     3654     0.84
REMARK 500   H5   FUL A   477     H62  MAN A   481     3654     0.93
REMARK 500   N    ASP B   329     H1   HOH B   576     3654     0.96
REMARK 500   C    GLY A   170     H2   HOH A   602     4555     0.97
REMARK 500   C    ASN B   328     H1   HOH B   576     3654     0.99
REMARK 500   N    ARG A   394     H2   HOH B   517     4555     0.99
REMARK 500  HH21  ARG B   210     H1   HOH A   553     4555     1.03
REMARK 500   H    ARG A   394     H2   HOH B   517     4555     1.05
REMARK 500   H4   FUL A   477     H61  MAN A   481     3654     1.06
REMARK 500   CA   ARG A   394     O    HOH B   517     4555     1.06
REMARK 500   NZ   LYS B   368     H1   HOH B   613     3654     1.09
REMARK 500   H3   FUL A   477     C4   MAN A   481     3654     1.19
REMARK 500   CA   ARG A   394     H2   HOH B   517     4555     1.20
REMARK 500   N    ARG A   394     O    HOH B   517     4555     1.21
REMARK 500   C5   FUL A   477     H61  MAN A   481     3654     1.22
REMARK 500   H4   FUL A   477     C6   MAN A   481     3654     1.27
REMARK 500   C3   FUL A   477     H4   MAN A   481     3654     1.30
REMARK 500   H5   FUL A   477     C6   MAN A   481     3654     1.33
REMARK 500   CB   THR A   455     H61  NAG B   478     4555     1.34
REMARK 500   CA   GLY A   170     H1   HOH A   602     4555     1.34
REMARK 500   O    GLY A   456     O3   MAN B   483     4555     1.34
REMARK 500   O    ASN B   328     H1   HOH B   576     3654     1.42
REMARK 500   HZ2  LYS B   368     H2   HOH B   613     3654     1.42
REMARK 500   CA   ARG A   394     H1   HOH B   517     4555     1.48
REMARK 500   C5   FUL A   477     H62  MAN A   481     3654     1.49
REMARK 500   O    LEU A   163     H1   HOH B   524     4555     1.51
REMARK 500   CG2  THR A   455     H1   NAG B   478     4555     1.53
REMARK 500   C    ARG A   394     H1   HOH B   517     4555     1.53
REMARK 500   CA   ASP B   329     H1   HOH B   576     3654     1.56
REMARK 500   CE   LYS B   368     H2   HOH B   613     3654     1.57
REMARK 500   C    ARG A   394     O    HOH B   517     4555     1.57
REMARK 500   NZ   LYS B   368     H2   HOH B   613     3654     1.58
REMARK 500   C    GLY A   170     O    HOH A   602     4555     1.59
REMARK 500   OD1  ASP A   313    HH12  ARG B   338     7554     1.59
REMARK 500   C    GLY A   170     H1   HOH A   602     4555     1.59
REMARK 500   O    GLY A   164     H    GLN B   173     4555     1.60
REMARK 500   OG1  THR A   455     C6   NAG B   478     4555     1.65
REMARK 500   OG1  THR A   455     O5   NAG B   478     4555     1.91
REMARK 500   O    ARG A   394     O    HOH B   517     4555     1.94
REMARK 500   CB   ARG A   394     O    HOH B   517     4555     1.95
REMARK 500   C    GLY A   456     O3   MAN B   483     4555     2.02
REMARK 500   N    GLY A   170     O    HOH A   602     4555     2.09
REMARK 500   OG1  THR A   455     C5   NAG B   478     4555     2.13
REMARK 500
REMARK 500 THIS ENTRY HAS      53 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 421   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES
REMARK 500    CYS B 421   CA  -  CB  -  SG  ANGL. DEV. =   6.8 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    TRP A  87       22.18     38.45
REMARK 500    SER A  88       50.77    -66.17
REMARK 500    PHE A 100      -49.36   -137.82
REMARK 500    LYS A 102      142.18   -175.97
REMARK 500    ASN A 104       18.02     46.01
REMARK 500    GLU A 119       73.13     44.34
REMARK 500    ALA A 133      138.33   -173.94
REMARK 500    HIS A 144        2.37    -69.34
REMARK 500    ASP A 147       20.87     82.70
REMARK 500    THR A 148        1.71    -65.84
REMARK 500    LEU A 163      106.86    -59.21
REMARK 500    LEU A 169      -22.91    -35.34
REMARK 500    CYS A 175      171.60    176.11
REMARK 500    ALA A 177      131.12   -173.06
REMARK 500    SER A 181      123.92    179.64
REMARK 500    ASP A 185      -17.65    -47.82
REMARK 500    LYS A 187      -30.51   -132.34
REMARK 500    ILE A 222       65.14     35.27
REMARK 500    GLU A 227       30.40     73.10
REMARK 500    ASP A 243      117.19   -167.98
REMARK 500    SER A 245      121.68   -179.04
REMARK 500    GLU A 259       57.40     79.17
REMARK 500    HIS A 264      155.15    173.76
REMARK 500    ALA A 269     -150.12   -101.55
REMARK 500    ALA A 272      132.43    -30.82
REMARK 500    HIS A 274       82.08    174.19
REMARK 500    GLU A 277       72.58     22.96
REMARK 500    TYR A 284      128.62    -24.38
REMARK 500    CYS A 291     -153.35   -110.94
REMARK 500    ASP A 293       96.92   -167.46
REMARK 500    TRP A 295      -75.50    -80.57
REMARK 500    LYS A 296       51.48   -149.82
REMARK 500    SER A 311     -177.43    -65.20
REMARK 500    SER A 315     -154.06   -171.98
REMARK 500    SER A 319      131.73    -37.78
REMARK 500    VAL A 322      135.35     71.28
REMARK 500    THR A 325      124.09   -170.29
REMARK 500    ASN A 328      -74.06    -64.29
REMARK 500    ASP A 329      133.68    158.43
REMARK 500    ASP A 330      -49.87    -21.98
REMARK 500    CYS A 337       -4.25     63.39
REMARK 500    GLN A 347      168.50    157.47
REMARK 500    VAL A 349      143.69   -171.68
REMARK 500    ALA A 353      164.66    175.41
REMARK 500    ASN A 356       97.58    168.34
REMARK 500    PRO A 386      151.74    -48.64
REMARK 500    ASN A 387       56.59     27.41
REMARK 500    SER A 404     -149.20   -128.60
REMARK 500    ARG A 430      151.16    -24.06
REMARK 500    LYS A 431      -75.88     81.68
REMARK 500
REMARK 500 THIS ENTRY HAS     108 RAMACHANDRAN OUTLIERS.
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 121         0.07    SIDE CHAIN
REMARK 500    TYR B 121         0.07    SIDE CHAIN
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    VAL A 174        24.4      L          L   OUTSIDE RANGE
REMARK 500    ARG A 300        24.8      L          L   OUTSIDE RANGE
REMARK 500    ARG A 430        23.3      L          L   OUTSIDE RANGE
REMARK 500    VAL B 174        24.4      L          L   OUTSIDE RANGE
REMARK 500    ARG B 300        24.8      L          L   OUTSIDE RANGE
REMARK 500    ARG B 430        23.3      L          L   OUTSIDE RANGE
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 487        DISTANCE =  7.29 ANGSTROMS
REMARK 525    HOH A 494        DISTANCE =  6.02 ANGSTROMS
REMARK 525    HOH A 554        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH A 556        DISTANCE =  8.96 ANGSTROMS
REMARK 525    HOH A 557        DISTANCE =  8.22 ANGSTROMS
REMARK 525    HOH A 560        DISTANCE =  9.13 ANGSTROMS
REMARK 525    HOH A 564        DISTANCE =  6.06 ANGSTROMS
REMARK 525    HOH A 568        DISTANCE =  9.69 ANGSTROMS
REMARK 525    HOH A 569        DISTANCE =  6.75 ANGSTROMS
REMARK 525    HOH A 570        DISTANCE =  5.93 ANGSTROMS
REMARK 525    HOH A 579        DISTANCE =  5.31 ANGSTROMS
REMARK 525    HOH A 582        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH A 584        DISTANCE = 10.77 ANGSTROMS
REMARK 525    HOH A 588        DISTANCE =  7.20 ANGSTROMS
REMARK 525    HOH A 589        DISTANCE =  5.94 ANGSTROMS
REMARK 525    HOH A 591        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH A 592        DISTANCE =  8.38 ANGSTROMS
REMARK 525    HOH A 597        DISTANCE =  6.85 ANGSTROMS
REMARK 525    HOH A 601        DISTANCE =  6.36 ANGSTROMS
REMARK 525    HOH B 502        DISTANCE =  6.02 ANGSTROMS
REMARK 525    HOH B 566        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH B 568        DISTANCE =  8.96 ANGSTROMS
REMARK 525    HOH B 569        DISTANCE =  8.22 ANGSTROMS
REMARK 525    HOH B 572        DISTANCE =  9.13 ANGSTROMS
REMARK 525    HOH B 580        DISTANCE =  9.69 ANGSTROMS
REMARK 525    HOH B 581        DISTANCE =  6.75 ANGSTROMS
REMARK 525    HOH B 591        DISTANCE =  5.31 ANGSTROMS
REMARK 525    HOH B 594        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH B 596        DISTANCE = 10.77 ANGSTROMS
REMARK 525    HOH B 600        DISTANCE =  7.20 ANGSTROMS
REMARK 525    HOH B 601        DISTANCE =  5.94 ANGSTROMS
REMARK 525    HOH B 603        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH B 604        DISTANCE =  8.38 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 470  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 293   O
REMARK 620 2 GLY A 297   O    98.8
REMARK 620 3 GLY A 345   O   110.8  94.4
REMARK 620 4 GLN A 347   O    92.1 167.3  87.7
REMARK 620 5 GLN A 347   OE1 156.5  80.6  92.6  86.8
REMARK 620 6 ASP A 324   OD2  87.4  80.2 161.7  94.0  69.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 470  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 293   O
REMARK 620 2 GLY B 297   O    98.8
REMARK 620 3 GLY B 345   O   110.8  94.4
REMARK 620 4 GLN B 347   O    92.1 167.3  87.7
REMARK 620 5 GLN B 347   OE1 156.5  80.6  92.6  86.8
REMARK 620 6 ASP B 324   OD2  87.4  80.2 161.7  94.0  69.3
REMARK 620 N                    1     2     3     4     5
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 NAG A 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 483
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 NAG B 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 482
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 483
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 484
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 485
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 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ST5 A 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ST5 B 471
DBREF  1ING A   82   469  UNP    P06820   NRAM_IATOK      82    469
DBREF  1ING B   82   469  UNP    P06820   NRAM_IATOK      82    469
SEQADV 1ING ASP A  339  UNP  P06820    ASN   339 CONFLICT
SEQADV 1ING 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 1ING ASN A   86  ASN  GLYCOSYLATION SITE
MODRES 1ING ASN A  146  ASN  GLYCOSYLATION SITE
MODRES 1ING ASN A  200  ASN  GLYCOSYLATION SITE
MODRES 1ING ASN A  234  ASN  GLYCOSYLATION SITE
MODRES 1ING ASN B   86  ASN  GLYCOSYLATION SITE
MODRES 1ING ASN B  146  ASN  GLYCOSYLATION SITE
MODRES 1ING ASN B  200  ASN  GLYCOSYLATION SITE
MODRES 1ING ASN B  234  ASN  GLYCOSYLATION SITE
MODRES 1ING THR B  455  THR  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    NAG  A 479      27
HET    BMA  A 480      21
HET    MAN  A 481      21
HET    MAN  A 482      22
HET    MAN  A 483      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    NAG  B 479      27
HET    BMA  B 480      21
HET    MAN  B 481      21
HET    MAN  B 482      22
HET    MAN  B 483      22
HET    NAG  B 484      27
HET    NAG  B 485      28
HET     CA  A 470       1
HET     CA  B 470       1
HET    ST5  A 471      23
HET    ST5  B 471      23
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     ST5 4-(ACETYLAMINO)-3-[(HYDROXYACETYL)AMINO]BENZOIC ACID
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL   3  NAG    16(C8 H15 N O6)
FORMUL   4  BMA    4(C6 H12 O6)
FORMUL   4  FUL    C6 H12 O5
FORMUL   5  MAN    6(C6 H12 O6)
FORMUL   8  FUC    C6 H12 O5
FORMUL  11   CA    2(CA 2+)
FORMUL  13  ST5    2(C11 H12 N2 O5)
FORMUL  15  HOH   *250(H2 O)
HELIX    1   1 SER A  105  ALA A  110  1                                   6
HELIX    2   2 LYS A  143  SER A  145  5                                   3
HELIX    3   3 SER B  105  ALA B  110  1                                   6
HELIX    4   4 LYS B  143  SER B  145  5                                   3
SHEET    1   A 3 THR A 157  GLU A 162  0
SHEET    2   A 3 CYS A 129  GLY A 135 -1  N  GLY A 135   O  THR A 157
SHEET    3   A 3 THR A 117  CYS A 124 -1  N  SER A 123   O  TYR A 130
SHEET    1   B 4 SER A 180  HIS A 184  0
SHEET    2   B 4 TRP A 189  GLY A 196 -1  N  VAL A 192   O  SER A 181
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  ASP A 243 -1  N  THR A 238   O  VAL A 231
SHEET    3   C 4 ASP A 251  ILE A 257 -1  N  ILE A 257   O  CYS A 237
SHEET    4   C 4 ILE A 265  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 ILE A 312  TYR A 316 -1  N  SER A 315   O  VAL A 302
SHEET    1   E 4 TRP A 352  ASN A 356  0
SHEET    2   E 4 ASP A 359  ARG A 364 -1  N  GLY A 363   O  TRP A 352
SHEET    3   E 4 TYR A 374  VAL A 379 -1  N  VAL A 379   O  LEU A 360
SHEET    4   E 4 GLN A 395  VAL A 398 -1  N  VAL A 398   O  TYR A 374
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 THR B 157  GLU B 162  0
SHEET    2   G 3 CYS B 129  GLY B 135 -1  N  GLY B 135   O  THR B 157
SHEET    3   G 3 THR B 117  CYS B 124 -1  N  SER B 123   O  TYR B 130
SHEET    1   H 4 SER B 180  HIS B 184  0
SHEET    2   H 4 TRP B 189  GLY B 196 -1  N  VAL B 192   O  SER B 181
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  ASP B 243 -1  N  THR B 238   O  VAL B 231
SHEET    3   I 4 ASP B 251  ILE B 257 -1  N  ILE B 257   O  CYS B 237
SHEET    4   I 4 ILE B 265  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 ILE B 312  TYR B 316 -1  N  SER B 315   O  VAL B 302
SHEET    1   K 4 TRP B 352  ASN B 356  0
SHEET    2   K 4 ASP B 359  ARG B 364 -1  N  GLY B 363   O  TRP B 352
SHEET    3   K 4 TYR B 374  VAL B 379 -1  N  VAL B 379   O  LEU B 360
SHEET    4   K 4 GLN B 395  VAL B 398 -1  N  VAL B 398   O  TYR B 374
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
SSBOND   1 CYS A   92    CYS A  417                          1555   1555  2.02
SSBOND   2 CYS A  124    CYS A  129                          1555   1555  2.04
SSBOND   3 CYS A  175    CYS A  193                          1555   1555  2.03
SSBOND   4 CYS A  183    CYS A  230                          1555   1555  2.02
SSBOND   5 CYS A  232    CYS A  237                          1555   1555  2.04
SSBOND   6 CYS A  278    CYS A  291                          1555   1555  2.04
SSBOND   7 CYS A  280    CYS A  289                          1555   1555  2.03
SSBOND   8 CYS A  318    CYS A  337                          1555   1555  2.04
SSBOND   9 CYS A  421    CYS A  447                          1555   1555  2.04
SSBOND  10 CYS B   92    CYS B  417                          1555   1555  2.02
SSBOND  11 CYS B  124    CYS B  129                          1555   1555  2.04
SSBOND  12 CYS B  175    CYS B  193                          1555   1555  2.03
SSBOND  13 CYS B  183    CYS B  230                          1555   1555  2.02
SSBOND  14 CYS B  232    CYS B  237                          1555   1555  2.04
SSBOND  15 CYS B  278    CYS B  291                          1555   1555  2.04
SSBOND  16 CYS B  280    CYS B  289                          1555   1555  2.03
SSBOND  17 CYS B  318    CYS B  337                          1555   1555  2.04
SSBOND  18 CYS B  421    CYS B  447                          1555   1555  2.04
LINK         C1  NAG A 472                 ND2 ASN A  86     1555   1555  1.46
LINK         O4  NAG A 472                 C1  NAG A 473     1555   1555  1.45
LINK         C1  NAG A 474                 ND2 ASN A 146     1555   1555  1.47
LINK         O4  NAG A 474                 C1  NAG A 475     1555   1555  1.45
LINK         O6  NAG A 474                 C1  FUL A 477     1555   1555  1.44
LINK         O4  NAG A 475                 C1  BMA A 476     1555   1555  1.47
LINK         C1  NAG A 478                 ND2 ASN A 200     1555   1555  1.45
LINK         O4  NAG A 478                 C1  NAG A 479     1555   1555  1.48
LINK         O6  NAG A 478                 C1  MAN A 483     1555   1555  1.43
LINK         O4  NAG A 479                 C1  BMA A 480     1555   1555  1.45
LINK         O3  BMA A 480                 C1  MAN A 481     1555   1555  1.45
LINK         O2  MAN A 481                 C1  MAN A 482     1555   1555  1.42
LINK         C1  NAG A 484                 ND2 ASN A 234     1555   1555  1.47
LINK         O4  NAG A 484                 C1  NAG A 485     1555   1555  1.44
LINK        CA    CA A 470                 O   ASP A 293     1555   1555  1.73
LINK        CA    CA A 470                 O   GLY A 297     1555   1555  2.36
LINK        CA    CA A 470                 O   GLY A 345     1555   1555  2.06
LINK        CA    CA A 470                 O   GLN A 347     1555   1555  2.01
LINK        CA    CA A 470                 OE1 GLN A 347     1555   1555  1.49
LINK         C1  NAG B 472                 ND2 ASN B  86     1555   1555  1.46
LINK         O4  NAG B 472                 C1  NAG B 473     1555   1555  1.45
LINK         C1  NAG B 474                 ND2 ASN B 146     1555   1555  1.47
LINK         O4  NAG B 474                 C1  NAG B 475     1555   1555  1.45
LINK         O6  NAG B 474                 C1  FUC B 477     1555   1555  1.44
LINK         O4  NAG B 475                 C1  BMA B 476     1555   1555  1.47
LINK         C1  NAG B 478                 ND2 ASN B 200     1555   1555  1.45
LINK         O4  NAG B 478                 C1  NAG B 479     1555   1555  1.48
LINK         O6  NAG B 478                 C1  MAN B 483     1555   1555  1.43
LINK         O4  NAG B 479                 C1  BMA B 480     1555   1555  1.45
LINK         O3  BMA B 480                 C1  MAN B 481     1555   1555  1.45
LINK         O2  MAN B 481                 C1  MAN B 482     1555   1555  1.42
LINK         C1  NAG B 484                 ND2 ASN B 234     1555   1555  1.47
LINK         O4  NAG B 484                 C1  NAG B 485     1555   1555  1.44
LINK        CA    CA B 470                 O   ASP B 293     1555   1555  1.73
LINK        CA    CA B 470                 O   GLY B 297     1555   1555  2.36
LINK        CA    CA B 470                 O   GLY B 345     1555   1555  2.06
LINK        CA    CA B 470                 O   GLN B 347     1555   1555  2.01
LINK        CA    CA B 470                 OE1 GLN B 347     1555   1555  1.49
LINK         OG1 THR B 455                 C6  NAG A 478     1555   1555  1.65
LINK        CA    CA A 470                 OD2 ASP A 324     1555   1555  3.28
LINK         C4  FUL A 477                 C6  MAN A 481     1555   3654  1.63
LINK         C5  FUL A 477                 C6  MAN A 481     1555   3654  1.66
LINK         C4  FUL A 477                 C6  MAN A 481     3654   1555  1.63
LINK         C5  FUL A 477                 C6  MAN A 481     3654   1555  1.66
LINK         OG1 THR B 455                 O5  NAG A 478     1555   1555  1.91
LINK         O   GLY B 456                 O3  MAN A 483     1555   1555  1.34
LINK         C   GLY B 456                 O3  MAN A 483     1555   1555  2.02
LINK        CA    CA B 470                 OD2 ASP B 324     1555   1555  3.28
LINK         O5  NAG B 478                 OG1 THR A 455     1555   4555  1.91
LINK         C6  NAG B 478                 OG1 THR A 455     1555   4555  1.65
LINK         O3  MAN B 483                 C   GLY A 456     1555   4555  2.02
LINK         O3  MAN B 483                 O   GLY A 456     1555   4555  1.34
CISPEP   1 TYR A  284    PRO A  285          0        -0.82
CISPEP   2 THR A  325    PRO A  326          0         0.87
CISPEP   3 TYR B  284    PRO B  285          0        -0.82
CISPEP   4 THR B  325    PRO B  326          0         0.87
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  5 ASN A  86  SER A  88  TYR A 284  NAG A 473
SITE     2 AC1  5 NAG A 485
SITE     1 AC2  1 NAG A 472
SITE     1 AC3  4 ASN A 146  TRP A 437  NAG A 475  FUL A 477
SITE     1 AC4  2 NAG A 474  BMA A 476
SITE     1 AC5  1 NAG A 475
SITE     1 AC6  2 NAG A 474  MAN A 481
SITE     1 AC7  8 ASP A 197  ASN A 200  NAG A 479  MAN A 483
SITE     2 AC7  8 TYR B 453  GLY B 454  THR B 455  HOH B 490
SITE     1 AC8  3 NAG A 478  BMA A 480  MAN A 483
SITE     1 AC9  3 NAG A 479  MAN A 481  MAN A 483
SITE     1 BC1  3 FUL A 477  BMA A 480  MAN A 482
SITE     1 BC2  2 MAN A 481  ASN B 463
SITE     1 BC3  8 ASP A 197  NAG A 478  NAG A 479  BMA A 480
SITE     2 BC3  8 VAL B 396  THR B 455  GLY B 456  SER B 457
SITE     1 BC4  2 ASN A 234  NAG A 485
SITE     1 BC5  2 NAG A 472  NAG A 484
SITE     1 BC6  5 ASN B  86  SER B  88  TYR B 284  NAG B 473
SITE     2 BC6  5 NAG B 485
SITE     1 BC7  1 NAG B 472
SITE     1 BC8  4 ASN B 146  TRP B 437  NAG B 475  FUC B 477
SITE     1 BC9  2 NAG B 474  BMA B 476
SITE     1 CC1  1 NAG B 475
SITE     1 CC2  1 NAG B 474
SITE     1 CC3  8 TYR A 453  GLY A 454  THR A 455  ASP B 197
SITE     2 CC3  8 ASN B 200  NAG B 479  MAN B 483  HOH B 518
SITE     1 CC4  3 NAG B 478  BMA B 480  MAN B 483
SITE     1 CC5  3 NAG B 479  MAN B 481  MAN B 483
SITE     1 CC6  2 BMA B 480  MAN B 482
SITE     1 CC7  1 MAN B 481
SITE     1 CC8  8 VAL A 396  THR A 455  GLY A 456  SER A 457
SITE     2 CC8  8 ASP B 197  NAG B 478  NAG B 479  BMA B 480
SITE     1 CC9  2 ASN B 234  NAG B 485
SITE     1 DC1  2 NAG B 472  NAG B 484
SITE     1 DC2  5 ASP A 293  GLY A 297  ASP A 324  GLY A 345
SITE     2 DC2  5 GLN A 347
SITE     1 DC3  5 ASP B 293  GLY B 297  ASP B 324  GLY B 345
SITE     2 DC3  5 GLN B 347
SITE     1 DC4 10 ARG A 118  ASP A 151  ARG A 152  ALA A 246
SITE     2 DC4 10 GLU A 276  ARG A 292  ASN A 294  ARG A 371
SITE     3 DC4 10 TYR A 406  HOH A 571
SITE     1 DC5 10 ARG B 118  ASP B 151  ARG B 152  ALA B 246
SITE     2 DC5 10 GLU B 276  ARG B 292  ASN B 294  ARG B 371
SITE     3 DC5 10 TYR B 406  HOH B 583
CRYST1  119.420  139.060  139.620  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      0.008374  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007191  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007162        0.00000
      
PROCHECK
Go to PROCHECK summary
 References