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PDBsum entry 1nn2

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Hydrolase (o-glycosyl) PDB id
1nn2
Jmol
Contents
Protein chain
388 a.a.
Ligands
NAG-NAG
NAG-NAG-BMA-MAN-
NAG-NGK-FUL
NAG-NAG-BMA-MAN-
MAN-MAN
NAG ×2
Metals
_CA
Waters ×258
HEADER    HYDROLASE (O-GLYCOSYL)                  28-MAR-91   1NN2
TITLE     THREE-DIMENSIONAL STRUCTURE OF THE NEURAMINIDASE OF INFLUENZA VIRUS
TITLE    2 A(SLASH)TOKYO(SLASH)3(SLASH)67 AT 2.2 ANGSTROMS RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.18;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/TOKYO/3/1967(H2N2));
SOURCE   3 ORGANISM_TAXID: 380960;
SOURCE   4 STRAIN: A/TOKYO/3/1967(H2N2)
KEYWDS    HYDROLASE (O-GLYCOSYL)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.N.VARGHESE,P.M.COLMAN
REVDAT   5   13-JUL-11 1NN2    1       VERSN
REVDAT   4   25-AUG-09 1NN2    1       SOURCE
REVDAT   3   24-FEB-09 1NN2    1       VERSN
REVDAT   2   01-APR-03 1NN2    1       JRNL
REVDAT   1   15-JUL-92 1NN2    0
JRNL        AUTH   J.N.VARGHESE,P.M.COLMAN
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF THE NEURAMINIDASE OF
JRNL        TITL 2 INFLUENZA VIRUS A/TOKYO/3/67 AT 2.2 A RESOLUTION.
JRNL        REF    J.MOL.BIOL.                   V. 221   473 1991
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   1920428
JRNL        DOI    10.1016/0022-2836(91)80068-6
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
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             : NULL
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) : 0.210
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            : 3022
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 221
REMARK   3   SOLVENT ATOMS            : 86
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) : 0.020
REMARK   3   BOND ANGLES            (DEGREES) : 3.90
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: NULL
REMARK   4
REMARK   4 1NN2 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        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   -X,Y,-Z
REMARK 290       6555   X,-Y,-Z
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2
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        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  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        0.00000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       69.80000
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       69.80000
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       95.50000
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       69.80000
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       69.80000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       95.50000
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       69.80000
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       69.80000
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       95.50000
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       69.80000
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       69.80000
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       95.50000
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       69.80000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       69.80000
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       95.50000
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       69.80000
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       69.80000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       95.50000
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       69.80000
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       69.80000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       95.50000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       69.80000
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       69.80000
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       95.50000
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
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  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      139.60000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      139.60000
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000      139.60000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      139.60000
REMARK 350   BIOMT3   4  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   HG   SER A   228     HZ3  LYS A   350              1.37
REMARK 500   HG   SER A   411    HH11  ARG A   420              1.37
REMARK 500   O4   NAG A   476E    H1   NGK A   477F             1.50
REMARK 500   O6   NAG A   472A    H1   FUL A   478I             1.52
REMARK 500   HG   SER A   279     HZ1  LYS A   350              1.58
REMARK 500   H    THR A   117     HG   SER A   440              1.60
REMARK 500   O6   NAG A   472A    C2   FUL A   478I             2.12
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   H1   HOH A   490     H1   HOH A   490    16665     0.83
REMARK 500   HZ2  LYS A   415     H1   HOH A   518     3655     1.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    HIS A 144   NE2   HIS A 144   CD2    -0.069
REMARK 500    HIS A 155   NE2   HIS A 155   CD2    -0.069
REMARK 500    HIS A 184   NE2   HIS A 184   CD2    -0.072
REMARK 500    HIS A 191   NE2   HIS A 191   CD2    -0.070
REMARK 500    HIS A 274   NE2   HIS A 274   CD2    -0.074
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    TRP A  87   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    TRP A  87   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG A 107   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG A 107   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    TRP A 115   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    TRP A 115   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES
REMARK 500    CYS A 124   CB  -  CA  -  C   ANGL. DEV. =  13.6 DEGREES
REMARK 500    CYS A 124   N   -  CA  -  CB  ANGL. DEV. = -21.9 DEGREES
REMARK 500    CYS A 124   CA  -  CB  -  SG  ANGL. DEV. =   7.2 DEGREES
REMARK 500    CYS A 129   CA  -  CB  -  SG  ANGL. DEV. =   7.9 DEGREES
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    MET A 160   CG  -  SD  -  CE  ANGL. DEV. =  15.0 DEGREES
REMARK 500    ARG A 172   CG  -  CD  -  NE  ANGL. DEV. = -14.4 DEGREES
REMARK 500    ARG A 172   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    TRP A 178   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TRP A 178   CB  -  CG  -  CD1 ANGL. DEV. =  -9.7 DEGREES
REMARK 500    TRP A 178   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.4 DEGREES
REMARK 500    TRP A 178   CG  -  CD2 -  CE3 ANGL. DEV. =   6.6 DEGREES
REMARK 500    CYS A 183   CA  -  CB  -  SG  ANGL. DEV. =   9.8 DEGREES
REMARK 500    TRP A 189   CD1 -  CG  -  CD2 ANGL. DEV. =   6.7 DEGREES
REMARK 500    TRP A 189   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    ARG A 210   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    TRP A 218   CD1 -  CG  -  CD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    TRP A 218   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG A 224   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES
REMARK 500    ARG A 224   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES
REMARK 500    GLN A 226   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES
REMARK 500    CYS A 230   CA  -  CB  -  SG  ANGL. DEV. =   7.0 DEGREES
REMARK 500    MET A 241   CG  -  SD  -  CE  ANGL. DEV. = -14.9 DEGREES
REMARK 500    ARG A 253   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES
REMARK 500    ARG A 253   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A 292   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ASP A 293   CA  -  C   -  N   ANGL. DEV. = -17.2 DEGREES
REMARK 500    TRP A 295   CD1 -  CG  -  CD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    TRP A 295   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES
REMARK 500    GLY A 297   CA  -  C   -  N   ANGL. DEV. = -20.4 DEGREES
REMARK 500    GLY A 297   O   -  C   -  N   ANGL. DEV. =  11.1 DEGREES
REMARK 500    ARG A 300   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG A 300   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ARG A 327   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES
REMARK 500    GLN A 347   CA  -  C   -  N   ANGL. DEV. = -12.3 DEGREES
REMARK 500    TRP A 352   CD1 -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES
REMARK 500    TRP A 352   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES
REMARK 500    TRP A 361   CD1 -  CG  -  CD2 ANGL. DEV. =   8.4 DEGREES
REMARK 500    TRP A 361   CG  -  CD1 -  NE1 ANGL. DEV. =  -7.1 DEGREES
REMARK 500    TRP A 361   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES
REMARK 500    ARG A 364   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG A 371   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG A 371   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    TRP A 383   CD1 -  CG  -  CD2 ANGL. DEV. =   7.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      68 ANGLE DEVIATIONS.
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       35.53     37.49
REMARK 500    PHE A 100      -40.91   -131.52
REMARK 500    PRO A 126        1.34    -65.64
REMARK 500    ASP A 147       40.48     70.49
REMARK 500    CYS A 175      168.95    179.58
REMARK 500    ASN A 200       48.96   -151.78
REMARK 500    ASN A 221       89.56   -160.56
REMARK 500    ILE A 222       85.71     43.75
REMARK 500    GLN A 226      -56.69    -27.97
REMARK 500    HIS A 274      114.17   -160.11
REMARK 500    GLU A 277       60.64     39.33
REMARK 500    TYR A 284      130.68    -30.94
REMARK 500    CYS A 291     -164.44   -117.35
REMARK 500    TRP A 295      -75.12    -99.68
REMARK 500    SER A 319      133.35    -32.54
REMARK 500    VAL A 322      118.46     59.68
REMARK 500    ASP A 329      157.39    141.51
REMARK 500    SER A 332       34.13    -92.19
REMARK 500    CYS A 337       -5.25     69.69
REMARK 500    ASN A 342       14.31     59.88
REMARK 500    GLN A 347      178.26     81.93
REMARK 500    ASN A 387       12.21     58.85
REMARK 500    SER A 404     -145.40   -126.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     NGK A  477F
REMARK 610     NAG A  485A
REMARK 610     NAG A  486B
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615   M RES C SSEQI
REMARK 615     NAG A  471B
REMARK 615     BMA A  474C
REMARK 615     MAN A  475D
REMARK 615     NAG A  476E
REMARK 615     NAG A  486B
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   1  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 293   O
REMARK 620 2 GLY A 297   O    86.3
REMARK 620 3 GLN A 347   O    89.9 170.5
REMARK 620 4 GLY A 345   O   109.0  91.8  97.7
REMARK 620 5 ASP A 324   OD2  67.0  69.3 101.3 160.6
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 470A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 472A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 473B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGK A 477F
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUL A 478I
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 479A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 480B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 481C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 482D
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 483E
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 484F
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 485A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1
DBREF  1NN2 A   82   469  UNP    P06820   NRAM_IATOK      82    469
SEQADV 1NN2 ASP A  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
MODRES 1NN2 ASN A   86  ASN  GLYCOSYLATION SITE
MODRES 1NN2 ASN A  146  ASN  GLYCOSYLATION SITE
MODRES 1NN2 ASN A  200  ASN  GLYCOSYLATION SITE
HET    NAG  A 470A     27
HET    NAG  A 471B     28
HET    NAG  A 472A     26
HET    NAG  A 473B     27
HET    BMA  A 474C     21
HET    MAN  A 475D     21
HET    NAG  A 476E     27
HET    NGK  A 477F     31
HET    FUL  A 478I     21
HET    NAG  A 479A     27
HET    NAG  A 480B     27
HET    BMA  A 481C     20
HET    MAN  A 482D     21
HET    MAN  A 483E     22
HET    MAN  A 484F     22
HET    NAG  A 485A     28
HET    NAG  A 486B     28
HET     CA  A   1       1
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     NGK 2-(ACETYLAMINO)-2-DEOXY-4-O-SULFO-ALPHA-D-
HETNAM   2 NGK  GALACTOPYRANOSE
HETNAM     FUL BETA-L-FUCOSE
HETNAM      CA CALCIUM ION
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL   2  NAG    9(C8 H15 N O6)
FORMUL   3  BMA    2(C6 H12 O6)
FORMUL   3  MAN    4(C6 H12 O6)
FORMUL   3  NGK    C8 H15 N O9 S
FORMUL   3  FUL    C6 H12 O5
FORMUL   7   CA    CA 2+
FORMUL   8  HOH   *86(H2 O)
HELIX    1   1 ASN A  104  SER A  109  1                                   6
HELIX    2   2 ASN A  142  ASN A  146  5                                   5
SHEET    1   A 4 GLY A  96  LYS A 102  0
SHEET    2   A 4 THR A 439  THR A 449 -1  N  VAL A 445   O  SER A 101
SHEET    3   A 4 ILE A 418  GLY A 429 -1  O  ARG A 420   N  GLY A 448
SHEET    4   A 4 SER A 407  GLU A 413 -1  O  GLY A 408   N  TYR A 423
SHEET    1   B 4 TRP A 115  CYS A 124  0
SHEET    2   B 4 CYS A 129  THR A 139 -1  N  TYR A 130   O  SER A 123
SHEET    3   B 4 THR A 157  GLU A 162 -1  O  THR A 157   N  GLY A 135
SHEET    4   B 4 ARG A 172  ILE A 176 -1  O  ARG A 172   N  MET A 160
SHEET    1   C 4 SER A 179  HIS A 184  0
SHEET    2   C 4 TRP A 189  ASP A 197 -1  N  LEU A 190   O  CYS A 183
SHEET    3   C 4 ASN A 200  TYR A 207 -1  N  ASN A 200   O  ASP A 197
SHEET    4   C 4 ARG A 210  GLY A 216 -1  O  ARG A 210   N  TYR A 207
SHEET    1   D 4 LYS A 261  PRO A 267  0
SHEET    2   D 4 ALA A 250  GLU A 258 -1  N  ILE A 254   O  SER A 266
SHEET    3   D 4 THR A 236  GLY A 244 -1  O  CYS A 237   N  ILE A 257
SHEET    4   D 4 ARG A 224  THR A 225 -1  N  ARG A 224   O  THR A 242
SHEET    1   E 4 LYS A 261  PRO A 267  0
SHEET    2   E 4 ALA A 250  GLU A 258 -1  N  ILE A 254   O  SER A 266
SHEET    3   E 4 THR A 236  GLY A 244 -1  O  CYS A 237   N  ILE A 257
SHEET    4   E 4 VAL A 231  ILE A 233 -1  O  VAL A 231   N  THR A 238
SHEET    1   F 4 GLU A 276  ARG A 283  0
SHEET    2   F 4 GLY A 286  ARG A 292 -1  O  GLY A 286   N  ARG A 283
SHEET    3   F 4 PRO A 301  ASN A 306 -1  O  PRO A 301   N  CYS A 291
SHEET    4   F 4 ILE A 312  TYR A 316 -1  O  ASP A 313   N  ASP A 304
SHEET    1   G 4 ALA A 353  ASN A 356  0
SHEET    2   G 4 ASP A 359  ARG A 364 -1  N  ASP A 359   O  ASN A 356
SHEET    3   G 4 SER A 372  ILE A 380 -1  N  GLU A 375   O  ARG A 364
SHEET    4   G 4 SER A 390  ARG A 403 -1  O  SER A 390   N  ILE A 380
SSBOND   1 CYS A   92    CYS A  417                          1555   1555  2.02
SSBOND   2 CYS A  124    CYS A  129                          1555   1555  2.00
SSBOND   3 CYS A  175    CYS A  193                          1555   1555  2.01
SSBOND   4 CYS A  183    CYS A  230                          1555   1555  2.01
SSBOND   5 CYS A  232    CYS A  237                          1555   1555  2.03
SSBOND   6 CYS A  278    CYS A  291                          1555   1555  2.02
SSBOND   7 CYS A  280    CYS A  289                          1555   1555  2.01
SSBOND   8 CYS A  318    CYS A  337                          1555   1555  2.02
SSBOND   9 CYS A  421    CYS A  447                          1555   1555  2.03
LINK         ND2 ASN A  86                 C1  NAG A 470A    1555   1555  1.45
LINK         ND2 ASN A 146                 C1  NAG A 472A    1555   1555  1.46
LINK         ND2 ASN A 200                 C1  NAG A 479A    1555   1555  1.46
LINK         O4  NAG A 470A                C1  NAG A 471B    1555   1555  1.43
LINK         O4  NAG A 472A                C1  NAG A 473B    1555   1555  1.42
LINK         O6  NAG A 472A                C1  FUL A 478I    1555   1555  1.49
LINK         O4  NAG A 473B                C1  BMA A 474C    1555   1555  1.45
LINK         O3  BMA A 474C                C1  MAN A 475D    1555   1555  1.44
LINK         O4  MAN A 475D                C1  NAG A 476E    1555   1555  1.43
LINK         O4  NAG A 476E                C1  NGK A 477F    1555   1555  1.46
LINK         O4  NAG A 479A                C1  NAG A 480B    1555   1555  1.44
LINK         O4  NAG A 480B                C1  BMA A 481C    1555   1555  1.41
LINK         O3  BMA A 481C                C1  MAN A 482D    1555   1555  1.40
LINK         O6  BMA A 481C                C1  MAN A 484F    1555   1555  1.46
LINK         O2  MAN A 482D                C1  MAN A 483E    1555   1555  1.44
LINK        CA    CA A   1                 O   ASP A 293     1555   1555  2.11
LINK        CA    CA A   1                 O   GLY A 297     1555   1555  1.66
LINK        CA    CA A   1                 O   GLN A 347     1555   1555  1.76
LINK        CA    CA A   1                 O   GLY A 345     1555   1555  1.67
LINK        CA    CA A   1                 OD2 ASP A 324     1555   1555  3.36
LINK         O6  NAG A 472A                O5  FUL A 478I    1555   1555  2.00
LINK         O4  NAG A 476E                O5  NGK A 477F    1555   1555  1.93
CISPEP   1 TYR A  284    PRO A  285          0        -1.02
CISPEP   2 THR A  325    PRO A  326          0        -4.53
CISPEP   3 ARG A  430    LYS A  431          0         0.09
SITE     1 AC1  5 GLU A  83  ASN A  86  SER A  88  TYR A 284
SITE     2 AC1  5 NAG A 485A
SITE     1 AC2  4 ASN A 146  TRP A 437  NAG A 473B FUL A 478I
SITE     1 AC3  1 NAG A 472A
SITE     1 AC4  5 GLU A 433  THR A 434  ARG A 435  ASN A 465
SITE     2 AC4  5 HOH A 488
SITE     1 AC5  3 ASN A 463  PHE A 466  NAG A 472A
SITE     1 AC6  6 ASN A 200  TYR A 453  GLY A 454  THR A 455
SITE     2 AC6  6 NAG A 480B HOH A 565
SITE     1 AC7  7 ASN A 393  ARG A 394  TYR A 453  NAG A 479A
SITE     2 AC7  7 BMA A 481C MAN A 482D HOH A 557
SITE     1 AC8  8 GLN A 391  ILE A 392  ASN A 393  ARG A 394
SITE     2 AC8  8 NAG A 480B MAN A 482D MAN A 483E MAN A 484F
SITE     1 AC9  5 GLN A 391  NAG A 480B BMA A 481C MAN A 483E
SITE     2 AC9  5 HOH A 550
SITE     1 BC1  2 BMA A 481C MAN A 482D
SITE     1 BC2  1 BMA A 481C
SITE     1 BC3  5 ILE A 233  ASN A 234  TYR A 284  PRO A 285
SITE     2 BC3  5 NAG A 470A
SITE     1 BC4  5 ASP A 293  GLY A 297  ASP A 324  GLY A 345
SITE     2 BC4  5 GLN A 347
CRYST1  139.600  139.600  191.000  90.00  90.00  90.00 I 4 2 2      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      0.007163  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007163  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005236        0.00000
      
PROCHECK
Go to PROCHECK summary
 References