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PDBsum entry 1a14

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Top Page protein ligands metals Protein-protein interface(s) links
Complex (antibody/antigen) PDB id
1a14
Jmol
Contents
Protein chains
388 a.a. *
120 a.a. *
104 a.a. *
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN
MAN
NAG
NDG
Metals
_CA
* Residue conservation analysis
HEADER    COMPLEX (ANTIBODY/ANTIGEN)              21-DEC-97   1A14
TITLE     COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN
TITLE    2 ANTIBODY WITH A 5 RESIDUE LINKER AND INFLUENZA VIRUS NEURAMINIDASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: N;
COMPND   4 FRAGMENT: RESIDUES 82 - 468;
COMPND   5 EC: 3.2.1.18;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: NC10 FV (HEAVY CHAIN);
COMPND   8 CHAIN: H;
COMPND   9 FRAGMENT: VH DOMAIN OF ANTI-NEURAMINIDASE ANTIBODY NC10 COVALENTLY
COMPND  10 JOINED BY A FIVE-RESIDUE POLYPEPTIDE LINKER;
COMPND  11 ENGINEERED: YES;
COMPND  12 MOL_ID: 3;
COMPND  13 MOLECULE: NC10 FV (LIGHT CHAIN);
COMPND  14 CHAIN: L;
COMPND  15 FRAGMENT: VL DOMAIN OF ANTI-NEURAMINIDASE ANTIBODY NC10 COVALENTLY
COMPND  16 JOINED BY A FIVE-RESIDUE POLYPEPTIDE LINKER;
COMPND  17 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_TAXID: 11320;
SOURCE   4 STRAIN: N9, A/TERN/AUSTRALIA/G70C/75;
SOURCE   5 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   8 ORGANISM_TAXID: 10090;
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  11 MOL_ID: 3;
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE  13 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE  14 ORGANISM_TAXID: 10090;
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    COMPLEX (ANTIBODY-ANTIGEN), SINGLE-CHAIN ANTIBODY, GLYCOSYLATED
KEYWDS   2 PROTEIN, COMPLEX (ANTIBODY-ANTIGEN) COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.L.MALBY,A.J.MCCOY,A.A.KORTT,P.J.HUDSON,P.M.COLMAN
REVDAT   4   13-JUL-11 1A14    1       VERSN
REVDAT   3   24-FEB-09 1A14    1       VERSN
REVDAT   2   01-APR-03 1A14    1       JRNL
REVDAT   1   13-MAY-98 1A14    0
JRNL        AUTH   R.L.MALBY,A.J.MCCOY,A.A.KORTT,P.J.HUDSON,P.M.COLMAN
JRNL        TITL   THREE-DIMENSIONAL STRUCTURES OF SINGLE-CHAIN
JRNL        TITL 2 FV-NEURAMINIDASE COMPLEXES.
JRNL        REF    J.MOL.BIOL.                   V. 279   901 1998
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   9642070
JRNL        DOI    10.1006/JMBI.1998.1794
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   R.L.MALBY,J.B.CALDWELL,L.C.GRUEN,V.R.HARLEY,N.IVANCIC,
REMARK   1  AUTH 2 A.A.KORTT,G.G.LILLEY,B.E.POWER,R.G.WEBSTER,P.M.COLMAN,
REMARK   1  AUTH 3 P.J.HUDSON
REMARK   1  TITL   RECOMBINANT ANTINEURAMINIDASE SINGLE CHAIN ANTIBODY:
REMARK   1  TITL 2 EXPRESSION, CHARACTERIZATION, AND CRYSTALLIZATION IN COMPLEX
REMARK   1  TITL 3 WITH ANTIGEN
REMARK   1  REF    PROTEINS                      V.  16    57 1993
REMARK   1  REFN                   ISSN 0887-3585
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 80.0
REMARK   3   NUMBER OF REFLECTIONS             : 27957
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : A POSTERIORI
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.200
REMARK   3   FREE R VALUE                     : 0.270
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
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            : 4800
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 112
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) : 5.00
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) : 0.014
REMARK   3   BOND ANGLES            (DEGREES) : 1.90
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  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : PARAM1.CHO
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : TOPH1.CHO
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1A14 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        : JUL-95
REMARK 200  TEMPERATURE           (KELVIN) : 283
REMARK 200  PH                             : 6.6-6.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-18B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : PHOTON FACTORY
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : WEIS
REMARK 200  DATA SCALING SOFTWARE          : PROTEIN
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29660
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 68.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.11800
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) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60
REMARK 200  COMPLETENESS FOR SHELL     (%) : 40.0
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1NMC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NC10 SCFV(5) AND N9 NA WERE MIXED
REMARK 280  TOGETHER (SCFV(5) IN FOUR-FOLD MOLAR EXCESS) WITH AND EQUAL
REMARK 280  VOLUME OF POTASSIUM PHOSPHATE BUFFER 1.7M PH6.6. THE DROP WAS
REMARK 280  EQUILIBRATED BY VAPOR DIFFUSION AGAINST PHOSPHATE BUFFER 1.3M
REMARK 280  PH6.8., VAPOR DIFFUSION
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       82.65000
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       82.65000
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       91.20000
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       82.65000
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       82.65000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       91.20000
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       82.65000
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       82.65000
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       91.20000
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       82.65000
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       82.65000
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       91.20000
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       82.65000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       82.65000
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       91.20000
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       82.65000
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       82.65000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       91.20000
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       82.65000
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       82.65000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       91.20000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       82.65000
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       82.65000
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       91.20000
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: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, H, L
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      165.30000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      165.30000
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      165.30000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      165.30000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     ARG N  304   CD   NE   CZ   NH1  NH2
REMARK 480     LYS N  435   CD   CE   NZ
REMARK 480     GLN H    1   CB   CG   CD   OE1  NE2
REMARK 480     GLN H    3   C    CG   CD   OE1  NE2
REMARK 480     GLN H    5   C    O    CG   CD   OE1  NE2
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 H    98     H    TYR H    99              1.53
REMARK 500   HG   SER H    87     H    VAL H   111              1.58
REMARK 500   ND2  ASN N    86     O    NDG N   477A             2.12
REMARK 500   O4   NAG N   469A    O5   NAG N   470B             2.19
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    ARG N 189   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG N 189   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    PRO N 267   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES
REMARK 500    PRO N 342   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES
REMARK 500    PRO H  52A  C   -  N   -  CA  ANGL. DEV. =   9.2 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    PHE N  84      126.63    -36.55
REMARK 500    LEU N  87       88.25    -65.90
REMARK 500    SER N  96     -164.37   -162.69
REMARK 500    TYR N 100      -55.21   -120.43
REMARK 500    TYR N 121      160.60    179.64
REMARK 500    THR N 148        8.71    -54.81
REMARK 500    THR N 188     -152.23   -139.76
REMARK 500    ASN N 200       29.51   -158.87
REMARK 500    ILE N 222       78.79     42.91
REMARK 500    THR N 225     -154.57   -116.30
REMARK 500    GLU N 277       73.87     42.69
REMARK 500    CYS N 291     -157.69   -107.79
REMARK 500    TRP N 295      -76.01    -52.47
REMARK 500    ASN N 346       45.40     37.45
REMARK 500    TYR N 374      117.56   -166.82
REMARK 500    VAL N 379       79.16   -116.81
REMARK 500    SER N 404     -126.01   -119.30
REMARK 500    TYR N 412A       4.13    -69.09
REMARK 500    ALA H  16     -158.64    -71.28
REMARK 500    SER H  17      102.32   -164.48
REMARK 500    SER H  25      142.81   -175.72
REMARK 500    PRO H  41       99.21    -65.71
REMARK 500    LEU H  82C     155.94    -46.66
REMARK 500    ALA H  88     -176.05    179.24
REMARK 500    SER H  98     -113.57     50.88
REMARK 500    TYR H 100A      34.36    -97.87
REMARK 500    THR L   8       87.28     75.60
REMARK 500    ASP L  28       97.78    -55.11
REMARK 500    ASP L  41       40.10    -95.64
REMARK 500    TYR L  50       61.07     68.41
REMARK 500    THR L  51      -63.41     62.71
REMARK 500    SER L  60      -19.19    -49.00
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 N 341         0.07    SIDE CHAIN
REMARK 500    TYR N 374         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    GLN N 226        23.7      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE THREE OLIGOSACCHARIDES COVALENTLY ATTACHED TO N9
REMARK 600 NEURAMINIDASE ARE NUMBERED BY THE ASN RESIDUE TO WHICH THEY
REMARK 600 ARE ATTACHED.
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     MAN N  475G
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 N 478  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY N 297   O
REMARK 620 2 ASP N 324   OD2  75.3
REMARK 620 3 ASN N 347   O   157.3  83.5
REMARK 620 4 ASP N 293   O    65.4  69.8  99.9
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG N 469A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG N 470B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA N 471C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN N 472D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN N 473E
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN N 474F
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN N 475G
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG N 476A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG N 477A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA N 478
DBREF  1A14 N   82   468  UNP    P03472   NRAM_IATRA      83    470
DBREF  1A14 H    1   111  GB     501094   AAA19165        23    142
DBREF  1A14 L    1   102  GB     501094   AAA19165       159    260
SEQRES   1 N  388  ARG ASP PHE ASN ASN LEU THR LYS GLY LEU CYS THR ILE
SEQRES   2 N  388  ASN SER TRP HIS ILE TYR GLY LYS ASP ASN ALA VAL ARG
SEQRES   3 N  388  ILE GLY GLU ASP SER ASP VAL LEU VAL THR ARG GLU PRO
SEQRES   4 N  388  TYR VAL SER CYS ASP PRO ASP GLU CYS ARG PHE TYR ALA
SEQRES   5 N  388  LEU SER GLN GLY THR THR ILE ARG GLY LYS HIS SER ASN
SEQRES   6 N  388  GLY THR ILE HIS ASP ARG SER GLN TYR ARG ALA LEU ILE
SEQRES   7 N  388  SER TRP PRO LEU SER SER PRO PRO THR VAL TYR ASN SER
SEQRES   8 N  388  ARG VAL GLU CYS ILE GLY TRP SER SER THR SER CYS HIS
SEQRES   9 N  388  ASP GLY LYS THR ARG MET SER ILE CYS ILE SER GLY PRO
SEQRES  10 N  388  ASN ASN ASN ALA SER ALA VAL ILE TRP TYR ASN ARG ARG
SEQRES  11 N  388  PRO VAL THR GLU ILE ASN THR TRP ALA ARG ASN ILE LEU
SEQRES  12 N  388  ARG THR GLN GLU SER GLU CYS VAL CYS HIS ASN GLY VAL
SEQRES  13 N  388  CYS PRO VAL VAL PHE THR ASP GLY SER ALA THR GLY PRO
SEQRES  14 N  388  ALA GLU THR ARG ILE TYR TYR PHE LYS GLU GLY LYS ILE
SEQRES  15 N  388  LEU LYS TRP GLU PRO LEU ALA GLY THR ALA LYS HIS ILE
SEQRES  16 N  388  GLU GLU CYS SER CYS TYR GLY GLU ARG ALA GLU ILE THR
SEQRES  17 N  388  CYS THR CYS ARG ASP ASN TRP GLN GLY SER ASN ARG PRO
SEQRES  18 N  388  VAL ILE ARG ILE ASP PRO VAL ALA MET THR HIS THR SER
SEQRES  19 N  388  GLN TYR ILE CYS SER PRO VAL LEU THR ASP ASN PRO ARG
SEQRES  20 N  388  PRO ASN ASP PRO THR VAL GLY LYS CYS ASN ASP PRO TYR
SEQRES  21 N  388  PRO GLY ASN ASN ASN ASN GLY VAL LYS GLY PHE SER TYR
SEQRES  22 N  388  LEU ASP GLY VAL ASN THR TRP LEU GLY ARG THR ILE SER
SEQRES  23 N  388  ILE ALA SER ARG SER GLY TYR GLU MET LEU LYS VAL PRO
SEQRES  24 N  388  ASN ALA LEU THR ASP ASP LYS SER LYS PRO THR GLN GLY
SEQRES  25 N  388  GLN THR ILE VAL LEU ASN THR ASP TRP SER GLY TYR SER
SEQRES  26 N  388  GLY SER PHE MET ASP TYR TRP ALA GLU GLY GLU CYS TYR
SEQRES  27 N  388  ARG ALA CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG PRO
SEQRES  28 N  388  LYS GLU ASP LYS VAL TRP TRP THR SER ASN SER ILE VAL
SEQRES  29 N  388  SER MET CYS SER SER THR GLU PHE LEU GLY GLN TRP ASP
SEQRES  30 N  388  TRP PRO ASP GLY ALA LYS ILE GLU TYR PHE LEU
SEQRES   1 H  120  GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS
SEQRES   2 H  120  PRO GLY ALA SER VAL ARG MET SER CYS LYS ALA SER GLY
SEQRES   3 H  120  TYR THR PHE THR ASN TYR ASN MET TYR TRP VAL LYS GLN
SEQRES   4 H  120  SER PRO GLY GLN GLY LEU GLU TRP ILE GLY ILE PHE TYR
SEQRES   5 H  120  PRO GLY ASN GLY ASP THR SER TYR ASN GLN LYS PHE LYS
SEQRES   6 H  120  ASP LYS ALA THR LEU THR ALA ASP LYS SER SER ASN THR
SEQRES   7 H  120  ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER
SEQRES   8 H  120  ALA VAL TYR TYR CYS ALA ARG SER GLY GLY SER TYR ARG
SEQRES   9 H  120  TYR ASP GLY GLY PHE ASP TYR TRP GLY GLN GLY THR THR
SEQRES  10 H  120  VAL THR VAL
SEQRES   1 L  104  ASP ILE GLU LEU THR GLN THR THR SER SER LEU SER ALA
SEQRES   2 L  104  SER LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER
SEQRES   3 L  104  GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN ASN
SEQRES   4 L  104  PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER
SEQRES   5 L  104  ASN LEU HIS SER GLU VAL PRO SER ARG PHE SER GLY SER
SEQRES   6 L  104  GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU
SEQRES   7 L  104  GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN ASP
SEQRES   8 L  104  PHE THR LEU PRO PHE THR PHE GLY GLY GLY THR ALA ALA
MODRES 1A14 ASN N  200  ASN  GLYCOSYLATION SITE
MODRES 1A14 ASN N  146  ASN  GLYCOSYLATION SITE
MODRES 1A14 ASN N   86  ASN  GLYCOSYLATION SITE
HET    NAG  N 469A     14
HET    NAG  N 470B     14
HET    BMA  N 471C     11
HET    MAN  N 472D     11
HET    MAN  N 473E     11
HET    MAN  N 474F     11
HET    MAN  N 475G     11
HET    NAG  N 476A     14
HET    NDG  N 477A     14
HET     CA  N 478       1
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM      CA CALCIUM ION
FORMUL   4  NAG    3(C8 H15 N O6)
FORMUL   4  BMA    C6 H12 O6
FORMUL   4  MAN    4(C6 H12 O6)
FORMUL   7  NDG    C8 H15 N O6
FORMUL   8   CA    CA 2+
HELIX    1   1 ALA N  105  GLU N  110  1                                   6
HELIX    2   2 ILE N  464  TYR N  466  5                                   3
HELIX    3   3 PHE H   29  ASN H   31  5                                   3
HELIX    4   4 GLN H   61  PHE H   63  5                                   3
HELIX    5   5 SER H   84  ASP H   86  5                                   3
HELIX    6   6 GLN L   80  ASP L   82  5                                   3
SHEET    1   A 4 TYR N 121  CYS N 124  0
SHEET    2   A 4 CYS N 129  SER N 135 -1  N  TYR N 132   O  TYR N 121
SHEET    3   A 4 ALA N 157  PRO N 162 -1  N  TRP N 161   O  PHE N 131
SHEET    4   A 4 ARG N 172  ILE N 176 -1  N  CYS N 175   O  LEU N 158
SHEET    1   B 4 SER N 179  HIS N 184  0
SHEET    2   B 4 ARG N 189  SER N 195 -1  N  ILE N 194   O  SER N 179
SHEET    3   B 4 SER N 202  TYR N 207 -1  N  TRP N 206   O  SER N 191
SHEET    4   B 4 PRO N 211  ASN N 216 -1  N  ILE N 215   O  ALA N 203
SHEET    1   C 4 VAL N 231  HIS N 233  0
SHEET    2   C 4 VAL N 236  ASP N 243 -1  N  PRO N 238   O  VAL N 231
SHEET    3   C 4 GLU N 251  LYS N 258 -1  N  PHE N 257   O  CYS N 237
SHEET    4   C 4 LYS N 261  PRO N 267 -1  N  GLU N 266   O  ILE N 254
SHEET    1   D 4 SER N 279  GLU N 283  0
SHEET    2   D 4 GLU N 286  THR N 290 -1  N  THR N 290   O  SER N 279
SHEET    3   D 4 PRO N 301  ASP N 306 -1  N  ILE N 305   O  ILE N 287
SHEET    4   D 4 THR N 311  TYR N 316 -1  N  GLN N 315   O  VAL N 302
SHEET    1   E 3 TRP N 361  ARG N 364  0
SHEET    2   E 3 TYR N 374  LYS N 378 -1  N  LEU N 377   O  LEU N 362
SHEET    3   E 3 GLN N 392  VAL N 398 -1  N  VAL N 398   O  TYR N 374
SHEET    1   F 4 SER N 407  MET N 411  0
SHEET    2   F 4 ALA N 420  GLY N 429 -1  N  TYR N 423   O  GLY N 408
SHEET    3   F 4 THR N 439  SER N 449 -1  N  MET N 446   O  PHE N 422
SHEET    4   F 4 SER N  96  LYS N 102 -1  N  GLY N 101   O  SER N 445
SHEET    1   G 4 GLN H   3  GLN H   6  0
SHEET    2   G 4 ARG H  19  SER H  25 -1  N  SER H  25   O  GLN H   3
SHEET    3   G 4 THR H  77  LEU H  82 -1  N  MET H  80   O  MET H  20
SHEET    4   G 4 ALA H  67  ASP H  72 -1  N  ASP H  72   O  THR H  77
SHEET    1   H 5 ASP H  56  TYR H  59  0
SHEET    2   H 5 GLY H  44  TYR H  52 -1  N  TYR H  52   O  ASP H  56
SHEET    3   H 5 ASN H  33  SER H  40 -1  N  SER H  40   O  GLY H  44
SHEET    4   H 5 VAL H  89  SER H  95 -1  N  ALA H  93   O  TYR H  35
SHEET    5   H 5 PHE H 100E TRP H 103 -1  N  TYR H 102   O  ARG H  94
SHEET    1   I 4 LEU L   4  THR L   7  0
SHEET    2   I 4 VAL L  19  ALA L  25 -1  N  ARG L  24   O  THR L   5
SHEET    3   I 4 ASP L  70  ILE L  75 -1  N  ILE L  75   O  VAL L  19
SHEET    4   I 4 PHE L  62  SER L  67 -1  N  SER L  67   O  ASP L  70
SHEET    1   J 4 THR L 102  ALA L 104  0
SHEET    2   J 4 ALA L  84  GLN L  90 -1  N  TYR L  86   O  THR L 102
SHEET    3   J 4 LEU L  33  GLN L  38 -1  N  GLN L  38   O  THR L  85
SHEET    4   J 4 VAL L  44  TYR L  49 -1  N  ILE L  48   O  TRP L  35
SSBOND   1 CYS N   92    CYS N  417                          1555   1555  2.03
SSBOND   2 CYS N  124    CYS N  129                          1555   1555  2.01
SSBOND   3 CYS N  175    CYS N  193                          1555   1555  2.02
SSBOND   4 CYS N  183    CYS N  230                          1555   1555  2.05
SSBOND   5 CYS N  232    CYS N  237                          1555   1555  2.04
SSBOND   6 CYS N  278    CYS N  291                          1555   1555  2.01
SSBOND   7 CYS N  280    CYS N  289                          1555   1555  2.01
SSBOND   8 CYS N  318    CYS N  337                          1555   1555  2.03
SSBOND   9 CYS N  421    CYS N  447                          1555   1555  2.03
SSBOND  10 CYS H   22    CYS H   92                          1555   1555  2.03
SSBOND  11 CYS L   23    CYS L   88                          1555   1555  2.02
LINK         C1  NAG N 469A                ND2 ASN N 200     1555   1555  1.46
LINK         O4  NAG N 469A                C1  NAG N 470B    1555   1555  1.33
LINK         O4  NAG N 470B                C1  BMA N 471C    1555   1555  1.40
LINK         O3  BMA N 471C                C1  MAN N 472D    1555   1555  1.39
LINK         O2  MAN N 472D                C1  MAN N 473E    1555   1555  1.40
LINK         O2  MAN N 473E                C1  MAN N 474F    1555   1555  1.39
LINK         C1  NAG N 476A                ND2 ASN N 146     1555   1555  1.45
LINK         C1  NDG N 477A                ND2 ASN N  86     1555   1555  1.54
LINK        CA    CA N 478                 O   GLY N 297     1555   1555  2.58
LINK        CA    CA N 478                 OD2 ASP N 324     1555   1555  3.40
LINK        CA    CA N 478                 O   ASN N 347     1555   1555  2.85
LINK        CA    CA N 478                 O   ASP N 293     1555   1555  3.06
CISPEP   1 ASN N  325    PRO N  326          0         0.64
CISPEP   2 ARG N  430    PRO N  431          0        -0.53
CISPEP   3 LEU L   94    PRO L   95          0         0.66
SITE     1 AC1  7 ASN N 199  ASN N 200  ARG N 220  LEU N 453
SITE     2 AC1  7 GLY N 454  GLN N 455  NAG N 470B
SITE     1 AC2  5 GLN N 392  GLY N 394  PHE N 452  NAG N 469A
SITE     2 AC2  5 BMA N 471C
SITE     1 AC3  6 LEU N 377  THR N 391  GLY N 394  NAG N 470B
SITE     2 AC3  6 MAN N 472D MAN N 475G
SITE     1 AC4  6 ARG N 364  GLU N 375  LEU N 377  BMA N 471C
SITE     2 AC4  6 MAN N 473E MAN N 474F
SITE     1 AC5  6 VAL N 321  ASP N 330  LYS N 389  PRO N 390
SITE     2 AC5  6 MAN N 472D MAN N 474F
SITE     1 AC6 10 ARG H 100  ASP H 100B TYR L  32  ARG N 327
SITE     2 AC6 10 ASN N 329  ASP N 330  ARG N 364  ILE N 366
SITE     3 AC6 10 MAN N 472D MAN N 473E
SITE     1 AC7  2 THR N 391  BMA N 471C
SITE     1 AC8  2 ASN N 146  TRP N 437
SITE     1 AC9  3 PHE N  84  ASN N  86  ASN N 234
SITE     1 BC1  4 ASP N 293  GLY N 297  ASP N 324  ASN N 347
CRYST1  165.300  165.300  182.400  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      0.006050  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006050  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005482        0.00000
      
PROCHECK
Go to PROCHECK summary
 References