spacer
spacer

PDBsum entry 1nmb

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Complex (hydrolase/immunoglobulin) PDB id
1nmb
Jmol
Contents
Protein chains
388 a.a. *
109 a.a. *
122 a.a. *
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN-MAN
NAG ×2
Metals
_CA
Waters ×83
* Residue conservation analysis
HEADER    COMPLEX (HYDROLASE/IMMUNOGLOBULIN)      17-JAN-95   1NMB
TITLE     THE STRUCTURE OF A COMPLEX BETWEEN THE NC10 ANTIBODY AND INFLUENZA
TITLE    2 VIRUS NEURAMINIDASE AND COMPARISON WITH THE OVERLAPPING BINDING SITE
TITLE    3 OF THE NC41 ANTIBODY
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: N9 NEURAMINIDASE;
COMPND   3 CHAIN: N;
COMPND   4 EC: 3.2.1.18;
COMPND   5 MUTATION: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: FAB NC10;
COMPND   8 CHAIN: L;
COMPND   9 OTHER_DETAILS: RESOLUTION OF 2.5 ANGSTROMS;
COMPND  10 MOL_ID: 3;
COMPND  11 MOLECULE: FAB NC10;
COMPND  12 CHAIN: H;
COMPND  13 OTHER_DETAILS: RESOLUTION OF 2.5 ANGSTROMS
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_TAXID: 11320;
SOURCE   4 MOL_ID: 2;
SOURCE   5 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   6 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   7 ORGANISM_TAXID: 10090;
SOURCE   8 OTHER_DETAILS: ISOLATED FROM MONOCLONAL MURINE ANTIBODY;
SOURCE   9 MOL_ID: 3;
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE  11 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE  12 ORGANISM_TAXID: 10090;
SOURCE  13 OTHER_DETAILS: ISOLATED FROM MONOCLONAL MURINE ANTIBODY
KEYWDS    COMPLEX (HYDROLASE-IMMUNOGLOBULIN), COMPLEX (HYDROLASE-
KEYWDS   2 IMMUNOGLOBULIN) COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.L.MALBY,W.R.TULIP,P.M.COLMAN
REVDAT   4   13-JUL-11 1NMB    1       VERSN
REVDAT   3   24-FEB-09 1NMB    1       VERSN
REVDAT   2   01-APR-03 1NMB    1       JRNL
REVDAT   1   15-SEP-95 1NMB    0
JRNL        AUTH   R.L.MALBY,W.R.TULIP,V.R.HARLEY,J.L.MCKIMM-BRESCHKIN,
JRNL        AUTH 2 W.G.LAVER,R.G.WEBSTER,P.M.COLMAN
JRNL        TITL   THE STRUCTURE OF A COMPLEX BETWEEN THE NC10 ANTIBODY AND
JRNL        TITL 2 INFLUENZA VIRUS NEURAMINIDASE AND COMPARISON WITH THE
JRNL        TITL 3 OVERLAPPING BINDING SITE OF THE NC41 ANTIBODY
JRNL        REF    STRUCTURE                     V.   2   733 1994
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   7994573
JRNL        DOI    10.1016/S0969-2126(00)00074-5
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   P.M.COLMAN,W.R.TULIP,J.N.VARGHESE,P.A.TULLOCH,A.T.BAKER,
REMARK   1  AUTH 2 W.G.LAVER,G.M.AIR,R.G.WEBSTER
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURES OF INFLUENZA VIRUS
REMARK   1  TITL 2 NEURAMINIDASE-ANTIBODY COMPLEXES
REMARK   1  REF    PHILOS.TRANS.R.SOC.LONDON,    V. 323   511 1989
REMARK   1  REF  2 SER.B
REMARK   1  REFN                   ISSN 0080-4622
REMARK   1 REFERENCE 2
REMARK   1  AUTH   W.R.TULIP,J.N.VARGHESE,R.G.WEBSTER,G.M.AIR,W.G.LAVER,
REMARK   1  AUTH 2 P.M.COLMAN
REMARK   1  TITL   CRYSTAL STRUCTURE OF NEURAMINIDASE-ANTIBODY COMPLEXES
REMARK   1  REF    COLD SPRING HARBOR            V. LIV   257 1989
REMARK   1  REF  2 SYMP.QUANT.BIOL.
REMARK   1  REFN                   ISSN 0091-7451
REMARK   1 REFERENCE 3
REMARK   1  AUTH   W.R.TULIP,V.R.HARLEY,R.G.WEBSTER,J.NOVOTNY
REMARK   1  TITL   N9 NEURAMINIDASE COMPLEXES WITH ANTIBODIES NC41 AND NC10:
REMARK   1  TITL 2 EMPIRICAL FREE ENERGY CALCULATIONS CAPTURE SPECIFICITY
REMARK   1  TITL 3 TRENDS OBSERVED WITH MUTANT BINDING DATA
REMARK   1  REF    BIOCHEMISTRY                  V.  33  7986 1994
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 4
REMARK   1  AUTH   W.R.TULIP,J.N.VARGHESE,W.G.LAVER,R.G.WEBSTER,P.M.COLMAN
REMARK   1  TITL   REFINED CRYSTAL STRUCTURE OF THE INFLUENZA VIRUS N9
REMARK   1  TITL 2 NEURAMINIDASE-NC41 COMPLEX
REMARK   1  REF    J.MOL.BIOL.                   V. 227   122 1992
REMARK   1  REFN                   ISSN 0022-2836
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)) : 2.000
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             : 31862
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            : 4859
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 112
REMARK   3   SOLVENT ATOMS            : 83
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) : 0.014
REMARK   3   BOND ANGLES            (DEGREES) : 2.00
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 WHOLE OF THE CONSTANT MODULE OF THE FAB (CL AND
REMARK   3  CH1) IS NOT OBSERVED IN ELECTRON DENSITY MAPS AND IS
REMARK   3  PRESUMABLY DISORDERED.
REMARK   3
REMARK   3  THE IDENTITY OF THR L 7 IS IN QUESTION AND IT COULD BE PRO.
REMARK   3  THEREFORE IT IS ASSIGNED AN OCCUPANCY OF 0.0.
REMARK   4
REMARK   4 1NMB 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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 65.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61
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       84.70000
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       84.70000
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       78.45000
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       84.70000
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       84.70000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       78.45000
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       84.70000
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       84.70000
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       78.45000
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       84.70000
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       84.70000
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       78.45000
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       84.70000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       84.70000
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       78.45000
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       84.70000
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       84.70000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       78.45000
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       84.70000
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       84.70000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       78.45000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       84.70000
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       84.70000
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       78.45000
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 300 REMARK: CARBOHYDRATE 200A - 200G IS COVALENTLY ATTACHED TO THE
REMARK 300 NEURAMINIDASE SUBUNIT WHICH IS NEIGHBORING TO THE ONE IN
REMARK 300 THIS FILE.
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, L, H
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET N     0
REMARK 465     ASN N     1
REMARK 465     PRO N     2
REMARK 465     ASN N     3
REMARK 465     GLN N     4
REMARK 465     LYS N     5
REMARK 465     ILE N     6
REMARK 465     LEU N     7
REMARK 465     CYS N     8
REMARK 465     THR N     9
REMARK 465     SER N    10
REMARK 465     ALA N    11
REMARK 465     THR N    12
REMARK 465     ALA N    13
REMARK 465     LEU N    14
REMARK 465     VAL N    15
REMARK 465     ILE N    16
REMARK 465     GLY N    17
REMARK 465     THR N    18
REMARK 465     ILE N    19
REMARK 465     ALA N    20
REMARK 465     VAL N    21
REMARK 465     LEU N    22
REMARK 465     ILE N    23
REMARK 465     GLY N    24
REMARK 465     ILE N    25
REMARK 465     VAL N    26
REMARK 465     ASN N    27
REMARK 465     LEU N    28
REMARK 465     GLY N    29
REMARK 465     LEU N    30
REMARK 465     ASN N    31
REMARK 465     ILE N    32
REMARK 465     GLY N    33
REMARK 465     LEU N    34
REMARK 465     HIS N    35
REMARK 465     LEU N    36
REMARK 465     LYS N    37
REMARK 465     PRO N    38
REMARK 465     SER N    39
REMARK 465     CYS N    40
REMARK 465     ASN N    41
REMARK 465     CYS N    42
REMARK 465     SER N    43
REMARK 465     ARG N    44
REMARK 465     SER N    45
REMARK 465     GLN N    46
REMARK 465     PRO N    47
REMARK 465     GLU N    48
REMARK 465     ALA N    49
REMARK 465     THR N    50
REMARK 465     ASN N    51
REMARK 465     ALA N    52
REMARK 465     SER N    53
REMARK 465     GLN N    54
REMARK 465     THR N    55
REMARK 465     ILE N    56
REMARK 465     ILE N    57
REMARK 465     ASN N    58
REMARK 465     ASN N    59
REMARK 465     TYR N    60
REMARK 465     TYR N    61
REMARK 465     ASN N    62
REMARK 465     GLU N    63
REMARK 465     THR N    64
REMARK 465     ASN N    65
REMARK 465     ILE N    66
REMARK 465     THR N    67
REMARK 465     GLN N    68
REMARK 465     ILE N    69
REMARK 465     SER N    70
REMARK 465     ASN N    71
REMARK 465     THR N    72
REMARK 465     ASN N    73
REMARK 465     ILE N    74
REMARK 465     GLN N    75
REMARK 465     VAL N    76
REMARK 465     GLU N    77
REMARK 465     GLU N    78
REMARK 465     ARG N    79
REMARK 465     ALA N    80
REMARK 465     SER N    81
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475   M RES C SSEQI
REMARK 475     THR L    7
REMARK 475     ALA L  109
REMARK 475     PRO H   41
REMARK 475     SER H  112
REMARK 475     SER H  113
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     GLN L   27   CB   CG   CD   OE1  NE2
REMARK 480     LYS L   45   CB   CG   CD   CE   NZ
REMARK 480     GLU L   81   CB   CG   CD   OE1  OE2
REMARK 480     ARG L  107   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     LEU H   11   CB   CG   CD1  CD2
REMARK 480     SER H   84   CB   OG
REMARK 480     ARG H  100   CB   CG   CD   NE   CZ   NH1  NH2
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   O4   NAG N   470B    O5   BMA N   471C             2.15
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   ND2  ASN N   200     C1   NAG N   469A    3655     1.46
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 N 175   CA  -  CB  -  SG  ANGL. DEV. =   9.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN N  85      172.34    -56.17
REMARK 500    LEU N  87       69.85    -67.96
REMARK 500    LYS N 102      118.00   -173.29
REMARK 500    ASP N 111       57.65   -154.27
REMARK 500    ASP N 113       68.61   -104.55
REMARK 500    ARG N 118      171.90    173.58
REMARK 500    PRO N 126        2.02    -54.68
REMARK 500    ASP N 127       21.76   -158.16
REMARK 500    SER N 164       -4.05     79.05
REMARK 500    PRO N 167       94.33    -69.58
REMARK 500    CYS N 175      169.16    179.37
REMARK 500    THR N 181      159.07    174.27
REMARK 500    ASN N 208       50.96     74.06
REMARK 500    ASN N 221       83.90   -159.21
REMARK 500    THR N 225     -153.71   -133.50
REMARK 500    THR N 247       34.40   -155.86
REMARK 500    LYS N 264      177.48    166.80
REMARK 500    GLU N 283      133.90    166.51
REMARK 500    CYS N 291     -162.12   -123.10
REMARK 500    THR N 311     -166.06   -115.50
REMARK 500    GLN N 315     -152.35   -171.55
REMARK 500    ASN N 346       44.64     71.83
REMARK 500    SER N 353      146.74   -173.73
REMARK 500    ARG N 371       68.36   -101.64
REMARK 500    ASN N 381       34.74     38.44
REMARK 500    GLN N 395      116.55   -177.90
REMARK 500    ILE N 397      -41.38   -135.67
REMARK 500    SER N 404     -144.06   -111.43
REMARK 500    PHE N 410      156.32    176.74
REMARK 500    PHE N 452       59.26   -102.62
REMARK 500    THR L   8      105.08    128.84
REMARK 500    ASN L  31      -11.44     80.72
REMARK 500    PRO L  40      -22.65    -35.50
REMARK 500    THR L  51      -60.96     70.06
REMARK 500    PRO L  59      124.67    -38.83
REMARK 500    ALA H  16     -166.66    -79.89
REMARK 500    ASN H  54       15.68   -157.92
REMARK 500    LYS H  64       28.81    -70.27
REMARK 500    ASP H  65      -56.11   -143.09
REMARK 500    SER H  82B      61.86     68.24
REMARK 500    ALA H  88     -160.81   -165.61
REMARK 500    SER H  98      -99.78     61.17
REMARK 500    TYR H 100A      54.58   -112.43
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 100         0.07    SIDE CHAIN
REMARK 500    TYR N 341         0.07    SIDE CHAIN
REMARK 500    TYR N 423         0.12    SIDE CHAIN
REMARK 500    TYR L  36         0.08    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    ASP N 151        23.9      L          L   OUTSIDE RANGE
REMARK 500    GLN N 226        23.2      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 83 SOLVENT ATOMS AND 1 CALCIUM ATOM INCLUDED IN MODEL.
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 ASN N 347   O   163.6
REMARK 620 3 HOH N 499   O    81.1  83.5
REMARK 620 4 ASP N 324   OD2  80.4 103.3  83.5
REMARK 620 5 ASP N 293   O    86.1 109.7 166.4  89.7
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 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 NAG 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  1NMB N    0   468  UNP    P05803   NRAM_IAWHM       1    470
DBREF  1NMB L    1   107  GB     501094   AAA19165       159    265
DBREF  1NMB H    1   112  GB     501094   AAA19165        23    143
SEQADV 1NMB GLN L    3  GB   501094    GLU   161 CONFLICT
SEQADV 1NMB MET L    4  GB   501094    LEU   162 CONFLICT
SEQADV 1NMB PRO H    7  GB   501094    SER    29 CONFLICT
SEQADV 1NMB LEU H  109  GB   501094    VAL   140 CONFLICT
SEQRES   1 N  470  MET ASN PRO ASN GLN LYS ILE LEU CYS THR SER ALA THR
SEQRES   2 N  470  ALA LEU VAL ILE GLY THR ILE ALA VAL LEU ILE GLY ILE
SEQRES   3 N  470  VAL ASN LEU GLY LEU ASN ILE GLY LEU HIS LEU LYS PRO
SEQRES   4 N  470  SER CYS ASN CYS SER ARG SER GLN PRO GLU ALA THR ASN
SEQRES   5 N  470  ALA SER GLN THR ILE ILE ASN ASN TYR TYR ASN GLU THR
SEQRES   6 N  470  ASN ILE THR GLN ILE SER ASN THR ASN ILE GLN VAL GLU
SEQRES   7 N  470  GLU ARG ALA SER ARG GLU PHE ASN ASN LEU THR LYS GLY
SEQRES   8 N  470  LEU CYS THR ILE ASN SER TRP HIS ILE TYR GLY LYS ASP
SEQRES   9 N  470  ASN ALA VAL ARG ILE GLY GLU ASP SER ASP VAL LEU VAL
SEQRES  10 N  470  THR ARG GLU PRO TYR VAL SER CYS ASP PRO ASP GLU CYS
SEQRES  11 N  470  ARG PHE TYR ALA LEU SER GLN GLY THR THR ILE ARG GLY
SEQRES  12 N  470  LYS HIS SER ASN GLY THR ILE HIS ASP ARG SER GLN TYR
SEQRES  13 N  470  ARG ASP LEU ILE SER TRP PRO LEU SER SER PRO PRO THR
SEQRES  14 N  470  VAL TYR ASN SER ARG VAL GLU CYS ILE GLY TRP SER SER
SEQRES  15 N  470  THR SER CYS HIS ASP GLY ARG ALA ARG MET SER ILE CYS
SEQRES  16 N  470  ILE SER GLY PRO ASN ASN ASN ALA SER ALA VAL ILE TRP
SEQRES  17 N  470  TYR ASN ARG ARG PRO VAL THR GLU ILE ASN THR TRP ALA
SEQRES  18 N  470  ARG ASN ILE LEU ARG THR GLN GLU SER GLU CYS VAL CYS
SEQRES  19 N  470  GLN ASN GLY VAL CYS PRO VAL VAL PHE THR ASP GLY SER
SEQRES  20 N  470  ALA THR GLY PRO ALA GLU THR ARG ILE TYR TYR PHE LYS
SEQRES  21 N  470  GLU GLY LYS ILE LEU LYS TRP GLU PRO LEU THR GLY THR
SEQRES  22 N  470  ALA LYS HIS ILE GLU GLU CYS SER CYS TYR GLY GLU GLN
SEQRES  23 N  470  ALA GLY VAL THR CYS THR CYS ARG ASP ASN TRP GLN GLY
SEQRES  24 N  470  SER ASN ARG PRO VAL ILE GLN ILE ASP PRO VAL ALA MET
SEQRES  25 N  470  THR HIS THR SER GLN TYR ILE CYS SER PRO VAL LEU THR
SEQRES  26 N  470  ASP ASN PRO ARG PRO ASN ASP PRO THR VAL GLY LYS CYS
SEQRES  27 N  470  ASN ASP PRO TYR PRO GLY ASN ASN ASN ASN GLY VAL LYS
SEQRES  28 N  470  GLY PHE SER TYR LEU ASP GLY GLY ASN THR TRP LEU GLY
SEQRES  29 N  470  ARG THR ILE SER ILE ALA SER ARG SER GLY TYR GLU MET
SEQRES  30 N  470  LEU LYS VAL PRO ASN ALA LEU THR ASP ASP ARG SER LYS
SEQRES  31 N  470  PRO THR GLN GLY GLN THR ILE VAL LEU ASN THR ASP TRP
SEQRES  32 N  470  SER GLY TYR SER GLY SER PHE MET ASP TYR TRP ALA GLU
SEQRES  33 N  470  GLY GLU CYS TYR ARG ALA CYS PHE TYR VAL GLU LEU ILE
SEQRES  34 N  470  ARG GLY ARG PRO LYS GLU ASP LYS VAL TRP TRP THR SER
SEQRES  35 N  470  ASN SER ILE VAL SER MET CYS SER SER THR GLU PHE LEU
SEQRES  36 N  470  GLY GLN TRP ASN TRP PRO ASP GLY ALA LYS ILE GLU TYR
SEQRES  37 N  470  PHE LEU
SEQRES   1 L  109  ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA
SEQRES   2 L  109  SER LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER
SEQRES   3 L  109  GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN ASN
SEQRES   4 L  109  PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER
SEQRES   5 L  109  ASN LEU HIS SER GLU VAL PRO SER ARG PHE SER GLY SER
SEQRES   6 L  109  GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU
SEQRES   7 L  109  GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN ASP
SEQRES   8 L  109  PHE THR LEU PRO PHE THR PHE GLY GLY GLY THR LYS LEU
SEQRES   9 L  109  GLU ILE ARG ARG ALA
SEQRES   1 H  122  GLN VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS
SEQRES   2 H  122  PRO GLY ALA SER VAL ARG MET SER CYS LYS ALA SER GLY
SEQRES   3 H  122  TYR THR PHE THR ASN TYR ASN MET TYR TRP VAL LYS GLN
SEQRES   4 H  122  SER PRO GLY GLN GLY LEU GLU TRP ILE GLY ILE PHE TYR
SEQRES   5 H  122  PRO GLY ASN GLY ASP THR SER TYR ASN GLN LYS PHE LYS
SEQRES   6 H  122  ASP LYS ALA THR LEU THR ALA ASP LYS SER SER ASN THR
SEQRES   7 H  122  ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER
SEQRES   8 H  122  ALA VAL TYR TYR CYS ALA ARG SER GLY GLY SER TYR ARG
SEQRES   9 H  122  TYR ASP GLY GLY PHE ASP TYR TRP GLY GLN GLY THR THR
SEQRES  10 H  122  LEU THR VAL SER SER
MODRES 1NMB ASN N   86  ASN  GLYCOSYLATION SITE
MODRES 1NMB ASN N  146  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    NAG  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      CA CALCIUM ION
FORMUL   4  NAG    4(C8 H15 N O6)
FORMUL   4  BMA    C6 H12 O6
FORMUL   4  MAN    4(C6 H12 O6)
FORMUL   7   CA    CA 2+
FORMUL   8  HOH   *83(H2 O)
HELIX    1   1 ALA N  105  ASP N  111  1                                   7
HELIX    2   2 LYS N  143  SER N  145  5                                   3
HELIX    3   3 ILE N  464  PHE N  467  5                                   4
HELIX    4   4 GLN L   80  ASP L   82  5                                   3
HELIX    5   5 PHE H   29  ASN H   31  5                                   3
HELIX    6   6 GLN H   61  PHE H   63  5                                   3
HELIX    7   7 SER H   84  ASP H   86  5                                   3
SHEET    1   A 4 TYR N 121  ASP N 125  0
SHEET    2   A 4 GLU N 128  LEU N 134 -1  N  TYR N 132   O  TYR N 121
SHEET    3   A 4 ASP 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  GLN N 233  0
SHEET    2   C 4 VAL N 236  GLY N 244 -1  N  PRO N 238   O  VAL N 231
SHEET    3   C 4 ALA N 250  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 GLY 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  VAL 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  PHE N 410  0
SHEET    2   F 4 CYS N 421  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  ASP N 103 -1  N  ASP N 103   O  ILE N 443
SHEET    1   G 2 SER L  10  ALA L  13  0
SHEET    2   G 2 LYS L 103  ILE L 106  1  N  LYS L 103   O  LEU L  11
SHEET    1   H 3 VAL L  19  ARG L  24  0
SHEET    2   H 3 ASP L  70  ILE L  75 -1  N  ILE L  75   O  VAL L  19
SHEET    3   H 3 PHE L  62  SER L  67 -1  N  SER L  67   O  ASP L  70
SHEET    1   I 3 THR L  85  GLN L  90  0
SHEET    2   I 3 LEU L  33  GLN L  38 -1  N  GLN L  38   O  THR L  85
SHEET    3   I 3 VAL L  44  ILE L  48 -1  N  ILE L  48   O  TRP L  35
SHEET    1   J 4 GLN H   3  GLN H   5  0
SHEET    2   J 4 SER H  17  SER H  25 -1  N  SER H  25   O  GLN H   3
SHEET    3   J 4 THR H  77  SER H  82A-1  N  LEU H  82   O  VAL H  18
SHEET    4   J 4 ALA H  67  ASP H  72 -1  N  ASP H  72   O  THR H  77
SHEET    1   K 6 ALA H   9  LYS H  13  0
SHEET    2   K 6 THR H 107  SER H 112  1  N  THR H 108   O  GLU H  10
SHEET    3   K 6 ALA H  88  ARG H  94 -1  N  TYR H  90   O  THR H 107
SHEET    4   K 6 MET H  34  SER H  40 -1  N  GLN H  39   O  VAL H  89
SHEET    5   K 6 GLY H  44  TYR H  52 -1  N  PHE H  51   O  MET H  34
SHEET    6   K 6 ASP H  56  TYR H  59 -1  N  SER H  58   O  ILE H  50
SHEET    1   L 2 ALA H  93  SER H  95  0
SHEET    2   L 2 PHE H 100E TRP H 103 -1  N  TYR H 102   O  ARG H  94
SSBOND   1 CYS N   92    CYS N  417                          1555   1555  2.02
SSBOND   2 CYS N  124    CYS N  129                          1555   1555  2.03
SSBOND   3 CYS N  175    CYS N  193                          1555   1555  2.03
SSBOND   4 CYS N  183    CYS N  230                          1555   1555  2.04
SSBOND   5 CYS N  232    CYS N  237                          1555   1555  2.01
SSBOND   6 CYS N  278    CYS N  291                          1555   1555  2.04
SSBOND   7 CYS N  280    CYS N  289                          1555   1555  2.02
SSBOND   8 CYS N  318    CYS N  337                          1555   1555  2.04
SSBOND   9 CYS N  421    CYS N  447                          1555   1555  2.03
SSBOND  10 CYS L   23    CYS L   88                          1555   1555  2.02
SSBOND  11 CYS H   22    CYS H   92                          1555   1555  2.06
LINK         ND2 ASN N  86                 C1  NAG N 477A    1555   1555  1.44
LINK         ND2 ASN N 146                 C1  NAG N 476A    1555   1555  1.41
LINK         O4  NAG N 469A                C1  NAG N 470B    1555   1555  1.49
LINK         O4  NAG N 470B                C1  BMA N 471C    1555   1555  1.39
LINK         O3  BMA N 471C                C1  MAN N 472D    1555   1555  1.42
LINK         O6  BMA N 471C                C1  MAN N 475G    1555   1555  1.47
LINK         O2  MAN N 472D                C1  MAN N 473E    1555   1555  1.43
LINK         O2  MAN N 473E                C1  MAN N 474F    1555   1555  1.39
LINK         ND2 ASN N 200                 C1  NAG N 469A    4565   1555  1.46
LINK        CA    CA N 478                 O   GLY N 297     1555   1555  2.32
LINK        CA    CA N 478                 O   ASN N 347     1555   1555  2.64
LINK        CA    CA N 478                 O   HOH N 499     1555   1555  2.55
LINK        CA    CA N 478                 OD2 ASP N 324     1555   1555  3.08
LINK        CA    CA N 478                 O   ASP N 293     1555   1555  2.37
CISPEP   1 ASN N  325    PRO N  326          0        -0.17
CISPEP   2 ARG N  430    PRO N  431          0         0.09
CISPEP   3 LEU L   94    PRO L   95          0        -0.09
SITE     1 AC1  6 ASN N 200  ARG N 220  LEU N 453  GLY N 454
SITE     2 AC1  6 GLN N 455  NAG N 470B
SITE     1 AC2  5 GLN N 392  GLY N 394  GLN N 455  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  5 ARG N 364  GLU N 375  BMA N 471C MAN N 473E
SITE     2 AC4  5 MAN N 474F
SITE     1 AC5  6 ASP N 330  ARG N 364  LYS N 389  PRO N 390
SITE     2 AC5  6 MAN N 472D MAN N 474F
SITE     1 AC6  9 ASP H 100B ARG N 327  ASN N 329  ASP N 330
SITE     2 AC6  9 ARG N 364  ILE N 366  ILE N 368  MAN N 472D
SITE     3 AC6  9 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  5 GLU N  83  PHE N  84  ASN N  86  GLN N 233
SITE     2 AC9  5 ASN N 234
SITE     1 BC1  5 ASP N 293  GLY N 297  ASP N 324  ASN N 347
SITE     2 BC1  5 HOH N 499
CRYST1  169.400  169.400  156.900  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      0.005903  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005903  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006373        0.00000
      
PROCHECK
Go to PROCHECK summary
 References