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PDBsum entry 1ncd

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Hydrolase(o-glycosyl) PDB id
1ncd
Jmol
Contents
Protein chains
389 a.a. *
214 a.a. *
221 a.a. *
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN
NAG
NAG-NAG
Metals
_CA
Waters ×69
* Residue conservation analysis
HEADER    HYDROLASE(O-GLYCOSYL)                   21-JAN-92   1NCD
TITLE     REFINED CRYSTAL STRUCTURE OF THE INFLUENZA VIRUS N9 NEURAMINIDASE-NC41
TITLE    2 FAB COMPLEX
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: INFLUENZA A SUBTYPE N9 NEURAMINIDASE;
COMPND   3 CHAIN: N;
COMPND   4 EC: 3.2.1.18;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: IGG2A-KAPPA NC41 FAB (LIGHT CHAIN);
COMPND   7 CHAIN: L;
COMPND   8 MOL_ID: 3;
COMPND   9 MOLECULE: IGG2A-KAPPA NC41 FAB (HEAVY CHAIN);
COMPND  10 CHAIN: H
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_TAXID: 11484;
SOURCE   4 STRAIN: (A/WHALE/MAINE/1/84(H13N9));
SOURCE   5 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   8 ORGANISM_TAXID: 10090;
SOURCE   9 MOL_ID: 3;
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE  11 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE  12 ORGANISM_TAXID: 10090
KEYWDS    HYDROLASE(O-GLYCOSYL)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    W.R.TULIP,J.N.VARGHESE,P.M.COLMAN
REVDAT   3   13-JUL-11 1NCD    1       VERSN
REVDAT   2   24-FEB-09 1NCD    1       VERSN
REVDAT   1   31-JAN-94 1NCD    0
JRNL        AUTH   W.R.TULIP,J.N.VARGHESE,W.G.LAVER,R.G.WEBSTER,P.M.COLMAN
JRNL        TITL   REFINED CRYSTAL STRUCTURE OF THE INFLUENZA VIRUS N9
JRNL        TITL 2 NEURAMINIDASE-NC41 FAB COMPLEX.
JRNL        REF    J.MOL.BIOL.                   V. 227   122 1992
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   1381757
JRNL        DOI    10.1016/0022-2836(92)90687-F
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   W.R.TULIP,J.N.VARGHESE,R.G.WEBSTER,W.G.LAVER,P.M.COLMAN
REMARK   1  TITL   CRYSTAL STRUCTURES OF TWO MUTANT NEURAMINIDASE-ANTIBODY
REMARK   1  TITL 2 COMPLEXES WITH AMINO ACID SUBSTITUTIONS IN THE INTERFACE
REMARK   1  REF    J.MOL.BIOL.                   V. 227   149 1992
REMARK   1  REFN                   ISSN 0022-2836
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 STRUCTURES OF NEURAMINIDASE-ANTIBODY COMPLEXES
REMARK   1  REF    COLD SPRING HARBOR            V.  54   257 1989
REMARK   1  REF  2 SYMP.QUANT.BIOL.
REMARK   1  REFN                   ISSN 0091-7451
REMARK   1 REFERENCE 3
REMARK   1  AUTH   P.M.COLMAN,W.G.LAVER,J.N.VARGHESE,A.T.BAKER,P.A.TULLOCH,
REMARK   1  AUTH 2 G.M.AIR,R.G.WEBSTER
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF A COMPLEX OF ANTIBODY WITH
REMARK   1  TITL 2 INFLUENZA VIRUS NEURAMINIDASE
REMARK   1  REF    NATURE                        V. 326   358 1987
REMARK   1  REFN                   ISSN 0028-0836
REMARK   2
REMARK   2 RESOLUTION.    2.90 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) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
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             : 18737
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) : 0.157
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            : 6401
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 115
REMARK   3   SOLVENT ATOMS            : 69
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) : 0.016
REMARK   3   BOND ANGLES            (DEGREES) : 3.60
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: THE COORDINATES OF THE CALCIUM ATOM ARE
REMARK   3  NOT WELL DETERMINED. THE REFERENCE STRUCTURE FOR THE CALCIUM ATOM
REMARK   3  IS THE N9 MUTANT S370L (PDB ENTRY 2NN9)
REMARK   4
REMARK   4 1NCD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
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   (%): 74.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 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+1/2,X+1/2,Z
REMARK 290       4555   Y+1/2,-X+1/2,Z
REMARK 290       5555   -X+1/2,Y+1/2,-Z
REMARK 290       6555   X+1/2,-Y+1/2,-Z
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       83.50000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       83.50000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       83.50000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       83.50000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       83.50000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       83.50000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       83.50000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       83.50000
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
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: THE COORDINATES OF THE CARBOHYDRATE IN THE EPITOPE CAN BE
REMARK 300 GENERATED FORM THE COORDINATES OF RESIDUES C 200A-C 200F BY
REMARK 300 APPLYING THE FOLLOWING TRANSFORMATION:
REMARK 300
REMARK 300       0.0     1.0     0.0     83.5
REMARK 300      -1.0     0.0     0.0     83.5
REMARK 300       0.0     0.0     1.0      0.0
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, 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 350   BIOMT1   2  0.000000  1.000000  0.000000       83.50000
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       83.50000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000       83.50000
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000      -83.50000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000      167.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
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 N 144   NE2   HIS N 144   CD2    -0.076
REMARK 500    HIS N 150   NE2   HIS N 150   CD2    -0.071
REMARK 500    HIS N 184   NE2   HIS N 184   CD2    -0.078
REMARK 500    HIS N 274   NE2   HIS N 274   CD2    -0.068
REMARK 500    HIS N 312   NE2   HIS N 312   CD2    -0.072
REMARK 500    HIS L  91   NE2   HIS L  91   CD2    -0.087
REMARK 500    HIS L 198   NE2   HIS L 198   CD2    -0.073
REMARK 500    HIS H 172   NE2   HIS H 172   CD2    -0.067
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 N  97   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP N  97   CB  -  CG  -  CD1 ANGL. DEV. =  -8.0 DEGREES
REMARK 500    TRP N  97   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES
REMARK 500    TRP N  97   CG  -  CD2 -  CE3 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ILE N  99   CB  -  CA  -  C   ANGL. DEV. = -12.1 DEGREES
REMARK 500    TYR N 100   CB  -  CG  -  CD2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ARG N 107   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG N 118   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    GLN N 136   CG  -  CD  -  NE2 ANGL. DEV. =  16.2 DEGREES
REMARK 500    ARG N 141   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES
REMARK 500    ARG N 156   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG N 156   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    ASP N 157   CA  -  CB  -  CG  ANGL. DEV. =  13.6 DEGREES
REMARK 500    TRP N 161   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP N 161   CB  -  CG  -  CD1 ANGL. DEV. =  -8.0 DEGREES
REMARK 500    TRP N 161   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.4 DEGREES
REMARK 500    TRP N 161   CG  -  CD2 -  CE3 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ARG N 172   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    CYS N 175   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES
REMARK 500    TRP N 178   CD1 -  CG  -  CD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    TRP N 178   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.5 DEGREES
REMARK 500    TRP N 206   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP N 206   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG N 210   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    TRP N 218   CD1 -  CG  -  CD2 ANGL. DEV. =   6.7 DEGREES
REMARK 500    TRP N 218   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ARG N 224   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    GLN N 226   N   -  CA  -  C   ANGL. DEV. =  17.8 DEGREES
REMARK 500    ARG N 253   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    TRP N 265   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    TRP N 265   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.5 DEGREES
REMARK 500    TRP N 265   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES
REMARK 500    TYR N 281   CB  -  CG  -  CD2 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    ARG N 292   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    TRP N 295   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    TRP N 295   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES
REMARK 500    TRP N 295   CG  -  CD2 -  CE3 ANGL. DEV. =   5.7 DEGREES
REMARK 500    GLY N 297   CA  -  C   -  N   ANGL. DEV. = -16.3 DEGREES
REMARK 500    ARG N 300   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ARG N 300   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG N 327   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    TRP N 361   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    TRP N 361   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES
REMARK 500    ARG N 364   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ARG N 387   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    TRP N 403   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP N 403   CB  -  CG  -  CD1 ANGL. DEV. =  -9.5 DEGREES
REMARK 500    TRP N 403   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES
REMARK 500    TRP N 403   CG  -  CD2 -  CE3 ANGL. DEV. =   6.7 DEGREES
REMARK 500    TYR N 406   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      98 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    SER N  96     -169.58   -170.11
REMARK 500    ARG N 118      159.45    178.12
REMARK 500    GLU N 119       82.60     56.05
REMARK 500    PRO N 167       92.30    -66.34
REMARK 500    ASN N 170        3.18   -152.77
REMARK 500    CYS N 175      174.31    174.83
REMARK 500    CYS N 183      149.63   -172.25
REMARK 500    ARG N 187      -66.60   -105.12
REMARK 500    ASN N 200       46.84   -154.13
REMARK 500    ARG N 220       25.34     46.74
REMARK 500    ILE N 222      102.28     45.21
REMARK 500    GLN N 226      -55.68    -27.03
REMARK 500    GLU N 251       78.21   -119.49
REMARK 500    GLU N 277       63.61     31.66
REMARK 500    CYS N 291     -150.09   -114.79
REMARK 500    TRP N 295      -97.83    -35.46
REMARK 500    VAL N 321       98.44    -68.84
REMARK 500    PRO N 331     -168.69    -66.08
REMARK 500    ASP N 356       50.47   -151.79
REMARK 500    ASN N 359       50.93   -102.67
REMARK 500    ASP N 386       23.66    -78.58
REMARK 500    SER N 404     -135.39   -128.39
REMARK 500    SER N 442     -169.72   -123.94
REMARK 500    ILE N 464       -6.73    -54.38
REMARK 500    SER L  30       49.02     36.08
REMARK 500    THR L  31       -0.16     71.23
REMARK 500    ALA L  51      -44.46     71.47
REMARK 500    ASP L  60       -0.89    -37.16
REMARK 500    HIS L  91       35.56   -140.82
REMARK 500    PRO L 141      175.14    -50.37
REMARK 500    SER L 168       32.69    -98.70
REMARK 500    LYS L 169      -93.51   -137.92
REMARK 500    ASN L 190      -50.47   -148.44
REMARK 500    THR L 200        1.72    -67.85
REMARK 500    THR L 202      -60.30   -135.82
REMARK 500    ASN L 210      141.93    178.28
REMARK 500    TYR H  27     -168.61   -112.93
REMARK 500    LYS H  43      -26.65   -171.95
REMARK 500    GLU H  62        5.29    -62.28
REMARK 500    ASN H  82B      74.67     42.59
REMARK 500    GLU H  85        6.12    -63.86
REMARK 500    ALA H  88     -169.19   -165.55
REMARK 500    PHE H  99      -11.46     81.62
REMARK 500    TYR H 102       99.22     56.90
REMARK 500    CYS H 128     -117.35     43.42
REMARK 500    THR H 134     -165.17     72.35
REMARK 500    SER H 180      -74.45     56.76
REMARK 500    SER H 216       64.79     92.23
REMARK 500    PRO H 225        2.84    -67.42
REMARK 500    ARG H 226       79.01    -20.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLY N  196     PRO N  197                  149.64
REMARK 500 GLY N  248     PRO N  249                  144.28
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 L 140         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 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   0  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN N 294   O
REMARK 620 2 ASP N 324   OD2 119.8
REMARK 620 3 GLY N 297   O   114.9  72.4
REMARK 620 4 ASP N 293   O    56.6  69.4  77.1
REMARK 620 5 ASN N 347   O    67.8  90.7 162.1  91.5
REMARK 620 6 ASN N 344   O    94.2 145.6  99.8 143.1  97.5
REMARK 620 N                    1     2     3     4     5
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 NAG N 475A
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 477B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA N 0
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF THE FOLLOWING RESIDUES DIFFERS FROM THE
REMARK 999 CHEMICAL SEQUENCE:
REMARK 999
REMARK 999  LYS H  46 WAS REFINED AS GLU
REMARK 999  THR H  87 WAS REFINED AS LYS
REMARK 999  VAL H 109 WAS REFINED AS LEU
REMARK 999  SER N  81 WAS REFINED AS ILE
DBREF  1NCD N   82   468  UNP    P05803   NRAM_IAWHM      83    470
DBREF  1NCD L    1   214  EMBL   Y11589   CAA72328         1    214
DBREF  1NCD H  114   227  UNP    P01865   GCAM_MOUSE       1    101
SEQADV 1NCD THR L   20  EMBL Y11589    SER    20 CONFLICT
SEQADV 1NCD ILE L   21  EMBL Y11589    VAL    21 CONFLICT
SEQADV 1NCD ASP L   28  EMBL Y11589    ILE    28 CONFLICT
SEQADV 1NCD SER L   30  EMBL Y11589    GLY    30 CONFLICT
SEQADV 1NCD ALA L   32  EMBL Y11589    ASN    32 CONFLICT
SEQADV 1NCD VAL L   34  EMBL Y11589    ALA    34 CONFLICT
SEQADV 1NCD LEU L   46  EMBL Y11589    ALA    46 CONFLICT
SEQADV 1NCD TRP L   50  EMBL Y11589    SER    50 CONFLICT
SEQADV 1NCD THR L   53  EMBL Y11589    TYR    53 CONFLICT
SEQADV 1NCD HIS L   55  EMBL Y11589    TYR    55 CONFLICT
SEQADV 1NCD ILE L   56  EMBL Y11589    SER    56 CONFLICT
SEQADV 1NCD ALA L   63  EMBL Y11589    THR    63 CONFLICT
SEQADV 1NCD TYR L   71  EMBL Y11589    PHE    71 CONFLICT
SEQADV 1NCD SER L   77  EMBL Y11589    ASN    77 CONFLICT
SEQADV 1NCD ALA L   80  EMBL Y11589    SER    80 CONFLICT
SEQADV 1NCD LEU L   85  EMBL Y11589    GLU    85 CONFLICT
SEQADV 1NCD TYR L   87  EMBL Y11589    PHE    87 CONFLICT
SEQADV 1NCD HIS L   91  EMBL Y11589    TYR    91 CONFLICT
SEQADV 1NCD TYR L   92  EMBL Y11589    ASN    92 CONFLICT
SEQADV 1NCD SER L   93  EMBL Y11589    ARG    93 CONFLICT
SEQADV 1NCD PRO L   94  EMBL Y11589    TYR    94 CONFLICT
SEQRES   1 N  389  ILE ARG GLU PHE ASN ASN LEU THR LYS GLY LEU CYS THR
SEQRES   2 N  389  ILE ASN SER TRP HIS ILE TYR GLY LYS ASP ASN ALA VAL
SEQRES   3 N  389  ARG ILE GLY GLU ASP SER ASP VAL LEU VAL THR ARG GLU
SEQRES   4 N  389  PRO TYR VAL SER CYS ASP PRO ASP GLU CYS ARG PHE TYR
SEQRES   5 N  389  ALA LEU SER GLN GLY THR THR ILE ARG GLY LYS HIS SER
SEQRES   6 N  389  ASN GLY THR ILE HIS ASP ARG SER GLN TYR ARG ASP LEU
SEQRES   7 N  389  ILE SER TRP PRO LEU SER SER PRO PRO THR VAL TYR ASN
SEQRES   8 N  389  SER ARG VAL GLU CYS ILE GLY TRP SER SER THR SER CYS
SEQRES   9 N  389  HIS ASP GLY ARG ALA ARG MET SER ILE CYS ILE SER GLY
SEQRES  10 N  389  PRO ASN ASN ASN ALA SER ALA VAL ILE TRP TYR ASN ARG
SEQRES  11 N  389  ARG PRO VAL THR GLU ILE ASN THR TRP ALA ARG ASN ILE
SEQRES  12 N  389  LEU ARG THR GLN GLU SER GLU CYS VAL CYS GLN ASN GLY
SEQRES  13 N  389  VAL CYS PRO VAL VAL PHE THR ASP GLY SER ALA THR GLY
SEQRES  14 N  389  PRO ALA GLU THR ARG ILE TYR TYR PHE LYS GLU GLY LYS
SEQRES  15 N  389  ILE LEU LYS TRP GLU PRO LEU THR GLY THR ALA LYS HIS
SEQRES  16 N  389  ILE GLU GLU CYS SER CYS TYR GLY GLU GLN ALA GLY VAL
SEQRES  17 N  389  THR CYS THR CYS ARG ASP ASN TRP GLN GLY SER ASN ARG
SEQRES  18 N  389  PRO VAL ILE GLN ILE ASP PRO VAL ALA MET THR HIS THR
SEQRES  19 N  389  SER GLN TYR ILE CYS SER PRO VAL LEU THR ASP ASN PRO
SEQRES  20 N  389  ARG PRO ASN ASP PRO THR VAL GLY LYS CYS ASN ASP PRO
SEQRES  21 N  389  TYR PRO GLY ASN ASN ASN ASN GLY VAL LYS GLY PHE SER
SEQRES  22 N  389  TYR LEU ASP GLY GLY ASN THR TRP LEU GLY ARG THR ILE
SEQRES  23 N  389  SER ILE ALA SER ARG SER GLY TYR GLU MET LEU LYS VAL
SEQRES  24 N  389  PRO ASN ALA LEU THR ASP ASP ARG SER LYS PRO THR GLN
SEQRES  25 N  389  GLY GLN THR ILE VAL LEU ASN THR ASP TRP SER GLY TYR
SEQRES  26 N  389  SER GLY SER PHE MET ASP TYR TRP ALA GLU GLY GLU CYS
SEQRES  27 N  389  TYR ARG ALA CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG
SEQRES  28 N  389  PRO LYS GLU ASP LYS VAL TRP TRP THR SER ASN SER ILE
SEQRES  29 N  389  VAL SER MET CYS SER SER THR GLU PHE LEU GLY GLN TRP
SEQRES  30 N  389  ASN TRP PRO ASP GLY ALA LYS ILE GLU TYR PHE LEU
SEQRES   1 L  214  ASP ILE VAL MET THR GLN SER PRO LYS PHE MET SER THR
SEQRES   2 L  214  SER VAL GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER
SEQRES   3 L  214  GLN ASP VAL SER THR ALA VAL VAL TRP TYR GLN GLN LYS
SEQRES   4 L  214  PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER
SEQRES   5 L  214  THR ARG HIS ILE GLY VAL PRO ASP ARG PHE ALA GLY SER
SEQRES   6 L  214  GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER VAL
SEQRES   7 L  214  GLN ALA GLU ASP LEU ALA LEU TYR TYR CYS GLN GLN HIS
SEQRES   8 L  214  TYR SER PRO PRO TRP THR PHE GLY GLY GLY THR LYS LEU
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS
SEQRES   1 H  221  GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS LYS
SEQRES   2 H  221  PRO GLY GLU THR VAL LYS ILE SER CYS LYS ALA SER GLY
SEQRES   3 H  221  TYR THR PHE THR ASN TYR GLY MET ASN TRP VAL LYS GLN
SEQRES   4 H  221  ALA PRO GLY LYS GLY LEU GLU TRP MET GLY TRP ILE ASN
SEQRES   5 H  221  THR ASN THR GLY GLU PRO THR TYR GLY GLU GLU PHE LYS
SEQRES   6 H  221  GLY ARG PHE ALA PHE SER LEU GLU THR SER ALA SER THR
SEQRES   7 H  221  ALA ASN LEU GLN ILE ASN ASN LEU LYS ASN GLU ASP LYS
SEQRES   8 H  221  ALA THR PHE PHE CYS ALA ARG GLY GLU ASP ASN PHE GLY
SEQRES   9 H  221  SER LEU SER ASP TYR TRP GLY GLN GLY THR THR LEU THR
SEQRES  10 H  221  VAL SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO
SEQRES  11 H  221  LEU ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL
SEQRES  12 H  221  THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO
SEQRES  13 H  221  VAL THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY
SEQRES  14 H  221  VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR
SEQRES  15 H  221  THR LEU SER SER SER VAL THR VAL THR SER SER THR TRP
SEQRES  16 H  221  PRO SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA
SEQRES  17 H  221  SER SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY
MODRES 1NCD ASN N   86  ASN  GLYCOSYLATION SITE
MODRES 1NCD ASN N  146  ASN  GLYCOSYLATION SITE
MODRES 1NCD ASN N  200  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    NAG  N 475A     14
HET    NAG  N 476A     14
HET    NAG  N 477B     14
HET     CA  N   0       1
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM      CA CALCIUM ION
FORMUL   4  NAG    5(C8 H15 N O6)
FORMUL   4  BMA    C6 H12 O6
FORMUL   4  MAN    3(C6 H12 O6)
FORMUL   7   CA    CA 2+
FORMUL   8  HOH   *69(H2 O)
HELIX    1  H1 ASN N  104  ASP N  111  1                                   8
HELIX    2  H2 GLY N  142  ASN N  146  1                                   5
HELIX    3  H3 ASN N  381  ASP N  385  1                                   5
HELIX    4  H4 LYS N  463  LEU N  468  1                                   6
SHEET    1   A 4 SER N  96  LYS N 102  0
SHEET    2   A 4 THR N 439  SER N 449 -1  O  SER N 445   N  TYR N 100
SHEET    3   A 4 CYS N 421  GLY N 429 -1  N  PHE N 422   O  MET N 446
SHEET    4   A 4 SER N 407  PHE N 410 -1  O  GLY N 408   N  TYR N 423
SHEET    1   B 4 LEU N 115  ASP N 125  0
SHEET    2   B 4 GLU N 128  THR N 139 -1  O  GLU N 128   N  ASP N 125
SHEET    3   B 4 ASP N 157  PRO N 162 -1  O  ASP N 157   N  SER N 135
SHEET    4   B 4 ARG N 172  ILE N 176 -1  N  ARG N 172   O  SER N 160
SHEET    1   C 4 SER N 179  HIS N 184  0
SHEET    2   C 4 ARG N 189  SER N 195 -1  N  MET N 190   O  CYS N 183
SHEET    3   C 4 SER N 202  TYR N 207 -1  N  SER N 202   O  SER N 195
SHEET    4   C 4 PRO N 211  ASN N 216 -1  N  VAL N 212   O  ILE N 205
SHEET    1   D 4 ARG N 224  THR N 225  0
SHEET    2   D 4 VAL N 236  GLY N 244 -1  N  THR N 242   O  ARG N 224
SHEET    3   D 4 ALA N 250  LYS N 258 -1  N  GLU N 251   O  ASP N 243
SHEET    4   D 4 LYS N 261  PRO N 267 -1  O  LYS N 261   N  LYS N 258
SHEET    1   E 4 GLU N 276  GLU N 283  0
SHEET    2   E 4 GLY N 286  ARG N 292 -1  O  GLY N 286   N  GLU N 283
SHEET    3   E 4 PRO N 301  ASP N 306 -1  O  PRO N 301   N  CYS N 291
SHEET    4   E 4 THR N 311  TYR N 316 -1  O  THR N 311   N  ASP N 306
SHEET    1   F 4 SER N 353  TYR N 354  0
SHEET    2   F 4 TRP N 361  ARG N 364 -1  O  TRP N 361   N  TYR N 354
SHEET    3   F 4 SER N 372  LYS N 378 -1  N  GLU N 375   O  ARG N 364
SHEET    4   F 4 GLN N 392  TRP N 403 -1  O  GLN N 392   N  LYS N 378
SHEET    1   G 4 MET L   4  GLN L   6  0
SHEET    2   G 4 VAL L  19  ALA L  25 -1  O  LYS L  24   N  THR L   5
SHEET    3   G 4 ASP L  70  ILE L  75 -1  N  TYR L  71   O  CYS L  23
SHEET    4   G 4 PHE L  62  SER L  67 -1  O  ALA L  63   N  THR L  74
SHEET    1   H 6 PHE L  10  SER L  14  0
SHEET    2   H 6 THR L 102  LYS L 107  1  O  LYS L 103   N  MET L  11
SHEET    3   H 6 ALA L  84  GLN L  90 -1  O  ALA L  84   N  LEU L 104
SHEET    4   H 6 VAL L  33  GLN L  38 -1  N  VAL L  34   O  GLN L  89
SHEET    5   H 6 PRO L  44  TYR L  49 -1  O  LYS L  45   N  GLN L  37
SHEET    6   H 6 THR L  53  ARG L  54 -1  N  THR L  53   O  TYR L  49
SHEET    1   I 4 THR L 114  PHE L 118  0
SHEET    2   I 4 GLY L 129  PHE L 139 -1  N  VAL L 133   O  PHE L 118
SHEET    3   I 4 TYR L 173  THR L 182 -1  N  TYR L 173   O  PHE L 139
SHEET    4   I 4 VAL L 159  TRP L 163 -1  O  LEU L 160   N  THR L 178
SHEET    1   J 4 SER L 153  ARG L 155  0
SHEET    2   J 4 ILE L 144  ILE L 150 -1  O  TRP L 148   N  ARG L 155
SHEET    3   J 4 TYR L 192  HIS L 198 -1  O  THR L 193   N  LYS L 149
SHEET    4   J 4 ILE L 205  PHE L 209 -1  O  ILE L 205   N  ALA L 196
SHEET    1   K 4 GLN H   3  GLN H   6  0
SHEET    2   K 4 VAL H  18  SER H  25 -1  N  LYS H  23   O  VAL H   5
SHEET    3   K 4 THR H  77  ILE H  82 -1  O  ALA H  78   N  CYS H  22
SHEET    4   K 4 PHE H  67  GLU H  72 -1  O  ALA H  68   N  GLN H  81
SHEET    1   L 5 PRO H  57  TYR H  59  0
SHEET    2   L 5 GLY H  44  ILE H  51 -1  O  TRP H  50   N  THR H  58
SHEET    3   L 5 MET H  34  ALA H  40 -1  O  MET H  34   N  ILE H  51
SHEET    4   L 5 ALA H  88  GLY H  95 -1  N  THR H  89   O  GLN H  39
SHEET    1   M 6 PRO H  57  TYR H  59  0
SHEET    2   M 6 GLY H  44  ILE H  51 -1  O  TRP H  50   N  THR H  58
SHEET    3   M 6 MET H  34  ALA H  40 -1  O  MET H  34   N  ILE H  51
SHEET    4   M 6 ALA H  88  GLY H  95 -1  N  THR H  89   O  GLN H  39
SHEET    5   M 6 THR H 107  VAL H 111 -1  O  THR H 107   N  PHE H  90
SHEET    6   M 6 GLU H  10  LYS H  12  1  N  GLU H  10   O  THR H 108
SHEET    1   N 4 SER H 120  LEU H 124  0
SHEET    2   N 4 SER H 137  TYR H 147 -1  N  GLY H 141   O  LEU H 124
SHEET    3   N 4 LEU H 184  THR H 194 -1  N  TYR H 185   O  TYR H 147
SHEET    4   N 4 HIS H 172  GLN H 179 -1  O  HIS H 172   N  SER H 190
SHEET    1   O 3 THR H 153  TRP H 157  0
SHEET    2   O 3 THR H 206  HIS H 212 -1  N  ASN H 209   O  THR H 156
SHEET    3   O 3 THR H 217  LYS H 222 -1  N  THR H 217   O  HIS H 212
SSBOND   1 CYS N   92    CYS N  417                          1555   1555  2.00
SSBOND   2 CYS N  124    CYS N  129                          1555   1555  2.01
SSBOND   3 CYS N  175    CYS N  193                          1555   1555  1.99
SSBOND   4 CYS N  183    CYS N  230                          1555   1555  2.00
SSBOND   5 CYS N  232    CYS N  237                          1555   1555  1.97
SSBOND   6 CYS N  278    CYS N  291                          1555   1555  2.03
SSBOND   7 CYS N  280    CYS N  289                          1555   1555  1.99
SSBOND   8 CYS N  318    CYS N  337                          1555   1555  1.97
SSBOND   9 CYS N  421    CYS N  447                          1555   1555  2.03
SSBOND  10 CYS L   23    CYS L   88                          1555   1555  2.01
SSBOND  11 CYS L  134    CYS L  194                          1555   1555  2.02
SSBOND  12 CYS L  214    CYS H  128                          1555   1555  2.02
SSBOND  13 CYS H   22    CYS H   92                          1555   1555  2.01
SSBOND  14 CYS H  142    CYS H  208                          1555   1555  2.01
LINK         ND2 ASN N  86                 C1  NAG N 475A    1555   1555  1.46
LINK         ND2 ASN N 146                 C1  NAG N 476A    1555   1555  1.45
LINK         ND2 ASN N 200                 C1  NAG N 469A    1555   1555  1.47
LINK         O4  NAG N 469A                C1  NAG N 470B    1555   1555  1.44
LINK         O4  NAG N 470B                C1  BMA N 471C    1555   1555  1.43
LINK         O3  BMA N 471C                C1  MAN N 472D    1555   1555  1.44
LINK         O2  MAN N 472D                C1  MAN N 473E    1555   1555  1.45
LINK         O2  MAN N 473E                C1  MAN N 474F    1555   1555  1.41
LINK         O4  NAG N 476A                C1  NAG N 477B    1555   1555  1.44
LINK        CA    CA N   0                 O   ASN N 294     1555   1555  3.21
LINK        CA    CA N   0                 OD2 ASP N 324     1555   1555  3.00
LINK        CA    CA N   0                 O   GLY N 297     1555   1555  1.63
LINK        CA    CA N   0                 O   ASP N 293     1555   1555  3.00
LINK        CA    CA N   0                 O   ASN N 347     1555   1555  2.10
LINK        CA    CA N   0                 O   ASN N 344     1555   1555  2.87
CISPEP   1 ASN N  325    PRO N  326          0         4.73
CISPEP   2 ARG N  430    PRO N  431          0        11.20
CISPEP   3 SER L    7    PRO L    8          0        -1.99
CISPEP   4 PRO L   94    PRO L   95          0       -13.79
CISPEP   5 TYR L  140    PRO L  141          0        -1.23
CISPEP   6 PHE H  148    PRO H  149          0         0.01
CISPEP   7 GLU H  150    PRO H  151          0         4.77
CISPEP   8 TRP H  199    PRO H  200          0         5.77
SITE     1 AC1  8 ASN N 199  ASN N 200  LEU N 453  GLY N 454
SITE     2 AC1  8 GLN N 455  NAG N 470B HOH N 502  HOH N 539
SITE     1 AC2  6 GLN N 392  GLY N 394  PHE N 452  NAG N 469A
SITE     2 AC2  6 BMA N 471C HOH N 502
SITE     1 AC3  6 LEU N 377  THR N 391  GLY N 394  NAG N 470B
SITE     2 AC3  6 MAN N 472D HOH N 536
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  7 VAL N 321  ASP N 330  ARG N 364  LYS N 389
SITE     2 AC5  7 PRO N 390  MAN N 472D MAN N 474F
SITE     1 AC6  8 ARG N 327  ASN N 329  ASP N 330  ARG N 364
SITE     2 AC6  8 ILE N 366  ILE N 368  MAN N 472D MAN N 473E
SITE     1 AC7  4 GLU N  83  ASN N  86  GLN N 233  ASN N 234
SITE     1 AC8  3 ASN N 146  TRP N 437  NAG N 477B
SITE     1 AC9  2 TRP N 437  NAG N 476A
SITE     1 BC1  6 ASP N 293  ASN N 294  GLY N 297  ASP N 324
SITE     2 BC1  6 ASN N 344  ASN N 347
CRYST1  167.000  167.000  124.000  90.00  90.00  90.00 P 4 21 2      8
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      0.005988  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005988  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008065        0.00000
      
PROCHECK
Go to PROCHECK summary
 References