spacer
spacer

PDBsum entry 1nsc

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase(o-glycosyl) PDB id
1nsc
Jmol
Contents
Protein chains
390 a.a. *
Ligands
NAG ×2
SIA ×2
Metals
_CA ×3
Waters ×1510
* Residue conservation analysis
HEADER    HYDROLASE(O-GLYCOSYL)                   24-MAY-93   1NSC
TITLE     INFLUENZA B VIRUS NEURAMINIDASE CAN SYNTHESIZE ITS OWN INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 3.2.1.18;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA B VIRUS (STRAIN B/BEIJING/1/87);
SOURCE   3 ORGANISM_TAXID: 11525;
SOURCE   4 STRAIN: B/BEIJING/1/87
KEYWDS    HYDROLASE(O-GLYCOSYL)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    W.P.BURMEISTER,R.W.H.RUIGROK,S.CUSACK
REVDAT   5   16-NOV-11 1NSC    1       HETATM
REVDAT   4   13-JUL-11 1NSC    1       VERSN
REVDAT   3   24-FEB-09 1NSC    1       VERSN
REVDAT   2   01-APR-03 1NSC    1       JRNL
REVDAT   1   31-OCT-93 1NSC    0
JRNL        AUTH   W.P.BURMEISTER,B.HENRISSAT,C.BOSSO,S.CUSACK,R.W.RUIGROK
JRNL        TITL   INFLUENZA B VIRUS NEURAMINIDASE CAN SYNTHESIZE ITS OWN
JRNL        TITL 2 INHIBITOR.
JRNL        REF    STRUCTURE                     V.   1    19 1993
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   8069621
JRNL        DOI    10.1016/0969-2126(93)90005-2
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   W.P.BURMEISTER,R.W.H.RUIGROK,S.CUSACK
REMARK   1  TITL   THE 2.2 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF INFLUENZA
REMARK   1  TITL 2 B NEURAMINIDASE AND ITS COMPLEX WITH SIALIC ACID
REMARK   1  REF    EMBO J.                       V.  11    49 1992
REMARK   1  REFN                   ISSN 0261-4189
REMARK   1 REFERENCE 2
REMARK   1  AUTH   W.P.BURMEISTER,R.S.DANIELS,S.DAYAN,J.GAGNON,S.CUSACK,
REMARK   1  AUTH 2 R.W.H.RUIGROK
REMARK   1  TITL   SEQUENCE AND CRYSTALLIZATION OF INFLUENZA VIRUS
REMARK   1  TITL 2 B(SLASH)BEIJING(SLASH)1(SLASH)87 NEURAMINIDASE
REMARK   1  REF    VIROLOGY                      V. 180   266 1991
REMARK   1  REFN                   ISSN 0042-6822
REMARK   2
REMARK   2 RESOLUTION.    1.70 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) : 1.70
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             : NULL
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.180
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            : 6072
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 73
REMARK   3   SOLVENT ATOMS            : 506
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) : 2.89
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1NSC 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   (%): 57.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.26667
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      148.53333
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  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      148.53333
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.26667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 19640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -111.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CA    CA A 470  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 656  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 539  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 612  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 698  LIES ON A SPECIAL POSITION.
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 A  344   CD   NE   CZ   NH1  NH2
REMARK 480     ARG B  344   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   HZ1  LYS B   127     H1   HOH B   505              1.24
REMARK 500   HZ1  LYS A   418     H1   HOH A   528              1.28
REMARK 500  HD21  ASN B   108     H2   HOH A   694              1.39
REMARK 500   HE2  HIS A   154     H    LEU B    96              1.39
REMARK 500   H1   HOH A   610     O    HOH A   612              1.55
REMARK 500   O    HOH B   698     H1   HOH B   699              1.57
REMARK 500   H1   HOH A   603     O    HOH A   612              1.57
REMARK 500   H    ILE B   114     HG   SER B   439              1.58
REMARK 500   H    ILE A   114     HG   SER A   439              1.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    HIS A 133   NE2   HIS A 133   CD2    -0.068
REMARK 500    HIS A 182   NE2   HIS A 182   CD2    -0.069
REMARK 500    HIS A 353   NE2   HIS A 353   CD2    -0.070
REMARK 500    HIS A 395   NE2   HIS A 395   CD2    -0.068
REMARK 500    HIS B 172   NE2   HIS B 172   CD2    -0.069
REMARK 500    HIS B 182   NE2   HIS B 182   CD2    -0.073
REMARK 500    HIS B 214   NE2   HIS B 214   CD2    -0.067
REMARK 500    HIS B 353   NE2   HIS B 353   CD2    -0.070
REMARK 500    HIS B 395   NE2   HIS B 395   CD2    -0.072
REMARK 500    HIS B 438   NE2   HIS B 438   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 A  79   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP A  79   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES
REMARK 500    ARG A  83   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    ARG A 101   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A 149   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 149   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ILE A 163   C   -  N   -  CA  ANGL. DEV. = -19.0 DEGREES
REMARK 500    TRP A 176   CD1 -  CG  -  CD2 ANGL. DEV. =   6.6 DEGREES
REMARK 500    TRP A 176   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES
REMARK 500    ARG A 185   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TRP A 187   CD1 -  CG  -  CD2 ANGL. DEV. =   7.3 DEGREES
REMARK 500    TRP A 187   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES
REMARK 500    LEU A 200   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES
REMARK 500    ARG A 222   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    CYS A 228   CA  -  CB  -  SG  ANGL. DEV. =   6.6 DEGREES
REMARK 500    ARG A 251   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A 251   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    ARG A 256   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A 259   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG A 291   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A 291   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A 314   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A 355   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    MET A 356   CG  -  SD  -  CE  ANGL. DEV. = -10.7 DEGREES
REMARK 500    TRP A 363   CD1 -  CG  -  CD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    TRP A 363   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES
REMARK 500    TRP A 387   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    TRP A 387   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES
REMARK 500    MET A 402   CA  -  CB  -  CG  ANGL. DEV. = -20.8 DEGREES
REMARK 500    TRP A 407   CD1 -  CG  -  CD2 ANGL. DEV. =   5.2 DEGREES
REMARK 500    TRP A 407   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES
REMARK 500    TRP A 437   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TRP A 437   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES
REMARK 500    TRP A 455   CD1 -  CG  -  CD2 ANGL. DEV. =   4.9 DEGREES
REMARK 500    TRP A 455   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES
REMARK 500    TRP B  79   CD1 -  CG  -  CD2 ANGL. DEV. =   7.1 DEGREES
REMARK 500    TRP B  79   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    ARG B 115   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG B 149   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    TRP B 176   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP B 176   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES
REMARK 500    TRP B 187   CD1 -  CG  -  CD2 ANGL. DEV. =   7.0 DEGREES
REMARK 500    TRP B 187   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG B 251   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG B 256   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG B 269   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG B 269   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    VAL B 270   N   -  CA  -  CB  ANGL. DEV. = -16.2 DEGREES
REMARK 500    VAL B 306   CA  -  CB  -  CG2 ANGL. DEV. =  -9.2 DEGREES
REMARK 500    ARG B 314   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      61 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    PRO A 164       81.69    -68.32
REMARK 500    ASN A 198       63.79   -159.06
REMARK 500    ASN A 219       81.41   -154.98
REMARK 500    ILE A 220       72.53     50.13
REMARK 500    THR A 223     -157.10   -139.00
REMARK 500    HIS A 272      112.18   -160.24
REMARK 500    SER A 282     -174.97   -170.73
REMARK 500    ASP A 383     -156.63     51.99
REMARK 500    TRP A 407     -121.79   -109.32
REMARK 500    ASN B 198       55.01   -161.36
REMARK 500    ASN B 219       84.63   -160.56
REMARK 500    ILE B 220       70.25     51.80
REMARK 500    THR B 223     -155.67   -137.18
REMARK 500    ASP B 383     -156.28     57.26
REMARK 500    TRP B 407     -119.32   -106.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 607        DISTANCE =  6.39 ANGSTROMS
REMARK 525    HOH A 620        DISTANCE =  5.78 ANGSTROMS
REMARK 525    HOH A 719        DISTANCE =  5.46 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 468  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 292   O
REMARK 620 2 THR A 296   O    85.5
REMARK 620 3 ASP A 323   OD2  96.7  96.0
REMARK 620 4 GLY A 343   O    99.2  80.0 163.2
REMARK 620 5 GLY A 345   O    89.5 164.0  99.6  85.8
REMARK 620 6 HOH A 647   O   177.4  92.4  85.0  78.9  92.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 470  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 167   OE1
REMARK 620 2 GLU B 167   OE1  90.7
REMARK 620 3 HOH B 539   O    93.7  90.7
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 469  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 323   OD2
REMARK 620 2 ASP B 292   O    92.5
REMARK 620 3 GLY B 343   O   166.7 100.6
REMARK 620 4 GLY B 345   O    98.5  87.8  84.4
REMARK 620 5 HOH B 572   O    89.2 177.4  77.8  90.0
REMARK 620 6 THR B 296   O    93.9  87.4  84.5 166.9  94.5
REMARK 620 N                    1     2     3     4     5
REMARK 700
REMARK 700 SHEET
REMARK 700 STRAND 4 OF SHEET RECORD *3A* AND *3B* IS IRREGULAR.
REMARK 700 STRAND 4 OF SHEET RECORD *5* IS VERY IRREGULAR.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CHA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: HIGH-AFFINITY CALCIUM-BINDING SITES
REMARK 800
REMARK 800 SITE_IDENTIFIER: CLA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: LOW-AFFINITY CALCIUM-BINDING SITES
REMARK 800
REMARK 800 SITE_IDENTIFIER: SIA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CHB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: HIGH-AFFINITY CALCIUM-BINDING SITES
REMARK 800
REMARK 800 SITE_IDENTIFIER: CLB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: LOW-AFFINITY CALCIUM-BINDING SITES
REMARK 800
REMARK 800 SITE_IDENTIFIER: SIB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 466
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 466
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA B 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 468
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 470
DBREF  1NSC A   76   465  UNP    P27907   NRAM_INBBE      76    465
DBREF  1NSC B   76   465  UNP    P27907   NRAM_INBBE      76    465
SEQRES   1 A  390  GLU PRO GLU TRP THR TYR PRO ARG LEU SER CYS GLN GLY
SEQRES   2 A  390  SER THR PHE GLN LYS ALA LEU LEU ILE SER PRO HIS ARG
SEQRES   3 A  390  PHE GLY GLU ALA ARG GLY ASN SER ALA PRO LEU ILE ILE
SEQRES   4 A  390  ARG GLU PRO PHE ILE ALA CYS GLY PRO LYS GLU CYS LYS
SEQRES   5 A  390  HIS PHE ALA LEU THR HIS TYR ALA ALA GLN PRO GLY GLY
SEQRES   6 A  390  TYR TYR ASN GLY THR ARG GLU ASP ARG ASN LYS LEU ARG
SEQRES   7 A  390  HIS LEU ILE SER VAL LYS LEU GLY LYS ILE PRO THR VAL
SEQRES   8 A  390  GLU ASN SER ILE PHE HIS MET ALA ALA TRP SER GLY SER
SEQRES   9 A  390  ALA CYS HIS ASP GLY ARG GLU TRP THR TYR ILE GLY VAL
SEQRES  10 A  390  ASP GLY PRO ASP SER ASN ALA LEU ILE LYS ILE LYS TYR
SEQRES  11 A  390  GLY GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA ASN
SEQRES  12 A  390  ASN ILE LEU ARG THR GLN GLU SER ALA CYS ASN CYS ILE
SEQRES  13 A  390  GLY GLY ASP CYS TYR LEU MET ILE THR ASP GLY SER ALA
SEQRES  14 A  390  SER GLY ILE SER LYS CYS ARG PHE LEU LYS ILE ARG GLU
SEQRES  15 A  390  GLY ARG ILE ILE LYS GLU ILE PHE PRO THR GLY ARG VAL
SEQRES  16 A  390  GLU HIS THR GLU GLU CYS THR CYS GLY PHE ALA SER ASN
SEQRES  17 A  390  LYS THR ILE GLU CYS ALA CYS ARG ASP ASN SER TYR THR
SEQRES  18 A  390  ALA LYS ARG PRO PHE VAL LYS LEU ASN VAL GLU THR ASP
SEQRES  19 A  390  THR ALA GLU ILE ARG LEU MET CYS THR GLU THR TYR LEU
SEQRES  20 A  390  ASP THR PRO ARG PRO ASP ASP GLY SER ILE THR GLY PRO
SEQRES  21 A  390  CYS GLU SER ASN GLY ASP LYS GLY ARG GLY GLY ILE LYS
SEQRES  22 A  390  GLY GLY PHE VAL HIS GLN ARG MET ALA SER LYS ILE GLY
SEQRES  23 A  390  ARG TRP TYR SER ARG THR MET SER LYS THR GLU ARG MET
SEQRES  24 A  390  GLY MET GLU LEU TYR VAL ARG TYR ASP GLY ASP PRO TRP
SEQRES  25 A  390  THR ASP SER ASP ALA LEU ALA HIS SER GLY VAL MET VAL
SEQRES  26 A  390  SER MET LYS GLU PRO GLY TRP TYR SER PHE GLY PHE GLU
SEQRES  27 A  390  ILE LYS ASP LYS LYS CYS ASP VAL PRO CYS ILE GLY ILE
SEQRES  28 A  390  GLU MET VAL HIS ASP GLY GLY LYS LYS THR TRP HIS SER
SEQRES  29 A  390  ALA ALA THR ALA ILE TYR CYS LEU MET GLY SER GLY GLN
SEQRES  30 A  390  LEU LEU TRP ASP THR VAL THR GLY VAL ASP MET ALA LEU
SEQRES   1 B  390  GLU PRO GLU TRP THR TYR PRO ARG LEU SER CYS GLN GLY
SEQRES   2 B  390  SER THR PHE GLN LYS ALA LEU LEU ILE SER PRO HIS ARG
SEQRES   3 B  390  PHE GLY GLU ALA ARG GLY ASN SER ALA PRO LEU ILE ILE
SEQRES   4 B  390  ARG GLU PRO PHE ILE ALA CYS GLY PRO LYS GLU CYS LYS
SEQRES   5 B  390  HIS PHE ALA LEU THR HIS TYR ALA ALA GLN PRO GLY GLY
SEQRES   6 B  390  TYR TYR ASN GLY THR ARG GLU ASP ARG ASN LYS LEU ARG
SEQRES   7 B  390  HIS LEU ILE SER VAL LYS LEU GLY LYS ILE PRO THR VAL
SEQRES   8 B  390  GLU ASN SER ILE PHE HIS MET ALA ALA TRP SER GLY SER
SEQRES   9 B  390  ALA CYS HIS ASP GLY ARG GLU TRP THR TYR ILE GLY VAL
SEQRES  10 B  390  ASP GLY PRO ASP SER ASN ALA LEU ILE LYS ILE LYS TYR
SEQRES  11 B  390  GLY GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA ASN
SEQRES  12 B  390  ASN ILE LEU ARG THR GLN GLU SER ALA CYS ASN CYS ILE
SEQRES  13 B  390  GLY GLY ASP CYS TYR LEU MET ILE THR ASP GLY SER ALA
SEQRES  14 B  390  SER GLY ILE SER LYS CYS ARG PHE LEU LYS ILE ARG GLU
SEQRES  15 B  390  GLY ARG ILE ILE LYS GLU ILE PHE PRO THR GLY ARG VAL
SEQRES  16 B  390  GLU HIS THR GLU GLU CYS THR CYS GLY PHE ALA SER ASN
SEQRES  17 B  390  LYS THR ILE GLU CYS ALA CYS ARG ASP ASN SER TYR THR
SEQRES  18 B  390  ALA LYS ARG PRO PHE VAL LYS LEU ASN VAL GLU THR ASP
SEQRES  19 B  390  THR ALA GLU ILE ARG LEU MET CYS THR GLU THR TYR LEU
SEQRES  20 B  390  ASP THR PRO ARG PRO ASP ASP GLY SER ILE THR GLY PRO
SEQRES  21 B  390  CYS GLU SER ASN GLY ASP LYS GLY ARG GLY GLY ILE LYS
SEQRES  22 B  390  GLY GLY PHE VAL HIS GLN ARG MET ALA SER LYS ILE GLY
SEQRES  23 B  390  ARG TRP TYR SER ARG THR MET SER LYS THR GLU ARG MET
SEQRES  24 B  390  GLY MET GLU LEU TYR VAL ARG TYR ASP GLY ASP PRO TRP
SEQRES  25 B  390  THR ASP SER ASP ALA LEU ALA HIS SER GLY VAL MET VAL
SEQRES  26 B  390  SER MET LYS GLU PRO GLY TRP TYR SER PHE GLY PHE GLU
SEQRES  27 B  390  ILE LYS ASP LYS LYS CYS ASP VAL PRO CYS ILE GLY ILE
SEQRES  28 B  390  GLU MET VAL HIS ASP GLY GLY LYS LYS THR TRP HIS SER
SEQRES  29 B  390  ALA ALA THR ALA ILE TYR CYS LEU MET GLY SER GLY GLN
SEQRES  30 B  390  LEU LEU TRP ASP THR VAL THR GLY VAL ASP MET ALA LEU
MODRES 1NSC ASN A  283  ASN  GLYCOSYLATION SITE
MODRES 1NSC ASN B  283  ASN  GLYCOSYLATION SITE
HET    NAG  A 466      28
HET    SIA  A 467      39
HET    NAG  B 466      28
HET    SIA  B 467      39
HET     CA  A 468       1
HET     CA  B 469       1
HET     CA  A 470       1
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     SIA O-SIALIC ACID
HETNAM      CA CALCIUM ION
FORMUL   3  NAG    2(C8 H15 N O6)
FORMUL   4  SIA    2(C11 H19 N O9)
FORMUL   7   CA    3(CA 2+)
FORMUL  10  HOH   *506(H2 O)
HELIX    1   1 SER A   98  GLY A  103  5                                   6
HELIX    2   2 PRO A  195  ASN A  198  5                                   4
HELIX    3   3 SER B   98  GLY B  103  5                                   6
HELIX    4   4 PRO B  195  ASN B  198  5                                   4
SHEET    1  1A 4 ILE A 113  CYS A 121  0
SHEET    2  1A 4 CYS A 126  THR A 132 -1  N  LEU A 131   O  ARG A 115
SHEET    3  1A 4 HIS A 154  LYS A 159  1  O  VAL A 158   N  HIS A 128
SHEET    4  1A 4 ILE A 170  ALA A 174 -1  O  ILE A 170   N  SER A 157
SHEET    1  2A 4 SER A 177  HIS A 182  0
SHEET    2  2A 4 TRP A 187  ASP A 193 -1  N  VAL A 192   O  SER A 177
SHEET    3  2A 4 LEU A 200  TYR A 205  1  N  LYS A 202   O  GLY A 191
SHEET    4  2A 4 ALA A 208  HIS A 214 -1  N  TYR A 213   O  ILE A 201
SHEET    1 3AA 4 ARG A 222  THR A 223  0
SHEET    2 3AA 4 ASP A 234  GLY A 242 -1  O  THR A 240   N  ARG A 222
SHEET    3 3AA 4 SER A 248  ARG A 256  1  N  LEU A 253   O  LEU A 237
SHEET    4 3AA 4 ARG A 259  ILE A 264 -1  N  ARG A 259   O  ARG A 256
SHEET    1 3BA 4 ASN A 229  ILE A 231  0
SHEET    2 3BA 4 ASP A 234  GLY A 242 -1  O  TYR A 236   N  ASN A 229
SHEET    3 3BA 4 SER A 248  ARG A 256  1  N  LEU A 253   O  LEU A 237
SHEET    4 3BA 4 ARG A 259  ILE A 264 -1  N  ARG A 259   O  ARG A 256
SHEET    1  4A 4 GLU A 274  PHE A 280  0
SHEET    2  4A 4 THR A 285  ARG A 291 -1  O  ARG A 291   N  GLU A 274
SHEET    3  4A 4 PRO A 300  ASN A 305  1  O  PRO A 300   N  CYS A 290
SHEET    4  4A 4 THR A 310  LEU A 315 -1  O  THR A 310   N  ASN A 305
SHEET    1  5A 4 PHE A 351  ARG A 355  0
SHEET    2  5A 4 ILE A 360  ARG A 366 -1  O  TRP A 363   N  VAL A 352
SHEET    3  5A 4 MET A 376  TYR A 382  1  N  GLU A 377   O  ARG A 366
SHEET    4  5A 4 ALA A 394  VAL A 400 -1  N  ALA A 394   O  VAL A 380
SHEET    1  6A 4 SER A 409  LYS A 415  0
SHEET    2  6A 4 ASP A 420  HIS A 430 -1  O  GLY A 425   N  PHE A 410
SHEET    3  6A 4 SER A 439  LEU A 447  1  O  ALA A 443   N  ILE A 426
SHEET    4  6A 4 PHE A  91  ILE A  97 -1  O  ILE A  97   N  THR A 442
SHEET    1  1B 4 ILE B 113  CYS B 121  0
SHEET    2  1B 4 CYS B 126  THR B 132 -1  N  LEU B 131   O  ARG B 115
SHEET    3  1B 4 HIS B 154  LYS B 159  1  O  VAL B 158   N  HIS B 128
SHEET    4  1B 4 ILE B 170  ALA B 174 -1  O  ILE B 170   N  SER B 157
SHEET    1  2B 4 SER B 177  HIS B 182  0
SHEET    2  2B 4 TRP B 187  ASP B 193 -1  N  VAL B 192   O  SER B 177
SHEET    3  2B 4 LEU B 200  TYR B 205  1  N  LYS B 202   O  GLY B 191
SHEET    4  2B 4 ALA B 208  HIS B 214 -1  N  TYR B 213   O  ILE B 201
SHEET    1 3AB 4 ARG B 222  THR B 223  0
SHEET    2 3AB 4 ASP B 234  GLY B 242 -1  O  THR B 240   N  ARG B 222
SHEET    3 3AB 4 SER B 248  ARG B 256  1  N  LEU B 253   O  LEU B 237
SHEET    4 3AB 4 ARG B 259  ILE B 264 -1  N  ARG B 259   O  ARG B 256
SHEET    1 3BB 4 ASN B 229  ILE B 231  0
SHEET    2 3BB 4 ASP B 234  GLY B 242 -1  O  TYR B 236   N  ASN B 229
SHEET    3 3BB 4 SER B 248  ARG B 256  1  N  LEU B 253   O  LEU B 237
SHEET    4 3BB 4 ARG B 259  ILE B 264 -1  N  ARG B 259   O  ARG B 256
SHEET    1  4B 4 GLU B 274  PHE B 280  0
SHEET    2  4B 4 THR B 285  ARG B 291 -1  O  ARG B 291   N  GLU B 274
SHEET    3  4B 4 PRO B 300  ASN B 305  1  O  PRO B 300   N  CYS B 290
SHEET    4  4B 4 THR B 310  LEU B 315 -1  O  THR B 310   N  ASN B 305
SHEET    1  5B 4 PHE B 351  ARG B 355  0
SHEET    2  5B 4 ILE B 360  ARG B 366 -1  O  TRP B 363   N  VAL B 352
SHEET    3  5B 4 MET B 376  TYR B 382  1  N  GLU B 377   O  ARG B 366
SHEET    4  5B 4 ALA B 394  VAL B 400 -1  N  ALA B 394   O  VAL B 380
SHEET    1  6B 4 SER B 409  LYS B 415  0
SHEET    2  6B 4 ASP B 420  HIS B 430 -1  O  GLY B 425   N  PHE B 410
SHEET    3  6B 4 SER B 439  LEU B 447  1  O  ALA B 443   N  ILE B 426
SHEET    4  6B 4 PHE B  91  ILE B  97 -1  O  ILE B  97   N  THR B 442
SSBOND   1 CYS A   86    CYS A  419                          1555   1555  2.01
SSBOND   2 CYS A  121    CYS A  126                          1555   1555  2.01
SSBOND   3 CYS A  181    CYS A  228                          1555   1555  2.02
SSBOND   4 CYS A  230    CYS A  235                          1555   1555  2.03
SSBOND   5 CYS A  276    CYS A  290                          1555   1555  2.04
SSBOND   6 CYS A  278    CYS A  288                          1555   1555  2.02
SSBOND   7 CYS A  317    CYS A  336                          1555   1555  2.02
SSBOND   8 CYS A  423    CYS A  446                          1555   1555  2.03
SSBOND   9 CYS B   86    CYS B  419                          1555   1555  2.01
SSBOND  10 CYS B  121    CYS B  126                          1555   1555  2.03
SSBOND  11 CYS B  181    CYS B  228                          1555   1555  2.04
SSBOND  12 CYS B  230    CYS B  235                          1555   1555  2.04
SSBOND  13 CYS B  276    CYS B  290                          1555   1555  2.02
SSBOND  14 CYS B  278    CYS B  288                          1555   1555  2.03
SSBOND  15 CYS B  317    CYS B  336                          1555   1555  2.02
SSBOND  16 CYS B  423    CYS B  446                          1555   1555  2.03
LINK         ND2 ASN A 283                 C1  NAG A 466     1555   1555  1.47
LINK         ND2 ASN B 283                 C1  NAG B 466     1555   1555  1.46
LINK        CA    CA A 468                 O   ASP A 292     1555   1555  2.28
LINK        CA    CA A 468                 O   THR A 296     1555   1555  2.33
LINK        CA    CA A 468                 OD2 ASP A 323     1555   1555  2.33
LINK        CA    CA A 468                 O   GLY A 343     1555   1555  2.31
LINK        CA    CA A 468                 O   GLY A 345     1555   1555  2.27
LINK        CA    CA A 468                 O   HOH A 647     1555   1555  2.34
LINK        CA    CA A 470                 OE1 GLU A 167     1555   1555  2.38
LINK        CA    CA A 470                 OE1 GLU B 167     1555   1555  2.35
LINK        CA    CA A 470                 O   HOH B 539     1555   1555  2.71
LINK        CA    CA B 469                 OD2 ASP B 323     1555   1555  2.35
LINK        CA    CA B 469                 O   ASP B 292     1555   1555  2.34
LINK        CA    CA B 469                 O   GLY B 343     1555   1555  2.45
LINK        CA    CA B 469                 O   GLY B 345     1555   1555  2.27
LINK        CA    CA B 469                 O   HOH B 572     1555   1555  2.35
LINK        CA    CA B 469                 O   THR B 296     1555   1555  2.36
LINK        CA    CA A 470                 O   HOH B 539     1555   4555  2.71
LINK        CA    CA A 470                 OE1 GLU A 167     1555   4555  2.38
LINK        CA    CA A 470                 OE1 GLU B 167     1555   4555  2.35
CISPEP   1 GLN A  137    PRO A  138          0        -6.40
CISPEP   2 THR A  324    PRO A  325          0         2.70
CISPEP   3 GLN B  137    PRO B  138          0        -3.11
CISPEP   4 THR B  324    PRO B  325          0         5.64
SITE     1 CHA  5 ASP A 323  GLY A 343  GLY A 345  THR A 296
SITE     2 CHA  5 ASP A 292
SITE     1 CLA  1 GLU A 167
SITE     1 SIA 10 ASP A 323  ARG A 115  ARG A 291  ARG A 149
SITE     2 SIA 10 ILE A 220  ARG A 222  TRP A 176  GLU A 274
SITE     3 SIA 10 ASP A 148  TYR A 408
SITE     1 CHB  5 ASP B 323  GLY B 343  GLY B 345  THR B 296
SITE     2 CHB  5 ASP B 292
SITE     1 CLB  1 GLU B 167
SITE     1 SIB 10 ASP B 323  ARG B 115  ARG B 291  ARG B 149
SITE     2 SIB 10 ILE B 220  ARG B 222  TRP B 176  GLU B 274
SITE     3 SIB 10 ASP B 148  TYR B 408
SITE     1 AC1  2 PRO A  82  ASN A 283
SITE     1 AC2 16 ARG A 115  GLU A 116  ASP A 148  ARG A 149
SITE     2 AC2 16 ARG A 222  ALA A 244  GLU A 274  GLU A 275
SITE     3 AC2 16 ARG A 291  ARG A 373  TYR A 408  HOH A 680
SITE     4 AC2 16 HOH A 681  HOH A 683  HOH A 686  HOH A 687
SITE     1 AC3  3 PRO B  82  ASN B 283  HOH B 512
SITE     1 AC4 16 ARG B 115  GLU B 116  ASP B 148  ARG B 149
SITE     2 AC4 16 ARG B 222  ALA B 244  GLU B 274  GLU B 275
SITE     3 AC4 16 ARG B 291  ARG B 373  TYR B 408  HOH B 682
SITE     4 AC4 16 HOH B 686  HOH B 687  HOH B 688  HOH B 690
SITE     1 AC5  6 ASP A 292  THR A 296  ASP A 323  GLY A 343
SITE     2 AC5  6 GLY A 345  HOH A 647
SITE     1 AC6  6 ASP B 292  THR B 296  ASP B 323  GLY B 343
SITE     2 AC6  6 GLY B 345  HOH B 572
SITE     1 AC7  3 GLU A 167  GLU B 167  HOH B 539
CRYST1   88.900   88.900  222.800  90.00  90.00 120.00 P 31 2 1     12
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      0.011249  0.006494  0.000000        0.00000
SCALE2      0.000000  0.012989  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004488        0.00000
MTRIX1   1  0.250000  0.433000 -0.866000        0.00000    1
MTRIX2   1  0.433000  0.750000  0.500000        0.00000    1
MTRIX3   1  0.866000 -0.500000  0.000000        0.00000    1
      
PROCHECK
Go to PROCHECK summary
 References