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PDBsum entry 1w1x

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Hydrolase PDB id
1w1x
Jmol
Contents
Protein chains
389 a.a.
Ligands
SIA ×8
BMA-MAN-MAN
MAN ×6
NAG ×12
GOL ×4
BMA ×3
MAN-MAN
PEG
Metals
_CA ×4
Waters ×1565
HEADER    HYDROLASE                               24-JUN-04   1W1X
TITLE     STRUCTURE OF NEURAMINIDASE FROM ENGLISH DUCK SUBTYPE N6
TITLE    2 COMPLEXED WITH 30 MM SIALIC ACID (NANA, NEU5AC), CRYSTAL
TITLE    3 SOAKED FOR 3 HOURS AT 277 K.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 EC: 3.2.1.18;
COMPND   5 ENGINEERED: YES;
COMPND   6 OTHER_DETAILS: COMPLEXED WITH SIALIC ACID
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_TAXID: 11320;
SOURCE   4 EXPRESSION_SYSTEM: GALLUS GALLUS;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 9031;
SOURCE   6 OTHER_DETAILS: INFLUENZA VIRUS GROWN IN EMBRIONATED
SOURCE   7  CHICKEN EGGS
KEYWDS    HYDROLASE, INFLUENZA TYPE A, NEURAMINIDASE, HB SITE, SIALIC
KEYWDS   2 ACID, SUBTYPE N6
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.RUDINO-PINERA,P.TUNNAH,S.J.CRENNELL,R.G.WEBSTER,W.G.LAVER,
AUTHOR   2 E.F.GARMAN
REVDAT   4   24-FEB-09 1W1X    1       VERSN
REVDAT   3   02-MAR-06 1W1X    1       REMARK
REVDAT   2   22-FEB-06 1W1X    1       TITLE  JRNL   REMARK
REVDAT   1   25-JAN-06 1W1X    0
JRNL        AUTH   E.RUDINO-PINERA,P.TUNNAH,S.J.CRENNELL,R.G.WEBSTER,
JRNL        AUTH 2 W.G.LAVER,E.F.GARMAN
JRNL        TITL   THE CRYSTAL STRUCTURE OF TYPE A INFLUENZA VIRUS
JRNL        TITL 2 NEURAMINIDASE OF THE N6 SUBTYPE REVEALS THE
JRNL        TITL 3 EXISTENCE OF TWO SEPARATE NEU5AC BINDING SITES
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.0  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.71
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 106203
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.167
REMARK   3   R VALUE            (WORKING SET) : 0.164
REMARK   3   FREE R VALUE                     : 0.207
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 5634
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7735
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830
REMARK   3   BIN FREE R VALUE SET COUNT          : 389
REMARK   3   BIN FREE R VALUE                    : 0.2950
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 12033
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 525
REMARK   3   SOLVENT ATOMS            : 1565
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 16.63
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.28
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.48000
REMARK   3    B22 (A**2) : 5.38000
REMARK   3    B33 (A**2) : -2.91000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.54000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.178
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.120
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.684
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12881 ; 0.028 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17524 ; 2.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1552 ; 6.435 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1932 ; 0.176 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9672 ; 0.012 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5911 ; 0.249 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1254 ; 0.161 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    36 ; 0.249 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.174 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7725 ; 1.228 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12473 ; 1.903 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5156 ; 3.244 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5051 ; 4.497 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: UNLIKE OTHER VIRAL NEURAMINIDASES
REMARK   3  SOLVED TO DATE, N6 HAS A FULL TETRAMER IN THE ASYMMETRIC UNIT
REMARK   4
REMARK   4 1W1X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  08-JUL-05.
REMARK 100 THE PDBE ID CODE IS EBI-20228.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-04
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SRS
REMARK 200  BEAMLINE                       : PX14.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9853
REMARK 200  MONOCHROMATOR                  : SILICON 11
REMARK 200  OPTICS                         : 1.2 METRE LONG SILICON
REMARK 200                                   SUBSTRATE, RHODIUM COATED
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 112032
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.780
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : 0.12000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1V0Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M NACL, 20% PEG 3350 AT
REMARK 280  293 K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-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       36.73200
REMARK 290   SMTRY3   2  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 350
REMARK 350 GENERATING THE BIOMOLECULE
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 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   CD   LYS A   295  -  O    HOH A  2206              2.13
REMARK 500   CE   LYS A   295  -  O    HOH A  2206              1.03
REMARK 500   NZ   LYS A   295  -  O    HOH A  2206              0.54
REMARK 500   ND2  ASN B  1207  -  C2   NAG A  1488              2.17
REMARK 500   ND2  ASN C  2152  -  C1   NAG C  3486              2.08
REMARK 500   N    ARG D  3088  -  O    HOH D  2033              2.14
REMARK 500   OE1  GLU D  3168  -  O    HOH D  2118              2.19
REMARK 500   OE1  GLU D  3283  -  O    HOH D  2216              2.13
REMARK 500   C1   BMA A  1480  -  O4   NAG A  1486              2.14
REMARK 500   O3   MAN A  1481  -  C1   MAN A  1483              2.18
REMARK 500   O5   BMA B  2480  -  O4   NAG B  2485              2.11
REMARK 500   O4   NAG C  4481  -  C1   BMA D  4480              2.18
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    TRP A 464   CE3   TRP A 464   CZ3     0.106
REMARK 500    SER B1286   CB    SER B1286   OG      0.081
REMARK 500    VAL B1452   CB    VAL B1452   CG1     0.127
REMARK 500    PHE B1475   CD2   PHE B1475   CE2     0.126
REMARK 500    VAL C2238   CB    VAL C2238   CG2     0.127
REMARK 500    TYR C2474   CE1   TYR C2474   CZ      0.084
REMARK 500    TYR D3176   CD2   TYR D3176   CE2     0.097
REMARK 500    LYS D3268   CE    LYS D3268   NZ      0.162
REMARK 500    TYR D3419   CE1   TYR D3419   CZ      0.080
REMARK 500    PHE D3475   CD1   PHE D3475   CE1     0.146
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    LEU A 128   CA  -  CB  -  CG  ANGL. DEV. =  16.3 DEGREES
REMARK 500    ASP A 131   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ARG A 231   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500    ARG A 231   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ASP A 300   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ASP A 392   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ASP B1117   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES
REMARK 500    LEU B1128   CA  -  CB  -  CG  ANGL. DEV. =  16.2 DEGREES
REMARK 500    ASP B1250   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    SER B1333   CB  -  CA  -  C   ANGL. DEV. =  12.4 DEGREES
REMARK 500    SER B1333   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES
REMARK 500    ASP B1337   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES
REMARK 500    ASP B1468   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    LEU C2128   CA  -  CB  -  CG  ANGL. DEV. =  16.0 DEGREES
REMARK 500    ASP C2131   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    CYS C2182   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES
REMARK 500    ASP C2313   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES
REMARK 500    ASP C2337   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    LEU D3128   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES
REMARK 500    ASP D3131   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP D3250   CB  -  CG  -  OD2 ANGL. DEV. =   7.9 DEGREES
REMARK 500    ARG D3307   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    SER D3333   N   -  CA  -  C   ANGL. DEV. = -19.2 DEGREES
REMARK 500    ASP D3376   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 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 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    ASP A 117      -45.74   -130.40
REMARK 500    ASN A 207       46.76   -156.76
REMARK 500    THR A 232     -157.53   -144.63
REMARK 500    LYS A 322     -157.61   -162.14
REMARK 500    SER A 333       98.26     86.49
REMARK 500    LEU B1093       48.16    -89.57
REMARK 500    ASP B1117      -44.77   -131.51
REMARK 500    ALA B1139      168.12    178.06
REMARK 500    CYS B1182      169.00    178.15
REMARK 500    ASN B1207       36.06   -157.37
REMARK 500    THR B1232     -154.61   -143.62
REMARK 500    CYS B1298     -169.42   -122.61
REMARK 500    LYS B1322     -158.34   -168.91
REMARK 500    SER B1333       93.82     85.63
REMARK 500    TRP B1466       53.52   -113.72
REMARK 500    TYR C2127     -179.16   -171.69
REMARK 500    ASN C2207       37.09   -155.57
REMARK 500    THR C2232     -155.66   -142.25
REMARK 500    CYS C2298     -164.09   -127.42
REMARK 500    LYS C2322     -161.59   -172.72
REMARK 500    SER C2333       93.97     92.87
REMARK 500    ASN C2366       59.75    -91.25
REMARK 500    TRP C2466       56.71   -103.78
REMARK 500    ASP D3117      -52.32   -126.75
REMARK 500    TYR D3127     -179.89   -178.85
REMARK 500    ASN D3207       42.78   -163.65
REMARK 500    THR D3232     -154.17   -143.79
REMARK 500    CYS D3298     -164.08   -121.65
REMARK 500    MET D3317       42.32     71.53
REMARK 500    LYS D3322     -151.22   -166.54
REMARK 500    SER D3333       94.39     86.70
REMARK 500    ASN D3366       52.21    -91.46
REMARK 500    TRP D3466       50.16   -104.81
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 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    THR A 332        24.8      L          L   OUTSIDE RANGE
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 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     BMA A 1480
REMARK 610     BMA D 4480
REMARK 610     MAN A 1483
REMARK 610     MAN B 2481
REMARK 610     MAN B 2483
REMARK 610     MAN C 3481
REMARK 610     MAN C 3483
REMARK 610     MAN C 3484
REMARK 610     NAG A 1488
REMARK 610     NAG C 3485
REMARK 610     NAG C 3486
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 A1479  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 300   O
REMARK 620 2 GLY A 304   O    86.8
REMARK 620 3 ASP A 331   OD2  94.4  96.1
REMARK 620 4 HOH A2259   O    87.6 100.2 163.6
REMARK 620 5 PRO A 354   O    99.5 155.3 107.1  56.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B2479  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B1300   O
REMARK 620 2 HOH B2261   O    87.6
REMARK 620 3 GLY B1304   O    87.8 104.1
REMARK 620 4 ASP B1331   OD2  93.7 161.4  94.5
REMARK 620 5 PRO B1354   O    92.2  59.1 163.2 102.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA C3479  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C2331   OD2
REMARK 620 2 ASP C2300   O    87.5
REMARK 620 3 GLY C2304   O    87.2  80.7
REMARK 620 4 PRO C2354   O   103.0  99.2 169.9
REMARK 620 5 HOH C3255   O   162.8  92.1 109.7  60.1
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA D4479  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D2288   O
REMARK 620 2 ASP D3300   O    83.0
REMARK 620 3 GLY D3304   O    96.9  82.7
REMARK 620 4 ASP D3331   OD2 167.2  91.0  93.5
REMARK 620 5 PRO D3354   O    61.4  94.7 158.3 108.1
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 SIA A1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1485
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1486
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1488
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA B2477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA B2478
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B2480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B2481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B2482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B2483
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B2484
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B2485
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B2487
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA C3477
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA C3478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C3480
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C3481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C3482
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C3483
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C3484
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3485
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3486
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3487
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C4481
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA D4477
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA D4478
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D4480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D4482
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C3479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA D4479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1487
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B2486
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C3476
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C3488
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D4483
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V0Z   RELATED DB: PDB
REMARK 900  STRUCTURE OF NEURAMINIDASE FROM ENGLISH DUCK
REMARK 900  SUBTYPE N6
REMARK 900 RELATED ID: 1W20   RELATED DB: PDB
REMARK 900  STRUCTURE OF NEURAMINIDASE FROM ENGLISH DUCK
REMARK 900  SUBTYPE N6 COMPLEXED WITH 30 MM SIALIC
REMARK 900  ACID (NANA, NEU5AC), CRYSTAL SOAKED FOR 3
REMARK 900  HOURS AT 291 K
REMARK 900 RELATED ID: 1W21   RELATED DB: PDB
REMARK 900  STRUCTURE OF NEURAMINIDASE FROM ENGLISH DUCK
REMARK 900  SUBTYPE N6 COMPLEXED WITH 30 MM SIALIC
REMARK 900  ACID (NANA, NEU5AC), CRYSTAL SOAKED FOR 43
REMARK 900  HOURS AT 291 K.
DBREF  1W1X A   88   476  UNP    Q6XV27   Q6XV27_9INFA    82    470
DBREF  1W1X B 1088  1476  UNP    Q6XV27   Q6XV27_9INFA    82    470
DBREF  1W1X C 2088  2476  UNP    Q6XV27   Q6XV27_9INFA    82    470
DBREF  1W1X D 3088  3476  UNP    Q6XV27   Q6XV27_9INFA    82    470
SEQRES   1 A  389  ARG THR PHE LEU ASN LEU THR LYS PRO LEU CYS GLU VAL
SEQRES   2 A  389  ASN SER TRP HIS ILE LEU SER LYS ASP ASN ALA ILE ARG
SEQRES   3 A  389  ILE GLY GLU ASP ALA HIS ILE LEU VAL THR ARG GLU PRO
SEQRES   4 A  389  TYR LEU SER CYS ASP PRO GLN GLY CYS ARG MET PHE ALA
SEQRES   5 A  389  LEU SER GLN GLY THR THR LEU ARG GLY ARG HIS ALA ASN
SEQRES   6 A  389  GLY THR ILE HIS ASP ARG SER PRO PHE ARG ALA LEU ILE
SEQRES   7 A  389  SER TRP GLU MET GLY GLN ALA PRO SER PRO TYR ASN THR
SEQRES   8 A  389  ARG VAL GLU CYS ILE GLY TRP SER SER THR SER CYS HIS
SEQRES   9 A  389  ASP GLY MET SER ARG MET SER ILE CYS MET SER GLY PRO
SEQRES  10 A  389  ASN ASN ASN ALA SER ALA VAL VAL TRP TYR GLY GLY ARG
SEQRES  11 A  389  PRO ILE THR GLU ILE PRO SER TRP ALA GLY ASN ILE LEU
SEQRES  12 A  389  ARG THR GLN GLU SER GLU CYS VAL CYS HIS LYS GLY VAL
SEQRES  13 A  389  CYS PRO VAL VAL MET THR ASP GLY PRO ALA ASN ASN ARG
SEQRES  14 A  389  ALA ALA THR LYS ILE ILE TYR PHE LYS GLU GLY LYS ILE
SEQRES  15 A  389  GLN LYS ILE GLU GLU LEU ALA GLY ASN ALA GLN HIS ILE
SEQRES  16 A  389  GLU GLU CYS SER CYS TYR GLY ALA GLY GLY VAL ILE LYS
SEQRES  17 A  389  CYS ILE CYS ARG ASP ASN TRP LYS GLY ALA ASN ARG PRO
SEQRES  18 A  389  VAL ILE THR ILE ASP PRO GLU MET MET THR HIS THR SER
SEQRES  19 A  389  LYS TYR LEU CYS SER LYS VAL LEU THR ASP THR SER ARG
SEQRES  20 A  389  PRO ASN ASP PRO THR ASN GLY ASN CYS ASP ALA PRO ILE
SEQRES  21 A  389  THR GLY GLY SER PRO ASP PRO GLY VAL LYS GLY PHE ALA
SEQRES  22 A  389  PHE LEU ASP GLY GLU ASN SER TRP LEU GLY ARG THR ILE
SEQRES  23 A  389  SER LYS ASP SER ARG SER GLY TYR GLU MET LEU LYS VAL
SEQRES  24 A  389  PRO ASN ALA GLU THR ASP ILE GLN SER GLY PRO ILE SER
SEQRES  25 A  389  ASN GLN VAL ILE VAL ASN ASN GLN ASN TRP SER GLY TYR
SEQRES  26 A  389  SER GLY ALA PHE ILE ASP TYR TRP ALA ASN LYS GLU CYS
SEQRES  27 A  389  PHE ASN PRO CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG
SEQRES  28 A  389  PRO LYS GLU SER SER VAL LEU TRP THR SER ASN SER ILE
SEQRES  29 A  389  VAL ALA LEU CYS GLY SER LYS LYS ARG LEU GLY SER TRP
SEQRES  30 A  389  SER TRP HIS ASP GLY ALA GLU ILE ILE TYR PHE GLU
SEQRES   1 B  389  ARG THR PHE LEU ASN LEU THR LYS PRO LEU CYS GLU VAL
SEQRES   2 B  389  ASN SER TRP HIS ILE LEU SER LYS ASP ASN ALA ILE ARG
SEQRES   3 B  389  ILE GLY GLU ASP ALA HIS ILE LEU VAL THR ARG GLU PRO
SEQRES   4 B  389  TYR LEU SER CYS ASP PRO GLN GLY CYS ARG MET PHE ALA
SEQRES   5 B  389  LEU SER GLN GLY THR THR LEU ARG GLY ARG HIS ALA ASN
SEQRES   6 B  389  GLY THR ILE HIS ASP ARG SER PRO PHE ARG ALA LEU ILE
SEQRES   7 B  389  SER TRP GLU MET GLY GLN ALA PRO SER PRO TYR ASN THR
SEQRES   8 B  389  ARG VAL GLU CYS ILE GLY TRP SER SER THR SER CYS HIS
SEQRES   9 B  389  ASP GLY MET SER ARG MET SER ILE CYS MET SER GLY PRO
SEQRES  10 B  389  ASN ASN ASN ALA SER ALA VAL VAL TRP TYR GLY GLY ARG
SEQRES  11 B  389  PRO ILE THR GLU ILE PRO SER TRP ALA GLY ASN ILE LEU
SEQRES  12 B  389  ARG THR GLN GLU SER GLU CYS VAL CYS HIS LYS GLY VAL
SEQRES  13 B  389  CYS PRO VAL VAL MET THR ASP GLY PRO ALA ASN ASN ARG
SEQRES  14 B  389  ALA ALA THR LYS ILE ILE TYR PHE LYS GLU GLY LYS ILE
SEQRES  15 B  389  GLN LYS ILE GLU GLU LEU ALA GLY ASN ALA GLN HIS ILE
SEQRES  16 B  389  GLU GLU CYS SER CYS TYR GLY ALA GLY GLY VAL ILE LYS
SEQRES  17 B  389  CYS ILE CYS ARG ASP ASN TRP LYS GLY ALA ASN ARG PRO
SEQRES  18 B  389  VAL ILE THR ILE ASP PRO GLU MET MET THR HIS THR SER
SEQRES  19 B  389  LYS TYR LEU CYS SER LYS VAL LEU THR ASP THR SER ARG
SEQRES  20 B  389  PRO ASN ASP PRO THR ASN GLY ASN CYS ASP ALA PRO ILE
SEQRES  21 B  389  THR GLY GLY SER PRO ASP PRO GLY VAL LYS GLY PHE ALA
SEQRES  22 B  389  PHE LEU ASP GLY GLU ASN SER TRP LEU GLY ARG THR ILE
SEQRES  23 B  389  SER LYS ASP SER ARG SER GLY TYR GLU MET LEU LYS VAL
SEQRES  24 B  389  PRO ASN ALA GLU THR ASP ILE GLN SER GLY PRO ILE SER
SEQRES  25 B  389  ASN GLN VAL ILE VAL ASN ASN GLN ASN TRP SER GLY TYR
SEQRES  26 B  389  SER GLY ALA PHE ILE ASP TYR TRP ALA ASN LYS GLU CYS
SEQRES  27 B  389  PHE ASN PRO CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG
SEQRES  28 B  389  PRO LYS GLU SER SER VAL LEU TRP THR SER ASN SER ILE
SEQRES  29 B  389  VAL ALA LEU CYS GLY SER LYS LYS ARG LEU GLY SER TRP
SEQRES  30 B  389  SER TRP HIS ASP GLY ALA GLU ILE ILE TYR PHE GLU
SEQRES   1 C  389  ARG THR PHE LEU ASN LEU THR LYS PRO LEU CYS GLU VAL
SEQRES   2 C  389  ASN SER TRP HIS ILE LEU SER LYS ASP ASN ALA ILE ARG
SEQRES   3 C  389  ILE GLY GLU ASP ALA HIS ILE LEU VAL THR ARG GLU PRO
SEQRES   4 C  389  TYR LEU SER CYS ASP PRO GLN GLY CYS ARG MET PHE ALA
SEQRES   5 C  389  LEU SER GLN GLY THR THR LEU ARG GLY ARG HIS ALA ASN
SEQRES   6 C  389  GLY THR ILE HIS ASP ARG SER PRO PHE ARG ALA LEU ILE
SEQRES   7 C  389  SER TRP GLU MET GLY GLN ALA PRO SER PRO TYR ASN THR
SEQRES   8 C  389  ARG VAL GLU CYS ILE GLY TRP SER SER THR SER CYS HIS
SEQRES   9 C  389  ASP GLY MET SER ARG MET SER ILE CYS MET SER GLY PRO
SEQRES  10 C  389  ASN ASN ASN ALA SER ALA VAL VAL TRP TYR GLY GLY ARG
SEQRES  11 C  389  PRO ILE THR GLU ILE PRO SER TRP ALA GLY ASN ILE LEU
SEQRES  12 C  389  ARG THR GLN GLU SER GLU CYS VAL CYS HIS LYS GLY VAL
SEQRES  13 C  389  CYS PRO VAL VAL MET THR ASP GLY PRO ALA ASN ASN ARG
SEQRES  14 C  389  ALA ALA THR LYS ILE ILE TYR PHE LYS GLU GLY LYS ILE
SEQRES  15 C  389  GLN LYS ILE GLU GLU LEU ALA GLY ASN ALA GLN HIS ILE
SEQRES  16 C  389  GLU GLU CYS SER CYS TYR GLY ALA GLY GLY VAL ILE LYS
SEQRES  17 C  389  CYS ILE CYS ARG ASP ASN TRP LYS GLY ALA ASN ARG PRO
SEQRES  18 C  389  VAL ILE THR ILE ASP PRO GLU MET MET THR HIS THR SER
SEQRES  19 C  389  LYS TYR LEU CYS SER LYS VAL LEU THR ASP THR SER ARG
SEQRES  20 C  389  PRO ASN ASP PRO THR ASN GLY ASN CYS ASP ALA PRO ILE
SEQRES  21 C  389  THR GLY GLY SER PRO ASP PRO GLY VAL LYS GLY PHE ALA
SEQRES  22 C  389  PHE LEU ASP GLY GLU ASN SER TRP LEU GLY ARG THR ILE
SEQRES  23 C  389  SER LYS ASP SER ARG SER GLY TYR GLU MET LEU LYS VAL
SEQRES  24 C  389  PRO ASN ALA GLU THR ASP ILE GLN SER GLY PRO ILE SER
SEQRES  25 C  389  ASN GLN VAL ILE VAL ASN ASN GLN ASN TRP SER GLY TYR
SEQRES  26 C  389  SER GLY ALA PHE ILE ASP TYR TRP ALA ASN LYS GLU CYS
SEQRES  27 C  389  PHE ASN PRO CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG
SEQRES  28 C  389  PRO LYS GLU SER SER VAL LEU TRP THR SER ASN SER ILE
SEQRES  29 C  389  VAL ALA LEU CYS GLY SER LYS LYS ARG LEU GLY SER TRP
SEQRES  30 C  389  SER TRP HIS ASP GLY ALA GLU ILE ILE TYR PHE GLU
SEQRES   1 D  389  ARG THR PHE LEU ASN LEU THR LYS PRO LEU CYS GLU VAL
SEQRES   2 D  389  ASN SER TRP HIS ILE LEU SER LYS ASP ASN ALA ILE ARG
SEQRES   3 D  389  ILE GLY GLU ASP ALA HIS ILE LEU VAL THR ARG GLU PRO
SEQRES   4 D  389  TYR LEU SER CYS ASP PRO GLN GLY CYS ARG MET PHE ALA
SEQRES   5 D  389  LEU SER GLN GLY THR THR LEU ARG GLY ARG HIS ALA ASN
SEQRES   6 D  389  GLY THR ILE HIS ASP ARG SER PRO PHE ARG ALA LEU ILE
SEQRES   7 D  389  SER TRP GLU MET GLY GLN ALA PRO SER PRO TYR ASN THR
SEQRES   8 D  389  ARG VAL GLU CYS ILE GLY TRP SER SER THR SER CYS HIS
SEQRES   9 D  389  ASP GLY MET SER ARG MET SER ILE CYS MET SER GLY PRO
SEQRES  10 D  389  ASN ASN ASN ALA SER ALA VAL VAL TRP TYR GLY GLY ARG
SEQRES  11 D  389  PRO ILE THR GLU ILE PRO SER TRP ALA GLY ASN ILE LEU
SEQRES  12 D  389  ARG THR GLN GLU SER GLU CYS VAL CYS HIS LYS GLY VAL
SEQRES  13 D  389  CYS PRO VAL VAL MET THR ASP GLY PRO ALA ASN ASN ARG
SEQRES  14 D  389  ALA ALA THR LYS ILE ILE TYR PHE LYS GLU GLY LYS ILE
SEQRES  15 D  389  GLN LYS ILE GLU GLU LEU ALA GLY ASN ALA GLN HIS ILE
SEQRES  16 D  389  GLU GLU CYS SER CYS TYR GLY ALA GLY GLY VAL ILE LYS
SEQRES  17 D  389  CYS ILE CYS ARG ASP ASN TRP LYS GLY ALA ASN ARG PRO
SEQRES  18 D  389  VAL ILE THR ILE ASP PRO GLU MET MET THR HIS THR SER
SEQRES  19 D  389  LYS TYR LEU CYS SER LYS VAL LEU THR ASP THR SER ARG
SEQRES  20 D  389  PRO ASN ASP PRO THR ASN GLY ASN CYS ASP ALA PRO ILE
SEQRES  21 D  389  THR GLY GLY SER PRO ASP PRO GLY VAL LYS GLY PHE ALA
SEQRES  22 D  389  PHE LEU ASP GLY GLU ASN SER TRP LEU GLY ARG THR ILE
SEQRES  23 D  389  SER LYS ASP SER ARG SER GLY TYR GLU MET LEU LYS VAL
SEQRES  24 D  389  PRO ASN ALA GLU THR ASP ILE GLN SER GLY PRO ILE SER
SEQRES  25 D  389  ASN GLN VAL ILE VAL ASN ASN GLN ASN TRP SER GLY TYR
SEQRES  26 D  389  SER GLY ALA PHE ILE ASP TYR TRP ALA ASN LYS GLU CYS
SEQRES  27 D  389  PHE ASN PRO CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG
SEQRES  28 D  389  PRO LYS GLU SER SER VAL LEU TRP THR SER ASN SER ILE
SEQRES  29 D  389  VAL ALA LEU CYS GLY SER LYS LYS ARG LEU GLY SER TRP
SEQRES  30 D  389  SER TRP HIS ASP GLY ALA GLU ILE ILE TYR PHE GLU
HET    SIA  A1477      21
HET    SIA  A1478      21
HET    BMA  A1480      11
HET    MAN  A1481      11
HET    MAN  A1482      11
HET    MAN  A1483      11
HET    NAG  A1484      14
HET    NAG  A1485      14
HET    NAG  A1486      14
HET    NAG  A1488      14
HET    SIA  B2477      21
HET    SIA  B2478      21
HET    BMA  B2480      11
HET    MAN  B2481      11
HET    MAN  B2482      11
HET    MAN  B2483      11
HET    NAG  B2484      14
HET    NAG  B2485      14
HET    NAG  B2487      14
HET    SIA  C3477      21
HET    SIA  C3478      21
HET    BMA  C3480      11
HET    MAN  C3481      11
HET    MAN  C3482      11
HET    MAN  C3483      11
HET    MAN  C3484      11
HET    NAG  C3485      14
HET    NAG  C3486      14
HET    NAG  C3487      14
HET    NAG  C4481      14
HET    SIA  D4477      21
HET    SIA  D4478      21
HET    BMA  D4480      11
HET    NAG  D4482      14
HET     CA  A1479       1
HET     CA  B2479       1
HET     CA  C3479       1
HET     CA  D4479       1
HET    GOL  A1487       6
HET    GOL  B2486       6
HET    PEG  C3476       7
HET    GOL  C3488       6
HET    GOL  D4483       6
HETNAM     SIA O-SIALIC ACID
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      CA CALCIUM ION
HETNAM     GOL GLYCEROL
HETNAM     PEG DI(HYDROXYETHYL)ETHER
HETSYN     NAG NAG
FORMUL   5  SIA    8(C11 H19 N O9)
FORMUL   7  BMA    4(C6 H12 O6)
FORMUL   8  MAN    10(C6 H12 O6)
FORMUL  11  NAG    12(C8 H15 N O6)
FORMUL  39   CA    4(CA 2+)
FORMUL  43  GOL    4(C3 H8 O3)
FORMUL  45  PEG    C4 H10 O3
FORMUL  48  HOH   *1565(H2 O1)
HELIX    1   1 ASN A  110  GLU A  116  1                                   7
HELIX    2   2 GLY A  148  ASN A  152  5                                   5
HELIX    3   3 GLU A  471  GLU A  476  5                                   6
HELIX    4   4 ASN B 1110  GLU B 1116  1                                   7
HELIX    5   5 GLY B 1148  ASN B 1152  5                                   5
HELIX    6   6 GLU B 1471  GLU B 1476  5                                   6
HELIX    7   7 ASN C 2110  GLU C 2116  1                                   7
HELIX    8   8 GLY C 2148  ASN C 2152  5                                   5
HELIX    9   9 PRO C 2204  ASN C 2207  5                                   4
HELIX   10  10 GLU C 2471  GLU C 2476  5                                   6
HELIX   11  11 ASN D 3110  GLU D 3116  1                                   7
HELIX   12  12 GLY D 3148  ASN D 3152  5                                   5
HELIX   13  13 GLU D 3471  GLU D 3476  5                                   6
SHEET    1  AA 4 SER A 102  LYS A 108  0
SHEET    2  AA 4 THR A 447  SER A 457 -1  O  ALA A 453   N  LEU A 106
SHEET    3  AA 4 PRO A 428  GLY A 437 -1  O  PRO A 428   N  GLY A 456
SHEET    4  AA 4 SER A 413  ILE A 417 -1  O  GLY A 414   N  TYR A 431
SHEET    1  AB 4 TYR A 127  ASP A 131  0
SHEET    2  AB 4 GLY A 134  SER A 141 -1  O  GLY A 134   N  ASP A 131
SHEET    3  AB 4 ALA A 163  GLU A 168 -1  O  ALA A 163   N  SER A 141
SHEET    4  AB 4 ARG A 179  ILE A 183 -1  O  ARG A 179   N  SER A 166
SHEET    1  AC 4 SER A 186  HIS A 191  0
SHEET    2  AC 4 ARG A 196  SER A 202 -1  O  MET A 197   N  CYS A 190
SHEET    3  AC 4 SER A 209  TYR A 214 -1  O  SER A 209   N  SER A 202
SHEET    4  AC 4 ARG A 217  PRO A 223 -1  O  ARG A 217   N  TYR A 214
SHEET    1  AD 3 VAL A 243  ASP A 250  0
SHEET    2  AD 3 ALA A 258  LYS A 265 -1  O  ALA A 258   N  ASP A 250
SHEET    3  AD 3 LYS A 268  GLU A 274 -1  O  LYS A 268   N  LYS A 265
SHEET    1  AE 4 SER A 286  ALA A 290  0
SHEET    2  AE 4 VAL A 293  ILE A 297 -1  O  VAL A 293   N  ALA A 290
SHEET    3  AE 4 PRO A 308  ASP A 313 -1  O  ILE A 310   N  CYS A 296
SHEET    4  AE 4 THR A 318  TYR A 323 -1  O  THR A 318   N  ASP A 313
SHEET    1  AF 4 ALA A 360  PHE A 361  0
SHEET    2  AF 4 TRP A 368  ARG A 371 -1  O  TRP A 368   N  PHE A 361
SHEET    3  AF 4 SER A 379  LYS A 385 -1  O  GLU A 382   N  ARG A 371
SHEET    4  AF 4 SER A 399  TRP A 409 -1  O  SER A 399   N  LYS A 385
SHEET    1  BA 4 SER B1102  LYS B1108  0
SHEET    2  BA 4 THR B1447  SER B1457 -1  O  ALA B1453   N  LEU B1106
SHEET    3  BA 4 PRO B1428  GLY B1437 -1  O  PRO B1428   N  GLY B1456
SHEET    4  BA 4 SER B1413  ILE B1417 -1  O  GLY B1414   N  TYR B1431
SHEET    1  BB 4 TYR B1127  ASP B1131  0
SHEET    2  BB 4 GLY B1134  SER B1141 -1  O  GLY B1134   N  ASP B1131
SHEET    3  BB 4 ALA B1163  GLU B1168 -1  O  ALA B1163   N  SER B1141
SHEET    4  BB 4 ARG B1179  ILE B1183 -1  O  ARG B1179   N  SER B1166
SHEET    1  BC 4 SER B1186  HIS B1191  0
SHEET    2  BC 4 ARG B1196  SER B1202 -1  O  MET B1197   N  CYS B1190
SHEET    3  BC 4 SER B1209  TYR B1214 -1  O  SER B1209   N  SER B1202
SHEET    4  BC 4 ARG B1217  PRO B1223 -1  O  ARG B1217   N  TYR B1214
SHEET    1  BD 3 CYS B1244  ASP B1250  0
SHEET    2  BD 3 ALA B1258  LYS B1265 -1  O  ALA B1258   N  ASP B1250
SHEET    3  BD 3 LYS B1268  GLU B1274 -1  O  LYS B1268   N  LYS B1265
SHEET    1  BE 4 GLU B1283  ALA B1290  0
SHEET    2  BE 4 VAL B1293  ARG B1299 -1  O  VAL B1293   N  ALA B1290
SHEET    3  BE 4 PRO B1308  ASP B1313 -1  O  PRO B1308   N  CYS B1298
SHEET    4  BE 4 THR B1318  TYR B1323 -1  O  THR B1318   N  ASP B1313
SHEET    1  BF 4 ALA B1360  PHE B1361  0
SHEET    2  BF 4 TRP B1368  ARG B1371 -1  O  TRP B1368   N  PHE B1361
SHEET    3  BF 4 SER B1379  LYS B1385 -1  O  GLU B1382   N  ARG B1371
SHEET    4  BF 4 SER B1399  TRP B1409 -1  O  SER B1399   N  LYS B1385
SHEET    1  CA 4 SER C2102  LYS C2108  0
SHEET    2  CA 4 THR C2447  SER C2457 -1  O  ALA C2453   N  LEU C2106
SHEET    3  CA 4 PRO C2428  GLY C2437 -1  O  PRO C2428   N  GLY C2456
SHEET    4  CA 4 SER C2413  ILE C2417 -1  O  GLY C2414   N  TYR C2431
SHEET    1  CB 4 LEU C2121  ASP C2131  0
SHEET    2  CB 4 GLY C2134  THR C2145 -1  O  GLY C2134   N  ASP C2131
SHEET    3  CB 4 ALA C2163  GLU C2168 -1  O  ALA C2163   N  SER C2141
SHEET    4  CB 4 ARG C2179  ILE C2183 -1  O  ARG C2179   N  SER C2166
SHEET    1  CC 4 SER C2187  HIS C2191  0
SHEET    2  CC 4 ARG C2196  SER C2202 -1  O  MET C2197   N  CYS C2190
SHEET    3  CC 4 SER C2209  TYR C2214 -1  O  SER C2209   N  SER C2202
SHEET    4  CC 4 ARG C2217  PRO C2223 -1  O  ARG C2217   N  TYR C2214
SHEET    1  CD 3 VAL C2243  ASP C2250  0
SHEET    2  CD 3 ALA C2258  LYS C2265 -1  O  ALA C2258   N  ASP C2250
SHEET    3  CD 3 LYS C2268  GLU C2274 -1  O  LYS C2268   N  LYS C2265
SHEET    1  CE 4 GLU C2283  ALA C2290  0
SHEET    2  CE 4 VAL C2293  ARG C2299 -1  O  VAL C2293   N  ALA C2290
SHEET    3  CE 4 PRO C2308  ASP C2313 -1  O  PRO C2308   N  CYS C2298
SHEET    4  CE 4 THR C2318  TYR C2323 -1  O  THR C2318   N  ASP C2313
SHEET    1  CF 4 ALA C2360  PHE C2361  0
SHEET    2  CF 4 TRP C2368  ARG C2371 -1  O  TRP C2368   N  PHE C2361
SHEET    3  CF 4 SER C2379  LYS C2385 -1  O  GLU C2382   N  ARG C2371
SHEET    4  CF 4 SER C2399  TRP C2409 -1  O  SER C2399   N  LYS C2385
SHEET    1  DA 4 SER D3102  LYS D3108  0
SHEET    2  DA 4 THR D3447  SER D3457 -1  O  ALA D3453   N  LEU D3106
SHEET    3  DA 4 PRO D3428  GLY D3437 -1  O  PRO D3428   N  GLY D3456
SHEET    4  DA 4 SER D3413  ILE D3417 -1  O  GLY D3414   N  TYR D3431
SHEET    1  DB 4 LEU D3121  ASP D3131  0
SHEET    2  DB 4 GLY D3134  THR D3145 -1  O  GLY D3134   N  ASP D3131
SHEET    3  DB 4 ALA D3163  GLU D3168 -1  O  ALA D3163   N  SER D3141
SHEET    4  DB 4 ARG D3179  ILE D3183 -1  O  ARG D3179   N  SER D3166
SHEET    1  DC 4 SER D3186  HIS D3191  0
SHEET    2  DC 4 ARG D3196  SER D3202 -1  O  MET D3197   N  CYS D3190
SHEET    3  DC 4 SER D3209  TYR D3214 -1  O  SER D3209   N  SER D3202
SHEET    4  DC 4 ARG D3217  PRO D3223 -1  O  ARG D3217   N  TYR D3214
SHEET    1  DD 3 CYS D3244  ASP D3250  0
SHEET    2  DD 3 ALA D3258  LYS D3265 -1  O  ALA D3258   N  ASP D3250
SHEET    3  DD 3 LYS D3268  GLU D3274 -1  O  LYS D3268   N  LYS D3265
SHEET    1  DE 4 GLU D3283  ALA D3290  0
SHEET    2  DE 4 VAL D3293  ARG D3299 -1  O  VAL D3293   N  ALA D3290
SHEET    3  DE 4 PRO D3308  ASP D3313 -1  O  PRO D3308   N  CYS D3298
SHEET    4  DE 4 THR D3318  TYR D3323 -1  O  THR D3318   N  ASP D3313
SHEET    1  DF 4 ALA D3360  PHE D3361  0
SHEET    2  DF 4 TRP D3368  ARG D3371 -1  O  TRP D3368   N  PHE D3361
SHEET    3  DF 4 SER D3379  LYS D3385 -1  O  GLU D3382   N  ARG D3371
SHEET    4  DF 4 SER D3399  TRP D3409 -1  O  SER D3399   N  LYS D3385
SSBOND   1 CYS A   98    CYS A  425                          1555   1555  2.16
SSBOND   2 CYS A  130    CYS A  135                          1555   1555  2.03
SSBOND   3 CYS A  182    CYS A  200                          1555   1555  2.11
SSBOND   4 CYS A  190    CYS A  237                          1555   1555  2.10
SSBOND   5 CYS A  239    CYS A  244                          1555   1555  2.06
SSBOND   6 CYS A  285    CYS A  298                          1555   1555  2.14
SSBOND   7 CYS A  287    CYS A  296                          1555   1555  2.08
SSBOND   8 CYS A  325    CYS A  343                          1555   1555  2.09
SSBOND   9 CYS A  429    CYS A  455                          1555   1555  2.05
SSBOND  10 CYS B 1098    CYS B 1425                          1555   1555  2.05
SSBOND  11 CYS B 1130    CYS B 1135                          1555   1555  2.07
SSBOND  12 CYS B 1182    CYS B 1200                          1555   1555  2.11
SSBOND  13 CYS B 1190    CYS B 1237                          1555   1555  2.04
SSBOND  14 CYS B 1239    CYS B 1244                          1555   1555  2.07
SSBOND  15 CYS B 1285    CYS B 1298                          1555   1555  2.15
SSBOND  16 CYS B 1287    CYS B 1296                          1555   1555  2.10
SSBOND  17 CYS B 1325    CYS B 1343                          1555   1555  2.05
SSBOND  18 CYS B 1429    CYS B 1455                          1555   1555  2.08
SSBOND  19 CYS C 2098    CYS C 2425                          1555   1555  2.05
SSBOND  20 CYS C 2130    CYS C 2135                          1555   1555  2.07
SSBOND  21 CYS C 2182    CYS C 2200                          1555   1555  2.14
SSBOND  22 CYS C 2190    CYS C 2237                          1555   1555  2.06
SSBOND  23 CYS C 2239    CYS C 2244                          1555   1555  2.07
SSBOND  24 CYS C 2285    CYS C 2298                          1555   1555  2.08
SSBOND  25 CYS C 2287    CYS C 2296                          1555   1555  2.08
SSBOND  26 CYS C 2325    CYS C 2343                          1555   1555  2.05
SSBOND  27 CYS C 2429    CYS C 2455                          1555   1555  2.07
SSBOND  28 CYS D 3098    CYS D 3425                          1555   1555  2.04
SSBOND  29 CYS D 3130    CYS D 3135                          1555   1555  2.05
SSBOND  30 CYS D 3182    CYS D 3200                          1555   1555  2.07
SSBOND  31 CYS D 3190    CYS D 3237                          1555   1555  2.06
SSBOND  32 CYS D 3239    CYS D 3244                          1555   1555  2.04
SSBOND  33 CYS D 3285    CYS D 3298                          1555   1555  2.16
SSBOND  34 CYS D 3287    CYS D 3296                          1555   1555  2.09
SSBOND  35 CYS D 3325    CYS D 3343                          1555   1555  2.04
SSBOND  36 CYS D 3429    CYS D 3455                          1555   1555  2.04
LINK         ND2 ASN A  92                 C1  NAG A1484     1555   1555  1.86
LINK         ND2 ASN A 152                 C1  NAG A1485     1555   1555  1.86
LINK        CA    CA A1479                 O   ASP A 300     1555   1555  2.53
LINK        CA    CA A1479                 O   GLY A 304     1555   1555  2.45
LINK        CA    CA A1479                 OD2 ASP A 331     1555   1555  2.43
LINK        CA    CA A1479                 O   HOH A2259     1555   1555  3.23
LINK        CA    CA A1479                 O   PRO A 354     1555   1555  2.62
LINK         O6  BMA A1480                 C1  MAN A1481     1555   1555  1.88
LINK         O6  MAN A1481                 C1  MAN A1482     1555   1555  1.85
LINK         C1  NAG A1486                 O4  NAG A1488     1555   1555  1.66
LINK         ND2 ASN B1152                 C1  NAG B2484     1555   1555  2.02
LINK        CA    CA B2479                 O   HOH B2261     1555   1555  2.98
LINK        CA    CA B2479                 O   PRO B1354     1555   1555  2.73
LINK        CA    CA B2479                 O   ASP B1300     1555   1555  2.40
LINK        CA    CA B2479                 OD2 ASP B1331     1555   1555  2.68
LINK        CA    CA B2479                 O   GLY B1304     1555   1555  2.51
LINK         C1  BMA B2480                 O4  NAG B2485     1555   1555  1.97
LINK         O6  MAN B2481                 C1  MAN B2482     1555   1555  1.78
LINK         C1  NAG B2485                 O4  NAG B2487     1555   1555  1.97
LINK         ND2 ASN C2207                 C1  NAG C3487     1555   1555  2.04
LINK        CA    CA C3479                 OD2 ASP C2331     1555   1555  2.80
LINK        CA    CA C3479                 O   PRO C2354     1555   1555  2.47
LINK        CA    CA C3479                 O   ASP C2300     1555   1555  2.56
LINK        CA    CA C3479                 O   GLY C2304     1555   1555  2.62
LINK        CA    CA C3479                 O   HOH C3255     1555   1555  3.04
LINK         O6  BMA C3480                 C1  MAN C3482     1555   1555  1.78
LINK         C1  BMA C3480                 O4  NAG C3485     1555   1555  1.99
LINK         O4  NAG C3487                 C1  NAG C4481     1555   1555  1.68
LINK         ND2 ASN D3152                 C1  NAG D4482     1555   1555  1.88
LINK         ND2 ASN D3207                 C1  NAG B2487     1555   1555  1.64
LINK        CA    CA D4479                 O   ASP D3300     1555   1555  2.60
LINK        CA    CA D4479                 O   GLY D3304     1555   1555  2.54
LINK        CA    CA D4479                 OD2 ASP D3331     1555   1555  2.56
LINK        CA    CA D4479                 O   PRO D3354     1555   1555  2.44
LINK        CA    CA D4479                 O   HOH D2288     1555   1555  3.02
CISPEP   1 SER A  351    PRO A  352          0         1.95
CISPEP   2 ARG A  438    PRO A  439          0        -1.55
CISPEP   3 SER B 1351    PRO B 1352          0        -0.41
CISPEP   4 ARG B 1438    PRO B 1439          0         0.74
CISPEP   5 SER C 2351    PRO C 2352          0        -7.79
CISPEP   6 ARG C 2438    PRO C 2439          0        -4.01
CISPEP   7 SER D 3351    PRO D 3352          0        -1.97
CISPEP   8 ARG D 3438    PRO D 3439          0         1.20
SITE     1 AC1 14 ARG A 124  GLU A 125  ASP A 157  ARG A 158
SITE     2 AC1 14 ALA A 253  GLU A 283  GLU A 284  ARG A 299
SITE     3 AC1 14 ASN A 301  ARG A 378  TYR A 412  HOH A2096
SITE     4 AC1 14 HOH A2373  HOH A2374
SITE     1 AC2  7 SER A 374  SER A 377  SER A 379  ASN A 406
SITE     2 AC2  7 GLN A 407  TRP A 409  HOH A2375
SITE     1 AC3  9 PRO A 397  ILE A 398  SER A 399  ASN A 400
SITE     2 AC3  9 MAN A1481  NAG A1486  HOH A2376  HOH A2377
SITE     3 AC3  9 HOH A2378
SITE     1 AC4  9 LEU A 384  PRO A 397  ASN A 400  BMA A1480
SITE     2 AC4  9 MAN A1482  MAN A1483  HOH A2379  HOH A2380
SITE     3 AC4  9 HOH A2383
SITE     1 AC5  6 ASP A 337  ARG A 371  MAN A1481  HOH A2381
SITE     2 AC5  6 HOH A2383  HOH A2384
SITE     1 AC6  8 GLU A 382  ASN A 400  VAL A 402  MAN A1481
SITE     2 AC6  8 HOH A2385  HOH A2386  HOH A2387  HOH A2388
SITE     1 AC7  4 ASN A  92  LYS A 241  HOH A2389  HOH A2390
SITE     1 AC8  7 ASN A 152  LEU A 445  HOH A2059  HOH A2391
SITE     2 AC8  7 HOH A2393  HOH A2394  TYR C2474
SITE     1 AC9  8 SER A 399  ASN A 400  BMA A1480  NAG A1488
SITE     2 AC9  8 HOH A2345  HOH A2395  HOH A2396  HOH A2397
SITE     1 BC1  5 ARG A 460  LEU A 461  GLY A 462  NAG A1486
SITE     2 BC1  5 ASN B1207
SITE     1 BC2 17 ARG B1124  GLU B1125  ASP B1157  ARG B1158
SITE     2 BC2 17 TRP B1185  ALA B1253  GLU B1283  GLU B1284
SITE     3 BC2 17 ARG B1299  ARG B1378  TYR B1412  HOH B2161
SITE     4 BC2 17 HOH B2162  HOH B2365  HOH B2366  HOH B2367
SITE     5 BC2 17 HOH B2368
SITE     1 BC3  5 SER B1374  SER B1377  SER B1379  ASN B1406
SITE     2 BC3  5 TRP B1409
SITE     1 BC4  7 ILE B1398  SER B1399  ASN B1400  HOH B2371
SITE     2 BC4  7 HOH B2372  MAN B2481  NAG B2485
SITE     1 BC5  7 GLU B1382  PRO B1397  ASN B1400  HOH B2374
SITE     2 BC5  7 BMA B2480  MAN B2482  MAN B2483
SITE     1 BC6  3 ASP B1337  ARG B1371  MAN B2481
SITE     1 BC7  6 GLU B1382  ASN B1400  VAL B1402  HOH B2377
SITE     2 BC7  6 HOH B2378  MAN B2481
SITE     1 BC8  7 TYR A 474  ASN B1152  LEU B1445  HOH B2063
SITE     2 BC8  7 HOH B2380  HOH B2381  HOH B2382
SITE     1 BC9  4 SER B1399  ASN B1400  BMA B2480  NAG B2487
SITE     1 CC1  7 LEU B1461  GLY B1462  SER B1463  HOH B2384
SITE     2 CC1  7 HOH B2385  NAG B2485  ASN D3207
SITE     1 CC2 17 ARG C2124  GLU C2125  ASP C2157  ARG C2158
SITE     2 CC2 17 ARG C2231  ALA C2253  GLU C2283  GLU C2284
SITE     3 CC2 17 ARG C2299  ARG C2378  TYR C2412  HOH C3186
SITE     4 CC2 17 HOH C3189  HOH C3357  HOH C3358  HOH C3360
SITE     5 CC2 17 HOH C3362
SITE     1 CC3  8 SER C2374  SER C2377  SER C2379  ASN C2406
SITE     2 CC3  8 GLN C2407  ASN C2408  TRP C2409  HOH C3363
SITE     1 CC4  7 ILE C2398  SER C2399  ASN C2400  HOH C3364
SITE     2 CC4  7 MAN C3481  MAN C3482  NAG C3485
SITE     1 CC5  3 HOH C3365  HOH C3366  BMA C3480
SITE     1 CC6  6 LEU C2384  PRO C2397  ASN C2400  BMA C3480
SITE     2 CC6  6 MAN C3483  MAN C3484
SITE     1 CC7  3 ASP C2337  ARG C2371  MAN C3482
SITE     1 CC8  6 GLU C2382  ASN C2400  VAL C2402  HOH C3369
SITE     2 CC8  6 HOH C3370  MAN C3482
SITE     1 CC9  5 SER C2102  SER C2399  ASN C2400  HOH C3364
SITE     2 CC9  5 BMA C3480
SITE     1 DC1  8 ASN C2152  LEU C2445  HOH C3073  HOH C3371
SITE     2 DC1  8 HOH C3372  HOH C3373  HOH D2394  TYR D3474
SITE     1 DC2  6 ASN C2207  HOH C3374  NAG C4481  LEU D3461
SITE     2 DC2  6 GLY D3462  SER D3463
SITE     1 DC3  5 HOH C3374  NAG C3487  SER D3399  ASN D3400
SITE     2 DC3  5 BMA D4480
SITE     1 DC4 17 HOH D2138  HOH D2216  HOH D2218  HOH D2397
SITE     2 DC4 17 HOH D2398  HOH D2399  ARG D3124  GLU D3125
SITE     3 DC4 17 ASP D3157  ARG D3158  ARG D3231  ALA D3253
SITE     4 DC4 17 GLU D3283  GLU D3284  ARG D3299  ARG D3378
SITE     5 DC4 17 TYR D3412
SITE     1 DC5  7 HOH D2400  SER D3374  SER D3377  SER D3379
SITE     2 DC5  7 ASN D3406  GLN D3407  TRP D3409
SITE     1 DC6  3 NAG C4481  HOH D2403  ASN D3400
SITE     1 DC7  9 TYR B1474  HOH D2101  HOH D2404  HOH D2405
SITE     2 DC7  9 HOH D2406  HOH D2407  HOH D2408  ASN D3152
SITE     3 DC7  9 LEU D3445
SITE     1 DC8  4 ASP A 300  GLY A 304  ASP A 331  PRO A 354
SITE     1 DC9  5 ASP B1300  GLY B1304  ASP B1331  PRO B1354
SITE     2 DC9  5 HOH B2261
SITE     1 EC1  5 ASP C2300  GLY C2304  ASP C2331  PRO C2354
SITE     2 EC1  5 HOH C3255
SITE     1 EC2  5 HOH D2288  ASP D3300  GLY D3304  ASP D3331
SITE     2 EC2  5 PRO D3354
SITE     1 EC3  4 GLN A 142  HIS A 150  SER A 159  ARG C2113
SITE     1 EC4  5 ARG A 113  GLN B1142  HIS B1150  ASN B1152
SITE     2 EC4  5 SER B1159
SITE     1 EC5 12 PRO A 218  GLU A 221  HIS C2104  LYS C2423
SITE     2 EC5 12 ASN C2427  CYS C2429  CYS C2455  GLY C2456
SITE     3 EC5 12 HOH C3298  HOH C3354  HOH C3355  HOH C3356
SITE     1 EC6  5 GLN C2142  HIS C2150  SER C2159  HOH C3083
SITE     2 EC6  5 ARG D3113
SITE     1 EC7  5 ARG B1113  HOH D2107  GLN D3142  HIS D3150
SITE     2 EC7  5 SER D3159
CRYST1  106.993   73.464  107.413  90.00  90.38  90.00 P 1 21 1      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      0.009346  0.000000  0.000063        0.00000
SCALE2      0.000000  0.013612  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009310        0.00000
      
PROCHECK
Go to PROCHECK summary
 References