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PDBsum entry 1v0z

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Hydrolase PDB id
1v0z
Jmol
Contents
Protein chains
389 a.a.
Ligands
GOL ×4
NAG-NAG ×2
NAG ×13
MAN-MAN-MAN-BMA-
MAN
NAG-NAG-BMA-MAN-
MAN-MAN-MAN
MAN-MAN
MAN ×3
BMA-NAG
PEG
BMA-MAN
Metals
_CA ×4
Waters ×1798
HEADER    HYDROLASE                               02-APR-04   1V0Z
TITLE     STRUCTURE OF NEURAMINIDASE FROM ENGLISH DUCK SUBTYPE N6
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
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
KEYWDS    GLYCOSIDASE, HYDROLASE
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 1V0Z    1       VERSN
REVDAT   3   02-MAR-06 1V0Z    1       REMARK
REVDAT   2   22-FEB-06 1V0Z    1       REMARK
REVDAT   1   25-JAN-06 1V0Z    0
JRNL        AUTH   E.RUDINO-PINERA,S.J.CRENNELL,R.G.WEBSTER,W.G.LAVER,
JRNL        AUTH 2 E.F.GARMAN
JRNL        TITL   THE CRYSTAL STRUCTURE OF INFLUENZA TYPE A VIRUS
JRNL        TITL 2 NEURAMINIDASE OF THE N6 SUBTYPE AT 1.85 A
JRNL        TITL 3 RESOLUTION
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.84 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.0
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) : 1.84
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 127094
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) : 0.151
REMARK   3   R VALUE            (WORKING SET) : 0.149
REMARK   3   FREE R VALUE                     : 0.190
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 6696
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) : 1.84
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.89
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8240
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1950
REMARK   3   BIN FREE R VALUE SET COUNT          : 429
REMARK   3   BIN FREE R VALUE                    : 0.2570
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 12036
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 513
REMARK   3   SOLVENT ATOMS            : 1798
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 18.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.07
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.02000
REMARK   3    B22 (A**2) : 2.34000
REMARK   3    B33 (A**2) : -1.31000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.04000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.126
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.119
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.072
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.321
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12862 ; 0.013 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17494 ; 1.428 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1552 ; 7.180 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   552 ;34.186 ;23.913
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2004 ;12.534 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;16.132 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1938 ; 0.101 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9604 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6209 ; 0.215 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  8618 ; 0.306 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1482 ; 0.142 ; 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):    46 ; 0.188 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    35 ; 0.145 ; 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):  7996 ; 0.656 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12480 ; 1.038 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5671 ; 1.828 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5014 ; 2.840 ; 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   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1V0Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  06-JUL-05.
REMARK 100 THE PDBE ID CODE IS EBI-20011.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-95
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SRS
REMARK 200  BEAMLINE                       : PX7.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 127094
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.840
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.960
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 6.700
REMARK 200  R MERGE                    (I) : 0.07000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.16000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1NNA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 PERCENT (W/V) PEG 3350,
REMARK 280  150 MM NACL
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       36.87750
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   CZ   ARG A   256  -  O    HOH A  2215              1.45
REMARK 500   NH1  ARG A   256  -  O    HOH A  2215              0.31
REMARK 500   CG   ASP A   353  -  O    HOH A  2301              1.83
REMARK 500   OD2  ASP A   353  -  O    HOH A  2301              0.53
REMARK 500   CZ   ARG B   256  -  O    HOH B  2202              2.03
REMARK 500   NH2  ARG B   256  -  O    HOH B  2202              0.87
REMARK 500   CZ   ARG B   460  -  O    HOH B  2386              1.25
REMARK 500   NH1  ARG B   460  -  O    HOH B  2386              2.18
REMARK 500   NH2  ARG B   460  -  O    HOH B  2386              0.17
REMARK 500   O    ASP B   468  -  O    HOH B  2402              1.97
REMARK 500   CZ   ARG C   256  -  O    HOH C  2210              1.55
REMARK 500   CZ   ARG C   256  -  O    HOH C  2208              1.72
REMARK 500   NH1  ARG C   256  -  O    HOH C  2210              0.29
REMARK 500   NH2  ARG C   256  -  O    HOH C  2208              0.40
REMARK 500   CD   GLU C   424  -  O    HOH C  2383              1.30
REMARK 500   OE1  GLU C   424  -  O    HOH C  2383              1.94
REMARK 500   OE2  GLU C   424  -  O    HOH C  2383              0.59
REMARK 500   NH1  ARG C   460  -  O    HOH C  2412              1.60
REMARK 500   CD   GLU C   471  -  O    HOH C  2428              2.12
REMARK 500   OE1  GLU C   471  -  O    HOH C  2428              0.87
REMARK 500   OD1  ASP D   117  -  O    HOH D  2029              1.31
REMARK 500   O6   BMA A  1490  -  C2   MAN A  1493              2.20
REMARK 500   C6   MAN A  1492  -  O    HOH A  2447              1.57
REMARK 500   O6   MAN A  1492  -  O    HOH A  2447              0.18
REMARK 500   C1   NAG B  1487  -  O4   NAG D  1481              2.15
REMARK 500   C4   MAN D  1483  -  O    HOH D  2460              2.17
REMARK 500   O4   MAN D  1483  -  O    HOH D  2460              0.93
REMARK 500   O    HOH A  2132  -  O    HOH A  2256              2.19
REMARK 500   O    HOH A  2357  -  O    HOH A  2362              2.20
REMARK 500   O    HOH B  2011  -  O    HOH B  2359              1.90
REMARK 500   O    HOH C  2005  -  O    HOH C  2008              2.19
REMARK 500   O    HOH C  2023  -  O    HOH C  2034              1.87
REMARK 500   O    HOH C  2181  -  O    HOH C  2381              2.11
REMARK 500   O    HOH C  2191  -  O    HOH C  2396              2.08
REMARK 500   O    HOH D  2065  -  O    HOH D  2095              2.14
REMARK 500   O    HOH D  2111  -  O    HOH D  2117              2.19
REMARK 500   O    HOH D  2196  -  O    HOH D  2378              2.12
REMARK 500   O    HOH D  2387  -  O    HOH D  2418              2.17
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. =  14.1 DEGREES
REMARK 500    LEU B 128   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES
REMARK 500    LEU C 128   CA  -  CB  -  CG  ANGL. DEV. =  16.3 DEGREES
REMARK 500    LEU D 128   CA  -  CB  -  CG  ANGL. DEV. =  15.4 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    ASN A 207       40.51   -159.26
REMARK 500    ASN A 228       77.03   -150.83
REMARK 500    THR A 232     -156.30   -145.58
REMARK 500    LYS A 271      146.29   -170.25
REMARK 500    CYS A 298     -166.36   -120.33
REMARK 500    LYS A 322     -156.29   -158.56
REMARK 500    TRP A 466       52.31   -105.50
REMARK 500    LEU B  93       44.49    -85.63
REMARK 500    ASN B 207       43.97   -161.35
REMARK 500    THR B 232     -157.52   -148.03
REMARK 500    LYS B 322     -159.05   -165.74
REMARK 500    TRP B 466       52.10   -112.05
REMARK 500    ASN C 207       41.48   -159.55
REMARK 500    THR C 232     -153.08   -142.09
REMARK 500    LYS C 271      147.22   -170.85
REMARK 500    CYS C 298     -168.75   -121.53
REMARK 500    LYS C 322     -158.36   -165.92
REMARK 500    TRP C 466       52.62   -103.82
REMARK 500    ASN D 207       38.99   -157.82
REMARK 500    ASN D 228       79.55   -150.38
REMARK 500    THR D 232     -156.51   -143.57
REMARK 500    LYS D 271      146.31   -175.43
REMARK 500    CYS D 298     -167.72   -121.88
REMARK 500    LYS D 322     -154.94   -160.42
REMARK 500    TRP D 466       52.14   -107.22
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 C 330        24.4      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     NAG A 1482
REMARK 610     NAG B 1479
REMARK 610     NAG B 1481
REMARK 610     NAG B 1482
REMARK 610     NAG B 1487
REMARK 610     NAG C 1480
REMARK 610     NAG C 1482
REMARK 610     NAG D 1479
REMARK 610     MAN B 1485
REMARK 610     MAN D 1483
REMARK 610     BMA C 1486
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 A1477  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 300   O
REMARK 620 2 GLY A 304   O    84.8
REMARK 620 3 ASP A 331   OD2  97.3  96.8
REMARK 620 4 PRO A 354   O    96.1 157.4 105.5
REMARK 620 5 HOH A2271   O   164.6  89.3  97.6  84.0
REMARK 620 6 HOH A2306   O    84.9  95.8 167.4  61.9  81.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B1477  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2300   O
REMARK 620 2 GLY B 304   O    95.2
REMARK 620 3 ASP B 300   O    79.2  86.0
REMARK 620 4 PRO B 354   O    65.8 160.4  94.9
REMARK 620 5 ASP B 331   OD2 168.3  94.9  95.5 104.6
REMARK 620 6 HOH B2271   O    88.1  88.4 165.5  86.0  98.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA C1477  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 331   OD2
REMARK 620 2 ASP C 300   O    94.8
REMARK 620 3 HOH C2283   O    96.4 168.6
REMARK 620 4 PRO C 354   O   100.8  96.6  79.5
REMARK 620 5 GLY C 304   O    99.2  87.8  92.2 159.1
REMARK 620 6 HOH C2311   O   159.7  89.3  79.6  59.0 100.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA D1477  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 331   OD2
REMARK 620 2 ASP D 300   O    97.5
REMARK 620 3 GLY D 304   O    96.3  85.3
REMARK 620 4 PRO D 354   O   104.5  96.6 158.7
REMARK 620 5 HOH D2309   O    96.3 165.8  89.8  83.3
REMARK 620 6 HOH D2342   O   168.3  82.9  95.4  63.9  84.3
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1487
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1495
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1485
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1488
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1489
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1490
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1491
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1492
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1493
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1494
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B1486
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1487
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B1485
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1485
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1486
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C1487
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA D1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1478
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A14   RELATED DB: PDB
REMARK 900  COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 5
REMARK 900   RESIDUE LINKER AND INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 1A4G   RELATED DB: PDB
REMARK 900  INFLUENZA VIRUS B/BEIJING/1/87 NEURAMINIDASE
REMARK 900   COMPLEXED WITH ZANAMIVIR
REMARK 900 RELATED ID: 1A4Q   RELATED DB: PDB
REMARK 900  INFLUENZA VIRUS B/BEIJING/1/87 NEURAMINIDASE
REMARK 900   COMPLEXED WITH DIHYDROPYRAN-PHENETHYL-PROPYL-
REMARK 900  CARBOXAMIDE
REMARK 900 RELATED ID: 1B9S   RELATED DB: PDB
REMARK 900  NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH
REMARK 900  CONSERVED RESIDUES AND WATER MOLECULES IN
REMARK 900  THE ACTIVE SITE
REMARK 900 RELATED ID: 1B9T   RELATED DB: PDB
REMARK 900  NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH
REMARK 900  CONSERVED RESIDUES AND WATER MOLECULES IN
REMARK 900  THE ACTIVE SITE
REMARK 900 RELATED ID: 1B9V   RELATED DB: PDB
REMARK 900  NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH
REMARK 900  CONSERVED RESIDUES AND WATER MOLECULES IN
REMARK 900  TEH ACTIVE SITE
REMARK 900 RELATED ID: 1BJI   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF TERN
REMARK 900   N9 INFLUENZA VIRUS NEURAMINIDASE COMPLEXED
REMARK 900  WITH THE GLAXO 6-CARBOXAMIDE SIALIC ACID
REMARK 900  ANALOGUE GR217029
REMARK 900 RELATED ID: 1E8T   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS
REMARK 900  HEMAGGLUTININ-NEURAMINIDASE
REMARK 900 RELATED ID: 1E8U   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS
REMARK 900  HEMAGGLUTININ-NEURAMINIDASE
REMARK 900 RELATED ID: 1E8V   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS
REMARK 900  HEMAGGLUTININ-NEURAMINIDASE
REMARK 900 RELATED ID: 1EUU   RELATED DB: PDB
REMARK 900  SIALIDASE OR NEURAMINIDASE, LARGE 68KD FORM
REMARK 900 RELATED ID: 1F8B   RELATED DB: PDB
REMARK 900  NATIVE INFLUENZA VIRUS NEURAMINIDASE IN
REMARK 900  COMPLEX WITHNEU5AC2EN
REMARK 900 RELATED ID: 1F8C   RELATED DB: PDB
REMARK 900  NATIVE INFLUENZA NEURAMINIDASE IN COMPLEX WITH
REMARK 900   4-AMINO-2-DEOXY-2,3-DEHYDRO-N-
REMARK 900  NEURAMINIC ACID
REMARK 900 RELATED ID: 1F8D   RELATED DB: PDB
REMARK 900  NATIVE INFLUENZA NEURAMINIDASE IN COMPLEX WITH
REMARK 900   9-AMINO-2-DEOXY-2,3-DEHYDRO-N-
REMARK 900  NEURAMINIC ACID
REMARK 900 RELATED ID: 1F8E   RELATED DB: PDB
REMARK 900  NATIVE INFLUENZA NEURAMINIDASE IN COMPLEX WITH
REMARK 900   4,9-DIAMINO-2-DEOXY-2,3-DEHYDRO-N-
REMARK 900  ACETYL-NEURAMINIC ACID
REMARK 900 RELATED ID: 1INF   RELATED DB: PDB
REMARK 900  INFLUENZA VIRUS B/LEE/40 NEURAMINIDASE
REMARK 900  COMPLEXED WITH BANA113 INHIBITOR
REMARK 900 RELATED ID: 1ING   RELATED DB: PDB
REMARK 900  INFLUENZA A SUBTYPE N2 NEURAMINIDASE COMPLEXED
REMARK 900   WITH AROMATIC BANA109 INHIBITOR
REMARK 900 RELATED ID: 1INH   RELATED DB: PDB
REMARK 900  INFLUENZA A SUBTYPE N2 NEURAMINIDASE COMPLEXED
REMARK 900   WITH AROMATIC BANA111 INHIBITOR
REMARK 900 RELATED ID: 1INV   RELATED DB: PDB
REMARK 900  INFLUENZA B/LEE/40 NEURAMINIDASE (SIALIDASE)
REMARK 900  COMPLEXED WITH EPANA INHIBITOR (4-ACETAMIDO-
REMARK 900  2,4-DIDEOXY-D-GLYCERO-ALPHA-D-GALACTO-1
REMARK 900  -OCTOPYRANOSYL) PHOSPHONIC ACID
REMARK 900 RELATED ID: 1INW   RELATED DB: PDB
REMARK 900  INFLUENZA A SUBTYPE N2 NEURAMINIDASE (
REMARK 900  SIALIDASE) COMPLEXED WITH APANA INHIBITOR (4-
REMARK 900  ACETAMIDO- 2,4-DIDEOXY-D-GLYCERO-BETA-D-
REMARK 900  GALACTO-1-OCTOPYRANOSYL) PHOSPHONIC ACID
REMARK 900 RELATED ID: 1INX   RELATED DB: PDB
REMARK 900  INFLUENZA A SUBTYPE N2 NEURAMINIDASE (
REMARK 900  SIALIDASE) COMPLEXED WITH EPANA INHIBITOR (4-
REMARK 900  ACETAMIDO- 2,4-DIDEOXY-D-GLYCERO-ALPHA-D-
REMARK 900  GALACTO-1-OCTOPYRANOSYL) PHOSPHONIC ACID
REMARK 900 RELATED ID: 1INY   RELATED DB: PDB
REMARK 900  INFLUENZA A SUBTYPE N9 NEURAMINIDASE (
REMARK 900  SIALIDASE) COMPLEXED WITH EPANA INHIBITOR (4-
REMARK 900  ACETAMIDO- 2,4-DIDEOXY-D-GLYCERO-ALPHA-D-
REMARK 900  GALACTO-1-OCTOPYRANOSYL) PHOSPHONIC ACID
REMARK 900 RELATED ID: 1IVB   RELATED DB: PDB
REMARK 900  INFLUENZA VIRUS B/LEE/40 NEURAMINIDASE (
REMARK 900  SIALIDASE) COMPLEXED WITH BANA105 INHIBITOR (4
REMARK 900  -(ACETYLAMINO)-3-HYDROXY-5-NITROBENZOIC ACID
REMARK 900  )
REMARK 900 RELATED ID: 1IVC   RELATED DB: PDB
REMARK 900  INFLUENZA A SUBTYPE N2 NEURAMINIDASE (
REMARK 900  SIALIDASE) COMPLEXED WITH AROMATIC BANA106
REMARK 900  INHIBITOR (4-(ACETYLAMINO)-5-AMINO-3-
REMARK 900  HYDROXYBENZOIC ACID)
REMARK 900 RELATED ID: 1IVD   RELATED DB: PDB
REMARK 900  INFLUENZA A SUBTYPE N2 NEURAMINIDASE (
REMARK 900  SIALIDASE) COMPLEXED WITH AROMATIC BANA105
REMARK 900  INHIBITOR (4-(ACETYLAMINO)-3-HYDROXY-5-
REMARK 900  NITROBENZOIC ACID)
REMARK 900 RELATED ID: 1IVE   RELATED DB: PDB
REMARK 900  INFLUENZA A SUBTYPE N2 NEURAMINIDASE (
REMARK 900  SIALIDASE) COMPLEXED WITH AROMATIC BANA108
REMARK 900  INHIBITOR (4-(ACETYLAMINO)-3-AMINOBENZOIC ACID
REMARK 900  )
REMARK 900 RELATED ID: 1IVF   RELATED DB: PDB
REMARK 900  INFLUENZA A SUBTYPE N2 NEURAMINIDASE (
REMARK 900  SIALIDASE) COMPLEXED WITH DANA INHIBITOR (2-
REMARK 900  DEOXY-2,3-DIDEHYDRO-D-N-ACETYLNEURAMINIC
REMARK 900  ACID)
REMARK 900 RELATED ID: 1IVG   RELATED DB: PDB
REMARK 900  INFLUENZA A SUBTYPE N2 NEURAMINIDASE (
REMARK 900  SIALIDASE)
REMARK 900 RELATED ID: 1KIT   RELATED DB: PDB
REMARK 900  VIBRIO CHOLERAE NEURAMINIDASE
REMARK 900 RELATED ID: 1L7F   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE INCOMPLEX WITH BCX-1812
REMARK 900 RELATED ID: 1L7G   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF E119G MUTANT INFLUENZA
REMARK 900  VIRUSNEURAMINIDASE IN COMPLEX WITH BCX-1812
REMARK 900 RELATED ID: 1L7H   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF R292K MUTANT INFLUENZA
REMARK 900  VIRUSNEURAMINIDASE IN COMPLEX WITH BCX-1812
REMARK 900 RELATED ID: 1MWE   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF TERN
REMARK 900   N9 INFLUENZA VIRUS NEURAMINIDASE COMPLEXED
REMARK 900  WITH SIALIC ACID AT 4 DEGREES C REVEALING
REMARK 900   A SECOND SIALIC ACID BINDING SITE
REMARK 900 RELATED ID: 1NCA   RELATED DB: PDB
REMARK 900  N9 NEURAMINIDASE-NC41 COMPLEX WITH FAB
REMARK 900 RELATED ID: 1NCB   RELATED DB: PDB
REMARK 900  N9 NEURAMINIDASE-NC41 MUTANT WITH ASN 329
REMARK 900  REPLACED BY ASP (N329D) COMPLEX WITH FAB
REMARK 900 RELATED ID: 1NCC   RELATED DB: PDB
REMARK 900  N9 NEURAMINIDASE-NC41 MUTANT WITH ILE 368
REMARK 900  REPLACED BY ARG (I368R) COMPLEX WITH FAB
REMARK 900 RELATED ID: 1NCD   RELATED DB: PDB
REMARK 900  N9 NEURAMINIDASE-NC41 COMPLEX WITH FAB
REMARK 900 RELATED ID: 1NMA   RELATED DB: PDB
REMARK 900  MOL_ID: 1; MOLECULE: N9 NEURAMINIDASE; CHAIN
REMARK 900  : N; EC: 3.2.1.18; MUTATION: WILD TYPE
REMARK 900  ; MOL_ID: 2; MOLECULE: FAB NC10; CHAIN: L
REMARK 900  , H; OTHER_DETAILS: RESOLUTION OF 3.0
REMARK 900  ANGSTROMS
REMARK 900 RELATED ID: 1NMB   RELATED DB: PDB
REMARK 900  MOL_ID: 1; MOLECULE: N9 NEURAMINIDASE; CHAIN
REMARK 900  : N; EC: 3.2.1.18; MUTATION: WILD TYPE
REMARK 900  ; MOL_ID: 2; MOLECULE: FAB NC10; CHAIN: L
REMARK 900  , H; OTHER_DETAILS: RESOLUTION OF 2.5
REMARK 900  ANGSTROMS
REMARK 900 RELATED ID: 1NMC   RELATED DB: PDB
REMARK 900  COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A
REMARK 900  15 RESIDUE LINKER AND INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 1NN2   RELATED DB: PDB
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 1NNA   RELATED DB: PDB
REMARK 900  NEURAMINIDASE (SIALIDASE)
REMARK 900 RELATED ID: 1NNB   RELATED DB: PDB
REMARK 900  NEURAMINIDASE (SIALIDASE) COMPLEXED WITH 2-
REMARK 900  DEOXY-2,3-DEHYDRO-N-ACETYL NEURAMINIC ACID
REMARK 900 RELATED ID: 1NNC   RELATED DB: PDB
REMARK 900  INFLUENZA VIRUS NEURAMINIDASE SUBTYPE N9 (TERN
REMARK 900  ) COMPLEXED WITH 4-GUANIDINO-NEU5AC2EN
REMARK 900  INHIBITOR
REMARK 900 RELATED ID: 1NSB   RELATED DB: PDB
REMARK 900  NEURAMINIDASE (SIALIDASE)
REMARK 900 RELATED ID: 1NSC   RELATED DB: PDB
REMARK 900  NEURAMINIDASE (SIALIDASE) COMPLEX WITH N-
REMARK 900  ACETYL NEURAMINIC ACID (SIALIC ACID)
REMARK 900 RELATED ID: 1NSD   RELATED DB: PDB
REMARK 900  NEURAMINIDASE (SIALIDASE) COMPLEX WITH 2,3-
REMARK 900  DEHYDRO-2-DEOXY-N-ACETYL NEURAMINIC ACID (
REMARK 900  DANA)
REMARK 900 RELATED ID: 1USR   RELATED DB: PDB
REMARK 900  NEWCASTLE DISEASE VIRUS HEMAGGLUTININ-
REMARK 900  NEURAMINIDASE COMPLEXED WITH THIOSIALOSIDE
REMARK 900 RELATED ID: 1USX   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE NEWCASTLE DISEASE
REMARK 900  VIRUS HEMAGGLUTININ-NEURAMINIDASE COMPLEXED WITH
REMARK 900   THIOSIALOSIDE
REMARK 900 RELATED ID: 1V2I   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE
REMARK 900  FROM HUMANPARAINFLUENZA VIRUS TYPE III
REMARK 900 RELATED ID: 1V3B   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE
REMARK 900  FROM HUMANPARAINFLUENZA VIRUS TYPE III
REMARK 900 RELATED ID: 1V3C   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE
REMARK 900  FROM HUMANPARAINFLUENZA VIRUS TYPE III:
REMARK 900  COMPLEX WITH NEU5AC
REMARK 900 RELATED ID: 1V3D   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE
REMARK 900  FROM HUMANPARAINFLUENZA VIRUS TYPE III:
REMARK 900  COMPLEX WITH NEU5AC2EN
REMARK 900 RELATED ID: 1V3E   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE
REMARK 900  FROM HUMANPARAINFLUENZA VIRUS TYPE III:
REMARK 900  COMPLEX WITH ZANAMAVIR
REMARK 900 RELATED ID: 1VCJ   RELATED DB: PDB
REMARK 900  INFLUENZA B VIRUS NEURAMINIDASE COMPLEXED WITH
REMARK 900   1-(4-CARBOXY-2-(3-PENTYLAMINO)PHENYL)-5
REMARK 900  -AMINOMETHYL-5-HYDROXYMETHYL-PYRROLIDIN-2-ONE
REMARK 900 RELATED ID: 1W1X   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 277 K.
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.
REMARK 900 RELATED ID: 1W8N   RELATED DB: PDB
REMARK 900  CONTRIBUTION OF THE ACTIVE SITE ASPARTIC
REMARK 900  ACID TO CATALYSIS IN THE BACTERIAL
REMARK 900  NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS.
REMARK 900 RELATED ID: 1W8O   RELATED DB: PDB
REMARK 900  CONTRIBUTION OF THE ACTIVE SITE ASPARTIC
REMARK 900  ACID TO CATALYSIS IN THE BACTERIAL
REMARK 900  NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS
REMARK 900 RELATED ID: 1XOE   RELATED DB: PDB
REMARK 900  N9 TERN INFLUENZA NEURAMINIDASE COMPLEXED WITH
REMARK 900   (2R,4R,5R)-5-(1-ACETYLAMINO-3-METHYL-
REMARK 900  BUTYL-PYRROLIDINE-2, 4-DICAROBYXYLIC ACID 4
REMARK 900  -METHYL ESTERDASE COMPLEXED WITH
REMARK 900 RELATED ID: 1XOG   RELATED DB: PDB
REMARK 900  N9 TERN INFLUENZA NEURAMINIDASE COMPLEXED WITH
REMARK 900   A 2,5-DISUBSTITUTED TETRAHYDROFURAN-5-
REMARK 900  CARBOXYLIC ACID
REMARK 900 RELATED ID: 1Z4V   RELATED DB: PDB
REMARK 900  PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ-
REMARK 900  NEURAMINIDASE(HN) WITH LIGAND DANA (SOAKED
REMARK 900  WITH DANA, PH 7.0)
REMARK 900 RELATED ID: 1Z4W   RELATED DB: PDB
REMARK 900  PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ-
REMARK 900  NEURAMINIDASE(HN) WITH LIGAND DANA (SOAKED
REMARK 900  WITH DANA, PH8.0)
REMARK 900 RELATED ID: 1Z4X   RELATED DB: PDB
REMARK 900  PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ-
REMARK 900  NEURAMINIDASE(HN) WITH LIGAND SIALYLLACTOSE (
REMARK 900  SOAKED WITH SIALYLLACTOSE,PH8.0)
REMARK 900 RELATED ID: 1Z4Y   RELATED DB: PDB
REMARK 900  PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ-
REMARK 900  NEURAMINIDASE(HN) (PH 8.0)
REMARK 900 RELATED ID: 1Z4Z   RELATED DB: PDB
REMARK 900  PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ-
REMARK 900  NEURAMINIDASE(HN) WITH LIGAND DANA(SOAKED
REMARK 900  WITH SIALIC ACID, PH7.0))
REMARK 900 RELATED ID: 1Z50   RELATED DB: PDB
REMARK 900  PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ-
REMARK 900  NEURAMINIDASE(HN) WITH LIGAND DANA (SOAKED
REMARK 900  WITH SIALIC ACID, PH 8.0)
REMARK 900 RELATED ID: 2BAT   RELATED DB: PDB
REMARK 900  NEURAMINIDASE N2 COMPLEX WITH SIALIC ACID (N
REMARK 900  -ACTYL NEURAMINIC ACID)
REMARK 900 RELATED ID: 2QWA   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A DRUG RESISTANT
REMARK 900  VARIANT R292K OF TERN N9 INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 2QWB   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF
REMARK 900  SIALIC ACID AND A DRUG RESISTANT VARIANT
REMARK 900  R292K OF TERN N9 INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 2QWC   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF
REMARK 900  NEU5AC2EN AND A DRUG RESISTANT VARIANT R292K
REMARK 900   OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 2QWD   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 4-
REMARK 900  AMINO-NEU5AC2EN AND A DRUG RESISTANT VARIANT
REMARK 900   R292K OF TERN N9 INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 2QWE   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 4-
REMARK 900  GUANIDINO-NEU5AC2EN AND A DRUG RESISTANT
REMARK 900  VARIANT R292K OF TERN N9 INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 2QWF   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF N-
REMARK 900  ACETYL-4-GUANIDINO-6- METHYL(PROPYL)
REMARK 900  CARBOXAMIDE-4,5-DIHYDRO-2H-PYRAN-2-
REMARK 900  CARBOXYLIC ACID AND A DRUG RESISTANT VARIANT
REMARK 900   R292K OF TERN N9 INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 2QWG   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 5-
REMARK 900  N-ACETYL-4-AMINO-6- DIETHYLCARBOXAMIDE-4,5
REMARK 900  -DIHYDRO-2H-PYRAN-2-CARBOXYLIC ACID AND A
REMARK 900   DRUG RESISTANT VARIANT R292K OF TERN N9
REMARK 900  INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 2QWH   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 5-
REMARK 900  N-ACETYL-5-AMINO-3- (1-ETHYLPROPOXY)-1-
REMARK 900  CYCLOHEXENE-1-CARBOXYLIC ACID (GS4071) AND A
REMARK 900   DRUG RESISTANT VARIANT R292K OF TERN N9
REMARK 900  INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 2QWI   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF N-
REMARK 900  ACETYL-4-GUANIDINO-6- METHYL(PROPYL)
REMARK 900  CARBOXAMIDE-4,5-DIHYDRO-2H-PYRAN-2-
REMARK 900  CARBOXYLIC ACID AND WILDTYPE TERN N9
REMARK 900  INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 2QWJ   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 5-
REMARK 900  N-ACETYL-4-AMINO-6- DIETHYLCARBOXAMIDE-4,5
REMARK 900  -DIHYDRO-2H-PYRAN-2-CARBOXYLIC ACID AND A
REMARK 900   DRUG RESISTANT VARIANT R292K OF TERN N9
REMARK 900  INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 2QWK   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 5-
REMARK 900  N-ACETYL-5-AMINO-3- (1-ETHYLPROPOXY)-1-
REMARK 900  CYCLOHEXENE-1-CARBOXYLIC ACID (GS4071) AND
REMARK 900  WILDTYPE TERN N9 INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 2SIL   RELATED DB: PDB
REMARK 900  SIALIDASE (NEURAMINIDASE)
REMARK 900 RELATED ID: 2SIM   RELATED DB: PDB
REMARK 900  SIALIDASE (NEURAMINIDASE)
REMARK 900 RELATED ID: 3NN9   RELATED DB: PDB
REMARK 900  NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH ASN
REMARK 900   329 REPLACED BY ASP) (N329D)
REMARK 900 RELATED ID: 4NN9   RELATED DB: PDB
REMARK 900  NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH ILE
REMARK 900   368 REPLACED BY ARG) (I368R)
REMARK 900 RELATED ID: 5NN9   RELATED DB: PDB
REMARK 900  NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH ALA
REMARK 900   369 REPLACED BY ASP) (A369D)
REMARK 900 RELATED ID: 6NN9   RELATED DB: PDB
REMARK 900  NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH LYS
REMARK 900   432 REPLACED BY ASN) (K432N)
REMARK 900 RELATED ID: 7NN9   RELATED DB: PDB
REMARK 900  NATIVE INFLUENZA VIRUS NEURAMINIDASE SUBTYPE
REMARK 900  N9 (TERN)
DBREF  1V0Z A   88   476  UNP    Q6XV27   Q6XV27_9INFA    82    470
DBREF  1V0Z B   88   476  UNP    Q6XV27   Q6XV27_9INFA    82    470
DBREF  1V0Z C   88   476  UNP    Q6XV27   Q6XV27_9INFA    82    470
DBREF  1V0Z D   88   476  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    NAG  A1479      14
HET    NAG  A1480      14
HET    NAG  A1481      14
HET    NAG  A1482      14
HET    MAN  A1483      11
HET    BMA  A1486      11
HET    MAN  A1487      11
HET    NAG  A1495      14
HET    MAN  A1484      11
HET    MAN  A1485      11
HET    NAG  A1488      14
HET    NAG  A1489      14
HET    BMA  A1490      11
HET    MAN  A1491      11
HET    MAN  A1492      11
HET    MAN  A1493      11
HET    MAN  A1494      11
HET    NAG  B1479      14
HET    NAG  B1480      14
HET    NAG  B1481      14
HET    NAG  B1482      14
HET    MAN  B1483      11
HET    BMA  B1486      11
HET    NAG  B1487      14
HET    MAN  B1484      11
HET    MAN  B1485      11
HET    NAG  C1480      14
HET    NAG  C1481      14
HET    NAG  C1482      14
HET    NAG  C1483      14
HET    NAG  C1484      14
HET    MAN  C1485      11
HET    BMA  C1486      11
HET    MAN  C1487      11
HET    NAG  D1479      14
HET    NAG  D1480      14
HET    NAG  D1481      14
HET    MAN  D1483      11
HET     CA  A1477       1
HET     CA  B1477       1
HET     CA  C1477       1
HET     CA  D1477       1
HET    GOL  A1478       6
HET    GOL  B1478       6
HET    PEG  C1478       7
HET    GOL  C1479       6
HET    GOL  D1478       6
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM      CA CALCIUM ION
HETNAM     GOL GLYCEROL
HETNAM     PEG DI(HYDROXYETHYL)ETHER
HETSYN     NAG NAG
FORMUL   5  NAG    20(C8 H15 N O6)
FORMUL   8  MAN    14(C6 H12 O6)
FORMUL   8  BMA    4(C6 H12 O6)
FORMUL  30   CA    4(CA 2+)
FORMUL  34  GOL    4(C3 H8 O3)
FORMUL  36  PEG    C4 H10 O3
FORMUL  39  HOH   *1798(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 PRO A  204  ASN A  207  5                                   4
HELIX    4   4 GLU A  471  GLU A  476  5                                   6
HELIX    5   5 ASN B  110  GLU B  116  1                                   7
HELIX    6   6 GLY B  148  ASN B  152  5                                   5
HELIX    7   7 PRO B  204  ASN B  207  5                                   4
HELIX    8   8 GLU B  471  GLU B  476  5                                   6
HELIX    9   9 ASN C  110  GLU C  116  1                                   7
HELIX   10  10 GLY C  148  ASN C  152  5                                   5
HELIX   11  11 GLU C  471  GLU C  476  5                                   6
HELIX   12  12 ASN D  110  GLU D  116  1                                   7
HELIX   13  13 GLY D  148  ASN D  152  5                                   5
HELIX   14  14 GLU D  471  GLU D  476  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 LEU A 121  ASP A 131  0
SHEET    2  AB 4 GLY A 134  THR A 145 -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 CYS A 244  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 GLU A 283  ALA A 290  0
SHEET    2  AE 4 VAL A 293  ARG A 299 -1  O  VAL A 293   N  ALA A 290
SHEET    3  AE 4 PRO A 308  ASP A 313 -1  O  PRO A 308   N  CYS A 298
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 B 102  LYS B 108  0
SHEET    2  BA 4 THR B 447  SER B 457 -1  O  ALA B 453   N  LEU B 106
SHEET    3  BA 4 PRO B 428  GLY B 437 -1  O  PRO B 428   N  GLY B 456
SHEET    4  BA 4 SER B 413  ILE B 417 -1  O  GLY B 414   N  TYR B 431
SHEET    1  BB 4 LEU B 121  CYS B 130  0
SHEET    2  BB 4 CYS B 135  THR B 145 -1  O  ARG B 136   N  SER B 129
SHEET    3  BB 4 ALA B 163  GLU B 168 -1  O  ALA B 163   N  SER B 141
SHEET    4  BB 4 ARG B 179  ILE B 183 -1  O  ARG B 179   N  SER B 166
SHEET    1  BC 4 SER B 186  HIS B 191  0
SHEET    2  BC 4 ARG B 196  SER B 202 -1  O  MET B 197   N  CYS B 190
SHEET    3  BC 4 SER B 209  TYR B 214 -1  O  SER B 209   N  SER B 202
SHEET    4  BC 4 ARG B 217  PRO B 223 -1  O  ARG B 217   N  TYR B 214
SHEET    1  BD 3 CYS B 244  ASP B 250  0
SHEET    2  BD 3 ALA B 258  LYS B 265 -1  O  ALA B 258   N  ASP B 250
SHEET    3  BD 3 LYS B 268  GLU B 274 -1  O  LYS B 268   N  LYS B 265
SHEET    1  BE 4 GLU B 283  ALA B 290  0
SHEET    2  BE 4 VAL B 293  ARG B 299 -1  O  VAL B 293   N  ALA B 290
SHEET    3  BE 4 PRO B 308  ASP B 313 -1  O  PRO B 308   N  CYS B 298
SHEET    4  BE 4 THR B 318  TYR B 323 -1  O  THR B 318   N  ASP B 313
SHEET    1  BF 4 ALA B 360  PHE B 361  0
SHEET    2  BF 4 TRP B 368  ARG B 371 -1  O  TRP B 368   N  PHE B 361
SHEET    3  BF 4 SER B 379  LYS B 385 -1  O  GLU B 382   N  ARG B 371
SHEET    4  BF 4 SER B 399  TRP B 409 -1  O  SER B 399   N  LYS B 385
SHEET    1  CA 4 SER C 102  LYS C 108  0
SHEET    2  CA 4 THR C 447  SER C 457 -1  O  ALA C 453   N  LEU C 106
SHEET    3  CA 4 PRO C 428  GLY C 437 -1  O  PRO C 428   N  GLY C 456
SHEET    4  CA 4 SER C 413  ILE C 417 -1  O  GLY C 414   N  TYR C 431
SHEET    1  CB 4 LEU C 121  ASP C 131  0
SHEET    2  CB 4 GLY C 134  THR C 145 -1  O  GLY C 134   N  ASP C 131
SHEET    3  CB 4 ALA C 163  GLU C 168 -1  O  ALA C 163   N  SER C 141
SHEET    4  CB 4 ARG C 179  ILE C 183 -1  O  ARG C 179   N  SER C 166
SHEET    1  CC 4 SER C 186  HIS C 191  0
SHEET    2  CC 4 ARG C 196  SER C 202 -1  O  MET C 197   N  CYS C 190
SHEET    3  CC 4 SER C 209  TYR C 214 -1  O  SER C 209   N  SER C 202
SHEET    4  CC 4 ARG C 217  PRO C 223 -1  O  ARG C 217   N  TYR C 214
SHEET    1  CD 3 CYS C 244  ASP C 250  0
SHEET    2  CD 3 ALA C 258  LYS C 265 -1  O  ALA C 258   N  ASP C 250
SHEET    3  CD 3 LYS C 268  GLU C 274 -1  O  LYS C 268   N  LYS C 265
SHEET    1  CE 4 GLU C 283  ALA C 290  0
SHEET    2  CE 4 VAL C 293  ARG C 299 -1  O  VAL C 293   N  ALA C 290
SHEET    3  CE 4 PRO C 308  ASP C 313 -1  O  PRO C 308   N  CYS C 298
SHEET    4  CE 4 THR C 318  TYR C 323 -1  O  THR C 318   N  ASP C 313
SHEET    1  CF 4 ALA C 360  PHE C 361  0
SHEET    2  CF 4 TRP C 368  ARG C 371 -1  O  TRP C 368   N  PHE C 361
SHEET    3  CF 4 SER C 379  LYS C 385 -1  O  GLU C 382   N  ARG C 371
SHEET    4  CF 4 SER C 399  TRP C 409 -1  O  SER C 399   N  LYS C 385
SHEET    1  DA 4 SER D 102  LYS D 108  0
SHEET    2  DA 4 THR D 447  SER D 457 -1  O  ALA D 453   N  LEU D 106
SHEET    3  DA 4 PRO D 428  GLY D 437 -1  O  PRO D 428   N  GLY D 456
SHEET    4  DA 4 SER D 413  ILE D 417 -1  O  GLY D 414   N  TYR D 431
SHEET    1  DB 4 LEU D 121  ASP D 131  0
SHEET    2  DB 4 GLY D 134  THR D 145 -1  O  GLY D 134   N  ASP D 131
SHEET    3  DB 4 ALA D 163  GLU D 168 -1  O  ALA D 163   N  SER D 141
SHEET    4  DB 4 ARG D 179  ILE D 183 -1  O  ARG D 179   N  SER D 166
SHEET    1  DC 4 SER D 186  HIS D 191  0
SHEET    2  DC 4 ARG D 196  SER D 202 -1  O  MET D 197   N  CYS D 190
SHEET    3  DC 4 SER D 209  TYR D 214 -1  O  SER D 209   N  SER D 202
SHEET    4  DC 4 ARG D 217  PRO D 223 -1  O  ARG D 217   N  TYR D 214
SHEET    1  DD 3 CYS D 244  ASP D 250  0
SHEET    2  DD 3 ALA D 258  LYS D 265 -1  O  ALA D 258   N  ASP D 250
SHEET    3  DD 3 LYS D 268  GLU D 274 -1  O  LYS D 268   N  LYS D 265
SHEET    1  DE 4 GLU D 283  ALA D 290  0
SHEET    2  DE 4 VAL D 293  ARG D 299 -1  O  VAL D 293   N  ALA D 290
SHEET    3  DE 4 PRO D 308  ASP D 313 -1  O  PRO D 308   N  CYS D 298
SHEET    4  DE 4 THR D 318  TYR D 323 -1  O  THR D 318   N  ASP D 313
SHEET    1  DF 4 ALA D 360  PHE D 361  0
SHEET    2  DF 4 TRP D 368  ARG D 371 -1  O  TRP D 368   N  PHE D 361
SHEET    3  DF 4 SER D 379  LYS D 385 -1  O  GLU D 382   N  ARG D 371
SHEET    4  DF 4 SER D 399  TRP D 409 -1  O  SER D 399   N  LYS D 385
SSBOND   1 CYS A   98    CYS A  425                          1555   1555  2.06
SSBOND   2 CYS A  130    CYS A  135                          1555   1555  2.03
SSBOND   3 CYS A  182    CYS A  200                          1555   1555  2.04
SSBOND   4 CYS A  190    CYS A  237                          1555   1555  2.04
SSBOND   5 CYS A  239    CYS A  244                          1555   1555  2.05
SSBOND   6 CYS A  285    CYS A  298                          1555   1555  2.09
SSBOND   7 CYS A  287    CYS A  296                          1555   1555  2.07
SSBOND   8 CYS A  325    CYS A  343                          1555   1555  2.05
SSBOND   9 CYS A  429    CYS A  455                          1555   1555  2.05
SSBOND  10 CYS B   98    CYS B  425                          1555   1555  2.05
SSBOND  11 CYS B  130    CYS B  135                          1555   1555  2.03
SSBOND  12 CYS B  182    CYS B  200                          1555   1555  2.05
SSBOND  13 CYS B  190    CYS B  237                          1555   1555  2.04
SSBOND  14 CYS B  239    CYS B  244                          1555   1555  2.04
SSBOND  15 CYS B  285    CYS B  298                          1555   1555  2.08
SSBOND  16 CYS B  287    CYS B  296                          1555   1555  2.05
SSBOND  17 CYS B  325    CYS B  343                          1555   1555  2.04
SSBOND  18 CYS B  429    CYS B  455                          1555   1555  2.05
SSBOND  19 CYS C   98    CYS C  425                          1555   1555  2.06
SSBOND  20 CYS C  130    CYS C  135                          1555   1555  2.04
SSBOND  21 CYS C  182    CYS C  200                          1555   1555  2.07
SSBOND  22 CYS C  190    CYS C  237                          1555   1555  2.03
SSBOND  23 CYS C  239    CYS C  244                          1555   1555  2.03
SSBOND  24 CYS C  285    CYS C  298                          1555   1555  2.07
SSBOND  25 CYS C  287    CYS C  296                          1555   1555  2.06
SSBOND  26 CYS C  325    CYS C  343                          1555   1555  2.04
SSBOND  27 CYS C  429    CYS C  455                          1555   1555  2.04
SSBOND  28 CYS D   98    CYS D  425                          1555   1555  2.05
SSBOND  29 CYS D  130    CYS D  135                          1555   1555  2.04
SSBOND  30 CYS D  182    CYS D  200                          1555   1555  2.03
SSBOND  31 CYS D  190    CYS D  237                          1555   1555  2.04
SSBOND  32 CYS D  239    CYS D  244                          1555   1555  2.03
SSBOND  33 CYS D  285    CYS D  298                          1555   1555  2.09
SSBOND  34 CYS D  287    CYS D  296                          1555   1555  2.05
SSBOND  35 CYS D  325    CYS D  343                          1555   1555  2.04
SSBOND  36 CYS D  429    CYS D  455                          1555   1555  2.03
LINK         ND2 ASN A  92                 C1  NAG A1479     1555   1555  1.44
LINK         ND2 ASN A 152                 C1  NAG A1481     1555   1555  1.44
LINK         ND2 ASN A 207                 C1  NAG A1488     1555   1555  1.45
LINK        CA    CA A1477                 O   ASP A 300     1555   1555  2.35
LINK        CA    CA A1477                 O   GLY A 304     1555   1555  2.44
LINK        CA    CA A1477                 OD2 ASP A 331     1555   1555  2.39
LINK        CA    CA A1477                 O   PRO A 354     1555   1555  2.46
LINK        CA    CA A1477                 O   HOH A2271     1555   1555  2.34
LINK        CA    CA A1477                 O   HOH A2306     1555   1555  3.01
LINK         O4  NAG A1479                 C1  NAG A1480     1555   1555  1.44
LINK         C1  MAN A1483                 O6  BMA A1486     1555   1555  1.34
LINK         O3  MAN A1483                 C1  MAN A1485     1555   1555  1.92
LINK         O6  MAN A1483                 C1  MAN A1484     1555   1555  1.85
LINK         O3  BMA A1486                 C1  MAN A1487     1555   1555  1.34
LINK         C1  BMA A1486                 O4  NAG A1495     1555   1555  1.44
LINK         O4  NAG A1488                 C1  NAG A1489     1555   1555  1.44
LINK         O4  NAG A1489                 C1  BMA A1490     1555   1555  1.44
LINK         O3  BMA A1490                 C1  MAN A1491     1555   1555  1.34
LINK         O6  BMA A1490                 C1  MAN A1493     1555   1555  1.34
LINK         O2  MAN A1491                 C1  MAN A1492     1555   1555  1.33
LINK         O3  MAN A1493                 C1  MAN A1494     1555   1555  1.81
LINK         ND2 ASN B 152                 C1  NAG B1480     1555   1555  1.82
LINK        CA    CA B1477                 OD2 ASP B 331     1555   1555  2.45
LINK        CA    CA B1477                 O   HOH B2300     1555   1555  2.66
LINK        CA    CA B1477                 O   ASP B 300     1555   1555  2.33
LINK        CA    CA B1477                 O   HOH B2271     1555   1555  2.30
LINK        CA    CA B1477                 O   PRO B 354     1555   1555  2.50
LINK        CA    CA B1477                 O   GLY B 304     1555   1555  2.41
LINK         O4  NAG B1482                 C1  NAG A1495     1555   1555  1.94
LINK         O6  MAN B1483                 C1  MAN B1484     1555   1555  1.90
LINK         C1  MAN B1483                 O6  BMA B1486     1555   1555  1.33
LINK         C1  BMA B1486                 O4  NAG B1487     1555   1555  1.42
LINK         ND2 ASN C 152                 C1  NAG C1481     1555   1555  1.75
LINK         ND2 ASN C 207                 C1  NAG C1483     1555   1555  1.75
LINK        CA    CA C1477                 O   HOH C2283     1555   1555  2.37
LINK        CA    CA C1477                 O   PRO C 354     1555   1555  2.58
LINK        CA    CA C1477                 OD2 ASP C 331     1555   1555  2.45
LINK        CA    CA C1477                 O   ASP C 300     1555   1555  2.31
LINK        CA    CA C1477                 O   HOH C2311     1555   1555  3.01
LINK        CA    CA C1477                 O   GLY C 304     1555   1555  2.31
LINK         O4  NAG C1483                 C1  NAG C1484     1555   1555  1.42
LINK         C1  MAN C1485                 O6  MAN A1493     1555   1555  1.92
LINK         O6  BMA C1486                 C1  MAN C1487     1555   1555  1.34
LINK         ND2 ASN D 152                 C1  NAG D1480     1555   1555  1.85
LINK         ND2 ASN D 207                 C1  NAG D1481     1555   1555  1.89
LINK        CA    CA D1477                 O   ASP D 300     1555   1555  2.33
LINK        CA    CA D1477                 O   GLY D 304     1555   1555  2.36
LINK        CA    CA D1477                 O   PRO D 354     1555   1555  2.35
LINK        CA    CA D1477                 O   HOH D2309     1555   1555  2.39
LINK        CA    CA D1477                 O   HOH D2342     1555   1555  2.80
LINK        CA    CA D1477                 OD2 ASP D 331     1555   1555  2.49
CISPEP   1 THR A  332    SER A  333          0         6.50
CISPEP   2 SER A  351    PRO A  352          0         1.51
CISPEP   3 ARG A  438    PRO A  439          0        -1.15
CISPEP   4 THR B  332    SER B  333          0         3.42
CISPEP   5 SER B  351    PRO B  352          0        -0.54
CISPEP   6 ARG B  438    PRO B  439          0         1.95
CISPEP   7 THR C  332    SER C  333          0         4.50
CISPEP   8 SER C  351    PRO C  352          0         3.82
CISPEP   9 ARG C  438    PRO C  439          0         0.56
CISPEP  10 THR D  332    SER D  333          0         3.35
CISPEP  11 SER D  351    PRO D  352          0         4.21
CISPEP  12 ARG D  438    PRO D  439          0        -0.50
SITE     1 AC1  4 ASN A  92  LYS A 241  NAG A1480  HOH A2431
SITE     1 AC2  1 NAG A1479
SITE     1 AC3  6 ASN A 152  LEU A 445  NAG A1482  HOH A2432
SITE     2 AC3  6 HOH A2434  TYR C 474
SITE     1 AC4  1 NAG A1481
SITE     1 AC5  7 LEU A 384  PRO A 397  ASN A 400  MAN A1484
SITE     2 AC5  7 MAN A1485  BMA A1486  HOH A2330
SITE     1 AC6  8 ILE A 398  SER A 399  ASN A 400  MAN A1483
SITE     2 AC6  8 MAN A1487  NAG A1495  HOH A2439  HOH A2440
SITE     1 AC7  1 BMA A1486
SITE     1 AC8  6 SER A 102  SER A 399  ASN A 400  BMA A1486
SITE     2 AC8  6 HOH A2453  NAG B1482
SITE     1 AC9  5 ASP A 337  ARG A 371  MAN A1483  HOH A2278
SITE     2 AC9  5 HOH A2435
SITE     1 BC1  8 GLU A 382  LEU A 384  ASN A 400  VAL A 402
SITE     2 BC1  8 MAN A1483  HOH A2436  HOH A2437  HOH A2438
SITE     1 BC2  7 ASN A 207  NAG A1489  HOH A2148  HOH A2151
SITE     2 BC2  7 ARG C 460  LEU C 461  GLY C 462
SITE     1 BC3  8 NAG A1488  BMA A1490  MAN A1491  HOH A2441
SITE     2 BC3  8 ASN C 101  SER C 399  ASN C 400  HOH C2412
SITE     1 BC4  8 NAG A1489  MAN A1491  MAN A1493  HOH A2442
SITE     2 BC4  8 HOH A2443  ILE C 398  SER C 399  ASN C 400
SITE     1 BC5  6 NAG A1489  BMA A1490  MAN A1492  HOH A2444
SITE     2 BC5  6 HOH A2445  HOH A2446
SITE     1 BC6  3 MAN A1491  HOH A2447  HOH A2448
SITE     1 BC7  7 BMA A1490  MAN A1494  LEU C 384  PRO C 397
SITE     2 BC7  7 ASN C 400  MAN C1485  HOH C2324
SITE     1 BC8  9 MAN A1493  HOH A2449  HOH A2450  HOH A2451
SITE     2 BC8  9 HOH A2452  GLU C 382  LEU C 384  ASN C 400
SITE     3 BC8  9 VAL C 402
SITE     1 BC9  4 THR B  89  ASN B  92  HOH B2419  HOH B2420
SITE     1 CC1  6 TYR A 474  ASN B 152  LEU B 445  NAG B1481
SITE     2 CC1  6 HOH B2421  HOH B2422
SITE     1 CC2  1 NAG B1480
SITE     1 CC3  5 LEU A 461  NAG A1495  ASN B 206  ASN B 207
SITE     2 CC3  5 HOH B2425
SITE     1 CC4  6 PRO B 397  ASN B 400  MAN B1484  MAN B1485
SITE     2 CC4  6 BMA B1486  HOH B2426
SITE     1 CC5  5 ILE B 398  SER B 399  ASN B 400  MAN B1483
SITE     2 CC5  5 NAG B1487
SITE     1 CC6  7 ASN B 101  SER B 399  ASN B 400  BMA B1486
SITE     2 CC6  7 HOH B2334  HOH B2434  NAG D1481
SITE     1 CC7  6 ASP B 337  ARG B 371  MAN B1483  HOH B2427
SITE     2 CC7  6 HOH B2428  HOH B2429
SITE     1 CC8  6 GLU B 382  ASN B 400  VAL B 402  MAN B1483
SITE     2 CC8  6 HOH B2431  HOH B2432
SITE     1 CC9  3 THR C  89  PHE C  90  ASN C  92
SITE     1 DC1  8 ASN C 152  NAG C1482  HOH C2062  HOH C2442
SITE     2 DC1  8 HOH C2444  HOH C2445  TYR D 474  HOH D2447
SITE     1 DC2  3 NAG C1481  HOH C2446  ILE D 473
SITE     1 DC3  5 ASN C 207  NAG C1484  LEU D 461  GLY D 462
SITE     2 DC3  5 SER D 463
SITE     1 DC4  6 NAG C1483  BMA C1486  ASN D 101  SER D 399
SITE     2 DC4  6 ASN D 400  ARG D 460
SITE     1 DC5  6 MAN A1493  ASP C 337  ARG C 371  HOH C2448
SITE     2 DC5  6 HOH C2449  HOH C2450
SITE     1 DC6  5 NAG C1484  MAN C1487  ILE D 398  SER D 399
SITE     2 DC6  5 ASN D 400
SITE     1 DC7  5 BMA C1486  LEU D 384  ASN D 400  MAN D1483
SITE     2 DC7  5 HOH D2362
SITE     1 DC8  5 PHE D  90  ASN D  92  THR D  94  LYS D 241
SITE     2 DC8  5 HOH D2454
SITE     1 DC9  7 TYR B 474  ASN D 152  LEU D 445  HOH D2078
SITE     2 DC9  7 HOH D2455  HOH D2456  HOH D2457
SITE     1 EC1  7 LEU B 461  GLY B 462  SER B 463  NAG B1487
SITE     2 EC1  7 HOH B2335  ASN D 207  HOH D2458
SITE     1 EC2  6 MAN C1487  ILE D 373  HOH D2363  HOH D2379
SITE     2 EC2  6 HOH D2384  HOH D2460
SITE     1 EC3  6 ASP A 300  GLY A 304  ASP A 331  PRO A 354
SITE     2 EC3  6 HOH A2271  HOH A2306
SITE     1 EC4  6 ASP B 300  GLY B 304  ASP B 331  PRO B 354
SITE     2 EC4  6 HOH B2271  HOH B2300
SITE     1 EC5  6 ASP C 300  GLY C 304  ASP C 331  PRO C 354
SITE     2 EC5  6 HOH C2283  HOH C2311
SITE     1 EC6  6 ASP D 300  GLY D 304  ASP D 331  PRO D 354
SITE     2 EC6  6 HOH D2309  HOH D2342
SITE     1 EC7  7 GLN A 142  HIS A 150  ASN A 152  SER A 159
SITE     2 EC7  7 HOH A2063  HOH A2429  ARG C 113
SITE     1 EC8  5 ARG A 113  GLN B 142  HIS B 150  ASN B 152
SITE     2 EC8  5 SER B 159
SITE     1 EC9 12 PRO A 218  ILE A 219  GLU A 221  HIS C 104
SITE     2 EC9 12 LYS C 423  ASN C 427  CYS C 429  CYS C 455
SITE     3 EC9 12 GLY C 456  HOH C2382  HOH C2438  HOH C2439
SITE     1 FC1  7 GLN C 142  HIS C 150  ASN C 152  SER C 159
SITE     2 FC1  7 PHE C 161  HOH C2441  ARG D 113
SITE     1 FC2  6 ARG B 113  GLN D 142  HIS D 150  SER D 159
SITE     2 FC2  6 HOH D2061  HOH D2453
CRYST1  106.482   73.755  106.809  90.00  90.37  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      0.009391  0.000000  0.000060        0.00000
SCALE2      0.000000  0.013558  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009363        0.00000
      
PROCHECK
Go to PROCHECK summary
 References