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PDBsum entry 2cml

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Hydrolase PDB id
2cml
Jmol
Contents
Protein chains
389 a.a.
Ligands
ZMR ×8
NAG-NAG ×2
NAG ×13
MAN-MAN-MAN
BMA ×3
MAN ×10
NAG-NAG-BMA
Metals
_CA ×4
Waters ×386
HEADER    HYDROLASE                               10-MAY-06   2CML
TITLE     STRUCTURE OF NEURAMINIDASE FROM ENGLISH DUCK SUBTYPE N6
TITLE    2 COMPLEXED WITH 30 MM ZANAMIVIR, CRYSTAL SOAKED FOR 3 HOURS
TITLE    3 AT 291 K.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: RESIDUES 82-470;
COMPND   5 SYNONYM: NEURAMINIDASE SUBTYPE N6;
COMPND   6 EC: 3.2.1.18;
COMPND   7 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;
SOURCE   6 OTHER_DETAILS: COMPLEXED WITH ZANAMIVIR
KEYWDS    HB SITE, HYDROLASE, SUBTYPE N6, GLYCOSIDASE, INFLUENZA TYPE
KEYWDS   2 A, SIALIC ACID, NEURAMINIDASE, TRANSMEMBRANE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.RUDINO-PINERA,P.TUNNAH,P.LUKACIK,S.J.CRENNELL,R.G.WEBSTER,
AUTHOR   2 W.G.LAVER,E.F.GARMAN
REVDAT   2   24-FEB-09 2CML    1       VERSN
REVDAT   1   05-JUN-07 2CML    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.    2.15 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
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) : 2.15
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.70
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.3
REMARK   3   NUMBER OF REFLECTIONS             : 76617
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) : 0.183
REMARK   3   R VALUE            (WORKING SET) : 0.180
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4038
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) : 2.15
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4712
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380
REMARK   3   BIN FREE R VALUE SET COUNT          : 217
REMARK   3   BIN FREE R VALUE                    : 0.3130
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          : 641
REMARK   3   SOLVENT ATOMS            : 386
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 17.32
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.81
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.26000
REMARK   3    B22 (A**2) : 2.31000
REMARK   3    B33 (A**2) : -1.05000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.11000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.300
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.217
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.650
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13027 ; 0.021 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17720 ; 2.037 ; 1.988
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1552 ; 8.665 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   552 ;35.829 ;23.913
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2004 ;15.079 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;18.897 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1936 ; 0.136 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9884 ; 0.008 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6032 ; 0.248 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  8449 ; 0.311 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   686 ; 0.190 ; 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 ; 0.209 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.178 ; 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):  7976 ; 0.937 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12474 ; 1.432 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5856 ; 2.483 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5246 ; 3.606 ; 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 : 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 2CML COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAY-06.
REMARK 100 THE PDBE ID CODE IS EBI-28695.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-JUN-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) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200H
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : CONFOCAL OSMIC BLUE
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80679
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.2
REMARK 200  DATA REDUNDANCY                : 2.000
REMARK 200  R MERGE                    (I) : 0.09000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25
REMARK 200  COMPLETENESS FOR SHELL     (%) : 65.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.28000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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       36.84250
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   ND2  ASN A    92  -  O5   NAG A  1480              2.19
REMARK 500   ND2  ASN D  3092  -  C2   NAG D  4482              2.13
REMARK 500   ND2  ASN D  3207  -  C1   NAG D  4484              2.09
REMARK 500   NZ   LYS D  3295  -  OE2  GLU D  3390              2.08
REMARK 500   C1   MAN A  1485  -  O6   BMA A  1709              2.07
REMARK 500   C1   BMA A  1709  -  O4   NAG B  2483              2.14
REMARK 500   O3   BMA C  1709  -  C1   MAN C  3490              2.10
REMARK 500   O    HOH A  2055  -  O    HOH A  2057              2.06
REMARK 500   O    HOH A  2055  -  O    HOH A  2058              2.15
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    GLU A 424   CG    GLU A 424   CD      0.114
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 B1128   CA  -  CB  -  CG  ANGL. DEV. =  16.6 DEGREES
REMARK 500    ARG B1378   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG B1378   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    LEU C2128   CA  -  CB  -  CG  ANGL. DEV. =  18.1 DEGREES
REMARK 500    LEU D3128   CA  -  CB  -  CG  ANGL. DEV. =  18.7 DEGREES
REMARK 500    ARG D3378   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 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    ARG A 124      172.83    178.80
REMARK 500    PRO A 160        0.44    -69.20
REMARK 500    ASN A 207       26.50   -169.98
REMARK 500    LEU A 230      126.26    -38.05
REMARK 500    THR A 232     -156.50   -145.62
REMARK 500    LYS A 322     -157.85   -166.41
REMARK 500    SER A 333      106.04     43.55
REMARK 500    SER A 448     -159.02   -144.20
REMARK 500    LEU B1093       41.42    -77.29
REMARK 500    ASP B1117      -50.63   -127.98
REMARK 500    ASN B1207       35.22   -166.82
REMARK 500    THR B1232     -149.70   -143.69
REMARK 500    ARG B1256      131.63    -37.88
REMARK 500    LYS B1322     -156.59   -158.65
REMARK 500    VAL B1328       93.05    -69.49
REMARK 500    SER B1333       94.40     63.85
REMARK 500    TRP B1466       52.70   -115.31
REMARK 500    ASP C2117      -44.95   -131.61
REMARK 500    ASN C2207       50.50   -159.91
REMARK 500    THR C2232     -156.13   -138.22
REMARK 500    TRP C2302      -64.60    -94.03
REMARK 500    LYS C2322     -157.66   -159.67
REMARK 500    SER C2333      125.70      9.07
REMARK 500    ASN C2366       53.08    -92.41
REMARK 500    TRP C2466       53.27   -105.21
REMARK 500    ASN D3207       33.78   -167.57
REMARK 500    ILE D3219      -53.06   -124.01
REMARK 500    ILE D3229       65.09     65.71
REMARK 500    THR D3232     -154.38   -137.55
REMARK 500    LYS D3322     -152.85   -151.50
REMARK 500    SER D3333      112.10     34.00
REMARK 500    ASN D3366       50.00    -84.71
REMARK 500    TRP D3466       53.17   -107.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 THR A  332     SER A  333                 -115.83
REMARK 500 THR B 1332     SER B 1333                 -140.97
REMARK 500 THR C 2332     SER C 2333                  -88.25
REMARK 500 THR D 3332     SER D 3333                 -110.07
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    SER A 333        21.9      L          L   OUTSIDE RANGE
REMARK 500    ASP B1109        24.5      L          L   OUTSIDE RANGE
REMARK 500    SER C2333        19.6      L          L   OUTSIDE RANGE
REMARK 500    THR D3330        24.7      L          L   OUTSIDE RANGE
REMARK 500    SER D3333        22.7      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 1483
REMARK 610     NAG B 2481
REMARK 610     NAG B 2482
REMARK 610     NAG B 2483
REMARK 610     NAG C 3486
REMARK 610     NAG C 3488
REMARK 610     NAG D 4482
REMARK 610     NAG D 4484
REMARK 610     MAN A 1485
REMARK 610     MAN B 2484
REMARK 610     MAN B 2485
REMARK 610     MAN B 2486
REMARK 610     MAN C 3484
REMARK 610     MAN C 3490
REMARK 610     MAN C 3492
REMARK 610     MAN D 4480
REMARK 610     MAN D 4481
REMARK 610     BMA A 1709
REMARK 610     BMA C 3493
REMARK 610     BMA D 4486
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    87.1
REMARK 620 3 ASP A 331   OD2  88.0  87.3
REMARK 620 4 PRO A 354   O   100.4 168.5 101.6
REMARK 620 5 HOH A2075   O    98.5  95.8 172.9  74.6
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 GLY B1304   O
REMARK 620 2 HOH B2071   O    90.2
REMARK 620 3 ASP B1300   O    85.0  84.0
REMARK 620 4 PRO B1354   O   156.5  68.1 101.0
REMARK 620 5 ASP B1331   OD2  94.6 174.5  93.8 107.6
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    88.4
REMARK 620 3 PRO C2354   O   106.2  96.3
REMARK 620 4 GLY C2304   O    87.0  83.9 166.8
REMARK 620 5 HOH C4065   O   172.4  98.5  69.9  96.9
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 ASP D3300   O
REMARK 620 2 GLY D3304   O    88.0
REMARK 620 3 ASP D3331   OD2  88.3  86.1
REMARK 620 4 PRO D3354   O    98.8 163.9 108.6
REMARK 620 5 HOH D2061   O    96.3  91.6 174.7  73.2
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1485
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN 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 BMA A1709
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B2480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B2481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B2482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B2483
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B2484
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B2485
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B2486
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C1709
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C3483
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C3484
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C3485
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3486
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3487
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3488
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3489
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C3490
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C3492
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C3493
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3494
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D4480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D4481
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D4482
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D4483
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D4484
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D4485
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D4486
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C3479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA D4479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR A1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR A1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR B2477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR B2478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR C3477
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR C3478
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR D4477
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR D4478
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: 1W1X   RELATED DB: PDB
REMARK 900  STRUCTURE OF NEURAMINIDASE FROM ENGLISH DUCK
REMARK 900  SUBTYPE N6 COPMPLEXED 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 COPMPLEXED 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  2CML A   88   476  UNP    Q6XV27   Q6XV27_9INFA    82    470
DBREF  2CML B 1088  1476  UNP    Q6XV27   Q6XV27_9INFA    82    470
DBREF  2CML C 2088  2476  UNP    Q6XV27   Q6XV27_9INFA    82    470
DBREF  2CML 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    NAG  A1480      14
HET    NAG  A1481      14
HET    NAG  A1482      14
HET    NAG  A1483      14
HET    MAN  A1485      11
HET    MAN  A1486      11
HET    MAN  A1487      11
HET    BMA  A1709      11
HET    NAG  B2480      14
HET    NAG  B2481      14
HET    NAG  B2482      14
HET    NAG  B2483      14
HET    MAN  B2484      11
HET    MAN  B2485      11
HET    MAN  B2486      11
HET    BMA  C1709      11
HET    NAG  C3480      14
HET    NAG  C3481      14
HET    MAN  C3483      11
HET    MAN  C3484      11
HET    MAN  C3485      11
HET    NAG  C3486      14
HET    NAG  C3487      14
HET    NAG  C3488      14
HET    NAG  C3489      14
HET    MAN  C3490      11
HET    MAN  C3492      11
HET    BMA  C3493      11
HET    NAG  C3494      14
HET    MAN  D4480      11
HET    MAN  D4481      11
HET    NAG  D4482      14
HET    NAG  D4483      14
HET    NAG  D4484      14
HET    NAG  D4485      14
HET    BMA  D4486      11
HET     CA  A1479       1
HET     CA  B2479       1
HET     CA  C3479       1
HET     CA  D4479       1
HET    ZMR  A1477      23
HET    ZMR  A1478      23
HET    ZMR  B2477      23
HET    ZMR  B2478      23
HET    ZMR  C3477      23
HET    ZMR  C3478      23
HET    ZMR  D4477      23
HET    ZMR  D4478      23
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM      CA CALCIUM ION
HETNAM     ZMR ZANAMIVIR
HETSYN     ZMR MODIFIED SIALIC ACID
HETSYN     NAG NAG
FORMUL   5  NAG    19(C8 H15 N O6)
FORMUL   9  MAN    13(C6 H12 O6)
FORMUL  12  BMA    4(C6 H12 O6)
FORMUL  41   CA    4(CA 2+)
FORMUL  45  ZMR    8(C12 H20 N4 O7)
FORMUL  53  HOH   *386(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 PRO B 1204  ASN B 1207  5                                   4
HELIX    7   7 GLU B 1471  GLU B 1476  5                                   6
HELIX    8   8 ASN C 2110  GLU C 2116  1                                   7
HELIX    9   9 GLY C 2148  ASN C 2152  5                                   5
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 CYS A 429  GLY A 437 -1  O  PHE A 430   N  LEU A 454
SHEET    4  AA 4 SER A 413  PHE A 416 -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 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 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 LEU B1121  CYS B1130  0
SHEET    2  BB 4 CYS B1135  THR B1145 -1  O  ARG B1136   N  SER B1129
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  CYS C2130  0
SHEET    2  CB 4 CYS C2135  THR C2145 -1  O  ARG C2136   N  SER C2129
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 C2186  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 TYR D3127  ASP D3131  0
SHEET    2  DB 4 GLY D3134  SER D3141 -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 PRO D3218  PRO D3223 -1  N  ILE D3219   O  VAL D3212
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  2.05
SSBOND   2 CYS A  130    CYS A  135                          1555   1555  2.06
SSBOND   3 CYS A  182    CYS A  200                          1555   1555  2.04
SSBOND   4 CYS A  190    CYS A  237                          1555   1555  1.98
SSBOND   5 CYS A  239    CYS A  244                          1555   1555  2.02
SSBOND   6 CYS A  285    CYS A  298                          1555   1555  2.13
SSBOND   7 CYS A  287    CYS A  296                          1555   1555  2.08
SSBOND   8 CYS A  325    CYS A  343                          1555   1555  2.03
SSBOND   9 CYS A  429    CYS A  455                          1555   1555  2.03
SSBOND  10 CYS B 1098    CYS B 1425                          1555   1555  2.04
SSBOND  11 CYS B 1130    CYS B 1135                          1555   1555  2.05
SSBOND  12 CYS B 1182    CYS B 1200                          1555   1555  2.08
SSBOND  13 CYS B 1190    CYS B 1237                          1555   1555  2.04
SSBOND  14 CYS B 1239    CYS B 1244                          1555   1555  2.02
SSBOND  15 CYS B 1285    CYS B 1298                          1555   1555  2.07
SSBOND  16 CYS B 1287    CYS B 1296                          1555   1555  2.05
SSBOND  17 CYS B 1325    CYS B 1343                          1555   1555  2.09
SSBOND  18 CYS B 1429    CYS B 1455                          1555   1555  2.02
SSBOND  19 CYS C 2098    CYS C 2425                          1555   1555  2.04
SSBOND  20 CYS C 2130    CYS C 2135                          1555   1555  2.07
SSBOND  21 CYS C 2182    CYS C 2200                          1555   1555  2.02
SSBOND  22 CYS C 2190    CYS C 2237                          1555   1555  2.02
SSBOND  23 CYS C 2239    CYS C 2244                          1555   1555  2.03
SSBOND  24 CYS C 2285    CYS C 2298                          1555   1555  2.07
SSBOND  25 CYS C 2287    CYS C 2296                          1555   1555  2.05
SSBOND  26 CYS C 2325    CYS C 2343                          1555   1555  2.05
SSBOND  27 CYS C 2429    CYS C 2455                          1555   1555  2.04
SSBOND  28 CYS D 3098    CYS D 3425                          1555   1555  2.05
SSBOND  29 CYS D 3130    CYS D 3135                          1555   1555  2.03
SSBOND  30 CYS D 3182    CYS D 3200                          1555   1555  2.01
SSBOND  31 CYS D 3190    CYS D 3237                          1555   1555  2.03
SSBOND  32 CYS D 3239    CYS D 3244                          1555   1555  2.03
SSBOND  33 CYS D 3285    CYS D 3298                          1555   1555  2.09
SSBOND  34 CYS D 3287    CYS D 3296                          1555   1555  2.06
SSBOND  35 CYS D 3325    CYS D 3343                          1555   1555  2.02
SSBOND  36 CYS D 3429    CYS D 3455                          1555   1555  2.02
LINK         ND2 ASN A  92                 C1  NAG A1480     1555   1555  1.85
LINK         ND2 ASN A 152                 C1  NAG A1482     1555   1555  1.81
LINK        CA    CA A1479                 O   ASP A 300     1555   1555  2.37
LINK        CA    CA A1479                 O   GLY A 304     1555   1555  2.43
LINK        CA    CA A1479                 OD2 ASP A 331     1555   1555  2.50
LINK        CA    CA A1479                 O   PRO A 354     1555   1555  2.38
LINK        CA    CA A1479                 O   HOH A2075     1555   1555  2.89
LINK         O4  NAG A1480                 C1  NAG A1481     1555   1555  1.95
LINK         O3  MAN A1485                 C1  MAN A1487     1555   1555  1.90
LINK         O6  MAN A1485                 C1  MAN A1486     1555   1555  1.91
LINK         ND2 ASN B1152                 C1  NAG B2480     1555   1555  1.72
LINK        CA    CA B2479                 OD2 ASP B1331     1555   1555  2.30
LINK        CA    CA B2479                 O   PRO B1354     1555   1555  2.39
LINK        CA    CA B2479                 O   ASP B1300     1555   1555  2.44
LINK        CA    CA B2479                 O   HOH B2071     1555   1555  2.66
LINK        CA    CA B2479                 O   GLY B1304     1555   1555  2.46
LINK         C1  BMA C1709                 O4  NAG C3481     1555   1555  1.63
LINK         O6  BMA C1709                 C1  MAN C3483     1555   1555  1.66
LINK         ND2 ASN C2152                 C1  NAG C3487     1555   1555  1.97
LINK         ND2 ASN C2207                 C1  NAG C3489     1555   1555  1.78
LINK        CA    CA C3479                 O   ASP C2300     1555   1555  2.47
LINK        CA    CA C3479                 O   PRO C2354     1555   1555  2.34
LINK        CA    CA C3479                 O   GLY C2304     1555   1555  2.55
LINK        CA    CA C3479                 OD2 ASP C2331     1555   1555  2.60
LINK        CA    CA C3479                 O   HOH C4065     1555   1555  2.78
LINK         O4  NAG C3480                 C1  NAG C3481     1555   1555  1.83
LINK         C1  NAG C3480                 ND2 ASN A 207     1555   1555  1.80
LINK         O3  MAN C3483                 C1  MAN C3485     1555   1555  2.00
LINK         O4  NAG C3489                 C1  NAG C3494     1555   1555  1.94
LINK         ND2 ASN D3152                 C1  NAG D4483     1555   1555  1.87
LINK        CA    CA D4479                 O   PRO D3354     1555   1555  2.33
LINK        CA    CA D4479                 O   HOH D2061     1555   1555  2.65
LINK        CA    CA D4479                 O   GLY D3304     1555   1555  2.52
LINK        CA    CA D4479                 O   ASP D3300     1555   1555  2.36
LINK        CA    CA D4479                 OD2 ASP D3331     1555   1555  2.55
LINK         O4  NAG D4484                 C1  NAG D4485     1555   1555  2.04
LINK         O4  NAG D4485                 O5  BMA D4486     1555   1555  2.01
CISPEP   1 SER A  351    PRO A  352          0         1.92
CISPEP   2 ARG A  438    PRO A  439          0        -1.01
CISPEP   3 SER B 1351    PRO B 1352          0        -1.17
CISPEP   4 ARG B 1438    PRO B 1439          0        -3.92
CISPEP   5 SER C 2351    PRO C 2352          0         2.79
CISPEP   6 ARG C 2438    PRO C 2439          0        -0.24
CISPEP   7 SER D 3351    PRO D 3352          0         7.27
CISPEP   8 ARG D 3438    PRO D 3439          0        -4.41
SITE     1 AC1  3 ASN A  92  LYS A 241  NAG A1481
SITE     1 AC2  1 NAG A1480
SITE     1 AC3  4 ASN A 152  LEU A 445  NAG A1483  TYR C2474
SITE     1 AC4  1 NAG A1482
SITE     1 AC5  7 LEU A 384  PRO A 397  ASN A 400  MAN A1486
SITE     2 AC5  7 MAN A1487  BMA A1709  HOH A2104
SITE     1 AC6  4 ASP A 337  ARG A 371  PRO A 397  MAN A1485
SITE     1 AC7  4 GLU A 382  ASN A 400  VAL A 402  MAN A1485
SITE     1 AC8  5 ILE A 398  SER A 399  ASN A 400  MAN A1485
SITE     2 AC8  5 NAG B2483
SITE     1 AC9  5 TYR A 474  ASN B1152  LEU B1445  HOH B2109
SITE     2 AC9  5 NAG B2481
SITE     1 BC1  1 NAG B2480
SITE     1 BC2  5 ARG A 460  LEU A 461  GLY A 462  ASN B1207
SITE     2 BC2  5 NAG B2483
SITE     1 BC3  4 SER A 399  ASN A 400  BMA A1709  NAG B2482
SITE     1 BC4  6 GLU B1382  PRO B1397  ASN B1400  MAN B2485
SITE     2 BC4  6 MAN B2486  BMA D4486
SITE     1 BC5  3 ASP B1337  ARG B1371  MAN B2484
SITE     1 BC6  4 GLU B1382  ASN B1400  VAL B1402  MAN B2484
SITE     1 BC7  7 PRO C2397  ILE C2398  SER C2399  ASN C2400
SITE     2 BC7  7 NAG C3481  MAN C3483  MAN C3490
SITE     1 BC8  6 ASN A 206  ASN A 207  ARG C2460  LEU C2461
SITE     2 BC8  6 GLY C2462  NAG C3481
SITE     1 BC9  6 BMA C1709  ASN C2101  SER C2399  ASN C2400
SITE     2 BC9  6 NAG C3480  MAN C3490
SITE     1 CC1  5 BMA C1709  PRO C2397  MAN C3484  MAN C3485
SITE     2 CC1  5 HOH C4067
SITE     1 CC2  3 ASP C2337  ARG C2371  MAN C3483
SITE     1 CC3  4 GLU C2382  ASN C2400  VAL C2402  MAN C3483
SITE     1 CC4  4 THR C2089  PHE C2090  ASN C2092  LYS C2241
SITE     1 CC5  4 ASN C2152  LEU C2445  NAG C3488  TYR D3474
SITE     1 CC6  1 NAG C3487
SITE     1 CC7  5 ASN C2207  NAG C3494  LEU D3461  GLY D3462
SITE     2 CC7  5 SER D3463
SITE     1 CC8  5 BMA C1709  NAG C3481  MAN C3492  HOH C4095
SITE     2 CC8  5 HOH C4096
SITE     1 CC9  1 MAN C3490
SITE     1 DC1  5 NAG C3494  PRO D3397  ILE D3398  ASN D3400
SITE     2 DC1  5 MAN D4480
SITE     1 DC2  4 NAG C3489  BMA C3493  SER D3399  ASN D3400
SITE     1 DC3  6 BMA C3493  GLU D3382  LEU D3384  PRO D3397
SITE     2 DC3  6 ASN D3400  MAN D4481
SITE     1 DC4  3 ILE D3373  GLU D3382  MAN D4480
SITE     1 DC5  2 ASN D3092  THR D3094
SITE     1 DC6  4 TYR B1474  HOH D2077  HOH D2078  ASN D3152
SITE     1 DC7  5 LEU B1461  GLY B1462  SER B1463  ASN D3207
SITE     2 DC7  5 NAG D4485
SITE     1 DC8  6 ASN B1101  SER B1399  ASN B1400  ARG B1460
SITE     2 DC8  6 NAG D4484  BMA D4486
SITE     1 DC9  5 ILE B1398  SER B1399  ASN B1400  MAN B2484
SITE     2 DC9  5 NAG D4485
SITE     1 EC1  5 ASP A 300  GLY A 304  ASP A 331  PRO A 354
SITE     2 EC1  5 HOH A2075
SITE     1 EC2  5 ASP B1300  GLY B1304  ASP B1331  PRO B1354
SITE     2 EC2  5 HOH B2071
SITE     1 EC3  5 ASP C2300  GLY C2304  ASP C2331  PRO C2354
SITE     2 EC3  5 HOH C4065
SITE     1 EC4  5 HOH D2061  ASP D3300  GLY D3304  ASP D3331
SITE     2 EC4  5 PRO D3354
SITE     1 EC5 16 ARG A 124  GLU A 125  ASP A 157  ARG A 158
SITE     2 EC5 16 ARG A 162  TRP A 185  ARG A 231  GLU A 234
SITE     3 EC5 16 ALA A 253  GLU A 283  GLU A 284  ARG A 299
SITE     4 EC5 16 ARG A 378  TYR A 412  HOH A2043  HOH A2102
SITE     1 EC6  7 SER A 374  SER A 377  SER A 379  ASN A 406
SITE     2 EC6  7 GLN A 407  ASN A 408  TRP A 409
SITE     1 EC7 17 ARG B1124  GLU B1125  ASP B1157  ARG B1158
SITE     2 EC7 17 ARG B1162  TRP B1185  ILE B1229  GLU B1234
SITE     3 EC7 17 ALA B1253  GLU B1283  GLU B1284  ARG B1299
SITE     4 EC7 17 ARG B1378  TYR B1412  HOH B2056  HOH B2107
SITE     5 EC7 17 HOH B2108
SITE     1 EC8  7 SER B1374  SER B1377  SER B1379  ASN B1406
SITE     2 EC8  7 GLN B1407  ASN B1408  TRP B1409
SITE     1 EC9 18 ARG C2124  GLU C2125  ASP C2157  ARG C2158
SITE     2 EC9 18 ARG C2162  TRP C2185  ILE C2229  ARG C2231
SITE     3 EC9 18 GLU C2234  ALA C2253  GLU C2283  GLU C2284
SITE     4 EC9 18 ARG C2299  ARG C2378  TYR C2412  HOH C4051
SITE     5 EC9 18 HOH C4091  HOH C4092
SITE     1 FC1  8 SER C2374  ASP C2376  SER C2377  SER C2379
SITE     2 FC1  8 ASN C2406  GLN C2407  ASN C2408  TRP C2409
SITE     1 FC2 14 ARG D3124  GLU D3125  ASP D3157  ARG D3158
SITE     2 FC2 14 ARG D3162  TRP D3185  ILE D3229  GLU D3234
SITE     3 FC2 14 ALA D3253  GLU D3283  GLU D3284  ARG D3299
SITE     4 FC2 14 ARG D3378  TYR D3412
SITE     1 FC3  8 SER D3374  ASP D3376  SER D3377  SER D3379
SITE     2 FC3  8 ASN D3406  GLN D3407  ASN D3408  TRP D3409
CRYST1  106.241   73.685  106.684  90.00  90.29  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      0.009413  0.000000  0.000048        0.00000
SCALE2      0.000000  0.013571  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009374        0.00000
      
PROCHECK
Go to PROCHECK summary
 References