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PDBsum entry 2bq9

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2bq9
Jmol
Contents
Protein chains
601 a.a.
Ligands
GAL ×3
GOL ×3
Metals
_NA ×3
Waters ×1494
HEADER    HYDROLASE                               27-APR-05   2BQ9
OBSLTE     19-AUG-05 2BQ9      2BZD
TITLE     GALACTOSE RECOGNITION BY THE CARBOHYDRATE-BINDING MODULE OF
TITLE    2 A BACTERIAL SIALIDASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BACTERIAL SIALIDASE;
COMPND   3 CHAIN: A, B, C;
COMPND   4 FRAGMENT: RESIDUES 47-647;
COMPND   5 SYNONYM: NEURAMINIDASE;
COMPND   6 EC: 3.2.1.18;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MICROMONOSPORA VIRIDIFACIENS;
SOURCE   3 ATCC: 31146;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS    SIALIDASE,CARBOHYDRATE BINDING MODULE, GLYCOSIDASE,
KEYWDS   2 HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.L.NEWSTEAD,G.L.TAYLOR
REVDAT   2   19-AUG-05 2BQ9    1       OBSLTE
REVDAT   1   29-APR-05 2BQ9    0
JRNL        AUTH   S.L.NEWSTEAD,J.N.WATSON,A.BENNETT,G.L.TAYLOR
JRNL        TITL   GALACTOSE RECOGNITION BY THE CARBOHYDRATE-BINDING
JRNL        TITL 2 MODULE OF A BACTERIAL SIALIDASE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. 2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 122.17
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9
REMARK   3   NUMBER OF REFLECTIONS             : 115262
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) : 0.186
REMARK   3   R VALUE            (WORKING SET) : 0.182
REMARK   3   FREE R VALUE                     : 0.258
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 6102
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH           : NULL
REMARK   3   BIN RESOLUTION RANGE LOW            : NULL
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   ALL ATOMS                : 15215
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.33
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.07000
REMARK   3    B22 (A**2) : 0.07000
REMARK   3    B33 (A**2) : -0.10000
REMARK   3    B12 (A**2) : 0.03000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.198
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.192
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.745
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
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 : 0
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 0
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : NULL
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : NULL
REMARK   3   ION PROBE RADIUS   : NULL
REMARK   3   SHRINKAGE RADIUS   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2BQ9 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 28-APR-2005.
REMARK 100 THE EBI ID CODE IS EBI-23818.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-2004
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               : ESRF
REMARK 200  BEAMLINE                       : ID14-EH2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)
REMARK 200  OPTICS                         : TOROIDAL MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM-4R)
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 121364
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 2.100
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3
REMARK 200  DATA REDUNDANCY                : 5.500
REMARK 200  R MERGE                    (I) : 0.15000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.44000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1W8O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16 % PEG 3350, 0.2 M DI-AMMONIUM
REMARK 280  HYDROGEN CITRATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,2/3+Z
REMARK 290       3555   -X+Y,-X,1/3+Z
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,1/3-Z
REMARK 290       6555   -X,-X+Y,2/3-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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      105.92000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       52.96000
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       52.96000
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      105.92000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 APPLY THE FOLLOWING TO CHAINS: A, X, Y, Z
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350 BIOMOLECULE: 3
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH X  36   LIES ON A SPECIAL POSITION.
REMARK 375      HOH X  95   LIES ON A SPECIAL POSITION.
REMARK 375      HOH Y 400   LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLU 260 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLU 260 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, GLU 260 TO ALA
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY C    47
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
REMARK 500   OE1  GLN B   441     NH1  ARG B   487              2.19
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLN A 451   CD    GLN A 451   NE2    0.119
REMARK 500    ILE B 189   CG1   ILE B 189   CD1    0.148
REMARK 500    VAL C 174   CB    VAL C 174   CG2    0.180
REMARK 500    ILE C 433   CG1   ILE C 433   CD1    0.142
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASN A  59   N   -  CA  -  C   ANGL. DEV. = 12.6 DEGREES
REMARK 500    PRO B  94   C   -  N   -  CA  ANGL. DEV. = 11.4 DEGREES
REMARK 500    LEU B 589   CA  -  CB  -  CG  ANGL. DEV. =-20.7 DEGREES
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FOR METAL ATOM NA    NA A1648  THE COORDINATION ANGLES ARE:
REMARK 600  1 ASN    528A  O
REMARK 600  2 ASN    533A  O        162.9
REMARK 600  3 THR    536A  O        110.3  77.6
REMARK 600  4 THR    536A  OG1       89.1  80.4  65.8
REMARK 600  5 ALA    639A  O         91.2 105.3  80.2 143.6
REMARK 600                             1     2     3     4
REMARK 600
REMARK 600 FOR METAL ATOM NA    NA B1648  THE COORDINATION ANGLES ARE:
REMARK 600  1 THR    536B  O
REMARK 600  2 ASN    528B  O        108.1
REMARK 600  3 ASP    531B  OD1      139.7  74.5
REMARK 600  4 ALA    639B  O         78.5  89.3 141.4
REMARK 600  5 GLU B  640B  OE1      144.6  84.7  75.0  68.6
REMARK 600  6 ASN    533B  O         85.6 162.3  87.9 104.6  90.4
REMARK 600  7 THR    536B  OG1       70.6  90.1  69.2 147.2 143.9  83.9
REMARK 600                             1     2     3     4     5     6
REMARK 600
REMARK 600 FOR METAL ATOM NA    NA C1648  THE COORDINATION ANGLES ARE:
REMARK 600  1 THR    536C  OG1
REMARK 600  2 THR    536C  O         74.8
REMARK 600  3 ASN    528C  O         98.0 119.4
REMARK 600  4 ASP    531C  OD1       77.9 152.7  64.5
REMARK 600  5 ASN    533C  O        101.8  97.4 141.7  88.0
REMARK 600  6 ALA    639C  O        155.7  83.1  83.8 123.7  91.0
REMARK 600                             1     2     3     4     5
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EUR   RELATED DB: PDB
REMARK 900  SIALIDASE
REMARK 900 RELATED ID: 1EUS   RELATED DB: PDB
REMARK 900  SIALIDASE COMPLEXED WITH 2-DEOXY-2,3-
REMARK 900  DEHYDRO-N- ACETYLNEURAMINIC ACID
REMARK 900 RELATED ID: 1EUT   RELATED DB: PDB
REMARK 900  SIALIDASE, LARGE 68KD FORM, COMPLEXED WITH
REMARK 900  GALACTOSE
REMARK 900 RELATED ID: 1EUU   RELATED DB: PDB
REMARK 900  SIALIDASE OR NEURAMINIDASE, LARGE 68KD FORM
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: 1WCQ   RELATED DB: PDB
REMARK 900  MUTAGENESIS OF THE NUCLEOPHILIC TYROSINE IN
REMARK 900  A BACTERIAL SIALIDASE TO PHENYLALANINE.
REMARK 900 RELATED ID: 2BER   RELATED DB: PDB
REMARK 900  Y370G ACTIVE SITE MUTANT OF THE SIALIDASE
REMARK 900  FROM MICROMONOSPORA VIRIDIFACIENS IN COMPLEX
REMARK 900  WITH BETA-NEU5AC (SIALIC ACID).
DBREF  2BQ9 A   47   647  UNP    Q02834   NANH_MICVI      47    647
DBREF  2BQ9 B   47   647  UNP    Q02834   NANH_MICVI      47    647
DBREF  2BQ9 C   47   647  UNP    Q02834   NANH_MICVI      47    647
SEQADV 2BQ9 ALA A  260  UNP  Q02834    GLU   260 ENGINEERED MUTATION
SEQADV 2BQ9 ALA B  260  UNP  Q02834    GLU   260 ENGINEERED MUTATION
SEQADV 2BQ9 ALA C  260  UNP  Q02834    GLU   260 ENGINEERED MUTATION
SEQRES   1 A  601  GLY GLU PRO LEU TYR THR GLU GLN ASP LEU ALA VAL ASN
SEQRES   2 A  601  GLY ARG GLU GLY PHE PRO ASN TYR ARG ILE PRO ALA LEU
SEQRES   3 A  601  THR VAL THR PRO ASP GLY ASP LEU LEU ALA SER TYR ASP
SEQRES   4 A  601  GLY ARG PRO THR GLY ILE ASP ALA PRO GLY PRO ASN SER
SEQRES   5 A  601  ILE LEU GLN ARG ARG SER THR ASP GLY GLY ARG THR TRP
SEQRES   6 A  601  GLY GLU GLN GLN VAL VAL SER ALA GLY GLN THR THR ALA
SEQRES   7 A  601  PRO ILE LYS GLY PHE SER ASP PRO SER TYR LEU VAL ASP
SEQRES   8 A  601  ARG GLU THR GLY THR ILE PHE ASN PHE HIS VAL TYR SER
SEQRES   9 A  601  GLN ARG GLN GLY PHE ALA GLY SER ARG PRO GLY THR ASP
SEQRES  10 A  601  PRO ALA ASP PRO ASN VAL LEU HIS ALA ASN VAL ALA THR
SEQRES  11 A  601  SER THR ASP GLY GLY LEU THR TRP SER HIS ARG THR ILE
SEQRES  12 A  601  THR ALA ASP ILE THR PRO ASP PRO GLY TRP ARG SER ARG
SEQRES  13 A  601  PHE ALA ALA SER GLY GLU GLY ILE GLN LEU ARG TYR GLY
SEQRES  14 A  601  PRO HIS ALA GLY ARG LEU ILE GLN GLN TYR THR ILE ILE
SEQRES  15 A  601  ASN ALA ALA GLY ALA PHE GLN ALA VAL SER VAL TYR SER
SEQRES  16 A  601  ASP ASP HIS GLY ARG THR TRP ARG ALA GLY GLU ALA VAL
SEQRES  17 A  601  GLY VAL GLY MET ASP ALA ASN LYS THR VAL GLU LEU SER
SEQRES  18 A  601  ASP GLY ARG VAL LEU LEU ASN SER ARG ASP SER ALA ARG
SEQRES  19 A  601  SER GLY TYR ARG LYS VAL ALA VAL SER THR ASP GLY GLY
SEQRES  20 A  601  HIS SER TYR GLY PRO VAL THR ILE ASP ARG ASP LEU PRO
SEQRES  21 A  601  ASP PRO THR ASN ASN ALA SER ILE ILE ARG ALA PHE PRO
SEQRES  22 A  601  ASP ALA PRO ALA GLY SER ALA ARG ALA LYS VAL LEU LEU
SEQRES  23 A  601  PHE SER ASN ALA ALA SER GLN THR SER ARG SER GLN GLY
SEQRES  24 A  601  THR ILE ARG MET SER CYS ASP ASP GLY GLN THR TRP PRO
SEQRES  25 A  601  VAL SER LYS VAL PHE GLN PRO GLY SER MET SER TYR SER
SEQRES  26 A  601  THR LEU THR ALA LEU PRO ASP GLY THR TYR GLY LEU LEU
SEQRES  27 A  601  TYR GLU PRO GLY THR GLY ILE ARG TYR ALA ASN PHE ASN
SEQRES  28 A  601  LEU ALA TRP LEU GLY GLY ILE CYS ALA PRO PHE THR ILE
SEQRES  29 A  601  PRO ASP VAL ALA LEU GLU PRO GLY GLN GLN VAL THR VAL
SEQRES  30 A  601  PRO VAL ALA VAL THR ASN GLN SER GLY ILE ALA VAL PRO
SEQRES  31 A  601  LYS PRO SER LEU GLN LEU ASP ALA SER PRO ASP TRP GLN
SEQRES  32 A  601  VAL GLN GLY SER VAL GLU PRO LEU MET PRO GLY ARG GLN
SEQRES  33 A  601  ALA LYS GLY GLN VAL THR ILE THR VAL PRO ALA GLY THR
SEQRES  34 A  601  THR PRO GLY ARG TYR ARG VAL GLY ALA THR LEU ARG THR
SEQRES  35 A  601  SER ALA GLY ASN ALA SER THR THR PHE THR VAL THR VAL
SEQRES  36 A  601  GLY LEU LEU ASP GLN ALA ARG MET SER ILE ALA ASP VAL
SEQRES  37 A  601  ASP SER GLU GLU THR ALA ARG GLU ASP GLY ARG ALA SER
SEQRES  38 A  601  ASN VAL ILE ASP GLY ASN PRO SER THR PHE TRP HIS THR
SEQRES  39 A  601  GLU TRP SER ARG ALA ASP ALA PRO GLY TYR PRO HIS ARG
SEQRES  40 A  601  ILE SER LEU ASP LEU GLY GLY THR HIS THR ILE SER GLY
SEQRES  41 A  601  LEU GLN TYR THR ARG ARG GLN ASN SER ALA ASN GLU GLN
SEQRES  42 A  601  VAL ALA ASP TYR GLU ILE TYR THR SER LEU ASN GLY THR
SEQRES  43 A  601  THR TRP ASP GLY PRO VAL ALA SER GLY ARG PHE THR THR
SEQRES  44 A  601  SER LEU ALA PRO GLN ARG ALA VAL PHE PRO ALA ARG ASP
SEQRES  45 A  601  ALA ARG TYR ILE ARG LEU VAL ALA LEU SER GLU GLN THR
SEQRES  46 A  601  GLY HIS LYS TYR ALA ALA VAL ALA GLU LEU GLU VAL GLU
SEQRES  47 A  601  GLY GLN ARG
SEQRES   1 B  601  GLY GLU PRO LEU TYR THR GLU GLN ASP LEU ALA VAL ASN
SEQRES   2 B  601  GLY ARG GLU GLY PHE PRO ASN TYR ARG ILE PRO ALA LEU
SEQRES   3 B  601  THR VAL THR PRO ASP GLY ASP LEU LEU ALA SER TYR ASP
SEQRES   4 B  601  GLY ARG PRO THR GLY ILE ASP ALA PRO GLY PRO ASN SER
SEQRES   5 B  601  ILE LEU GLN ARG ARG SER THR ASP GLY GLY ARG THR TRP
SEQRES   6 B  601  GLY GLU GLN GLN VAL VAL SER ALA GLY GLN THR THR ALA
SEQRES   7 B  601  PRO ILE LYS GLY PHE SER ASP PRO SER TYR LEU VAL ASP
SEQRES   8 B  601  ARG GLU THR GLY THR ILE PHE ASN PHE HIS VAL TYR SER
SEQRES   9 B  601  GLN ARG GLN GLY PHE ALA GLY SER ARG PRO GLY THR ASP
SEQRES  10 B  601  PRO ALA ASP PRO ASN VAL LEU HIS ALA ASN VAL ALA THR
SEQRES  11 B  601  SER THR ASP GLY GLY LEU THR TRP SER HIS ARG THR ILE
SEQRES  12 B  601  THR ALA ASP ILE THR PRO ASP PRO GLY TRP ARG SER ARG
SEQRES  13 B  601  PHE ALA ALA SER GLY GLU GLY ILE GLN LEU ARG TYR GLY
SEQRES  14 B  601  PRO HIS ALA GLY ARG LEU ILE GLN GLN TYR THR ILE ILE
SEQRES  15 B  601  ASN ALA ALA GLY ALA PHE GLN ALA VAL SER VAL TYR SER
SEQRES  16 B  601  ASP ASP HIS GLY ARG THR TRP ARG ALA GLY GLU ALA VAL
SEQRES  17 B  601  GLY VAL GLY MET ASP ALA ASN LYS THR VAL GLU LEU SER
SEQRES  18 B  601  ASP GLY ARG VAL LEU LEU ASN SER ARG ASP SER ALA ARG
SEQRES  19 B  601  SER GLY TYR ARG LYS VAL ALA VAL SER THR ASP GLY GLY
SEQRES  20 B  601  HIS SER TYR GLY PRO VAL THR ILE ASP ARG ASP LEU PRO
SEQRES  21 B  601  ASP PRO THR ASN ASN ALA SER ILE ILE ARG ALA PHE PRO
SEQRES  22 B  601  ASP ALA PRO ALA GLY SER ALA ARG ALA LYS VAL LEU LEU
SEQRES  23 B  601  PHE SER ASN ALA ALA SER GLN THR SER ARG SER GLN GLY
SEQRES  24 B  601  THR ILE ARG MET SER CYS ASP ASP GLY GLN THR TRP PRO
SEQRES  25 B  601  VAL SER LYS VAL PHE GLN PRO GLY SER MET SER TYR SER
SEQRES  26 B  601  THR LEU THR ALA LEU PRO ASP GLY THR TYR GLY LEU LEU
SEQRES  27 B  601  TYR GLU PRO GLY THR GLY ILE ARG TYR ALA ASN PHE ASN
SEQRES  28 B  601  LEU ALA TRP LEU GLY GLY ILE CYS ALA PRO PHE THR ILE
SEQRES  29 B  601  PRO ASP VAL ALA LEU GLU PRO GLY GLN GLN VAL THR VAL
SEQRES  30 B  601  PRO VAL ALA VAL THR ASN GLN SER GLY ILE ALA VAL PRO
SEQRES  31 B  601  LYS PRO SER LEU GLN LEU ASP ALA SER PRO ASP TRP GLN
SEQRES  32 B  601  VAL GLN GLY SER VAL GLU PRO LEU MET PRO GLY ARG GLN
SEQRES  33 B  601  ALA LYS GLY GLN VAL THR ILE THR VAL PRO ALA GLY THR
SEQRES  34 B  601  THR PRO GLY ARG TYR ARG VAL GLY ALA THR LEU ARG THR
SEQRES  35 B  601  SER ALA GLY ASN ALA SER THR THR PHE THR VAL THR VAL
SEQRES  36 B  601  GLY LEU LEU ASP GLN ALA ARG MET SER ILE ALA ASP VAL
SEQRES  37 B  601  ASP SER GLU GLU THR ALA ARG GLU ASP GLY ARG ALA SER
SEQRES  38 B  601  ASN VAL ILE ASP GLY ASN PRO SER THR PHE TRP HIS THR
SEQRES  39 B  601  GLU TRP SER ARG ALA ASP ALA PRO GLY TYR PRO HIS ARG
SEQRES  40 B  601  ILE SER LEU ASP LEU GLY GLY THR HIS THR ILE SER GLY
SEQRES  41 B  601  LEU GLN TYR THR ARG ARG GLN ASN SER ALA ASN GLU GLN
SEQRES  42 B  601  VAL ALA ASP TYR GLU ILE TYR THR SER LEU ASN GLY THR
SEQRES  43 B  601  THR TRP ASP GLY PRO VAL ALA SER GLY ARG PHE THR THR
SEQRES  44 B  601  SER LEU ALA PRO GLN ARG ALA VAL PHE PRO ALA ARG ASP
SEQRES  45 B  601  ALA ARG TYR ILE ARG LEU VAL ALA LEU SER GLU GLN THR
SEQRES  46 B  601  GLY HIS LYS TYR ALA ALA VAL ALA GLU LEU GLU VAL GLU
SEQRES  47 B  601  GLY GLN ARG
SEQRES   1 C  601  GLY GLU PRO LEU TYR THR GLU GLN ASP LEU ALA VAL ASN
SEQRES   2 C  601  GLY ARG GLU GLY PHE PRO ASN TYR ARG ILE PRO ALA LEU
SEQRES   3 C  601  THR VAL THR PRO ASP GLY ASP LEU LEU ALA SER TYR ASP
SEQRES   4 C  601  GLY ARG PRO THR GLY ILE ASP ALA PRO GLY PRO ASN SER
SEQRES   5 C  601  ILE LEU GLN ARG ARG SER THR ASP GLY GLY ARG THR TRP
SEQRES   6 C  601  GLY GLU GLN GLN VAL VAL SER ALA GLY GLN THR THR ALA
SEQRES   7 C  601  PRO ILE LYS GLY PHE SER ASP PRO SER TYR LEU VAL ASP
SEQRES   8 C  601  ARG GLU THR GLY THR ILE PHE ASN PHE HIS VAL TYR SER
SEQRES   9 C  601  GLN ARG GLN GLY PHE ALA GLY SER ARG PRO GLY THR ASP
SEQRES  10 C  601  PRO ALA ASP PRO ASN VAL LEU HIS ALA ASN VAL ALA THR
SEQRES  11 C  601  SER THR ASP GLY GLY LEU THR TRP SER HIS ARG THR ILE
SEQRES  12 C  601  THR ALA ASP ILE THR PRO ASP PRO GLY TRP ARG SER ARG
SEQRES  13 C  601  PHE ALA ALA SER GLY GLU GLY ILE GLN LEU ARG TYR GLY
SEQRES  14 C  601  PRO HIS ALA GLY ARG LEU ILE GLN GLN TYR THR ILE ILE
SEQRES  15 C  601  ASN ALA ALA GLY ALA PHE GLN ALA VAL SER VAL TYR SER
SEQRES  16 C  601  ASP ASP HIS GLY ARG THR TRP ARG ALA GLY GLU ALA VAL
SEQRES  17 C  601  GLY VAL GLY MET ASP ALA ASN LYS THR VAL GLU LEU SER
SEQRES  18 C  601  ASP GLY ARG VAL LEU LEU ASN SER ARG ASP SER ALA ARG
SEQRES  19 C  601  SER GLY TYR ARG LYS VAL ALA VAL SER THR ASP GLY GLY
SEQRES  20 C  601  HIS SER TYR GLY PRO VAL THR ILE ASP ARG ASP LEU PRO
SEQRES  21 C  601  ASP PRO THR ASN ASN ALA SER ILE ILE ARG ALA PHE PRO
SEQRES  22 C  601  ASP ALA PRO ALA GLY SER ALA ARG ALA LYS VAL LEU LEU
SEQRES  23 C  601  PHE SER ASN ALA ALA SER GLN THR SER ARG SER GLN GLY
SEQRES  24 C  601  THR ILE ARG MET SER CYS ASP ASP GLY GLN THR TRP PRO
SEQRES  25 C  601  VAL SER LYS VAL PHE GLN PRO GLY SER MET SER TYR SER
SEQRES  26 C  601  THR LEU THR ALA LEU PRO ASP GLY THR TYR GLY LEU LEU
SEQRES  27 C  601  TYR GLU PRO GLY THR GLY ILE ARG TYR ALA ASN PHE ASN
SEQRES  28 C  601  LEU ALA TRP LEU GLY GLY ILE CYS ALA PRO PHE THR ILE
SEQRES  29 C  601  PRO ASP VAL ALA LEU GLU PRO GLY GLN GLN VAL THR VAL
SEQRES  30 C  601  PRO VAL ALA VAL THR ASN GLN SER GLY ILE ALA VAL PRO
SEQRES  31 C  601  LYS PRO SER LEU GLN LEU ASP ALA SER PRO ASP TRP GLN
SEQRES  32 C  601  VAL GLN GLY SER VAL GLU PRO LEU MET PRO GLY ARG GLN
SEQRES  33 C  601  ALA LYS GLY GLN VAL THR ILE THR VAL PRO ALA GLY THR
SEQRES  34 C  601  THR PRO GLY ARG TYR ARG VAL GLY ALA THR LEU ARG THR
SEQRES  35 C  601  SER ALA GLY ASN ALA SER THR THR PHE THR VAL THR VAL
SEQRES  36 C  601  GLY LEU LEU ASP GLN ALA ARG MET SER ILE ALA ASP VAL
SEQRES  37 C  601  ASP SER GLU GLU THR ALA ARG GLU ASP GLY ARG ALA SER
SEQRES  38 C  601  ASN VAL ILE ASP GLY ASN PRO SER THR PHE TRP HIS THR
SEQRES  39 C  601  GLU TRP SER ARG ALA ASP ALA PRO GLY TYR PRO HIS ARG
SEQRES  40 C  601  ILE SER LEU ASP LEU GLY GLY THR HIS THR ILE SER GLY
SEQRES  41 C  601  LEU GLN TYR THR ARG ARG GLN ASN SER ALA ASN GLU GLN
SEQRES  42 C  601  VAL ALA ASP TYR GLU ILE TYR THR SER LEU ASN GLY THR
SEQRES  43 C  601  THR TRP ASP GLY PRO VAL ALA SER GLY ARG PHE THR THR
SEQRES  44 C  601  SER LEU ALA PRO GLN ARG ALA VAL PHE PRO ALA ARG ASP
SEQRES  45 C  601  ALA ARG TYR ILE ARG LEU VAL ALA LEU SER GLU GLN THR
SEQRES  46 C  601  GLY HIS LYS TYR ALA ALA VAL ALA GLU LEU GLU VAL GLU
SEQRES  47 C  601  GLY GLN ARG
HET    GAL  A1649      12
HET    GAL  B1649      12
HET    GAL  C1649      12
HET     NA  A1648       1
HET     NA  B1648       1
HET     NA  C1648       1
HET    GOL  A1650       6
HET    GOL  B1650       6
HET    GOL  C1650       6
HETNAM     GAL BETA-D-GALACTOSE
HETNAM      NA SODIUM ION
HETNAM     GOL GLYCEROL
FORMUL   4  GAL    3(C6 H12 O6)
FORMUL   7   NA    3(NA 1+)
FORMUL  10  GOL    3(C3 H8 O3)
FORMUL  13  HOH   *1494(H2 O1)
HELIX    1   1 THR A  190  ILE A  193  5                                   4
HELIX    2   2 ALA A  326  LYS A  329  5                                   4
HELIX    3   3 ASN A  397  GLY A  402  1                                   6
HELIX    4   4 ASP A  505  MET A  509  5                                   5
HELIX    5   5 ARG A  525  ASP A  531  5                                   7
HELIX    6   6 THR B  190  ILE B  193  5                                   4
HELIX    7   7 ALA B  326  LYS B  329  5                                   4
HELIX    8   8 ASN B  397  GLY B  402  1                                   6
HELIX    9   9 ASP B  505  MET B  509  5                                   5
HELIX   10  10 ARG B  525  ASP B  531  5                                   7
HELIX   11  11 THR C  190  THR C  194  5                                   5
HELIX   12  12 ALA C  326  LYS C  329  5                                   4
HELIX   13  13 ASN C  397  GLY C  402  1                                   6
HELIX   14  14 ASP C  505  MET C  509  5                                   5
HELIX   15  15 ARG C  525  ASP C  531  5                                   7
SHEET    1  AA 4 TYR A  51  VAL A  58  0
SHEET    2  AA 4 GLY A 390  PHE A 396 -1  O  ILE A 391   N  LEU A  56
SHEET    3  AA 4 TYR A 381  TYR A 385 -1  O  TYR A 381   N  PHE A 396
SHEET    4  AA 4 SER A 371  ALA A 375 -1  O  THR A 372   N  LEU A 384
SHEET    1  AB 4 ASN A  66  VAL A  74  0
SHEET    2  AB 4 LEU A  80  ARG A  87 -1  O  LEU A  81   N  THR A  73
SHEET    3  AB 4 SER A  98  SER A 104 -1  O  SER A  98   N  GLY A  86
SHEET    4  AB 4 GLN A 115  SER A 118 -1  O  GLN A 115   N  GLN A 101
SHEET    1  AC 5 SER A 185  THR A 188  0
SHEET    2  AC 5 HIS A 171  SER A 177 -1  O  VAL A 174   N  ARG A 187
SHEET    3  AC 5 ILE A 143  SER A 150 -1  O  ILE A 143   N  SER A 177
SHEET    4  AC 5 GLY A 128  VAL A 136 -1  O  GLY A 128   N  SER A 150
SHEET    5  AC 5 GLY A 207  GLU A 208  1  O  GLY A 207   N  TYR A 134
SHEET    1  AD 3 SER A 201  ALA A 204  0
SHEET    2  AD 3 LEU A 221  ILE A 228 -1  O  THR A 226   N  PHE A 203
SHEET    3  AD 3 ILE A 210  GLN A 211 -1  O  ILE A 210   N  ILE A 222
SHEET    1  AE 4 SER A 201  ALA A 204  0
SHEET    2  AE 4 LEU A 221  ILE A 228 -1  O  THR A 226   N  PHE A 203
SHEET    3  AE 4 PHE A 234  SER A 241 -1  O  GLN A 235   N  ILE A 227
SHEET    4  AE 4 ARG A 249  ALA A 250 -1  O  ARG A 249   N  TYR A 240
SHEET    1  AF 4 ASN A 261  GLU A 265  0
SHEET    2  AF 4 VAL A 271  SER A 275 -1  O  LEU A 272   N  VAL A 264
SHEET    3  AF 4 TYR A 283  SER A 289 -1  O  LYS A 285   N  SER A 275
SHEET    4  AF 4 THR A 300  PRO A 306 -1  O  THR A 300   N  VAL A 286
SHEET    1  AG 4 SER A 313  ARG A 316  0
SHEET    2  AG 4 LEU A 331  ALA A 336 -1  O  LEU A 332   N  ILE A 315
SHEET    3  AG 4 SER A 343  SER A 350 -1  O  THR A 346   N  ASN A 335
SHEET    4  AG 4 VAL A 359  SER A 367 -1  O  VAL A 359   N  MET A 349
SHEET    1  AH 4 PHE A 408  THR A 409  0
SHEET    2  AH 4 GLN A 420  VAL A 427 -1  O  ALA A 426   N  THR A 409
SHEET    3  AH 4 ALA A 463  THR A 470 -1  O  ALA A 463   N  VAL A 427
SHEET    4  AH 4 GLN A 449  VAL A 454 -1  O  GLN A 449   N  THR A 470
SHEET    1  AI 4 VAL A 413  LEU A 415  0
SHEET    2  AI 4 ASN A 492  VAL A 501  1  O  THR A 498   N  VAL A 413
SHEET    3  AI 4 GLY A 478  ARG A 487 -1  O  GLY A 478   N  VAL A 501
SHEET    4  AI 4 SER A 439  ASP A 443 -1  O  SER A 439   N  ARG A 487
SHEET    1  AJ 5 SER A 510  VAL A 514  0
SHEET    2  AJ 5 HIS A 552  ARG A 571 -1  O  SER A 555   N  ALA A 512
SHEET    3  AJ 5 GLN A 610  ALA A 626 -1  O  GLN A 610   N  TYR A 569
SHEET    4  AJ 5 ASP A 582  SER A 588 -1  O  GLU A 584   N  VAL A 625
SHEET    5  AJ 5 ASP A 595  ARG A 602 -1  O  ASP A 595   N  THR A 587
SHEET    1  AK 4 SER A 510  VAL A 514  0
SHEET    2  AK 4 HIS A 552  ARG A 571 -1  O  SER A 555   N  ALA A 512
SHEET    3  AK 4 ALA A 637  GLY A 645 -1  N  ALA A 639   O  THR A 570
SHEET    4  AK 4 TRP A 538  HIS A 539 -1  O  TRP A 538   N  VAL A 638
SHEET    1  BA 4 TYR B  51  VAL B  58  0
SHEET    2  BA 4 GLY B 390  PHE B 396 -1  O  ILE B 391   N  LEU B  56
SHEET    3  BA 4 TYR B 381  TYR B 385 -1  O  TYR B 381   N  PHE B 396
SHEET    4  BA 4 SER B 371  ALA B 375 -1  O  THR B 372   N  LEU B 384
SHEET    1  BB 4 ASN B  66  VAL B  74  0
SHEET    2  BB 4 LEU B  80  ARG B  87 -1  O  LEU B  81   N  THR B  73
SHEET    3  BB 4 SER B  98  SER B 104 -1  O  SER B  98   N  GLY B  86
SHEET    4  BB 4 GLN B 115  SER B 118 -1  O  GLN B 115   N  GLN B 101
SHEET    1  BC 5 SER B 185  THR B 188  0
SHEET    2  BC 5 HIS B 171  SER B 177 -1  O  VAL B 174   N  ARG B 187
SHEET    3  BC 5 ILE B 143  SER B 150 -1  O  ILE B 143   N  SER B 177
SHEET    4  BC 5 GLY B 128  VAL B 136 -1  O  GLY B 128   N  SER B 150
SHEET    5  BC 5 GLY B 207  GLU B 208  1  O  GLY B 207   N  TYR B 134
SHEET    1  BD 3 SER B 201  ALA B 204  0
SHEET    2  BD 3 LEU B 221  ILE B 228 -1  O  THR B 226   N  PHE B 203
SHEET    3  BD 3 ILE B 210  GLN B 211 -1  O  ILE B 210   N  ILE B 222
SHEET    1  BE 4 SER B 201  ALA B 204  0
SHEET    2  BE 4 LEU B 221  ILE B 228 -1  O  THR B 226   N  PHE B 203
SHEET    3  BE 4 PHE B 234  SER B 241 -1  O  GLN B 235   N  ILE B 227
SHEET    4  BE 4 ARG B 249  ALA B 250 -1  O  ARG B 249   N  TYR B 240
SHEET    1  BF 4 ASN B 261  GLU B 265  0
SHEET    2  BF 4 VAL B 271  SER B 275 -1  O  LEU B 272   N  VAL B 264
SHEET    3  BF 4 TYR B 283  SER B 289 -1  O  LYS B 285   N  SER B 275
SHEET    4  BF 4 THR B 300  PRO B 306 -1  O  THR B 300   N  VAL B 286
SHEET    1  BG 4 SER B 313  ARG B 316  0
SHEET    2  BG 4 LEU B 331  ALA B 336 -1  O  LEU B 332   N  ILE B 315
SHEET    3  BG 4 SER B 343  SER B 350 -1  O  THR B 346   N  ASN B 335
SHEET    4  BG 4 VAL B 359  SER B 367 -1  O  VAL B 359   N  MET B 349
SHEET    1  BH 4 PHE B 408  THR B 409  0
SHEET    2  BH 4 GLN B 420  THR B 428 -1  O  ALA B 426   N  THR B 409
SHEET    3  BH 4 GLN B 462  THR B 470 -1  O  ALA B 463   N  VAL B 427
SHEET    4  BH 4 GLN B 449  VAL B 454 -1  O  GLN B 449   N  THR B 470
SHEET    1  BI 4 VAL B 413  LEU B 415  0
SHEET    2  BI 4 ALA B 493  VAL B 501  1  O  THR B 498   N  VAL B 413
SHEET    3  BI 4 GLY B 478  ARG B 487 -1  O  GLY B 478   N  VAL B 501
SHEET    4  BI 4 SER B 439  ASP B 443 -1  O  SER B 439   N  ARG B 487
SHEET    1  BJ 9 SER B 510  VAL B 514  0
SHEET    2  BJ 9 HIS B 552  ARG B 571 -1  O  SER B 555   N  ALA B 512
SHEET    3  BJ 9 TRP B 538  HIS B 539  0
SHEET    4  BJ 9 ALA B 637  GLY B 645 -1  O  VAL B 638   N  TRP B 538
SHEET    5  BJ 9 HIS B 552  ARG B 571 -1  N  SER B 565   O  GLU B 644
SHEET    6  BJ 9 ASP B 595  ARG B 602  0
SHEET    7  BJ 9 ASP B 582  SER B 588 -1  O  TYR B 583   N  GLY B 601
SHEET    8  BJ 9 GLN B 610  ALA B 626 -1  N  ARG B 620   O  SER B 588
SHEET    9  BJ 9 HIS B 552  ARG B 571 -1  O  HIS B 552   N  ALA B 626
SHEET    1  CA 4 TYR C  51  VAL C  58  0
SHEET    2  CA 4 GLY C 390  PHE C 396 -1  O  ILE C 391   N  LEU C  56
SHEET    3  CA 4 TYR C 381  TYR C 385 -1  O  TYR C 381   N  PHE C 396
SHEET    4  CA 4 SER C 371  ALA C 375 -1  O  THR C 372   N  LEU C 384
SHEET    1  CB 4 TYR C  67  VAL C  74  0
SHEET    2  CB 4 LEU C  80  GLY C  86 -1  O  LEU C  81   N  THR C  73
SHEET    3  CB 4 SER C  98  SER C 104 -1  O  SER C  98   N  GLY C  86
SHEET    4  CB 4 GLN C 115  SER C 118 -1  O  GLN C 115   N  GLN C 101
SHEET    1  CC 5 SER C 185  THR C 188  0
SHEET    2  CC 5 HIS C 171  SER C 177 -1  O  VAL C 174   N  ARG C 187
SHEET    3  CC 5 ILE C 143  SER C 150 -1  O  ILE C 143   N  SER C 177
SHEET    4  CC 5 GLY C 128  VAL C 136 -1  O  GLY C 128   N  SER C 150
SHEET    5  CC 5 GLY C 207  GLU C 208  1  O  GLY C 207   N  TYR C 134
SHEET    1  CD 7 SER C 201  ALA C 204  0
SHEET    2  CD 7 LEU C 221  ILE C 228 -1  O  THR C 226   N  PHE C 203
SHEET    3  CD 7 ILE C 210  GLN C 211 -1  O  ILE C 210   N  ILE C 222
SHEET    4  CD 7 LEU C 221  ILE C 228 -1  O  ILE C 222   N  ILE C 210
SHEET    5  CD 7 ARG C 249  ALA C 250  0
SHEET    6  CD 7 PHE C 234  SER C 241 -1  O  TYR C 240   N  ARG C 249
SHEET    7  CD 7 LEU C 221  ILE C 228 -1  O  LEU C 221   N  SER C 241
SHEET    1  CE 4 ASN C 261  GLU C 265  0
SHEET    2  CE 4 VAL C 271  SER C 275 -1  O  LEU C 272   N  VAL C 264
SHEET    3  CE 4 TYR C 283  SER C 289 -1  O  LYS C 285   N  SER C 275
SHEET    4  CE 4 THR C 300  PRO C 306 -1  O  THR C 300   N  VAL C 286
SHEET    1  CF 4 SER C 313  ARG C 316  0
SHEET    2  CF 4 LEU C 331  ALA C 336 -1  O  LEU C 332   N  ILE C 315
SHEET    3  CF 4 SER C 343  SER C 350 -1  O  THR C 346   N  ASN C 335
SHEET    4  CF 4 VAL C 359  SER C 367 -1  O  VAL C 359   N  MET C 349
SHEET    1  CG 4 PHE C 408  THR C 409  0
SHEET    2  CG 4 GLN C 420  THR C 428 -1  O  ALA C 426   N  THR C 409
SHEET    3  CG 4 GLN C 462  THR C 470 -1  O  ALA C 463   N  VAL C 427
SHEET    4  CG 4 GLN C 449  VAL C 454 -1  O  GLN C 449   N  THR C 470
SHEET    1  CH 4 VAL C 413  LEU C 415  0
SHEET    2  CH 4 GLY C 491  VAL C 501  1  O  THR C 498   N  VAL C 413
SHEET    3  CH 4 GLY C 478  THR C 488 -1  O  GLY C 478   N  VAL C 501
SHEET    4  CH 4 SER C 439  ASP C 443 -1  O  SER C 439   N  ARG C 487
SHEET    1  CI 9 SER C 510  VAL C 514  0
SHEET    2  CI 9 HIS C 552  ARG C 571 -1  O  SER C 555   N  ALA C 512
SHEET    3  CI 9 TRP C 538  HIS C 539  0
SHEET    4  CI 9 ALA C 637  GLY C 645 -1  O  VAL C 638   N  TRP C 538
SHEET    5  CI 9 HIS C 552  ARG C 571 -1  N  SER C 565   O  GLU C 644
SHEET    6  CI 9 ASP C 595  ARG C 602  0
SHEET    7  CI 9 ASP C 582  SER C 588 -1  O  TYR C 583   N  GLY C 601
SHEET    8  CI 9 GLN C 610  ALA C 626 -1  N  ARG C 620   O  SER C 588
SHEET    9  CI 9 HIS C 552  ARG C 571 -1  O  HIS C 552   N  ALA C 626
SSBOND   1 CYS A  351    CYS A  405
SSBOND   2 CYS B  351    CYS B  405
SSBOND   3 CYS C  351    CYS C  405
LINK        NA    NA A1648                 O   ASN A 528
LINK        NA    NA A1648                 O   ASN A 533
LINK        NA    NA A1648                 O   THR A 536
LINK        NA    NA A1648                 OG1 THR A 536
LINK        NA    NA A1648                 O   ALA A 639
LINK        NA    NA B1648                 O   THR B 536
LINK        NA    NA B1648                 O   ASN B 528
LINK        NA    NA B1648                 OD1 ASP B 531
LINK        NA    NA B1648                 O   ALA B 639
LINK        NA    NA B1648                 OE1BGLU B 640
LINK        NA    NA B1648                 O   ASN B 533
LINK        NA    NA B1648                 OG1 THR B 536
LINK        NA    NA C1648                 O   THR C 536
LINK        NA    NA C1648                 O   ASN C 528
LINK        NA    NA C1648                 OD1 ASP C 531
LINK        NA    NA C1648                 O   ASN C 533
LINK        NA    NA C1648                 O   ALA C 639
LINK        NA    NA C1648                 OG1 THR C 536
CISPEP   1 ALA A   93    PRO A   94          0         2.17
CISPEP   2 ALA A  124    PRO A  125          0        -7.99
CISPEP   3 TYR A  550    PRO A  551          0        -0.11
CISPEP   4 GLY A  596    PRO A  597          0         0.69
CISPEP   5 ALA B   93    PRO B   94          0         8.01
CISPEP   6 ALA B  124    PRO B  125          0        -3.37
CISPEP   7 TYR B  550    PRO B  551          0         0.02
CISPEP   8 GLY B  596    PRO B  597          0         0.46
CISPEP   9 ALA C   93    PRO C   94          0        11.00
CISPEP  10 ALA C  124    PRO C  125          0         1.45
CISPEP  11 TYR C  550    PRO C  551          0         2.94
CISPEP  12 GLY C  596    PRO C  597          0         8.48
CRYST1  141.457  141.457  158.880  90.00  90.00 120.00 P 32 2 1     18
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      0.007069  0.004081  0.000000        0.00000
SCALE2      0.000000  0.008163  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006294        0.00000
      
PROCHECK
Go to PROCHECK summary
 References