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PDBsum entry 1w8n

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Hydrolase PDB id
1w8n
Jmol
Contents
Protein chain
601 a.a. *
Ligands
GAL
DAN
Metals
_NA
Waters ×516
* Residue conservation analysis
HEADER    HYDROLASE                               24-SEP-04   1W8N
TITLE     CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS
TITLE    2 IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA
TITLE    3 VIRIDIFACIENS.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BACTERIAL SIALIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 47-647;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MICROMONOSPORA VIRIDIFACIENS;
SOURCE   3 ORGANISM_TAXID: 1881;
SOURCE   4 ATCC: 31146;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS    GLYCOSIDASE, HYDROLASE, NEURAMINIDASE, BETA- PROPELLER FOLD.
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.NEWSTEAD,J.N.WATSON,V.DOOKHUN,A.J.BENNET,G.TAYLOR
REVDAT   4   13-JUL-11 1W8N    1       VERSN
REVDAT   3   24-FEB-09 1W8N    1       VERSN
REVDAT   2   10-NOV-04 1W8N    1       JRNL
REVDAT   1   30-SEP-04 1W8N    0
JRNL        AUTH   J.N.WATSON,S.NEWSTEAD,V.DOOKHUN,G.TAYLOR,A.J.BENNET
JRNL        TITL   CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS
JRNL        TITL 2 IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA
JRNL        TITL 3 VIRIDIFACIENS
JRNL        REF    FEBS LETT.                    V. 577   265 2004
JRNL        REFN                   ISSN 0014-5793
JRNL        PMID   15527797
JRNL        DOI    10.1016/J.FEBSLET.2004.10.016
REMARK   2
REMARK   2 RESOLUTION.    2.1  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 87.71
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.1
REMARK   3   NUMBER OF REFLECTIONS             : 37473
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) : 0.168
REMARK   3   R VALUE            (WORKING SET) : 0.166
REMARK   3   FREE R VALUE                     : 0.219
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1984
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2845
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040
REMARK   3   BIN FREE R VALUE SET COUNT          : 147
REMARK   3   BIN FREE R VALUE                    : 0.2490
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4556
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 33
REMARK   3   SOLVENT ATOMS            : 516
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.41
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.58000
REMARK   3    B22 (A**2) : -0.08000
REMARK   3    B33 (A**2) : 0.66000
REMARK   3    B12 (A**2) : 0.00000
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): 0.202
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.180
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.119
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.467
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4695 ; 0.021 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  4137 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6414 ; 1.773 ; 1.945
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9599 ; 0.909 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   600 ; 7.218 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   713 ; 0.104 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5369 ; 0.009 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   969 ; 0.006 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   949 ; 0.206 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5276 ; 0.266 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2880 ; 0.091 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   436 ; 0.200 ; 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):    14 ; 0.293 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    44 ; 0.312 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    26 ; 0.225 ; 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):  2986 ; 0.929 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4811 ; 1.483 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1709 ; 2.356 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1603 ; 3.541 ; 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  : 3
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    47        A   402
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0010  43.0860  26.1960
REMARK   3    T TENSOR
REMARK   3      T11:   0.1655 T22:   0.1773
REMARK   3      T33:   0.1272 T12:   0.0169
REMARK   3      T13:  -0.0017 T23:   0.0511
REMARK   3    L TENSOR
REMARK   3      L11:   0.4267 L22:   1.2112
REMARK   3      L33:   1.1207 L12:  -0.1779
REMARK   3      L13:   0.0391 L23:  -0.4104
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0136 S12:   0.0264 S13:  -0.1110
REMARK   3      S21:   0.1278 S22:  -0.0622 S23:  -0.0801
REMARK   3      S31:  -0.1729 S32:  -0.0027 S33:   0.0758
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   403        A   502
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4740  74.4040   8.5290
REMARK   3    T TENSOR
REMARK   3      T11:   0.4566 T22:   0.0544
REMARK   3      T33:   0.0092 T12:  -0.0160
REMARK   3      T13:  -0.0469 T23:  -0.0137
REMARK   3    L TENSOR
REMARK   3      L11:   1.7131 L22:   1.3392
REMARK   3      L33:   4.0821 L12:   0.3723
REMARK   3      L13:   0.9677 L23:   0.5738
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2704 S12:   0.0744 S13:   0.0701
REMARK   3      S21:  -0.0919 S22:   0.1284 S23:   0.0144
REMARK   3      S31:  -0.5011 S32:   0.0243 S33:   0.1420
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   503        A   647
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0880  51.3040 -11.3350
REMARK   3    T TENSOR
REMARK   3      T11:   0.2666 T22:   0.1806
REMARK   3      T33:   0.0350 T12:  -0.0052
REMARK   3      T13:  -0.0555 T23:  -0.0110
REMARK   3    L TENSOR
REMARK   3      L11:   0.8201 L22:   3.0441
REMARK   3      L33:   1.9636 L12:   0.0891
REMARK   3      L13:  -0.4954 L23:   0.9228
REMARK   3    S TENSOR
REMARK   3      S11:   0.0049 S12:  -0.2312 S13:  -0.0996
REMARK   3      S21:   0.1757 S22:  -0.1278 S23:  -0.0306
REMARK   3      S31:  -0.1193 S32:  -0.1392 S33:   0.1228
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 1W8N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-SEP-04.
REMARK 100 THE PDBE ID CODE IS EBI-21141.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-MAY-03
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : NULL
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-MSC MICROMAX-007
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : OSMIC MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU-MSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44697
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.920
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.0
REMARK 200  DATA REDUNDANCY                : 5.600
REMARK 200  R MERGE                    (I) : 0.07000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1EUT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.9
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16 % PEG 3350, 0.2M AMMONIUM
REMARK 280  CITRATE.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-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       23.30100
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.93250
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.80400
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.93250
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.30100
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.80400
REMARK 290   SMTRY3   4  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 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED MUTATION IN CHAIN A, ASP 92 TO GLY
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   OE2  GLU A   522     O    HOH A  2435              2.13
REMARK 500   O6   GAL A  1648     O    HOH A  2513              2.13
REMARK 500   O    HOH A  2068     O    HOH A  2131              2.18
REMARK 500   O    HOH A  2112     O    HOH A  2224              2.18
REMARK 500   O    HOH A  2214     O    HOH A  2275              2.02
REMARK 500   O    HOH A  2269     O    HOH A  2270              2.11
REMARK 500   O    HOH A  2448     O    HOH A  2450              2.08
REMARK 500   O    HOH A  2468     O    HOH A  2471              2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A  2218     O    HOH A  2492     2565     2.19
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    ALA A 473   CA    ALA A 473   CB      0.140
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    ARG A 187   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A 202   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ARG A 202   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.5 DEGREES
REMARK 500    ASP A 242   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG A 342   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ASP A 447   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP A 618   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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
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    ILE A  69       83.66     80.09
REMARK 500    ASP A 131       71.23     67.63
REMARK 500    GLN A 151      -94.19   -121.83
REMARK 500    ASP A 259     -159.45   -178.03
REMARK 500    THR A 309       84.05     78.98
REMARK 500    SER A 369     -109.13    -98.04
REMARK 500    ALA A 581      -95.35   -125.53
REMARK 500
REMARK 500 REMARK: NULL
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                              NA A1650  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 536   O
REMARK 620 2 ASN A 528   O   108.9
REMARK 620 3 ASN A 533   O    89.6 156.8
REMARK 620 4 ALA A 639   O    81.2  88.2 108.9
REMARK 620 N                    1     2     3
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL A1648
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1650
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A1649
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
DBREF  1W8N A   47   647  UNP    Q02834   NANH_MICVI      47    647
SEQADV 1W8N GLY A   92  UNP  Q02834    ASP    92 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 GLY 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 GLU 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
HET    GAL  A1648      12
HET     NA  A1650       1
HET    DAN  A1649      20
HETNAM     GAL BETA-D-GALACTOSE
HETNAM      NA SODIUM ION
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
FORMUL   2  GAL    C6 H12 O6
FORMUL   3   NA    NA 1+
FORMUL   4  DAN    C11 H17 N O8
FORMUL   5  HOH   *516(H2 O)
HELIX    1   1 THR A  190  ILE A  193  5                                   4
HELIX    2   2 SER A  325  LYS A  329  5                                   5
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
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 TYR A  67  VAL A  74  0
SHEET    2  AB 4 LEU A  80  GLY A  86 -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  THR A 428 -1  O  ALA A 426   N  THR A 409
SHEET    3  AH 4 GLN A 462  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 ALA A 493  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
SSBOND   1 CYS A  351    CYS A  405                          1555   1555  2.01
LINK        NA    NA A1650                 O   THR A 536     1555   1555  2.55
LINK        NA    NA A1650                 O   ASN A 528     1555   1555  2.45
LINK        NA    NA A1650                 O   ASN A 533     1555   1555  2.40
LINK        NA    NA A1650                 O   ALA A 639     1555   1555  2.46
CISPEP   1 ALA A   93    PRO A   94          0         7.77
CISPEP   2 ALA A  124    PRO A  125          0         1.19
CISPEP   3 TYR A  550    PRO A  551          0        -2.33
CISPEP   4 GLY A  596    PRO A  597          0         7.55
SITE     1 AC1  6 GLU A 522  HIS A 539  TRP A 542  ARG A 572
SITE     2 AC1  6 HOH A2435  HOH A2513
SITE     1 AC2  5 ASN A 528  ASP A 531  ASN A 533  THR A 536
SITE     2 AC2  5 ALA A 639
SITE     1 AC3 15 ARG A  68  ILE A  69  ARG A  87  ASP A 131
SITE     2 AC3 15 PHE A 155  PHE A 203  PHE A 234  ASP A 259
SITE     3 AC3 15 ARG A 276  ARG A 342  TYR A 370  HOH A2063
SITE     4 AC3 15 HOH A2514  HOH A2515  HOH A2516
CRYST1   46.602  111.608  143.865  90.00  90.00  90.00 P 21 21 21    4
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      0.021458  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008960  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006951        0.00000
      
PROCHECK
Go to PROCHECK summary
 References