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PDBsum entry 1wcq

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1wcq
Jmol
Contents
Protein chains
601 a.a.
Ligands
GOL ×7
DAN ×3
Metals
_NA ×3
Waters ×1078
HEADER    HYDROLASE                               19-NOV-04   1WCQ
TITLE     MUTAGENESIS OF THE NUCLEOPHILIC TYROSINE IN A BACTERIAL
TITLE    2 SIALIDASE TO PHENYLALANINE.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE;
COMPND   3 CHAIN: A, B, C;
COMPND   4 FRAGMENT: SIALIDASE, 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 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    HYDROLASE, SIALIDASE, MICROMONOSPORA VIRIDIFACIENS, HYDROLASE
KEYWDS   2 NEURAMINIDASE, GLYCOSIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.NEWSTEAD,J.N.WATSON,A.J.BENNET,G.TAYLOR
REVDAT   4   13-JUL-11 1WCQ    1       VERSN
REVDAT   3   24-FEB-09 1WCQ    1       VERSN
REVDAT   2   20-DEC-06 1WCQ    1       JRNL
REVDAT   1   12-OCT-05 1WCQ    0
JRNL        AUTH   J.N.WATSON,S.NEWSTEAD,A.A.NARINE,G.TAYLOR,A.J.BENNET
JRNL        TITL   TWO NUCLEOPHILIC MUTANTS OF THE MICROMONOSPORA
JRNL        TITL 2 VIRIDIFACIENS SIALIDASE OPERATE WITH RETENTION OF
JRNL        TITL 3 CONFIGURATION BY TWO DIFFERENT MECHANISMS.
JRNL        REF    CHEMBIOCHEM                   V.   6  1439 2005
JRNL        REFN                   ISSN 1439-4227
JRNL        PMID   16206228
JRNL        DOI    10.1002/CBIC.200500114
REMARK   2
REMARK   2 RESOLUTION.    2.1  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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 124.03
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 105259
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) : 0.178
REMARK   3   R VALUE            (WORKING SET) : 0.175
REMARK   3   FREE R VALUE                     : 0.238
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 5544
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) : 7713
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2090
REMARK   3   BIN FREE R VALUE SET COUNT          : 430
REMARK   3   BIN FREE R VALUE                    : 0.2950
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 13650
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 105
REMARK   3   SOLVENT ATOMS            : 1078
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) : 29.34
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.81000
REMARK   3    B22 (A**2) : -0.81000
REMARK   3    B33 (A**2) : 1.21000
REMARK   3    B12 (A**2) : -0.40000
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): 0.212
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.191
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.138
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.672
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14069 ; 0.021 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 19207 ; 1.835 ; 1.952
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1798 ; 7.114 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   643 ;34.507 ;23.266
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2043 ;14.261 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   131 ;19.651 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2122 ; 0.124 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11049 ; 0.008 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6223 ; 0.206 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9311 ; 0.308 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1097 ; 0.145 ; 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):    86 ; 0.187 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    36 ; 0.223 ; 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):  8950 ; 0.903 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14427 ; 1.448 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5331 ; 2.593 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4780 ; 3.806 ; 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  : 9
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): -24.8260  59.3720  84.8720
REMARK   3    T TENSOR
REMARK   3      T11:   -.0777 T22:   -.1067
REMARK   3      T33:    .0643 T12:   -.0614
REMARK   3      T13:   -.0079 T23:   -.0930
REMARK   3    L TENSOR
REMARK   3      L11:   1.4046 L22:    .6543
REMARK   3      L33:    .5617 L12:   -.3235
REMARK   3      L13:    .0112 L23:   -.2626
REMARK   3    S TENSOR
REMARK   3      S11:    .0816 S12:    .0646 S13:   -.1853
REMARK   3      S21:    .0124 S22:   -.0199 S23:   -.0572
REMARK   3      S31:   -.0146 S32:   -.0124 S33:   -.0617
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):   5.6050  47.7890  68.3770
REMARK   3    T TENSOR
REMARK   3      T11:   -.1741 T22:   -.1228
REMARK   3      T33:    .2590 T12:    .0682
REMARK   3      T13:    .0076 T23:   -.1221
REMARK   3    L TENSOR
REMARK   3      L11:   1.8408 L22:    .9048
REMARK   3      L33:   6.3884 L12:    .2445
REMARK   3      L13:   1.7474 L23:   1.3086
REMARK   3    S TENSOR
REMARK   3      S11:    .2988 S12:    .1370 S13:   -.2006
REMARK   3      S21:    .0385 S22:    .2020 S23:   -.1857
REMARK   3      S31:    .3268 S32:    .5608 S33:   -.5008
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): -14.4640  58.3670  45.2730
REMARK   3    T TENSOR
REMARK   3      T11:   -.1236 T22:   -.0949
REMARK   3      T33:    .0631 T12:   -.0364
REMARK   3      T13:    .0178 T23:   -.1027
REMARK   3    L TENSOR
REMARK   3      L11:   2.4865 L22:   2.0841
REMARK   3      L33:   1.0863 L12:    .5322
REMARK   3      L13:   -.6312 L23:   -.8017
REMARK   3    S TENSOR
REMARK   3      S11:    .0810 S12:    .0643 S13:    .0037
REMARK   3      S21:   -.0564 S22:    .1119 S23:    .1561
REMARK   3      S31:    .1550 S32:    .0070 S33:   -.1929
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    47        B   402
REMARK   3    ORIGIN FOR THE GROUP (A):  62.7240 -27.6390  41.4140
REMARK   3    T TENSOR
REMARK   3      T11:   -.0572 T22:    .0044
REMARK   3      T33:   -.1097 T12:    .0042
REMARK   3      T13:    .0331 T23:   -.0427
REMARK   3    L TENSOR
REMARK   3      L11:    .6535 L22:   2.4941
REMARK   3      L33:    .5194 L12:   -.4412
REMARK   3      L13:   -.2141 L23:   -.1862
REMARK   3    S TENSOR
REMARK   3      S11:    .0217 S12:    .1391 S13:   -.0734
REMARK   3      S21:    .2022 S22:   -.0694 S23:    .0967
REMARK   3      S31:   -.1270 S32:   -.0060 S33:    .0477
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   403        B   502
REMARK   3    ORIGIN FOR THE GROUP (A):  53.7630   7.6470  38.4640
REMARK   3    T TENSOR
REMARK   3      T11:    .0753 T22:   -.0616
REMARK   3      T33:   -.1251 T12:   -.0068
REMARK   3      T13:    .0721 T23:    .0494
REMARK   3    L TENSOR
REMARK   3      L11:   4.4861 L22:   1.8552
REMARK   3      L33:   1.0476 L12:   -.9415
REMARK   3      L13:   1.3881 L23:   -.4578
REMARK   3    S TENSOR
REMARK   3      S11:   -.0120 S12:    .2783 S13:    .0888
REMARK   3      S21:    .1514 S22:   -.0416 S23:    .0070
REMARK   3      S31:   -.3092 S32:    .1693 S33:    .0536
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   503        B   647
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0770  -8.7160  42.7690
REMARK   3    T TENSOR
REMARK   3      T11:   -.0559 T22:   -.0249
REMARK   3      T33:    .0772 T12:    .1386
REMARK   3      T13:    .1342 T23:    .1192
REMARK   3    L TENSOR
REMARK   3      L11:    .2972 L22:   2.8697
REMARK   3      L33:    .8385 L12:    .3616
REMARK   3      L13:    .2069 L23:   -.5114
REMARK   3    S TENSOR
REMARK   3      S11:   -.0246 S12:   -.0061 S13:    .0237
REMARK   3      S21:    .1478 S22:    .2637 S23:    .5106
REMARK   3      S31:   -.1135 S32:   -.1289 S33:   -.2391
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C    49        C   402
REMARK   3    ORIGIN FOR THE GROUP (A):   -.9240  22.7040  27.2890
REMARK   3    T TENSOR
REMARK   3      T11:   -.0311 T22:   -.1010
REMARK   3      T33:    .0488 T12:    .0180
REMARK   3      T13:   -.0418 T23:    .0400
REMARK   3    L TENSOR
REMARK   3      L11:    .2365 L22:    .9287
REMARK   3      L33:    .9509 L12:    .2242
REMARK   3      L13:   -.0303 L23:   -.1874
REMARK   3    S TENSOR
REMARK   3      S11:   -.0962 S12:    .0271 S13:    .0951
REMARK   3      S21:    .0795 S22:    .0963 S23:    .1325
REMARK   3      S31:   -.1921 S32:   -.0064 S33:    .0000
REMARK   3
REMARK   3   TLS GROUP : 8
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   403        C   502
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0490  23.2480  58.0860
REMARK   3    T TENSOR
REMARK   3      T11:    .0586 T22:    .0573
REMARK   3      T33:   -.1525 T12:   -.0450
REMARK   3      T13:   -.0037 T23:    .0594
REMARK   3    L TENSOR
REMARK   3      L11:   7.8726 L22:    .8041
REMARK   3      L33:   4.0348 L12:   1.2259
REMARK   3      L13:  -4.4630 L23:  -1.0854
REMARK   3    S TENSOR
REMARK   3      S11:    .0710 S12:   -.9053 S13:   -.2436
REMARK   3      S21:   -.1363 S22:   -.2943 S23:    .0237
REMARK   3      S31:   -.1926 S32:    .8793 S33:    .2232
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   503        C   647
REMARK   3    ORIGIN FOR THE GROUP (A):  37.6250  34.5690  33.9360
REMARK   3    T TENSOR
REMARK   3      T11:   -.0859 T22:   -.0132
REMARK   3      T33:   -.0202 T12:   -.0078
REMARK   3      T13:    .0260 T23:    .0475
REMARK   3    L TENSOR
REMARK   3      L11:   1.7582 L22:   2.0748
REMARK   3      L33:   1.8404 L12:    .3658
REMARK   3      L13:   -.5490 L23:    .1501
REMARK   3    S TENSOR
REMARK   3      S11:    .0128 S12:   -.3252 S13:   -.0383
REMARK   3      S21:    .0842 S22:   -.0401 S23:   -.0226
REMARK   3      S31:   -.0949 S32:    .2659 S33:    .0273
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 1WCQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-NOV-04.
REMARK 100 THE PDBE ID CODE IS EBI-21729.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-SEP-04
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 5.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-2
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
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 110911
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.830
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 7.200
REMARK 200  R MERGE                    (I) : 0.07000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.47000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.500
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 1EUU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.7
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16 % PEG 3350, 0.2 M AMMONIUM
REMARK 280  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,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+1/3
REMARK 290       6555   -X,-X+Y,-Z+2/3
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      106.83333
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       53.41667
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       53.41667
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      106.83333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3,
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 350 BIOMOLECULE:  2
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: B
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:  3
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: C
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 375
REMARK 375 SPECIAL POSITION
REMARK 375      HOH C2019  LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, B, C: TYR 370 TO PHE
REMARK 400  CATALYTIC ACTIVITY: HYDROLYSIS OF ALPHA-(2->3)-, ALPHA-(2->6)-,
REMARK 400  ALPHA-(2->8)-GLYCOSIDIC LINKAGES OF TERMINAL SIALIC RESIDUES IN
REMARK 400  OLIGOSACCHARIDES, GLYCOPROTEINS, GLYCOLIPIDS, COLOMINIC ACID AND
REMARK 400  SYNTHETIC SUBSTRATES.
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 465     GLU C    48
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   O    ASN B    59     O    HOH B  2007              2.19
REMARK 500   O    HOH B  2005     O    HOH B  2013              2.15
REMARK 500   O    HOH B  2026     O    HOH B  2048              2.18
REMARK 500   O    HOH B  2084     O    HOH B  2178              2.10
REMARK 500   O    HOH C  2063     O    HOH C  2125              1.89
REMARK 500   O    HOH C  2064     O    HOH C  2065              2.15
REMARK 500   O    HOH C  2144     O    HOH C  2145              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLN A 451   CD    GLN A 451   NE2     0.426
REMARK 500    GLN A 451   CD    GLN A 451   OE1    -0.135
REMARK 500    GLN A 451   CG    GLN A 451   CD      0.150
REMARK 500    ASP B 595   CB    ASP B 595   CG      0.180
REMARK 500    ASP B 595   CG    ASP B 595   OD1     0.484
REMARK 500    ARG B 617   CZ A  ARG B 617   NH1A    0.084
REMARK 500    GLN C 419   CD    GLN C 419   OE1     0.168
REMARK 500    GLN C 419   CG    GLN C 419   CD      0.161
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 202   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A 202   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    GLN A 451   CG  -  CD  -  NE2 ANGL. DEV. = -21.2 DEGREES
REMARK 500    ASP A 505   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ARG A 553   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG A 553   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    ASP A 557   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ARG B  87   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ASP B  92   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ARG B 152   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG B 202   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG B 202   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    CYS B 351   CA  -  CB  -  SG  ANGL. DEV. =  -7.3 DEGREES
REMARK 500    ASP B 595   CB  -  CG  -  OD1 ANGL. DEV. = -25.3 DEGREES
REMARK 500    ASP B 595   CB  -  CG  -  OD2 ANGL. DEV. =  14.7 DEGREES
REMARK 500    ARG B 617   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ASP C  92   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG C 138   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG C 202   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG C 202   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    ARG C 602   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
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       79.24     79.58
REMARK 500    PRO A  94       33.31    -88.26
REMARK 500    ASP A 131       68.53     68.12
REMARK 500    GLN A 151      -93.33   -131.11
REMARK 500    ASP A 179       36.92   -147.22
REMARK 500    ASP A 259     -166.94   -168.98
REMARK 500    GLU A 260      120.16    -34.69
REMARK 500    THR A 309       78.27     66.52
REMARK 500    ALA A 337       41.95    -86.99
REMARK 500    SER A 369     -112.24    -96.41
REMARK 500    SER A 565       16.61   -155.69
REMARK 500    ALA A 581      -94.00   -107.75
REMARK 500    ILE B  69       83.03     75.51
REMARK 500    ASP B  92     -179.29    -65.12
REMARK 500    ASP B 131       76.76     73.11
REMARK 500    GLN B 151      -90.02   -124.47
REMARK 500    ASP B 259     -157.19   -167.20
REMARK 500    THR B 309       76.88     74.68
REMARK 500    SER B 338      132.95   -176.61
REMARK 500    ASP B 352       43.28   -140.43
REMARK 500    MET B 368      106.11   -169.89
REMARK 500    SER B 369     -104.11    -99.95
REMARK 500    CYS B 405       68.77    -66.82
REMARK 500    SER B 516      137.66   -171.49
REMARK 500    SER B 565       10.98   -152.82
REMARK 500    ALA B 581      -90.62   -111.94
REMARK 500    ILE C  69       81.23     82.11
REMARK 500    ASP C 131       74.15     70.20
REMARK 500    GLN C 151      -87.24   -127.62
REMARK 500    THR C 194       73.88   -119.37
REMARK 500    ALA C 218      126.76    -38.77
REMARK 500    ASP C 259     -154.10   -170.56
REMARK 500    THR C 309       78.48     76.16
REMARK 500    ASP C 352       49.84   -141.25
REMARK 500    SER C 369     -102.03   -101.71
REMARK 500    SER C 565       11.62   -147.07
REMARK 500    ALA C 581      -92.58   -111.04
REMARK 500    ALA C 619      139.60   -176.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ASP B 595         0.08    SIDE CHAIN
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 A1648  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 639   O
REMARK 620 2 ASN A 533   O   103.4
REMARK 620 3 ASN A 528   O    88.2 168.4
REMARK 620 4 ASP A 531   OD1 139.3 100.6  70.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA B1648  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 528   O
REMARK 620 2 ALA B 639   O    85.0
REMARK 620 3 THR B 536   O   102.5  75.1
REMARK 620 4 ASP B 531   OD1  73.8 142.2 139.4
REMARK 620 5 ASN B 533   O   167.2 107.6  83.1  94.4
REMARK 620 6 GLU B 640   OE2  91.0  75.5 146.2  74.0  90.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA C1648  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 528   O
REMARK 620 2 ASN C 533   O   163.8
REMARK 620 3 THR C 536   O    95.8  86.9
REMARK 620 4 THR C 536   OG1  89.0  77.0  69.8
REMARK 620 5 ALA C 639   O    84.8 111.4  81.1 149.4
REMARK 620 6 GLU C 640   OE2  94.4  89.8 154.1 134.2  76.2
REMARK 620 N                    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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1648
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA B1648
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA C1648
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A1651
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B1652
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN C1651
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1649
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1650
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1649
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1650
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1651
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1649
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1650
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
DBREF  1WCQ A   47   647  UNP    Q02834   NANH_MICVI      47    647
DBREF  1WCQ B   47   647  UNP    Q02834   NANH_MICVI      47    647
DBREF  1WCQ C   47   647  UNP    Q02834   NANH_MICVI      47    647
SEQADV 1WCQ PHE A  370  UNP  Q02834    TYR   370 ENGINEERED MUTATION
SEQADV 1WCQ PHE B  370  UNP  Q02834    TYR   370 ENGINEERED MUTATION
SEQADV 1WCQ PHE C  370  UNP  Q02834    TYR   370 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 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 PHE 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 GLU 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 PHE 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 GLU 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 PHE 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     NA  A1648       1
HET     NA  B1648       1
HET     NA  C1648       1
HET    DAN  A1651      20
HET    DAN  B1652      20
HET    DAN  C1651      20
HET    GOL  A1649       6
HET    GOL  A1650       6
HET    GOL  B1649       6
HET    GOL  B1650       6
HET    GOL  B1651       6
HET    GOL  C1649       6
HET    GOL  C1650       6
HETNAM      NA SODIUM ION
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
HETNAM     GOL GLYCEROL
FORMUL   4   NA    3(NA 1+)
FORMUL   7  DAN    3(C11 H17 N O8)
FORMUL  10  GOL    7(C3 H8 O3)
FORMUL  17  HOH   *1078(H2 O)
HELIX    1   1 ALA A  326  LYS A  329  5                                   4
HELIX    2   2 ASN A  397  GLY A  402  1                                   6
HELIX    3   3 ASP A  505  MET A  509  5                                   5
HELIX    4   4 ARG A  525  ASP A  531  5                                   7
HELIX    5   5 THR B  190  THR B  194  5                                   5
HELIX    6   6 ALA B  326  LYS B  329  5                                   4
HELIX    7   7 ASN B  397  GLY B  402  1                                   6
HELIX    8   8 ASP B  505  MET B  509  5                                   5
HELIX    9   9 ARG B  525  ASP B  531  5                                   7
HELIX   10  10 THR C  190  THR C  194  5                                   5
HELIX   11  11 TYR C  214  ALA C  218  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 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 TRP A 594  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 TYR B  67  VAL B  74  0
SHEET    2  BB 4 LEU B  80  GLY B  86 -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 GLY B 491  VAL B 501  1  O  THR B 498   N  VAL B 413
SHEET    3  BI 4 GLY B 478  THR B 488 -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
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
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
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 ASN C 492  VAL C 501  1  O  THR C 498   N  VAL C 413
SHEET    3  CH 4 GLY C 478  ARG C 487 -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
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 TRP C 594  ARG C 602
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                          1555   1555  2.04
SSBOND   2 CYS B  351    CYS B  405                          1555   1555  2.04
SSBOND   3 CYS C  351    CYS C  405                          1555   1555  2.02
LINK        NA    NA A1648                 O   ALA A 639     1555   1555  2.35
LINK        NA    NA A1648                 O   ASN A 533     1555   1555  2.20
LINK        NA    NA A1648                 O   ASN A 528     1555   1555  2.30
LINK        NA    NA A1648                 OD1 ASP A 531     1555   1555  2.53
LINK        NA    NA B1648                 O   ASN B 528     1555   1555  2.35
LINK        NA    NA B1648                 O   ALA B 639     1555   1555  2.38
LINK        NA    NA B1648                 O   THR B 536     1555   1555  2.45
LINK        NA    NA B1648                 OD1 ASP B 531     1555   1555  2.48
LINK        NA    NA B1648                 O   ASN B 533     1555   1555  2.42
LINK        NA    NA B1648                 OE2 GLU B 640     1555   1555  2.44
LINK        NA    NA C1648                 O   ASN C 533     1555   1555  2.21
LINK        NA    NA C1648                 O   THR C 536     1555   1555  2.20
LINK        NA    NA C1648                 OG1 THR C 536     1555   1555  2.50
LINK        NA    NA C1648                 O   ALA C 639     1555   1555  2.27
LINK        NA    NA C1648                 OE2 GLU C 640     1555   1555  2.32
LINK        NA    NA C1648                 O   ASN C 528     1555   1555  2.32
CISPEP   1 ALA A   93    PRO A   94          0         7.61
CISPEP   2 ALA A  124    PRO A  125          0         2.11
CISPEP   3 TYR A  550    PRO A  551          0        -1.00
CISPEP   4 GLY A  596    PRO A  597          0         9.40
CISPEP   5 ALA B   93    PRO B   94          0        -2.18
CISPEP   6 ALA B  124    PRO B  125          0         0.44
CISPEP   7 TYR B  550    PRO B  551          0         0.49
CISPEP   8 GLY B  596    PRO B  597          0         7.58
CISPEP   9 ALA C   93    PRO C   94          0        11.98
CISPEP  10 ALA C  124    PRO C  125          0        -5.44
CISPEP  11 TYR C  550    PRO C  551          0         3.19
CISPEP  12 GLY C  596    PRO C  597          0         6.51
SITE     1 AC1  6 ASN A 528  ASP A 531  ASN A 533  THR A 536
SITE     2 AC1  6 ALA A 639  GLU A 640
SITE     1 AC2  6 ASN B 528  ASP B 531  ASN B 533  THR B 536
SITE     2 AC2  6 ALA B 639  GLU B 640
SITE     1 AC3  6 ASN C 528  ASP C 531  ASN C 533  THR C 536
SITE     2 AC3  6 ALA C 639  GLU C 640
SITE     1 AC4 14 ARG A  68  ILE A  69  ARG A  87  ASP A  92
SITE     2 AC4 14 ASP A 131  PHE A 203  ASP A 259  ARG A 276
SITE     3 AC4 14 ARG A 342  PHE A 370  HOH A2024  HOH A2025
SITE     4 AC4 14 HOH A2318  HOH A2320
SITE     1 AC5 15 ARG B  68  ILE B  69  ARG B  87  ASP B  92
SITE     2 AC5 15 ASP B 131  PHE B 203  ASP B 259  GLU B 260
SITE     3 AC5 15 ARG B 276  ARG B 342  PHE B 370  HOH B2082
SITE     4 AC5 15 HOH B2397  HOH B2398  HOH B2399
SITE     1 AC6 15 ARG C  68  ILE C  69  ARG C  87  ASP C  92
SITE     2 AC6 15 ASP C 131  PHE C 203  PHE C 234  ASP C 259
SITE     3 AC6 15 GLU C 260  ARG C 276  ARG C 342  PHE C 370
SITE     4 AC6 15 HOH C2044  HOH C2358  HOH C2359
SITE     1 AC7  2 HIS A 633  LYS A 634
SITE     1 AC8  5 ARG A 571  THR A 605  LEU A 607  HOH A2316
SITE     2 AC8  5 HOH A2317
SITE     1 AC9  4 PHE B 363  PRO B 365  TRP B 400  SER B 439
SITE     1 BC1  5 GLU B 522  HIS B 539  TRP B 542  ARG B 572
SITE     2 BC1  5 HOH B2367
SITE     1 BC2  5 ARG B 617  HOH B2395  HOH B2396  ARG C  61
SITE     2 BC2  5 GLN C 364
SITE     1 BC3  5 VAL C 116  VAL C 117  SER C 118  ALA C 119
SITE     2 BC3  5 HIS C 186
SITE     1 BC4  5 GLU C 522  HIS C 539  TRP C 542  ARG C 572
SITE     2 BC4  5 GLU C 578
CRYST1  143.258  143.258  160.250  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      0.006980  0.004030  0.000000        0.00000
SCALE2      0.000000  0.008060  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006240        0.00000
      
PROCHECK
Go to PROCHECK summary
 References