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PDBsum entry 2bzd

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2bzd
Jmol
Contents
Protein chains
601 a.a.
Ligands
GAL ×3
GOL ×3
Metals
_NA ×3
Waters ×1496
HEADER    HYDROLASE                               16-AUG-05   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 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    SIALIDASE, HYDROLASE, CARBOHYDRATE BINDING MODULE, GLYCOSIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.L.NEWSTEAD,G.TAYLOR
REVDAT   4   13-JUL-11 2BZD    1       VERSN
REVDAT   3   24-FEB-09 2BZD    1       VERSN
REVDAT   2   26-OCT-05 2BZD    1       AUTHOR JRNL
REVDAT   1   19-AUG-05 2BZD    0
SPRSDE     19-AUG-05 2BZD      2BQ9
JRNL        AUTH   S.L.NEWSTEAD,J.N.WATSON,A.J.BENNET,G.TAYLOR
JRNL        TITL   GALACTOSE RECOGNITION BY THE CARBOHYDRATE-BINDING MODULE OF
JRNL        TITL 2 A BACTERIAL SIALIDASE.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  61  1483 2005
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   16239725
JRNL        DOI    10.1107/S0907444905026132
REMARK   2
REMARK   2 RESOLUTION.    2.0  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) : 2.00
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) : 0.197
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.267
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           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8504
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460
REMARK   3   BIN FREE R VALUE SET COUNT          : 476
REMARK   3   BIN FREE R VALUE                    : 0.3490
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 13663
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 57
REMARK   3   SOLVENT ATOMS            : 1496
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) : 17.61
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.12000
REMARK   3    B22 (A**2) : 0.12000
REMARK   3    B33 (A**2) : -0.18000
REMARK   3    B12 (A**2) : 0.06000
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): 0.210
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.199
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.157
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.637
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14039 ; 0.016 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 19178 ; 1.603 ; 1.949
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1799 ; 7.075 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   642 ;33.959 ;23.255
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2046 ;15.791 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   131 ;19.554 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2125 ; 0.103 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11035 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6769 ; 0.215 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9231 ; 0.305 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1450 ; 0.178 ; 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):   113 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    51 ; 0.277 ; 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):  8959 ; 0.699 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14446 ; 1.146 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5293 ; 1.957 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4732 ; 2.928 ; 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  : 6
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:    .0020 T22:   -.0023
REMARK   3      T33:    .0835 T12:   -.0200
REMARK   3      T13:   -.0814 T23:   -.0430
REMARK   3    L TENSOR
REMARK   3      L11:   3.4730 L22:   4.6446
REMARK   3      L33:   1.3381 L12:  -1.3866
REMARK   3      L13:    .6879 L23:    .5391
REMARK   3    S TENSOR
REMARK   3      S11:    .0305 S12:    .0257 S13:    .0291
REMARK   3      S21:    .2426 S22:   -.1381 S23:    .2380
REMARK   3      S31:    .0145 S32:   -.0040 S33:    .1076
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:    .0942 T22:    .0581
REMARK   3      T33:    .6987 T12:    .2039
REMARK   3      T13:    .3055 T23:    .0242
REMARK   3    L TENSOR
REMARK   3      L11:   6.1815 L22:   1.4602
REMARK   3      L33:  18.8495 L12:  -1.1882
REMARK   3      L13:   1.7590 L23:  -1.8306
REMARK   3    S TENSOR
REMARK   3      S11:    .8333 S12:   -.0301 S13:   1.6833
REMARK   3      S21:   -.4185 S22:   -.2141 S23:   -.7732
REMARK   3      S31:    .5239 S32:   1.1742 S33:   -.6192
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:    .0949 T22:   -.0971
REMARK   3      T33:    .0017 T12:   -.0596
REMARK   3      T13:   -.0430 T23:   -.0618
REMARK   3    L TENSOR
REMARK   3      L11:   3.5191 L22:   4.7522
REMARK   3      L33:   2.1244 L12:    .9410
REMARK   3      L13:  -1.4487 L23:  -1.4147
REMARK   3    S TENSOR
REMARK   3      S11:   -.0771 S12:   -.0276 S13:    .0417
REMARK   3      S21:   -.4197 S22:   -.0214 S23:   -.0586
REMARK   3      S31:    .2685 S32:   -.2667 S33:    .0985
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:   -.0995 T22:    .0173
REMARK   3      T33:   -.0188 T12:    .0230
REMARK   3      T13:   -.0567 T23:   -.0708
REMARK   3    L TENSOR
REMARK   3      L11:    .9996 L22:   2.6161
REMARK   3      L33:    .9237 L12:   -.0477
REMARK   3      L13:   -.2207 L23:   -.3897
REMARK   3    S TENSOR
REMARK   3      S11:    .1263 S12:   -.0578 S13:    .0606
REMARK   3      S21:    .1159 S22:   -.1891 S23:   -.1453
REMARK   3      S31:   -.1137 S32:    .1780 S33:    .0627
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:    .0501 T22:    .0101
REMARK   3      T33:   -.0212 T12:   -.0687
REMARK   3      T13:    .1022 T23:   -.0430
REMARK   3    L TENSOR
REMARK   3      L11:   7.4733 L22:   1.4604
REMARK   3      L33:   1.2265 L12:  -1.6483
REMARK   3      L13:   1.7996 L23:   -.4704
REMARK   3    S TENSOR
REMARK   3      S11:    .1399 S12:    .1014 S13:    .1870
REMARK   3      S21:   -.0098 S22:   -.0352 S23:   -.2462
REMARK   3      S31:   -.2152 S32:    .3763 S33:   -.1047
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:   -.0443 T22:   -.0987
REMARK   3      T33:   -.0667 T12:    .1023
REMARK   3      T13:    .1360 T23:    .0755
REMARK   3    L TENSOR
REMARK   3      L11:    .9905 L22:   3.8226
REMARK   3      L33:   1.2643 L12:   -.2568
REMARK   3      L13:    .3185 L23:   -.2691
REMARK   3    S TENSOR
REMARK   3      S11:   -.1558 S12:   -.0202 S13:   -.0185
REMARK   3      S21:    .1870 S22:    .2686 S23:    .3113
REMARK   3      S31:    .0023 S32:    .0591 S33:   -.1128
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 2BZD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-AUG-05.
REMARK 100 THE PDBE ID CODE IS EBI-25349.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-04
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                       : ID14-2
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   : 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
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16 % PEG 3350, 0.2 M
REMARK 280  DI-AMMONIUM 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,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      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 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 X  36  LIES ON A SPECIAL POSITION.
REMARK 375      HOH Y 391  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 400
REMARK 400 RELEASES SIALIC ACIDS FOR USE AS CARBON AND ENERGY SOURCES
REMARK 400 FOR THIS NON-PATHOGENIC BACTERIUM WHILE IN PATHOGENIC
REMARK 400 MICROORGANISMS.
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           DISTANCE
REMARK 500   NH1  ARG C   276     O3   GOL C  1650              2.13
REMARK 500   O    HOH B  2031     O    HOH B  2032              2.15
REMARK 500   O    HOH B  2362     O    HOH B  2363              2.19
REMARK 500   O    HOH C  2132     O    HOH C  2261              2.13
REMARK 500   O    HOH C  2505     O    HOH C  2508              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 B  2100     O    HOH A  2295     1545     2.20
REMARK 500   O    HOH C  2025     O    HOH B  2427     5555     2.09
REMARK 500   O    HOH C  2155     O    HOH C  2155     4555     1.90
REMARK 500   O    HOH C  2247     O    HOH C  2247     6555     2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    LEU B 589   CA  -  CB  -  CG  ANGL. DEV. = -15.5 DEGREES
REMARK 500    ASP C  92   CB  -  CG  -  OD1 ANGL. DEV. =   8.9 DEGREES
REMARK 500    ARG C 202   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG C 202   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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    ASN A  59       95.27    -64.78
REMARK 500    ILE A  69       83.53     69.15
REMARK 500    ASP A  92     -179.46    -68.91
REMARK 500    PRO A  94       47.11    -98.86
REMARK 500    PRO A  96       56.68    -67.37
REMARK 500    ASP A 131       76.64     67.34
REMARK 500    GLN A 151      -83.53   -119.33
REMARK 500    THR A 162       13.98   -143.24
REMARK 500    LEU A 182      -61.53    -96.99
REMARK 500    TRP A 199       93.73    -67.26
REMARK 500    ARG A 220      126.31    -38.12
REMARK 500    ALA A 231        1.07    -69.97
REMARK 500    ASP A 259     -169.68    179.94
REMARK 500    ALA A 260      121.53    -29.95
REMARK 500    ARG A 280       62.99     60.89
REMARK 500    THR A 309       71.83     75.03
REMARK 500    ALA A 336      102.74    -57.59
REMARK 500    ALA A 337       41.14    -77.04
REMARK 500    SER A 369     -107.26    -91.24
REMARK 500    ALA A 406       65.39   -158.52
REMARK 500    ASN A 429       99.28    -68.34
REMARK 500    SER A 565       13.50   -148.69
REMARK 500    GLU A 578       29.26   -141.13
REMARK 500    ALA A 581      -97.11   -105.33
REMARK 500    ILE B  69       76.79     77.28
REMARK 500    ASP B 131       68.48     69.70
REMARK 500    GLN B 151      -94.48   -122.13
REMARK 500    ASP B 259     -162.25   -172.64
REMARK 500    THR B 309       74.07     74.37
REMARK 500    ASP B 352       43.69   -148.60
REMARK 500    SER B 369     -106.31    -91.52
REMARK 500    PRO B 446      -31.18    -33.86
REMARK 500    SER B 453      148.34   -170.44
REMARK 500    SER B 516      139.47   -171.54
REMARK 500    SER B 565       11.76   -144.88
REMARK 500    ALA B 581      -97.61   -110.43
REMARK 500    ASN C  59      120.50    -34.94
REMARK 500    ILE C  69       78.68     80.74
REMARK 500    ASP C  92     -178.41    -61.30
REMARK 500    PRO C  94       36.15    -95.12
REMARK 500    ASP C 131       67.78     70.70
REMARK 500    GLN C 151      -85.21   -130.45
REMARK 500    TRP C 199       98.90    -66.96
REMARK 500    ASP C 259     -161.93   -175.87
REMARK 500    THR C 309       80.61     74.03
REMARK 500    SER C 369     -103.72   -100.95
REMARK 500    PRO C 417      155.07    -49.51
REMARK 500    THR C 475      135.33    -33.43
REMARK 500    LEU C 504      160.02    -47.26
REMARK 500    GLU C 517      137.28   -171.50
REMARK 500
REMARK 500 THIS ENTRY HAS      51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ASP A 447        24.8      L          L   OUTSIDE RANGE
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 ASN A 528   O
REMARK 620 2 ASN A 533   O   162.8
REMARK 620 3 THR A 536   O   110.9  78.7
REMARK 620 4 ALA A 639   O    90.5 105.5  80.1
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 THR B 536   O
REMARK 620 2 ASN B 528   O   109.7
REMARK 620 3 ALA B 639   O    78.8  92.0
REMARK 620 4 GLU B 640B  OE1 145.2  88.6  71.0
REMARK 620 5 ASN B 533   O    85.6 160.2 103.5  85.1
REMARK 620 N                    1     2     3     4
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 THR C 536   O
REMARK 620 2 ASN C 528   O   118.9
REMARK 620 3 ASN C 533   O    95.8 145.3
REMARK 620 N                    1     2
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 A1649
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL B1649
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL C1649
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1648
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA B1648
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA C1648
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1650
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1650
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
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
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).
REMARK 900 RELATED ID: 2BQ9   RELATED DB: PDB
REMARK 900  GALACTOSE RECOGNITION BY THE CARBOHYDRATE-
REMARK 900  BINDING MODULE OF A BACTERIAL SIALIDASE
DBREF  2BZD A   47   647  UNP    Q02834   NANH_MICVI      47    647
DBREF  2BZD B   47   647  UNP    Q02834   NANH_MICVI      47    647
DBREF  2BZD C   47   647  UNP    Q02834   NANH_MICVI      47    647
SEQADV 2BZD ALA A  260  UNP  Q02834    GLU   260 ENGINEERED MUTATION
SEQADV 2BZD ALA B  260  UNP  Q02834    GLU   260 ENGINEERED MUTATION
SEQADV 2BZD 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   *1496(H2 O)
HELIX    1   1 THR A  190  ILE A  193  5                                   4
HELIX    2   2 TYR A  214  ALA A  218  5                                   5
HELIX    3   3 ALA A  326  LYS A  329  5                                   4
HELIX    4   4 ASN A  397  GLY A  402  1                                   6
HELIX    5   5 ASP A  505  MET A  509  5                                   5
HELIX    6   6 ARG A  525  ASP A  531  5                                   7
HELIX    7   7 THR B  190  ILE B  193  5                                   4
HELIX    8   8 ALA B  326  LYS B  329  5                                   4
HELIX    9   9 ASN B  397  GLY B  402  1                                   6
HELIX   10  10 ASP B  505  MET B  509  5                                   5
HELIX   11  11 ARG B  525  ASP B  531  5                                   7
HELIX   12  12 THR C  190  THR C  194  5                                   5
HELIX   13  13 ALA C  326  LYS C  329  5                                   4
HELIX   14  14 ASN C  397  GLY C  402  1                                   6
HELIX   15  15 ASP C  505  MET C  509  5                                   5
HELIX   16  16 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 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
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 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
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 ASN C  66  VAL C  74  0
SHEET    2  CB 4 LEU C  80  ARG C  87 -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 ASP C 595  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  2.00
SSBOND   3 CYS C  351    CYS C  405                          1555   1555  1.98
LINK        NA    NA A1648                 O   ASN A 528     1555   1555  2.43
LINK        NA    NA A1648                 O   ASN A 533     1555   1555  2.18
LINK        NA    NA A1648                 O   THR A 536     1555   1555  2.49
LINK        NA    NA A1648                 O   ALA A 639     1555   1555  2.34
LINK        NA    NA B1648                 O   ASN B 533     1555   1555  2.43
LINK        NA    NA B1648                 O   ASN B 528     1555   1555  2.31
LINK        NA    NA B1648                 O   ALA B 639     1555   1555  2.26
LINK        NA    NA B1648                 OE1BGLU B 640     1555   1555  2.34
LINK        NA    NA B1648                 O   THR B 536     1555   1555  2.46
LINK        NA    NA C1648                 O   ASN C 528     1555   1555  2.41
LINK        NA    NA C1648                 O   ASN C 533     1555   1555  2.29
LINK        NA    NA C1648                 O   THR C 536     1555   1555  2.39
CISPEP   1 ALA A   93    PRO A   94          0         3.20
CISPEP   2 ALA A  124    PRO A  125          0        -6.99
CISPEP   3 TYR A  550    PRO A  551          0         2.34
CISPEP   4 GLY A  596    PRO A  597          0         0.65
CISPEP   5 ALA B   93    PRO B   94          0         8.54
CISPEP   6 ALA B  124    PRO B  125          0        -2.95
CISPEP   7 TYR B  550    PRO B  551          0         0.08
CISPEP   8 GLY B  596    PRO B  597          0         2.23
CISPEP   9 ALA C   93    PRO C   94          0        11.17
CISPEP  10 ALA C  124    PRO C  125          0        -1.17
CISPEP  11 TYR C  550    PRO C  551          0         4.51
CISPEP  12 GLY C  596    PRO C  597          0        13.21
SITE     1 AC1  8 GLU A 522  HIS A 539  TRP A 542  ARG A 572
SITE     2 AC1  8 GLU A 578  TYR A 635  HOH A2358  HOH A2359
SITE     1 AC2  8 GLU B 522  HIS B 539  TRP B 542  ARG B 572
SITE     2 AC2  8 TYR B 635  HOH B2487  HOH B2488  HOH C2635
SITE     1 AC3  6 GLU C 522  HIS C 539  TRP C 542  ARG C 572
SITE     2 AC3  6 TYR C 635  HOH C2645
SITE     1 AC4  6 ASN A 528  ASP A 531  ASN A 533  THR A 536
SITE     2 AC4  6 ALA A 639  GLU A 640
SITE     1 AC5  6 ASN B 528  ASP B 531  ASN B 533  THR B 536
SITE     2 AC5  6 ALA B 639  GLU B 640
SITE     1 AC6  6 ASN C 528  ASP C 531  ASN C 533  THR C 536
SITE     2 AC6  6 ALA C 639  GLU C 640
SITE     1 AC7  6 ARG A  68  ARG A 276  ARG A 342  TYR A 370
SITE     2 AC7  6 HOH A2360  HOH A2361
SITE     1 AC8  4 ARG B  68  ARG B 276  ARG B 342  TYR B 370
SITE     1 AC9  7 ARG C  68  ASP C  92  ARG C 276  ARG C 342
SITE     2 AC9  7 TYR C 370  HOH C2356  HOH C2646
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