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PDBsum entry 3gvj

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Hydrolase PDB id
3gvj
Jmol
Contents
Protein chain
670 a.a.
Ligands
SLB-SIA-SIA-SIA-
SIA
SIA-SIA-SIA-SLB
Waters ×850
HEADER    HYDROLASE                               31-MAR-09   3GVJ
TITLE     CRYSTAL STRUCTURE OF AN ENDO-NEURAMINIDASENF MUTANT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ENDO-N-ACETYLNEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 246-910;
COMPND   5 SYNONYM: ENDO-ALPHA-SIALIDASE, GP17 PROTEIN;
COMPND   6 EC: 3.2.1.129;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE K1F;
SOURCE   3 ORGANISM_COMMON: BACTERIOPHAGE K1F;
SOURCE   4 ORGANISM_TAXID: 344021;
SOURCE   5 GENE: SIA, 17, 17.0;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    ENDO-NEURAMINIDASE; POLYSIALIC ACID; TRIPLE-BETA HELIX, GLYCOSIDASE,
KEYWDS   2 HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.C.SCHULZ,A.DICKMANNS,R.FICNER
REVDAT   3   13-JUL-11 3GVJ    1       VERSN
REVDAT   2   28-APR-10 3GVJ    1       JRNL
REVDAT   1   02-MAR-10 3GVJ    0
JRNL        AUTH   E.C.SCHULZ,D.SCHWARZER,M.FRANK,K.STUMMEYER,M.MUHLENHOFF,
JRNL        AUTH 2 A.DICKMANNS,R.GERARDY-SCHAHN,R.FICNER
JRNL        TITL   STRUCTURAL BASIS FOR THE RECOGNITION AND CLEAVAGE OF
JRNL        TITL 2 POLYSIALIC ACID BY THE BACTERIOPHAGE K1F TAILSPIKE PROTEIN
JRNL        TITL 3 ENDONF.
JRNL        REF    J.MOL.BIOL.                   V. 397   341 2010
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   20096705
JRNL        DOI    10.1016/J.JMB.2010.01.028
REMARK   2
REMARK   2 RESOLUTION.    1.48 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0039
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) : 1.48
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 147036
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) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.194
REMARK   3   FREE R VALUE                     : 0.216
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 7739
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) : 1.48
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.52
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10697
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780
REMARK   3   BIN FREE R VALUE SET COUNT          : 564
REMARK   3   BIN FREE R VALUE                    : 0.2880
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5253
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 182
REMARK   3   SOLVENT ATOMS            : 850
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) : 16.44
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.24000
REMARK   3    B22 (A**2) : 0.24000
REMARK   3    B33 (A**2) : -0.37000
REMARK   3    B12 (A**2) : 0.12000
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): 0.067
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.068
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.050
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.524
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5787 ; 0.009 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7925 ; 1.471 ; 1.967
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   723 ; 7.095 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   281 ;33.346 ;23.488
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   853 ;11.887 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    43 ;13.912 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   866 ; 0.131 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4567 ; 0.006 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3431 ; 0.515 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5587 ; 0.880 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2356 ; 1.505 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2319 ; 2.228 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 3
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   245        A   275
REMARK   3    ORIGIN FOR THE GROUP (A):  50.3220  47.5632  33.1273
REMARK   3    T TENSOR
REMARK   3      T11:   0.0038 T22:   0.0287
REMARK   3      T33:   0.0096 T12:   0.0001
REMARK   3      T13:  -0.0009 T23:  -0.0093
REMARK   3    L TENSOR
REMARK   3      L11:   1.7031 L22:   1.0908
REMARK   3      L33:   0.6063 L12:  -0.2032
REMARK   3      L13:  -0.1706 L23:  -0.0238
REMARK   3    S TENSOR
REMARK   3      S11:   0.0049 S12:  -0.2146 S13:   0.0920
REMARK   3      S21:   0.0381 S22:   0.0018 S23:  -0.0764
REMARK   3      S31:   0.0076 S32:   0.0233 S33:  -0.0067
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   777        A   910
REMARK   3    ORIGIN FOR THE GROUP (A):  61.5597  35.8090 -44.5517
REMARK   3    T TENSOR
REMARK   3      T11:   0.0045 T22:   0.0025
REMARK   3      T33:   0.0027 T12:  -0.0011
REMARK   3      T13:   0.0010 T23:   0.0021
REMARK   3    L TENSOR
REMARK   3      L11:   0.1403 L22:   0.1475
REMARK   3      L33:   0.4466 L12:  -0.0308
REMARK   3      L13:   0.0242 L23:  -0.0483
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0046 S12:   0.0187 S13:   0.0171
REMARK   3      S21:  -0.0225 S22:  -0.0019 S23:  -0.0132
REMARK   3      S31:  -0.0078 S32:   0.0046 S33:   0.0064
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   423        A   511
REMARK   3    ORIGIN FOR THE GROUP (A):  34.4063   3.4790 -12.3910
REMARK   3    T TENSOR
REMARK   3      T11:   0.0241 T22:   0.0099
REMARK   3      T33:   0.0473 T12:   0.0007
REMARK   3      T13:  -0.0335 T23:   0.0013
REMARK   3    L TENSOR
REMARK   3      L11:   0.8052 L22:   0.5553
REMARK   3      L33:   0.4579 L12:   0.1200
REMARK   3      L13:   0.5034 L23:   0.1069
REMARK   3    S TENSOR
REMARK   3      S11:   0.0732 S12:   0.0084 S13:  -0.1108
REMARK   3      S21:   0.0280 S22:  -0.0023 S23:  -0.0300
REMARK   3      S31:   0.0405 S32:  -0.0319 S33:  -0.0709
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES      : RESIDUAL ONLY
REMARK   4
REMARK   4 3GVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB052359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : BESSY
REMARK 200  BEAMLINE                       : 14.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 164778
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.9
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.09000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50
REMARK 200  COMPLETENESS FOR SHELL     (%) : 46.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.35900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 8000, 0.1M TRIS/HCL, PH
REMARK 280  7.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290       9555   -X+Y+1/3,-X+2/3,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        0.00000
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        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.54500
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.37832
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       58.66000
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       59.54500
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       34.37832
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       58.66000
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       59.54500
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       34.37832
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       58.66000
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       68.75664
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      117.32000
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       68.75664
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      117.32000
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       68.75664
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      117.32000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 51920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -145.0 KCAL/MOL
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   BIOMT1   2 -0.500000 -0.866025  0.000000      119.09000
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       59.54500
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      103.13497
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A1420  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A1485  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A1096  LIES ON A SPECIAL POSITION.
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   O8   SLB A  2001     O6   SIA A  2002              2.19
REMARK 500   O6   SIA A  2008     O8   SLB A  2009              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    TYR A 296   CD1   TYR A 296   CE1    -0.090
REMARK 500    GLU A 297   CD    GLU A 297   OE2    -0.067
REMARK 500    TYR A 344   CE1   TYR A 344   CZ     -0.081
REMARK 500    TYR A 344   CE2   TYR A 344   CD2    -0.097
REMARK 500    GLU A 373   CD    GLU A 373   OE1    -0.080
REMARK 500    GLY A 504   C     THR A 505   N       0.149
REMARK 500    GLU A 576   CD    GLU A 576   OE2    -0.068
REMARK 500    TYR A 661   CZ    TYR A 661   CE2    -0.088
REMARK 500    GLY A 851   C     GLY A 851   O      -0.096
REMARK 500    GLU A 873   CD    GLU A 873   OE2    -0.071
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    MET A 503   CA  -  C   -  N   ANGL. DEV. =  30.1 DEGREES
REMARK 500    MET A 503   O   -  C   -  N   ANGL. DEV. = -28.3 DEGREES
REMARK 500    LEU A 620   CA  -  CB  -  CG  ANGL. DEV. =  17.8 DEGREES
REMARK 500    ARG A 865   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    VAL A 251      -42.25   -131.78
REMARK 500    ASP A 285       85.72    -69.11
REMARK 500    GLU A 310       -3.95     75.63
REMARK 500    ASP A 321       76.75   -153.01
REMARK 500    ASN A 338       -2.35     73.02
REMARK 500    SER A 347     -156.49   -133.05
REMARK 500    ARG A 354       15.81     58.19
REMARK 500    ARG A 396       59.48     39.93
REMARK 500    SER A 528      163.23     80.37
REMARK 500    ASP A 533     -157.11   -156.50
REMARK 500    HIS A 624       34.18     73.82
REMARK 500    HIS A 628       -6.18     73.02
REMARK 500    TYR A 665       79.05   -118.57
REMARK 500    VAL A 704       68.82     33.05
REMARK 500    ASP A 711     -127.32     53.61
REMARK 500    SER A 740     -130.47     50.84
REMARK 500    SER A 806      -21.62   -147.23
REMARK 500    SER A 808       68.45     63.35
REMARK 500    SER A 878       -7.32     75.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ARG A  243     GLY A  244                   39.08
REMARK 500 GLN A  330     ASP A  331                  -30.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    MET A 503        -13.51
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    VAL A 704        24.5      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A1096        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH A1102        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH A1229        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH A1287        DISTANCE =  5.84 ANGSTROMS
REMARK 525    HOH A1335        DISTANCE =  5.01 ANGSTROMS
REMARK 525    HOH A1339        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH A1378        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH A1462        DISTANCE =  5.47 ANGSTROMS
REMARK 525    HOH A1464        DISTANCE =  5.69 ANGSTROMS
REMARK 525    HOH A1474        DISTANCE =  5.42 ANGSTROMS
REMARK 525    HOH A1483        DISTANCE =  6.25 ANGSTROMS
REMARK 525    HOH A1485        DISTANCE =  6.05 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SLB A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A 2008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SLB A 2009
DBREF  3GVJ A  246   910  UNP    Q858B1   Q858B1_BPK1F   246    910
SEQADV 3GVJ VAL A  241  UNP  Q858B1              EXPRESSION TAG
SEQADV 3GVJ PRO A  242  UNP  Q858B1              EXPRESSION TAG
SEQADV 3GVJ ARG A  243  UNP  Q858B1              EXPRESSION TAG
SEQADV 3GVJ GLY A  244  UNP  Q858B1              EXPRESSION TAG
SEQADV 3GVJ SER A  245  UNP  Q858B1              EXPRESSION TAG
SEQADV 3GVJ ALA A  647  UNP  Q858B1    ARG   647 ENGINEERED
SEQRES   1 A  670  VAL PRO ARG GLY SER ALA LYS GLY ASP GLY VAL THR ASP
SEQRES   2 A  670  ASP THR ALA ALA LEU THR SER ALA LEU ASN ASP THR PRO
SEQRES   3 A  670  VAL GLY GLN LYS ILE ASN GLY ASN GLY LYS THR TYR LYS
SEQRES   4 A  670  VAL THR SER LEU PRO ASP ILE SER ARG PHE ILE ASN THR
SEQRES   5 A  670  ARG PHE VAL TYR GLU ARG ILE PRO GLY GLN PRO LEU TYR
SEQRES   6 A  670  TYR ALA SER GLU GLU PHE VAL GLN GLY GLU LEU PHE LYS
SEQRES   7 A  670  ILE THR ASP THR PRO TYR TYR ASN ALA TRP PRO GLN ASP
SEQRES   8 A  670  LYS ALA PHE VAL TYR GLU ASN VAL ILE TYR ALA PRO TYR
SEQRES   9 A  670  MET GLY SER ASP ARG HIS GLY VAL SER ARG LEU HIS VAL
SEQRES  10 A  670  SER TRP VAL LYS SER GLY ASP ASP GLY GLN THR TRP SER
SEQRES  11 A  670  THR PRO GLU TRP LEU THR ASP LEU HIS PRO ASP TYR PRO
SEQRES  12 A  670  THR VAL ASN TYR HIS CYS MET SER MET GLY VAL CYS ARG
SEQRES  13 A  670  ASN ARG LEU PHE ALA MET ILE GLU THR ARG THR LEU ALA
SEQRES  14 A  670  LYS ASN ALA LEU THR ASN CYS ALA LEU TRP ASP ARG PRO
SEQRES  15 A  670  MET SER ARG SER LEU HIS LEU THR GLY GLY ILE THR LYS
SEQRES  16 A  670  ALA ALA ASN GLN ARG TYR ALA THR ILE HIS VAL PRO ASP
SEQRES  17 A  670  HIS GLY LEU PHE VAL GLY ASP PHE VAL ASN PHE SER ASN
SEQRES  18 A  670  SER ALA VAL THR GLY VAL SER GLY ASP MET THR VAL ALA
SEQRES  19 A  670  THR VAL ILE ASP LYS ASP ASN PHE THR VAL LEU THR PRO
SEQRES  20 A  670  ASN GLN GLN THR SER ASP LEU ASN ASN ALA GLY LYS ASN
SEQRES  21 A  670  TRP HIS MET GLY THR SER PHE HIS LYS SER PRO TRP ARG
SEQRES  22 A  670  LYS THR ASP LEU GLY LEU ILE PRO SER VAL THR GLU VAL
SEQRES  23 A  670  HIS SER PHE ALA THR ILE ASP ASN ASN GLY PHE ALA MET
SEQRES  24 A  670  GLY TYR HIS GLN GLY ASP VAL ALA PRO ARG GLU VAL GLY
SEQRES  25 A  670  LEU PHE TYR PHE PRO ASP ALA PHE ASN SER PRO SER ASN
SEQRES  26 A  670  TYR VAL ARG ARG GLN ILE PRO SER GLU TYR GLU PRO ASP
SEQRES  27 A  670  ALA SER GLU PRO CYS ILE LYS TYR TYR ASP GLY VAL LEU
SEQRES  28 A  670  TYR LEU ILE THR ARG GLY THR ARG GLY ASP ARG LEU GLY
SEQRES  29 A  670  SER SER LEU HIS ARG SER ARG ASP ILE GLY GLN THR TRP
SEQRES  30 A  670  GLU SER LEU ARG PHE PRO HIS ASN VAL HIS HIS THR THR
SEQRES  31 A  670  LEU PRO PHE ALA LYS VAL GLY ASP ASP LEU ILE MET PHE
SEQRES  32 A  670  GLY SER GLU ALA ALA GLU ASN GLU TRP GLU ALA GLY ALA
SEQRES  33 A  670  PRO ASP ASP ARG TYR LYS ALA SER TYR PRO ARG THR PHE
SEQRES  34 A  670  TYR ALA ARG LEU ASN VAL ASN ASN TRP ASN ALA ASP ASP
SEQRES  35 A  670  ILE GLU TRP VAL ASN ILE THR ASP GLN ILE TYR GLN GLY
SEQRES  36 A  670  GLY ILE VAL ASN SER GLY VAL GLY VAL GLY SER VAL VAL
SEQRES  37 A  670  VAL LYS ASP ASN TYR ILE TYR TYR MET PHE GLY GLY GLU
SEQRES  38 A  670  ASP HIS PHE ASN PRO TRP THR TYR GLY ASP ASN SER ALA
SEQRES  39 A  670  LYS ASP PRO PHE LYS SER ASP GLY HIS PRO SER ASP LEU
SEQRES  40 A  670  TYR CYS TYR LYS MET LYS ILE GLY PRO ASP ASN ARG VAL
SEQRES  41 A  670  SER ARG ASP PHE ARG TYR GLY ALA VAL PRO ASN ARG ALA
SEQRES  42 A  670  VAL PRO VAL PHE PHE ASP THR ASN GLY VAL ARG THR VAL
SEQRES  43 A  670  PRO ALA PRO MET GLU PHE THR GLY ASP LEU GLY LEU GLY
SEQRES  44 A  670  HIS VAL THR ILE ARG ALA SER THR SER SER ASN ILE ARG
SEQRES  45 A  670  SER GLU VAL LEU MET GLU GLY GLU TYR GLY PHE ILE GLY
SEQRES  46 A  670  LYS SER ILE PRO THR ASP ASN PRO ALA GLY GLN ARG ILE
SEQRES  47 A  670  ILE PHE CYS GLY GLY GLU GLY THR SER SER THR THR GLY
SEQRES  48 A  670  ALA GLN ILE THR LEU TYR GLY ALA ASN ASN THR ASP SER
SEQRES  49 A  670  ARG ARG ILE VAL TYR ASN GLY ASP GLU HIS LEU PHE GLN
SEQRES  50 A  670  SER ALA ASP VAL LYS PRO TYR ASN ASP ASN VAL THR ALA
SEQRES  51 A  670  LEU GLY GLY PRO SER ASN ARG PHE THR THR ALA TYR LEU
SEQRES  52 A  670  GLY SER ASN PRO ILE VAL THR
HET    SLB  A2001      21
HET    SIA  A2002      20
HET    SIA  A2003      20
HET    SIA  A2004      20
HET    SIA  A2005      20
HET    SIA  A2006      20
HET    SIA  A2007      20
HET    SIA  A2008      20
HET    SLB  A2009      21
HETNAM     SLB 5-N-ACETYL-BETA-D-NEURAMINIC ACID
HETNAM     SIA O-SIALIC ACID
HETSYN     SLB BETA-SIALIC ACID
FORMUL   2  SLB    2(C11 H19 N O9)
FORMUL   2  SIA    7(C11 H19 N O9)
FORMUL   4  HOH   *850(H2 O)
HELIX    1   1 ASP A  254  THR A  265  1                                  12
HELIX    2   2 ASP A  285  SER A  287  5                                   3
HELIX    3   3 PRO A  572  GLU A  576  5                                   5
HELIX    4   4 ASN A  832  GLY A  835  5                                   4
HELIX    5   5 SER A  847  GLY A  851  5                                   5
SHEET    1   A 8 ASP A 249  ASP A 253  0
SHEET    2   A 8 THR A 277  LYS A 279  1  O  THR A 277   N  GLY A 250
SHEET    3   A 8 ARG A 293  TYR A 296  1  O  ARG A 293   N  TYR A 278
SHEET    4   A 8 LEU A 304  ALA A 307 -1  O  TYR A 306   N  PHE A 294
SHEET    5   A 8 VAL A 686  ASP A 690  1  O  ASN A 687   N  TYR A 305
SHEET    6   A 8 ARG A 667  ASN A 674 -1  N  TYR A 670   O  VAL A 686
SHEET    7   A 8 ASP A 639  SER A 645 -1  N  MET A 642   O  ALA A 671
SHEET    8   A 8 PHE A 633  VAL A 636 -1  N  VAL A 636   O  ASP A 639
SHEET    1   B 2 ILE A 271  ASN A 272  0
SHEET    2   B 2 PHE A 289  ILE A 290  1  O  ILE A 290   N  ILE A 271
SHEET    1   C 4 GLY A 314  LYS A 318  0
SHEET    2   C 4 ASP A 746  LYS A 753 -1  O  CYS A 749   N  PHE A 317
SHEET    3   C 4 TYR A 713  GLY A 720 -1  N  ILE A 714   O  MET A 752
SHEET    4   C 4 GLY A 703  LYS A 710 -1  N  VAL A 708   O  TYR A 715
SHEET    1   D 3 TYR A 325  ALA A 327  0
SHEET    2   D 3 VAL A 339  SER A 347 -1  O  SER A 347   N  TYR A 325
SHEET    3   D 3 PHE A 334  TYR A 336 -1  N  PHE A 334   O  TYR A 341
SHEET    1   E 4 TYR A 325  ALA A 327  0
SHEET    2   E 4 VAL A 339  SER A 347 -1  O  SER A 347   N  TYR A 325
SHEET    3   E 4 HIS A 356  SER A 362 -1  O  VAL A 360   N  ALA A 342
SHEET    4   E 4 GLU A 373  TRP A 374 -1  O  GLU A 373   N  TRP A 359
SHEET    1   F 3 VAL A 385  HIS A 388  0
SHEET    2   F 3 ARG A 398  THR A 407 -1  O  GLU A 404   N  HIS A 388
SHEET    3   F 3 MET A 392  CYS A 395 -1  N  GLY A 393   O  PHE A 400
SHEET    1   G 4 VAL A 385  HIS A 388  0
SHEET    2   G 4 ARG A 398  THR A 407 -1  O  GLU A 404   N  HIS A 388
SHEET    3   G 4 LEU A 413  PRO A 422 -1  O  THR A 414   N  THR A 405
SHEET    4   G 4 ARG A 513  GLY A 518 -1  O  LEU A 517   N  CYS A 416
SHEET    1   H 4 SER A 426  THR A 430  0
SHEET    2   H 4 ASN A 500  THR A 505 -1  O  MET A 503   N  LEU A 427
SHEET    3   H 4 PHE A 456  SER A 460 -1  N  SER A 460   O  HIS A 502
SHEET    4   H 4 GLY A 469  THR A 472 -1  O  MET A 471   N  VAL A 457
SHEET    1   I 5 THR A 475  ASP A 478  0
SHEET    2   I 5 ASN A 481  LEU A 485 -1  O  THR A 483   N  THR A 475
SHEET    3   I 5 TYR A 441  HIS A 445 -1  N  ILE A 444   O  PHE A 482
SHEET    4   I 5 ILE A 433  LYS A 435 -1  N  THR A 434   O  THR A 443
SHEET    5   I 5 LEU A 494  ASN A 495 -1  O  LEU A 494   N  LYS A 435
SHEET    1   J 4 GLU A 525  THR A 531  0
SHEET    2   J 4 PHE A 537  GLN A 543 -1  O  ALA A 538   N  ALA A 530
SHEET    3   J 4 GLU A 550  PHE A 556 -1  O  PHE A 554   N  MET A 539
SHEET    4   J 4 VAL A 567  GLN A 570 -1  O  ARG A 569   N  LEU A 553
SHEET    1   K 4 ALA A 579  TYR A 587  0
SHEET    2   K 4 VAL A 590  GLY A 597 -1  O  TYR A 592   N  LYS A 585
SHEET    3   K 4 SER A 606  SER A 610 -1  O  SER A 610   N  LEU A 591
SHEET    4   K 4 GLU A 618  ARG A 621 -1  O  GLU A 618   N  ARG A 609
SHEET    1   L 2 PHE A 777  PHE A 778  0
SHEET    2   L 2 ARG A 784  THR A 785 -1  O  THR A 785   N  PHE A 777
SHEET    1   M 3 ARG A 837  CYS A 841  0
SHEET    2   M 3 GLN A 853  TYR A 857 -1  O  ILE A 854   N  PHE A 840
SHEET    3   M 3 ILE A 867  ASN A 870 -1  O  ASN A 870   N  GLN A 853
LINK         O8  SLB A2001                 C2  SIA A2002     1555   1555  1.45
LINK         O8  SIA A2002                 C2  SIA A2003     1555   1555  1.45
LINK         O8  SIA A2003                 C2  SIA A2004     1555   1555  1.44
LINK         O8  SIA A2004                 C2  SIA A2005     1555   1555  1.43
LINK         C2  SIA A2006                 O8  SIA A2007     1555   1555  1.39
LINK         C2  SIA A2007                 O8  SIA A2008     1555   1555  1.44
LINK         C2  SIA A2008                 O8  SLB A2009     1555   1555  1.43
CISPEP   1 TYR A  382    PRO A  383          0         8.90
CISPEP   2 MET A  503    GLY A  504          0        -5.04
CISPEP   3 ALA A  547    PRO A  548          0        -2.34
SITE     1 AC1  2 HOH A1267  SIA A2002
SITE     1 AC2 13 HOH A 162  SER A 462  VAL A 464  THR A 465
SITE     2 AC2 13 GLY A 466  VAL A 467  SER A 468  HOH A1091
SITE     3 AC2 13 HOH A1166  HOH A1267  HOH A1324  SLB A2001
SITE     4 AC2 13 SIA A2003
SITE     1 AC3 14 HOH A  34  HOH A 150  HOH A 218  PHE A 459
SITE     2 AC3 14 SER A 460  ASN A 461  SER A 468  THR A 728
SITE     3 AC3 14 HOH A1148  HOH A1188  HOH A1205  HOH A1215
SITE     4 AC3 14 SIA A2002  SIA A2004
SITE     1 AC4  7 HOH A 174  ASN A 461  HOH A1043  HOH A1217
SITE     2 AC4  7 HOH A1281  SIA A2003  SIA A2005
SITE     1 AC5  7 ASN A 461  LYS A 499  ASN A 500  HIS A 502
SITE     2 AC5  7 HOH A1217  HOH A1428  SIA A2004
SITE     1 AC6 10 HOH A  16  SER A 808  ILE A 811  ARG A 812
SITE     2 AC6 10 TYR A 821  THR A 846  HOH A1000  HOH A1018
SITE     3 AC6 10 HOH A1500  SIA A2007
SITE     1 AC7  9 HOH A  16  HOH A  69  THR A 846  SER A 847
SITE     2 AC7  9 HOH A1189  HOH A1316  HOH A1323  SIA A2006
SITE     3 AC7  9 SIA A2008
SITE     1 AC8 13 HOH A 105  HOH A 134  TYR A 821  ARG A 837
SITE     2 AC8 13 THR A 846  SER A 848  GLN A 853  HOH A1064
SITE     3 AC8 13 HOH A1111  HOH A1189  HOH A1430  SIA A2007
SITE     4 AC8 13 SLB A2009
SITE     1 AC9 11 HOH A  79  HOH A 207  SER A 848  ASN A 870
SITE     2 AC9 11 GLN A 877  SER A 878  HOH A1149  HOH A1194
SITE     3 AC9 11 HOH A1224  HOH A1318  SIA A2008
CRYST1  119.090  119.090  175.980  90.00  90.00 120.00 H 3           9
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      0.008397  0.004848  0.000000        0.00000
SCALE2      0.000000  0.009696  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005682        0.00000
      
PROCHECK
Go to PROCHECK summary
 References