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PDBsum entry 3gvl

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Hydrolase PDB id
3gvl
Jmol
Contents
Protein chain
670 a.a.
Ligands
SLB
SLB-SIA
Waters ×1401
HEADER    HYDROLASE                               31-MAR-09   3GVL
TITLE     CRYSTAL STRUCTURE OF ENDO-NEURAMINIDASENF
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
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   06-JUL-11 3GVL    1       TITLE
REVDAT   2   28-APR-10 3GVL    1       JRNL
REVDAT   1   02-MAR-10 3GVL    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.    1.41 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) : 1.41
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.64
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 170020
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) : 0.169
REMARK   3   R VALUE            (WORKING SET) : 0.169
REMARK   3   FREE R VALUE                     : 0.188
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 8949
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) : 1.41
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.45
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12566
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480
REMARK   3   BIN FREE R VALUE SET COUNT          : 662
REMARK   3   BIN FREE R VALUE                    : 0.2770
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5259
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 62
REMARK   3   SOLVENT ATOMS            : 1401
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.01
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.07000
REMARK   3    B22 (A**2) : -0.07000
REMARK   3    B33 (A**2) : 0.10000
REMARK   3    B12 (A**2) : -0.03000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.053
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.054
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.038
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.985
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5763 ; 0.008 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7937 ; 1.434 ; 1.946
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   768 ; 8.071 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   284 ;33.280 ;23.803
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   890 ;11.467 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    39 ;13.200 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   862 ; 0.140 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4587 ; 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):  3483 ; 0.470 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5707 ; 0.876 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2280 ; 1.419 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2180 ; 2.144 ; 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  : NULL
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3GVL COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB052361.
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   : 184838
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.410
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.640
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.07400
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) : 1.41
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.53000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
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       59.54600
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.37890
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       58.66033
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       59.54600
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       34.37890
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       58.66033
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       59.54600
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       34.37890
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       58.66033
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       68.75780
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      117.32067
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       68.75780
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      117.32067
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       68.75780
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      117.32067
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: 45750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 66240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -189.0 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      119.09200
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       59.54600
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      103.13670
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 A1370  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A1775  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 978  LIES ON A SPECIAL POSITION.
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     HIS A  350   CA   CB   CG   ND1  CD2  CE1  NE2
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     2     O6   SIA A     1              2.11
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    GLY A 504   N   -  CA  -  C   ANGL. DEV. =  18.6 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    GLU A 310       -4.56     74.90
REMARK 500    ASP A 321       76.55   -152.79
REMARK 500    ASN A 338       -2.66     72.62
REMARK 500    SER A 347     -158.05   -131.66
REMARK 500    HIS A 350       85.19    -68.98
REMARK 500    ARG A 354       16.72     58.08
REMARK 500    SER A 528      160.18     80.02
REMARK 500    HIS A 624       32.92     70.98
REMARK 500    HIS A 628       -5.55     72.07
REMARK 500    VAL A 704       64.73     33.71
REMARK 500    ASP A 711     -126.18     53.53
REMARK 500    SER A 740     -131.11     50.87
REMARK 500    SER A 806      -19.17   -145.63
REMARK 500    SER A 808       70.01     59.12
REMARK 500    SER A 878       -8.85     76.81
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 MET A  503     GLY A  504                  114.76
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 A 913        DISTANCE =  9.70 ANGSTROMS
REMARK 525    HOH A 914        DISTANCE =  7.63 ANGSTROMS
REMARK 525    HOH A 915        DISTANCE =  6.54 ANGSTROMS
REMARK 525    HOH A 916        DISTANCE =  7.11 ANGSTROMS
REMARK 525    HOH A 944        DISTANCE =  5.06 ANGSTROMS
REMARK 525    HOH A 949        DISTANCE =  7.12 ANGSTROMS
REMARK 525    HOH A 977        DISTANCE =  6.60 ANGSTROMS
REMARK 525    HOH A 979        DISTANCE =  6.54 ANGSTROMS
REMARK 525    HOH A 981        DISTANCE =  7.22 ANGSTROMS
REMARK 525    HOH A 984        DISTANCE =  5.54 ANGSTROMS
REMARK 525    HOH A 986        DISTANCE =  5.89 ANGSTROMS
REMARK 525    HOH A 990        DISTANCE =  6.45 ANGSTROMS
REMARK 525    HOH A 991        DISTANCE =  7.37 ANGSTROMS
REMARK 525    HOH A 996        DISTANCE =  7.03 ANGSTROMS
REMARK 525    HOH A1002        DISTANCE =  8.91 ANGSTROMS
REMARK 525    HOH A1004        DISTANCE =  7.69 ANGSTROMS
REMARK 525    HOH A1010        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH A1068        DISTANCE =  5.73 ANGSTROMS
REMARK 525    HOH A1076        DISTANCE =  5.39 ANGSTROMS
REMARK 525    HOH A1081        DISTANCE =  6.22 ANGSTROMS
REMARK 525    HOH A1082        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH A1086        DISTANCE =  5.49 ANGSTROMS
REMARK 525    HOH A1096        DISTANCE =  5.39 ANGSTROMS
REMARK 525    HOH A1100        DISTANCE =  5.52 ANGSTROMS
REMARK 525    HOH A1103        DISTANCE =  6.13 ANGSTROMS
REMARK 525    HOH A1104        DISTANCE =  8.62 ANGSTROMS
REMARK 525    HOH A1109        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH A1111        DISTANCE =  5.86 ANGSTROMS
REMARK 525    HOH A1112        DISTANCE =  5.28 ANGSTROMS
REMARK 525    HOH A1113        DISTANCE =  5.47 ANGSTROMS
REMARK 525    HOH A1175        DISTANCE =  6.18 ANGSTROMS
REMARK 525    HOH A1177        DISTANCE =  6.75 ANGSTROMS
REMARK 525    HOH A1196        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH A1224        DISTANCE =  6.00 ANGSTROMS
REMARK 525    HOH A1281        DISTANCE =  7.83 ANGSTROMS
REMARK 525    HOH A1283        DISTANCE =  7.18 ANGSTROMS
REMARK 525    HOH A1287        DISTANCE =  6.19 ANGSTROMS
REMARK 525    HOH A1288        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH A1291        DISTANCE =  6.30 ANGSTROMS
REMARK 525    HOH A1297        DISTANCE =  7.25 ANGSTROMS
REMARK 525    HOH A1299        DISTANCE =  5.99 ANGSTROMS
REMARK 525    HOH A1301        DISTANCE =  6.16 ANGSTROMS
REMARK 525    HOH A1304        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH A1393        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH A1655        DISTANCE =  5.64 ANGSTROMS
REMARK 525    HOH A1679        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH A1712        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH A1722        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH A1726        DISTANCE =  5.46 ANGSTROMS
REMARK 525    HOH A1733        DISTANCE =  5.20 ANGSTROMS
REMARK 525    HOH A1759        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH A1768        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH A1793        DISTANCE =  5.06 ANGSTROMS
REMARK 525    HOH A1816        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH A1824        DISTANCE =  7.33 ANGSTROMS
REMARK 525    HOH A1828        DISTANCE =  5.42 ANGSTROMS
REMARK 525    HOH A1829        DISTANCE =  5.41 ANGSTROMS
REMARK 525    HOH A1844        DISTANCE =  5.36 ANGSTROMS
REMARK 525    HOH A1846        DISTANCE =  5.54 ANGSTROMS
REMARK 525    HOH A1848        DISTANCE =  6.37 ANGSTROMS
REMARK 525    HOH A1861        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH A1880        DISTANCE =  6.76 ANGSTROMS
REMARK 525    HOH A1887        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH A1895        DISTANCE =  5.39 ANGSTROMS
REMARK 525    HOH A1898        DISTANCE =  5.63 ANGSTROMS
REMARK 525    HOH A1900        DISTANCE =  6.54 ANGSTROMS
REMARK 525    HOH A1902        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH A1903        DISTANCE =  6.26 ANGSTROMS
REMARK 525    HOH A1909        DISTANCE =  6.83 ANGSTROMS
REMARK 525    HOH A1916        DISTANCE =  8.63 ANGSTROMS
REMARK 525    HOH A1918        DISTANCE =  6.88 ANGSTROMS
REMARK 525    HOH A1923        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH A1924        DISTANCE =  8.76 ANGSTROMS
REMARK 525    HOH A1925        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH A1926        DISTANCE =  7.11 ANGSTROMS
REMARK 525    HOH A1927        DISTANCE =  7.52 ANGSTROMS
REMARK 525    HOH A2010        DISTANCE =  5.41 ANGSTROMS
REMARK 525    HOH A2013        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH A2018        DISTANCE =  7.69 ANGSTROMS
REMARK 525    HOH A2022        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH A2025        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH A2026        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH A2052        DISTANCE =  7.12 ANGSTROMS
REMARK 525    HOH A2058        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH A2064        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH A2066        DISTANCE =  5.32 ANGSTROMS
REMARK 525    HOH A2067        DISTANCE =  6.15 ANGSTROMS
REMARK 525    HOH A2069        DISTANCE = 10.09 ANGSTROMS
REMARK 525    HOH A2071        DISTANCE =  5.14 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 911
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SLB A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GVJ   RELATED DB: PDB
REMARK 900 RELATED ID: 3GVK   RELATED DB: PDB
DBREF  3GVL A  246   910  UNP    Q858B1   Q858B1_BPK1F   246    910
SEQADV 3GVL VAL A  241  UNP  Q858B1              EXPRESSION TAG
SEQADV 3GVL PRO A  242  UNP  Q858B1              EXPRESSION TAG
SEQADV 3GVL ARG A  243  UNP  Q858B1              EXPRESSION TAG
SEQADV 3GVL GLY A  244  UNP  Q858B1              EXPRESSION TAG
SEQADV 3GVL SER A  245  UNP  Q858B1              EXPRESSION TAG
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 ARG 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  A 911      21
HET    SLB  A   2      21
HET    SIA  A   1      20
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   3  SIA    C11 H19 N O9
FORMUL   4  HOH   *1401(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  GLY A 644   O  PHE A 669
SHEET    8   A 8 PHE A 633  VAL A 636 -1  N  ALA A 634   O  ILE A 641
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  LYS A 751   N  GLU A 315
SHEET    3   C 4 TYR A 713  GLY A 720 -1  N  PHE A 718   O  TYR A 748
SHEET    4   C 4 GLY A 703  LYS A 710 -1  N  SER A 706   O  MET A 717
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  ARG A 513   N  ASP A 420
SHEET    1   H 4 ARG A 425  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  ASN A 458   O  GLY A 504
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 556   N  PHE A 537
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  LEU A 620   N  LEU A 607
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 A   2                 C2  SIA A   1     1555   1555  1.35
CISPEP   1 GLN A  330    ASP A  331          0       -25.01
CISPEP   2 TYR A  382    PRO A  383          0         7.54
CISPEP   3 ALA A  547    PRO A  548          0        -4.62
SITE     1 AC1 16 HOH A  96  HOH A 156  HOH A 231  TYR A 821
SITE     2 AC1 16 ARG A 837  ILE A 839  THR A 846  SER A 848
SITE     3 AC1 16 GLN A 853  ASN A 870  HOH A1007  HOH A1594
SITE     4 AC1 16 HOH A1660  HOH A1697  HOH A1938  HOH A1972
SITE     1 AC2 14 SIA A   1  HOH A 111  SER A 462  ALA A 463
SITE     2 AC2 14 THR A 465  GLY A 466  VAL A 467  SER A 468
SITE     3 AC2 14 HOH A1042  HOH A1162  HOH A1376  HOH A1381
SITE     4 AC2 14 HOH A1630  HOH A1962
SITE     1 AC3  9 SLB A   2  HOH A 111  SER A 460  ASN A 461
SITE     2 AC3  9 SER A 468  THR A 728  HOH A1069  HOH A1394
SITE     3 AC3  9 HOH A1630
CRYST1  119.092  119.092  175.981  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