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PDBsum entry 2f61

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2f61
Jmol
Contents
Protein chain
497 a.a.
Ligands
NDG
SO4 ×6
NAG-NAG
Waters ×406
HEADER    HYDROLASE                               28-NOV-05   2F61
TITLE     CRYSTAL STRUCTURE OF PARTIALLY DEGLYCOSYLATED ACID BETA-GLUCOSIDASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ACID BETA-GLUCOSIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: BETA-GLUCOCEREBROSIDASE, GLUCOSYLCERAMIDASE, D-GLUCOSYL-N-
COMPND   5 ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE, IMIGLUCERASE;
COMPND   6 EC: 3.2.1.45;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: GBA, GC;
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: CHO;
SOURCE  10 EXPRESSION_SYSTEM_CELL: OVARY
KEYWDS    ALPHA/BETA, TIM BARREL, IMMUNOGLOBULIN FOLD, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.S.HEGDE,G.GRABOWSKI
REVDAT   4   13-JUL-11 2F61    1       VERSN
REVDAT   3   24-FEB-09 2F61    1       VERSN
REVDAT   2   28-FEB-06 2F61    1       JRNL
REVDAT   1   27-DEC-05 2F61    0
JRNL        AUTH   B.LIOU,A.KAZIMIERCZUK,M.ZHANG,C.R.SCOTT,R.S.HEGDE,
JRNL        AUTH 2 G.A.GRABOWSKI
JRNL        TITL   ANALYSES OF VARIANT ACID BETA-GLUCOSIDASES: EFFECTS OF
JRNL        TITL 2 GAUCHER DISEASE MUTATIONS.
JRNL        REF    J.BIOL.CHEM.                  V. 281  4242 2006
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   16293621
JRNL        DOI    10.1074/JBC.M511110200
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.98
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 302034.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 84.6
REMARK   3   NUMBER OF REFLECTIONS             : 41894
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 SET) : 0.196
REMARK   3   FREE R VALUE                     : 0.256
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 4212
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.10
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6061
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520
REMARK   3   BIN FREE R VALUE                    : 0.3350
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 673
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7860
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 72
REMARK   3   SOLVENT ATOMS            : 406
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.10
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 13.80000
REMARK   3    B22 (A**2) : -4.35000
REMARK   3    B33 (A**2) : -9.46000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.00
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.89
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.460 ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.360 ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.840 ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.670 ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.36
REMARK   3   BSOL        : 33.85
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN.TOP
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.TOP
REMARK   3  PARAMETER FILE  3  : WATER.TOP
REMARK   3  PARAMETER FILE  4  : ION.TOP
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_REP.PARAM
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.PARAM
REMARK   3  TOPOLOGY FILE  3   : WATER_REP.PARAM
REMARK   3  TOPOLOGY FILE  4   : ION.PARAM
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2F61 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-05.
REMARK 100 THE RCSB ID CODE IS RCSB035494.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41998
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.980
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.0
REMARK 200  DATA REDUNDANCY                : 4.200
REMARK 200  R MERGE                    (I) : 0.09200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY: 1OGS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2-1.4 M AMMONIUM SULPHATE, 96 MM NA-
REMARK 280  CITRATE, 10 MM MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.77000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.77000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       54.32000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      142.21500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       54.32000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      142.21500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       45.77000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       54.32000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      142.21500
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       45.77000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       54.32000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      142.21500
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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    PRO A  32   C   -  N   -  CA  ANGL. DEV. =   9.5 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  19     -158.00   -127.73
REMARK 500    PHE A  75     -134.13   -132.45
REMARK 500    ALA A 124     -156.51     81.96
REMARK 500    TYR A 133      160.39    176.47
REMARK 500    LEU A 156      -77.31    -98.14
REMARK 500    ASN A 192     -162.85   -129.12
REMARK 500    GLU A 233      142.63    170.07
REMARK 500    GLU A 235       64.91     36.25
REMARK 500    LEU A 249       93.59   -167.34
REMARK 500    LEU A 281      -79.72     61.41
REMARK 500    HIS A 311      -84.25   -109.25
REMARK 500    TRP A 312      122.43     49.94
REMARK 500    TYR A 313     -163.27    -72.08
REMARK 500    THR A 323      -73.73   -105.75
REMARK 500    LYS A 346      121.04    -32.78
REMARK 500    HIS A 374       -1.17     69.88
REMARK 500    TRP A 381     -138.11    -87.35
REMARK 500    ARG A 395      140.39   -177.30
REMARK 500    PHE A 397       -4.26   -149.32
REMARK 500    PHE A 423      -66.61   -105.84
REMARK 500    ILE A 427       79.42   -119.92
REMARK 500    VAL A 477      -53.13   -121.62
REMARK 500    CYS B  23      132.59   -171.08
REMARK 500    THR B  63       16.46   -164.59
REMARK 500    PHE B  75     -147.36   -136.01
REMARK 500    ALA B 124     -158.17     81.67
REMARK 500    ARG B 131      143.35   -176.53
REMARK 500    ALA B 136       76.21   -150.23
REMARK 500    LEU B 144       43.52     73.78
REMARK 500    LEU B 156      -73.39   -111.55
REMARK 500    ASN B 192     -158.84   -119.82
REMARK 500    GLU B 233      142.28    168.73
REMARK 500    GLU B 235       64.86     34.61
REMARK 500    ASP B 263      -72.72   -118.49
REMARK 500    LEU B 281      -80.62     66.56
REMARK 500    LEU B 314       -6.82    -53.12
REMARK 500    ALA B 322       -3.92    -56.32
REMARK 500    THR B 323      -82.30   -124.81
REMARK 500    LYS B 346      152.34    -49.85
REMARK 500    PHE B 347       21.10    -77.96
REMARK 500    TRP B 348       -7.48   -154.50
REMARK 500    GLN B 350      158.93    -46.60
REMARK 500    HIS B 374       -3.94     70.55
REMARK 500    TRP B 381     -138.00    -78.17
REMARK 500    PHE B 423      -60.04   -109.69
REMARK 500    GLN B 440      148.83   -172.29
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 A1653        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH A1673        DISTANCE =  5.51 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1505
DBREF  2F61 A    1   497  GB     183028   AAA35880        40    536
DBREF  2F61 B    1   497  GB     183028   AAA35880        40    536
SEQRES   1 A  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 A  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 A  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 A  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 A  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 A  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 A  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 A  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 A  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 A  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 A  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 A  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 A  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 A  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 A  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 A  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 A  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 A  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 A  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 A  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 A  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 A  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 A  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 A  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 A  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 A  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 A  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 A  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 A  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 A  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 A  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 A  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 A  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 A  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 A  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 A  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 A  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 A  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 A  497  HIS ARG GLN
SEQRES   1 B  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 B  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 B  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 B  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 B  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 B  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 B  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 B  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 B  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 B  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 B  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 B  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 B  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 B  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 B  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 B  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 B  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 B  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 B  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 B  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 B  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 B  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 B  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 B  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 B  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 B  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 B  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 B  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 B  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 B  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 B  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 B  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 B  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 B  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 B  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 B  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 B  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 B  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 B  497  HIS ARG GLN
MODRES 2F61 ASN A   19  ASN  GLYCOSYLATION SITE
MODRES 2F61 ASN B   19  ASN  GLYCOSYLATION SITE
HET    NDG  A1001      14
HET    NAG  B1001      14
HET    NAG  B1002      14
HET    SO4  A1500       5
HET    SO4  A1502       5
HET    SO4  A1501       5
HET    SO4  B1503       5
HET    SO4  B1504       5
HET    SO4  B1505       5
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     SO4 SULFATE ION
FORMUL   3  NDG    C8 H15 N O6
FORMUL   4  NAG    2(C8 H15 N O6)
FORMUL   5  SO4    6(O4 S 2-)
FORMUL  11  HOH   *406(H2 O)
HELIX    1   1 THR A   86  LEU A   94  1                                   9
HELIX    2   2 SER A   97  SER A  110  1                                  14
HELIX    3   3 PRO A  150  LYS A  155  1                                   6
HELIX    4   4 LEU A  156  ALA A  168  1                                  13
HELIX    5   5 PRO A  182  LYS A  186  5                                   5
HELIX    6   6 ASP A  203  HIS A  223  1                                  21
HELIX    7   7 GLU A  235  LEU A  241  5                                   7
HELIX    8   8 THR A  252  ASP A  263  1                                  12
HELIX    9   9 ASP A  263  ASN A  270  1                                   8
HELIX   10  10 GLN A  284  LEU A  288  5                                   5
HELIX   11  11 PRO A  289  THR A  297  1                                   9
HELIX   12  12 ASP A  298  LYS A  303  1                                   6
HELIX   13  13 PRO A  319  PHE A  331  1                                  13
HELIX   14  14 SER A  356  TYR A  373  1                                  18
HELIX   15  15 ILE A  406  LYS A  408  5                                   3
HELIX   16  16 GLN A  414  LYS A  425  1                                  12
HELIX   17  17 THR B   86  LEU B   94  1                                   9
HELIX   18  18 SER B   97  SER B  110  1                                  14
HELIX   19  19 PRO B  150  LYS B  155  1                                   6
HELIX   20  20 LEU B  156  ALA B  168  1                                  13
HELIX   21  21 PRO B  182  LYS B  186  5                                   5
HELIX   22  22 ASP B  203  HIS B  223  1                                  21
HELIX   23  23 SER B  237  LEU B  241  5                                   5
HELIX   24  24 THR B  252  ASP B  263  1                                  12
HELIX   25  25 ASP B  263  ASN B  270  1                                   8
HELIX   26  26 LEU B  286  LEU B  288  5                                   3
HELIX   27  27 PRO B  289  THR B  297  1                                   9
HELIX   28  28 ASP B  298  LYS B  303  1                                   6
HELIX   29  29 THR B  323  PHE B  331  1                                   9
HELIX   30  30 SER B  356  TYR B  373  1                                  18
HELIX   31  31 ILE B  406  LYS B  408  5                                   3
HELIX   32  32 GLN B  414  LYS B  425  1                                  12
SHEET    1   A 4 PRO A   6  LYS A   7  0
SHEET    2   A 4 VAL A  15  ASN A  19 -1  O  VAL A  15   N  LYS A   7
SHEET    3   A 4 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18
SHEET    4   A 4 ILE A 402  ASP A 405 -1  N  ILE A 403   O  TYR A 412
SHEET    1   B 9 GLU A  50  PRO A  55  0
SHEET    2   B 9 THR A  36  THR A  43 -1  N  ARG A  39   O  SER A  52
SHEET    3   B 9 SER A 488  TRP A 494 -1  O  LEU A 493   N  SER A  38
SHEET    4   B 9 ALA A 456  ASN A 462 -1  N  VAL A 458   O  TYR A 492
SHEET    5   B 9 LEU A 444  MET A 450 -1  N  ASP A 445   O  LEU A 461
SHEET    6   B 9 GLN A 432  ALA A 438 -1  N  GLN A 432   O  MET A 450
SHEET    7   B 9 LEU A  65  LYS A  77 -1  N  GLN A  70   O  GLY A 435
SHEET    8   B 9 VAL A 468  ASP A 474  1  O  LYS A 473   N  LEU A  69
SHEET    9   B 9 GLY A 478  SER A 484 -1  O  LEU A 480   N  ILE A 472
SHEET    1   C 9 GLY A  80  ALA A  84  0
SHEET    2   C 9 ILE A 118  MET A 123  1  O  ARG A 120   N  GLY A  83
SHEET    3   C 9 SER A 173  PRO A 178  1  O  LEU A 175   N  VAL A 121
SHEET    4   C 9 ALA A 229  THR A 231  1  O  THR A 231   N  ALA A 176
SHEET    5   C 9 ARG A 277  ASP A 283  1  O  LEU A 279   N  VAL A 230
SHEET    6   C 9 GLY A 307  VAL A 310  1  O  ALA A 309   N  MET A 280
SHEET    7   C 9 MET A 335  ALA A 341  1  O  MET A 335   N  ILE A 308
SHEET    8   C 9 VAL A 375  ASN A 382  1  O  VAL A 376   N  LEU A 336
SHEET    9   C 9 GLY A  80  ALA A  84  1  N  GLY A  82   O  ASP A 380
SHEET    1   D 4 PRO B   6  LYS B   7  0
SHEET    2   D 4 VAL B  15  ASN B  19 -1  O  VAL B  15   N  LYS B   7
SHEET    3   D 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18
SHEET    4   D 4 ILE B 402  ASP B 405 -1  N  ASP B 405   O  THR B 410
SHEET    1   E 9 GLU B  50  PRO B  55  0
SHEET    2   E 9 THR B  36  THR B  43 -1  N  ARG B  39   O  SER B  52
SHEET    3   E 9 SER B 488  TRP B 494 -1  O  LEU B 493   N  SER B  38
SHEET    4   E 9 ALA B 456  ASN B 462 -1  N  VAL B 458   O  TYR B 492
SHEET    5   E 9 LEU B 444  MET B 450 -1  N  ASP B 445   O  LEU B 461
SHEET    6   E 9 GLN B 432  VAL B 437 -1  N  GLN B 432   O  MET B 450
SHEET    7   E 9 LEU B  65  LYS B  77 -1  N  THR B  68   O  VAL B 437
SHEET    8   E 9 VAL B 468  ASP B 474  1  O  LYS B 473   N  LEU B  69
SHEET    9   E 9 GLY B 478  SER B 484 -1  O  GLY B 478   N  ASP B 474
SHEET    1   F 9 GLY B  80  ALA B  84  0
SHEET    2   F 9 ILE B 118  MET B 123  1  O  ARG B 120   N  GLY B  83
SHEET    3   F 9 SER B 173  PRO B 178  1  O  LEU B 175   N  VAL B 121
SHEET    4   F 9 ALA B 229  THR B 231  1  O  THR B 231   N  ALA B 176
SHEET    5   F 9 ARG B 277  GLN B 284  1  O  LEU B 279   N  VAL B 230
SHEET    6   F 9 GLY B 307  TYR B 313  1  O  GLY B 307   N  MET B 280
SHEET    7   F 9 MET B 335  CYS B 342  1  O  GLU B 340   N  TRP B 312
SHEET    8   F 9 VAL B 375  ASN B 382  1  O  VAL B 376   N  LEU B 336
SHEET    9   F 9 GLY B  80  ALA B  84  1  N  GLY B  82   O  ASP B 380
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.04
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.04
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.04
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.05
LINK         ND2 ASN A  19                 C1  NDG A1001     1555   1555  1.46
LINK         ND2 ASN B  19                 C1  NAG B1001     1555   1555  1.45
LINK         O4  NAG B1001                 C1  NAG B1002     1555   1555  1.38
CISPEP   1 LEU A  288    PRO A  289          0         0.15
CISPEP   2 GLY A  390    PRO A  391          0         0.21
CISPEP   3 LEU B  288    PRO B  289          0         0.23
CISPEP   4 GLY B  390    PRO B  391          0         0.55
SITE     1 AC1  3 ASN A  19  TYR A  22  HOH A1701
SITE     1 AC2  5 ASN B  19  NAG B1002  HOH B1632  HOH B1646
SITE     2 AC2  5 HOH B1694
SITE     1 AC3  2 NAG B1001  HOH B1691
SITE     1 AC4  6 TYR A  11  SER A  12  ARG A 353  SER A 356
SITE     2 AC4  6 TRP A 357  ASP A 358
SITE     1 AC5  6 THR A  63  GLN A 440  LYS A 473  HOH A1590
SITE     2 AC5  6 HOH A1683  HOH A1689
SITE     1 AC6  3 LYS A  79  TRP A 228  ARG A 277
SITE     1 AC7  7 SER A 242  TYR B  11  SER B  12  SER B 356
SITE     2 AC7  7 TRP B 357  ASP B 358  HOH B1650
SITE     1 AC8  5 GLY B 193  LYS B 194  SER B 242  GLY B 243
SITE     2 AC8  5 HOH B1674
SITE     1 AC9  2 ARG B  44  SER B  45
CRYST1  108.640  284.430   91.540  90.00  90.00  90.00 C 2 2 21     16
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      0.009200  0.000000  0.000000        0.00000
SCALE2      0.000000  0.003520  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010920        0.00000
      
PROCHECK
Go to PROCHECK summary
 References