spacer
spacer

PDBsum entry 2v3f

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2v3f
Jmol
Contents
Protein chain
497 a.a.
Ligands
NAG-NAG-MAN
BTB ×2
SO4 ×12
FUC ×2
NAG-NAG
Waters ×805
HEADER    HYDROLASE                               17-JUN-07   2V3F
TITLE     ACID-BETA-GLUCOSIDASE PRODUCED IN CARROT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID-BETA-GLUCOSIDASE,
COMPND   5  D-GLUCOSYL-N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE,
COMPND   6  IMIGLUCERASE;
COMPND   7 EC: 3.2.1.45;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: DAUCUS CAROTA;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4039
KEYWDS    ALTERNATIVE INITIATION, SPHINGOLIPID METABOLISM, GAUCHER
KEYWDS   2 DISEASE, DISEASE MUTATION, LIPID METABOLISM, POLYMORPHISM,
KEYWDS   3 GLYCOPROTEIN, PHARMACEUTICAL, N-BUTYL-DEOXYNOJIRIMYCIN,
KEYWDS   4 ALTERNATIVE SPLICING, ACID-BETA-GLUCOSIDASE, MEMBRANE,
KEYWDS   5 LYSOSOME, HYDROLASE, GLYCOSIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.SHAALTIEL,D.BARTFELD,S.HASHMUELI,G.BAUM,E.BRILL-ALMON,
AUTHOR   2 G.GALILI,O.DYM,S.A.BOLDIN-ADAMSKY,I.SILMAN,J.L.SUSSMAN,
AUTHOR   3 A.H.FUTERMAN,D.AVIEZER,
AUTHOR   4 ISRAEL STRUCTURAL PROTEOMICS CENTER(ISPC)
REVDAT   3   24-FEB-09 2V3F    1       VERSN
REVDAT   2   06-MAY-08 2V3F    1       AUTHOR
REVDAT   1   08-APR-08 2V3F    0
JRNL        AUTH   Y.SHAALTIEL,D.BARTFELD,S.HASHMUELI,G.BAUM,
JRNL        AUTH 2 E.BRILL-ALMON,G.GALILI,O.DYM,S.A.BOLDIN-ADAMSKY,
JRNL        AUTH 3 I.SILMAN,J.L.SUSSMAN,A.H.FUTERMAN,D.AVIEZER
JRNL        TITL   PRODUCTION OF GLUCOCEREBROSIDASE WITH TERMINAL
JRNL        TITL 2 MANNOSE GLYCANS FOR ENZYME REPLACEMENT THERAPY OF
JRNL        TITL 3 GAUCHER'S DISEASE USING A PLANT CELL SYSTEM.
JRNL        REF    PLANT BIOTECHNOL.J.           V.   5   579 2007
JRNL        REFN                   ISSN 1467-7644
JRNL        PMID   17524049
JRNL        DOI    10.1111/J.1467-7652.2007.00263.X
REMARK   2
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 1.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.56
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9
REMARK   3   NUMBER OF REFLECTIONS             : 66326
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) : 0.154
REMARK   3   R VALUE            (WORKING SET) : 0.149
REMARK   3   FREE R VALUE                     : 0.196
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 7449
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) : 1.95
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4966
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.73
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1510
REMARK   3   BIN FREE R VALUE SET COUNT          : 553
REMARK   3   BIN FREE R VALUE                    : 0.2170
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7785
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 175
REMARK   3   SOLVENT ATOMS            : 805
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.60
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.162
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.145
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.082
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.790
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8202 ; 0.014 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11214 ; 1.371 ; 1.967
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   992 ; 7.556 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   355 ;36.897 ;23.437
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1237 ;14.122 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;21.089 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1231 ; 0.096 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6218 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3817 ; 0.195 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5589 ; 0.308 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   781 ; 0.174 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    36 ; 0.160 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.133 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5078 ; 0.850 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7989 ; 1.313 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3596 ; 2.027 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3207 ; 3.057 ; 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 : 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: NULL
REMARK   4
REMARK   4 2V3F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUN-07.
REMARK 100 THE PDBE ID CODE IS EBI-32937.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID23-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0723
REMARK 200  MONOCHROMATOR                  : C AND AL
REMARK 200  OPTICS                         : MIRRORD
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74750
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.95
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0
REMARK 200  DATA REDUNDANCY                : 4
REMARK 200  R MERGE                    (I) : 0.10
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.9
REMARK 200  R MERGE FOR SHELL          (I) : 0.25
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 6.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1OGS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.6
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMSO4 0.2M, BIS-TRIS PH6.5, PEG
REMARK 280  3350 25%, HEXAMINECOCL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       48.55200
REMARK 290   SMTRY3   2  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 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE:  1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE:  2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     PRO A    29
REMARK 465     THR A    30
REMARK 465     PHE A    31
REMARK 465     LEU A   499
REMARK 465     VAL A   500
REMARK 465     ASP A   501
REMARK 465     THR A   502
REMARK 465     MET A   503
REMARK 465     GLU B    -1
REMARK 465     PHE B     0
REMARK 465     ASP B    27
REMARK 465     PRO B    28
REMARK 465     PRO B    29
REMARK 465     THR B    30
REMARK 465     PHE B    31
REMARK 465     PRO B    32
REMARK 465     LEU B   498
REMARK 465     LEU B   499
REMARK 465     VAL B   500
REMARK 465     ASP B   501
REMARK 465     THR B   502
REMARK 465     MET B   503
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLU A  72    CD   OE1  OE2
REMARK 470     ASN A 146    OD1  ND2
REMARK 470     LYS A 155    CE   NZ
REMARK 470     ARG A 211    CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 222    CD   OE1  OE2
REMARK 470     LYS A 224    CE   NZ
REMARK 470     LYS A 408    CE   NZ
REMARK 470     LYS A 441    CG   CD   CE   NZ
REMARK 470     LYS A 466    CG   CD   CE   NZ
REMARK 470     LEU A 498    CA   C    O    CB   CG   CD1  CD2
REMARK 470     GLU B 111    CD   OE1  OE2
REMARK 470     LYS B 155    CD   CE   NZ
REMARK 470     ARG B 211    NE   CZ   NH1  NH2
REMARK 470     LYS B 441    CD   CE   NZ
REMARK 470     GLN B 497    CA   C    O    CB   CG   CD   OE1  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   O    HOH A  2021  -  O    HOH A  2054              2.18
REMARK 500   O    HOH A  2023  -  O    HOH A  2054              2.08
REMARK 500   O    HOH A  2038  -  O    HOH A  2044              2.19
REMARK 500   O    HOH A  2139  -  O    HOH A  2153              2.10
REMARK 500   O    HOH A  2221  -  O    HOH A  2251              1.73
REMARK 500   O    HOH A  2269  -  O    HOH A  2316              1.92
REMARK 500   O    HOH B  2016  -  O    HOH B  2019              2.17
REMARK 500   O    HOH B  2230  -  O    HOH B  2295              2.09
REMARK 500   O    HOH B  2248  -  O    HOH B  2295              1.75
REMARK 500   O    HOH B  2279  -  O    HOH B  2282              2.07
REMARK 500   O    HOH B  2296  -  O    HOH B  2336              2.19
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 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    TYR A  11     -165.38   -100.07
REMARK 500    ALA A  33      156.08    -43.94
REMARK 500    GLN A  70       78.96   -119.90
REMARK 500    PHE A  75     -132.70   -118.33
REMARK 500    ALA A 124     -151.30     66.46
REMARK 500    LEU A 156      -67.66   -107.39
REMARK 500    GLU A 233      137.84    175.30
REMARK 500    GLU A 235       66.11     36.76
REMARK 500    ASP A 263      -70.25   -122.28
REMARK 500    LEU A 281      -87.20     71.44
REMARK 500    THR A 323      -72.83   -113.49
REMARK 500    HIS A 374        3.57     83.39
REMARK 500    TRP A 381     -134.28    -87.21
REMARK 500    ALA A 476       -0.72     62.50
REMARK 500    TYR A 487       -3.08     76.19
REMARK 500    ASN B  19     -157.81   -146.07
REMARK 500    PHE B  75     -133.03   -117.25
REMARK 500    ALA B 124     -151.32     67.90
REMARK 500    CYS B 126     -163.62   -129.07
REMARK 500    LEU B 156      -67.34   -101.70
REMARK 500    GLU B 233      137.86    174.12
REMARK 500    GLU B 235       64.76     38.34
REMARK 500    ASP B 263      -63.98   -121.08
REMARK 500    LEU B 281      -84.82     76.04
REMARK 500    THR B 323      -74.20   -115.75
REMARK 500    HIS B 374       -1.48     84.61
REMARK 500    TRP B 381     -134.74    -88.30
REMARK 500    TYR B 487       -8.98     77.78
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 PHE A   26     ASP A   27                  148.88
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 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "BC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A1508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB B1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB A1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B1508
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1506
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1507
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1506
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OGS   RELATED DB: PDB
REMARK 900  HUMAN ACID-BETA-GLUCOSIDASE
REMARK 900 RELATED ID: 1Y7V   RELATED DB: PDB
REMARK 900  X-RAY STRUCTURE OF HUMAN ACID-BETA-
REMARK 900  GLUCOSIDASE COVALENTLYBOUND TO CONDURITOL B
REMARK 900  EPOXIDE
REMARK 900 RELATED ID: 2F61   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PARTIALLY DEGLYCOSYLATED
REMARK 900  ACID BETA-GLUCOSIDASE
REMARK 900 RELATED ID: 2J25   RELATED DB: PDB
REMARK 900  PARTIALLY DEGLYCOSYLATED GLUCOCERAMIDASE
REMARK 900 RELATED ID: 2V3D   RELATED DB: PDB
REMARK 900  ACID-BETA-GLUCOSIDASE WITH N-BUTYL-
REMARK 900  DEOXYNOJIRIMYCIN
REMARK 900 RELATED ID: 2V3E   RELATED DB: PDB
REMARK 900  ACID-BETA-GLUCOSIDASE WITH N-NONYL-
REMARK 900  DEOXYNOJIRIMYCIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 IN ADDITION TO THE NATIVE SEQUENCE OF HUMAN ACID-BETA-GLUCOSIDASE,
REMARK 999 THE MOLECULE HAS 2 AMINO ACIDS AT THE N-TERMINAL, AND 6 AMINO ACIDS
REMARK 999 AT THE C-TERMINAL
DBREF  2V3F A   -1     0  PDB    2V3F     2V3F            -1      0
DBREF  2V3F A    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  2V3F A  498   503  PDB    2V3F     2V3F           498    503
DBREF  2V3F B   -1     0  PDB    2V3F     2V3F            -1      0
DBREF  2V3F B    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  2V3F B  498   503  PDB    2V3F     2V3F           498    503
SEQADV 2V3F HIS A  495  UNP  P04062    ARG   534 CONFLICT
SEQADV 2V3F HIS B  495  UNP  P04062    ARG   534 CONFLICT
SEQRES   1 A  505  GLU PHE ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR
SEQRES   2 A  505  SER SER VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP
SEQRES   3 A  505  SER PHE ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE
SEQRES   4 A  505  SER ARG TYR GLU SER THR ARG SER GLY ARG ARG MET GLU
SEQRES   5 A  505  LEU SER MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR
SEQRES   6 A  505  GLY LEU LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN
SEQRES   7 A  505  LYS VAL LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA
SEQRES   8 A  505  ALA LEU ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN
SEQRES   9 A  505  LEU LEU LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY
SEQRES  10 A  505  TYR ASN ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE
SEQRES  11 A  505  SER ILE ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP
SEQRES  12 A  505  PHE GLN LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR
SEQRES  13 A  505  LYS LEU LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU
SEQRES  14 A  505  ALA GLN ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR
SEQRES  15 A  505  SER PRO THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY
SEQRES  16 A  505  LYS GLY SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS
SEQRES  17 A  505  GLN THR TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA
SEQRES  18 A  505  TYR ALA GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA
SEQRES  19 A  505  GLU ASN GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO
SEQRES  20 A  505  PHE GLN CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP
SEQRES  21 A  505  PHE ILE ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER
SEQRES  22 A  505  THR HIS HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN
SEQRES  23 A  505  ARG LEU LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR
SEQRES  24 A  505  ASP PRO GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL
SEQRES  25 A  505  HIS TRP TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR
SEQRES  26 A  505  LEU GLY GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU
SEQRES  27 A  505  PHE ALA SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU
SEQRES  28 A  505  GLN SER VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN
SEQRES  29 A  505  TYR SER HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL
SEQRES  30 A  505  VAL GLY TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU
SEQRES  31 A  505  GLY GLY PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO
SEQRES  32 A  505  ILE ILE VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN
SEQRES  33 A  505  PRO MET PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE
SEQRES  34 A  505  PRO GLU GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN
SEQRES  35 A  505  LYS ASN ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP
SEQRES  36 A  505  GLY SER ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS
SEQRES  37 A  505  ASP VAL PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE
SEQRES  38 A  505  LEU GLU THR ILE SER PRO GLY TYR SER ILE HIS THR TYR
SEQRES  39 A  505  LEU TRP HIS ARG GLN LEU LEU VAL ASP THR MET
SEQRES   1 B  505  GLU PHE ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR
SEQRES   2 B  505  SER SER VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP
SEQRES   3 B  505  SER PHE ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE
SEQRES   4 B  505  SER ARG TYR GLU SER THR ARG SER GLY ARG ARG MET GLU
SEQRES   5 B  505  LEU SER MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR
SEQRES   6 B  505  GLY LEU LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN
SEQRES   7 B  505  LYS VAL LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA
SEQRES   8 B  505  ALA LEU ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN
SEQRES   9 B  505  LEU LEU LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY
SEQRES  10 B  505  TYR ASN ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE
SEQRES  11 B  505  SER ILE ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP
SEQRES  12 B  505  PHE GLN LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR
SEQRES  13 B  505  LYS LEU LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU
SEQRES  14 B  505  ALA GLN ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR
SEQRES  15 B  505  SER PRO THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY
SEQRES  16 B  505  LYS GLY SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS
SEQRES  17 B  505  GLN THR TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA
SEQRES  18 B  505  TYR ALA GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA
SEQRES  19 B  505  GLU ASN GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO
SEQRES  20 B  505  PHE GLN CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP
SEQRES  21 B  505  PHE ILE ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER
SEQRES  22 B  505  THR HIS HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN
SEQRES  23 B  505  ARG LEU LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR
SEQRES  24 B  505  ASP PRO GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL
SEQRES  25 B  505  HIS TRP TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR
SEQRES  26 B  505  LEU GLY GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU
SEQRES  27 B  505  PHE ALA SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU
SEQRES  28 B  505  GLN SER VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN
SEQRES  29 B  505  TYR SER HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL
SEQRES  30 B  505  VAL GLY TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU
SEQRES  31 B  505  GLY GLY PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO
SEQRES  32 B  505  ILE ILE VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN
SEQRES  33 B  505  PRO MET PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE
SEQRES  34 B  505  PRO GLU GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN
SEQRES  35 B  505  LYS ASN ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP
SEQRES  36 B  505  GLY SER ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS
SEQRES  37 B  505  ASP VAL PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE
SEQRES  38 B  505  LEU GLU THR ILE SER PRO GLY TYR SER ILE HIS THR TYR
SEQRES  39 B  505  LEU TRP HIS ARG GLN LEU LEU VAL ASP THR MET
HET    MAN  A1500      11
HET    FUC  A1508      10
HET    NAG  A1498      14
HET    NAG  A1499      14
HET    BTB  B1500      14
HET    NAG  B1498      14
HET    NAG  B1499      14
HET    BTB  A1501      14
HET    FUC  B1508      10
HET    SO4  B1501       5
HET    SO4  A1502       5
HET    SO4  A1503       5
HET    SO4  A1504       5
HET    SO4  A1505       5
HET    SO4  B1502       5
HET    SO4  B1503       5
HET    SO4  B1504       5
HET    SO4  B1505       5
HET    SO4  B1506       5
HET    SO4  B1507       5
HET    SO4  A1506       5
HETNAM     BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-
HETNAM   2 BTB  HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM     SO4 SULFATE ION
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM     MXY 2-O-METHYL FUCOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETSYN     BTB BIS-TRIS BUFFER
HETSYN     NAG NAG
FORMUL   3  BTB    2(C8 H19 N O5)
FORMUL   4  SO4    12(O4 S 2-)
FORMUL   5  FUC    2(C6 H12 O5)
FORMUL   6  MXY    C7 H14 O5
FORMUL   7  NAG    4(C8 H15 N O6)
FORMUL   8  MAN    C6 H12 O6
FORMUL   9  HOH   *805(H2 O1)
HELIX    1   1 THR A   86  ALA A   95  1                                  10
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  LEU A  185  5                                   4
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 LEU A  286  LEU A  288  5                                   3
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 LEU A  314  ALA A  318  5                                   5
HELIX   14  14 PRO A  319  PHE A  331  1                                  13
HELIX   15  15 SER A  356  TYR A  373  1                                  18
HELIX   16  16 ILE A  406  ASP A  409  5                                   4
HELIX   17  17 GLN A  414  LYS A  425  1                                  12
HELIX   18  18 THR B   86  ALA B   95  1                                  10
HELIX   19  19 SER B   97  SER B  110  1                                  14
HELIX   20  20 PRO B  150  LYS B  155  1                                   6
HELIX   21  21 LEU B  156  ALA B  168  1                                  13
HELIX   22  22 PRO B  182  LEU B  185  5                                   4
HELIX   23  23 ASP B  203  HIS B  223  1                                  21
HELIX   24  24 GLU B  235  LEU B  241  5                                   7
HELIX   25  25 THR B  252  ASP B  263  1                                  12
HELIX   26  26 ASP B  263  ASN B  270  1                                   8
HELIX   27  27 LEU B  286  LEU B  288  5                                   3
HELIX   28  28 PRO B  289  THR B  297  1                                   9
HELIX   29  29 ASP B  298  LYS B  303  1                                   6
HELIX   30  30 LEU B  314  ALA B  318  5                                   5
HELIX   31  31 THR B  323  PHE B  331  1                                   9
HELIX   32  32 SER B  356  TYR B  373  1                                  18
HELIX   33  33 ILE B  406  ASP B  409  5                                   4
HELIX   34  34 GLN B  414  LYS B  425  1                                  12
SHEET    1  AA 4 PRO A   6  LYS A   7  0
SHEET    2  AA 4 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7
SHEET    3  AA 4 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18
SHEET    4  AA 4 ILE A 402  ASP A 405 -1  O  ILE A 403   N  TYR A 412
SHEET    1  AB 9 GLU A  50  PRO A  55  0
SHEET    2  AB 9 THR A  36  SER A  42 -1  O  PHE A  37   N  GLY A  54
SHEET    3  AB 9 ILE A 489  TRP A 494 -1  O  ILE A 489   N  SER A  42
SHEET    4  AB 9 ALA A 456  ASN A 462 -1  O  ALA A 456   N  TRP A 494
SHEET    5  AB 9 LEU A 444  MET A 450 -1  O  ASP A 445   N  LEU A 461
SHEET    6  AB 9 GLN A 432  ALA A 438 -1  O  GLN A 432   N  MET A 450
SHEET    7  AB 9 LEU A  65  LYS A  77 -1  O  THR A  68   N  VAL A 437
SHEET    8  AB 9 VAL A 468  ASP A 474  1  O  PRO A 469   N  LEU A  65
SHEET    9  AB 9 GLY A 478  SER A 484 -1  O  GLY A 478   N  ASP A 474
SHEET    1  AC 9 GLY A  80  ALA A  84  0
SHEET    2  AC 9 VAL A 375  ASN A 382  1  O  TRP A 378   N  GLY A  82
SHEET    3  AC 9 MET A 335  GLU A 340  1  O  LEU A 336   N  VAL A 376
SHEET    4  AC 9 GLY A 307  HIS A 311  1  O  ILE A 308   N  PHE A 337
SHEET    5  AC 9 ARG A 277  GLN A 284  1  O  MET A 280   N  ALA A 309
SHEET    6  AC 9 ALA A 229  THR A 231  1  O  VAL A 230   N  LEU A 279
SHEET    7  AC 9 SER A 173  PRO A 178  1  O  ALA A 176   N  THR A 231
SHEET    8  AC 9 ILE A 118  MET A 123  1  O  ILE A 119   N  LEU A 175
SHEET    9  AC 9 GLY A  80  ALA A  84  1  O  GLY A  83   N  ARG A 120
SHEET    1  BA 4 PRO B   6  LYS B   7  0
SHEET    2  BA 4 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7
SHEET    3  BA 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18
SHEET    4  BA 4 ILE B 402  ASP B 405 -1  O  ILE B 403   N  TYR B 412
SHEET    1  BB 9 GLU B  50  PRO B  55  0
SHEET    2  BB 9 THR B  36  SER B  42 -1  O  PHE B  37   N  GLY B  54
SHEET    3  BB 9 ILE B 489  TRP B 494 -1  O  ILE B 489   N  SER B  42
SHEET    4  BB 9 ALA B 456  ASN B 462 -1  O  ALA B 456   N  TRP B 494
SHEET    5  BB 9 LEU B 444  MET B 450 -1  O  ASP B 445   N  LEU B 461
SHEET    6  BB 9 GLN B 432  ALA B 438 -1  O  GLN B 432   N  MET B 450
SHEET    7  BB 9 LEU B  65  LYS B  77 -1  O  THR B  68   N  VAL B 437
SHEET    8  BB 9 VAL B 468  ASP B 474  1  O  PRO B 469   N  LEU B  65
SHEET    9  BB 9 GLY B 478  SER B 484 -1  O  GLY B 478   N  ASP B 474
SHEET    1  BC 9 GLY B  80  ALA B  84  0
SHEET    2  BC 9 VAL B 375  ASN B 382  1  O  TRP B 378   N  GLY B  82
SHEET    3  BC 9 MET B 335  GLU B 340  1  O  LEU B 336   N  VAL B 376
SHEET    4  BC 9 GLY B 307  HIS B 311  1  O  ILE B 308   N  PHE B 337
SHEET    5  BC 9 ARG B 277  GLN B 284  1  O  MET B 280   N  ALA B 309
SHEET    6  BC 9 ALA B 229  THR B 231  1  O  VAL B 230   N  LEU B 279
SHEET    7  BC 9 SER B 173  PRO B 178  1  O  ALA B 176   N  THR B 231
SHEET    8  BC 9 ILE B 118  MET B 123  1  O  ILE B 119   N  LEU B 175
SHEET    9  BC 9 GLY B  80  ALA B  84  1  O  GLY B  83   N  ARG B 120
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.09
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.11
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.07
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.12
LINK         ND2 ASN A  19                 C1  NAG A1498     1555   1555  1.45
LINK         O3  NAG A1498                 C1  FUC A1508     1555   1555  1.45
LINK         O4  NAG A1498                 C1  NAG A1499     1555   1555  1.44
LINK         O4  NAG A1499                 C1  MAN A1500     1555   1555  1.44
LINK         ND2 ASN B  19                 C1  NAG B1498     1555   1555  1.43
LINK         O3  NAG B1498                 C1  FUC B1508     1555   1555  1.46
LINK         O4  NAG B1498                 C1  NAG B1499     1555   1555  1.44
CISPEP   1 LEU A  288    PRO A  289          0         2.90
CISPEP   2 GLY A  390    PRO A  391          0         7.79
CISPEP   3 LEU B  288    PRO B  289          0         3.50
CISPEP   4 GLY B  390    PRO B  391          0         7.49
SITE     1 AC1  2 NAG A1499  HOH A2402
SITE     1 AC2  3 NAG A1498  NAG A1499  HOH A2412
SITE     1 AC3  6 ILE A   5  ASN A  19  NAG A1499  FUC A1508
SITE     2 AC3  6 HOH A2015  HOH A2400
SITE     1 AC4  4 NAG A1498  MAN A1500  FUC A1508  HOH A2401
SITE     1 AC5 16 ASP B 127  PHE B 128  TRP B 179  ASN B 234
SITE     2 AC5 16 GLU B 235  TYR B 244  PHE B 246  TYR B 313
SITE     3 AC5 16 GLU B 340  CYS B 342  SER B 345  TRP B 381
SITE     4 AC5 16 VAL B 398  HOH B2204  HOH B2316  HOH B2380
SITE     1 AC6  7 ASN B  19  TYR B  22  NAG B1499  FUC B1508
SITE     2 AC6  7 HOH B2376  HOH B2377  HOH B2393
SITE     1 AC7  4 NAG B1498  FUC B1508  HOH B2378  HOH B2379
SITE     1 AC8 14 ASP A 127  PHE A 128  TRP A 179  ASN A 234
SITE     2 AC8 14 GLU A 235  TYR A 244  PHE A 246  TYR A 313
SITE     3 AC8 14 GLU A 340  CYS A 342  TRP A 381  ASN A 396
SITE     4 AC8 14 VAL A 398  HOH A2403
SITE     1 AC9  4 NAG B1498  NAG B1499  HOH B2392  HOH B2393
SITE     1 BC1  3 ARG B  44  SER B  45  HOH B2381
SITE     1 BC2  3 ARG A  44  SER A  45  HOH A2404
SITE     1 BC3  6 GLY A 193  LYS A 194  SER A 242  GLY A 243
SITE     2 BC3  6 HOH A2186  HOH A2190
SITE     1 BC4  4 LYS A  79  TRP A 228  ARG A 277  HOH A2406
SITE     1 BC5  6 TYR A  11  SER A  12  ARG A 353  SER A 356
SITE     2 BC5  6 ASP A 358  HOH A2407
SITE     1 BC6  6 GLY B 193  LYS B 194  GLY B 243  HOH B2168
SITE     2 BC6  6 HOH B2383  HOH B2384
SITE     1 BC7  6 LYS B  79  TRP B 228  ARG B 277  HIS B 306
SITE     2 BC7  6 HOH B2328  HOH B2385
SITE     1 BC8  7 TYR B  11  SER B  12  ARG B 353  SER B 356
SITE     2 BC8  7 ASP B 358  HOH B2386  HOH B2387
SITE     1 BC9  7 PRO B   3  CYS B   4  GLY B  46  ARG B  47
SITE     2 BC9  7 ARG B  48  GLU B  50  HOH B2039
SITE     1 CC1  5 ARG B 285  HIS B 365  HOH B2388  HOH B2389
SITE     2 CC1  5 HOH B2390
SITE     1 CC2  9 GLY B 265  LEU B 268  ALA B 269  HIS B 274
SITE     2 CC2  9 VAL B 276  TYR B 304  HOH B2226  HOH B2242
SITE     3 CC2  9 HOH B2391
SITE     1 CC3  6 ARG A 285  HIS A 365  THR A 369  HOH A2409
SITE     2 CC3  6 HOH A2410  HOH A2411
CRYST1   68.088   97.104   82.932  90.00 104.43  90.00 P 1 21 1      4
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      0.014687  0.000000  0.003779        0.00000
SCALE2      0.000000  0.010298  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012451        0.00000
      
PROCHECK
Go to PROCHECK summary
 References