spacer
spacer

PDBsum entry 2xwd

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2xwd
Jmol
Contents
Protein chain
493 a.a.
Ligands
NAG-NAG-MAN-FUC
SO4 ×10
LGS ×2
NAG-NAG-BMA-FUC
Waters ×266
HEADER    HYDROLASE                               01-NOV-10   2XWD
TITLE     X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH 5N,6O-(N'-(N-
TITLE    2 OCTYL)IMINO)NOJIRIMYCIN IN THE ACTIVE SITE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: ACID-BETA-GLUCOSIDASE, ALGLUCERASE,
COMPND   5  BETA-GLUCOCEREBROSIDASE, D-GLUCOSYL-N-ACYLSPHINGOSINE
COMPND   6  GLUCOHYDROLASE, 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_COMMON: CARROT;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4039
KEYWDS    GLUCOCEREBROSIDASE, HYDROLASE, GAUCHER DISEASE, SPHINGOLIPID
KEYWDS   2 METABOLISM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.BRUMSHTEIN,M.AGUILAR-MONCAYO,J.M.BENITO,C.ORTIZ MELLET,
AUTHOR   2 J.M.GARCIA FERNANDEZ,I.SILMAN,Y.SHAALTIEL,J.L.SUSSMAN,A.H.FUTERMAN
REVDAT   1   14-SEP-11 2XWD    0
JRNL        AUTH   B.BRUMSHTEIN,M.AGUILAR-MONCAYO,J.M.BENITO,
JRNL        AUTH 2 J.M.GARCIA FERNANDEZ,I.SILMAN,Y.SHAALTIEL,D.AVIEZER,
JRNL        AUTH 3 J.L.SUSSMAN,A.H.FUTERMAN,C.ORTIZ MELLET
JRNL        TITL   CYCLODEXTRIN-MEDIATED CRYSTALLIZATION OF ACID BETA-
JRNL        TITL 2 GLUCOSIDASE IN COMPLEX WITH AMPHIPHILIC BICYCLIC
JRNL        TITL 3 NOJIRIMYCIN ANALOGUES.
JRNL        REF    ORG.BIOMOL.CHEM.              V.   9  4160 2011
JRNL        REFN                   ISSN 1477-0520
JRNL        PMID   21483943
JRNL        DOI    10.1039/C1OB05200D
REMARK   2
REMARK   2 RESOLUTION.    2.66 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0088
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.66
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.92
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.79
REMARK   3   NUMBER OF REFLECTIONS             : 28378
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) : 0.15348
REMARK   3   R VALUE            (WORKING SET) : 0.15003
REMARK   3   FREE R VALUE                     : 0.21893
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1
REMARK   3   FREE R VALUE TEST SET COUNT      : 1510
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.657
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.726
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1821
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.62
REMARK   3   BIN R VALUE           (WORKING SET) : 0.194
REMARK   3   BIN FREE R VALUE SET COUNT          : 102
REMARK   3   BIN FREE R VALUE                    : 0.290
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7721
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 196
REMARK   3   SOLVENT ATOMS            : 266
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.304
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.03
REMARK   3    B22 (A**2) : -0.02
REMARK   3    B33 (A**2) : -0.02
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : -0.01
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.319
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.205
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.711
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8155 ; 0.016 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11126 ; 1.581 ; 1.966
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   981 ; 6.731 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   348 ;37.490 ;23.448
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1213 ;16.240 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    39 ;20.043 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1232 ; 0.111 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6162 ; 0.007 ; 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):  4916 ; 0.689 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7926 ; 1.349 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3239 ; 2.110 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3200 ; 3.368 ; 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 : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 8
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     -1       A      25      3
REMARK   3           1     B     -1       B      25      3
REMARK   3           2     A     27       A      50      3
REMARK   3           2     B     27       B      50      3
REMARK   3           3     A     65       A     168      3
REMARK   3           3     B     65       B     168      3
REMARK   3           4     A    170       A     311      3
REMARK   3           4     B    170       B     311      3
REMARK   3           5     A    320       A     340      3
REMARK   3           5     B    320       B     340      3
REMARK   3           6     A    360       A     395      3
REMARK   3           6     B    360       B     395      3
REMARK   3           7     A    400       A     449      3
REMARK   3           7     B    400       B     449      3
REMARK   3           8     A    456       A     497      3
REMARK   3           8     B    456       B     497      3
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1756 ;  0.05 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1756 ;  0.05 ;  0.05
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1666 ;  0.07 ;  5.00
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1666 ;  0.07 ;  5.00
REMARK   3   TIGHT THERMAL      1    A (A**2):   1756 ;  0.12 ;  0.50
REMARK   3   TIGHT THERMAL      1    B (A**2):   1756 ;  0.12 ;  0.50
REMARK   3   LOOSE THERMAL      1    A (A**2):   1666 ;  0.15 ; 10.00
REMARK   3   LOOSE THERMAL      1    B (A**2):   1666 ;  0.15 ; 10.00
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   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3   RIDING POSITIONS.
REMARK   4
REMARK   4 2XWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-NOV-10.
REMARK 100 THE PDBE ID CODE IS EBI-46040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-09
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                       : ID23-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : PT COATED SI MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28378
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.66
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.90
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 7.7
REMARK 200  R MERGE                    (I) : 0.18
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.66
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.72
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.3
REMARK 200  R MERGE FOR SHELL          (I) : 0.55
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.00
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 2J25
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 0.1 M TRIS PH
REMARK 280  6.5, 25% W/V PEG3350
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       48.30850
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 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: PISA
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: PISA
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     GLU A    -1
REMARK 465     ASP A    27
REMARK 465     PRO A    28
REMARK 465     PRO A    29
REMARK 465     THR A    30
REMARK 465     PHE A    31
REMARK 465     LEU A   498
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     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     LEU A  34    CG   CD1  CD2
REMARK 470     GLN A 143    CG   CD   OE1  NE2
REMARK 470     LYS A 155    CE   NZ
REMARK 470     ARG A 163    NE   CZ   NH1  NH2
REMARK 470     ARG A 277    NE   CZ   NH1  NH2
REMARK 470     GLU A 300    CG   CD   OE1  OE2
REMARK 470     LYS A 321    CE   NZ
REMARK 470     LYS A 346    CE   NZ
REMARK 470     PHE A 347    CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 441    CD   CE   NZ
REMARK 470     LYS A 466    CE   NZ
REMARK 470     GLN A 497    CG   CD   OE1  NE2
REMARK 470     PHE B   0    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LEU B  34    CG   CD1  CD2
REMARK 470     GLU B 111    CG   CD   OE1  OE2
REMARK 470     LYS B 155    CG   CD   CE   NZ
REMARK 470     LYS B 441    CD   CE   NZ
REMARK 470     ARG B 463    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 466    CD   CE   NZ
REMARK 470     GLN B 497    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  2029     O    HOH A  2081              1.84
REMARK 500   O    HOH A  2107     O    HOH A  2108              2.00
REMARK 500   O    HOH B  2036     O    HOH B  2117              2.05
REMARK 500   OG   SER B    12     O3   SO4 B  1502              2.09
REMARK 500   O    HOH A  2005     O    HOH A  2010              2.09
REMARK 500   O    HOH B  2094     O    HOH B  2095              2.13
REMARK 500   O    HOH B  2018     O    HOH B  2050              2.15
REMARK 500   O4   NAG A  1498     O5   NAG A  1499              2.15
REMARK 500   O    HOH B  2066     O    HOH B  2068              2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 111   CB    GLU A 111   CG      0.136
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    ASP A 218   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 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    PHE A  75     -134.77   -122.92
REMARK 500    ALA A 124     -161.96     69.04
REMARK 500    ASN A 146       32.39    -95.55
REMARK 500    LEU A 156      -72.35   -106.22
REMARK 500    ASN A 192     -164.32   -115.78
REMARK 500    GLU A 233      135.13    166.17
REMARK 500    LEU A 249      109.00   -160.70
REMARK 500    LEU A 281      -82.05     68.92
REMARK 500    THR A 323      -73.39   -118.01
REMARK 500    SER A 356      108.49    -57.60
REMARK 500    TRP A 381     -141.65    -79.18
REMARK 500    ASN A 382      126.81    -39.85
REMARK 500    VAL A 477      -35.84   -141.45
REMARK 500    TYR A 487      -12.46     68.37
REMARK 500    ASN B  19     -158.45   -140.31
REMARK 500    PHE B  75     -130.12   -123.09
REMARK 500    ALA B 124     -166.50     67.78
REMARK 500    ASN B 146       30.87    -93.65
REMARK 500    LEU B 156      -73.31   -108.74
REMARK 500    ASN B 192     -163.87   -120.94
REMARK 500    SER B 196     -169.75   -129.04
REMARK 500    GLU B 233      130.91    170.54
REMARK 500    TYR B 244      125.85    -38.60
REMARK 500    LEU B 249      112.24   -161.08
REMARK 500    LEU B 281      -77.51     68.04
REMARK 500    ALA B 318       86.00   -151.65
REMARK 500    THR B 323      -75.88   -114.51
REMARK 500    HIS B 374        0.38     81.19
REMARK 500    TRP B 381     -142.97    -85.02
REMARK 500    ASN B 382      121.01    -35.44
REMARK 500    VAL B 477      -36.33   -139.97
REMARK 500    TYR B 487      -12.41     74.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PHE B  26        21.4      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     LGS A 1510
REMARK 610     LGS B 1510
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 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 SO4 A1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LGS A1510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LGS B1510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800  SUGAR BOUND TO ASN A  19 RESIDUES 1498 TO 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF
REMARK 800  SUGAR BOUND TO ASN B  19 RESIDUES 1498 TO 1501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y7V   RELATED DB: PDB
REMARK 900  X-RAY STRUCTURE OF HUMAN ACID-BETA-GLUCOSIDASE
REMARK 900  COVALENTLYBOUND TO CONDURITOL B EPOXIDE
REMARK 900 RELATED ID: 2F61   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PARTIALLY DEGLYCOSYLATED ACID BETA-
REMARK 900  GLUCOSIDASE
REMARK 900 RELATED ID: 2V3F   RELATED DB: PDB
REMARK 900  ACID-BETA-GLUCOSIDASE PRODUCED IN CARROT
REMARK 900 RELATED ID: 2J25   RELATED DB: PDB
REMARK 900  PARTIALLY DEGLYCOSYLATED GLUCOCERAMIDASE
REMARK 900 RELATED ID: 2V3E   RELATED DB: PDB
REMARK 900  ACID-BETA-GLUCOSIDASE WITH N-NONYL-DEOXYNOJIRIMYCIN
REMARK 900 RELATED ID: 2WKL   RELATED DB: PDB
REMARK 900  VELAGLUCERASE ALFA
REMARK 900 RELATED ID: 2V3D   RELATED DB: PDB
REMARK 900  ACID-BETA-GLUCOSIDASE WITH N-BUTYL-DEOXYNOJIRIMYCIN
REMARK 900 RELATED ID: 1OGS   RELATED DB: PDB
REMARK 900  HUMAN ACID-BETA-GLUCOSIDASE
REMARK 900 RELATED ID: 2XWE   RELATED DB: PDB
REMARK 900  X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH 5N,6S
REMARK 900  -(N'-(N-OCTYL)IMINO)-6-THIONOJIRIMYCIN IN THE ACTIVE
REMARK 900   SITE
REMARK 900 RELATED ID: 2WCG   RELATED DB: PDB
REMARK 900  X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH N-
REMARK 900  OCTYL(CYCLIC GUANIDINE)-NOJIRIMYCIN IN THE ACTIVE SITE
DBREF  2XWD A    1   497  UNP    P04062   GLCM_HUMAN      20    516
DBREF  2XWD B    1   497  UNP    P04062   GLCM_HUMAN      20    516
SEQADV 2XWD GLU A   -1  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD PHE A    0  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD HIS A  495  UNP  P04062    ARG   514 VARIANT
SEQADV 2XWD LEU A  498  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD LEU A  499  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD VAL A  500  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD ASP A  501  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD THR A  502  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD MET A  503  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD GLU B   -1  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD PHE B    0  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD HIS B  495  UNP  P04062    ARG   514 VARIANT
SEQADV 2XWD LEU B  498  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD LEU B  499  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD VAL B  500  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD ASP B  501  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD THR B  502  UNP  P04062              EXPRESSION TAG
SEQADV 2XWD MET B  503  UNP  P04062              EXPRESSION TAG
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    NAG  A1498      14
HET    NAG  A1499      14
HET    MAN  A1500      11
HET    FUC  A1501      10
HET    SO4  A1502       5
HET    SO4  A1503       5
HET    SO4  A1504       5
HET    SO4  A1505       5
HET    SO4  A1506       5
HET    LGS  A1510      16
HET    NAG  B1498      14
HET    NAG  B1499      14
HET    BMA  B1500      11
HET    FUC  B1501      10
HET    SO4  B1502       5
HET    SO4  B1503       5
HET    SO4  B1504       5
HET    SO4  B1505       5
HET    SO4  B1506       5
HET    LGS  B1510      32
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM     SO4 SULFATE ION
HETNAM     LGS (3Z,5S,6R,7S,8R,8AR)-3-(OCTYLIMINO)HEXAHYDRO
HETNAM   2 LGS  [1,3]OXAZOLO[3,4-A]PYRIDINE-5,6,7,8-TETROL
HETNAM     BMA BETA-D-MANNOSE
FORMUL   3  NAG    4(C8 H15 N O6)
FORMUL   4  MAN    C6 H12 O6
FORMUL   5  FUC    2(C6 H12 O5)
FORMUL   6  SO4    10(O4 S 2-)
FORMUL   7  LGS    2(C15 H28 N2 O5)
FORMUL   8  BMA    C6 H12 O6
FORMUL   9  HOH   *266(H2 O)
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 SER A  237  LEU A  241  5                                   5
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 SER B  237  LEU B  241  5                                   5
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  LEU B  372  1                                  17
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 VAL A 305  HIS A 311  1  O  HIS A 306   N  MET A 335
SHEET    5  AC 9 ARG A 277  GLN A 284  1  O  LEU A 278   N  HIS A 306
SHEET    6  AC 9 PHE A 227  THR A 231  1  O  TRP A 228   N  ARG A 277
SHEET    7  AC 9 SER A 173  PRO A 178  1  O  LEU A 174   N  TRP A 228
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  LEU B 174   N  ALA B 229
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  2.12
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.17
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.06
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.14
LINK         ND2 ASN A  19                 C1  NAG A1498     1555   1555  1.40
LINK         O3  NAG A1498                 C1  FUC A1501     1555   1555  1.45
LINK         O4  NAG A1498                 C1  NAG A1499     1555   1555  1.40
LINK         O4  NAG A1499                 C1  MAN A1500     1555   1555  1.41
LINK         ND2 ASN B  19                 C1  NAG B1498     1555   1555  1.40
LINK         O4  NAG B1498                 C1  NAG B1499     1555   1555  1.41
LINK         O3  NAG B1498                 C1  FUC B1501     1555   1555  1.43
LINK         O4  NAG B1499                 C1  BMA B1500     1555   1555  1.41
CISPEP   1 LEU A  288    PRO A  289          0         1.93
CISPEP   2 GLY A  390    PRO A  391          0         1.97
CISPEP   3 LEU B  288    PRO B  289          0        -0.61
CISPEP   4 GLY B  390    PRO B  391          0         5.55
SITE     1 AC1  2 GLU A 254  ARG A 257
SITE     1 AC2  5 GLY A 193  LYS A 194  SER A 242  GLY A 243
SITE     2 AC2  5 HOH A2048
SITE     1 AC3  4 LYS A  79  TRP A 228  HIS A 306  HOH A2137
SITE     1 AC4  7 TYR A  11  SER A  12  ARG A 353  SER A 356
SITE     2 AC4  7 TRP A 357  ASP A 358  HOH A2136
SITE     1 AC5  3 ARG A  44  SER A  45  HOH A2013
SITE     1 AC6 10 ASP A 127  PHE A 128  TRP A 179  ASN A 234
SITE     2 AC6 10 GLU A 235  PHE A 246  TYR A 313  GLU A 340
SITE     3 AC6 10 SER A 345  TRP A 381
SITE     1 AC7  6 TYR B  11  SER B  12  ARG B 353  SER B 356
SITE     2 AC7  6 TRP B 357  ASP B 358
SITE     1 AC8  5 LYS B  79  TRP B 228  ARG B 277  HIS B 306
SITE     2 AC8  5 HOH B2127
SITE     1 AC9  3 ARG B  44  SER B  45  HOH B2007
SITE     1 BC1  4 GLY B 193  LYS B 194  SER B 242  GLY B 243
SITE     1 BC2  2 GLU B 254  ARG B 257
SITE     1 BC3 12 ASP B 127  PHE B 128  TRP B 179  ASN B 234
SITE     2 BC3 12 GLU B 235  TYR B 244  PHE B 246  TYR B 313
SITE     3 BC3 12 GLU B 340  SER B 345  TRP B 381  ASN B 396
SITE     1 BC4  1 ASN A  19
SITE     1 BC5  2 ASN B  19  HOH B2128
CRYST1   68.036   96.617   83.164  90.00 103.69  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      0.014698  0.000000  0.003580        0.00000
SCALE2      0.000000  0.010350  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012376        0.00000
      
PROCHECK
Go to PROCHECK summary
 References