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PDBsum entry 1e55

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Top Page protein ligands Protein-protein interface(s) links
Glycoside hydrolase PDB id
1e55
Jmol
Contents
Protein chains
492 a.a. *
Ligands
GLC-DHR ×2
Waters ×602
* Residue conservation analysis
HEADER    GLYCOSIDE HYDROLASE                     18-JUL-00   1E55
TITLE     CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT
TITLE    2 (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH
TITLE    3 THE COMPETITIVE INHIBITOR DHURRIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA-GLUCOSIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 3.2.1.21;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_COMMON: MAIZE;
SOURCE   3 STRAIN: CV. MUTIN;
SOURCE   4 TISSUE: COLEOPTILE;
SOURCE   5 ORGANELLE: CHLOROPLAST;
SOURCE   6 PLASMID: PET-21A;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_CELL: PLYS S CELLS;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-21A;
SOURCE  11 EXPRESSION_SYSTEM_GENE: GLU1
KEYWDS    GLYCOSIDE HYDROLASE, BETA-GLUCOSIDASE, FAMILY 1, RETENTION
KEYWDS   2 OF THE ANOMERIC CONFIGURATION, INACTIVE MUTANT E191D,
KEYWDS   3 COMPLEX WITH DHURRIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.CZJZEK,M.CICEK,D.R.BEVAN,V.ZAMBONI,B.HENRISSAT,A.ESEN
REVDAT   2   24-FEB-09 1E55    1       VERSN
REVDAT   1   11-DEC-00 1E55    0
JRNL        AUTH   M.CZJZEK,M.CICEK,V.ZAMBONI,D.R.BEVAN,B.HENRISSAT,
JRNL        AUTH 2 A.ESEN
JRNL        TITL   THE MECHANISM OF SUBSTRATE (AGLYCONE) SPECIFICITY
JRNL        TITL 2 IN BETA -GLUCOSIDASES IS REVEALED BY CRYSTAL
JRNL        TITL 3 STRUCTURES OF MUTANT MAIZE BETA -GLUCOSIDASE-
JRNL        TITL 4 DIMBOA, -DIMBOAGLC, AND -DHURRIN COMPLEXES
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  97 13555 2000
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   11106394
JRNL        DOI    10.1073/PNAS.97.25.13555
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.CICEK,A.ESEN
REMARK   1  TITL   EXPRESSION OF SOLUBLE AND CATALYTICALLY ACTIVE
REMARK   1  TITL 2 PLANT (MONOCOT) BETA-GLUCOSIDASES IN E. COLI
REMARK   1  REF    BIOTECHNOL.BIOENG.            V.  63   392 1999
REMARK   1  REFN
REMARK   1  PMID   10099619
REMARK   1  DOI    10.1002/(SICI)1097-0290(19990520)63:4<392::AI
REMARK   1  DOI  2 D-BIT2>3.0.CO;2-M
REMARK   2
REMARK   2 RESOLUTION.    2.0  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.0
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.05
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.00
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.5
REMARK   3   NUMBER OF REFLECTIONS             : 69029
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                     : 0.235
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 3513
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.0
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.7
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6284
REMARK   3   BIN R VALUE           (WORKING SET) : 0.309
REMARK   3   BIN FREE R VALUE                    : 0.327
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.9
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 342
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7950
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 44
REMARK   3   SOLVENT ATOMS            : 602
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.1
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23
REMARK   3   ESD FROM SIGMAA              (A) : 0.30
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 6.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.28
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.0062
REMARK   3   BOND ANGLES            (DEGREES) : 1.35
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.5
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.902
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.3604
REMARK   3   BSOL        : 41.17
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : 0.274 ; 5
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE-DHUR.PARAM
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE-DHUR.TOP
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1E55 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUL-00.
REMARK 100 THE PDBE ID CODE IS EBI-5172.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-00
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69098
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.100
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : 3.000
REMARK 200  R MERGE                    (I) : 0.11700
REMARK 200  R SYM                      (I) : 0.08400
REMARK 200   FOR THE DATA SET  : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.39700
REMARK 200  R SYM FOR SHELL            (I) : 0.28400
REMARK 200   FOR SHELL         : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS 1.0
REMARK 200 STARTING MODEL: 1E1E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 44.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22 % PEG 4000, 5 % ISOPROPANOL,
REMARK 280  0.1 M HEPES PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   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       45.90000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.75000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.50000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.75000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.90000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.50000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A,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 400
REMARK 400 COMPOUND
REMARK 400  CHAIN A, B ENGINEERED MUTATION GLU191ASP
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     SER A     1
REMARK 465     ALA A     2
REMARK 465     ARG A     3
REMARK 465     VAL A     4
REMARK 465     GLY A     5
REMARK 465     SER A     6
REMARK 465     GLN A     7
REMARK 465     ASN A     8
REMARK 465     GLY A     9
REMARK 465     LYS A   502
REMARK 465     LYS A   503
REMARK 465     PRO A   504
REMARK 465     SER A   505
REMARK 465     LYS A   506
REMARK 465     LYS A   507
REMARK 465     ILE A   508
REMARK 465     LEU A   509
REMARK 465     THR A   510
REMARK 465     PRO A   511
REMARK 465     ALA A   512
REMARK 465     SER B     1
REMARK 465     ALA B     2
REMARK 465     ARG B     3
REMARK 465     VAL B     4
REMARK 465     GLY B     5
REMARK 465     SER B     6
REMARK 465     GLN B     7
REMARK 465     ASN B     8
REMARK 465     GLY B     9
REMARK 465     VAL B    10
REMARK 465     GLN B    11
REMARK 465     LYS B   502
REMARK 465     LYS B   503
REMARK 465     PRO B   504
REMARK 465     SER B   505
REMARK 465     LYS B   506
REMARK 465     LYS B   507
REMARK 465     ILE B   508
REMARK 465     LEU B   509
REMARK 465     THR B   510
REMARK 465     PRO B   511
REMARK 465     ALA B   512
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    GLN A  11       92.18    -57.45
REMARK 500    ALA A  42       46.31     39.90
REMARK 500    TRP A 143       -7.44     75.54
REMARK 500    PHE A 156        0.93    -68.47
REMARK 500    ASP A 158      105.70    -41.00
REMARK 500    LYS A 162      -59.91   -137.36
REMARK 500    PRO A 219       45.45    -79.03
REMARK 500    ARG A 307     -120.90     49.08
REMARK 500    TYR A 382       72.64   -150.69
REMARK 500    SER A 458       95.35     85.80
REMARK 500    GLU A 464       50.25   -110.33
REMARK 500    TRP A 465     -127.99     54.35
REMARK 500    ASN A 482     -152.25    -79.31
REMARK 500    ASN A 483       56.13    -99.00
REMARK 500    SER B  70       41.56   -107.70
REMARK 500    TRP B 143       -8.80     72.40
REMARK 500    ASP B 158      104.05    -42.07
REMARK 500    LYS B 162      -56.36   -126.28
REMARK 500    ARG B 307     -126.78     48.15
REMARK 500    ASN B 450       34.75    -91.00
REMARK 500    SER B 458       94.25     83.11
REMARK 500    TRP B 465     -126.34     56.52
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHR A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHR B 514
REMARK 900
REMARK 900 RELATED ID: 1E1E   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF A MONOCOT (MAIZE ZMGLU1)
REMARK 900  BETA-GLUCOSIDASE
REMARK 900 RELATED ID: 1E1F   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF A MONOCOT (MAIZE ZMGLU1)
REMARK 900  BETA-GLUCOSIDASE IN COMPLEX WITH
REMARK 900  P-NITROPHENYL-BETA-D-THIOGLUCOSIDE
REMARK 900 RELATED ID: 1E4L   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE
REMARK 900  ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D
REMARK 900 RELATED ID: 1E4N   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE
REMARK 900  ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH THE
REMARK 900  NATURAL AGLYCONE DIMBOA
REMARK 900 RELATED ID: 1E56   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE
REMARK 900  ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH THE
REMARK 900  NATURAL SUBSTRATE DIMBOA-BETA-D-GLUCOSIDE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE N- AND C-TERMINAL RESID. WERE NOT SEEN IN DENSITY MAPS
DBREF  1E55 A    1   512  UNP    P49235   BGLC_MAIZE      55    566
DBREF  1E55 B    1   512  UNP    P49235   BGLC_MAIZE      55    566
SEQADV 1E55 ASP A  191  UNP  P49235    GLU   245 ENGINEERED MUTATION
SEQADV 1E55 ASP B  191  UNP  P49235    GLU   245 ENGINEERED MUTATION
SEQRES   1 A  512  SER ALA ARG VAL GLY SER GLN ASN GLY VAL GLN MET LEU
SEQRES   2 A  512  SER PRO SER GLU ILE PRO GLN ARG ASP TRP PHE PRO SER
SEQRES   3 A  512  ASP PHE THR PHE GLY ALA ALA THR SER ALA TYR GLN ILE
SEQRES   4 A  512  GLU GLY ALA TRP ASN GLU ASP GLY LYS GLY GLU SER ASN
SEQRES   5 A  512  TRP ASP HIS PHE CYS HIS ASN HIS PRO GLU ARG ILE LEU
SEQRES   6 A  512  ASP GLY SER ASN SER ASP ILE GLY ALA ASN SER TYR HIS
SEQRES   7 A  512  MET TYR LYS THR ASP VAL ARG LEU LEU LYS GLU MET GLY
SEQRES   8 A  512  MET ASP ALA TYR ARG PHE SER ILE SER TRP PRO ARG ILE
SEQRES   9 A  512  LEU PRO LYS GLY THR LYS GLU GLY GLY ILE ASN PRO ASP
SEQRES  10 A  512  GLY ILE LYS TYR TYR ARG ASN LEU ILE ASN LEU LEU LEU
SEQRES  11 A  512  GLU ASN GLY ILE GLU PRO TYR VAL THR ILE PHE HIS TRP
SEQRES  12 A  512  ASP VAL PRO GLN ALA LEU GLU GLU LYS TYR GLY GLY PHE
SEQRES  13 A  512  LEU ASP LYS SER HIS LYS SER ILE VAL GLU ASP TYR THR
SEQRES  14 A  512  TYR PHE ALA LYS VAL CYS PHE ASP ASN PHE GLY ASP LYS
SEQRES  15 A  512  VAL LYS ASN TRP LEU THR PHE ASN ASP PRO GLN THR PHE
SEQRES  16 A  512  THR SER PHE SER TYR GLY THR GLY VAL PHE ALA PRO GLY
SEQRES  17 A  512  ARG CYS SER PRO GLY LEU ASP CYS ALA TYR PRO THR GLY
SEQRES  18 A  512  ASN SER LEU VAL GLU PRO TYR THR ALA GLY HIS ASN ILE
SEQRES  19 A  512  LEU LEU ALA HIS ALA GLU ALA VAL ASP LEU TYR ASN LYS
SEQRES  20 A  512  HIS TYR LYS ARG ASP ASP THR ARG ILE GLY LEU ALA PHE
SEQRES  21 A  512  ASP VAL MET GLY ARG VAL PRO TYR GLY THR SER PHE LEU
SEQRES  22 A  512  ASP LYS GLN ALA GLU GLU ARG SER TRP ASP ILE ASN LEU
SEQRES  23 A  512  GLY TRP PHE LEU GLU PRO VAL VAL ARG GLY ASP TYR PRO
SEQRES  24 A  512  PHE SER MET ARG SER LEU ALA ARG GLU ARG LEU PRO PHE
SEQRES  25 A  512  PHE LYS ASP GLU GLN LYS GLU LYS LEU ALA GLY SER TYR
SEQRES  26 A  512  ASN MET LEU GLY LEU ASN TYR TYR THR SER ARG PHE SER
SEQRES  27 A  512  LYS ASN ILE ASP ILE SER PRO ASN TYR SER PRO VAL LEU
SEQRES  28 A  512  ASN THR ASP ASP ALA TYR ALA SER GLN GLU VAL ASN GLY
SEQRES  29 A  512  PRO ASP GLY LYS PRO ILE GLY PRO PRO MET GLY ASN PRO
SEQRES  30 A  512  TRP ILE TYR MET TYR PRO GLU GLY LEU LYS ASP LEU LEU
SEQRES  31 A  512  MET ILE MET LYS ASN LYS TYR GLY ASN PRO PRO ILE TYR
SEQRES  32 A  512  ILE THR GLU ASN GLY ILE GLY ASP VAL ASP THR LYS GLU
SEQRES  33 A  512  THR PRO LEU PRO MET GLU ALA ALA LEU ASN ASP TYR LYS
SEQRES  34 A  512  ARG LEU ASP TYR ILE GLN ARG HIS ILE ALA THR LEU LYS
SEQRES  35 A  512  GLU SER ILE ASP LEU GLY SER ASN VAL GLN GLY TYR PHE
SEQRES  36 A  512  ALA TRP SER LEU LEU ASP ASN PHE GLU TRP PHE ALA GLY
SEQRES  37 A  512  PHE THR GLU ARG TYR GLY ILE VAL TYR VAL ASP ARG ASN
SEQRES  38 A  512  ASN ASN CYS THR ARG TYR MET LYS GLU SER ALA LYS TRP
SEQRES  39 A  512  LEU LYS GLU PHE ASN THR ALA LYS LYS PRO SER LYS LYS
SEQRES  40 A  512  ILE LEU THR PRO ALA
SEQRES   1 B  512  SER ALA ARG VAL GLY SER GLN ASN GLY VAL GLN MET LEU
SEQRES   2 B  512  SER PRO SER GLU ILE PRO GLN ARG ASP TRP PHE PRO SER
SEQRES   3 B  512  ASP PHE THR PHE GLY ALA ALA THR SER ALA TYR GLN ILE
SEQRES   4 B  512  GLU GLY ALA TRP ASN GLU ASP GLY LYS GLY GLU SER ASN
SEQRES   5 B  512  TRP ASP HIS PHE CYS HIS ASN HIS PRO GLU ARG ILE LEU
SEQRES   6 B  512  ASP GLY SER ASN SER ASP ILE GLY ALA ASN SER TYR HIS
SEQRES   7 B  512  MET TYR LYS THR ASP VAL ARG LEU LEU LYS GLU MET GLY
SEQRES   8 B  512  MET ASP ALA TYR ARG PHE SER ILE SER TRP PRO ARG ILE
SEQRES   9 B  512  LEU PRO LYS GLY THR LYS GLU GLY GLY ILE ASN PRO ASP
SEQRES  10 B  512  GLY ILE LYS TYR TYR ARG ASN LEU ILE ASN LEU LEU LEU
SEQRES  11 B  512  GLU ASN GLY ILE GLU PRO TYR VAL THR ILE PHE HIS TRP
SEQRES  12 B  512  ASP VAL PRO GLN ALA LEU GLU GLU LYS TYR GLY GLY PHE
SEQRES  13 B  512  LEU ASP LYS SER HIS LYS SER ILE VAL GLU ASP TYR THR
SEQRES  14 B  512  TYR PHE ALA LYS VAL CYS PHE ASP ASN PHE GLY ASP LYS
SEQRES  15 B  512  VAL LYS ASN TRP LEU THR PHE ASN ASP PRO GLN THR PHE
SEQRES  16 B  512  THR SER PHE SER TYR GLY THR GLY VAL PHE ALA PRO GLY
SEQRES  17 B  512  ARG CYS SER PRO GLY LEU ASP CYS ALA TYR PRO THR GLY
SEQRES  18 B  512  ASN SER LEU VAL GLU PRO TYR THR ALA GLY HIS ASN ILE
SEQRES  19 B  512  LEU LEU ALA HIS ALA GLU ALA VAL ASP LEU TYR ASN LYS
SEQRES  20 B  512  HIS TYR LYS ARG ASP ASP THR ARG ILE GLY LEU ALA PHE
SEQRES  21 B  512  ASP VAL MET GLY ARG VAL PRO TYR GLY THR SER PHE LEU
SEQRES  22 B  512  ASP LYS GLN ALA GLU GLU ARG SER TRP ASP ILE ASN LEU
SEQRES  23 B  512  GLY TRP PHE LEU GLU PRO VAL VAL ARG GLY ASP TYR PRO
SEQRES  24 B  512  PHE SER MET ARG SER LEU ALA ARG GLU ARG LEU PRO PHE
SEQRES  25 B  512  PHE LYS ASP GLU GLN LYS GLU LYS LEU ALA GLY SER TYR
SEQRES  26 B  512  ASN MET LEU GLY LEU ASN TYR TYR THR SER ARG PHE SER
SEQRES  27 B  512  LYS ASN ILE ASP ILE SER PRO ASN TYR SER PRO VAL LEU
SEQRES  28 B  512  ASN THR ASP ASP ALA TYR ALA SER GLN GLU VAL ASN GLY
SEQRES  29 B  512  PRO ASP GLY LYS PRO ILE GLY PRO PRO MET GLY ASN PRO
SEQRES  30 B  512  TRP ILE TYR MET TYR PRO GLU GLY LEU LYS ASP LEU LEU
SEQRES  31 B  512  MET ILE MET LYS ASN LYS TYR GLY ASN PRO PRO ILE TYR
SEQRES  32 B  512  ILE THR GLU ASN GLY ILE GLY ASP VAL ASP THR LYS GLU
SEQRES  33 B  512  THR PRO LEU PRO MET GLU ALA ALA LEU ASN ASP TYR LYS
SEQRES  34 B  512  ARG LEU ASP TYR ILE GLN ARG HIS ILE ALA THR LEU LYS
SEQRES  35 B  512  GLU SER ILE ASP LEU GLY SER ASN VAL GLN GLY TYR PHE
SEQRES  36 B  512  ALA TRP SER LEU LEU ASP ASN PHE GLU TRP PHE ALA GLY
SEQRES  37 B  512  PHE THR GLU ARG TYR GLY ILE VAL TYR VAL ASP ARG ASN
SEQRES  38 B  512  ASN ASN CYS THR ARG TYR MET LYS GLU SER ALA LYS TRP
SEQRES  39 B  512  LEU LYS GLU PHE ASN THR ALA LYS LYS PRO SER LYS LYS
SEQRES  40 B  512  ILE LEU THR PRO ALA
HET    GLC  A 513      12
HET    GLC  B 513      12
HET    DHR  A 514      10
HET    DHR  B 514      10
HETNAM     GLC ALPHA-D-GLUCOSE
HETNAM     DHR (2S)-HYDROXY(4-HYDROXYPHENYL)ETHANENITRILE
HETSYN     GLC BETA-GLUCOSE
HETSYN     GLC BETA-GLUCOPYRANOSIDE
HETSYN     DHR PARA-HYDROXY-S-MANDELONITRILE
FORMUL   3  GLC    2(C6 H12 O6)
FORMUL   5  DHR    2(C8 H7 N O2)
FORMUL   7  HOH   *602(H2 O1)
HELIX    1   1 GLN A   20  PHE A   24  5                                   5
HELIX    2   2 SER A   35  GLU A   40  1                                   6
HELIX    3   3 SER A   51  HIS A   60  1                                  10
HELIX    4   4 PRO A   61  ILE A   64  5                                   4
HELIX    5   5 ASN A   75  TYR A   80  1                                   6
HELIX    6   6 MET A   79  MET A   90  1                                  12
HELIX    7   7 SER A  100  LEU A  105  1                                   6
HELIX    8   8 ASN A  115  ASN A  132  1                                  18
HELIX    9   9 PRO A  146  GLY A  154  1                                   9
HELIX   10  10 GLY A  155  ASP A  158  5                                   4
HELIX   11  11 LYS A  162  GLY A  180  1                                  19
HELIX   12  12 ASP A  191  GLY A  201  1                                  11
HELIX   13  13 VAL A  225  TYR A  249  1                                  25
HELIX   14  14 SER A  271  LEU A  286  1                                  16
HELIX   15  15 LEU A  286  GLY A  296  1                                  11
HELIX   16  16 PRO A  299  ARG A  307  1                                   9
HELIX   17  17 GLU A  308  LEU A  310  5                                   3
HELIX   18  18 LYS A  314  ALA A  322  1                                   9
HELIX   19  19 LEU A  351  ALA A  356  5                                   6
HELIX   20  20 PRO A  383  LYS A  396  1                                  14
HELIX   21  21 PRO A  420  ASN A  426  1                                   7
HELIX   22  22 ASP A  427  LEU A  447  1                                  21
HELIX   23  23 GLU A  464  GLY A  468  5                                   5
HELIX   24  24 LYS A  489  ALA A  501  1                                  13
HELIX   25  25 GLN B   20  PHE B   24  5                                   5
HELIX   26  26 SER B   35  GLU B   40  1                                   6
HELIX   27  27 SER B   51  HIS B   60  1                                  10
HELIX   28  28 PRO B   61  ILE B   64  5                                   4
HELIX   29  29 ASN B   75  TYR B   80  1                                   6
HELIX   30  30 MET B   79  MET B   90  1                                  12
HELIX   31  31 SER B  100  LEU B  105  1                                   6
HELIX   32  32 ASN B  115  ASN B  132  1                                  18
HELIX   33  33 PRO B  146  GLY B  154  1                                   9
HELIX   34  34 GLY B  155  ASP B  158  5                                   4
HELIX   35  35 LYS B  162  GLY B  180  1                                  19
HELIX   36  36 ASP B  191  GLY B  201  1                                  11
HELIX   37  37 VAL B  225  TYR B  249  1                                  25
HELIX   38  38 SER B  271  LEU B  286  1                                  16
HELIX   39  39 LEU B  286  GLY B  296  1                                  11
HELIX   40  40 PRO B  299  ARG B  307  1                                   9
HELIX   41  41 GLU B  308  LEU B  310  5                                   3
HELIX   42  42 LYS B  314  ALA B  322  1                                   9
HELIX   43  43 LEU B  351  ALA B  356  5                                   6
HELIX   44  44 TYR B  382  LYS B  396  1                                  15
HELIX   45  45 PRO B  420  ASN B  426  1                                   7
HELIX   46  46 ASP B  427  LEU B  447  1                                  21
HELIX   47  47 GLU B  464  GLY B  468  5                                   5
HELIX   48  48 LYS B  489  ALA B  501  1                                  13
SHEET    1   A 8 MET A 327  TYR A 332  0
SHEET    2   A 8 ARG A 255  VAL A 262  1  N  LEU A 258   O  MET A 327
SHEET    3   A 8 ASN A 185  LEU A 187  1  N  TRP A 186   O  ARG A 255
SHEET    4   A 8 GLU A 135  THR A 139  1  N  VAL A 138   O  ASN A 185
SHEET    5   A 8 ALA A  94  SER A  98  1  N  TYR A  95   O  GLU A 135
SHEET    6   A 8 THR A  29  ALA A  33  1  N  ALA A  32   O  ALA A  94
SHEET    7   A 8 VAL A 451  TRP A 457  1  N  TYR A 454   O  THR A  29
SHEET    8   A 8 ILE A 402  ILE A 404  1  N  ILE A 402   O  GLN A 452
SHEET    1   B 3 GLY A 264  PRO A 267  0
SHEET    2   B 3 SER A 335  ASN A 340  1  N  ARG A 336   O  GLY A 264
SHEET    3   B 3 ALA A 358  GLU A 361 -1  N  GLU A 361   O  PHE A 337
SHEET    1   C 2 VAL A 476  ASP A 479  0
SHEET    2   C 2 THR A 485  MET A 488 -1  N  TYR A 487   O  TYR A 477
SHEET    1   D 9 GLY B 453  TRP B 457  0
SHEET    2   D 9 THR B  29  ALA B  33  1  N  THR B  29   O  TYR B 454
SHEET    3   D 9 ALA B  94  SER B  98  1  N  ALA B  94   O  ALA B  32
SHEET    4   D 9 GLU B 135  THR B 139  1  N  GLU B 135   O  TYR B  95
SHEET    5   D 9 ASN B 185  LEU B 187  1  N  ASN B 185   O  VAL B 138
SHEET    6   D 9 ARG B 255  VAL B 262  1  N  ARG B 255   O  TRP B 186
SHEET    7   D 9 MET B 327  TYR B 332  1  N  MET B 327   O  LEU B 258
SHEET    8   D 9 ILE B 402  GLU B 406  1  N  TYR B 403   O  LEU B 328
SHEET    9   D 9 VAL B 451  TYR B 454  1  N  GLN B 452   O  ILE B 402
SHEET    1   E 3 GLY B 264  PRO B 267  0
SHEET    2   E 3 SER B 335  ASN B 340  1  N  ARG B 336   O  GLY B 264
SHEET    3   E 3 ALA B 358  GLU B 361 -1  N  GLU B 361   O  PHE B 337
SHEET    1   F 2 VAL B 476  ASP B 479  0
SHEET    2   F 2 THR B 485  MET B 488 -1  N  TYR B 487   O  TYR B 477
SSBOND   1 CYS A  210    CYS A  216                          1555   1555  2.04
SSBOND   2 CYS B  210    CYS B  216                          1555   1555  2.03
LINK         CZ  PHE A 466                 O6  DHR A 514     1555   1555  1.79
LINK         O1  GLC A 513                 C1  DHR A 514     1555   1555  1.62
LINK         O1  GLC B 513                 C2  DHR B 514     1555   1555  1.98
LINK         O1  GLC B 513                 C1  DHR B 514     1555   1555  1.54
CISPEP   1 ALA A  206    PRO A  207          0         0.23
CISPEP   2 ALA B  206    PRO B  207          0         0.15
SITE     1 AC1 11 HIS A 142  ASP A 191  THR A 194  TYR A 333
SITE     2 AC1 11 GLU A 406  TRP A 457  GLU A 464  TYR A 473
SITE     3 AC1 11 DHR A 514  HOH A2275  HOH A2298
SITE     1 AC2 11 ASP B 191  TYR B 333  TRP B 378  GLU B 406
SITE     2 AC2 11 TRP B 457  GLU B 464  TYR B 473  DHR B 514
SITE     3 AC2 11 HOH B2127  HOH B2288  HOH B2302
SITE     1 AC3  4 PHE A 198  PHE A 466  GLC A 513  HOH A2300
SITE     1 AC4  6 TRP B 143  THR B 194  PHE B 198  TRP B 378
SITE     2 AC4  6 PHE B 466  GLC B 513
CRYST1   91.800   95.000  117.500  90.00  90.00  90.00 P 21 21 21    8
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      0.010893  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010526  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008511        0.00000
MTRIX1   1 -0.823600  0.366290 -0.433020       57.07482    1
MTRIX2   1  0.372980 -0.225380 -0.900050       60.46521    1
MTRIX3   1 -0.427270 -0.902790  0.049010       75.30616    1
      
PROCHECK
Go to PROCHECK summary
 References