HEADER HYDROLASE 03-MAY-00 1E1E
TITLE CRYSTAL STRUCTURE OF A MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE
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_SCIENTIFIC: ZEA MAYS;
SOURCE 3 ORGANISM_COMMON: MAIZE;
SOURCE 4 ORGANISM_TAXID: 4577;
SOURCE 5 STRAIN: CV. MUTIN;
SOURCE 6 TISSUE: COLEOPTILE;
SOURCE 7 ORGANELLE: CHLOROPLAST;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_VARIANT: PLYS S;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-21A;
SOURCE 12 EXPRESSION_SYSTEM_GENE: GLU1
KEYWDS GLYCOSIDE HYDROLASE, BETA-GLUCOSIDASE, FAMILY 1, RETENTION OF THE
KEYWDS 2 ANOMERIC CONFIGURATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.CZJZEK,M.CICEK,D.R.BEVAN,B.HENRISSAT,A.ESEN
REVDAT 4 06-DEC-23 1E1E 1 REMARK
REVDAT 3 16-SEP-15 1E1E 1 HEADER TITLE SOURCE KEYWDS
REVDAT 3 2 1 REMARK VERSN FORMUL
REVDAT 2 24-FEB-09 1E1E 1 VERSN
REVDAT 1 19-FEB-01 1E1E 0
JRNL AUTH M.CZJZEK,M.CICEK,V.ZAMBONI,W.P.BURMEISTER,D.R.BEVAN,
JRNL AUTH 2 B.HENRISSAT,A.ESEN
JRNL TITL CRYSTAL STRUCTURE OF A MONOCOTYLEDON (MAIZE ZMGLU1)
JRNL TITL 2 BETA-GLUCOSIDASE AND A MODEL OF ITS COMPLEX WITH
JRNL TITL 3 P-NITROPHENYL BETA-D-THIOGLUCOSIDE
JRNL REF BIOCHEM.J. V. 354 37 2001
JRNL REFN ISSN 0264-6021
JRNL PMID 11171077
JRNL DOI 10.1042/0264-6021:3540037
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.BANDARANAYAKE,A.ESEN
REMARK 1 TITL NUCLEOTIDE SEQUENCE OF A CDNA CORRESPONDING TO A SECOND
REMARK 1 TITL 2 BETA-GLUCOSIDASE GENE IN MAIZE
REMARK 1 REF PLANT PHYSIOL. V. 110 1048 1996
REMARK 1 REFN ISSN 0032-0889
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.100
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 38334
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) : 0.256
REMARK 3 FREE R VALUE : 0.322
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1900
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.75
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3750
REMARK 3 BIN R VALUE (WORKING SET) : 0.4400
REMARK 3 BIN FREE R VALUE : 0.4800
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 201
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 : 7971
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 331
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.39
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) : 0.44
REMARK 3 ESD FROM SIGMAA (A) : 0.63
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) : 0.59
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.83
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.350
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.899
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 : 0.33
REMARK 3 BSOL : 48.69
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 0.362 ; 10
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1E1E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1290004904.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 549492
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.07400
REMARK 200 R SYM FOR SHELL (I) : 0.20700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: PDB ENTRY 1CBG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, PH 5.60
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 59.17000
REMARK 290 SMTRY3 2 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 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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.7 KCAL/MOL
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 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 VAL A 10
REMARK 465 GLN A 11
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 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: 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 2165 O HOH A 2206 1.53
REMARK 500 O HOH B 2090 O HOH B 2091 1.61
REMARK 500 N HIS B 55 O HOH B 2024 1.89
REMARK 500 O SER B 51 O HOH B 2024 1.95
REMARK 500 O HOH A 2107 O HOH A 2108 2.01
REMARK 500 O GLY B 9 O HOH B 2003 2.02
REMARK 500 O HOH B 2022 O HOH B 2023 2.06
REMARK 500 NE1 TRP A 378 O HOH A 2165 2.06
REMARK 500 O TYR A 298 O HOH A 2139 2.06
REMARK 500 O HOH A 2199 O HOH A 2203 2.08
REMARK 500 O ILE A 370 O HOH A 2162 2.09
REMARK 500 OH TYR B 95 O HOH B 2032 2.15
REMARK 500 OE1 GLU A 464 O HOH A 2201 2.15
REMARK 500 O HOH A 2198 O HOH A 2200 2.15
REMARK 500 O SER B 163 OD2 ASP B 167 2.15
REMARK 500 OE1 GLU A 191 O HOH A 2107 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
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 LEU A 13 -138.61 -164.54
REMARK 500 SER A 14 132.58 178.13
REMARK 500 PRO A 15 -79.06 -41.72
REMARK 500 ASP A 22 28.85 -74.88
REMARK 500 HIS A 60 47.92 -141.32
REMARK 500 PRO A 61 -1.27 -55.75
REMARK 500 ILE A 72 -38.10 -135.55
REMARK 500 HIS A 142 57.78 -118.88
REMARK 500 TRP A 143 -17.48 82.43
REMARK 500 TYR A 153 22.33 -163.26
REMARK 500 HIS A 161 83.28 46.89
REMARK 500 LYS A 162 -55.89 175.99
REMARK 500 THR A 194 -70.96 -66.72
REMARK 500 PHE A 195 -60.27 -27.01
REMARK 500 TYR A 218 67.24 -112.42
REMARK 500 PRO A 219 44.26 -53.80
REMARK 500 VAL A 262 133.75 -170.43
REMARK 500 ASN A 285 -75.63 -93.18
REMARK 500 ARG A 307 -105.40 23.18
REMARK 500 ARG A 309 1.52 -67.01
REMARK 500 TYR A 333 -48.27 -132.00
REMARK 500 SER A 344 170.99 179.36
REMARK 500 TYR A 357 55.10 28.17
REMARK 500 ILE A 370 -3.92 -58.61
REMARK 500 TRP A 378 -9.75 -149.32
REMARK 500 TYR A 382 62.23 -151.79
REMARK 500 ASN A 399 60.71 38.42
REMARK 500 ASN A 407 129.43 -175.36
REMARK 500 ASP A 413 83.84 -151.06
REMARK 500 ASN A 426 78.82 -104.46
REMARK 500 SER A 458 96.35 69.40
REMARK 500 TRP A 465 -138.93 48.55
REMARK 500 ASN A 482 -117.57 -127.61
REMARK 500 ASP B 22 23.14 -73.25
REMARK 500 SER B 68 -168.59 -65.54
REMARK 500 SER B 70 52.38 -110.63
REMARK 500 ILE B 72 -40.66 -134.22
REMARK 500 ASN B 75 43.45 30.97
REMARK 500 PRO B 102 6.14 -67.83
REMARK 500 ILE B 104 -31.09 -155.80
REMARK 500 PRO B 106 11.31 -62.53
REMARK 500 ILE B 119 1.23 -63.43
REMARK 500 TYR B 121 -72.42 -41.33
REMARK 500 TRP B 143 -13.65 77.34
REMARK 500 LYS B 152 -82.83 -74.13
REMARK 500 HIS B 161 22.32 81.00
REMARK 500 LYS B 162 -22.85 -154.44
REMARK 500 PHE B 179 -33.46 -142.01
REMARK 500 ASP B 215 66.80 -102.27
REMARK 500 VAL B 225 -44.99 -132.08
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2018 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH A2035 DISTANCE = 7.17 ANGSTROMS
REMARK 525 HOH A2040 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A2041 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH A2042 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH A2061 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A2077 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A2087 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A2099 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B2017 DISTANCE = 7.99 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CBG RELATED DB: PDB
REMARK 900 HYDROLASE (O-GLYCOSYL)
REMARK 900 RELATED ID: 1E1F RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A MONOCOT (MAIZE ZMGLU1)BETA-GLUCOSIDASE IN
REMARK 900 COMPLEX WITH P-NITROPHENYL-BETA-D-THIOGLUCOSIDE
REMARK 900 RELATED ID: 1E4L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1)
REMARK 900 BETA-GLUCOSIDASE GLU191ASP
REMARK 900 RELATED ID: 1E4N RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1)
REMARK 900 BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH THE NATURAL AGLYCONE
REMARK 900 DIMBOA
DBREF 1E1E A 1 512 UNP P49235 BGLC_MAIZE 55 566
DBREF 1E1E B 1 512 UNP P49235 BGLC_MAIZE 55 566
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 GLU 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 GLU 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
FORMUL 3 HOH *331(H2 O)
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 ASN A 44 LYS A 48 5 5
HELIX 4 4 SER A 51 HIS A 60 1 10
HELIX 5 5 PRO A 61 ILE A 64 5 4
HELIX 6 6 ASN A 75 TYR A 80 1 6
HELIX 7 7 MET A 79 MET A 90 1 12
HELIX 8 8 SER A 100 LEU A 105 1 6
HELIX 9 9 ASN A 115 ASN A 132 1 18
HELIX 10 10 PRO A 146 TYR A 153 1 8
HELIX 11 11 GLY A 154 ASP A 158 5 5
HELIX 12 12 LYS A 162 GLY A 180 1 19
HELIX 13 13 GLU A 191 GLY A 201 1 11
HELIX 14 14 VAL A 225 TYR A 249 1 25
HELIX 15 15 SER A 271 LEU A 286 1 16
HELIX 16 16 LEU A 286 ARG A 295 1 10
HELIX 17 17 PRO A 299 ALA A 306 1 8
HELIX 18 18 ARG A 307 LEU A 310 5 4
HELIX 19 19 LYS A 314 ALA A 322 1 9
HELIX 20 20 LEU A 351 ALA A 356 5 6
HELIX 21 21 TYR A 382 LYS A 396 1 15
HELIX 22 22 PRO A 420 LEU A 425 1 6
HELIX 23 23 ASP A 427 LEU A 447 1 21
HELIX 24 24 GLU A 464 GLY A 468 5 5
HELIX 25 25 LYS A 489 ALA A 501 1 13
HELIX 26 26 SER B 14 ILE B 18 5 5
HELIX 27 27 GLN B 20 PHE B 24 5 5
HELIX 28 28 SER B 35 GLU B 40 1 6
HELIX 29 29 SER B 51 HIS B 60 1 10
HELIX 30 30 PRO B 61 ILE B 64 5 4
HELIX 31 31 ASN B 75 TYR B 80 1 6
HELIX 32 32 MET B 79 GLY B 91 1 13
HELIX 33 33 SER B 100 ILE B 104 5 5
HELIX 34 34 ASN B 115 ASN B 132 1 18
HELIX 35 35 PRO B 146 GLY B 154 1 9
HELIX 36 36 LYS B 162 PHE B 179 1 18
HELIX 37 37 GLU B 191 GLY B 201 1 11
HELIX 38 38 VAL B 225 TYR B 249 1 25
HELIX 39 39 SER B 271 LEU B 286 1 16
HELIX 40 40 LEU B 286 ARG B 295 1 10
HELIX 41 41 PRO B 299 ALA B 306 1 8
HELIX 42 42 ARG B 307 LEU B 310 5 4
HELIX 43 43 LEU B 351 ALA B 356 5 6
HELIX 44 44 PRO B 383 LYS B 396 1 14
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 9 GLU A 135 PRO A 136 0
SHEET 2 A 9 ALA A 94 ARG A 96 1 N TYR A 95 O GLU A 135
SHEET 3 A 9 THR A 29 ALA A 33 1 O ALA A 32 N ARG A 96
SHEET 4 A 9 VAL A 451 TRP A 457 1 O GLN A 452 N THR A 29
SHEET 5 A 9 ILE A 402 GLU A 406 1 O ILE A 402 N GLN A 452
SHEET 6 A 9 MET A 327 ASN A 340 1 O LEU A 328 N TYR A 403
SHEET 7 A 9 ARG A 255 PRO A 267 1 O LEU A 258 N GLY A 329
SHEET 8 A 9 ASN A 185 ASN A 190 1 O TRP A 186 N GLY A 257
SHEET 9 A 9 VAL A 138 PHE A 141 1 O VAL A 138 N LEU A 187
SHEET 1 A1 7 GLU A 135 PRO A 136 0
SHEET 2 A1 7 ALA A 94 ARG A 96 1 N TYR A 95 O GLU A 135
SHEET 3 A1 7 THR A 29 ALA A 33 1 O ALA A 32 N ARG A 96
SHEET 4 A1 7 VAL A 451 TRP A 457 1 O GLN A 452 N THR A 29
SHEET 5 A1 7 ILE A 402 GLU A 406 1 O ILE A 402 N GLN A 452
SHEET 6 A1 7 MET A 327 ASN A 340 1 O LEU A 328 N TYR A 403
SHEET 7 A1 7 ALA A 358 GLU A 361 -1 O SER A 359 N LYS A 339
SHEET 1 B 2 ASP A 411 VAL A 412 0
SHEET 2 B 2 GLU A 471 ARG A 472 -1 O ARG A 472 N ASP A 411
SHEET 1 C 2 VAL A 476 VAL A 478 0
SHEET 2 C 2 ARG A 486 MET A 488 0
SHEET 1 D 9 THR B 29 ALA B 33 0
SHEET 2 D 9 VAL B 451 TRP B 457 1 O GLN B 452 N THR B 29
SHEET 3 D 9 ILE B 402 GLU B 406 1 O ILE B 402 N GLN B 452
SHEET 4 D 9 LEU B 328 ASN B 331 1 O LEU B 328 N TYR B 403
SHEET 5 D 9 ARG B 255 ASP B 261 1 O LEU B 258 N GLY B 329
SHEET 6 D 9 ASN B 185 ASN B 190 1 O TRP B 186 N GLY B 257
SHEET 7 D 9 GLU B 135 PHE B 141 1 O VAL B 138 N LEU B 187
SHEET 8 D 9 ALA B 94 SER B 98 1 O TYR B 95 N TYR B 137
SHEET 9 D 9 THR B 29 ALA B 33 1 O ALA B 32 N ARG B 96
SHEET 1 E 3 GLY B 264 PRO B 267 0
SHEET 2 E 3 SER B 335 ASN B 340 1 O ARG B 336 N VAL B 266
SHEET 3 E 3 ALA B 358 GLU B 361 -1 O SER B 359 N LYS B 339
SHEET 1 F 2 ASP B 411 VAL B 412 0
SHEET 2 F 2 GLU B 471 ARG B 472 -1 O ARG B 472 N ASP B 411
SHEET 1 G 2 VAL B 476 VAL B 478 0
SHEET 2 G 2 ARG B 486 MET B 488 0
SSBOND 1 CYS A 210 CYS A 216 1555 1555 2.03
SSBOND 2 CYS B 210 CYS B 216 1555 1555 2.03
CISPEP 1 ALA A 206 PRO A 207 0 -0.26
CISPEP 2 ALA B 206 PRO B 207 0 0.17
CRYST1 62.880 118.340 77.100 90.00 90.30 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 0.015903 0.000000 0.000083 0.00000
SCALE2 0.000000 0.008450 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012970 0.00000
MTRIX1 1 0.885640 0.350570 0.304560 32.21348 1
MTRIX2 1 -0.321820 -0.009490 0.946750 27.02837 1
MTRIX3 1 0.334790 -0.936490 0.104410 32.03502 1
(ATOM LINES ARE NOT SHOWN.)
END
