HEADER HYDROLASE 09-FEB-03 1OCQ
TITLE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.08
TITLE 2 ANGSTROM RESOLUTION WITH CELLOBIO-DERIVED ISOFAGOMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOGLUCANASE 5A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC CORE DOMAIN ONLY, RESIDUES 27-329;
COMPND 5 SYNONYM: ENDO-1,4-BETA-GLUCANASE, ALKALINE CELLULASE, CEL5A;
COMPND 6 EC: 3.2.1.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS AGARADHAERENS;
SOURCE 3 ORGANISM_TAXID: 76935;
SOURCE 4 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1423;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: PL2306;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PMOL995;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: THERMAMYL-AMYLASE PROMOTER
KEYWDS CELLULOSE DEGRADATION, HYDROLASE, GLYCOSIDASE, ENDOGLUCANASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VARROT,J.MACDONALD,R.V.STICK,S.G.WITHERS,G.J.DAVIES
REVDAT 6 13-DEC-23 1OCQ 1 HETSYN
REVDAT 5 29-JUL-20 1OCQ 1 COMPND REMARK HETNAM HETSYN
REVDAT 5 2 1 SITE
REVDAT 4 06-MAR-19 1OCQ 1 REMARK LINK
REVDAT 3 22-JUL-15 1OCQ 1 SOURCE REMARK VERSN HETSYN
REVDAT 3 2 1 FORMUL SITE
REVDAT 2 24-FEB-09 1OCQ 1 VERSN
REVDAT 1 26-JUN-03 1OCQ 0
JRNL AUTH A.VARROT,C.A.TARLING,J.M.MACDONALD,R.V.STICK,D.L.ZECHEL,
JRNL AUTH 2 S.G.WITHERS,G.J.DAVIES
JRNL TITL DIRECT OBSERVATION OF THE PROTONATION STATE OF AN IMINO
JRNL TITL 2 SUGAR GLYCOSIDASE INHIBITOR UPON BINDING
JRNL REF J.AM.CHEM.SOC. V. 125 7496 2003
JRNL REFN ISSN 0002-7863
JRNL PMID 12812472
JRNL DOI 10.1021/JA034917K
REMARK 2
REMARK 2 RESOLUTION. 1.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 119168
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) : 0.115
REMARK 3 R VALUE (WORKING SET) : 0.115
REMARK 3 FREE R VALUE : 0.127
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6322
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.11
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8574
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1590
REMARK 3 BIN FREE R VALUE SET COUNT : 476
REMARK 3 BIN FREE R VALUE : 0.1700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2377
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 445
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.11000
REMARK 3 B22 (A**2) : -0.53000
REMARK 3 B33 (A**2) : -0.58000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.022
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.022
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.015
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.306
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.985
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.983
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2511 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2114 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3421 ; 1.766 ; 1.929
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4950 ; 2.130 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 303 ; 6.433 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 361 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2830 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 495 ; 0.009 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 495 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2429 ; 0.273 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1255 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 248 ; 0.162 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 13 ; 0.163 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 35 ; 0.274 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 37 ; 0.127 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1499 ; 1.358 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2416 ; 2.046 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1012 ; 2.690 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1003 ; 3.876 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1OCQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1290012118.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.20
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) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126591
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.080
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.37700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTR 6A3H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS USED AT A CONCENTRATION OF
REMARK 280 10MG/ML. IT WAS INCUBATED WITH 5MM CELLOBIO-DERIVED ISOFAGOMINE
REMARK 280 FOR AN HOUR PRIOR CRYSTALLISATION. THE VAPOR DIFFUSION METHOD
REMARK 280 WAS USED. 1.3 M AMMONIUM SULPHATE WERE USED AS PRECIPITANT. 20 %
REMARK 280 GLYCEROL WAS ADDED FOR CRYOPROTECTION, PH 5.20
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 27.51150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.44950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.83850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.44950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.51150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.83850
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 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENDOHYDROLYSES 1,4-BETA-D-GLUCOSIDIC LINKAGES IN CELLULOSE,
REMARK 400 LICHENIN AND CEREAL BETA-D-GLUCANS.
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 ASP A 1
REMARK 465 ASN A 2
REMARK 465 ASP A 3
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 74 CB - CG - OD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP A 144 CB - CG - OD1 ANGL. DEV. = 7.3 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 LEU A 103 -79.05 -158.04
REMARK 500 ALA A 137 93.91 -164.45
REMARK 500 ASN A 168 6.76 -155.89
REMARK 500 ASN A 188 60.94 -150.96
REMARK 500 ASP A 237 -153.80 -132.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 62 0.09 SIDE CHAIN
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 A2015 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A2021 DISTANCE = 7.93 ANGSTROMS
REMARK 525 HOH A2023 DISTANCE = 9.05 ANGSTROMS
REMARK 525 HOH A2036 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A2067 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A2176 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A2316 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A2317 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A2439 DISTANCE = 7.23 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AB" 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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A3H RELATED DB: PDB
REMARK 900 ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6A RESOLUTION
REMARK 900 RELATED ID: 1E5J RELATED DB: PDB
REMARK 900 ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS IN THE TETRAGONAL
REMARK 900 CRYSTAL FORM IN COMPLEX WITH METHYL-4II-S-ALPHA- CELLOBIOSYL-4II-
REMARK 900 THIO-BETA-CELLOBIOSIDE
REMARK 900 RELATED ID: 1H11 RELATED DB: PDB
REMARK 900 2-DEOXY-2-FLURO-B-D-CELLOTRIOSYL/ENZYME INTERMEDIATE COMPLEX OF THE
REMARK 900 ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.08 ANGSTROM
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1H2J RELATED DB: PDB
REMARK 900 ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS IN THE ORTHORHOMBIC
REMARK 900 CRYSTAL FORM IN COMPLEX WITH UNHYDROLYSED AND COVALENTLY LINKED 2,4-
REMARK 900 DINITROPHENYL-2-DEOXY-2FLUORO- CELLOBIOSIDE AT 1.15 A RESOLUTION
REMARK 900 RELATED ID: 1H5V RELATED DB: PDB
REMARK 900 THIOPENTASACCHARIDE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM
REMARK 900 BACILLUS AGARADHARENS AT 1.1 A RESOLUTION IN THE TETRAGONAL CRYSTAL
REMARK 900 FORM
REMARK 900 RELATED ID: 1HF6 RELATED DB: PDB
REMARK 900 ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS IN THE ORTHORHOMBIC
REMARK 900 CRYSTAL FORM IN COMPLEX WITH CELLOTRIOSE
REMARK 900 RELATED ID: 1QHZ RELATED DB: PDB
REMARK 900 NATIVE TETRAGONAL STRUCTURE OF THE ENDOGLUCANASE CEL5A FROM
REMARK 900 BACILLUS AGARADHAERENS
REMARK 900 RELATED ID: 1QI0 RELATED DB: PDB
REMARK 900 ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS IN THE TETRAGONAL
REMARK 900 CRYSTAL FORM IN COMPLEX WITH CELLOBIOSE
REMARK 900 RELATED ID: 1QI2 RELATED DB: PDB
REMARK 900 ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS IN THE TETRAGONAL
REMARK 900 CRYSTAL FORM IN COMPLEX WITH 2',4'-DINITROPHENYL 2-DEOXY-2- FLUORO-
REMARK 900 B-D-CELLOTRIOSIDE
REMARK 900 RELATED ID: 2A3H RELATED DB: PDB
REMARK 900 CELLOBIOSE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS
REMARK 900 AGARADHERANS AT 2.0 A RESOLUTION
REMARK 900 RELATED ID: 3A3H RELATED DB: PDB
REMARK 900 CELLOTRIOSE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS
REMARK 900 AGARADHERANS AT 1.6 A RESOLUTION
REMARK 900 RELATED ID: 4A3H RELATED DB: PDB
REMARK 900 2',4' DINITROPHENYL-2-DEOXY-2-FLURO-B-D -CELLOBIOSIDE COMPLEX OF
REMARK 900 THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS AT 1.6 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 5A3H RELATED DB: PDB
REMARK 900 2-DEOXY-2-FLURO-B-D-CELLOBIOSYL/ENZYME INTERMEDIATE COMPLEX OF THE
REMARK 900 ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.8 ANGSTROMS
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 6A3H RELATED DB: PDB
REMARK 900 2-DEOXY-2-FLURO-B-D-CELLOTRIOSYL/ENZYME INTERMEDIATE COMPLEX OF THE
REMARK 900 ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.6 ANGSTROM
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 7A3H RELATED DB: PDB
REMARK 900 NATIVE ENDOGLUCANASE CEL5A CATALYTIC CORE DOMAIN AT 0.95 ANGSTROMS
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 8A3H RELATED DB: PDB
REMARK 900 CELLOBIOSE-DERIVED IMIDAZOLE COMPLEX OF THE ENDOGLUCANASE CEL5A
REMARK 900 FROM BACILLUS AGARADHAERENS AT 0.97 A RESOLUTION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 26 RESIDUES IN THE DATABASE CORRESPOND TO THE
REMARK 999 PROSEQUENCE. OUR NUMBERING BEGIN AT THE FIRST RESIDUE
REMARK 999 OBTAINED AFTER CLEAVAGE OF THE PROSEQUENCE
DBREF 1OCQ A 1 303 UNP O85465 GUN5_BACAG 27 329
SEQRES 1 A 303 ASP ASN ASP SER VAL VAL GLU GLU HIS GLY GLN LEU SER
SEQRES 2 A 303 ILE SER ASN GLY GLU LEU VAL ASN GLU ARG GLY GLU GLN
SEQRES 3 A 303 VAL GLN LEU LYS GLY MET SER SER HIS GLY LEU GLN TRP
SEQRES 4 A 303 TYR GLY GLN PHE VAL ASN TYR GLU SER MET LYS TRP LEU
SEQRES 5 A 303 ARG ASP ASP TRP GLY ILE ASN VAL PHE ARG ALA ALA MET
SEQRES 6 A 303 TYR THR SER SER GLY GLY TYR ILE ASP ASP PRO SER VAL
SEQRES 7 A 303 LYS GLU LYS VAL LYS GLU ALA VAL GLU ALA ALA ILE ASP
SEQRES 8 A 303 LEU ASP ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU SER
SEQRES 9 A 303 ASP ASN ASP PRO ASN ILE TYR LYS GLU GLU ALA LYS ASP
SEQRES 10 A 303 PHE PHE ASP GLU MET SER GLU LEU TYR GLY ASP TYR PRO
SEQRES 11 A 303 ASN VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY SER
SEQRES 12 A 303 ASP VAL THR TRP GLY ASN GLN ILE LYS PRO TYR ALA GLU
SEQRES 13 A 303 GLU VAL ILE PRO ILE ILE ARG ASN ASN ASP PRO ASN ASN
SEQRES 14 A 303 ILE ILE ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL
SEQRES 15 A 303 HIS HIS ALA ALA ASP ASN GLN LEU ALA ASP PRO ASN VAL
SEQRES 16 A 303 MET TYR ALA PHE HIS PHE TYR ALA GLY THR HIS GLY GLN
SEQRES 17 A 303 ASN LEU ARG ASP GLN VAL ASP TYR ALA LEU ASP GLN GLY
SEQRES 18 A 303 ALA ALA ILE PHE VAL SER GLU TRP GLY THR SER ALA ALA
SEQRES 19 A 303 THR GLY ASP GLY GLY VAL PHE LEU ASP GLU ALA GLN VAL
SEQRES 20 A 303 TRP ILE ASP PHE MET ASP GLU ARG ASN LEU SER TRP ALA
SEQRES 21 A 303 ASN TRP SER LEU THR HIS LYS ASP GLU SER SER ALA ALA
SEQRES 22 A 303 LEU MET PRO GLY ALA ASN PRO THR GLY GLY TRP THR GLU
SEQRES 23 A 303 ALA GLU LEU SER PRO SER GLY THR PHE VAL ARG GLU LYS
SEQRES 24 A 303 ILE ARG GLU SER
HET IFM A 500 10
HET BGC A 501 11
HET GOL A 502 6
HET GOL A 503 12
HET SO4 A 505 5
HETNAM IFM 5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN IFM AFEGOSTAT; ISOFAGOMINE; (3R,4R,5R)-5-(HYDROXYMETHYL)
HETSYN 2 IFM PIPERIDINE-3,4-DIOL
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 IFM C6 H13 N O3
FORMUL 3 BGC C6 H12 O6
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 6 SO4 O4 S 2-
FORMUL 7 HOH *445(H2 O)
HELIX 1 1 SER A 4 GLY A 10 1 7
HELIX 2 2 GLY A 36 GLY A 41 1 6
HELIX 3 3 GLN A 42 VAL A 44 5 3
HELIX 4 4 ASN A 45 ASP A 55 1 11
HELIX 5 5 SER A 77 ASP A 93 1 17
HELIX 6 6 TYR A 111 GLY A 127 1 17
HELIX 7 7 GLN A 150 ASN A 164 1 15
HELIX 8 8 THR A 175 GLN A 180 1 6
HELIX 9 9 ASP A 181 ASP A 187 1 7
HELIX 10 10 GLY A 207 GLN A 220 1 14
HELIX 11 11 PHE A 241 ARG A 255 1 15
HELIX 12 12 THR A 285 GLU A 288 5 4
HELIX 13 13 SER A 290 SER A 303 1 14
SHEET 1 AA 2 SER A 13 SER A 15 0
SHEET 2 AA 2 GLU A 18 VAL A 20 -1 O GLU A 18 N SER A 15
SHEET 1 AB 9 LYS A 30 SER A 34 0
SHEET 2 AB 9 TRP A 259 LEU A 264 1 O TRP A 259 N GLY A 31
SHEET 3 AB 9 ILE A 224 GLY A 230 1 O VAL A 226 N ALA A 260
SHEET 4 AB 9 VAL A 195 TYR A 202 1 O TYR A 197 N PHE A 225
SHEET 5 AB 9 ILE A 171 VAL A 173 1 O ILE A 171 N MET A 196
SHEET 6 AB 9 VAL A 132 GLU A 135 1 O TYR A 134 N ILE A 172
SHEET 7 AB 9 TYR A 95 HIS A 101 1 O VAL A 96 N ILE A 133
SHEET 8 AB 9 VAL A 60 TYR A 66 1 O PHE A 61 N ILE A 97
SHEET 9 AB 9 LYS A 30 SER A 34 1 O MET A 32 N ARG A 62
LINK O4 IFM A 500 C1 BGC A 501 1555 1555 1.42
CISPEP 1 TRP A 262 SER A 263 0 0.77
CRYST1 55.023 69.677 76.899 90.00 90.00 90.00 P 21 21 21 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 0.018174 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014352 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013004 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
