HEADER HYDROLASE 16-JUL-15 5A8P
TITLE CRYSTAL STRUCTURE BETA-GLUCANASE SDGLUC5_26A FROM SACCHAROPHAGUS
TITLE 2 DEGRADANS IN COMPLEX WITH TETRASACCHARIDE B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE RETAINING B-GLYCOSIDASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 1-365;
COMPND 5 SYNONYM: SDGLUC5_26A;
COMPND 6 EC: 3.2.1.73;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPHAGUS DEGRADANS 2-40;
SOURCE 3 ORGANISM_TAXID: 203122;
SOURCE 4 ATCC: 43961;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PDEST
KEYWDS HYDROLASE, CAZYME, GLYCOSIDE HYDROLASE, BETA-GLUCANASE, GH5_26
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SULZENBACHER,M.LAFOND,T.FREYD,B.HENRISSAT,R.M.COUTINHO,J.G.BERRIN,
AUTHOR 2 M.L.GARRON
REVDAT 5 10-JAN-24 5A8P 1 HETSYN
REVDAT 4 29-JUL-20 5A8P 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 13-SEP-17 5A8P 1 REMARK
REVDAT 2 06-APR-16 5A8P 1 JRNL
REVDAT 1 20-JAN-16 5A8P 0
JRNL AUTH M.LAFOND,G.SULZENBACHER,T.FREYD,B.HENRISSAT,J.G.BERRIN,
JRNL AUTH 2 M.L.GARRON
JRNL TITL THE QUATERNARY STRUCTURE OF A GLYCOSIDE HYDROLASE DICTATES
JRNL TITL 2 SPECIFICITY TOWARDS BETA-GLUCANS
JRNL REF J.BIOL.CHEM. V. 291 7183 2016
JRNL REFN ISSN 0021-9258
JRNL PMID 26755730
JRNL DOI 10.1074/JBC.M115.695999
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 25216
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1330
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1850
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1970
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2775
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 99
REMARK 3 SOLVENT ATOMS : 276
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.172
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.091
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.754
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3009 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2761 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4104 ; 1.138 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6383 ; 0.717 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 349 ; 5.937 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 145 ;36.916 ;24.276
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 471 ;11.619 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;14.576 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 434 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3313 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 721 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 873 ; 0.231 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2635 ; 0.162 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1479 ; 0.187 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1556 ; 0.080 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 88 ; 0.130 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.080 ; 0.200
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): 35 ; 0.287 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 47 ; 0.119 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.219 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 29 A 364
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0155 54.8653 45.2915
REMARK 3 T TENSOR
REMARK 3 T11: 0.0222 T22: 0.0067
REMARK 3 T33: 0.0093 T12: 0.0064
REMARK 3 T13: 0.0067 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.4813 L22: 0.2887
REMARK 3 L33: 0.4147 L12: -0.0698
REMARK 3 L13: -0.1493 L23: -0.1149
REMARK 3 S TENSOR
REMARK 3 S11: 0.0216 S12: -0.0178 S13: 0.0367
REMARK 3 S21: 0.0523 S22: 0.0193 S23: 0.0264
REMARK 3 S31: -0.0562 S32: -0.0375 S33: -0.0408
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 : 1.20
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. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 5A8P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1290064390.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8856
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26553
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 48.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.90
REMARK 200 R MERGE FOR SHELL (I) : 0.77000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: WWPDB ENTRY 5A8O
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULPHATE, 0.1 M SODIUM
REMARK 280 CACODYLATE BUFFER PH 6.0, 25% (W/V) PEG 8000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+3/4,X+1/4,-Z+1/4
REMARK 290 14555 -Y+3/4,-X+3/4,-Z+3/4
REMARK 290 15555 Y+1/4,-X+1/4,Z+3/4
REMARK 290 16555 -Y+1/4,X+3/4,Z+1/4
REMARK 290 17555 X+3/4,Z+1/4,-Y+1/4
REMARK 290 18555 -X+1/4,Z+3/4,Y+1/4
REMARK 290 19555 -X+3/4,-Z+3/4,-Y+3/4
REMARK 290 20555 X+1/4,-Z+1/4,Y+3/4
REMARK 290 21555 Z+3/4,Y+1/4,-X+1/4
REMARK 290 22555 Z+1/4,-Y+1/4,X+3/4
REMARK 290 23555 -Z+1/4,Y+3/4,X+1/4
REMARK 290 24555 -Z+3/4,-Y+3/4,-X+3/4
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 72.19100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.19100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.19100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.19100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 72.19100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.19100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 72.19100
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 72.19100
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 72.19100
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 72.19100
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 72.19100
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 72.19100
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 72.19100
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 72.19100
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 72.19100
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 72.19100
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 72.19100
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 72.19100
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 108.28650
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 36.09550
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 36.09550
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 108.28650
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 108.28650
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 108.28650
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 36.09550
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 36.09550
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 108.28650
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 36.09550
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 108.28650
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 36.09550
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 108.28650
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 36.09550
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 36.09550
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 36.09550
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 108.28650
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 36.09550
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 108.28650
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 108.28650
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 108.28650
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 36.09550
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 36.09550
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 108.28650
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 108.28650
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 36.09550
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 36.09550
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 36.09550
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 36.09550
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 108.28650
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 36.09550
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 108.28650
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 36.09550
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 108.28650
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 108.28650
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 108.28650
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -131.6 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 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 1.000000 0.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2069 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2070 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2273 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2274 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 LYS A 5
REMARK 465 PHE A 6
REMARK 465 LEU A 7
REMARK 465 ALA A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 LEU A 11
REMARK 465 CYS A 12
REMARK 465 LEU A 13
REMARK 465 LEU A 14
REMARK 465 ALA A 15
REMARK 465 SER A 16
REMARK 465 ALA A 17
REMARK 465 SER A 18
REMARK 465 ALA A 19
REMARK 465 LEU A 20
REMARK 465 SER A 21
REMARK 465 ALA A 22
REMARK 465 ASN A 23
REMARK 465 ASN A 24
REMARK 465 SER A 25
REMARK 465 ALA A 26
REMARK 465 PRO A 27
REMARK 465 SER A 28
REMARK 465 ARG A 365
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG SER A 38 OD2 ASP A 41 13455 2.17
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 GLU A 245 54.38 -91.64
REMARK 500 TRP A 278 -30.98 -149.20
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 PGE A 1376
REMARK 610 PGE A 1377
REMARK 610 PGE A 1378
REMARK 610 PGE A 1379
REMARK 610 PGE A 1380
REMARK 610 PGE A 1381
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1370 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 178 O
REMARK 620 2 VAL A 181 O 94.0
REMARK 620 3 HOH A2153 O 103.4 91.6
REMARK 620 4 HOH A2154 O 96.8 169.0 83.9
REMARK 620 5 HOH A2160 O 115.9 91.4 140.2 85.6
REMARK 620 N 1 2 3 4
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: 5A8M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SELENOMETHIONINE DERIVATIVE OF BETA-
REMARK 900 GLUCANASE SDGLUC5_26A FROM SACCHAROPHAGUS DEGRADANS
REMARK 900 RELATED ID: 5A8N RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NATIVE FORM OF BETA-GLUCANASE SDGLUC5_26A
REMARK 900 FROM SACCHAROPHAGUS DEGRADANS
REMARK 900 RELATED ID: 5A8O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA-GLUCANASE SDGLUC5_26A FROM SACCHAROPHAGUS
REMARK 900 DEGRADANS IN COMPLEX WITH CELLOTETRAOSE
REMARK 900 RELATED ID: 5A8Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE BETA-GLUCANASE SDGLUC5_26A FROM SACCHAROPHAGUS
REMARK 900 DEGRADANS IN COMPLEX WITH TETRASACCHARIDE A OBTAINED BY SOAKING
REMARK 900 RELATED ID: 5A94 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE BETA-GLUCANASE SDGLUC5_26A FROM SACCHAROPHAGUS
REMARK 900 DEGRADANS IN COMPLEX WITH TETRASACCHARIDE A , FORM 1
REMARK 900 RELATED ID: 5A95 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE BETA-GLUCANASE SDGLUC5_26A FROM SACCHAROPHAGUS
REMARK 900 DEGRADANS IN COMPLEX WITH TETRASACCHARIDE A , FORM 2
DBREF 5A8P A 1 365 UNP Q21KE5 Q21KE5_SACD2 1 365
SEQADV 5A8P ARG A 82 UNP Q21KE5 GLN 82 CONFLICT
SEQADV 5A8P GLN A 176 UNP Q21KE5 LYS 176 CONFLICT
SEQADV 5A8P GLN A 291 UNP Q21KE5 GLU 291 ENGINEERED MUTATION
SEQRES 1 A 365 MET ARG THR THR LYS PHE LEU ALA LEU ALA LEU CYS LEU
SEQRES 2 A 365 LEU ALA SER ALA SER ALA LEU SER ALA ASN ASN SER ALA
SEQRES 3 A 365 PRO SER ASN ASP TRP TRP ASP ILE PRO TYR PRO SER GLN
SEQRES 4 A 365 PHE ASP VAL LYS SER LEU LYS THR GLN SER PHE ILE SER
SEQRES 5 A 365 VAL LYS GLY ASN LYS PHE ILE ASP ASP LYS GLY LYS THR
SEQRES 6 A 365 PHE THR PHE ARG GLY VAL ASN ILE ALA ASP THR GLY LYS
SEQRES 7 A 365 LEU LEU SER ARG ASN GLN TRP GLN LYS SER LEU PHE GLU
SEQRES 8 A 365 GLU LEU ALA ASN ASN TRP GLY VAL ASN THR ILE ARG LEU
SEQRES 9 A 365 PRO ILE HIS PRO VAL SER TRP ARG LYS LEU GLY PRO ASP
SEQRES 10 A 365 VAL TYR LEU GLY HIS ILE ASP GLU ALA VAL ARG TRP ALA
SEQRES 11 A 365 ASN ASP LEU GLY ILE TYR LEU ILE LEU ASP TRP HIS SER
SEQRES 12 A 365 ILE GLY TYR LEU PRO THR GLU GLN TYR GLN HIS PRO MET
SEQRES 13 A 365 TYR ASP THR THR ILE LYS GLU THR ARG ASP PHE TRP ARG
SEQRES 14 A 365 ARG ILE THR PHE ARG TYR GLN ASN VAL PRO THR VAL ALA
SEQRES 15 A 365 VAL TYR GLU LEU PHE ASN GLU PRO THR THR MET GLY ASN
SEQRES 16 A 365 THR LEU GLY GLU ARG ASN TRP ALA GLU TRP LYS THR LEU
SEQRES 17 A 365 ASN GLU SER LEU ILE ASP MET ILE TYR ALA SER ASP LYS
SEQRES 18 A 365 THR VAL ILE PRO LEU VAL ALA GLY PHE ASN TRP ALA TYR
SEQRES 19 A 365 ASP LEU SER PRO ILE LYS LYS ALA PRO ILE GLU ARG GLU
SEQRES 20 A 365 GLY ILE ALA TYR ALA ALA HIS PRO TYR PRO GLN LYS ALA
SEQRES 21 A 365 LYS PRO GLU VAL LYS ASN ASP LYS ASN PHE PHE LYS LEU
SEQRES 22 A 365 TRP ASP GLU LYS TRP GLY PHE ALA ALA ASP THR TYR PRO
SEQRES 23 A 365 VAL ILE ALA THR GLN LEU GLY TRP VAL GLN PRO ASP GLY
SEQRES 24 A 365 TYR GLY ALA HIS ILE PRO VAL LYS ASP ASP GLY SER TYR
SEQRES 25 A 365 GLY PRO ARG ILE VAL LYS TYR MET GLN LYS LYS GLY VAL
SEQRES 26 A 365 SER TYR THR VAL TRP VAL PHE ASP PRO ASP TRP SER PRO
SEQRES 27 A 365 THR MET ILE ASN ASP TRP ASP PHE THR PRO SER GLU GLN
SEQRES 28 A 365 GLY ALA PHE PHE LYS GLN VAL MET LEU GLU ALA LYS LYS
SEQRES 29 A 365 ARG
HET BGC B 1 12
HET BGC B 2 11
HET BGC B 3 11
HET BGC B 4 11
HET CL A1369 1
HET MG A1370 1
HET SO4 A1371 5
HET SO4 A1372 5
HET GOL A1373 6
HET GOL A1374 6
HET GOL A1375 6
HET PGE A1376 4
HET PGE A1377 4
HET PGE A1378 4
HET PGE A1379 4
HET PGE A1380 4
HET PGE A1381 4
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 BGC 4(C6 H12 O6)
FORMUL 3 CL CL 1-
FORMUL 4 MG MG 2+
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 GOL 3(C3 H8 O3)
FORMUL 10 PGE 6(C6 H14 O4)
FORMUL 16 HOH *276(H2 O)
HELIX 1 1 ASP A 30 ILE A 34 5 5
HELIX 2 2 ASP A 41 LEU A 45 5 5
HELIX 3 3 ASP A 75 ARG A 82 1 8
HELIX 4 4 GLN A 86 TRP A 97 1 12
HELIX 5 5 HIS A 107 GLY A 115 1 9
HELIX 6 6 GLY A 115 GLY A 134 1 20
HELIX 7 7 HIS A 154 ASP A 158 5 5
HELIX 8 8 THR A 160 TYR A 175 1 16
HELIX 9 9 ASN A 201 ALA A 218 1 18
HELIX 10 10 GLY A 229 TYR A 234 1 6
HELIX 11 11 LEU A 236 LYS A 241 5 6
HELIX 12 12 ASN A 266 TRP A 278 1 13
HELIX 13 13 GLY A 279 THR A 284 5 6
HELIX 14 14 SER A 311 GLY A 324 1 14
HELIX 15 15 SER A 349 LYS A 364 1 16
SHEET 1 AA 3 ILE A 51 LYS A 54 0
SHEET 2 AA 3 LYS A 57 ASP A 60 -1 O LYS A 57 N LYS A 54
SHEET 3 AA 3 THR A 65 PHE A 66 -1 O PHE A 66 N PHE A 58
SHEET 1 AB 9 ARG A 69 ASN A 72 0
SHEET 2 AB 9 SER A 326 VAL A 329 1 O TYR A 327 N GLY A 70
SHEET 3 AB 9 VAL A 287 ALA A 289 1 O VAL A 287 N SER A 326
SHEET 4 AB 9 ALA A 250 ALA A 252 1 O TYR A 251 N ILE A 288
SHEET 5 AB 9 ILE A 224 VAL A 227 1 O PRO A 225 N ALA A 250
SHEET 6 AB 9 VAL A 181 GLU A 185 1 O ALA A 182 N ILE A 224
SHEET 7 AB 9 TYR A 136 TRP A 141 1 O LEU A 137 N ALA A 182
SHEET 8 AB 9 THR A 101 ILE A 106 1 O ILE A 102 N ILE A 138
SHEET 9 AB 9 ARG A 69 ASN A 72 1 O VAL A 71 N ARG A 103
SHEET 1 AC 3 GLN A 151 TYR A 152 0
SHEET 2 AC 3 ILE A 144 TYR A 146 -1 O TYR A 146 N GLN A 151
SHEET 3 AC 3 GLU A 189 PRO A 190 1 O GLU A 189 N GLY A 145
LINK O3 BGC B 1 C1 BGC B 2 1555 1555 1.41
LINK O4 BGC B 2 C1 BGC B 3 1555 1555 1.41
LINK O4 BGC B 3 C1 BGC B 4 1555 1555 1.43
LINK O VAL A 178 MG MG A1370 1555 1555 2.30
LINK O VAL A 181 MG MG A1370 1555 1555 2.26
LINK MG MG A1370 O HOH A2153 1555 1555 2.43
LINK MG MG A1370 O HOH A2154 1555 1555 2.41
LINK MG MG A1370 O HOH A2160 1555 1555 2.41
CISPEP 1 ILE A 304 PRO A 305 0 4.05
CISPEP 2 TRP A 330 VAL A 331 0 -2.18
CISPEP 3 SER A 337 PRO A 338 0 -6.60
CRYST1 144.382 144.382 144.382 90.00 90.00 90.00 P 41 3 2 24
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 0.006926 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006926 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006926 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
