HEADER HYDROLASE 31-MAR-04 1V0L
TITLE XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN COMPLEX WITH XYLOBIO-
TITLE 2 ISOFAGOMINE AT PH 5.8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC MODULE, RESIDUES 42-354;
COMPND 5 SYNONYM: XYLANASE A, 1,4-BETA-D-XYLAN XYLANOHYDROLASE A;
COMPND 6 EC: 3.2.1.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS;
SOURCE 3 ORGANISM_TAXID: 1916;
SOURCE 4 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1916;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: IAF 19
KEYWDS GLYCOSIDE HYDROLASE FAMILY 10, XYLANASE, XYLAN DEGRADATION,
KEYWDS 2 ISOFAGOMINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.M.GLOSTER,S.J.WILLIAMS,S.ROBERTS,C.A.TARLING,J.WICKI,S.G.WITHERS,
AUTHOR 2 G.J.DAVIES
REVDAT 4 13-DEC-23 1V0L 1 HETSYN LINK
REVDAT 3 29-JUL-20 1V0L 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 24-FEB-09 1V0L 1 VERSN
REVDAT 1 16-AUG-04 1V0L 0
JRNL AUTH T.M.GLOSTER,S.J.WILLIAMS,S.ROBERTS,C.A.TARLING,J.WICKI,
JRNL AUTH 2 S.G.WITHERS,G.J.DAVIES
JRNL TITL ATOMIC RESOLUTION ANALYSES OF THE BINDING OF
JRNL TITL 2 XYLOBIOSE-DERIVED DEOXYNOJIRIMYCIN AND ISOFAGOMINE TO
JRNL TITL 3 XYLANASE XYN10A
JRNL REF CHEM.COMMUN.(CAMB.) V. 16 1794 2004
JRNL REFN ISSN 1359-7345
JRNL PMID 15306887
JRNL DOI 10.1039/B405152A
REMARK 2
REMARK 2 RESOLUTION. 0.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0000
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) : 0.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 133506
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) : 0.119
REMARK 3 R VALUE (WORKING SET) : 0.118
REMARK 3 FREE R VALUE : 0.137
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6992
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) : 0.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.01
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9127
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1560
REMARK 3 BIN FREE R VALUE SET COUNT : 510
REMARK 3 BIN FREE R VALUE : 0.1690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2331
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 641
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 7.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09000
REMARK 3 B22 (A**2) : -0.21000
REMARK 3 B33 (A**2) : 0.30000
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): 0.021
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.022
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.011
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.973
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2580 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2245 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3524 ; 1.727 ; 1.906
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5246 ; 0.881 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 317 ; 6.416 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 423 ;11.919 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 397 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2903 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 545 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 535 ; 0.327 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2299 ; 0.242 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1276 ; 0.133 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 338 ; 0.163 ; 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 ; 0.124 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 56 ; 0.350 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 80 ; 0.150 ; 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): 2018 ; 1.740 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2571 ; 2.106 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1185 ; 2.622 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 951 ; 3.365 ; 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 : 1.20
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. RESIDUE 1 AND THE LAST 11 RESIDUES ARE TOO DISORDERED
REMARK 3 TO BE BUILT IN DENSITY
REMARK 4
REMARK 4 1V0L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1290014015.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91680
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : TORROIDAL MIRROR
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 : 140638
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.980
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.40600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.230
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1OD8
REMARK 200
REMARK 200 REMARK: STRUCTURE ISOMORPHOUS WITH STARTING MODEL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MG/ML PROTEIN, 0.1 M MES 18% PEG
REMARK 280 5KMME, 7.5% ISOPROPANOL, PH 5.80
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 33.00900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.12700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.04900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.12700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.00900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.04900
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 CONTRIBUTES TO THE HYDROLYSIS OF HEMICELLULOSE, WHICH IS
REMARK 400 THE MAJOR COMPONENT OF PLANT CELL-WALLS.
REMARK 400 XLNA AND XLNB SEEM TO ACT SEQUENTIALLY ON THE SUBSTRATE
REMARK 400 TO YIELD XYLOBIOSE AND XYLOSE AS CARBON SOURCES.
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 ALA A 1
REMARK 465 ASP A 304
REMARK 465 SER A 305
REMARK 465 SER A 306
REMARK 465 GLU A 307
REMARK 465 PRO A 308
REMARK 465 PRO A 309
REMARK 465 ALA A 310
REMARK 465 ASP A 311
REMARK 465 GLY A 312
REMARK 465 GLY A 313
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 152 CD GLU A 152 OE2 0.295
REMARK 500 GLU A 152 CD GLU A 152 OE2 2.012
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 GLU A 152 OE1 - CD - OE2 ANGL. DEV. = 100.1 DEGREES
REMARK 500 GLU A 152 OE1 - CD - OE2 ANGL. DEV. = 20.5 DEGREES
REMARK 500 GLU A 152 CG - CD - OE2 ANGL. DEV. = -31.1 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 GLU A 236 41.38 -147.16
REMARK 500 VAL A 268 -77.62 -99.44
REMARK 500 THR A 279 61.94 34.06
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 GLU A 152 0.19 SIDE CHAIN
REMARK 500 TYR A 169 0.07 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 A2047 DISTANCE = 7.36 ANGSTROMS
REMARK 525 HOH A2051 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH A2099 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A2148 DISTANCE = 5.86 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E0V RELATED DB: PDB
REMARK 900 XYLANASE 10A FROM SREPTOMYCES LIVIDANS. CELLOBIOSYL-ENZYME
REMARK 900 INTERMEDIATE AT 1.7 A
REMARK 900 RELATED ID: 1E0W RELATED DB: PDB
REMARK 900 XYLANASE 10A FROM SREPTOMYCES LIVIDANS. NATIVE STRUCTURE AT 1.2
REMARK 900 ANGSTROM RESOLUTION
REMARK 900 RELATED ID: 1E0X RELATED DB: PDB
REMARK 900 XYLANASE 10A FROM SREPTOMYCES LIVIDANS. XYLOBIOSYL-ENZYME
REMARK 900 INTERMEDIATE AT 1.65 A
REMARK 900 RELATED ID: 1KNL RELATED DB: PDB
REMARK 900 STREPTOMYCES LIVIDANS XYLAN BINDING DOMAIN CBM13
REMARK 900 RELATED ID: 1KNM RELATED DB: PDB
REMARK 900 STREPTOMYCES LIVIDANS XYLAN BINDING DOMAIN CBM13 IN COMPLEXWITH
REMARK 900 LACTOSE
REMARK 900 RELATED ID: 1MC9 RELATED DB: PDB
REMARK 900 STREPROMYCES LIVIDANS XYLAN BINDING DOMAIN CBM13 IN COMPLEXWITH
REMARK 900 XYLOPENTAOSE
REMARK 900 RELATED ID: 1OD8 RELATED DB: PDB
REMARK 900 XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN COMPLEX WITH XYLOBIO-
REMARK 900 ISOFAGOMINE LACTAM
REMARK 900 RELATED ID: 1V0K RELATED DB: PDB
REMARK 900 XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN COMPLEX WITH XYLOBIO-
REMARK 900 DEOXYNOJIRIMYCIN AT PH 5.8
REMARK 900 RELATED ID: 1V0M RELATED DB: PDB
REMARK 900 XYLANASE XYN10 FROM STREPTOMYCES LIVIDANS IN COMPLEX WITH XYLOBIO-
REMARK 900 DEOXYNOJIRIMYCIN AT PH 7.5
REMARK 900 RELATED ID: 1V0N RELATED DB: PDB
REMARK 900 XYLANASE XYN10 FROM STREPTOMYCES LIVIDANS IN COMPLEX WITH XYLOBIO-
REMARK 900 ISOFAGOMINE AT PH 7.5
REMARK 900 RELATED ID: 1XAS RELATED DB: PDB
REMARK 900 1,4-BETA-D-XYLAN XYLANOHYDROLASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 41 RESIDUES IN THE DATABASE CORRESPOND
REMARK 999 TO THE SIGNAL PEPTIDE. THE NUMBERING USED IN THE
REMARK 999 PDB FILE IS AFTER CLEAVAGE OF THE SIGNAL PEPTIDE.
REMARK 999 RESIDUE 1 AND THE LAST 11 RESIDUES ARE TOO DISORDERED
REMARK 999 TO BE BUILT IN DENSITY
DBREF 1V0L A 1 313 UNP P26514 XYNA_STRLI 42 354
SEQRES 1 A 313 ALA GLU SER THR LEU GLY ALA ALA ALA ALA GLN SER GLY
SEQRES 2 A 313 ARG TYR PHE GLY THR ALA ILE ALA SER GLY ARG LEU SER
SEQRES 3 A 313 ASP SER THR TYR THR SER ILE ALA GLY ARG GLU PHE ASN
SEQRES 4 A 313 MET VAL THR ALA GLU ASN GLU MET LYS ILE ASP ALA THR
SEQRES 5 A 313 GLU PRO GLN ARG GLY GLN PHE ASN PHE SER SER ALA ASP
SEQRES 6 A 313 ARG VAL TYR ASN TRP ALA VAL GLN ASN GLY LYS GLN VAL
SEQRES 7 A 313 ARG GLY HIS THR LEU ALA TRP HIS SER GLN GLN PRO GLY
SEQRES 8 A 313 TRP MET GLN SER LEU SER GLY SER ALA LEU ARG GLN ALA
SEQRES 9 A 313 MET ILE ASP HIS ILE ASN GLY VAL MET ALA HIS TYR LYS
SEQRES 10 A 313 GLY LYS ILE VAL GLN TRP ASP VAL VAL ASN GLU ALA PHE
SEQRES 11 A 313 ALA ASP GLY SER SER GLY ALA ARG ARG ASP SER ASN LEU
SEQRES 12 A 313 GLN ARG SER GLY ASN ASP TRP ILE GLU VAL ALA PHE ARG
SEQRES 13 A 313 THR ALA ARG ALA ALA ASP PRO SER ALA LYS LEU CYS TYR
SEQRES 14 A 313 ASN ASP TYR ASN VAL GLU ASN TRP THR TRP ALA LYS THR
SEQRES 15 A 313 GLN ALA MET TYR ASN MET VAL ARG ASP PHE LYS GLN ARG
SEQRES 16 A 313 GLY VAL PRO ILE ASP CYS VAL GLY PHE GLN SER HIS PHE
SEQRES 17 A 313 ASN SER GLY SER PRO TYR ASN SER ASN PHE ARG THR THR
SEQRES 18 A 313 LEU GLN ASN PHE ALA ALA LEU GLY VAL ASP VAL ALA ILE
SEQRES 19 A 313 THR GLU LEU ASP ILE GLN GLY ALA PRO ALA SER THR TYR
SEQRES 20 A 313 ALA ASN VAL THR ASN ASP CYS LEU ALA VAL SER ARG CYS
SEQRES 21 A 313 LEU GLY ILE THR VAL TRP GLY VAL ARG ASP SER ASP SER
SEQRES 22 A 313 TRP ARG SER GLU GLN THR PRO LEU LEU PHE ASN ASN ASP
SEQRES 23 A 313 GLY SER LYS LYS ALA ALA TYR THR ALA VAL LEU ASP ALA
SEQRES 24 A 313 LEU ASN GLY GLY ASP SER SER GLU PRO PRO ALA ASP GLY
SEQRES 25 A 313 GLY
HET XIF A1304 8
HET XYP A1305 9
HETNAM XIF PIPERIDINE-3,4-DIOL
HETNAM XYP BETA-D-XYLOPYRANOSE
HETSYN XIF XYLOSE-DERIVED ISOFAGOMINE
HETSYN XYP BETA-D-XYLOSE; D-XYLOSE; XYLOSE
FORMUL 2 XIF C5 H11 N O2
FORMUL 3 XYP C5 H10 O5
FORMUL 4 HOH *641(H2 O)
HELIX 1 1 THR A 4 GLN A 11 1 8
HELIX 2 2 ALA A 21 LEU A 25 5 5
HELIX 3 3 ASP A 27 PHE A 38 1 12
HELIX 4 4 LYS A 48 GLU A 53 1 6
HELIX 5 5 PHE A 61 ASN A 74 1 14
HELIX 6 6 PRO A 90 SER A 95 1 6
HELIX 7 7 SER A 97 TYR A 116 1 20
HELIX 8 8 SER A 141 SER A 146 1 6
HELIX 9 9 ASP A 149 ASP A 162 1 14
HELIX 10 10 TRP A 179 GLY A 196 1 18
HELIX 11 11 ASN A 217 ALA A 227 1 11
HELIX 12 12 PRO A 243 ALA A 256 1 14
HELIX 13 13 ASP A 270 SER A 273 5 4
HELIX 14 14 ARG A 275 THR A 279 5 5
HELIX 15 15 LYS A 290 ASN A 301 1 12
SHEET 1 AA11 TYR A 15 ILE A 20 0
SHEET 2 AA11 CYS A 260 VAL A 265 1 O LEU A 261 N TYR A 15
SHEET 3 AA11 ASP A 231 ILE A 239 1 O VAL A 232 N LEU A 261
SHEET 4 AA11 CYS A 201 PHE A 204 1 O VAL A 202 N ALA A 233
SHEET 5 AA11 LYS A 166 ASP A 171 1 O TYR A 169 N GLY A 203
SHEET 6 AA11 GLN A 122 ASN A 127 1 O TRP A 123 N CYS A 168
SHEET 7 AA11 GLN A 77 ALA A 84 1 O GLY A 80 N ASP A 124
SHEET 8 AA11 MET A 40 ALA A 43 1 O VAL A 41 N ARG A 79
SHEET 9 AA11 TYR A 15 ILE A 20 1 O THR A 18 N THR A 42
SHEET 10 AA11 CYS A 260 VAL A 265 1 O LEU A 261 N TYR A 15
SHEET 11 AA11 TYR A 15 ILE A 20 1 O TYR A 15 N ILE A 263
SSBOND 1 CYS A 168 CYS A 201 1555 1555 2.10
SSBOND 2 CYS A 254 CYS A 260 1555 1555 2.18
LINK O4 XIF A1304 C1 XYP A1305 1555 1555 1.40
CISPEP 1 HIS A 81 THR A 82 0 0.26
CRYST1 66.018 46.098 86.254 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 0.015147 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021693 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011594 0.00000
(ATOM LINES ARE NOT SHOWN.)
END