Header list of 1e5b.pdb file
Complete list - 31 20 Bytes
HEADER HYDROLASE 24-JUL-00 1E5B
TITLE INTERNAL XYLAN BINDING DOMAIN FROM C. FIMI XYN10A, R262G MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XYLANASE D;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: XYLAN BINDING DOMAIN 1;
COMPND 5 SYNONYM: XBD1,ENDO-1,4-BETA-XYLANASE D;
COMPND 6 EC: 3.2.1.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CELLULOMONAS FIMI;
SOURCE 3 ORGANISM_TAXID: 1708;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM83
KEYWDS HYDROLASE, XYLAN BINDING DOMAIN, XYLANASE, BETA-SHEET
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR P.J.SIMPSON,X.HEFANG,D.N.BOLAM,H.J.GILBERT,M.P.WILLIAMSON
REVDAT 3 24-OCT-18 1E5B 1 SOURCE
REVDAT 2 24-FEB-09 1E5B 1 VERSN
REVDAT 1 25-MAY-01 1E5B 0
JRNL AUTH P.J.SIMPSON,X.HEFANG,D.N.BOLAM,H.J.GILBERT,M.P.WILLIAMSON
JRNL TITL THE STRUCTURAL BASIS FOR THE LIGAND SPECIFICITY OF FAMILY 2
JRNL TITL 2 CARBOHYDRATE BINDING NODULES
JRNL REF J.BIOL.CHEM. V. 275 41137 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10973978
JRNL DOI 10.1074/JBC.M006948200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: YASAP
REMARK 4
REMARK 4 1E5B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1290005190.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 50MM SODIUM PHOSPHATE, 10MM
REMARK 210 AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY; DQF-COSY; NOESY; E.COSY;
REMARK 210 HSQC; NOESY-HMQC; TOCSY-HMQC;
REMARK 210 HNHA; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : MSI FELIX 97.0
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY/
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMISED AVERAGE STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HETERONUCLEAR NMR
REMARK 210 SPECTROSCOPY ON A UNIFORMLY 15N-LABELLED SAMPLE OF XBD1 (R262G)
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 CHAIN A MUTATION: R262G
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 THR A 254 105.30 -167.91
REMARK 500 ALA A 256 -86.01 -101.37
REMARK 500 GLU A 258 146.90 -170.43
REMARK 500 SER A 260 41.95 -82.98
REMARK 500 ASP A 261 -37.79 -156.84
REMARK 500 GLN A 285 171.33 -49.43
REMARK 500 ALA A 293 147.06 -176.32
REMARK 500 SER A 298 68.87 -170.46
REMARK 500 SER A 309 23.06 -155.83
REMARK 500 MET A 318 88.36 -61.56
REMARK 500 ASN A 320 45.77 38.57
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 255 0.15 SIDE CHAIN
REMARK 500 ARG A 302 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XBD RELATED DB: PDB
REMARK 900 INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D,
REMARK 900 NMR, MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1XBD RELATED DB: PDB
REMARK 900 INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D,
REMARK 900 NMR, 5 STRUCTURES
REMARK 900 RELATED ID: 1E5C RELATED DB: PDB
REMARK 900 INTERNAL XYLAN BINDING DOMAIN FROM C. FIMI XYN10A, R262G MUTANT
DBREF 1E5B A 247 333 UNP P54865 XYND_CELFI 247 333
SEQADV 1E5B GLY A 262 UNP P54865 ARG 262 ENGINEERED MUTATION
SEQRES 1 A 87 THR GLY CYS SER VAL THR ALA THR ARG ALA GLU GLU TRP
SEQRES 2 A 87 SER ASP GLY PHE ASN VAL THR TYR SER VAL SER GLY SER
SEQRES 3 A 87 SER ALA TRP THR VAL ASN LEU ALA LEU ASN GLY SER GLN
SEQRES 4 A 87 THR ILE GLN ALA SER TRP ASN ALA ASN VAL THR GLY SER
SEQRES 5 A 87 GLY SER THR ARG THR VAL THR PRO ASN GLY SER GLY ASN
SEQRES 6 A 87 THR PHE GLY VAL THR VAL MET LYS ASN GLY SER SER THR
SEQRES 7 A 87 THR PRO ALA ALA THR CYS ALA GLY SER
SHEET 1 A 4 CYS A 249 TRP A 259 0
SHEET 2 A 4 GLY A 262 VAL A 269 -1 N THR A 266 O THR A 254
SHEET 3 A 4 ASN A 311 MET A 318 -1 O PHE A 313 N TYR A 267
SHEET 4 A 4 THR A 286 TRP A 291 -1 N GLN A 288 O THR A 316
SHEET 1 B 4 ASN A 294 GLY A 297 0
SHEET 2 B 4 THR A 301 PRO A 306 -1 O THR A 303 N THR A 296
SHEET 3 B 4 TRP A 275 LEU A 281 -1 O LEU A 279 N ARG A 302
SHEET 4 B 4 PRO A 326 CYS A 330 -1 O ALA A 327 N ALA A 280
SSBOND 1 CYS A 249 CYS A 330 1555 1555 2.02
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 31 20 Bytes