Header list of 1heh.pdb file
Complete list - 9 20 Bytes
HEADER HYDROLASE(XYLAN DEGRADATION) 22-NOV-00 1HEH
TITLE C-TERMINAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE 11A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE D;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: XYLAN BINDING DOMAIN 2;
COMPND 5 SYNONYM: XYLANASE D, CBM2B-2, XBD2;
COMPND 6 EC: 3.2.1.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CELLULOMONAS FIMI;
SOURCE 3 ORGANISM_TAXID: 1708;
SOURCE 4 STRAIN: JM83;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS HYDROLASE(XYLAN DEGRADATION), HYDROLASE, XYLAN BINDING DOMAIN,
KEYWDS 2 XYLANASE, BETA-SHEET
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR P.J.SIMPSON,X.HEFANG,D.N.BOLAM,P.WHITE,S.M.HANCOCK,H.J.GILBERT,
AUTHOR 2 M.P.WILLIAMSON
REVDAT 4 14-JUN-23 1HEH 1 REMARK
REVDAT 3 15-JAN-20 1HEH 1 REMARK
REVDAT 2 24-FEB-09 1HEH 1 VERSN
REVDAT 1 10-MAY-01 1HEH 0
JRNL AUTH D.N.BOLAM,H.XIE,P.WHITE,P.J.SIMPSON,S.M.HANCOCK,
JRNL AUTH 2 M.P.WILLIAMSON,H.J.GILBERT
JRNL TITL EVIDENCE FOR SYNERGY BETWEEN FAMILY 2B CARBOHYDRATE BINDING
JRNL TITL 2 MODULES IN CELLULOMONAS FIMI XYLANASE 11A
JRNL REF BIOCHEMISTRY V. 40 2468 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11327868
JRNL DOI 10.1021/BI002564L
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 PROTOCOL. DETAILS IN THE JRNL
REMARK 3 CITATION.
REMARK 4
REMARK 4 1HEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1290005577.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : SODIUM PHOSPHATE 50 MM, SODIUM
REMARK 210 AZIDE 10 MM
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
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : 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 : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: MINIMISED AVERAGE FROM BEST 23 OUT OF 50. THE STRUCTURE
REMARK 210 WAS DETERMINED USING HETERONUCLEAR NMR SPECTROSCOPY ON A
REMARK 210 UNIFORMLY 15N-LABELLED SAMPLE OF XBD2
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: C
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 ENDOHYDROLYSIS OF 1,4-BETA-D-XYLOSIDIC LINKAGES IN XYLANS.
REMARK 400 BELONGS TO CELLULASE FAMILY G (FAMILY 11 OF GLYCOSYL
REMARK 400 HYDROLASES).
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 C 568 161.58 -40.22
REMARK 500 SER C 581 -70.67 -101.64
REMARK 500 SER C 583 46.92 -85.43
REMARK 500 VAL C 587 32.52 -160.03
REMARK 500 LEU C 592 -167.93 -65.02
REMARK 500 ALA C 604 168.23 162.94
REMARK 500 SER C 609 22.83 -156.93
REMARK 500 SER C 610 108.47 169.89
REMARK 500 ASN C 618 20.98 -152.25
REMARK 500 SER C 620 113.67 164.17
REMARK 500 ASN C 631 29.60 43.06
REMARK 500 SER C 633 -148.57 -88.42
REMARK 500 SER C 634 -112.93 -171.50
REMARK 500 CYS C 641 69.62 -160.38
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 C 566 0.22 SIDE CHAIN
REMARK 500 ARG C 573 0.14 SIDE CHAIN
REMARK 500 ARG C 616 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HEJ RELATED DB: PDB
REMARK 900 C-TERMINAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE 11A
REMARK 900 (5 STRUCTURES)
REMARK 900 RELATED ID: 1E5B RELATED DB: PDB
REMARK 900 INTERNAL XYLAN BINDING DOMAIN FROM C. FIMI XYN10A, R262G MUTANT
REMARK 900 RELATED ID: 1E5C RELATED DB: PDB
REMARK 900 INTERNAL XYLAN BINDING DOMAIN FROM C. FIMI XYN10A, R262G MUTANT
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: 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: 4900 RELATED DB: BMRB
DBREF 1HEH C 557 644 UNP P54865 XYND_CELFI 557 644
SEQRES 1 C 88 THR GLY SER CYS SER VAL SER ALA VAL ARG GLY GLU GLU
SEQRES 2 C 88 TRP ALA ASP ARG PHE ASN VAL THR TYR SER VAL SER GLY
SEQRES 3 C 88 SER SER SER TRP VAL VAL THR LEU GLY LEU ASN GLY GLY
SEQRES 4 C 88 GLN SER VAL GLN SER SER TRP ASN ALA ALA LEU THR GLY
SEQRES 5 C 88 SER SER GLY THR VAL THR ALA ARG PRO ASN GLY SER GLY
SEQRES 6 C 88 ASN SER PHE GLY VAL THR PHE TYR LYS ASN GLY SER SER
SEQRES 7 C 88 ALA THR PRO GLY ALA THR CYS ALA THR GLY
SHEET 1 A 4 VAL C 562 GLU C 568 0
SHEET 2 A 4 ARG C 573 SER C 581 -1 N SER C 579 O SER C 563
SHEET 3 A 4 SER C 623 TYR C 629 -1 O PHE C 624 N TYR C 578
SHEET 4 A 4 VAL C 598 TRP C 602 -1 O TRP C 602 N GLY C 625
SHEET 1 B 4 GLY C 638 ALA C 642 0
SHEET 2 B 4 VAL C 587 LEU C 592 -1 N THR C 589 O THR C 640
SHEET 3 B 4 VAL C 613 ARG C 616 -1 O VAL C 613 N LEU C 590
SHEET 4 B 4 ALA C 605 GLY C 608 -1 O ALA C 605 N ARG C 616
SSBOND 1 CYS C 560 CYS C 641 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 - 9 20 Bytes