Header list of 1e8p.pdb file
Complete list - 20 201 Bytes
HEADER CELLULOSE DOCKING DOMAIN 28-SEP-00 1E8P
TITLE CHARACTERISATION OF THE CELLULOSE DOCKING DOMAIN FROM PIROMYCES EQUI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOGLUCANASE 45A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CELLULOSE DOCKING DOMAIN;
COMPND 5 SYNONYM: DOCKERIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PIROMYCES EQUI;
SOURCE 3 ORGANISM_TAXID: 99929;
SOURCE 4 GENE: CEL45A;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS CELLULOSE DOCKING DOMAIN, CELLULASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR S.RAGHOTHAMA,R.Y.EBERHARDT,P.WHITE,G.P.HAZLEWOOD,H.J.GILBERT,
AUTHOR 2 P.J.SIMPSON,M.P.WILLIAMSON
REVDAT 3 20-JUN-18 1E8P 1 COMPND SOURCE JRNL DBREF
REVDAT 3 2 1 SEQADV
REVDAT 2 24-FEB-09 1E8P 1 VERSN
REVDAT 1 07-SEP-01 1E8P 0
JRNL AUTH S.RAGHOTHAMA,R.Y.EBERHARDT,P.SIMPSON,D.WIGELSWORTH,P.WHITE,
JRNL AUTH 2 G.P.HAZLEWOOD,T.NAGY,H.J.GILBERT,M.P.WILLIAMSON
JRNL TITL CHARACTERIZATION OF A CELLULOSOME DOCKERIN DOMAIN FROM THE
JRNL TITL 2 ANAEROBIC FUNGUS PIROMYCES EQUI.
JRNL REF NAT. STRUCT. BIOL. V. 8 775 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11524680
JRNL DOI 10.1038/NSB0901-775
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
REMARK 4
REMARK 4 1E8P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1290005401.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 50 MM SODIUM PHOSPHATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D - HSQC/NOESY; HNHA; HNHB; 2D
REMARK 210 - HSQC; 15N DECOUPLED TOCSY; DQF-
REMARK 210 COSY; E.COSY
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
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 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: MINIMISED AVERAGE STRUCTURE. THE STRUCTURE WAS DETERMINED
REMARK 210 USING STANDARD 2D & 3D NMR TECHNIQUES.
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 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 SER A 2 25.10 -154.93
REMARK 500 CYS A 3 103.67 -43.68
REMARK 500 ASN A 11 -150.52 -75.06
REMARK 500 ASN A 15 93.15 57.70
REMARK 500 SER A 18 16.99 -151.20
REMARK 500 THR A 24 110.40 -170.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E8Q RELATED DB: PDB
REMARK 900 CHARACTERISATION OF THE CELLULOSE DOCKING DOMAIN FROM PIROMYCES EQUI
REMARK 900 RELATED ID: 3322 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SER 2, NMR SAMPLE HAS SER AT THIS POSITION
DBREF 1E8P A 1 46 UNP Q9P868 Q9P868_PIREQ 20 65
SEQADV 1E8P SER A 2 UNP Q9P868 ALA 21 CONFLICT
SEQRES 1 A 46 ALA SER CYS TRP ALA GLN SER GLN GLY TYR ASN CYS CYS
SEQRES 2 A 46 ASN ASN PRO SER SER THR LYS VAL GLU TYR THR ASP ALA
SEQRES 3 A 46 SER GLY GLN TRP GLY VAL GLN ASN GLY GLN TRP CYS GLY
SEQRES 4 A 46 ILE ASP TYR SER TYR GLY GLN
HELIX 1 1 CYS A 3 GLN A 8 5 6
HELIX 2 2 ASN A 15 THR A 19 5 5
SHEET 1 A 3 GLN A 36 ILE A 40 0
SHEET 2 A 3 GLY A 28 GLN A 33 -1 N GLN A 33 O GLN A 36
SHEET 3 A 3 VAL A 21 ASP A 25 -1 N ASP A 25 O GLY A 28
SSBOND 1 CYS A 3 CYS A 12 1555 1555 2.02
SSBOND 2 CYS A 13 CYS A 38 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 - 20 201 Bytes