Header list of 1e8r.pdb file
Complete list - 25 20 Bytes
HEADER HYDROLASE 28-SEP-00 1E8R
TITLE SOLUTION STRUCTURE OF TYPE X CBD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TYPE X CELLULOSE BINDING DOMAIN (CBDX);
COMPND 5 EC: 3.2.1.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS FLUORESCENS;
SOURCE 3 ORGANISM_TAXID: 294;
SOURCE 4 PLASMID: BL21;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS HYDROLASE, BETA STRANDS, ANTIPARALLEL SHEETS
EXPDTA SOLUTION NMR
NUMMDL 5
AUTHOR S.RAGHOTHAMA,P.J.SIMPSON,H.J.GILBERT,M.P.WILLIAMSON
REVDAT 3 24-FEB-09 1E8R 1 VERSN
REVDAT 2 23-OCT-00 1E8R 1 ENDMDL
REVDAT 1 03-OCT-00 1E8R 0
SPRSDE 03-OCT-00 1E8R 1CT7
JRNL AUTH S.RAGHOTHAMA,P.J.SIMPSON,L.SZABO,T.NAGY,
JRNL AUTH 2 H.J.GILBERT,M.P.WILLIAMSON
JRNL TITL SOLUTION STRUCTURE OF THE CBM10 CELLULOSE BINDING
JRNL TITL 2 MODULE FROM PSEUDOMONAS XYLANASE A
JRNL REF BIOCHEMISTRY V. 39 978 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10653641
JRNL DOI 10.1021/BI992163+
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 1E8R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-00.
REMARK 100 THE PDBE ID CODE IS EBI-5402.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 323.00
REMARK 210 PH : 4.50
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM CBDX; 50MM SODIUM
REMARK 210 PHOSPHATE BUFFER; 100MM
REMARK 210 SODIUM CHLORIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, DQF-COSY,
REMARK 210 E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500; 600
REMARK 210 SPECTROMETER MODEL : DRX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 97.0, X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA : 5 STRUCTURES CHOSEN AT
REMARK 210 RANDOM FROM THE 21
REMARK 210 LOWEST ENERGY STRUCTURES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR 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 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 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 1 ASN A 26 92.13 -62.15
REMARK 500 1 GLN A 47 16.25 59.36
REMARK 500 1 ALA A 52 168.04 -41.09
REMARK 500 1 ARG A 53 -79.06 -56.30
REMARK 500 1 CYS A 56 -76.67 -72.67
REMARK 500 2 ALA A 52 167.85 -41.97
REMARK 500 2 ARG A 53 -78.25 -58.19
REMARK 500 2 CYS A 56 -74.06 -85.25
REMARK 500 2 ALA A 58 31.66 -90.36
REMARK 500 3 GLN A 47 19.30 59.87
REMARK 500 3 ALA A 52 165.41 -40.32
REMARK 500 3 ARG A 53 -77.45 -57.22
REMARK 500 3 CYS A 56 -76.13 -84.14
REMARK 500 4 ASN A 26 93.58 -59.95
REMARK 500 4 GLN A 47 16.87 58.88
REMARK 500 4 ALA A 52 168.18 -41.75
REMARK 500 4 ARG A 53 -79.06 -56.46
REMARK 500 4 CYS A 56 -76.75 -72.24
REMARK 500 5 TRP A 27 95.01 -68.97
REMARK 500 5 GLN A 47 16.50 59.29
REMARK 500 5 ALA A 52 166.07 -40.46
REMARK 500 5 ARG A 53 -77.75 -56.27
REMARK 500 5 CYS A 56 -75.49 -76.51
REMARK 500 5 GLN A 59 161.58 -44.85
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 1 ARG A 48 0.20 SIDE CHAIN
REMARK 500 1 ARG A 53 0.32 SIDE CHAIN
REMARK 500 2 ARG A 48 0.21 SIDE CHAIN
REMARK 500 2 ARG A 53 0.31 SIDE CHAIN
REMARK 500 3 ARG A 48 0.28 SIDE CHAIN
REMARK 500 3 ARG A 53 0.32 SIDE CHAIN
REMARK 500 4 ARG A 48 0.22 SIDE CHAIN
REMARK 500 4 ARG A 53 0.24 SIDE CHAIN
REMARK 500 5 ARG A 48 0.20 SIDE CHAIN
REMARK 500 5 ARG A 53 0.23 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CLX RELATED DB: PDB
REMARK 900 CATALYTIC CORE OF XYLANASE A
REMARK 900 RELATED ID: 1CT7 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF TYPE X CBD
REMARK 900 RELATED ID: 1QLD RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF TYPE X CBM
DBREF 1E8R A 20 69 UNP P14768 XYNA_PSEFL 179 228
SEQADV 1E8R MET A 20 PIR S06047 SER 179 CLONING ARTIFACT
SEQRES 1 A 50 MET GLY ASN GLN GLN CYS ASN TRP TYR GLY THR LEU TYR
SEQRES 2 A 50 PRO LEU CYS VAL THR THR THR ASN GLY TRP GLY TRP GLU
SEQRES 3 A 50 ASP GLN ARG SER CYS ILE ALA ARG SER THR CYS ALA ALA
SEQRES 4 A 50 GLN PRO ALA PRO PHE GLY ILE VAL GLY SER GLY
HELIX 1 1 ARG A 53 ALA A 57 1 5
SHEET 1 A 4 GLN A 24 ASN A 26 0
SHEET 2 A 4 LEU A 31 CYS A 35 -1 O TYR A 32 N CYS A 25
SHEET 3 A 4 ARG A 48 ALA A 52 1 N ILE A 51 O PRO A 33
SHEET 4 A 4 TRP A 42 GLU A 45 -1 N GLY A 43 O CYS A 50
SSBOND 1 CYS A 25 CYS A 56 1555 1555 2.01
SSBOND 2 CYS A 35 CYS A 50 1555 1555 2.02
CISPEP 1 ALA A 61 PRO A 62 1 0.26
CISPEP 2 ALA A 61 PRO A 62 2 0.11
CISPEP 3 ALA A 61 PRO A 62 3 -0.04
CISPEP 4 ALA A 61 PRO A 62 4 0.28
CISPEP 5 ALA A 61 PRO A 62 5 -0.16
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
MODEL 1
Complete list - 25 20 Bytes