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HEADER LUMINESCENT PROTEIN 26-JUL-01 1JO5 TITLE RHODOBACTER SPHAEROIDES LIGHT HARVESTING 1 BETA SUBUNIT IN DETERGENT TITLE 2 MICELLES COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIGHT-HARVESTING PROTEIN B-875; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: BETA SUBUNIT SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES; SOURCE 3 ORGANISM_TAXID: 1063; SOURCE 4 STRAIN: SK102 KEYWDS HELIX-TURN-HELIX, DETERGENT MICELLE, MEMBRANE PROTEIN, LUMINESCENT KEYWDS 2 PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR P.L.SORGEN,S.M.CAHILL,R.D.KRUEGER-KOPLIN,S.T.KRUEGER-KOPLIN, AUTHOR 2 C.G.SCHENCK,M.E.GIRVIN REVDAT 4 23-FEB-22 1JO5 1 REMARK REVDAT 3 24-FEB-09 1JO5 1 VERSN REVDAT 2 01-APR-03 1JO5 1 JRNL REVDAT 1 27-FEB-02 1JO5 0 JRNL AUTH P.L.SORGEN,S.M.CAHILL,R.D.KRUEGER-KOPLIN,S.T.KRUEGER-KOPLIN, JRNL AUTH 2 C.C.SCHENCK,M.E.GIRVIN JRNL TITL STRUCTURE OF THE RHODOBACTER SPHAEROIDES LIGHT-HARVESTING 1 JRNL TITL 2 BETA SUBUNIT IN DETERGENT MICELLES. JRNL REF BIOCHEMISTRY V. 41 31 2002 JRNL REFN ISSN 0006-2960 JRNL PMID 11772000 JRNL DOI 10.1021/BI011576J REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER ET AL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1JO5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-01. REMARK 100 THE DEPOSITION ID IS D_1000013995. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 50 MM PHOSPHATE BUFFER REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.7 MM LH1 BETA SUBUNIT, 15N13C, REMARK 210 8% ZWITTERGENT 3:12, 50MM REMARK 210 PHOSPHATE BUFFER, PH 6.5, 310K, REMARK 210 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.0.3, NMRPIPE 1.8, CNS REMARK 210 1.0 REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED IN 8% ZWITTERGENT 3:12 REMARK 210 DETERGENT 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 2 SER A 4 -61.07 71.79 REMARK 500 2 ASP A 5 46.61 -80.94 REMARK 500 3 LYS A 3 98.94 60.38 REMARK 500 3 ASP A 5 28.63 44.16 REMARK 500 4 ASP A 2 -71.08 -62.68 REMARK 500 4 SER A 4 -77.89 -158.09 REMARK 500 4 LEU A 27 21.03 45.60 REMARK 500 5 LYS A 3 54.26 -91.98 REMARK 500 7 SER A 4 -67.11 -158.17 REMARK 500 7 ASP A 5 37.32 -160.54 REMARK 500 7 LEU A 27 22.77 43.38 REMARK 500 7 TRP A 28 44.41 -95.93 REMARK 500 8 ASP A 2 76.07 59.92 REMARK 500 8 LYS A 3 80.75 60.49 REMARK 500 8 TRP A 28 32.59 -87.73 REMARK 500 9 SER A 4 54.08 -158.50 REMARK 500 9 LEU A 6 41.34 -75.79 REMARK 500 9 THR A 9 -14.51 71.27 REMARK 500 10 SER A 4 -60.79 71.64 REMARK 500 10 ASP A 5 47.05 -81.12 REMARK 500 REMARK 500 REMARK: NULL DBREF 1JO5 A 1 48 UNP P02951 LHB1_RHOSH 1 48 SEQRES 1 A 48 ALA ASP LYS SER ASP LEU GLY TYR THR GLY LEU THR ASP SEQRES 2 A 48 GLU GLN ALA GLN GLU LEU HIS SER VAL TYR MET SER GLY SEQRES 3 A 48 LEU TRP LEU PHE SER ALA VAL ALA ILE VAL ALA HIS LEU SEQRES 4 A 48 ALA VAL TYR ILE TRP ARG PRO TRP PHE HELIX 1 1 SER A 4 GLY A 10 5 7 HELIX 2 2 LEU A 11 GLY A 26 1 16 HELIX 3 3 TRP A 28 ARG A 45 1 18 CRYST1 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 - 23 20 Bytes