Header list of 1dx7.pdb file
Complete list - 25 20 Bytes
HEADER LIGHT-HARVESTING PROTEIN 21-DEC-99 1DX7
TITLE LIGHT-HARVESTING COMPLEX 1 BETA SUBUNIT FROM RHODOBACTER SPHAEROIDES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIGHT HARVESTING 1 B(B850B) POLYPEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LIGHT-HARVESTING PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES;
SOURCE 3 ORGANISM_TAXID: 1063;
SOURCE 4 CELLULAR_LOCATION: MEMBRANE;
SOURCE 5 GENE: PUFB, EBL86_10065;
SOURCE 6 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1063;
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: MEMBRANE
KEYWDS LIGHT-HARVESTING PROTEIN, BACTERIOCHLOROPHYLL BINDING, MEMBRANE
KEYWDS 2 PROTEIN, LIGHT HARVESTING, PHOTOSYNTHESIS
EXPDTA SOLUTION NMR
NUMMDL 6
AUTHOR M.J.CONROY,W.WESTERHUIS,P.S.PARKES-LOACH,P.A.LOACH,C.N.HUNTER,
AUTHOR 2 M.P.WILLIAMSON
REVDAT 4 25-SEP-19 1DX7 1 COMPND SOURCE REMARK DBREF
REVDAT 3 24-FEB-09 1DX7 1 VERSN
REVDAT 2 04-APR-05 1DX7 1 ATOM
REVDAT 1 18-APR-00 1DX7 0
JRNL AUTH M.J.CONROY,W.WESTERHUIS,P.S.PARKES-LOACH,P.A.LOACH,
JRNL AUTH 2 C.N.HUNTER,M.P.WILLIAMSON
JRNL TITL THE SOLUTION STRUCTURE OF RHODOBACTER SPHAEROIDES LH1 B
JRNL TITL 2 REVEALS TWO HELICAL DOMAINS SEPARATED BY A FLEXIBLE REGION:
JRNL TITL 3 STRUCTURAL CONSEQUENCES FOR THE LH1 COMPLEX
JRNL REF J.MOL.BIOL. V. 298 83 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10756106
JRNL DOI 10.1006/JMBI.2000.3649
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1F
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DX7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1290001864.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 6
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: SOLVENT: 1:1 CHLOROFORM-D:METHANOL-D3
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O SER A 4 N LEU A 6 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 1 LYS A 3 -97.66 -82.28
REMARK 500 1 ASP A 5 43.37 15.06
REMARK 500 1 LEU A 6 52.00 17.31
REMARK 500 1 LEU A 11 -29.28 -37.88
REMARK 500 1 THR A 12 -70.09 -50.68
REMARK 500 1 ASP A 13 -32.60 -31.41
REMARK 500 1 HIS A 20 -77.39 -88.36
REMARK 500 1 SER A 21 -70.57 -35.63
REMARK 500 1 SER A 25 -71.06 -81.83
REMARK 500 1 ALA A 40 -34.38 -33.79
REMARK 500 1 TRP A 47 -50.14 -151.36
REMARK 500 2 TYR A 8 -79.80 -97.58
REMARK 500 2 THR A 9 -84.14 42.50
REMARK 500 2 THR A 12 -77.16 -47.77
REMARK 500 2 ASP A 13 -30.38 -31.76
REMARK 500 2 HIS A 20 -78.62 -88.83
REMARK 500 2 SER A 21 -71.64 -34.99
REMARK 500 2 TYR A 23 -70.27 -51.60
REMARK 500 2 MET A 24 -34.81 -32.18
REMARK 500 2 PHE A 30 -32.81 -39.56
REMARK 500 2 LEU A 39 -66.88 -93.68
REMARK 500 2 ALA A 40 -32.82 -33.75
REMARK 500 2 TRP A 47 -51.57 -158.36
REMARK 500 3 ASP A 2 -93.46 -117.34
REMARK 500 3 LYS A 3 -3.32 76.64
REMARK 500 3 TYR A 8 -79.50 -58.87
REMARK 500 3 THR A 9 -135.86 17.22
REMARK 500 3 ASP A 13 -42.92 -27.25
REMARK 500 3 HIS A 20 -72.16 -113.92
REMARK 500 3 SER A 21 -75.14 -40.07
REMARK 500 3 TYR A 23 -81.32 -78.24
REMARK 500 3 MET A 24 -25.60 -39.93
REMARK 500 3 LEU A 39 -112.05 -76.81
REMARK 500 3 ALA A 40 -7.13 -48.14
REMARK 500 3 ARG A 45 177.77 -53.68
REMARK 500 3 TRP A 47 17.16 -149.04
REMARK 500 4 ASP A 2 -96.74 -164.47
REMARK 500 4 LYS A 3 -0.97 74.28
REMARK 500 4 THR A 9 -72.90 -53.90
REMARK 500 4 LEU A 11 -79.78 -41.54
REMARK 500 4 THR A 12 -33.45 -27.04
REMARK 500 4 MET A 24 -28.64 -38.91
REMARK 500 4 LEU A 29 -68.73 -95.64
REMARK 500 4 ARG A 45 178.62 -50.17
REMARK 500 4 TRP A 47 -48.35 -145.99
REMARK 500 5 LYS A 3 -35.95 178.35
REMARK 500 5 THR A 12 -74.81 -46.74
REMARK 500 5 ASP A 13 -32.57 -31.26
REMARK 500 5 HIS A 20 -80.76 -91.16
REMARK 500 5 SER A 21 -71.93 -34.31
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
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 45 0.30 SIDE CHAIN
REMARK 500 2 ARG A 45 0.32 SIDE CHAIN
REMARK 500 3 ARG A 45 0.19 SIDE CHAIN
REMARK 500 4 ARG A 45 0.17 SIDE CHAIN
REMARK 500 5 ARG A 45 0.26 SIDE CHAIN
REMARK 500 6 ARG A 45 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4616 RELATED DB: BMRB
DBREF 1DX7 A 1 48 UNP Q7B300 Q7B300_RHOSH 2 49
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 LYS A 3 LEU A 6 5 4
HELIX 2 2 GLY A 7 HIS A 20 1 14
HELIX 3 3 HIS A 20 SER A 31 1 12
HELIX 4 4 ALA A 32 TRP A 44 1 13
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