Header list of 1psf.pdb file
Complete list - 25 201 Bytes
HEADER PHOTOSYSTEM I 13-APR-94 1PSF
TITLE THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF PSAE FROM THE
TITLE 2 CYANOBACTERIUM SYNECHOCOCCUS SP. STRAIN PCC 7002: A PHOTOSYSTEM I
TITLE 3 PROTEIN THAT SHOWS STRUCTURAL HOMOLOGY WITH SH3 DOMAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYSTEM I ACCESSORY PROTEIN E;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 32049;
SOURCE 4 STRAIN: PCC 7002
KEYWDS PHOTOSYSTEM I
EXPDTA SOLUTION NMR
AUTHOR C.J.FALZONE,Y.-H.KAO,J.ZHAO,D.A.BRYANT,J.T.J.LECOMTE
REVDAT 4 13-JUL-11 1PSF 1 VERSN
REVDAT 3 24-FEB-09 1PSF 1 VERSN
REVDAT 2 01-APR-03 1PSF 1 JRNL
REVDAT 1 20-APR-95 1PSF 0
JRNL AUTH C.J.FALZONE,Y.H.KAO,J.ZHAO,D.A.BRYANT,J.T.LECOMTE
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF PSAE FROM THE
JRNL TITL 2 CYANOBACTERIUM SYNECHOCOCCUS SP. STRAIN PCC 7002, A
JRNL TITL 3 PHOTOSYSTEM I PROTEIN THAT SHOWS STRUCTURAL HOMOLOGY WITH
JRNL TITL 4 SH3 DOMAINS.
JRNL REF BIOCHEMISTRY V. 33 6052 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 8193119
JRNL DOI 10.1021/BI00186A004
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.J.FALZONE,Y.-H.KAO,J.ZHAO,K.L.MACLAUGHLIN,D.A.BRYANT,
REMARK 1 AUTH 2 J.T.J.LECOMTE
REMARK 1 TITL 1H AND 15N NMR ASSIGNMENTS OF PSAE, A PHOTOSYSTEM I SUBUNIT
REMARK 1 TITL 2 FROM THE CYANOBACTERIUM SYNECHOCOCCUS SP. STRAIN PCC 7002
REMARK 1 REF BIOCHEMISTRY V. 33 6043 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PSF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
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 : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
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: NULL
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 ILE A 2 97.53 -62.76
REMARK 500 LYS A 29 39.38 -97.06
REMARK 500 SER A 49 125.35 -176.53
REMARK 500 LEU A 55 -76.25 -115.92
REMARK 500 VAL A 67 106.81 -58.47
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 A 4 0.28 SIDE CHAIN
REMARK 500 ARG A 12 0.27 SIDE CHAIN
REMARK 500 ARG A 39 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PSE RELATED DB: PDB
DBREF 1PSF A 1 69 UNP P31969 PSAE_SYNP2 1 69
SEQRES 1 A 69 ALA ILE GLU ARG GLY SER LYS VAL LYS ILE LEU ARG LYS
SEQRES 2 A 69 GLU SER TYR TRP TYR GLY ASP VAL GLY THR VAL ALA SER
SEQRES 3 A 69 ILE ASP LYS SER GLY ILE ILE TYR PRO VAL ILE VAL ARG
SEQRES 4 A 69 PHE ASN LYS VAL ASN TYR ASN GLY PHE SER GLY SER ALA
SEQRES 5 A 69 GLY GLY LEU ASN THR ASN ASN PHE ALA GLU HIS GLU LEU
SEQRES 6 A 69 GLU VAL VAL GLY
SHEET 1 A 5 THR A 57 PHE A 60 0
SHEET 2 A 5 VAL A 36 ARG A 39 -1 N VAL A 36 O PHE A 60
SHEET 3 A 5 VAL A 21 SER A 26 -1 N THR A 23 O ARG A 39
SHEET 4 A 5 LYS A 7 ILE A 10 -1 N VAL A 8 O GLY A 22
SHEET 5 A 5 LEU A 65 VAL A 67 -1 O GLU A 66 N LYS A 9
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 - 25 201 Bytes