Header list of 2fft.pdb file
Complete list - r 9 2 Bytes
HEADER PLANT PROTEIN 20-DEC-05 2FFT TITLE NMR STRUCTURE OF SPINACH THYLAKOID SOLUBLE PHOSPHOPROTEIN OF 9 KDA IN TITLE 2 SDS MICELLES COMPND MOL_ID: 1; COMPND 2 MOLECULE: THYLAKOID SOLUBLE PHOSPHOPROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA; SOURCE 3 ORGANISM_COMMON: SPINACH; SOURCE 4 ORGANISM_TAXID: 3562; SOURCE 5 GENE: TSP9; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVP13 KEYWDS THYLAKOID SOLUBLE PHOSPHOPROTEIN, TSP9, STRUCTURAL GENOMICS, PSI, KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, CENTER FOR EUKARYOTIC STRUCTURAL KEYWDS 3 GENOMICS, CESG, PLANT PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.SONG,I.CARLBERG,M.S.LEE,J.L.MARKLEY,CENTER FOR EUKARYOTIC AUTHOR 2 STRUCTURAL GENOMICS (CESG) REVDAT 4 09-MAR-22 2FFT 1 REMARK SEQADV REVDAT 3 10-NOV-09 2FFT 1 JRNL REVDAT 2 24-FEB-09 2FFT 1 VERSN REVDAT 1 17-JAN-06 2FFT 0 JRNL AUTH J.SONG,M.S.LEE,I.CARLBERG,A.V.VENER,J.L.MARKLEY JRNL TITL MICELLE-INDUCED FOLDING OF SPINACH THYLAKOID SOLUBLE JRNL TITL 2 PHOSPHOPROTEIN OF 9 KDA AND ITS FUNCTIONAL IMPLICATIONS. JRNL REF BIOCHEMISTRY V. 45 15633 2006 JRNL REFN ISSN 0006-2960 JRNL PMID 17176085 JRNL DOI 10.1021/BI062148M REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 2.1 REMARK 3 AUTHORS : GUENTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 STRUCTURES ARE BASED ON A TOTAL OF 767 NOE RESTRAINTS (355 INTRA, REMARK 3 278 SEQUENTIAL, 134 MEDIUM AND REMARK 3 0 LONG RANGE INTERMOLECULR) AND 38 PHI AND PSI DIHEDRAL ANGLE REMARK 3 CONSTRAINTS. REMARK 4 REMARK 4 2FFT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1000035827. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 175 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 10 MM HEPES, 100MM NACL, 75 MM REMARK 210 SDS, 0.5 MM 13C,15N-LABELED TSP9, REMARK 210 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H,15N-HSQC; 1H,13C-HSQC; REMARK 210 HNCACB; CBCACONH; CCONH; REMARK 210 HCCHTOCSY; HBACONH; 13C-EDITED REMARK 210 1H,1H-NOESY; 15C-EDITED 1H,1H- REMARK 210 NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 1.1, SPARKY 3.72, NMRPIPE REMARK 210 97.027.12.56, CYANA 2.1 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: ALL TRIPLE-RESONANCE AND NOESY SPECTRA WERE ACQUIRED USING REMARK 210 THE SPECTROMETERS EQUIPPED WITH A CRYOGENIC PROBE. 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 1 LYS A 4 -176.08 56.51 REMARK 500 1 LYS A 10 104.62 -174.45 REMARK 500 1 LYS A 25 -76.70 68.07 REMARK 500 1 GLN A 28 -71.57 -110.22 REMARK 500 1 PHE A 29 27.04 -162.39 REMARK 500 1 ASP A 33 70.97 62.45 REMARK 500 1 PRO A 34 79.54 -69.71 REMARK 500 1 LEU A 36 -74.06 -163.15 REMARK 500 1 LYS A 42 -173.34 59.19 REMARK 500 1 SER A 43 -66.70 -141.42 REMARK 500 1 SER A 46 40.61 -168.76 REMARK 500 1 LYS A 51 163.59 63.07 REMARK 500 1 SER A 56 127.44 -173.70 REMARK 500 1 THR A 61 -48.01 -140.66 REMARK 500 1 LYS A 67 -37.13 -174.69 REMARK 500 1 LYS A 68 88.25 60.78 REMARK 500 1 PHE A 76 -68.44 -106.61 REMARK 500 1 LYS A 83 55.81 -167.84 REMARK 500 2 LYS A 4 87.42 62.43 REMARK 500 2 GLU A 8 77.06 62.14 REMARK 500 2 LYS A 10 81.01 -161.57 REMARK 500 2 GLN A 11 48.30 -142.07 REMARK 500 2 THR A 24 78.95 56.10 REMARK 500 2 LYS A 25 -176.64 -60.60 REMARK 500 2 ASP A 27 -177.79 56.85 REMARK 500 2 PHE A 29 26.79 -152.64 REMARK 500 2 ASP A 33 72.25 54.28 REMARK 500 2 LEU A 36 -73.88 -122.01 REMARK 500 2 LYS A 50 -69.05 -94.64 REMARK 500 2 THR A 54 -65.20 -99.05 REMARK 500 2 THR A 55 74.04 56.95 REMARK 500 2 LYS A 58 -68.78 72.33 REMARK 500 2 LYS A 59 -168.77 62.37 REMARK 500 2 PRO A 65 76.22 -69.69 REMARK 500 2 LYS A 68 179.84 59.14 REMARK 500 2 LYS A 83 79.08 55.83 REMARK 500 3 LYS A 4 64.30 -111.52 REMARK 500 3 ALA A 7 -70.79 -56.95 REMARK 500 3 GLU A 8 -58.84 -161.22 REMARK 500 3 THR A 9 83.78 52.53 REMARK 500 3 GLN A 11 176.56 59.67 REMARK 500 3 LYS A 13 30.82 -149.20 REMARK 500 3 LYS A 25 174.61 -54.62 REMARK 500 3 GLN A 28 -173.68 59.46 REMARK 500 3 GLU A 31 27.04 -145.57 REMARK 500 3 LEU A 36 -74.27 -130.93 REMARK 500 3 ASP A 40 -39.38 -170.67 REMARK 500 3 LYS A 42 108.31 -163.31 REMARK 500 3 SER A 44 -56.84 -155.84 REMARK 500 3 THR A 47 142.17 -171.35 REMARK 500 REMARK 500 THIS ENTRY HAS 413 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GO.78855 RELATED DB: TARGETDB DBREF 2FFT A 2 84 GB 27529048 CAD45559 21 103 SEQADV 2FFT SER A 1 GB 27529048 CLONING ARTIFACT SEQRES 1 A 84 SER ALA ALA LYS GLY THR ALA GLU THR LYS GLN GLU LYS SEQRES 2 A 84 SER PHE VAL ASP TRP LEU LEU GLY LYS ILE THR LYS GLU SEQRES 3 A 84 ASP GLN PHE TYR GLU THR ASP PRO ILE LEU ARG GLY GLY SEQRES 4 A 84 ASP VAL LYS SER SER GLY SER THR SER GLY LYS LYS GLY SEQRES 5 A 84 GLY THR THR SER GLY LYS LYS GLY THR VAL SER ILE PRO SEQRES 6 A 84 SER LYS LYS LYS ASN GLY ASN GLY GLY VAL PHE GLY GLY SEQRES 7 A 84 LEU PHE ALA LYS LYS ASP HELIX 1 1 SER A 14 THR A 24 1 11 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 - r 9 2 Bytes