Header list of 1ftt.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN 03-OCT-95 1FTT TITLE THYROID TRANSCRIPTION FACTOR 1 HOMEODOMAIN (RATTUS NORVEGICUS) COMPND MOL_ID: 1; COMPND 2 MOLECULE: THYROID TRANSCRIPTION FACTOR 1 HOMEODOMAIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: TTF-1 HD; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: PH = 4.0 - 4.1, T = 287 - 289 K, NAN3 (W/V) = 0.2 - COMPND 7 0.5% SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 GENE: RAT TTF-1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT7.7; SOURCE 10 EXPRESSION_SYSTEM_GENE: RAT TTF-1 KEYWDS DNA BINDING PROTEIN, HOMEODOMAIN, TRANSCRIPTION FACTOR EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR F.FOGOLARI,G.ESPOSITO,G.DAMANTE,S.FORMISANO,R.DI LAURO,P.VIGLINO REVDAT 3 23-FEB-22 1FTT 1 REMARK REVDAT 2 24-FEB-09 1FTT 1 VERSN REVDAT 1 29-JAN-96 1FTT 0 JRNL AUTH G.ESPOSITO,F.FOGOLARI,G.DAMANTE,S.FORMISANO,G.TELL, JRNL AUTH 2 A.LEONARDI,R.DI LAURO,P.VIGLINO JRNL TITL ANALYSIS OF THE SOLUTION STRUCTURE OF THE HOMEODOMAIN OF RAT JRNL TITL 2 THYROID TRANSCRIPTION FACTOR 1 BY 1H-NMR SPECTROSCOPY AND JRNL TITL 3 RESTRAINED MOLECULAR MECHANICS. JRNL REF EUR.J.BIOCHEM. V. 241 101 1996 JRNL REFN ISSN 0014-2956 JRNL PMID 8898894 JRNL DOI 10.1111/J.1432-1033.1996.0101T.X REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH P.VIGLINO,F.FOGOLARI,S.FORMISANO,N.BORTOLOTTI,G.DAMANTE, REMARK 1 AUTH 2 R.DI LAURO,G.ESPOSITO REMARK 1 TITL STRUCTURAL STUDY OF RAT THYROID TRANSCRIPTION FACTOR 1 REMARK 1 TITL 2 HOMEODOMAIN (TTF-1 HD) BY NUCLEAR MAGNETIC RESONANCE REMARK 1 REF FEBS LETT. V. 336 397 1993 REMARK 1 REFN ISSN 0014-5793 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER REMARK 3 AUTHORS : BIOSYM TECHNOLOGIES REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1FTT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000173419. 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 : 20 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 1 VAL A 6 -71.25 -67.49 REMARK 500 1 PHE A 8 175.65 60.73 REMARK 500 1 HIS A 39 98.26 109.72 REMARK 500 1 ALA A 60 67.48 67.53 REMARK 500 1 LYS A 61 149.51 57.51 REMARK 500 1 ALA A 64 -114.19 -91.40 REMARK 500 2 ARG A 2 90.15 -162.50 REMARK 500 2 ARG A 4 -71.97 -138.25 REMARK 500 2 VAL A 6 -72.43 -66.77 REMARK 500 2 LEU A 7 50.87 -159.71 REMARK 500 2 GLN A 22 -72.13 -87.44 REMARK 500 2 HIS A 39 104.08 123.76 REMARK 500 2 GLN A 59 93.10 72.21 REMARK 500 2 LYS A 61 -82.16 60.34 REMARK 500 2 LYS A 63 -63.68 75.25 REMARK 500 2 ALA A 65 -47.86 74.79 REMARK 500 3 ARG A 4 -62.32 160.69 REMARK 500 3 HIS A 39 95.89 100.08 REMARK 500 3 LYS A 63 -52.72 75.01 REMARK 500 3 ALA A 64 -78.38 -149.47 REMARK 500 3 ALA A 65 -80.91 61.95 REMARK 500 3 GLN A 66 40.36 71.24 REMARK 500 4 ARG A 2 -149.17 58.49 REMARK 500 4 LYS A 3 99.39 71.16 REMARK 500 4 HIS A 39 103.39 107.50 REMARK 500 4 LEU A 40 -174.44 -179.19 REMARK 500 4 ALA A 60 -171.60 61.63 REMARK 500 4 LYS A 61 -56.21 73.99 REMARK 500 4 ASP A 62 76.09 -68.51 REMARK 500 4 LYS A 63 -22.14 143.41 REMARK 500 4 GLN A 66 -37.89 -167.60 REMARK 500 5 PHE A 8 -179.74 62.81 REMARK 500 5 GLN A 22 -73.18 -107.12 REMARK 500 5 HIS A 39 79.43 119.64 REMARK 500 5 ALA A 60 -104.68 49.83 REMARK 500 5 LYS A 61 -103.73 38.12 REMARK 500 5 ALA A 64 80.56 -172.79 REMARK 500 5 ALA A 65 -47.84 -141.10 REMARK 500 5 GLN A 66 41.78 -76.44 REMARK 500 6 LYS A 3 -73.69 -163.22 REMARK 500 6 ARG A 4 -54.12 -153.28 REMARK 500 6 ARG A 5 161.62 69.57 REMARK 500 6 VAL A 6 -84.48 -80.19 REMARK 500 6 LEU A 7 37.36 -99.72 REMARK 500 6 GLN A 22 -54.76 -138.17 REMARK 500 6 HIS A 39 74.46 107.00 REMARK 500 6 GLN A 59 -63.02 70.04 REMARK 500 6 ALA A 60 -93.50 58.46 REMARK 500 6 LYS A 61 104.88 -168.86 REMARK 500 6 LYS A 63 59.19 -100.72 REMARK 500 REMARK 500 THIS ENTRY HAS 173 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LYS A 61 ASP A 62 5 -148.15 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 TYR A 14 0.09 SIDE CHAIN REMARK 500 1 TYR A 25 0.08 SIDE CHAIN REMARK 500 2 TYR A 54 0.07 SIDE CHAIN REMARK 500 4 TYR A 25 0.08 SIDE CHAIN REMARK 500 5 ARG A 58 0.08 SIDE CHAIN REMARK 500 6 TYR A 25 0.10 SIDE CHAIN REMARK 500 7 TYR A 14 0.07 SIDE CHAIN REMARK 500 7 TYR A 54 0.09 SIDE CHAIN REMARK 500 8 TYR A 25 0.07 SIDE CHAIN REMARK 500 12 TYR A 14 0.09 SIDE CHAIN REMARK 500 13 ARG A 31 0.09 SIDE CHAIN REMARK 500 15 TYR A 14 0.07 SIDE CHAIN REMARK 500 15 ARG A 31 0.09 SIDE CHAIN REMARK 500 15 TYR A 54 0.08 SIDE CHAIN REMARK 500 16 TYR A 25 0.07 SIDE CHAIN REMARK 500 17 TYR A 14 0.07 SIDE CHAIN REMARK 500 18 TYR A 14 0.09 SIDE CHAIN REMARK 500 18 TYR A 25 0.07 SIDE CHAIN REMARK 500 19 TYR A 54 0.06 SIDE CHAIN REMARK 500 20 ARG A 19 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1FTT A 1 67 UNP P23441 TITF1_RAT 161 227 SEQRES 1 A 68 MET ARG ARG LYS ARG ARG VAL LEU PHE SER GLN ALA GLN SEQRES 2 A 68 VAL TYR GLU LEU GLU ARG ARG PHE LYS GLN GLN LYS TYR SEQRES 3 A 68 LEU SER ALA PRO GLU ARG GLU HIS LEU ALA SER MET ILE SEQRES 4 A 68 HIS LEU THR PRO THR GLN VAL LYS ILE TRP PHE GLN ASN SEQRES 5 A 68 HIS ARG TYR LYS MET LYS ARG GLN ALA LYS ASP LYS ALA SEQRES 6 A 68 ALA GLN GLN HELIX 1 1 GLN A 10 GLN A 22 1 13 HELIX 2 2 ALA A 28 MET A 37 1 10 HELIX 3 3 PRO A 42 ARG A 58 1 17 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 - b 23 2 Bytes