Header list of 2dba.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL PROTEIN 15-DEC-05 2DBA TITLE THE SOLUTION STRUCTURE OF THE TETRATRICO PEPTIDE REPEAT OF HUMAN TITLE 2 SMOOTH MUSCLE CELL ASSOCIATED PROTEIN-1, ISOFORM 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SMOOTH MUSCLE CELL ASSOCIATED PROTEIN-1, ISOFORM 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: TPR, RESIDUES 8-142; COMPND 5 SYNONYM: SMOOTH MUSCLE CELL ASSOCIATED PROTEIN-1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: UNC45A; SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050302-63; SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS TETRATRICOPEPTIDE REPEAT, SMOOTH MUSCLE CELL ASSOCIATED PROTEIN-1, KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 4 INITIATIVE, RSGI, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.TOCHIO,A.SASAGAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2DBA 1 REMARK SEQADV REVDAT 2 24-FEB-09 2DBA 1 VERSN REVDAT 1 15-JUN-06 2DBA 0 JRNL AUTH N.TOCHIO,A.SASAGAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL THE SOLUTION STRUCTURE OF THE TETRATRICO PEPTIDE REPEAT OF JRNL TITL 2 HUMAN SMOOTH MUSCLE CELL ASSOCIATED PROTEIN-1, ISOFORM 2 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2DBA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1000025211. 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 : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.3MM TPRX3 DOMAIN U-15N,13C; REMARK 210 20MM D-TRIS HCL; 100MM NACL; 1MM REMARK 210 D-DTT; 0.02% NAN3; 90% H2O, 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.932, CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH REMARK 210 THE LEAST RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 MET A 8 37.36 38.78 REMARK 500 1 THR A 15 141.39 -173.29 REMARK 500 1 ALA A 25 94.82 -51.61 REMARK 500 1 GLN A 30 -68.27 -90.64 REMARK 500 1 ASP A 43 93.92 -57.95 REMARK 500 1 LEU A 78 46.25 -96.16 REMARK 500 1 GLU A 79 47.97 36.30 REMARK 500 1 ASP A 95 -70.70 -110.92 REMARK 500 1 ASN A 132 103.05 -51.92 REMARK 500 1 VAL A 134 -31.84 -35.55 REMARK 500 2 SER A 5 146.66 -35.58 REMARK 500 2 MET A 8 136.94 -171.68 REMARK 500 2 PRO A 20 -171.78 -69.77 REMARK 500 2 THR A 22 141.45 -171.42 REMARK 500 2 ASP A 43 89.37 -55.78 REMARK 500 2 ASP A 58 46.17 -80.35 REMARK 500 2 THR A 60 157.50 -49.81 REMARK 500 2 LEU A 78 45.42 -92.32 REMARK 500 2 GLU A 79 46.04 36.32 REMARK 500 2 ASP A 95 -67.25 -94.84 REMARK 500 2 ARG A 114 57.35 -106.21 REMARK 500 2 ASN A 132 95.53 -52.78 REMARK 500 2 PRO A 145 86.26 -69.69 REMARK 500 2 SER A 146 45.19 34.61 REMARK 500 3 PRO A 16 -168.17 -69.77 REMARK 500 3 GLU A 17 144.14 -37.25 REMARK 500 3 PRO A 18 84.06 -69.79 REMARK 500 3 PRO A 20 -178.74 -69.72 REMARK 500 3 ALA A 25 50.01 -100.54 REMARK 500 3 SER A 26 75.93 -110.14 REMARK 500 3 GLN A 30 -65.73 -90.95 REMARK 500 3 LEU A 31 -34.74 -39.32 REMARK 500 3 ASP A 43 93.54 -50.00 REMARK 500 3 ASP A 58 85.99 -61.12 REMARK 500 3 THR A 60 159.52 -49.55 REMARK 500 3 LEU A 78 45.52 -90.67 REMARK 500 3 GLU A 79 50.16 33.40 REMARK 500 3 ARG A 114 59.44 -118.09 REMARK 500 3 ASN A 132 91.93 -47.14 REMARK 500 3 VAL A 134 -29.45 -39.98 REMARK 500 3 PRO A 145 94.65 -69.82 REMARK 500 3 SER A 146 43.87 38.46 REMARK 500 4 PRO A 13 -177.23 -69.68 REMARK 500 4 ALA A 25 49.22 39.45 REMARK 500 4 ASP A 43 92.79 -58.35 REMARK 500 4 LEU A 78 39.47 -86.32 REMARK 500 4 GLU A 79 43.00 37.64 REMARK 500 4 ASP A 95 -68.32 -104.86 REMARK 500 4 ALA A 118 -39.18 -39.47 REMARK 500 4 GLN A 123 -38.02 -35.02 REMARK 500 REMARK 500 THIS ENTRY HAS 273 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002005909.1 RELATED DB: TARGETDB DBREF 2DBA A 8 142 UNP Q9H3U1 Q9H3U1_HUMAN 1 137 SEQADV 2DBA GLY A 1 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA SER A 2 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA SER A 3 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA GLY A 4 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA SER A 5 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA SER A 6 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA GLY A 7 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA SER A 143 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA GLY A 144 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA PRO A 145 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA SER A 146 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA SER A 147 UNP Q9H3U1 CLONING ARTIFACT SEQADV 2DBA GLY A 148 UNP Q9H3U1 CLONING ARTIFACT SEQRES 1 A 148 GLY SER SER GLY SER SER GLY MET THR VAL SER GLY PRO SEQRES 2 A 148 GLY THR PRO GLU PRO ARG PRO ALA THR PRO GLY ALA SER SEQRES 3 A 148 SER VAL GLU GLN LEU ARG LYS GLU GLY ASN GLU LEU PHE SEQRES 4 A 148 LYS CYS GLY ASP TYR GLY GLY ALA LEU ALA ALA TYR THR SEQRES 5 A 148 GLN ALA LEU GLY LEU ASP ALA THR PRO GLN ASP GLN ALA SEQRES 6 A 148 VAL LEU HIS ARG ASN ARG ALA ALA CYS HIS LEU LYS LEU SEQRES 7 A 148 GLU ASP TYR ASP LYS ALA GLU THR GLU ALA SER LYS ALA SEQRES 8 A 148 ILE GLU LYS ASP GLY GLY ASP VAL LYS ALA LEU TYR ARG SEQRES 9 A 148 ARG SER GLN ALA LEU GLU LYS LEU GLY ARG LEU ASP GLN SEQRES 10 A 148 ALA VAL LEU ASP LEU GLN ARG CYS VAL SER LEU GLU PRO SEQRES 11 A 148 LYS ASN LYS VAL PHE GLN GLU ALA LEU ARG ASN ILE SER SEQRES 12 A 148 GLY PRO SER SER GLY HELIX 1 1 SER A 27 LYS A 40 1 14 HELIX 2 2 ASP A 43 GLY A 56 1 14 HELIX 3 3 THR A 60 LEU A 78 1 19 HELIX 4 4 ASP A 80 ASP A 95 1 16 HELIX 5 5 ASP A 98 GLY A 113 1 16 HELIX 6 6 ARG A 114 GLU A 129 1 16 HELIX 7 7 ASN A 132 GLY A 144 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 - r 9 2 Bytes