Header list of 1qvp.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 28-AUG-03 1QVP TITLE C TERMINAL SH3-LIKE DOMAIN FROM DIPHTHERIA TOXIN REPRESSOR RESIDUES TITLE 2 144-226. COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIPHTHERIA TOXIN REPRESSOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 144-226; COMPND 5 SYNONYM: IRON-DEPENDENT DIPHTHERIA TOX REGULATORY ELEMENT, TOX COMPND 6 REGULATORY FACTOR; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM DIPHTHERIAE; SOURCE 3 ORGANISM_TAXID: 1717; SOURCE 4 GENE: DTXR; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-15B KEYWDS REPRESSOR, DTXR, C-TERMINAL DOMAIN, PROKARYOTIC SH3 DOMAIN, KEYWDS 2 TRANSCRIPTION REGULATION, PEPTIDE-BINDING, GENE REGULATION, DNA KEYWDS 3 BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 13 MDLTYP MINIMIZED AVERAGE AUTHOR G.P.WYLIE,V.RANGACHARI,E.A.BIENKIEWICZ,V.MARIN,N.BHATTACHARYA, AUTHOR 2 J.F.LOVE,J.R.MURPHY,T.M.LOGAN REVDAT 5 02-MAR-22 1QVP 1 REMARK SEQADV REVDAT 4 21-APR-09 1QVP 1 REMARK REVDAT 3 24-FEB-09 1QVP 1 VERSN REVDAT 2 15-MAR-05 1QVP 1 JRNL REVDAT 1 02-NOV-04 1QVP 0 JRNL AUTH G.P.WYLIE,V.RANGACHARI,E.A.BIENKIEWICZ,V.MARIN, JRNL AUTH 2 N.BHATTACHARYA,J.F.LOVE,J.R.MURPHY,T.M.LOGAN JRNL TITL PROLYLPEPTIDE BINDING BY THE PROKARYOTIC SH3-LIKE DOMAIN OF JRNL TITL 2 THE DIPHTHERIA TOXIN REPRESSOR: A REGULATORY SWITCH. JRNL REF BIOCHEMISTRY V. 44 40 2005 JRNL REFN ISSN 0006-2960 JRNL PMID 15628844 JRNL DOI 10.1021/BI048035P REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1QVP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-03. REMARK 100 THE DEPOSITION ID IS D_1000020125. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1-2 MM DTXR144-226 U-15N; 10MM REMARK 210 POTASSIUM PHOSPHATE BUFFER PH6.5; REMARK 210 1-2 MM DTXR144-226 U-15N AND U- REMARK 210 13C; 10MM POTASSIUM PHOSPHATE REMARK 210 BUFFER PH6.5 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNCACB; REMARK 210 CBCA(CO)NH; HNCO; H(C)(CO)NH- REMARK 210 TOCSY; HC(CO)NH-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 720 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 64 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 13 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: FOR LISTING OF EXPERIMENTS RUN PLEASE SEE THE PRIMARY REMARK 210 CITATION 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 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 MET A 143 -76.03 -68.94 REMARK 500 1 ASP A 144 -56.88 72.22 REMARK 500 1 ALA A 146 63.33 -174.06 REMARK 500 1 ALA A 147 112.62 67.49 REMARK 500 1 SER A 158 -155.35 -98.26 REMARK 500 1 GLU A 170 106.98 60.77 REMARK 500 1 ILE A 171 -76.64 -146.55 REMARK 500 1 PHE A 172 -84.33 59.97 REMARK 500 1 GLN A 173 74.04 -165.05 REMARK 500 1 PHE A 179 47.87 -104.08 REMARK 500 1 THR A 180 -61.98 -130.06 REMARK 500 1 ASP A 199 80.81 -68.05 REMARK 500 1 ASN A 207 -75.31 63.57 REMARK 500 1 ASP A 215 167.70 60.45 REMARK 500 1 ASP A 216 -80.61 60.56 REMARK 500 1 LEU A 217 72.55 -110.04 REMARK 500 1 ALA A 218 -75.46 -164.71 REMARK 500 1 THR A 220 -142.68 52.34 REMARK 500 1 ILE A 221 142.73 64.98 REMARK 500 1 GLU A 224 -165.47 -104.38 REMARK 500 1 GLU A 225 -168.26 68.07 REMARK 500 2 MET A 143 -64.11 -148.95 REMARK 500 2 ASP A 144 101.64 60.49 REMARK 500 2 ALA A 145 -50.02 -140.91 REMARK 500 2 ALA A 146 -77.53 175.99 REMARK 500 2 PRO A 148 178.38 -49.00 REMARK 500 2 THR A 150 -82.00 -176.17 REMARK 500 2 ALA A 156 53.20 -92.40 REMARK 500 2 THR A 157 -41.99 -137.26 REMARK 500 2 SER A 158 110.07 -171.74 REMARK 500 2 MET A 159 -57.99 108.94 REMARK 500 2 ARG A 161 -70.44 -150.06 REMARK 500 2 GLU A 170 -73.46 -94.94 REMARK 500 2 PHE A 172 98.41 -169.24 REMARK 500 2 GLN A 173 -52.67 77.88 REMARK 500 2 GLU A 175 -46.91 -160.27 REMARK 500 2 ASP A 177 -82.31 59.03 REMARK 500 2 PHE A 179 45.05 -92.08 REMARK 500 2 THR A 180 -67.45 -137.17 REMARK 500 2 ASP A 184 39.42 -90.22 REMARK 500 2 ALA A 185 111.23 -165.28 REMARK 500 2 ASP A 186 70.87 -65.93 REMARK 500 2 ARG A 188 -168.97 -123.20 REMARK 500 2 ASN A 207 -72.23 64.63 REMARK 500 2 LEU A 213 175.25 177.16 REMARK 500 2 ASP A 215 177.77 57.77 REMARK 500 2 ASP A 216 -83.10 62.58 REMARK 500 2 LEU A 217 45.04 -90.41 REMARK 500 2 ALA A 218 -88.40 -174.74 REMARK 500 2 GLU A 225 174.59 58.44 REMARK 500 REMARK 500 THIS ENTRY HAS 305 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7998 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFTS FOR THIS ENTRY REMARK 900 RELATED ID: 1BYM RELATED DB: PDB REMARK 900 PDB FILE FOR THE C TERMINAL DOMAIN OF THIS SAME PROTEIN RESIDUES REMARK 900 130-226 DBREF 1QVP A 144 226 UNP P33120 DTXR_CORDI 144 226 SEQADV 1QVP GLY A 140 UNP P33120 CLONING ARTIFACT SEQADV 1QVP SER A 141 UNP P33120 CLONING ARTIFACT SEQADV 1QVP HIS A 142 UNP P33120 CLONING ARTIFACT SEQADV 1QVP MET A 143 UNP P33120 CLONING ARTIFACT SEQRES 1 A 87 GLY SER HIS MET ASP ALA ALA ALA PRO GLY THR ARG VAL SEQRES 2 A 87 ILE ASP ALA ALA THR SER MET PRO ARG LYS VAL ARG ILE SEQRES 3 A 87 VAL GLN ILE ASN GLU ILE PHE GLN VAL GLU THR ASP GLN SEQRES 4 A 87 PHE THR GLN LEU LEU ASP ALA ASP ILE ARG VAL GLY SER SEQRES 5 A 87 GLU VAL GLU ILE VAL ASP ARG ASP GLY HIS ILE THR LEU SEQRES 6 A 87 SER HIS ASN GLY LYS ASP VAL GLU LEU LEU ASP ASP LEU SEQRES 7 A 87 ALA HIS THR ILE ARG ILE GLU GLU LEU HELIX 1 1 THR A 176 PHE A 179 5 4 HELIX 2 2 THR A 180 ALA A 185 1 6 SHEET 1 A 5 LYS A 209 VAL A 211 0 SHEET 2 A 5 ILE A 202 HIS A 206 -1 N HIS A 206 O LYS A 209 SHEET 3 A 5 GLU A 192 ASP A 197 -1 N VAL A 196 O THR A 203 SHEET 4 A 5 LYS A 162 GLN A 167 -1 N VAL A 163 O VAL A 193 SHEET 5 A 5 ARG A 222 GLU A 224 -1 O GLU A 224 N ARG A 164 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 2 2 Bytes