Header list of 1qw1.pdb file
Complete list - v 6 2 Bytes
HEADER GENE REGULATION 29-AUG-03 1QW1
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF DTXR RESIDUES 110-226
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPHTHERIA TOXIN REPRESSOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 110-226;
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
EXPDTA SOLUTION NMR
NUMMDL 14
MDLTYP MINIMIZED AVERAGE
AUTHOR G.P.WYLIE,V.RANGACHARI,E.A.BIENKIEWICZ,J.F.LOVE,J.R.MURPHY,T.M.LOGAN
REVDAT 3 06-NOV-19 1QW1 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1QW1 1 VERSN
REVDAT 1 15-MAR-05 1QW1 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 1QW1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000020137.
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 DTXR110-226 U-15N, 50 MM
REMARK 210 POTASSIUM PHOSPHATE, PH 6.5; 1-2
REMARK 210 MM DTXR110-226 U-15N U-13C, 50
REMARK 210 MM POTASSIUM PHOSPHATE, PH 6.5;
REMARK 210 1-2 MM DTXR110-226 U-15N U-13C,
REMARK 210 50 MM POTASSIUM PHOSPHATE, PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D
REMARK 210 NOESY; HNCACB; H(C)(CO)NH-TOCSY;
REMARK 210 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 : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
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: PLEASE SEE PRIMARY CITATION FOR MORE DETAILS ON THE
REMARK 210 EXPERIMENTS RECORDED.
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 O ARG A 151 H ASP A 154 1.52
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 HIS A 108 -88.85 59.61
REMARK 500 1 MET A 109 86.31 48.33
REMARK 500 1 LEU A 120 72.70 -110.81
REMARK 500 1 VAL A 123 -166.36 -107.94
REMARK 500 1 SER A 124 172.96 75.13
REMARK 500 1 SER A 126 76.20 -111.56
REMARK 500 1 ASN A 130 141.77 49.20
REMARK 500 1 ILE A 132 -27.46 136.92
REMARK 500 1 PRO A 133 53.66 -66.47
REMARK 500 1 VAL A 140 -61.59 145.30
REMARK 500 1 ASN A 142 122.47 169.25
REMARK 500 1 ASP A 144 -40.94 -164.61
REMARK 500 1 ALA A 146 154.07 65.70
REMARK 500 1 PRO A 148 79.15 -32.31
REMARK 500 1 ARG A 151 118.45 69.54
REMARK 500 1 ALA A 156 34.94 -175.43
REMARK 500 1 THR A 157 -33.39 -157.30
REMARK 500 1 SER A 158 48.27 -82.92
REMARK 500 1 MET A 159 61.62 62.95
REMARK 500 1 ARG A 161 -47.48 -146.12
REMARK 500 1 LYS A 162 95.02 -170.04
REMARK 500 1 GLN A 167 -175.65 -178.63
REMARK 500 1 ILE A 168 -60.83 -136.10
REMARK 500 1 ASN A 169 -71.19 178.32
REMARK 500 1 GLU A 170 -163.05 -173.62
REMARK 500 1 PHE A 172 -58.53 -26.86
REMARK 500 1 VAL A 174 37.86 -168.71
REMARK 500 1 GLU A 175 77.31 -112.95
REMARK 500 1 ILE A 187 90.11 32.93
REMARK 500 1 SER A 191 -161.45 -72.19
REMARK 500 1 ARG A 198 105.39 -169.98
REMARK 500 1 ASN A 207 -55.49 -19.40
REMARK 500 1 GLU A 212 -66.46 -93.77
REMARK 500 1 LEU A 213 77.18 57.03
REMARK 500 1 ALA A 218 46.10 -90.22
REMARK 500 1 ILE A 223 -154.01 -123.43
REMARK 500 2 SER A 107 -67.82 69.74
REMARK 500 2 MET A 109 94.16 58.86
REMARK 500 2 ASP A 122 -71.49 -114.36
REMARK 500 2 ARG A 125 -43.99 -162.34
REMARK 500 2 PRO A 127 176.19 -56.39
REMARK 500 2 ILE A 132 -32.05 148.91
REMARK 500 2 VAL A 140 101.71 58.60
REMARK 500 2 ASN A 142 96.13 -164.57
REMARK 500 2 ASP A 144 -48.66 -154.85
REMARK 500 2 ALA A 145 89.56 -153.72
REMARK 500 2 ARG A 151 30.56 74.60
REMARK 500 2 VAL A 152 -70.75 52.51
REMARK 500 2 ILE A 153 85.09 -44.04
REMARK 500 2 ASP A 154 -45.54 168.06
REMARK 500
REMARK 500 THIS ENTRY HAS 505 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BYM RELATED DB: PDB
REMARK 900 STRUCTURE OF C-TERMINAL DOMAIN OF DTXR RESIDUES 130-226
REMARK 900 RELATED ID: 1QVP RELATED DB: PDB
REMARK 900 STRUCTURE OF C-TERMINAL DOMAIN OF DTXR RESIDUES 144-226
REMARK 900 RELATED ID: 6852 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS FOR C-TERMINAL DOMAIN OF DTXR RESIDUES 110-226
DBREF 1QW1 A 110 226 UNP P33120 DTXR_CORDI 110 226
SEQADV 1QW1 GLY A 106 UNP P33120 CLONING ARTIFACT
SEQADV 1QW1 SER A 107 UNP P33120 CLONING ARTIFACT
SEQADV 1QW1 HIS A 108 UNP P33120 CLONING ARTIFACT
SEQADV 1QW1 MET A 109 UNP P33120 CLONING ARTIFACT
SEQRES 1 A 121 GLY SER HIS MET ASP GLU VAL GLU ARG ARG LEU VAL LYS
SEQRES 2 A 121 VAL LEU LYS ASP VAL SER ARG SER PRO PHE GLY ASN PRO
SEQRES 3 A 121 ILE PRO GLY LEU ASP GLU LEU GLY VAL GLY ASN SER ASP
SEQRES 4 A 121 ALA ALA ALA PRO GLY THR ARG VAL ILE ASP ALA ALA THR
SEQRES 5 A 121 SER MET PRO ARG LYS VAL ARG ILE VAL GLN ILE ASN GLU
SEQRES 6 A 121 ILE PHE GLN VAL GLU THR ASP GLN PHE THR GLN LEU LEU
SEQRES 7 A 121 ASP ALA ASP ILE ARG VAL GLY SER GLU VAL GLU ILE VAL
SEQRES 8 A 121 ASP ARG ASP GLY HIS ILE THR LEU SER HIS ASN GLY LYS
SEQRES 9 A 121 ASP VAL GLU LEU LEU ASP ASP LEU ALA HIS THR ILE ARG
SEQRES 10 A 121 ILE GLU GLU LEU
HELIX 1 1 GLN A 178 LEU A 183 1 6
SHEET 1 A 2 GLU A 194 ASP A 197 0
SHEET 2 A 2 ILE A 202 SER A 205 -1 O SER A 205 N GLU A 194
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 - v 6 2 Bytes