Header list of 1umq.pdb file
Complete list - 9 20 Bytes
HEADER DNA BINDING PROTEIN 28-AUG-03 1UMQ
TITLE SOLUTION STRUCTURE AND DNA BINDING OF THE EFFECTOR DOMAIN FROM THE
TITLE 2 GLOBAL REGULATOR PRRA(REGA) FROM R. SPHAEROIDES: INSIGHTS INTO DNA
TITLE 3 BINDING SPECIFICITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYNTHETIC APPARATUS REGULATORY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA BINDING DOMAIN, RESIDUES 125-184;
COMPND 5 SYNONYM: REGA, REGA PROTEIN, RESPONSE REGULATOR, PRRA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES;
SOURCE 3 ORGANISM_TAXID: 1063;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS DNA-BINDING PROTEIN, RESPONSE REGULATOR, DNA BINDING DOMAIN, HELIX-
KEYWDS 2 TURN-HELIX, SENSORY TRANSDUCTION, PHOSPHORYLATION, TRANSCRIPTION
KEYWDS 3 REGULATION, DNA-BINDING, ACTIVATOR, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 5
AUTHOR C.LAGURI,M.K.PHILLIPS-JONES,M.P.WILLIAMSON
REVDAT 4 14-JUN-23 1UMQ 1 REMARK
REVDAT 3 15-JAN-20 1UMQ 1 REMARK
REVDAT 2 24-FEB-09 1UMQ 1 VERSN
REVDAT 1 21-NOV-03 1UMQ 0
JRNL AUTH C.LAGURI,M.K.PHILLIPS-JONES,M.P.WILLIAMSON
JRNL TITL SOLUTION STRUCTURE AND DNA BINDING OF THE EFFECTOR DOMAIN
JRNL TITL 2 FROM THE GLOBAL REGULATOR PRRA(REGA) FROM RHODOBACTER
JRNL TITL 3 SPHAEROIDES: INSIGHTS INTO DNA BINDING SPECIFICITY
JRNL REF NUCLEIC ACIDS RES. V. 31 6778 2003
JRNL REFN ISSN 0305-1048
JRNL PMID 14627811
JRNL DOI 10.1093/NAR/GKG891
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.2
REMARK 3 AUTHORS : LINGE ET AL 2003
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT IN EXPLICIT WATER AS
REMARK 3 DESCRIBED IN THE REFERENCE ABOVE
REMARK 4
REMARK 4 1UMQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1290013385.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 275
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 0.6
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 13C-15N EDITED NOESY;
REMARK 210 CBCA(CO)NH; HNCA; HNCACB; HNCO;
REMARK 210 HN(CA)CO; HCCH; CCH TOCSY; 15N
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA 1.2
REMARK 210 METHOD USED : DISTANCE AND DIHEDRAL RESTRAINTS
REMARK 210 (TALOS)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA : RANDOM
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED PRRA C-TERMINAL DOMAIN
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 400
REMARK 400 COMPOUND
REMARK 400 INVOLVED IN TRANSACTIVATING ANAEROBIC EXPRESSION OF THE
REMARK 400 PHOTOSYNTHETIC APPARATUS. IT IS A TRANSCRIPTIONAL REGULATOR THAT
REMARK 400 IS RESPONSIBLE FOR ACTIVATING EXPRESSION OF THE PUF, PUH, AND PUC
REMARK 400 OPERONS IN RESPONSE TO A DECREASE IN OXYGEN TENSION.
REMARK 400
REMARK 400 THIS ENTRY CORRESPONDS TO RESIDUES 125 THROUGH 184
REMARK 400 OF THE INTACT PROTEIN.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-5
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 14
REMARK 465 VAL A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 HIS A 20
REMARK 465 MET A 21
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 HG3 MET A 66 HB THR A 70 1.35
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 ALA A 23 177.70 61.69
REMARK 500 1 PRO A 29 119.84 -32.32
REMARK 500 1 ASN A 65 69.65 62.94
REMARK 500 1 PRO A 80 29.82 -77.80
REMARK 500 2 SER A 27 117.25 74.25
REMARK 500 2 PRO A 29 106.05 -30.18
REMARK 500 2 GLU A 33 -117.39 61.88
REMARK 500 2 SER A 37 142.84 71.47
REMARK 500 2 ASP A 54 80.76 67.05
REMARK 500 2 ARG A 78 97.03 -48.27
REMARK 500 2 PRO A 80 34.48 -71.94
REMARK 500 3 SER A 27 -37.18 -156.19
REMARK 500 3 LEU A 28 107.56 67.81
REMARK 500 3 PRO A 29 103.68 -26.90
REMARK 500 3 SER A 37 125.42 65.80
REMARK 500 3 ASP A 54 76.89 60.48
REMARK 500 3 PRO A 80 41.90 -70.25
REMARK 500 4 PRO A 29 111.09 -31.65
REMARK 500 4 PRO A 35 -37.52 -38.97
REMARK 500 4 ARG A 78 46.97 -79.34
REMARK 500 5 ALA A 23 -155.53 -80.90
REMARK 500 5 SER A 27 164.95 179.05
REMARK 500 5 PRO A 29 112.01 -30.10
REMARK 500 5 GLU A 33 -167.52 66.98
REMARK 500 5 PRO A 35 -39.28 -37.54
REMARK 500 5 ASP A 54 72.34 56.95
REMARK 500 5 ARG A 78 39.72 -77.97
REMARK 500 5 SER A 79 -54.35 -147.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5920 RELATED DB: BMRB
DBREF 1UMQ A 1 21 PDB 1UMQ 1UMQ 1 21
DBREF 1UMQ A 22 81 UNP Q53228 REGA_RHOSH 125 184
SEQRES 1 A 81 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 81 LEU VAL PRO ARG GLY SER HIS MET LEU ALA LYS GLY GLU
SEQRES 3 A 81 SER LEU PRO PRO PRO PRO GLU ASN PRO MET SER ALA ASP
SEQRES 4 A 81 ARG VAL ARG TRP GLU HIS ILE GLN ARG ILE TYR GLU MET
SEQRES 5 A 81 CYS ASP ARG ASN VAL SER GLU THR ALA ARG ARG LEU ASN
SEQRES 6 A 81 MET HIS ARG ARG THR LEU GLN ARG ILE LEU ALA LYS ARG
SEQRES 7 A 81 SER PRO ARG
HELIX 1 1 ALA A 38 CYS A 53 1 16
HELIX 2 2 VAL A 57 LEU A 64 1 8
HELIX 3 3 ARG A 68 LYS A 77 1 10
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 - 9 20 Bytes