Header list of 1p94.pdb file
Complete list - b 23 2 Bytes
HEADER CELL CYCLE 09-MAY-03 1P94
TITLE NMR STRUCTURE OF PARG SYMMETRIC DIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMID PARTITION PROTEIN PARG;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA;
SOURCE 3 ORGANISM_TAXID: 28901;
SOURCE 4 GENE: PARG;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-22-B(+)
KEYWDS RIBBON-HELIX-HELIX, DIMER, DNA BINDING, CELL CYCLE
EXPDTA SOLUTION NMR
NUMMDL 11
MDLTYP MINIMIZED AVERAGE
AUTHOR A.P.GOLOVANOV,D.BARILLA,M.GOLOVANOVA,F.HAYES,L.Y.LIAN
REVDAT 3 23-FEB-22 1P94 1 REMARK
REVDAT 2 24-FEB-09 1P94 1 VERSN
REVDAT 1 13-JAN-04 1P94 0
JRNL AUTH A.P.GOLOVANOV,D.BARILLA,M.GOLOVANOVA,F.HAYES,L.Y.LIAN
JRNL TITL PARG, A PROTEIN REQUIRED FOR ACTIVE PARTITION OF BACTERIAL
JRNL TITL 2 PLASMIDS, HAS A DIMERIC RIBBON-HELIX-HELIX STRUCTURE.
JRNL REF MOL.MICROBIOL. V. 50 1141 2003
JRNL REFN ISSN 0950-382X
JRNL PMID 14622405
JRNL DOI 10.1046/J.1365-2958.2003.03750.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.HAYES
REMARK 1 TITL THE PARTITION SYSTEM OF MULTIDRUG RESISTANCE PLASMID TP228
REMARK 1 TITL 2 INCLUDES A NOVEL PROTEIN THAT EPITOMIZES AN EVOLUTIONARILY
REMARK 1 TITL 3 DISTINCT SUBGROUP OF THE PARA SUPERFAMILY
REMARK 1 REF MOL.MICROBIOL. V. 37 528 2000
REMARK 1 REFN ISSN 0950-382X
REMARK 1 DOI 10.1046/J.1365-2958.2000.02030.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, CNS 1.0
REMARK 3 AUTHORS : DELAGLIO ET AL. (NMRPIPE), BRUNGER ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE PARG STRUCTURE IS BASED ON 2230 AMBIGUOUS NOE RESTRAINTS, 82
REMARK 3 HYDROGEN BOND RESTRAINTS, AND 144 CSI-BASED DIHEDRAL ANGLE
REMARK 3 RESTRAINTS.
REMARK 3 N-TERMINAL REGION OF PARG (1-32) IS UNSTRUCTURED. THE C-TERMINAL
REMARK 3 REGION (33-76) IS STRUCTURED.
REMARK 4
REMARK 4 1P94 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019162.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 150 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM PARG U-15N,13C; 100 MM
REMARK 210 NACL, 50 MM PHOSPHATE BUFFER, 1
REMARK 210 MM DTT; 90% H2O, 10% D2O; 1 MM
REMARK 210 PARG U-15N; 100 MM NACL, 50 MM
REMARK 210 PHOSPHATE BUFFER, 1 MM DTT; 100%
REMARK 210 D2O; 1 MM PARG U-15N; 100 MM
REMARK 210 NACL, 50 MM PHOSPHATE BUFFER, 1
REMARK 210 MM DTT; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.01, ARIA 1.1, CNS 1.0
REMARK 210 METHOD USED : ARIA PROTOCOL (NILGES, M. ET
REMARK 210 AL., (1997) J. MOL. BIOL. 269,
REMARK 210 408-422) WAS USED TO DEAL WITH
REMARK 210 AMBIGUOUS DISTANCE RESTRAINTS
REMARK 210 AND FOR SOME NOE ASSIGNMENTS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY,TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: BEST REPRESENTATIVE CONFORMER (MODEL 1) IN THIS ENSEMBLE
REMARK 210 WAS OBTAINED BY ENERGY MINIMIZATION OF THE AVERAGE
REMARK 210 STRUCTURE, CALCULATED FOR MODELS 2-11
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 HD2 LYS A 11 H MET A 13 1.34
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 7 45.26 -103.25
REMARK 500 1 VAL A 10 -74.36 -40.12
REMARK 500 1 LYS A 12 8.21 145.99
REMARK 500 1 MET A 13 15.63 54.66
REMARK 500 1 THR A 14 27.04 45.59
REMARK 500 1 GLU A 22 73.62 54.23
REMARK 500 1 THR A 26 78.92 -63.81
REMARK 500 1 ALA A 27 155.74 -47.39
REMARK 500 1 VAL A 29 -55.55 73.85
REMARK 500 1 VAL A 37 -37.47 -146.47
REMARK 500 1 ASN A 38 103.97 57.48
REMARK 500 1 LEU B 3 35.69 -85.21
REMARK 500 1 GLU B 4 -25.14 61.07
REMARK 500 1 LYS B 5 -13.86 65.63
REMARK 500 1 VAL B 10 57.54 76.98
REMARK 500 1 LYS B 11 88.33 52.31
REMARK 500 1 LYS B 12 35.80 38.73
REMARK 500 1 MET B 13 89.65 48.03
REMARK 500 1 GLU B 22 37.85 31.99
REMARK 500 1 ARG B 23 35.91 -77.06
REMARK 500 1 VAL B 25 55.64 26.89
REMARK 500 1 THR B 26 -32.83 -39.30
REMARK 500 1 ALA B 27 69.93 12.94
REMARK 500 1 PRO B 28 80.90 -29.01
REMARK 500 2 SER A 2 -75.41 70.06
REMARK 500 2 SER A 9 -147.16 56.17
REMARK 500 2 SER A 31 72.73 57.40
REMARK 500 2 LYS A 33 59.54 -115.57
REMARK 500 2 ALA B 6 -169.58 69.43
REMARK 500 2 HIS B 7 143.33 -170.38
REMARK 500 2 SER B 9 115.16 62.90
REMARK 500 2 PRO B 28 -168.17 -75.08
REMARK 500 2 SER B 31 -138.97 52.78
REMARK 500 3 HIS A 7 52.35 -141.26
REMARK 500 3 MET A 13 58.26 -100.86
REMARK 500 3 LEU A 21 36.10 -149.41
REMARK 500 3 MET B 13 38.03 -95.60
REMARK 500 3 ARG B 19 80.18 55.42
REMARK 500 4 SER A 2 48.09 -75.25
REMARK 500 4 LEU A 3 -84.19 -154.83
REMARK 500 4 LYS A 5 -156.35 -121.71
REMARK 500 4 LYS A 11 -163.83 -124.79
REMARK 500 4 LEU B 3 -70.98 -70.93
REMARK 500 4 HIS B 7 40.31 70.65
REMARK 500 5 SER A 2 36.14 -145.90
REMARK 500 5 LYS A 5 96.83 67.10
REMARK 500 5 LYS A 11 -74.80 73.28
REMARK 500 5 GLU A 17 72.33 55.32
REMARK 500 5 LEU A 21 28.85 -152.27
REMARK 500 5 LYS B 5 93.24 66.82
REMARK 500
REMARK 500 THIS ENTRY HAS 96 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5563 RELATED DB: BMRB
REMARK 900 NMR SIGNAL ASSIGNMENTS, EXPERIMENTAL CONDITIONS
DBREF 1P94 A 1 76 UNP Q9KJ82 Q9KJ82_SALNE 1 76
DBREF 1P94 B 1 76 UNP Q9KJ82 Q9KJ82_SALNE 1 76
SEQRES 1 A 76 MET SER LEU GLU LYS ALA HIS THR SER VAL LYS LYS MET
SEQRES 2 A 76 THR PHE GLY GLU ASN ARG ASP LEU GLU ARG VAL VAL THR
SEQRES 3 A 76 ALA PRO VAL SER SER GLY LYS ILE LYS ARG VAL ASN VAL
SEQRES 4 A 76 ASN PHE ASP GLU GLU LYS HIS THR ARG PHE LYS ALA ALA
SEQRES 5 A 76 CYS ALA ARG LYS GLY THR SER ILE THR ASP VAL VAL ASN
SEQRES 6 A 76 GLN LEU VAL ASP ASN TRP LEU LYS GLU ASN GLU
SEQRES 1 B 76 MET SER LEU GLU LYS ALA HIS THR SER VAL LYS LYS MET
SEQRES 2 B 76 THR PHE GLY GLU ASN ARG ASP LEU GLU ARG VAL VAL THR
SEQRES 3 B 76 ALA PRO VAL SER SER GLY LYS ILE LYS ARG VAL ASN VAL
SEQRES 4 B 76 ASN PHE ASP GLU GLU LYS HIS THR ARG PHE LYS ALA ALA
SEQRES 5 B 76 CYS ALA ARG LYS GLY THR SER ILE THR ASP VAL VAL ASN
SEQRES 6 B 76 GLN LEU VAL ASP ASN TRP LEU LYS GLU ASN GLU
HELIX 1 1 GLU A 43 GLY A 57 1 15
HELIX 2 2 SER A 59 ASN A 75 1 17
HELIX 3 3 GLU B 43 GLY B 57 1 15
HELIX 4 4 SER B 59 ASN B 75 1 17
SHEET 1 A 2 ILE A 34 ASP A 42 0
SHEET 2 A 2 ILE B 34 ASP B 42 -1 O PHE B 41 N LYS A 35
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