Header list of 2an7.pdb file
Complete list - g 9 2 Bytes
HEADER DNA BINDING PROTEIN 11-AUG-05 2AN7
TITLE SOLUTION STRUCTURE OF THE BACTERIAL ANTIDOTE PARD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN PARD;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: RK2-RP4
KEYWDS BACTERIAL ANTIDOTE, RIBBON-HELIX-HELIX, DNA-BINDING MOTIF, PLASMID
KEYWDS 2 ADDICTION, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR M.OBERER,K.ZANGGER,K.GRUBER,W.KELLER
REVDAT 4 14-JUN-23 2AN7 1 REMARK
REVDAT 3 26-FEB-20 2AN7 1 REMARK
REVDAT 2 24-FEB-09 2AN7 1 JRNL VERSN
REVDAT 1 05-SEP-06 2AN7 0
JRNL AUTH M.OBERER,K.ZANGGER,K.GRUBER,W.KELLER
JRNL TITL THE SOLUTION STRUCTURE OF PARD, THE ANTIDOTE OF THE PARDE
JRNL TITL 2 TOXIN ANTITOXIN MODULE, PROVIDES THE STRUCTURAL BASIS FOR
JRNL TITL 3 DNA AND TOXIN BINDING.
JRNL REF PROTEIN SCI. V. 16 1676 2007
JRNL REFN ISSN 0961-8368
JRNL PMID 17656583
JRNL DOI 10.1110/PS.062680707
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.OBERER,K.ZANGGER,S.PRYTULLA,W.KELLER
REMARK 1 TITL THE ANTI-TOXIN PARD OF PLASMID RK2 CONSISTS OF TWO
REMARK 1 TITL 2 STRUCTURALLY DISTINCT MOIETIES AND BELONGS TO THE
REMARK 1 TITL 3 RIBBON-HELIX-HELIX FAMILY OF DNA-BINDING PROTEINS
REMARK 1 REF BIOCHEM.J. V. 361 41 2002
REMARK 1 REFN ISSN 0264-6021
REMARK 1 PMID 11743881
REMARK 1 DOI 10.1042/0264-6021:3610041
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AN7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000034090.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 180MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6MM PARD U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER PH 6.0; 50MM
REMARK 210 KCL, 0.1% NAN3, 90% H2O, 10% D2O;
REMARK 210 0.6MM PARD U-15N; 20MM
REMARK 210 PHOSPHATE BUFFER PH 6.0; 50MM
REMARK 210 KCL, 0.1% NAN3, 90% H2O, 10% D2O;
REMARK 210 0.3MM PARD U-15N, 13C + 0.3MM
REMARK 210 PARD UNLABELED; 20MM PHOSPHATE
REMARK 210 BUFFER PH 6.0; 50MM KCL, 0.1%
REMARK 210 NAN3, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 13C,15N-EDITED,
REMARK 210 13C,15N-FILTERED NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1, NMRPIPE 2005, NMRVIEW
REMARK 210 4.6
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
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: 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: 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
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 52 -81.99 -92.35
REMARK 500 1 ASN A 58 120.14 62.89
REMARK 500 1 ALA A 62 -43.80 -176.05
REMARK 500 1 LYS A 64 131.87 64.49
REMARK 500 1 VAL A 65 35.21 -148.31
REMARK 500 1 SER A 66 121.64 62.28
REMARK 500 1 THR A 67 -45.27 -176.04
REMARK 500 1 GLU A 76 121.11 -177.39
REMARK 500 1 ASP A 81 -70.03 66.94
REMARK 500 1 ASN B 155 31.69 -152.07
REMARK 500 1 ASP B 159 63.24 -160.45
REMARK 500 1 LEU B 161 108.09 55.19
REMARK 500 1 ALA B 162 53.73 -166.77
REMARK 500 1 SER B 169 -72.42 -86.51
REMARK 500 1 GLU B 176 -38.89 -177.81
REMARK 500 1 ASP B 181 -68.94 68.37
REMARK 500 2 ALA A 62 -48.42 -175.72
REMARK 500 2 LYS A 64 -73.19 65.48
REMARK 500 2 VAL A 65 -96.36 -141.11
REMARK 500 2 SER A 66 51.22 -165.24
REMARK 500 2 THR A 67 -168.67 62.07
REMARK 500 2 LYS A 68 -79.54 -52.09
REMARK 500 2 SER A 69 -163.07 59.00
REMARK 500 2 VAL A 70 72.05 56.55
REMARK 500 2 ILE A 73 115.10 61.95
REMARK 500 2 GLU A 76 -169.76 -56.20
REMARK 500 2 GLU A 77 -163.35 -61.27
REMARK 500 2 SER A 79 -41.81 -169.68
REMARK 500 2 ASP A 81 80.57 48.31
REMARK 500 2 GLU B 148 -41.35 -147.66
REMARK 500 2 ARG B 156 174.31 59.26
REMARK 500 2 ASN B 158 87.96 -58.59
REMARK 500 2 ALA B 162 42.96 -176.84
REMARK 500 2 SER B 166 88.65 -58.19
REMARK 500 2 LYS B 168 85.92 61.07
REMARK 500 2 VAL B 170 156.88 59.17
REMARK 500 2 GLU B 176 107.79 -175.82
REMARK 500 2 LEU B 178 -70.20 66.58
REMARK 500 3 SER A 2 89.50 -59.92
REMARK 500 3 ALA A 40 12.88 -145.35
REMARK 500 3 ARG A 56 -165.00 41.04
REMARK 500 3 ILE A 57 69.39 -159.68
REMARK 500 3 LEU A 61 -71.16 62.67
REMARK 500 3 ALA A 62 37.13 -177.12
REMARK 500 3 LYS A 64 -69.46 67.55
REMARK 500 3 LYS A 68 118.92 62.98
REMARK 500 3 SER A 69 -57.20 -158.96
REMARK 500 3 VAL A 70 155.63 60.33
REMARK 500 3 ILE A 73 86.29 -159.61
REMARK 500 3 GLU A 76 101.81 59.40
REMARK 500
REMARK 500 THIS ENTRY HAS 597 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4792 RELATED DB: BMRB
DBREF 2AN7 A 1 83 UNP P22995 PARD4_ECOLI 1 83
DBREF 2AN7 B 101 183 UNP P22995 PARD4_ECOLI 1 83
SEQRES 1 A 83 MET SER ARG LEU THR ILE ASP MET THR ASP GLN GLN HIS
SEQRES 2 A 83 GLN SER LEU LYS ALA LEU ALA ALA LEU GLN GLY LYS THR
SEQRES 3 A 83 ILE LYS GLN TYR ALA LEU GLU ARG LEU PHE PRO GLY ASP
SEQRES 4 A 83 ALA ASP ALA ASP GLN ALA TRP GLN GLU LEU LYS THR MET
SEQRES 5 A 83 LEU GLY ASN ARG ILE ASN ASP GLY LEU ALA GLY LYS VAL
SEQRES 6 A 83 SER THR LYS SER VAL GLY GLU ILE LEU ASP GLU GLU LEU
SEQRES 7 A 83 SER GLY ASP ARG ALA
SEQRES 1 B 83 MET SER ARG LEU THR ILE ASP MET THR ASP GLN GLN HIS
SEQRES 2 B 83 GLN SER LEU LYS ALA LEU ALA ALA LEU GLN GLY LYS THR
SEQRES 3 B 83 ILE LYS GLN TYR ALA LEU GLU ARG LEU PHE PRO GLY ASP
SEQRES 4 B 83 ALA ASP ALA ASP GLN ALA TRP GLN GLU LEU LYS THR MET
SEQRES 5 B 83 LEU GLY ASN ARG ILE ASN ASP GLY LEU ALA GLY LYS VAL
SEQRES 6 B 83 SER THR LYS SER VAL GLY GLU ILE LEU ASP GLU GLU LEU
SEQRES 7 B 83 SER GLY ASP ARG ALA
HELIX 1 1 THR A 9 GLY A 24 1 16
HELIX 2 2 THR A 26 LEU A 35 1 10
HELIX 3 3 ASP A 41 LEU A 53 1 13
HELIX 4 4 THR B 109 GLY B 124 1 16
HELIX 5 5 THR B 126 PHE B 136 1 11
HELIX 6 6 ASP B 141 LYS B 150 1 10
SHEET 1 A 2 SER A 2 MET A 8 0
SHEET 2 A 2 SER B 102 MET B 108 -1 O ILE B 106 N LEU A 4
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 - g 9 2 Bytes