Header list of 2adn.pdb file
Complete list - 10 20 Bytes
HEADER DNA BINDING PROTEIN 20-JUL-05 2ADN
TITLE SOLUTION STRUCTURE OF THE BACTERIAL ANTITOXIN CCDA: IMPLICATIONS FOR
TITLE 2 DNA AND TOXIN BINDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CCDA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CCDA CONFORMER B, LETA CONFORMER B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SG22622;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PKK-/CCDAR70K/
KEYWDS RIBBON-HELIX-HELIX, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR T.MADL,L.VANMELDEREN,M.OBERER,W.KELLER,L.KHATAI,K.ZANGGER
REVDAT 4 10-NOV-21 2ADN 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2ADN 1 VERSN
REVDAT 2 10-APR-07 2ADN 1 JRNL
REVDAT 1 22-AUG-06 2ADN 0
JRNL AUTH T.MADL,L.VAN MELDEREN,N.MINE,M.RESPONDEK,M.OBERER,W.KELLER,
JRNL AUTH 2 L.KHATAI,K.ZANGGER
JRNL TITL STRUCTURAL BASIS FOR NUCLEIC ACID AND TOXIN RECOGNITION OF
JRNL TITL 2 THE BACTERIAL ANTITOXIN CCDA
JRNL REF J.MOL.BIOL. V. 364 170 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 17007877
JRNL DOI 10.1016/J.JMB.2006.08.082
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER (CNS),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ADN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033770.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM CCDA U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER; 0.5MM CCDA U-
REMARK 210 15N,13C; 20MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 2D NOESY
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 : NMRPIPE, VNMR, NMRVIEW
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 O ILE B 124 H VAL B 128 1.43
REMARK 500 O ILE A 24 H VAL A 28 1.55
REMARK 500 O ASP B 121 H ASN B 123 1.57
REMARK 500 O ASP A 21 H ASN A 23 1.57
REMARK 500 O LEU A 27 H THR A 31 1.59
REMARK 500 O MET A 32 H ALA A 36 1.60
REMARK 500 O MET B 132 H ALA B 136 1.60
REMARK 500 O MET B 132 N ALA B 136 2.14
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 THR A 8 94.84 -65.82
REMARK 500 VAL A 9 -120.73 -84.32
REMARK 500 ASP A 10 -32.74 75.27
REMARK 500 ASP A 21 62.78 168.25
REMARK 500 VAL A 22 69.62 -59.67
REMARK 500 ARG A 40 44.79 -167.30
REMARK 500 ALA A 41 -73.82 66.90
REMARK 500 LYS A 45 -74.75 -169.60
REMARK 500 VAL A 46 -69.70 67.01
REMARK 500 GLU A 47 111.11 -160.54
REMARK 500 GLN A 49 109.24 -179.34
REMARK 500 MET A 52 -77.15 63.76
REMARK 500 GLU A 54 -89.81 -131.42
REMARK 500 VAL A 55 25.62 -157.09
REMARK 500 ALA A 56 -71.84 -172.19
REMARK 500 ARG A 57 124.70 157.95
REMARK 500 PHE A 58 -99.46 -133.90
REMARK 500 ILE A 59 159.25 58.96
REMARK 500 ALA A 66 -108.60 -71.62
REMARK 500 ASP A 67 40.12 173.61
REMARK 500 LYS A 70 179.41 61.68
REMARK 500 THR B 108 91.25 -55.84
REMARK 500 VAL B 109 -108.79 -82.40
REMARK 500 ASP B 110 -41.44 73.44
REMARK 500 ASP B 121 62.37 169.78
REMARK 500 VAL B 122 69.43 -63.24
REMARK 500 ILE B 124 -33.71 -132.72
REMARK 500 LEU B 139 68.60 29.64
REMARK 500 ARG B 140 55.82 -151.33
REMARK 500 ALA B 141 -165.99 -56.64
REMARK 500 TRP B 144 79.29 -169.87
REMARK 500 GLU B 147 -72.97 -98.85
REMARK 500 MET B 152 93.31 -172.11
REMARK 500 GLU B 154 -95.81 -136.25
REMARK 500 VAL B 155 94.97 142.84
REMARK 500 ALA B 156 -65.84 -172.91
REMARK 500 ARG B 157 133.00 -177.18
REMARK 500 PHE B 158 71.30 -163.49
REMARK 500 SER B 164 -59.88 -168.71
REMARK 500 ALA B 166 -72.09 66.42
REMARK 500 ASP B 167 -40.48 -179.76
REMARK 500 GLU B 168 37.58 -147.68
REMARK 500 ASP B 171 -68.34 -133.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ADL RELATED DB: PDB
REMARK 900 CCDA CONFORMER A
DBREF 2ADN A 1 72 UNP Q9S0Z5 Q9S0Z5_ECOLI 1 72
DBREF 2ADN B 101 172 UNP Q9S0Z5 Q9S0Z5_ECOLI 1 72
SEQADV 2ADN LYS A 70 UNP Q9S0Z5 ARG 70 ENGINEERED MUTATION
SEQADV 2ADN LYS B 170 UNP Q9S0Z5 ARG 70 ENGINEERED MUTATION
SEQRES 1 A 72 MET LYS GLN ARG ILE THR VAL THR VAL ASP SER ASP SER
SEQRES 2 A 72 TYR GLN LEU LEU LYS ALA TYR ASP VAL ASN ILE SER GLY
SEQRES 3 A 72 LEU VAL SER THR THR MET GLN ASN GLU ALA ARG ARG LEU
SEQRES 4 A 72 ARG ALA GLU ARG TRP LYS VAL GLU ASN GLN GLU GLY MET
SEQRES 5 A 72 VAL GLU VAL ALA ARG PHE ILE GLU MET ASN GLY SER PHE
SEQRES 6 A 72 ALA ASP GLU ASN LYS ASP TRP
SEQRES 1 B 72 MET LYS GLN ARG ILE THR VAL THR VAL ASP SER ASP SER
SEQRES 2 B 72 TYR GLN LEU LEU LYS ALA TYR ASP VAL ASN ILE SER GLY
SEQRES 3 B 72 LEU VAL SER THR THR MET GLN ASN GLU ALA ARG ARG LEU
SEQRES 4 B 72 ARG ALA GLU ARG TRP LYS VAL GLU ASN GLN GLU GLY MET
SEQRES 5 B 72 VAL GLU VAL ALA ARG PHE ILE GLU MET ASN GLY SER PHE
SEQRES 6 B 72 ALA ASP GLU ASN LYS ASP TRP
HELIX 1 1 SER A 13 TYR A 20 1 8
HELIX 2 2 ILE A 24 ARG A 38 1 15
HELIX 3 3 SER B 113 ALA B 119 1 7
HELIX 4 4 ILE B 124 ARG B 138 1 15
SHEET 1 A 2 ARG A 4 VAL A 9 0
SHEET 2 A 2 GLN B 103 THR B 108 -1 O VAL B 107 N ILE A 5
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
Complete list - 10 20 Bytes