Header list of 1ev0.pdb file
Complete list - b 16 2 Bytes
HEADER CELL CYCLE 19-APR-00 1EV0
TITLE SOLUTION STRUCTURE OF THE MINE TOPOLOGICAL SPECIFICITY DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MINE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: MINE TOPOLOGICAL SPECIFICITY DOMAIN;
COMPND 5 SYNONYM: CELL DIVISION TOPOLOGICAL SPECIFICITY FACTOR;
COMPND 6 ENGINEERED: 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_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS MINE, TOPOLOGICAL SPECIFICITY, CELL DIVISION, MINCD, MINICELL, CELL
KEYWDS 2 CYCLE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.F.KING,M.W.MACIEJEWSKI,B.PAN,G.P.MULLEN
REVDAT 4 16-FEB-22 1EV0 1 REMARK
REVDAT 3 24-FEB-09 1EV0 1 VERSN
REVDAT 2 01-APR-03 1EV0 1 JRNL
REVDAT 1 01-NOV-00 1EV0 0
JRNL AUTH G.F.KING,Y.L.SHIH,M.W.MACIEJEWSKI,N.P.BAINS,B.PAN,
JRNL AUTH 2 S.L.ROWLAND,G.P.MULLEN,L.I.ROTHFIELD
JRNL TITL STRUCTURAL BASIS FOR THE TOPOLOGICAL SPECIFICITY FUNCTION OF
JRNL TITL 2 MINE.
JRNL REF NAT.STRUCT.BIOL. V. 7 1013 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 11062554
JRNL DOI 10.1038/80917
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.A.J.DE BOER,R.E.CROSSLEY,L.I.ROTHFIELD
REMARK 1 TITL A DIVISION INHIBITOR AND A TOPOLOGICAL SPECIFICITY FACTOR
REMARK 1 TITL 2 CODED FOR BY THE MINICELL LOCUS DETERMINE PROPER PLACEMENT
REMARK 1 TITL 3 OF THE DIVISION SEPTUM IN E. COLI
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 56 641 1989
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.R.ZHAO,P.A.J.DE BOER,L.I.ROTHFIELD
REMARK 1 TITL PROPER PLACEMENT OF THE ESCHERICHIA COLI DIVISION SITE
REMARK 1 TITL 2 REQUIRES TWO FUNCTIONS THAT ARE ASSOCIATED WITH DIFFERENT
REMARK 1 TITL 3 DOMAINS OF THE MINE PROTEIN
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 92 4313 1995
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.M.RASKIN,P.A.J.DE BOER
REMARK 1 TITL THE MINE RING: AN FTSZ-INDEPENDENT CELL STRUCTURE REQUIRED
REMARK 1 TITL 2 FOR SELECTION OF THE CORRECT DIVISION SITE IN E. COLI
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 91 685 1997
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.F.KING,S.L.ROWLAND,B.PAN,J.P.MACKAY,G.P.MULLEN,
REMARK 1 AUTH 2 L.I.ROTHFIELD
REMARK 1 TITL THE DIMERIZATION AND TOPOLOGICAL SPECIFICITY FUNCTIONS OF
REMARK 1 TITL 2 MINE RESIDE IN A STRUCTURALLY AUTONOMOUS C-TERMINAL DOMAIN
REMARK 1 REF MOL.MICROBIOL. V. 31 1161 1999
REMARK 1 REFN ISSN 0950-382X
REMARK 1 DOI 10.1046/J.1365-2958.1999.01256.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97.0, X-PLOR 3.851
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS (FELIX), AXEL BRUNGER (X
REMARK 3 -PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 900 STRUCTURES WERE CALCULATED USING
REMARK 3 TORSION ANGLE DYNAMICS (DYANA).
REMARK 3 THE BEST 60 STRUCTURES WERE THEN
REMARK 3 REFINED USING DYNAMICAL SIMULATED
REMARK 3 ANNEALING IN X-PLOR.
REMARK 4
REMARK 4 1EV0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010916.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.7
REMARK 210 IONIC STRENGTH : 0.075
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3.0 MM U-15N,13C MINE; 20 MM
REMARK 210 SODIUM PHOSPHATE; 50 MM NACL; 15
REMARK 210 MM DTT; 1 MM EDTA; 0.02% SODIUM
REMARK 210 AZIDE; 1 MM 4-(2-AMINOETHYL)
REMARK 210 BENZENESULFONYL FLUORIDE; PH 5.7;
REMARK 210 3.5 MM U-15N MINE; 20 MM SODIUM
REMARK 210 PHOSPHATE; 50 MM NACL; 15 MM DTT;
REMARK 210 1 MM EDTA; 0.02% SODIUM AZIDE;
REMARK 210 1 MM 4-(2-AMINOETHYL)
REMARK 210 BENZENESULFONYL FLUORIDE; PH 5.7;
REMARK 210 2.13 MM UNLABELED MINE; 2.06 MM
REMARK 210 U-15N,13C MINE; 20 MM SODIUM
REMARK 210 PHOSPHATE; 50 MM NACL; 15 MM DTT;
REMARK 210 1.5 MM EDTA; 0.02% SODIUM AZIDE;
REMARK 210 0.2 MM PMSF; PH 5.7; 3.0 MM U-
REMARK 210 15N,13C MINE; 20 MM SODIUM
REMARK 210 PHOSPHATE; 50 MM NACL; 15 MM DTT;
REMARK 210 1.5 MM EDTA; 0.02% SODIUM AZIDE;
REMARK 210 0.2 MM PMSF; PH 5.7
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_HNHA
REMARK 210 AND 3D_HNHB; 2D HMQC-J; 3D_15N-
REMARK 210 SEPARATED_TOCSY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 3D_CBCA(CO)NH
REMARK 210 AND 3D_HNCACB; 3D HNCO; 3D HCCH-
REMARK 210 TOCSY; 3D_C(CO)NH_TOCSY AND 3D_
REMARK 210 HC(CO)NH_TOCSY; 13C AND 15N 3D_
REMARK 210 EDITED/FILTERED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED
REMARK 210 BY DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY AND LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 NMR SPECTROSCOPY. INTERMONOMER NOES
REMARK 210 WERE DETERMINED USING A HETEROLABELED
REMARK 210 PROTEIN SAMPLE.
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: 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 VAL A 54 -138.47 -150.49
REMARK 500 1 GLN A 55 106.85 -170.96
REMARK 500 1 ILE A 74 88.14 -150.02
REMARK 500 1 GLU A 83 -170.37 -61.11
REMARK 500 1 ALA A 84 139.67 -177.50
REMARK 500 1 GLU A 85 -39.67 -176.79
REMARK 500 1 VAL B 54 -138.45 -150.47
REMARK 500 1 GLN B 55 106.87 -170.97
REMARK 500 1 ILE B 74 88.13 -150.05
REMARK 500 1 GLU B 83 -170.36 -61.15
REMARK 500 1 ALA B 84 139.70 -177.49
REMARK 500 1 GLU B 85 -39.63 -176.82
REMARK 500 2 HIS A 37 -4.54 77.13
REMARK 500 2 VAL A 54 -138.51 -151.17
REMARK 500 2 GLN A 55 107.22 -170.62
REMARK 500 2 GLU A 83 -168.91 -60.72
REMARK 500 2 ALA A 84 -171.09 -171.56
REMARK 500 2 GLU A 86 67.69 60.06
REMARK 500 2 HIS B 37 -4.42 77.01
REMARK 500 2 VAL B 54 -138.55 -151.11
REMARK 500 2 GLN B 55 107.20 -170.59
REMARK 500 2 GLU B 83 -168.89 -60.73
REMARK 500 2 ALA B 84 -171.08 -171.54
REMARK 500 3 HIS A 37 -1.44 76.04
REMARK 500 3 VAL A 54 -138.14 -150.73
REMARK 500 3 GLN A 55 108.50 -173.31
REMARK 500 3 GLU A 85 -61.40 -173.62
REMARK 500 3 GLU A 86 39.19 -177.20
REMARK 500 3 HIS B 37 -1.44 76.07
REMARK 500 3 VAL B 54 -138.25 -150.73
REMARK 500 3 GLN B 55 108.49 -173.19
REMARK 500 3 GLU B 85 -61.52 -173.62
REMARK 500 3 GLU B 86 39.16 -177.15
REMARK 500 4 VAL A 54 -138.28 -151.09
REMARK 500 4 GLN A 55 109.28 -172.45
REMARK 500 4 GLU A 83 -169.15 -60.13
REMARK 500 4 GLU A 85 75.31 -176.27
REMARK 500 4 GLU A 86 34.25 -172.01
REMARK 500 4 VAL B 54 -138.38 -151.08
REMARK 500 4 GLN B 55 109.29 -172.37
REMARK 500 4 GLU B 83 -169.10 -60.21
REMARK 500 4 GLU B 85 75.29 -176.13
REMARK 500 4 GLU B 86 34.36 -172.08
REMARK 500 5 VAL A 54 -138.48 -151.41
REMARK 500 5 GLN A 55 107.39 -170.05
REMARK 500 5 LEU A 75 102.61 -160.60
REMARK 500 5 ALA A 84 118.64 179.95
REMARK 500 5 GLU A 85 43.38 -177.07
REMARK 500 5 VAL B 54 -138.50 -151.41
REMARK 500 5 GLN B 55 107.41 -170.05
REMARK 500
REMARK 500 THIS ENTRY HAS 221 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EV0 A 31 88 UNP P0A734 MINE_ECOLI 31 88
DBREF 1EV0 B 31 88 UNP P0A734 MINE_ECOLI 31 88
SEQRES 1 A 58 ARG SER ASP ALA GLU PRO HIS TYR LEU PRO GLN LEU ARG
SEQRES 2 A 58 LYS ASP ILE LEU GLU VAL ILE CYS LYS TYR VAL GLN ILE
SEQRES 3 A 58 ASP PRO GLU MET VAL THR VAL GLN LEU GLU GLN LYS ASP
SEQRES 4 A 58 GLY ASP ILE SER ILE LEU GLU LEU ASN VAL THR LEU PRO
SEQRES 5 A 58 GLU ALA GLU GLU LEU LYS
SEQRES 1 B 58 ARG SER ASP ALA GLU PRO HIS TYR LEU PRO GLN LEU ARG
SEQRES 2 B 58 LYS ASP ILE LEU GLU VAL ILE CYS LYS TYR VAL GLN ILE
SEQRES 3 B 58 ASP PRO GLU MET VAL THR VAL GLN LEU GLU GLN LYS ASP
SEQRES 4 B 58 GLY ASP ILE SER ILE LEU GLU LEU ASN VAL THR LEU PRO
SEQRES 5 B 58 GLU ALA GLU GLU LEU LYS
HELIX 1 1 ARG A 31 GLU A 35 5 5
HELIX 2 2 TYR A 38 VAL A 54 1 17
HELIX 3 3 ASP A 57 GLU A 59 5 3
HELIX 4 4 ARG B 31 GLU B 35 5 5
HELIX 5 5 TYR B 38 VAL B 54 1 17
HELIX 6 6 ASP B 57 GLU B 59 5 3
SHEET 1 A 4 VAL A 61 LYS A 68 0
SHEET 2 A 4 ILE A 72 LEU A 81 -1 O ILE A 72 N LYS A 68
SHEET 3 A 4 ILE B 72 LEU B 81 -1 N SER B 73 O LEU A 81
SHEET 4 A 4 VAL B 61 LYS B 68 -1 N THR B 62 O ASN B 78
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 16 2 Bytes