Header list of 1qey.pdb file
Complete list - v 20 2 Bytes
HEADER GENE REGULATION 03-APR-99 1QEY
TITLE NMR STRUCTURE DETERMINATION OF THE TETRAMERIZATION DOMAIN OF THE MNT
TITLE 2 REPRESSOR: AN ASYMMETRIC A-HELICAL ASSEMBLY IN SLOW EXCHANGE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (REGULATORY PROTEIN MNT);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: C-TERMINAL TETRAMERIZATION DOMAIN;
COMPND 5 SYNONYM: MNT-C;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: CHYMOTRYPTIC FRAGMENT OF WILD-TYPE PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE P22;
SOURCE 3 ORGANISM_TAXID: 10754;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: X90;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PTM203-ST6
KEYWDS OLIGOMERIZATION, TRANSCRIPTIONAL CONTROL, P22 MNT REPRESSOR, GENE
KEYWDS 2 REGULATION
EXPDTA SOLUTION NMR
NUMMDL 27
AUTHOR I.M.A.NOOREN,A.V.E.GEORGE,R.KAPTEIN,R.T.SAUER,R.BOELENS
REVDAT 6 20-NOV-19 1QEY 1 JRNL REMARK
REVDAT 5 24-FEB-09 1QEY 1 VERSN
REVDAT 4 19-APR-00 1QEY 1 SOURCE REMARK
REVDAT 3 03-NOV-99 1QEY 1 COMPND JRNL REMARK
REVDAT 2 30-AUG-99 1QEY 1 REMARK
REVDAT 1 18-AUG-99 1QEY 0
JRNL AUTH I.M.NOOREN,R.KAPTEIN,R.T.SAUER,R.BOELENS
JRNL TITL THE TETRAMERIZATION DOMAIN OF THE MNT REPRESSOR CONSISTS OF
JRNL TITL 2 TWO RIGHT-HANDED COILED COILS.
JRNL REF NAT.STRUCT.BIOL. V. 6 755 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10426954
JRNL DOI 10.1038/11531
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.M.NOOREN,A.V.GEORGE,R.KAPTEIN,R.T.SAUER,R.BOELENS
REMARK 1 TITL NMR STRUCTURE DETERMINATION OF THE TETRAMERIZATION DOMAIN OF
REMARK 1 TITL 2 THE MNT REPRESSOR: AN ASYMMETRIC ALPHA-HELICAL ASSEMBLY IN
REMARK 1 TITL 3 SLOW EXCHANGE.
REMARK 1 REF J.BIOMOL.NMR V. 15 39 1999
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 20703962
REMARK 1 DOI 10.1023/A:1008312309535
REMARK 1 REFERENCE 2
REMARK 1 AUTH I.M.NOOREN,G.E.FOLKERS,R.KAPTEIN,R.T.SAUER,R.BOELENS
REMARK 1 TITL STRUCTURE AND DYNAMICS OF THE TETRAMERIC MNT REPRESSOR AND A
REMARK 1 TITL 2 MODEL FOR ITS DNA COMPLEX.
REMARK 1 REF J.BIOMOL.STRUCT.DYN. V.PL 1 113 2000
REMARK 1 REFN ESSN 1538-0254
REMARK 1 PMID 22607414
REMARK 1 DOI 10.1080/07391102.2000.10506611
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.D.WALDBURGER,R.T.SAUER
REMARK 1 TITL DOMAINS OF MNT REPRESSOR: ROLES IN TETRAMER FORMATION,
REMARK 1 TITL 2 PROTEIN STABILITY, AND OPERATOR DNA BINDING.
REMARK 1 REF BIOCHEMISTRY V. 34 13109 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 7548071
REMARK 1 DOI 10.1021/BI00040A023
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR V3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE LITERATURE
REMARK 4
REMARK 4 1QEY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000780.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : 50 MM KPI, 200 MM NACL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 27
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY, LEAST RESTRAINT
REMARK 210 VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 ASN B 53 175.37 177.73
REMARK 500 1 ASN D 53 175.48 177.82
REMARK 500 2 ASN A 53 54.58 -95.36
REMARK 500 2 THR A 73 -73.81 -68.39
REMARK 500 2 ASN C 53 54.52 -95.44
REMARK 500 2 THR C 73 -73.94 -68.47
REMARK 500 3 THR A 73 -71.64 -61.75
REMARK 500 3 THR C 73 -71.25 -61.90
REMARK 500 4 ASN A 53 74.48 59.33
REMARK 500 4 ASN C 53 73.96 59.57
REMARK 500 5 THR A 73 -72.44 -62.30
REMARK 500 5 THR A 81 -81.21 -56.40
REMARK 500 5 THR B 81 63.40 -68.37
REMARK 500 5 THR C 73 -72.46 -62.32
REMARK 500 5 THR C 81 -81.20 -56.22
REMARK 500 5 THR D 81 63.34 -68.37
REMARK 500 6 THR A 81 -79.89 -66.48
REMARK 500 6 LYS B 80 -71.01 -74.24
REMARK 500 6 THR C 81 -79.82 -66.51
REMARK 500 6 LYS D 80 -70.94 -74.30
REMARK 500 7 ASN A 53 92.25 62.40
REMARK 500 7 THR A 73 -71.11 -65.58
REMARK 500 7 THR A 81 -78.44 -50.83
REMARK 500 7 ASN C 53 92.34 62.37
REMARK 500 7 THR C 73 -71.09 -65.60
REMARK 500 7 THR C 81 -78.51 -51.05
REMARK 500 8 ASN A 53 88.69 -178.27
REMARK 500 8 THR A 73 -70.44 -64.88
REMARK 500 8 THR A 81 -78.22 -55.06
REMARK 500 8 ASN C 53 88.67 -178.37
REMARK 500 8 THR C 73 -70.58 -64.84
REMARK 500 8 THR C 81 -78.15 -55.06
REMARK 500 9 ASN A 53 104.95 60.38
REMARK 500 9 THR A 73 -70.24 -63.60
REMARK 500 9 ASN C 53 105.05 60.40
REMARK 500 9 THR C 73 -70.22 -63.63
REMARK 500 10 THR A 73 -70.68 -66.90
REMARK 500 10 THR B 81 44.35 -168.23
REMARK 500 10 THR C 73 -70.54 -66.92
REMARK 500 10 THR D 81 44.55 -168.28
REMARK 500 11 THR A 73 -71.45 -57.62
REMARK 500 11 THR C 73 -71.55 -57.74
REMARK 500 12 THR A 81 -77.66 -60.34
REMARK 500 12 THR B 81 64.56 -68.73
REMARK 500 12 THR C 81 -77.54 -60.57
REMARK 500 12 THR D 81 64.52 -68.58
REMARK 500 13 ASN A 53 88.52 -62.44
REMARK 500 13 THR A 73 -70.23 -60.65
REMARK 500 13 ASN C 53 88.55 -62.38
REMARK 500 13 THR C 73 -70.28 -60.83
REMARK 500
REMARK 500 THIS ENTRY HAS 118 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QEY A 52 82 UNP P03049 RMNT_BPP22 52 82
DBREF 1QEY B 52 82 UNP P03049 RMNT_BPP22 52 82
DBREF 1QEY C 52 82 UNP P03049 RMNT_BPP22 52 82
DBREF 1QEY D 52 82 UNP P03049 RMNT_BPP22 52 82
SEQRES 1 A 31 ARG ASN ASP ALA GLU ARG LEU ALA ASP GLU GLN SER GLU
SEQRES 2 A 31 LEU VAL LYS LYS MET VAL PHE ASP THR LEU LYS ASP LEU
SEQRES 3 A 31 TYR LYS LYS THR THR
SEQRES 1 B 31 ARG ASN ASP ALA GLU ARG LEU ALA ASP GLU GLN SER GLU
SEQRES 2 B 31 LEU VAL LYS LYS MET VAL PHE ASP THR LEU LYS ASP LEU
SEQRES 3 B 31 TYR LYS LYS THR THR
SEQRES 1 C 31 ARG ASN ASP ALA GLU ARG LEU ALA ASP GLU GLN SER GLU
SEQRES 2 C 31 LEU VAL LYS LYS MET VAL PHE ASP THR LEU LYS ASP LEU
SEQRES 3 C 31 TYR LYS LYS THR THR
SEQRES 1 D 31 ARG ASN ASP ALA GLU ARG LEU ALA ASP GLU GLN SER GLU
SEQRES 2 D 31 LEU VAL LYS LYS MET VAL PHE ASP THR LEU LYS ASP LEU
SEQRES 3 D 31 TYR LYS LYS THR THR
HELIX 1 1 ASP A 54 THR A 81 1 28
HELIX 2 2 ASP B 54 LYS B 80 1 27
HELIX 3 3 ASP C 54 THR C 81 1 28
HELIX 4 4 ASP D 54 LYS D 80 1 27
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 - v 20 2 Bytes