Header list of 1mnt.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION REGULATION 28-JUN-94 1MNT
TITLE SOLUTION STRUCTURE OF DIMERIC MNT REPRESSOR (1-76)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MNT REPRESSOR;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE P22;
SOURCE 3 ORGANISM_TAXID: 10754
KEYWDS TRANSCRIPTION REGULATION
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR M.J.M.BURGERING,R.BOELENS,D.E.GILBERT,J.N.BREG,K.L.KNIGHT,R.T.SAUER,
AUTHOR 2 R.KAPTEIN
REVDAT 3 23-FEB-22 1MNT 1 REMARK
REVDAT 2 24-FEB-09 1MNT 1 VERSN
REVDAT 1 30-SEP-94 1MNT 0
JRNL AUTH M.J.BURGERING,R.BOELENS,D.E.GILBERT,J.N.BREG,K.L.KNIGHT,
JRNL AUTH 2 R.T.SAUER,R.KAPTEIN
JRNL TITL SOLUTION STRUCTURE OF DIMERIC MNT REPRESSOR (1-76).
JRNL REF BIOCHEMISTRY V. 33 15036 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 7999761
JRNL DOI 10.1021/BI00254A012
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.J.M.BURGERING,R.BOELENS,R.KAPTEIN
REMARK 1 TITL OBSERVATION OF INTER-SUBUNIT NOES IN A DIMERIC P22 MNT
REMARK 1 TITL 2 REPRESSOR MUTANT BY A TIME-SHARED [15N, 13C] DOUBLE HALF
REMARK 1 TITL 3 FILTER TECHNIQUE
REMARK 1 REF J.BIOMOL.NMR V. 3 709 1993
REMARK 1 REFN ISSN 0925-2738
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.N.BREG,J.H.J.VAN OPHEUSDEN,M.J.M.BURGERING,R.BOELENS,
REMARK 1 AUTH 2 R.KAPTEIN
REMARK 1 TITL STRUCTURE OF ARC REPRESSOR IN SOLUTION: EVIDENCE FOR A
REMARK 1 TITL 2 FAMILY OF B-SHEET DNA-BINDING PROTEIN
REMARK 1 REF NATURE V. 346 586 1990
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.L.KNIGHT,R.T.SAUER
REMARK 1 TITL THE MNT REPRESSOR OF BACTERIOPHAGE P22: ROLE OF THE
REMARK 1 TITL 2 C-TERMINAL RESIDUES IN OPERATOR BINDING AND TETRAMER
REMARK 1 TITL 3 FORMATION
REMARK 1 REF BIOCHEMISTRY V. 27 2088 1988
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MNT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175094.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 LYS A 67
REMARK 465 LYS A 68
REMARK 465 MET A 69
REMARK 465 VAL A 70
REMARK 465 PHE A 71
REMARK 465 ASP A 72
REMARK 465 THR A 73
REMARK 465 LEU A 74
REMARK 465 LYS A 75
REMARK 465 ASP A 76
REMARK 465 LYS B 67
REMARK 465 LYS B 68
REMARK 465 MET B 69
REMARK 465 VAL B 70
REMARK 465 PHE B 71
REMARK 465 ASP B 72
REMARK 465 THR B 73
REMARK 465 LEU B 74
REMARK 465 LYS B 75
REMARK 465 ASP B 76
DBREF 1MNT A 1 76 UNP P03049 RMNT_BPP22 1 76
DBREF 1MNT B 1 76 UNP P03049 RMNT_BPP22 1 76
SEQRES 1 A 76 ALA ARG ASP ASP PRO HIS PHE ASN PHE ARG MET PRO MET
SEQRES 2 A 76 GLU VAL ARG GLU LYS LEU LYS PHE ARG ALA GLU ALA ASN
SEQRES 3 A 76 GLY ARG SER MET ASN SER GLU LEU LEU GLN ILE VAL GLN
SEQRES 4 A 76 ASP ALA LEU SER LYS PRO SER PRO VAL THR GLY TYR ARG
SEQRES 5 A 76 ASN ASP ALA GLU ARG LEU ALA ASP GLU GLN SER GLU LEU
SEQRES 6 A 76 VAL LYS LYS MET VAL PHE ASP THR LEU LYS ASP
SEQRES 1 B 76 ALA ARG ASP ASP PRO HIS PHE ASN PHE ARG MET PRO MET
SEQRES 2 B 76 GLU VAL ARG GLU LYS LEU LYS PHE ARG ALA GLU ALA ASN
SEQRES 3 B 76 GLY ARG SER MET ASN SER GLU LEU LEU GLN ILE VAL GLN
SEQRES 4 B 76 ASP ALA LEU SER LYS PRO SER PRO VAL THR GLY TYR ARG
SEQRES 5 B 76 ASN ASP ALA GLU ARG LEU ALA ASP GLU GLN SER GLU LEU
SEQRES 6 B 76 VAL LYS LYS MET VAL PHE ASP THR LEU LYS ASP
HELIX 1 H1A MET A 13 ASN A 26 1ALPHA_HELIX 14
HELIX 2 H2A GLU A 33 LYS A 44 1ALPHA_HELIX 12
HELIX 3 H3A ASN A 53 VAL A 66 1ALPHA_HELIX 14
HELIX 4 H1B MET B 13 ASN B 26 1ALPHA_HELIX 14
HELIX 5 H2B GLU B 33 LYS B 44 1ALPHA_HELIX 12
HELIX 6 H3B ASN B 53 VAL B 66 1ALPHA_HELIX 14
SHEET 1 S1 2 PRO A 5 MET A 11 0
SHEET 2 S1 2 PRO B 5 MET B 11 1
CISPEP 1 GLU A 24 ALA A 25 1 24.54
CISPEP 2 VAL A 48 THR A 49 1 -12.95
CISPEP 3 GLY A 50 TYR A 51 1 -6.02
CISPEP 4 PHE B 9 ARG B 10 1 -9.78
CISPEP 5 VAL B 48 THR B 49 1 -2.92
CISPEP 6 PHE A 9 ARG A 10 2 -12.54
CISPEP 7 VAL A 48 THR A 49 2 5.02
CISPEP 8 ASN A 53 ASP A 54 2 12.77
CISPEP 9 ALA B 1 ARG B 2 2 -9.40
CISPEP 10 ASN B 53 ASP B 54 2 14.23
CISPEP 11 GLY A 50 TYR A 51 3 3.21
CISPEP 12 VAL B 48 THR B 49 3 2.37
CISPEP 13 ASN B 53 ASP B 54 3 -14.84
CISPEP 14 SER A 46 PRO A 47 4 -23.60
CISPEP 15 GLY A 50 TYR A 51 4 -10.29
CISPEP 16 ASP A 54 ALA A 55 4 9.21
CISPEP 17 ALA B 1 ARG B 2 4 -10.43
CISPEP 18 PHE B 9 ARG B 10 4 -11.42
CISPEP 19 ARG B 52 ASN B 53 4 -16.25
CISPEP 20 ASN B 53 ASP B 54 4 -6.14
CISPEP 21 ALA A 1 ARG A 2 5 -8.86
CISPEP 22 GLY A 50 TYR A 51 5 -3.78
CISPEP 23 PHE B 9 ARG B 10 5 -12.54
CISPEP 24 ARG B 52 ASN B 53 5 -12.28
CISPEP 25 PHE A 9 ARG A 10 6 -9.77
CISPEP 26 ARG A 52 ASN A 53 6 22.56
CISPEP 27 ASN A 53 ASP A 54 6 6.07
CISPEP 28 VAL B 48 THR B 49 6 11.84
CISPEP 29 GLY B 50 TYR B 51 6 -12.89
CISPEP 30 VAL A 48 THR A 49 7 18.54
CISPEP 31 ARG A 52 ASN A 53 7 -18.68
CISPEP 32 PHE B 9 ARG B 10 7 -19.16
CISPEP 33 VAL B 48 THR B 49 7 -12.25
CISPEP 34 GLY B 50 TYR B 51 7 4.62
CISPEP 35 ASP A 3 ASP A 4 8 27.77
CISPEP 36 VAL A 48 THR A 49 8 -14.66
CISPEP 37 ASN A 53 ASP A 54 8 -14.92
CISPEP 38 VAL B 48 THR B 49 8 -22.04
CISPEP 39 ARG B 52 ASN B 53 8 3.51
CISPEP 40 SER B 46 PRO B 47 9 -0.97
CISPEP 41 ALA B 55 GLU B 56 9 24.05
CISPEP 42 PHE A 9 ARG A 10 10 -17.65
CISPEP 43 LYS A 44 PRO A 45 10 -7.99
CISPEP 44 SER B 46 PRO B 47 11 -3.12
CISPEP 45 GLY B 50 TYR B 51 11 -16.19
CISPEP 46 ASN B 53 ASP B 54 11 12.37
CISPEP 47 ASN A 53 ASP A 54 12 3.66
CISPEP 48 VAL B 48 THR B 49 12 -13.35
CISPEP 49 GLY B 50 TYR B 51 13 22.03
CISPEP 50 SER B 46 PRO B 47 14 -8.00
CISPEP 51 GLY B 50 TYR B 51 14 0.08
CISPEP 52 GLY A 50 TYR A 51 15 -1.69
CISPEP 53 ASN A 53 ASP A 54 15 -2.09
CISPEP 54 ARG B 52 ASN B 53 15 16.80
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