BMRB Entry 4355

Title:
Backbone 1H, 13C, 15N Chemical Shift Assignments for the Asymmetric Strands of the Tetramerization Domain of the Mnt Repressor   PubMed: 10426954
Deposition date:
1999-06-13
Original release date:
1999-10-07
Authors:
Nooren, Irene; Kaptein, Robert; Sauer, Robert; Boelens, Rolf
Citation:

Citation: Nooren, Irene; Kaptein, Robert; Sauer, Robert; Boelens, Rolf. "The Tetramerization Domain of the Mnt Repressor Consists of two Right-handed Coiled Coils"  Nat. Struct. Biol. 6, 755-759 (1999).

Assembly members:

Assembly members:
homotetrameric peptide, polymer, 37 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Bacteriophage P22   Taxonomy ID: 10754   Superkingdom: Viruses   Kingdom: not available   Genus/species: not available Bacteriophage P22

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTM203-st6

Experimental source:

Natural source:   Common Name: Bacteriophage P22   Taxonomy ID: 10754   Superkingdom: Viruses   Kingdom: not available   Genus/species: not available Bacteriophage P22

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTM203-st6

Entity Sequences (FASTA):

Entity Sequences (FASTA):
homotetrameric peptide: RNDAERLADEQSELVKKMVF DTLKDLYKKTTHHHHHH

Data sets:
Data typeCount
13C chemical shifts266
15N chemical shifts68
1H chemical shifts463

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Mnt-C subunit A1
2Mnt-C subunit B1
3Mnt-C subunit C1
4Mnt-C subunit D1

Entities:

Entity 1, Mnt-C subunit A 37 residues - Formula weight is not available

1   ARGASNASPALAGLUARGLEUALAASPGLU
2   GLNSERGLULEUVALLYSLYSMETVALPHE
3   ASPTHRLEULYSASPLEUTYRLYSLYSTHR
4   THRHISHISHISHISHISHIS

Samples:

15N_labelled: homotetrameric peptide, [U-95% 15N], 3.0 mM

13C_15N_labelled: homotetrameric peptide, [U-95% 13C; U-95% 15N], 3.0 mM

10%_13C_labelled: homotetrameric peptide, [U-10% 13C], 3.0 mM

unlabelled_labelled_mixture: homotetrameric peptide, [50/50 U-95% 13C; U-95% 15N / unlabelled], 3.0 mM

conditions_1: ionic strength: 0.20 M; pH: 5.2; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D (1H,15N)-HSQCnot availablenot availablenot available
2D (1H,1H) NOESYnot availablenot availablenot available
3D TOCSY (15N,1H) HSQCnot availablenot availablenot available
3D NOESY (15N,1H) HSQCnot availablenot availablenot available
3D HNCOnot availablenot availablenot available
3D HNCAnot availablenot availablenot available
3D HN(CO)CAnot availablenot availablenot available
3D HNHAnot availablenot availablenot available
3D HCACOnot availablenot availablenot available
3D TOCSY (13C,1H) HSQCnot availablenot availablenot available
3D HNHBnot availablenot availablenot available
3D H(C)CH DISPSYnot availablenot availablenot available
3D HCC(H) DISPSYnot availablenot availablenot available

Software:

Regine - bookkeeping

NMR spectrometers:

  • Bruker AMXT 600 MHz
  • Varian Unity-Plus 750 MHz

Related Database Links:

BMRB 4356
PDB
DBJ BAF80731 BAG12614
EMBL CAA25989
GB AAF75057 AAM81380 ADM32399 ADW81950 AKJ74157
REF NP_059641 WP_015975190
SP P03049
TPG DAA00978

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts