BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15910

Title: NMR solution structure of the Bacillus subtilis ClpC N-domain   PubMed: 19361434

Authors: Kojetin, Douglas; McLaughlin, Patrick; Thompson, Richele; Rance, Mark; Cavanagh, John

Citation: Kojetin, Douglas; McLaughlin, Patrick; Thompson, Richele; Dubnau, David; Prepiak, Peter; Rance, Mark; Cavanagh, John. "Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions"  J. Mol. Biol. 387, 639-652 (2009).

Assembly members:
N-ClpCR, polymer, 146 residues, Formula weight is not available

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
N-ClpCR: HMMFGRFTERAQKVLALAQE EALRLGHNNIGTEHILLGLV REGEGIAAKALQALGLGSEK IQKEVESLIGRGQEMSQTIH YTPRAKKVIELSMDEARKLG HSYVGTEHILLGLIREGEGV AARVLNNLGVSLNKARQQVL QLLGSN

Data sets:
Data typeCount
heteronuclear NOE values236
residual dipolar couplings78
T1 relaxation values236
T2 relaxation values236

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-ClpCR1

Entities:

Entity 1, N-ClpCR 146 residues - Formula weight is not available

One additional, unobservable residue (His) was added to the N-terminus of the protein as a consequence of the removal of the His tag.

1   HISMETMETPHEGLYARGPHETHRGLUARG
2   ALAGLNLYSVALLEUALALEUALAGLNGLU
3   GLUALALEUARGLEUGLYHISASNASNILE
4   GLYTHRGLUHISILELEULEUGLYLEUVAL
5   ARGGLUGLYGLUGLYILEALAALALYSALA
6   LEUGLNALALEUGLYLEUGLYSERGLULYS
7   ILEGLNLYSGLUVALGLUSERLEUILEGLY
8   ARGGLYGLNGLUMETSERGLNTHRILEHIS
9   TYRTHRPROARGALALYSLYSVALILEGLU
10   LEUSERMETASPGLUALAARGLYSLEUGLY
11   HISSERTYRVALGLYTHRGLUHISILELEU
12   LEUGLYLEUILEARGGLUGLYGLUGLYVAL
13   ALAALAARGVALLEUASNASNLEUGLYVAL
14   SERLEUASNLYSALAARGGLNGLNVALLEU
15   GLNLEULEUGLYSERASN

Samples:

sample_1: N-ClpCR, [U-13C; U-15N], 0.5-1.0 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: N-ClpCR, [U-15N], 0.5 – 1.0 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 305.15 K

Experiments:

NameSampleSample stateSample conditions
2D [1H,1H]-NOESYsample_2isotropicsample_conditions_1
3D [1H,15N,1H]-NOESY-HSQCsample_1isotropicsample_conditions_1
3D [1H,13C,1H]-NOESY-HSQCsample_1isotropicsample_conditions_1
2D [1H,13C]-NOESY-HSQCsample_1isotropicsample_conditions_1
4D [1H,13C]-HMQC-NOESY-[1H,13C]-HMQCsample_1isotropicsample_conditions_1
4D [1H,13C]-HMQC-NOESY-[1H,15N]-HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2anisotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O, . - chemical shift assignment, structure solution

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

Relax v1.2, d, . - model-free analysis of relaxation data

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

BMRB 15383
PDB
GB ALC83305
REF WP_053605144