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 11011

Title: Solution structure of the N-terminal soluble domains of Bacillus subtilis CopA   PubMed: 18215122

Deposition date: 2007-10-29 Original release date: 2008-06-27

Authors: Singleton, Chloe; Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Tenori, Leonardo; Kihlken, Margaret; Boetzel, Ruth; Le Brun, Nick

Citation: Singleton, Chloe; Banci, Lucia; Ciofi-Baffoni, Simone; Tenori, Leonardo; Kihlken, Margaret; Boetzel, Ruth; Le Brun, Nick. "Structure and Cu(I)-binding properties of the N-terminal soluble domains of Bacillus subtilis CopA"  Biochem. J. 411, 571-579 (2008).

Assembly members:
CopA, polymer, 147 residues, 15936.320 Da.

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):
CopA: MLSEQKEIAMQVSGMTCAAC AARIEKGLKRMPGVTDANVN LATETSNVIYDPAETGTAAI QEKIEKLGYHVVTEKAEFDI EGMTCAACANRIEKRLNKIE GVANAPVNFALETVTVEYNP KEASVSDLKEAVDKLGYKLK LKGEQDS

Data sets:
Data typeCount
13C chemical shifts418
15N chemical shifts149
1H chemical shifts875

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 147 residues - 15936.320 Da.

1   METLEUSERGLUGLNLYSGLUILEALAMET
2   GLNVALSERGLYMETTHRCYSALAALACYS
3   ALAALAARGILEGLULYSGLYLEULYSARG
4   METPROGLYVALTHRASPALAASNVALASN
5   LEUALATHRGLUTHRSERASNVALILETYR
6   ASPPROALAGLUTHRGLYTHRALAALAILE
7   GLNGLULYSILEGLULYSLEUGLYTYRHIS
8   VALVALTHRGLULYSALAGLUPHEASPILE
9   GLUGLYMETTHRCYSALAALACYSALAASN
10   ARGILEGLULYSARGLEUASNLYSILEGLU
11   GLYVALALAASNALAPROVALASNPHEALA
12   LEUGLUTHRVALTHRVALGLUTYRASNPRO
13   LYSGLUALASERVALSERASPLEULYSGLU
14   ALAVALASPLYSLEUGLYTYRLYSLEULYS
15   LEULYSGLYGLUGLNASPSER

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

DYANA, Guntert, Braun and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAI86922 BAM55428 BAM59441 GAK81833
EMBL CAB15355 CCU60411 CEI58885 CEJ79011 CJR54553
GB ADV94160 AEP92386 AFQ59202 AGA23186 AGE64955
REF NP_391230 WP_003242925 WP_014477985 WP_015483692 WP_015714705
SP O32220

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