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 15275

Title: Soution Structure of Af54 M-domain   PubMed: 18618268

Deposition date: 2007-05-31 Original release date: 2008-07-15

Authors: Ilangovan, Udayar; Hinck, Andrew

Citation: Ilangovan, Udayar; Bhuiyan, Shakhawat; Hinck, Cynthia; Hoyle, Jeffrey; Pakhomova, Olga; Zwieb, Christian; Hinck, Andrew. "A. fulgidus SRP54 M-domain"  J. Biomol. NMR 41, 241-248 (2008).

Assembly members:
af54, polymer, 115 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: 2234   Superkingdom: Archaea   Kingdom: not available   Genus/species: Archaeoglobus fulgidus

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

Entity Sequences (FASTA):
af54: MEKGTFTLKDIYKQIEAMNK MGPVRKIFEMLPFGLGLKVD NDVMEMTQEKMKKFRVIMDS MTEEELLNPKIIDSSRIRRI AIGSGTSPQEVKELLNYYKT MKNLMKKMKKNKLPI

Data sets:
Data typeCount
13C chemical shifts397
15N chemical shifts90
1H chemical shifts594

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1srp541

Entities:

Entity 1, srp54 115 residues - Formula weight is not available

1   METGLULYSGLYTHRPHETHRLEULYSASP
2   ILETYRLYSGLNILEGLUALAMETASNLYS
3   METGLYPROVALARGLYSILEPHEGLUMET
4   LEUPROPHEGLYLEUGLYLEULYSVALASP
5   ASNASPVALMETGLUMETTHRGLNGLULYS
6   METLYSLYSPHEARGVALILEMETASPSER
7   METTHRGLUGLUGLULEULEUASNPROLYS
8   ILEILEASPSERSERARGILEARGARGILE
9   ALAILEGLYSERGLYTHRSERPROGLNGLU
10   VALLYSGLULEULEUASNTYRTYRLYSTHR
11   METLYSASNLEUMETLYSLYSMETLYSLYS
12   ASNLYSLEUPROILE

Samples:

sample_1: af54, [U-95% 15N], 0.5 ± 0.05 mM; sodium phosphate 25 mM; sodium azide 0.02 % (w/v); H2O 95%; D2O 5%

sample_2: af54, [U-95% 13C; U-95% 15N], 0.5 ± 0.05 mM; af54, [U-95% 15N], 0.5 ± 0.05 mM; sodium phosphate 25 mM; sodium azide 0.02 % (w/v); H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0 M; pH: 5.5; pressure: 1 atm; temperature: 300 K

sample_conditions_2: ionic strength: 0 M; pH: 5.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1

Software:

NMRView v5.0.4, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectral Visualization

X-PLOR NIH v2.9.6, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
GB AAB90619 AIG97502
REF WP_010878126
SP O29633

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