BMRB Entry 16615

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16615

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Title:
Backbone assignment of E. coli HU protein
Deposition date:
2009-11-23
Original release date:
2012-08-03
Authors:
Augustyniak, Rafal; Castaing, Bertrand; Damblon, Christian
Citation:

Citation: Augustyniak, Rafal; Castaing, Bertrand; Damblon, Christian. "Backbone NMR assignment of E. coli HU proteins."  .

Assembly members:

Assembly members:
HU_beta2, polymer, 90 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HU_beta2: MNKSQLIDKIAAGADISKAA AGRALDAIIASVTESLKEGD DVALVGFGTFAVKERAARTG RNPQTGKEITIAAAKVPSFR AGKALKDAVN

Data sets:
Data typeCount
13C chemical shifts239
15N chemical shifts76
1H chemical shifts76

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HU-beta2, chain 11
2HU-beta2, chain 21

Entities:

Entity 1, HU-beta2, chain 1 90 residues - Formula weight is not available

1   METASNLYSSERGLNLEUILEASPLYSILE
2   ALAALAGLYALAASPILESERLYSALAALA
3   ALAGLYARGALALEUASPALAILEILEALA
4   SERVALTHRGLUSERLEULYSGLUGLYASP
5   ASPVALALALEUVALGLYPHEGLYTHRPHE
6   ALAVALLYSGLUARGALAALAARGTHRGLY
7   ARGASNPROGLNTHRGLYLYSGLUILETHR
8   ILEALAALAALALYSVALPROSERPHEARG
9   ALAGLYLYSALALEULYSASPALAVALASN

Samples:

sample_1: HU beta2, [U-99% 13C; U-99% 15N], 1.54 mM; D2O 5%; sodium phosphate 20 mM; sodium chloride 200 mM; DTT 0.05 mM; DSS 0.1 mM; H2O 95%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_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 CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

VNMR, Varian - collection

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

ANALYSIS v2.0.7, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 25329
PDB
DBJ BAA11644 BAB33917 BAE76220 BAG75990 BAI23814
EMBL CAA30692 CAA34539 CAD08910 CAP74974 CAQ30913
GB AAB40196 AAC73543 AAG54790 AAL19406 AAN42041
PIR AF0558
PRF 1410323A
REF NP_308521 NP_414974 NP_455048 NP_459447 NP_706334
SP P0A1R8 P0A1R9 P0ACF4 P0ACF5 P0ACF6
AlphaFold P0A1R8 P0A1R9 P0ACF4 P0ACF5 P0ACF6

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks