BMRB Entry 15152

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15152
MolProbity Validation Chart

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Title:
Hydrogenase isoenzymes formation protein HypC
Deposition date:
2007-03-01
Original release date:
2007-10-24
Authors:
Wang, Lei; Jin, Changwen
Citation:

Citation: Wang, Lei; Xia, B.; Jin, Changwen. "Solution structure of hydrogenase isoenzymes formation protein HypC from Escherichia coli"  Biochem Biophys Res Commun. 361, 665-669 (2007).
PubMed: 17669368

Assembly members:

Assembly members:
HypC, polymer, 90 residues, 9742.051 Da.

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: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HypC: MCIGVPGQIRTIDGNQAKVD VCGIQRDVDLTLVGSCDENG QPRVGQWVLVHVGFAMSVIN EAEARDTLDALQNMFDVEPD VGALLYGEEK

Data sets:
Data typeCount
13C chemical shifts362
15N chemical shifts100
1H chemical shifts603

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HypC1

Entities:

Entity 1, HypC 90 residues - 9742.051 Da.

1   METCYSILEGLYVALPROGLYGLNILEARG
2   THRILEASPGLYASNGLNALALYSVALASP
3   VALCYSGLYILEGLNARGASPVALASPLEU
4   THRLEUVALGLYSERCYSASPGLUASNGLY
5   GLNPROARGVALGLYGLNTRPVALLEUVAL
6   HISVALGLYPHEALAMETSERVALILEASN
7   GLUALAGLUALAARGASPTHRLEUASPALA
8   LEUGLNASNMETPHEASPVALGLUPROASP
9   VALGLYALALEULEUTYRGLYGLUGLULYS

Samples:

sample_1: HypC, [U-95% 15N], 1 mM; potassium phosphate 30 mM; KCl 30 mM; dithiothreitol 25 uM; sodium azide 0.02%

sample_2: HypC, [U-95% 13C; U-95% 15N], 1 mM; potassium phosphate 30 mM; KCl 30 mM; dithiothreitol 25 uM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.06 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

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

CYANA v2, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v7, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB37007 BAE76805 BAG78500 BAI26986 BAI32015
EMBL CAA38414 CAP77164 CAQ33060 CAQ87912 CAQ99647
GB AAA69238 AAC75770 AAG57836 AAN44236 AAN81737
REF NP_311611 NP_417208 NP_708529 WP_000334869 WP_000334872
SP P0AAM3 P0AAM4 P0AAM5 P0AAM6
AlphaFold P0AAM3 P0AAM4 P0AAM5 P0AAM6

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