BMRB Entry 15152

Name: Hydrogenase isoenzymes formation protein HypC
Published: 2007-10-24

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PDB ID: 2ot2
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
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Hydrogenase isoenzymes formation protein HypC PubMed: 17669368

Deposition date: 2007-03-01 Original release date: 2007-10-24

Authors: Wang, Lei; Jin, Changwen

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).

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

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

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

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	362
15N chemical shifts	100
1H chemical shifts	603

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HypC	1

Entities:

Entity 1, HypC 90 residues - 9742.051 Da.

1	MET	CYS	ILE	GLY	VAL	PRO	GLY	GLN	ILE	ARG
2	THR	ILE	ASP	GLY	ASN	GLN	ALA	LYS	VAL	ASP
3	VAL	CYS	GLY	ILE	GLN	ARG	ASP	VAL	ASP	LEU
4	THR	LEU	VAL	GLY	SER	CYS	ASP	GLU	ASN	GLY
5	GLN	PRO	ARG	VAL	GLY	GLN	TRP	VAL	LEU	VAL
6	HIS	VAL	GLY	PHE	ALA	MET	SER	VAL	ILE	ASN
7	GLU	ALA	GLU	ALA	ARG	ASP	THR	LEU	ASP	ALA
8	LEU	GLN	ASN	MET	PHE	ASP	VAL	GLU	PRO	ASP
9	VAL	GLY	ALA	LEU	LEU	TYR	GLY	GLU	GLU	LYS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_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

PDB	2OT2
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

Biological Magnetic Resonance Data Bank