BMRB Entry 15661

Name: Solution NMR Structure of protein hp1203 from Helicobacter pylori 26695
Published: 2009-05-07

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PDB ID: 2k0z
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15661
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of protein hp1203 from Helicobacter pylori 26695

Deposition date:

2008-02-18

Original release date:

2009-05-07

Authors:

Wu, Bin; Yee, Adelinda; Lemak, Alexander; Cort, John; Semest, Anthony; Kenney, Michael; Arrowsmith, Cheryl

Citation:

Citation: Wu, Bin; Yee, Adelinda; Lemak, Alexander; Cort, John; Semest, Anthony; Kenney, Michael; Arrowsmith, Cheryl. "Solution NMR structure of protein hp1203 from helicobacter pyloric 26695/Northeast Structure Genomics Consortium (NESG) target PT1/Ontario Center for Structural Proteomics target hp1203" .

Assembly members:

Assembly members:
hp1203, polymer, 110 residues, 25879.195 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 210 Superkingdom: Bacteria Kingdom: not available Genus/species: Helicobacter pylori

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: p11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hp1203: MLEDYAISLEEVNFNDFIVV DVRELDEYEELHLPNATLIS VNDQEKLADFLSQHKDKKVL LHCRAGRRALDAAKSMHELG YTPYYLEGNVYDFEKYGFRM VYDDTCDKKN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	479
15N chemical shifts	119
1H chemical shifts	795

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unknown_function_protein_hp1203_from_Helicobacter_pylori_26695	1

Entities:

Entity 1, unknown_function_protein_hp1203_from_Helicobacter_pylori_26695 110 residues - 25879.195 Da.

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

Samples:

sample_1: unknown function protein hp1203 from Helicobacter pylori 26695, [U-99% 13C; U-99% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 10 mM; H2O 90%; D2O 10%

sample_2: unknown function protein hp1203 from Helicobacter pylori 26695, [U-7% 13C; U-99% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 10 mM; H2O 90%; D2O 10%

sample_conditions_2: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K

sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
aiv 3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.95, Goddard - data analysis, peak picking

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.0, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct v2.1.0, Huang, Tejero, Powers and Montelione - Validation

NMR spectrometers:

Varian INOVA 500 MHz
Varian INOVA 600 MHz

PDB	2K0Z
DBJ	BAJ56270 BAJ58734 BAJ60256 BAO97236
EMBL	CAX29900 CBI65819
GB	AAD08279 ABF85232 ACI27917 ACX99708 ADN80346
REF	NP_208015 WP_000888636 WP_000888781 WP_000888783 WP_000888785

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

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