BMRB Entry 17530

Name: Solution NMR structure of the AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, Northeast Structural Genomics Consortium Target ReR242
Published: 2011-04-11

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PDB ID: 2lak
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17530
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution NMR structure of the AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, Northeast Structural Genomics Consortium Target ReR242

Deposition date: 2011-03-16 Original release date: 2011-04-11

Authors: Yang, Yunhuang; Ramelot, Theresa; Cort, John; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Rost, Nair; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Yang, Yunhuang; Ramelot, Theresa; Cort, John; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Rost, Nair; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, Northeast Structural Genomics Consortium Target ReR242" Not known ., .-..

Assembly members:
AHSA1-like_protein_RHE_CH02687_(1-152)_from_Rhizobium_etli, polymer, 160 residues, 17575.8 Da.

Natural source: Common Name: Rhizobium etli Taxonomy ID: 29449 Superkingdom: Bacteria Kingdom: not available Genus/species: Rhizobium etli

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

Entity Sequences (FASTA):
AHSA1-like_protein_RHE_CH02687_(1-152)_from_Rhizobium_etli: MEKAMPESFVVRREAHLAAP PAAVFALMTDPEKILRWMGT EAEVEPEPGGLYLVNVTGAR FARGSFREVVPVHRLAYSFG WDGSEVVPPGSSLVEIDLIE QGGGTLLRLTHSGLPSAEQC AGHEEGWAHYLGRLTEVAAG RDPGPDPFYGRRLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	639
15N chemical shifts	154
1H chemical shifts	1017

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AHSA1-like protein RHE_CH02687 (1-152)	1

Entities:

Entity 1, AHSA1-like protein RHE_CH02687 (1-152) 160 residues - 17575.8 Da.

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

Samples:

NC_sample: AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, [U-100% 13C; U-100% 15N], 0.72 ± 0.07 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 mM; DTT 10 ± 0.5 mM

NC5_sample: AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, [U-5% 13C; U-100% 15N], 0.76 ± 0.07 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 mM

NC_sample_in_D2O: AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, [U-100% 13C; U-100% 15N], 0.72 ± 0.07 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC-CT	NC5_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC5_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY_aliph	NC_sample	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HNCA	NC_sample	isotropic	sample_conditions_1
3D HN(CO)CA	NC_sample	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D H(CCO)NH	NC_sample	isotropic	sample_conditions_1
3D C(CCO)NH	NC_sample	isotropic	sample_conditions_1
3D HCCH-COSY	NC_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D CCH-TOCSY	NC_sample_in_D2O	isotropic	sample_conditions_1
4D CC-NOESY	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC-aromatic	NC_sample	isotropic	sample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.1, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift autoassignment

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

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance III 850 MHz

PDB	2LAK
GB	ABC91458 AGS22491
REF	WP_041678693

Biological Magnetic Resonance Data Bank