BMRB Entry 16576

Name: Solution Structure Of Protein BH0266 From Bacillus halodurans. Northeast Structural Genomics Consortium Target BhR97a
Published: 2010-01-07

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PDB ID: 2kq1
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/BMR16576
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure Of Protein BH0266 From Bacillus halodurans. Northeast Structural Genomics Consortium Target BhR97a

Deposition date:

2009-10-23

Original release date:

2010-01-07

Authors:

Wu, Yibing; Eletsky, Alexander; Lee, Dan; Sathyamoorthy, Bharathwaj; Buchwald, William; Hua, Jia; Ciccosanti, Colleen; He, Yunfen; Hamilton, Keith; Acton, T.B.; Xiao, R.; Everett, J.K.; Lee, Hsiau-Wei; Prestegard, Jim; Montelione, G.T.; Szyperski, Thomas

Citation:

Citation: Barb, Adam; Cort, John; Seetharaman, Jayaraman; Lew, Scott; Lee, Hsiau-Wei; Acton, Thomas; Xiao, Rong; Kennedy, Michael; Tong, Liang; Montelione, Gaetano; Prestegard, James. "Structures of domains I and IV from YbbR are representative of a widely distributed protein family" Protein Sci. 20, 396-405 (2011).
PubMed: 21154411

Assembly members:

Assembly members:
BH0266, polymer, 119 residues, 13589.194 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: BL21(DE3)+ Magic

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BH0266: MPTFDHGNLSLGELELTVLY DEERYDIVEQTETVQVDLEG PRGVLTVFRFARPSYEVFVD LTEAGEGSHTVDVEHRGFPG DLAVTVEPRMARVQLEERQT VSVPVTVEMINLEHHHHHH

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	358
15N chemical shifts	113
1H chemical shifts	763

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BH0266	1

Entities:

Entity 1, BH0266 119 residues - 13589.194 Da.

1

MET

PRO

THR

PHE

ASP

HIS

GLY

ASN

LEU

SER

2

LEU

GLY

GLU

LEU

GLU

LEU

THR

VAL

LEU

TYR

3

ASP

GLU

ARG

TYR

ASP

ILE

VAL

GLU

GLN

4

THR

GLU

THR

VAL

GLN

VAL

ASP

LEU

GLU

GLY

5

PRO

ARG

GLY

VAL

LEU

THR

VAL

PHE

ARG

PHE

6

ALA

ARG

PRO

SER

TYR

GLU

VAL

PHE

VAL

ASP

7

LEU

THR

GLU

ALA

GLY

GLU

GLY

SER

HIS

THR

8

VAL

ASP

VAL

GLU

HIS

ARG

GLY

PHE

PRO

GLY

9

ASP

LEU

ALA

VAL

THR

VAL

GLU

PRO

ARG

MET

10

ALA

ARG

VAL

GLN

LEU

GLU

ARG

GLN

THR

11

VAL

SER

VAL

PRO

VAL

THR

VAL

GLU

MET

ILE

12

ASN

LEU

GLU

HIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_2: entity, [U-5% 13C; U-99% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 288 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
simNOESY	sample_1	isotropic	sample_conditions_1

Software:

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

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

XEASY, Bartels et al. - data analysis

NMR spectrometers:

Varian INOVA 600 MHz
Bruker DMX 800 MHz

PDB	2KQ1
DBJ	BAB03985
GB	KOO36863
REF	WP_010896448 WP_053432100