BMRB Entry 16592

Name: Solution NMR structure of a domain from BT9727_4915 from Bacillus thuringiensis, Northeast Structural Genomics Consortium Target BuR95A
Published: 2009-11-30

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PDB ID: 2kq8
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/BMR16592
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution NMR structure of a domain from BT9727_4915 from Bacillus thuringiensis, Northeast Structural Genomics Consortium Target BuR95A

Deposition date: 2009-10-30 Original release date: 2009-11-30

Authors: He, Yunfen; Mills, Jeffrey; Wu, Yibing; Eletsky, Alexander; Wang, Huang; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; Szyperski, Thomas

Citation: He, Yunfen; Mills, Jeffrey; Wu, Yibing; Eletsky, Alexander; Wang, Huang; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; Szyperski, Thomas. "Solution NMR structure of a domain from BT9727_4915 from Bacillus thuringiensis, Northeast Structural Genomics Consortium Target BuR95A" Not known ., .-..

Assembly members:
BT9727_4915, polymer, 70 residues, 7893.819 Da.

Natural source: Common Name: B. thuringiensis Taxonomy ID: 1428 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus thuringiensis

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

Entity Sequences (FASTA):
BT9727_4915: MIGDYYINASALNVRSGEGT NYRIIGALPQGQKVQVISEN SGWSKINYNGQTGYIGTRYL SKLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	149
15N chemical shifts	53
1H chemical shifts	314

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BT9727_4915	1

Entities:

Entity 1, BT9727_4915 70 residues - 7893.819 Da.

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

Samples:

NC: BuR95A, [U-98% 13C; U-98% 15N], 0.905 mM; H2O 90 % v/v; D2O, [U-100% 2H], 10 % v/v; NH4OAc 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; DSS 50 uM

NC5: BuR95A, [U-5% 13C; U-98% 15N], 1.041 mM; H2O 90 % v/v; D2O, [U-100% 2H], 10 % v/v; NH4OAc 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; DSS 50 uM

sample_conditions_1: ionic strength: 217.5 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC	isotropic	sample_conditions_1
GFT (4,3)D CABCA(CO)NHN	NC	isotropic	sample_conditions_1
GFT (4,3)D HNNCABCA	NC	isotropic	sample_conditions_1
GFT (4,3)D HABCAB(CO)NHN	NC	isotropic	sample_conditions_1
3D HNCA	NC	isotropic	sample_conditions_1
simNOESY	NC	isotropic	sample_conditions_1
3D 1H-15N TOCSY	NC5	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC5	isotropic	sample_conditions_1

Software:

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

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

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

PSVS, Bhattacharya and Montelione - refinement

TALOS, Cornilescu, Delaglio and Bax - refinement

XEASY, Bartels et al. - chemical shift assignment

VNMRJ, Varian - collection

TOPSPIN, Bruker Biospin - collection

PROSA, Guntert - processing

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

Molmol, Koradi, Billeter and Wuthrich - refinement

SPSCAN, Glaser - processing

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance 800 MHz

Biological Magnetic Resonance Data Bank