BMRB Entry 15482

Name: Solution NMR Structure of R. sphaeroides protein RSP_1027: Northeast Structural Genomics Consortium Target RhR95.
Published: 2007-10-02

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15482

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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 R. sphaeroides protein RSP_1027: Northeast Structural Genomics Consortium Target RhR95.

Deposition date:

2007-09-21

Original release date:

2007-10-02

Authors:

Eletsky, Alexander; Sukumaran, Dinesh; Zhang, Qi; Parish, David; Xu, Duanxiang; Wang, Huang; Janjua, Haleema; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Eletsky, Alexander; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of R. sphaeroides protein RHOS4_26430: Northeast Structural Genomics Consortium Target RhR95" Proteins: Struct. Funct. Genet. ., .-..

Assembly members:

Assembly members:
rhr95_protein, polymer, 80 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Rhodobacter sphaeroides Taxonomy ID: 1063 Superkingdom: Bacteria Kingdom: not available Genus/species: Rhodobacter sphaeroides

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rhr95_protein: MRRQPKTRQESARMSIEAPE TVVVSTWKVACDGGEGALGH PRVWLSIPHETGFVECGYCD RRYIHESFAAAKLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	296
15N chemical shifts	80
1H chemical shifts	463

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein	1

Entities:

Entity 1, protein 80 residues - Formula weight is not available

8-residue C-terminal His-tag LEHHHHHH

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

Samples:

NC: rhr95_protein, [U-100% 13C; U-100% 15N], 0.7 mM; calcium chloride 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; sodium azide 0.02%; H2O 95%; D2O 5%

NC5: rhr95_protein, [U-5% 13C; U-100% 15N], 0.7 mM; calcium chloride 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; sodium azide 0.02%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 135 mM; pH: 5.5; 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 aliphatic	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
(4,3)D GFT CABCA(CO)NHN	NC	isotropic	sample_conditions_1
(4,3)D GFT HNNCABCA	NC	isotropic	sample_conditions_1
(4,3)D GFT HABCABCA(CO)NHN	NC	isotropic	sample_conditions_1
(4,3)D GFT HCCH-COSY aliphatic	NC	isotropic	sample_conditions_1
(4,3)D GFT HCCH-COSY aromatic	NC	isotropic	sample_conditions_1
2D 1H-15N long-range HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C ct-HSQC 28ms	NC5	isotropic	sample_conditions_1
3D 1H-15N/13C NOESY	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	NC	isotropic	sample_conditions_1
2D 1H-13C ct-HSQC aliphatic	NC	isotropic	sample_conditions_1
2D 1H-13C ct-HSQC aromatic	NC	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	NC	isotropic	sample_conditions_1
2D 1H-13C ct-HSQC 56ms	NC5	isotropic	sample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

PROSA v6.0.2, Guntert - processing

CARA v1.8.4, Keller - chemical shift assignment, data analysis, peak picking

AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution

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

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization

PSVS, Bhattacharya and Montelione - structure validation

XEASY v1.3.12, Bartels et al. - data analysis

NMR spectrometers:

Varian INOVA 750 MHz

PDB	2JVM
GB	ABA80211 ABN77790 ACM02281 EGJ22528 EKX58095
REF	WP_002721359 YP_354112

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

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