BMRB Entry 15344

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PDB ID: 2jrt
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/BMR15344
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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:

The solution structure of the protein coded by gene RHOS4_12090 of R. sphaeroides. Northeast structural genomics target RhR5

Deposition date:

2007-06-28

Original release date:

2008-02-21

Authors:

Wang, Lincong; Chen, Chen; Nwosu, Chioma; Cunningham, Kellie; Owens, Leah; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation:

Citation: Wang, Lincong; Montelione, Gaetano. "The solution structure of the protein coded by gene RHOS4_12090 of R. sphaeroides. Northeast structural genomics target RhR5" Proteins ., .-..

Assembly members:

Assembly members:
RhR5, polymer, 95 residues, 10881.731 Da.

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: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RhR5: MYLKRVDGPRQVTLPDGTVL SRADLPPLDTRRWVASRKAA VVKAVIHGLITEREALDRYS LSEEEFALWRSAVAAHGEKA LKVTMIQKYRQLHHH

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	415
15N chemical shifts	97
1H chemical shifts	672

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RhR5	1

Entities:

Entity 1, RhR5 95 residues - 10881.731 Da.

Residues 93-95 represent a non-native affinity tag

1

MET

TYR

LEU

LYS

ARG

VAL

ASP

GLY

PRO

ARG

2

GLN

VAL

THR

LEU

PRO

ASP

GLY

THR

VAL

LEU

3

SER

ARG

ALA

ASP

LEU

PRO

LEU

ASP

THR

4

ARG

TRP

VAL

ALA

SER

ARG

LYS

ALA

5

VAL

LYS

ALA

VAL

ILE

HIS

GLY

LEU

ILE

6

THR

GLU

ARG

GLU

ALA

LEU

ASP

ARG

TYR

SER

7

LEU

SER

GLU

PHE

ALA

LEU

TRP

ARG

8

SER

ALA

VAL

ALA

HIS

GLY

GLU

LYS

ALA

9

LEU

LYS

VAL

THR

MET

ILE

GLN

LYS

TYR

ARG

10

GLN

LEU

HIS

Samples:

sample_1: RhR5, [U-5% 13C; U-100% 15N], 1.0 mM; DTT 10 mM; sodium chloride 100 mM

sample_2: RhR5, [U-100% 13C; U-100% 15N], 1.0 mM; DTT 10 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293.0 K

Experiments:

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

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

SPARKY, Goddard - data analysis

X-PLOR, Brunger - structure solution

PSVS, Bhattacharya and Montelione - validation

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2JRT
GB	ABA78777 ABN76388 ACM00792 EGJ21075
REF	WP_002719769 WP_011840915 YP_352678