BMRB Entry 15652

Name: Solution NMR structure of the uncharacterized protein from Rhodospirillum rubrum gene locus Rru_A0810. Northeast Structural Genomics Target RrR43.
Published: 2008-02-07

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PDB ID: 2k0m
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/BMR15652
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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 the uncharacterized protein from Rhodospirillum rubrum gene locus Rru_A0810. Northeast Structural Genomics Target RrR43.

Deposition date:

2008-02-04

Original release date:

2008-02-07

Authors:

Rossi, Paolo; Wang, Huang; Jiang, Mei; Foote, Erica; Xiao, Rong; Liu, Jinfeng; Swapna, G.V.T.; Acton, Thomas; Baran, Michael; Rost, Burkhard; Montelione, Gaetano

Citation:

Citation: Rossi, Paolo; Xiao, Rong; Acton, Thomas; Montelione, Gaetano. "Solution NMR structure of the uncharacterized protein from Rhodospirillum rubrum gene locus Rru_A0810. Northeast Structural Genomics Target RrR43." .

Assembly members:

Assembly members:
RrR43, polymer, 104 residues, 11870.668 Da.

Natural source:

Natural source: Common Name: Rhodospirillum rubrum Taxonomy ID: 1085 Superkingdom: Bacteria Kingdom: not available Genus/species: Rhodospirillum rubrum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RrR43: MAKAQPIEIAGHEFARKADA LAFMKVMLNRYRPGDIVSTV DGAFLVEALKRHPDATSKIG PGVRNFEVRSADYGTQCFWI LRTDGSEERFSYKKCVLEHH HHHH

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	435
15N chemical shifts	90
1H chemical shifts	677

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RrR43	1

Entities:

Entity 1, RrR43 104 residues - 11870.668 Da.

97-104 C-term LEHHHHHH Ni affinity tag.

1

MET

ALA

LYS

ALA

GLN

PRO

ILE

GLU

ILE

ALA

2

GLY

HIS

GLU

PHE

ALA

ARG

LYS

ALA

ASP

ALA

3

LEU

ALA

PHE

MET

LYS

VAL

MET

LEU

ASN

ARG

4

TYR

ARG

PRO

GLY

ASP

ILE

VAL

SER

THR

VAL

5

ASP

GLY

ALA

PHE

LEU

VAL

GLU

ALA

LEU

LYS

6

ARG

HIS

PRO

ASP

ALA

THR

SER

LYS

ILE

GLY

7

PRO

GLY

VAL

ARG

ASN

PHE

GLU

VAL

ARG

SER

8

ALA

ASP

TYR

GLY

THR

GLN

CYS

PHE

TRP

ILE

9

LEU

ARG

THR

ASP

GLY

SER

GLU

ARG

PHE

10

SER

TYR

LYS

CYS

VAL

LEU

GLU

HIS

11

HIS

Samples:

sample_1: RrR43, [U-5% 13C; U-100% 15N], 1.15 mM; MES 20 mM; DTT 10 mM; sodium azide 0.02%; sodium chloride 100 mM; DSS 50 uM; calcium chloride 5 mM

sample_2: RrR43, [U-100% 13C; U-100% 15N], 1.05 mM; MES 20 mM; DTT 10 mM; sodium azide 0.02%; sodium chloride 100 mM; DSS 50 uM; calcium chloride 5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

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

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

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

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

PSVS, Bhattacharya and Montelione - validation

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

TOPSPIN v1.3, Bruker Biospin - collection

SPARKY v3.112, Goddard - data analysis

Molmol v2k2, Koradi, Billeter and Wuthrich - visualization

ProcheckNMR, Laskowski and MacArthur - refinement

MolProbity, Richardson - validation

NMR spectrometers:

Bruker Avance 800 MHz

PDB	2K0M
GB	ABC21614 AEO47305
REF	WP_011388568 YP_425901