BMRB Entry 15324

Name: A novel domain-swapped solution NMR structure of protein RPA2121 from Rhodopseudomonas palustris
Published: 2009-10-09

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PDB ID: 2jra
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15324
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

A novel domain-swapped solution NMR structure of protein RPA2121 from Rhodopseudomonas palustris

Deposition date:

2007-06-21

Original release date:

2009-10-09

Authors:

Wu, Bin; Yee, Adelinda; Lemak, Alexander; Cort, John; Bansal, Sonal; Semest, Anthony; Guido, Valerie; Kennedy, Michael; Prestegard, James; Arrowsmith, Cheryl

Citation:

Citation: Wu, Bin; Yee, Adelinda; Lemak, Alexander; Cort, John; Bansal, Sonal; Semest, Anthony; Guido, Valerie; Kennedy, Michael; Prestegard, James; Arrowsmith, Cheryl. "A novel domain-swapped solution NMR structure of protein RPA2121 from Rhodopseudomonas palustris" .

Assembly members:

Assembly members:
unknown_function_protein_RPA2121, polymer, 67 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Rhodopseudomonas palustris Taxonomy ID: 1076 Superkingdom: Bacteria Kingdom: not available Genus/species: Rhodopseudomonas palustris

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: p15Tvlic

Entity Sequences (FASTA):

Entity Sequences (FASTA):
unknown_function_protein_RPA2121: MMTASDRLGADPTQAASSPG GARAVSIVGNQIDSRELFTV DREIVIAHGDDRYRLRLTSQ NKLILTK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	267
15N chemical shifts	64
1H chemical shifts	446

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit 1	1
2	subunit 2	1

Entities:

Entity 1, subunit 1 67 residues - Formula weight is not available

1

MET

THR

ALA

SER

ASP

ARG

LEU

GLY

ALA

2

ASP

PRO

THR

GLN

ALA

SER

PRO

GLY

3

GLY

ALA

ARG

ALA

VAL

SER

ILE

VAL

GLY

ASN

4

GLN

ILE

ASP

SER

ARG

GLU

LEU

PHE

THR

VAL

5

ASP

ARG

GLU

ILE

VAL

ILE

ALA

HIS

GLY

ASP

6

ASP

ARG

TYR

ARG

LEU

ARG

LEU

THR

SER

GLN

7

ASN

LYS

LEU

ILE

LEU

THR

LYS

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHA	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D IPAP 15N-HSQC	sample_2	isotropic	sample_conditions_1

PDB	2JRA
EMBL	CAE27562
REF	WP_011157676

BMRB Entry 15324

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: