BMRB Entry 30070

Name: The NMR Solution Structure of RPA3313
Published: 2016-06-09

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PDB ID: 5jn6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30070
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

The NMR Solution Structure of RPA3313

Deposition date:

2016-04-29

Original release date:

2016-06-09

Authors:

Catazaro, Jonathan; Lowe, Austin; Powers, Robert; Structural Genomics Consortium (SGC), SGC

Citation:

Citation: Catazaro, Jonathan; Lowe, Austin; Cerny, Ronald; Powers, Robert. "The NMR Solution Structure and Function of RPA3313: A Hypothetical Protein from R. palustris" Proteins 85, 93-102 (2017).
PubMed: 27802574

Assembly members:

Assembly members:
Uncharacterized protein, polymer, 91 residues, 9887.637 Da.

Natural source:

Natural source: Common Name: a-proteobacteria Taxonomy ID: 258594 Superkingdom: Bacteria Kingdom: not available Genus/species: Rhodopseudomonas Rhodopseudomonas palustris

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Uncharacterized protein: MGSSHHHHHHSSGRENLYFQ GMGKAYYDIVGSDNRWGIRH DDDPTGDYSSKEAAFEAACA AASNAIKFGHEVRITVPGND GSETNLGVITN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	246
15N chemical shifts	68
1H chemical shifts	422

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 91 residues - 9887.637 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

ARG

GLU

ASN

LEU

TYR

PHE

GLN

3

GLY

MET

GLY

LYS

ALA

TYR

ASP

ILE

VAL

4

GLY

SER

ASP

ASN

ARG

TRP

GLY

ILE

ARG

HIS

5

ASP

PRO

THR

GLY

ASP

TYR

SER

6

LYS

GLU

ALA

PHE

GLU

ALA

CYS

ALA

7

ALA

SER

ASN

ALA

ILE

LYS

PHE

GLY

HIS

8

GLU

VAL

ARG

ILE

THR

VAL

PRO

GLY

ASN

ASP

9

GLY

SER

GLU

THR

ASN

LEU

GLY

VAL

ILE

THR

10

ASN

Samples:

sample_1: RPA3313, none, 1 mM; MES 18 mM; sodium azide 0.1%; sodium chloride 80 mM

sample_conditions_1: ionic strength: 80 mM; pH: 5.6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CC(CA)NH	sample_1	isotropic	sample_conditions_1
3D HCC(CO)NH	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	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
3D HNHA	sample_1	isotropic	sample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment, peak picking

X-PLOR NIH v2.41.1, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Bruker Avance III 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks