BMRB Entry 30559

Name: Solution structure of the Tudor domain of PSHCP
Published: 2019-08-16

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PDB ID: 6nnb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30559
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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:

Solution structure of the Tudor domain of PSHCP

Deposition date:

2019-01-14

Original release date:

2019-08-16

Authors:

Bauer, Katherine; Pelligrini, M.; Ragusa, Michael

Citation:

Citation: Bauer, Katherine; Dicovitsky, R.; Pellegrini, M.; Zhaxybayeva, O.; Ragusa, Michael. "The structure of a highly-conserved picocyanobacterial protein reveals a Tudor domain with an RNA-binding function" J. Biol. Chem. 294, 14333-14344 (2019).
PubMed: 31391250

Assembly members:

Assembly members:
PSHCP, polymer, 59 residues, 6471.392 Da.

Natural source:

Natural source: Common Name: Prochlorococcus marinus (strain MIT 9303) Taxonomy ID: 59922 Superkingdom: Bacteria Kingdom: not available Genus/species: Prochlorococcus Prochlorococcus marinus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PSHCP: SNAMELDLQPGDVVKVLESA ALGWVRARVIRVKSGGRVVV QSDQGREFTARGNQVRLIE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	247
15N chemical shifts	61
1H chemical shifts	409

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 59 residues - 6471.392 Da.

1

SER

ASN

ALA

MET

GLU

LEU

ASP

LEU

GLN

PRO

2

GLY

ASP

VAL

LYS

VAL

LEU

GLU

SER

ALA

3

ALA

LEU

GLY

TRP

VAL

ARG

ALA

ARG

VAL

ILE

4

ARG

VAL

LYS

SER

GLY

ARG

VAL

5

GLN

SER

ASP

GLN

GLY

ARG

GLU

PHE

THR

ALA

6

ARG

GLY

ASN

GLN

VAL

ARG

LEU

ILE

GLU

Samples:

sample_1: PSHCP, [U-15N], 1.4 mM; sodium phosphate 20 mM; sodium chloride 200 mM; TCEP 0.2 mM

sample_2: PSHCP, [U-15N, -13C], 1.6 mM; sodium phosphate 20 mM; sodium chloride 200 mM; TCEP 0.2 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_15N-separated_NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-separated_NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	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 H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
2D_NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - processing

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 700 MHz

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