BMRB Entry 34046

Name: NMR structure of the C-terminal domain of the Bacteriophage T5 decoration protein pb10
Published: 2017-07-26

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PDB ID: 5lxk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34046
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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: NMR structure of the C-terminal domain of the Bacteriophage T5 decoration protein pb10 PubMed: 28165000

Deposition date: 2016-09-22 Original release date: 2017-07-26

Authors: Vernhes, E.; Gilquin, B.; Cuniasse, P.; Boulanger, P.; Zinn-justin, S.

Citation: Vernhes, Emeline; Renouard, Madalena; Gilquin, Bernard; Cuniasse, Philippe; Durand, Dominique; England, Patrick; Hoos, Sylviane; Huet, Alexis; Conway, James; Glukhov, Anatoly; Ksenzenko, Vladimir; Jacquet, Eric; Nhiri, Naima; Zinn-Justin, Sophie; Boulanger, Pascale. "High affinity anchoring of the decoration protein pb10 onto the bacteriophage T5 capsid" Sci. Rep. 7, 41662-41662 (2017).

Assembly members:
Decoration protein, polymer, 101 residues, 10339.291 Da.

Natural source: Common Name: viruses Taxonomy ID: 10726 Superkingdom: Viruses Kingdom: not available Genus/species: T5likevirus Enterobacteria phage T5

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

Entity Sequences (FASTA):
Decoration protein: ALTLSKDLTASMSVEEGAAL TLSVTATGGTGPYTYAWTKD GSPIPDASGATYTKPTAAAE DAGSYKVTVTDSKQVSKDST TCAVTVNPTVPGGLEHHHHH H

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	381
15N chemical shifts	91
1H chemical shifts	581

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_1 101 residues - 10339.291 Da.

1

ALA

LEU

THR

LEU

SER

LYS

ASP

LEU

THR

ALA

2

SER

MET

SER

VAL

GLU

GLY

ALA

LEU

3

THR

LEU

SER

VAL

THR

ALA

THR

GLY

THR

4

GLY

PRO

TYR

THR

TYR

ALA

TRP

THR

LYS

ASP

5

GLY

SER

PRO

ILE

PRO

ASP

ALA

SER

GLY

ALA

6

THR

TYR

THR

LYS

PRO

THR

ALA

GLU

7

ASP

ALA

GLY

SER

TYR

LYS

VAL

THR

VAL

THR

8

ASP

SER

LYS

GLN

VAL

SER

LYS

ASP

SER

THR

9

THR

CYS

ALA

VAL

THR

VAL

ASN

PRO

THR

VAL

10

PRO

GLY

LEU

GLU

HIS

11

HIS

Samples:

sample_1: c72, [U-99% 13C; U-99% 15N], 200 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 25 mM; pH: 7.2; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D TOCSY-NOESY	sample_1	isotropic	sample_conditions_1
3D HNHA	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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(COCA)	sample_1	isotropic	sample_conditions_1
3D HN(CA)NNH	sample_1	isotropic	sample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CcpNMR, CCPN - data analysis, peak picking

INCA, Savarin P., Zinn-Justin S., Gilquin B., 19,2001, J. Biomol NMR, pp. 49-62 - structure calculation

NMR spectrometers:

Bruker DRX(600) 600 MHz
Bruker DRX(700) 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts