BMRB Entry 34047

Name: NMR structure of the N-terminal domain of the Bacteriophage T5 decoration protein pb10
Published: 2017-04-13

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PDB ID: 5lxl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34047
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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:

NMR structure of the N-terminal domain of the Bacteriophage T5 decoration protein pb10

Deposition date:

2016-09-22

Original release date:

2017-04-13

Authors:

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

Citation:

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).
PubMed: 28165000

Assembly members:

Assembly members:
Decoration protein, polymer, 86 residues, 9758.273 Da.

Natural source:

Natural source: Common Name: Escherichia phage T5 Taxonomy ID: 10726 Superkingdom: Viruses Kingdom: not available Genus/species: T5virus not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Decoration protein: MGIDYSGLRTIFGEKLPESH IFFATVAAHKYVPSYAFLRR ELGLSSAHTNRKVWKKFVEA YGKAIPPAPPAPPLTLSKLE HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	332
15N chemical shifts	68
1H chemical shifts	521

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 86 residues - 9758.273 Da.

1

MET

GLY

ILE

ASP

TYR

SER

GLY

LEU

ARG

THR

2

ILE

PHE

GLY

GLU

LYS

LEU

PRO

GLU

SER

HIS

3

ILE

PHE

ALA

THR

VAL

ALA

HIS

LYS

4

TYR

VAL

PRO

SER

TYR

ALA

PHE

LEU

ARG

5

GLU

LEU

GLY

LEU

SER

ALA

HIS

THR

ASN

6

ARG

LYS

VAL

TRP

LYS

PHE

VAL

GLU

ALA

7

TYR

GLY

LYS

ALA

ILE

PRO

ALA

PRO

8

ALA

PRO

LEU

THR

LEU

SER

LYS

LEU

GLU

9

HIS

Samples:

sample_1: n77, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D HSQC	sample_1	isotropic	sample_conditions_1
3D TOCSY-NOESY	sample_1	isotropic	sample_conditions_1
3D HN-HA	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCO	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 DRX600 600 MHz
Bruker DRX700 700 MHz

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