BMRB Entry 27196

Name: Solution-NMR assignment of the Ig-like domain of bacteriophage T5 tail tube protein pb6
Published: 2017-08-04

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27196

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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-NMR assignment of the Ig-like domain of bacteriophage T5 tail tube protein pb6

Deposition date:

2017-08-02

Original release date:

2017-08-04

Authors:

Paul, Schanda; Kurauskas, Vilius; Breyton, Cecile; Arnaud, Charles-Adrien

Citation:

Citation: Fraga, Hugo; Arnaud, Charles-Adrien; Gauto, Diego; Audin, Maxime; Kurauskas, Vilius; Macek, Pavel; Krichel, Carsten; Guan, Jia-Ying; Boisbouvier, Jerome; Sprangers, Remco; Breyton, Cecile; Schanda, Paul. "Solid-State NMR H-N-(C)-H and H-N-C-C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins." Chemphyschem 18, 2697-2703 (2017).
PubMed: 28792111

Assembly members:

Assembly members:
Igdomain, polymer, 103 residues, 10543.7874 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Igdomain: AVTAITVKSAGNVTTLNRSA TLQMSVEVTPSSARNKEVTW AITAGDAATINATGLLRADA SKTGAVTVEATAKDGSGVKG TKVITVTAGGENLYFQGHHH HHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	276
15N chemical shifts	95
1H chemical shifts	95

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Igdomain	1

Entities:

Entity 1, Igdomain 103 residues - 10543.7874 Da.

1

ALA

VAL

THR

ALA

ILE

THR

VAL

LYS

SER

ALA

2

GLY

ASN

VAL

THR

LEU

ASN

ARG

SER

ALA

3

THR

LEU

GLN

MET

SER

VAL

GLU

VAL

THR

PRO

4

SER

ALA

ARG

ASN

LYS

GLU

VAL

THR

TRP

5

ALA

ILE

THR

ALA

GLY

ASP

ALA

THR

ILE

6

ASN

ALA

THR

GLY

LEU

ARG

ALA

ASP

ALA

7

SER

LYS

THR

GLY

ALA

VAL

THR

VAL

GLU

ALA

8

THR

ALA

LYS

ASP

GLY

SER

GLY

VAL

LYS

GLY

9

THR

LYS

VAL

ILE

THR

VAL

THR

ALA

GLY

10

GLU

ASN

LEU

TYR

PHE

GLN

GLY

HIS

11

HIS

Samples:

Igdomain_13C15N: Igdomain, [U-100% 13C; U-100% 15N], 10.9 ± 0.5000 kg/m3; MES buffer 10.0 ± 0.0010 mM; MgCl2 2.0 ± 0.0001 mM; NaCl 100.0 ± 0.0050 mM

sample1: ionic strength: 0.110 M; pH: 6.500; pressure: 1.000 atm; temperature: 301.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	Igdomain_13C15N	isotropic	sample1
3D HN(CO)CA	Igdomain_13C15N	isotropic	sample1
Bruker_7_HNCOCACB (H[N[co[ca[CB]]]])	Igdomain_13C15N	isotropic	sample1
2D 1H-15N HSQC/HMQC	Igdomain_13C15N	isotropic	sample1
3D HNCA	Igdomain_13C15N	isotropic	sample1
3D HNCACB	Igdomain_13C15N	isotropic	sample1

Software:

CcpNmr_Analysis v2.3, CCPN - chemical shift assignment

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