BMRB Entry 26844

Name: NMR assignments for the insertion domain of bacteriophage Sf6 coat protein
Published: 2018-10-03

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PDB ID: 6mpo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26844
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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 assignments for the insertion domain of bacteriophage Sf6 coat protein

Deposition date:

2016-07-05

Original release date:

2018-10-03

Authors:

Tripler, Therese; Teschke, Carolyn; Alexandrescu, Andrei

Citation:

Citation: Tripler, Therese; Teschke, Carolyn; Alexandresu, Andrei. "NMR assignments for the insertion domain of bacteriophage Sf6 coat protein" Biomol. NMR Assignments 11, 35-38 (2017).
PubMed: 27798771

Assembly members:

Assembly members:
Sf6id, polymer, 124 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Sf6 Bacteriophage Taxonomy ID: 38018 Superkingdom: Virsues Kingdom: not available Genus/species: Sf6 Bacteriophage

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Shigella flexneri Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Sf6id: GAFGGTLTVKTQPTVTYNAV KDSYQFTVTLTGATASVTGF LKAGDQVKFTNTYWLQQQTK QALYNGATPISFTATVTADA NSDSGGDVTVTLSGVPIYDT TNPQYNSVSRQVEAGDAVSV VGTA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	448
15N chemical shifts	132
1H chemical shifts	754

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Sf6id	1

Entities:

Entity 1, Sf6id 124 residues - Formula weight is not available

contains C-terminal 6x his-tag

1

GLY

ALA

PHE

GLY

THR

LEU

THR

VAL

LYS

2

THR

GLN

PRO

THR

VAL

THR

TYR

ASN

ALA

VAL

3

LYS

ASP

SER

TYR

GLN

PHE

THR

VAL

THR

LEU

4

THR

GLY

ALA

THR

ALA

SER

VAL

THR

GLY

PHE

5

LEU

LYS

ALA

GLY

ASP

GLN

VAL

LYS

PHE

THR

6

ASN

THR

TYR

TRP

LEU

GLN

THR

LYS

7

GLN

ALA

LEU

TYR

ASN

GLY

ALA

THR

PRO

ILE

8

SER

PHE

THR

ALA

THR

VAL

THR

ALA

ASP

ALA

9

ASN

SER

ASP

SER

GLY

ASP

VAL

THR

VAL

10

THR

LEU

SER

GLY

VAL

PRO

ILE

TYR

ASP

THR

11

THR

ASN

PRO

GLN

TYR

ASN

SER

VAL

SER

ARG

12

GLN

VAL

GLU

ALA

GLY

ASP

ALA

VAL

SER

VAL

13

VAL

GLY

THR

ALA

Samples:

sample_1: insertion domain, [U-100% 15N], 1.5 mM; insertion domain, [U-100% 13C; U-100% 15N], 2.1 mM; H2O 90%; D2O 10%

sample_2: insertion domain, [U-100% 13C; U-100% 15N], 2.1 mM; D2O 100%

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC NH2 only	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
HNCACO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

Software:

Ccpnmr_analysis, CCPN - chemical shift assignment, peak picking

Felix, Accelrys Software Inc. - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 600 MHz

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