BMRB Entry 16057

Name: NMR structure of protein gp15 of bacteriophage SPP1
Published: 2009-05-20

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PDB ID: 2kbz
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16057
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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 protein gp15 of bacteriophage SPP1

Deposition date:

2008-12-12

Original release date:

2009-05-20

Authors:

Gallopin, Matthieu; Gilquin, Bernard; Zinn-Justin, Sophie

Citation:

Citation: Lhuillier, Sophie; Gallopin, Matthieu; Gilquin, Bernard; Brasiles, Sandrine; Lancelot, Nathalie; Letellier, Guillaume; Gilles, Mathilde; Dethan, Guillaume; Orlova, Elena; Couprie, Joel; Tavares, Paulo; Zinn-Justin, Sophie. "Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism for viral DNA gating" Proc. Natl. Acad. Sci. U.S.A. 106, 8507-8512 (2009).
PubMed: 19433794

Assembly members:

Assembly members:
gp15, polymer, 99 residues, 11270.051 Da.

Natural source:

Natural source: Common Name: Bacteriophage SPP1 Taxonomy ID: 10724 Superkingdom: Viruses Kingdom: not available Genus/species: Bacteriophage SPP1

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
gp15: QRVKRLLSITNDKHDEYLTE MVPLLVEFAKDECHNPFIDK DGNESIPSGVLIFVAKAAQF YMTNAGLTGRSMDTVSYNFA TEIPSTILKKLNPYRKMAR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	382
15N chemical shifts	93
1H chemical shifts	666

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 99 residues - 11270.051 Da.

1

GLN

ARG

VAL

LYS

ARG

LEU

SER

ILE

THR

2

ASN

ASP

LYS

HIS

ASP

GLU

TYR

LEU

THR

GLU

3

MET

VAL

PRO

LEU

VAL

GLU

PHE

ALA

LYS

4

ASP

GLU

CYS

HIS

ASN

PRO

PHE

ILE

ASP

LYS

5

ASP

GLY

ASN

GLU

SER

ILE

PRO

SER

GLY

VAL

6

LEU

ILE

PHE

VAL

ALA

LYS

ALA

GLN

PHE

7

TYR

MET

THR

ASN

ALA

GLY

LEU

THR

GLY

ARG

8

SER

MET

ASP

THR

VAL

SER

TYR

ASN

PHE

ALA

9

THR

GLU

ILE

PRO

SER

THR

ILE

LEU

LYS

10

LEU

ASN

PRO

TYR

ARG

LYS

MET

ALA

ARG

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D H-D exchange	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N nOe transfer	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1
3D HNCACB	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 HCCH COSY	sample_2	isotropic	sample_conditions_1
3D HCCH TOCSY	sample_2	isotropic	sample_conditions_1

PDB	2KBZ 5A20 5A21
EMBL	CAA61872 CAA66546
REF	NP_690676

BMRB Entry 16057

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: