BMRB Entry 18475

Name: The solution structure of Phage P2 gpX
Published: 2013-05-20

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PDB ID: 2ltf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18475
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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:

The solution structure of Phage P2 gpX

Deposition date:

2012-05-22

Original release date:

2013-05-20

Authors:

Maxwell, Karen; Bona, Diane; Chang, Tom; Edwards, Aled; Davidson, Alan

Citation:

Citation: Maxwell, Karen; Fatehi Hassanabad, Mostafa; Chang, Tom; Pirani, Nawaz; Bona, Diane; Edwards, Aled; Davidson, Alan. "Structural and functional studies of gpX of Escherichia coli phage P2 reveal a widespread role for LysM domains in the baseplates of contractile-tailed phages." J. Bacteriol. 195, 5461-5468 (2013).
PubMed: 24097944

Assembly members:

Assembly members:
P2_gpX, polymer, 71 residues, 7591.617 Da.

Natural source:

Natural source: Common Name: Bacteriophage P2 Taxonomy ID: 10679 Superkingdom: Viruses Kingdom: not available Genus/species: Bacteriophage P2

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
P2_gpX: MKTFALQGDTLDAICVRYYG RTEGVVETVLAANPGLAELG AVLPHGTAVELPDVQTAPVA ETVNLWEVEHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	208
15N chemical shifts	68
1H chemical shifts	462

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	P2_gpX	1

Entities:

Entity 1, P2_gpX 71 residues - 7591.617 Da.

1

MET

LYS

THR

PHE

ALA

LEU

GLN

GLY

ASP

THR

2

LEU

ASP

ALA

ILE

CYS

VAL

ARG

TYR

GLY

3

ARG

THR

GLU

GLY

VAL

GLU

THR

VAL

LEU

4

ALA

ASN

PRO

GLY

LEU

ALA

GLU

LEU

GLY

5

ALA

VAL

LEU

PRO

HIS

GLY

THR

ALA

VAL

GLU

6

LEU

PRO

ASP

VAL

GLN

THR

ALA

PRO

VAL

ALA

7

GLU

THR

VAL

ASN

LEU

TRP

GLU

VAL

GLU

HIS

8

HIS

Name	Sample	Sample state	Sample conditions
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
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

PDB	2LTF
DBJ	BAP10043 BAT37380 BAT38781 GAL53203
EMBL	CAC43076 CAC43081 CAC43090 CAC43095 CAC43100
GB	AAD03274 AAN28225 AAO64727 AAP04444 ACB19449
REF	NP_046763 NP_839856 WP_000846398 WP_000846399 WP_000846400
SP	P51772
AlphaFold	P51772

BMRB Entry 18475

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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