BMRB Entry 18475

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

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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:
Data typeCount
13C chemical shifts208
15N chemical shifts68
1H chemical shifts462

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1P2_gpX1

Entities:

Entity 1, P2_gpX 71 residues - 7591.617 Da.

1   METLYSTHRPHEALALEUGLNGLYASPTHR
2   LEUASPALAILECYSVALARGTYRTYRGLY
3   ARGTHRGLUGLYVALVALGLUTHRVALLEU
4   ALAALAASNPROGLYLEUALAGLULEUGLY
5   ALAVALLEUPROHISGLYTHRALAVALGLU
6   LEUPROASPVALGLNTHRALAPROVALALA
7   GLUTHRVALASNLEUTRPGLUVALGLUHIS
8   HIS

Samples:

sample_1: P2_gpX, [U-100% 13C; U-100% 15N], 1.1 mM; sodium phosphate 25 mM; sodium chloride 200 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_2: P2 gpX, [U-100% 13C; U-100% 15N], 1.1 mM; sodium phosphate 25 mM; sodium chloride 200 mM; DTT 2 mM; D2O 100%

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert P. - refinement

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
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

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