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The solution structure of Phage P2 gpX
Authors
Maxwell, K.L., Bona, D., Chang, T.L., Edwards, A.M., Davidson, A.R.
Assembly
P2 gpX
Entity
1. P2 gpX (polymer), 71 monomers, 7585.488 Da Detail

MKTFALQGDT LDAICVRYYG RTEGVVETVL AANPGLAELG AVLPHGTAVE LPDVQTAPVA ETVNLWEVEH H


Formula weight
7585.488 Da
Source organism
Escherichia virus P2
Exptl. method
solution NMR
Refine. method
distance geometry
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 81.1 %, Completeness (bb): 80.4 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All81.1 % (625 of 771)88.1 % (342 of 388)69.1 % (215 of 311)94.4 % (68 of 72)
Backbone80.4 % (336 of 418)92.4 % (133 of 144)66.2 % (137 of 207)98.5 % (66 of 67)
Sidechain83.7 % (350 of 418)85.7 % (209 of 244)82.2 % (139 of 169)40.0 % (2 of 5)
Aromatic44.0 % (22 of 50)64.0 % (16 of 25)20.8 % (5 of 24)100.0 % (1 of 1)
Methyl94.4 % (102 of 108)92.6 % (50 of 54)96.3 % (52 of 54)

1. P2 gpX

MKTFALQGDT LDAICVRYYG RTEGVVETVL AANPGLAELG AVLPHGTAVE LPDVQTAPVA ETVNLWEVEH H

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 6.8


#NameIsotope labelingTypeConcentration
1P2_gpX[U-100% 13C; U-100% 15N]1.1 mM
2sodium phosphatenatural abundance25 mM
3sodium chloridenatural abundance200 mM
4DTTnatural abundance2 mM
5H2Onatural abundance90 %
6D2Onatural abundance10 %
Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 273 K, pH 6.8


#NameIsotope labelingTypeConcentration
7P2 gpX[U-100% 13C; U-100% 15N]1.1 mM
8sodium phosphatenatural abundance25 mM
9sodium chloridenatural abundance200 mM
10DTTnatural abundance2 mM
11D2Onatural abundance100 %

LACS Plot; CA
Referencing offset: -0.11 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.11 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.01 ppm, Outliers: 1 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 2LTF, Strand ID: A Detail


Release date
2013-05-19
Citation
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
Maxwell, K.L., Fatehi Hassanabad, M., Chang, T., Pirani, N., Bona, D., Edwards, A.M., Davidson, A.R.
J. Bacteriol. (2013), 195, 5461-5468, PubMed 24097944 , DOI 10.1128/JB.00805-13 ,
Entries sharing articles Swiss-Prot: 1 entries Detail
  Swiss-Prot: P08557 released on 1988-08-01
    Title CIRCN_BPMU Entity DNA circularization protein N
Related entities 1. P2 gpX, : 1 : 1 : 4 entities Detail
Experiments performed 14 experiments Detail
NMR combined restraints 3 contents Detail
Keywords LysM, Phage P2, phage tail