BMRB Entry 27201

Title:
Partial solid-state NMR assignment of bacteriophage tail protein pb6 (C-ter domain assigned)
Deposition date:
2017-08-05
Original release date:
2017-09-05
Authors:
Schanda, Paul; Krichel, Carsten; Arnaud, Charles-Adrien; Breyton, Cecile
Citation:

Citation: Fraga, Hugo; Arnaud, Charles-Adrien; Gauto, Diego; Audin, Maxime; Kurauskas, Vilius; Macek, Pavel; Krichel, Carsten; Guan, Jia-Ying; Boisbouvier, Jerome; Sprangers, Remco; Breyton, Cecile; Schanda, Paul. "Solid-State NMR H-N-(C)-H and H-N-C-C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins."  Chemphyschem 18, 2697-2703 (2017).
PubMed: 28792111

Assembly members:

Assembly members:
PB6_full_length, polymer, 464 residues, 50405.3222 Da.

Natural source:

Natural source:   Common Name: Enterobacteria phage T5   Taxonomy ID: 10726   Superkingdom: Viruses   Kingdom: not available   Genus/species: Bacteriophage T5

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pb6-pLIM13

Data sets:
Data typeCount
13C chemical shifts202
15N chemical shifts81
1H chemical shifts81

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PB6 full length1

Entities:

Entity 1, PB6 full length 464 residues - 50405.3222 Da.

1   METSERLEUGLNLEULEUARGASNTHRARG
2   ILEPHEVALSERTHRVALLYSTHRGLYHIS
3   ASNLYSTHRASNTHRGLNGLUILELEUVAL
4   GLNASPASPILESERTRPGLYGLNASPSER
5   ASNSERTHRASPILETHRVALASNGLUALA
6   GLYPROARGPROTHRARGGLYSERLYSARG
7   PHEASNASPSERLEUASNALAALAGLUTRP
8   SERPHESERTHRTYRILELEUPROTYRLYS
9   ASPLYSASNTHRSERLYSGLNILEVALPRO
10   ASPTYRMETLEUTRPHISALALEUSERSER
11   GLYARGALAILEASNLEUGLUGLYTHRTHR
12   GLYALAHISASNASNALATHRASNPHEMET
13   VALASNPHELYSASPASNSERTYRHISGLU
14   LEUALAMETLEUHISILETYRILELEUTHR
15   ASPLYSTHRTRPSERTYRILEASPSERCYS
16   GLNILEASNGLNALAGLUVALASNVALASP
17   ILEGLUASPILEGLYARGVALTHRTRPSER
18   GLYASNGLYASNGLNLEUILEPROLEUASP
19   GLUGLNPROPHEASPPROASPGLNILEGLY
20   ILEASPASPGLUTHRTYRMETTHRILEGLN
21   GLYSERTYRILELYSASNLYSLEUTHRILE
22   LEULYSILELYSASPMETASPTHRASNLYS
23   SERTYRASPILEPROILETHRGLYGLYTHR
24   PHETHRILEASNASNASNILETHRTYRLEU
25   THRPROASNVALMETSERARGVALTHRILE
26   PROILEGLYSERPHETHRGLYALAPHEGLU
27   LEUTHRGLYSERLEUTHRALATYRLEUASN
28   ASPLYSSERLEUGLYSERMETGLULEUTYR
29   LYSASPLEUILELYSTHRLEULYSVALVAL
30   ASNARGPHEGLUILEALALEUVALLEUGLY
31   GLYGLUTYRASPASPGLUARGPROALAALA
32   ILELEUVALALALYSGLNALAHISVALASN
33   ILEPROTHRILEGLUTHRASPASPVALLEU
34   GLYTHRSERVALGLUPHELYSALAILEPRO
35   SERASPLEUASPALAGLYASPGLUGLYTYR
36   LEUGLYPHESERSERLYSTYRTHRARGTHR
37   THRILEASNASNLEUILEVALASNGLYASP
38   GLYALATHRASPALAVALTHRALAILETHR
39   VALLYSSERALAGLYASNVALTHRTHRLEU
40   ASNARGSERALATHRLEUGLNMETSERVAL
41   GLUVALTHRPROSERSERALAARGASNLYS
42   GLUVALTHRTRPALAILETHRALAGLYASP
43   ALAALATHRILEASNALATHRGLYLEULEU
44   ARGALAASPALASERLYSTHRGLYALAVAL
45   THRVALGLUALATHRALALYSASPGLYSER
46   GLYVALLYSGLYTHRLYSVALILETHRVAL
47   THRALAGLYGLY

Samples:

sample_1: PB6 full length, [U-13C; U-15N; U-2H], 2.5 mg; Sodium chloride 100 mM; Tris 20 mM

sample_conditions_1: ionic strength: 0.120 M; pH: 6.9; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
fibers_hCANH_DCN_950 (H[N_[CA]].onebond)sample_1isotropicsample_conditions_1
fibers_hCANH_DCNILV (H[N_[CA]].onebond)sample_1isotropicsample_conditions_1
fibers_hCOCANH_DCNILV (H[N_[CA[CO]]].onebond)sample_1isotropicsample_conditions_1
fibers_hCOCAcoNH_DCNILV (H[N[CO[CA]]])sample_1isotropicsample_conditions_1
fibers_HcacoNH_DCNILV (HcacoNH)sample_1isotropicsample_conditions_1
fibers_HcocaNH_DCNILV (HNcocanH)sample_1isotropicsample_conditions_1
fibers_HCAcoNH_4D_DCNILV (HCAcoNH)sample_1isotropicsample_conditions_1
fibers_hCOcaNH_DCNILV (H[N_[ca[CO]]].onebond)sample_1isotropicsample_conditions_1
fibers_4DHCAcoNH_DCNILV (HCAcoNH)sample_1isotropicsample_conditions_1
fibers_NCACB_DCNILV (N_CA_CB.onebond,relayed-alternate)sample_1isotropicsample_conditions_1
fibers_NCACX (N_CA_C.onebond,relayed)sample_1isotropicsample_conditions_1

Software:

CcpNmr_Analysis v2.3, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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