BMRB Entry 18566

Title:
Telokin-like domain (TL-domain) from P22 coat protein
Deposition date:
2012-07-03
Original release date:
2012-11-02
Authors:
Rizzo, Alessandro; Fraser, LaTasha; Sheftic, Sarah; Suhanovsky, Margaret; Teschke, Carolyn; Alexandrescu, Andrei
Citation:

Citation: Rizzo, Alessandro; Fraser, LaTasha; Sheftic, Sarah; Suhanovsky, Margaret; Teschke, Carolyn; Alexandrescu, Andrei. "NMR assignments for the telokin-like domain of bacteriophage P22 coat protein."  Biomol. NMR Assignments 7, 257-260 (2013).
PubMed: 22987227

Assembly members:

Assembly members:
TL-domain, polymer, 124 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Enterobacteria phage P22   Taxonomy ID: 10754   Superkingdom: Viruses   Kingdom: not available   Genus/species: Bacteriophage P22

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30b

Data sets:
Data typeCount
13C chemical shifts511
15N chemical shifts119
1H chemical shifts804

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TL-domain1

Entities:

Entity 1, TL-domain 124 residues - Formula weight is not available

G222 is non-native glycine that was included as part of the thrombin cleavage site. but for the sake of the numbering scheme is included here as 222

1   GLYSERTHRALATHRGLYILETHRVALSER
2   GLYALAGLNSERPHELYSPROVALALATRP
3   GLNLEUASPASNASPGLYASNLYSVALASN
4   VALASPASNARGPHEALATHRVALTHRLEU
5   SERALATHRTHRGLYMETLYSARGGLYASP
6   LYSILESERPHEALAGLYVALLYSPHELEU
7   GLYGLNMETALALYSASNVALLEUALAGLN
8   ASPALATHRPHESERVALVALARGVALVAL
9   ASPGLYTHRHISVALGLUILETHRPROLYS
10   PROVALALALEUASPASPVALSERLEUSER
11   PROGLUGLNARGALATYRALAASNVALASN
12   THRSERLEUALAASPALAMETALAVALASN
13   ILELEUASNVAL

Samples:

TL-domain-13C_15N: TL-domain, [U-13C; U-15N], 1.5 mM; sodium phosphate 20 mM; sodium azide 0.2 % w/v

TL-domain-13C_15N_in_D2O: TL-domain, [U-13C; U-15N], 1.5 mM; sodium phosphate 20 mM; sodium azide 0.2 % w/v

TL-domain-15N: TL-domain, [U-15N], 1.5 mM; sodium phosphate 20 mM; sodium azide 0.2 % w/v

TL-domain-unlabelled: TL-domain 1.5 mM; sodium phosphate 20 mM; sodium azide 0.2 % w/v

sample_condition_1: ionic strength: 20 mM; pH: 6.00; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCTL-domain-15Nisotropicsample_condition_1
2D 1H-13C HSQCTL-domain-13C_15N_in_D2Oisotropicsample_condition_1
2D DQF-COSYTL-domain-unlabelledisotropicsample_condition_1
2D DQF-TOCSYTL-domain-unlabelledisotropicsample_condition_1
3D C(CO)NHTL-domain-13C_15Nisotropicsample_condition_1
3D HNCOTL-domain-13C_15Nisotropicsample_condition_1
3D HNCATL-domain-13C_15Nisotropicsample_condition_1
3D HNCACBTL-domain-13C_15Nisotropicsample_condition_1
3D HN(CO)CATL-domain-13C_15Nisotropicsample_condition_1
3D H(CCO)NHTL-domain-13C_15Nisotropicsample_condition_1
3D HCCH-TOCSYTL-domain-13C_15N_in_D2Oisotropicsample_condition_1
3D HNHATL-domain-15Nisotropicsample_condition_1
3D 1H-15N NOESYTL-domain-15Nisotropicsample_condition_1
3D 1H-15N NOESYTL-domain-15Nisotropicsample_condition_1
3D HNHBTL-domain-15Nisotropicsample_condition_1
3D HN(CA)COTL-domain-13C_15Nisotropicsample_condition_1
2D H-H NOESY (50ms)TL-domain-unlabelledisotropicsample_condition_1
3D CCH-TOCSYTL-domain-13C_15N_in_D2Oisotropicsample_condition_1

Software:

FELIX, Accelrys Software Inc. - processing

ANALYSIS, CCPN - chemical shift assignment

VNMRJ, Varian - collection

NMR spectrometers:

  • Varian Inova 600 MHz

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