BMRB Entry 15672

Title:
MMLV p12-CA(NTD)
Deposition date:
2008-02-24
Original release date:
2008-06-27
Authors:
Kyere, Sampson; Joseph, Prem Raj; Summers, Michael
Citation:

Citation: Kyere, Sampson; Joseph, Prem Raj; Summers, Michael. "The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct"  PLoS. ONE. 3, 1902-1902 (2008).
PubMed: 18382677

Assembly members:

Assembly members:
MMLV_p12CAN_protein, polymer, 224 residues, 24630.2 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts156
15N chemical shifts158
1H chemical shifts158

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 224 residues - 24630.2 Da.

Residues 217-224 represent a non-native affinity tag.

1   PROALALEUTHRPROSERLEUGLYALALYS
2   PROLYSPROGLNVALLEUSERASPSERGLY
3   GLYPROLEUILEASPLEULEUTHRGLUASP
4   PROPROPROTYRARGASPPROARGPROPRO
5   PROSERASPARGASPGLYASNGLYGLYGLU
6   ALATHRPROALAGLYGLUALAPROASPPRO
7   SERPROMETALASERARGLEUARGGLYARG
8   ARGGLUPROPROVALALAASPSERTHRTHR
9   SERGLNALAPHEPROLEUARGALAGLYGLY
10   ASNGLYGLNLEUGLNTYRTRPPROPHESER
11   SERSERASPLEUTYRASNTRPLYSASNASN
12   ASNPROSERPHESERGLUASPPROGLYLYS
13   LEUTHRALALEUILEGLUSERVALLEUILE
14   THRHISGLNPROTHRTRPASPASPCYSGLN
15   GLNLEULEUGLYTHRLEULEUTHRGLYGLU
16   GLULYSGLNARGVALLEULEUGLUALAARG
17   LYSALAVALARGGLYASPASPGLYARGPRO
18   THRGLNLEUPROASNGLUVALASPALAALA
19   PHEPROLEUGLUARGPROASPTRPASPTYR
20   THRTHRGLNALAGLYARGASNHISLEUVAL
21   HISTYRARGGLNLEULEULEUALAGLYLEU
22   GLNASNALAGLYARGSERHISHISHISHIS
23   HISHISHISHIS

Samples:

sample_1: MMLV p12CAN protein, [U-99% 13C; U-99% 15N], 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - data analysis, peak picking

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker AMX 600 MHz

Related Database Links:

EMBL CAA24507
GB AAA46499 AAB59942 AAB64159 AAC82566 AAC82568
PRF 0711245A
REF NP_057858 NP_057933 NP_057934 NP_955527 NP_955585
SP P03332 P03334 P03355 P32594 Q8UN02
AlphaFold P03332 P03334 P03355 P32594 Q8UN02

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