BMRB Entry 15059

Title:
1H, 13C, and 15N Chemical Shift Assignments for the muscular LIM protein MLP/CRP3.
Deposition date:
2006-11-30
Original release date:
2007-06-26
Authors:
Thomas, Schallus; Claudia, Muhle-Goll
Citation:

Citation: Schallus, Thomas; Edlich, Christian; Stier, Gunter; Muhle-Goll, Claudia. "1H, 13C, and 15N assignment of the muscular LIM protein MLP/CRP3"  Biomol. NMR Assignments 1, 41-43 (2007).
PubMed: 19636821

Assembly members:

Assembly members:
MLP, polymer, 194 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24

Data sets:
Data typeCount
13C chemical shifts485
15N chemical shifts163
1H chemical shifts852

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MLP1
2ZINC (II) ION, 12
3ZINC (II) ION, 22
4ZINC (II) ION, 32
5ZINC (II) ION, 42

Entities:

Entity 1, MLP 194 residues - Formula weight is not available

1   METALAASNTRPGLYGLYGLYALALYSCYS
2   GLYALACYSGLULYSTHRVALTYRHISALA
3   GLUGLUILEGLNCYSASNGLYARGSERPHE
4   HISLYSTHRCYSPHEHISCYSMETALACYS
5   ARGLYSALALEUASPSERTHRTHRVALALA
6   ALAHISGLUSERGLUILETYRCYSLYSVAL
7   CYSTYRGLYARGARGTYRGLYPROLYSGLY
8   ILEGLYTYRGLYGLNGLYALAGLYCYSLEU
9   SERTHRASPTHRGLYGLUHISLEUGLYLEU
10   GLNPHEGLNGLNSERPROLYSPROALAARG
11   SERVALTHRTHRSERASNPROSERLYSPHE
12   THRALALYSPHEGLYGLUSERGLULYSCYS
13   PROARGCYSGLYLYSSERVALTYRALAALA
14   GLULYSVALMETGLYGLYGLYLYSPROTRP
15   HISLYSTHRCYSPHEARGCYSALAILECYS
16   GLYLYSSERLEUGLUSERTHRASNVALTHR
17   ASPLYSASPGLYGLULEUTYRCYSLYSVAL
18   CYSTYRALALYSASNPHEGLYPROTHRGLY
19   ILEGLYPHEGLYGLYLEUTHRGLNGLNVAL
20   GLULYSLYSGLU

Entity 2, ZINC (II) ION, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: MLP, [U-100% 13C; U-100% 15N], 1.0 mM; ZINC (II) ION, none, 1.0 mM; KHPO4, none, 20 mM; KCl, none, 150 mM; DTT, none, 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

DBJ BAA13721 BAB22580 BAB27741 BAG36097 BAI46094
EMBL CAA90039
GB AAA91104 AAA92571 AAD00183 AAD00189 AAF28868
REF NP_001165839 NP_001185770 NP_003467 NP_038836 XP_001095430
SP P50461 P50462
AlphaFold P50461 P50462 P50461 P50462

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