BMRB Entry 16992

Title:
1H,13C,15N backbone and sidechain assignment of human Raf kinase inhibitor protein from Escherichia coli
Deposition date:
2010-06-09
Original release date:
2010-10-14
Authors:
Cuiying, Yi
Citation:

Citation: Yi, Cuiying; Peng, Yu; Guo, Chenyun; Lin, Donghai. "(1)H, ( 13)C, ( 15)N backbone and side-chain resonance assignments of the human Raf-1 kinase inhibitor protein."  Biomol. NMR Assignments 5, 63-66 (2011).
PubMed: 20924725

Assembly members:

Assembly members:
RKIP, polymer, 202 residues, Formula weight is not available

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: PET28a

Data sets:
Data typeCount
13C chemical shifts722
15N chemical shifts172
1H chemical shifts1172

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RKIP1

Entities:

Entity 1, RKIP 202 residues - Formula weight is not available

1   METSERTYRTYRHISHISHISHISHISHIS
2   GLUGLYVALARGTHRMETPROVALASPLEU
3   SERLYSTRPSERGLYPROLEUSERLEUGLN
4   GLUVALASPGLUGLNPROGLNHISPROLEU
5   HISVALTHRTYRALAGLYALAALAVALASP
6   GLULEUGLYLYSVALLEUTHRPROTHRGLN
7   VALLYSASNARGPROTHRSERILESERTRP
8   ASPGLYLEUASPSERGLYLYSLEUTYRTHR
9   LEUVALLEUTHRASPPROASPALAPROSER
10   ARGLYSASPPROLYSTYRARGGLUTRPHIS
11   HISPHELEUVALVALASNMETLYSGLYASN
12   ASPILESERSERGLYTHRVALLEUSERASP
13   TYRVALGLYSERGLYPROPROLYSGLYTHR
14   GLYLEUHISARGTYRVALTRPLEUVALTYR
15   GLUGLNASPARGPROLEULYSCYSASPGLU
16   PROILELEUSERASNARGSERGLYASPHIS
17   ARGGLYLYSPHELYSVALALASERPHEARG
18   LYSLYSTYRGLULEUARGALAPROVALALA
19   GLYTHRCYSTYRGLNALAGLUTRPASPASP
20   TYRVALPROLYSLEUTYRGLUGLNLEUSER
21   GLYLYS

Samples:

sample_1: acetic acid 200 mM; H2O 95%; D2O 5%; RKIP, [U-100% 13C; U-100% 15N], 3 mM; DTT 5 mM

sample_conditions_1: ionic strength: 0.4 M; pH: 4.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 17382 18204
PDB
DBJ BAA03684 BAE88027 BAE88359 BAG34868 BAG61396
EMBL CAA51652 CAA53031 CAA59404 CAH93256
GB AAB32876 AAD14234 AAH08714 AAH17396 AAH31102
PRF 2117380B
REF NP_001126915 NP_001233128 NP_002558 XP_002753109 XP_004054017
SP P30086 P48737 Q5R4R0
AlphaFold Q5R4R0 P48737 P30086

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