BMRB Entry 18760

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR18760

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Title:
Backbone 15N, 1H, and CA Chemical Shift Assignments for Y254L/T257A IkappaBalpha (67-287)
Deposition date:
2012-10-02
Original release date:
2013-02-07
Authors:
Cervantes, Carla; Handley, Lindsey; Komives, Elizabeth
Citation:

Citation: Cervantes, Carla; Handley, Lindsey; Sue, Shih-Che; Dyson, H. Jane; Komives, Elizabeth. "Long-Range Effects and Functional Consequences of Stabilizing Mutations in the Ankyrin Repeat Domain of IB."  J. Mol. Biol. 425, 902-913 (2013).
PubMed: 23274114

Assembly members:

Assembly members:
YLTA_IkappaBalpha, polymer, 221 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: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YLTA_IkappaBalpha: KQQLTEDGDSFLHLAIIHEE KALTMEVIRQVKGDLAFLNF QNNLQQTPLHLAVITNQPEI AEALLGAGCDPELRDFRGNT PLHLACEQGCLASVGVLTQS CTTPHLHSILKATNYNGHTC LHLASIHGYLGIVELLVSLG ADVNAQEPCNGRTALHLAVD LQNPDLVSLLLKCGADVNRV TYQGYSPLQLAWGRPSTRIQ QQLGQLTLENLQMLPESEDE E

Data sets:
Data typeCount
13C chemical shifts201
15N chemical shifts188
1H chemical shifts188

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YLTA IkappaBalpha1

Entities:

Entity 1, YLTA IkappaBalpha 221 residues - Formula weight is not available

This is the native human IkappaBalpha (67-287), except with consensus mutations at Y254 and T257.

1   LYSGLNGLNLEUTHRGLUASPGLYASPSER
2   PHELEUHISLEUALAILEILEHISGLUGLU
3   LYSALALEUTHRMETGLUVALILEARGGLN
4   VALLYSGLYASPLEUALAPHELEUASNPHE
5   GLNASNASNLEUGLNGLNTHRPROLEUHIS
6   LEUALAVALILETHRASNGLNPROGLUILE
7   ALAGLUALALEULEUGLYALAGLYCYSASP
8   PROGLULEUARGASPPHEARGGLYASNTHR
9   PROLEUHISLEUALACYSGLUGLNGLYCYS
10   LEUALASERVALGLYVALLEUTHRGLNSER
11   CYSTHRTHRPROHISLEUHISSERILELEU
12   LYSALATHRASNTYRASNGLYHISTHRCYS
13   LEUHISLEUALASERILEHISGLYTYRLEU
14   GLYILEVALGLULEULEUVALSERLEUGLY
15   ALAASPVALASNALAGLNGLUPROCYSASN
16   GLYARGTHRALALEUHISLEUALAVALASP
17   LEUGLNASNPROASPLEUVALSERLEULEU
18   LEULYSCYSGLYALAASPVALASNARGVAL
19   THRTYRGLNGLYTYRSERPROLEUGLNLEU
20   ALATRPGLYARGPROSERTHRARGILEGLN
21   GLNGLNLEUGLYGLNLEUTHRLEUGLUASN
22   LEUGLNMETLEUPROGLUSERGLUASPGLU
23   GLU

Samples:

YLTA_IkappaBalpha_3x-labelled: YLTA IkappaBalpha, [U-13C; U-15N; U-2H], 0.1 mM; sodium chloride 50 mM; 2H-Tris, [U-99% 2H], 25 mM; EDTA 1 mM; CHAPS 5 mM; sodium azide 2 mM; DTT 2 mM; protease inhibitor cocktail 1%; D2O, [U-100% 2H], 10%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAYLTA_IkappaBalpha_3x-labelledisotropicsample_conditions_1
3D HN(CO)CAYLTA_IkappaBalpha_3x-labelledisotropicsample_conditions_1
3D HNCACBYLTA_IkappaBalpha_3x-labelledisotropicsample_conditions_1

Software:

NMRView, One Moon Scientific, Inc. - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18756 18759
PDB
DBJ BAE89638 BAG36213 BAI46793
EMBL CAB65556
GB AAA16489 AAH02601 AAH04983 AAK51149 AAP35754
REF NP_001244679 NP_001271861 NP_065390 XP_002753867 XP_002824720
SP P25963
AlphaFold P25963

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