BMRB Entry 50707

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50707

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Title:
Backbone 1H, 13C and 15N chemical shift assignments of the N-terminal Bro1 domain of human ALIX.
Deposition date:
2021-01-13
Original release date:
2021-10-06
Authors:
Elias, Ruben; Deshmukh, Lalit
Citation:

Citation: Elias, Ruben; Ramaraju, Bhargavi; Deshmukh, Lalit. "Mechanistic Roles of Tyrosine Phosphorylation in Reversible Amyloids, Autoinhibition, and Endosomal Membrane Association of ALIX"  J. Biol. Chem. 297, 101328-101328 (2021).
PubMed: 34688656

Assembly members:

Assembly members:
entity_1, polymer, 361 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):
entity_1: GHMATFISVQLKKTSEVDLA KPLVKFIQQTYPSGGEEQAQ YCRAAEELSKLRRAAVGRPL DKHEGALETLLRYYDQICSI EPKFPFSENQICLTFTWKDA FDKGSLFGGSVKLALASLGY EKSCVLFNCAALASQIAAEQ NLDNDEGLKIAAKHYQFASG AFLHIKETVLSALSREPTVD ISPDTVGTLSLIMLAQAQEV FFLKATRDKMKDAIIAKLAN QAADYFGDAFKQCQYKDTLP KEVFPVLAAKHCIMQANAEY HQSILAKQQKKFGEEIARLQ HAAELIKTVASRYDEYVNVK DFSDKINRALAAAKKDNDFI YHDRVPDLKDLDPIGKATLV KSTPVNVPISQKFTDLFEKM V

Data sets:
Data typeCount
13C chemical shifts904
15N chemical shifts302
1H chemical shifts302

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Bro1 domain of human ALIX1

Entities:

Entity 1, Bro1 domain of human ALIX 361 residues - Formula weight is not available

1   GLYHISMETALATHRPHEILESERVALGLN
2   LEULYSLYSTHRSERGLUVALASPLEUALA
3   LYSPROLEUVALLYSPHEILEGLNGLNTHR
4   TYRPROSERGLYGLYGLUGLUGLNALAGLN
5   TYRCYSARGALAALAGLUGLULEUSERLYS
6   LEUARGARGALAALAVALGLYARGPROLEU
7   ASPLYSHISGLUGLYALALEUGLUTHRLEU
8   LEUARGTYRTYRASPGLNILECYSSERILE
9   GLUPROLYSPHEPROPHESERGLUASNGLN
10   ILECYSLEUTHRPHETHRTRPLYSASPALA
11   PHEASPLYSGLYSERLEUPHEGLYGLYSER
12   VALLYSLEUALALEUALASERLEUGLYTYR
13   GLULYSSERCYSVALLEUPHEASNCYSALA
14   ALALEUALASERGLNILEALAALAGLUGLN
15   ASNLEUASPASNASPGLUGLYLEULYSILE
16   ALAALALYSHISTYRGLNPHEALASERGLY
17   ALAPHELEUHISILELYSGLUTHRVALLEU
18   SERALALEUSERARGGLUPROTHRVALASP
19   ILESERPROASPTHRVALGLYTHRLEUSER
20   LEUILEMETLEUALAGLNALAGLNGLUVAL
21   PHEPHELEULYSALATHRARGASPLYSMET
22   LYSASPALAILEILEALALYSLEUALAASN
23   GLNALAALAASPTYRPHEGLYASPALAPHE
24   LYSGLNCYSGLNTYRLYSASPTHRLEUPRO
25   LYSGLUVALPHEPROVALLEUALAALALYS
26   HISCYSILEMETGLNALAASNALAGLUTYR
27   HISGLNSERILELEUALALYSGLNGLNLYS
28   LYSPHEGLYGLUGLUILEALAARGLEUGLN
29   HISALAALAGLULEUILELYSTHRVALALA
30   SERARGTYRASPGLUTYRVALASNVALLYS
31   ASPPHESERASPLYSILEASNARGALALEU
32   ALAALAALALYSLYSASPASNASPPHEILE
33   TYRHISASPARGVALPROASPLEULYSASP
34   LEUASPPROILEGLYLYSALATHRLEUVAL
35   LYSSERTHRPROVALASNVALPROILESER
36   GLNLYSPHETHRASPLEUPHEGLULYSMET
37   VAL

Samples:

sample_1: Bro1 domain of human ALIX, [U-13C; U-15N; U-2H], 0.75 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CcpNMR - data analysis

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UNP Q8WUM4
AlphaFold Q9UKL5

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