BMRB Entry 54025

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR54025

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Title:
1H, 13C, and 15N backbone resonance assignments of zinc-a2-glycoprotein (ZAG), a lipid-mobilizing protein structurally related to class I HLA molecules
Deposition date:
2026-09-18
Original release date:
2026-09-24
Authors:
Corbin, Elizabeth; Miles, Uri; McShan, Andrew
Citation:

Citation: Corbin, Elizabeth; Miles, Uri; McShan, Andrew. "1H, 13C, and 15N backbone resonance assignments of zinc-a2-glycoprotein, a lipid-mobilizing protein structurally related to class I HLA molecules "  .

Assembly members:

Assembly members:
entity_1, polymer, 279 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: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MQENQDGRYSLTYIYTGLSK HVEDVPAFQALGSLNDLQFF RYNSKDRKSQPMGLWRQVEG MEDWKQDSQLQKAREDIFME TLKDIVEYYNDSNGSHVLQG RFGCEIENNRSSGAFWKYYY DGKDYIEFNKEIPAWVPFDP AAQITKQKWEAEPVYVQRAK AYLEEECPATLRKYLKYSKN ILDRQDPPSVVVTSHQAPGE KKKLKCLAYDFYPGKIDVHW TRAGEVQEPELRGDVLHNGN GTYQSWVVVAVPPQDTAPYS CHVQHSSLAQPLVVPWEAS

Data sets:
Data typeCount
13C chemical shifts767
15N chemical shifts246
1H chemical shifts246

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ZAG1

Entities:

Entity 1, ZAG 279 residues - Formula weight is not available

1   METGLNGLUASNGLNASPGLYARGTYRSER
2   LEUTHRTYRILETYRTHRGLYLEUSERLYS
3   HISVALGLUASPVALPROALAPHEGLNALA
4   LEUGLYSERLEUASNASPLEUGLNPHEPHE
5   ARGTYRASNSERLYSASPARGLYSSERGLN
6   PROMETGLYLEUTRPARGGLNVALGLUGLY
7   METGLUASPTRPLYSGLNASPSERGLNLEU
8   GLNLYSALAARGGLUASPILEPHEMETGLU
9   THRLEULYSASPILEVALGLUTYRTYRASN
10   ASPSERASNGLYSERHISVALLEUGLNGLY
11   ARGPHEGLYCYSGLUILEGLUASNASNARG
12   SERSERGLYALAPHETRPLYSTYRTYRTYR
13   ASPGLYLYSASPTYRILEGLUPHEASNLYS
14   GLUILEPROALATRPVALPROPHEASPPRO
15   ALAALAGLNILETHRLYSGLNLYSTRPGLU
16   ALAGLUPROVALTYRVALGLNARGALALYS
17   ALATYRLEUGLUGLUGLUCYSPROALATHR
18   LEUARGLYSTYRLEULYSTYRSERLYSASN
19   ILELEUASPARGGLNASPPROPROSERVAL
20   VALVALTHRSERHISGLNALAPROGLYGLU
21   LYSLYSLYSLEULYSCYSLEUALATYRASP
22   PHETYRPROGLYLYSILEASPVALHISTRP
23   THRARGALAGLYGLUVALGLNGLUPROGLU
24   LEUARGGLYASPVALLEUHISASNGLYASN
25   GLYTHRTYRGLNSERTRPVALVALVALALA
26   VALPROPROGLNASPTHRALAPROTYRSER
27   CYSHISVALGLNHISSERSERLEUALAGLN
28   PROLEUVALVALPROTRPGLUALASER

Samples:

sample_1: Zinc-a2-glycoprotein (ZAG), [U-100% 13C; U-100% 15N; U-100% 2H], 600 uM; NaCl 100 mM; sodium phosphate 20 mM; EDTA 1 mM; NaN3 0.02 % w/v

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_1isotropicsample_conditions_1

Software:

NMRbox - data analysis

SPARKY - chemical shift assignment

TALOS-N - data analysis

NMRPipe - chemical shift assignment

TOPSPIN - collection

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Related Database Links:

UNP P25311
AlphaFold P25311

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