BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15617

Title: Northeast Structural Genomics Consortium Target YG1 (Alg13), Chemical Shift Assignments   PubMed: 18547528

Deposition date: 2008-01-04 Original release date: 2008-01-24

Authors: Wang, Xu; Weldeghorghis, Thomas; Zhang, Gufeng; Imepriali, Barbara; Montelione, Gaetano; Prestegard, James

Citation: Wang, Xu; Weldeghorghis, Thomas; Zhang, Gufeng; Imepriali, Barbara; Prestegard, James. "Solution Structure of Alg13: The Sugar Donor Subunit of a Yeast N-Acetylglucosamine Transferase"  Structure 16, 965-975 (2008).

Assembly members:
Alg13, polymer, 224 residues, 25066.6 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
Alg13: MGSSHHHHHHSSGLVPRGSH MLEGIIEEKALFVTCGATVP FPKLVSCVLSDEFCQELIQY GFVRLIIQFGRNYSSEFEHL VQERGGQRESQKIPIDQFGC GDTARQYVLMNGKLKVIGFD FSTKMQSIIRDYSDLVISHA GTGSILDSLRLNKPLIVCVN DSLMDNHQQQIADKFVELGY VWSCAPTETGLIAGLRASQT EKLKPFPVSHNPSFERLLVE TIYS

Data sets:
Data typeCount
13C chemical shifts668
15N chemical shifts189
1H chemical shifts754
residual dipolar couplings115

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1alg131

Entities:

Entity 1, alg13 224 residues - 25066.6 Da.

The first 23 residues of the protein are part of a His-Thrombin cleavage site tag. Alg13 starts at G24

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METLEUGLUGLYILEILEGLUGLULYSALA
4   LEUPHEVALTHRCYSGLYALATHRVALPRO
5   PHEPROLYSLEUVALSERCYSVALLEUSER
6   ASPGLUPHECYSGLNGLULEUILEGLNTYR
7   GLYPHEVALARGLEUILEILEGLNPHEGLY
8   ARGASNTYRSERSERGLUPHEGLUHISLEU
9   VALGLNGLUARGGLYGLYGLNARGGLUSER
10   GLNLYSILEPROILEASPGLNPHEGLYCYS
11   GLYASPTHRALAARGGLNTYRVALLEUMET
12   ASNGLYLYSLEULYSVALILEGLYPHEASP
13   PHESERTHRLYSMETGLNSERILEILEARG
14   ASPTYRSERASPLEUVALILESERHISALA
15   GLYTHRGLYSERILELEUASPSERLEUARG
16   LEUASNLYSPROLEUILEVALCYSVALASN
17   ASPSERLEUMETASPASNHISGLNGLNGLN
18   ILEALAASPLYSPHEVALGLULEUGLYTYR
19   VALTRPSERCYSALAPROTHRGLUTHRGLY
20   LEUILEALAGLYLEUARGALASERGLNTHR
21   GLULYSLEULYSPROPHEPROVALSERHIS
22   ASNPROSERPHEGLUARGLEULEUVALGLU
23   THRILETYRSER

Samples:

triple_label: Alg13, [U-13C; U-15N; U-2H], 0.35 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 0.02%

methyl_label: Alg13, [U-15N; U-2H; 13C,1H Leu, Val, Ile.D1 methyl], 0.35 mM; sodium phosphate 20 mM; sodium chloride 100 mM

methyl_phe_label: Alg13, [U-15N; U-2H; 13C,1H Leu, Val, Ile.D1 methyl; 1H-Phe], 0.35 mM; sodium phosphate 20 mM; sodium chloride 100 mM

gel_aligned: Alg13, [U-13C; U-15N; U-2H], 0.35 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 0.02%; acrylamide 3.5 w/v; (3-acrylamidopropyl)-trimethylammonium chloride 3.5 w/v

sample_conditions_1: ionic strength: 0.1 M; pH: 6.7; pressure: 1 atm; temperature: 297 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCtriple_labelisotropicsample_conditions_1
3D HNCACBtriple_labelisotropicsample_conditions_1
3D HNCAtriple_labelisotropicsample_conditions_1
3D HN(CO)CAtriple_labelisotropicsample_conditions_1
3D HN(COCA)CBtriple_labelisotropicsample_conditions_1
3D HNCACOtriple_labelisotropicsample_conditions_1
3D HNCOtriple_labelisotropicsample_conditions_1
3D 1H-15N NOESYmethyl_labelisotropicsample_conditions_1
3D 1H-13C NOESYmethyl_labelisotropicsample_conditions_1
3D 1H-13C NOESYmethyl_phe_labelisotropicsample_conditions_1
2D S3-TROSYgel_alignedanisotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Varian Unity 600 MHz
  • Varian Unity 900 MHz

Related Database Links:

PDB
DBJ GAA23342
EMBL CAA96749 CAY79713
GB AHY79326 AJP38744 AJR76064 AJR76565 AJR77063
REF NP_011468
SP P53178
TPG DAA08054

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts