BMRB Entry 11310

Title:
Solution structure of the C-terminal domain of mouse phosphoacetylglucosamine mutase (PAGM)
Deposition date:
2010-08-10
Original release date:
2011-08-19
Authors:
Yoneyama, M.; Tochio, N.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Yoneyama, M.; Tochio, N.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the C-terminal domain of mouse phosphoacetylglucosamine mutase (PAGM)"  .

Assembly members:

Assembly members:
C-terminal domain, polymer, 112 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P040113-52

Data sets:
Data typeCount
13C chemical shifts440
15N chemical shifts103
1H chemical shifts719

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal domain1

Entities:

Entity 1, C-terminal domain 112 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYALAILETYR
2   VALASPLEUPROASNARGGLNLEULYSVAL
3   LYSVALALAASPARGARGVALILESERTHR
4   THRASPALAGLUARGGLNALAVALTHRPRO
5   PROGLYLEUGLNGLUALAILEASNASPLEU
6   VALLYSLYSTYRTHRLEUALAARGALAPHE
7   VALARGPROSERGLYTHRGLUASPILEVAL
8   ARGVALTYRALAGLUALAASNSERGLNGLU
9   SERALAASPARGLEUALATYRGLUVALSER
10   LEULEUVALPHEGLNLEUALAGLYGLYILE
11   GLYGLUARGPROGLNPROSERGLYPROSER
12   SERGLY

Samples:

sample_1: C-terminal domain of Phosphoacetylglucosamine mutase(PAGM), [U-13C; U-15N], 1 mM; Phosphate Buffer Na 20 mM; NaCl 300 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 320 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delagio, F. - processing

NMRView v5.0.4, Jhonson, B. A. - data analysis

Kujira v0.896, Kobayashi, N. - data analysis

CYANA v1.0.8, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB28834 BAC25733 BAC29478 BAC33692 BAC34728
GB AAI38701 EDL26495
REF NP_082628 XP_011240958
SP Q9CYR6
AlphaFold Q9CYR6

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