BMRB Entry 15480

Title:
1H assignments of W60G mutant of human beta2-microglobulin
Deposition date:
2007-09-19
Original release date:
2007-10-15
Authors:
Esposito, Gennaro; Corazza, Alessandra; Rennella, Enrico; Gumral, Devrim; Mimmi, Maria Chiara; Fogolari, Federico; Viglino, Paolo; Raimondi, Sara; Giorgetti, Sofia; Bolognesi, Benedetta; Merlini, Giampaolo; Stoppini, Monica; Bellotti, Vittorio
Citation:

Citation: Esposito, Gennaro; Ricagno, Stefano; Corazza, Alessandra; Rennella, Enrico; Gumral, Devrim; Mimmi, Maria Chiara; Betto, Elena; Pucillo, Carlo E.M.; Fogolari, Federico; Viglino, Paolo; Raimondi, Sara; Giorgetti, Sofia; Bolognesi, Benedetta; Merlini, Giampaolo; Stoppini, Monica; Bolognesi, Martino; Bellotti, Vittorio. "The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties"  J. Mol. Biol. 378, 885-895 (2008).
PubMed: 18395224

Assembly members:

Assembly members:
w60g-b2m, polymer, 100 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: PHN1

Data sets:
Data typeCount
1H chemical shifts690

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1w60g-b2m1

Entities:

Entity 1, w60g-b2m 100 residues - Formula weight is not available

1   METILEGLNARGTHRPROLYSILEGLNVAL
2   TYRSERARGHISPROALAGLUASNGLYLYS
3   SERASNPHELEUASNCYSTYRVALSERGLY
4   PHEHISPROSERASPILEGLUVALASPLEU
5   LEULYSASNGLYGLUARGILEGLULYSVAL
6   GLUHISSERASPLEUSERPHESERLYSASP
7   GLYSERPHETYRLEULEUTYRTYRTHRGLU
8   PHETHRPROTHRGLULYSASPGLUTYRALA
9   CYSARGVALASNHISVALTHRLEUSERGLN
10   PROLYSILEVALLYSTRPASPARGASPMET

Samples:

sample_1: w60g-b2m 0.5-0.9 mM; phosphate 70 mM; NaCl 100 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.6; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1

Software:

FELIX, Accelrys Software Inc. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

BMRB 16587 17165 17166 19099 19113 19116 19118 19119 19120 19121 19122 19123 3078 3079
PDB
DBJ BAA35182 BAG38125 BAG72952
EMBL CAA23830 CAG33347 CAH92078
GB AAA51811 AAA87972 AAA88008 AAB25312 AAB35347
REF NP_001009066 NP_001127503 NP_004039 XP_004056148 XP_004056149
SP P16213 P61769 P61770 P61771
AlphaFold P61771 P16213 P61769 P61770