BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16587

Title: Chemical shifts of a native-like folding intermediate of beta2-microglobulin   PubMed: 20028983

Deposition date: 2009-10-27 Original release date: 2010-02-09

Authors: Rennella, Enrico; Esposito, Gennaro; Corazza, Alessandra; Giorgetti, Sofia; Stoppini, Monica; Bellotti, Vittorio

Citation: Corazza, Alessandra; Rennella, Enrico; Schanda, Paul; Mimmi, Maria Chiara; Cutuil, Thomas; Raimondi, Sara; Giorgetti, Sofia; Fogolari, Federico; Viglino, Paolo; Frydman, Lucio; Gal, Maayan; Bellotti, Vittorio; Brutscher, Bernhard; Esposito, Gennaro. "Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein beta2-microglobulin revealed by real-time two-dimensional NMR."  J. Biol. Chem. 285, 5827-5835 (2010).

Assembly members:
W60G beta2-microglobulin, polymer, 100 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
W60G beta2-microglobulin: MIQRTPKIQVYSRHPAENGK SNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKD GSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM

Data sets:
Data typeCount
15N chemical shifts65
1H chemical shifts398

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1W60G beta2-microglobulin1

Entities:

Entity 1, W60G beta2-microglobulin 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 beta2-microglobulin, [U-100% 15N], 0.6 mM; H2O, [U-100% 2H], 0.08 v/v; H2O 0.74 v/v; TFE, [U-99% 2H], 0.18 v/v; sodium chloride 100 mM; sodium phosphate 70 mM

sample_conditions_1: pH: 6.6; pressure: 1 atm; temperature: 306 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

FELIX, Accelrys Software Inc. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

BMRB 15480 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

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