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 5169

Title: NMR solution structure of the human beta2-microglobulin   PubMed: 11847272

Authors: Verdone, G.; Corazza, A.; Viglino, P.; Pettirossi, F.; Giorgetti, S.; Mangione, P.; Andreola, A.; Stoppini, M.; Bellotti, V.; Esposito, G.

Citation: Verdone, G.; Corazza, A.; Viglino, P.; Pettirossi, F.; Giorgetti, S.; Mangione, P.; Andreola, A.; Stoppini, M.; Bellotti, V.; Esposito, G.. "The Solution Structure of Human Beta2-microglobulin reveals the Prodromes of its Amyloid Transition "  Protein Sci. 11, 487-499 (2002).

Assembly members:
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):
beta2-microglobulin: MIQRTPKIQVYSRHPAENGK SNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM

Data sets:
Data typeCount
1H chemical shifts631
coupling constants66

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1beta2-microglobulin1

Entities:

Entity 1, beta2-microglobulin 100 residues - Formula weight is not available

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

Samples:

sample_1: beta2-microglobulin 0.68 mM; phosphate buffer 70 mM; NaCl 100 mM; H2O 90%; D2O 10%

sample_2: beta2-microglobulin 0.37 mM; phosphate buffer 70 mM; NaCl 100 mM; D2O 100%

sample_cond_1: pH: 6.4 na; temperature: 310 K; ionic strength: 190 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D TOCSYnot availablenot availablenot available
2D DQFnot availablenot availablenot available

Software:

XWINNMR v2.6 - collection

FELIX v2000 - processing, data analysis

DIANA v1.5 - structure solution

DISCOVER v2000 - refinement

NMR spectrometers:

  • Bruker AVANCE 500.13 MHz

Related Database Links:

BMRB 15480 16587 17165 17166 19099 19113 19116 19118 19119 19120 19121 19122 19123 3078 3079 5782 5783 5784
PDB
DBJ BAA35182 BAG38125 BAG64583 BAG72952
EMBL CAA23830 CAG33347 CAH92078
GB AAA51811 AAA87972 AAA88008 AAB25312 AAB35347
REF NP_001009066 NP_001127503 NP_004039 XP_003266894 XP_003266898
SP P16213 P61769 P61770 P61771