BMRB Entry 27878

Name: K1-K9 fragments of beta2-microglobulin
Published: 2019-11-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27878

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

K1-K9 fragments of beta2-microglobulin

Deposition date:

2019-04-16

Original release date:

2019-11-22

Authors:

Muta, Hiroya; So, Masatomo; Sakurai, Kazumasa; Goto, Yuji

Citation:

Citation: Muta, Hiroya; So, Masatomo; Sakurai, Kazumasa; Kardos, Jozsef; Naiki, Hironobu; Goto, Yuji. "Amyloid formation under complicated conditions in which beta2-microglobulin coexists with its proteolytic fragments" Biochemistry 58, 4925-4934 (2019).
PubMed: 31724398

Assembly members:

Assembly members:
K1, polymer, 7 residues, Formula weight is not available
K2, polymer, 13 residues, Formula weight is not available
K4, polymer, 7 residues, Formula weight is not available
K5, polymer, 10 residues, Formula weight is not available
K7, polymer, 16 residues, Formula weight is not available
K8, polymer, 3 residues, Formula weight is not available
K9, polymer, 5 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: pColdB2M

Entity Sequences (FASTA):

Entity Sequences (FASTA):
K1: MIQRTPK
K2: IQVYSRHPAENGK
K4: NGERIEK
K5: VEHSDLSFSK
K7: DEYACRVNHVTLSQPK
K8: IVK
K9: WDRDM

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	60
15N chemical shifts	50
1H chemical shifts	50

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	K1	1
2	K2	2
3	K4	3
4	K5	4
5	K7	5
6	K8	6
7	K9	7

Entities:

Entity 1, K1 7 residues - Formula weight is not available

1

MET

ILE

GLN

ARG

THR

PRO

LYS

Entity 2, K2 13 residues - Formula weight is not available

1

ILE

GLN

VAL

TYR

SER

ARG

HIS

PRO

ALA

GLU

2

ASN

GLY

LYS

Entity 3, K4 7 residues - Formula weight is not available

1

ASN

GLY

GLU

ARG

ILE

GLU

LYS

Entity 4, K5 10 residues - Formula weight is not available

1

VAL

GLU

HIS

SER

ASP

LEU

SER

PHE

SER

LYS

Entity 5, K7 16 residues - Formula weight is not available

1

ASP

GLU

TYR

ALA

CYS

ARG

VAL

ASN

HIS

VAL

2

THR

LEU

SER

GLN

PRO

LYS

Entity 6, K8 3 residues - Formula weight is not available

1

ILE

VAL

LYS

Entity 7, K9 5 residues - Formula weight is not available

1

TRP

ASP

ARG

ASP

MET

Samples:

sample_1: K1 peptides, [U-99% 13C; U-99% 15N], 50 uM; K2 peptides, [U-99% 13C; U-99% 15N], 50 uM; K4 peptides, [U-99% 13C; U-99% 15N], 50 uM; K5 peptides, [U-99% 13C; U-99% 15N], 50 uM; K7 peptides, [U-99% 13C; U-99% 15N], 50 uM; K8 peptides, [U-99% 13C; U-99% 15N], 50 uM; K9 peptides, [U-99% 13C; U-99% 15N], 50 uM; HCl 10 mM; sodium chloride 100 mM; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 1.5; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 950 MHz

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