BMRB Entry 25289

Name: Atomic-resolution 3D structure of amyloid-beta fibrils: the Osaka mutation
Published: 2014-11-24

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PDB ID: 2mvx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25289
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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:

Atomic-resolution 3D structure of amyloid-beta fibrils: the Osaka mutation

Deposition date:

2014-10-17

Original release date:

2014-11-24

Authors:

Schuetz, Anne; Vagt, Toni; Huber, Matthias; Ovchinnikova, Oxana; Cadalbert, Riccardo; Wall, Joseph; Guentert, Peter; Bockmann, Anja; Glockshuber, Rudi; Meier, Beat

Citation:

Citation: Schuetz, Anne; Vagt, Toni; Huber, Matthias; Ovchinnikova, Oxana; Cadalbert, Riccardo; Wall, Joseph; Guentert, Peter; Bockmann, Anja; Glockshuber, Rudi; Meier, Beat. "Atomic-Resolution Three-Dimensional Structure of Amyloid beta Fibrils Bearing the Osaka Mutation" Angew. Chem. Int. Ed. Engl. 54, 331-335 (2015).
PubMed: 25395337

Assembly members:

Assembly members:
amyloid_beta, polymer, 39 residues, 4206.777 Da.

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: pET T7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
amyloid_beta: DAEFRHDSGYEVHHQKLVFF ADVGSNKGAIIGLMVGGVV

Data sets:

assigned_chemical_shifts

Data type	Count
13C chemical shifts	477
15N chemical shifts	91

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	1
3	entity_3	1
4	entity_4	1
5	entity_5	1
6	entity_6	1
7	entity_7	1
8	entity_8	1
9	entity_9	1
10	entity_10	1

Entities:

Entity 1, entity_1 39 residues - 4206.777 Da.

1

ASP

ALA

GLU

PHE

ARG

HIS

ASP

SER

GLY

TYR

2

GLU

VAL

HIS

GLN

LYS

LEU

VAL

PHE

3

ALA

ASP

VAL

GLY

SER

ASN

LYS

GLY

ALA

ILE

4

ILE

GLY

LEU

MET

VAL

GLY

VAL

Name	Sample	Sample state	Sample conditions
NCA	uniform_13C15N	solid	sample_conditions_1
NCO	uniform_13C15N	solid	sample_conditions_1
DARR 15 ms	uniform_13C	solid	sample_conditions_1
PAIN 6 ms	uniform_13C15N	solid	sample_conditions_1
PAIN 6 ms	mixed_13C-15N	solid	sample_conditions_1
DARR 400 ms	uniform_13C	solid	sample_conditions_1
DARR 400 ms	diluted	solid	sample_conditions_1
PAR 8 ms	uniform_13C	solid	sample_conditions_1
PAR 8 ms	diluted	solid	sample_conditions_1
CHHC 500 us	uniform_13C	solid	sample_conditions_1
CHHC 500 us	diluted	solid	sample_conditions_1
PDSD 4 s	2-13C-glucose	solid	sample_conditions_1

Related Database Links:

BMRB	11435 15775 17159 17186 17764 17793 17794 17795 17796 18052 18127 18128 18129 18131 19009 19309 19393 25218 25429 26508 26516
PDB	1AML 1BA4 1IYT 1Z0Q 2BEG 2G47 2LFM 2LMN 2LMO 2LMP 2LMQ 2LP1 2M4J 2M9R 2M9S 2MVX 2MXU 2OTK 2WK3 3IFN 4M1C 4MVI 4MVL 4NGE 4ONG
DBJ	BAA22264 BAA84580 BAD51938 BAE01907 BAG10647
EMBL	CAA30050 CAA31830 CAA39589 CAA39590 CAA39591
GB	AAA35540 AAA36829 AAA51722 AAA51726 AAA51727
PIR	A60045 D60045 E60045 G60045 PQ0438
PRF	1303338A 1403400A 1405204A 1507304A 1507304B
REF	NP_000475 NP_001006601 NP_001013036 NP_001070264 NP_001127014
SP	P05067 P53601 P79307 Q28053 Q28280
TPG	DAA33655
AlphaFold	P05067 P53601 P79307 Q28053 Q28280

BMRB Entry 25289

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: