BMRB Entry 20074

Name: Protein Fibril
Published: 2009-02-10

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PDB ID: 2kib
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR20074
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Protein Fibril

Deposition date:

2009-02-05

Original release date:

2009-02-10

Authors:

Nielsen, Jakob; Bjerring, Morten; Jeppesen, Martin; Pedersen, Ronnie; Pedersen, Jan; Hein, Kim; Vosegaard, Thomas; Skrydstrup, Troels; Otzen, Daniel; Nielsen, Niels Christian

Citation:

Citation: Nielsen, Jakob; Bjerring, Morten; Jeppesen, Martin; Pedersen, Ronnie; Pedersen, Jan; Hein, Kim; Vosegaard, Thomas; Skrydstrup, Troels; Otzen, Daniel; Nielsen, Niels Christian. "Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid-State NMR Spectroscopy" Angew. Chem. Int. Ed. Engl. 48, 2118-2121 (2009).
PubMed: 19130518

Assembly members:

Assembly members:
NFGAILchain, polymer, 10 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NFGAILchain: SNNFGAILSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_A1

Data type	Count
13C chemical shifts	120
15N chemical shifts	24

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit A1 peptide 1	1
2	subunit A2 peptide 1	1
3	subunit B1 peptide 1	1
4	subunit B2 peptide 1	1
5	subunit A1 peptide 2	1
6	subunit A2 peptide 2	1
7	subunit B1 peptide 2	1
8	subunit B2 peptide 2	1

Entities:

Entity 1, subunit A1 peptide 1 10 residues - Formula weight is not available

NFGAILS is part of the decapeptide SNNFGAILSS, but structure data is only provided for the NFGAILS segment

1

SER

ASN

PHE

GLY

ALA

ILE

LEU

SER

Samples:

SNNFGAILSS_U_13C_15N-_labeled_for_NFGAIL: NFGAIL, [U-100% 13C; U-100% 15N], 2.5 mg; H2O%; HEPES mM

sample_conditions_1: pH: 7.2; temperature: 263 K

Experiments:

Name	Sample	Sample state	Sample conditions
NCA	SNNFGAILSS_U_13C_15N-_labeled_for_NFGAIL	solid	sample_conditions_1
NCO	SNNFGAILSS_U_13C_15N-_labeled_for_NFGAIL	solid	sample_conditions_1
2D 13C-13C DARR 2.5 ms mixing	SNNFGAILSS_U_13C_15N-_labeled_for_NFGAIL	solid	sample_conditions_1
2D 13C-13C DARR 5 ms mixing	SNNFGAILSS_U_13C_15N-_labeled_for_NFGAIL	solid	sample_conditions_1
2D 13C-13C DARR 20 ms mixing	SNNFGAILSS_U_13C_15N-_labeled_for_NFGAIL	solid	sample_conditions_1
2D 13C-13C DARR 40 ms mixing	SNNFGAILSS_U_13C_15N-_labeled_for_NFGAIL	solid	sample_conditions_1
2D 13C-13C DARR 100 ms mixing	SNNFGAILSS_U_13C_15N-_labeled_for_NFGAIL	solid	sample_conditions_1
2D 13C-13C DARR 200 ms mixing	SNNFGAILSS_U_13C_15N-_labeled_for_NFGAIL	solid	sample_conditions_1

Software:

X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization

NMR spectrometers:

Bruker Avance 700 MHz