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 25558

Title: MAX1 peptide fibril

Deposition date: 2015-03-30 Original release date: 2015-07-27

Authors: Nagy-Smith, Katelyn; Moore, Eric; Schneider, Joel; Tycko, Robert

Citation: Nagy-Smith, Katelyn; Moore, Eric; Schneider, Joel; Tycko, Robert. "Molecular-level Architecture of Self-Assembled Peptide Fibrils from Solid State NMR"  Not known ., .-..

Assembly members:
MAX1, polymer, 21 residues, 2238.995 Da.

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
MAX1: VKVKVKVKVXPTKVKVKVKV X

Data sets:
Data typeCount
13C chemical shifts37
15N chemical shifts4

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21
3entity_31
4entity_41
5entity_51
6entity_61
7entity_71
8entity_81

Entities:

Entity 1, entity_1 21 residues - 2238.995 Da.

Residue 10 is a D-proline.

1   VALLYSVALLYSVALLYSVALLYSVALDPR
2   PROTHRLYSVALLYSVALLYSVALLYSVAL
3   NH2

Samples:

sample_1: MAX1, [13CO-V1; 15N-V20],

sample_2: MAX1, [13CO-V3; 15N-V18],

sample_3: MAX1, [13CO-V5; 15N-V16],

sample_4: MAX1, [13CO-V7; 15N-V14],

sample_5: MAX1, [13CO-V1; 13CO-V16],

sample_6: MAX1, [13CO-V3; 13CO-V16],

sample_7: MAX1, [13CO-V5; 13CO-V16],

sample_8: MAX1, [13CO-V7; 13CO-V16],

sample_9: MAX1, [13CO-P10; U-15N,13C-(K8, V9, )11, T12, K13],

sample_10: MAX1, [U-15N,13C-(V1, P11, T12, V20)],

sample_conditions_1: ionic strength: 0 M; pH: 9; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
REDORsample_1solidsample_conditions_1
REDORsample_2solidsample_conditions_1
REDORsample_3solidsample_conditions_1
REDORsample_4solidsample_conditions_1
PITHIRDS-CTsample_1solidsample_conditions_1
PITHIRDS-CTsample_2solidsample_conditions_1
PITHIRDS-CTsample_3solidsample_conditions_1
PITHIRDS-CTsample_4solidsample_conditions_1
PITHIRDS-CTsample_5solidsample_conditions_1
PITHIRDS-CTsample_6solidsample_conditions_1
PITHIRDS-CTsample_7solidsample_conditions_1
PITHIRDS-CTsample_8solidsample_conditions_1
15N-BAREsample_9solidsample_conditions_1
13C-BAREsample_9solidsample_conditions_1
2D RAD/DARRsample_10solidsample_conditions_1
2D NCACXsample_10isotropicsample_conditions_1
2D RAD/DARRsample_9isotropicsample_conditions_1
2D NCACXsample_9isotropicsample_conditions_1

Software:

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - stage 1 of structure development

NAMD, Klaus Schulten and coworkers - stage 2 of structure development

NMR spectrometers:

  • Varian InfinityPlus 400 MHz
  • Bruker Avance III 400 MHz
  • Varian Infinity 750 MHz