BMRB Entry 25558
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25558
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Citation: Nagy-Smith, Katelyn; Moore, Eric; Schneider, Joel; Tycko, Robert. "Molecular-level Architecture of Self-Assembled Peptide Fibrils from Solid State NMR" .
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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 37 |
| 15N chemical shifts | 4 |
Additional metadata:
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 |
Entities:
Entity 1, entity_1 21 residues - 2238.995 Da.
Residue 10 is a D-proline.
| 1 | VAL | LYS | VAL | LYS | VAL | LYS | VAL | LYS | VAL | DPR | ||||
| 2 | PRO | THR | LYS | VAL | LYS | VAL | LYS | VAL | LYS | VAL | ||||
| 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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| REDOR | sample_1 | solid | sample_conditions_1 |
| REDOR | sample_2 | solid | sample_conditions_1 |
| REDOR | sample_3 | solid | sample_conditions_1 |
| REDOR | sample_4 | solid | sample_conditions_1 |
| PITHIRDS-CT | sample_1 | solid | sample_conditions_1 |
| PITHIRDS-CT | sample_2 | solid | sample_conditions_1 |
| PITHIRDS-CT | sample_3 | solid | sample_conditions_1 |
| PITHIRDS-CT | sample_4 | solid | sample_conditions_1 |
| PITHIRDS-CT | sample_5 | solid | sample_conditions_1 |
| PITHIRDS-CT | sample_6 | solid | sample_conditions_1 |
| PITHIRDS-CT | sample_7 | solid | sample_conditions_1 |
| PITHIRDS-CT | sample_8 | solid | sample_conditions_1 |
| 15N-BARE | sample_9 | solid | sample_conditions_1 |
| 13C-BARE | sample_9 | solid | sample_conditions_1 |
| 2D RAD/DARR | sample_10 | solid | sample_conditions_1 |
| 2D NCACX | sample_10 | isotropic | sample_conditions_1 |
| 2D RAD/DARR | sample_9 | isotropic | sample_conditions_1 |
| 2D NCACX | sample_9 | isotropic | sample_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