BMRB Entry 18811
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18811
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Title: Structural Characterization of Minor Ampullate Spidroin Domains and their Distinct Roles in Fibroin Solubility and Fiber Formation PubMed: 23418525
Deposition date: 2012-10-30 Original release date: 2013-02-21
Authors: Yang, Daiwen; Gao, Zhenwei; Lin, Zhi; Huang, Weidong; Lai, Chong Cheong; Fan, Jing-song
Citation: Gao, Zhenwei; Lin, Zhi; Huang, Weidong; Lai, Chong Cheong; Fan, Jing-Song; Yang, Daiwen. "Structural characterization of minor ampullate spidroin domains and their distinct roles in fibroin solubility and fiber formation." PLoS ONE 8, e56142-e56142 (2013).
Assembly members:
Spidroin, polymer, 107 residues, 10505.787 Da.
Natural source: Common Name: Spiders Taxonomy ID: 171624 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Nephila antipodiana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Spidroin: VGTTVASTTSRLSTAEASSR
ISTAASTLVSGGYLNTAALP
SVIADLFAQVGASSPGVSDS
EVLIQVLLEIVSSLIHILSS
SSVGQVDFSSVGSSAAAVGQ
SMQVVMG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 313 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 678 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Spidroin_1 | 1 |
| 2 | Spidroin_2 | 1 |
Entities:
Entity 1, Spidroin_1 107 residues - 10505.787 Da.
| 1 | VAL | GLY | THR | THR | VAL | ALA | SER | THR | THR | SER | ||||
| 2 | ARG | LEU | SER | THR | ALA | GLU | ALA | SER | SER | ARG | ||||
| 3 | ILE | SER | THR | ALA | ALA | SER | THR | LEU | VAL | SER | ||||
| 4 | GLY | GLY | TYR | LEU | ASN | THR | ALA | ALA | LEU | PRO | ||||
| 5 | SER | VAL | ILE | ALA | ASP | LEU | PHE | ALA | GLN | VAL | ||||
| 6 | GLY | ALA | SER | SER | PRO | GLY | VAL | SER | ASP | SER | ||||
| 7 | GLU | VAL | LEU | ILE | GLN | VAL | LEU | LEU | GLU | ILE | ||||
| 8 | VAL | SER | SER | LEU | ILE | HIS | ILE | LEU | SER | SER | ||||
| 9 | SER | SER | VAL | GLY | GLN | VAL | ASP | PHE | SER | SER | ||||
| 10 | VAL | GLY | SER | SER | ALA | ALA | ALA | VAL | GLY | GLN | ||||
| 11 | SER | MET | GLN | VAL | VAL | MET | GLY |
Samples:
sample_1: CTD, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 10 mM; sodium azide 0.01%; EDTA 5 mM; sodium chloride 50 mM; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 0.06 M; pH: 6.8; pressure: 1 atm; temperature: 307 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D MQ-CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 4D 13C, 15N-edited NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
Molmol, Koradi, Billeter and Wuthrich - data analysis
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - processing
NMRspy, Daiwen Yang, Yu Zheng - chemical shift assignment, NOE assignment, peak picking
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts