BMRB Entry 18654
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18654
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Title: NMR Structures of Single-chain Insulin
Deposition date: 2012-08-09 Original release date: 2012-09-07
Authors: Weiss, Michael; Yang, Yanwu
Citation: Yang, Yanwu; Wan, Zhu-li; Hua, Qing-xin; Phillips, Nelson; Huang, Kun; Yeh, I-Ju; Liu, Yule; Hu, Shi-Quan; Hattier, Thomas; Whittaker, Jonathan; Weiss, Michael. "Dynamic repair of an amyloidogenic protein: insulin fibrillation is blocked by tethering a nascent alpha-helix" Not known ., .-..
Assembly members:
Single-chain Insulin, polymer, 57 residues, 6382.218 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Pichia pastoris
Entity Sequences (FASTA):
Single-chain Insulin: FVNQHLCGSDLVEALYLVCG
ERGFFYTDPTGGGPRRGIVE
QCCHSICSLYQLENYCN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 191 |
| 15N chemical shifts | 54 |
| 1H chemical shifts | 368 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Single-chain Insulin | 1 |
Entities:
Entity 1, Single-chain Insulin 57 residues - 6382.218 Da.
| 1 | PHE | VAL | ASN | GLN | HIS | LEU | CYS | GLY | SER | ASP | ||||
| 2 | LEU | VAL | GLU | ALA | LEU | TYR | LEU | VAL | CYS | GLY | ||||
| 3 | GLU | ARG | GLY | PHE | PHE | TYR | THR | ASP | PRO | THR | ||||
| 4 | GLY | GLY | GLY | PRO | ARG | ARG | GLY | ILE | VAL | GLU | ||||
| 5 | GLN | CYS | CYS | HIS | SER | ILE | CYS | SER | LEU | TYR | ||||
| 6 | GLN | LEU | GLU | ASN | TYR | CYS | ASN |
Samples:
sample_1: Single Chain Insulin, [U-100% 13C; U-100% 15N], 0.9 mM; H2O 93%; H2O 7%
sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D Time-shared NOESY (4D-N15,C13-edited and 4D-C13,C13-edited NOESY) | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PIPP, Garrett - peak picking
xwinnmr, Bruker Biospin - collection
InsightII, Accelrys Software Inc. - data analysis
Molmol, Koradi, Billeter and Wuthrich - structure display
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts