BMRB Entry 16380
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16380
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Title: NMR solution structure of A2LD1 (gi:13879369) PubMed: 20944236
Deposition date: 2009-06-30 Original release date: 2009-08-07
Authors: Pedrini, Bill; Serrano, Pedro; Mohanty, Biswaranjan; Geralt, Michael; Herrmann, Torsten; Wuthrich, Kurt; Wilson, Ian
Citation: Serrano, Pedro; Pedrini, Bill; Geralt, Michael; Jaudzems, Kristaps; Mohanty, Biswaranjan; Horst, Reto; Herrmann, Torsten; Elsliger, Marc-Andre; Wilson, Ian; Wuthrich, Kurt. "Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites" Acta Crystallogr. Sect F Struct. Biol. Cryst. Commun. 66, 1393-1405 (2010).
Assembly members:
gi-13879369, polymer, 149 residues, 17099.287 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
gi-13879369: MAHIFVYGTLKRGQPNHKVM
LDHSHGLAAFRGRGCTVESF
PLVIAGEHNIPWLLYLPGKG
HCVTGEIYEVDEQMLRFLDD
FEDCPSMYQRTALQVQVLEW
EGDGDPGDSVQCFVYTTATY
APEWLFLPYHESYDSEGPHG
LRYNPRENR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 471 |
| 15N chemical shifts | 153 |
| 1H chemical shifts | 951 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | gi-13879369 | 1 |
Entities:
Entity 1, gi-13879369 149 residues - 17099.287 Da.
| 1 | MET | ALA | HIS | ILE | PHE | VAL | TYR | GLY | THR | LEU | ||||
| 2 | LYS | ARG | GLY | GLN | PRO | ASN | HIS | LYS | VAL | MET | ||||
| 3 | LEU | ASP | HIS | SER | HIS | GLY | LEU | ALA | ALA | PHE | ||||
| 4 | ARG | GLY | ARG | GLY | CYS | THR | VAL | GLU | SER | PHE | ||||
| 5 | PRO | LEU | VAL | ILE | ALA | GLY | GLU | HIS | ASN | ILE | ||||
| 6 | PRO | TRP | LEU | LEU | TYR | LEU | PRO | GLY | LYS | GLY | ||||
| 7 | HIS | CYS | VAL | THR | GLY | GLU | ILE | TYR | GLU | VAL | ||||
| 8 | ASP | GLU | GLN | MET | LEU | ARG | PHE | LEU | ASP | ASP | ||||
| 9 | PHE | GLU | ASP | CYS | PRO | SER | MET | TYR | GLN | ARG | ||||
| 10 | THR | ALA | LEU | GLN | VAL | GLN | VAL | LEU | GLU | TRP | ||||
| 11 | GLU | GLY | ASP | GLY | ASP | PRO | GLY | ASP | SER | VAL | ||||
| 12 | GLN | CYS | PHE | VAL | TYR | THR | THR | ALA | THR | TYR | ||||
| 13 | ALA | PRO | GLU | TRP | LEU | PHE | LEU | PRO | TYR | HIS | ||||
| 14 | GLU | SER | TYR | ASP | SER | GLU | GLY | PRO | HIS | GLY | ||||
| 15 | LEU | ARG | TYR | ASN | PRO | ARG | GLU | ASN | ARG |
Samples:
sample_1: gi-13879369, [U-100% 13C; U-100% 15N], 1.1 ± 0.1 mM; sodium phosphate 25 mM; sodium chloride 50 mM; DTT, [U-100% 2H], 4.5 mM; DTT 0.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 80.25 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 5D APSY CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY HACANH | sample_1 | isotropic | sample_conditions_1 |
| 3D APSY (HA)CANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D aliphatic 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D aromatic 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment
ATNOS, Herrmann, Guntert and Wuthrich - peak picking
CANDID, Herrmann, Guntert and Wuthrich - collection of distance restraints
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
GAPRO, Hiller, Fiorito, Wider Wuthrich - Geometric analysis of 2D APSY projections
MATCH, Volk, Herrmann, Wuthrich - Backbione assignment from APSY peaks
ASCAN, Fiorito, Herrmann, Wuthrich - Sidechain assignment with NOESY spectra
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAC34147 |
| GB | AAH06662 EDL00632 EDL00634 |
| REF | NP_663441 XP_006518983 |
| SP | Q923B0 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts