BMRB Entry 16607
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16607
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Title: SOLUTION STRUCTURE OF THE AL-09 H87Y IMMUNOGLOBULIN LIGHT CHAIN VARIABLE DOMAIN
Deposition date: 2009-11-11 Original release date: 2010-05-13
Authors: Volkman, B.; Peterson, F.; Ramirez-Alvarado, M.; Baden, E.
Citation: Baden, E.; Peterson, F.; Owen, B.; Volkman, B.; Ramirez-Alvarado, M.. "TBA" To be published ., .-..
Assembly members:
AL-09_H87Y, polymer, 110 residues, 12154.475 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: Escherichia coli
Entity Sequences (FASTA):
AL-09_H87Y: STDIQMTQSPSSLSASVGDR
VTITCQASQDINNYLIWYQQ
KPGQAPKLLIYDASTLETGV
PSRFSGSGSGTEFTFTISSL
QPEDLATYYCQQYDNLPYTF
GQGTKLEIKR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 906 |
| 15N chemical shifts | 229 |
| 1H chemical shifts | 1489 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AL-09 H87Y_1 | 1 |
| 2 | AL-09 H87Y_2 | 1 |
Entities:
Entity 1, AL-09 H87Y_1 110 residues - 12154.475 Da.
Numbering in the second monomer, chain B, is offset by 200. The ST dipeptide at the N-terminus is a cloning artifact.
| 1 | SER | THR | ASP | ILE | GLN | MET | THR | GLN | SER | PRO | |
| 2 | SER | SER | LEU | SER | ALA | SER | VAL | GLY | ASP | ARG | |
| 3 | VAL | THR | ILE | THR | CYS | GLN | ALA | SER | GLN | ASP | |
| 4 | ILE | ASN | ASN | TYR | LEU | ILE | TRP | TYR | GLN | GLN | |
| 5 | LYS | PRO | GLY | GLN | ALA | PRO | LYS | LEU | LEU | ILE | |
| 6 | TYR | ASP | ALA | SER | THR | LEU | GLU | THR | GLY | VAL | |
| 7 | PRO | SER | ARG | PHE | SER | GLY | SER | GLY | SER | GLY | |
| 8 | THR | GLU | PHE | THR | PHE | THR | ILE | SER | SER | LEU | |
| 9 | GLN | PRO | GLU | ASP | LEU | ALA | THR | TYR | TYR | CYS | |
| 10 | GLN | GLN | TYR | ASP | ASN | LEU | PRO | TYR | THR | PHE | |
| 11 | GLY | GLN | GLY | THR | LYS | LEU | GLU | ILE | LYS | ARG |
Samples:
sample_1: AL-09 H87Y, [U-100% 13C; U-100% 15N], 0.8 mM; MES, [U-2H], 10 mM; sodium azide 0.02%; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 8 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D_15N-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D_13C-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D_13C-separated_NOESY (AROMATIC) | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement
TOPSPIN v2.1, Bruker - collection
NMRPipe v2007, Delagio,F. et al. - processing
XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis
GARANT v2.1, C. Bartels - data analysis
CYANA v2.1, Guntert, P. - structural calculation
NMR spectrometers:
- Bruker Avance III 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts