BMRB Entry 15480
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                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_full
BMRB Entry DOI: doi:10.13018/BMR15480
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Title: 1H assignments of W60G mutant of human beta2-microglobulin PubMed: 18395224
Deposition date: 2007-09-19 Original release date: 2007-10-15
Authors: Esposito, Gennaro; Corazza, Alessandra; Rennella, Enrico; Gumral, Devrim; Mimmi, Maria Chiara; Fogolari, Federico; Viglino, Paolo; Raimondi, Sara; Giorgetti, Sofia; Bolognesi, Benedetta; Merlini, Giampaolo; Stoppini, Monica; Bellotti, Vittorio
Citation: Esposito, Gennaro; Ricagno, Stefano; Corazza, Alessandra; Rennella, Enrico; Gumral, Devrim; Mimmi, Maria Chiara; Betto, Elena; Pucillo, Carlo E.M.; Fogolari, Federico; Viglino, Paolo; Raimondi, Sara; Giorgetti, Sofia; Bolognesi, Benedetta; Merlini, Giampaolo; Stoppini, Monica; Bolognesi, Martino; Bellotti, Vittorio. "The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties" J. Mol. Biol. 378, 885-895 (2008).
Assembly members:
w60g-b2m, polymer, 100 residues,  Formula weight is not available
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):
w60g-b2m: MIQRTPKIQVYSRHPAENGK
SNFLNCYVSGFHPSDIEVDL
LKNGERIEKVEHSDLSFSKD
GSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
- assigned_chemical_shifts
 
| Data type | Count | 
| 1H chemical shifts | 690 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | w60g-b2m | 1 | 
Entities:
Entity 1, w60g-b2m 100 residues - Formula weight is not available
| 1 | MET | ILE | GLN | ARG | THR | PRO | LYS | ILE | GLN | VAL | |
| 2 | TYR | SER | ARG | HIS | PRO | ALA | GLU | ASN | GLY | LYS | |
| 3 | SER | ASN | PHE | LEU | ASN | CYS | TYR | VAL | SER | GLY | |
| 4 | PHE | HIS | PRO | SER | ASP | ILE | GLU | VAL | ASP | LEU | |
| 5 | LEU | LYS | ASN | GLY | GLU | ARG | ILE | GLU | LYS | VAL | |
| 6 | GLU | HIS | SER | ASP | LEU | SER | PHE | SER | LYS | ASP | |
| 7 | GLY | SER | PHE | TYR | LEU | LEU | TYR | TYR | THR | GLU | |
| 8 | PHE | THR | PRO | THR | GLU | LYS | ASP | GLU | TYR | ALA | |
| 9 | CYS | ARG | VAL | ASN | HIS | VAL | THR | LEU | SER | GLN | |
| 10 | PRO | LYS | ILE | VAL | LYS | TRP | ASP | ARG | ASP | MET | 
Samples:
sample_1: w60g-b2m 0.5-0.9 mM; phosphate 70 mM; NaCl 100 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.6; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 | 
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 | 
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 | 
Software:
FELIX, Accelrys Software Inc. - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
 
Related Database Links:
| BMRB | 16587 17165 17166 19099 19113 19116 19118 19119 19120 19121 19122 19123 3078 3079 | 
| PDB | |
| DBJ | BAA35182 BAG38125 BAG72952 | 
| EMBL | CAA23830 CAG33347 CAH92078 | 
| GB | AAA51811 AAA87972 AAA88008 AAB25312 AAB35347 | 
| REF | NP_001009066 NP_001127503 NP_004039 XP_004056148 XP_004056149 | 
| SP | P16213 P61769 P61770 P61771 |