BMRB Entry 10010
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10010
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Title: bovine beta-lactoglobulin A34C mutant PubMed: 16368109
Deposition date: 2005-10-31 Original release date: 2007-06-13
Authors: Sakurai, Kazumasa; Goto, Yuji
Citation: Sakurai, Kazumasa; Goto, Yuji. "Dynamics and Mechanism of the Tanford Transition of Bovine beta-Lactoglobulin Studied using Heteronuclear NMR Spectroscopy" J. Mol. Biol. 356, 483-496 (2006).
Assembly members:
BLG_A34C, polymer, 165 residues, 18400 Da.
Natural source: Common Name: Cow Taxonomy ID: 9913 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bos taurus
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
BLG_A34C: EAEAYVTQTMKGLDIQKVAG
TWYSLAMAASDISLLDCQSA
PLRVYVEELKPTPEGDLEIL
LQKWENDECAQKKIIAEKTK
IPAVFKIDALNENKVLVLDT
DYKKYLLFCMENSAEPEQSL
VCQCLVRTPEVDDEALEKFD
KALKALPMHIRLSFNPTQLE
EQCHI
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 463 |
15N chemical shifts | 147 |
1H chemical shifts | 147 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | BLG A34C, 1 | 1 |
2 | BLG A34C, 2 | 1 |
Entities:
Entity 1, BLG A34C, 1 165 residues - 18400 Da.
The first three residues are signal sequence necessary for the expression. The native sequence numbering starts at the forth residue. -3 EAE -1 1 AYVTQ TMKGL DIQKV AGTWY 20 21 SLAMA ASDIS LLDAQ SAPLR 40 41 VYVEE LKPTP EGDLE ILLQK 60 61 WENDE CAQKK IIAEK TKIPA 80 81 VFKID ALNEN KVLVL DTDYK 100 101 KYLLF CMENS AEPEQ SLVCQ 120 121 CLVRT PEVDD EALEK FDKAL 140 141 KALPM HIRLS FNPTQ LEEQC 160 161 HI 162
1 | GLU | ALA | GLU | ALA | TYR | VAL | THR | GLN | THR | MET | ||||
2 | LYS | GLY | LEU | ASP | ILE | GLN | LYS | VAL | ALA | GLY | ||||
3 | THR | TRP | TYR | SER | LEU | ALA | MET | ALA | ALA | SER | ||||
4 | ASP | ILE | SER | LEU | LEU | ASP | CYS | GLN | SER | ALA | ||||
5 | PRO | LEU | ARG | VAL | TYR | VAL | GLU | GLU | LEU | LYS | ||||
6 | PRO | THR | PRO | GLU | GLY | ASP | LEU | GLU | ILE | LEU | ||||
7 | LEU | GLN | LYS | TRP | GLU | ASN | ASP | GLU | CYS | ALA | ||||
8 | GLN | LYS | LYS | ILE | ILE | ALA | GLU | LYS | THR | LYS | ||||
9 | ILE | PRO | ALA | VAL | PHE | LYS | ILE | ASP | ALA | LEU | ||||
10 | ASN | GLU | ASN | LYS | VAL | LEU | VAL | LEU | ASP | THR | ||||
11 | ASP | TYR | LYS | LYS | TYR | LEU | LEU | PHE | CYS | MET | ||||
12 | GLU | ASN | SER | ALA | GLU | PRO | GLU | GLN | SER | LEU | ||||
13 | VAL | CYS | GLN | CYS | LEU | VAL | ARG | THR | PRO | GLU | ||||
14 | VAL | ASP | ASP | GLU | ALA | LEU | GLU | LYS | PHE | ASP | ||||
15 | LYS | ALA | LEU | LYS | ALA | LEU | PRO | MET | HIS | ILE | ||||
16 | ARG | LEU | SER | PHE | ASN | PRO | THR | GLN | LEU | GLU | ||||
17 | GLU | GLN | CYS | HIS | ILE |
Samples:
sample_1: beta-lactoglobulin A34C polypeptide, [U-99% 13C; U-99.3% 15N], 2 ± 0.2 mM; Hydrochloric acid7 9 mM
conditions_for_BLG_A34C_at_pH_6.5: ionic strength: 0.000 M; pH: 6.5; temperature: 313 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
1H15N HSQC | sample_1 | not available | conditions_for_BLG_A34C_at_pH_6.5 |
CBCA(CO)NH | sample_1 | not available | conditions_for_BLG_A34C_at_pH_6.5 |
HNCACB | sample_1 | not available | conditions_for_BLG_A34C_at_pH_6.5 |
HNCO | sample_1 | not available | conditions_for_BLG_A34C_at_pH_6.5 |
HNCACO | sample_1 | not available | conditions_for_BLG_A34C_at_pH_6.5 |
Software:
pipp.com -
NMR spectrometers:
- Bruker DRX 800 MHz
Related Database Links:
PDB | |
EMBL | CAA06532 CAA32835 CAA88303 CAY39357 |
GB | AAA30411 AAI08214 ABF48380 ACG59280 AFB74990 |
PRF | 0601265A |
REF | NP_001277893 NP_776354 XP_005888577 XP_006062245 |
SP | P02754 P02755 |
TPG | DAA24277 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts