BMRB Entry 25029
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25029
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Title: Specific and Non-Specific Interactions in Ultra-Weak Protein-Protein Associations Revealed by Solvent Paramagnetic Relaxation Enhancements PubMed: 24969589
Deposition date: 2014-06-19 Original release date: 2014-06-24
Authors: Johansson, Helle; Jensen, Malene; Gesmar, Henrik; Meier, Sebastian; Vinther, Joachim; Keeler, Camille; Hodsdon, Michael; Led, Jens
Citation: Johansson, Helle; Jensen, Malene Ringkjobing; Gesmar, Henrik; Meier, Sebastian; Vinther, Joachim; Keeler, Camille; Hodsdon, Michael; Led, Jens. "Specific and nonspecific interactions in ultraweak protein-protein associations revealed by solvent paramagnetic relaxation enhancements." J. Am. Chem. Soc. 136, 10277-10286 (2014).
Assembly members:
hGH, polymer, 191 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):
hGH: FPTIPLSRLFDNAMLRAHRL
HQLAFDTYQEFEEAYIPKEQ
KYSFLQNPQTSLCFSESIPT
PSNREETQQKSNLELLRISL
LLIQSWLEPVQFLRSVFANS
LVYGASDSNVYDLLKDLEEG
IQTLMGRLEDGSPRTGQIFK
QTYSKFDTNSHNDDALLKNY
GLLYCFRKDMDKVETFLRIV
QCRSVEGSCGF
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 455 |
1H chemical shifts | 148 |
15N chemical shifts | 148 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | hGH | 1 |
Entities:
Entity 1, hGH 191 residues - Formula weight is not available
1 | PHE | PRO | THR | ILE | PRO | LEU | SER | ARG | LEU | PHE | ||||
2 | ASP | ASN | ALA | MET | LEU | ARG | ALA | HIS | ARG | LEU | ||||
3 | HIS | GLN | LEU | ALA | PHE | ASP | THR | TYR | GLN | GLU | ||||
4 | PHE | GLU | GLU | ALA | TYR | ILE | PRO | LYS | GLU | GLN | ||||
5 | LYS | TYR | SER | PHE | LEU | GLN | ASN | PRO | GLN | THR | ||||
6 | SER | LEU | CYS | PHE | SER | GLU | SER | ILE | PRO | THR | ||||
7 | PRO | SER | ASN | ARG | GLU | GLU | THR | GLN | GLN | LYS | ||||
8 | SER | ASN | LEU | GLU | LEU | LEU | ARG | ILE | SER | LEU | ||||
9 | LEU | LEU | ILE | GLN | SER | TRP | LEU | GLU | PRO | VAL | ||||
10 | GLN | PHE | LEU | ARG | SER | VAL | PHE | ALA | ASN | SER | ||||
11 | LEU | VAL | TYR | GLY | ALA | SER | ASP | SER | ASN | VAL | ||||
12 | TYR | ASP | LEU | LEU | LYS | ASP | LEU | GLU | GLU | GLY | ||||
13 | ILE | GLN | THR | LEU | MET | GLY | ARG | LEU | GLU | ASP | ||||
14 | GLY | SER | PRO | ARG | THR | GLY | GLN | ILE | PHE | LYS | ||||
15 | GLN | THR | TYR | SER | LYS | PHE | ASP | THR | ASN | SER | ||||
16 | HIS | ASN | ASP | ASP | ALA | LEU | LEU | LYS | ASN | TYR | ||||
17 | GLY | LEU | LEU | TYR | CYS | PHE | ARG | LYS | ASP | MET | ||||
18 | ASP | LYS | VAL | GLU | THR | PHE | LEU | ARG | ILE | VAL | ||||
19 | GLN | CYS | ARG | SER | VAL | GLU | GLY | SER | CYS | GLY | ||||
20 | PHE |
Samples:
sample_1: hGH, [U-100% 13C; U-100% 15N], 0.175 mM; NaCl 25 mM; NaH2PO4 15.4 mM; Na2HPO4 9.5 mM; NaN3 1.54 mM
sample_conditions_1: temperature: 298 K; pH: 7; pressure: 1 atm; ionic strength: 0.0706 M
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
BMRB | 4689 |
PDB | |
DBJ | BAJ21175 |
EMBL | CAA23778 CAA23779 |
GB | AAA52549 AAA72260 AAA98618 AAC42099 AAF23135 |
PRF | 1403262B |
REF | NP_000506 NP_001184093 NP_001277233 XP_002827754 XP_003262698 |
SP | P01241 P58756 |
TPE | CDW51387 CDW51389 CDW51391 CDW51396 CDW51399 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts