BMRB Entry 16173
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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/BMR16173
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Title: The structure of the cataract causing P23T mutant of human gamma-D crystallin PubMed: 19216553
Deposition date: 2009-02-12 Original release date: 2009-03-05
Authors: Jung, Jinwon; Byeon, In-Ja; Wang, Yongting; King, Jonathan; Gronenborn, Angela
Citation: Jung, Jinwon; Byeon, In-Ja; Wang, Yongting; King, Jonathan; Gronenborn, Angela. "The structure of the cataract causing P23T mutant of HgD crystallin exhibits local distinctive conformational and dynamic changes." Biochemistry 48, 2597-2609 (2009).
Assembly members:
p23t, polymer, 182 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):
p23t: MKHHHHHHQGKITLYEDRGF
QGRHYECSSDHTNLQPYLSR
CNSARVDSGCWMLYEQPNYS
GLQYFLRRGDYADHQQWMGL
SDSVRSCRLIPHSGSHRIRL
YEREDYRGQMIEFTEDCSCL
QDRFRFNEIHSLNVLEGSWV
LYELSNYRGRQYLLMPGDYR
RYQDWGATNARVGSLRRVID
FS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 678 |
| 15N chemical shifts | 191 |
| 1H chemical shifts | 1149 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | p23t | 1 |
Entities:
Entity 1, p23t 182 residues - Formula weight is not available
| 1 | MET | LYS | HIS | HIS | HIS | HIS | HIS | HIS | GLN | GLY | ||||
| 2 | LYS | ILE | THR | LEU | TYR | GLU | ASP | ARG | GLY | PHE | ||||
| 3 | GLN | GLY | ARG | HIS | TYR | GLU | CYS | SER | SER | ASP | ||||
| 4 | HIS | THR | ASN | LEU | GLN | PRO | TYR | LEU | SER | ARG | ||||
| 5 | CYS | ASN | SER | ALA | ARG | VAL | ASP | SER | GLY | CYS | ||||
| 6 | TRP | MET | LEU | TYR | GLU | GLN | PRO | ASN | TYR | SER | ||||
| 7 | GLY | LEU | GLN | TYR | PHE | LEU | ARG | ARG | GLY | ASP | ||||
| 8 | TYR | ALA | ASP | HIS | GLN | GLN | TRP | MET | GLY | LEU | ||||
| 9 | SER | ASP | SER | VAL | ARG | SER | CYS | ARG | LEU | ILE | ||||
| 10 | PRO | HIS | SER | GLY | SER | HIS | ARG | ILE | ARG | LEU | ||||
| 11 | TYR | GLU | ARG | GLU | ASP | TYR | ARG | GLY | GLN | MET | ||||
| 12 | ILE | GLU | PHE | THR | GLU | ASP | CYS | SER | CYS | LEU | ||||
| 13 | GLN | ASP | ARG | PHE | ARG | PHE | ASN | GLU | ILE | HIS | ||||
| 14 | SER | LEU | ASN | VAL | LEU | GLU | GLY | SER | TRP | VAL | ||||
| 15 | LEU | TYR | GLU | LEU | SER | ASN | TYR | ARG | GLY | ARG | ||||
| 16 | GLN | TYR | LEU | LEU | MET | PRO | GLY | ASP | TYR | ARG | ||||
| 17 | ARG | TYR | GLN | ASP | TRP | GLY | ALA | THR | ASN | ALA | ||||
| 18 | ARG | VAL | GLY | SER | LEU | ARG | ARG | VAL | ILE | ASP | ||||
| 19 | PHE | SER |
Samples:
sample_1: p23t, [U-99% 13C; U-99% 15N], 0.2-0.8 mM; sodium phosphate 20 mM; DTT 5 mM; D2O 5%; H2O 95%
sample_2: p23t, [U-99% 13C; U-99% 15N], 0.2-0.8 mM; sodium phosphate 20 mM; DTT 5 mM; D2O, [U-2H], 5%; H2O, [U-2H], 5%; Pentaethylene glycol monododecyl ether 5%; hexanol 5.2%
sample_conditions_1: ionic strength: 0.025333 M; pH: 6.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | anisotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | anisotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
CYANA, Brunger A. T. et.al. - geometry optimization, structure solution
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| GB | AAA52112 AAB38686 AAI17339 AAI17341 AAY24041 |
| REF | NP_001129137 NP_008822 XP_003820863 XP_004033174 |
| SP | P07320 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts