BMRB Entry 16173

Title:
The structure of the cataract causing P23T mutant of human gamma-D crystallin
Deposition date:
2009-02-12
Original release date:
2009-03-05
Authors:
Jung, Jinwon; Byeon, In-Ja; Wang, Yongting; King, Jonathan; Gronenborn, Angela
Citation:

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).
PubMed: 19216553

Assembly members:

Assembly members:
p23t, polymer, 182 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16b

Data sets:
Data typeCount
13C chemical shifts678
15N chemical shifts191
1H chemical shifts1149

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1p23t1

Entities:

Entity 1, p23t 182 residues - Formula weight is not available

1   METLYSHISHISHISHISHISHISGLNGLY
2   LYSILETHRLEUTYRGLUASPARGGLYPHE
3   GLNGLYARGHISTYRGLUCYSSERSERASP
4   HISTHRASNLEUGLNPROTYRLEUSERARG
5   CYSASNSERALAARGVALASPSERGLYCYS
6   TRPMETLEUTYRGLUGLNPROASNTYRSER
7   GLYLEUGLNTYRPHELEUARGARGGLYASP
8   TYRALAASPHISGLNGLNTRPMETGLYLEU
9   SERASPSERVALARGSERCYSARGLEUILE
10   PROHISSERGLYSERHISARGILEARGLEU
11   TYRGLUARGGLUASPTYRARGGLYGLNMET
12   ILEGLUPHETHRGLUASPCYSSERCYSLEU
13   GLNASPARGPHEARGPHEASNGLUILEHIS
14   SERLEUASNVALLEUGLUGLYSERTRPVAL
15   LEUTYRGLULEUSERASNTYRARGGLYARG
16   GLNTYRLEULEUMETPROGLYASPTYRARG
17   ARGTYRGLNASPTRPGLYALATHRASNALA
18   ARGVALGLYSERLEUARGARGVALILEASP
19   PHESER

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:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2anisotropicsample_conditions_1
3D HN(CO)CAsample_2anisotropicsample_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
AlphaFold P07320

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks