BMRB Entry 19910

Title:
Solution structure of the P22S mutant of N-terminal CS domain of human Shq1
Deposition date:
2014-04-16
Original release date:
2015-01-12
Authors:
Singh, Mahavir; Wang, Zhonghua; Cascio, Duilio; Feigon, Juli
Citation:

Citation: Singh, Mahavir; Wang, Zhonghua; Cascio, Duilio; Feigon, Juli. "Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1"  J. Mol. Biol. ., .-..
PubMed: 25553844

Assembly members:

Assembly members:
P22S_mutant_of_human_Shq1_CS_domain, polymer, 133 residues, 10870.401 Da.

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: pET41 Ek/LIC

Data sets:
Data typeCount
1H chemical shifts549
13C chemical shifts366
15N chemical shifts90

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1P22S mutant of N-terminal CS domain of human Shq11

Entities:

Entity 1, P22S mutant of N-terminal CS domain of human Shq1 133 residues - 10870.401 Da.

Residues -36 to 0 represent a non-native residues after removal of Gst affinity tag by thrombin

1   GLYSERTHRALAILEGLYMETLYSGLUTHR
2   ALAALAALALYSPHEGLUARGGLNHISMET
3   ASPSERPROASPLEUGLYTHRGLYGLYGLY
4   SERGLYASPASPASPASPLYSMETLEUTHR
5   PROALAPHEASPLEUSERGLNASPPROASP
6   PHELEUTHRILEALAILEARGVALSERTYR
7   ALAARGVALSERGLUPHEASPVALTYRPHE
8   GLUGLYSERASPPHELYSPHETYRALALYS
9   PROTYRPHELEUARGLEUTHRLEUPROGLY
10   ARGILEVALGLUASNGLYSERGLUGLNGLY
11   SERTYRASPALAASPLYSGLYILEPHETHR
12   ILEARGLEUPROLYSGLUTHRPROGLYGLN
13   HISPHEGLUGLYLEUASNMETLEUTHRALA
14   LEULEUALA

Samples:

sample_1: P22S mutant of human Shq1 CS domain, [U-15N], 0.5 – 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; H2O 95%; D2O 5%

sample_2: P22S mutant of human Shq1 CS domain, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; H2O 95%; D2O 5%

sample_3: P22S mutant of human Shq1 CS domain, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; D2O 100%

sample_conditions_1: temperature: 298 K; pH: 7; pressure: 1 atm; ionic strength: 100 mM

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection, processing, data analysis

TOPSPIN, Bruker Biospin - collection, data analysis, processing

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, chemical shift assignment, processing

SPARKY, Goddard - data analysis, chemical shift assignment, chemical shift calculation

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift calculation, data analysis, processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 500 MHz

Related Database Links:

BMRB 25167
PDB
GB AAH17204 AAH17274 AAH25270 AAH32671 AAH39830
REF NP_060600 XP_001082636 XP_001141951 XP_003264945 XP_003780373
SP Q6PI26
AlphaFold Q6PI26

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