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BMRB Entry 34362

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34362

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Title: tSH2 domain of transcription elongation factor Spt6 complexed with tyrosine phosphorylated CTD

Deposition date: 2019-02-24 Original release date: 2020-07-10

Authors: Brazda, P.; Krejcikova, M.; Smirakova, E.; Kubicek, K.; Stefl, R.

Citation: Brazda, P.; Krejcikova, M.; Kasiliauskaite, A.; Smirakova, E.; Klumpler, T.; Vacha, R.; Kubicek, K.; Stefl, R.. "tSH2 domain of transcription elongation factor Spt6 complexed with tyrosine phosphorylated CTD"  . ., .-..

Assembly members:
tSH2 domain of transcription elongation factor Spt6, polymer, 196 residues, 23257.482 Da.
Tyrosine phosphorylated CTD, polymer, 16 residues, 1801.647 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: .

Entity Sequences (FASTA):
tSH2 domain of transcription elongation factor Spt6: SHRVINHPYYFPFNGKQAED YLRSKERGDFVIRQSSRGDD HLAITWKLDKDLFQHVDIQE LEKENPLALGKVLVVEGQRY HDLDQIIVEYLQNKIRLLNE LTSNEKFKAGTKKEVVKFIE DYSKVNPKKSVYYFSLNYEN PGWFYLIFKLNAESKLYIWN VKLTHTGFFLVNYNYPTVIQ LCNGFKTLLKSSNTRN
Tyrosine phosphorylated CTD: PSXSPTSPSXSPTSPS

Data sets:
Data typeCount
13C chemical shifts504
15N chemical shifts156
1H chemical shifts1046

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 196 residues - 23257.482 Da.

1   SERHISARGVALILEASNHISPROTYRTYR
2   PHEPROPHEASNGLYLYSGLNALAGLUASP
3   TYRLEUARGSERLYSGLUARGGLYASPPHE
4   VALILEARGGLNSERSERARGGLYASPASP
5   HISLEUALAILETHRTRPLYSLEUASPLYS
6   ASPLEUPHEGLNHISVALASPILEGLNGLU
7   LEUGLULYSGLUASNPROLEUALALEUGLY
8   LYSVALLEUVALVALGLUGLYGLNARGTYR
9   HISASPLEUASPGLNILEILEVALGLUTYR
10   LEUGLNASNLYSILEARGLEULEUASNGLU
11   LEUTHRSERASNGLULYSPHELYSALAGLY
12   THRLYSLYSGLUVALVALLYSPHEILEGLU
13   ASPTYRSERLYSVALASNPROLYSLYSSER
14   VALTYRTYRPHESERLEUASNTYRGLUASN
15   PROGLYTRPPHETYRLEUILEPHELYSLEU
16   ASNALAGLUSERLYSLEUTYRILETRPASN
17   VALLYSLEUTHRHISTHRGLYPHEPHELEU
18   VALASNTYRASNTYRPROTHRVALILEGLN
19   LEUCYSASNGLYPHELYSTHRLEULEULYS
20   SERSERASNTHRARGASN

Entity 2, entity_2 16 residues - 1801.647 Da.

1   PROSERPTRSERPROTHRSERPROSERPTR
2   SERPROTHRSERPROSER

Samples:

sample_1: spt6, [U-99% 15N], 0.5 ± 0.05 mM

sample_2: spt6, [U-99% 13C; U-99% 15N], 0.5 ± 0.05 mM

sample_3: spt6 0.5 ± 0.05 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7; pressure: 1 Pa; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment

CYANA v3.97-3.98.5, Guntert, Mumenthaler and Wuthrich - structure calculation

AMBER v16, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

TOPSPIN v3.5, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 700 MHz
  • Bruker AvanceIII 850 MHz
  • Bruker AvanceIII 950 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts