BMRB Entry 19842

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19842

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Title:
Backbone and sidechain 1H, 13C, and 15N chemical shift assignments for the HEAT2 domain of human eIF4G
Deposition date:
2014-03-06
Original release date:
2016-11-28
Authors:
Edmonds, Katherine; Wagner, Gerhard
Citation:

Citation: Edmonds, Katherine; Wagner, Gerhard. "1H, 13C, and 15N backbone and sidechain chemical shift assignments for the HEAT2 domain of human eIF4GI"  Biomol. NMR Assignments 9, 157-160 (2015).
PubMed: 24929364

Assembly members:

Assembly members:
HEAT2_domain, polymer, 193 residues, 21600.1 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: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HEAT2_domain: GAALSEEELEKKSKAIIEEY LHLNDMKEAVQCVQELASPS LLFIFVRHGVESTLERSAIA REHMGQLLHQLLCAGHLSTA QYYQGLYEILELAEDMEIDI PHVWLYLAELVTPILQEGGV PMGELFREITKPLRPLGKAA SLLLEILGLLCKSMGPKKVG TLWREAGLSWKEFLPEGQDI GAFVAEQKVEYTL

Data sets:
Data typeCount
13C chemical shifts889
15N chemical shifts207
1H chemical shifts1451

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HEAT2 domain, 11
2HEAT2 domain, 21

Entities:

Entity 1, HEAT2 domain, 1 193 residues - 21600.1 Da.

1   GLYALAALALEUSERGLUGLUGLULEUGLU
2   LYSLYSSERLYSALAILEILEGLUGLUTYR
3   LEUHISLEUASNASPMETLYSGLUALAVAL
4   GLNCYSVALGLNGLULEUALASERPROSER
5   LEULEUPHEILEPHEVALARGHISGLYVAL
6   GLUSERTHRLEUGLUARGSERALAILEALA
7   ARGGLUHISMETGLYGLNLEULEUHISGLN
8   LEULEUCYSALAGLYHISLEUSERTHRALA
9   GLNTYRTYRGLNGLYLEUTYRGLUILELEU
10   GLULEUALAGLUASPMETGLUILEASPILE
11   PROHISVALTRPLEUTYRLEUALAGLULEU
12   VALTHRPROILELEUGLNGLUGLYGLYVAL
13   PROMETGLYGLULEUPHEARGGLUILETHR
14   LYSPROLEUARGPROLEUGLYLYSALAALA
15   SERLEULEULEUGLUILELEUGLYLEULEU
16   CYSLYSSERMETGLYPROLYSLYSVALGLY
17   THRLEUTRPARGGLUALAGLYLEUSERTRP
18   LYSGLUPHELEUPROGLUGLYGLNASPILE
19   GLYALAPHEVALALAGLUGLNLYSVALGLU
20   TYRTHRLEU

Samples:

HCN-H2O: HEAT2 domain, [U-13C; U-15N], 2 mM; TRIS 20 mM; sodium chloride 150 mM; EDTA 1 mM; DTT 1 mM; H2O 95%; D2O 5%

HCN-D2O: HEAT2 domain, [U-13C; U-15N], 2 mM; TRIS 20 mM; sodium chloride 150 mM; EDTA, [U-2H], 1 mM; DTT, [U-2H], 1 mM; D2O 100%

DCN-H2O: HEAT2 domain, [U-13C; U-15N; U-2H], 1 mM; TRIS 20 mM; sodium chloride 150 mM; EDTA 1 mM; DTT 1 mM; H2O 95%; D2O 5%

ILV-D2O: HEAT2 domain, [U-12C; U-15N; U-2H ILV-Me 1H,13C], 2 mM; TRIS 20 mM; sodium chloride 150 mM; EDTA, [U-2H], 1 mM; DTT, [U-2H], 1 mM; D2O 100%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBDCN-H2Oisotropicsample_conditions_1
3D HN(COCA)CBDCN-H2Oisotropicsample_conditions_1
3D HNCADCN-H2Oisotropicsample_conditions_1
3D HNCODCN-H2Oisotropicsample_conditions_1
3D HN(CO)CADCN-H2Oisotropicsample_conditions_1
3D HN(CA)CODCN-H2Oisotropicsample_conditions_1
2D 1H-15N HSQCDCN-H2Oisotropicsample_conditions_1
3D HBHA(CO)NHHCN-H2Oisotropicsample_conditions_1
3D C(CO)NHHCN-H2Oisotropicsample_conditions_1
3D H(CCO)NHHCN-H2Oisotropicsample_conditions_1
2D 1H-15N HSQCHCN-H2Oisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticHCN-D2Oisotropicsample_conditions_1
3D HCCH-TOCSYHCN-D2Oisotropicsample_conditions_1
3D HCCH-COSYHCN-D2Oisotropicsample_conditions_1
3D HNHAHCN-H2Oisotropicsample_conditions_1
3D HNHBHCN-H2Oisotropicsample_conditions_1
2D 1H-13C HSQC aromaticHCN-D2Oisotropicsample_conditions_1
2D HBCBCGCDCEHEHCN-D2Oisotropicsample_conditions_1
2D HBCBCGCDHDHCN-D2Oisotropicsample_conditions_1
2D hCaNHCN-H2Oisotropicsample_conditions_1
3D 1H-15N NOESYHCN-H2Oisotropicsample_conditions_1
3D 1H-13C NOESY aromaticHCN-D2Oisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticHCN-D2Oisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticHCN-D2Oisotropicsample_conditions_1
4D 1H-13C NOESY aliphaticILV-D2Oisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticILV-D2Oisotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - Secondary structure assignment

VNMR, Varian - collection

xwinnmr, Bruker Biospin - collection

VNMRJ, Varian - collection

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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