BMRB Entry 6140

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6140

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
1H, 13C and 15N backbone assignment of a 32 kDa hypothetical protein from Arabidopsis thaliana, At3g16450.1
Deposition date:
2004-03-16
Original release date:
2004-12-16
Authors:
Sugimori, Nozomi; Torizawa, Takuya; Aceti, David; Thao, Sandy; Markley, John; Kainosho, Masatsune
Citation:

Citation: Sugimori, Nozomi; Torizawa, Takuya; Aceti, David; Thao, Sandy; Markley, John; Kainosho, Masatsune. "1H, 13C and 15N backbone assignment of a 32 kDa hypothetical protein from Arabidopsis thaliana, At3g16450.1"  J. Biomol. NMR 30, 357-358 (2004).

Assembly members:

Assembly members:
At3g16450.1, polymer, 299 residues, 31891.48 Da.

Natural source:

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Esherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
At3g16450.1: AQKVEAGGGAGGASWDDGVH DGVRKVHVGQGQDGVSSINV VYAKDSQDVEGGEHGKKTLL GFETFEVDADDYIVAVQVTY DNVFGQDSDIITSITFNTFK GKTSPPYGLETQKKFVLKDK NGGKLVGFHGRAGEALYALG AYFATTTTPVTPAKKLSAIG GDEGTAWDDGAYDGVKKVYV GQGQDGISAVKFEYNKGAEN IVGGEHGKPTLLGFEEFEID YPSEYITAVEGTYDKIFGSD GLIITMLRFKTNKQTSAPFG LEAGTAFELKEEGHKIVGFH GKASELLHQFGVHVMPLTN

Data sets:
Data typeCount
1H chemical shifts607
13C chemical shifts805
15N chemical shifts291

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1At3g16450.11

Entities:

Entity 1, At3g16450.1 299 residues - 31891.48 Da.

1   ALAGLNLYSVALGLUALAGLYGLYGLYALA
2   GLYGLYALASERTRPASPASPGLYVALHIS
3   ASPGLYVALARGLYSVALHISVALGLYGLN
4   GLYGLNASPGLYVALSERSERILEASNVAL
5   VALTYRALALYSASPSERGLNASPVALGLU
6   GLYGLYGLUHISGLYLYSLYSTHRLEULEU
7   GLYPHEGLUTHRPHEGLUVALASPALAASP
8   ASPTYRILEVALALAVALGLNVALTHRTYR
9   ASPASNVALPHEGLYGLNASPSERASPILE
10   ILETHRSERILETHRPHEASNTHRPHELYS
11   GLYLYSTHRSERPROPROTYRGLYLEUGLU
12   THRGLNLYSLYSPHEVALLEULYSASPLYS
13   ASNGLYGLYLYSLEUVALGLYPHEHISGLY
14   ARGALAGLYGLUALALEUTYRALALEUGLY
15   ALATYRPHEALATHRTHRTHRTHRPROVAL
16   THRPROALALYSLYSLEUSERALAILEGLY
17   GLYASPGLUGLYTHRALATRPASPASPGLY
18   ALATYRASPGLYVALLYSLYSVALTYRVAL
19   GLYGLNGLYGLNASPGLYILESERALAVAL
20   LYSPHEGLUTYRASNLYSGLYALAGLUASN
21   ILEVALGLYGLYGLUHISGLYLYSPROTHR
22   LEULEUGLYPHEGLUGLUPHEGLUILEASP
23   TYRPROSERGLUTYRILETHRALAVALGLU
24   GLYTHRTYRASPLYSILEPHEGLYSERASP
25   GLYLEUILEILETHRMETLEUARGPHELYS
26   THRASNLYSGLNTHRSERALAPROPHEGLY
27   LEUGLUALAGLYTHRALAPHEGLULEULYS
28   GLUGLUGLYHISLYSILEVALGLYPHEHIS
29   GLYLYSALASERGLULEULEUHISGLNPHE
30   GLYVALHISVALMETPROLEUTHRASN

Samples:

sample_1: At3g16450.1, [U-98% 13C; U-99.6% 15N], 0.76 mM; Bis-Tris, [U-98% D], 20 mM; potasium chloride 100 mM; D2O 10%; H2O 90%

cond_set_1: pH: 6.8; temperature: 300.5 K; ionic strength: 0.15 M

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCsample_1not availablecond_set_1
HNCOsample_1not availablecond_set_1
HN(CA)COsample_1not availablecond_set_1
CT-HNCAsample_1not availablecond_set_1
CT-HN(CO)CAsample_1not availablecond_set_1
HNCACBsample_1not availablecond_set_1
HN(CO)CACBsample_1not availablecond_set_1
HBHANHsample_1not availablecond_set_1
HBHA(CO)NHsample_1not availablecond_set_1

Software:

XWINNMR v3.5 - data processing

SPARKY v3.106 - analysis

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 15607
PDB
DBJ BAB01144 BAH20032
GB AAB63632 AAK55736 AAM65267 AAM91376 AEE75817
REF NP_001030711 NP_188266 NP_850596
SP O04311
AlphaFold O04311

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