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Biological Magnetic Resonance Data Bank


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BMRB Entry 15607

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15607
MolProbity Validation Chart

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Title: Putative 32 kDa myrosinase binding protein At3g16450.1 from Arabidopsis   PubMed: 19021763

Deposition date: 2007-12-28 Original release date: 2008-11-25

Authors: Takeda, Mitsuhiro; Sugimori, Nozomi; Torizawa, Takuya; Terauchi, Tsutomu; Ono, Akira; Yagi, Hirokazu; Yamaguchi, Yoshiki; Kato, Koichi; Ikeya, Teppei; Guntert, Peter; Aceti, David; Markley, John; Kainosho, Masatsune

Citation: Takeda, Mitsuhiro; Sugimori, Nozomi; Torizawa, Takuya; Terauchi, Tsutomu; Ono, Akira; Yagi, Hirokazu; Yamaguchi, Yoshiki; Kato, Koichi; Ikeya, Teppei; Jee, Jungoo; Guntert, Peter; Aceti, David; Markley, John; Kainosho, Masatsune. "Structure of the putative 32 kDa myrosinase-binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR."  FEBS J. 275, 5873-5884 (2008).

Assembly members:
At3g16450.1, polymer, 299 residues, 31936.729 Da.

Natural source:   Common Name: not available   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free

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

Data sets:
Data typeCount
13C chemical shifts766
15N chemical shifts300
1H chemical shifts1397

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1At3g164501

Entities:

Entity 1, At3g16450 299 residues - 31936.729 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, stereo-array isotope labeling (SAIL), 0.2 mM; potassium chloride 100 mM; bis-TRIS-d19, [U-99% 2H], 20 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 bar; temperature: 300.65 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

CYANA v2.2, Guntert, Mumenthaler and Wuthrich - structure solution

CYANA, Goddard - chemical shift assignment

OPALP v1.4, (OPALP) Koradi, Billeter, Guntert - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

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

Download simulated HSQC data in one of the following formats:
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