BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16029

Title: Solution NMR structure of ubiquitin-like domain of Arabidopsis thaliana protein At2g32350. Northeast Structural Genomics Consortium target AR3433A

Authors: Eletsky, Alexander; Mills, Jeffrey; Sukumaran, Dinesh; Hua, Jia; Shastry, Ritu; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Everret, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas

Citation: Eletsky, Alexander; Mills, Jeffrey; Sukumaran, Dinesh; Hua, Jia; Shastry, Ritu; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Everret, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of ubiquitin-like domain of Arabidopsis thaliana protein At2g32350."  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:
ar3433a_protein, polymer, 94 residues, 11005.629 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
ar3433a_protein: MGHHHHHHSHAAVRKIHVTV KFPSKQFTVEVDRTETVSSL KDKIHIVENTPIKRMQLYYS GIELADDYRNLNEYGITEFS EIVVFLKSINRAKD

Data sets:
Data typeCount
13C chemical shifts381
15N chemical shifts91
1H chemical shifts627

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ar3433a_protein1

Entities:

Entity 1, ar3433a_protein 94 residues - 11005.629 Da.

Residues 1-10 represent a non-native affinity tag. This is a Ubiquitin-like domain (70-153) of At2g32350 protein

1   METGLYHISHISHISHISHISHISSERHIS
2   ALAALAVALARGLYSILEHISVALTHRVAL
3   LYSPHEPROSERLYSGLNPHETHRVALGLU
4   VALASPARGTHRGLUTHRVALSERSERLEU
5   LYSASPLYSILEHISILEVALGLUASNTHR
6   PROILELYSARGMETGLNLEUTYRTYRSER
7   GLYILEGLULEUALAASPASPTYRARGASN
8   LEUASNGLUTYRGLYILETHRGLUPHESER
9   GLUILEVALVALPHELEULYSSERILEASN
10   ARGALALYSASP

Samples:

NC: ar3433a protein, [U-100% 13C; U-100% 15N], 1.09 mM; DSS 50 uM; sodium chloride 200 mM; MES 20 mM; calcium cloride 5 mM; DTT 10 mM; sodium azide 0.02%; protease inhibitors 1 X; H2O 90%; D2O 10%

NC5: ar3433a protein, [U-5% 13C; U-100% 15N], 1.15 mM; DSS 50 uM; sodium chloride 200 mM; MES 20 mM; calcium cloride 5 mM; DTT 10 mM; sodium azide 0.02%; protease inhibitors 1 X; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 215 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQC (ali)NCisotropicsample_conditions_1
2D 1H-13C CT-HSQC (ali)NCisotropicsample_conditions_1
2D 1H-13C HSQC (aro)NCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HCCH-COSY (ali)NCisotropicsample_conditions_1
3D HCCH-TOCSYNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY (aro)NCisotropicsample_conditions_1
3D HCCH-COSY (aro)NCisotropicsample_conditions_1
3D 1H-15N,13Cali,13Caro NOESYNCisotropicsample_conditions_1
2D 1H-15N LR-HSQC (His)NCisotropicsample_conditions_1
2D 1H-13C CT-HSQC (ali)NC5isotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

PROSA v6.0.2, Guntert - processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TALOS v2003.027.13.05, Cornilescu, Delaglio and Bax - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution, structure validation

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.3, Bhattacharya and Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
GB AAC69943 AEC08672
REF NP_180794