BMRB Entry 16101

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16101
MolProbity Validation Chart

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Title:
NMR solution Structure of O64736 protein from Arabidopsis thaliana:Northeast Structural Genomics Consortium MEGA Target AR3445A
Deposition date:
2008-12-31
Original release date:
2009-02-19
Authors:
G. V. T., Swapna; Shastry, Ritu; Foote, E. L.; Ciccosanti, Colleen; Jiang, Mei; Xiao, Rong; Nair, R; Everett, John; Huang, Yuanpeng; Acton, Thomas; Rost, B.; Montelione, Gaetano
Citation:

Citation: G. V. T., Swapna; Montelione, Gaetano. "NMR solution structure of O64736 protein from Arabidopsis thaliana"  .

Assembly members:

Assembly members:
AR3445A, polymer, 85 residues, 9196.865 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: Escherichia coli   Vector: pET 14-15C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AR3445A: MGHHHHHHSHSTIKLTVKFG GKSIPLSVSPDCTVKDLKSQ LQPITNVLPRGQKLIFKGKV LVETSTLKQSDVGSGAKLML MASQG

Data sets:
Data typeCount
13C chemical shifts342
15N chemical shifts76
1H chemical shifts560

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AR3445A1

Entities:

Entity 1, AR3445A 85 residues - 9196.865 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   SERTHRILELYSLEUTHRVALLYSPHEGLY
3   GLYLYSSERILEPROLEUSERVALSERPRO
4   ASPCYSTHRVALLYSASPLEULYSSERGLN
5   LEUGLNPROILETHRASNVALLEUPROARG
6   GLYGLNLYSLEUILEPHELYSGLYLYSVAL
7   LEUVALGLUTHRSERTHRLEULYSGLNSER
8   ASPVALGLYSERGLYALALYSLEUMETLEU
9   METALASERGLNGLY

Samples:

sample_1: sample_1, [U-100% 13C; U-100% 15N], 1.8 ± 0.1 mM; CaCL2 5.0 mM; NACL 200 mM

sample_2: sample_2, [U-10% 13C; U-100% 15N], 1.80 ± 0.1 mM; CaCL2 5.0 mM; NACL 200 mM

sample_conditions_1: ionic strength: 205 M; pH: 6.5; pressure: 1.0 atm; temperature: 293 K

sample_conditions_2: ionic strength: 205 M; pH: 6.5; pressure: 1.0 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

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

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

CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.1, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAC16962 AEC08345 EFH55508
REF NP_001189636 XP_002879249
SP P0C895
AlphaFold P0C895

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