Mass: 10852.132 Da / Num. of mol.: 1 / Fragment: sequence database residues 10-96 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: At3g10220 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)+ Magic / References: UniProt: Q67Z52
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR Details: This is a methods development target from the Northeast Structural Genomics Consortium. RMSD of the structure was calculated on only the core residues (13-26,29-37,57-63,67-73,77,88-95) as ...Details: This is a methods development target from the Northeast Structural Genomics Consortium. RMSD of the structure was calculated on only the core residues (13-26,29-37,57-63,67-73,77,88-95) as obtained from FindCore software (Ref: Snyder et al., Proteins: Structure, Function and Bioinformatics, Vol 59, 2005, 673-686).
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
3
3D 1H-15N NOESY
1
2
1
3D 1H-13Caliphatic NOESY
1
3
1
3D 1H-13C aromatic NOESY
1
4
1
2D 1H-15N HSQC
1
5
1
2D 1H-13C HSQC
1
6
3
2D 1H-15N HSQC
1
7
3
2D 1H-13C HSQC
1
8
3
3DHBHA(CO)NH
1
9
3
3DCBCA(CO)NH
1
10
3
(4,3)D GFT-HNNCABCA
1
11
3
(4,3)D GFT-CABCA(CO)NHN
1
12
3
3D HNCO
1
13
3
3D HNCA
1
14
2
3D HN(CA)CB
1
15
4
3D HNHA
1
16
3
3DH(CCO)NH
1
17
3
3D (H)CCH-TOCSY
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
0.78 mM [U-100% 13C; U-100% 15N] AR3436A, 90% H2O/10% D2O
90% H2O/10% D2O
2
0.95 mM [U-100% 13C; U-100% 15N] AR3436A, 90% H2O/10% D2O
90% H2O/10% D2O
3
0.4 mM [U-100% 13C; U-100% 15N] AR3436A, 90% H2O/10% D2O
90% H2O/10% D2O
4
0.56 mM [U-10% 13C; U-100% 15N] AR3436A, 90% H2O/10% D2O
Method: simulated annealing / Software ordinal: 1 Details: The structure was obtained using triple resonance NMR spectroscopy. GFT-NMR experiments were used for backbone assignments. Automated NOESY assignments were made using AUTOSTRUCTURE and ...Details: The structure was obtained using triple resonance NMR spectroscopy. GFT-NMR experiments were used for backbone assignments. Automated NOESY assignments were made using AUTOSTRUCTURE and CYANA-2.1. Dihedral angle constraints were obtained from TALOS. The assignments were validated using AVS software. Final structure factors determined using PSVS: ordered residues: 29-33, 15-21, 89-94, 57-62, 39-50, 79-82. Ramachandran statistics for ordered residues: Most favored region: 84.4%, additionally favored region: 15.6%, generously aloowed: 0.1%. Procheck scores for ordered residues (RAW/Z): Phi/psi -0.51/-1.69, all -0.33/-1.95, MolProbity clash scores (RAW/Z) - 15.41/-1.12. RPF scores for the goodness fit to NOESY data: Recall-0.993, Precision-0.878, F-measure-0.932, final dp score-0.756.
NMR constraints
NOE constraints total: 584 / NOE intraresidue total count: 116 / NOE long range total count: 149 / NOE medium range total count: 93 / NOE sequential total count: 226 / Protein phi angle constraints total count: 100 / Protein psi angle constraints total count: 100
NMR representative
Selection criteria: lowest energy
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 140 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0.01 Å / Maximum upper distance constraint violation: 0.2 Å
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