Mass: 11596.175 Da / Num. of mol.: 1 / Fragment: sequence database residues 70-155 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: UPF3A, RENT3A, UPF3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)+ magic / References: UniProt: Q9H1J1
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR Details: HR4714B is a 97 residue protein consisiting of a 10 residue N-terminal tag. N-HSQC spectrum shows only 71 peaks out of the 87 peaks (excluding tag) that are expected. The line broeadening of ...Details: HR4714B is a 97 residue protein consisiting of a 10 residue N-terminal tag. N-HSQC spectrum shows only 71 peaks out of the 87 peaks (excluding tag) that are expected. The line broeadening of the peaks occur from residue D45 to S54. Also, M11, R16, S81 NH's are missing from N-HSQC spectrum. The reason for line broadening is not known.
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
2D 1H-15N HSQC
1
2
1
2D 1H-15N HSQC
1
3
1
2D 1H-13C HSQC
1
4
1
2D 1H-13C HSQC
1
5
2
2D 1H-13C HSQC
1
6
1
3DCBCA(CO)NH
1
7
1
3D HNCO
1
8
1
3D HNCA
1
9
1
3D HN(CA)CB
1
10
1
3DHBHA(CO)NH
1
11
1
3D C(CO)NH-TOCSY
1
12
1
3D CCH-TOCSY
1
13
2
3D HNHA
1
14
1
3D simul NOESY
1
15
1
3D arom NOESY
NMR details
Text: The Structure was obtained using triple resonance NMR spectroscopy for backbone and side chain assignments. Automated NOESY assignments were made using Autostructure and CYANA3.0. Dihedral ...Text: The Structure was obtained using triple resonance NMR spectroscopy for backbone and side chain assignments. Automated NOESY assignments were made using Autostructure and CYANA3.0. Dihedral angle constraints were obtained using TALOS. The structure calculation was done excluding the 10-residue N-terminal tag. Completeness of assignment excluding the tag: Backbone - 80%, Sidechain - 80%. Peaks for 13 residues in NHSQC spectra are missing due to line broadening.
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
0.82 mM [U-100% 13C; U-100% 15N] HR4714B, 90% H2O/10% D2O
90% H2O/10% D2O
2
0.9 mM [U-10% 13C; U-99% 15N] HR4714B, 90% H2O/10% D2O
Method: simulated annealing / Software ordinal: 1 Details: Final structure quality (excluding 10 residue tag) determined using PSVS-v1.4: Ordered residues are defines as: 10-19,22-34,36-45,54-72,76-94. (a) RMSD (ordered residues) all backbone aroms: ...Details: Final structure quality (excluding 10 residue tag) determined using PSVS-v1.4: Ordered residues are defines as: 10-19,22-34,36-45,54-72,76-94. (a) RMSD (ordered residues) all backbone aroms: 0.6A. and heavy atoms 1.0A. (b) Ramachandran statistics for ordered residues: Most favored region: 85.1% Additionally favored region: 14.8% Generaously allowed region: 0.1% Disallowed region: 0.1%. (c) Procheck scores for ordered residues (RAW/Z): Phi/psi -0.73/-2.56, all -0.65/-3.84, (d) Molprobity clashscores (RAW/Z)22.41/-2.32 (e) RPF scores for the goodness fit to NOESY data: Recall: 89, Precision: 94, F-measure: 92, final dp-score - (f) RMS deviation for bond angles - 6.15, RMS deviation for bond lengths 0.01A.
NMR constraints
NOE constraints total: 1729 / NOE intraresidue total count: 281 / NOE long range total count: 333 / NOE medium range total count: 536 / NOE sequential total count: 471 / Protein phi angle constraints total count: 108 / Protein psi angle constraints total count: 108
NMR representative
Selection criteria: lowest energy
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0.25 Å / Maximum torsion angle constraint violation: 8.5 ° / Maximum upper distance constraint violation: 1.7 Å
NMR ensemble rms
Distance rms dev: 0.01 Å
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