Mass: 9920.542 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermosynechococcus vestitus BP-1 (bacteria) Strain: NIES-2133 / IAM M-273 / BP-1 / Gene: tll0553 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q8DLE2
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Sample state
Spectrometer-ID
Type
1
1
1
isotropic
1
2D 1H-13C HSQC aliphatic
1
2
1
isotropic
4
2D 1H-13C HSQC aromatic
1
3
1
isotropic
1
3DCBCA(CO)NH
1
4
1
isotropic
1
3D HNCA
1
5
1
isotropic
1
3D HN(CA)CB
1
6
1
isotropic
1
2D 1H-15N HSQC
1
10
1
isotropic
4
3D 1H-13C NOESY aliphatic
1
9
1
isotropic
4
3D 1H-13C NOESY aromatic
1
8
1
isotropic
3
3DC(CO)NH
1
7
1
isotropic
4
3DHBHA(CO)NH
1
11
1
isotropic
3
3DH(CCO)NH
1
12
1
isotropic
4
3D (H)CCH-TOCSY
1
13
1
isotropic
4
3D 1H-15N NOESY
1
14
1
isotropic
4
2D (HB)CB(CGCDCE)HDHAROMATIC
1
15
1
isotropic
4
2D (HB)CB(CGCD)HDAROMATIC
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Sample preparation
Details
Type: solution Contents: 100 mM MOPS, 50 mM sodium chloride, 2 mM TCEP, 90% H2O/10% D2O Label: 15N, 13C / Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)
Component
Isotopic labeling
Solution-ID
100mM
MOPS
naturalabundance
1
50mM
sodiumchloride
naturalabundance
1
2mM
TCEP
naturalabundance
1
Sample conditions
Ionic strength: 50 mM / Label: Conditions_1 / pH: 6.5 / Pressure: 1 atm / Temperature: 308 K
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NMR measurement
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Bruker AVANCE III HD
Bruker
AVANCEIIIHD
750
1
Bruker AVANCE NEO
Bruker
AVANCENEO
800
2
Bruker AVANCE III HD
Bruker
AVANCEIIIHD
600
3
Varian Uniform NMR System
Varian
UniformNMRSystem
800
4
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Processing
NMR software
Name
Developer
Classification
Poky
Manthey, I. et al. POKY software tools encapsulating assignment strategies for solution and solid-state protein NMR data. J Struct Biol X 6, 100073 (2022). https://doi.org:10.1016/j.yjsbx.2022.100073
chemicalshiftassignment
PINE Server
Lee, W. et al. I-PINE web server: an integrative probabilistic NMR assignment system for proteins. J Biomol NMR 73, 213-222 (2019). https://doi.org:10.1007/s10858-019-00255-3
chemicalshiftassignment
TopSpin
BrukerBiospin
collection
NMRPipe
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
processing
PONDEROSA-C/S
Lee, W., Stark, J. L. & Markley, J. L. PONDEROSA-C/S: client-server based software package for automated protein 3D structure determination. J Biomol NMR 60, 73-75 (2014). https://doi.org:10.1007/s10858-014-9855-x
structurecalculation
X-PLOR NIH
Schwieters, Kuszewski, TjandraandClore
structurecalculation
X-PLOR NIH
Schwieters, Kuszewski, TjandraandClore
refinement
AUDANA
Lee, W., Petit, C. M., Cornilescu, G., Stark, J. L. & Markley, J. L. The AUDANA algorithm for automated protein 3D structure determination from NMR NOE data. J Biomol NMR 65, 51-57 (2016). https://doi.org:10.1007/s10858-016-0036-y
structurecalculation
TALOS-N
Shen, Y. & Bax, A. Protein structural information derived from NMR chemical shift with the neural network program TALOS-N. Methods Mol Biol 1260, 17-32 (2015). https://doi.org:10.1007/978-1-4939-2239-0_2
structurecalculation
Refinement
Method: simulated annealing / Software ordinal: 9
NMR representative
Selection criteria: lowest energy
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20
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