BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	86.3 % (924 of 1071)	85.0 % (470 of 553)	88.5 % (362 of 409)	84.4 % (92 of 109)
Backbone	97.7 % (549 of 562)	97.4 % (191 of 196)	97.4 % (266 of 273)	98.9 % (92 of 93)
Sidechain	77.3 % (459 of 594)	78.2 % (279 of 357)	81.4 % (180 of 221)	0.0 % (0 of 16)
Aromatic	0.0 % (0 of 78)	0.0 % (0 of 39)	0.0 % (0 of 39)
Methyl	98.0 % (96 of 98)	98.0 % (48 of 49)	98.0 % (48 of 49)

1. entity 1

GAKGDLVSFR IDESGRAACV NAVRQKKRAT VDSIKGQFGF LNFEVEDGKK LFFHMSEVQG NTVALHPGDT VEFSVVTNQR NGKSSACNVL KIND

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Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.8, Details 0.24 mM [U-99% 13C; U-99% 15N] protein, 50 mM sodium phosphate, 50 mM sodium chloride, 1 mM DTT, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	protein	[U-99% 13C; U-99% 15N]	0.24 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	1 mM

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.8, Details 0.24 mM [U-99% 13C; U-99% 15N] protein, 50 mM sodium phosphate, 50 mM sodium chloride, 1 mM DTT, 100% D2O

#	Name	Isotope labeling	Concentration
5	protein	[U-99% 13C; U-99% 15N]	0.24 mM
6	sodium phosphate	natural abundance	50 mM
7	sodium chloride	natural abundance	50 mM
8	DTT	natural abundance	1 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 6Y96, Strand ID: A Detail

Release date

2020-07-12

Citation

Pseudo-RNA-Binding Domains Mediate RNA Structure Specificity in Upstream of N-Ras
Hollmann, N.M., Jagtap, P.K.A., Masiewicz, P., Guitart, T., Simon, B., Provaznik, J., Stein, F., Haberkant, P., Sweetapple, L.J., Villacorte, L., Mooijman, D., Benes, V., Savitski, M., Gebauer, F., Hennig, J.
Cell Rep. (2020), 32, 107930-107930, PubMed 32697992 , DOI 10.1016/j.celrep.2020.107930 , Abstract

Related entities 1. Upstream of N-ras, isoform A, : 1 : 1 : 25 entities Detail

Experiments performed 11 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.8, Details 0.24 mM [U-99% 13C; U-99% 15N] protein, 50 mM sodium phosphate, 50 mM sodium chloride, 1 mM DTT, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	protein	[U-99% 13C; U-99% 15N]	0.24 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	1 mM

2 3D HNCA

Instrument

Bruker AVANCE III - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	protein	[U-99% 13C; U-99% 15N]	0.24 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	1 mM

3 3D HNCACB

Instrument

Bruker AVANCE III - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	protein	[U-99% 13C; U-99% 15N]	0.24 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	1 mM

4 3D CBCA(CO)NH

Instrument

Bruker AVANCE III - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	protein	[U-99% 13C; U-99% 15N]	0.24 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	1 mM

5 3D HNCO

Instrument

Bruker AVANCE III - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	protein	[U-99% 13C; U-99% 15N]	0.24 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	1 mM

6 3D HCCH-TOCSY

Instrument

Bruker AVANCE III - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.8, Details 0.24 mM [U-99% 13C; U-99% 15N] protein, 50 mM sodium phosphate, 50 mM sodium chloride, 1 mM DTT, 100% D2O

#	Name	Isotope labeling	Concentration
5	protein	[U-99% 13C; U-99% 15N]	0.24 mM
6	sodium phosphate	natural abundance	50 mM
7	sodium chloride	natural abundance	50 mM
8	DTT	natural abundance	1 mM

7 3D HBHA(CO)NH

Instrument

Bruker AVANCE III - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	protein	[U-99% 13C; U-99% 15N]	0.24 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	1 mM

8 2D 1H-13C HSQC aliphatic

Instrument

Bruker AVANCE III - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
5	protein	[U-99% 13C; U-99% 15N]	0.24 mM
6	sodium phosphate	natural abundance	50 mM
7	sodium chloride	natural abundance	50 mM
8	DTT	natural abundance	1 mM

9 2D 1H-1H NOESY

Instrument

Bruker AVANCE III - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
5	protein	[U-99% 13C; U-99% 15N]	0.24 mM
6	sodium phosphate	natural abundance	50 mM
7	sodium chloride	natural abundance	50 mM
8	DTT	natural abundance	1 mM

10 3D 1H-15N NOESY

Instrument

Bruker AVANCE III - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	protein	[U-99% 13C; U-99% 15N]	0.24 mM
2	sodium phosphate	natural abundance	50 mM
3	sodium chloride	natural abundance	50 mM
4	DTT	natural abundance	1 mM

11 3D 1H-13C NOESY

Instrument

Bruker AVANCE III - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
5	protein	[U-99% 13C; U-99% 15N]	0.24 mM
6	sodium phosphate	natural abundance	50 mM
7	sodium chloride	natural abundance	50 mM
8	DTT	natural abundance	1 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34498_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr34498_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1013		97.9 (chain: 1, length: 94)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 94, Sequence coverage: 97.9%
- Total number of assignments
  - ¹H chemical shifts: 562
  - ¹³C chemical shifts: 360
  - ¹⁵N chemical shifts: 91
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	553	466	84.3
¹³C chemical shifts	409	360	88.0
¹⁵N chemical shifts	109	91	83.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	196	188	95.9
¹³C chemical shifts	188	180	95.7
¹⁵N chemical shifts	93	91	97.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	357	278	77.9
¹³C chemical shifts	221	180	81.4
¹⁵N chemical shifts	16	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	48	96.0
¹³C chemical shifts	50	48	96.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	0	0.0
¹³C chemical shifts	39	0	0.0

Keywords CSD, RBP, RNA BINDING PROTEIN

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Found 1 Document (0.574 seconds)

BMRB: 34498

Sample #1

Sample #2

Related entities 1. Upstream of N-ras, isoform A, : 1 : 1 : 25 entities Detail

Experiments performed 11 experiments Detail

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Chemical shift validation 3 contents Detail