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Found 1 Document (1.584 seconds)

BMRB: 34247

6G03

NMR Solution Structure of yeast TSR2(1-152)

Authors

Michel, E., Schuetz, S., Damberger, F.F., Allain, F.H.-T., Panse, V.G.

Assembly

Pre-rRNA-processing protein TSR2

Entity

1. Pre-rRNA-processing protein TSR2 (polymer, Thiol state: all free), 156 monomers, 17919.90 Da Detail

SGSHMSTQYI DETAFVQAEQ GKTNLMFSDE KQQARFELGV SMVIYKWDAL DVAVENSWGG PDSAEKRDWI TGIVVDLFKN EKVVDAALIE ETLLYAMIDE FETNVEDDSA LPIAVEVINI YNDCFNLNYN KVEKLYLEWQ EKQRTKKSKR VVHIEG

Formula weight

17919.9 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 91.4 %, Completeness (bb): 85.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	91.4 % (1690 of 1849)	97.7 % (934 of 956)	81.1 % (583 of 719)	99.4 % (173 of 174)
Backbone	85.2 % (794 of 932)	98.4 % (312 of 317)	71.4 % (329 of 461)	99.4 % (153 of 154)
Sidechain	97.9 % (1044 of 1066)	97.3 % (622 of 639)	98.8 % (402 of 407)	100.0 % (20 of 20)
Aromatic	98.8 % (162 of 164)	98.8 % (81 of 82)	98.7 % (77 of 78)	100.0 % (4 of 4)
Methyl	96.7 % (174 of 180)	95.6 % (86 of 90)	97.8 % (88 of 90)

1. entity 1

SGSHMSTQYI DETAFVQAEQ GKTNLMFSDE KQQARFELGV SMVIYKWDAL DVAVENSWGG PDSAEKRDWI TGIVVDLFKN EKVVDAALIE ETLLYAMIDE FETNVEDDSA LPIAVEVINI YNDCFNLNYN KVEKLYLEWQ EKQRTKKSKR VVHIEG

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 0.8 mM [U-13C; U-15N] Tsr2(1-152), 20 mM sodium phosphate, 1 mM [U-2H] DTT, 10 uM EDTA, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	8.9960013E8 Hz	internal	indirect	0.2514495
¹H	water	protons	8.9960013E8 Hz	internal	direct	1.0
¹⁵N	water	protons	8.9960013E8 Hz	internal	indirect	0.1013291

Referencing offset: -0.15 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	8.9960013E8 Hz	internal	indirect	0.2514495
¹H	water	protons	8.9960013E8 Hz	internal	direct	1.0
¹⁵N	water	protons	8.9960013E8 Hz	internal	indirect	0.1013291

Referencing offset: -0.15 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	8.9960013E8 Hz	internal	indirect	0.2514495
¹H	water	protons	8.9960013E8 Hz	internal	direct	1.0
¹⁵N	water	protons	8.9960013E8 Hz	internal	indirect	0.1013291

Referencing offset: 0.16 ppm, Outliers: 3 Detail

Release date

2018-09-10

Citation

Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2
Schuetz, S., Michel, E., Damberger, F.F., Oplova, M., Pena, C., Leitner, A., Aebersold, R., Allain, F.H.-T., Panse, V.G.
Nat. Commun. (2018), 9, 3669-3669, PubMed 30201955 , DOI 10.1038/s41467-018-06160-x , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 34248 released on 2018-09-12
Title NMR Solution Structure of Yeast TSR2(1-152) in Complex with S26A(100-119)

Related entities 1. Pre-rRNA-processing protein TSR2, : 1 : 1 : 2 : 3 entities Detail

Interaction partners 1. Pre-rRNA-processing protein TSR2, : 17 interactors Detail

More details for 17 interactors identified by 5 citations

Experiments performed 11 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 293.15 K, pH 7.0, Details 0.8 mM [U-13C; U-15N] Tsr2(1-152), 20 mM sodium phosphate, 1 mM [U-2H] DTT, 10 uM EDTA, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

2 3D HNCA

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

3 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

4 3D HNCACB

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

5 3D 1H-15N TOCSY

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

6 3D C(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

7 3D H(CCO)NH

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

8 3D HCCH-TOCSY

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

9 3D 1H-15N NOESY

Instrument

Bruker Avance - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

10 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

11 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	Tsr2(1-152)	[U-13C; U-15N]	0.8 mM
2	sodium phosphate	natural abundance	20 mM
3	DTT	[U-2H]	1 mM
4	EDTA	natural abundance	10 uM

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_34247_6g03.nef
Input source #2: Coordindates	6g03.cif
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

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
SGSHMSTQYIDETAFVQAEQGKTNLMFSDEKQQARFELGVSMVIYKWDALDVAVENSWGGPDSAEKRDWITGIVVDLFKNEKVVDAALIEETLLYAMIDE
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SGSHMSTQYIDETAFVQAEQGKTNLMFSDEKQQARFELGVSMVIYKWDALDVAVENSWGGPDSAEKRDWITGIVVDLFKNEKVVDAALIEETLLYAMIDE

-------110-------120-------130-------140-------150------
FETNVEDDSALPIAVEVINIYNDCFNLNYNKVEKLYLEWQEKQRTKKSKRVVHIEG
||||||||||||||||||||||||||||||||||||||||||||||||||||||||
FETNVEDDSALPIAVEVINIYNDCFNLNYNKVEKLYLEWQEKQRTKKSKRVVHIEG

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	156	0	0	100.0

Content subtype: combined_34247_6g03.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1675		99.4 (chain: A, length: 156)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	5043 (1)	noe	99.4 (chain: A, length: 156)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 156, Sequence coverage: 99.4%
- Total number of assignments
  - ¹H chemical shifts: 942
  - ¹³C chemical shifts: 560
  - ¹⁵N chemical shifts: 173
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- 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: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	956	942	98.5
¹³C chemical shifts	719	560	77.9
¹⁵N chemical shifts	178	173	97.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	317	314	99.1
¹³C chemical shifts	312	155	49.7
¹⁵N chemical shifts	154	152	98.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	639	628	98.3
¹³C chemical shifts	407	405	99.5
¹⁵N chemical shifts	24	21	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	94	93	98.9
¹³C chemical shifts	94	94	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	82	81	98.8
¹³C chemical shifts	78	77	98.7
¹⁵N chemical shifts	4	4	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 156, Sequence coverage: 99.4%
- Total number of restraints: 4926
- Weight of restraints: 1.0 (4926)
- Potential type of restraints: upper-bound-parabolic (4926)
- Range of distance target values: 2.4, 7.0 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Keywords TRANSPORT PROTEIN, alpha-helical protein, escortin, eukaryotic specific segments, nuclear unloading factor, nucleus, ribosome maturation, transport of ribosomal protein S26

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Found 1 Document (1.584 seconds)

BMRB: 34247

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. Pre-rRNA-processing protein TSR2, : 1 : 1 : 2 : 3 entities Detail

Interaction partners 1. Pre-rRNA-processing protein TSR2, : 17 interactors Detail

Experiments performed 11 experiments Detail

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NMR combined restraints 3 contents Detail