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Found 1 Document (0.609 seconds)

BMRB: 18435

2LSL

Solution structure of the C-terminal domain of Tetrahymena telomerase protein p65

Authors

Singh, M., Wang, Z., Koo, B., Patel, A., Cascio, D., Collins, K., Feigon, J.

Assembly

C-terminal domain of Tetrahymena telomerase protein p65

Entity

1. C-terminal domain of Tetrahymena telomerase protein p65 (polymer, Thiol state: all free), 137 monomers, 16168.09 Da Detail

MHHHHHHSVS IDVEIKQNCL IKIINIPQGT LKAEVVLAVR HLGYEFYCDY IDENSNQINS NLIQQDQHPQ LNDLLKEGQA MIRFQNSDEQ RLAIQKLLNH NNNKLQIEIR GQICDVISTI PEDEEKNYWN YIKFKKN

Formula weight

16168.09 Da

Source organism

Tetrahymena thermophila

Exptl. method

solution NMR

Refine. method

simulated annealing, torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 92.7 %, Completeness: 80.4 %, Completeness (bb): 91.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	80.4 % (1358 of 1689)	77.5 % (689 of 889)	85.1 % (542 of 637)	77.9 % (127 of 163)
Backbone	91.7 % (748 of 816)	90.9 % (250 of 275)	92.4 % (376 of 407)	91.0 % (122 of 134)
Sidechain	72.9 % (733 of 1006)	71.5 % (439 of 614)	79.6 % (289 of 363)	17.2 % (5 of 29)
Aromatic	29.7 % (35 of 118)	35.6 % (21 of 59)	22.4 % (13 of 58)	100.0 % (1 of 1)
Methyl	88.2 % (134 of 152)	86.8 % (66 of 76)	89.5 % (68 of 76)

1. entity

MHHHHHHSVS IDVEIKQNCL IKIINIPQGT LKAEVVLAVR HLGYEFYCDY IDENSNQINS NLIQQDQHPQ LNDLLKEGQA MIRFQNSDEQ RLAIQKLLNH NNNKLQIEIR GQICDVISTI PEDEEKNYWN YIKFKKN

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	p65	natural abundance	1 mM
2	H2O	natural abundance	90 %
3	D2O	[U-100% 2H]	10 %
4	sodium phosphate	natural abundance	20 mM
5	sodium chloride	natural abundance	50 mM
6	DTT	natural abundance	1 mM
7	sodium azide	natural abundance	0.01 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
8	p65	natural abundance	1 mM
9	D2O	[U-100% 2H]	100 %
10	sodium phosphate	natural abundance	20 mM
11	sodium chloride	natural abundance	50 mM
12	DTT	natural abundance	1 mM
13	sodium azide	natural abundance	0.01 %

Protein Blocks Logo

Calculated from 20 models in PDB: 2LSL, Strand ID: A Detail

Release date

2012-06-17

Citation

Structural basis for telomerase RNA recognition and RNP assembly by the holoenzyme La family protein p65
Singh, M., Wang, Z., Koo, B., Patel, A., Cascio, D., Collins, K., Feigon, J.
Mol. Cell (2012), 47, 16-26, PubMed 22705372 , DOI 10.1016/j.molcel.2012.05.018 , Abstract

Related entities 1. C-terminal domain of Tetrahymena telomerase protein p65, : 1 : 2 entities Detail

Experiments performed 11 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	p65	natural abundance	1 mM
2	H2O	natural abundance	90 %
3	D2O	[U-100% 2H]	10 %
4	sodium phosphate	natural abundance	20 mM
5	sodium chloride	natural abundance	50 mM
6	DTT	natural abundance	1 mM
7	sodium azide	natural abundance	0.01 %

2 3D CBCA(CO)NH

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	p65	natural abundance	1 mM
2	H2O	natural abundance	90 %
3	D2O	[U-100% 2H]	10 %
4	sodium phosphate	natural abundance	20 mM
5	sodium chloride	natural abundance	50 mM
6	DTT	natural abundance	1 mM
7	sodium azide	natural abundance	0.01 %

3 3D HNCACB

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	p65	natural abundance	1 mM
2	H2O	natural abundance	90 %
3	D2O	[U-100% 2H]	10 %
4	sodium phosphate	natural abundance	20 mM
5	sodium chloride	natural abundance	50 mM
6	DTT	natural abundance	1 mM
7	sodium azide	natural abundance	0.01 %

4 3D HNCO

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	p65	natural abundance	1 mM
2	H2O	natural abundance	90 %
3	D2O	[U-100% 2H]	10 %
4	sodium phosphate	natural abundance	20 mM
5	sodium chloride	natural abundance	50 mM
6	DTT	natural abundance	1 mM
7	sodium azide	natural abundance	0.01 %

5 3D HNCACO

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	p65	natural abundance	1 mM
2	H2O	natural abundance	90 %
3	D2O	[U-100% 2H]	10 %
4	sodium phosphate	natural abundance	20 mM
5	sodium chloride	natural abundance	50 mM
6	DTT	natural abundance	1 mM
7	sodium azide	natural abundance	0.01 %

6 3D HBHA(CO)NH

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	p65	natural abundance	1 mM
2	H2O	natural abundance	90 %
3	D2O	[U-100% 2H]	10 %
4	sodium phosphate	natural abundance	20 mM
5	sodium chloride	natural abundance	50 mM
6	DTT	natural abundance	1 mM
7	sodium azide	natural abundance	0.01 %

7 3D H(CCO)NH

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	p65	natural abundance	1 mM
2	H2O	natural abundance	90 %
3	D2O	[U-100% 2H]	10 %
4	sodium phosphate	natural abundance	20 mM
5	sodium chloride	natural abundance	50 mM
6	DTT	natural abundance	1 mM
7	sodium azide	natural abundance	0.01 %

8 3D HCCH-TOCSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
8	p65	natural abundance	1 mM
9	D2O	[U-100% 2H]	100 %
10	sodium phosphate	natural abundance	20 mM
11	sodium chloride	natural abundance	50 mM
12	DTT	natural abundance	1 mM
13	sodium azide	natural abundance	0.01 %

9 3D HCCH-COSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
8	p65	natural abundance	1 mM
9	D2O	[U-100% 2H]	100 %
10	sodium phosphate	natural abundance	20 mM
11	sodium chloride	natural abundance	50 mM
12	DTT	natural abundance	1 mM
13	sodium azide	natural abundance	0.01 %

10 3D 1H-13C NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
8	p65	natural abundance	1 mM
9	D2O	[U-100% 2H]	100 %
10	sodium phosphate	natural abundance	20 mM
11	sodium chloride	natural abundance	50 mM
12	DTT	natural abundance	1 mM
13	sodium azide	natural abundance	0.01 %

11 3D 1H-15N NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	p65	natural abundance	1 mM
2	H2O	natural abundance	90 %
3	D2O	[U-100% 2H]	10 %
4	sodium phosphate	natural abundance	20 mM
5	sodium chloride	natural abundance	50 mM
6	DTT	natural abundance	1 mM
7	sodium azide	natural abundance	0.01 %

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_18435_2lsl.nef
Input source #2: Coordindates	2lsl.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

-------370-------380-------390-------400-------410-------420-----450-------460-------470-------480--
MHHHHHHSVSIDVEIKQNCLIKIINIPQGTLKAEVVLAVRHLGYEFYCDYIDENSNQINSNLIQQDQHPQLNDLLKEGQAMIRFQNSDEQRLAIQKLLNH
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MHHHHHHSVSIDVEIKQNCLIKIINIPQGTLKAEVVLAVRHLGYEFYCDYIDENSNQINSNLIQQDQHPQLNDLLKEGQAMIRFQNSDEQRLAIQKLLNH
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

-----490-------500-------510---------
NNNKLQIEIRGQICDVISTIPEDEEKNYWNYIKFKKN
|||||||||||||||||||||||||||||||||||||
NNNKLQIEIRGQICDVISTIPEDEEKNYWNYIKFKKN
-------110-------120-------130-------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	137	0	0	100.0

Content subtype: combined_18435_2lsl.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1319		92.7 (chain: A, length: 137)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	2911 (1)	noe	94.9 (chain: A, length: 137)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	62 (1)	hbond	38.0 (chain: A, length: 137)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	222 (222)	.	92.7 (chain: A, length: 137)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_5	OK	115 (115)	.	83.9 (chain: A, length: 137)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 137, Sequence coverage: 92.7%
- Total number of assignments
  - ¹H chemical shifts: 666
  - ¹³C chemical shifts: 532
  - ¹⁵N chemical shifts: 121
- 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	889	666	74.9
¹³C chemical shifts	637	532	83.5
¹⁵N chemical shifts	167	121	72.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	275	247	89.8
¹³C chemical shifts	274	253	92.3
¹⁵N chemical shifts	134	120	89.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	614	419	68.2
¹³C chemical shifts	363	279	76.9
¹⁵N chemical shifts	33	1	3.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	78	65	83.3
¹³C chemical shifts	78	62	79.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	59	15	25.4
¹³C chemical shifts	58	11	19.0
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 137, Sequence coverage: 94.9%
- Total number of restraints: 2909
- Weight of restraints: 1.0 (2909)
- Potential type of restraints: square-well-parabolic (2909)
- Range of distance target values: 2.65, 4.15 (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
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 137, Sequence coverage: 38.0%
  - Total number of restraints: 62
  - Weight of restraints: 1.0 (62)
  - Potential type of restraints: square-well-parabolic (62)
  - Range of distance target values: 2.05, 3.0 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 137, Sequence coverage: 92.7%
- Total number of restraints: 222
- Total number of restraints per polymer type: 222
- Weight of restraints: 1.0 (222)
- Potential type of restraints: square-well-parabolic (222)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_5
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 137, Sequence coverage: 83.9%
- Total number of restraints: 115
- Potential type of restraints: square-well-parabolic (115)
- Range of observed RDC values: -22.17, 27.74 (Hz)
- Histogram of observed RDC values
- RDC restraints per residue
  - Chain_ID: A
    None

Keywords La protein, LARP7, p65, RRM, Solution structure, Telomerase, Tetrahymena

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Found 1 Document (0.609 seconds)

BMRB: 18435

Sample #1

Sample #2

Related entities 1. C-terminal domain of Tetrahymena telomerase protein p65, : 1 : 2 entities Detail

Experiments performed 11 experiments Detail

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NMR combined restraints 6 contents Detail