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Found 1 Document (0.754 seconds)

BMRB: 16244

2KH9

Backbone NH Assignments for Prp24-RRM23 Bound to AGAGAU RNA

Authors

Martin-Tumasz, S.A., Butcher, S.E.

Assembly

U6 snRNP (fragment)

Entity

1. Prp24-RRM23 (polymer, Thiol state: not reported), 186 monomers, 21426.14 Da Detail

MTECTLWMTN FPPSYTQRNI RDLLQDINVV ALSIRLPSLR FNTSRRFAYI DVTSKEDARY CVEKLNGLKI EGYTLVTKVS NPLEKSKRTD SATLEGREIM IRNLSTELLD ENLLRESFEG FGSIEKINIP AGQKEHSFNN CCAFMVFENK DSAERALQMN RSLLGNREIS VSLADKKPLE HHHHHH

2. AGAGAU (polymer, Thiol state: not present), 6 monomers, 2002.210 Da Detail

AGAGAU

Total weight

23428.352 Da

Max. entity weight

21426.14 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

solution NMR

Refine. method

simulated annealing, torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 69.8 %, Completeness: 19.7 %, Completeness (bb): 45.5 % Detail

Polymer type: polypeptide(L) polyribonucleotide

	Total	¹H	¹⁵N
All	19.7 % (277 of 1406)	12.0 % (144 of 1204)	65.8 % (133 of 202)
Backbone	45.5 % (268 of 589)	33.0 % (135 of 409)	73.9 % (133 of 180)
Sidechain	1.1 % (9 of 817)	1.1 % (9 of 795)	0.0 % (0 of 22)
Aromatic	0.0 % (0 of 93)	0.0 % (0 of 89)	0.0 % (0 of 4)
Methyl	4.0 % (4 of 100)	4.0 % (4 of 100)

1. Prp24-RRM23

2. AGAGAU

AGAGAU

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298.15 K, pH 7

#	Name	Isotope labeling	Concentration
1	Prp24-RRM23	[U-99% 13C; U-99% 15N]	500 uM
2	TRIS	natural abundance	10 mM
3	potassium chloride	natural abundance	50 mM
4	DTT	natural abundance	1 mM
5	AGAGAU	natural abundance	5 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298.15 K, pH 7

#	Name	Isotope labeling	Concentration
8	Prp24-RRM23	[U-99% 13C; U-99% 15N]	500 uM
9	TRIS	natural abundance	10 mM
10	potassium chloride	natural abundance	50 mM
11	DTT	natural abundance	1 mM
12	DSS	natural abundance	10 uM
13	AGAGAU	natural abundance	5 mM
14	H2O	natural abundance	90 %
15	D2O	natural abundance	10 %

Protein Blocks Logo

Calculated from 10 models in PDB: 2KH9, Strand ID: A Detail

Release date

2009-09-03

Citation

(1)H, (13)C and (15)N resonance assignments of a ribonucleoprotein complex consisting of Prp24-RRM2 bound to a fragment of U6 RNA
Martin-Tumasz, S., Butcher, S.E.
Biomol. NMR Assign. (2009), 3, 227-230, PubMed 19693704 , DOI 10.1007/s12104-009-9181-5 , Abstract

Entries sharing articles BMRB: 3 entries Detail

  BMRB: 16230 released on 2009-09-03
    Title Solution Structure of Yeast Prp24-RRM2 Bound to a Fragment of U6 RNA
  BMRB: 16243 released on 2009-09-03
    Title Backbone NH Assignments for Prp24-RRM23
  BMRB: 16246 released on 2009-09-03
    Title Resonance Assignments for Yeast Prp24-RRM2

Related entities 1. Prp24-RRM23, : 168 entities Detail

Experiments performed 4 experiments Detail

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_16244_2kh9.nef
Input source #2: Coordindates	2kh9.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	Error

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

----120-------130-------140-------150-------160-------170-------180-------190-------200-----
MTECTLWMTNFPPSYTQRNIRDLLQDINVVALSIRLPSLRFNTSRRFAYIDVTSKEDARYCVEKLNGLKIEGYTLVTKVSNPLELEHHHHHH
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MTECTLWMTNFPPSYTQRNIRDLLQDINVVALSIRLPSLRFNTSRRFAYIDVTSKEDARYCVEKLNGLKIEGYTLVTKVSNPLELEHHHHHH
--------10--------20--------30--------40--------50--------60--------70--------80--------90--

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

-50---
AGAGAU
||||||
AGAGAU
------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	92	0	0	100.0
B	B	6	0	0	100.0

Content subtype: combined_16244_2kh9.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Error	256		No information
1	Distance restraints	CNS/XPLOR_distance_constraints_4	Error	2577 (1)	noe	90.2 (chain: A, length: 92), 100.0 (chain: B, length: 6)
2	Distance restraints	CNS/XPLOR_distance_constraints_2	Error	49 (1)	hbond	43.5 (chain: A, length: 92), 50.0 (chain: B, length: 6)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_5	OK	137 (137)	.	77.2 (chain: A, length: 92), 100.0 (chain: B, length: 6)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_6	OK	130 (130)	.	85.9 (chain: A, length: 92)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Error

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_4
- Status: Error
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 92, Sequence coverage: 90.2%
  - Entity_assembly_ID: B, Chain length: 6, Sequence coverage: 100.0%
- Total number of restraints: 2517
- Weight of restraints: 1.0 (2517)
- Potential type of restraints: square-well-parabolic (2517)
- Range of distance target values: 2.55, 9.0 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_2
  - Status: Error
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 92, Sequence coverage: 43.5%
    - Entity_assembly_ID: B, Chain length: 6, Sequence coverage: 50.0%
  - Total number of restraints: 49
  - Weight of restraints: 1.0 (49)
  - Potential type of restraints: square-well-parabolic (49)
  - Range of distance target values: 2.0, 3.0 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_5
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 92, Sequence coverage: 77.2%
  - Entity_assembly_ID: B, Chain length: 6, Sequence coverage: 100.0%
- Total number of restraints: 137
- Total number of restraints per polymer type: 137
- Weight of restraints: 1.0 (137)
- Potential type of restraints: square-well-parabolic (137)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_6

Status: OK
Experiment type: .

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 92, Sequence coverage: 85.9%

----120-------130-------140-------150-------160-------170-------180-------190-------200-----
MTECTLWMTNFPPSYTQRNIRDLLQDINVVALSIRLPSLRFNTSRRFAYIDVTSKEDARYCVEKLNGLKIEGYTLVTKVSNPLELEHHHHHH
  ||||||||| |||||||||||||| |||||||||||||| | |||||||||||||||||||||||||||||||||||| |||||      
..ECTLWMTNF.PSYTQRNIRDLLQD.NVVALSIRLPSLRF.T.RRFAYIDVTSKEDARYCVEKLNGLKIEGYTLVTKVS.PLELE      
----120-------130-------140-------150-------160-------170-------180-------190---------

Total number of restraints: 130
Potential type of restraints: undefined (130)
Range of observed RDC values: 100.0, -100.0 (Hz)
RDC restraints per residue
- Chain_ID: A
  None

Keywords Protein/RNA, RRM, snRNP, Splicing

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Found 1 Document (0.754 seconds)

BMRB: 16244

Sample #1

Sample #2

Entries sharing articles BMRB: 3 entries Detail

Related entities 1. Prp24-RRM23, : 168 entities Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 6 contents Detail