BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	69.1 % (815 of 1179)	82.1 % (505 of 615)	47.0 % (219 of 466)	92.9 % (91 of 98)
Backbone	83.9 % (485 of 578)	96.9 % (186 of 192)	70.5 % (208 of 295)	100.0 % (91 of 91)
Sidechain	60.9 % (425 of 698)	75.4 % (319 of 423)	39.6 % (106 of 268)	0.0 % (0 of 7)
Aromatic	1.8 % (2 of 112)	3.6 % (2 of 56)	0.0 % (0 of 55)	0.0 % (0 of 1)
Methyl	62.2 % (61 of 98)	100.0 % (49 of 49)	24.5 % (12 of 49)

1. RNA binding protein La-like protein

TDHQTVYVKP VPPTATLEQL TEFFSKHGTV QAVWRRYFAG KKDAPPESRT KPSVFVVFNS SEEAEAFQKA PPMYDDVQLT AEMKTTYLER KAEEIAAKK

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.8, Details 0.5 mM [U-13C; U-15N] RRM, 200 mM sodium chloride, 20 mM sodium phosphate, 2 mM DTT, 2 mM EDTA, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	RRM	[U-13C; U-15N]	protein	0.5 mM
2	DTT	natural abundance		2 mM
3	EDTA	natural abundance		2 mM
4	sodium chloride	natural abundance	salt	200 mM
5	sodium phosphate	natural abundance	buffer	20 mM
6	H2O	natural abundance	solvent	90 %
7	D2O	[U-2H]	solvent	10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 2.98 ppm, Outliers: 3 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 2.98 ppm, Outliers: 3 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 0.01 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5ZUH, Strand ID: A Detail

Release date

2018-06-12

Citation

A telomerase subunit homolog La protein from Trypanosoma brucei plays an essential role in ribosomal biogenesis
Shan, F., Mei, S., Zhang, J., Zhang, X., Xu, C., Liao, S., Tu, X.
FEBS J. (2019), 286, 3129-3147, PubMed 30993866 , DOI 10.1111/febs.14853 , Abstract

Related entities 1. RNA binding protein La-like protein, : 1 : 28 entities Detail

Experiments performed 2 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_36185_5zuh.nef
Input source #2: Coordindates	5zuh.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

-------20--------30--------40--------50--------60--------70--------80--------90-------100-------110
TDHQTVYVKPVPPTATLEQLTEFFSKHGTVQAVWRRYFAGKKDAPPESRTKPSVFVVFNSSEEAEAFQKAPPMYDDVQLTAEMKTTYLERKAEEIAAKK
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
TDHQTVYVKPVPPTATLEQLTEFFSKHGTVQAVWRRYFAGKKDAPPESRTKPSVFVVFNSSEEAEAFQKAPPMYDDVQLTAEMKTTYLERKAEEIAAKK
--------10--------20--------30--------40--------50--------60--------70--------80--------90---------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	99	0	0	100.0

Content subtype: combined_36185_5zuh.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	805		97.0 (chain: A, length: 99)
1	Distance restraints	DYANA/DIANA_distance_constraints_4	Warning	1032 (1)	noe	100.0 (chain: A, length: 99)
2	Distance restraints	DYANA/DIANA_distance_constraints_3	Warning	108 (1)	hbond	42.4 (chain: A, length: 99)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	185 (185)	.	99.0 (chain: A, length: 99)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 99, Sequence coverage: 97.0%
- Total number of assignments
  - ¹H chemical shifts: 519
  - ¹³C chemical shifts: 195
  - ¹⁵N chemical shifts: 91
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- 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	615	508	82.6
¹³C chemical shifts	466	195	41.8
¹⁵N chemical shifts	102	91	89.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	192	187	97.4
¹³C chemical shifts	198	96	48.5
¹⁵N chemical shifts	91	91	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	423	321	75.9
¹³C chemical shifts	268	99	36.9
¹⁵N chemical shifts	11	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	51	51	100.0
¹³C chemical shifts	51	11	21.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	56	2	3.6
¹³C chemical shifts	55	0	0.0
¹⁵N chemical shifts	1	0	0.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_4
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 99, Sequence coverage: 100.0%
- Total number of restraints: 1032
- Weight of restraints: 1.0 (1032)
- Potential type of restraints: upper-bound-parabolic (1032)
- Range of distance target values: 2.8, 6.5 (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: DYANA/DIANA_distance_constraints_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 99, Sequence coverage: 42.4%
  - Total number of restraints: 108
  - Weight of restraints: 1.0 (108)
  - Potential type of restraints: upper-bound-parabolic (108)
  - Range of distance target values: 1.95, 3.15 (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

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 99, Sequence coverage: 99.0%
- Total number of restraints: 185
- Total number of restraints per polymer type: 185
- Weight of restraints: 1.0 (185)
- Potential type of restraints: square-well-parabolic (185)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords La motif, RNA BINDING PROTEIN, RNA-binding, RRM domian, Trypanosoma brucei

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Found 1 Document (0.613 seconds)

BMRB: 36185

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. RNA binding protein La-like protein, : 1 : 28 entities Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail