BMRBj - BMREntryMaster

Found 1 Document (0.443 seconds)

BMRB: 18620

NMR Chemical Shift Assignments of N terminal RRM domain of La protein

Authors

Bouras, G., Argyriou, A.I., Apostolidi, M., Chasapis, C.T., Stathopoulos, C., Bentrop, D., Spyroulias, G.A.

Assembly

RRM domain

Entity

1. RRM domain (polymer, Thiol state: all free), 99 monomers, 11412.69 Da Detail

GKTLYSKGWP EDTTIEKVQE FFNANGGYKV VSVRLRKKSD KSFKGSFLAD FETEEIVNKI ITEAPKLGEK ELIYQTFKQF SDEKKDEKEK FFASTNGDK

Formula weight

11412.69 Da

Source organism

Dictyostelium discoideum

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 82.9 %, Completeness (bb): 97.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	82.9 % (1014 of 1223)	74.1 % (478 of 645)	91.8 % (434 of 473)	97.1 % (102 of 105)
Backbone	97.8 % (577 of 590)	97.5 % (198 of 203)	98.3 % (285 of 290)	96.9 % (94 of 97)
Sidechain	73.0 % (529 of 725)	63.3 % (280 of 442)	87.6 % (241 of 275)	100.0 % (8 of 8)
Aromatic	38.1 % (48 of 126)	27.0 % (17 of 63)	48.4 % (30 of 62)	100.0 % (1 of 1)
Methyl	100.0 % (82 of 82)	100.0 % (41 of 41)	100.0 % (41 of 41)

1. RRM

GKTLYSKGWP EDTTIEKVQE FFNANGGYKV VSVRLRKKSD KSFKGSFLAD FETEEIVNKI ITEAPKLGEK ELIYQTFKQF SDEKKDEKEK FFASTNGDK

Show sample condition

Sample #1

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

#	Name	Isotope labeling	Type	Concentration
1	RRM	[U-98% 15N]		0.35 mM
2	buffer salts	natural abundance		50 mM

Sample #2

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

#	Name	Isotope labeling	Type	Concentration
3	RRM	[U-98% 13C; U-98% 15N]		0.35 mM
4	buffer salts	natural abundance		50 mM

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: -0.05 ppm, Outliers: 2 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: -0.05 ppm, Outliers: 2 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: 2 Detail

LACS Plot; CO

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: 0.07 ppm, Outliers: 1 Detail

Release date

2012-07-26

Citation

¹H, ¹⁵N, ¹³C assignment and secondary structure determination of two domains of La protein from D. discoideum
Apostolidi, M., Vourtsis, D.J., Chasapis, C.T., Stathopoulos, C., Bentrop, D., Spyroulias, G.A.
Biomol. NMR Assign. (2014), 8, 47-51, PubMed 23239108 , DOI 10.1007/s12104-012-9450-6 , Abstract

Related entities 1. RRM domain, : 1 : 14 entities Detail

Experiments performed 8 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr18620_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: bmr18620_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1068		100.0 (chain: 1, length: 99)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 99, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 536
  - ¹³C chemical shifts: 430
  - ¹⁵N chemical shifts: 102
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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	442	256	57.9
¹³C chemical shifts	275	237	86.2
¹⁵N chemical shifts	10	8	80.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	645	454	70.4
¹³C chemical shifts	473	430	90.9
¹⁵N chemical shifts	107	102	95.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	203	198	97.5
¹³C chemical shifts	198	193	97.5
¹⁵N chemical shifts	97	94	96.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	63	7	11.1
¹³C chemical shifts	62	27	43.5
¹⁵N chemical shifts	1	1	100.0

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Found 1 Document (0.443 seconds)

BMRB: 18620

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. RRM domain, : 1 : 14 entities Detail

Experiments performed 8 experiments Detail

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Chemical shift validation 3 contents Detail