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BMRB: 5224

7CRG

1H, 13C and 15N Chemical shifts assignments for the C-terminal domain (region 428-547) of human lamin A/C

Authors

Krimm, I., Couprie, J., Ostlund, C., Worman, H.J., Zinn-Justin, S.

Assembly

C-terminal domain of human lamin A/C

Entity

1. C-terminal domain of human lamin A/C (polymer, Thiol state: all free), 120 monomers, 13287.76 Da Detail

SSFSQHARTS GRVAVEEVDE EGKFVRLRNK SNEDQSMGNW QIKRQNGDDP LLTYRFPPKF TLKAGQVVTI WAAGAGATHS PPTDLVWKAQ NTWGCGNSLR TALINSTGEE VAMRKLVRSV

Formula weight

13287.76 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 92.6 %, Completeness (bb): 96.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	92.6 % (1271 of 1373)	91.6 % (655 of 715)	92.8 % (488 of 526)	97.0 % (128 of 132)
Backbone	96.8 % (687 of 710)	96.3 % (236 of 245)	96.6 % (338 of 350)	98.3 % (113 of 115)
Sidechain	89.7 % (693 of 773)	89.1 % (419 of 470)	90.6 % (259 of 286)	88.2 % (15 of 17)
Aromatic	76.0 % (79 of 104)	88.5 % (46 of 52)	62.5 % (30 of 48)	75.0 % (3 of 4)
Methyl	100.0 % (122 of 122)	100.0 % (61 of 61)	100.0 % (61 of 61)

1. lamin A/C

SSFSQHARTS GRVAVEEVDE EGKFVRLRNK SNEDQSMGNW QIKRQNGDDP LLTYRFPPKF TLKAGQVVTI WAAGAGATHS PPTDLVWKAQ NTWGCGNSLR TALINSTGEE VAMRKLVRSV

Show sample condition

Sample

Temperature 303 (±2) K

#	Name	Isotope labeling	Type	Concentration
1	lamin A/C	[U-13C; U-15N]		0.5 ~ 1.5 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	TSP	methyl protons	internal	direct	1.0
¹⁵N	TSP	methyl protons	internal	indirect	0.1013292
¹³C	TSP	methyl protons	internal	indirect	0.2514501

Referencing offset: 0.14 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	TSP	methyl protons	internal	direct	1.0
¹⁵N	TSP	methyl protons	internal	indirect	0.1013292
¹³C	TSP	methyl protons	internal	indirect	0.2514501

Referencing offset: 0.14 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	TSP	methyl protons	internal	direct	1.0
¹⁵N	TSP	methyl protons	internal	indirect	0.1013292
¹³C	TSP	methyl protons	internal	indirect	0.2514501

Referencing offset: -0.05 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	TSP	methyl protons	internal	direct	1.0
¹⁵N	TSP	methyl protons	internal	indirect	0.1013292
¹³C	TSP	methyl protons	internal	indirect	0.2514501

Referencing offset: 0.76 ppm, Outliers: 5 Detail

Release date

2002-08-21

Citation

1H, 13C and 15N resonance assignments of the C-terminal domain of human lamin A/C
Krimm, I., Couprie, J., Ostlund, C., Worman, H.J., Zinn-Justin, S.
J. Biomol. NMR (2002), 22, 371-372, PubMed 12018485 , Abstract

Related entities 1. C-terminal domain of human lamin A/C, : 1 : 3 : 6 : 100 entities Detail

Interaction partners 1. C-terminal domain of human lamin A/C, : 92 interactors Detail

More details for 92 interactors identified by 53 citations

Experiments performed 8 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5224_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: bmr5224_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	SET_1_LAMIN	Warning	1421		100.0 (chain: 1, length: 120)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: SET_1_LAMIN
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 120, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 802
  - ¹³C chemical shifts: 492
  - ¹⁵N chemical shifts: 127
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
5	GLN	CD	179.5
32	ASN	CG	175.9
41	GLN	CD	179.5
66	GLN	CD	179.8
90	GLN	CD	179.0
97	ASN	CG	176.5
105	ASN	CG	178.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	715	676	94.5
¹³C chemical shifts	526	485	92.2
¹⁵N chemical shifts	141	127	90.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	245	243	99.2
¹³C chemical shifts	240	228	95.0
¹⁵N chemical shifts	115	112	97.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	470	433	92.1
¹³C chemical shifts	286	257	89.9
¹⁵N chemical shifts	26	15	57.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	63	63	100.0
¹³C chemical shifts	63	63	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	52	46	88.5
¹³C chemical shifts	48	28	58.3
¹⁵N chemical shifts	4	3	75.0

Keywords lamin, LMNA, dystrophy, intermediate filament

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Found 1 Document (5.207 seconds)

BMRB: 5224

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. C-terminal domain of human lamin A/C, : 1 : 3 : 6 : 100 entities Detail

Interaction partners 1. C-terminal domain of human lamin A/C, : 92 interactors Detail

Experiments performed 8 experiments Detail

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Chemical shift validation 3 contents Detail