BMRBj - BMREntryMaster

Found 1 Document (0.654 seconds)

BMRB: 51422

6O20

1H, 13C and 15N backbone chemical shifts for human calmodulin in aqueous solution

Authors

Jimenez, M., Comas, L., Pantoja-Uceda, D., Valdes, P.

Assembly

CaM

Entity

1. CaM, entity 1 (polymer, Thiol state: not present), 148 monomers, 16706.21 Da Detail

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

2. CaM, entity CA (non-polymer), 40.078 × 4 Da

Total weight

16866.523 Da

Max. entity weight

16706.21 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 46.4 %, Completeness (bb): 82.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	46.4 % (778 of 1676)	21.8 % (189 of 867)	68.8 % (444 of 645)	88.4 % (145 of 164)
Backbone	82.9 % (733 of 884)	51.5 % (157 of 305)	99.5 % (431 of 433)	99.3 % (145 of 146)
Sidechain	19.5 % (181 of 929)	5.9 % (33 of 562)	42.4 % (148 of 349)	0.0 % (0 of 18)
Aromatic	0.0 % (0 of 100)	0.0 % (0 of 50)	0.0 % (0 of 50)
Methyl	15.5 % (22 of 142)	8.5 % (6 of 71)	22.5 % (16 of 71)

1. entity 1

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

Show sample condition

Sample

Solvent system water, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
1	CaM	[U-100% 13C; U-100% 15N]	0.25 mM
2	D2O	[U-2H]	10 % v/v
3	H2O	natural abundance	90 % v/v
4	Tris-HCl	natural abundance	20 mM
5	NaCl	natural abundance	10 mM
6	CaCl2	natural abundance	5 mM

Release date

2022-04-27

Citation

Structure and function of the N-terminal extension of the formin INF2
Labat-de-Hoz, L., Comas, L., Rubio-Ramos, A., Casares-Arias, J., Fernandez-Martin, L., Pantoja-Uceda, D., Martin, M., Kremer, L., Jimenez, M., Correas, I., Alonso, M.A.
Cell. Mol. Life Sci. (2022), 79, 571-571, PubMed 36306014 , DOI 10.1007/s00018-022-04581-y , Abstract

Entries sharing articles BMRB: 4 entries Detail

  BMRB: 51407 released on 2022-04-21
    Title 1H and 13C chemical shifts for a peptide encompassing residues 2-36 of the human formin INF2 in aqueous solution
  BMRB: 51408 released on 2022-04-21
    Title 1H and 13C chemical shifts for a peptide encompassing residues 2-36 of the human formin INF2 in 30% TFE
  BMRB: 51388 released on 2022-04-05
    Title 1H and 13C chemical shifts for a peptide encompassing residues 2-19 of the human formin INF2 in 30% TFE
  BMRB: 51389 released on 2022-04-05
    Title 1H and 13C chemical shifts for a peptide encompassing residues 2-19 of the human formin INF2 in aqueous solution

Related entities 1. CaM, entity 1, : 1 : 111 : 6 : 3 : 178 entities Detail

Interaction partners 1. CaM, entity 1, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 7 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr51422_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: bmr51422_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	721		100.0 (chain: 1, length: 148)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 148, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 431
  - ¹H chemical shifts: 145
  - ¹⁵N chemical shifts: 145
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- 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 (%)
¹³C chemical shifts	645	431	66.8
¹H chemical shifts	867	145	16.7
¹⁵N chemical shifts	164	145	88.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	433	431	99.5
¹H chemical shifts	305	145	47.5
¹⁵N chemical shifts	146	145	99.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	349	135	38.7
¹H chemical shifts	562	0	0.0
¹⁵N chemical shifts	18	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	80	11	13.8
¹H chemical shifts	80	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	50	0	0.0
¹H chemical shifts	50	0	0.0

Keywords calmodulin, formins, calcium, actin, NMR

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Found 1 Document (0.654 seconds)

BMRB: 51422

Sample

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. CaM, entity 1, : 1 : 111 : 6 : 3 : 178 entities Detail

Interaction partners 1. CaM, entity 1, : 1 interactors Detail

Experiments performed 7 experiments Detail

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Chemical shift validation 4 contents Detail