BMRBj - BMREntryMaster

Found 1 Document (2.489 seconds)

BMRB: 51407

1H and 13C chemical shifts for a peptide encompassing residues 2-36 of the human formin INF2 in aqueous solution

Authors

Jimenez, M.

Assembly

INF2(2-36)

Entity

1. INF2(2-36) (polymer, Thiol state: not present), 36 monomers, 3794.074 Da Detail

SVKEGAQRKW AALKEKLGPQ DSDPTEANLE SADPEX

Formula weight

3794.074 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.2 %, Completeness: 87.3 %, Completeness (bb): 78.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	87.3 % (309 of 354)	96.6 % (200 of 207)	74.1 % (109 of 147)
Backbone	78.5 % (135 of 172)	98.6 % (68 of 69)	65.0 % (67 of 103)
Sidechain	95.3 % (205 of 215)	95.7 % (132 of 138)	94.8 % (73 of 77)
Aromatic	100.0 % (11 of 11)	100.0 % (6 of 6)	100.0 % (5 of 5)
Methyl	100.0 % (28 of 28)	100.0 % (14 of 14)	100.0 % (14 of 14)

1. entity 1

SVKEGAQRKW AALKEKLGPQ DSDPTEANLE SADPEX

Show sample condition

Sample

Solvent system water, Pressure 1 atm, Temperature 278 K, pH 5.5

#	Name	Isotope labeling	Concentration
1	INF2(2-36)	natural abundance	1 mM
2	D2O	[U-2H]	10 % v/v
3	H2O	natural abundance	90 % v/v
4	DSS	natural abundance	0.1 mM

Release date

2022-04-21

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: 51422 released on 2022-04-27
    Title 1H, 13C and 15N backbone chemical shifts for human calmodulin 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. INF2(2-36), : 2 : 6 entities Detail

Interaction partners 1. INF2(2-36), : 49 interactors Detail

More details for 49 interactors identified by 8 citations

Experiments performed 6 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr51407_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

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
1	36	NH2	AMINO GROUP	Assigned chemical shifts

Content subtype: bmr51407_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	351		100.0 (chain: 1, length: 36)
1	Chemical shift references	chem_shift_reference_1	OK	2		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: 1, Chain length: 36, Sequence coverage: 100.0%

--------10--------20--------30------
SVKEGAQRKWAALKEKLGPQDSDPTEANLESADPEX
||||||||||||||||||||||||||||||||||||
SVKEGAQRKWAALKEKLGPQDSDPTEANLESADPEX

Total number of assignments
- ¹H chemical shifts: 246
- ¹³C chemical shifts: 105

Completeness of assignments

Entity_assemble_ID: 1

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
3	LYS	HZ1	7.608
3	LYS	HZ2	7.608
3	LYS	HZ3	7.608
8	ARG	HH11	6.515
8	ARG	HH12	6.515
8	ARG	HH21	6.939
8	ARG	HH22	6.939
9	LYS	HZ1	7.613
9	LYS	HZ2	7.613
9	LYS	HZ3	7.613
14	LYS	HZ1	7.609
14	LYS	HZ2	7.609
14	LYS	HZ3	7.609
16	LYS	HZ1	7.605
16	LYS	HZ2	7.605
16	LYS	HZ3	7.605

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	209	202	96.7
¹³C chemical shifts	147	105	71.4

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	69	68	98.6
¹³C chemical shifts	103	63	61.2

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	140	134	95.7
¹³C chemical shifts	77	73	94.8

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	14	14	100.0
¹³C chemical shifts	14	14	100.0

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0
¹³C chemical shifts	5	5	100.0

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

Keywords formins, INF2, actin, calmodulin-binding, peptide model

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Found 1 Document (2.489 seconds)

BMRB: 51407

Sample

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. INF2(2-36), : 2 : 6 entities Detail

Interaction partners 1. INF2(2-36), : 49 interactors Detail

Experiments performed 6 experiments Detail

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Chemical shift validation 3 contents Detail