BMRBj - BMREntryMaster

Found 1 Document (0.423 seconds)

BMRB: 18828

NMR Assignment of Arabidopsis thaliana cytochrome c in its reduced state

Authors

Moreno-Beltran, B., Diaz-Moreno, I., Diaz-Quintana, A.J., De la Rosa, M.A.

Assembly

holocytochrome c

Entity

1. cytochrome c peptide (polymer, Thiol state: all other bound), 111 monomers, 12107.62 Da Detail

ASFDEAPPGN PKAGEKIFRT KCAQCHTVEK GAGHKQGPNL NGLFGRQSGT TPGYSYSAAN KSMAVNWEEK TLYDYLLNPK KYIPGTKMVF PGLKKPQDRA DLIAYLKEGT A

2. HEME C (non-polymer), 618.503 Da

Total weight

12726.123 Da

Max. entity weight

12107.62 Da

Entity Connection

covalent 2 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	covalent	sing	1:CYS22:SG	2:HEC1:HEC
2	covalent	sing	1:CYS25:SG	2:HEC1:HEC

Source organism

Arabidopsis thaliana

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 89.2 %, Completeness: 30.4 %, Completeness (bb): 61.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	30.4 % (240 of 790)	19.2 % (130 of 677)	97.3 % (110 of 113)
Backbone	61.2 % (200 of 327)	44.9 % (101 of 225)	97.1 % (99 of 102)
Sidechain	8.6 % (40 of 463)	6.4 % (29 of 452)	100.0 % (11 of 11)
Aromatic	3.6 % (2 of 55)	1.9 % (1 of 54)	100.0 % (1 of 1)
Methyl	2.2 % (1 of 46)	2.2 % (1 of 46)

1. cytochrome c peptide

ASFDEAPPGN PKAGEKIFRT KCAQCHTVEK GAGHKQGPNL NGLFGRQSGT TPGYSYSAAN KSMAVNWEEK TLYDYLLNPK KYIPGTKMVF PGLKKPQDRA DLIAYLKEGT A

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Concentration
1	polymer	[U-99% 15N]	2 mM
2	sodium phosphate	natural abundance	5 mM
3	H2O	natural abundance	90 %
4	D2O	natural abundance	10 %

Release date

2014-02-13

Citation

Communication between (L)-galactono-1,4-lactone dehydrogenase and cytochrome c
Hervas, M., Bashir, Q., Leferink, N.G.H., Ferreira, P., Moreno-Beltran, B., Westphal, A.H., Diaz-Moreno, I., Medina, M., de la Rosa, M.A., Ubbink, M., Navarro, J.A., van Berkel, W.J.H.
FEBS J. (2013), 280, 1830-1840, PubMed 23438074 , DOI 10.1111/febs.12207 , Abstract

Related entities 1. cytochrome c peptide, : 2 : 234 entities Detail

Interaction partners 1. cytochrome c peptide, : 3 interactors Detail

More details for 3 interactors identified by 1 citations

Experiments performed 3 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr18828_3.str
Diamagnetism of the molecular assembly	False (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:22:CYS:SG	2:1:HEC:HEC	unknown	unknown	n/a
1:25:CYS:SG	2:1:HEC:HEC	unknown	unknown	n/a

Non-standard residues

None

Content subtype: bmr18828_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	234		89.2 (chain: 1, length: 111)
1	Chemical shift references	DSS	OK	2		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 111, Sequence coverage: 89.2%
- Total number of assignments
  - ¹H chemical shifts: 122
  - ¹⁵N chemical shifts: 112
- Completeness of assignments
  - Entity_assemble_ID: 1
- Tautomeric state of HIS
- 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)
26	HIS	HD1	9.492
26	HIS	ND1	129.797

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	677	121	17.9
¹⁵N chemical shifts	116	111	95.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	225	99	44.0
¹⁵N chemical shifts	102	99	97.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	452	22	4.9
¹⁵N chemical shifts	14	12	85.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	48	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	54	1	1.9
¹⁵N chemical shifts	1	1	100.0

Keywords cytochrome c, electron transfer, flavoprotein, L galactono-1, 4 lactone dehydrogenase, NMR

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Found 1 Document (0.423 seconds)

BMRB: 18828

Sample

Related entities 1. cytochrome c peptide, : 2 : 234 entities Detail

Interaction partners 1. cytochrome c peptide, : 3 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 4 contents Detail