BMRBj - BMREntryMaster

Found 1 Document (1.588 seconds)

BMRB: 4808

1HKO

1H, 13C and 15N chemical shifts of bovine ferrous cytochrome b5 in complex with horse heart ferrous cytochrome c

Authors

Hom, K., Ma, Q., Wolfe, G., Zhang, H., Storch, E.M., Daggett, V., Basus, V.J., Waskell, L.

Assembly

ferrous cytochrome b5 complexed with ferrous cytochrome c

Entity

1. ferrous cytochrome b5 (polymer, Thiol state: not present), 82 monomers, 9462.250 Da Detail

AVKYYTLEEI QKHNDSKSTW LILHYKVYDL TKFLEEHPGG EEVLREQAGG DATENFEDVG HSTDARELSK TFIIGELHPD DR

2. cytochrome c (polymer, Thiol state: all other bound), 104 monomers, 11701.40 Da Detail

GDVEKGKKIF VQKCAQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGFTYTD ANKNKGITWK EETLMEYLEN PKKYIPGTKM IFAGIKKKTE REDLIAYLKK ATNE

3. HEM (non-polymer), 616.487 Da
4. HEC (non-polymer), 618.503 Da

Total weight

22398.64 Da

Max. entity weight

11701.4 Da

Source organism

Bos taurus , Equus caballus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 46.2 %, Completeness: 32.6 %, Completeness (bb): 35.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	32.6 % (722 of 2218)	36.4 % (423 of 1163)	25.6 % (220 of 861)	40.7 % (79 of 194)
Backbone	35.1 % (388 of 1104)	43.0 % (165 of 384)	26.7 % (144 of 540)	43.9 % (79 of 180)
Sidechain	30.5 % (391 of 1282)	33.2 % (259 of 779)	27.0 % (132 of 489)	0.0 % (0 of 14)
Aromatic	15.8 % (30 of 190)	15.8 % (15 of 95)	16.1 % (15 of 93)	0.0 % (0 of 2)
Methyl	42.6 % (75 of 176)	46.6 % (41 of 88)	38.6 % (34 of 88)

1. ferrous cytochrome b5

AVKYYTLEEI QKHNDSKSTW LILHYKVYDL TKFLEEHPGG EEVLREQAGG DATENFEDVG HSTDARELSK TFIIGELHPD DR

2. cytochrome c

GDVEKGKKIF VQKCAQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGFTYTD ANKNKGITWK EETLMEYLEN PKKYIPGTKM IFAGIKKKTE REDLIAYLKK ATNE

Show sample condition

Sample

Temperature 298 (±1) K

#	Name	Isotope labeling	Concentration
1	ferrous cytochrome b5	[U-90% 13C; U-90% 15N]	0.3 mM
2	PROTOPORPHYRIN IX CONTAINING FE		0.0 ~ 0.0 mM
3	cytochrome c		0.0 ~ 0.0 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	0.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: -0.27 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	0.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: -0.27 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	0.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: 0.01 ppm, Outliers: 1 Detail

Release date

2000-11-14

Citation 1

NMR studies of the association of cytochrome b5 with cytochrome c
Hom, K., Ma, Q., Wolfe, G., Zhang, H., Storch, E.M., Daggett, V., Basus, V.J., Waskell, L.
Biochemistry (2000), 39, 14025-14039, PubMed 11087350 , Abstract

Show more 1 citaion

Citation 2

NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 , Abstract

Hide non-primary 1 citaion

Related entities 1. ferrous cytochrome b5, : 1 : 12 : 250 entities Detail

Related entities 2. cytochrome c, : 40 entities Detail

Interaction partners 1. ferrous cytochrome b5, : 4 interactors Detail

More details for 4 interactors identified by 4 citations

Experiments performed 7 experiments Detail

Chemical shift validation 6 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4808_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: bmr4808_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	774		100.0 (chain: 1, length: 82)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 82, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 484
  - ¹³C chemical shifts: 212
  - ¹⁵N chemical shifts: 78
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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)
41	GLU	CD	182.2
46	GLU	CD	183.2
58	ASP	CG	178.67

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	496	402	81.0
¹³C chemical shifts	377	209	55.4
¹⁵N chemical shifts	88	78	88.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	168	158	94.0
¹³C chemical shifts	164	82	50.0
¹⁵N chemical shifts	80	78	97.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	328	244	74.4
¹³C chemical shifts	213	127	59.6
¹⁵N chemical shifts	8	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	42	41	97.6
¹³C chemical shifts	42	34	81.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	15	31.9
¹³C chemical shifts	46	15	32.6
¹⁵N chemical shifts	1	0	0.0

Keywords bovine cytochrome b5, heteronuclear NMR

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Found 1 Document (1.588 seconds)

BMRB: 4808

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. ferrous cytochrome b5, : 1 : 12 : 250 entities Detail

Related entities 2. cytochrome c, : 40 entities Detail

Interaction partners 1. ferrous cytochrome b5, : 4 interactors Detail

Experiments performed 7 experiments Detail

Instrument

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Chemical shift validation 6 contents Detail