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Found 1 Document (1.324 seconds)

BMRB: 6967

2FWL

1H and 15N assignment of cytochrome c552 from Thermus thermophilus in the oxidized state

Authors

Muresanu, L., Pristovsek, P., Loehr, F., Maneg, O., Mukrasch, M.D., Rueterjans, H., Ludwig, B., Luecke, C.

Assembly

cytochrome c552

Entity

1. cytochrome c552 (polymer, Thiol state: all other bound), 133 monomers, 14404.69 Da Detail

MAQADGAKIY AQCAGCHQQN GQGIPGAFPP LAGHVAEILA KEGGREYLIL VLLYGLQGQI EVKGMKYNGV MSSFAQLKDE EIAAVLNHIA TAWGDAKKVK GFKPFTAEEV KKLRAKKLTP QQVLTERKKL GLK

2. HEM (non-polymer), 616.487 Da

Total weight

15021.178 Da

Max. entity weight

14404.69 Da

Entity Connection

metal coordination 2, covalent 2 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	covalent	sing	2:HEM1:CAB	1:CYS13:SG
2	covalent	sing	2:HEM1:CAC	1:CYS16:SG
3	metal coordination	sing	2:HEM1:FE	1:HIS17:NE2
4	metal coordination	sing	2:HEM1:FE	1:MET71:SD

Source organism

Thermus thermophilus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 97.0 %, Completeness (bb): 98.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	97.0 % (931 of 960)	96.6 % (790 of 818)	99.3 % (141 of 142)
Backbone	98.5 % (398 of 404)	98.2 % (271 of 276)	99.2 % (127 of 128)
Sidechain	95.9 % (533 of 556)	95.8 % (519 of 542)	100.0 % (14 of 14)
Aromatic	95.9 % (47 of 49)	95.8 % (46 of 48)	100.0 % (1 of 1)
Methyl	100.0 % (79 of 79)	100.0 % (79 of 79)

1. cytochrome c552

MAQADGAKIY AQCAGCHQQN GQGIPGAFPP LAGHVAEILA KEGGREYLIL VLLYGLQGQI EVKGMKYNGV MSSFAQLKDE EIAAVLNHIA TAWGDAKKVK GFKPFTAEEV KKLRAKKLTP QQVLTERKKL GLK

Show sample condition

Sample #1

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Type	Concentration
1	cytochrome c552	protein	2 mM
2	potassium phosphate	buffer	20 mM
3	potassium hexacyanoferrate (III)	oxidizing agent	5 mM

Sample #2

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	cytochrome c552	[U-98% 15N]	protein	2 mM
5	potassium phosphate		buffer	20 mM
6	potassium hexacyanoferrate (III)		oxidizing agent	5 mM

Release date

2006-04-26

Citation

The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase. A combined NMR and computational approach
Muresanu, L., Pristovsek, P., Loehr, F., Maneg, O., Mukrasch, M.D., Rueterjans, H., Ludwig, B., Luecke, C.
J. Biol. Chem. (2006), 281, 14503-14513, PubMed 16554303 , DOI 10.1074/jbc.M601108200 , Abstract

Related entities 1. cytochrome c552, : 1 : 7 : 21 entities Detail

Experiments performed 5 experiments Detail

1 1H-1H_TOCSY

Instrument

Model Bruker DMX (600 MHz)

Sample #1

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Type	Concentration
1	cytochrome c552	protein	2 mM
2	potassium phosphate	buffer	20 mM
3	potassium hexacyanoferrate (III)	oxidizing agent	5 mM

Sample #2

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	cytochrome c552	[U-98% 15N]	protein	2 mM
5	potassium phosphate		buffer	20 mM
6	potassium hexacyanoferrate (III)		oxidizing agent	5 mM

2 1H-1H_NOESY

Instrument

Model Bruker DMX (600 MHz)

Sample #1

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Type	Concentration
1	cytochrome c552	protein	2 mM
2	potassium phosphate	buffer	20 mM
3	potassium hexacyanoferrate (III)	oxidizing agent	5 mM

Sample #2

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	cytochrome c552	[U-98% 15N]	protein	2 mM
5	potassium phosphate		buffer	20 mM
6	potassium hexacyanoferrate (III)		oxidizing agent	5 mM

3 15N-1H_TROSY

Instrument

Model Bruker DMX (600 MHz)

Sample #1

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Type	Concentration
1	cytochrome c552	protein	2 mM
2	potassium phosphate	buffer	20 mM
3	potassium hexacyanoferrate (III)	oxidizing agent	5 mM

Sample #2

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	cytochrome c552	[U-98% 15N]	protein	2 mM
5	potassium phosphate		buffer	20 mM
6	potassium hexacyanoferrate (III)		oxidizing agent	5 mM

4 15N-1H_TOCSY-TROSY

Instrument

Model Bruker DMX (600 MHz)

Sample #1

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Type	Concentration
1	cytochrome c552	protein	2 mM
2	potassium phosphate	buffer	20 mM
3	potassium hexacyanoferrate (III)	oxidizing agent	5 mM

Sample #2

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	cytochrome c552	[U-98% 15N]	protein	2 mM
5	potassium phosphate		buffer	20 mM
6	potassium hexacyanoferrate (III)		oxidizing agent	5 mM

5 15N-1H_NOESY-TROSY

Instrument

Model Bruker DMX (600 MHz)

Sample #1

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Type	Concentration
1	cytochrome c552	protein	2 mM
2	potassium phosphate	buffer	20 mM
3	potassium hexacyanoferrate (III)	oxidizing agent	5 mM

Sample #2

Temperature 298 (±0.1) K, pH 6.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
4	cytochrome c552	[U-98% 15N]	protein	2 mM
5	potassium phosphate		buffer	20 mM
6	potassium hexacyanoferrate (III)		oxidizing agent	5 mM

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6967_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)
2:1:HEM:CAB	1:13:CYS:SG	unknown	unknown	n/a
2:1:HEM:CAC	1:16:CYS:SG	unknown	unknown	n/a
2:1:HEM:FE	1:17:HIS:NE2	unknown	unknown	n/a
2:1:HEM:FE	1:71:MET:SD	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
2	1	HEM	PROTOPORPHYRIN IX CONTAINING FE	Assigned chemical shifts

Content subtype: bmr6967_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	1113		100.0 (chain: 1, length: 133), 100.0 (chain: 2, length: 1)
1	Chemical shift references	chemical_shift_referencing	OK	2		No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 133, Sequence coverage: 100.0%
  - Entity_assembly_ID: 2, Chain length: 1, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 969
  - ¹⁵N chemical shifts: 144
- Completeness of assignments
  - Entity_assemble_ID: 1
  - Entity_assemble_ID: 2
- 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)
127	ARG	HH21	9.56
127	ARG	HH22	9.56

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	818	801	97.9
¹⁵N chemical shifts	145	144	99.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	276	275	99.6
¹⁵N chemical shifts	128	127	99.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	542	526	97.0
¹⁵N chemical shifts	17	17	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	82	80	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	48	46	95.8
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	24	6	25.0
¹⁵N chemical shifts	4	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	24	6	25.0
¹⁵N chemical shifts	4	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	4	4	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹⁵N chemical shifts	2	0	0.0

Keywords heme c, redox protein

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Found 1 Document (1.324 seconds)

BMRB: 6967

Sample #1

Sample #2

Related entities 1. cytochrome c552, : 1 : 7 : 21 entities Detail

Experiments performed 5 experiments Detail

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Chemical shift validation 4 contents Detail