BMRBj - BMREntryMaster

Found 1 Document (1.14 seconds)

BMRB: 4800

1DY7

Chemical shifts of 1H resonances of the heme protons and of the side chain protons of the two axial ligands, His69 and Met106, and of Trp109 of the isolated c domain of Paracoccus pantotrophus in the reduced state

Authors

Steensma, E., Gordon, E., Oster, L.M., Ferguson, S.J., Hajdu, J.

Assembly

isolated reduced c domain of the cytochrome cd1 nitrite reductase

Entity

1. isolated reduced c domain (polymer, Thiol state: all other bound), 133 monomers, 14242.56 Da Detail

QEQVAPPKDP AAALEDHKTR TDNRYEPSLD NLAQQDVAAP GAPEGVSALS DAQYNEANKI YFERCAGCHG VLRKGATGKA LTPDLTRDLG FDYLQSFITY GSPAGMPNWG TSGELSAEQV DLMANYLLLD PAA

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

Total weight

14861.0625 Da

Max. entity weight

14242.56 Da

Entity Connection

thioether 2 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	thioether	sing	1:CYS65:SG	2:HEC1:CAB
2	thioether	sing	1:CYS68:SG	2:HEC1:CAC

Source organism

Paracoccus pantotrophus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 4.5 %, Completeness: 2.3 %, Completeness (bb): 2.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	2.3 % (17 of 751)	2.3 % (17 of 751)
Backbone	2.6 % (7 of 267)	2.6 % (7 of 267)
Sidechain	2.1 % (10 of 484)	2.1 % (10 of 484)
Aromatic	10.2 % (5 of 49)	10.2 % (5 of 49)
Methyl	1.5 % (1 of 68)	1.5 % (1 of 68)

1. isolated reduced c domain

QEQVAPPKDP AAALEDHKTR TDNRYEPSLD NLAQQDVAAP GAPEGVSALS DAQYNEANKI YFERCAGCHG VLRKGATGKA LTPDLTRDLG FDYLQSFITY GSPAGMPNWG TSGELSAEQV DLMANYLLLD PAA

Show sample condition

Sample

Temperature 278 (±1) K, Details The sample contains a slight excess of sodium ascorbate

#	Name	Concentration
1	isolated reduced c domain	1.0 ~ 2.0 mM
2	sodium phosphate	50 mM
3	sodium chloride	100 mM
4	sodium ascorbate	0.0 ~ 0.0 mM

Chem. Shift Complete2

Sequence coverage: 6.8 %, Completeness: 3.3 %, Completeness (bb): 3.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	3.3 % (50 of 1502)	3.3 % (50 of 1502)
Backbone	3.2 % (17 of 534)	3.2 % (17 of 534)
Sidechain	3.4 % (33 of 968)	3.4 % (33 of 968)
Aromatic	12.2 % (12 of 98)	12.2 % (12 of 98)
Methyl	2.9 % (4 of 136)	2.9 % (4 of 136)

1. isolated reduced c domain

QEQVAPPKDP AAALEDHKTR TDNRYEPSLD NLAQQDVAAP GAPEGVSALS DAQYNEANKI YFERCAGCHG VLRKGATGKA LTPDLTRDLG FDYLQSFITY GSPAGMPNWG TSGELSAEQV DLMANYLLLD PAA

Show sample condition

Sample

Temperature 278 (±1) K, Details The sample contains a slight excess of sodium ascorbate

#	Name	Concentration
1	isolated reduced c domain	1.0 ~ 2.0 mM
2	sodium phosphate	50 mM
3	sodium chloride	100 mM
4	sodium ascorbate	0.0 ~ 0.0 mM

Chem. Shift Complete3

Sequence coverage: 5.3 %, Completeness: 3.2 %, Completeness (bb): 3.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	3.2 % (73 of 2253)	3.2 % (73 of 2253)
Backbone	3.4 % (27 of 801)	3.4 % (27 of 801)
Sidechain	3.2 % (46 of 1452)	3.2 % (46 of 1452)
Aromatic	8.2 % (12 of 147)	8.2 % (12 of 147)
Methyl	2.9 % (6 of 204)	2.9 % (6 of 204)

1. isolated reduced c domain

QEQVAPPKDP AAALEDHKTR TDNRYEPSLD NLAQQDVAAP GAPEGVSALS DAQYNEANKI YFERCAGCHG VLRKGATGKA LTPDLTRDLG FDYLQSFITY GSPAGMPNWG TSGELSAEQV DLMANYLLLD PAA

Show sample condition

Sample

Temperature 300 (±1) K, Details The sample contains a slight excess of sodium ascorbate

#	Name	Concentration
1	isolated reduced c domain	1.0 ~ 2.0 mM
2	sodium phosphate	50 mM
3	sodium chloride	100 mM
4	sodium ascorbate	0.0 ~ 0.0 mM

Chem. Shift Complete4

Sequence coverage: 7.5 %, Completeness: 3.7 %, Completeness (bb): 3.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	3.7 % (112 of 3004)	3.7 % (112 of 3004)
Backbone	3.6 % (38 of 1068)	3.6 % (38 of 1068)
Sidechain	3.9 % (75 of 1936)	3.9 % (75 of 1936)
Aromatic	10.2 % (20 of 196)	10.2 % (20 of 196)
Methyl	3.3 % (9 of 272)	3.3 % (9 of 272)

1. isolated reduced c domain

QEQVAPPKDP AAALEDHKTR TDNRYEPSLD NLAQQDVAAP GAPEGVSALS DAQYNEANKI YFERCAGCHG VLRKGATGKA LTPDLTRDLG FDYLQSFITY GSPAGMPNWG TSGELSAEQV DLMANYLLLD PAA

Show sample condition

Sample

Temperature 300 (±1) K, Details The sample contains a slight excess of sodium ascorbate

#	Name	Concentration
1	isolated reduced c domain	1.0 ~ 2.0 mM
2	sodium phosphate	50 mM
3	sodium chloride	100 mM
4	sodium ascorbate	0.0 ~ 0.0 mM

Release date

2001-03-11

Citation

Heme Ligation and Conformational Plasticity in the Isolated c Domain of Cytochrome cd1 Nitrite Reductase
Steensma, E., Gordon, E., Oster, L.M., Ferguson, S.J., Hajdu, J.
J. Biol. Chem. (2001), 276, 5846-5855, PubMed , DOI:

Related entities 1. isolated reduced c domain, : 1 : 7 : 1 : 9 entities Detail

Experiments performed 4 experiments Detail

Chemical shift validation 7 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4800_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)
1:65:CYS:SG	2:1:HEC:CAB	unknown	unknown	n/a
1:68:CYS:SG	2:1:HEC:CAC	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
2	1	HEC	HEME C	Assigned chemical shifts

Content subtype: bmr4800_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	shift_Cond1_haem	Warning	23	100.0 (chain: 2, length: 1)
2	Assigned chemical shifts	shift_Cond1	Warning	15	No information
3	Assigned chemical shifts	shift_Cond2_haem	Warning	23	100.0 (chain: 2, length: 1)
4	Assigned chemical shifts	shift_Cond2	Warning	16	No information
1	Chemical shift references	chemical_shift_reference	OK	1	No information

Assigned chemical shifts

Saveframe: shift_Cond1_haem
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 2, Chain length: 1, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 23
- Completeness of assignments
  - Entity_assemble_ID: 2
- Histogram of normalized assigned chemical shifts
Saveframe: shift_Cond1
- Status: Warning
- Total number of assignments
  - ¹H chemical shifts: 15
- Histogram of normalized assigned chemical shifts
Saveframe: shift_Cond2_haem
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 2, Chain length: 1, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 23
- Completeness of assignments
  - Entity_assemble_ID: 2
- Histogram of normalized assigned chemical shifts
Saveframe: shift_Cond2
- Status: Warning
- Total number of assignments
  - ¹H chemical shifts: 16
- Histogram of normalized assigned chemical shifts

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Found 1 Document (1.14 seconds)

BMRB: 4800

Sample

Sample

Sample

Sample

Related entities 1. isolated reduced c domain, : 1 : 7 : 1 : 9 entities Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 7 contents Detail