BMRBj - BMREntryMaster

Found 1 Document (1.437 seconds)

BMRB: 1719

1NMI

Proton Nuclear Magnetic Resonance as a Probe of Differences in Structure between the C102T and F82S,C102T Variants of Iso-1-cytochrome c from the Yeast Saccharomyces cerevisiae

Authors

Gao, Y., Boyd, J., Pielak, G.J., Williams, R.J.P.

Assembly

cytochrome c

Entity

1. cytochrome c (polymer), 108 monomers, 13086.38 Da Detail

TEFKAGSAKK GATLFKTRXL QXHTVEKGGP HKVGPNLHGI FGRHSGQAEG YSYTDANIKK NVLWDENNMS EYLTNPXKYI PGTKMAFGGL KKEKDRNDLI TYLKKATE

Formula weight

13086.38 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 93.5 %, Completeness: 69.5 %, Completeness (bb): 92.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	69.5 % (454 of 653)	69.5 % (454 of 653)
Backbone	92.7 % (202 of 218)	92.7 % (202 of 218)
Sidechain	57.9 % (252 of 435)	57.9 % (252 of 435)
Aromatic	51.9 % (28 of 54)	51.9 % (28 of 54)
Methyl	91.3 % (42 of 46)	91.3 % (42 of 46)

1. cytochrome c

TEFKAGSAKK GATLFKTRXL QXHTVEKGGP HKVGPNLHGI FGRHSGQAEG YSYTDANIKK NVLWDENNMS EYLTNPXKYI PGTKMAFGGL KKEKDRNDLI TYLKKATE

Show sample condition

Sample

Temperature 300 K, pH 7

Release date

1995-07-30

Citation

Proton Nuclear Magnetic Resonance as a Probe of Differences in Structure between the C102T and F82S,C102T Variants of Iso-1-cytochrome c from the Yeast Saccharomyces cerevisiae
Gao, Y., Boyd, J., Pielak, G.J., Williams, R.J.P.
Biochemistry (1991), 30, 7033-7040, PubMed , DOI:

Related entities 1. cytochrome c, : 1 : 67 : 168 entities Detail

Interaction partners 1. cytochrome c, : 4 interactors Detail

More details for 4 interactors identified by 4 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr1719_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: bmr1719_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignment_data_set_one	Warning	539		93.5 (chain: 1, length: 108)

Assigned chemical shifts

Saveframe: chemical_shift_assignment_data_set_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 108, Sequence coverage: 93.5%
- Total number of assignments
  - ¹H chemical shifts: 539
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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)
54	THR	HG1	8.57
83	THR	HG1	9.23

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Found 1 Document (1.437 seconds)

BMRB: 1719

Sample

Related entities 1. cytochrome c, : 1 : 67 : 168 entities Detail

Interaction partners 1. cytochrome c, : 4 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail