BMRBj - BMREntryMaster

Found 1 Document (1.066 seconds)

BMRB: 1162

1Q5J

Sequence-specific 1H-NMR assignment and conformation of proteolytic fragment 163-231 of bacterioopsin

Authors

Barsukov, I.L., Abdulaeva, G.V., Arseniev, A.S., Bystrov, V.F.

Assembly

bacteriorhodopsin

Entity

1. bacteriorhodopsin (polymer), 69 monomers, 7530.977 Da Detail

MRPQVASTFK VLRNVTVVLW SAYPVVWLIG SEGAGIVPLN IETLLFMVLD VSAKVGFGLI LLRSRAIFG

Formula weight

7530.977 Da

Source organism

Halobacterium salinarum

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 92.8 %, Completeness: 80.8 %, Completeness (bb): 92.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	80.8 % (336 of 416)	80.8 % (336 of 416)
Backbone	92.9 % (131 of 141)	92.9 % (131 of 141)
Sidechain	74.5 % (205 of 275)	74.5 % (205 of 275)
Aromatic	44.4 % (16 of 36)	44.4 % (16 of 36)
Methyl	90.0 % (54 of 60)	90.0 % (54 of 60)

1. bacteriorhodopsin

MRPQVASTFK VLRNVTVVLW SAYPVVWLIG SEGAGIVPLN IETLLFMVLD VSAKVGFGLI LLRSRAIFG

Show sample condition

Sample

Temperature 303 K, pH 8

Release date

1995-07-30

Citation

Sequence-specific 1H-NMR assignment and conformation of proteolytic fragment 163-231 of bacterioopsin
Barsukov, I.L., Abdulaeva, G.V., Arseniev, A.S., Bystrov, V.F.
Eur. J. Biochem. (1990), 192, 321-327, PubMed 2209589 , DOI: , Abstract

Related entities 1. bacteriorhodopsin, : 1 : 100 : 32 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr1162_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: bmr1162_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignment_data_set_one	Warning	440		91.3 (chain: 1, length: 69)

Assigned chemical shifts

Saveframe: chemical_shift_assignment_data_set_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 69, Sequence coverage: 91.3%
- Total number of assignments
  - ¹H chemical shifts: 440
- 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)
16	THR	HG1	4.83
21	SER	HG	5.12
43	THR	HG1	4.68
52	SER	HG	4.28

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (1.066 seconds)

BMRB: 1162

Sample

Related entities 1. bacteriorhodopsin, : 1 : 100 : 32 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail