BMRBj - BMREntryMaster

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val	Val err	Ambig. code
1	1	1	LEU	HA	H	5.010	0.013	1
2	1	1	LEU	H1	H	7.340	0.013	1
3	1	2	DLE	H	H	7.350	0.013	1
4	1	2	DLE	HA	H	4.550	0.013	1
5	1	3	LEU	H	H	8.040	0.013	1
6	1	3	LEU	HA	H	3.500	0.013	1
7	1	4	LEU	H	H	8.200	0.013	1
8	1	4	LEU	HA	H	4.220	0.013	1
9	1	5	DPR	HA	H	4.240	0.013	1
10	1	6	N9K	H11	H	8.030	0.013	1

Release date

2023-10-01

Citation

Connecting Hydrophobic Surfaces in Cyclic Peptides Increases Membrane Permeability
Hoang, H.N., Hill, T.A., Fairlie, D.P.
Angew. Chem Int Ed Engl. (2021), 60, 8385-8390, PubMed 33185961 , DOI 10.1002/anie.202012643 , Abstract

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 30839 released on 2021-08-30
    Title Connecting hydrophobic surfaces in cyclic peptides increases membrane permeability
  BMRB: 30840 released on 2021-08-30
    Title Connecting hydrophobic surfaces in cyclic peptides increases membrane permeability

Experiments performed 1 experiments Detail

#	Name	Isotope labeling	Type	Concentration
1	cyclic peptide LEU-DLE-LEU-LEU-DPR-N9K	natural abundance		1.0 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30838_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	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)
1:1:LEU:N	1:6:N9K:C24	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
1	2	DLE	D-LEUCINE	Assigned chemical shifts
1	5	DPR	D-PROLINE	Assigned chemical shifts
1	6	N9K	(2~{S})-3-(4-hydroxyphenyl)-2-(methylamino)propanoic acid	Assigned chemical shifts

Content subtype: bmr30838_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	10		100.0 (chain: 1, length: 6)
1	Chemical shift references	chem_shift_reference_1	OK	1		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 6, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 10
- 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
2	DLE
5	DPR
6	N9K

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	21	5	23.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	5	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	0	0.0

Keywords PEPTIDE BINDING PROTEIN, cyclic peptide

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 (0.501 seconds)

BMRB: 30838

Entries sharing articles BMRB: 2 entries Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail