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

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Found 1 Document (0.281 seconds)

BMRB: 30838

Entries sharing articles BMRB: 2 entries Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail