BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	87.4 % (104 of 119)	100.0 % (62 of 62)	68.8 % (33 of 48)	100.0 % (9 of 9)
Backbone	79.0 % (49 of 62)	100.0 % (20 of 20)	60.6 % (20 of 33)	100.0 % (9 of 9)
Sidechain	97.1 % (66 of 68)	100.0 % (42 of 42)	92.3 % (24 of 26)
Aromatic	50.0 % (2 of 4)	100.0 % (2 of 2)	0.0 % (0 of 2)
Methyl	100.0 % (12 of 12)	100.0 % (6 of 6)	100.0 % (6 of 6)

1. entity 1

CTASIPPICH XXXR

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 Pa, Temperature 298 K, pH 3.5, Details 1 mM protein, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	protein	natural abundance		1 mM

Protein Blocks Logo

Calculated from 24 models in PDB: 6BVW, Strand ID: A Detail

Release date

2018-01-17

Citation

Development of Novel Melanocortin Receptor Agonists Based on the Cyclic Peptide Framework of Sunflower Trypsin Inhibitor-1
Durek, T., Cromm, P.M., White, A.M., Schroeder, C.I., Kaas, Q., Weidmann, J., Ahmad Fuaad, A., Cheneval, O., Harvey, P.J., Daly, N.L., Zhou, Y., Dellsen, A., Osterlund, T., Larsson, N., Knerr, L., Bauer, U., Kessler, H., Cai, M., Hruby, V.J., Plowright, A.T., Craik, D.J.
J. Med. Chem. (2018), 61, 3674-3684, PubMed 29605997 , DOI 10.1021/acs.jmedchem.8b00170 , Abstract

Related entities 1. Trypsin inhibitor 1 HFRW-3, : 1 : 2 entities Detail

Experiments performed 5 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30381_6bvw.nef
Input source #2: Coordindates	6bvw.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
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

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
A:1:CYS:SG	A:9:CYS:SG	oxidized, CA 55.252, CB 50.31 ppm	oxidized, CA 55.461, CB 46.876 ppm	2.122

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)
1:10:HIS:C	1:11:DPN:N	unknown	unknown	n/a
1:11:DPN:C	1:12:MMO:N	unknown	unknown	n/a
1:12:MMO:C	1:13:E9M:N	unknown	unknown	n/a
1:13:E9M:C	1:14:ARG:N	unknown	unknown	n/a
1:14:ARG:C	1:1:CYS:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	11	DPN	D-PHENYLALANINE	Assigned chemical shifts, Coordinates
A	12	MMO	N~2~-methyl-L-arginine	Assigned chemical shifts, Distance restraints, Coordinates
A	13	E9M	N-methyl-L-tryptophan	Assigned chemical shifts, Coordinates

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10----
CTASIPPICHXXXR
||||||||||||||
CTASIPPICHXXXR

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	14	0	0	100.0

Content subtype: combined_30381_6bvw.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	6		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	138		100.0 (chain: A, length: 14)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	92 (1)	noe	85.7 (chain: A, length: 14)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	2 (1)	hbond	14.3 (chain: A, length: 14)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	13 (13)	.	64.3 (chain: A, length: 14)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 14, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 83
  - ¹³C chemical shifts: 41
  - ¹⁵N chemical shifts: 14
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Comp_index_ID	Comp_ID
11	DPN
12	MMO
13	E9M

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	62	61	98.4
¹³C chemical shifts	48	33	68.8
¹⁵N chemical shifts	10	10	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	20	19	95.0
¹³C chemical shifts	22	9	40.9
¹⁵N chemical shifts	9	9	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	42	42	100.0
¹³C chemical shifts	26	24	92.3
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0
¹³C chemical shifts	6	6	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	2	2	100.0
¹³C chemical shifts	2	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 14, Sequence coverage: 85.7%
- Total number of restraints: 92
- Weight of restraints: 1.0 (92)
- Potential type of restraints: square-well-parabolic (92)
- Range of distance target values: 1.39, 2.75 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 14, Sequence coverage: 14.3%
  - Total number of restraints: 2
  - Weight of restraints: 1.0 (2)
  - Potential type of restraints: square-well-parabolic (2)
  - Range of distance target values: 1.15, 1.65 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 14, Sequence coverage: 64.3%
- Total number of restraints: 13
- Total number of restraints per polymer type: 13
- Weight of restraints: 1.0 (13)
- Potential type of restraints: square-well-parabolic (13)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords BIOSYNTHETIC PROTEIN, cyclic peptide, melanocortin, pharmacophore

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BMRB: 30381

Sample

Related entities 1. Trypsin inhibitor 1 HFRW-3, : 1 : 2 entities Detail

Experiments performed 5 experiments Detail

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NMR combined restraints 5 contents Detail