BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	82.1 % (276 of 336)	100.0 % (188 of 188)	51.6 % (64 of 124)	100.0 % (24 of 24)
Backbone	75.0 % (114 of 152)	100.0 % (50 of 50)	51.3 % (40 of 78)	100.0 % (24 of 24)
Sidechain	86.2 % (181 of 210)	100.0 % (138 of 138)	59.7 % (43 of 72)
Aromatic	50.0 % (6 of 12)	100.0 % (6 of 6)	0.0 % (0 of 6)
Methyl	100.0 % (4 of 4)	100.0 % (2 of 2)	100.0 % (2 of 2)

1. entity 1

HDPEKRKECE KKYTDPKKRE ECKRKA

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 null, Temperature 298 (±0.1) K, pH 3.0 (±0.1), Details 1.0 mg/mL design peptide NC_cHH_D1, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	design peptide NC_cHH_D1	natural abundance		1.0 mg/mL

Sample #2

Solvent system 100% D2O, Pressure 1 null, Temperature 298 (±0.1) K, pH 3.0 (±0.1), Details 1.0 mg/mL design peptide NC_cHH_D1, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	design peptide NC_cHH_D1	natural abundance		1.0 mg/mL

Protein Blocks Logo

Calculated from 20 models in PDB: 5KWZ, Strand ID: A Detail

Release date

2016-09-15

Citation

Accurate de novo design of hyperstable constrained peptides
Bhardwaj, G., Mulligan, V.K., Bahl, C.D., Gilmore, J.M., Harvey, P.J., Cheneval, O., Buchko, G.W., Pulavarti, S.V., Kaas, Q., Eletsky, A., Huang, P.S., Johnsen, W.A., Greisen, P.J., Rocklin, G.J., Song, Y., Linsky, T.W., Watkins, A., Rettie, S.A., Xu, X., Carter, L.P., Bonneau, R., Olson, J.M., Coutsias, E., Correnti, C.E., Szyperski, T., Craik, D.J., Baker, D.
Nature (2016), 538, 329-335, PubMed 27626386 , DOI 10.1038/nature19791 , Abstract

Related entities 1. Designed peptide NC cHH D1, : 2 entities Detail

Experiments performed 6 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30143_5kwz.nef
Input source #2: Coordindates	5kwz.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	None
Whether the assembly contains a cyclic polymer	True (see coordinates for details)
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
A:9:CYS:SG	A:22:CYS:SG	oxidized, CA 57.597, CB 37.736 ppm	oxidized, CA 59.356, CB 34.531 ppm	2.033

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Sequence alignments

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

--------10--------20------
HDPEKRKECEKKYTDPKKREECKRKA
||||||||||||||||||||||||||
HDPEKRKECEKKYTDPKKREECKRKA

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	26	0	0	100.0

Content subtype: combined_30143_5kwz.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	2		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	272		100.0 (chain: A, length: 26)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	279 (1)	noe	100.0 (chain: A, length: 26)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	24 (1)	hbond	76.9 (chain: A, length: 26)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	52 (52)	.	100.0 (chain: A, length: 26)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 191
  - ¹³C chemical shifts: 57
  - ¹⁵N chemical shifts: 24
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
5	LYS	HZ1	7.394
5	LYS	HZ2	7.394
5	LYS	HZ3	7.394

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	188	188	100.0
¹³C chemical shifts	124	57	46.0
¹⁵N chemical shifts	27	24	88.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	50	100.0
¹³C chemical shifts	52	18	34.6
¹⁵N chemical shifts	24	24	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	138	138	100.0
¹³C chemical shifts	72	39	54.2
¹⁵N chemical shifts	3	0	0.0

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0
¹³C chemical shifts	6	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: 26, Sequence coverage: 100.0%
- Total number of restraints: 279
- Weight of restraints: 1.0 (279)
- Potential type of restraints: square-well-parabolic (279)
- Range of distance target values: 2.08, 3.65 (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: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 76.9%
  - Total number of restraints: 24
  - Weight of restraints: 1.0 (24)
  - Potential type of restraints: square-well-parabolic (24)
  - Range of distance target values: 1.0, 1.5 (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: 26, Sequence coverage: 100.0%
- Total number of restraints: 52
- Total number of restraints per polymer type: 52
- Weight of restraints: 1.0 (52)
- Potential type of restraints: square-well-parabolic (52)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords de novo protein, designed peptide

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Found 1 Document (0.523 seconds)

BMRB: 30143

Sample #1

Sample #2

Related entities 1. Designed peptide NC cHH D1, : 2 entities Detail

Experiments performed 6 experiments Detail

Instrument

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Sample

Instrument

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Sample

Instrument

Sample

NMR combined restraints 5 contents Detail