BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	84.6 % (220 of 260)	95.8 % (138 of 144)	63.8 % (60 of 94)	100.0 % (22 of 22)
Backbone	81.7 % (103 of 126)	100.0 % (41 of 41)	65.2 % (43 of 66)	100.0 % (19 of 19)
Sidechain	88.5 % (138 of 156)	94.2 % (97 of 103)	76.0 % (38 of 50)	100.0 % (3 of 3)
Methyl	100.0 % (6 of 6)	100.0 % (3 of 3)	100.0 % (3 of 3)

1. entity 1

NPEDCRQDPE ANKSPEECKK LK

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 283 (±.1) K, pH 3.0 (±0.1), Details 1.0 mg/mL design peptide NC_cHHH_D1, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	design peptide NC_cHHH_D1	natural abundance		1.0 mg/mL

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 283 (±.1) K, pH 3.0 (±0.1), Details 1.0 mg/mL design peptide NC_cHHH_D1, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	design peptide NC_cHHH_D1	natural abundance		1.0 mg/mL

Protein Blocks Logo

Calculated from 20 models in PDB: 5KX1, Strand ID: A Detail

Release date

2016-09-15

Citation

Accurate de novo design of hyperstable constrained peptides
Baker, D., 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.
Nature (2016), 538, 329-335, PubMed 27626386 , DOI 10.1038/nature19791 , Abstract

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_30145_5kx1.nef
Input source #2: Coordindates	5kx1.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:5:CYS:SG	A:18:CYS:SG	oxidized, CA 56.734, CB 40.39 ppm	oxidized, CA 57.78, CB 39.258 ppm	2.032

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--
NPEDCRQDPEANKSPEECKKLK
||||||||||||||||||||||
NPEDCRQDPEANKSPEECKKLK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	22	0	0	100.0

Content subtype: combined_30145_5kx1.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	OK	218		100.0 (chain: A, length: 22)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	185 (1)	noe	100.0 (chain: A, length: 22)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	6 (1)	hbond	27.3 (chain: A, length: 22)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	42 (42)	.	100.0 (chain: A, length: 22)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 22, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 136
  - ¹³C chemical shifts: 60
  - ¹⁵N chemical shifts: 22
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	144	136	94.4
¹³C chemical shifts	94	60	63.8
¹⁵N chemical shifts	23	22	95.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	41	41	100.0
¹³C chemical shifts	44	22	50.0
¹⁵N chemical shifts	19	19	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	103	95	92.2
¹³C chemical shifts	50	38	76.0
¹⁵N chemical shifts	4	3	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	3	3	100.0
¹³C chemical shifts	3	3	100.0

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: 22, Sequence coverage: 100.0%
- Total number of restraints: 184
- Weight of restraints: 1.0 (184)
- Potential type of restraints: square-well-parabolic (184)
- Range of distance target values: 2.5, 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: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 22, Sequence coverage: 27.3%
  - Total number of restraints: 6
  - Weight of restraints: 1.0 (6)
  - Potential type of restraints: square-well-parabolic (6)
  - 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: 22, Sequence coverage: 100.0%
- Total number of restraints: 42
- Total number of restraints per polymer type: 42
- Weight of restraints: 1.0 (42)
- Potential type of restraints: square-well-parabolic (42)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords de novo protein, designed peptide

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BMRB: 30145

Sample #1

Sample #2

Experiments performed 6 experiments Detail

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Sample

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NMR combined restraints 5 contents Detail