BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	81.9 % (262 of 320)	97.1 % (169 of 174)	58.3 % (70 of 120)	88.5 % (23 of 26)
Backbone	78.3 % (119 of 152)	98.0 % (49 of 50)	62.8 % (49 of 78)	87.5 % (21 of 24)
Sidechain	86.1 % (167 of 194)	96.8 % (120 of 124)	66.2 % (45 of 68)	100.0 % (2 of 2)
Aromatic	50.0 % (10 of 20)	100.0 % (10 of 10)	0.0 % (0 of 10)
Methyl	100.0 % (12 of 12)	100.0 % (6 of 6)	100.0 % (6 of 6)

1. entity 1

NDKCKELKKR YPNCEVRCDX PRYEVHC

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 null, Temperature 298 (±0.1) K, pH 3.0 (±0.05), Details 1.0 mg/mL NC_HEE_D1, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	NC_HEE_D1	natural abundance		1.0 mg/mL

Sample #2

Solvent system 100% D2O, Pressure 1 null, Temperature 298 (±0.1) K, pH 3.0 (±0.05), Details 1.0 mg/mL NC_HEE_D1, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	NC_HEE_D1	natural abundance		1.0 mg/mL

Protein Blocks Logo

Calculated from 20 models in PDB: 5KVN, 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 HEE 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_30138_5kvn.nef
Input source #2: Coordindates	5kvn.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:4:CYS:SG	A:18:CYS:SG	oxidized, CA 59.813, CB 40.7 ppm	oxidized, CA 53.95, CB 45.132 ppm	2.032
A:14:CYS:SG	A:27:CYS:SG	oxidized, CB 48.403 ppm	oxidized, CA 54.322, CB 43.642 ppm	2.031

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)
1:19:ASP:C	1:20:DPR:N	unknown	unknown	n/a
1:20:DPR:C	1:21:PRO:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	20	DPR	D-PROLINE	Assigned chemical shifts, Distance restraints, Torsion angle restraints, Coordinates

Sequence alignments

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

--------10--------20-------
NDKCKELKKRYPNCEVRCDXPRYEVHC
|||||||||||||||||||||||||||
NDKCKELKKRYPNCEVRCDXPRYEVHC

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	27	0	0	100.0

Content subtype: combined_30138_5kvn.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	4		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	278		100.0 (chain: A, length: 27)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	410 (1)	noe	100.0 (chain: A, length: 27)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	20 (1)	hbond	48.1 (chain: A, length: 27)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	50 (50)	.	96.3 (chain: A, length: 27)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 27, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 182
  - ¹³C chemical shifts: 73
  - ¹⁵N chemical shifts: 23
- 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
20	DPR

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
10	ARG	HH11	7.051
10	ARG	HH12	7.051
17	ARG	HH11	7.234
17	ARG	HH12	7.234
22	ARG	HH11	7.228
22	ARG	HH12	7.228

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	174	169	97.1
¹³C chemical shifts	120	69	57.5
¹⁵N chemical shifts	29	23	79.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	49	98.0
¹³C chemical shifts	52	24	46.2
¹⁵N chemical shifts	24	21	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	124	120	96.8
¹³C chemical shifts	68	45	66.2
¹⁵N chemical shifts	5	2	40.0

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	10	10	100.0
¹³C chemical shifts	10	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: 27, Sequence coverage: 100.0%
- Total number of restraints: 410
- Weight of restraints: 1.0 (410)
- Potential type of restraints: square-well-parabolic (410)
- Range of distance target values: 2.28, 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: 27, Sequence coverage: 48.1%
  - Total number of restraints: 20
  - Weight of restraints: 1.0 (20)
  - Potential type of restraints: square-well-parabolic (20)
  - 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: 27, Sequence coverage: 96.3%
- Total number of restraints: 50
- Total number of restraints per polymer type: 50
- Weight of restraints: 1.0 (50)
- Potential type of restraints: square-well-parabolic (50)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords DE NOVO PROTEIN, designed 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 (0.574 seconds)

BMRB: 30138

Sample #1

Sample #2

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

Experiments performed 6 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail