BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	82.7 % (239 of 289)	96.8 % (149 of 154)	61.6 % (69 of 112)	91.3 % (21 of 23)
Backbone	80.0 % (112 of 140)	97.8 % (45 of 46)	63.9 % (46 of 72)	95.5 % (21 of 22)
Sidechain	86.1 % (149 of 173)	96.3 % (104 of 108)	70.3 % (45 of 64)	0.0 % (0 of 1)
Aromatic	46.2 % (12 of 26)	92.3 % (12 of 13)	0.0 % (0 of 13)
Methyl	100.0 % (10 of 10)	100.0 % (5 of 5)	100.0 % (5 of 5)

1. entity 1

CSYTCXPQTY TFPTCEEAKK MKKRC

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_EEH_D1, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	design peptide NC_EEH_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_EEH_D1, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	design peptide NC_EEH_D1	natural abundance		1.0 mg/mL

Protein Blocks Logo

Calculated from 20 models in PDB: 5KWX, 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

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_30142_5kwx.nef
Input source #2: Coordindates	5kwx.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:15:CYS:SG	oxidized, CA 57.051, CB 45.821 ppm	oxidized, CA 56.523, CB 39.566 ppm	2.033
A:5:CYS:SG	A:25:CYS:SG	oxidized, CA 51.875, CB 41.739 ppm	oxidized, CA 56.743, CB 42.863 ppm	2.035

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)
1:5:CYS:C	1:6:DPR:N	unknown	unknown	n/a
1:6:DPR:C	1:7:PRO:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	6	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-----
CSYTCXPQTYTFPTCEEAKKMKKRC
|||||||||||||||||||||||||
CSYTCXPQTYTFPTCEEAKKMKKRC

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	25	0	0	100.0

Content subtype: combined_30142_5kwx.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	250		100.0 (chain: A, length: 25)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	285 (1)	noe	100.0 (chain: A, length: 25)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	14 (1)	hbond	36.0 (chain: A, length: 25)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	38 (38)	.	84.0 (chain: A, length: 25)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 25, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 156
  - ¹³C chemical shifts: 73
  - ¹⁵N chemical shifts: 21
- 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
6	DPR

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	154	149	96.8
¹³C chemical shifts	112	69	61.6
¹⁵N chemical shifts	24	21	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	46	45	97.8
¹³C chemical shifts	48	24	50.0
¹⁵N chemical shifts	22	21	95.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	108	104	96.3
¹³C chemical shifts	64	45	70.3
¹⁵N chemical shifts	2	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	5	83.3
¹³C chemical shifts	6	5	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	12	92.3
¹³C chemical shifts	13	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: 25, Sequence coverage: 100.0%
- Total number of restraints: 284
- Weight of restraints: 1.0 (284)
- Potential type of restraints: square-well-parabolic (284)
- 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: 25, Sequence coverage: 36.0%
  - Total number of restraints: 14
  - Weight of restraints: 1.0 (14)
  - Potential type of restraints: square-well-parabolic (14)
  - 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: 25, Sequence coverage: 84.0%
- Total number of restraints: 38
- Total number of restraints per polymer type: 38
- Weight of restraints: 1.0 (38)
- Potential type of restraints: square-well-parabolic (38)
- 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: 30142

Sample #1

Sample #2

Experiments performed 6 experiments Detail

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NMR combined restraints 5 contents Detail