BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	75.3 % (305 of 405)	85.8 % (188 of 219)	54.7 % (82 of 150)	97.2 % (35 of 36)
Backbone	74.3 % (156 of 210)	90.3 % (65 of 72)	55.3 % (57 of 103)	97.1 % (34 of 35)
Sidechain	76.3 % (174 of 228)	83.7 % (123 of 147)	62.5 % (50 of 80)	100.0 % (1 of 1)
Aromatic	50.0 % (8 of 16)	100.0 % (8 of 8)	0.0 % (0 of 8)
Methyl	100.0 % (18 of 18)	100.0 % (9 of 9)	100.0 % (9 of 9)

1. W35

CKQRRRYRGS EEECRKYAEE LSRRTGCEVE VECET

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Sample

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 (±0.5) K, pH 4.8 (±0.2), Details 50 mM sodium chloride, 25 mM sodium acetate, 1 mM [U-99% 15N] W35, 93% H2O/7% D2O

#	Name	Isotope labeling	Concentration
1	W35	[U-99% 15N]	1 (±0.2) mM
2	sodium acetate	natural abundance	25 (±1.0) mM
3	sodium chloride	natural abundance	50 (±2.0) mM
4	H2O	natural abundance	93 %
5	D2O	natural abundance	7 %

Protein Blocks Logo

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

Release date

2016-09-21

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

Entries sharing articles BMRB: 12 entries Detail

  BMRB: 30204 released on 2017-03-16
    Title Solution structure of the de novo mini protein gHH_44
  BMRB: 30069 released on 2016-09-21
    Title Solution structure of the de novo miniprotein EEHE_02
  BMRB: 30138 released on 2016-09-15
    Title NMR Solution Structure of Designed Peptide NC_HEE_D1
  BMRB: 30140 released on 2016-09-15
    Title NMR Solution Structure of Designed Peptide NC_EHE_D1
  BMRB: 30141 released on 2016-09-15
    Title NMR Solution Structure of Designed Peptide NC_EEH_D2
  BMRB: 30142 released on 2016-09-15
    Title NMR Solution Structure of Designed Peptide NC_EEH_D1
  BMRB: 30143 released on 2016-09-15
    Title NMR Solution Structure of Designed Peptide NC_cHH_D1
  BMRB: 30144 released on 2016-09-15
    Title NMR Solution Structure of Designed Peptide NC_cHh_DL_D1
  BMRB: 30145 released on 2016-09-15
    Title NMR Solution Structure of Designed Peptide NC_cHHH_D1
  BMRB: 30146 released on 2016-09-15
    Title NMR Solution Structure of Designed Peptide NC_cEE_D1
  BMRB: 26045 released on 2016-09-12
    Title Solution structure of the de novo mini protein HHH_06
  BMRB: 26046 released on 2016-09-12
    Title Solution structure of the de novo mini protein EEH_04

Related entities 1. W35, : 5 entities Detail

Experiments performed 8 experiments Detail

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30067_5jhi.nef
Input source #2: Coordindates	5jhi.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	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:27:CYS:SG	oxidized, CA 55.0, CB 48.3 ppm	oxidized, CA 52.4, CB 41.8 ppm	2.031
A:14:CYS:SG	A:33:CYS:SG	unknown, CA 59.0 ppm	oxidized, CA 55.2, CB 39.8 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--------30-----
CKQRRRYRGSEEECRKYAEELSRRTGCEVEVECET
|||||||||||||||||||||||||||||||||||
CKQRRRYRGSEEECRKYAEELSRRTGCEVEVECET

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	35	0	0	100.0

Content subtype: combined_30067_5jhi.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	317		100.0 (chain: A, length: 35)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	475 (1)	noe	100.0 (chain: A, length: 35)
2	Distance restraints	DYANA/DIANA_distance_constraints_5	Warning	12 (1)	undefined	11.4 (chain: A, length: 35)
3	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	40 (1)	hbond	71.4 (chain: A, length: 35)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	54 (54)	.	94.3 (chain: A, length: 35)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 200
  - ¹³C chemical shifts: 76
  - ¹⁵N chemical shifts: 41
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- 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	219	200	91.3
¹³C chemical shifts	150	76	50.7
¹⁵N chemical shifts	43	41	95.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	72	69	95.8
¹³C chemical shifts	70	29	41.4
¹⁵N chemical shifts	35	34	97.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	147	131	89.1
¹³C chemical shifts	80	47	58.8
¹⁵N chemical shifts	8	7	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	9	100.0
¹³C chemical shifts	9	9	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	8	100.0
¹³C chemical shifts	8	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: 35, Sequence coverage: 100.0%
- Total number of restraints: 475
- Weight of restraints: 1.0 (475)
- Potential type of restraints: square-well-parabolic (475)
- Range of distance target values: 2.28, 3.67 (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: DYANA/DIANA_distance_constraints_5
  - Status: Warning
  - Experiment type: undefined
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 11.4%
  - Total number of restraints: 12
  - Weight of restraints: 1.0 (12)
  - Potential type of restraints: upper-bound-parabolic (12)
  - Range of distance target values: 2.0, 3.1 (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_3
    - Status: OK
    - Experiment type: hbond
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 71.4%
    - Total number of restraints: 40
    - Weight of restraints: 1.0 (40)
    - Potential type of restraints: square-well-parabolic (40)
    - Range of distance target values: 1.9, 2.85 (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_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 35, Sequence coverage: 94.3%
- Total number of restraints: 54
- Total number of restraints per polymer type: 54
- Weight of restraints: 1.0 (54)
- Potential type of restraints: square-well-parabolic (54)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords DE NOVO PROTEIN

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Found 1 Document (0.671 seconds)

BMRB: 30067

Sample

Entries sharing articles BMRB: 12 entries Detail

Related entities 1. W35, : 5 entities Detail

Experiments performed 8 experiments Detail

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NMR combined restraints 6 contents Detail