BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	73.5 % (1091 of 1484)	78.1 % (611 of 782)	65.7 % (378 of 575)	80.3 % (102 of 127)
Backbone	70.9 % (508 of 716)	82.2 % (199 of 242)	58.7 % (210 of 358)	85.3 % (99 of 116)
Sidechain	75.3 % (666 of 884)	73.9 % (399 of 540)	79.6 % (265 of 333)	18.2 % (2 of 11)
Aromatic	27.1 % (19 of 70)	48.6 % (17 of 35)	0.0 % (0 of 33)	100.0 % (2 of 2)
Methyl	92.1 % (129 of 140)	92.9 % (65 of 70)	91.4 % (64 of 70)

1. entity 1

MGSSHHHHHH SSGLVPRGSH MGLLVLIWSN DKKLIEEARK MAEKANLYLL TLETDDKKIE DILKSLGPPV KILVLLEDTK DADKVKKEIE KKARKKNLPV RIRKVTSPDE AKRWIKEFSE E

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Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.8 mM [U-99% 13C; U-99% 15N] de novo protein RO2_20, 21.1 mM potassium phosphate monobasic, 28.9 mM sodium phosphate dibasic, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	de novo protein RO2_20	[U-99% 13C; U-99% 15N]	0.8 mM
2	potassium phosphate monobasic	natural abundance	21.1 mM
3	sodium phosphate dibasic	natural abundance	28.9 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 6VGB, Strand ID: A Detail

Release date

2020-05-05

Citation

Slow Transition Path Times Reveal a Complex Folding Barrier in a Designed Protein
Pan, X., Thompson, M.C., Zhang, Y., Liu, L., Fraser, J.S., Kelly, M., Kortemme, T.
Front. Chem. (2020), 8, 587824-587824, PubMed 33365300 , DOI 10.3389/fchem.2020.587824 , Abstract

Related entities 1. De novo designed protein ROS2 36830, : 1 : 6 entities Detail

Experiments performed 7 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AVANCE - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.8 mM [U-99% 13C; U-99% 15N] de novo protein RO2_20, 21.1 mM potassium phosphate monobasic, 28.9 mM sodium phosphate dibasic, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	de novo protein RO2_20	[U-99% 13C; U-99% 15N]	0.8 mM
2	potassium phosphate monobasic	natural abundance	21.1 mM
3	sodium phosphate dibasic	natural abundance	28.9 mM

2 2D 1H-13C HSQC

Instrument

Bruker AVANCE - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	de novo protein RO2_20	[U-99% 13C; U-99% 15N]	0.8 mM
2	potassium phosphate monobasic	natural abundance	21.1 mM
3	sodium phosphate dibasic	natural abundance	28.9 mM

3 3D CBCA(CO)NH

Instrument

Bruker DRX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	de novo protein RO2_20	[U-99% 13C; U-99% 15N]	0.8 mM
2	potassium phosphate monobasic	natural abundance	21.1 mM
3	sodium phosphate dibasic	natural abundance	28.9 mM

4 3D HNCACB

Instrument

Bruker DRX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	de novo protein RO2_20	[U-99% 13C; U-99% 15N]	0.8 mM
2	potassium phosphate monobasic	natural abundance	21.1 mM
3	sodium phosphate dibasic	natural abundance	28.9 mM

5 3D HCCH-TOCSY

Instrument

Bruker AVANCE - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	de novo protein RO2_20	[U-99% 13C; U-99% 15N]	0.8 mM
2	potassium phosphate monobasic	natural abundance	21.1 mM
3	sodium phosphate dibasic	natural abundance	28.9 mM

6 3D 1H-15N NOESY

Instrument

Bruker AVANCE - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	de novo protein RO2_20	[U-99% 13C; U-99% 15N]	0.8 mM
2	potassium phosphate monobasic	natural abundance	21.1 mM
3	sodium phosphate dibasic	natural abundance	28.9 mM

7 3D 1H-13C NOESY

Instrument

Bruker AVANCE - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	de novo protein RO2_20	[U-99% 13C; U-99% 15N]	0.8 mM
2	potassium phosphate monobasic	natural abundance	21.1 mM
3	sodium phosphate dibasic	natural abundance	28.9 mM

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_30708_6vgb.nef
Input source #2: Coordindates	6vgb.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

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--------40--------50--------60--------70--------80--------90-------100
MGSSHHHHHHSSGLVPRGSHMGLLVLIWSNDKKLIEEARKMAEKANLYLLTLETDDKKIEDILKSLGPPVKILVLLEDTKDADKVKKEIEKKARKKNLPV
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MGSSHHHHHHSSGLVPRGSHMGLLVLIWSNDKKLIEEARKMAEKANLYLLTLETDDKKIEDILKSLGPPVKILVLLEDTKDADKVKKEIEKKARKKNLPV

-------110-------120-
RIRKVTSPDEAKRWIKEFSEE
|||||||||||||||||||||
RIRKVTSPDEAKRWIKEFSEE

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	121	0	0	100.0

Content subtype: combined_30708_6vgb.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1083		86.0 (chain: A, length: 121)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	5074 (1)	noe	85.1 (chain: A, length: 121)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	96 (1)	hbond	55.4 (chain: A, length: 121)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 121, Sequence coverage: 86.0%
- Total number of assignments
  - ¹H chemical shifts: 612
  - ¹³C chemical shifts: 370
  - ¹⁵N chemical shifts: 101
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	782	612	78.3
¹³C chemical shifts	575	370	64.3
¹⁵N chemical shifts	127	101	79.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	242	204	84.3
¹³C chemical shifts	242	103	42.6
¹⁵N chemical shifts	116	99	85.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	540	408	75.6
¹³C chemical shifts	333	267	80.2
¹⁵N chemical shifts	11	2	18.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	73	67	91.8
¹³C chemical shifts	73	65	89.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	35	17	48.6
¹³C chemical shifts	33	0	0.0
¹⁵N chemical shifts	2	2	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 121, Sequence coverage: 85.1%
- Total number of restraints: 5074
- Weight of restraints: 1.0 (5074)
- Potential type of restraints: square-well-parabolic (5074)
- Range of distance target values: 2.02, 6.13 (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: 121, Sequence coverage: 55.4%
  - Total number of restraints: 96
  - Weight of restraints: 1.0 (96)
  - Potential type of restraints: square-well-parabolic (96)
  - Range of distance target values: 2.21, 3.22 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Keywords DE NOVO PROTEIN, Rossmann fold

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Found 1 Document (0.843 seconds)

BMRB: 30708

Sample

Related entities 1. De novo designed protein ROS2 36830, : 1 : 6 entities Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 4 contents Detail