BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	67.6 % (983 of 1455)	68.9 % (523 of 759)	62.4 % (352 of 564)	81.8 % (108 of 132)
Backbone	71.3 % (525 of 736)	81.5 % (203 of 249)	59.6 % (220 of 369)	86.4 % (102 of 118)
Sidechain	66.9 % (561 of 838)	62.7 % (320 of 510)	74.8 % (235 of 314)	42.9 % (6 of 14)
Aromatic	6.5 % (4 of 62)	6.5 % (2 of 31)	0.0 % (0 of 29)	100.0 % (2 of 2)
Methyl	94.4 % (136 of 144)	93.1 % (67 of 72)	95.8 % (69 of 72)

1. entity 1

MGSSHHHHHH SSGLVPRGSH MRLVVLIVSN DKKLIEEARK MAEKANLELI TVPGSPEEAI RLAQEIAEKA PGPVKVLVLI TGSADPDEKT KAKKAAEEAR KWNVRVRTVT SPDEAKRWIK EFSEE

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.74 mM [U-99% 13C; U-99% 15N] de novo protein RO2_1, 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_1	[U-99% 13C; U-99% 15N]	0.74 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: 6VGA, Strand ID: A Detail

Release date

2020-05-05

Citation

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

Related entities 1. De novo designed protein ROS2 835, : 1 : 7 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 0.74 mM [U-99% 13C; U-99% 15N] de novo protein RO2_1, 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_1	[U-99% 13C; U-99% 15N]	0.74 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_1	[U-99% 13C; U-99% 15N]	0.74 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_1	[U-99% 13C; U-99% 15N]	0.74 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_1	[U-99% 13C; U-99% 15N]	0.74 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_1	[U-99% 13C; U-99% 15N]	0.74 mM
2	potassium phosphate monobasic	natural abundance	21.1 mM
3	sodium phosphate dibasic	natural abundance	28.9 mM

6 3D 1H-13C NOESY

Instrument

Bruker AVANCE - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	de novo protein RO2_1	[U-99% 13C; U-99% 15N]	0.74 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_1	[U-99% 13C; U-99% 15N]	0.74 mM
2	potassium phosphate monobasic	natural abundance	21.1 mM
3	sodium phosphate dibasic	natural abundance	28.9 mM

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30707_6vga.nef
Input source #2: Coordindates	6vga.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
MGSSHHHHHHSSGLVPRGSHMRLVVLIVSNDKKLIEEARKMAEKANLELITVPGSPEEAIRLAQEIAEKAPGPVKVLVLITGSADPDEKTKAKKAAEEAR
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MGSSHHHHHHSSGLVPRGSHMRLVVLIVSNDKKLIEEARKMAEKANLELITVPGSPEEAIRLAQEIAEKAPGPVKVLVLITGSADPDEKTKAKKAAEEAR

-------110-------120-----
KWNVRVRTVTSPDEAKRWIKEFSEE
|||||||||||||||||||||||||
KWNVRVRTVTSPDEAKRWIKEFSEE

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	125	0	0	100.0

Content subtype: combined_30707_6vga.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	959		84.0 (chain: A, length: 125)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	2323 (1)	noe	84.0 (chain: A, length: 125)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	50 (1)	hbond	55.2 (chain: A, length: 125)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	226 (226)	.	98.4 (chain: A, length: 125)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 125, Sequence coverage: 84.0%
- Total number of assignments
  - ¹H chemical shifts: 520
  - ¹³C chemical shifts: 335
  - ¹⁵N chemical shifts: 104
- 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	759	520	68.5
¹³C chemical shifts	564	335	59.4
¹⁵N chemical shifts	132	104	78.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	249	204	81.9
¹³C chemical shifts	250	105	42.0
¹⁵N chemical shifts	118	99	83.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	510	316	62.0
¹³C chemical shifts	314	230	73.2
¹⁵N chemical shifts	14	5	35.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	75	66	88.0
¹³C chemical shifts	75	66	88.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	31	2	6.5
¹³C chemical shifts	29	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: 125, Sequence coverage: 84.0%
- Total number of restraints: 2323
- Weight of restraints: 1.0 (2323)
- Potential type of restraints: square-well-parabolic (2323)
- Range of distance target values: 2.57, 4.92 (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: 125, Sequence coverage: 55.2%
  - Total number of restraints: 50
  - Weight of restraints: 1.0 (50)
  - Potential type of restraints: square-well-parabolic (50)
  - Range of distance target values: 2.21, 2.21 (Å)
  - 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: 125, Sequence coverage: 98.4%
- Total number of restraints: 226
- Total number of restraints per polymer type: 226
- Weight of restraints: 1.0 (226)
- Potential type of restraints: square-well-parabolic (226)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords DE NOVO PROTEIN, Rossmann fold

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Found 1 Document (0.895 seconds)

BMRB: 30707

Sample

Related entities 1. De novo designed protein ROS2 835, : 1 : 7 entities Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 5 contents Detail