BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	73.5 % (1096 of 1491)	78.0 % (610 of 782)	65.4 % (378 of 578)	82.4 % (108 of 131)
Backbone	71.5 % (526 of 736)	83.1 % (206 of 248)	59.2 % (218 of 368)	85.0 % (102 of 120)
Sidechain	75.5 % (661 of 875)	74.3 % (397 of 534)	78.5 % (259 of 330)	45.5 % (5 of 11)
Aromatic	15.8 % (12 of 76)	28.9 % (11 of 38)	0.0 % (0 of 37)	100.0 % (1 of 1)
Methyl	90.0 % (126 of 140)	90.0 % (63 of 70)	90.0 % (63 of 70)

1. entity 1

MGSSHHHHHH SSGLVPRGSH MTLFVLILSN DKKLIEEARK MAEKANLILI TVGDEEELKK AIKKADDIAK KQNSSEAKIL ILLEKPVSPE YEKKLQKYAD AEVRVRTVTS PDEAKRWIKE FSEE

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.76 mM [U-99% 13C; U-99% 15N] de novo protein RO2_25, 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_25	[U-99% 13C; U-99% 15N]	0.76 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: 6VG7, 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 49223, : 1 : 24 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 0.76 mM [U-99% 13C; U-99% 15N] de novo protein RO2_25, 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_25	[U-99% 13C; U-99% 15N]	0.76 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_25	[U-99% 13C; U-99% 15N]	0.76 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_25	[U-99% 13C; U-99% 15N]	0.76 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_25	[U-99% 13C; U-99% 15N]	0.76 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_25	[U-99% 13C; U-99% 15N]	0.76 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_25	[U-99% 13C; U-99% 15N]	0.76 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_25	[U-99% 13C; U-99% 15N]	0.76 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_30706_6vg7.nef
Input source #2: Coordindates	6vg7.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
MGSSHHHHHHSSGLVPRGSHMTLFVLILSNDKKLIEEARKMAEKANLILITVGDEEELKKAIKKADDIAKKQNSSEAKILILLEKPVSPEYEKKLQKYAD
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MGSSHHHHHHSSGLVPRGSHMTLFVLILSNDKKLIEEARKMAEKANLILITVGDEEELKKAIKKADDIAKKQNSSEAKILILLEKPVSPEYEKKLQKYAD

-------110-------120----
AEVRVRTVTSPDEAKRWIKEFSEE
||||||||||||||||||||||||
AEVRVRTVTSPDEAKRWIKEFSEE

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	124	0	0	100.0

Content subtype: combined_30706_6vg7.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1079		83.9 (chain: A, length: 124)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	3803 (1)	noe	83.9 (chain: A, length: 124)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	36 (1)	hbond	41.9 (chain: A, length: 124)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	230 (230)	.	98.4 (chain: A, length: 124)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 124, Sequence coverage: 83.9%
- Total number of assignments
  - ¹H chemical shifts: 607
  - ¹³C chemical shifts: 366
  - ¹⁵N chemical shifts: 106
- 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	607	77.6
¹³C chemical shifts	578	366	63.3
¹⁵N chemical shifts	131	106	80.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	248	206	83.1
¹³C chemical shifts	248	104	41.9
¹⁵N chemical shifts	120	101	84.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	534	401	75.1
¹³C chemical shifts	330	262	79.4
¹⁵N chemical shifts	11	5	45.5

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	14	36.8
¹³C chemical shifts	37	0	0.0
¹⁵N chemical shifts	1	1	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: 124, Sequence coverage: 83.9%
- Total number of restraints: 3803
- Weight of restraints: 1.0 (3803)
- Potential type of restraints: square-well-parabolic (3803)
- Range of distance target values: 2.44, 6.0 (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: 124, Sequence coverage: 41.9%
  - Total number of restraints: 36
  - Weight of restraints: 1.0 (36)
  - Potential type of restraints: square-well-parabolic (36)
  - 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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 124, Sequence coverage: 98.4%
- Total number of restraints: 230
- Total number of restraints per polymer type: 230
- Weight of restraints: 1.0 (230)
- Potential type of restraints: square-well-parabolic (230)
- 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 (0.509 seconds)

BMRB: 30706

Sample

Related entities 1. De novo designed protein ROS2 49223, : 1 : 24 entities Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 5 contents Detail