BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	88.5 % (571 of 645)	83.5 % (274 of 328)	92.2 % (236 of 256)	100.0 % (61 of 61)
Backbone	96.7 % (325 of 336)	95.7 % (111 of 116)	96.3 % (158 of 164)	100.0 % (56 of 56)
Sidechain	82.3 % (297 of 361)	76.9 % (163 of 212)	89.6 % (129 of 144)	100.0 % (5 of 5)
Aromatic	64.7 % (44 of 68)	64.7 % (22 of 34)	63.6 % (21 of 33)	100.0 % (1 of 1)
Methyl	95.3 % (61 of 64)	93.8 % (30 of 32)	96.9 % (31 of 32)

1. entity 1

MTFKLIINGK TLKGETTTEA VDAATAEKVF KQYFNDNGID GEWTYDDATK TFTITE

Show sample condition

Sample #1

Solvent system 90% H2O, 10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100 uM EDTA, 0.02 % sodium azide, 90% H2O, 10% D2O

#	Name	Isotope labeling	Concentration
1	EDTA	natural abundance	100 uM
2	protein (GB1)	[U-98% 15N]	1 mM
3	sodium azide	natural abundance	0.02 %
4	sodium phosphate	natural abundance	10 mM

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100 uM EDTA, 0.02 % sodium azide, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
5	EDTA	natural abundance	100 uM
6	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
7	sodium azide	natural abundance	0.02 %
8	sodium phosphate	natural abundance	10 mM

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100 uM EDTA, 0.02 % sodium azide, 100% D2O

#	Name	Isotope labeling	Concentration
9	EDTA	natural abundance	100 uM
10	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
11	sodium azide	natural abundance	0.02 %
12	sodium phosphate	natural abundance	10 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.3 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.3 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.18 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 0.09 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 5UBS, Strand ID: A Detail

Release date

2017-02-01

Citation

Rational design of proteins that exchange on functional timescales
Davey, J.A., Damry, A.M., Goto, N.K., Chica, R.A.
Nat. Chem. Biol. (2017), 13, 1280-1285, PubMed 29058725 , DOI 10.1038/nchembio.2503 , Abstract

Entries sharing articles BMRB: 5 entries Detail

  BMRB: 27030 released on 2017-02-09
    Title Chemical shift assignments of DANCER-0, a dynamic pentamutant of the B1 domain of streptococcal protein G (GB1)
  BMRB: 27031 released on 2017-02-09
    Title Chemical shift assignment of DANCER-1, a natively folded and dynamic hexamutant of the B1 domain of streptococcal protein G (GB1)
  BMRB: 27032 released on 2017-02-09
    Title Chemical shift assignment of DANCER-3, a natively folded and dynamic pentamutant of the B1 domain of streptococcal protein G (GB1)
  BMRB: 30220 released on 2017-02-01
    Title Solution NMR Structure of NERD-C, a natively folded tetramutant of the B1 domain of streptococcal protein G (GB1)
  BMRB: 30223 released on 2017-02-01
    Title Solution NMR-derived model of the minor species of DANCER-2, a dynamic and natively folded pentamutant of the B1 domain of streptococcal protein G (GB1)

Related entities 1. Immunoglobulin G-binding protein G, : 1 : 104 entities Detail

Interaction partners 1. Immunoglobulin G-binding protein G, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 13 experiments Detail

1 3D 1H-15N NOESY

Instrument

Varian Inova - 500 MHz

Sample

State isotropic, Solvent system 90% H2O, 10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100 uM EDTA, 0.02 % sodium azide, 90% H2O, 10% D2O

#	Name	Isotope labeling	Concentration
1	EDTA	natural abundance	100 uM
2	protein (GB1)	[U-98% 15N]	1 mM
3	sodium azide	natural abundance	0.02 %
4	sodium phosphate	natural abundance	10 mM

2 3D 1H-13C NOESY aliphatic

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100 uM EDTA, 0.02 % sodium azide, 100% D2O

#	Name	Isotope labeling	Concentration
9	EDTA	natural abundance	100 uM
10	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
11	sodium azide	natural abundance	0.02 %
12	sodium phosphate	natural abundance	10 mM

3 3D 1H-13C NOESY aromatic

Instrument

Bruker AVANCE III HD - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
9	EDTA	natural abundance	100 uM
10	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
11	sodium azide	natural abundance	0.02 %
12	sodium phosphate	natural abundance	10 mM

4 3D HNCACB

Instrument

Varian Inova - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100 uM EDTA, 0.02 % sodium azide, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
5	EDTA	natural abundance	100 uM
6	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
7	sodium azide	natural abundance	0.02 %
8	sodium phosphate	natural abundance	10 mM

5 3D HNCO

Instrument

Varian Inova - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
5	EDTA	natural abundance	100 uM
6	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
7	sodium azide	natural abundance	0.02 %
8	sodium phosphate	natural abundance	10 mM

6 2D 1H-13C HSQC

Instrument

Varian Inova - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
9	EDTA	natural abundance	100 uM
10	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
11	sodium azide	natural abundance	0.02 %
12	sodium phosphate	natural abundance	10 mM

7 2D 1H-13C HSQC

Instrument

Varian Inova - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
5	EDTA	natural abundance	100 uM
6	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
7	sodium azide	natural abundance	0.02 %
8	sodium phosphate	natural abundance	10 mM

8 2D 1H-15N HSQC

Instrument

Varian Inova - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	EDTA	natural abundance	100 uM
2	protein (GB1)	[U-98% 15N]	1 mM
3	sodium azide	natural abundance	0.02 %
4	sodium phosphate	natural abundance	10 mM

9 3D 1H-15N TOCSY

Instrument

Varian Inova - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	EDTA	natural abundance	100 uM
2	protein (GB1)	[U-98% 15N]	1 mM
3	sodium azide	natural abundance	0.02 %
4	sodium phosphate	natural abundance	10 mM

10 3D HCCH-COSY

Instrument

Varian Inova - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
9	EDTA	natural abundance	100 uM
10	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
11	sodium azide	natural abundance	0.02 %
12	sodium phosphate	natural abundance	10 mM

11 3D HCCH-TOCSY

Instrument

Varian Inova - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
9	EDTA	natural abundance	100 uM
10	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
11	sodium azide	natural abundance	0.02 %
12	sodium phosphate	natural abundance	10 mM

12 3D CCH-TOCSY

Instrument

Varian Inova - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
9	EDTA	natural abundance	100 uM
10	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
11	sodium azide	natural abundance	0.02 %
12	sodium phosphate	natural abundance	10 mM

13 3D CBCA(CO)NH

Instrument

Varian Inova - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
5	EDTA	natural abundance	100 uM
6	protein (GB1)	[U-99% 13C; U-98% 15N]	1 mM
7	sodium azide	natural abundance	0.02 %
8	sodium phosphate	natural abundance	10 mM

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30221_5ubs.nef
Input source #2: Coordindates	5ubs.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------
MTFKLIINGKTLKGETTTEAVDAATAEKVFKQYFNDNGIDGEWTYDDATKTFTITE
||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MTFKLIINGKTLKGETTTEAVDAATAEKVFKQYFNDNGIDGEWTYDDATKTFTITE

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	56	0	0	100.0

Content subtype: combined_30221_5ubs.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	581		100.0 (chain: A, length: 56)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	710 (1)	noe	100.0 (chain: A, length: 56)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	90 (90)	.	98.2 (chain: A, length: 56)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 56, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 280
  - ¹³C chemical shifts: 240
  - ¹⁵N chemical shifts: 61
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	328	279	85.1
¹³C chemical shifts	256	240	93.8
¹⁵N chemical shifts	61	61	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	116	114	98.3
¹³C chemical shifts	112	110	98.2
¹⁵N chemical shifts	56	56	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	212	165	77.8
¹³C chemical shifts	144	130	90.3
¹⁵N chemical shifts	5	5	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	33	31	93.9
¹³C chemical shifts	33	31	93.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	34	22	64.7
¹³C chemical shifts	33	21	63.6
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 56, Sequence coverage: 100.0%
- Total number of restraints: 710
- Weight of restraints: 1.0 (710)
- Potential type of restraints: upper-bound-parabolic (710)
- Range of distance target values: 2.78, 5.5 (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

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 56, Sequence coverage: 98.2%
- Total number of restraints: 90
- Total number of restraints per polymer type: 90
- Weight of restraints: 1.0 (90)
- Potential type of restraints: square-well-parabolic (90)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords DE NOVO PROTEIN, computational design, conformational exchange, dynamics, immunoglobulin-binding

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BMRB: 30221

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 5 entries Detail

Related entities 1. Immunoglobulin G-binding protein G, : 1 : 104 entities Detail

Interaction partners 1. Immunoglobulin G-binding protein G, : 1 interactors Detail

Experiments performed 13 experiments Detail

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NMR combined restraints 4 contents Detail