BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	86.9 % (545 of 627)	83.3 % (265 of 318)	88.3 % (219 of 248)	100.0 % (61 of 61)
Backbone	97.3 % (327 of 336)	95.7 % (111 of 116)	97.6 % (160 of 164)	100.0 % (56 of 56)
Sidechain	78.4 % (269 of 343)	76.2 % (154 of 202)	80.9 % (110 of 136)	100.0 % (5 of 5)
Aromatic	35.4 % (17 of 48)	66.7 % (16 of 24)	0.0 % (0 of 23)	100.0 % (1 of 1)
Methyl	97.1 % (68 of 70)	97.1 % (34 of 35)	97.1 % (34 of 35)

1. entity 1

MTFKLIINGK TLKGETTTEA VDAATAEKVL KQYANDNGID GEWTYDDATK TFTVTE

Show sample condition

Sample #1

Solvent system 90% H2O, 10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1.0 mM [U-98% 15N] protein (GB1), 10 mM sodium phosphate, 90% H2O, 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	protein (GB1)	[U-98% 15N]		1.0 mM
2	sodium phosphate	natural abundance		10 mM

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1.0 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
3	protein (GB1)	[U-99% 13C; U-98% 15N]		1.0 mM
4	sodium phosphate	natural abundance		10 mM

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1.0 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100% D2O

#	Name	Isotope labeling	Type	Concentration
5	protein (GB1)	[U-99% 13C; U-98% 15N]		1.0 mM
6	sodium phosphate	natural abundance		10 mM

Chem. Shift Complete2

Sequence coverage: 100.0 %, Completeness: 76.6 %, Completeness (bb): 77.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	76.6 % (960 of 1254)	77.8 % (495 of 636)	79.2 % (393 of 496)	59.0 % (72 of 122)
Backbone	77.4 % (520 of 672)	77.6 % (180 of 232)	83.8 % (275 of 328)	58.0 % (65 of 112)
Sidechain	79.0 % (542 of 686)	78.0 % (315 of 404)	80.9 % (220 of 272)	70.0 % (7 of 10)
Aromatic	35.4 % (34 of 96)	66.7 % (32 of 48)	0.0 % (0 of 46)	100.0 % (2 of 2)
Methyl	97.1 % (136 of 140)	97.1 % (68 of 70)	97.1 % (68 of 70)

1. entity 1

MTFKLIINGK TLKGETTTEA VDAATAEKVL KQYANDNGID GEWTYDDATK TFTVTE

Show sample condition

Sample #1

Solvent system 90% H2O, 10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1.0 mM [U-98% 15N] protein (GB1), 10 mM sodium phosphate, 90% H2O, 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	protein (GB1)	[U-98% 15N]		1.0 mM
2	sodium phosphate	natural abundance		10 mM

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1.0 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
3	protein (GB1)	[U-99% 13C; U-98% 15N]		1.0 mM
4	sodium phosphate	natural abundance		10 mM

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1.0 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100% D2O

#	Name	Isotope labeling	Type	Concentration
5	protein (GB1)	[U-99% 13C; U-98% 15N]		1.0 mM
6	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: -0.31 ppm, Outliers: 2 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: -0.31 ppm, Outliers: 2 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: -0.16 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 5UB0, 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: 30221 released on 2017-02-01
    Title Solution NMR Structure of NERD-S, a natively folded pentamutant of the B1 domain of streptococcal protein G (GB1) with a solvent-exposed Trp43
  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 : 3 : 102 entities Detail

Sample

#	Name	Isotope labeling	Type	Concentration
3	protein (GB1)	[U-99% 13C; U-98% 15N]		1.0 mM
4	sodium phosphate	natural abundance		10 mM

6 3D CCH-TOCSY

Instrument

Varian Inova - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1.0 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100% D2O

#	Name	Isotope labeling	Type	Concentration
5	protein (GB1)	[U-99% 13C; U-98% 15N]		1.0 mM
6	sodium phosphate	natural abundance		10 mM

7 3D HNCO

Instrument

Varian Inova - 500 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
3	protein (GB1)	[U-99% 13C; U-98% 15N]		1.0 mM
4	sodium phosphate	natural abundance		10 mM

8 3D HCCH-COSY

Instrument

Varian Inova - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1.0 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100% D2O

#	Name	Isotope labeling	Type	Concentration
5	protein (GB1)	[U-99% 13C; U-98% 15N]		1.0 mM
6	sodium phosphate	natural abundance		10 mM

9 3D HCCH-TOCSY

Instrument

Varian Inova - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1.0 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100% D2O

#	Name	Isotope labeling	Type	Concentration
5	protein (GB1)	[U-99% 13C; U-98% 15N]		1.0 mM
6	sodium phosphate	natural abundance		10 mM

10 2D 1H-13C HSQC

Instrument

Varian Inova - 500 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
3	protein (GB1)	[U-99% 13C; U-98% 15N]		1.0 mM
4	sodium phosphate	natural abundance		10 mM

11 2D 1H-13C HSQC

Instrument

Varian Inova - 500 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1.0 mM [U-99% 13C; U-98% 15N] protein (GB1), 10 mM sodium phosphate, 100% D2O

#	Name	Isotope labeling	Type	Concentration
5	protein (GB1)	[U-99% 13C; U-98% 15N]		1.0 mM
6	sodium phosphate	natural abundance		10 mM

12 2D 1H-15N HSQC

Instrument

Varian Inova - 500 MHz

Sample

State isotropic, Solvent system 90% H2O, 10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 1.0 mM [U-98% 15N] protein (GB1), 10 mM sodium phosphate, 90% H2O, 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	protein (GB1)	[U-98% 15N]		1.0 mM
2	sodium phosphate	natural abundance		10 mM

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30220_5ub0.nef
Input source #2: Coordindates	5ub0.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------
MTFKLIINGKTLKGETTTEAVDAATAEKVLKQYANDNGIDGEWTYDDATKTFTVTE
||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MTFKLIINGKTLKGETTTEAVDAATAEKVLKQYANDNGIDGEWTYDDATKTFTVTE

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_30220_5ub0.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	564		100.0 (chain: A, length: 56)
2	Assigned chemical shifts	assigned_chemical_shifts_2	Warning	383		100.0 (chain: A, length: 56)
1	Distance restraints	DYANA/DIANA_distance_constraints_3	Warning	953 (1)	noe	100.0 (chain: A, length: 56)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	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: 282
  - ¹³C chemical shifts: 221
  - 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
Saveframe: assigned_chemical_shifts_2
- 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: 217
  - ¹³C chemical shifts: 166
- 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	318	281	88.4
¹³C chemical shifts	248	221	89.1
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	111	99.1
¹⁵N chemical shifts	56	56	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	202	167	82.7
¹³C chemical shifts	136	110	80.9
¹⁵N chemical shifts	5	5	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	36	34	94.4
¹³C chemical shifts	36	34	94.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	24	16	66.7
¹³C chemical shifts	23	0	0.0
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	318	217	68.2
¹³C chemical shifts	248	166	66.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	116	59	50.9
¹³C chemical shifts	112	56	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	202	158	78.2
¹³C chemical shifts	136	110	80.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	36	34	94.4
¹³C chemical shifts	36	34	94.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	24	15	62.5
¹³C chemical shifts	23	0	0.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_3
- 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: 953
- Weight of restraints: 1.0 (953)
- Potential type of restraints: upper-bound-parabolic (953)
- Range of distance target values: 2.56, 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_2
- 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: 30220

Sample #1

Sample #2

Sample #3

Sample #1

Sample #2

Sample #3

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 : 3 : 102 entities Detail

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

Experiments performed 12 experiments Detail

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NMR combined restraints 5 contents Detail