BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	88.0 % (638 of 725)	88.3 % (325 of 368)	86.8 % (250 of 288)	91.3 % (63 of 69)
Backbone	90.9 % (349 of 384)	89.5 % (119 of 133)	92.0 % (172 of 187)	90.6 % (58 of 64)
Sidechain	85.8 % (343 of 400)	87.7 % (206 of 235)	82.5 % (132 of 160)	100.0 % (5 of 5)
Aromatic	63.4 % (52 of 82)	75.6 % (31 of 41)	50.0 % (20 of 40)	100.0 % (1 of 1)
Methyl	93.9 % (62 of 66)	87.9 % (29 of 33)	100.0 % (33 of 33)

1. entity 1

MHHHHHHGMT FKLIINGKTL KGETTTEAVD AATAEKVFKQ YANDNGLDGE WTYDDATKTF TITE

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: -0.18 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: -0.18 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: -0.13 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: 0.17 ppm, Outliers: 5 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 6NJF, Strand ID: A Detail

Release date

2018-11-13

Citation

Origin of conformational dynamics in a globular protein
Damry, A.M., Mayer, M.M., Broom, A., Goto, N.K., Chica, R.A.
Commun. Biol. (2019), 2, 433-433, PubMed 31799435 , DOI 10.1038/s42003-019-0681-2 , Abstract

Related entities 1. Immunoglobulin G-binding protein G, : 1 : 105 entities Detail

Experiments performed 13 experiments Detail

1 3D 1H-15N NOESY

Instrument

Bruker AVANCE III - 600 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

2 3D 1H-13C NOESY aliphatic

Instrument

Bruker AVANCE III - 600 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

3 3D 1H-13C NOESY aromatic

Instrument

Bruker AVANCE III - 600 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

4 3D HNCACB

Instrument

Bruker AVANCE III - 600 MHz

Sample

State isotropic, 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

5 3D CBCA(CO)NH

Instrument

Bruker AVANCE III - 600 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

6 3D HNCO

Instrument

Bruker AVANCE III - 600 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

7 3D HCCH-COSY

Instrument

Bruker AVANCE III - 600 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

8 3D HCCH-TOCSY

Instrument

Bruker AVANCE III - 600 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 CCH-TOCSY

Instrument

Bruker AVANCE III - 600 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

Bruker AVANCE III - 600 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-15N HSQC

Instrument

Bruker AVANCE III - 600 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

12 3D 1H-15N TOCSY

Instrument

Bruker AVANCE III - 600 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

13 2D 1H-13C HSQC

Instrument

Bruker AVANCE III - 600 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

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30532_3.str
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

Content subtype: bmr30532_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	683		90.6 (chain: 1, length: 64)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 64, Sequence coverage: 90.6%
- Total number of assignments
  - ¹³C chemical shifts: 242
  - ¹H chemical shifts: 379
  - ¹⁵N chemical shifts: 62
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	288	242	84.0
¹H chemical shifts	368	319	86.7
¹⁵N chemical shifts	69	62	89.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	128	114	89.1
¹H chemical shifts	133	117	88.0
¹⁵N chemical shifts	64	57	89.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	160	128	80.0
¹H chemical shifts	235	202	86.0
¹⁵N chemical shifts	5	5	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	35	33	94.3
¹H chemical shifts	35	30	85.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	40	18	45.0
¹H chemical shifts	41	29	70.7
¹⁵N chemical shifts	1	1	100.0

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

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.508 seconds)

BMRB: 30532

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Immunoglobulin G-binding protein G, : 1 : 105 entities Detail

Experiments performed 13 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail