1H, 13C, and 15N Chemical Shift Assignments for in vitro GB1
Polymer type: polypeptide(L)
Total | 1H | 13C | 15N | |
---|---|---|---|---|
All | 99.4 % (628 of 632) | 98.8 % (316 of 320) | 100.0 % (250 of 250) | 100.0 % (62 of 62) |
Backbone | 99.4 % (340 of 342) | 98.3 % (117 of 119) | 100.0 % (166 of 166) | 100.0 % (57 of 57) |
Sidechain | 99.4 % (340 of 342) | 99.0 % (199 of 201) | 100.0 % (136 of 136) | 100.0 % (5 of 5) |
Aromatic | 96.4 % (54 of 56) | 92.9 % (26 of 28) | 100.0 % (27 of 27) | 100.0 % (1 of 1) |
Methyl | 100.0 % (66 of 66) | 100.0 % (33 of 33) | 100.0 % (33 of 33) |
1. entity
MGTYKLILNG KTLKGETTTE AVDAATAEKV FKQYANDNGV DGEWTYDDAT KTFTVTESolvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | Protein G B1 | carbons | 0.0 ppm | internal | direct | 0.252 |
1H | Protein G B1 | protons | 0.0 ppm | internal | direct | 1.0 |
15N | Protein G B1 | nitrogen | 0.0 ppm | internal | direct | 0.101 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | Protein G B1 | carbons | 0.0 ppm | internal | direct | 0.252 |
1H | Protein G B1 | protons | 0.0 ppm | internal | direct | 1.0 |
15N | Protein G B1 | nitrogen | 0.0 ppm | internal | direct | 0.101 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | Protein G B1 | carbons | 0.0 ppm | internal | direct | 0.252 |
1H | Protein G B1 | protons | 0.0 ppm | internal | direct | 1.0 |
15N | Protein G B1 | nitrogen | 0.0 ppm | internal | direct | 0.101 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | Protein G B1 | carbons | 0.0 ppm | internal | direct | 0.252 |
1H | Protein G B1 | protons | 0.0 ppm | internal | direct | 1.0 |
15N | Protein G B1 | nitrogen | 0.0 ppm | internal | direct | 0.101 |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 295 K, pH 7.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Protein G B1 | [U-100% 13C; U-100% 15N] | 1 mM | |
2 | H2O | natural abundance | 90 % | |
3 | D2O | natural abundance | 10 % |
Properties
Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints | combined_25909_2n9k.nef |
Input source #2: Coordindates | 2n9k.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
NoneOther bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)
NoneNon-standard residues
NoneSequence alignments
--------10--------20--------30--------40--------50------- MGTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE ||||||||||||||||||||||||||||||||||||||||||||||||||||||||| MGTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE
Chain assignments
Entity_assembly_ID (NMR) | Auth_asym_ID (model) | Length | Unmapped | Conflict | Sequence coverage (%) |
---|---|---|---|---|---|
A | A | 57 | 0 | 0 | 100.0 |
Content subtype: combined_25909_2n9k.nef
Assigned chemical shifts
--------10--------20--------30--------40--------50------- MGTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE ||||||||||||||||||||||||||||||||||||||||||||||||||||||||| MGTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE
Comp_index_ID | Comp_ID | Atom_ID | CS value (ppm) |
---|---|---|---|
44 | TRP | CE2 | 151.51 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 320 | 316 | 98.8 |
13C chemical shifts | 250 | 250 | 100.0 |
15N chemical shifts | 62 | 62 | 100.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 119 | 117 | 98.3 |
13C chemical shifts | 114 | 114 | 100.0 |
15N chemical shifts | 57 | 57 | 100.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 201 | 199 | 99.0 |
13C chemical shifts | 136 | 136 | 100.0 |
15N chemical shifts | 5 | 5 | 100.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 34 | 34 | 100.0 |
13C chemical shifts | 34 | 34 | 100.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 28 | 26 | 92.9 |
13C chemical shifts | 27 | 27 | 100.0 |
15N chemical shifts | 1 | 1 | 100.0 |
Distance restraints
--------10--------20--------30--------40--------50------- MGTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE ||||||||||||||||||||||||||||||||||||||||||||||||||||||||| MGTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE
Dihedral angle restraints
--------10--------20--------30--------40--------50------- MGTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE |||||||||||||||||||||||||||||||||||||||||||||||||||||||| .GTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE