Solution structure of lipase binding domain LID1 of foldase from Pseudomonas aeruginosa
Polymer type: polypeptide(L)
Total | 1H | 13C | 15N | |
---|---|---|---|---|
All | 83.1 % (853 of 1026) | 87.0 % (462 of 531) | 79.3 % (318 of 401) | 77.7 % (73 of 94) |
Backbone | 84.3 % (445 of 528) | 85.1 % (154 of 181) | 86.6 % (226 of 261) | 75.6 % (65 of 86) |
Sidechain | 83.3 % (484 of 581) | 88.0 % (308 of 350) | 75.3 % (168 of 223) | 100.0 % (8 of 8) |
Aromatic | 33.0 % (29 of 88) | 65.9 % (29 of 44) | 0.0 % (0 of 44) | |
Methyl | 98.0 % (98 of 100) | 96.0 % (48 of 50) | 100.0 % (50 of 50) |
1. Lipase chaperone
MGHHHHHHLP TSFRGTSVDG SFSVDASGNL LITRDIRNLF DAFLSAVGEE PLQQSLDRLR AYIAAELQEP ARGQALALMQ QYIDYKKELSolvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7.4, Details 530 uM [U-13C; U-15N] Lipase-interaction domain 1, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Lipase-interaction domain 1 | [U-13C; U-15N] | 530 uM | |
2 | Na3PO4 | natural abundance | 20 mM |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.1013291 |
Bruker AvanceIII - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7.4, Details 530 uM [U-13C; U-15N] Lipase-interaction domain 1, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Lipase-interaction domain 1 | [U-13C; U-15N] | 530 uM | |
2 | Na3PO4 | natural abundance | 20 mM |
Bruker AvanceIII - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7.4, Details 530 uM [U-13C; U-15N] Lipase-interaction domain 1, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Lipase-interaction domain 1 | [U-13C; U-15N] | 530 uM | |
2 | Na3PO4 | natural abundance | 20 mM |
Bruker AvanceIII - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7.4, Details 530 uM [U-13C; U-15N] Lipase-interaction domain 1, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Lipase-interaction domain 1 | [U-13C; U-15N] | 530 uM | |
2 | Na3PO4 | natural abundance | 20 mM |
Bruker AvanceIII - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7.4, Details 530 uM [U-13C; U-15N] Lipase-interaction domain 1, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Lipase-interaction domain 1 | [U-13C; U-15N] | 530 uM | |
2 | Na3PO4 | natural abundance | 20 mM |
Bruker AvanceIII - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7.4, Details 530 uM [U-13C; U-15N] Lipase-interaction domain 1, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Lipase-interaction domain 1 | [U-13C; U-15N] | 530 uM | |
2 | Na3PO4 | natural abundance | 20 mM |
Bruker AvanceIII - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7.4, Details 530 uM [U-13C; U-15N] Lipase-interaction domain 1, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Lipase-interaction domain 1 | [U-13C; U-15N] | 530 uM | |
2 | Na3PO4 | natural abundance | 20 mM |
Bruker AvanceIII - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7.4, Details 530 uM [U-13C; U-15N] Lipase-interaction domain 1, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Lipase-interaction domain 1 | [U-13C; U-15N] | 530 uM | |
2 | Na3PO4 | natural abundance | 20 mM |
Properties
Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints | combined_34286_6gsf.nef |
Input source #2: Coordindates | 6gsf.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
--60-------70--------80--------90-------100-------110-------120-------130-------140------ MGHHHHHHLPTSFRGTSVDGSFSVDASGNLLITRDIRNLFDAFLSAVGEEPLQQSLDRLRAYIAAELQEPARGQALALMQQYIDYKKEL ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| MGHHHHHHLPTSFRGTSVDGSFSVDASGNLLITRDIRNLFDAFLSAVGEEPLQQSLDRLRAYIAAELQEPARGQALALMQQYIDYKKEL --------10--------20--------30--------40--------50--------60--------70--------80---------
Chain assignments
Entity_assembly_ID (NMR) | Auth_asym_ID (model) | Length | Unmapped | Conflict | Sequence coverage (%) |
---|---|---|---|---|---|
A | A | 89 | 0 | 0 | 100.0 |
Content subtype: combined_34286_6gsf.nef
Assigned chemical shifts
--60-------70--------80--------90-------100-------110-------120-------130-------140------ MGHHHHHHLPTSFRGTSVDGSFSVDASGNLLITRDIRNLFDAFLSAVGEEPLQQSLDRLRAYIAAELQEPARGQALALMQQYIDYKKEL |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| .......HLPTSFRGTSVDGSFSVDASGNLLITRDIRNLFDAFLSAVGEEPLQQSLDRLRAYIAAELQEPARGQALALMQQYIDYKKEL
Comp_index_ID | Comp_ID | Atom_ID | CS value (ppm) |
---|---|---|---|
86 | ASN | CG | 174.176 |
95 | ASN | CG | 173.099 |
110 | GLN | CD | 177.619 |
111 | GLN | CD | 177.304 |
125 | GLN | CD | 178.077 |
131 | GLN | CD | 176.199 |
137 | GLN | CD | 177.314 |
138 | GLN | CD | 177.301 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 531 | 466 | 87.8 |
13C chemical shifts | 401 | 318 | 79.3 |
15N chemical shifts | 100 | 71 | 71.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 181 | 154 | 85.1 |
13C chemical shifts | 178 | 149 | 83.7 |
15N chemical shifts | 86 | 63 | 73.3 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 350 | 312 | 89.1 |
13C chemical shifts | 223 | 169 | 75.8 |
15N chemical shifts | 14 | 8 | 57.1 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 52 | 51 | 98.1 |
13C chemical shifts | 52 | 50 | 96.2 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 44 | 29 | 65.9 |
13C chemical shifts | 44 | 0 | 0.0 |
Distance restraints
--60-------70--------80--------90-------100-------110-------120-------130-------140------ MGHHHHHHLPTSFRGTSVDGSFSVDASGNLLITRDIRNLFDAFLSAVGEEPLQQSLDRLRAYIAAELQEPARGQALALMQQYIDYKKEL ||||||| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| .......HLPTSFR.TSVDGSFSVDASGNLLITRDIRNLFDAFLSAVGEEPLQQSLDRLRAYIAAELQEPARGQALALMQQYIDYKKEL
Dihedral angle restraints
--60-------70--------80--------90-------100-------110-------120-------130-------140------ MGHHHHHHLPTSFRGTSVDGSFSVDASGNLLITRDIRNLFDAFLSAVGEEPLQQSLDRLRAYIAAELQEPARGQALALMQQYIDYKKEL ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| ......HHLPTSFRGTSVDGSFSVDASGNLLITRDIRNLFDAFLSAVGEEPLQQSLDRLRAYIAAELQEPARGQALALMQQYIDYKKEL