De novo designed Rossmann fold protein ROS2_49223
MGSSHHHHHH SSGLVPRGSH MTLFVLILSN DKKLIEEARK MAEKANLILI TVGDEEELKK AIKKADDIAK KQNSSEAKIL ILLEKPVSPE YEKKLQKYAD AEVRVRTVTS PDEAKRWIKE FSEE
Polymer type: polypeptide(L)
Total | 1H | 13C | 15N | |
---|---|---|---|---|
All | 73.5 % (1096 of 1491) | 78.0 % (610 of 782) | 65.4 % (378 of 578) | 82.4 % (108 of 131) |
Backbone | 71.5 % (526 of 736) | 83.1 % (206 of 248) | 59.2 % (218 of 368) | 85.0 % (102 of 120) |
Sidechain | 75.5 % (661 of 875) | 74.3 % (397 of 534) | 78.5 % (259 of 330) | 45.5 % (5 of 11) |
Aromatic | 15.8 % (12 of 76) | 28.9 % (11 of 38) | 0.0 % (0 of 37) | 100.0 % (1 of 1) |
Methyl | 90.0 % (126 of 140) | 90.0 % (63 of 70) | 90.0 % (63 of 70) |
1. entity 1
MGSSHHHHHH SSGLVPRGSH MTLFVLILSN DKKLIEEARK MAEKANLILI TVGDEEELKK AIKKADDIAK KQNSSEAKIL ILLEKPVSPE YEKKLQKYAD AEVRVRTVTS PDEAKRWIKE FSEESolvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.76 mM [U-99% 13C; U-99% 15N] de novo protein RO2_25, 21.1 mM potassium phosphate monobasic, 28.9 mM sodium phosphate dibasic, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | de novo protein RO2_25 | [U-99% 13C; U-99% 15N] | 0.76 mM | |
2 | potassium phosphate monobasic | natural abundance | 21.1 mM | |
3 | sodium phosphate dibasic | natural abundance | 28.9 mM |
Bruker AVANCE - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.76 mM [U-99% 13C; U-99% 15N] de novo protein RO2_25, 21.1 mM potassium phosphate monobasic, 28.9 mM sodium phosphate dibasic, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | de novo protein RO2_25 | [U-99% 13C; U-99% 15N] | 0.76 mM | |
2 | potassium phosphate monobasic | natural abundance | 21.1 mM | |
3 | sodium phosphate dibasic | natural abundance | 28.9 mM |
Bruker AVANCE - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.76 mM [U-99% 13C; U-99% 15N] de novo protein RO2_25, 21.1 mM potassium phosphate monobasic, 28.9 mM sodium phosphate dibasic, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | de novo protein RO2_25 | [U-99% 13C; U-99% 15N] | 0.76 mM | |
2 | potassium phosphate monobasic | natural abundance | 21.1 mM | |
3 | sodium phosphate dibasic | natural abundance | 28.9 mM |
Bruker DRX - 500 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.76 mM [U-99% 13C; U-99% 15N] de novo protein RO2_25, 21.1 mM potassium phosphate monobasic, 28.9 mM sodium phosphate dibasic, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | de novo protein RO2_25 | [U-99% 13C; U-99% 15N] | 0.76 mM | |
2 | potassium phosphate monobasic | natural abundance | 21.1 mM | |
3 | sodium phosphate dibasic | natural abundance | 28.9 mM |
Bruker DRX - 500 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.76 mM [U-99% 13C; U-99% 15N] de novo protein RO2_25, 21.1 mM potassium phosphate monobasic, 28.9 mM sodium phosphate dibasic, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | de novo protein RO2_25 | [U-99% 13C; U-99% 15N] | 0.76 mM | |
2 | potassium phosphate monobasic | natural abundance | 21.1 mM | |
3 | sodium phosphate dibasic | natural abundance | 28.9 mM |
Bruker AVANCE - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.76 mM [U-99% 13C; U-99% 15N] de novo protein RO2_25, 21.1 mM potassium phosphate monobasic, 28.9 mM sodium phosphate dibasic, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | de novo protein RO2_25 | [U-99% 13C; U-99% 15N] | 0.76 mM | |
2 | potassium phosphate monobasic | natural abundance | 21.1 mM | |
3 | sodium phosphate dibasic | natural abundance | 28.9 mM |
Bruker AVANCE - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.76 mM [U-99% 13C; U-99% 15N] de novo protein RO2_25, 21.1 mM potassium phosphate monobasic, 28.9 mM sodium phosphate dibasic, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | de novo protein RO2_25 | [U-99% 13C; U-99% 15N] | 0.76 mM | |
2 | potassium phosphate monobasic | natural abundance | 21.1 mM | |
3 | sodium phosphate dibasic | natural abundance | 28.9 mM |
Bruker AVANCE - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 7.0, Details 0.76 mM [U-99% 13C; U-99% 15N] de novo protein RO2_25, 21.1 mM potassium phosphate monobasic, 28.9 mM sodium phosphate dibasic, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | de novo protein RO2_25 | [U-99% 13C; U-99% 15N] | 0.76 mM | |
2 | potassium phosphate monobasic | natural abundance | 21.1 mM | |
3 | sodium phosphate dibasic | natural abundance | 28.9 mM |
Properties
Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints | combined_30706_6vg7.nef |
Input source #2: Coordindates | 6vg7.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--------60--------70--------80--------90-------100 MGSSHHHHHHSSGLVPRGSHMTLFVLILSNDKKLIEEARKMAEKANLILITVGDEEELKKAIKKADDIAKKQNSSEAKILILLEKPVSPEYEKKLQKYAD |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| MGSSHHHHHHSSGLVPRGSHMTLFVLILSNDKKLIEEARKMAEKANLILITVGDEEELKKAIKKADDIAKKQNSSEAKILILLEKPVSPEYEKKLQKYAD -------110-------120---- AEVRVRTVTSPDEAKRWIKEFSEE |||||||||||||||||||||||| AEVRVRTVTSPDEAKRWIKEFSEE
Chain assignments
Entity_assembly_ID (NMR) | Auth_asym_ID (model) | Length | Unmapped | Conflict | Sequence coverage (%) |
---|---|---|---|---|---|
A | A | 124 | 0 | 0 | 100.0 |
Content subtype: combined_30706_6vg7.nef
Assigned chemical shifts
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 MGSSHHHHHHSSGLVPRGSHMTLFVLILSNDKKLIEEARKMAEKANLILITVGDEEELKKAIKKADDIAKKQNSSEAKILILLEKPVSPEYEKKLQKYAD |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| ....................MTLFVLILSNDKKLIEEARKMAEKANLILITVGDEEELKKAIKKADDIAKKQNSSEAKILILLEKPVSPEYEKKLQKYAD -------110-------120---- AEVRVRTVTSPDEAKRWIKEFSEE |||||||||||||||||||||||| AEVRVRTVTSPDEAKRWIKEFSEE
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 782 | 607 | 77.6 |
13C chemical shifts | 578 | 366 | 63.3 |
15N chemical shifts | 131 | 106 | 80.9 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 248 | 206 | 83.1 |
13C chemical shifts | 248 | 104 | 41.9 |
15N chemical shifts | 120 | 101 | 84.2 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 534 | 401 | 75.1 |
13C chemical shifts | 330 | 262 | 79.4 |
15N chemical shifts | 11 | 5 | 45.5 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 73 | 65 | 89.0 |
13C chemical shifts | 73 | 65 | 89.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 38 | 14 | 36.8 |
13C chemical shifts | 37 | 0 | 0.0 |
15N chemical shifts | 1 | 1 | 100.0 |
Distance restraints
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 MGSSHHHHHHSSGLVPRGSHMTLFVLILSNDKKLIEEARKMAEKANLILITVGDEEELKKAIKKADDIAKKQNSSEAKILILLEKPVSPEYEKKLQKYAD |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| ....................MTLFVLILSNDKKLIEEARKMAEKANLILITVGDEEELKKAIKKADDIAKKQNSSEAKILILLEKPVSPEYEKKLQKYAD -------110-------120---- AEVRVRTVTSPDEAKRWIKEFSEE |||||||||||||||||||||||| AEVRVRTVTSPDEAKRWIKEFSEE
Dihedral angle restraints
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 MGSSHHHHHHSSGLVPRGSHMTLFVLILSNDKKLIEEARKMAEKANLILITVGDEEELKKAIKKADDIAKKQNSSEAKILILLEKPVSPEYEKKLQKYAD ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| .GSSHHHHHHSSGLVPRGSHMTLFVLILSNDKKLIEEARKMAEKANLILITVGDEEELKKAIKKADDIAKKQNSSEAKILILLEKPVSPEYEKKLQKYAD --------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 -------110-------120---- AEVRVRTVTSPDEAKRWIKEFSEE ||||||||||||||||||||||| AEVRVRTVTSPDEAKRWIKEFSE -------110-------120---