The NMR structure of protein-glutaminase from Chryseobacterium proteolyticum
LASVIPDVAT LNSLFNQIKN QSCGTSTASS PCITFRYPVD GCYARAHKMR QILMNNGYDC EKQFVYGNLK ASTGTCCVAW SYHVAILVSY KNASGVTEKR IIDPSLFSSG PVTDTAWRNA CVNTSCGSAS VSSYANTAGN VYYRSPSNSY LYDNNLINTN CVLTKFSLLS GCSPSPAPDV SSCGF
Polymer type: polypeptide(L)
Total | 1H | 13C | 15N | |
---|---|---|---|---|
All | 97.8 % (1982 of 2027) | 97.8 % (1012 of 1035) | 97.6 % (775 of 794) | 98.5 % (195 of 198) |
Backbone | 97.8 % (1068 of 1092) | 97.6 % (363 of 372) | 97.6 % (531 of 544) | 98.9 % (174 of 176) |
Sidechain | 98.1 % (1088 of 1109) | 97.9 % (649 of 663) | 98.6 % (418 of 424) | 95.5 % (21 of 22) |
Aromatic | 91.7 % (165 of 180) | 90.0 % (81 of 90) | 93.2 % (82 of 88) | 100.0 % (2 of 2) |
Methyl | 99.5 % (191 of 192) | 99.0 % (95 of 96) | 100.0 % (96 of 96) |
1. protein-glutaminase
LASVIPDVAT LNSLFNQIKN QSCGTSTASS PCITFRYPVD GCYARAHKMR QILMNNGYDC EKQFVYGNLK ASTGTCCVAW SYHVAILVSY KNASGVTEKR IIDPSLFSSG PVTDTAWRNA CVNTSCGSAS VSSYANTAGN VYYRSPSNSY LYDNNLINTN CVLTKFSLLS GCSPSPAPDV SSCGFSolvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | na | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | na | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | na | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | na | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | na | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | na | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | na | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | na | indirect | 0.1013291 |
Varian INOVA - 800 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 800 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 800 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 800 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 600 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 600 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 600 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 600 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 600 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 600 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 600 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 600 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 800 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 800 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Varian INOVA - 800 MHz
State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | protein glutaminase | [U-13C; U-15N] | 1.15 mM | |
2 | D2O | natural abundance | 5 % | |
3 | H2O | natural abundance | 95 % |
Properties
Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints | combined_16675_2ksv.nef |
Input source #2: Coordindates | 2ksv.cif |
Diamagnetism of the molecular assembly | True (excluding Oxygen atoms) |
Whether the assembly has a disulfide bond | True (see coordinates for details) |
Whether the assembly has a other bond | None |
Whether the assembly contains a cyclic polymer | None |
Overall data processing status | Warning |
Disulfide bonds
Ptnr_site_1 | Ptnr_site_2 | Redox_state_prediction_1 | Redox_state_prediction_2 | Distance (Ã…) |
---|---|---|---|---|
A:158:CYS:SG | A:167:CYS:SG | oxidized, CA 55.619, CB 38.825 ppm | oxidized, CA 53.737, CB 42.466 ppm | 2.076 |
A:211:CYS:SG | A:307:CYS:SG | oxidized, CA 54.344, CB 44.527 ppm | oxidized, CA 57.5, CB 43.933 ppm | 1.995 |
A:212:CYS:SG | A:261:CYS:SG | oxidized, CA 56.568, CB 46.13 ppm | oxidized, CA 53.909, CB 40.77 ppm | 2.109 |
A:296:CYS:SG | A:318:CYS:SG | oxidized, CA 59.841, CB 38.37 ppm | oxidized, CA 54.33, CB 38.241 ppm | 2.051 |
Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)
NoneNon-standard residues
NoneSequence alignments
--140-------150-------160-------170-------180-------190-------200-------210-------220-------230----- LASVIPDVATLNSLFNQIKNQSCGTSTASSPCITFRYPVDGCYARAHKMRQILMNNGYDCEKQFVYGNLKASTGTCCVAWSYHVAILVSYKNASGVTEKR |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| LASVIPDVATLNSLFNQIKNQSCGTSTASSPCITFRYPVDGCYARAHKMRQILMNNGYDCEKQFVYGNLKASTGTCCVAWSYHVAILVSYKNASGVTEKR --------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 --240-------250-------260-------270-------280-------290-------300-------310-------320 IIDPSLFSSGPVTDTAWRNACVNTSCGSASVSSYANTAGNVYYRSPSNSYLYDNNLINTNCVLTKFSLLSGCSPSPAPDVSSCGF ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| IIDPSLFSSGPVTDTAWRNACVNTSCGSASVSSYANTAGNVYYRSPSNSYLYDNNLINTNCVLTKFSLLSGCSPSPAPDVSSCGF -------110-------120-------130-------140-------150-------160-------170-------180-----
Chain assignments
Entity_assembly_ID (NMR) | Auth_asym_ID (model) | Length | Unmapped | Conflict | Sequence coverage (%) |
---|---|---|---|---|---|
A | A | 185 | 0 | 0 | 100.0 |
Content subtype: combined_16675_2ksv.nef
Assigned chemical shifts
--140-------150-------160-------170-------180-------190-------200-------210-------220-------230----- LASVIPDVATLNSLFNQIKNQSCGTSTASSPCITFRYPVDGCYARAHKMRQILMNNGYDCEKQFVYGNLKASTGTCCVAWSYHVAILVSYKNASGVTEKR |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| LASVIPDVATLNSLFNQIKNQSCGTSTASSPCITFRYPVDGCYARAHKMRQILMNNGYDCEKQFVYGNLKASTGTCCVAWSYHVAILVSYKNASGVTEKR --240-------250-------260-------270-------280-------290-------300-------310-------320 IIDPSLFSSGPVTDTAWRNACVNTSCGSASVSSYANTAGNVYYRSPSNSYLYDNNLINTNCVLTKFSLLSGCSPSPAPDVSSCGF ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| IIDPSLFSSGPVTDTAWRNACVNTSCGSASVSSYANTAGNVYYRSPSNSYLYDNNLINTNCVLTKFSLLSGCSPSPAPDVSSCGF
Comp_index_ID | Comp_ID | Atom_ID | CS value (ppm) |
---|---|---|---|
147 | ASN | CG | 175.312 |
151 | ASN | CG | 176.293 |
152 | GLN | CD | 179.987 |
155 | ASN | CG | 175.84 |
156 | GLN | CD | 179.816 |
157 | SER | HG | 6.725 |
162 | THR | HG1 | 6.19 |
169 | THR | HG1 | 6.35 |
171 | ARG | HH11 | 6.747 |
171 | ARG | HH12 | 6.747 |
171 | ARG | HH21 | 7.147 |
171 | ARG | HH22 | 7.147 |
171 | ARG | CZ | 158.581 |
171 | ARG | NH1 | 67.855 |
171 | ARG | NH2 | 73.309 |
180 | ARG | HH11 | 7.308 |
180 | ARG | HH12 | 7.308 |
180 | ARG | CZ | 160.64 |
182 | HIS | HD1 | 8.957 |
182 | HIS | HE2 | 10.747 |
182 | HIS | NE2 | 164.497 |
185 | ARG | HH11 | 6.65 |
185 | ARG | HH12 | 6.65 |
185 | ARG | HH21 | 6.948 |
185 | ARG | HH22 | 6.948 |
186 | GLN | CD | 179.512 |
190 | ASN | CG | 176.097 |
195 | CYS | HG | 2.086 |
197 | LYS | HZ1 | 8.937 |
197 | LYS | HZ2 | 8.937 |
197 | LYS | HZ3 | 8.937 |
197 | LYS | NZ | 35.904 |
198 | GLN | CD | 179.642 |
203 | ASN | CG | 177.35 |
218 | HIS | HD1 | 12.72 |
227 | ASN | CG | 176.524 |
253 | ARG | HH11 | 6.389 |
253 | ARG | HH12 | 6.389 |
253 | ARG | HH21 | 6.814 |
253 | ARG | HH22 | 6.814 |
253 | ARG | CZ | 157.966 |
253 | ARG | NH1 | 69.404 |
254 | ASN | CG | 176.275 |
256 | CYS | HG | 2.222 |
258 | ASN | CG | 177.84 |
271 | ASN | CG | 174.37 |
272 | THR | HG1 | 4.069 |
275 | ASN | CG | 176.328 |
279 | ARG | HH11 | 6.295 |
279 | ARG | HH12 | 6.295 |
279 | ARG | CZ | 158.929 |
279 | ARG | NH1 | 70.142 |
283 | ASN | CG | 177.968 |
289 | ASN | CG | 176.806 |
290 | ASN | CG | 177.576 |
293 | ASN | CG | 178.447 |
294 | THR | HG1 | 6.354 |
295 | ASN | CG | 175.299 |
299 | THR | HG1 | 5.396 |
302 | SER | HG | 5.343 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 1035 | 1020 | 98.6 |
13C chemical shifts | 794 | 774 | 97.5 |
15N chemical shifts | 204 | 199 | 97.5 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 372 | 369 | 99.2 |
13C chemical shifts | 370 | 357 | 96.5 |
15N chemical shifts | 176 | 173 | 98.3 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 663 | 651 | 98.2 |
13C chemical shifts | 424 | 417 | 98.3 |
15N chemical shifts | 28 | 26 | 92.9 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 98 | 98 | 100.0 |
13C chemical shifts | 98 | 98 | 100.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 90 | 81 | 90.0 |
13C chemical shifts | 88 | 82 | 93.2 |
15N chemical shifts | 2 | 2 | 100.0 |
Covalent bonds
Distance restraints
--140-------150-------160-------170-------180-------190-------200-------210-------220-------230----- LASVIPDVATLNSLFNQIKNQSCGTSTASSPCITFRYPVDGCYARAHKMRQILMNNGYDCEKQFVYGNLKASTGTCCVAWSYHVAILVSYKNASGVTEKR |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| LASVIPDVATLNSLFNQIKNQSCGTSTASSPCITFRYPVDGCYARAHKMRQILMNNGYDCEKQFVYGNLKASTGTCCVAWSYHVAILVSYKNASGVTEKR --240-------250-------260-------270-------280-------290-------300-------310-------320 IIDPSLFSSGPVTDTAWRNACVNTSCGSASVSSYANTAGNVYYRSPSNSYLYDNNLINTNCVLTKFSLLSGCSPSPAPDVSSCGF ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| IIDPSLFSSGPVTDTAWRNACVNTSCGSASVSSYANTAGNVYYRSPSNSYLYDNNLINTNCVLTKFSLLSGCSPSPAPDVSSCGF
Dihedral angle restraints
--140-------150-------160-------170-------180-------190-------200-------210-------220-------230----- LASVIPDVATLNSLFNQIKNQSCGTSTASSPCITFRYPVDGCYARAHKMRQILMNNGYDCEKQFVYGNLKASTGTCCVAWSYHVAILVSYKNASGVTEKR ||||||||||||||||||||||||||||||||||||| ||||||||||||||||||||||||| ||||| |||||||||||||||||||||||||| ..SVIPDVATLNSLFNQIKNQSCGTSTASSPCITFRYPV...YARAHKMRQILMNNGYDCEKQFVYG.LKAST.TCCVAWSYHVAILVSYKNASGVTEKR --140-------150-------160-------170-------180-------190-------200-------210-------220-------230----- --240-------250-------260-------270-------280-------290-------300-------310-------320 IIDPSLFSSGPVTDTAWRNACVNTSCGSASVSSYANTAGNVYYRSPSNSYLYDNNLINTNCVLTKFSLLSGCSPSPAPDVSSCGF ||||||||| ||||||||||||||| |||||||||| |||||||| ||||||||||||||||||||| |||||||| ||| IIDPSLFSS.PVTDTAWRNACVNTS...ASVSSYANTA.NVYYRSPS.SYLYDNNLINTNCVLTKFSLL.GCSPSPAP.VSS --240-------250-------260-------270-------280-------290-------300-------310-------