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- PDB-9hde: Crystal structure of methionine gamma-lyase (K209Q variant) from ... -

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Basic information

Entry
Database: PDB / ID: 9hde
TitleCrystal structure of methionine gamma-lyase (K209Q variant) from Brevibacterium aurantiacum in complex with PLP and alpha-ketobutyrate
ComponentsCystathionine gamma-synthase
KeywordsLYASE / Complex / inhibitor / methionine / PLP
Function / homology
Function and homology information


homocysteine desulfhydrase / methionine gamma-lyase / methionine gamma-lyase activity / cystathionine gamma-lyase activity / cysteine biosynthetic process via cystathionine / transsulfuration / pyridoxal phosphate binding / cytoplasm
Similarity search - Function
Cys/Met metabolism, pyridoxal phosphate-dependent enzyme / Cys/Met metabolism PLP-dependent enzyme / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase
Similarity search - Domain/homology
Chem-4LM / DI(HYDROXYETHYL)ETHER / L-methionine gamma-lyase
Similarity search - Component
Biological speciesBrevibacterium aurantiacum (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.522 Å
AuthorsKopecny, D. / Ferchaud, N. / Briozzo, P.
Funding support Czech Republic, France, 4items
OrganizationGrant numberCountry
Ministry of Education, Youth and Sports of the Czech RepublicMOBILITY 8J23FR011 Czech Republic
Other governmentFR 49271QH PHC BARRANDE
Agence Nationale de la Recherche (ANR)France 2023 ANR-11-IDEX-0003, Jean d'Alembert fellowship at Paris-Saclay France
Other privateIMEBATRACA
CitationJournal: To Be Published
Title: Functional and structural characterization of methionine gamma-lyases from Brevibacterium bacteria: insights into cofactor retention
Authors: Ferchaud, N. / Boyer, A. / Odegard, B. / Hentati, S. / Simonson, T. / Machover, D. / Kopecny, D. / Briozzo, P.
History
DepositionNov 12, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 22, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Cystathionine gamma-synthase
B: Cystathionine gamma-synthase
C: Cystathionine gamma-synthase
D: Cystathionine gamma-synthase
E: Cystathionine gamma-synthase
F: Cystathionine gamma-synthase
G: Cystathionine gamma-synthase
H: Cystathionine gamma-synthase
I: Cystathionine gamma-synthase
J: Cystathionine gamma-synthase
K: Cystathionine gamma-synthase
L: Cystathionine gamma-synthase
M: Cystathionine gamma-synthase
N: Cystathionine gamma-synthase
O: Cystathionine gamma-synthase
P: Cystathionine gamma-synthase
Q: Cystathionine gamma-synthase
R: Cystathionine gamma-synthase
S: Cystathionine gamma-synthase
T: Cystathionine gamma-synthase
U: Cystathionine gamma-synthase
V: Cystathionine gamma-synthase
W: Cystathionine gamma-synthase
X: Cystathionine gamma-synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,037,77670
Polymers1,027,66624
Non-polymers10,10946
Water7,746430
1
A: Cystathionine gamma-synthase
B: Cystathionine gamma-synthase
C: Cystathionine gamma-synthase
D: Cystathionine gamma-synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)173,59918
Polymers171,2784
Non-polymers2,32214
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area20900 Å2
ΔGint-187 kcal/mol
Surface area43820 Å2
MethodPISA
2
E: Cystathionine gamma-synthase
F: Cystathionine gamma-synthase
G: Cystathionine gamma-synthase
H: Cystathionine gamma-synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)172,89711
Polymers171,2784
Non-polymers1,6197
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19610 Å2
ΔGint-151 kcal/mol
Surface area43860 Å2
MethodPISA
3
I: Cystathionine gamma-synthase
J: Cystathionine gamma-synthase
K: Cystathionine gamma-synthase
L: Cystathionine gamma-synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)172,79110
Polymers171,2784
Non-polymers1,5136
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19250 Å2
ΔGint-151 kcal/mol
Surface area44080 Å2
MethodPISA
4
M: Cystathionine gamma-synthase
N: Cystathionine gamma-synthase
O: Cystathionine gamma-synthase
P: Cystathionine gamma-synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)173,08913
Polymers171,2784
Non-polymers1,8119
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19920 Å2
ΔGint-173 kcal/mol
Surface area44140 Å2
MethodPISA
5
Q: Cystathionine gamma-synthase
R: Cystathionine gamma-synthase
S: Cystathionine gamma-synthase
T: Cystathionine gamma-synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)172,5998
Polymers171,2784
Non-polymers1,3214
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19210 Å2
ΔGint-131 kcal/mol
Surface area43740 Å2
MethodPISA
6
U: Cystathionine gamma-synthase
V: Cystathionine gamma-synthase
W: Cystathionine gamma-synthase
X: Cystathionine gamma-synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)172,80110
Polymers171,2784
Non-polymers1,5236
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19400 Å2
ΔGint-144 kcal/mol
Surface area43800 Å2
MethodPISA
Unit cell
Length a, b, c (Å)133.328, 155.89, 232.079
Angle α, β, γ (deg.)90, 90.24, 90
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein ...
Cystathionine gamma-synthase / Methionine gamma-lyase (MGL)


Mass: 42819.430 Da / Num. of mol.: 24
Source method: isolated from a genetically manipulated source
Details: N-terminal His-tag, mutation K209Q / Source: (gene. exp.) Brevibacterium aurantiacum (bacteria)
Gene: BAUR9175_03070, BAUR920_03040, BAURA63_02933, BAURA86_00394
Production host: Escherichia coli (E. coli) / Strain (production host): T7 express / References: UniProt: A0A2H1K3G9, methionine gamma-lyase
#2: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C4H10O3
#3: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 15 / Source method: obtained synthetically / Formula: SO4
#4: Chemical...
ChemComp-4LM / (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid


Mass: 330.230 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: C12H15N2O7P / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 430 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.48 Å3/Da / Density % sol: 47.59 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: Well solution 0.1 M Tris-HCl, pH 8.5, 0.1 M Lithium sulfate, 32% PEG4000, 1 mM PLP, 20 mM Methionine, Cryoprotection: 10% PEG400

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 2 / Wavelength: 0.98399 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Mar 29, 2023
Details: a convex prefocussing mirror and a Kirkpatrick-Baez pair of focussing mirrors
RadiationMonochromator: Cryogenically cooled channel cut crystal monochromator
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98399 Å / Relative weight: 1
ReflectionResolution: 2.522→232.077 Å / Num. obs: 214191 / % possible obs: 93.6 % / Redundancy: 6.32 %
Details: Some remarks regarding the mmCIF items written, the PDB Exchange Dictionary (PDBx/mmCIF) Version 5.0 supporting the data files in the current PDB archive (dictionary version 5.325, last ...Details: Some remarks regarding the mmCIF items written, the PDB Exchange Dictionary (PDBx/mmCIF) Version 5.0 supporting the data files in the current PDB archive (dictionary version 5.325, last updated 2020-04-13: http://mmcif.wwpdb.org/dictionaries/mmcif_pdbx_v50.dic/Index/) and the actual quantities provided by MRFANA (https://github.com/githubgphl/MRFANA) from the autoPROC package (https://www.globalphasing.com/autoproc/). In general, the mmCIF categories here should provide items that are currently used in the PDB archive. If there are alternatives, the one recommended by the PDB developers has been selected. The distinction between *_all and *_obs quantities is not always clear: often only one version is actively used within the PDB archive (or is the one recommended by PDB developers). The intention of distinguishing between classes of reflections before and after some kind of observation criterion was applied, can in principle be useful - but such criteria change in various ways throughout the data processing steps (rejection of overloaded or too partial reflections, outlier/misfit rejections during scaling etc) and there is no retrospect computation of data scaling/merging statistics for the reflections used in the final refinement (where another observation criterion might have been applied). Typical data processing will usually only provide one version of statistics at various stages and these are given in the recommended item here, irrespective of the "_all" and "_obs" connotation, see e.g. the use of _reflns.pdbx_Rmerge_I_obs, _reflns.pdbx_Rrim_I_all and _reflns.pdbx_Rpim_I_all. Please note that all statistics related to "merged intensities" (or "merging") are based on inverse-variance weighting of the individual measurements making up a symmetry-unique reflection. This is standard for several decades now, even if some of the dictionary definitions seem to suggest that a simple "mean" or "average" intensity is being used instead. R-values are always given for all symmetry-equivalent reflections following Friedel's law, i.e. Bijvoet pairs are not treated separately (since we want to describe the overall mean intensity and not the mean I(+) and I(-) here). The Rrim metric is identical to the Rmeas R-value and only differs in name. _reflns.pdbx_number_measured_all is the number of measured intensities just before the final merging step (at which point no additional rejection takes place). _reflns.number_obs is the number of symmetry-unique observations, i.e. the result of merging those measurements via inverse-variance weighting. _reflns.pdbx_netI_over_sigmaI is based on the merged intensities (_reflns.number_obs) as expected. _reflns.pdbx_redundancy is synonymous with "multiplicity". The per-shell item _reflns_shell.number_measured_all corresponds to the overall value _reflns.pdbx_number_measured_all. The per-shell item _reflns_shell.number_unique_all corresponds to the overall value _reflns.number_obs. The per-shell item _reflns_shell.percent_possible_all corresponds to the overall value _reflns.percent_possible_obs. The per-shell item _reflns_shell.meanI_over_sigI_obs corresponds to the overall value given as _reflns.pdbx_netI_over_sigmaI. But be aware of the incorrect definition of the former in the current dictionary!
CC1/2: 0.98 / CC1/2 anomalous: -0.043 / Rmerge(I) obs: 0.3218 / Rpim(I) all: 0.1356 / Rrim(I) all: 0.3498 / AbsDiff over sigma anomalous: 0.773 / Baniso tensor eigenvalue 1: 33.7 Å2 / Baniso tensor eigenvalue 2: 54.6 Å2 / Baniso tensor eigenvalue 3: 37 Å2 / Baniso tensor eigenvector 1 ortho1: 0.9167 / Baniso tensor eigenvector 1 ortho2: 0 / Baniso tensor eigenvector 1 ortho3: -0.3996 / Baniso tensor eigenvector 2 ortho1: 0 / Baniso tensor eigenvector 2 ortho2: 1 / Baniso tensor eigenvector 2 ortho3: 0 / Baniso tensor eigenvector 3 ortho1: 0.3996 / Baniso tensor eigenvector 3 ortho2: 0 / Baniso tensor eigenvector 3 ortho3: 0.9167 / Aniso diffraction limit 1: 2.852 Å / Aniso diffraction limit 2: 3.152 Å / Aniso diffraction limit 3: 2.522 Å / Aniso diffraction limit axis 1 ortho1: 0.90493 / Aniso diffraction limit axis 1 ortho2: 0 / Aniso diffraction limit axis 1 ortho3: 0.42547 / Aniso diffraction limit axis 2 ortho1: 0 / Aniso diffraction limit axis 2 ortho2: 1 / Aniso diffraction limit axis 2 ortho3: 0 / Aniso diffraction limit axis 3 ortho1: -0.42547 / Aniso diffraction limit axis 3 ortho2: 0 / Aniso diffraction limit axis 3 ortho3: 0.90493 / Net I/σ(I): 5.9 / Num. measured all: 1354142 / Observed signal threshold: 1.2 / Orthogonalization convention: pdb / % possible anomalous: 93.2 / % possible ellipsoidal: 93.6 / % possible ellipsoidal anomalous: 93.2 / % possible spherical: 67.2 / % possible spherical anomalous: 66.5 / Redundancy anomalous: 3.21 / Signal type: local
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. measured obsNum. unique allNum. unique obsCC1/2CC1/2 anomalousRpim(I) allRrim(I) allAbsDiff over sigma anomalous% possible anomalous% possible ellipsoidal% possible ellipsoidal anomalous% possible spherical% possible spherical anomalousRedundancy anomalous% possible all
7.857-232.0776.310.068116.72675366753610709107090.996-0.3240.02930.07430.62297.899.297.899.297.83.399.2
6.228-7.8576.020.118711.43644676446710710107100.993-0.1750.05130.12960.73198.999.998.999.998.93.0999.9
5.438-6.2286.350.16039.87679626796210710107100.988-0.0950.06740.17420.7599.699.999.699.999.63.2399.9
4.938-5.4386.270.17739.33671176711710709107090.985-0.1080.07550.19310.76998.999.998.999.998.93.299.9
4.582-4.9385.730.17169.34613646136410712107120.984-0.0830.07660.18840.7897.999.997.999.997.92.9499.9
4.31-4.5826.170.19578.95660866608610706107060.982-0.0840.08370.21320.77599.399.999.399.999.33.1499.9
4.093-4.316.350.22668.07680616806110711107110.976-0.0740.09510.24620.76999.799.999.799.999.73.2299.9
3.914-4.0936.410.27817686576865710709107090.964-0.0540.1160.30170.78199.899.999.899.999.83.2599.9
3.763-3.9146.470.30686.38692516925110709107090.959-0.0360.1270.33240.78499.799.999.799.999.73.2799.9
3.632-3.7636.520.36125.57698276982710709107090.947-0.0270.1490.39120.78499.899.999.899.999.83.399.9
3.518-3.6326.560.46144.49702457024510709107090.916-0.0290.18950.49940.78699.999.899.999.899.93.3199.8
3.417-3.5186.580.53963.87704487044810711107110.881-0.0170.22170.5840.79199.799.899.799.899.73.3299.8
3.326-3.4176.60.67753.12707377073710710107100.850.0030.27840.73320.79399.899.899.899.899.83.3399.8
3.244-3.3266.160.73962.7659806598010710107100.7730.0010.31750.80630.79499.899.899.899.899.83.1199.8
3.17-3.2445.850.81952.34626976269710709107090.691-0.0240.36310.89830.78598.498.898.498.898.42.9698.8
3.095-3.1696.270.96352.1671756717510710107100.621-0.0070.41051.04880.78891.591.991.589.889.43.1791.9
3.015-3.0956.461.12841.81691776917710709107090.5590.0030.47291.2250.79585.886.385.876.976.43.2786.3
2.929-3.0156.531.2271.67699616996110710107100.5020.0010.51121.33090.78881.381.781.363.162.43.3181.7
2.82-2.9296.561.24031.64702397023910709107090.48-0.0110.5141.34440.78675.576.175.543.8433.3476.1
2.522-2.826.271.21921.63671556715510710107100.44-0.0090.51621.32630.79461.561.661.511.911.53.261.6

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Processing

Software
NameVersionClassification
MxCuBEdata collection
autoPROC1.0.5data processing
XDSJan 10, 2022data reduction
Aimless0.7.7data scaling
STARANISO2.3.79data scaling
Coot0.9.8model building
BUSTER2.10.4refinement
PHASER2.7phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.522→232.08 Å / Cor.coef. Fo:Fc: 0.885 / Cor.coef. Fo:Fc free: 0.876 / Cross valid method: THROUGHOUT / SU Rfree Blow DPI: 0.413
RfactorNum. reflection% reflectionSelection details
Rfree0.2652 10624 -RANDOM
Rwork0.2577 ---
obs0.2581 214191 67.2 %-
Displacement parametersBiso mean: 59.77 Å2
Baniso -1Baniso -2Baniso -3
1-1.2175 Å20 Å22.9363 Å2
2---3.5211 Å20 Å2
3---2.3036 Å2
Refine analyzeLuzzati coordinate error obs: 0.45 Å
Refinement stepCycle: LAST / Resolution: 2.522→232.08 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms67475 0 652 430 68557
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.008136785HARMONIC2
X-RAY DIFFRACTIONt_angle_deg0.96247597HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d40701SINUSOIDAL2
X-RAY DIFFRACTIONt_gen_planes23192HARMONIC5
X-RAY DIFFRACTIONt_it136785HARMONIC10
X-RAY DIFFRACTIONt_chiral_improper_torsion9303SEMIHARMONIC5
X-RAY DIFFRACTIONt_ideal_dist_contact111694SEMIHARMONIC4
X-RAY DIFFRACTIONt_omega_torsion2.39
X-RAY DIFFRACTIONt_other_torsion15.47
LS refinement shellResolution: 2.522→2.71 Å
RfactorNum. reflection% reflection
Rfree0.3368 178 -
Rwork0.3399 --
obs--6.84 %
Refinement TLS params.

Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.2120.3061-0.12571.05070.28210.30140.3450.01380.01930.0138-0.27380.0930.01930.093-0.0711-0.2327-0.18630.18880.26-0.30480.0128-11.6722-3.269741.2098
20.4578-0.1395-0.17931.22240.30592.35070.00620.35940.55040.3594-0.0798-0.0230.5504-0.0230.07360.2039-0.10550.05330.11250.0673-0.244212.242741.8221106.8833
31.78420.46780.41320.94420.25430.38110.0295-0.1276-0.1455-0.1276-0.0555-0.2375-0.1455-0.23750.0260.06210.04770.1101-0.24380.03090.121255.7682-2.44089.2407
41.62440.2618-0.69221.0094-0.05392.0954-0.70180.19790.60190.19790.3692-0.02520.6019-0.02520.33260.1729-0.04030.2241-0.098-0.1293-0.036550.9253-33.083683.0464
51.06550.39230.2931.043-0.06290.6260.1114-0.13960.0828-0.1396-0.0604-0.05560.0828-0.0556-0.0510.0104-0.00480.037-0.1957-0.05340.18655.0864-34.65729.6609
61.36510.6636-0.3041.2669-0.1470.63020.00510.11690.09210.1169-0.1260.35690.09210.35690.1209-0.010.0320.0624-0.10940.00920.16754.736144.688332.975
71.77690.5105-0.6520.9416-0.26741.18540.24940.185-0.24140.1850.0665-0.31-0.2414-0.31-0.31590.06860.06210.1809-0.1885-0.02440.211815.558273.681231.9491
81.28420.12450.0831.26710.340.8550.26850.1710.04840.171-0.0391-0.18150.0484-0.1815-0.2294-0.0151-0.17-0.1106-0.12040.1870.171173.6738-34.614841.0822
91.74510.3482-0.01772.22170.48011.4937-0.06860.18020.73830.18020.27830.63240.73830.6324-0.2096-0.11670.2306-0.16780.2185-0.303-0.198178.745648.939174.6079
101.4480.081-0.0061.046-0.21340.7274-0.0884-0.0460.2118-0.0460.069-0.33680.2118-0.33680.01940.0801-0.10430.0956-0.127-0.0190.05618.529541.203133.1305
111.82730.1939-0.21460.9717-0.13060.3141-0.5609-0.00820.3914-0.00820.3491-0.42470.3914-0.42470.21180.0045-0.30420.28360.20590.0474-0.19514.5585-36.45184.1675
121.2731-0.08950.08070.6637-0.29291.54820.17030.12-0.58360.12-0.12980.0679-0.58360.0679-0.04040.3327-0.05360.15230.0967-0.1886-0.24197.241173.8691105.6927
131.9658-0.1296-0.72190.820.24680.356-0.34790.249-0.11260.2490.3729-0.5397-0.1126-0.5397-0.025-0.10340.0129-0.00360.34570.2659-0.18111.6626-4.14483.4455
142.69120.40650.13480.86190.10880.20550.14340.04480.03910.0448-0.11270.15920.03910.1592-0.0307-0.02750.0032-0.0038-0.1355-0.16560.21756.3854-36.0539.8316
150.06890.35020.33621.41330.5122.23130.0026-0.0426-0.2243-0.04260.23090.3456-0.22430.3456-0.2335-0.1184-0.20390.01340.3042-0.1062-0.035875.103281.190875.9997
161.4536-0.152-0.38411.08040.15550.51870.0670.17990.53870.17990.0818-0.09150.5387-0.0915-0.14880.39060.0639-0.2272-0.0292-0.0608-0.222860.994945.4958106.4011
171.94340.0242-0.75410.7218-0.25931.583-0.23090.0089-0.24990.00890.3194-0.0196-0.2499-0.0196-0.08850.074-0.0651-0.0938-0.0697-0.02390.023648.0173-0.802883.4792
180.7592-0.0090.20271.1424-0.16651.85120.10610.3549-0.34890.35490.04790.0338-0.34890.0338-0.1540.13270.0207-0.06460.0946-0.0832-0.137156.277377.8649107.1587
191.45740.07010.36670.8848-0.09860.2020.12740.0506-0.10420.0506-0.02080.0788-0.10420.0788-0.10670.0407-0.13020.08910.0005-0.10940.091873.3455-2.187541.1391
200.23080.04390.25961.89330.40271.73830.0466-0.0962-0.808-0.0962-0.1464-0.9914-0.808-0.99140.09980.02890.30450.10580.2824-0.1305-0.2154-9.743570.284273.4815
212.06840.43050.00831.08090.33490.55740.1646-0.0846-0.0482-0.0846-0.0905-0.0715-0.0482-0.0715-0.0741-0.04650.00160.099-0.08910.01880.21497.0407-3.61219.8718
222.4009-0.0967-0.0690.91840.09790.65270.2636-0.15530.0243-0.1553-0.1954-0.20980.0243-0.2098-0.0682-0.219-0.26660.00450.28610.23620.0448-11.265-35.756441.7133
230.22160.3461-0.08251.4530.17321.98610.08830.0590.29020.059-0.2002-0.53120.2902-0.53120.11190.0635-0.21020.09760.2306-0.068-0.1597-5.986837.706375.4746
241.18010.2392-0.56281.0863-0.43090.93110.28810.0758-0.40260.0758-0.11470.3762-0.40260.3762-0.17340.125-0.19340.1318-0.1566-0.10140.082951.910776.898832.9257
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{ E|* }E2 - 389
2X-RAY DIFFRACTION1{ E|* }E395
3X-RAY DIFFRACTION1{ E|* }E396 - 410
4X-RAY DIFFRACTION2{ T|* }T4 - 389
5X-RAY DIFFRACTION2{ T|* }T395
6X-RAY DIFFRACTION2{ T|* }T396 - 400
7X-RAY DIFFRACTION3{ B|* }B3 - 389
8X-RAY DIFFRACTION3{ B|* }B395 - 398
9X-RAY DIFFRACTION3{ B|* }B399 - 445
10X-RAY DIFFRACTION3{ B|* }B446
11X-RAY DIFFRACTION3{ B|* }B448 - 450
12X-RAY DIFFRACTION4{ K|* }K3 - 389
13X-RAY DIFFRACTION4{ K|* }K395
14X-RAY DIFFRACTION4{ K|* }K396 - 404
15X-RAY DIFFRACTION5{ A|* }A3 - 389
16X-RAY DIFFRACTION5{ A|* }A395 - 399
17X-RAY DIFFRACTION5{ A|* }A400 - 446
18X-RAY DIFFRACTION6{ P|* }P2 - 389
19X-RAY DIFFRACTION6{ P|* }P395 - 396
20X-RAY DIFFRACTION6{ P|* }P397 - 417
21X-RAY DIFFRACTION6{ P|* }P418
22X-RAY DIFFRACTION7{ N|* }N2 - 389
23X-RAY DIFFRACTION7{ N|* }N395 - 396
24X-RAY DIFFRACTION7{ N|* }N397 - 419
25X-RAY DIFFRACTION7{ N|* }N420
26X-RAY DIFFRACTION8{ D|* }D3 - 389
27X-RAY DIFFRACTION8{ D|* }D395 - 396
28X-RAY DIFFRACTION8{ D|* }D397 - 422
29X-RAY DIFFRACTION9{ W|* }W3 - 388
30X-RAY DIFFRACTION9{ W|* }W395
31X-RAY DIFFRACTION9{ W|* }W396 - 398
32X-RAY DIFFRACTION10{ M|* }M2 - 389
33X-RAY DIFFRACTION10{ M|* }M395 - 396
34X-RAY DIFFRACTION10{ M|* }M398 - 438
35X-RAY DIFFRACTION11{ J|* }J3 - 389
36X-RAY DIFFRACTION11{ J|* }J395 - 396
37X-RAY DIFFRACTION11{ J|* }J397 - 402
38X-RAY DIFFRACTION12{ S|* }S2 - 389
39X-RAY DIFFRACTION12{ S|* }S395
40X-RAY DIFFRACTION12{ S|* }S396 - 402
41X-RAY DIFFRACTION13{ I|* }I2 - 388
42X-RAY DIFFRACTION13{ I|* }I395
43X-RAY DIFFRACTION13{ I|* }I396 - 401
44X-RAY DIFFRACTION14{ G|* }G3 - 389
45X-RAY DIFFRACTION14{ G|* }G395
46X-RAY DIFFRACTION14{ G|* }G396 - 428
47X-RAY DIFFRACTION15{ X|* }X2 - 388
48X-RAY DIFFRACTION15{ X|* }X395
49X-RAY DIFFRACTION15{ X|* }X396 - 397
50X-RAY DIFFRACTION16{ V|* }V4 - 388
51X-RAY DIFFRACTION16{ V|* }V395 - 396
52X-RAY DIFFRACTION16{ V|* }V397 - 399
53X-RAY DIFFRACTION17{ L|* }L2 - 389
54X-RAY DIFFRACTION17{ L|* }L395 - 396
55X-RAY DIFFRACTION17{ L|* }L397 - 404
56X-RAY DIFFRACTION18{ U|* }U3 - 389
57X-RAY DIFFRACTION18{ U|* }U395
58X-RAY DIFFRACTION18{ U|* }U396 - 400
59X-RAY DIFFRACTION19{ C|* }C3 - 389
60X-RAY DIFFRACTION19{ C|* }C395 - 396
61X-RAY DIFFRACTION19{ C|* }C397 - 425
62X-RAY DIFFRACTION20{ R|* }R3 - 389
63X-RAY DIFFRACTION20{ R|* }R395
64X-RAY DIFFRACTION20{ R|* }R396 - 399
65X-RAY DIFFRACTION21{ H|* }H3 - 389
66X-RAY DIFFRACTION21{ H|* }H395 - 397
67X-RAY DIFFRACTION21{ H|* }H398 - 431
68X-RAY DIFFRACTION22{ F|* }F2 - 388
69X-RAY DIFFRACTION22{ F|* }F395 - 396
70X-RAY DIFFRACTION22{ F|* }F397 - 410
71X-RAY DIFFRACTION23{ Q|* }Q2 - 389
72X-RAY DIFFRACTION23{ Q|* }Q395
73X-RAY DIFFRACTION23{ Q|* }Q396 - 408
74X-RAY DIFFRACTION24{ O|* }O2 - 389
75X-RAY DIFFRACTION24{ O|* }O395 - 396
76X-RAY DIFFRACTION24{ O|* }O397 - 424

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