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- PDB-7kr7: Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H56A mutant w... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7kr7
TitleDihydrodipicolinate synthase (DHDPS) from C.jejuni, H56A mutant with pyruvate bound in the active site and L-lysine at the allosteric site
Components4-hydroxy-tetrahydrodipicolinate synthase
KeywordsLYASE / Dihydrodipicolinate synthase
Function / homology
Function and homology information


(R,S)-4-hydroxy-2-oxoglutarate aldolase activity / 4-hydroxy-tetrahydrodipicolinate synthase / 4-hydroxy-tetrahydrodipicolinate synthase activity / glyoxylate catabolic process / diaminopimelate biosynthetic process / lysine biosynthetic process via diaminopimelate / cytosol
Similarity search - Function
4-hydroxy-tetrahydrodipicolinate synthase, DapA / Schiff base-forming aldolase, conserved site / Dihydrodipicolinate synthase signature 1. / Schiff base-forming aldolase, active site / Dihydrodipicolinate synthase signature 2. / DapA-like / Dihydrodipicolinate synthetase family / Dihydrodipicolinate synthetase family / Aldolase-type TIM barrel
Similarity search - Domain/homology
ACETATE ION / LYSINE / DI(HYDROXYETHYL)ETHER / TRIETHYLENE GLYCOL / 4-hydroxy-tetrahydrodipicolinate synthase
Similarity search - Component
Biological speciesCampylobacter jejuni subsp. jejuni serotype O:2 (Campylobacter)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.22 Å
AuthorsSaran, S. / Sanders, D.A.R.
Funding support Canada, 1items
OrganizationGrant numberCountry
Natural Sciences and Engineering Research Council (NSERC, Canada) Canada
CitationJournal: To Be Published
Title: ALLOSTERIC SITE RESIDUE 'H56' CAPS THE INHIBITOR AT THE TIGHT DIMER INTERFACE FOR TRANSMITTING THE ALLOSTERIC INHIBITION SIGNALS IN Cj.DHDPS
Authors: Saran, S. / Skovpen, Y. / Yazdi, M.M. / Palmer, D.R.J. / Sanders, D.A.R.
History
DepositionNov 18, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 24, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.2Nov 29, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 4-hydroxy-tetrahydrodipicolinate synthase
B: 4-hydroxy-tetrahydrodipicolinate synthase
C: 4-hydroxy-tetrahydrodipicolinate synthase
D: 4-hydroxy-tetrahydrodipicolinate synthase
E: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)208,34146
Polymers204,7096
Non-polymers3,63240
Water20,5911143
1
A: 4-hydroxy-tetrahydrodipicolinate synthase
E: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,32514
Polymers68,2362
Non-polymers1,08812
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4810 Å2
ΔGint-13 kcal/mol
Surface area21080 Å2
MethodPISA
2
B: 4-hydroxy-tetrahydrodipicolinate synthase
C: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,60318
Polymers68,2362
Non-polymers1,36716
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5770 Å2
ΔGint-12 kcal/mol
Surface area21180 Å2
MethodPISA
3
D: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,41314
Polymers68,2362
Non-polymers1,17712
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4960 Å2
ΔGint-22 kcal/mol
Surface area21690 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.800, 231.240, 199.540
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 3 through 204 or (resid 205...
21(chain B and (resid 3 through 204 or (resid 205...
31(chain C and (resid 3 through 165 or (resid 166...
41(chain D and (resid 3 through 165 or (resid 166...
51(chain E and (resid 3 through 165 or (resid 166...
61(chain F and (resid 3 through 204 or (resid 205...

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11LYSLYSLYSLYS(chain A and (resid 3 through 204 or (resid 205...AA3 - 20415 - 216
12GLYGLYGLYGLY(chain A and (resid 3 through 204 or (resid 205...AA205217
13LYSLYSPHEPHE(chain A and (resid 3 through 204 or (resid 205...AA3 - 29815 - 310
14LYSLYSPHEPHE(chain A and (resid 3 through 204 or (resid 205...AA3 - 29815 - 310
21LYSLYSLYSLYS(chain B and (resid 3 through 204 or (resid 205...BB3 - 20415 - 216
22GLYGLYGLYGLY(chain B and (resid 3 through 204 or (resid 205...BB205217
23LYSLYSPHEPHE(chain B and (resid 3 through 204 or (resid 205...BB3 - 29815 - 310
24LYSLYSPHEPHE(chain B and (resid 3 through 204 or (resid 205...BB3 - 29815 - 310
31LYSLYSVALVAL(chain C and (resid 3 through 165 or (resid 166...CC3 - 16515 - 177
32KPIKPIKPIKPI(chain C and (resid 3 through 165 or (resid 166...CC166178
33LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
34LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
35LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
36LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
37LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
38LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
39LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
310LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
311LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
312LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
313LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
314LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
315LYSLYSPHEPHE(chain C and (resid 3 through 165 or (resid 166...CC3 - 29815 - 310
41LYSLYSVALVAL(chain D and (resid 3 through 165 or (resid 166...DD3 - 16515 - 177
42KPIKPIKPIKPI(chain D and (resid 3 through 165 or (resid 166...DD166178
43LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
44LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
45LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
46LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
47LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
48LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
49LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
410LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
411LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
412LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
413LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
414LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
415LYSLYSPHEPHE(chain D and (resid 3 through 165 or (resid 166...DD3 - 29815 - 310
51LYSLYSVALVAL(chain E and (resid 3 through 165 or (resid 166...EE3 - 16515 - 177
52KPIKPIKPIKPI(chain E and (resid 3 through 165 or (resid 166...EE166178
53LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
54LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
55LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
56LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
57LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
58LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
59LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
510LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
511LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
512LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
513LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
514LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
515LYSLYSPHEPHE(chain E and (resid 3 through 165 or (resid 166...EE3 - 29815 - 310
61LYSLYSLYSLYS(chain F and (resid 3 through 204 or (resid 205...FF3 - 20415 - 216
62GLYGLYGLYGLY(chain F and (resid 3 through 204 or (resid 205...FF205217
63ASPASPPHEPHE(chain F and (resid 3 through 204 or (resid 205...FF2 - 29814 - 310
64ASPASPPHEPHE(chain F and (resid 3 through 204 or (resid 205...FF2 - 29814 - 310

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Components

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Protein , 1 types, 6 molecules ABCDEF

#1: Protein
4-hydroxy-tetrahydrodipicolinate synthase / HTPA synthase


Mass: 34118.191 Da / Num. of mol.: 6 / Mutation: H56A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) (Campylobacter)
Strain: ATCC 700819 / NCTC 11168 / Gene: dapA, Cj0806 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9PPB4, 4-hydroxy-tetrahydrodipicolinate synthase

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Non-polymers , 8 types, 1183 molecules

#2: Chemical
ChemComp-LYS / LYSINE


Type: L-peptide linking / Mass: 147.195 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C6H15N2O2 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C6H14O4 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C2H6O2 / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C2H3O2 / Feature type: SUBJECT OF INVESTIGATION
#7: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C4H10O3 / Feature type: SUBJECT OF INVESTIGATION
#8: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3 / Feature type: SUBJECT OF INVESTIGATION
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1143 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.42 Å3/Da / Density % sol: 49.12 %
Crystal growTemperature: 288.15 K / Method: microbatch
Details: 0.3 M Magnesium acetate, 12 % PEG 8000, 0.1 M Sodium acetate (pH 7.4)

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Aug 1, 2019
RadiationMonochromator: Double beam / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.22→45.8 Å / Num. obs: 97699 / % possible obs: 99.7 % / Redundancy: 15 % / CC1/2: 0.995 / Net I/σ(I): 14.46
Reflection shellResolution: 2.22→2.29 Å / Rmerge(I) obs: 0.228 / Num. unique obs: 9423 / % possible all: 97.16

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Processing

Software
NameVersionClassification
XSCALEdata scaling
PHENIX1.17.1_3660refinement
PDB_EXTRACT3.27data extraction
HKL-3000data reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4LY8

4ly8


Resolution: 2.22→45.8 Å / SU ML: 0.18 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 17.63 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1893 4884 5 %
Rwork0.1489 92801 -
obs0.1509 97685 99.66 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 110.23 Å2 / Biso mean: 25.9063 Å2 / Biso min: 0.7 Å2
Refinement stepCycle: final / Resolution: 2.22→45.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13577 0 180 1143 14900
Biso mean--38.07 33.16 -
Num. residues----1783
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5358X-RAY DIFFRACTION1.82TORSIONAL
12B5358X-RAY DIFFRACTION1.82TORSIONAL
13C5358X-RAY DIFFRACTION1.82TORSIONAL
14D5358X-RAY DIFFRACTION1.82TORSIONAL
15E5358X-RAY DIFFRACTION1.82TORSIONAL
16F5358X-RAY DIFFRACTION1.82TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.22-2.250.21971540.1588293495
2.25-2.270.2081560.1543296997
2.27-2.30.23391610.1572304999
2.3-2.330.22691610.15643070100
2.33-2.360.21021610.15123046100
2.36-2.390.21721620.1523085100
2.39-2.430.20461620.14833074100
2.43-2.460.19471640.14423117100
2.46-2.50.18421600.143039100
2.5-2.540.20631630.14253090100
2.54-2.590.18581610.13723070100
2.59-2.630.18451630.14063088100
2.63-2.680.20791630.1423095100
2.68-2.740.18881620.14523083100
2.74-2.80.19061620.1453077100
2.8-2.860.19671630.15413104100
2.86-2.930.20981630.15733090100
2.93-3.010.19541600.16543051100
3.01-3.10.19711640.15983114100
3.1-3.20.21961630.16033085100
3.2-3.320.22871630.16953112100
3.32-3.450.18821640.1693107100
3.45-3.610.20831640.16333112100
3.61-3.80.17171620.14423087100
3.8-4.030.18121650.13713135100
4.03-4.340.1741660.13293143100
4.34-4.780.16781650.12733139100
4.78-5.470.16081650.14423140100
5.47-6.890.17041680.16193200100
6.89-100.14171740.13923296100
Refinement TLS params.

Method: refined / 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)
11.2310.15770.33452.1586-0.22361.62780.01-0.11060.11360.22690.0130.1404-0.0912-0.1057-0.02180.1910.0520.01080.21780.04940.2495-76.302-65.49619.504
20.6832-0.30851.05236.2707-1.20882.24060.0544-0.26770.02860.12850.03480.5846-0.0681-0.3199-0.17330.13910.05580.03220.27130.07960.3246-84.854-68.98618.126
30.2323-0.61850.09794.82670.52911.0644-0.05640.14240.0495-0.0009-0.1060.2824-0.0535-0.28220.05050.12580.0253-0.01720.24110.07290.2639-81.817-73.74410.487
40.8712-0.1925-0.43021.9193-0.04341.1231-0.01550.0937-0.0076-0.19720.090.1730.0599-0.1237-0.04530.1723-0.0265-0.02540.16160.0440.1604-73.034-81.6627.828
50.2948-0.0241-0.22161.37540.53160.7822-0.0313-0.00760.0531-0.03490.03030.01330.0354-0.05-0.01220.1748-0.0068-0.01880.21480.05150.198-63.401-72.4314.413
62.57950.1361-0.18341.7169-0.22323.4936-0.00810.0240.39-0.04960.0705-0.1075-0.1960.1103-0.05960.15960.0074-0.01890.12110.00610.2364-57.768-59.2813.319
71.18420.19980.14214.0023-1.18962.057-0.0469-0.10750.04190.51410.10220.0258-0.1575-0.0804-0.04320.23780.02060.00230.19230.00740.1412-65.416-65.87331.115
81.4215-0.34360.05671.36490.17641.2851-0.00960.1385-0.0105-0.1931-0.0423-0.15610.120.16790.03340.1536-0.02740.02930.21720.08030.2381-25.788-78.301-2.478
91.1480.1996-0.37292.4789-2.51674.4937-0.0686-0.05080.18390.1433-0.0262-0.2303-0.29890.09420.13510.1481-0.0324-0.03870.19980.04090.3271-22.223-74.6058.302
100.7781-0.0483-0.47651.4234-0.28681.1095-0.1065-0.06590.18760.0689-0.0313-0.137-0.08930.0910.12730.1539-0.0038-0.04620.17790.03810.2195-30.913-76.3816.532
110.4304-0.25860.06350.97940.00431.9699-0.06460.00240.14240.10940.0169-0.1278-0.046-0.0550.05240.1676-0.0131-0.03590.19250.0390.2469-40.606-68.82810.385
121.6742-0.0206-0.28874.12580.26931.14020.00180.26820.2597-0.29530.07750.2039-0.077-0.0646-0.06760.1598-0.0161-0.01150.23070.07330.1824-46.346-69.83-5.498
131.9982-0.10320.2573.5034-1.05182.3909-0.04820.2269-0.0315-0.50510.0171-0.11420.297-0.12580.03060.21910.00510.01740.19220.02140.1445-38.63-88.299-8.899
142.11411.35991.04313.83771.12971.9806-0.02090.05020.06830.18270.0107-0.2166-0.10530.18280.02390.2110.0338-0.01130.24390.08870.1896-25.455-100.55728.112
150.91020.9308-0.90822.102-0.30111.2410.03930.0136-0.04470.2279-0.0394-0.0795-0.02720.2091-0.01880.19580.0156-0.03430.26280.08080.2516-24.291-100.43631.223
160.3035-0.8910.65254.3445-0.71632.2726-0.0459-0.283-0.1640.1650.0512-0.5388-0.03660.20930.05920.11120.0186-0.02840.24290.05770.2792-17.501-101.0824.254
170.6379-0.83861.10832.345-2.09254.1866-0.04160.0417-0.1318-0.08560.0316-0.07250.18340.11580.02120.15540.01940.04350.1720.03820.247-23.125-104.55617.468
181.2250.2101-0.09421.6734-0.350.9467-0.03720.0301-0.0123-0.19480.0352-0.14970.12690.08730.00320.18420.01070.02180.16410.03310.1538-33.388-101.37811.819
191.73040.7425-0.19562.16740.61932.8513-0.0671-0.0081-0.0471-0.08820.0122-0.12020.1320.05330.08620.20490.00070.00160.16680.03860.1955-39.655-108.15413.209
200.77270.19580.09690.4312-0.00210.9683-0.0382-0.073-0.058-0.01020.0250.00410.0402-0.0250.00560.20270.0190.00420.20930.05530.2143-42.332-107.8427.509
212.04980.4611-0.3015.7643-0.14461.4487-0.0726-0.3073-0.2010.23680.0770.0710.2907-0.0701-0.03110.19640.01660.00870.23630.0510.1324-45.212-104.13137.374
221.7720.5377-0.29362.1561-0.36242.3212-0.0141-0.22850.1380.282-0.0408-0.0782-0.2605-0.00920.02570.2219-0.0058-0.04730.23780.01750.1898-32.117-88.92238.085
231.3376-0.1583-0.08821.4602-0.11512.7909-0.06620.09670.0962-0.0417-0.01030.1996-0.1847-0.27380.04790.1697-0.0185-0.04520.28170.01620.2441-29.35-132.79438.735
240.6840.3054-0.38482.07560.24711.5272-0.0405-0.22270.11170.10660.0230.17660.0793-0.98-0.03840.1695-0.0302-0.020.45980.00760.2909-36.563-136.89942.853
251.2583-0.52040.371.4897-0.42791.5106-0.03180.1063-0.1425-0.16720.04360.10410.2869-0.2319-0.02230.1953-0.0719-0.0110.2044-0.02740.1611-25.225-148.70544.092
260.5581-0.4441-0.23121.021-0.10720.5891-0.06270.1184-0.003-0.00880.00530.04460.1754-0.0930.07420.2461-0.0408-0.03060.2393-0.01350.1845-15.038-147.17633.565
272.5670.44720.19811.87750.99852.5434-0.12680.47970.1388-0.31890.10940.1289-0.04980.0063-0.03830.2243-0.0076-0.03140.26470.04630.1915-13.349-132.18525.954
280.55680.1606-0.01641.2848-0.95053.76690.01590.10060.16570.0403-0.0405-0.042-0.2933-0.0750.06040.18010.0478-0.02070.18720.01840.224-18.693-121.38342.316
291.013-0.14480.16491.8160.04121.76250.0391-0.0169-0.0438-0.1610.06030.36110.1633-0.3418-0.09650.1632-0.04970.00130.23840.07240.2936-80.607-104.59522.513
300.71020.02380.13161.0764-0.18090.6632-0.0255-0.1106-0.08170.14540.07250.121-0.0311-0.1095-0.03390.16330.00140.02710.18690.06060.153-67.651-98.45131.685
312.8351-1.37181.48122.7608-3.10624.7212-0.1492-0.0788-0.2119-0.1240.0159-0.08330.1706-0.09760.1150.1969-0.01950.02050.1466-0.0080.2056-58.386-112.70618.733
321.0607-0.11960.29623.4009-0.93852.0105-0.04260.0919-0.1006-0.32110.19830.01240.17610.016-0.16910.2477-0.0439-0.04590.22530.00220.2232-71.526-106.6927.661
332.48061.4151.22623.40490.60711.95930.0841-0.1455-0.2146-0.0964-0.0588-0.11680.1898-0.19820.02440.2375-0.01140.04560.20190.01660.1444-20.639-149.43472.476
341.5986-0.74891.11740.80850.052.7375-0.0643-0.1296-0.19030.1210.04870.15560.2258-0.1809-0.00350.3037-0.04480.04580.21180.01920.2244-20.935-152.38874.069
352.1667-0.47712.40462.4472-1.2326.34590.0726-0.32190.04770.1856-0.04110.20330.4511-0.8013-0.14560.2799-0.0690.08370.2974-0.0020.2247-29.152-147.26473.07
361.4031-0.67320.741.9109-1.84574.1196-0.0734-0.21350.15440.2456-0.02350.103-0.1876-0.02850.05880.1981-0.01310.04320.1994-0.04140.1871-25.005-138.73271.805
371.19490.3177-0.1671.42070.30161.0728-0.0025-0.16460.130.04930.04830.06590.0374-0.0294-0.02510.17060.0108-0.00880.1708-0.00380.1622-16.963-133.83164.043
382.3667-0.6636-0.3032.69030.36881.9127-0.0212-0.12760.21780.0313-0.01430.0647-0.1357-0.01730.03290.1693-0.024-0.02930.1969-0.02120.1684-9.837-130.5769.164
390.98490.6253-0.21971.4355-0.90460.7552-0.0224-0.091-0.00310.0228-0.03220.02060.00190.04420.04230.20020.0219-0.00310.17870.00160.1204-3.374-140.43272.659
402.6022-0.01980.31882.43350.94533.0058-0.1395-0.3267-0.15190.26190.0642-0.09230.25170.22620.00530.29930.0498-0.00620.21880.04640.2075-0.804-151.78977.324
411.2589-0.96241.56721.5309-0.42492.695-0.0331-0.1683-0.12410.0775-0.05490.06810.4649-0.25710.0560.3303-0.05520.03010.18820.00460.2146-17.035-160.57763.099
423.56340.6099-0.23742.34740.34224.10250.0925-0.1014-0.6309-0.1328-0.0301-0.07570.9630.35750.00030.39320.0512-0.0190.15050.02310.3521-7.321-165.76568.584
430.0626-0.0660.09140.0762-0.1260.133-0.0064-0.05830.0511-0.0480.01890.0403-0.0098-0.0104-0.01850.1324-0.0212-0.00560.08310.03430.2459-43.281-105.6530.066
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 3:55 )A3 - 55
2X-RAY DIFFRACTION2( CHAIN A AND RESID 56:70 )A56 - 70
3X-RAY DIFFRACTION3( CHAIN A AND RESID 71:98 )A71 - 98
4X-RAY DIFFRACTION4( CHAIN A AND RESID 99:148 )A99 - 148
5X-RAY DIFFRACTION5( CHAIN A AND RESID 149:214 )A149 - 214
6X-RAY DIFFRACTION6( CHAIN A AND RESID 215:248 )A215 - 248
7X-RAY DIFFRACTION7( CHAIN A AND RESID 249:298 )A249 - 298
8X-RAY DIFFRACTION8( CHAIN B AND RESID 3:70 )B3 - 70
9X-RAY DIFFRACTION9( CHAIN B AND RESID 71:98 )B71 - 98
10X-RAY DIFFRACTION10( CHAIN B AND RESID 99:148 )B99 - 148
11X-RAY DIFFRACTION11( CHAIN B AND RESID 149:214 )B149 - 214
12X-RAY DIFFRACTION12( CHAIN B AND RESID 215:248 )B215 - 248
13X-RAY DIFFRACTION13( CHAIN B AND RESID 249:298 )B249 - 298
14X-RAY DIFFRACTION14( CHAIN C AND RESID 3:23 )C3 - 23
15X-RAY DIFFRACTION15( CHAIN C AND RESID 24:55 )C24 - 55
16X-RAY DIFFRACTION16( CHAIN C AND RESID 56:70 )C56 - 70
17X-RAY DIFFRACTION17( CHAIN C AND RESID 71:98 )C71 - 98
18X-RAY DIFFRACTION18( CHAIN C AND RESID 99:148 )C99 - 148
19X-RAY DIFFRACTION19( CHAIN C AND RESID 149:171 )C149 - 171
20X-RAY DIFFRACTION20( CHAIN C AND RESID 172:226 )C172 - 226
21X-RAY DIFFRACTION21( CHAIN C AND RESID 227:248 )C227 - 248
22X-RAY DIFFRACTION22( CHAIN C AND RESID 249:298 )C249 - 298
23X-RAY DIFFRACTION23( CHAIN D AND RESID 3:55 )D3 - 55
24X-RAY DIFFRACTION24( CHAIN D AND RESID 56:70 )D56 - 70
25X-RAY DIFFRACTION25( CHAIN D AND RESID 71:148 )D71 - 148
26X-RAY DIFFRACTION26( CHAIN D AND RESID 149:214 )D149 - 214
27X-RAY DIFFRACTION27( CHAIN D AND RESID 215:248 )D215 - 248
28X-RAY DIFFRACTION28( CHAIN D AND RESID 249:298 )D249 - 298
29X-RAY DIFFRACTION29( CHAIN E AND RESID 3:70 )E3 - 70
30X-RAY DIFFRACTION30( CHAIN E AND RESID 71:229 )E71 - 229
31X-RAY DIFFRACTION31( CHAIN E AND RESID 230:248 )E230 - 248
32X-RAY DIFFRACTION32( CHAIN E AND RESID 249:298 )E249 - 298
33X-RAY DIFFRACTION33( CHAIN F AND RESID 3:23 )F3 - 23
34X-RAY DIFFRACTION34( CHAIN F AND RESID 24:55 )F24 - 55
35X-RAY DIFFRACTION35( CHAIN F AND RESID 56:70 )F56 - 70
36X-RAY DIFFRACTION36( CHAIN F AND RESID 71:98 )F71 - 98
37X-RAY DIFFRACTION37( CHAIN F AND RESID 99:148 )F99 - 148
38X-RAY DIFFRACTION38( CHAIN F AND RESID 149:171 )F149 - 171
39X-RAY DIFFRACTION39( CHAIN F AND RESID 172:214 )F172 - 214
40X-RAY DIFFRACTION40( CHAIN F AND RESID 215:248 )F215 - 248
41X-RAY DIFFRACTION41( CHAIN F AND RESID 249:279 )F249 - 279
42X-RAY DIFFRACTION42( CHAIN F AND RESID 280:298 )F280 - 298
43X-RAY DIFFRACTION43( CHAIN A AND RESID 301:301 ) OR ( CHAIN C AND RESID 301:301 ) OR ( CHAIN B AND RESID 301:301 ) OR ( CHAIN E AND RESID 301:301 ) OR ( CHAIN D AND RESID 301:301 ) OR ( CHAIN F AND RESID 301:301 )A301
44X-RAY DIFFRACTION43( CHAIN A AND RESID 301:301 ) OR ( CHAIN C AND RESID 301:301 ) OR ( CHAIN B AND RESID 301:301 ) OR ( CHAIN E AND RESID 301:301 ) OR ( CHAIN D AND RESID 301:301 ) OR ( CHAIN F AND RESID 301:301 )C301
45X-RAY DIFFRACTION43( CHAIN A AND RESID 301:301 ) OR ( CHAIN C AND RESID 301:301 ) OR ( CHAIN B AND RESID 301:301 ) OR ( CHAIN E AND RESID 301:301 ) OR ( CHAIN D AND RESID 301:301 ) OR ( CHAIN F AND RESID 301:301 )B301
46X-RAY DIFFRACTION43( CHAIN A AND RESID 301:301 ) OR ( CHAIN C AND RESID 301:301 ) OR ( CHAIN B AND RESID 301:301 ) OR ( CHAIN E AND RESID 301:301 ) OR ( CHAIN D AND RESID 301:301 ) OR ( CHAIN F AND RESID 301:301 )E301
47X-RAY DIFFRACTION43( CHAIN A AND RESID 301:301 ) OR ( CHAIN C AND RESID 301:301 ) OR ( CHAIN B AND RESID 301:301 ) OR ( CHAIN E AND RESID 301:301 ) OR ( CHAIN D AND RESID 301:301 ) OR ( CHAIN F AND RESID 301:301 )D301
48X-RAY DIFFRACTION43( CHAIN A AND RESID 301:301 ) OR ( CHAIN C AND RESID 301:301 ) OR ( CHAIN B AND RESID 301:301 ) OR ( CHAIN E AND RESID 301:301 ) OR ( CHAIN D AND RESID 301:301 ) OR ( CHAIN F AND RESID 301:301 )F301

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