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- PDB-7kxg: Dihydrodipicolinate synthase (DHDPS) from C.jejuni with pyruvate ... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7kxg
TitleDihydrodipicolinate synthase (DHDPS) from C.jejuni with pyruvate bound in the active site and L-histidine bound at the allosteric site
Components4-hydroxy-tetrahydrodipicolinate synthase
KeywordsLYASE
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 / HISTIDINE / 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: 2.28 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: Reversing the roles of a crucial hydrogen-bonding pair: a lysine-insensitive mutant of Campylobacter jejuni dihydrodipicolinate synthase, H59K, binds histidine in its allosteric site
Authors: Yazdi, M.M. / Saran, S. / Sanders, D.A.R. / Palmer, D.R.J.
History
DepositionDec 3, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 8, 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)209,30061
Polymers205,1126
Non-polymers4,18855
Water13,007722
1
A: 4-hydroxy-tetrahydrodipicolinate synthase
B: 4-hydroxy-tetrahydrodipicolinate synthase
C: 4-hydroxy-tetrahydrodipicolinate synthase
D: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,44641
Polymers136,7414
Non-polymers2,70537
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16580 Å2
ΔGint-84 kcal/mol
Surface area38460 Å2
MethodPISA
2
E: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules

E: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,70840
Polymers136,7414
Non-polymers2,96736
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_654-x+1,y,-z-1/21
Buried area14700 Å2
ΔGint-88 kcal/mol
Surface area39030 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.310, 231.720, 202.350
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 67 or (resid 68...
21(chain B and (resid 3 through 67 or (resid 68...
31(chain C and (resid 3 through 67 or (resid 68...
41(chain D and (resid 3 through 67 or (resid 68...
51(chain E and (resid 3 through 67 or (resid 68...
61(chain F and (resid 3 through 73 or (resid 74...

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
11LYSLYSVALVAL(chain A and (resid 3 through 67 or (resid 68...AA3 - 6715 - 79
12GLUGLUGLUGLU(chain A and (resid 3 through 67 or (resid 68...AA6880
13LYSLYSPHEPHE(chain A and (resid 3 through 67 or (resid 68...AA3 - 29815 - 310
14LYSLYSPHEPHE(chain A and (resid 3 through 67 or (resid 68...AA3 - 29815 - 310
15LYSLYSPHEPHE(chain A and (resid 3 through 67 or (resid 68...AA3 - 29815 - 310
21LYSLYSVALVAL(chain B and (resid 3 through 67 or (resid 68...BB3 - 6715 - 79
22GLUGLUGLUGLU(chain B and (resid 3 through 67 or (resid 68...BB6880
23LYSLYSPHEPHE(chain B and (resid 3 through 67 or (resid 68...BB3 - 29815 - 310
31LYSLYSVALVAL(chain C and (resid 3 through 67 or (resid 68...CC3 - 6715 - 79
32GLUGLUGLUGLU(chain C and (resid 3 through 67 or (resid 68...CC6880
33ASPASPPHEPHE(chain C and (resid 3 through 67 or (resid 68...CC2 - 29814 - 310
34ASPASPPHEPHE(chain C and (resid 3 through 67 or (resid 68...CC2 - 29814 - 310
35ASPASPPHEPHE(chain C and (resid 3 through 67 or (resid 68...CC2 - 29814 - 310
36ASPASPPHEPHE(chain C and (resid 3 through 67 or (resid 68...CC2 - 29814 - 310
41LYSLYSVALVAL(chain D and (resid 3 through 67 or (resid 68...DD3 - 6715 - 79
42GLUGLUGLUGLU(chain D and (resid 3 through 67 or (resid 68...DD6880
43LYSLYSPHEPHE(chain D and (resid 3 through 67 or (resid 68...DD3 - 29815 - 310
51LYSLYSVALVAL(chain E and (resid 3 through 67 or (resid 68...EE3 - 6715 - 79
52GLUGLUGLUGLU(chain E and (resid 3 through 67 or (resid 68...EE6880
53LYSLYSPHEPHE(chain E and (resid 3 through 67 or (resid 68...EE3 - 29815 - 310
54LYSLYSPHEPHE(chain E and (resid 3 through 67 or (resid 68...EE3 - 29815 - 310
55LYSLYSPHEPHE(chain E and (resid 3 through 67 or (resid 68...EE3 - 29815 - 310
56LYSLYSPHEPHE(chain E and (resid 3 through 67 or (resid 68...EE3 - 29815 - 310
61LYSLYSTHRTHR(chain F and (resid 3 through 73 or (resid 74...FF3 - 7315 - 85
62LYSLYSLYSLYS(chain F and (resid 3 through 73 or (resid 74...FF7486
63ASPASPPHEPHE(chain F and (resid 3 through 73 or (resid 74...FF2 - 29814 - 310
64ASPASPPHEPHE(chain F and (resid 3 through 73 or (resid 74...FF2 - 29814 - 310
65ASPASPPHEPHE(chain F and (resid 3 through 73 or (resid 74...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: 34185.258 Da / Num. of mol.: 6
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, 777 molecules

#2: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 17 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C6H14O4 / Feature type: SUBJECT OF INVESTIGATION
#4: 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
#5: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C2H6O2 / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical
ChemComp-HIS / HISTIDINE


Type: L-peptide linking / Mass: 156.162 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C6H10N3O2 / Feature type: SUBJECT OF INVESTIGATION
#7: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H3O2 / 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.: 722 / 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: 2.44 Å3/Da / Density % sol: 49.54 %
Crystal growTemperature: 288.15 K / Method: microbatch / pH: 7.4
Details: 0.3 M Magnesium acetate, 10 % 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 PILATUS 6M / Detector: PIXEL / Date: Jul 25, 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: 2.28→46.36 Å / Num. obs: 90357 / % possible obs: 98.71 % / Redundancy: 15 % / CC1/2: 0.999 / Net I/σ(I): 18.94
Reflection shellResolution: 2.28→2.362 Å / Rmerge(I) obs: 0.2129 / Num. unique obs: 7985 / % possible all: 88.09

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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: 2.28→46.36 Å / SU ML: 0.22 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 20.15 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2082 4518 5 %
Rwork0.1695 85822 -
obs0.1715 90340 98.73 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 97.43 Å2 / Biso mean: 37.7335 Å2 / Biso min: 18.15 Å2
Refinement stepCycle: final / Resolution: 2.28→46.36 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13646 0 204 722 14572
Biso mean--53.51 39.6 -
Num. residues----1784
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5286X-RAY DIFFRACTION4.593TORSIONAL
12B5286X-RAY DIFFRACTION4.593TORSIONAL
13C5286X-RAY DIFFRACTION4.593TORSIONAL
14D5286X-RAY DIFFRACTION4.593TORSIONAL
15E5286X-RAY DIFFRACTION4.593TORSIONAL
16F5286X-RAY DIFFRACTION4.593TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.28-2.310.2741260.2231239283
2.31-2.330.2591320.2042251988
2.33-2.360.23881410.2016267693
2.36-2.390.2641480.1983282099
2.39-2.420.24811510.19282869100
2.42-2.460.22431500.19622836100
2.46-2.490.22531510.18522880100
2.49-2.530.22761530.1832900100
2.53-2.570.20331500.18592852100
2.57-2.610.24691510.18152877100
2.61-2.650.24691520.18012879100
2.65-2.70.24151510.18272864100
2.7-2.760.22291530.18452902100
2.76-2.810.23271500.17852859100
2.81-2.870.24441520.18332890100
2.87-2.940.27191520.18562886100
2.94-3.010.2241510.18852874100
3.01-3.090.22491520.19152883100
3.09-3.190.22991520.19392887100
3.19-3.290.25371530.19452904100
3.29-3.410.25371510.18892882100
3.41-3.540.18921540.18032914100
3.54-3.70.19871520.16442887100
3.7-3.90.18351530.15992911100
3.9-4.140.18231530.14592907100
4.14-4.460.15931530.1372917100
4.46-4.910.16321550.13042942100
4.91-5.620.1891560.15242957100
5.62-7.080.19591560.16642967100
7.08-100.16931640.1445308999
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)
10.8830.3589-0.32290.20820.09010.5532-0.0113-0.0993-0.15310.01110.0790.2421-0.0158-0.2792-0.00050.3148-0.017-0.03530.29880.05860.3467-33.53165.363-19.576
20.4813-0.1579-0.55590.47720.56840.83990.1142-0.0758-0.01830.0726-0.12130.4656-0.1282-0.3759-0.00230.24870.0075-0.02110.40040.06220.4075-40.54172.088-13.699
30.5146-0.47580.1010.82540.10870.25360.0492-0.1183-0.10360.0272-0.06440.1017-0.1223-0.0031-0.00020.26710.00620.02010.32820.06180.2836-30.27681.849-7.859
40.1460.2889-0.0120.80140.23250.0692-0.0162-0.0271-0.09820.02480.0080.07430.0394-0.0731-0.00040.24240.00160.00830.29820.06980.2549-20.71372.547-4.458
50.50380.09220.15150.49320.18970.09580.04810.0935-0.3169-0.20460.0139-0.12960.19860.10570.00010.26520.0178-0.00530.31790.0440.37-14.97459.433-13.241
60.0856-0.1317-0.02610.1699-0.01650.0369-0.03510.15180.0343-0.43080.0243-0.03930.1207-0.011800.36110.0143-0.02140.30320.03210.2553-26.15769.28-31.221
70.2394-0.02550.17380.011-0.05520.27160.03690.1372-0.346-0.4359-0.1029-0.34890.3520.0511-0.00580.36330.04420.07210.34140.02080.3631-16.97261.252-31.17
80.051-0.02530.04240.7720.14110.11710.1283-0.0699-0.13470.3882-0.2043-0.31640.0931-0.0362-0.03280.2304-0.0055-0.04480.21250.08450.312914.77578.3521.431
90.212-0.149-0.12890.32130.23490.1559-0.1313-0.10970.02030.19020.0254-0.2908-0.085-0.0391-0.00050.2723-0.0148-0.05190.2920.10950.360515.18278.4814.712
100.0076-0.0474-0.03290.16090.09840.0578-0.3173-0.20930.2506-0.5088-0.0415-1.0930.15580.498-0.00240.3265-0.0296-0.00360.43260.16590.591624.20679.1170.381
110.01550.02430.05590.27810.210.4188-0.0150.0574-0.13850.0208-0.1166-0.33170.04680.4898-0.00120.24560.01470.02250.35040.11750.378320.47574.953-8.668
120.68540.5692-0.44920.8586-0.06480.5602-0.00640.0084-0.0673-0.1497-0.079-0.1157-0.01020.111200.24560.02820.03770.30110.08870.309111.79176.496-16.723
130.679-0.0139-0.22180.4944-0.15930.2649-0.0171-0.2524-0.0186-0.08140.026-0.2146-0.16590.0240.0140.24820.02320.03240.28330.07970.29686.52568.822-16.703
140.0828-0.0038-0.11060.11160.08090.2270.0467-0.048-0.03670.0337-0.0153-0.02850.0174-0.077900.24260.00730.01440.30140.08050.30890.0268.567-3.757
150.28070.0460.11650.1813-0.07390.05540.0236-0.0059-0.061-0.0350.18980.0210.0699-0.12560.00260.2457-0.0096-0.0020.35080.08030.2903-5.97771.6784.813
160.2433-0.19460.04710.27190.11420.1365-0.0414-0.04450.02540.199-0.1158-0.2593-0.06370.03320.00010.3099-0.0306-0.01010.27570.0740.29727.70790.5075.813
170.45250.0970.30060.8924-0.06820.18960.032-0.52150.23060.6736-0.08490.2623-0.4861-0.2277-0.14470.3385-0.00570.01470.43280.05730.2928-1.05685.52412.995
180.2831-0.17750.09550.7501-0.09570.1970.1145-0.00570.120.02760.14650.288-0.027-0.03110.02350.27890.06080.0240.35250.08280.3435-34.962104.608-23.445
190.25820.20960.37160.2290.29190.4679-0.0401-0.1169-0.01190.0927-0.02220.1342-0.0292-0.1338-0.00020.2990.0940.02660.39770.06250.3675-36.535107.445-20.575
200.09590.02680.05380.05250.08050.15390.18250.07120.0844-0.29830.44870.69360.2759-0.6790.01220.31780.0338-0.07210.45810.0960.5326-44.191102.26-24.427
210.03840.0217-0.36151.48180.08321.26380.02820.0899-0.0273-0.2156-0.02990.15810.1356-0.04240.00010.23380.0267-0.01910.29890.06880.2544-31.25692.549-31.288
220.30470.35330.16110.7274-0.13120.4006-0.01630.01080.0963-0.04330.0078-0.01770.023-0.031-00.26850.05460.0320.28470.07560.269-19.521103.439-31.532
230.3434-0.1135-0.09120.1712-0.1310.1252-0.00010.01840.0870.0248-0.2556-0.2461-0.08720.2676-0.00020.26860.04030.01660.28370.06640.3121-15.236113.698-20.962
240.13570.11560.20490.06540.1530.23810.1477-0.17920.04870.23220.02670.0871-0.0356-0.06240.00010.32710.05760.07840.32490.0510.3074-31.32103.127-8.023
250.07730.10070.03050.19380.01570.1880.0118-0.26110.40320.32910.0280.0535-0.2776-0.0305-0.00130.39890.02860.01360.2978-0.02450.4174-23.821112.758-6.757
260.05050.17460.08470.51050.10860.03850.09690.102-0.0286-0.1069-0.2135-0.320.03860.0799-0.00330.27340.06150.11580.33690.16240.418517.83100.056-31.297
270.0974-0.2268-0.28730.49410.62090.70950.1135-0.08530.1186-0.0161-0.1655-0.35460.0620.3307-0.00050.2180.0050.03250.38930.13320.480222.184102.621-21.479
280.5116-0.38010.11450.6372-0.59060.6059-0.0638-0.05310.08190.1283-0.0659-0.1194-0.0051-0.0114-0.00670.2506-0.0098-0.0020.26060.06460.29619.653101.232-12.527
290.2819-0.2291-0.16560.4545-0.12320.26770.02540.07880.0963-0.027-0.09-0.0498-0.03170.0342-00.27340.02930.04140.31850.07870.31991.304108.311-24.276
300.2525-0.03190.11450.0204-0.06020.07130.03130.2380.2115-0.22910.14790.0883-0.1235-0.05080.00150.29010.03410.04350.4290.10320.3124-2.812101.77-38.091
310.37250.43270.00290.7931-0.36250.29880.06560.2234-0.1211-0.3413-0.167-0.28270.4261-0.1253-0.01010.29430.09670.07970.3470.09880.26139.89688.511-38.794
320.9157-0.124-0.0040.6445-0.09350.822-0.2222-0.15680.0453-0.03360.18930.2994-0.108-0.20870.00120.37280.08890.01770.340.02580.358214.501140.926-43.495
330.3264-0.1301-0.06340.4314-0.41230.4471-0.1715-0.1993-0.00560.11370.05720.2625-0.1103-0.1084-0.00380.42110.1213-0.01090.2688-0.02630.239627.132146.839-34.591
340.5930.1549-0.12280.09850.11840.4138-0.1708-0.356-0.29670.37070.07490.11430.1467-0.42630.0190.35420.17020.06670.42560.0780.207728.816131.932-26.919
350.25150.29270.3960.20020.33130.5274-0.151-0.1146-0.306-0.10090.00310.00550.1153-0.1595-0.00150.28950.01970.07810.26760.07210.340324.038121.099-43.315
360.78450.09540.29710.98930.34370.2161-0.16030.1750.093-0.49990.05950.3103-0.3287-0.0467-0.13290.5644-0.0417-0.12460.37430.05550.27723.222148.755-74.348
370.3903-0.24240.03540.23460.0040.0144-0.22990.19040.2511-0.26420.04440.3267-0.38910.0677-0.01930.5968-0.0829-0.14370.4250.07220.425722.425152.722-75.451
380.7049-0.7369-0.58840.7960.63130.5022-0.59790.51390.007-0.1513-0.27130.36540.0776-0.2025-0.28820.5031-0.1024-0.15550.48560.06220.388213.572148.156-74.647
390.46390.23580.05930.22940.22230.2489-0.28040.2411-0.041-0.23880.2030.08080.1697-0.1564-0.0120.4403-0.094-0.05140.32170.02760.28218.166138.842-72.691
400.789-0.0204-0.00030.45460.40810.3472-0.19830.2625-0.0826-0.13820.16610.1343-0.14930.051500.3894-0.0631-0.02720.3216-0.00590.295426.048133.802-65.111
410.76930.54020.19390.62270.01050.5093-0.16020.26340.1434-0.1170.0490.1156-0.16560.1675-0.02880.395-0.09060.05370.3685-0.04530.275433.178130.559-70.246
420.73530.12190.1550.0385-0.08820.4661-0.22220.4611-0.006-0.15260.02850.0499-0.1830.222-0.00270.4689-0.1497-0.01020.39510.01640.244739.816140.352-73.522
430.41080.08290.11030.42120.2330.5778-0.32680.50750.2778-0.288-0.0442-0.0539-0.386-0.0851-0.1290.5614-0.1974-0.04870.41720.09480.300542.752151.659-77.975
440.1270.0341-0.12030.0123-0.03310.1007-0.14730.24260.254-0.05290.03460.0542-0.4535-0.1556-0.00370.6027-0.029-0.1270.31340.08090.41526.224160.624-64.215
450.7928-0.12440.16850.0881-0.00250.5825-0.17980.2980.9248-0.0992-0.11860.0473-0.71950.2502-0.0070.6588-0.1088-0.1370.32810.18980.494536.077165.635-69.423
460.03510.1267-0.1352-0.0243-0.21840.1952-0.0257-0.0017-0.1471-0.0159-0.0166-0.071-0.0607-0.053700.38320.0196-0.01070.3180.07050.4238-0.468105.648-30.647
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 56:98 )A56 - 98
3X-RAY DIFFRACTION3( CHAIN A AND RESID 99:148 )A99 - 148
4X-RAY DIFFRACTION4( CHAIN A AND RESID 149:214 )A149 - 214
5X-RAY DIFFRACTION5( CHAIN A AND RESID 215:248 )A215 - 248
6X-RAY DIFFRACTION6( CHAIN A AND RESID 249:279 )A249 - 279
7X-RAY DIFFRACTION7( CHAIN A AND RESID 280:298 )A280 - 298
8X-RAY DIFFRACTION8( CHAIN B AND RESID 3:23 )B3 - 23
9X-RAY DIFFRACTION9( CHAIN B AND RESID 24:55 )B24 - 55
10X-RAY DIFFRACTION10( CHAIN B AND RESID 56:70 )B56 - 70
11X-RAY DIFFRACTION11( CHAIN B AND RESID 71:98 )B71 - 98
12X-RAY DIFFRACTION12( CHAIN B AND RESID 99:148 )B99 - 148
13X-RAY DIFFRACTION13( CHAIN B AND RESID 149:171 )B149 - 171
14X-RAY DIFFRACTION14( CHAIN B AND RESID 172:226 )B172 - 226
15X-RAY DIFFRACTION15( CHAIN B AND RESID 227:248 )B227 - 248
16X-RAY DIFFRACTION16( CHAIN B AND RESID 249:279 )B249 - 279
17X-RAY DIFFRACTION17( CHAIN B AND RESID 280:298 )B280 - 298
18X-RAY DIFFRACTION18( CHAIN C AND RESID 2:23 )C2 - 23
19X-RAY DIFFRACTION19( CHAIN C AND RESID 24:55 )C24 - 55
20X-RAY DIFFRACTION20( CHAIN C AND RESID 56:70 )C56 - 70
21X-RAY DIFFRACTION21( CHAIN C AND RESID 71:148 )C71 - 148
22X-RAY DIFFRACTION22( CHAIN C AND RESID 149:226 )C149 - 226
23X-RAY DIFFRACTION23( CHAIN C AND RESID 227:248 )C227 - 248
24X-RAY DIFFRACTION24( CHAIN C AND RESID 249:279 )C249 - 279
25X-RAY DIFFRACTION25( CHAIN C AND RESID 280:298 )C280 - 298
26X-RAY DIFFRACTION26( CHAIN D AND RESID 3:55 )D3 - 55
27X-RAY DIFFRACTION27( CHAIN D AND RESID 56:98 )D56 - 98
28X-RAY DIFFRACTION28( CHAIN D AND RESID 99:148 )D99 - 148
29X-RAY DIFFRACTION29( CHAIN D AND RESID 149:229 )D149 - 229
30X-RAY DIFFRACTION30( CHAIN D AND RESID 230:248 )D230 - 248
31X-RAY DIFFRACTION31( CHAIN D AND RESID 249:298 )D249 - 298
32X-RAY DIFFRACTION32( CHAIN E AND RESID 3:148 )E3 - 148
33X-RAY DIFFRACTION33( CHAIN E AND RESID 149:214 )E149 - 214
34X-RAY DIFFRACTION34( CHAIN E AND RESID 215:248 )E215 - 248
35X-RAY DIFFRACTION35( CHAIN E AND RESID 249:298 )E249 - 298
36X-RAY DIFFRACTION36( CHAIN F AND RESID 2:23 )F2 - 23
37X-RAY DIFFRACTION37( CHAIN F AND RESID 24:55 )F24 - 55
38X-RAY DIFFRACTION38( CHAIN F AND RESID 56:70 )F56 - 70
39X-RAY DIFFRACTION39( CHAIN F AND RESID 71:98 )F71 - 98
40X-RAY DIFFRACTION40( CHAIN F AND RESID 99:148 )F99 - 148
41X-RAY DIFFRACTION41( CHAIN F AND RESID 149:171 )F149 - 171
42X-RAY DIFFRACTION42( CHAIN F AND RESID 172:214 )F172 - 214
43X-RAY DIFFRACTION43( CHAIN F AND RESID 215:248 )F215 - 248
44X-RAY DIFFRACTION44( CHAIN F AND RESID 249:279 )F249 - 279
45X-RAY DIFFRACTION45( CHAIN F AND RESID 280:298 )F280 - 298
46X-RAY DIFFRACTION46( CHAIN A AND RESID 308:308 ) OR ( CHAIN C AND RESID 308:308 ) OR ( CHAIN B AND RESID 311:311 ) OR ( CHAIN E AND RESID 307:307 ) OR ( CHAIN D AND RESID 310:310 ) OR ( CHAIN F AND RESID 310:310 )A308
47X-RAY DIFFRACTION46( CHAIN A AND RESID 308:308 ) OR ( CHAIN C AND RESID 308:308 ) OR ( CHAIN B AND RESID 311:311 ) OR ( CHAIN E AND RESID 307:307 ) OR ( CHAIN D AND RESID 310:310 ) OR ( CHAIN F AND RESID 310:310 )C308
48X-RAY DIFFRACTION46( CHAIN A AND RESID 308:308 ) OR ( CHAIN C AND RESID 308:308 ) OR ( CHAIN B AND RESID 311:311 ) OR ( CHAIN E AND RESID 307:307 ) OR ( CHAIN D AND RESID 310:310 ) OR ( CHAIN F AND RESID 310:310 )B311
49X-RAY DIFFRACTION46( CHAIN A AND RESID 308:308 ) OR ( CHAIN C AND RESID 308:308 ) OR ( CHAIN B AND RESID 311:311 ) OR ( CHAIN E AND RESID 307:307 ) OR ( CHAIN D AND RESID 310:310 ) OR ( CHAIN F AND RESID 310:310 )E307
50X-RAY DIFFRACTION46( CHAIN A AND RESID 308:308 ) OR ( CHAIN C AND RESID 308:308 ) OR ( CHAIN B AND RESID 311:311 ) OR ( CHAIN E AND RESID 307:307 ) OR ( CHAIN D AND RESID 310:310 ) OR ( CHAIN F AND RESID 310:310 )D310
51X-RAY DIFFRACTION46( CHAIN A AND RESID 308:308 ) OR ( CHAIN C AND RESID 308:308 ) OR ( CHAIN B AND RESID 311:311 ) OR ( CHAIN E AND RESID 307:307 ) OR ( CHAIN D AND RESID 310:310 ) OR ( CHAIN F AND RESID 310:310 )F310

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