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- PDB-7kpc: Dihydrodipicolinate synthase (DHDPS) from C.jejuni, E88Q mutant w... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7kpc
TitleDihydrodipicolinate synthase (DHDPS) from C.jejuni, E88Q mutant with pyruvate bound in the active site and L-lysine bound 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: 1.76 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: THE ALLOSTERIC SITE RESIDUE, E88 INTERACTS WITH THE INHIBITORS TO TRANSMIT THE ALLOSTERIC INHIBITION SIGNALS IN Cj.DHDPS BY FORMING A HYDROGEN BOND.
Authors: Saran, S. / Majdi Yazdi, M. / Chung, I. / Sanders, D.A.R.
History
DepositionNov 10, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 17, 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)212,00494
Polymers205,1066
Non-polymers6,89888
Water27,7251539
1
A: 4-hydroxy-tetrahydrodipicolinate synthase
D: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,92536
Polymers68,3692
Non-polymers2,55734
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7970 Å2
ΔGint-31 kcal/mol
Surface area21200 Å2
MethodPISA
2
B: 4-hydroxy-tetrahydrodipicolinate synthase
C: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,77831
Polymers68,3692
Non-polymers2,41029
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8400 Å2
ΔGint-12 kcal/mol
Surface area21460 Å2
MethodPISA
3
E: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,30027
Polymers68,3692
Non-polymers1,93225
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8170 Å2
ΔGint-13 kcal/mol
Surface area21380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.350, 231.610, 199.850
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 4 through 31 or (resid 32...
21(chain B and (resid 4 through 20 or (resid 21...
31(chain C and (resid 4 through 20 or (resid 21...
41(chain D and (resid 4 through 20 or (resid 21...
51(chain E and (resid 4 through 20 or (resid 21...
61(chain F and (resid 4 through 20 or (resid 21...

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
11ASNASNILEILE(chain A and (resid 4 through 31 or (resid 32...AA4 - 3116 - 43
12LYSLYSLYSLYS(chain A and (resid 4 through 31 or (resid 32...AA3244
13ASNASNPHEPHE(chain A and (resid 4 through 31 or (resid 32...AA4 - 29816 - 310
14ASNASNPHEPHE(chain A and (resid 4 through 31 or (resid 32...AA4 - 29816 - 310
15ASNASNPHEPHE(chain A and (resid 4 through 31 or (resid 32...AA4 - 29816 - 310
21ASNASNGLYGLY(chain B and (resid 4 through 20 or (resid 21...BB4 - 2016 - 32
22LYSLYSLYSLYS(chain B and (resid 4 through 20 or (resid 21...BB2133
23LYSLYSPHEPHE(chain B and (resid 4 through 20 or (resid 21...BB3 - 29815 - 310
24LYSLYSPHEPHE(chain B and (resid 4 through 20 or (resid 21...BB3 - 29815 - 310
25LYSLYSPHEPHE(chain B and (resid 4 through 20 or (resid 21...BB3 - 29815 - 310
26LYSLYSPHEPHE(chain B and (resid 4 through 20 or (resid 21...BB3 - 29815 - 310
31ASNASNGLYGLY(chain C and (resid 4 through 20 or (resid 21...CC4 - 2016 - 32
32LYSLYSLYSLYS(chain C and (resid 4 through 20 or (resid 21...CC2133
33ASPASPPHEPHE(chain C and (resid 4 through 20 or (resid 21...CC2 - 29814 - 310
34ASPASPPHEPHE(chain C and (resid 4 through 20 or (resid 21...CC2 - 29814 - 310
35ASPASPPHEPHE(chain C and (resid 4 through 20 or (resid 21...CC2 - 29814 - 310
36ASPASPPHEPHE(chain C and (resid 4 through 20 or (resid 21...CC2 - 29814 - 310
37ASPASPPHEPHE(chain C and (resid 4 through 20 or (resid 21...CC2 - 29814 - 310
41ASNASNGLYGLY(chain D and (resid 4 through 20 or (resid 21...DD4 - 2016 - 32
42LYSLYSLYSLYS(chain D and (resid 4 through 20 or (resid 21...DD2133
43LYSLYSPHEPHE(chain D and (resid 4 through 20 or (resid 21...DD3 - 29815 - 310
44LYSLYSPHEPHE(chain D and (resid 4 through 20 or (resid 21...DD3 - 29815 - 310
45LYSLYSPHEPHE(chain D and (resid 4 through 20 or (resid 21...DD3 - 29815 - 310
46LYSLYSPHEPHE(chain D and (resid 4 through 20 or (resid 21...DD3 - 29815 - 310
51ASNASNGLYGLY(chain E and (resid 4 through 20 or (resid 21...EE4 - 2016 - 32
52LYSLYSLYSLYS(chain E and (resid 4 through 20 or (resid 21...EE2133
53LYSLYSPHEPHE(chain E and (resid 4 through 20 or (resid 21...EE3 - 29815 - 310
54LYSLYSPHEPHE(chain E and (resid 4 through 20 or (resid 21...EE3 - 29815 - 310
55LYSLYSPHEPHE(chain E and (resid 4 through 20 or (resid 21...EE3 - 29815 - 310
56LYSLYSPHEPHE(chain E and (resid 4 through 20 or (resid 21...EE3 - 29815 - 310
57LYSLYSPHEPHE(chain E and (resid 4 through 20 or (resid 21...EE3 - 29815 - 310
61ASNASNGLYGLY(chain F and (resid 4 through 20 or (resid 21...FF4 - 2016 - 32
62LYSLYSLYSLYS(chain F and (resid 4 through 20 or (resid 21...FF2133
63ASPASPPHEPHE(chain F and (resid 4 through 20 or (resid 21...FF2 - 29814 - 310
64ASPASPPHEPHE(chain F and (resid 4 through 20 or (resid 21...FF2 - 29814 - 310
65ASPASPPHEPHE(chain F and (resid 4 through 20 or (resid 21...FF2 - 29814 - 310
66ASPASPPHEPHE(chain F and (resid 4 through 20 or (resid 21...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: 34184.273 Da / Num. of mol.: 6 / Mutation: E88Q
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, 1627 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.: 14 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 15 / Source method: obtained synthetically / Formula: C2H3O2 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 28 / Source method: obtained synthetically / Formula: C2H6O2 / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical
ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Formula: C6H14O4 / Feature type: SUBJECT OF INVESTIGATION
#7: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 12 / 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.: 3 / Source method: obtained synthetically / Formula: C3H8O3 / Feature type: SUBJECT OF INVESTIGATION
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1539 / 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: 2.51 Å3/Da / Density % sol: 50.91 %
Crystal growTemperature: 288.15 K / Method: microbatch / pH: 7.4
Details: 0.7 M Magnesium acetate, 10 % PEG 8000, 0.1 M Sodium acetate (pH 7.4), 60 mM L-lysine

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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: 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: 1.76→43.7 Å / Num. obs: 194466 / % possible obs: 99.7 % / Redundancy: 15 % / CC1/2: 0.999 / Net I/σ(I): 21.73
Reflection shellResolution: 1.76→1.82 Å / Rmerge(I) obs: 0.419 / Num. unique obs: 32180 / % possible all: 97.6

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Processing

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

4ly8


Resolution: 1.76→43.7 Å / SU ML: 0.17 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 16.11 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1686 9724 5 %
Rwork0.1418 184722 -
obs0.1431 194446 99.73 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 92.6 Å2 / Biso mean: 25.6572 Å2 / Biso min: 12.27 Å2
Refinement stepCycle: final / Resolution: 1.76→43.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13571 0 388 1539 15498
Biso mean--53.85 36.25 -
Num. residues----1783
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5052X-RAY DIFFRACTION5.504TORSIONAL
12B5052X-RAY DIFFRACTION5.504TORSIONAL
13C5052X-RAY DIFFRACTION5.504TORSIONAL
14D5052X-RAY DIFFRACTION5.504TORSIONAL
15E5052X-RAY DIFFRACTION5.504TORSIONAL
16F5052X-RAY DIFFRACTION5.504TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.76-1.780.28673120.23725911622396
1.78-1.80.25463130.21245951626498
1.8-1.820.24133190.18916065638499
1.82-1.850.22593210.17626095641699
1.85-1.870.20563230.170861466469100
1.87-1.90.22233240.180661546478100
1.9-1.920.22073200.168360776397100
1.92-1.950.19653200.155660876407100
1.95-1.980.2113260.1561766502100
1.98-2.010.20193220.138261256447100
2.01-2.050.1743220.131161226444100
2.05-2.090.17993250.137561696494100
2.09-2.130.1853230.134761426465100
2.13-2.170.16933230.127561306453100
2.17-2.220.16423240.129961576481100
2.22-2.270.16563220.131361266448100
2.27-2.330.16673250.129161736498100
2.33-2.390.18163240.136661526476100
2.39-2.460.18033240.136961496473100
2.46-2.540.15333250.134161786503100
2.54-2.630.15863240.131961646488100
2.63-2.730.17113260.133861986524100
2.73-2.860.17413260.139961786504100
2.86-3.010.14683250.143861776502100
3.01-3.20.1743260.144161936519100
3.2-3.440.17773270.149762216548100
3.44-3.790.1593270.1462196546100
3.79-4.340.13173300.127162676597100
4.34-5.460.14933320.131263096641100
5.47-43.70.14683440.15265116855100
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)
11.22490.38280.20332.0147-0.83791.5996-0.0115-0.0520.14620.16560.06020.2237-0.0787-0.0564-0.06850.17350.0470.0040.18530.04270.2228-76.087-65.40219.89
21.7412-0.1054-0.09924.9325-0.97672.95060.0039-0.07-0.04090.1310.16410.74480.0748-0.3657-0.1530.14550.03540.02290.25540.05120.2705-84.644-69.48218.066
30.9863-0.5695-0.16732.07580.12340.7445-0.02610.04680.0215-0.07120.05070.19910.0225-0.1235-0.02220.1181-0.0145-0.01930.15420.05130.1518-75.631-79.2178.659
40.52510.0123-0.15611.33670.34990.6687-0.02970.05950.0679-0.03030.04540.00530.0152-0.0409-0.00770.14080.0024-0.01530.17590.04480.1702-63.134-70.0945.519
51.55980.2172-0.11882.2375-2.09744.38420.00280.01710.18590.0837-0.0863-0.1905-0.21650.14290.04180.15150.031-0.01410.15540.00140.209-55.29-60.8714.537
60.33910.4137-0.17772.3376-0.57250.7751-0.0002-0.12910.0250.40160.0529-0.0146-0.1401-0.0346-0.04260.26060.0217-0.00190.21340.0180.1842-65.401-66.11831.08
71.44260.05480.13432.2010.03541.01910.01420.12550.0452-0.153-0.0735-0.27150.0610.12910.06270.1374-0.01630.03470.19170.06580.2088-25.514-78.395-2.423
80.95680.0562-0.61261.0044-0.34461.5955-0.0117-0.03630.12180.0468-0.028-0.1736-0.04830.17080.04340.1174-0.009-0.03860.1460.03930.2018-27.925-76.04313.698
90.4323-0.20790.04840.5117-0.11171.7348-0.04180.03620.12790.03270.0064-0.0751-0.0321-0.01720.02950.1489-0.015-0.0180.16340.03690.218-40.524-68.6167.675
101.4252-0.1836-0.15875.47950.14781.0176-0.00430.11630.1443-0.24980.04110.1899-0.0482-0.1112-0.03670.1687-0.0150.00150.21650.05680.176-48.537-71.658-4.939
111.7330.01480.03253.468-1.08532.4599-0.00580.19640.0431-0.4401-0.0177-0.03680.2267-0.02870.01280.21980.00250.0050.18910.01150.1622-38.295-88.247-8.874
120.74930.1809-0.13181.5251-0.24341.32120.0176-0.139-0.04180.1158-0.0906-0.2046-0.0070.12070.08120.16390.0192-0.0340.21810.0710.2152-24.576-100.62630.078
132.2879-0.05660.50444.592-1.30193.12350.06770.04710.1009-0.074-0.1703-0.54450.01360.37370.14040.14080.0266-0.00270.24470.04950.2883-17.216-100.63723.538
140.8972-0.19660.37570.767-0.36331.2363-0.00350.066-0.0567-0.0785-0.0577-0.14430.09930.13530.06360.16210.01130.01760.14970.0390.1827-29.684-102.3513.729
150.43190.12960.21410.5257-0.09221.2961-0.034-0.0464-0.0891-0.04090.0078-0.0280.08480.00530.02360.18670.01170.00370.17380.03460.2028-41.83-107.66720.552
161.6268-0.2255-0.02412.81820.10130.7714-0.026-0.1974-0.15650.1323-0.02370.01090.09290.0040.05310.20070.0129-0.00770.23230.0620.156-42.629-106.25437.277
170.92030.28820.02152.305-0.86131.94950.0006-0.2188-0.03660.3622-0.0692-0.1311-0.17260.08930.06940.2411-0.0017-0.04130.24140.02480.1923-31.92-89.1938.235
181.1556-0.30510.10761.6579-0.10321.71280.0672-0.004-0.0504-0.05530.06450.31260.091-0.2669-0.12040.1654-0.03980.00150.22440.06940.2483-80.329-104.68622.598
191.09510.96340.01364.7128-0.25161.11420.0319-0.2201-0.05370.23810.00430.33440.0509-0.2852-0.04770.1573-0.00410.04530.26350.0850.2032-80.579-96.8731.815
200.5748-0.0430.14021.0575-0.18870.5312-0.0351-0.1002-0.03250.12260.05410.0689-0.0434-0.0756-0.01270.17980.00310.01040.1910.04480.1482-65.195-96.46932.002
211.5298-0.16970.09811.3071-1.39672.9252-0.019-0.0324-0.17450.02760.0021-0.0180.05520.07970.01750.1846-0.01870.00350.14610.01560.211-60.225-114.52122.626
220.3912-0.49280.00692.6916-0.4331.38540.05150.0439-0.0894-0.20230.06050.32050.1134-0.1533-0.09110.2221-0.0262-0.05190.20310.03750.2226-74.159-102.9588.373
231.84780.0101-0.00943.1893-1.29772.1676-0.02820.0665-0.2027-0.38220.0904-0.05230.2642-0.0405-0.11060.3086-0.0188-0.03680.2084-0.01410.235-67.457-112.3856.496
242.0845-1.2956-0.80383.24761.46953.41-0.08270.0576-0.1159-0.0053-0.05620.3109-0.0356-0.30860.13010.162-0.023-0.03380.26580.03310.2133-28.723-134.66839.53
251.18430.2591-0.08781.0019-0.36022.759-0.02990.18790.1383-0.0950.05980.1714-0.0335-0.2496-0.02360.162-0.0039-0.04090.24790.02240.2112-29.746-131.73638.258
262.58270.12911.47722.3535-0.18916.7880.0173-0.2282-0.05780.07310.0710.33510.1978-0.9805-0.14350.1527-0.0386-0.01590.34910.01680.2782-36.39-137.18143.276
271.5035-0.61890.35271.3468-0.38561.3965-0.0330.1052-0.1152-0.0580.04020.16490.2257-0.2188-0.01450.2316-0.0641-0.00320.2203-0.02180.1845-25.17-148.99644.283
281.5037-0.1479-0.39832.6937-0.35041.6098-0.11260.0968-0.1626-0.03240.0660.22110.279-0.17190.06020.2764-0.0475-0.00070.2042-0.02280.1751-17.605-153.65737.525
290.9424-0.2376-0.2611.2586-0.20970.6302-0.05270.1773-0.0104-0.15030.0230.01750.1181-0.11650.02140.2127-0.0432-0.02940.22890.00040.1586-14.746-141.49128.997
302.2182-0.0983-0.77592.422.37315.8367-0.03190.29920.099-0.2026-0.0094-0.0117-0.0706-0.1067-0.01520.1774-0.0036-0.03540.20180.0430.1857-10.057-130.2728.764
310.17190.3521-0.41621.2378-0.752.92590.02190.10720.1630.00910.01460.0958-0.2182-0.2271-0.0250.18690.03-0.01680.21360.01750.2074-21.066-123.74746.165
322.0841-0.0628-0.1911.6396-0.59622.59630.10120.18560.16510.10790.05980.0477-0.12160.0427-0.02550.20530.0255-0.01560.16540.05320.2543-14.996-118.35736.434
331.83930.70391.12712.65390.58731.96520.1471-0.1496-0.16850.0708-0.08880.02610.3141-0.2366-0.00880.268-0.03640.04650.21920.01070.1686-20.532-149.73572.617
341.5628-0.39951.10271.03750.06512.2147-0.0224-0.1606-0.21130.16810.0350.13190.231-0.2332-0.03130.2836-0.04540.0460.2090.01420.1902-20.836-152.66174.25
353.51550.07971.81052.8914-0.01626.3211-0.0498-0.16160.08090.0394-0.06840.23470.0528-0.68610.10990.2394-0.02710.05010.2708-0.00850.2114-29.138-147.22572.79
361.2481-0.18070.09232.0049-1.94584.1488-0.0375-0.13060.07580.15750.01660.1380.0267-0.2338-0.02770.1988-0.0220.02680.1997-0.03830.1876-25.014-138.92371.92
371.15420.1373-0.04770.8443-0.06481.1012-0.0228-0.07660.02910.063800.08260.0758-0.02980.020.18510.00390.00010.1576-0.00690.1654-16.969-134.05464.193
382.0027-0.5886-0.02211.2466-0.63630.5288-0.0202-0.08980.12350.1232-0.006-0.02490.0142-0.0110.03890.19330-0.01380.1828-0.01810.1477-6.325-132.33870.247
391.28760.3849-0.01140.821-0.17230.3713-0.0316-0.1476-0.0440.0688-0.0201-0.00280.15290.07480.04580.25460.0160.00180.19850.01070.1564-4.392-147.22774.122
401.65580.07760.04621.50940.40951.6824-0.0924-0.2232-0.0430.1430.0113-0.08360.09620.05690.06540.29520.0454-0.00260.21910.03620.2043-0.71-152.02177.356
411.2062-0.56531.53361.4441-0.09372.23120.0289-0.1651-0.18430.0920.02640.09680.4753-0.2569-0.05060.3302-0.04370.02280.1890.00530.2111-17.018-160.82863.298
422.38920.14850.13361.5971-0.24932.83850.1008-0.0083-0.455-0.0092-0.02090.01150.72670.1606-0.04830.40370.013-0.01110.16840.02060.3032-7.807-166.06168.552
430.4241-0.2340.32360.3467-0.31460.1434-0.0862-0.07020.06270.03490.10070.0152-0.0097-0.0585-0.04330.18640.02460.01660.1756-0.01470.1178-43.161-105.83630.117
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 4:55 )A4 - 55
2X-RAY DIFFRACTION2( CHAIN A AND RESID 56:70 )A56 - 70
3X-RAY DIFFRACTION3( CHAIN A AND RESID 71:148 )A71 - 148
4X-RAY DIFFRACTION4( CHAIN A AND RESID 149:226 )A149 - 226
5X-RAY DIFFRACTION5( CHAIN A AND RESID 227:248 )A227 - 248
6X-RAY DIFFRACTION6( CHAIN A AND RESID 249:298 )A249 - 298
7X-RAY DIFFRACTION7( CHAIN B AND RESID 3:70 )B3 - 70
8X-RAY DIFFRACTION8( CHAIN B AND RESID 71:148 )B71 - 148
9X-RAY DIFFRACTION9( CHAIN B AND RESID 149:226 )B149 - 226
10X-RAY DIFFRACTION10( CHAIN B AND RESID 227:248 )B227 - 248
11X-RAY DIFFRACTION11( CHAIN B AND RESID 249:298 )B249 - 298
12X-RAY DIFFRACTION12( CHAIN C AND RESID 3:55 )C3 - 55
13X-RAY DIFFRACTION13( CHAIN C AND RESID 56:70 )C56 - 70
14X-RAY DIFFRACTION14( CHAIN C AND RESID 71:148 )C71 - 148
15X-RAY DIFFRACTION15( CHAIN C AND RESID 149:214 )C149 - 214
16X-RAY DIFFRACTION16( CHAIN C AND RESID 215:248 )C215 - 248
17X-RAY DIFFRACTION17( CHAIN C AND RESID 249:298 )C249 - 298
18X-RAY DIFFRACTION18( CHAIN D AND RESID 3:70 )D3 - 70
19X-RAY DIFFRACTION19( CHAIN D AND RESID 71:98 )D71 - 98
20X-RAY DIFFRACTION20( CHAIN D AND RESID 99:214 )D99 - 214
21X-RAY DIFFRACTION21( CHAIN D AND RESID 215:248 )D215 - 248
22X-RAY DIFFRACTION22( CHAIN D AND RESID 249:279 )D249 - 279
23X-RAY DIFFRACTION23( CHAIN D AND RESID 280:298 )D280 - 298
24X-RAY DIFFRACTION24( CHAIN E AND RESID 3:23 )E3 - 23
25X-RAY DIFFRACTION25( CHAIN E AND RESID 24:55 )E24 - 55
26X-RAY DIFFRACTION26( CHAIN E AND RESID 56:70 )E56 - 70
27X-RAY DIFFRACTION27( CHAIN E AND RESID 71:148 )E71 - 148
28X-RAY DIFFRACTION28( CHAIN E AND RESID 149:171 )E149 - 171
29X-RAY DIFFRACTION29( CHAIN E AND RESID 172:229 )E172 - 229
30X-RAY DIFFRACTION30( CHAIN E AND RESID 230:248 )E230 - 248
31X-RAY DIFFRACTION31( CHAIN E AND RESID 249:279 )E249 - 279
32X-RAY DIFFRACTION32( CHAIN E AND RESID 280:298 )E280 - 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 149:191 )F149 - 191
39X-RAY DIFFRACTION39( CHAIN F AND RESID 192:214 )F192 - 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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