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- PDB-7koc: 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: 7koc
TitleDihydrodipicolinate synthase (DHDPS) from C.jejuni, E88Q mutant with pyruvate bound in the active 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 / 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: 2.06 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 8, 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

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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)206,77527
Polymers205,1066
Non-polymers1,66921
Water21,6181200
1
A: 4-hydroxy-tetrahydrodipicolinate synthase
C: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,06911
Polymers68,3692
Non-polymers7009
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4430 Å2
ΔGint-13 kcal/mol
Surface area21560 Å2
MethodPISA
2
B: 4-hydroxy-tetrahydrodipicolinate synthase
D: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,00710
Polymers68,3692
Non-polymers6388
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3600 Å2
ΔGint-32 kcal/mol
Surface area21820 Å2
MethodPISA
3
E: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,6996
Polymers68,3692
Non-polymers3304
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4190 Å2
ΔGint-14 kcal/mol
Surface area22100 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.250, 233.320, 202.330
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 31 or (resid 32...
21(chain B and (resid 3 through 31 or (resid 32...
31(chain C and (resid 3 through 86 or resid 88...
41(chain D and (resid 3 through 31 or (resid 32...
51(chain E and (resid 3 through 31 or (resid 32...
61(chain F and (resid 3 through 31 or (resid 32...

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
11LYSLYSILEILE(chain A and (resid 3 through 31 or (resid 32...AA3 - 3115 - 43
12LYSLYSLYSLYS(chain A and (resid 3 through 31 or (resid 32...AA3244
13LYSLYSPHEPHE(chain A and (resid 3 through 31 or (resid 32...AA3 - 29815 - 310
14LYSLYSPHEPHE(chain A and (resid 3 through 31 or (resid 32...AA3 - 29815 - 310
15LYSLYSPHEPHE(chain A and (resid 3 through 31 or (resid 32...AA3 - 29815 - 310
16LYSLYSPHEPHE(chain A and (resid 3 through 31 or (resid 32...AA3 - 29815 - 310
21LYSLYSILEILE(chain B and (resid 3 through 31 or (resid 32...BB3 - 3115 - 43
22LYSLYSLYSLYS(chain B and (resid 3 through 31 or (resid 32...BB3244
23LYSLYSPHEPHE(chain B and (resid 3 through 31 or (resid 32...BB3 - 29815 - 310
31LYSLYSTHRTHR(chain C and (resid 3 through 86 or resid 88...CC3 - 8615 - 98
32GLNGLNMETMET(chain C and (resid 3 through 86 or resid 88...CC88 - 290100 - 302
33LYSLYSLYSLYS(chain C and (resid 3 through 86 or resid 88...CC291303
34LYSLYSPHEPHE(chain C and (resid 3 through 86 or resid 88...CC3 - 29815 - 310
35LYSLYSPHEPHE(chain C and (resid 3 through 86 or resid 88...CC3 - 29815 - 310
36LYSLYSPHEPHE(chain C and (resid 3 through 86 or resid 88...CC3 - 29815 - 310
37LYSLYSPHEPHE(chain C and (resid 3 through 86 or resid 88...CC3 - 29815 - 310
38LYSLYSPHEPHE(chain C and (resid 3 through 86 or resid 88...CC3 - 29815 - 310
41LYSLYSILEILE(chain D and (resid 3 through 31 or (resid 32...DD3 - 3115 - 43
42LYSLYSLYSLYS(chain D and (resid 3 through 31 or (resid 32...DD3244
43LYSLYSPHEPHE(chain D and (resid 3 through 31 or (resid 32...DD3 - 29815 - 310
44LYSLYSPHEPHE(chain D and (resid 3 through 31 or (resid 32...DD3 - 29815 - 310
45LYSLYSPHEPHE(chain D and (resid 3 through 31 or (resid 32...DD3 - 29815 - 310
46LYSLYSPHEPHE(chain D and (resid 3 through 31 or (resid 32...DD3 - 29815 - 310
51LYSLYSILEILE(chain E and (resid 3 through 31 or (resid 32...EE3 - 3115 - 43
52LYSLYSLYSLYS(chain E and (resid 3 through 31 or (resid 32...EE3244
53LYSLYSPHEPHE(chain E and (resid 3 through 31 or (resid 32...EE3 - 29815 - 310
54LYSLYSPHEPHE(chain E and (resid 3 through 31 or (resid 32...EE3 - 29815 - 310
55LYSLYSPHEPHE(chain E and (resid 3 through 31 or (resid 32...EE3 - 29815 - 310
61LYSLYSILEILE(chain F and (resid 3 through 31 or (resid 32...FF3 - 3115 - 43
62LYSLYSLYSLYS(chain F and (resid 3 through 31 or (resid 32...FF3244
63LYSLYSPHEPHE(chain F and (resid 3 through 31 or (resid 32...FF3 - 29815 - 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 , 6 types, 1221 molecules

#2: Chemical
ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C6H14O4 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


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


Mass: 59.044 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H3O2 / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H10O3 / Feature type: SUBJECT OF INVESTIGATION
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1200 / 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: 2.45 Å3/Da / Density % sol: 49.85 %
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)

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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: Nov 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: 2.06→46.41 Å / Num. obs: 124406 / % possible obs: 100 % / Redundancy: 15 % / CC1/2: 0.999 / Net I/σ(I): 16.52
Reflection shellResolution: 2.06→2.134 Å / Rmerge(I) obs: 0.8667 / Num. unique obs: 12352 / % possible all: 99.98

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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: 2.06→46.41 Å / SU ML: 0.2 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 18.74 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1913 6218 5 %
Rwork0.163 118167 -
obs0.1644 124385 99.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 94.2 Å2 / Biso mean: 36.2649 Å2 / Biso min: 18.92 Å2
Refinement stepCycle: final / Resolution: 2.06→46.41 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13592 0 108 1200 14900
Biso mean--43.4 42.53 -
Num. residues----1776
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5322X-RAY DIFFRACTION5.188TORSIONAL
12B5322X-RAY DIFFRACTION5.188TORSIONAL
13C5322X-RAY DIFFRACTION5.188TORSIONAL
14D5322X-RAY DIFFRACTION5.188TORSIONAL
15E5322X-RAY DIFFRACTION5.188TORSIONAL
16F5322X-RAY DIFFRACTION5.188TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork
2.06-2.080.29172070.24353920
2.08-2.110.26752050.21523911
2.11-2.130.23462060.20913902
2.13-2.160.24632030.20123866
2.16-2.190.24042080.19843936
2.19-2.220.23392060.18813919
2.22-2.250.23332050.18263888
2.25-2.280.20442040.17123882
2.28-2.320.2052050.17023900
2.32-2.360.22132070.16213934
2.36-2.40.19322050.16373908
2.4-2.440.19152060.16593909
2.44-2.490.21282060.16323923
2.49-2.540.19542060.16453916
2.54-2.60.20332070.15943929
2.6-2.660.20322060.15953907
2.66-2.720.2122060.16353914
2.72-2.80.21352050.1693906
2.8-2.880.18052080.16743948
2.88-2.970.22842070.16743939
2.97-3.080.1932080.17053944
3.08-3.20.20112070.17033937
3.2-3.350.21522070.17683934
3.35-3.520.18042090.17443960
3.52-3.740.16892080.15723964
3.74-4.030.18352100.14473987
4.03-4.440.16772090.13913965
4.44-5.080.15252110.13314010
5.08-6.390.17682120.16724027
6.4-100.15342190.15054182
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)
11.1805-0.0726-0.19841.6650.31591.22470.03980.0548-0.0069-0.0767-0.0562-0.3650.1722-0.0086-0.00980.2312-0.00420.02880.29630.17470.386714.9137.8711-1.4848
21.0390.2230.15542.24390.05170.4266-0.01050.0931-0.05210.0422-0.1313-0.6007-0.03080.20280.13160.24830.00070.03510.36290.1620.461318.252737.5457-3.2045
30.53810.1319-0.05110.9454-0.47672.23160.0129-0.03810.13540.0762-0.1625-0.4014-0.1270.29770.10150.2247-0.0206-0.05490.31980.14110.410316.975140.136314.2026
40.5088-0.37410.1310.9292-0.25610.57850.00620.07160.16170.0501-0.0608-0.133-0.089-0.02240.06080.2302-0.033-0.02320.27770.11330.32073.581845.656611.1736
50.91560.0358-0.35771.9611-0.22770.60120.09030.19130.1708-0.2375-0.0562-0.0106-0.0277-0.0664-0.0450.26440.00390.01120.38960.1430.3263-3.486146.1333-5.3432
61.28730.0397-0.0581.624-0.56051.42470.01310.2325-0.1507-0.286-0.0209-0.09820.2469-0.03930.03540.2801-0.00060.01860.31340.09220.30254.245627.6398-8.721
71.1163-0.08720.47471.0161-0.311.1270.04080.01750.1940.16060.0170.2412-0.0639-0.1054-0.06080.27770.0190.01450.29190.09540.3404-33.478251.005119.5843
82.25570.3209-0.32233.2381-1.60923.69940.09650.2054-0.1133-0.22530.38410.92990.1944-0.9197-0.22050.2361-0.0115-0.01140.41840.11510.4398-42.644747.94518.3304
90.7345-1.00270.24786.58160.39660.59150.09280.1897-0.05840.0394-0.11090.73520.0044-0.0905-0.04280.2580.00870.01150.40150.10840.346-39.140142.295510.4603
101.1197-0.0306-0.01611.44690.02480.88980.07120.11650.0460.0021-0.04650.20040.129-0.0914-0.00060.2573-0.0155-0.01630.35210.07060.2619-30.292234.4667.8397
110.60450.015-0.29840.96790.41110.51930.02710.21720.163-0.0961-0.0010.0247-0.0098-0.0992-0.02740.24230.0114-0.02030.33210.10860.27-20.63543.73614.4676
121.5355-0.24690.11441.2171-0.21721.4298-0.00920.18320.42960.0568-0.0043-0.1211-0.14250.03990.0830.22340.0015-0.01290.28350.0970.3384-14.953156.777713.2107
130.33140.68360.05081.8627-0.54530.8527-0.0039-0.11820.10940.47650.06260.0343-0.1658-0.0262-0.01950.32850.00760.00920.30390.0580.2626-26.06447.087231.2043
143.2687-0.47150.34172.1371-0.06011.97330.03-0.350.44260.3461-0.0213-0.2823-0.04720.1-0.03060.3289-0.0408-0.04440.30660.01530.2908-17.422455.684930.7096
150.34360.0443-0.21040.60220.04280.72740.0593-0.0878-0.03470.1822-0.1391-0.3723-0.07190.08930.0830.2976-0.0322-0.09580.36330.19760.461417.692515.992231.1101
162.51260.5488-0.11756.3399-0.57882.46760.05770.3324-0.1667-0.70050.1037-0.59910.28380.1152-0.20050.2896-0.0086-0.03260.46230.20840.565525.695415.150525.8504
170.51610.03250.09031.1038-0.64471.1367-0.0895-0.0506-0.149-0.0595-0.0833-0.36820.05840.17250.1360.20640.0087-0.00720.27240.12290.371913.079113.929614.2391
180.80540.3347-0.00120.8699-0.08320.8542-0.0162-0.0357-0.1076-0.0573-0.033-0.08970.0359-0.00240.06290.2622-0.0225-0.02480.26190.1130.33130.7868.622721.0168
191.2532-0.3525-0.03262.1501-0.26440.6940.0553-0.4729-0.32610.412-0.05960.05560.1111-0.1755-0.01420.2687-0.0641-0.04910.36740.13660.3054-0.672710.230737.6652
200.60310.0631-0.22461.1835-0.58251.28520.095-0.29520.03580.4041-0.1748-0.1665-0.4225-0.02260.10570.3674-0.0817-0.12050.3960.1250.33769.801727.536138.7673
211.24010.19720.29081.4415-0.10651.83520.0840.0672-0.1724-0.13020.11720.31220.0062-0.2209-0.13820.2648-0.0476-0.01040.3590.10460.3483-35.557111.595222.1258
220.9207-0.3298-0.14421.5629-0.77851.63020.09540.0734-0.09440.0243-0.01410.37990.0355-0.3799-0.06140.2774-0.0938-0.00340.39310.07530.3944-39.14410.559921.9653
231.06680.09630.20181.46190.15961.557-0.0228-0.1349-0.04240.1640.03620.2661-0.132-0.283-0.00010.2501-0.02760.01630.31860.09880.2466-31.380723.530131.3995
240.4255-0.15070.09971.21630.33450.7075-0.0156-0.1076-0.11150.21010.0030.026-0.0254-0.12190.00640.2818-0.0482-0.0190.31430.11120.2781-19.150815.206232.451
251.8719-1.17710.43931.1031-0.42471.23390.0445-0.0936-0.44780.1078-0.1438-0.11220.3922-0.09230.19680.2781-0.07940.00150.27040.09940.3427-20.6701-0.810327.9444
262.189-0.32970.83771.9902-1.41683.4263-0.02280.0992-0.3576-0.0541-0.1807-0.24350.2707-0.09340.1090.2552-0.06160.0240.29160.04880.3492-15.42583.359218.7172
270.9703-0.52060.11242.5535-0.13440.96460.06720.1743-0.1584-0.43090.04820.12680.1343-0.018-0.11680.3007-0.0523-0.05070.33650.0430.3017-28.64719.39477.3836
281.1533-0.2399-0.26781.1756-0.15691.0337-0.277-0.57240.53170.30580.1722-0.3579-0.34340.07770.01950.53430.1409-0.19450.4411-0.15190.338862.597535.5101-26.1882
291.80911.7864-2.222.6583-1.03654.2918-0.2284-0.3348-0.14090.0461-0.2035-0.4822-0.05370.5265-0.14370.55730.1752-0.25890.59-0.11990.453371.517931.7831-25.8941
300.80960.3803-0.811.83691.89984.2044-0.382-0.51610.08390.31420.0611-0.3198-0.13710.26510.05290.42780.1318-0.10680.3828-0.0050.276866.968522.5783-28.27
311.57880.10550.28471.0380.02060.8034-0.2503-0.2986-0.08170.10710.1238-0.1513-0.1421-0.09420.13410.34910.0834-0.02340.24360.01780.2459.19617.7069-35.9902
321.9967-1.12820.60221.8942-0.84841.4772-0.2741-0.4117-0.12480.19990.1968-0.0292-0.1152-0.15450.06190.34120.10240.02520.34640.05110.19152.020714.4566-30.9481
331.90470.15810.19540.91440.83610.7888-0.3032-0.5101-0.0110.33740.2363-0.0609-0.1143-0.14060.08240.44760.1597-0.02510.4004-0.00550.207445.324124.2982-27.7105
340.68960.0976-0.20170.17280.06441.6253-0.4063-0.61170.37050.38460.1930.1178-0.3435-0.33680.08660.58030.2492-0.06080.5272-0.12880.300242.358235.5735-23.2321
350.5022-0.3104-0.39150.72030.94781.4094-0.2458-0.29740.70530.11270.0914-0.0244-0.5348-0.0436-0.13340.60010.1078-0.24380.2915-0.16510.527555.100946.6433-34.6931
361.59210.5827-0.27441.76190.21361.3356-0.17490.3686-0.1655-0.10950.1647-0.33790.04190.35680.02040.2634-0.08010.07510.3844-0.06530.327371.626617.7807-60.3236
371.64780.1243-0.19171.2346-0.07681.4386-0.17580.2465-0.2584-0.11930.2178-0.49480.00320.2746-0.04450.3167-0.08470.07660.3935-0.09490.441275.163116.5718-59.9412
381.7792-0.9544-0.82941.98870.37492.4715-0.40320.21840.07860.07530.1072-0.4372-0.22640.67150.31890.355-0.1453-0.00280.42020.01650.385775.561828.8575-57.1614
391.0967-0.09080.31241.08780.15711.3066-0.30270.26680.2618-0.1240.1331-0.2966-0.2840.21110.11880.4078-0.1119-0.05830.26920.05040.335162.884135.1381-57.1283
401.2410.25960.38660.5726-0.05930.6202-0.26420.38770.0788-0.19540.1513-0.0455-0.22240.14650.15420.4271-0.16690.01090.39150.0080.255356.764527.2035-68.7202
410.9749-0.0553-0.44650.6576-0.78682.0409-0.17710.6761-0.2068-0.25480.0774-0.1386-0.07630.28290.10080.3751-0.15540.07890.4917-0.09070.236256.605415.9008-74.1221
421.2057-0.21850.35211.06640.49692.3513-0.17410.333-0.40450.06030.1076-0.01570.22640.21510.06040.3082-0.00890.08250.2996-0.08950.409361.40464.9275-57.7491
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 23 )A3 - 23
2X-RAY DIFFRACTION2chain 'A' and (resid 24 through 70 )A24 - 70
3X-RAY DIFFRACTION3chain 'A' and (resid 71 through 129 )A71 - 129
4X-RAY DIFFRACTION4chain 'A' and (resid 130 through 214 )A130 - 214
5X-RAY DIFFRACTION5chain 'A' and (resid 215 through 248 )A215 - 248
6X-RAY DIFFRACTION6chain 'A' and (resid 249 through 298 )A249 - 298
7X-RAY DIFFRACTION7chain 'B' and (resid 3 through 55 )B3 - 55
8X-RAY DIFFRACTION8chain 'B' and (resid 56 through 70 )B56 - 70
9X-RAY DIFFRACTION9chain 'B' and (resid 71 through 98 )B71 - 98
10X-RAY DIFFRACTION10chain 'B' and (resid 99 through 148 )B99 - 148
11X-RAY DIFFRACTION11chain 'B' and (resid 149 through 214 )B149 - 214
12X-RAY DIFFRACTION12chain 'B' and (resid 215 through 248 )B215 - 248
13X-RAY DIFFRACTION13chain 'B' and (resid 249 through 279 )B249 - 279
14X-RAY DIFFRACTION14chain 'B' and (resid 280 through 298 )B280 - 298
15X-RAY DIFFRACTION15chain 'C' and (resid 3 through 55 )C3 - 55
16X-RAY DIFFRACTION16chain 'C' and (resid 56 through 70 )C56 - 70
17X-RAY DIFFRACTION17chain 'C' and (resid 71 through 148 )C71 - 148
18X-RAY DIFFRACTION18chain 'C' and (resid 149 through 214 )C149 - 214
19X-RAY DIFFRACTION19chain 'C' and (resid 215 through 248 )C215 - 248
20X-RAY DIFFRACTION20chain 'C' and (resid 249 through 298 )C249 - 298
21X-RAY DIFFRACTION21chain 'D' and (resid 3 through 23 )D3 - 23
22X-RAY DIFFRACTION22chain 'D' and (resid 24 through 70 )D24 - 70
23X-RAY DIFFRACTION23chain 'D' and (resid 71 through 148 )D71 - 148
24X-RAY DIFFRACTION24chain 'D' and (resid 149 through 214 )D149 - 214
25X-RAY DIFFRACTION25chain 'D' and (resid 215 through 229 )D215 - 229
26X-RAY DIFFRACTION26chain 'D' and (resid 230 through 248 )D230 - 248
27X-RAY DIFFRACTION27chain 'D' and (resid 249 through 298 )D249 - 298
28X-RAY DIFFRACTION28chain 'E' and (resid 3 through 55 )E3 - 55
29X-RAY DIFFRACTION29chain 'E' and (resid 56 through 70 )E56 - 70
30X-RAY DIFFRACTION30chain 'E' and (resid 71 through 98 )E71 - 98
31X-RAY DIFFRACTION31chain 'E' and (resid 99 through 148 )E99 - 148
32X-RAY DIFFRACTION32chain 'E' and (resid 149 through 171 )E149 - 171
33X-RAY DIFFRACTION33chain 'E' and (resid 172 through 214 )E172 - 214
34X-RAY DIFFRACTION34chain 'E' and (resid 215 through 248 )E215 - 248
35X-RAY DIFFRACTION35chain 'E' and (resid 249 through 298 )E249 - 298
36X-RAY DIFFRACTION36chain 'F' and (resid 3 through 23 )F3 - 23
37X-RAY DIFFRACTION37chain 'F' and (resid 24 through 70 )F24 - 70
38X-RAY DIFFRACTION38chain 'F' and (resid 71 through 99 )F71 - 99
39X-RAY DIFFRACTION39chain 'F' and (resid 100 through 171 )F100 - 171
40X-RAY DIFFRACTION40chain 'F' and (resid 172 through 214 )F172 - 214
41X-RAY DIFFRACTION41chain 'F' and (resid 215 through 248 )F215 - 248
42X-RAY DIFFRACTION42chain 'F' and (resid 249 through 298 )F249 - 298

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