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- PDB-7kxh: 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: 7kxh
TitleDihydrodipicolinate synthase (DHDPS) from C.jejuni with pyruvate bound in the active site and R,R-bislysine bound at the allosteric site in C2221 space group
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
Chem-3VN / 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: 1.94 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: B-FACTOR ANALYSIS SUGGEST THAT L-LYSINE AND R, R-BISLYSINE ALLOSTERICALLY INHIBIT Cj.DHDPS ENZYME BY DECREASING PROTEIN DYNAMICS.
Authors: Saran, S. / Sanders, D.A.R.
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)209,01851
Polymers205,1126
Non-polymers3,90645
Water15,295849
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)139,34235
Polymers136,7414
Non-polymers2,60131
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16310 Å2
ΔGint-77 kcal/mol
Surface area39560 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)139,35132
Polymers136,7414
Non-polymers2,61028
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_555-x,y,-z+1/21
Buried area14130 Å2
ΔGint-63 kcal/mol
Surface area38640 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.090, 231.560, 198.620
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 290 or (resid 291...
31(chain C and (resid 3 through 31 or (resid 32...
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 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
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
21LYSLYSMETMET(chain B and (resid 3 through 290 or (resid 291...BB3 - 29015 - 302
22LYSLYSLYSLYS(chain B and (resid 3 through 290 or (resid 291...BB291303
23LYSLYSPHEPHE(chain B and (resid 3 through 290 or (resid 291...BB3 - 29815 - 310
24LYSLYSPHEPHE(chain B and (resid 3 through 290 or (resid 291...BB3 - 29815 - 310
25LYSLYSPHEPHE(chain B and (resid 3 through 290 or (resid 291...BB3 - 29815 - 310
26LYSLYSPHEPHE(chain B and (resid 3 through 290 or (resid 291...BB3 - 29815 - 310
27LYSLYSPHEPHE(chain B and (resid 3 through 290 or (resid 291...BB3 - 29815 - 310
28LYSLYSPHEPHE(chain B and (resid 3 through 290 or (resid 291...BB3 - 29815 - 310
29LYSLYSPHEPHE(chain B and (resid 3 through 290 or (resid 291...BB3 - 29815 - 310
31LYSLYSILEILE(chain C and (resid 3 through 31 or (resid 32...CC3 - 3115 - 43
32LYSLYSLYSLYS(chain C and (resid 3 through 31 or (resid 32...CC3244
33LYSLYSPHEPHE(chain C and (resid 3 through 31 or (resid 32...CC3 - 29815 - 310
34LYSLYSPHEPHE(chain C and (resid 3 through 31 or (resid 32...CC3 - 29815 - 310
35LYSLYSPHEPHE(chain C and (resid 3 through 31 or (resid 32...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
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
56LYSLYSPHEPHE(chain E and (resid 3 through 31 or (resid 32...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
66ASPASPPHEPHE(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 , 7 types, 894 molecules

#2: Chemical ChemComp-3VN / (2R,5R)-2,5-diamino-2,5-bis(4-aminobutyl)hexanedioic acid / bis-Lysine


Mass: 318.412 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C14H30N4O4 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 10 / 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-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 9 / 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.: 5 / Source method: obtained synthetically / Formula: C4H10O3 / Feature type: SUBJECT OF INVESTIGATION
#7: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C2H6O2 / Feature type: SUBJECT OF INVESTIGATION
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 849 / 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: 2.38 Å3/Da / Density % sol: 48.43 %
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), 120 mM R,R-bislysine

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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: Oct 29, 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: 1.94→43.58 Å / Num. obs: 144548 / % possible obs: 99.93 % / Redundancy: 15 % / CC1/2: 0.99 / Net I/σ(I): 16.2
Reflection shellResolution: 1.94→2.009 Å / Rmerge(I) obs: 0.384 / Num. unique obs: 14317 / % possible all: 99.93

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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: 1.94→43.58 Å / SU ML: 0.22 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 19.54 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.192 7225 5 %
Rwork0.1644 137298 -
obs0.1658 144523 99.94 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 90.41 Å2 / Biso mean: 36.827 Å2 / Biso min: 15.63 Å2
Refinement stepCycle: final / Resolution: 1.94→43.58 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13662 0 255 849 14766
Biso mean--54.91 42.12 -
Num. residues----1777
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5358X-RAY DIFFRACTION1.653TORSIONAL
12B5358X-RAY DIFFRACTION1.653TORSIONAL
13C5358X-RAY DIFFRACTION1.653TORSIONAL
14D5358X-RAY DIFFRACTION1.653TORSIONAL
15E5358X-RAY DIFFRACTION1.653TORSIONAL
16F5358X-RAY DIFFRACTION1.653TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork
1.94-1.960.34982400.31614554
1.96-1.990.31972380.29764523
1.99-2.010.27732380.24594524
2.01-2.030.27152390.22994545
2.03-2.060.26782400.22114551
2.06-2.090.24822390.21394537
2.09-2.120.23962380.19564521
2.12-2.150.2142370.18024509
2.15-2.180.21442410.17644583
2.18-2.220.20852380.17544517
2.22-2.260.22922400.17574554
2.26-2.30.23092410.17294580
2.3-2.340.21542370.16884510
2.34-2.390.18572400.15914566
2.39-2.440.22262390.15724544
2.44-2.50.20022420.15854578
2.5-2.560.20152390.14914551
2.56-2.630.17492400.14324571
2.63-2.710.1812390.15154549
2.71-2.80.20452410.15114583
2.8-2.90.21562400.16154558
2.9-3.010.18822420.16264595
3.01-3.150.16772420.15874598
3.15-3.320.17952410.16494568
3.32-3.520.18782430.15964624
3.52-3.80.16262410.16124588
3.8-4.180.17922440.14674626
4.18-4.780.15872450.14174668
4.78-6.020.18232460.16724678
6.02-100.18052550.16024845
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)
11.41480.2625-0.80041.6239-0.25242.74240.0821-0.11030.05770.23090.09580.2523-0.0396-0.1022-0.21210.3080.06990.03120.28480.05760.3546-76.0329-67.33918.5943
22.45530.8905-0.45631.421-0.5652.5718-0.1759-0.22160.09470.17780.16360.3764-0.1413-0.2329-0.01240.27210.09790.02350.29290.03860.2807-76.3211-64.637520.4281
31.90361.2565-0.75047.2723-2.21693.1131-0.0814-0.16530.0640.22790.45850.8336-0.1025-0.6762-0.33820.25250.06540.04890.4180.07690.4288-84.7232-69.590918.226
41.1718-0.59790.3843.63770.13640.9793-0.0634-0.0183-0.0874-0.26540.11280.41480.0277-0.2326-0.05190.22430.00680.00990.31770.07660.3482-81.7191-73.770110.682
50.3620.0982-0.20731.0587-0.06150.3158-0.07330.03530.0217-0.04110.06670.11140.0052-0.07330.00770.24290.013-0.00830.27520.04790.2666-67.4808-76.52856.0377
61.7687-0.26130.32641.9284-1.13923.06630.0060.02570.25920.10980.0121-0.0817-0.21860.25280.01920.23830.0217-0.01940.2414-0.00460.3194-57.5369-59.520213.509
71.5620.17040.1432.8222-0.69921.97410.0026-0.260.06890.74170.0347-0.2098-0.22570.0156-0.08990.40390.0430.01150.3470.00250.3064-65.2329-66.037331.3483
81.0324-0.23360.19981.8762-0.25541.1411-0.04490.1539-0.0129-0.3215-0.026-0.22470.10090.16790.01750.2795-0.02520.05610.32150.06850.352-27.6449-78.313-3.3254
98.21080.9097-0.60014.45432.80643.83780.0835-0.1681-0.26080.0077-0.018-0.5350.35750.3549-0.04730.1538-0.0060.03620.31330.02210.3533-19.0447-79.08380.6177
100.4739-0.21490.02510.8599-0.30160.5174-0.0567-0.02020.10420.0621-0.0006-0.1691-0.01410.07320.0520.2319-0.0128-0.01930.26560.03370.3109-34.2455-72.286610.7321
111.45630.18810.00235.9824-0.13331.0294-0.12230.20.2665-0.17240.13550.1003-0.1186-0.1675-0.07970.2346-0.01980.00130.29840.06010.26-48.7534-71.864-4.8543
121.755-0.3160.24072.9522-1.24032.39970.00540.2779-0.1071-0.43680.0141-0.00040.221-0.11450.01910.3638-0.01970.0170.2998-0.00520.2541-38.4866-88.4695-8.9718
130.89230.3964-0.34151.9901-0.2810.96270.0358-0.2048-0.01890.263-0.0912-0.2453-0.02410.14070.03150.26670.0324-0.03260.3560.09230.3274-24.4239-100.793929.9765
140.87590.03010.36961.3348-0.37221.57950.00050.038-0.1006-0.1177-0.0435-0.20110.11790.17790.04270.23780.03020.03810.25780.05330.3088-27.4282-102.449815.4171
150.60260.32710.0740.6492-0.04951.144-0.0561-0.1042-0.1324-0.03680.0125-0.03690.0934-0.01670.04230.26980.0280.00630.25730.05360.306-41.2116-108.177522.9252
161.10460.31110.07085.90260.15830.9677-0.0079-0.2389-0.1190.53390.07960.04510.0776-0.0237-0.13320.31410.0294-0.00980.41320.07430.2648-44.9019-104.411437.3169
170.85850.1468-0.18722.2491-0.95351.99150.0099-0.2893-0.02080.475-0.0322-0.1233-0.25350.04860.0090.3860.0015-0.04540.40940.03430.3167-31.7737-89.168938.1185
181.8041-0.16051.48471.8567-0.43523.42670.1644-0.1832-0.2101-0.00310.1620.38940.1138-0.3181-0.2560.2336-0.00790.03530.34760.11310.3464-78.0874-104.401622.7259
191.2667-1.06560.02093.5457-1.01761.58910.04030.0121-0.21940.03780.08470.41720.176-0.2596-0.10140.2639-0.058-0.01880.34740.08520.3893-79.1574-107.124821.0799
202.10550.62710.36854.35690.50442.09530.0203-0.20430.00730.49220.22951.1818-0.2066-0.5154-0.27720.28790.00370.07880.43580.11740.4788-85.9204-100.91725.2915
211.13120.429-0.19152.18660.13761.3773-0.044-0.2213-0.02920.34620.33060.4289-0.0033-0.2697-0.20440.28870.03340.08210.4020.150.3767-80.6041-96.947831.6883
220.60490.08450.33641.2264-0.22430.477-0.0377-0.1403-0.09460.2020.0750.0887-0.0526-0.102-0.02640.29730.01710.03740.34820.0870.281-65.16-98.507331.6083
231.5962-0.11860.07352.514-2.22564.3697-0.1011-0.0054-0.1832-0.0487-0.0806-0.21210.27480.18040.16440.2588-0.00980.02310.27130.0250.3635-58.0479-113.782420.6489
240.1308-0.3093-0.00563.4242-0.59371.7432-0.04270.08-0.0699-0.41460.15830.29070.1379-0.1742-0.09040.3257-0.0191-0.04440.32930.07280.3723-74.5139-102.958.3165
253.06490.6453-0.48954.692-1.73533.1180.09740.2555-0.1545-0.77930.1613-0.14110.4068-0.2353-0.2160.427-0.0126-0.04360.298-0.0070.3518-67.3392-112.62136.3527
261.4403-0.06140.30261.07560.01971.7682-0.02280.14840.0711-0.10240.02550.2964-0.04-0.2850.03350.3108-0.042-0.09120.37120.04220.346-29.4798-133.079438.5672
271.8288-0.15690.22522.8833-2.07018.01210.0648-0.1198-0.1552-0.0941-0.21060.4820.2933-1.00930.0320.2679-0.0738-0.06740.47860.03860.4444-36.557-137.512643.1839
280.759-0.4488-0.32781.0801-0.07061.1940.01360.1562-0.2022-0.09270.03380.21740.4629-0.2683-0.0540.4658-0.1092-0.08060.3603-0.01610.3657-23.5545-150.263942.3398
291.2478-0.5858-0.49281.9230.08390.82590.02330.203-0.1269-0.0998-0.02710.0530.256-0.1786-0.03620.3546-0.0521-0.07670.33680.00640.2711-14.8763-141.75629.4716
301.86320.17360.12082.76992.14185.2493-0.03850.2681-0.0505-0.41750.01760.17530.0895-0.1461-0.02820.3559-0.0021-0.05970.33320.04740.3459-10.7898-131.858526.7792
310.40530.5762-0.67341.6466-0.77012.92330.08020.0530.16740.0674-0.09010.0984-0.2164-0.1485-0.02430.32210.027-0.04220.29080.0110.3311-21.0254-123.953145.9827
323.2388-0.18950.83881.7246-0.87863.4745-0.12170.12020.47220.1-0.1465-0.0993-0.35760.00990.21980.33920.0133-0.02550.30270.05680.4447-15.157-118.746736.6279
332.01481.24340.85533.4041.06931.86820.1644-0.3066-0.12980.1505-0.14450.07160.4404-0.4805-0.00370.4741-0.0897-0.01480.35970.04250.28-20.5575-149.921572.3762
341.396-0.36480.92731.3386-0.18922.82840.0266-0.1739-0.2060.3664-0.08540.13570.3571-0.16970.04320.5489-0.1118-0.01230.3680.06470.3717-20.8978-152.753773.7847
351.23730.346-0.07982.242-0.84622.03850.0853-0.25880.00620.1559-0.02120.34910.0616-0.1919-0.06460.3366-0.04850.00970.35370.01480.2982-24.5159-140.94669.5139
361.366-0.09090.07931.0855-0.1480.79940.0127-0.16580.02890.1198-0.0250.02460.0782-0.07190.01350.331-0.0275-0.00910.284-0.0050.2545-13.1598-132.011666.2403
371.30170.4054-0.28091.558-0.18040.65020.0349-0.1412-0.08070.11830.01780.00520.2149-0.0141-0.06460.3860.0021-0.05760.29420.05170.2353-3.5485-143.129774.5028
382.24990.87790.95043.46771.79424.1685-0.1023-0.297-0.18910.48220.0401-0.19450.36040.29160.13080.48090.0136-0.03240.32360.09540.38971.2424-153.04974.9771
391.6749-0.12650.89531.7948-0.41212.42550.0161-0.184-0.48250.1970.0685-0.14260.643-0.0461-0.11350.6746-0.0688-0.07520.31790.0410.4962-13.1769-163.203365.2882
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 55 )A24 - 55
3X-RAY DIFFRACTION3chain 'A' and (resid 56 through 70 )A56 - 70
4X-RAY DIFFRACTION4chain 'A' and (resid 71 through 98 )A71 - 98
5X-RAY DIFFRACTION5chain 'A' and (resid 99 through 214 )A99 - 214
6X-RAY DIFFRACTION6chain 'A' and (resid 215 through 248 )A215 - 248
7X-RAY DIFFRACTION7chain 'A' and (resid 249 through 298 )A249 - 298
8X-RAY DIFFRACTION8chain 'B' and (resid 3 through 55 )B3 - 55
9X-RAY DIFFRACTION9chain 'B' and (resid 56 through 70 )B56 - 70
10X-RAY DIFFRACTION10chain 'B' and (resid 71 through 226 )B71 - 226
11X-RAY DIFFRACTION11chain 'B' and (resid 227 through 248 )B227 - 248
12X-RAY DIFFRACTION12chain 'B' and (resid 249 through 298 )B249 - 298
13X-RAY DIFFRACTION13chain 'C' and (resid 3 through 55 )C3 - 55
14X-RAY DIFFRACTION14chain 'C' and (resid 56 through 148 )C56 - 148
15X-RAY DIFFRACTION15chain 'C' and (resid 149 through 226 )C149 - 226
16X-RAY DIFFRACTION16chain 'C' and (resid 227 through 248 )C227 - 248
17X-RAY DIFFRACTION17chain 'C' and (resid 249 through 298 )C249 - 298
18X-RAY DIFFRACTION18chain 'D' and (resid 3 through 23 )D3 - 23
19X-RAY DIFFRACTION19chain 'D' and (resid 24 through 55 )D24 - 55
20X-RAY DIFFRACTION20chain 'D' and (resid 56 through 70 )D56 - 70
21X-RAY DIFFRACTION21chain 'D' and (resid 71 through 98 )D71 - 98
22X-RAY DIFFRACTION22chain 'D' and (resid 99 through 226 )D99 - 226
23X-RAY DIFFRACTION23chain 'D' and (resid 227 through 248 )D227 - 248
24X-RAY DIFFRACTION24chain 'D' and (resid 249 through 279 )D249 - 279
25X-RAY DIFFRACTION25chain 'D' and (resid 280 through 298 )D280 - 298
26X-RAY DIFFRACTION26chain 'E' and (resid 3 through 55 )E3 - 55
27X-RAY DIFFRACTION27chain 'E' and (resid 56 through 70 )E56 - 70
28X-RAY DIFFRACTION28chain 'E' and (resid 71 through 171 )E71 - 171
29X-RAY DIFFRACTION29chain 'E' and (resid 172 through 226 )E172 - 226
30X-RAY DIFFRACTION30chain 'E' and (resid 227 through 248 )E227 - 248
31X-RAY DIFFRACTION31chain 'E' and (resid 249 through 279 )E249 - 279
32X-RAY DIFFRACTION32chain 'E' and (resid 280 through 298 )E280 - 298
33X-RAY DIFFRACTION33chain 'F' and (resid 3 through 23 )F3 - 23
34X-RAY DIFFRACTION34chain 'F' and (resid 24 through 55 )F24 - 55
35X-RAY DIFFRACTION35chain 'F' and (resid 56 through 115 )F56 - 115
36X-RAY DIFFRACTION36chain 'F' and (resid 116 through 171 )F116 - 171
37X-RAY DIFFRACTION37chain 'F' and (resid 172 through 226 )F172 - 226
38X-RAY DIFFRACTION38chain 'F' and (resid 227 through 248 )F227 - 248
39X-RAY DIFFRACTION39chain 'F' and (resid 249 through 298 )F249 - 298

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