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- PDB-7kr8: Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H56A mutant w... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7kr8
TitleDihydrodipicolinate synthase (DHDPS) from C.jejuni, H56A mutant with pyruvate bound in the active 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 / 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: 2.12 Å
AuthorsSaran, S. / Sanders, D.A.R.
Funding support Canada, 1items
OrganizationGrant numberCountry
Natural Sciences and Engineering Research Council (NSERC, Canada) Canada
CitationJournal: To Be Published
Title: ALLOSTERIC SITE RESIDUE 'H56' CAPS THE INHIBITOR AT THE TIGHT DIMER INTERFACE FOR TRANSMITTING THE ALLOSTERIC INHIBITION SIGNALS IN Cj.DHDPS
Authors: Saran, S. / Skovpen, Y. / Yazdi, M.M. / Palmer, D.R.J. / Sanders, D.A.R.
History
DepositionNov 19, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 24, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.2Nov 29, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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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)207,67545
Polymers204,7096
Non-polymers2,96639
Water18,0871004
1
A: 4-hydroxy-tetrahydrodipicolinate synthase
B: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,13713
Polymers68,2362
Non-polymers90011
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4710 Å2
ΔGint-18 kcal/mol
Surface area22060 Å2
MethodPISA
2
C: 4-hydroxy-tetrahydrodipicolinate synthase
E: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,05015
Polymers68,2362
Non-polymers81413
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5400 Å2
ΔGint-27 kcal/mol
Surface area21920 Å2
MethodPISA
3
D: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,48917
Polymers68,2362
Non-polymers1,25215
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5170 Å2
ΔGint-1 kcal/mol
Surface area22140 Å2
MethodPISA
Unit cell
Length a, b, c (Å)84.930, 231.650, 200.170
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 20 or (resid 21...
21(chain B and (resid 3 through 20 or (resid 21...
31(chain C and (resid 3 through 20 or (resid 21...
41(chain D and (resid 3 through 70 or (resid 71...
51(chain E and (resid 3 through 20 or (resid 21...
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
11LYSLYSGLYGLY(chain A and (resid 3 through 20 or (resid 21...AA3 - 2015 - 32
12LYSLYSLYSLYS(chain A and (resid 3 through 20 or (resid 21...AA2133
13ASPASPPHEPHE(chain A and (resid 3 through 20 or (resid 21...AA2 - 29814 - 310
14ASPASPPHEPHE(chain A and (resid 3 through 20 or (resid 21...AA2 - 29814 - 310
15ASPASPPHEPHE(chain A and (resid 3 through 20 or (resid 21...AA2 - 29814 - 310
21LYSLYSGLYGLY(chain B and (resid 3 through 20 or (resid 21...BB3 - 2015 - 32
22LYSLYSLYSLYS(chain B and (resid 3 through 20 or (resid 21...BB2133
23LYSLYSPHEPHE(chain B and (resid 3 through 20 or (resid 21...BB3 - 29815 - 310
24LYSLYSPHEPHE(chain B and (resid 3 through 20 or (resid 21...BB3 - 29815 - 310
25LYSLYSPHEPHE(chain B and (resid 3 through 20 or (resid 21...BB3 - 29815 - 310
26LYSLYSPHEPHE(chain B and (resid 3 through 20 or (resid 21...BB3 - 29815 - 310
31LYSLYSGLYGLY(chain C and (resid 3 through 20 or (resid 21...CC3 - 2015 - 32
32LYSLYSLYSLYS(chain C and (resid 3 through 20 or (resid 21...CC2133
33LYSLYSPHEPHE(chain C and (resid 3 through 20 or (resid 21...CC3 - 29815 - 310
34LYSLYSPHEPHE(chain C and (resid 3 through 20 or (resid 21...CC3 - 29815 - 310
35LYSLYSPHEPHE(chain C and (resid 3 through 20 or (resid 21...CC3 - 29815 - 310
36LYSLYSPHEPHE(chain C and (resid 3 through 20 or (resid 21...CC3 - 29815 - 310
41LYSLYSCYSCYS(chain D and (resid 3 through 70 or (resid 71...DD3 - 7015 - 82
42LYSLYSLYSLYS(chain D and (resid 3 through 70 or (resid 71...DD7183
43LYSLYSPHEPHE(chain D and (resid 3 through 70 or (resid 71...DD3 - 29815 - 310
44LYSLYSPHEPHE(chain D and (resid 3 through 70 or (resid 71...DD3 - 29815 - 310
45LYSLYSPHEPHE(chain D and (resid 3 through 70 or (resid 71...DD3 - 29815 - 310
46LYSLYSPHEPHE(chain D and (resid 3 through 70 or (resid 71...DD3 - 29815 - 310
51LYSLYSGLYGLY(chain E and (resid 3 through 20 or (resid 21...EE3 - 2015 - 32
52LYSLYSLYSLYS(chain E and (resid 3 through 20 or (resid 21...EE2133
53LYSLYSPHEPHE(chain E and (resid 3 through 20 or (resid 21...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
64LYSLYSPHEPHE(chain F and (resid 3 through 31 or (resid 32...FF3 - 29815 - 310
65LYSLYSPHEPHE(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: 34118.191 Da / Num. of mol.: 6 / Mutation: H56A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) (Campylobacter)
Strain: ATCC 700819 / NCTC 11168 / Gene: dapA, Cj0806 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9PPB4, 4-hydroxy-tetrahydrodipicolinate synthase

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Non-polymers , 6 types, 1043 molecules

#2: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: C2H6O2 / 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-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C2H3O2 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Mg / 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: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1004 / 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: 2.4 Å3/Da / Density % sol: 48.85 %
Crystal growTemperature: 288.15 K / Method: microbatch / pH: 7.4
Details: 0.3 M Magnesium acetate, 12 % PEG 8000, 0.1 M Sodium acetate (pH 7.4)

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Aug 1, 2019
RadiationMonochromator: Double beam / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.12→43.74 Å / Num. obs: 111734 / % possible obs: 99.9 % / Redundancy: 15 % / CC1/2: 0.998 / Net I/σ(I): 13.14
Reflection shellResolution: 2.12→2.196 Å / Rmerge(I) obs: 0.866 / Num. unique obs: 11025 / % 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: 2.12→43.74 Å / SU ML: 0.22 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 20.09 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2091 5587 5 %
Rwork0.1734 106132 -
obs0.1752 111719 99.94 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 131.8 Å2 / Biso mean: 33.7368 Å2 / Biso min: 18.2 Å2
Refinement stepCycle: final / Resolution: 2.12→43.74 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13564 0 191 1004 14759
Biso mean--59.68 39.67 -
Num. residues----1777
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5322X-RAY DIFFRACTION6.019TORSIONAL
12B5322X-RAY DIFFRACTION6.019TORSIONAL
13C5322X-RAY DIFFRACTION6.019TORSIONAL
14D5322X-RAY DIFFRACTION6.019TORSIONAL
15E5322X-RAY DIFFRACTION6.019TORSIONAL
16F5322X-RAY DIFFRACTION6.019TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork
2.12-2.140.27211820.24823462
2.14-2.170.27731850.23273519
2.17-2.20.28631840.22983493
2.2-2.220.27821850.22313499
2.22-2.250.26621840.21273502
2.25-2.280.25771860.21013538
2.28-2.320.23981840.20363491
2.32-2.350.28271850.19463523
2.35-2.390.25371840.19883498
2.39-2.430.23031860.19193523
2.43-2.470.24191850.1933511
2.47-2.510.22411840.18443514
2.51-2.560.24311850.17713515
2.56-2.610.21941860.17673529
2.61-2.670.22251850.17613516
2.67-2.730.20511860.17443522
2.73-2.80.21741850.17013521
2.8-2.880.22981850.18173518
2.88-2.960.22211860.1883523
2.96-3.060.22591860.1913542
3.06-3.170.21631860.17933534
3.17-3.290.20881860.18313536
3.29-3.440.22991870.18423548
3.44-3.620.21551880.17663569
3.62-3.850.18061870.15483563
3.85-4.150.17781860.1453539
4.15-4.570.15391900.13693593
4.57-5.230.16891890.14573598
5.23-6.580.17761910.17253635
6.58-100.19541990.15363758
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)
11.1379-0.1972-0.02651.2187-0.08721.23340.0007-0.14770.17570.0197-0.0218-0.0367-0.17330.11620.00670.28820.0223-0.01630.2721-0.00330.186519.768933.2266-26.5462
20.9561-0.1234-0.52890.8016-0.16491.2983-0.0689-0.15380.21630.1942-0.1062-0.2418-0.0240.19110.00460.346-0.0137-0.05440.2781-0.01480.258120.52137.2347-25.3918
31.63011.1505-1.49591.116-1.47935.5-0.2558-0.0916-0.11120.0847-0.314-0.35190.17540.60620.02540.29460.0162-0.03480.35370.02860.327329.125532.4196-25.641
40.3913-0.2628-0.23481.55111.86433.4190.0349-0.09790.09260.08690.118-0.2924-0.14610.333-0.03410.2781-0.0004-0.03270.29480.01060.266725.05622.9243-28.6395
50.8839-0.2132-0.02220.7576-0.06630.959-0.0494-0.0723-0.05610.03080.0165-0.0939-0.0729-0.02580.03150.25260.01320.00530.22840.00550.219414.498717.3526-34.0307
60.73890.26570.19050.88180.24350.428-0.0711-0.1124-0.0490.11010.01970.0278-0.00060.00520.02530.28680.02850.00760.2636-0.00370.20593.156925.0287-27.2354
71.03460.1219-0.04491.2414-0.49611.6193-0.1576-0.30410.19520.2957-0.0020.1553-0.153-0.0333-0.01380.37010.0755-0.00510.3226-0.03270.2550.304736.3248-22.6948
80.6443-0.5598-0.76970.77360.29161.1648-0.0635-0.16340.13460.10520.0655-0.0165-0.170.2233-0.01150.3516-0.0323-0.04860.2352-0.0130.245916.78545.2485-36.5405
91.5196-0.12520.30961.2105-0.17312.4582-0.156-0.13070.417-0.1136-0.17640.039-0.6778-0.17550.00020.45930.0666-0.03590.2846-0.0350.34297.118450.3153-31.2609
100.8079-0.0292-0.18550.81960.10910.97980.00250.0838-0.0848-0.01460.0447-0.19040.04840.13160.05250.2478-0.01480.04390.3156-0.02110.28329.419716.8193-61.2046
111.3161-0.0594-1.03251.33670.03565.1155-0.0474-0.43560.14930.165-0.1263-0.2906-0.23540.9215-0.010.2505-0.06380.03270.4669-0.00610.393237.158120.6189-57.161
120.9288-0.1758-0.62741.3720.26181.2991-0.09780.11010.09920.00630.0869-0.1899-0.12390.1772-0.00210.2748-0.0526-0.03360.3130.01190.251427.244333.43-54.8653
130.3766-0.05050.19240.66970.04230.7374-0.08420.06330.0072-0.05370.0425-0.0809-0.15080.07370.02360.2745-0.04510.020.2630.0070.211716.207631.6263-64.1427
141.02990.1679-0.1020.9069-0.29871.3488-0.00950.2654-0.0559-0.13890.0958-0.0372-0.09110.06720.01180.2685-0.03360.03790.3123-0.04540.243213.639916.5208-73.6655
150.0752-0.1117-0.00880.66630.74821.9076-0.03520.0171-0.17350.1117-0.07510.06740.20220.05760.03460.23980.01610.0430.2311-0.01250.269418.56315.6499-57.508
160.66430.1116-0.25531.42440.26770.67070.03970.08310.0606-0.1724-0.06520.3264-0.0631-0.0503-0.02890.2435-0.0009-0.04660.2645-0.05960.3181-14.766978.2863-103.7539
170.2190.29060.51210.9956-0.23551.01270.0049-0.0223-0.03950.0746-0.01440.3234-0.0295-0.1213-0.00840.1811-0.00360.03920.249-0.06130.3393-16.246376.4466-88.7906
180.2827-0.1943-0.1310.57830.27270.9242-0.01260.0246-0.08180.0454-0.01410.0921-0.00740.03730.00020.1764-0.02590.00620.2173-0.02540.2334-1.875368.7208-92.3399
190.91940.1385-0.00982.5021-0.23220.5709-0.14280.2679-0.149-0.1170.2421-0.21040.07980.15050.0070.24690.00170.01340.2941-0.07140.23696.227371.7481-105.0023
200.8963-0.23130.02551.45310.39861.0920.04780.1295-0.0206-0.3612-0.02840.044-0.21190.023-0.01610.3218-0.0111-0.00570.2612-0.00820.2223-3.851988.4545-109.1355
211.08850.0659-0.09231.17980.29490.74020.0086-0.0329-0.10250.19850.0803-0.30320.02880.15320.00570.24630.0351-0.01410.2357-0.04730.28533.469365.5835-80.4759
221.5991.0680.4576.61022.25992.77870.10220.09460.1548-0.30920.2455-0.6384-0.43580.5445-0.04210.2312-0.0424-0.0250.335-0.06070.42142.499768.5656-81.5499
230.4363-0.4825-0.12773.6979-0.52460.3166-0.0080.1069-0.0267-0.1089-0.1127-0.46480.08920.17150.00130.1956-0.00650.00040.3118-0.04740.369239.352974.0204-89.5438
240.5614-0.14130.12661.501-0.1950.6935-0.01970.0352-0.0480.03620.0461-0.1717-0.14980.0724-0.00480.2355-0.01440.02830.2475-0.03980.26530.52481.9181-92.1318
250.3621-0.04250.23350.9038-0.25050.3959-0.04280.0169-0.0739-0.03050.0798-0.0128-0.0230.01050.01240.211-0.00140.02380.2292-0.03970.221720.86772.6411-95.5054
260.6125-0.0567-0.25170.88620.4381.10950.0477-0.004-0.2864-0.02840.02830.15760.009-0.10770.01770.2217-0.00060.00270.2437-0.01320.301615.217459.6619-86.5766
270.27130.4402-0.12521.04110.23630.48770.1375-0.0238-0.010.4579-0.0571-0.14020.17240.00590.01420.3040.0268-0.04270.2351-0.02780.254626.214669.4858-68.6937
281.4183-0.5258-0.11371.93080.75191.0547-0.0812-0.247-0.12250.5840.08040.31660.3046-0.030.07260.3435-0.00070.02680.28850.01740.239817.616560.9637-69.0241
290.54670.0173-0.06561.39540.26680.8770.0946-0.02760.09720.0808-0.13940.43160.0731-0.1956-0.0210.2063-0.0110.04940.2951-0.08350.3367-19.7136100.6474-70.9362
300.12840.089-0.0411.01290.22151.3382-0.01240.02330.0017-0.081-0.09730.2018-0.0512-0.1618-0.0080.2119-0.0002-0.00470.2488-0.04580.2757-12.9372102.4811-86.2333
310.14350.1668-0.11410.62650.4850.798-0.0012-0.05480.0787-0.0526-0.02580.0488-0.05250.0458-0.02010.22390.0040.02190.235-0.03530.2354-1.3557108.0718-76.9925
320.83550.2343-0.10213.18750.12160.46730.0059-0.32730.150.37950.0163-0.01440.002-0.0444-0.01450.23930.02160.00250.3062-0.05170.23612.4419104.137-62.7595
330.30630.1884-0.11291.54580.59791.11950.1078-0.18880.07920.4143-0.14570.17820.41230.0675-0.0150.3744-0.04050.08850.309-0.0230.2501-10.41988.8749-61.8369
340.79490.0637-0.38841.21830.02141.21210.12310.01140.0078-0.10140.1352-0.277-0.18040.066-0.01780.229-0.01930.01430.2888-0.08390.322335.1567104.9978-77.4721
350.7324-0.6010.20991.46590.39071.06380.05930.01240.1133-0.1120.057-0.4045-0.07820.2237-0.01580.2438-0.05750.03910.3152-0.07250.353736.4672107.6672-79.3033
361.4049-0.4516-0.43111.54830.11941.84040.0225-0.4286-0.32560.44480.1468-0.37670.39660.5406-0.06540.27070.0015-0.05280.4313-0.12680.491443.8912102.6901-75.0865
370.33140.4528-0.31121.3683-0.0240.9216-0.0029-0.08770.03830.13320.0738-0.21630.10880.2187-0.00740.24620.0223-0.0360.301-0.06280.286531.202992.7948-68.5165
380.9942-0.19460.041.3772-0.51381.4588-0.0130.09490.02210.2138-0.0605-0.0772-0.05030.1625-0.00640.3228-0.01920.01030.2902-0.05530.241921.564295.3064-63.3601
390.4680.0931-0.06740.708-0.00780.3164-0.0283-0.07190.1048-0.03860.03220.03380.00360.0464-0.00920.2085-0.01890.01790.2277-0.05270.241418.2512108.0508-70.7653
401.1554-0.1528-0.64481.36941.09522.30890.06360.05490.1141-0.2051-0.25310.0969-0.2968-0.1514-0.00590.2565-0.02560.01050.2529-0.03080.311615.3764112.9497-81.5343
410.095-0.36180.07111.33450.13510.6307-0.0316-0.0956-0.0699-0.23420.2006-0.2358-0.17980.0599-0.00130.2824-0.04060.07490.2992-0.05060.306331.6997103.2208-91.9892
421.08050.18140.13711.95531.04711.4843-0.02220.14560.138-0.33770.1143-0.03080.02650.1130.04570.4001-0.03850.05220.34070.00330.358824.2051112.5619-94.0131
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 23 )A2 - 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 171 )A99 - 171
6X-RAY DIFFRACTION6chain 'A' and (resid 172 through 214 )A172 - 214
7X-RAY DIFFRACTION7chain 'A' and (resid 215 through 248 )A215 - 248
8X-RAY DIFFRACTION8chain 'A' and (resid 249 through 279 )A249 - 279
9X-RAY DIFFRACTION9chain 'A' and (resid 280 through 298 )A280 - 298
10X-RAY DIFFRACTION10chain 'B' and (resid 3 through 55 )B3 - 55
11X-RAY DIFFRACTION11chain 'B' and (resid 56 through 70 )B56 - 70
12X-RAY DIFFRACTION12chain 'B' and (resid 71 through 129 )B71 - 129
13X-RAY DIFFRACTION13chain 'B' and (resid 130 through 214 )B130 - 214
14X-RAY DIFFRACTION14chain 'B' and (resid 215 through 248 )B215 - 248
15X-RAY DIFFRACTION15chain 'B' and (resid 249 through 298 )B249 - 298
16X-RAY DIFFRACTION16chain 'C' and (resid 3 through 55 )C3 - 55
17X-RAY DIFFRACTION17chain 'C' and (resid 56 through 148 )C56 - 148
18X-RAY DIFFRACTION18chain 'C' and (resid 149 through 226 )C149 - 226
19X-RAY DIFFRACTION19chain 'C' and (resid 227 through 248 )C227 - 248
20X-RAY DIFFRACTION20chain 'C' and (resid 249 through 298 )C249 - 298
21X-RAY DIFFRACTION21chain 'D' and (resid 3 through 55 )D3 - 55
22X-RAY DIFFRACTION22chain 'D' and (resid 56 through 70 )D56 - 70
23X-RAY DIFFRACTION23chain 'D' and (resid 71 through 98 )D71 - 98
24X-RAY DIFFRACTION24chain 'D' and (resid 99 through 148 )D99 - 148
25X-RAY DIFFRACTION25chain 'D' and (resid 149 through 214 )D149 - 214
26X-RAY DIFFRACTION26chain 'D' and (resid 215 through 248 )D215 - 248
27X-RAY DIFFRACTION27chain 'D' and (resid 249 through 279 )D249 - 279
28X-RAY DIFFRACTION28chain 'D' and (resid 280 through 298 )D280 - 298
29X-RAY DIFFRACTION29chain 'E' and (resid 3 through 70 )E3 - 70
30X-RAY DIFFRACTION30chain 'E' and (resid 71 through 148 )E71 - 148
31X-RAY DIFFRACTION31chain 'E' and (resid 149 through 226 )E149 - 226
32X-RAY DIFFRACTION32chain 'E' and (resid 227 through 248 )E227 - 248
33X-RAY DIFFRACTION33chain 'E' and (resid 249 through 298 )E249 - 298
34X-RAY DIFFRACTION34chain 'F' and (resid 3 through 23 )F3 - 23
35X-RAY DIFFRACTION35chain 'F' and (resid 24 through 55 )F24 - 55
36X-RAY DIFFRACTION36chain 'F' and (resid 56 through 70 )F56 - 70
37X-RAY DIFFRACTION37chain 'F' and (resid 71 through 148 )F71 - 148
38X-RAY DIFFRACTION38chain 'F' and (resid 149 through 171 )F149 - 171
39X-RAY DIFFRACTION39chain 'F' and (resid 172 through 229 )F172 - 229
40X-RAY DIFFRACTION40chain 'F' and (resid 230 through 248 )F230 - 248
41X-RAY DIFFRACTION41chain 'F' and (resid 249 through 279 )F249 - 279
42X-RAY DIFFRACTION42chain 'F' and (resid 280 through 298 )F280 - 298

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