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- PDB-6s1i: Crystal Structure of DYRK1A with small molecule inhibitor -

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Basic information

Entry
Database: PDB / ID: 6s1i
TitleCrystal Structure of DYRK1A with small molecule inhibitor
ComponentsDual specificity tyrosine-phosphorylation-regulated kinase 1A
KeywordsTRANSFERASE / Kinase / catalytic domain / phosphorylated
Function / homology
Function and homology information


negative regulation of heterochromatin formation / peptidyl-serine autophosphorylation / dual-specificity kinase / [RNA-polymerase]-subunit kinase / tau-protein kinase activity / negative regulation of microtubule polymerization / negative regulation of DNA damage response, signal transduction by p53 class mediator / amyloid-beta formation / negative regulation of mRNA splicing, via spliceosome / G0 and Early G1 ...negative regulation of heterochromatin formation / peptidyl-serine autophosphorylation / dual-specificity kinase / [RNA-polymerase]-subunit kinase / tau-protein kinase activity / negative regulation of microtubule polymerization / negative regulation of DNA damage response, signal transduction by p53 class mediator / amyloid-beta formation / negative regulation of mRNA splicing, via spliceosome / G0 and Early G1 / peptidyl-tyrosine autophosphorylation / cytoskeletal protein binding / RNA polymerase II CTD heptapeptide repeat kinase activity / peptidyl-threonine phosphorylation / protein serine/threonine/tyrosine kinase activity / tubulin binding / positive regulation of RNA splicing / non-membrane spanning protein tyrosine kinase activity / peptidyl-tyrosine phosphorylation / tau protein binding / circadian rhythm / nervous system development / peptidyl-serine phosphorylation / actin binding / protein autophosphorylation / protein tyrosine kinase activity / transcription coactivator activity / histone H3T45 kinase activity / protein kinase activity / nuclear speck / protein phosphorylation / axon / ribonucleoprotein complex / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / dendrite / positive regulation of DNA-templated transcription / nucleoplasm / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Dual specificity tyrosine-phosphorylation-regulated kinase 1A/1B, catalytic domain / : / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. ...Dual specificity tyrosine-phosphorylation-regulated kinase 1A/1B, catalytic domain / : / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Chem-KR8 / Dual specificity tyrosine-phosphorylation-regulated kinase 1A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.38 Å
AuthorsSorrell, F.J. / Henderson, S.H. / Redondo, C. / Burgess-Brown, N.A. / von Delft, F. / Arrowsmith, C.H. / Bountra, C. / Edwards, A.M. / Elkins, J.M.
CitationJournal: Acs Med.Chem.Lett. / Year: 2020
Title: Mining Public Domain Data to Develop Selective DYRK1A Inhibitors.
Authors: Henderson, S.H. / Sorrell, F. / Bennett, J. / Hanley, M.T. / Robinson, S. / Hopkins Navratilova, I. / Elkins, J.M. / Ward, S.E.
History
DepositionJun 18, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 26, 2019Provider: repository / Type: Initial release
Revision 1.1Aug 21, 2019Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.2Aug 11, 2021Group: Advisory / Database references / Refinement description
Category: citation / citation_author ...citation / citation_author / database_2 / pdbx_unobs_or_zero_occ_residues / refine
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine.pdbx_diffrn_id
Revision 1.3Jan 24, 2024Group: 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 1.4Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
B: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
C: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
D: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)171,17920
Polymers168,3264
Non-polymers2,85316
Water11,656647
1
A: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,6744
Polymers42,0821
Non-polymers5933
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,9646
Polymers42,0821
Non-polymers8835
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,9646
Polymers42,0821
Non-polymers8835
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,5764
Polymers42,0821
Non-polymers4943
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)244.317, 64.504, 147.586
Angle α, β, γ (deg.)90.000, 115.740, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-653-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 135 through 147 or (resid 148...
21(chain B and (resid 135 through 147 or (resid 148...
31(chain C and (resid 135 through 147 or (resid 148...
41(chain D and (resid 135 through 211 or (resid 212...

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
11VALVALTYRTYR(chain A and (resid 135 through 147 or (resid 148...AA135 - 14711 - 23
12ILEILEVALVAL(chain A and (resid 135 through 147 or (resid 148...AA148 - 14924 - 25
13VALVALLYSLYS(chain A and (resid 135 through 147 or (resid 148...AA135 - 48111 - 357
14VALVALLYSLYS(chain A and (resid 135 through 147 or (resid 148...AA135 - 48111 - 357
15VALVALLYSLYS(chain A and (resid 135 through 147 or (resid 148...AA135 - 48111 - 357
16VALVALLYSLYS(chain A and (resid 135 through 147 or (resid 148...AA135 - 48111 - 357
21VALVALTYRTYR(chain B and (resid 135 through 147 or (resid 148...BB135 - 14711 - 23
22ILEILEVALVAL(chain B and (resid 135 through 147 or (resid 148...BB148 - 14924 - 25
23VALVALLYSLYS(chain B and (resid 135 through 147 or (resid 148...BB135 - 48111 - 357
24VALVALLYSLYS(chain B and (resid 135 through 147 or (resid 148...BB135 - 48111 - 357
25VALVALLYSLYS(chain B and (resid 135 through 147 or (resid 148...BB135 - 48111 - 357
26VALVALLYSLYS(chain B and (resid 135 through 147 or (resid 148...BB135 - 48111 - 357
31VALVALTYRTYR(chain C and (resid 135 through 147 or (resid 148...CC135 - 14711 - 23
32ILEILEVALVAL(chain C and (resid 135 through 147 or (resid 148...CC148 - 14924 - 25
33VALVALLYSLYS(chain C and (resid 135 through 147 or (resid 148...CC135 - 48111 - 357
34VALVALLYSLYS(chain C and (resid 135 through 147 or (resid 148...CC135 - 48111 - 357
35VALVALLYSLYS(chain C and (resid 135 through 147 or (resid 148...CC135 - 48111 - 357
36VALVALLYSLYS(chain C and (resid 135 through 147 or (resid 148...CC135 - 48111 - 357
41VALVALASNASN(chain D and (resid 135 through 211 or (resid 212...DD135 - 21111 - 87
42LYSLYSLYSLYS(chain D and (resid 135 through 211 or (resid 212...DD21288
43VALVALLYSLYS(chain D and (resid 135 through 211 or (resid 212...DD135 - 48111 - 357
44VALVALLYSLYS(chain D and (resid 135 through 211 or (resid 212...DD135 - 48111 - 357
45VALVALLYSLYS(chain D and (resid 135 through 211 or (resid 212...DD135 - 48111 - 357
46VALVALLYSLYS(chain D and (resid 135 through 211 or (resid 212...DD135 - 48111 - 357

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Components

#1: Protein
Dual specificity tyrosine-phosphorylation-regulated kinase 1A / Dual specificity YAK1-related kinase / HP86 / Protein kinase minibrain homolog / hMNB


Mass: 42081.535 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: DYRK1A, DYRK, MNB, MNBH / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q13627, dual-specificity kinase
#2: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: SO4
#3: Chemical
ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#4: Chemical
ChemComp-KR8 / ~{N}-methyl-~{N}-phenyl-4-pyrazolo[1,5-b]pyridazin-3-yl-pyrimidin-2-amine


Mass: 302.333 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C17H14N6 / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 647 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

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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: 3.25 Å3/Da / Density % sol: 62.12 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop
Details: 37% PEG400 -- 0.2M lithium sulfate -- 0.1M tris pH 8.8

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9762 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Sep 21, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9762 Å / Relative weight: 1
ReflectionResolution: 2.38→110.03 Å / Num. obs: 83417 / % possible obs: 99.9 % / Redundancy: 3.3 % / Biso Wilson estimate: 40.48 Å2 / CC1/2: 0.992 / Rmerge(I) obs: 0.083 / Rpim(I) all: 0.053 / Rrim(I) all: 0.099 / Net I/σ(I): 7.6 / Num. measured all: 274154 / Scaling rejects: 116
Reflection shell

Diffraction-ID: 1 / % possible all: 99.8

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs
2.38-2.443.40.8682058560970.6310.5541.0331.5
10.64-110.033.10.074310610130.9810.0490.08917.3

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
Aimless0.5.32data scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACT3.25data extraction
DIALSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4mq1

4mq1


Resolution: 2.38→70.972 Å / SU ML: 0.35 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 26.09 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2279 4184 5.1 %
Rwork0.2006 77916 -
obs0.202 82100 98.17 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 125.52 Å2 / Biso mean: 52.3464 Å2 / Biso min: 23.24 Å2
Refinement stepCycle: final / Resolution: 2.38→70.972 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11164 0 192 647 12003
Biso mean--61.12 47.63 -
Num. residues----1383
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A4046X-RAY DIFFRACTION8.5TORSIONAL
12B4046X-RAY DIFFRACTION8.5TORSIONAL
13C4046X-RAY DIFFRACTION8.5TORSIONAL
14D4046X-RAY DIFFRACTION8.5TORSIONAL
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 (%)
2.3797-2.40670.39811280.35592434256294
2.4067-2.43510.39271320.34972537266996
2.4351-2.46480.35021390.33432519265896
2.4648-2.4960.36631240.31722513263796
2.496-2.52880.34391460.30982528267496
2.5288-2.56340.36531370.31792570270797
2.5634-2.60010.42251360.31662544268097
2.6001-2.63890.31811240.28932574269897
2.6389-2.68010.32411550.26812576273198
2.6801-2.72410.31691330.25442547268098
2.7241-2.7710.3061180.26152593271198
2.771-2.82140.31281520.25462575272798
2.8214-2.87570.28971530.2582565271898
2.8757-2.93440.31691640.25692596276099
2.9344-2.99820.27061540.22572544269899
2.9982-3.06790.23271540.22942625277999
3.0679-3.14470.22961430.21792582272599
3.1447-3.22970.25351400.22342664280499
3.2297-3.32470.23831470.21832569271699
3.3247-3.4320.25381410.20082635277699
3.432-3.55470.21051280.18122633276199
3.5547-3.6970.17681410.17322629277099
3.697-3.86530.20041550.16672600275599
3.8653-4.0690.1751310.15132664279599
4.069-4.32390.14641470.14722627277499
4.3239-4.65770.15711410.13222634277599
4.6577-5.12630.16251150.13872651276699
5.1263-5.86780.24141400.184126832823100
5.8678-7.39160.19511200.187327382858100
7.3916-71.00360.16651460.17722767291399
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)
13.62140.68140.47854.44860.25124.38260.2080.08750.01960.09220.0323-0.77020.11010.6454-0.27880.4660.03990.03550.4445-0.09820.4053-54.954516.807166.1114
21.03560.2957-0.04692.0880.82251.14030.0498-0.2008-0.02640.27050.058-0.16840.11560.0011-0.09410.43580.00130.00060.30020.03850.3225-63.99684.4517159.5472
33.51391.1626-2.27172.3757-0.96672.00060.1763-0.30131.07360.46250.02980.4896-0.7318-0.2518-0.3870.76860.06610.20140.3448-0.10110.9365-75.054920.3728153.2162
40.77460.27240.49131.6445-0.61752.06960.0146-0.0280.07020.1449-0.00250.0283-0.2225-0.1316-0.010.35790.02830.06320.27270.01740.3367-74.59689.3676142.2842
55.94573.04432.30786.08452.69758.1601-0.30020.90941.1015-0.9703-0.05630.2502-0.8888-0.4190.19970.51210.15610.10450.48250.10460.4624-83.47617.3254130.2058
65.59112.36740.99687.89526.86856.2070.05321.06112.0074-1.91690.3398-0.077-1.6837-0.7652-0.37140.6397-0.01520.04670.63320.23980.5485-70.299813.9434121.2103
70.43420.17520.27091.8502-0.4412.41260.1039-0.0868-0.16590.0504-0.05310.04610.1453-0.1602-0.05130.2655-0.03520.02150.2850.02060.3537-75.3122-5.1119142.1721
88.8156-1.6246-3.07337.31413.16995.5042-0.4269-0.2533-1.03340.790.20680.07291.0843-0.01520.38040.5566-0.02670.09330.40050.14620.4386-78.5554-11.1128153.2726
93.416-0.79890.59866.8014-0.7823.50680.0774-0.10970.43290.21910.1148-0.9235-0.31750.4637-0.15360.4831-0.0660.05620.3911-0.1230.4574-56.1041-24.4826174
102.9151-0.5899-1.92495.28730.97124.74730.1870.3635-0.0153-0.0952-0.16790.1424-0.229-0.53660.04970.5603-0.06650.10760.4209-0.05890.2855-76.0573-30.0804172.5896
111.7661-1.324-0.73492.06282.24963.39440.20850.09790.2852-0.08840.0338-0.3126-0.1902-0.0079-0.34840.5482-0.04550.13580.30270.01940.4381-67.4738-19.1998178.53
122.4381-1.0031-0.24854.01231.54111.9333-0.01220.02960.1703-0.3560.0389-0.16610.03840.06460.00180.49770.00030.06130.34930.0180.2774-79.214-19.7032182.4184
133.22822.25470.79017.16053.96442.30680.8306-0.5173-2.39950.33140.5511-1.47381.45880.7695-1.34130.61850.2387-0.00320.72490.01290.8639-76.7061-39.3791189.0176
141.4518-0.0205-0.43211.3751-0.24431.9284-0.0503-0.106-0.1018-0.08010.0699-0.09610.16070.17560.00980.42820.05680.05590.35760.00460.2725-80.5978-28.5902198.5621
152.70680.62160.1335.19873.23282.00630.0434-0.5852-0.35680.4259-0.02960.06710.6541-0.02450.16180.56330.05430.04740.52230.09630.2867-82.7903-32.8509212.7471
162.22390.93240.42984.34921.52493.105-0.11950.06720.2415-0.08550.10250.2424-0.2519-0.09950.03220.38730.0320.05110.2987-0.00040.2569-89.4802-14.512195.4935
172.98750.8190.55843.51330.14973.40680.3803-0.3811-0.53520.13-0.3009-0.59860.18790.6265-0.06980.5118-0.1365-0.10561.02660.1160.5165-114.4973-35.3433158.6039
184.14941.6726-0.89025.519-1.06378.4642-0.29080.40350.4531-0.52720.540.1241-0.4039-0.132-0.14750.6579-0.2068-0.10921.07030.1770.5209-128.0251-18.7072155.5981
191.8838-0.13521.2063.45181.27432.04040.1980.1448-0.3298-0.49180.1984-0.2421-0.39950.2938-0.2970.5862-0.1822-0.03220.92690.05190.4267-118.2999-27.51156.3486
201.0805-0.15240.71631.47570.141.7481-0.11610.28380.0107-0.04440.13540.012-0.057-0.2358-0.02960.5072-0.1553-0.00520.76240.13470.366-120.0547-14.5196169.0629
214.5683-2.46250.55191.4184-0.1950.1730.3023-0.7172-1.5976-1.26610.90692.18531.6711-2.3987-1.5490.8671-0.329-0.17431.2022-0.0320.8725-138.1039-25.6791170.578
221.34730.3783-0.10692.3673-0.80113.3437-0.13060.30570.0421-0.13850.20680.40010.0734-0.6697-0.07440.4193-0.10530.00230.7330.10750.4097-131.8883-18.7197183.4846
231.58213.1962-0.07032.02751.11491.8649-0.1518-0.8141-0.43721.65930.02640.8621-0.0539-0.98170.06330.5827-0.0960.1831.24310.16250.6434-142.31-20.5148198.5056
242.3084-0.37260.69232.5517-1.4325.0406-0.04070.31320.40060.05880.18660.2635-0.5896-0.3727-0.10830.47080.02010.06930.57760.10610.4291-125.3283-4.9695183.1109
253.9773-0.8317-0.28164.87471.36963.81720.57190.2858-1.2140.0214-0.16250.35280.8135-0.139-0.34830.66460.0044-0.3150.8206-0.07980.78-122.0358-20.1904116.7014
264.6964-1.95042.62072.4526-0.56712.30040.24850.9948-0.4458-0.6433-0.17020.35760.17390.36-0.0160.56040.0938-0.15460.7633-0.10750.4445-110.4354-10.6481113.7414
274.2005-1.00680.78952.84630.0651.96350.33180.3766-0.7246-0.3723-0.2660.31830.1821-0.0973-0.15360.377-0.0041-0.06260.6026-0.08990.4531-101.0328-16.9057126.1406
283.09851.5146-4.09533.5255-0.30046.47510.5621-0.26581.1178-0.2769-0.41531.2159-0.6377-0.5927-0.72350.30190.03610.05940.8670.07691.3777-111.15411.1221132.7242
292.0014-0.3951-0.26752.40470.22271.53140.1141-0.14280.00660.1264-0.15330.2681-0.0858-0.4520.03780.3637-0.04520.02410.60460.03530.3629-102.941-2.7999144.0181
303.6649-2.179-0.78322.04491.36021.9624-0.3989-0.7792-0.72170.41460.23330.37420.24550.42770.10430.4418-0.06730.02040.6540.20630.4766-93.912-16.5681149.6358
314.0058-2.09250.42772.71350.76121.40290.13420.2009-0.32320.2814-0.16070.02170.10150.0529-0.01740.3416-0.0644-0.0460.46760.04670.3975-88.4024-11.4811137.9909
328.90293.4186-3.63447.8562-1.05922.4922-0.02050.3003-0.4069-0.433-0.7256-0.56080.18681.22140.47130.45760.01270.04940.72420.05070.4214-84.4034-10.2109128.3255
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 135:216)A135 - 216
2X-RAY DIFFRACTION2(chain A and resid 217:313)A217 - 313
3X-RAY DIFFRACTION3(chain A and resid 314:322)A314 - 322
4X-RAY DIFFRACTION4(chain A and resid 323:389)A323 - 389
5X-RAY DIFFRACTION5(chain A and resid 390:408)A390 - 408
6X-RAY DIFFRACTION6(chain A and resid 409:414)A409 - 414
7X-RAY DIFFRACTION7(chain A and resid 415:474)A415 - 474
8X-RAY DIFFRACTION8(chain A and resid 475:481)A475 - 481
9X-RAY DIFFRACTION9(chain B and resid 135:197)B135 - 197
10X-RAY DIFFRACTION10(chain B and resid 198:217)B198 - 217
11X-RAY DIFFRACTION11(chain B and resid 218:255)B218 - 255
12X-RAY DIFFRACTION12(chain B and resid 256:313)B256 - 313
13X-RAY DIFFRACTION13(chain B and resid 314:322)B314 - 322
14X-RAY DIFFRACTION14(chain B and resid 323:391)B323 - 391
15X-RAY DIFFRACTION15(chain B and resid 392:422)B392 - 422
16X-RAY DIFFRACTION16(chain B and resid 423:481)B423 - 481
17X-RAY DIFFRACTION17(chain C and resid 135:201)C135 - 201
18X-RAY DIFFRACTION18(chain C and resid 202:219)C202 - 219
19X-RAY DIFFRACTION19(chain C and resid 220:243)C220 - 243
20X-RAY DIFFRACTION20(chain C and resid 244:313)C244 - 313
21X-RAY DIFFRACTION21(chain C and resid 314:322)C314 - 322
22X-RAY DIFFRACTION22(chain C and resid 323:395)C323 - 395
23X-RAY DIFFRACTION23(chain C and resid 396:411)C396 - 411
24X-RAY DIFFRACTION24(chain C and resid 412:481)C412 - 481
25X-RAY DIFFRACTION25(chain D and resid 135:196)D135 - 196
26X-RAY DIFFRACTION26(chain D and resid 197:237)D197 - 237
27X-RAY DIFFRACTION27(chain D and resid 238:313)D238 - 313
28X-RAY DIFFRACTION28(chain D and resid 314:321)D314 - 321
29X-RAY DIFFRACTION29(chain D and resid 322:412)D322 - 412
30X-RAY DIFFRACTION30(chain D and resid 413:438)D413 - 438
31X-RAY DIFFRACTION31(chain D and resid 439:469)D439 - 469
32X-RAY DIFFRACTION32(chain D and resid 470:481)D470 - 481

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