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- PDB-5brm: Structural basis for Mob1-dependent activation of the core Mst-La... -

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Basic information

Entry
Database: PDB / ID: 5brm
TitleStructural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in Hippo signaling
Components
  • MOB kinase activator 1A
  • Serine/threonine-protein kinase 3
KeywordsTransferase/Signaling Protein / Mst2 / Mob1 / Hippo / Transferase-Signaling Protein complex
Function / homology
Function and homology information


negative regulation of cell growth involved in contact inhibition / protein localization to centrosome / positive regulation of hippo signaling / hippo signaling / transcription regulator activator activity / Signaling by Hippo / regulation of MAPK cascade / protein kinase activator activity / protein serine/threonine kinase activator activity / protein import into nucleus ...negative regulation of cell growth involved in contact inhibition / protein localization to centrosome / positive regulation of hippo signaling / hippo signaling / transcription regulator activator activity / Signaling by Hippo / regulation of MAPK cascade / protein kinase activator activity / protein serine/threonine kinase activator activity / protein import into nucleus / protein tetramerization / negative regulation of canonical Wnt signaling pathway / protein kinase activity / protein phosphorylation / non-specific serine/threonine protein kinase / protein stabilization / intracellular signal transduction / positive regulation of apoptotic process / protein serine kinase activity / protein serine/threonine kinase activity / apoptotic process / centrosome / magnesium ion binding / protein-containing complex / extracellular exosome / ATP binding / metal ion binding / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
: / MOB kinase activator / Mst1 SARAH domain / C terminal SARAH domain of Mst1 / MOB kinase activator family / MOB kinase activator superfamily / Mob1/phocein family / Mob1/phocein family / SARAH domain / SARAH domain profile. ...: / MOB kinase activator / Mst1 SARAH domain / C terminal SARAH domain of Mst1 / MOB kinase activator family / MOB kinase activator superfamily / Mob1/phocein family / Mob1/phocein family / SARAH domain / SARAH domain profile. / : / Butyryl-CoA Dehydrogenase, subunit A; domain 3 / p53-like tetramerisation domain superfamily / 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 / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Serine/threonine-protein kinase 3 / MOB kinase activator 1A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.651 Å
AuthorsLuo, X. / Ni, L.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM085004 United States
CitationJournal: Genes Dev. / Year: 2015
Title: Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in Hippo signaling.
Authors: Ni, L. / Zheng, Y. / Hara, M. / Pan, D. / Luo, X.
History
DepositionMay 31, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 8, 2015Provider: repository / Type: Initial release
Revision 1.1Jul 15, 2015Group: Source and taxonomy
Revision 1.2Jul 22, 2015Group: Database references
Revision 1.3Sep 20, 2017Group: Author supporting evidence / Database references ...Author supporting evidence / Database references / Derived calculations / Source and taxonomy
Category: citation / entity_src_gen ...citation / entity_src_gen / pdbx_audit_support / pdbx_entity_src_syn / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag ..._citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_entity_src_syn.pdbx_alt_source_flag / _pdbx_struct_oper_list.symmetry_operation
Revision 1.4Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_conn_type / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.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 1.6Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MOB kinase activator 1A
B: MOB kinase activator 1A
C: MOB kinase activator 1A
D: MOB kinase activator 1A
E: MOB kinase activator 1A
F: MOB kinase activator 1A
G: Serine/threonine-protein kinase 3
H: Serine/threonine-protein kinase 3
I: Serine/threonine-protein kinase 3
J: Serine/threonine-protein kinase 3
K: Serine/threonine-protein kinase 3
L: Serine/threonine-protein kinase 3
M: Serine/threonine-protein kinase 3
N: Serine/threonine-protein kinase 3
O: Serine/threonine-protein kinase 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)158,75121
Polymers158,35915
Non-polymers3926
Water1086
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)142.188, 142.188, 135.981
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number152
Space group name H-MP3121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails (eV)
11chain A
21chain B
31chain C
41chain D
51chain E
61chain F
12chain I
22chain J
32chain K
42chain L

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASPASPZNZNchain AAA - P52 - 30113
21ASPASPZNZNchain BBB - Q52 - 30113
31ASPASPZNZNchain CCC - R52 - 30113
41ASPASPZNZNchain DDD - S52 - 30113
51ASPASPZNZNchain EEE - T52 - 30113
61ASPASPZNZNchain FFF - U52 - 30113
12TPOTPOASPASPchain III378 - 3988 - 28
22TPOTPOASPASPchain JJJ378 - 3988 - 28
32TPOTPOASPASPchain KKK378 - 3988 - 28
42TPOTPOPHEPHEchain LLL378 - 3978 - 27

NCS ensembles :
ID
1
2

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Components

#1: Protein
MOB kinase activator 1A / Mob1 alpha / Mob1A / Mob1 homolog 1B / Mps one binder kinase activator-like 1B


Mass: 20724.754 Da / Num. of mol.: 6 / Fragment: UNP residues 41-216
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MOB1A, C2orf6, MOB4B, MOBK1B, MOBKL1B / Plasmid: pGEX-6p / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9H8S9
#2: Protein/peptide
Serine/threonine-protein kinase 3 / Mammalian STE20-like protein kinase 2 / MST-2 / STE20-like kinase MST2 / Serine/threonine-protein kinase Krs-1


Mass: 3778.892 Da / Num. of mol.: 9 / Fragment: UNP residues 371-401 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
References: UniProt: Q13188, non-specific serine/threonine protein kinase
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Formula: H2O
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: 2.51 Å3/Da / Density % sol: 50.91 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: 2.4 M Na Malonate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97929 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 11, 2013 / Details: monochromator
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97929 Å / Relative weight: 1
ReflectionResolution: 2.65→40 Å / Num. obs: 46680 / % possible obs: 99.5 % / Observed criterion σ(I): 0 / Redundancy: 11 % / Biso Wilson estimate: 38.38 Å2 / Rmerge(I) obs: 0.091 / Χ2: 0.963 / Net I/av σ(I): 25.585 / Net I/σ(I): 11.3 / Num. measured all: 512365
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique allΧ2% possible all
2.65-2.76.311.822320.93997.9
2.7-2.748.322800.83499.9
2.74-2.89.90.96723110.85699.9
2.8-2.8510.90.89622740.883100
2.85-2.9211.60.77122930.887100
2.92-2.9811.80.71222920.891100
2.98-3.0611.90.62123040.927100
3.06-3.1411.90.46522740.95499.8
3.14-3.2311.90.34523310.96999.9
3.23-3.34120.25723000.99199.8
3.34-3.4611.80.20722941.10199.7
3.46-3.6120.14423001.00799.4
3.6-3.7611.70.11522951.07999.2
3.76-3.9611.70.09323181.04899.5
3.96-4.2111.60.07323160.98699.4
4.21-4.5311.50.06523120.96599.4
4.53-4.9811.40.06123080.97299.4
4.98-5.711.40.06323721.03199.9
5.7-7.1811.50.05723780.87499.8
7.18-4010.60.05824270.99397.8

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Processing

Software
NameVersionClassification
PHENIXrefinement
HKL-2000data scaling
PDB_EXTRACT3.15data extraction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1pi1

1pi1


Resolution: 2.651→39.295 Å / SU ML: 0.33 / Cross valid method: FREE R-VALUE / σ(F): 1.5 / Phase error: 27.15 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2681 2004 4.83 %random selection
Rwork0.2441 39468 --
obs0.2452 41472 89.28 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 172.2 Å2 / Biso mean: 56.5769 Å2 / Biso min: 10.42 Å2
Refinement stepCycle: final / Resolution: 2.651→39.295 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8906 0 6 6 8918
Biso mean--39.39 31.94 -
Num. residues----1060
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0069179
X-RAY DIFFRACTIONf_angle_d0.99412387
X-RAY DIFFRACTIONf_chiral_restr0.0381305
X-RAY DIFFRACTIONf_plane_restr0.0051574
X-RAY DIFFRACTIONf_dihedral_angle_d13.0393355
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A6092X-RAY DIFFRACTION12.277TORSIONAL
12B6092X-RAY DIFFRACTION12.277TORSIONAL
13C6092X-RAY DIFFRACTION12.277TORSIONAL
14D6092X-RAY DIFFRACTION12.277TORSIONAL
15E6092X-RAY DIFFRACTION12.277TORSIONAL
16F6092X-RAY DIFFRACTION12.277TORSIONAL
21I283X-RAY DIFFRACTION12.277TORSIONAL
22J283X-RAY DIFFRACTION12.277TORSIONAL
23K283X-RAY DIFFRACTION12.277TORSIONAL
24L283X-RAY DIFFRACTION12.277TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.651-2.71730.3611800.30121412149246
2.7173-2.79070.2957960.30691871196760
2.7907-2.87280.3461100.30362201231171
2.8728-2.96550.33651270.30692634276183
2.9655-3.07150.31881490.30942912306194
3.0715-3.19440.341540.28663116327099
3.1944-3.33970.2771620.27731433305100
3.3397-3.51570.29031600.249731303290100
3.5157-3.73580.25641580.24033119327799
3.7358-4.0240.26471590.22983130328999
4.024-4.42840.26731580.21353146330499
4.4284-5.06810.20411640.20131633327100
5.0681-6.38080.25751580.225332163374100
6.3808-39.29930.22971690.22743275344498
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)
10.89630.07920.10030.89530.15312.4566-0.1021-0.00080.0021-0.0107-0.03220.09970.1259-0.24350.01690.23840.0157-0.03490.2539-0.06340.04718.0532-57.4108-0.4959
26.3741.90621.56424.4660.48254.14290.06040.1327-0.1165-0.1236-0.09180.41690.104-0.45060.03250.1857-0.0316-0.10040.1996-0.13670.25231.7616-72.5646-0.9786
32.7607-0.8190.66771.2823-1.30631.3488-0.09880.58580.1912-0.4406-0.01840.4952-0.242-0.42990.05310.31350.0925-0.22320.4166-0.13920.3012-1.3222-60.5972-8.434
40.94340.17710.6110.79270.46911.6864-0.11740.02640.1035-0.047-0.10860.1528-0.0873-0.1688-0.22930.22920.003-0.05620.2558-0.1380.08148.7943-56.75833.1208
52.12290.48510.03710.40380.05051.06270.0244-0.32470.15070.1127-0.07990.0327-0.2149-0.18320.06210.3387-0.0393-0.0170.1773-0.03040.02836.0317-47.50125.5108
62.3856-0.28231.24890.6498-0.34233.3218-0.2044-0.37880.05530.1511-0.04310.1782-0.0472-0.41870.20440.4608-0.06740.08480.2149-0.080.12821.3334-54.442712.6791
70.83130.0737-0.23382.8954-0.46251.5253-0.05310.13270.0765-0.0902-0.0467-0.2501-0.00750.10720.07730.21770.08150.11560.20940.13850.146656.8243-40.3972.6172
81.9902-0.3380.22051.1316-0.33331.1166-0.203-0.3770.30410.24820.051-0.0815-0.1963-0.0782-0.0540.1831-0.0191-0.04480.36720.13540.312866.41-34.079514.3942
92.6579-0.13680.85843.96561.71754.3879-0.1527-0.5283-0.15990.80820.2533-0.68730.41750.5289-0.08490.4618-0.0623-0.03690.66940.31220.683176.7746-35.949411.5778
102.0914-0.07320.15231.67250.08430.6647-0.11550.3404-0.4658-0.2238-0.027-0.14950.25910.19210.47990.30220.12290.28640.43180.21060.556267.0003-46.7932-0.2094
110.6018-0.0559-0.00350.7147-0.03560.9579-0.0946-0.2764-0.14130.1819-0.0312-0.02960.0224-0.0271-0.14120.26120.09380.09720.23420.22010.060354.1547-41.695511.9916
121.1843-0.167-0.39510.9984-0.70192.1722-0.14220.1392-0.217-0.1702-0.126-0.1672-0.04030.0281-0.13640.2953-0.12270.15130.37830.01580.143447.8545-49.5769-4.6267
132.3805-2.10820.83973.85130.58111.17770.15650.2796-0.3576-0.1414-0.25870.36080.2596-0.07270.0730.6056-0.04330.20350.525-0.38230.765939.5935-68.7237-11.1909
149.55314.56030.21042.3237-0.92817.2-0.12140.56640.3952-0.5390.01910.0014-0.2090.17810.07490.8805-0.07010.21870.6193-0.140.516239.5361-55.9196-24.5689
155.2139-4.36964.72763.7308-4.18054.98-0.20950.12550.30750.0407-0.0455-0.2764-0.19950.0840.26351.0535-0.35010.28640.9205-0.31010.662238.6905-64.5748-21.6243
160.38970.0026-0.19010.78760.08431.3359-0.08160.2562-0.1782-0.3101-0.025-0.07560.0232-0.0573-0.02140.7315-0.13770.25190.7963-0.21670.332347.2204-56.2816-16.5137
171.2717-0.0298-0.40942.60160.29193.4114-0.12450.1349-0.0289-0.32540.121-0.1498-0.29950.55780.01440.79780.0290.15060.79340.19760.275752.0019-38.5166-15.3211
181.93250.2168-0.6750.5757-0.0632.0161-0.42480.2289-0.3893-0.19230.0844-0.08110.2777-0.17320.16660.4707-0.06650.15110.2884-0.00620.10641.1921-53.788-4.0227
196.5909-1.65050.62716.0218-0.33155.1524-0.0640.1313-0.3254-0.1869-0.06470.20230.424-0.28650.08160.1986-0.08020.06240.3892-0.07880.269530.1597-56.9161-0.9269
200.8197-0.4608-0.26850.92370.0111.3517-0.0453-0.04450.14910.032-0.0286-0.057-0.0760.20210.04780.2105-0.0258-0.03920.29620.13661.040525.507-3.3201-0.0202
215.9538-3.056-3.44367.79262.74057.92980.0238-0.00130.16980.0922-0.08450.2434-0.5088-0.38740.11590.54910.1450.1960.33470.02431.13483.9342-10.62651.8236
220.9348-0.2124-0.07390.51950.36850.2684-0.3111-0.2094-0.75050.46460.21380.3250.2949-0.06380.04880.53320.03840.30380.3749-0.02961.47046.9139-0.361110.8928
230.18370.4585-0.09891.2828-0.42010.27820.00490.06830.0447-0.1149-0.09950.0250.01550.01070.01730.34410.0376-0.08880.33160.02171.436313.26011.943-2.2992
240.85680.9415-0.25322.3878-0.60430.5615-0.0108-0.07060.44410.1738-0.12030.3275-0.0783-0.0622-0.0360.2732-0.0960.11660.3023-0.06641.193221.9633-3.68175.4709
252.41742.0584-0.51442.0772-0.77422.645-0.1225-0.25280.09250.5221-0.33560.0728-0.1189-0.0590.30750.6238-0.15350.18060.4637-0.26191.284922.0225-3.104617.8364
262.81571.5833-0.82992.3273-0.54691.468-0.06280.15960.3473-0.1522-0.1844-0.10910.00030.20550.09860.1677-0.0261-0.07310.32640.24470.567838.255-6.4281-6.6584
275.0136-3.66653.47463.3726-1.22734.90240.03220.10850.3158-0.0205-0.1988-0.7507-0.00320.80560.17050.28180.08390.07150.54580.32980.965654.2554-14.105-8.9928
283.4305-0.2051.59383.27191.98764.5451-0.270.9201-0.0872-0.68790.15760.1915-0.02610.00590.07070.8566-0.13850.17791.14860.25950.606946.8766-13.8205-22.1249
297.41051.75931.77381.06460.66141.9162-0.08440.25470.1037-0.48110.0174-0.09220.1151-0.2077-0.06510.4610.0231-0.05730.57880.37490.585636.485-8.5368-16.9971
303.1477-0.29650.52161.0320.54971.7875-0.18140.1748-0.3085-0.1505-0.10110.0860.1546-0.0417-0.24780.219-0.0645-0.07620.38370.32090.644734.6857-15.1003-10.217
312.8323-0.3196-2.50973.65910.97682.7560.2482-0.2340.25850.3966-0.18770.2176-0.22770.1246-0.07830.3877-0.1813-0.19610.4530.32480.857248.84741.16193.2183
325.4555-1.47220.69711.8725-0.45371.5305-0.0364-0.1676-0.10290.0486-0.0428-0.05130.0221-0.0245-0.01430.14930.0293-0.01630.22510.19670.591237.8638-14.58031.8167
333.3274-2.08430.79422.77810.20744.6935-0.1043-0.0577-0.30930.13860.02690.13810.19090.1270.04270.240.12560.01080.41810.19370.749647.0168-19.63792.0191
341.9973-0.0515-0.15421.9167-0.54131.5364-0.11640.41810.4439-0.4937-0.05820.2461-0.1185-0.38440.02860.55770.1182-0.14290.4710.06040.25880.5205-37.6933-10.8829
356.4585-4.68520.454.7324-0.46625.0978-0.08580.21540.5161-0.48540.06620.7073-0.8866-0.70570.010.77390.1254-0.20460.4440.29350.9188-0.0319-19.9664-12.7367
361.7569-1.29590.13781.09070.15970.60140.15120.39810.7157-0.1974-0.0041-0.052-0.8036-0.1648-0.07931.14810.0813-0.1250.73340.4320.93375.159-26.5701-25.4313
370.60810.576-0.82331.00280.1292.9231-0.0080.34190.1407-0.3748-0.06480.0469-0.0177-0.05560.05350.87050.1549-0.07870.75120.21860.30862.3114-35.4541-20.4
381.6988-1.22081.54840.9776-1.31891.83410.00890.157-0.2001-0.2397-0.0664-0.03990.44450.29580.04230.93790.04540.28080.94690.01440.357214.7156-48.7426-19.2913
392.8639-0.45090.7146.2455-1.14113.8552-0.02990.1135-0.1369-0.56620.0192-1.7262-0.03880.91330.02940.73840.06730.44480.91860.09850.828921.8003-45.1451-17.6527
400.6630.5679-0.48890.94790.4111.84150.00890.33030.5847-0.5811-0.1335-0.072-0.16510.12650.03710.59890.0991-0.03720.39540.24120.41995.7785-31.1487-10.9773
411.53880.0577-1.71581.10110.87625.11840.03450.0522-0.17450.17330.06050.34220.0063-0.2158-0.09120.42110.1745-0.06590.40420.07831.0502-12.7183-31.7036-2.6333
425.9441.1485-0.00134.4905-0.26734.07840.066-0.1460.3756-0.0902-0.2526-0.0929-0.25190.10020.09750.31810.08070.01410.17080.08640.38536.532-34.5971-1.2988
431.92590.99332.33427.7548-0.77716.711-0.02780.12840.634-0.1291-0.1467-0.1318-0.93890.60350.13670.5497-0.15870.21750.26860.03520.8316.7215-23.7188-0.6495
441.0027-0.1436-0.2021.9728-0.56061.18370.0095-0.2656-0.12550.5936-0.12110.1075-0.06910.0850.09650.33170.0538-0.0090.3463-0.01230.15359.8758-67.492916.0631
450.5993-0.986-0.56773.31413.2153.6144-0.1708-0.43060.20650.52210.3231-0.32230.03570.5754-0.15520.6017-0.1153-0.0690.5512-0.10590.167217.4135-51.730915.2501
463.06141.17741.11290.84020.06321.77350.0635-0.64370.6960.3252-0.1736-0.233-0.347-0.19790.01420.39250.00680.03140.49510.05480.295460.4545-33.200220.2357
472.5518-0.6185-1.79427.431-1.4121.73540.0731-0.68390.46930.3821-0.08190.3824-0.2713-0.39020.02940.52350.2620.0630.6270.0140.34642.4943-32.73918.6311
482.9089-2.07653.47951.4973-2.49654.18460.0756-0.2518-0.389-0.07570.32640.40790.1717-0.7798-0.41970.5729-0.02030.13780.799-0.14160.606229.3438-65.2835-9.8402
495.11931.93434.24862.30750.99483.76290.1733-0.9713-0.03021.0573-0.05670.60010.1531-0.547-0.11630.68180.06890.19550.6260.00020.72735.3232-66.40557.2967
505.4686-3.3176-4.61282.01412.80453.914-0.2566-0.3109-0.05721.22020.12760.66460.36180.02450.11660.83830.07150.16520.7714-0.2240.935210.2746-4.022918.5075
511.2138-0.25971.67183.6507-0.31462.30320.0532-0.21980.7460.165-0.0242-0.1-0.65740.1878-0.04641.14980.01540.16960.75150.02720.977118.9103-18.782618.3361
525.1649-1.2522-0.02593.06321.32992.1276-0.15-0.0723-0.01630.19540.1309-0.14860.02960.4301-0.01610.3880.15740.01470.80490.43090.643754.237-13.9849-2.9674
533.73844.6840.74466.60441.46310.53060.0186-0.29870.50930.3711-0.0183-0.5708-0.24490.3836-0.01160.74810.015-0.18210.68110.1110.948251.7854-9.177510.9301
540.2123-0.3510.11610.92360.08930.34670.18730.03680.36050.2223-0.1750.1791-0.4699-0.0364-0.08570.5804-0.0192-0.03860.75810.01581.3464-1.5064-20.9959-2.9683
550.72891.2797-0.14023.6638-2.89085.28910.12440.30860.3817-0.16840.24620.8997-0.3829-0.718-0.3160.65540.1127-0.04440.7782-0.02940.4485-4.7597-43.2155-17.1684
562.4689-0.79731.61053.625-3.71814.72170.25440.5496-0.0446-0.9702-0.1494-0.00850.1520.0826-0.04280.48180.126-0.03720.6429-0.08790.168811.3319-57.1213-11.2373
578.35267.19046.44876.40766.33617.8064-0.26780.3428-0.1494-0.59240.27480.4260.1203-0.150.00480.74050.21480.04020.7709-0.1340.596314.2121-57.4412-14.0783
580.3098-0.0746-0.13140.7078-0.10271.3904-0.05230.1249-0.0095-0.1417-0.003-0.065-0.01240.0253-0.02910.5688-0.060.18510.59780.1080.201258.173-41.7213-6.8318
591.6653-1.318-0.94841.11290.57260.9936-0.02270.1277-0.3163-0.09030.0313-0.07310.1257-0.0409-0.00750.57660.041-0.11340.34640.2430.988123.1845-3.7506-8.6407
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 52 through 94 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 95 through 110 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 111 through 143 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 144 through 175 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 176 through 192 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 193 through 211 )A0
7X-RAY DIFFRACTION7chain 'B' and (resid 52 through 85 )B0
8X-RAY DIFFRACTION8chain 'B' and (resid 86 through 100 )B0
9X-RAY DIFFRACTION9chain 'B' and (resid 101 through 110 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 111 through 143 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 144 through 212 )B0
12X-RAY DIFFRACTION12chain 'C' and (resid 52 through 75 )C0
13X-RAY DIFFRACTION13chain 'C' and (resid 76 through 95 )C0
14X-RAY DIFFRACTION14chain 'C' and (resid 96 through 105 )C0
15X-RAY DIFFRACTION15chain 'C' and (resid 106 through 110 )C0
16X-RAY DIFFRACTION16chain 'C' and (resid 111 through 126 )C0
17X-RAY DIFFRACTION17chain 'C' and (resid 127 through 136 )C0
18X-RAY DIFFRACTION18chain 'C' and (resid 137 through 197 )C0
19X-RAY DIFFRACTION19chain 'C' and (resid 198 through 211 )C0
20X-RAY DIFFRACTION20chain 'D' and (resid 52 through 75 )D0
21X-RAY DIFFRACTION21chain 'D' and (resid 76 through 85 )D0
22X-RAY DIFFRACTION22chain 'D' and (resid 86 through 110 )D0
23X-RAY DIFFRACTION23chain 'D' and (resid 111 through 126 )D0
24X-RAY DIFFRACTION24chain 'D' and (resid 127 through 193 )D0
25X-RAY DIFFRACTION25chain 'D' and (resid 194 through 211 )D0
26X-RAY DIFFRACTION26chain 'E' and (resid 52 through 85 )E0
27X-RAY DIFFRACTION27chain 'E' and (resid 86 through 95 )E0
28X-RAY DIFFRACTION28chain 'E' and (resid 96 through 110 )E0
29X-RAY DIFFRACTION29chain 'E' and (resid 111 through 131 )E0
30X-RAY DIFFRACTION30chain 'E' and (resid 132 through 165 )E0
31X-RAY DIFFRACTION31chain 'E' and (resid 166 through 175 )E0
32X-RAY DIFFRACTION32chain 'E' and (resid 176 through 197 )E0
33X-RAY DIFFRACTION33chain 'E' and (resid 198 through 211 )E0
34X-RAY DIFFRACTION34chain 'F' and (resid 52 through 85 )F0
35X-RAY DIFFRACTION35chain 'F' and (resid 86 through 95 )F0
36X-RAY DIFFRACTION36chain 'F' and (resid 96 through 110 )F0
37X-RAY DIFFRACTION37chain 'F' and (resid 111 through 126 )F0
38X-RAY DIFFRACTION38chain 'F' and (resid 127 through 136 )F0
39X-RAY DIFFRACTION39chain 'F' and (resid 137 through 143 )F0
40X-RAY DIFFRACTION40chain 'F' and (resid 144 through 165 )F0
41X-RAY DIFFRACTION41chain 'F' and (resid 166 through 175 )F0
42X-RAY DIFFRACTION42chain 'F' and (resid 176 through 197 )F0
43X-RAY DIFFRACTION43chain 'F' and (resid 198 through 211 )F0
44X-RAY DIFFRACTION44chain 'G' and (resid 377 through 391 )G0
45X-RAY DIFFRACTION45chain 'G' and (resid 392 through 398 )G0
46X-RAY DIFFRACTION46chain 'H' and (resid 377 through 393 )H0
47X-RAY DIFFRACTION47chain 'H' and (resid 394 through 399 )H0
48X-RAY DIFFRACTION48chain 'I' and (resid 379 through 392 )I0
49X-RAY DIFFRACTION49chain 'I' and (resid 393 through 398 )I0
50X-RAY DIFFRACTION50chain 'J' and (resid 379 through 393 )J0
51X-RAY DIFFRACTION51chain 'J' and (resid 394 through 398 )J0
52X-RAY DIFFRACTION52chain 'K' and (resid 379 through 393 )K0
53X-RAY DIFFRACTION53chain 'K' and (resid 394 through 398 )K0
54X-RAY DIFFRACTION54chain 'L' and (resid 379 through 397 )L0
55X-RAY DIFFRACTION55chain 'M' and (resid 380 through 389 )M0
56X-RAY DIFFRACTION56chain 'M' and (resid 390 through 394 )M0
57X-RAY DIFFRACTION57chain 'M' and (resid 395 through 396 )M0
58X-RAY DIFFRACTION58chain 'N' and (resid 385 through 396 )N0
59X-RAY DIFFRACTION59chain 'O' and (resid 386 through 393 )O0

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