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- PDB-4lgd: Structural Basis for Autoactivation of Human Mst2 Kinase and Its ... -

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Basic information

Entry
Database: PDB / ID: 4lgd
TitleStructural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5
Components
  • Ras association domain family member 5, RASSF5
  • Serine/threonine-protein kinase 3
KeywordsSIGNALING PROTEIN / Hippo / Mst autoactivation / RASSF / SARAH domain / dimerization
Function / homology
Function and homology information


regulation of cell differentiation involved in embryonic placenta development / cell differentiation involved in embryonic placenta development / primitive hemopoiesis / neural tube formation / positive regulation of extrinsic apoptotic signaling pathway via death domain receptors / negative regulation of lymphocyte proliferation / positive regulation of hippo signaling / lymphocyte proliferation / endocardium development / negative regulation of organ growth ...regulation of cell differentiation involved in embryonic placenta development / cell differentiation involved in embryonic placenta development / primitive hemopoiesis / neural tube formation / positive regulation of extrinsic apoptotic signaling pathway via death domain receptors / negative regulation of lymphocyte proliferation / positive regulation of hippo signaling / lymphocyte proliferation / endocardium development / negative regulation of organ growth / hippo signaling / transcription regulator activator activity / regulation of protein localization to nucleus / Signaling by Hippo / protein localization to centrosome / organ growth / hepatocyte apoptotic process / regulation of MAPK cascade / extrinsic apoptotic signaling pathway via death domain receptors / positive regulation of fat cell differentiation / canonical Wnt signaling pathway / JNK cascade / protein serine/threonine kinase activator activity / central nervous system development / epithelial cell proliferation / positive regulation of protein ubiquitination / phosphatidylinositol 3-kinase/protein kinase B signal transduction / protein tetramerization / positive regulation of JNK cascade / negative regulation of canonical Wnt signaling pathway / protein import into nucleus / negative regulation of epithelial cell proliferation / microtubule / eukaryotic translation initiation factor 2alpha kinase activity / 3-phosphoinositide-dependent protein kinase activity / DNA-dependent protein kinase activity / ribosomal protein S6 kinase activity / histone H3S10 kinase activity / histone H2AXS139 kinase activity / histone H3S28 kinase activity / histone H4S1 kinase activity / histone H2BS14 kinase activity / histone H3T3 kinase activity / histone H2AS121 kinase activity / Rho-dependent protein serine/threonine kinase activity / histone H2BS36 kinase activity / histone H3S57 kinase activity / histone H2AT120 kinase activity / AMP-activated protein kinase activity / histone H2AS1 kinase activity / histone H3T6 kinase activity / histone H3T11 kinase activity / histone H3T45 kinase activity / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / non-specific serine/threonine protein kinase / protein kinase activity / protein stabilization / intracellular signal transduction / protein phosphorylation / positive regulation of apoptotic process / protein serine kinase activity / protein serine/threonine kinase activity / apoptotic process / centrosome / magnesium ion binding / signal transduction / protein-containing complex / ATP binding / metal ion binding / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Helix Hairpins - #4270 / Ras association domain-containing protein 5 / Ras association domain-containing protein 1-6 / Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain / : / Mst1 SARAH domain / C terminal SARAH domain of Mst1 / SARAH domain / SARAH domain profile. / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #110 ...Helix Hairpins - #4270 / Ras association domain-containing protein 5 / Ras association domain-containing protein 1-6 / Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain / : / Mst1 SARAH domain / C terminal SARAH domain of Mst1 / SARAH domain / SARAH domain profile. / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #110 / Ras association (RalGDS/AF-6) domain / Ras association (RalGDS/AF-6) domain / : / Ras-associating (RA) domain profile. / Ras-associating (RA) domain / p53-like tetramerisation domain superfamily / Phorbol esters/diacylglycerol binding domain (C1 domain) / Zinc finger phorbol-ester/DAG-type signature. / Zinc finger phorbol-ester/DAG-type profile. / Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains) / Protein kinase C-like, phorbol ester/diacylglycerol-binding domain / C1-like domain superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Helix Hairpins / Ubiquitin-like domain superfamily / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / 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 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / Serine/threonine-protein kinase 3 / Ras association domain-containing protein 5
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / molecular replacement-SAD / Resolution: 3.05 Å
AuthorsLuo, X. / Ni, L. / Tomchick, D.R.
CitationJournal: Structure / Year: 2013
Title: Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5.
Authors: Ni, L. / Li, S. / Yu, J. / Min, J. / Brautigam, C.A. / Tomchick, D.R. / Pan, D. / Luo, X.
History
DepositionJun 27, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 18, 2013Provider: repository / Type: Initial release
Revision 1.1Oct 30, 2013Group: Database references
Revision 1.2Aug 9, 2017Group: Source and taxonomy / Category: entity_src_gen
Revision 1.3Nov 15, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.4Feb 28, 2018Group: Data collection / Experimental preparation / Refinement description
Category: diffrn_radiation / exptl_crystal ...diffrn_radiation / exptl_crystal / exptl_crystal_grow / software
Item: _diffrn_radiation.pdbx_diffrn_protocol / _diffrn_radiation.pdbx_monochromatic_or_laue_m_l ..._diffrn_radiation.pdbx_diffrn_protocol / _diffrn_radiation.pdbx_monochromatic_or_laue_m_l / _exptl_crystal.density_Matthews / _exptl_crystal.density_percent_sol / _exptl_crystal_grow.method / _exptl_crystal_grow.pdbx_pH_range
Revision 1.5Sep 20, 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 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Serine/threonine-protein kinase 3
B: Serine/threonine-protein kinase 3
C: Serine/threonine-protein kinase 3
D: Serine/threonine-protein kinase 3
E: Ras association domain family member 5, RASSF5
F: Ras association domain family member 5, RASSF5
G: Ras association domain family member 5, RASSF5
H: Ras association domain family member 5, RASSF5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)201,41528
Polymers198,3598
Non-polymers3,05620
Water00
1
A: Serine/threonine-protein kinase 3
E: Ras association domain family member 5, RASSF5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,2165
Polymers49,5902
Non-polymers6273
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2760 Å2
ΔGint-26 kcal/mol
Surface area23710 Å2
MethodPISA
2
C: Serine/threonine-protein kinase 3
G: Ras association domain family member 5, RASSF5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,2627
Polymers49,5902
Non-polymers6735
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2860 Å2
ΔGint-31 kcal/mol
Surface area23590 Å2
MethodPISA
3
D: Serine/threonine-protein kinase 3
H: Ras association domain family member 5, RASSF5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,4318
Polymers49,5902
Non-polymers8426
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2080 Å2
ΔGint-18 kcal/mol
Surface area21960 Å2
MethodPISA
4
B: Serine/threonine-protein kinase 3
F: Ras association domain family member 5, RASSF5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,5058
Polymers49,5902
Non-polymers9156
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
A: Serine/threonine-protein kinase 3
B: Serine/threonine-protein kinase 3
E: Ras association domain family member 5, RASSF5
F: Ras association domain family member 5, RASSF5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,72113
Polymers99,1804
Non-polymers1,5419
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8490 Å2
ΔGint-75 kcal/mol
Surface area41720 Å2
MethodPISA
6
C: Serine/threonine-protein kinase 3
D: Serine/threonine-protein kinase 3
G: Ras association domain family member 5, RASSF5
H: Ras association domain family member 5, RASSF5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,69415
Polymers99,1804
Non-polymers1,51411
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9570 Å2
ΔGint-88 kcal/mol
Surface area40920 Å2
MethodPISA
Unit cell
Length a, b, c (Å)123.403, 237.136, 95.862
Angle α, β, γ (deg.)90.000, 100.700, 90.000
Int Tables number5
Space group name H-MC121

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Components

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Protein / Protein/peptide , 2 types, 8 molecules ABCDEFGH

#1: Protein
Serine/threonine-protein kinase 3 / Mammalian STE20-like protein kinase 2 / MST-2 / STE20-like kinase MST2 / Serine/threonine-protein ...Mammalian STE20-like protein kinase 2 / MST-2 / STE20-like kinase MST2 / Serine/threonine-protein kinase Krs-1 / Serine/threonine-protein kinase 3 36kDa subunit / MST2/N / Serine/threonine-protein kinase 3 20kDa subunit / MST2/C


Mass: 43626.164 Da / Num. of mol.: 4
Fragment: kinase domain, SARAH domain, UNP residues 1-313, 428-491
Mutation: D146N
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: STK3, KRS1, MST2 / Plasmid: pET29 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q13188, non-specific serine/threonine protein kinase
#2: Protein/peptide
Ras association domain family member 5, RASSF5 / New ras effector 1 / Regulator for cell adhesion and polarization enriched in lymphoid tissues / RAPL


Mass: 5963.654 Da / Num. of mol.: 4 / Fragment: SARAH domain, UNP residues 365-413
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RASSF5, NORE1, RAPL / Plasmid: pGEX-6p / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q8WWW0

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Non-polymers , 4 types, 20 molecules

#3: Chemical
ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER


Mass: 506.196 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H17N6O12P3 / Comment: AMP-PNP, energy-carrying molecule analogue*YM
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#5: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: SO4
#6: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Na

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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

Crystal
IDDensity Matthews (Å3/Da)Density % sol (%)
13.4764.59
23.4764.59
Crystal growTemperature: 293 K / Method: vapor diffusion
Details: 0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
PH range: 8.5

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21002
Diffraction source
SourceSiteBeamlineIDWavelength
SYNCHROTRONAPS 19-ID10.97929
SYNCHROTRONAPS 19-ID20.97921
Detector
TypeIDDetectorDateDetails
ADSC QUANTUM 315r1CCDFeb 12, 2011MONOCHROMATOR
ADSC QUANTUM 315r2CCDMar 14, 2011MONOCHROMATOR
Radiation
IDMonochromatorProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SAGITALLY FOCUSED SI(111)SINGLE WAVELENGTHMx-ray1
2SAGITALLY FOCUSED SI(111)SINGLE WAVELENGTHMx-ray1
Radiation wavelength
IDWavelength (Å)Relative weight
10.979291
20.979211
ReflectionResolution: 3.05→46.049 Å / Num. obs: 50456 / % possible obs: 98.2 % / Observed criterion σ(I): 0 / Redundancy: 4.1 % / Biso Wilson estimate: 71.84 Å2 / Rmerge(I) obs: 0.109 / Net I/σ(I): 14.4
Reflection scaleGroup code: 1
Reflection shellResolution: 3.05→3.1 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.762 / Mean I/σ(I) obs: 1.6 / % possible all: 90.7

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHENIX1.8_1069refinement
PDB_EXTRACT3.11data extraction
PHASESphasing
RefinementMethod to determine structure: molecular replacement-SAD
Starting model: PDB ENTRY 4LG4

4lg4


Resolution: 3.05→30 Å / SU ML: 0.29 / σ(F): 0 / Phase error: 32.15 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.244 2524 5 %
Rwork0.199 --
obs0.202 50374 98.6 %
all-65746 -
Solvent computationShrinkage radii: 0.99 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 135.9 Å2
Refinement stepCycle: LAST / Resolution: 3.05→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12609 0 176 0 12785
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00613027
X-RAY DIFFRACTIONf_angle_d0.6117577
X-RAY DIFFRACTIONf_dihedral_angle_d14.5575083
X-RAY DIFFRACTIONf_chiral_restr0.0361935
X-RAY DIFFRACTIONf_plane_restr0.0022230
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.0532-3.11190.39331240.29382308X-RAY DIFFRACTION85
3.1119-3.17530.35341320.30452498X-RAY DIFFRACTION93
3.1753-3.24430.33681420.29322618X-RAY DIFFRACTION98
3.2443-3.31970.2981330.25872672X-RAY DIFFRACTION99
3.3197-3.40260.30381310.24082690X-RAY DIFFRACTION99
3.4026-3.49440.28991390.22222690X-RAY DIFFRACTION100
3.4944-3.59710.27561430.20232682X-RAY DIFFRACTION100
3.5971-3.7130.23631650.1912691X-RAY DIFFRACTION100
3.713-3.84540.25841270.18912698X-RAY DIFFRACTION100
3.8454-3.9990.25841330.17342701X-RAY DIFFRACTION100
3.999-4.18060.22471480.17742702X-RAY DIFFRACTION100
4.1806-4.40030.2091490.16732665X-RAY DIFFRACTION100
4.4003-4.6750.21821310.16422691X-RAY DIFFRACTION100
4.675-5.03440.22421590.18962694X-RAY DIFFRACTION100
5.0344-5.5380.2411310.20722713X-RAY DIFFRACTION100
5.538-6.33260.2881360.21592721X-RAY DIFFRACTION100
6.3326-7.95280.21771360.20442713X-RAY DIFFRACTION100
7.9528-29.6520.20061650.17682703X-RAY DIFFRACTION99
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)
10.27550.06180.13470.19430.03320.1136-0.70480.5229-0.6099-0.5725-0.1386-0.13110.95320.3967-0.07032.70331.10190.051.7573-0.11561.874433.3768-71.101316.7739
20.0903-0.0702-0.04240.0510.00070.0248-0.7201-0.27260.13750.4030.03730.08630.51990.138402.89810.15350.25291.7597-0.07881.374935.7405-57.487814.5636
30.0760.03050.05020.00180.00330.0453-0.1556-0.3079-0.3530.01790.205-0.226-0.056-0.3078-0.00032.05810.62510.09760.9359-0.10641.431936.8545-61.519825.6929
40.08520.19920.00360.43570.3570.68830.22160.0702-0.38860.28170.68260.73850.99520.07490.2952.23270.49050.08780.9103-0.12290.917122.7867-58.176528.4377
50.480.00020.21780.2385-0.14480.14540.23971.098-0.19430.46980.17950.03360.63210.58590.04821.82740.50130.1010.9005-0.13011.002928.9479-50.983225.1448
60.66770.28110.14750.84860.40190.5844-0.4799-0.2444-0.1590.99520.56230.3008-0.2350.22540.92631.72020.47440.42290.53350.18650.721418.249-41.937531.2699
70.0508-0.05680.05360.0413-0.01140.00750.22710.23410.29350.7457-0.6096-0.1932-0.3355-0.46440.00012.48180.07130.11911.12440.10691.653511.2766-71.775418.3566
8-0.00790.00890.0482-0.0071-0.02360.0291-0.6448-0.4206-0.40660.25830.10360.3161-0.09070.2706-0.00012.15370.00750.20121.0069-0.04071.369821.3249-81.8802-0.6008
90.02750.00180.02790.0236-0.0110.0110.62820.31550.26880.12390.59450.0663-0.0381-0.3440.0020.7893-0.21320.26151.00810.0952.09119.9015-63.4374-11.2906
100.0076-0.0093-0.0289-0.00560.0070.0293-0.2274-0.0909-0.03180.1478-0.4462-0.1969-0.04720.10700.9849-0.0234-0.07640.9835-0.24921.81160.8238-41.2496-21.5916
110.2353-0.0032-0.25590.3001-0.07710.1818-0.0626-0.5043-0.3081-0.2062-0.030.02280.33160.175700.9080.1541-0.06540.645-0.07410.670923.4163-31.6941-23.8233
120.3317-0.2056-0.2990.40120.2430.52840.0284-0.16460.075-0.3257-0.061-0.12910.3860.0981-0.00020.52470.112-0.01020.60450.02490.551722.2771-25.2343-12.8967
130.0247-0.2366-0.21461.25521.01961.0466-0.27990.26740.1341.305-0.09930.39621.9350.0272-0.02860.07750.17720.16340.63470.04240.570117.6769-24.6851.6615
140.00290.0193-0.01010.0029-0.0180.0259-0.1527-0.3069-0.17180.698-0.22610.420.38690.1928-01.31510.26090.09170.90630.01640.706927.0791-25.333814.899
150.28730.2339-0.31940.78330.1210.44040.2802-0.13460.08231.32350.03210.2578-0.41040.13840.08080.3040.27230.18470.6302-0.03860.578318.6211-8.73797.8759
160.4461-0.0601-0.01190.3441-0.21620.5153-0.31350.39390.1481-0.3591-0.1899-0.45020.78650.12760.00320.15140.21320.13140.9901-0.12920.843740.9563-19.9535-14.5696
170.00820.001-0.00370.00510.0003-0.0061-0.0030.1827-0.026-0.09560.1107-0.0009-0.0588-0.1175-02.02550.18470.54992.02580.20372.15252.4416-43.2949-28.075
180.0044-0.0070.00640.0023-0.0033-0-0.0032-0.1989-0.00940.05970.1085-0.10530.0629-0.0207-01.51170.12820.34432.74830.50441.801655.2402-48.6452-13.1814
19-0.01230.01810.02450.02850.05310.0257-0.4697-0.50450.1766-0.02050.37330.14920.0442-0.1496-02.65620.59420.29012.0480.24481.676555.4657-53.849510.1501
200.30280.12050.23570.0833-0.10610.3132-0.6082-0.31140.48440.49880.23240.0088-0.934-0.2185-0.00011.05960.0873-0.1540.9447-0.2321.073533.400337.86834.1304
210.0090.535-0.23090.8288-0.10170.6761-0.3033-0.06840.0598-0.34720.2771-0.0201-0.06480.1424-0.00030.67710.1181-0.13780.6164-0.03420.685626.906523.099522.5197
220.79490.3877-0.24660.79330.17080.5294-0.17890.22780.1479-1.02720.35750.31040.163-0.00950.00130.96510.0337-0.13060.62090.11730.627616.915921.857614.6154
230.1641-0.127-0.16470.16680.41610.96370.370.0529-0.1479-0.81480.50360.5037-1.2092-0.46020.12281.14430.0595-0.32040.90960.28161.26685.097543.104647.1477
24-0.00610.0146-0.0109-0.0126-0.01290.0477-0.120.3355-0.16090.2387-0.7870.63090.2765-0.1480.00010.48840.0179-0.04151.0294-0.12931.171-13.700813.498760.6545
250.1460.02520.06430.21260.03610.48950.19690.01120.00930.11-0.15330.0646-0.68730.1423-0.00560.22330.0954-0.02150.621-0.02830.7098.04793.248367.5427
260.2756-0.0539-0.38190.0556-0.12080.5808-0.53270.1458-0.0568-0.03310.4035-0.14910.511-0.2924-0.03370.4772-0.0997-0.14590.6194-0.03780.53963.18773.622658.3747
270.1933-0.21740.25090.0742-0.2890.46790.17920.15410.08330.9462-0.15760.14651.0868-0.1519-0.01520.3040.292-0.10860.7655-0.02350.500913.8924-14.441852.0799
280.39130.412-0.19650.28030.2080.29780.1477-0.12290.0201-0.1393-0.01980.1009-0.20160.10700.53980.139-0.02350.4963-0.00450.40529.7545-4.202742.3007
290.3581-0.23670.16020.46340.43760.5669-0.09670.15930.0152-0.16180.04810.0070.92660.216300.94340.18950.05480.6593-0.01560.551415.4503-15.919936.0141
300.0090.163-0.0151-0.01870.10070.0137-0.2366-0.8858-0.56620.04660.0566-0.1771-0.09260.0567-0.00050.90180.1143-0.01991.1404-0.03080.538925.6015-8.967165.9416
310.0279-0.0107-0.00340.0070.0030.01480.5718-0.2120.0182-0.062-0.111-0.0020.03640.1378-0.00021.02120.28890.00582.21610.03121.363141.438620.123862.7501
320.01060.02350.01710.0102-0.00470.00680.0253-0.0812-0.22660.10920.49440.4789-0.29620.1550.00010.767-0.1633-0.12971.7674-0.24431.122752.360727.598140.7763
330.16630.12520.03270.10330.10410.2268-0.15660.1309-0.14480.2544-0.20620.20550.08710.26530.00011.10770.06640.19340.9338-0.06021.211314.0945-48.9809-17.1816
340.00850.0114-0.02660.02560.01730.02780.42220.0979-0.06480.06240.68860.0925-0.35730.42540.00012.08330.05860.22380.92150.0741.161726.29-78.9945-8.6353
350.1390.0748-0.04870.07290.04710.02940.4354-0.1193-0.4286-0.1867-0.12380.25310.08160.21420.00463.39781.69320.73542.4893-0.02341.430947.4217-59.1034.9299
360.00070.0043-0.00230.0066-0.00570.003-0.06490.05340.01940.0478-0.09440.2306-0.04980.0717-00.8249-0.1406-0.20570.9908-0.09240.7589-6.49328.007453.6329
370.35921.265-0.2641.45060.02581.8811-0.1224-0.19940.3187-0.58570.5420.9153-1.7333-0.27960.2045-0.029-0.2936-0.39790.52750.05820.88946.518333.501356.5771
380.00920.00750.0059-0.00040.0011-0.00120.0660.04530.0213-0.19020.29860.2893-0.1741-0.0758-0.00011.01050.2448-0.08521.4593-0.1791.174243.554923.429935.527
390.08680.11240.09460.00660.07760.0614-0.50810.4404-0.27891.3610.05350.6965-0.02720.4226-0.01761.35990.0550.23091.1836-0.26081.23836.941429.054457.3256
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 16 through 51 )
2X-RAY DIFFRACTION2chain 'A' and (resid 52 through 75 )
3X-RAY DIFFRACTION3chain 'A' and (resid 76 through 91 )
4X-RAY DIFFRACTION4chain 'A' and (resid 92 through 140 )
5X-RAY DIFFRACTION5chain 'A' and (resid 141 through 176 )
6X-RAY DIFFRACTION6chain 'A' and (resid 177 through 287 )
7X-RAY DIFFRACTION7chain 'A' and (resid 288 through 313 )
8X-RAY DIFFRACTION8chain 'A' and (resid 437 through 453 )
9X-RAY DIFFRACTION9chain 'A' and (resid 454 through 474 )
10X-RAY DIFFRACTION10chain 'A' and (resid 475 through 488 )
11X-RAY DIFFRACTION11chain 'B' and (resid 10 through 39 )
12X-RAY DIFFRACTION12chain 'B' and (resid 40 through 139 )
13X-RAY DIFFRACTION13chain 'B' and (resid 140 through 216 )
14X-RAY DIFFRACTION14chain 'B' and (resid 217 through 233 )
15X-RAY DIFFRACTION15chain 'B' and (resid 234 through 283 )
16X-RAY DIFFRACTION16chain 'B' and (resid 284 through 313 )
17X-RAY DIFFRACTION17chain 'B' and (resid 443 through 455 )
18X-RAY DIFFRACTION18chain 'B' and (resid 456 through 463 )
19X-RAY DIFFRACTION19chain 'B' and (resid 464 through 488 )
20X-RAY DIFFRACTION20chain 'C' and (resid 12 through 75 )
21X-RAY DIFFRACTION21chain 'C' and (resid 76 through 216 )
22X-RAY DIFFRACTION22chain 'C' and (resid 217 through 313 )
23X-RAY DIFFRACTION23chain 'C' and (resid 437 through 473 )
24X-RAY DIFFRACTION24chain 'C' and (resid 474 through 490 )
25X-RAY DIFFRACTION25chain 'D' and (resid 11 through 63 )
26X-RAY DIFFRACTION26chain 'D' and (resid 64 through 99 )
27X-RAY DIFFRACTION27chain 'D' and (resid 100 through 139 )
28X-RAY DIFFRACTION28chain 'D' and (resid 140 through 216 )
29X-RAY DIFFRACTION29chain 'D' and (resid 217 through 283 )
30X-RAY DIFFRACTION30chain 'D' and (resid 284 through 313 )
31X-RAY DIFFRACTION31chain 'D' and (resid 455 through 473 )
32X-RAY DIFFRACTION32chain 'D' and (resid 474 through 489 )
33X-RAY DIFFRACTION33chain 'E' and (resid 367 through 399 )
34X-RAY DIFFRACTION34chain 'E' and (resid 400 through 413 )
35X-RAY DIFFRACTION35chain 'F' and (resid 370 through 398 )
36X-RAY DIFFRACTION36chain 'G' and (resid 366 through 373 )
37X-RAY DIFFRACTION37chain 'G' and (resid 374 through 413 )
38X-RAY DIFFRACTION38chain 'H' and (resid 366 through 373 )
39X-RAY DIFFRACTION39chain 'H' and (resid 374 through 405 )

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