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- PDB-3obv: Autoinhibited Formin mDia1 Structure -

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Basic information

Entry
Database: PDB / ID: 3obv
TitleAutoinhibited Formin mDia1 Structure
Components(Protein diaphanous homolog 1) x 2
KeywordsSTRUCTURAL PROTEIN / AUTOINHIBITION / ACTIN / NUCLEATION / CYTOSKELETON
Function / homology
Function and homology information


negative regulation of neuron projection regeneration / multicellular organismal locomotion / RHOF GTPase cycle / RHOB GTPase cycle / ERBB2 Regulates Cell Motility / RHOC GTPase cycle / RHOD GTPase cycle / RHOA GTPase cycle / actin nucleation / neuron projection retraction ...negative regulation of neuron projection regeneration / multicellular organismal locomotion / RHOF GTPase cycle / RHOB GTPase cycle / ERBB2 Regulates Cell Motility / RHOC GTPase cycle / RHOD GTPase cycle / RHOA GTPase cycle / actin nucleation / neuron projection retraction / RHO GTPases Activate Formins / protein localization to microtubule / profilin binding / cellular response to histamine / regulation of microtubule-based process / regulation of release of sequestered calcium ion into cytosol / axon midline choice point recognition / regulation of cytoskeleton organization / brush border / synaptic vesicle endocytosis / ephrin receptor signaling pathway / cytoskeleton organization / actin filament polymerization / Neutrophil degranulation / actin filament / sensory perception of sound / brain development / protein localization / mitotic spindle / ruffle membrane / small GTPase binding / neuron projection development / presynapse / gene expression / actin binding / regulation of cell shape / actin cytoskeleton organization / transmembrane transporter binding / neuron projection / positive regulation of cell migration / centrosome / identical protein binding / nucleus / cytoplasm
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #630 / Formin, FH3 diaphanous domain / Formin, FH2 domain / Formin Homology Region 1 / Diaphanous, GTPase-binding domain superfamily / Diaphanous autoregulatory (DAD) domain / Diaphanous autoregulatory domain (DAD) profile. / Formin, FH3 domain / Formin, GTPase-binding domain / Diaphanous FH3 Domain ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #630 / Formin, FH3 diaphanous domain / Formin, FH2 domain / Formin Homology Region 1 / Diaphanous, GTPase-binding domain superfamily / Diaphanous autoregulatory (DAD) domain / Diaphanous autoregulatory domain (DAD) profile. / Formin, FH3 domain / Formin, GTPase-binding domain / Diaphanous FH3 Domain / Diaphanous GTPase-binding Domain / Diaphanous FH3 Domain / Diaphanous GTPase-binding Domain / Rho GTPase-binding/formin homology 3 (GBD/FH3) domain / Rho GTPase-binding/formin homology 3 (GBD/FH3) domain profile. / Formin, FH2 domain / Formin, FH2 domain superfamily / Formin Homology 2 Domain / Formin homology-2 (FH2) domain profile. / Formin Homology 2 Domain / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / Recoverin; domain 1 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Armadillo-like helical / Alpha Horseshoe / Armadillo-type fold / Up-down Bundle / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
sucrose / Protein diaphanous homolog 1
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD, MOLECULAR REPLACEMENT / MAD / molecular replacement / Resolution: 2.75 Å
AuthorsTomchick, D.R. / Rosen, M.K. / Otomo, T.
CitationJournal: Plos One / Year: 2010
Title: Crystal structure of the Formin mDia1 in autoinhibited conformation.
Authors: Otomo, T. / Tomchick, D.R. / Otomo, C. / Machius, M. / Rosen, M.K.
History
DepositionAug 9, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 24, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Apr 25, 2012Group: Database references
Revision 1.3Nov 8, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / database_PDB_caveat / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_validate_chiral / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.type / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_atom_id / _pdbx_validate_chiral.auth_comp_id / _pdbx_validate_chiral.auth_seq_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Feb 21, 2024Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Protein diaphanous homolog 1
E: Protein diaphanous homolog 1
B: Protein diaphanous homolog 1
F: Protein diaphanous homolog 1
C: Protein diaphanous homolog 1
G: Protein diaphanous homolog 1
D: Protein diaphanous homolog 1
H: Protein diaphanous homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)365,90316
Polymers363,1648
Non-polymers2,7388
Water0
1
A: Protein diaphanous homolog 1
E: Protein diaphanous homolog 1
B: Protein diaphanous homolog 1
F: Protein diaphanous homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)182,9518
Polymers181,5824
Non-polymers1,3694
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21330 Å2
ΔGint-137 kcal/mol
Surface area76780 Å2
MethodPISA
2
C: Protein diaphanous homolog 1
G: Protein diaphanous homolog 1
D: Protein diaphanous homolog 1
H: Protein diaphanous homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)182,9518
Polymers181,5824
Non-polymers1,3694
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22040 Å2
ΔGint-136 kcal/mol
Surface area77630 Å2
MethodPISA
Unit cell
Length a, b, c (Å)93.926, 208.519, 131.516
Angle α, β, γ (deg.)90.00, 102.74, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
12B
22D

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111METMETVALVALchain A and (resseq 138:161 or resseq 177:192 or resseq...AA138 - 1618 - 31
121GLUGLUGLUGLUchain A and (resseq 138:161 or resseq 177:192 or resseq...AA177 - 19247 - 62
131ASPASPLYSLYSchain A and (resseq 138:161 or resseq 177:192 or resseq...AA201 - 44471 - 314
211METMETVALVALchain C and (resseq 138:161 or resseq 177:192 or resseq...CE138 - 1618 - 31
221GLUGLUGLUGLUchain C and (resseq 138:161 or resseq 177:192 or resseq...CE177 - 19247 - 62
231ASPASPLYSLYSchain C and (resseq 138:161 or resseq 177:192 or resseq...CE201 - 44471 - 314
112METMETVALVALchain B and (resseq 138:161 or resseq 177:192 or resseq...BC138 - 1618 - 31
122GLUGLUGLUGLUchain B and (resseq 138:161 or resseq 177:192 or resseq...BC177 - 19247 - 62
132ASPASPLYSLYSchain B and (resseq 138:161 or resseq 177:192 or resseq...BC201 - 44471 - 314
212METMETVALVALchain D and (resseq 138:161 or resseq 177:192 or resseq...DG138 - 1618 - 31
222GLUGLUGLUGLUchain D and (resseq 138:161 or resseq 177:192 or resseq...DG177 - 19247 - 62
232ASPASPLYSLYSchain D and (resseq 138:161 or resseq 177:192 or resseq...DG201 - 44471 - 314

NCS ensembles :
ID
1
2

NCS oper:
IDCodeMatrixVector
1given(0.988766, -0.003049, 0.149444), (-0.00319, -0.999995, 0.000706), (0.149441, -0.001175, -0.98877)0.668729, 18.2229, -6.97453
2given(0.988654, 0.001787, 0.150199), (0.001369, -0.999995, 0.00289), (0.150204, -0.002652, -0.988652)0.505, 17.906401, -6.95406
DetailsThe biomolecule is a dimer. There are two biomolecule in the asymmetric unit. Biomolecule one which contains chain A, E, B, and F, biomolecule two contains chain C, G, D and H

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Components

#1: Protein
Protein diaphanous homolog 1 / Diaphanous-related formin-1 / DRF1 / p140mDIA / mDIA1


Mass: 37721.316 Da / Num. of mol.: 4 / Fragment: N-terminal fragment, UNP residues 131-457
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Diaph1, Diap1 / Plasmid: pET11A / Production host: Escherichia coli (E. coli) / References: UniProt: O08808
#2: Protein
Protein diaphanous homolog 1 / Diaphanous-related formin-1 / DRF1 / p140mDIA / mDIA1


Mass: 53069.777 Da / Num. of mol.: 4 / Fragment: C-terminal fragment, UNP residues 753-1209
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Diaph1, Diap1 / Plasmid: pET11A / Production host: Escherichia coli (E. coli) / References: UniProt: O08808
#3: Polysaccharide
beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose / sucrose /


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Details: oligosaccharide with reducing-end-to-reducing-end glycosidic bond
References: sucrose
DescriptorTypeProgram
DFrufb2-1DGlcpaGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[ha122h-2b_2-5][a2122h-1a_1-5]/1-2/a2-b1WURCSPDB2Glycan 1.1.0
[][a-L-Psif]{[(2+1)][a-D-Altp]{}}LINUCSPDB-CARE
Compound detailsAUTHOR STATE THAT THE LOOP REGION OF PROTEIN DIAPHANOUS HOMOLOG 1 WAS REMOVED FOR CRYSTALLIZATION. ...AUTHOR STATE THAT THE LOOP REGION OF PROTEIN DIAPHANOUS HOMOLOG 1 WAS REMOVED FOR CRYSTALLIZATION. THERE ARE FOUR COPIES OF PROTEIN DIAPHANOUS HOMOLOG 1 IN THE ASYMMETRIC UNTI MADE OF N-TERMINAL(CHAIN A,B,C,D) AND C-TERMINAL(E,F,G,H) OF THE PROTEIN RESPECTIVELY

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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: 3.46 Å3/Da / Density % sol: 64.44 %
Crystal growTemperature: 293 K / pH: 6.75
Details: 10% PEG 1500, 25% sucrose, 0.1 M MES pH 6.75, 0.15 M NaCl, 1 mM DTT, vapor diffusion, hanging drop, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97937
DetectorType: SBC-3 / Detector: CCD / Date: May 13, 2005 / Details: MONOCHROMATOR
RadiationMonochromator: SAGITALLY FOCUSED SI(111) / Protocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97937 Å / Relative weight: 1
ReflectionResolution: 2.75→50 Å / Num. obs: 123292 / % possible obs: 95.4 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Rmerge(I) obs: 0.054 / Net I/σ(I): 14.3
Reflection shellResolution: 2.75→2.81 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.541 / % possible all: 60.5

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Phasing

Phasing
Method
MAD
molecular replacement

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Processing

Software
NameVersionClassificationNB
SCALEPACKdata scaling
AMoREphasing
MLPHAREphasing
DMphasing
PHENIX1.6.4_486refinement
PDB_EXTRACT3.1data extraction
DENZOdata reduction
HKL-3000data scaling
RefinementMethod to determine structure: MAD, MOLECULAR REPLACEMENT / Resolution: 2.75→29.95 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.45 / σ(F): 1.34 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.261 1799 1.47 %
Rwork0.199 --
obs0.2 122258 95.8 %
all-122258 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 63.74 Å2 / ksol: 0.33 e/Å3
Displacement parametersBiso mean: 102.03 Å2
Baniso -1Baniso -2Baniso -3
1-5.536 Å20 Å2-8.3433 Å2
2--8.0751 Å20 Å2
3----13.6111 Å2
Refine analyzeLuzzati sigma a free: 0.45 Å
Refinement stepCycle: LAST / Resolution: 2.75→29.95 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24040 0 184 0 24224
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00924585
X-RAY DIFFRACTIONf_angle_d1.3533045
X-RAY DIFFRACTIONf_dihedral_angle_d17.3419940
X-RAY DIFFRACTIONf_chiral_restr0.1923716
X-RAY DIFFRACTIONf_plane_restr0.0044293
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A5633X-RAY DIFFRACTIONPOSITIONAL0.039
12C5633X-RAY DIFFRACTIONPOSITIONAL0.039
21B5626X-RAY DIFFRACTIONPOSITIONAL0.068
22D5626X-RAY DIFFRACTIONPOSITIONAL0.068
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.75-2.84820.42611240.35248435X-RAY DIFFRACTION67
2.8482-2.96220.37711730.302611509X-RAY DIFFRACTION92
2.9622-3.09680.39611790.273612465X-RAY DIFFRACTION100
3.0968-3.25990.30891910.265412586X-RAY DIFFRACTION100
3.2599-3.46390.27851880.229612548X-RAY DIFFRACTION100
3.4639-3.73090.25832010.211612521X-RAY DIFFRACTION100
3.7309-4.10550.24342050.180112564X-RAY DIFFRACTION100
4.1055-4.69760.24352010.158512559X-RAY DIFFRACTION100
4.6976-5.9110.26661790.189112589X-RAY DIFFRACTION100
5.911-29.94760.21181580.176112683X-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)
10.4573-0.1051-0.450.9241-0.14540.4505-0.1035-0.1913-0.25320.67060.00970.7434-0.16820.03830.00020.81990.15930.45170.69110.12730.760617.36424.518235.6115
20.2329-0.5855-0.89831.70491.36542.01790.08730.0036-0.10130.21320.00080.03350.1473-0.0109-0.00010.31320.0830.06220.29880.09820.446340.9282-6.4329.8969
30.1192-0.23280.25460.263-0.30340.36850.1907-0.7586-0.24191.13650.0397-0.6864-0.2750.3306-0.00010.66780.1216-0.21650.5989-0.22960.473275.9906-62.966115.37
40.4933-0.20620.34790.69330.61010.5434-0.1010.0052-0.19940.37120.0403-0.08720.0893-0.34860.00010.82690.1890.18221.17130.04290.621820.6773-72.882930.993
50.859-0.53170.5490.29380.30471.438-0.13010.09190.1803-0.27890.23060.19290.1721-0.8299-0.00150.39050.0618-0.12370.78910.0610.476113.5049-58.456-10.2904
60.16630.1899-0.70640.12350.27280.2499-0.23850.1709-0.2937-0.37380.18-0.30250.1354-0.2062-0.00030.70140.0098-0.06650.54790.11490.4342.0772-31.6057-35.8582
70.03350.05660.03530.04550.06030.03450.31570.22470.5830.4564-0.1841-0.89780.01210.31040.00130.95590.02220.15750.5786-0.02890.52266.8527-1.9239-55.2481
80.16510.19970.09830.14710.13790.0794-0.51540.5882-0.3041-1.12520.2408-0.9489-0.77540.0946-0.00340.7715-0.11480.56441.2358-0.04320.845190.508-2.881-57.461
90.81281.0504-0.93811.4211-0.78431.64460.05410.2082-0.1967-0.12590.1467-0.1807-0.0510.1395-00.29030.11680.13240.4768-0.06560.393864.4752-8.3693-30.2973
100.14970.20840.134-0.02890.11920.0681-0.03810.1491-0.1475-0.99980.04160.2847-0.1169-0.0722-0.00010.94440.0762-0.25181.22040.01380.619915.5478-53.5174-38.3801
110.2984-0.57850.48250.5611-0.51440.25310.44350.5574-0.3543-0.6518-0.61750.0117-0.31-0.2145-0.00081.02090.2263-0.02481.4803-0.32550.800866.0866-77.7873-53.6573
120.6241-0.2287-0.13390.18190.37890.9295-0.020.02190.15880.09070.1047-0.39910.0457-0.08320.00020.5171-0.08210.02160.4565-0.10940.678676.6318-67.6578-12.6405
130.1699-0.2025-1.0604-0.06920.06040.47340.01360.09880.14620.51850.2559-0.61640.1851-0.1977-0.00010.76860.1788-0.14550.494-0.03990.552557.4755-36.322112.4729
140.1991-0.04840.06520.05780.02280.0181-0.0105-0.85980.2870.19150.17460.22890.48020.2470.00040.93720.06790.13210.45660.23020.580440.3694-3.731334.9292
150.6593-0.01810.6241.1280.12970.5355-0.05920.1379-0.0467-0.695-0.14260.49520.00960.1248-0.00010.6266-0.0372-0.27140.45020.00720.468622.764613.5756-39.6281
160.31260.41410.98381.50751.46322.60270.03690.02290.0535-0.09630.00290.0607-0.07380.015-0.00010.2342-0.0253-0.02830.20650.06570.359242.408724.5084-10.6802
170.06970.0360.08770.0435-0.09040.09060.12310.62480.4695-0.8384-0.336-0.37310.56530.1469-0.00020.9557-0.10770.22151.0514-0.21720.819978.076580.9479-10.9355
180.441-0.30820.0470.81550.17280.2195-0.0341-0.1492-0.0343-0.74080.22420.02230.3133-0.28460.00041.042-0.2962-0.28760.83830.11460.439425.764891.0239-34.6279
190.24770.0585-0.36540.19750.30491.10720.00550.0178-0.0430.00290.42860.44410.1041-0.49450.00020.3196-0.243-0.02750.85310.31750.74912.446576.64215.1441
200.21540.10420.4740.00020.14340.3853-0.17910.0295-0.10520.16190.36440.22470.1036-0.0525-0.00020.62240.0860.15120.71890.0870.541536.776749.730634.7126
210.0355-0.05150.03930.08610.03690.02910.048-0.6775-0.3266-0.1008-0.0781-0.35510.1139-0.06080.0010.67020.0638-0.03530.4739-0.03230.433657.598919.977256.7867
220.4558-0.05270.5010.71680.07630.3801-0.709-0.08440.24810.78690.2381-0.49280.1445-0.1765-0.00010.75490.1681-0.32420.8070.07970.521781.614221.133562.2283
230.6571-1.04371.30651.0648-1.32342.5430.0297-0.09990.09430.07530.07090.04370.05720.0607-00.2904-0.015-0.06850.2703-0.00580.24959.954826.332132.7022
240.1473-0.0866-0.15210.00510.06650.0413-0.04730.49160.64261.0482-0.10480.5929-0.31970.2269-0.00060.9357-0.05420.17151.39860.15880.89669.495771.60432.8806
250.4660.5879-0.11690.4782-0.04940.28210.10720.2730.08790.3184-0.4018-0.04130.076-0.2086-0.00010.7187-0.14720.1460.8032-0.21260.568557.455196.156456.2745
260.3835-0.23440.02210.31290.18141.19760.09080.0297-0.0264-0.14740.0207-0.2728-0.1293-0.14390.00010.3794-0.0580.05880.4639-0.10150.608274.253285.680516.9168
270.04360.82451.2570.96441.08141.27310.0454-0.0164-0.0653-0.2450.432-0.6274-0.0108-0.08110.05720.6617-0.24640.12930.5826-0.06750.622158.305853.0413-12.341
280.0004-0.0014-0.00020.00160.0005-0.0004-0.0392-0.00910.0199-0.097-0.0811-0.04520.0150.0216-0.00052.18350.27280.55052.28030.24961.722130.6156-9.49484.7996
290.00150.0021-0.00030.00180.0013-0.0005-0.0647-0.02350.0315-0.0271-0.05290.03750.1094-0.10190.00042.0555-0.2216-0.45342.3211-0.28721.23373.85-14.9538-25.5541
300.0014-0.0021-0.00010.00110.0012-0.0007-0.03210.0038-0.0148-0.033-0.0974-0.0148-0.15750.00590.00041.7966-0.03950.53232.2848-0.56411.76469.568133.17729.6847
310.00150.00140.00020.0011-0.0005-0.00040.0139-0.0111-0.0480.0893-0.01920.0247-0.0033-0.0052-0.00022.1244-0.38010.24392.52770.24991.958731.559127.8654-6.988
320.00050.00020.00050.000700.00140.0095-0.0326-0.0085-0.01480.0197-0.0257-0.0264-0.0085-0.00052.1085-0.12350.06142.64670.15512.139761.6902-13.9861-0.2335
330.00170.00070.0010.0020.00210.0010.0046-0.02340.031-0.00270.00170.006-0.05050.00140.00012.64070.47230.22982.51330.81141.662843.1712-9.7798-20.5871
340.0012-0.001-0.00030.00120.00060.001-0.0195-0.00160.03380.02140.038-0.04340.00970.0218-0.00043.0803-0.0534-0.48881.82180.74051.701740.384628.183220.1186
350.00140.000100.00020.00050.0005-0.01110.04870.0214-0.0164-0.0529-0.02060.00430.0296-02.04880.23180.33552.3148-0.13132.713861.705932.41481.9585
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 131:196)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 197:452)
3X-RAY DIFFRACTION3(CHAIN E AND RESID 754:805)
4X-RAY DIFFRACTION4(CHAIN E AND RESID 829:937)
5X-RAY DIFFRACTION5(CHAIN E AND RESID 938:1118)
6X-RAY DIFFRACTION6(CHAIN E AND RESID 1119:1173)
7X-RAY DIFFRACTION7(CHAIN E AND RESID 1174:1195)
8X-RAY DIFFRACTION8(CHAIN B AND RESID 132:192)
9X-RAY DIFFRACTION9(CHAIN B AND RESID 200:457)
10X-RAY DIFFRACTION10(CHAIN F AND RESID 754:805)
11X-RAY DIFFRACTION11(CHAIN F AND RESID 830:939)
12X-RAY DIFFRACTION12(CHAIN F AND RESID 940:1118)
13X-RAY DIFFRACTION13(CHAIN F AND RESID 1119:1170)
14X-RAY DIFFRACTION14(CHAIN F AND RESID 1171:1196)
15X-RAY DIFFRACTION15(CHAIN C AND RESID 131:196)
16X-RAY DIFFRACTION16(CHAIN C AND RESID 197:452)
17X-RAY DIFFRACTION17(CHAIN G AND RESID 754:805)
18X-RAY DIFFRACTION18(CHAIN G AND RESID 829:937)
19X-RAY DIFFRACTION19(CHAIN G AND RESID 938:1118)
20X-RAY DIFFRACTION20(CHAIN G AND RESID 1119:1173)
21X-RAY DIFFRACTION21(CHAIN G AND RESID 1174:1196)
22X-RAY DIFFRACTION22(CHAIN D AND RESID 131:196)
23X-RAY DIFFRACTION23(CHAIN D AND RESID 197:457)
24X-RAY DIFFRACTION24(CHAIN H AND RESID 753:804)
25X-RAY DIFFRACTION25(CHAIN H AND RESID 830:937)
26X-RAY DIFFRACTION26(CHAIN H AND RESID 938:1118)
27X-RAY DIFFRACTION27(CHAIN H AND RESID 1119:1173)
28X-RAY DIFFRACTION28(CHAIN A AND RESID 2001:2001)
29X-RAY DIFFRACTION29(CHAIN B AND RESID 2002:2002)
30X-RAY DIFFRACTION30(CHAIN D AND RESID 2003:2003)
31X-RAY DIFFRACTION31(CHAIN C AND RESID 2004:2004)
32X-RAY DIFFRACTION32(CHAIN A AND RESID 2005:2005)
33X-RAY DIFFRACTION33(CHAIN B AND RESID 2006:2006)
34X-RAY DIFFRACTION34(CHAIN D AND RESID 2007:2007)
35X-RAY DIFFRACTION35(CHAIN C AND RESID 2008:2008)

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