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- PDB-5jcz: Rab11 bound to MyoVa-GTD -

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Basic information

Entry
Database: PDB / ID: 5jcz
TitleRab11 bound to MyoVa-GTD
Components
  • Ras-related protein Rab-11A
  • Unconventional myosin-Va
KeywordsMOTOR PROTEIN / myosin / complex / Rab / motor cargo recognition
Function / homology
Function and homology information


regulation of early endosome to recycling endosome transport / regulation of protein localization to centrosome / synaptic vesicle endosomal processing / early endosome to recycling endosome transport / regulation of endocytic recycling / establishment of protein localization to organelle / postsynaptic recycling endosome / positive regulation of mitotic cytokinetic process / vesicle transport along actin filament / establishment of vesicle localization ...regulation of early endosome to recycling endosome transport / regulation of protein localization to centrosome / synaptic vesicle endosomal processing / early endosome to recycling endosome transport / regulation of endocytic recycling / establishment of protein localization to organelle / postsynaptic recycling endosome / positive regulation of mitotic cytokinetic process / vesicle transport along actin filament / establishment of vesicle localization / plasma membrane to endosome transport / post-Golgi vesicle-mediated transport / insulin-responsive compartment / amyloid-beta clearance by transcytosis / regulation of cilium assembly / regulation of protein transport / presynaptic endosome / exosomal secretion / neurotransmitter receptor transport, endosome to postsynaptic membrane / astral microtubule organization / vesicle-mediated transport in synapse / VxPx cargo-targeting to cilium / protein transmembrane transport / filopodium tip / actin filament-based movement / regulation of vesicle-mediated transport / myosin V binding / RAB geranylgeranylation / multivesicular body assembly / melanosome transport / protein localization to cilium / Golgi to plasma membrane protein transport / establishment of protein localization to membrane / myosin complex / protein localization to cell surface / TBC/RABGAPs / syntaxin binding / dynein light intermediate chain binding / mitotic metaphase chromosome alignment / microfilament motor activity / Insulin processing / exocytosis / Regulation of MITF-M-dependent genes involved in pigmentation / cleavage furrow / positive regulation of epithelial cell migration / mitotic spindle assembly / positive regulation of G2/M transition of mitotic cell cycle / transport vesicle / vesicle-mediated transport / phagocytic vesicle / ruffle / multivesicular body / centriole / Anchoring of the basal body to the plasma membrane / actin filament organization / cytoplasmic vesicle membrane / trans-Golgi network membrane / small monomeric GTPase / regulation of cytokinesis / protein localization to plasma membrane / positive regulation of protein localization to plasma membrane / FCGR3A-mediated phagocytosis / Translocation of SLC2A4 (GLUT4) to the plasma membrane / trans-Golgi network / regulation of long-term neuronal synaptic plasticity / recycling endosome / Regulation of actin dynamics for phagocytic cup formation / small GTPase binding / Schaffer collateral - CA1 synapse / cellular response to insulin stimulus / recycling endosome membrane / neuron projection development / spindle pole / actin filament binding / synaptic vesicle membrane / endocytic vesicle membrane / Vasopressin regulates renal water homeostasis via Aquaporins / melanosome / actin cytoskeleton / protein transport / growth cone / G protein activity / cytoplasmic vesicle / microtubule binding / vesicle / calmodulin binding / neuron projection / Golgi membrane / GTPase activity / centrosome / GTP binding / glutamatergic synapse / Golgi apparatus / ATP hydrolysis activity / protein-containing complex / RNA binding / extracellular exosome / ATP binding / membrane / cytosol
Similarity search - Function
: / Myosin 5a, cargo-binding domain / Class V myosin, motor domain / Dilute domain / DIL domain / Dilute domain profile. / DIL / IQ calmodulin-binding motif / Small GTPase Rab domain profile. / Myosin, N-terminal, SH3-like ...: / Myosin 5a, cargo-binding domain / Class V myosin, motor domain / Dilute domain / DIL domain / Dilute domain profile. / DIL / IQ calmodulin-binding motif / Small GTPase Rab domain profile. / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Short calmodulin-binding motif containing conserved Ile and Gln residues. / IQ motif, EF-hand binding site / Myosin motor domain profile. / Myosin head, motor domain / Myosin head (motor domain) / Myosin. Large ATPases. / IQ motif profile. / Kinesin motor domain superfamily / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Small GTP-binding protein domain / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / BERYLLIUM TRIFLUORIDE ION / GUANOSINE-5'-DIPHOSPHATE / Ras-related protein Rab-11A / Unconventional myosin-Va
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.056 Å
AuthorsPylypenko, O. / Attanda, W. / Gauquelin, C. / Malherbes, G. / Houdusse, A.
CitationJournal: Elife / Year: 2016
Title: Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes.
Authors: Pylypenko, O. / Welz, T. / Tittel, J. / Kollmar, M. / Chardon, F. / Malherbe, G. / Weiss, S. / Michel, C.I. / Samol-Wolf, A. / Grasskamp, A.T. / Hume, A. / Goud, B. / Baron, B. / England, P. ...Authors: Pylypenko, O. / Welz, T. / Tittel, J. / Kollmar, M. / Chardon, F. / Malherbe, G. / Weiss, S. / Michel, C.I. / Samol-Wolf, A. / Grasskamp, A.T. / Hume, A. / Goud, B. / Baron, B. / England, P. / Titus, M.A. / Schwille, P. / Weidemann, T. / Houdusse, A. / Kerkhoff, E.
History
DepositionApr 15, 2016Deposition site: RCSB / Processing site: PDBE
Revision 1.0Sep 28, 2016Provider: repository / Type: Initial release
Revision 2.0Oct 24, 2018Group: Atomic model / Data collection / Derived calculations
Category: atom_site / pdbx_nonpoly_scheme ...atom_site / pdbx_nonpoly_scheme / struct_conn / struct_conn_type
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 / _pdbx_nonpoly_scheme.auth_seq_num
Revision 2.1Jan 10, 2024Group: 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
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_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ras-related protein Rab-11A
B: Unconventional myosin-Va
C: Unconventional myosin-Va
D: Ras-related protein Rab-11A
E: Unconventional myosin-Va
I: Ras-related protein Rab-11A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)199,08833
Polymers196,3546
Non-polymers2,73427
Water20,7891154
1
A: Ras-related protein Rab-11A
B: Unconventional myosin-Va
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,53813
Polymers65,4512
Non-polymers1,08711
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
C: Unconventional myosin-Va
D: Ras-related protein Rab-11A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,44013
Polymers65,4512
Non-polymers98911
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
E: Unconventional myosin-Va
I: Ras-related protein Rab-11A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,1097
Polymers65,4512
Non-polymers6585
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)215.790, 128.420, 89.020
Angle α, β, γ (deg.)90.00, 98.27, 90.00
Int Tables number5
Space group name H-MC121

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Components

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Protein , 2 types, 6 molecules ADIBCE

#1: Protein Ras-related protein Rab-11A / Rab-11 / YL8


Mass: 20100.598 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RAB11A, RAB11 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P62491
#2: Protein Unconventional myosin-Va / Dilute myosin heavy chain / non-muscle / Myosin heavy chain 12 / Myosin-12 / Myoxin


Mass: 45350.605 Da / Num. of mol.: 3 / Fragment: UNP residues 1437-1828
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MYO5A, MYH12 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9Y4I1

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Non-polymers , 7 types, 1181 molecules

#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#5: Chemical ChemComp-BEF / BERYLLIUM TRIFLUORIDE ION


Mass: 66.007 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: BeF3
#6: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: C2H6O2
#7: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#8: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1154 / Source method: isolated from a natural source / Formula: H2O

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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: 3.11 Å3/Da / Density % sol: 60.43 %
Crystal growTemperature: 290 K / Method: vapor diffusion, hanging drop
Details: 7% (w/v) PEG-8000, 50 mM Bicine, 50 mM Tris, 30mM sodium fluoride, 20% (v/v) ethylene glycol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.98011 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jun 6, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98011 Å / Relative weight: 1
ReflectionResolution: 2.056→48.88 Å / Num. obs: 146774 / % possible obs: 98.6 % / Redundancy: 7.7 % / Net I/σ(I): 20.58
Reflection shellResolution: 2.056→2.18 Å / Rmerge(I) obs: 0.555

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
XDSdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4LX1

4lx1


Resolution: 2.056→48.879 Å / SU ML: 0.2 / Cross valid method: FREE R-VALUE / σ(F): 2 / Phase error: 21.55
RfactorNum. reflection% reflection
Rfree0.2083 7338 5 %
Rwork0.1797 --
obs0.1811 146754 98.57 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.056→48.879 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12385 0 172 1154 13711
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00212915
X-RAY DIFFRACTIONf_angle_d0.59317456
X-RAY DIFFRACTIONf_dihedral_angle_d12.5434791
X-RAY DIFFRACTIONf_chiral_restr0.0222027
X-RAY DIFFRACTIONf_plane_restr0.0032212
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.0558-2.07920.27762300.23844371X-RAY DIFFRACTION93
2.0792-2.10360.2452410.23314579X-RAY DIFFRACTION98
2.1036-2.12930.2752450.22014656X-RAY DIFFRACTION98
2.1293-2.15620.25212400.21084559X-RAY DIFFRACTION98
2.1562-2.18460.25252410.20684581X-RAY DIFFRACTION98
2.1846-2.21450.24592450.1964656X-RAY DIFFRACTION98
2.2145-2.24620.22252420.19314587X-RAY DIFFRACTION98
2.2462-2.27970.21642440.19154647X-RAY DIFFRACTION98
2.2797-2.31530.23942390.19014545X-RAY DIFFRACTION98
2.3153-2.35330.21692470.1894684X-RAY DIFFRACTION98
2.3533-2.39390.24982410.1864577X-RAY DIFFRACTION98
2.3939-2.43740.2192450.18074660X-RAY DIFFRACTION99
2.4374-2.48430.23382450.18164649X-RAY DIFFRACTION98
2.4843-2.5350.232440.18664633X-RAY DIFFRACTION99
2.535-2.59010.22992440.19044643X-RAY DIFFRACTION99
2.5901-2.65030.23752440.18424629X-RAY DIFFRACTION99
2.6503-2.71660.22652460.18944674X-RAY DIFFRACTION99
2.7166-2.79010.25932460.1984681X-RAY DIFFRACTION99
2.7901-2.87220.24412440.20224641X-RAY DIFFRACTION99
2.8722-2.96480.23632460.19624661X-RAY DIFFRACTION99
2.9648-3.07080.23732460.19184681X-RAY DIFFRACTION99
3.0708-3.19370.21622460.19244683X-RAY DIFFRACTION99
3.1937-3.3390.22012460.18874660X-RAY DIFFRACTION99
3.339-3.5150.20042460.18624680X-RAY DIFFRACTION99
3.515-3.73520.21452470.1724703X-RAY DIFFRACTION99
3.7352-4.02350.1692490.16044727X-RAY DIFFRACTION99
4.0235-4.42810.17732470.14984696X-RAY DIFFRACTION100
4.4281-5.06830.18242490.14674720X-RAY DIFFRACTION100
5.0683-6.38330.21862500.18954754X-RAY DIFFRACTION100
6.3833-48.89320.1882530.18714799X-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)
11.21870.37490.32530.894-0.83560.8531-0.0510.241-0.2691-0.29350.05510.0631-0.0346-0.1675-0.00010.43580.0109-0.00840.30190.01910.453139.24776.087423.6072
2-0.01990.0407-0.01880.1836-0.12080.0521-0.09970.10550.2324-0.20980.31450.7030.0056-0.8396-0.00050.49890.0291-0.05140.39710.11950.613428.244314.554124.2261
30.3892-0.110.61730.5344-0.23670.83360.10780.483-0.2797-0.3122-0.09080.2013-0.2483-0.0109-0.00010.5104-0.0538-0.02590.39310.02470.507541.55261.664920.3488
40.42840.14450.30540.4364-0.14670.23290.1421-0.9909-0.30040.51140.09140.0053-0.1969-0.02080.00010.53390.0061-0.01920.46050.13840.535335.34450.163737.7625
50.53390.3186-0.10630.33510.17380.6576-0.0543-0.4331-0.0730.26820.0363-0.2245-0.01850.0455-0.00010.51480.0586-0.04940.36730.11660.402741.961213.147439.0585
61.27210.84710.21150.47190.13790.3017-0.03740.0081-0.0193-0.23450.0464-0.2067-0.00180.0784-0.00010.48320.0077-0.03780.29680.0410.415844.563617.250331.2864
70.117-0.06680.03140.0052-0.03280.0279-0.17790.1550.53240.1613-0.2457-1.6075-0.41311.05980.00050.5469-0.0007-0.07470.42330.04910.597953.167719.55636.362
80.1817-0.2455-0.27920.26840.27760.29020.23310.3507-0.0572-0.3513-0.14-0.15390.21680.3866-0.00020.4831-0.0106-0.04610.30130.06280.419545.832217.703926.3875
90.21620.24210.27140.26990.30820.25390.32780.6341-0.2423-0.5628-0.4848-0.58780.17550.49490.00020.51650.00440.00810.38720.01560.584751.3775.096222.5457
101.1832-0.2594-0.48461.03060.350.93770.07011.0308-0.6022-0.167-0.01880.15310.7083-0.3772-0.00010.789-0.32520.03771.1519-0.27530.713714.5318-9.1887-22.5256
111.24950.5261-0.6630.4406-0.35673.1154-0.19530.5059-0.3041-0.06590.1715-0.08260.43-0.5596-0.00040.5088-0.15150.01680.6503-0.11060.649317.396-5.2054-1.212
123.5014-0.50930.28161.63551.1892.0159-0.0826-0.4609-0.28840.21070.03950.16770.0492-0.20720.00010.4037-0.01350.00470.42670.09730.557218.9522-1.568329.7316
130.51260.28580.86391.0927-1.42211.7301-0.28510.7483-0.0843-0.22220.3078-0.07170.3421-1.344100.5227-0.1804-0.00830.9478-0.06130.628215.0548-2.6198-5.1943
140.4603-0.21510.12370.42190.30880.4263-0.1166-0.22990.16390.39480.0631-0.26350.06440.413700.60930.0264-0.07610.41740.02050.489247.406445.694748.878
151.3226-0.49170.70212.79771.31282.3234-0.00060.0214-0.00660.22880.0479-0.08630.02110.106700.38280.0007-0.03850.2240.07540.353440.410844.208238.5684
160.42610.69950.0081.0581-0.30340.54390.22360.37010.2088-0.0781-0.0817-0.042-0.8018-0.23010.00020.4802-0.0043-0.020.39350.12770.462642.499149.674819.3188
170.9511-0.04660.81351.53540.00910.635-0.08720.17640.0681-0.01430.1623-0.30690.3630.73890.00010.4089-0.00390.01650.61040.03630.489450.978437.35159.5939
180.6399-0.3403-0.2041.40710.70771.46120.03840.140.0075-0.06460.0131-0.12380.09420.1588-00.3569-0.01450.02410.43210.08550.33541.218338.31681.4743
190.1982-0.2694-0.1310.29060.27430.45110.09780.2657-0.1752-0.3923-0.18910.14050.0276-0.4553-0.00010.59130.00710.00630.62960.0940.408131.669942.3268-14.553
200.58680.5380.64710.85150.1731.23040.84620.4862-0.1761-1.1368-0.56020.0915-0.3384-0.11010.00220.81230.1314-0.02330.78890.05280.441835.121345.0548-21.0402
210.3060.1872-0.45310.11560.81911.3051-0.0280.1575-0.07010.12560.0926-0.0801-0.0227-0.0005-0.00010.42290.0162-0.01020.35170.07130.440938.828542.554626.0177
221.01-0.1945-0.8621.5838-0.14490.5552-0.0558-0.0856-0.06050.18510.0376-0.2318-0.10210.093300.4413-0.01850.0220.54420.02580.461544.842819.3352-3.9304
230.45380.7232-0.35441.59960.60691.08370.03360.0878-0.05870.27750.03710.2021-0.1749-0.2149-00.45860.00940.05720.51570.07110.476438.454721.734-2.6255
241.19970.5685-0.44741.99831.14511.0738-0.04460.502-0.1049-0.53410.0743-0.4284-0.23560.097500.5121-0.01370.11370.59470.06620.49347.899423.5674-12.0212
250.0040.0449-0.00190.10680.02940.047-0.27790.09310.1331-0.11390.24150.18960.1856-0.1909-0.00020.4691-0.01470.05660.682-0.09870.502336.950710.9939-13.5378
260.1009-0.09260.06520.1358-0.06190.4108-0.11270.7575-0.1814-1.22450.1768-0.11330.1408-0.07520.00350.7093-0.01950.18720.8676-0.05990.49541.226514.0679-22.2978
270.8284-0.44830.83871.49210.28531.2150.12130.1269-0.4394-0.0317-0.0806-0.19270.39090.107900.4608-0.02170.06860.611-0.1020.52939.38625.8923-11.9081
280.0650.0684-0.00140.121-0.11590.10890.0736-0.0345-0.874-0.2635-0.347-0.64070.29690.22570.00020.46560.02030.07210.60970.04240.794352.777410.4962-3.8701
291.25760.1990.60021.1699-0.71990.96190.24620.67410.424-0.7134-0.0242-0.3852-1.0166-0.59460.04770.76920.22570.08050.84310.22650.541122.836172.7868-2.2549
301.8169-1.2898-1.82551.99560.20723.52430.14970.52970.0655-0.3245-0.1245-0.0883-0.2691-0.72760.00460.38760.0643-0.00290.65480.11980.371921.990965.19744.7729
310.1349-0.0160.0543-0.0927-0.1750.77230.04090.26960.08710.21150.3023-0.29960.30730.33530.00010.38850.0514-0.0150.47270.04490.529129.518869.017921.9787
320.956-0.60270.06120.6438-0.0724.9821-0.0856-0.10180.15540.09450.05030.1264-0.3006-0.9677-0.00010.38910.09950.00470.47650.02550.465721.511173.207641.8932
330.8818-0.1354-0.02170.51190.12112.50610.06310.05970.08910.07860.04890.172-0.2023-0.57470.00130.48850.07540.02580.4660.05710.472623.582666.848933.6849
340.4090.598-0.2910.943-0.27190.2337-0.09720.36310.2171-0.29030.22660.64750.0618-0.39890.01230.07690.12650.16580.29080.06360.48962.722980.920550.2931
350.46530.64870.79595.57211.89311.5541-0.27130.1836-0.3338-1.3963-0.2291.055-0.1216-0.2326-0.3469-0.5610.00540.4990.45470.13290.01042.904171.333549.1233
360.9370.45640.62170.20830.28250.40340.2283-0.5995-0.35420.3392-0.04450.1804-0.1243-0.5970.08240.28630.09960.12260.2762-0.01420.41579.982582.806247.9739
370.06270.01190.00790.5386-0.69440.93380.1501-0.16470.14050.15120.66720.16680.0067-0.3340.07840.3448-0.02480.05120.4008-0.25130.526812.988984.467359.1054
380.143-0.13560.00620.1135-0.05690.0137-0.4622-0.31180.3033-0.31090.57950.2546-0.1309-0.22910.0060.3361-0.03420.04310.4491-0.09970.3721-0.199383.346863.3598
391.1864-0.23411.04691.2916-0.04962.32270.0919-0.0576-0.28560.25770.30920.05530.4401-0.31760.46130.06820.1530.18560.1201-0.1260.5379-0.146689.8456.6149
400.3738-0.78470.86411.6761-1.84072.0080.14090.081-0.1469-0.5137-0.1722-0.01350.6216-0.07850.0043-0.2103-0.15780.1680.59090.04780.3107-14.30677.406556.8092
410.0672-0.04880.1580.1968-0.24560.45150.0715-0.2060.1320.09320.29510.1664-0.3332-0.20160.0498-0.1730.20070.31540.4322-0.28170.5355-10.517690.811462.4617
420.39130.488-0.3560.5887-0.41590.3076-0.05990.79030.0425-0.5877-0.0590.19430.318-0.5772-0.00970.25380.0748-0.02540.46850.04660.4809-7.748485.080452.0764
430.57310.4853-0.9940.7819-1.15781.9161-0.38670.4388-0.8286-0.26540.25540.10580.7943-0.2844-0.037-0.56710.32070.31740.1302-0.09660.3687-0.995692.977546.4259
440.0464-0.0141-0.04580.1515-0.01520.08180.0167-0.0919-0.22190.16450.1830.4497-0.1323-0.28730.00110.48750.0259-0.06320.31180.0770.499932.256217.045328.4256
450.08890.03170.03020.1212-0.03390.0573-0.2629-0.1347-0.24670.31560.3269-0.01690.04640.20740.00060.4587-0.03760.03060.6190.00850.449931.321517.8517-8.6289
460.05180.01030.00140.006-0.00420.00890.1121-0.0319-0.0172-0.11180.338-0.21290.2144-0.14440.00040.2794-0.10220.06910.231-0.05180.5416-0.691173.327553.505
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 6 through 33 )
2X-RAY DIFFRACTION2chain 'A' and (resid 34 through 45 )
3X-RAY DIFFRACTION3chain 'A' and (resid 46 through 67 )
4X-RAY DIFFRACTION4chain 'A' and (resid 68 through 85 )
5X-RAY DIFFRACTION5chain 'A' and (resid 86 through 112 )
6X-RAY DIFFRACTION6chain 'A' and (resid 113 through 135 )
7X-RAY DIFFRACTION7chain 'A' and (resid 136 through 145 )
8X-RAY DIFFRACTION8chain 'A' and (resid 146 through 160 )
9X-RAY DIFFRACTION9chain 'A' and (resid 161 through 177 )
10X-RAY DIFFRACTION10chain 'B' and (resid 1471 through 1544 )
11X-RAY DIFFRACTION11chain 'B' and (resid 1545 through 1702 )
12X-RAY DIFFRACTION12chain 'B' and (resid 1703 through 1807 )
13X-RAY DIFFRACTION13chain 'B' and (resid 1808 through 1853 )
14X-RAY DIFFRACTION14chain 'C' and (resid 1469 through 1489 )
15X-RAY DIFFRACTION15chain 'C' and (resid 1490 through 1593 )
16X-RAY DIFFRACTION16chain 'C' and (resid 1594 through 1627 )
17X-RAY DIFFRACTION17chain 'C' and (resid 1628 through 1679 )
18X-RAY DIFFRACTION18chain 'C' and (resid 1680 through 1753 )
19X-RAY DIFFRACTION19chain 'C' and (resid 1754 through 1783 )
20X-RAY DIFFRACTION20chain 'C' and (resid 1784 through 1808 )
21X-RAY DIFFRACTION21chain 'C' and (resid 1809 through 1853 )
22X-RAY DIFFRACTION22chain 'D' and (resid 5 through 33 )
23X-RAY DIFFRACTION23chain 'D' and (resid 34 through 55 )
24X-RAY DIFFRACTION24chain 'D' and (resid 56 through 85 )
25X-RAY DIFFRACTION25chain 'D' and (resid 86 through 95 )
26X-RAY DIFFRACTION26chain 'D' and (resid 96 through 112 )
27X-RAY DIFFRACTION27chain 'D' and (resid 113 through 160 )
28X-RAY DIFFRACTION28chain 'D' and (resid 161 through 177 )
29X-RAY DIFFRACTION29chain 'E' and (resid 1471 through 1523 )
30X-RAY DIFFRACTION30chain 'E' and (resid 1524 through 1593 )
31X-RAY DIFFRACTION31chain 'E' and (resid 1594 through 1627 )
32X-RAY DIFFRACTION32chain 'E' and (resid 1628 through 1783 )
33X-RAY DIFFRACTION33chain 'E' and (resid 1784 through 1853 )
34X-RAY DIFFRACTION34chain 'I' and (resid 11 through 33 )
35X-RAY DIFFRACTION35chain 'I' and (resid 34 through 45 )
36X-RAY DIFFRACTION36chain 'I' and (resid 46 through 67 )
37X-RAY DIFFRACTION37chain 'I' and (resid 68 through 86 )
38X-RAY DIFFRACTION38chain 'I' and (resid 87 through 112 )
39X-RAY DIFFRACTION39chain 'I' and (resid 113 through 124 )
40X-RAY DIFFRACTION40chain 'I' and (resid 125 through 135 )
41X-RAY DIFFRACTION41chain 'I' and (resid 136 through 145 )
42X-RAY DIFFRACTION42chain 'I' and (resid 146 through 160 )
43X-RAY DIFFRACTION43chain 'I' and (resid 161 through 174 )
44X-RAY DIFFRACTION44chain 'F'
45X-RAY DIFFRACTION45chain 'G'
46X-RAY DIFFRACTION46chain 'H'

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