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- PDB-5aqj: Fragment-based screening of HSP70 sheds light on the functional r... -

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Basic information

Entry
Database: PDB / ID: 5aqj
TitleFragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues
Components
  • BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
  • HEAT SHOCK COGNATE 71 KDA PROTEIN
KeywordsCHAPERONE / HEAT SHOCK PROTEIN / HSP70 / HSP72 / HSC70 / ATPASE / BAG1 / FRAGMENT
Function / homology
Function and homology information


lumenal side of lysosomal membrane / regulation of protein import / negative regulation of supramolecular fiber organization / positive regulation of protein refolding / prostaglandin binding / positive regulation of lysosomal membrane permeability / lysosomal matrix / A1 adenosine receptor binding / protein carrier chaperone / response to nickel cation ...lumenal side of lysosomal membrane / regulation of protein import / negative regulation of supramolecular fiber organization / positive regulation of protein refolding / prostaglandin binding / positive regulation of lysosomal membrane permeability / lysosomal matrix / A1 adenosine receptor binding / protein carrier chaperone / response to nickel cation / clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane / Respiratory syncytial virus genome transcription / protein transmembrane import into intracellular organelle / Lipophagy / chaperone-mediated autophagy translocation complex disassembly / slow axonal transport / clathrin-uncoating ATPase activity / GABA synthesis, release, reuptake and degradation / protein targeting to lysosome involved in chaperone-mediated autophagy / adenyl-nucleotide exchange factor activity / late endosomal microautophagy / response to odorant / positive regulation by host of viral genome replication / synaptic vesicle uncoating / C3HC4-type RING finger domain binding / positive regulation of smooth muscle cell apoptotic process / negative regulation of NLRP3 inflammasome complex assembly / clathrin coat disassembly / ATP-dependent protein disaggregase activity / CHL1 interactions / regulation of protein complex stability / photoreceptor ribbon synapse / maintenance of postsynaptic specialization structure / membrane organization / Prp19 complex / glycinergic synapse / presynaptic cytosol / postsynaptic specialization membrane / protein folding chaperone complex / positive regulation of mRNA splicing, via spliceosome / postsynaptic cytosol / regulation of postsynapse organization / negative regulation of cardiac muscle cell apoptotic process / Lysosome Vesicle Biogenesis / intermediate filament / chaperone-mediated autophagy / cellular response to steroid hormone stimulus / Golgi Associated Vesicle Biogenesis / phosphatidylserine binding / non-chaperonin molecular chaperone ATPase / positive regulation of proteolysis / chaperone cofactor-dependent protein refolding / HSF1-dependent transactivation / response to unfolded protein / estrous cycle / Regulation of HSF1-mediated heat shock response / regulation of protein-containing complex assembly / autophagosome / Attenuation phase / Protein methylation / ATP metabolic process / protein folding chaperone / skeletal muscle tissue development / positive regulation of phagocytosis / forebrain development / heat shock protein binding / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / cellular response to cadmium ion / cellular response to starvation / photoreceptor inner segment / lysosomal lumen / mRNA Splicing - Major Pathway / cerebellum development / dendritic shaft / response to activity / kidney development / AUF1 (hnRNP D0) binds and destabilizes mRNA / response to progesterone / G protein-coupled receptor binding / ATP-dependent protein folding chaperone / peptide binding / spliceosomal complex / Late endosomal microautophagy / regulation of protein stability / PKR-mediated signaling / terminal bouton / ADP binding / mRNA splicing, via spliceosome / Chaperone Mediated Autophagy / cellular response to hydrogen peroxide / G1/S transition of mitotic cell cycle / positive regulation of T cell mediated cytotoxicity / protein import into nucleus / unfolded protein binding / melanosome / synaptic vesicle / late endosome / protein folding / response to estradiol / MHC class II protein complex binding
Similarity search - Function
BAG domain / BAG domain superfamily / Molecular chaperone regulator BAG / BAG domain / BAG domain / BAG domain profile. / BAG domains, present in regulator of Hsp70 proteins / Defensin A-like - #30 / Defensin A-like / Heat shock hsp70 proteins family signature 2. ...BAG domain / BAG domain superfamily / Molecular chaperone regulator BAG / BAG domain / BAG domain / BAG domain profile. / BAG domains, present in regulator of Hsp70 proteins / Defensin A-like - #30 / Defensin A-like / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 3. / Heat shock protein 70, conserved site / Heat shock protein 70kD, peptide-binding domain superfamily / Heat shock protein 70 family / Hsp70 protein / Heat shock protein 70kD, C-terminal domain superfamily / ATPase, substrate binding domain, subdomain 4 / Actin; Chain A, domain 4 / ATPase, nucleotide binding domain / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / ATPase, nucleotide binding domain / Ubiquitin family / Ubiquitin homologues / Nucleotidyltransferase; domain 5 / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Alpha-Beta Complex / Up-down Bundle / 2-Layer Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
9H-purine-6,8-diamine / Heat shock cognate 71 kDa protein / BAG family molecular chaperone regulator 1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.96 Å
AuthorsJones, A.M. / Westwood, I.M. / Osborne, J.D. / Matthews, T.P. / Cheeseman, M.D. / Rowlands, M.G. / Jeganathan, F. / Burke, R. / Lee, D. / Kadi, N. ...Jones, A.M. / Westwood, I.M. / Osborne, J.D. / Matthews, T.P. / Cheeseman, M.D. / Rowlands, M.G. / Jeganathan, F. / Burke, R. / Lee, D. / Kadi, N. / Liu, M. / Richards, M. / McAndrew, C. / Yahya, N. / Dobson, S.E. / Jones, K. / Workman, P. / Collins, I. / van Montfort, R.L.M.
CitationJournal: Sci Rep / Year: 2016
Title: A fragment-based approach applied to a highly flexible target: Insights and challenges towards the inhibition of HSP70 isoforms.
Authors: Jones, A.M. / Westwood, I.M. / Osborne, J.D. / Matthews, T.P. / Cheeseman, M.D. / Rowlands, M.G. / Jeganathan, F. / Burke, R. / Lee, D. / Kadi, N. / Liu, M. / Richards, M. / McAndrew, C. / ...Authors: Jones, A.M. / Westwood, I.M. / Osborne, J.D. / Matthews, T.P. / Cheeseman, M.D. / Rowlands, M.G. / Jeganathan, F. / Burke, R. / Lee, D. / Kadi, N. / Liu, M. / Richards, M. / McAndrew, C. / Yahya, N. / Dobson, S.E. / Jones, K. / Workman, P. / Collins, I. / van Montfort, R.L.
History
DepositionSep 22, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 5, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 13, 2017Group: Data collection / Database references / Category: citation / citation_author / diffrn_detector
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.name / _diffrn_detector.type
Revision 1.2Jan 10, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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: HEAT SHOCK COGNATE 71 KDA PROTEIN
B: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
C: HEAT SHOCK COGNATE 71 KDA PROTEIN
D: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
E: HEAT SHOCK COGNATE 71 KDA PROTEIN
F: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)170,26533
Polymers167,7566
Non-polymers2,50927
Water15,781876
1
E: HEAT SHOCK COGNATE 71 KDA PROTEIN
F: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,76511
Polymers55,9192
Non-polymers8469
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3740 Å2
ΔGint0.3 kcal/mol
Surface area22160 Å2
MethodPISA
2
A: HEAT SHOCK COGNATE 71 KDA PROTEIN
B: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,5819
Polymers55,9192
Non-polymers6627
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3480 Å2
ΔGint1.2 kcal/mol
Surface area21860 Å2
MethodPISA
3
C: HEAT SHOCK COGNATE 71 KDA PROTEIN
D: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,91913
Polymers55,9192
Non-polymers1,00011
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4470 Å2
ΔGint1.7 kcal/mol
Surface area22160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)233.982, 40.937, 206.081
Angle α, β, γ (deg.)90.00, 123.32, 90.00
Int Tables number5
Space group name H-MC121

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Components

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Protein , 2 types, 6 molecules ACEBDF

#1: Protein HEAT SHOCK COGNATE 71 KDA PROTEIN / HEAT SHOCK 70 KDA PROTEIN 8 / LIPOPOLYSACCHARIDE-ASSOCIATED PROTEIN 1 / LAP-1 / LPS-ASSOCIATED PROTEIN 1


Mass: 42406.980 Da / Num. of mol.: 3 / Fragment: NUCLEOTIDE BINDING DOMAIN, RESIDUES 1-381
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): AI / References: UniProt: P11142, EC: 3.6.3.51
#2: Protein BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1 / BAG-1 / BCL-2-ASSOCIATED ATHANOGENE 1


Mass: 13511.571 Da / Num. of mol.: 3 / Fragment: RESIDUES 222-334
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): AI / References: UniProt: Q99933

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Non-polymers , 6 types, 903 molecules

#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-Q88 / 9H-purine-6,8-diamine / 8-aminoadenine


Mass: 150.141 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C5H6N6
#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#7: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 876 / 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: 2.46 Å3/Da / Density % sol: 49.96 % / Description: NONE
Crystal growpH: 8.5
Details: 16-26% (W/V) PEG3350, 0.1 M K-NA TARTRATE, 0.1 M TRIS.HCL PH 8.5 AND 25% (V/V) GLYCEROL

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.9696
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 7, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9696 Å / Relative weight: 1
ReflectionResolution: 1.96→38.99 Å / Num. obs: 118741 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 37.28 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 10
Reflection shellResolution: 1.96→1.99 Å / Redundancy: 3.4 % / Rmerge(I) obs: 1.12 / Mean I/σ(I) obs: 1 / % possible all: 99.9

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Processing

Software
NameVersionClassification
BUSTER2.10.2refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1HX1

1hx1


Resolution: 1.96→38.99 Å / Cor.coef. Fo:Fc: 0.9504 / Cor.coef. Fo:Fc free: 0.9382 / SU R Cruickshank DPI: 0.157 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.162 / SU Rfree Blow DPI: 0.141 / SU Rfree Cruickshank DPI: 0.14
Details: IDEAL-DIST CONTACT TERM CONTACT SETUP. ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
RfactorNum. reflection% reflectionSelection details
Rfree0.2212 5801 4.89 %RANDOM
Rwork0.1903 ---
obs0.1918 118738 99.94 %-
Displacement parametersBiso mean: 55.11 Å2
Baniso -1Baniso -2Baniso -3
1--2.0366 Å20 Å2-6.1946 Å2
2--4.1051 Å20 Å2
3----2.0684 Å2
Refine analyzeLuzzati coordinate error obs: 0.27 Å
Refinement stepCycle: LAST / Resolution: 1.96→38.99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11295 0 160 876 12331
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0111634HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.0415712HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d4117SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes329HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1722HARMONIC5
X-RAY DIFFRACTIONt_it11634HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion2.92
X-RAY DIFFRACTIONt_other_torsion15.99
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion1580SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies3HARMONIC1
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact14021SEMIHARMONIC4
LS refinement shellResolution: 1.96→2.01 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2556 411 4.74 %
Rwork0.2243 8257 -
all0.2258 8668 -
obs--99.86 %
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)
15.59010.7079-2.01791.2649-1.2793.8307-0.17490.1964-0.3261-0.524-0.229-0.55570.4293-0.0190.4039-0.11340.06460.0816-0.27930.23010.3923217.1141-12.996911.1139
21.43911.6386-1.58135.3725-0.87171.48070.2237-0.1410.20340.1394-0.1957-0.2708-0.3868-0.1399-0.028-0.0635-0.0208-0.1645-0.16310.1760.2282208.51022.520522.897
31.3625-0.6637-0.7994.0911-0.66632.74120.0684-0.32690.05770.3801-0.3129-0.7054-0.30440.31710.2445-0.2023-0.0744-0.1871-0.25160.25760.3766217.2072-1.161722.179
41.3166-0.30620.3721.5224-0.10171.56070.25660.16670.0925-0.2768-0.3329-0.9325-0.06520.14210.0763-0.05640.09210.2477-0.19440.2850.4834221.49072.02251.9076
54.64420.4238-0.52841.9398-1.3233-0.1717-0.0033-0.0609-0.0918-0.4512-0.1192-0.12410.0673-0.26930.12240.07460.0459-0.0148-0.03260.0059-0.1633186.44131.39216.2309
62.18511.1008-0.99981.9709-2.99131.9711-0.0628-0.140.1139-0.1767-0.1249-0.2540.06190.06790.18780.00990.0227-0.0559-0.00380.0014-0.0754188.9693-3.963211.2818
72.99490.1228-0.82974.0713-1.39322.02670.08190.33220.1276-0.65120.01190.06830.1805-0.401-0.09380.1430.0256-0.02260.0188-0.0243-0.1862185.139-6.27153.3786
80.6561.6967-1.50612.24810.22593.0641-0.11690.06450.2324-0.1372-0.0866-0.31540.0146-0.14340.20350.13170.20560.2688-0.14160.25730.1433206.697610.9416-6.1691
93.67871.3022-1.331401.76361.7099-0.02360.47580.0557-0.4325-0.1578-0.3121-0.18240.24030.18140.05450.19970.3385-0.10780.31110.0258213.06232.058-9.0206
104.027-0.83910.88092.4049-0.94133.76880.10920.3063-0.2817-0.452-0.2081-0.8666-0.16930.01530.09880.02760.13760.2918-0.27330.1590.0767213.778-4.6896-5.1814
111.3271.66180.84713.49312.68331.99980.1557-0.30160.03680.0451-0.0376-0.08210.08970.0513-0.1181-0.05350.0481-0.02210.06070.0105-0.1899185.8175-22.619723.198
120.22671.54050.00643.87831.09860.80960.0812-0.12580.11750.01670.0003-0.2292-0.16330.1244-0.0815-0.02930.0669-0.0890.19-0.05960.0573189.3802-11.889926.8807
132.4301-0.898-0.32215.50462.32072.2295-0.0029-0.67650.37150.07330.0237-0.0228-0.0193-0.0887-0.0208-0.10560.0277-0.01570.1562-0.0486-0.0893181.9866-13.029924.6218
140.96710.1265-0.46273.23370.14131.1304-0.1204-0.0045-0.1291-0.16030.08510.06680.0494-0.01690.0353-0.0072-0.11390.052-0.00270.0026-0.0656215.0068-21.337978.0736
150.7790.2662-0.44518.0579-2.57622.671-0.0111-0.17270.12150.21860.08520.2754-0.2148-0.0233-0.07410.0657-0.07730.08280.0119-0.0109-0.0438211.5542-5.66686.3313
160.6857-0.418-0.12813.593-0.06931.0906-0.1388-0.0601-0.0428-0.04080.1573-0.2132-0.09550.1947-0.0185-0.0462-0.13450.06150.0224-0.0114-0.0504222.0175-20.139480.0974
171.28070.4555-0.01171.43710.49371.5156-0.15830.13690.0076-0.6090.2349-0.3848-0.22170.2736-0.07660.2017-0.26190.1680.0074-0.0249-0.0294224.7057-13.035163.0557
184.45950.1298-1.671200.37091.62340.0172-0.40310.0985-0.28630.09590.21920.0323-0.1038-0.11310.1186-0.1056-0.2281-0.19550.06590.059188.8298-13.350464.6749
190.50250.9412-0.62371.7926-1.15242.8379-0.22910.02520.0715-0.22620.2010.26080.05470.14660.0281-0.0515-0.0917-0.1449-0.14960.0621-0.0475190.9894-18.530970.3045
203.76541.4231-1.0712.1216-0.39431.4493-0.24760.3170.2968-0.75590.25090.2851-0.23770.0336-0.00330.3179-0.2025-0.1152-0.1150.0703-0.142201.6101-14.137257.2976
211.15720.29530.34021.88090.01760.8203-0.26550.4243-0.0308-0.96960.315-0.2136-0.09180.2215-0.04950.3457-0.29070.1005-0.01970.0118-0.2003217.2043-19.380955.7089
220.17530.42691.18751.38393.10747.21120.1838-0.1243-0.2566-0.00960.23460.07230.2886-0.2163-0.41840.0447-0.028-0.0854-0.04120.12480.1346188.2909-37.315782.5741
231.19-0.49650.74491.1988-1.20525.0135-0.0837-0.3193-0.30690.18650.15190.1943-0.23490.2583-0.0682-0.0819-0.0384-0.00840.03710.12920.0333192.8627-24.720193.6584
241.90550.56261.32443.81194.16568.1707-0.0599-0.1654-0.028-0.2994-0.06290.4263-0.1398-0.3150.1228-0.0814-0.0388-0.086-0.13240.10880.1159183.4638-29.814379.2984
251.2223-0.325-1.73893.66191.79853.8628-0.0339-0.2085-0.12160.12570.0027-0.01540.20410.20560.03120.1251-0.38940.3223-0.0341-0.2746-0.0986135.276-10.849747.6908
260.9631-1.4746-0.58882.78180.75131.63780.11350.26690.1452-0.45380.0375-0.1836-0.27020.0159-0.1510.2581-0.40640.39090.0295-0.3057-0.0626142.52666.43233.5774
270.501-0.206-0.57511.1732-0.56960.96130.04030.13560.0588-0.32830.02050.0467-0.078-0.2076-0.06080.2132-0.40540.33850.0819-0.3162-0.0164130.3464-0.611443.466
285.66081.5433-0.43652.7504-0.65620.92010.1405-0.05330.2576-0.03190.02280.1953-0.09210.0643-0.16340.0752-0.36460.31920.0491-0.3272-0.0826135.10785.824463.2384
292.3101-0.9473-1.12041.55611.56594.1426-0.09550.0834-0.00780.17460.163-0.18210.27710.1366-0.06750.1425-0.38970.25020.1667-0.3737-0.037167.43743.447450.5534
302.97930.9691-2.79213.40951.17759.6048-0.18170.1468-0.0926-0.21010.12-0.05490.2326-0.09920.0617-0.013-0.40120.31540.1059-0.425-0.0816164.1269-2.183145.9718
311.8302-0.046-0.62551.51211.8032.2576-0.19120.09-0.25420.24910.2541-0.46690.29230.134-0.06290.1327-0.37260.32290.2039-0.42360.0029168.7461-4.143752.9534
322.10240.7697-0.09350.72150.03181.12-0.0089-0.19010.0160.21760.02840.0541-0.0580.1865-0.01950.1384-0.35380.30090.0774-0.3065-0.0816142.45883.439964.7374
330.5788-1.40082.31941.112-2.54795.95090.3530.14960.1503-0.3319-0.25710.16270.09830-0.09590.161-0.34270.25430.1474-0.3462-0.0856164.8231-19.074428.8674
340.3424-0.39351.48580.9444-0.193.19360.1584-0.12330.2907-0.307-0.1025-0.0451-0.05570.0413-0.05590.0592-0.40970.36410.1252-0.4186-0.0864161.569-9.965130.3476
351.6188-0.40932.56321.5769-1.13843.2378-0.06230.29250.1235-0.34940.067-0.3043-0.1810.1391-0.00470.1147-0.43060.43650.196-0.44930.0126169.8765-11.429431.5403
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{ A|1 - 41 }
2X-RAY DIFFRACTION2{ A|42 - 89 }
3X-RAY DIFFRACTION3{ A|90 - 151 }
4X-RAY DIFFRACTION4{ A|152 - 229 }
5X-RAY DIFFRACTION5{ A|230 - 249 }
6X-RAY DIFFRACTION6{ A|250 - 275 }
7X-RAY DIFFRACTION7{ A|276 - 306 }
8X-RAY DIFFRACTION8{ A|307 - 324 }
9X-RAY DIFFRACTION9{ A|325 - 343 }
10X-RAY DIFFRACTION10{ A|344 - 381 }
11X-RAY DIFFRACTION11{ B|147 - 187 }
12X-RAY DIFFRACTION12{ B|188 - 230 }
13X-RAY DIFFRACTION13{ B|231 - 260 }
14X-RAY DIFFRACTION14{ C|1 - 80 }
15X-RAY DIFFRACTION15{ C|81 - 109 }
16X-RAY DIFFRACTION16{ C|110 - 151 }
17X-RAY DIFFRACTION17{ C|152 - 229 }
18X-RAY DIFFRACTION18{ C|230 - 249 }
19X-RAY DIFFRACTION19{ C|250 - 275 }
20X-RAY DIFFRACTION20{ C|276 - 343 }
21X-RAY DIFFRACTION21{ C|344 - 381 }
22X-RAY DIFFRACTION22{ D|149 - 187 }
23X-RAY DIFFRACTION23{ D|188 - 223 }
24X-RAY DIFFRACTION24{ D|224 - 260 }
25X-RAY DIFFRACTION25{ E|0 - 41 }
26X-RAY DIFFRACTION26{ E|42 - 109 }
27X-RAY DIFFRACTION27{ E|110 - 182 }
28X-RAY DIFFRACTION28{ E|183 - 229 }
29X-RAY DIFFRACTION29{ E|230 - 249 }
30X-RAY DIFFRACTION30{ E|250 - 276 }
31X-RAY DIFFRACTION31{ E|277 - 306 }
32X-RAY DIFFRACTION32{ E|307 - 381 }
33X-RAY DIFFRACTION33{ F|150 - 192 }
34X-RAY DIFFRACTION34{ F|193 - 230 }
35X-RAY DIFFRACTION35{ F|231 - 260 }

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