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- PDB-4i5l: Structural mechanism of trimeric PP2A holoenzyme involving PR70: ... -

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Basic information

Entry
Database: PDB / ID: 4i5l
TitleStructural mechanism of trimeric PP2A holoenzyme involving PR70: insight for Cdc6 dephosphorylation
Components
  • (Serine/threonine-protein phosphatase 2A ...) x 3
  • Microcystin-LR (MCLR) bound form
KeywordsHYDROLASE/TOXIN / EF Hand / Phosphatase / CDC6 (Substrate) / HYDROLASE-TOXIN complex
Function / homology
Function and homology information


cellular response to vasopressin / positive regulation of chromosome segregation / CDC6 association with the ORC:origin complex / meiotic spindle elongation / Integration of energy metabolism / PP2A-mediated dephosphorylation of key metabolic factors / regulation of microtubule binding / MASTL Facilitates Mitotic Progression / mitotic sister chromatid separation / regulation of meiotic cell cycle process involved in oocyte maturation ...cellular response to vasopressin / positive regulation of chromosome segregation / CDC6 association with the ORC:origin complex / meiotic spindle elongation / Integration of energy metabolism / PP2A-mediated dephosphorylation of key metabolic factors / regulation of microtubule binding / MASTL Facilitates Mitotic Progression / mitotic sister chromatid separation / regulation of meiotic cell cycle process involved in oocyte maturation / protein phosphatase type 2A complex / meiotic sister chromatid cohesion, centromeric / peptidyl-serine dephosphorylation / peptidyl-threonine dephosphorylation / positive regulation of microtubule binding / Regulation of glycolysis by fructose 2,6-bisphosphate metabolism / Inhibition of replication initiation of damaged DNA by RB1/E2F1 / female meiotic nuclear division / protein antigen binding / protein phosphatase regulator activity / GABA receptor binding / traversing start control point of mitotic cell cycle / DNA replication checkpoint signaling / APC truncation mutants have impaired AXIN binding / AXIN missense mutants destabilize the destruction complex / Truncations of AMER1 destabilize the destruction complex / Initiation of Nuclear Envelope (NE) Reformation / ERKs are inactivated / Transcription of E2F targets under negative control by DREAM complex / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / Beta-catenin phosphorylation cascade / Signaling by GSK3beta mutants / CTNNB1 S33 mutants aren't phosphorylated / CTNNB1 S37 mutants aren't phosphorylated / CTNNB1 S45 mutants aren't phosphorylated / CTNNB1 T41 mutants aren't phosphorylated / negative regulation of epithelial to mesenchymal transition / mitotic DNA replication checkpoint signaling / cellular response to angiotensin / regulation of mitotic metaphase/anaphase transition / regulation of growth / Disassembly of the destruction complex and recruitment of AXIN to the membrane / negative regulation of glycolytic process through fructose-6-phosphate / positive regulation of NLRP3 inflammasome complex assembly / myosin phosphatase activity / intercellular bridge / regulation of cyclin-dependent protein serine/threonine kinase activity / CTLA4 inhibitory signaling / protein serine/threonine phosphatase activity / Platelet sensitization by LDL / G1/S-Specific Transcription / negative regulation of DNA replication / protein-serine/threonine phosphatase / regulation of cell differentiation / ERK/MAPK targets / positive regulation of cytokinesis / T cell homeostasis / regulation of G1/S transition of mitotic cell cycle / DNA replication origin binding / mesoderm development / phosphoprotein phosphatase activity / chromosome, centromeric region / DARPP-32 events / lateral plasma membrane / Activation of the pre-replicative complex / DNA replication initiation / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / spindle midzone / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Activation of ATR in response to replication stress / Cyclin A/B1/B2 associated events during G2/M transition / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Resolution of Sister Chromatid Cohesion / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / protein dephosphorylation / meiotic cell cycle / protein tyrosine phosphatase activity / chromosome segregation / Assembly of the pre-replicative complex / RHO GTPases Activate Formins / response to lead ion / Spry regulation of FGF signaling / RAF activation / regulation of protein phosphorylation / Degradation of beta-catenin by the destruction complex / PKR-mediated signaling / tau protein binding / positive regulation of protein serine/threonine kinase activity / mitotic spindle / CDK-mediated phosphorylation and removal of Cdc6 / kinase binding / spindle pole / Orc1 removal from chromatin
Similarity search - Function
Recoverin; domain 1 - #230 / Recoverin; domain 1 - #220 / PP2A regulatory subunit B'', EF-hand domain / : / EF-hand domain / P2R3B, EF-hand / Cell division protein Cdc6/18 / Cdc6, C-terminal / CDC6, C terminal / CDC6, C terminal winged helix domain ...Recoverin; domain 1 - #230 / Recoverin; domain 1 - #220 / PP2A regulatory subunit B'', EF-hand domain / : / EF-hand domain / P2R3B, EF-hand / Cell division protein Cdc6/18 / Cdc6, C-terminal / CDC6, C terminal / CDC6, C terminal winged helix domain / : / AAA domain / AAA lid domain / AAA lid domain / HEAT repeat / HEAT repeat / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / HEAT repeat profile. / HEAT, type 2 / HEAT repeats / Metallo-dependent phosphatases / Purple Acid Phosphatase; chain A, domain 2 / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / Metallo-dependent phosphatase-like / EF-hand / Recoverin; domain 1 / EF-hand domain pair / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / 4-Layer Sandwich / Armadillo-like helical / Alpha Horseshoe / EF-hand domain pair / Armadillo-type fold / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Microcystin-LR (MCLR) bound form / MALONATE ION / : / DI(HYDROXYETHYL)ETHER / : / Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform / Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform / Cell division control protein 6 homolog / Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
Similarity search - Component
Biological speciesHomo sapiens (human)
Microcystis aeruginosa (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.43 Å
AuthorsWlodarchak, N. / Satyshur, K.A. / Guo, F. / Xing, Y.
CitationJournal: Cell Res. / Year: 2013
Title: Structure of the Ca(2+)-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation.
Authors: Wlodarchak, N. / Guo, F. / Satyshur, K.A. / Jiang, L. / Jeffrey, P.D. / Sun, T. / Stanevich, V. / Mumby, M.C. / Xing, Y.
History
DepositionNov 28, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 8, 2013Provider: repository / Type: Initial release
Revision 1.1May 15, 2013Group: Structure summary
Revision 1.2Jul 24, 2013Group: Database references
Revision 1.3Aug 9, 2017Group: Advisory / Refinement description / Source and taxonomy
Category: entity_src_gen / pdbx_validate_polymer_linkage / software
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / pdbx_validate_main_chain_plane / pdbx_validate_peptide_omega / pdbx_validate_rmsd_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _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.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_value_order / _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 phosphatase 2A 65 kDa regulatory subunit A alpha isoform
B: Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct
C: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha
D: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
E: Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct
F: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha
G: Microcystin-LR (MCLR) bound form
H: Microcystin-LR (MCLR) bound form
hetero molecules


Theoretical massNumber of molelcules
Total (without water)299,71530
Polymers297,8618
Non-polymers1,85422
Water9,566531
1
A: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
B: Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct
C: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha
G: Microcystin-LR (MCLR) bound form
hetero molecules


Theoretical massNumber of molelcules
Total (without water)150,07217
Polymers148,9314
Non-polymers1,14113
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
E: Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct
F: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha
H: Microcystin-LR (MCLR) bound form
hetero molecules


  • defined by author
  • 150 kDa, 4 polymers
Theoretical massNumber of molelcules
Total (without water)149,64313
Polymers148,9314
Non-polymers7129
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)94.234, 101.071, 343.396
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Serine/threonine-protein phosphatase 2A ... , 3 types, 6 molecules ADBECF

#1: Protein Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform / Medium tumor antigen-associated 61 kDa protein / PP2A subunit A isoform PR65-alpha / PP2A subunit A ...Medium tumor antigen-associated 61 kDa protein / PP2A subunit A isoform PR65-alpha / PP2A subunit A isoform R1-alpha


Mass: 64906.918 Da / Num. of mol.: 2 / Fragment: PP2A A alpha subunit (9-589)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PPP2R1A / Plasmid: pCool / Cell line (production host): DH5a / Production host: Escherichia coli (E. coli) / References: UniProt: P30153
#2: Protein Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct / PP2A subunit B isoform PR48 / Protein phosphatase 2A 48 kDa regulatory subunit


Mass: 47227.238 Da / Num. of mol.: 2
Fragment: UNP Q9Y5P8 residues 122-490 and UNP Q99741 residues 70-90
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PPP2R3B, PPP2R3L / Plasmid: PQlinkG / Cell line (production host): DH5a / Production host: Escherichia coli (E. coli) / References: UniProt: Q9Y5P8, UniProt: Q99741
#3: Protein Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha / PP2A-alpha / Replication protein C / RP-C


Mass: 35780.281 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PPP2CA / Plasmid: FBQH / Cell line (production host): High5 / Production host: Trichoplusia ni (cabbage looper)
References: UniProt: P67775, protein-serine/threonine phosphatase

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Protein/peptide , 1 types, 2 molecules GH

#4: Protein/peptide Microcystin-LR (MCLR) bound form


Type: Oligopeptide / Class: Toxin / Mass: 1016.211 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Microcystis aeruginosa (bacteria) / References: NOR: NOR00109, Microcystin-LR (MCLR) bound form

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Non-polymers , 5 types, 553 molecules

#5: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: C4H10O3
#6: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#7: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mn
#8: Chemical ChemComp-MLI / MALONATE ION


Mass: 102.046 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H2O4
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 531 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsTHE LINKER IS DERIVED FROM JMJD6

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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: 2.74 Å3/Da / Density % sol: 55.06 %
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop / pH: 5
Details: 0.1M Na Malonate, 12% PEG 3350 + 6.2mg/mL protein in buffer Tris, 150mM NaCl , pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 0.97919 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Dec 12, 2011
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97919 Å / Relative weight: 1
ReflectionResolution: 2.43→49.85 Å / Num. all: 125017 / Num. obs: 123017 / % possible obs: 98.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7 % / Rsym value: 0.093 / Net I/σ(I): 19.15
Reflection shellResolution: 2.42→2.46 Å / Redundancy: 6.7 % / Mean I/σ(I) obs: 2.74 / Rsym value: 0.615 / % possible all: 89.7

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHASERMRphasing
REFMAC5.7.0029refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.43→49.85 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.928 / SU B: 14.686 / SU ML: 0.166 / Cross valid method: THROUGHOUT / ESU R: 0.339 / ESU R Free: 0.236 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.22776 6193 5 %RANDOM
Rwork0.17906 ---
obs0.18148 116785 98.63 %-
all-116785 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 42.92 Å2
Baniso -1Baniso -2Baniso -3
1-0.44 Å2-0 Å2-0 Å2
2---0.41 Å2-0 Å2
3----0.03 Å2
Refinement stepCycle: LAST / Resolution: 2.43→49.85 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19789 0 106 531 20426
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.01920319
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.3371.9727451
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.37552471
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.66424.129947
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.72153525
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.39915134
X-RAY DIFFRACTIONr_chiral_restr0.1020.23092
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02115252
X-RAY DIFFRACTIONr_gen_planes_other0.0060.024627
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.428→2.491 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.3 431 -
Rwork0.238 8158 -
obs--94.66 %
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)
11.3945-0.95720.28855.3370.74932.29690.0553-0.097-0.0068-0.24450.05350.11370.0232-0.1277-0.10880.09850.0780.02990.09510.03420.180469.64274.079108.545
20.786-0.19880.31981.81520.45990.7125-0.0266-0.04590.08030.13530.0943-0.17230.09650.0311-0.06770.1250.09680.02080.12070.00730.172484.07651.55115.285
30.3102-0.36130.3050.86190.61734.212-0.0683-0.01020.0388-0.03670.0232-0.0550.14680.46620.04510.15890.1090.05250.15630.04250.188497.87736.2992.786
42.50040.385-0.65050.9528-0.92972.09160.06090.17570.06730.0096-0.0702-0.0739-0.00940.1220.00920.09890.07570.07910.10680.07720.180697.63641.26670.509
51.9421-0.6617-0.33531.241-0.25430.38770.0230.0448-0.0096-0.0289-0.0633-0.0273-0.06370.10560.04030.1119-0.03240.01590.14590.03320.103477.45566.15556.869
611.72613.2691-8.33511.6062-2.32535.9627-0.1726-0.37120.72890.26660.50780.48590.170.2295-0.33510.35430.21550.13060.49990.09630.607457.46279.585120.676
71.9396-1.2275-1.56821.99210.92842.63650.0089-0.10390.09480.13850.060.0935-0.29670.0486-0.06890.24310.07340.01430.1003-0.07670.097642.63562.645133.019
81.23720.1017-0.8511.47920.40140.9858-0.0485-0.0443-0.0365-0.0798-0.07540.0627-0.097-0.11520.1240.13850.0432-0.01150.1245-0.03460.113546.67243.873116.673
92.1130.0455-1.50221.0067-0.42162.7315-0.1439-0.2807-0.1445-0.1144-0.05730.03410.08330.14610.20120.15030.0220.03870.1210.01620.129262.19239.457107.617
102.58520.44270.09334.05830.09963.3408-0.24580.2538-0.3282-0.47990.2234-0.21490.5118-0.02770.02250.2473-0.05440.11910.1092-0.04340.093865.16734.00888.647
114.13320.37480.08831.35680.06584.2149-0.07520.33710.1829-0.19380.02590.2786-0.1857-0.08840.04930.18120.01220.0060.06550.02110.091661.93546.26193.194
121.152-0.7931-0.84973.5762-0.13713.82860.0461-0.31230.38460.36470.05910.1925-0.47730.0429-0.10520.2103-0.00460.05710.1345-0.12910.241952.16569.22574.865
130.9363-0.1824-0.0491.5255-0.10910.7094-0.07640.032-0.1115-0.01540.06790.32960.02450.00190.00860.0924-0.04140.01140.0799-0.01390.194947.61250.14864.639
140.9923-0.4865-0.70384.0499-2.0373.8314-0.20630.0401-0.201-0.362-0.1499-0.4230.5320.31560.35610.1658-0.02370.06010.1257-0.01660.173262.21246.41163.708
154.8654-1.69-0.88991.6591-0.22680.43820.0378-0.34010.06380.08510.11170.1822-0.07150.0708-0.14950.21690.1807-0.00760.2453-0.14160.258350.32952.9-21.684
161.71150.01840.43351.8530.27180.63080.02880.0753-0.268-0.1471-0.14380.0818-0.0362-0.02370.1150.17530.1286-0.00350.137-0.02340.146171.28136.797-29.249
170.8188-0.53711.17781.09870.27835.23440.12-0.0114-0.16250.0143-0.1924-0.02390.70910.1840.07240.19010.09410.02190.17320.14270.249386.9422.507-7.352
182.7236-0.3504-1.87961.43570.87353.9287-0.2782-0.3501-0.14920.35450.00710.00660.55020.11480.27110.28380.0720.07470.19650.15660.166583.38323.27315.14
190.8842-0.0654-0.09674.0096-1.03230.35330.1389-0.1141-0.00070.6017-0.05190.4776-0.04880.0059-0.0870.3715-0.10730.14270.10340.01120.109458.57842.91628.837
201.05342.0114-0.73584.7066-3.24784.6139-0.08070.28160.395-0.61640.11860.66420.83650.4555-0.03780.47560.43920.1020.65260.05480.478445.54364.284-33.579
212.2692-1.56671.73091.1892-1.13512.9291-0.02880.02690.11040.06240.10180.00250.1442-0.0713-0.0730.13680.0852-0.06470.18680.0420.169861.18577.028-48.016
222.6508-0.43890.74270.8535-1.0391.3581-0.1364-0.11060.21430.0914-0.0621-0.0947-0.18610.09220.19850.21060.0622-0.08330.1285-0.01920.096180.47373.263-32.012
230.95770.72040.12540.9506-0.48390.97970.0243-0.14940.0255-0.0455-0.2608-0.0999-0.08250.17060.23650.22390.0768-0.04080.20930.0570.076384.77757.931-22.499
240.89790.54881.70760.7870.54557.00380.3366-0.2798-0.08980.3469-0.433-0.22770.3880.70140.09650.2978-0.1642-0.05820.53810.16380.085190.16955.526-3.415
251.87091.0167-0.3574.53740.31915.49260.2677-0.3940.06730.4656-0.3781-0.0020.0599-0.17640.11040.1662-0.04390.00240.2083-0.01150.006977.90558.625-7.959
264.2434-0.86121.33570.90070.72415.4280.0520.6258-0.3346-0.2205-0.32910.6761-0.0578-0.41750.27710.2555-0.1297-0.19280.3899-0.14870.595554.1167.6169.837
271.4178-0.9674-0.38712.07110.32061.1565-0.07290.00650.23460.26530.0379-0.14830.0840.02470.03510.2072-0.1113-0.05270.11790.01960.071472.68873.52420.058
284.0268-1.0892-4.34372.0391-0.27938.6452-0.2564-0.1641-0.08370.3495-0.0567-0.22920.4030.36440.31310.2283-0.0854-0.050.16570.02130.041877.68759.61522.132
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A8 - 82
2X-RAY DIFFRACTION2A83 - 217
3X-RAY DIFFRACTION3A218 - 335
4X-RAY DIFFRACTION4A336 - 400
5X-RAY DIFFRACTION5A401 - 589
6X-RAY DIFFRACTION6B120 - 140
7X-RAY DIFFRACTION7B141 - 230
8X-RAY DIFFRACTION8B231 - 345
9X-RAY DIFFRACTION9B346 - 409
10X-RAY DIFFRACTION10B410 - 444
11X-RAY DIFFRACTION11B445 - 478
12X-RAY DIFFRACTION12C1 - 41
13X-RAY DIFFRACTION13C42 - 264
14X-RAY DIFFRACTION14C265 - 298
15X-RAY DIFFRACTION15D8 - 82
16X-RAY DIFFRACTION16D83 - 217
17X-RAY DIFFRACTION17D218 - 335
18X-RAY DIFFRACTION18D336 - 400
19X-RAY DIFFRACTION19D401 - 589
20X-RAY DIFFRACTION20E120 - 140
21X-RAY DIFFRACTION21E141 - 230
22X-RAY DIFFRACTION22E231 - 345
23X-RAY DIFFRACTION23E346 - 409
24X-RAY DIFFRACTION24E410 - 444
25X-RAY DIFFRACTION25E445 - 479
26X-RAY DIFFRACTION26F1 - 41
27X-RAY DIFFRACTION27F42 - 264
28X-RAY DIFFRACTION28F265 - 298

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