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- PDB-6tz6: Crystal Structure of Candida Albicans Calcineurin A, Calcineurin ... -

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Basic information

Entry
Database: PDB / ID: 6tz6
TitleCrystal Structure of Candida Albicans Calcineurin A, Calcineurin B, FKBP12 and FK506 (Tacrolimus)
Components
  • Calcineurin subunit B
  • FK506-binding protein 1
  • Serine/threonine-protein phosphatase
KeywordsHydrolase/Isomerase/Calcium Binding / Calcineurin / FK506 / antifungal / Hydrolase-Isomerase-Calcium Binding complex
Function / homology
Function and homology information


regulation of homoserine biosynthetic process / protein serine/threonine phosphatase activity => GO:0004722 / protein serine/threonine phosphatase activity => GO:0004722 / calcium-dependent protein serine/threonine phosphatase regulator activity / calmodulin-dependent protein phosphatase activity / fungal biofilm matrix / calcineurin-mediated signaling / macrolide binding / protein-serine/threonine phosphatase / peptidylprolyl isomerase ...regulation of homoserine biosynthetic process / protein serine/threonine phosphatase activity => GO:0004722 / protein serine/threonine phosphatase activity => GO:0004722 / calcium-dependent protein serine/threonine phosphatase regulator activity / calmodulin-dependent protein phosphatase activity / fungal biofilm matrix / calcineurin-mediated signaling / macrolide binding / protein-serine/threonine phosphatase / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / protein folding / chromatin organization / calmodulin binding / calcium ion binding / extracellular region / cytoplasm
Similarity search - Function
Calcineurin B protein / PP2B, metallophosphatase domain / PP2B / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Metallo-dependent phosphatases / Purple Acid Phosphatase; chain A, domain 2 / Chitinase A; domain 3 - #40 / Calcineurin-like phosphoesterase domain, ApaH type ...Calcineurin B protein / PP2B, metallophosphatase domain / PP2B / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Metallo-dependent phosphatases / Purple Acid Phosphatase; chain A, domain 2 / Chitinase A; domain 3 - #40 / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Chitinase A; domain 3 / FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / FKBP-type peptidyl-prolyl cis-trans isomerase domain / FKBP-type peptidyl-prolyl cis-trans isomerase / Peptidyl-prolyl cis-trans isomerase domain superfamily / EF-hand / Recoverin; domain 1 / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / 4-Layer Sandwich / EF-hand domain pair / Roll / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
: / 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN / PHOSPHATE ION / Serine/threonine-protein phosphatase / Calcineurin regulatory subunit / FK506-binding protein 1
Similarity search - Component
Biological speciesCandida albicans (yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.55 Å
AuthorsFox III, D. / Lukacs, C.M.
Citation
Journal: Nat Commun / Year: 2019
Title: Harnessing calcineurin-FK506-FKBP12 crystal structures from invasive fungal pathogens to develop antifungal agents.
Authors: Juvvadi, P.R. / Fox 3rd, D. / Bobay, B.G. / Hoy, M.J. / Gobeil, S.M.C. / Venters, R.A. / Chang, Z. / Lin, J.J. / Averette, A.F. / Cole, D.C. / Barrington, B.C. / Wheaton, J.D. / Ciofani, M. ...Authors: Juvvadi, P.R. / Fox 3rd, D. / Bobay, B.G. / Hoy, M.J. / Gobeil, S.M.C. / Venters, R.A. / Chang, Z. / Lin, J.J. / Averette, A.F. / Cole, D.C. / Barrington, B.C. / Wheaton, J.D. / Ciofani, M. / Trzoss, M. / Li, X. / Lee, S.C. / Chen, Y.L. / Mutz, M. / Spicer, L.D. / Schumacher, M.A. / Heitman, J. / Steinbach, W.J.
#1: Journal: Nat Commun / Year: 2019
Title: Harnessing calcineurin-FK506-FKBP12 crystal structures from invasive fungal pathogens to develop antifungal agents
Authors: Juvvadi, P.R. / Fox III, D. / Bobay, B.G. / Hoy, M.J. / Gobeil, S.M. / Venters, R.A. / Chang, Z. / Lin, J.J. / Averette, A.F. / Cole, D.C. / Barrington, B.C. / Wheaton, J.D. / Ciofani, M. / ...Authors: Juvvadi, P.R. / Fox III, D. / Bobay, B.G. / Hoy, M.J. / Gobeil, S.M. / Venters, R.A. / Chang, Z. / Lin, J.J. / Averette, A.F. / Cole, D.C. / Barrington, B.C. / Wheaton, J.D. / Ciofani, M. / Trzoss, M. / Li, X. / Lee, S.C. / Chen, Y. / Mutz, M. / Spicer, L.D. / Schumacher, M.A. / Heitman, J. / Steinbach, W.J.
History
DepositionAug 10, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 18, 2019Provider: repository / Type: Initial release
Revision 1.1Oct 2, 2019Group: Data collection / Database references / Category: citation / citation_author
Revision 1.2Oct 11, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
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_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Serine/threonine-protein phosphatase
B: Calcineurin subunit B
C: FK506-binding protein 1
D: Serine/threonine-protein phosphatase
E: Calcineurin subunit B
F: FK506-binding protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)163,07924
Polymers160,5396
Non-polymers2,54018
Water5,062281
1
A: Serine/threonine-protein phosphatase
B: Calcineurin subunit B
C: FK506-binding protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)81,47211
Polymers80,2703
Non-polymers1,2038
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Serine/threonine-protein phosphatase
E: Calcineurin subunit B
F: FK506-binding protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)81,60713
Polymers80,2703
Non-polymers1,33810
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)62.470, 142.850, 175.610
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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Protein , 3 types, 6 molecules ADBECF

#1: Protein Serine/threonine-protein phosphatase


Mass: 47252.438 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Candida albicans (strain WO-1) (yeast) / Strain: WO-1 / Gene: CAWG_01301 / Plasmid: PEMB40 / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: C4YFI3, protein-serine/threonine phosphatase
#2: Protein Calcineurin subunit B


Mass: 19453.877 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Candida albicans (strain WO-1) (yeast) / Strain: WO-1 / Gene: CAWG_04882 / Plasmid: PET15B / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: C4YS24
#3: Protein FK506-binding protein 1 / FKBP / Peptidyl-prolyl cis-trans isomerase / PPIase / Rapamycin-binding protein


Mass: 13563.345 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Candida albicans (strain SC5314 / ATCC MYA-2876) (yeast)
Strain: SC5314 / ATCC MYA-2876
Gene: RBP1, RBP11, CaO19.11186, CaO19.3702, RBP2, RBP12, CAALFM_C702570CA, CaJ7.0299, CaO19.13810, CaO19.6452
Plasmid: pET15b / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P28870, peptidylprolyl isomerase

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Non-polymers , 7 types, 299 molecules

#4: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: PO4
#5: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#6: Chemical ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe
#7: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#8: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Ca
#9: Chemical ChemComp-FK5 / 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN / K506


Mass: 804.018 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C44H69NO12 / Feature type: SUBJECT OF INVESTIGATION / Comment: medication*YM
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 281 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.45 Å3/Da / Density % sol: 49.79 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7.29
Details: CANDIDA ALBICANS VCID8024 [CALCINEURIN A FUSED TO CALCINEURIN B] AND R8065 [FKBP12] IN A SEC PURIFIED COMPLEX MEDIATED BY FK506/TACROLIMUS AT 10.2 MG/ ML AND SUPPLEMENTED WITH 25.6UM R8065 ...Details: CANDIDA ALBICANS VCID8024 [CALCINEURIN A FUSED TO CALCINEURIN B] AND R8065 [FKBP12] IN A SEC PURIFIED COMPLEX MEDIATED BY FK506/TACROLIMUS AT 10.2 MG/ ML AND SUPPLEMENTED WITH 25.6UM R8065 AND 32UM FK506. PROTEIN BUFFER INCLUDES 10MM TRIS PH 7.5, 50 MM NACL, 1.0MM CACL2. THE PROTEIN COMPLEX WAS CRYSTALLIZED AGAINST OPTIMIZATION SCREEN AMP_PROPLEX_A10 (OPT SCREEN BASED ON PROPLEX CONDITION A10) WELL B7: 0.1M TRIS-HCL, 15.91% PEG 2,000 MME, 0.1M POTASSIUM CHLORIDE, AND CRYO-PROTECTED WITH 20% ETHYLENE GLYCOL
PH range: 7.29

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.9786 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 27, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9786 Å / Relative weight: 1
ReflectionResolution: 2.55→50 Å / Num. obs: 51429 / % possible obs: 98.4 % / Observed criterion σ(I): -3 / Redundancy: 4.4 % / CC1/2: 0.998 / Rmerge(I) obs: 0.083 / Rrim(I) all: 0.094 / Net I/σ(I): 16.87
Reflection shellResolution: 2.55→2.62 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.56 / Mean I/σ(I) obs: 3.4 / Num. unique obs: 3787 / CC1/2: 0.826 / Rrim(I) all: 0.635 / % possible all: 99.2

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Processing

Software
NameClassification
XDSdata reduction
XSCALEdata scaling
PHENIXrefinement
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1TCO

1tco


Resolution: 2.55→34.996 Å / SU ML: 0.3 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.03
RfactorNum. reflection% reflection
Rfree0.2286 1999 3.89 %
Rwork0.182 --
obs0.1839 51342 98.47 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.55→34.996 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9363 0 148 281 9792
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0089802
X-RAY DIFFRACTIONf_angle_d0.91613361
X-RAY DIFFRACTIONf_dihedral_angle_d12.1225816
X-RAY DIFFRACTIONf_chiral_restr0.0481494
X-RAY DIFFRACTIONf_plane_restr0.0061745
LS refinement shell

Refine-ID: X-RAY DIFFRACTION

Resolution (Å)Highest resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.5501-2.61390.2894142351999
2.6139-2.68450.2878141346199
2.6845-2.76350.3074142351699
2.7635-2.85260.2929142349899
2.8526-2.95450.2424142351699
2.9545-3.07280.224141349199
3.0728-3.21250.238144352299
3.2125-3.38180.2609142352799
3.3818-3.59340.2559142352099
3.5934-3.87060.2287143352998
3.8706-4.25950.18281430.1471351699
4.2595-4.87440.16211450.1333358298
4.8744-6.13580.2151144355898
6.13580.2264146358894
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)
11.1646-0.1714-0.28041.38630.45123.5663-0.22370.3423-0.1185-0.1363-0.1330.09170.7916-0.50660.39210.3382-0.11080.08350.36080.01750.34932.0176-30.5972-14.4281
21.79640.61710.41874.00731.92122.4861-0.0573-0.0488-0.01650.1202-0.06850.53340.1121-0.3650.09350.1649-0.01970.01490.20830.06250.17766.6262-22.6545-7.1958
32.08640.3230.13392.20160.83830.5988-0.056-0.013-0.09850.02480.0553-0.04590.11840.1065-0.00960.16580.00540.00950.18590.02010.094618.7457-20.9057-7.0758
42.70070.0906-0.07272.53360.63081.32620.0157-0.18220.22160.20850.1451-0.30470.06430.2105-0.10580.17570.0155-0.01970.2167-0.03420.179425.2102-9.1941-1.0511
52.1926-0.82460.95511.11590.15190.74410.11880.17230.21870.02010.2714-0.9427-0.02090.5293-0.15410.2372-0.0088-0.05530.4988-0.19250.681343.7036-10.9946-4.8165
61.4130.95210.49392.4229-0.21962.52220.0378-0.1306-0.31120.04620.1801-0.7250.34390.5365-0.2410.24790.1054-0.07710.4121-0.07150.300637.0307-21.5091-3.6203
74.21721.10830.89373.6455-0.60614.34180.01750.034-0.22180.26710.2482-0.65070.27890.6483-0.26410.21080.1203-0.02140.3076-0.09070.322135.222-25.8714-6.5299
82.12920.48970.88760.90230.04121.949-0.30610.1745-0.15550.07030.1825-0.3-0.1586-0.03190.1320.27670.0936-0.02560.21480.00420.17823.6232-28.9079-14.2071
90.1736-0.0075-0.044-0.0004-0.00060.0106-0.2870.46850.3073-0.5202-0.10320.1407-0.4070.00960.21810.6957-0.0181-0.05370.6460.02080.1818.8128-17.7213-47.7702
102222-7.039120.8241-8.58435.63150.16830.6799-4.1686-6.124111.5328-1.50510.9952-0.12180.161.0309-0.2950.73817.1143-16.2077-66.8296
111.27250.0166-0.09410.65821.35212.78960.23030.59880.1222-0.7647-0.2870.14930.1247-0.17720.01011.1251-0.3052-0.24191.19080.26770.46-2.1974-13.5934-67.0483
122.78050.12613.63964.5569-0.6145.37860.3441-0.4304-0.6270.40690.01070.05922.14260.587-0.3121.5136-0.1195-0.07230.94890.0480.45094.5435-27.3239-62.9772
131.7394-0.10330.37041.31430.47592.1751-0.06120.5274-0.0942-0.50440.0990.16140.2891-0.2522-0.05470.9292-0.0275-0.26510.8582-0.02080.30076.2777-25.1328-53.9457
143.59372.1559-0.00842.82381.76582.0490.1672-0.0115-0.20030.0016-0.07090.21480.4568-0.4928-0.0611.3085-0.3945-0.56851.09660.07960.8903-5.6895-28.7677-57.7089
153.3334-0.6227-0.55322.56770.25554.4560.51090.18-0.1725-0.32-0.17610.6659-0.2374-0.93930.01840.7065-0.0163-0.30441.03120.16540.5121-4.6049-16.1293-55.8434
164.151-1.4277-1.82680.93510.78330.85760.38680.6960.2085-0.6769-0.07970.3419-0.0802-0.2092-0.25090.54740.0264-0.15820.77710.01640.4219-2.6391-18.6351-43.9052
170.7555-0.02350.8812.25220.25942.43080.03730.2758-0.4493-0.353-0.12410.39590.5214-0.32070.10130.5338-0.0453-0.06210.5285-0.120.22136.0203-29.5663-35.8879
182.26170.4579-1.94393.2346-2.03435.97570.2976-0.65870.23320.11-0.21350.597-0.1182-0.6011-0.08520.3591-0.0689-0.0340.6891-0.14730.4693-5.6835-22.5682-31.7118
190.87071.03240.99583.8626-0.41832.10810.5072-0.12331.33920.03950.18040.0437-2.87140.0136-0.59191.13350.0541-0.04440.5717-0.15720.77622.4354-10.3168-41.9266
202.09381.09290.39880.8557-0.43221.52540.12270.75-0.1234-0.3916-0.1546-0.8717-0.08690.71920.04610.7404-0.02510.22050.81760.07470.58134.7273-17.5274-42.3486
211.2790.07060.04934.9912.0283.59790.07190.1679-0.0917-0.02690.1703-0.41490.38880.3103-0.13570.6224-0.00980.01260.40010.03480.272624.6221-19.4813-37.665
220.21490.40380.79772.7731-1.19036.6476-0.04260.35970.0282-0.34450.1442-0.18620.19390.3263-0.09780.7208-0.14930.2210.77580.07230.415129.2478-14.3541-47.1232
230.88330.44340.24270.22310.12250.0673-0.0569-0.1672-0.231-0.0930.014-0.08020.05160.28690.28530.6155-0.04960.52150.95560.02180.874237.5117-14.8278-48.4468
240.39590.90320.31413.4812-1.31853.62170.15460.5130.3505-0.4153-0.07190.0874-0.84280.24920.01580.70460.00580.14290.48740.11510.390225.7932-8.3202-40.6656
252.0422-1.47712.41827.03271.79395.08020.09610.19670.82510.6025-0.20570.7407-0.861-0.4632-0.01070.6090.00120.1010.45850.02290.456917.2707-7.4307-35.3926
262.30870.53630.94672.00020.01780.4740.174-0.0077-0.28340.3977-0.1183-1.04-0.1120.00120.05370.6127-0.09170.04790.5830.08850.327332.085-17.7541-36.9375
272.81471.3386-0.98784.9556-1.39391.4834-0.0323-0.0216-0.0153-0.10840.00110.19810.106-0.24590.02430.80660.05620.20631.2998-0.47870.959234.0147-28.5421-47.4513
281.9351-0.8380.27651.9925-0.46462.9983-0.05330.12080.95760.0611-0.2803-0.0334-1.00630.68610.27920.4969-0.2279-0.03410.43120.04080.721225.432125.8571-6.587
291.3657-0.3814-0.14351.66710.25231.06990.0932-0.36310.66860.3153-0.07270.5047-0.1480.157-0.00170.3322-0.0750.07530.2815-0.10660.516814.098112.35832.3306
302.10690.1513-0.11992.2599-0.18581.36680.1066-0.25770.51540.1887-0.07890.6355-0.2829-0.0631-0.02970.2644-0.02370.05870.2449-0.04160.51119.006410.81-2.6189
310.12750.2464-0.06490.5328-0.11930.1020.058-0.1930.65470.31280.04291.2119-0.1427-0.2950.12360.33020.09510.25660.4702-0.00171.5048-11.074710.7007-1.468
321.74850.17910.05061.3203-0.06720.4839-0.20120.03770.83710.19710.09360.9098-0.121-0.29390.08410.59080.03320.04740.3070.00971.08554.066724.497-8.0742
330.6401-0.0373-0.96370.024-0.04451.87820.07260.1404-0.1874-0.4060.094-0.10150.3212-0.4702-0.06850.7262-0.1483-0.00040.56830.30390.709619.662620.912-43.3968
342.53310.9912-1.2320.9548-1.16536.06790.190.1037-0.2299-0.25340.59450.84490.2501-0.4952-0.60650.9617-0.2432-0.09611.11530.17540.792931.057519.8353-64.1082
350.87180.0949-0.38710.97030.94711.1907-0.39040.31460.17-0.2998-0.1899-0.5294-0.29580.49160.52420.8393-0.04970.10480.78950.23441.135926.251633.4714-59.299
362.0560.3546-2.89370.8303-0.6774.1287-0.40350.49770.2444-0.18650.194-0.0452-0.25160.03980.16980.7058-0.245900.8230.18060.68917.121528.8517-50.9111
374.7398-1.7241.45923.71311.77584.2090.45770.04930.5949-0.12880.178-0.1388-0.31920.1869-0.49530.8359-0.20490.12770.62950.17650.677627.11329.6502-47.2417
386.36464.29613.13363.6682.11332.65370.2475-0.161-0.172-0.06420.0392-0.33360.33880.124-0.13191.0455-0.2368-0.21250.7830.48811.328534.192332.969-52.5351
396.2179-0.11150.95592.20822.86393.9089-0.00830.41030.655-0.22060.28840.11340.1036-0.0522-0.25440.943-0.05570.08580.68970.16080.818733.095519.5827-52.236
400.51920.52510.59252.356-1.73013.64970.01480.23030.3604-0.29990.11420.06780.09210.3277-0.2250.7805-0.17030.15810.81640.28690.672131.359720.8468-40.0567
410.3870.5838-0.15141.6141-0.40922.3797-0.19570.2450.6157-0.1625-0.0721-0.0846-0.65530.46250.17130.6414-0.175-0.08060.4940.26710.835425.052329.4817-29.0496
425.1205-0.53172.58833.59891.80742.5953-0.17940.38060.2311-0.48430.25380.07140.0340.42750.02920.6045-0.1666-0.05590.83950.43630.956233.58118.884-30.6224
430.01780.0899-0.19050.5376-1.39534.23820.4631-0.1411-0.3244-0.52-0.00280.1511.2519-0.2353-0.34231.183-0.2034-0.15330.70510.26010.858925.812512.5212-38.8743
444.9655-4.09-5.15574.374.40015.37730.43950.09410.0808-0.10450.1657-0.09340.1704-0.4835-0.46851.0281-0.227-0.22790.75760.14140.5906-7.666711.6058-37.6703
450.65570.3676-0.54490.47180.0841.0446-0.0815-0.0374-0.2535-0.05680.14440.0372-0.2107-0.6799-0.01870.599-0.0485-0.10360.74650.24790.6586-4.227923.0185-37.1849
462.2367-0.91611.28813.16961.05042.2602-0.3844-0.281-0.1438-0.20270.2036-0.30490.03840.01230.15040.7204-0.198-0.11740.57690.22990.74334.56916.676-25.8475
476.8964-0.71250.02285.8658-0.88340.39650.0410.97470.4910.15890.3661-0.2553-0.6076-0.0307-0.34390.6436-0.0947-0.11330.60750.19250.43534.112524.5704-39.6996
480.62040.3319-0.85223.8713.52465.46110.15190.43280.0048-0.45460.1620.0728-0.149-0.4354-0.2140.8976-0.2983-0.12960.92360.29330.495-0.44317.3891-43.1126
490.8630.43990.73061.2980.27851.1441-0.1979-0.11530.1656-0.1093-0.04650.025-0.1736-0.35510.29870.6827-0.0719-0.31381.20510.26120.5723-8.31119.084-43.0213
501.3562-0.6294-1.1193.22650.13161.9537-0.03560.0597-0.09470.1011-0.0412-0.12530.2-0.24780.10160.6644-0.1583-0.22960.6070.2010.49533.180514.0006-35.7225
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 62 through 91 )
2X-RAY DIFFRACTION2chain 'A' and (resid 92 through 123 )
3X-RAY DIFFRACTION3chain 'A' and (resid 124 through 220 )
4X-RAY DIFFRACTION4chain 'A' and (resid 221 through 281 )
5X-RAY DIFFRACTION5chain 'A' and (resid 282 through 320 )
6X-RAY DIFFRACTION6chain 'A' and (resid 321 through 339 )
7X-RAY DIFFRACTION7chain 'A' and (resid 340 through 374 )
8X-RAY DIFFRACTION8chain 'A' and (resid 375 through 397 )
9X-RAY DIFFRACTION9chain 'A' and (resid 398 through 419 )
10X-RAY DIFFRACTION10chain 'A' and (resid 420 through 420 )
11X-RAY DIFFRACTION11chain 'B' and (resid 19 through 31 )
12X-RAY DIFFRACTION12chain 'B' and (resid 32 through 47 )
13X-RAY DIFFRACTION13chain 'B' and (resid 48 through 64 )
14X-RAY DIFFRACTION14chain 'B' and (resid 65 through 73 )
15X-RAY DIFFRACTION15chain 'B' and (resid 74 through 89 )
16X-RAY DIFFRACTION16chain 'B' and (resid 90 through 101 )
17X-RAY DIFFRACTION17chain 'B' and (resid 102 through 142 )
18X-RAY DIFFRACTION18chain 'B' and (resid 143 through 158 )
19X-RAY DIFFRACTION19chain 'B' and (resid 159 through 169 )
20X-RAY DIFFRACTION20chain 'C' and (resid 4 through 34 )
21X-RAY DIFFRACTION21chain 'C' and (resid 35 through 60 )
22X-RAY DIFFRACTION22chain 'C' and (resid 61 through 68 )
23X-RAY DIFFRACTION23chain 'C' and (resid 69 through 85 )
24X-RAY DIFFRACTION24chain 'C' and (resid 86 through 100 )
25X-RAY DIFFRACTION25chain 'C' and (resid 101 through 111 )
26X-RAY DIFFRACTION26chain 'C' and (resid 112 through 119 )
27X-RAY DIFFRACTION27chain 'C' and (resid 120 through 122 )
28X-RAY DIFFRACTION28chain 'D' and (resid 65 through 106 )
29X-RAY DIFFRACTION29chain 'D' and (resid 107 through 143 )
30X-RAY DIFFRACTION30chain 'D' and (resid 144 through 281 )
31X-RAY DIFFRACTION31chain 'D' and (resid 282 through 359 )
32X-RAY DIFFRACTION32chain 'D' and (resid 360 through 397 )
33X-RAY DIFFRACTION33chain 'D' and (resid 398 through 419 )
34X-RAY DIFFRACTION34chain 'E' and (resid 19 through 30 )
35X-RAY DIFFRACTION35chain 'E' and (resid 31 through 46 )
36X-RAY DIFFRACTION36chain 'E' and (resid 47 through 56 )
37X-RAY DIFFRACTION37chain 'E' and (resid 57 through 64 )
38X-RAY DIFFRACTION38chain 'E' and (resid 65 through 73 )
39X-RAY DIFFRACTION39chain 'E' and (resid 74 through 89 )
40X-RAY DIFFRACTION40chain 'E' and (resid 90 through 101 )
41X-RAY DIFFRACTION41chain 'E' and (resid 102 through 151 )
42X-RAY DIFFRACTION42chain 'E' and (resid 152 through 158 )
43X-RAY DIFFRACTION43chain 'E' and (resid 159 through 169 )
44X-RAY DIFFRACTION44chain 'F' and (resid 4 through 12 )
45X-RAY DIFFRACTION45chain 'F' and (resid 13 through 34 )
46X-RAY DIFFRACTION46chain 'F' and (resid 35 through 46 )
47X-RAY DIFFRACTION47chain 'F' and (resid 47 through 60 )
48X-RAY DIFFRACTION48chain 'F' and (resid 61 through 68 )
49X-RAY DIFFRACTION49chain 'F' and (resid 69 through 85 )
50X-RAY DIFFRACTION50chain 'F' and (resid 86 through 124 )

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