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- PDB-8xwx: Crystal structure of FIS1-BAP31 complex from human -

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Basic information

Entry
Database: PDB / ID: 8xwx
TitleCrystal structure of FIS1-BAP31 complex from human
Components
  • B-cell receptor-associated protein 31
  • Mitochondrial fission 1 protein
KeywordsAPOPTOSIS / MAM complex / mitochondria / ER.
Function / homology
Function and homology information


positive regulation of retrograde protein transport, ER to cytosol / response to flavonoid / negative regulation of fatty acid transport / negative regulation of ATP metabolic process / response to fluoride / response to hypobaric hypoxia / Class I peroxisomal membrane protein import / protein localization to endoplasmic reticulum exit site / Apoptotic execution phase / positive regulation of ERAD pathway ...positive regulation of retrograde protein transport, ER to cytosol / response to flavonoid / negative regulation of fatty acid transport / negative regulation of ATP metabolic process / response to fluoride / response to hypobaric hypoxia / Class I peroxisomal membrane protein import / protein localization to endoplasmic reticulum exit site / Apoptotic execution phase / positive regulation of ERAD pathway / mitochondria-associated endoplasmic reticulum membrane contact site / perinuclear endoplasmic reticulum / peroxisome fission / mitochondrial fragmentation involved in apoptotic process / cellular response to peptide / cellular response to toxic substance / mitochondrial fission / positive regulation of ubiquitin-dependent protein catabolic process / cellular response to lipid / clathrin-coated vesicle / peroxisomal membrane / protein targeting to mitochondrion / Golgi cisterna membrane / positive regulation of mitochondrial fission / Apoptotic cleavage of cellular proteins / response to muscle activity / RSV-host interactions / MHC class I protein binding / RHOA GTPase cycle / endoplasmic reticulum to Golgi vesicle-mediated transport / positive regulation of intrinsic apoptotic signaling pathway / lipid droplet / endoplasmic reticulum-Golgi intermediate compartment membrane / response to endoplasmic reticulum stress / lumenal side of endoplasmic reticulum membrane / mitochondrion organization / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / intracellular protein transport / cellular response to glucose stimulus / response to nutrient levels / peroxisome / positive regulation of neuron apoptotic process / spermatogenesis / molecular adaptor activity / mitochondrial outer membrane / Golgi membrane / apoptotic process / lipid binding / endoplasmic reticulum membrane / protein-containing complex binding / endoplasmic reticulum / protein-containing complex / mitochondrion / identical protein binding / membrane / plasma membrane / cytosol
Similarity search - Function
B-cell receptor-associated protein 29/31 / BAP29/BAP31, transmembrane domain / Bap31/Bap29 cytoplasmic coiled-coil domain / Bap31/Bap29 transmembrane region / Bap31/Bap29 cytoplasmic coiled-coil domain / Mitochondria fission 1 protein / Fis1, N-terminal tetratricopeptide repeat / Fis1, C-terminal tetratricopeptide repeat / Mitochondria fission protein Fis1, cytosolic domain / Fis1 N-terminal tetratricopeptide repeat ...B-cell receptor-associated protein 29/31 / BAP29/BAP31, transmembrane domain / Bap31/Bap29 cytoplasmic coiled-coil domain / Bap31/Bap29 transmembrane region / Bap31/Bap29 cytoplasmic coiled-coil domain / Mitochondria fission 1 protein / Fis1, N-terminal tetratricopeptide repeat / Fis1, C-terminal tetratricopeptide repeat / Mitochondria fission protein Fis1, cytosolic domain / Fis1 N-terminal tetratricopeptide repeat / Fis1 C-terminal tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily
Similarity search - Domain/homology
BETA-MERCAPTOETHANOL / B-cell receptor-associated protein 31 / Mitochondrial fission 1 protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.69 Å
AuthorsNguyen, M.D. / Bong, S.M. / Lee, B.I.
Funding support Korea, Republic Of, 2items
OrganizationGrant numberCountry
National Research Foundation (NRF, Korea)2018R1A5A2023127 Korea, Republic Of
National Research Foundation (NRF, Korea)2019R1A2C1002545 Korea, Republic Of
Citation
Journal: Commun Biol / Year: 2025
Title: Crystal structure of Fis1 and Bap31 provides information on protein-protein interactions at mitochondria-associated ER membranes.
Authors: Nguyen, M.D. / Kim, Y. / Bae, S.H. / Kim, S. / Yeo, H.K. / Ha, N.C. / Cho, G. / Moon, S. / Cho, K.H. / Jang, H. / Bong, S.M. / Lee, B.I.
#1: Journal: Acta Crystallogr D Struct Biol / Year: 2019
Title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix.
Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty ...Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams /
Abstract: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks.
History
DepositionJan 17, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 15, 2024Provider: repository / Type: Initial release
Revision 1.1Aug 13, 2025Group: Database references / Structure summary / Category: citation / citation_author / pdbx_entry_details
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.pdbx_database_id_DOI / _citation.title / _citation.year / _pdbx_entry_details.has_protein_modification
Revision 1.2Aug 20, 2025Group: Database references / Category: citation
Item: _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
E: B-cell receptor-associated protein 31
A: Mitochondrial fission 1 protein
G: B-cell receptor-associated protein 31
D: B-cell receptor-associated protein 31
F: B-cell receptor-associated protein 31
C: Mitochondrial fission 1 protein
B: Mitochondrial fission 1 protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,8679
Polymers75,6937
Non-polymers1742
Water45025
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.632, 237.267, 90.622
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number21
Space group name H-MC222
Space group name HallC22
Symmetry operation#1: x,y,z
#2: x,-y,-z
#3: -x,y,-z
#4: -x,-y,z
#5: x+1/2,y+1/2,z
#6: x+1/2,-y+1/2,-z
#7: -x+1/2,y+1/2,-z
#8: -x+1/2,-y+1/2,z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1(chain "A" and (resid 3 through 18 or resid 21...
d_2ens_1(chain "B" and (resid 3 through 18 or resid 21...
d_3ens_1(chain "C" and (resid 3 through 18 or resid 21...
d_1ens_2(chain "D" and (resid 170 or resid 172 through 203...
d_2ens_2(chain "F" and (resid 170 or resid 172 through 203...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_11ens_1ALAALAGLUGLUAB3 - 185 - 20
d_12ens_1PHEPHEALAALAAB21 - 3923 - 41
d_13ens_1CYSCYSGLUGLUAB41 - 5943 - 61
d_14ens_1LEULEUPROPROAB61 - 6363 - 65
d_15ens_1GLYGLYSERSERAB65 - 6667 - 68
d_16ens_1GLUGLUGLUGLUAB6870
d_17ens_1GLNGLNVALVALAB70 - 9472 - 96
d_18ens_1GLYGLYLEULEUAB96 - 9898 - 100
d_19ens_1THRTHRPROPROAB100 - 102102 - 104
d_110ens_1ALAALAGLUGLUAB107 - 111109 - 113
d_111ens_1LEULEULYSLYSAB113 - 119115 - 121
d_21ens_1ALAALAGLUGLUBG3 - 185 - 20
d_22ens_1PHEPHEALAALABG21 - 3923 - 41
d_23ens_1CYSCYSGLUGLUBG41 - 5943 - 61
d_24ens_1LEULEUPROPROBG61 - 6363 - 65
d_25ens_1GLYGLYSERSERBG65 - 6667 - 68
d_26ens_1GLUGLUGLUGLUBG6870
d_27ens_1GLNGLNVALVALBG70 - 9472 - 96
d_28ens_1GLYGLYLEULEUBG96 - 9898 - 100
d_29ens_1THRTHRPROPROBG100 - 102102 - 104
d_210ens_1ALAALAGLUGLUBG107 - 111109 - 113
d_211ens_1LEULEULYSLYSBG113 - 119115 - 121
d_31ens_1ALAALAGLUGLUCF3 - 185 - 20
d_32ens_1PHEPHEALAALACF21 - 3923 - 41
d_33ens_1CYSCYSGLUGLUCF41 - 5943 - 61
d_34ens_1LEULEUPROPROCF61 - 6363 - 65
d_35ens_1GLYGLYSERSERCF65 - 6667 - 68
d_36ens_1GLUGLUVALVALCF69 - 9471 - 96
d_37ens_1GLYGLYLEULEUCF96 - 9898 - 100
d_38ens_1THRTHRPROPROCF100 - 102102 - 104
d_39ens_1ALAALAGLUGLUCF107 - 111109 - 113
d_310ens_1LEULEULYSLYSCF113 - 119115 - 121
d_11ens_2VALVALVALVALDD1705
d_12ens_2ASNASNGLUGLUDD172 - 2037 - 38
d_13ens_2ALAALAARGARGDD205 - 21340 - 48
d_14ens_2GLNGLNLEULEUDD215 - 23350 - 68
d_21ens_2VALVALVALVALFE1705
d_22ens_2ASNASNGLUGLUFE172 - 2037 - 38
d_23ens_2ALAALAARGARGFE205 - 21340 - 48
d_24ens_2GLNGLNLEULEUFE215 - 23350 - 68

NCS ensembles :
ID
ens_1
ens_2

NCS oper:
IDCodeMatrixVector
1given(-0.86279582209, -0.500522724544, 0.0711362889023), (-0.504405130336, 0.842798232493, -0.187794046228), (0.0340416491179, -0.197909427574, -0.979629023969)76.1972068975, 28.2095241993, 72.0043077603
2given(0.905874670702, -0.410457491195, -0.104478365715), (0.423324970345, 0.869458311883, 0.254633488331), (-0.013676639312, -0.274894328459, 0.961377167254)-9.94365442973, -40.1918791561, -11.5554189336
3given(-0.849129247239, -0.528180085996, -0.00230613112325), (-0.528184191425, 0.849127849217, 0.00183183319154), (0.000990662348064, 0.00277352514165, -0.999995663064)79.8839306777, 22.618648922, 70.1826806363

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Components

#1: Protein
B-cell receptor-associated protein 31 / BCR-associated protein 31 / Bap31


Mass: 8053.073 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BCAP31, BAP31 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P51572
#2: Protein Mitochondrial fission 1 protein / FIS1 homolog / hFis1


Mass: 14493.609 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FIS1 / Production host: Escherichia coli (E. coli) / Strain (production host): DE3 / Variant (production host): pLysS / References: UniProt: Q9Y3D6
#3: Chemical ChemComp-BME / BETA-MERCAPTOETHANOL


Mass: 78.133 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6OS
#4: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 25 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN
Has protein modificationN

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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: 3.72 Å3/Da / Density % sol: 66.9 %
Crystal growTemperature: 287 K / Method: vapor diffusion, sitting drop / pH: 7.4
Details: 100 mM sodium acetate pH 4.6, 1.5 M lithium sulfate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PAL/PLS / Beamline: 5C (4A) / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Dec 2, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.69→40.96 Å / Num. obs: 27276 / % possible obs: 85.8 % / Observed criterion σ(F): 1.35 / Redundancy: 8.2 % / Biso Wilson estimate: 36.52 Å2 / CC1/2: 0.993 / CC star: 0.998 / Rpim(I) all: 0.018 / Rrim(I) all: 0.05 / Net I/σ(I): 99.8
Reflection shellResolution: 2.69→2.76 Å / Num. unique obs: 946 / CC1/2: 0.57 / CC star: 0.852 / Rpim(I) all: 0.587 / % possible all: 42.16

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Processing

Software
NameVersionClassification
PHENIX1.21rc1_5156refinement
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.69→40.96 Å / SU ML: 0.3878 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 30.1803
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2868 2000 7.33 %
Rwork0.2536 25276 -
obs0.256 27276 85.8 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 54.22 Å2
Refinement stepCycle: LAST / Resolution: 2.69→40.96 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4730 0 9 25 4764
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00544779
X-RAY DIFFRACTIONf_angle_d0.78176391
X-RAY DIFFRACTIONf_chiral_restr0.0404724
X-RAY DIFFRACTIONf_plane_restr0.0051816
X-RAY DIFFRACTIONf_dihedral_angle_d21.88131850
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2BAX-RAY DIFFRACTIONTorsion NCS1.08336378198
ens_1d_3BAX-RAY DIFFRACTIONTorsion NCS1.03313440872
ens_2d_2DDX-RAY DIFFRACTIONTorsion NCS0.781961312362
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.69-2.760.4621700.3237876X-RAY DIFFRACTION42.16
2.76-2.830.3151870.28851110X-RAY DIFFRACTION53.44
2.83-2.920.35791040.27831305X-RAY DIFFRACTION63.41
2.92-3.010.32051200.28551528X-RAY DIFFRACTION73.34
3.01-3.120.37021360.31031715X-RAY DIFFRACTION82.78
3.12-3.240.34441510.2761914X-RAY DIFFRACTION91.21
3.24-3.390.34211580.29091986X-RAY DIFFRACTION95.2
3.39-3.570.31061620.26762056X-RAY DIFFRACTION98.75
3.57-3.790.28471660.24492087X-RAY DIFFRACTION99.91
3.79-4.080.29431660.24052099X-RAY DIFFRACTION100
4.08-4.490.23391660.21722105X-RAY DIFFRACTION99.96
4.49-5.140.22411680.21812113X-RAY DIFFRACTION99.91
5.14-6.470.32691700.29552156X-RAY DIFFRACTION99.83
6.48-40.960.23091760.22442226X-RAY DIFFRACTION99.05
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.950889428884-1.803123227650.3218093026576.43909966396-1.035967711030.2435116663270.0177872834309-0.00254945614953-0.2408926910240.0691162201937-0.001106486701390.0001553102613750.138834282330.00787634299908-0.02744386739730.6689847168560.374569233435-0.03514361768990.35931065916-0.002979782267450.45555389508623.724153415453.1216430965.4844519986
26.13029406061-2.52855591464-1.426740370278.585382015982.597588197354.46012319320.0420494377941-0.2660702938670.3685377426920.204770491010.0817642752161-0.162450715924-0.6828442532030.0540398135063-0.1255268322420.237037908870.00962555014885-0.08140790558440.151935456587-0.007508591691550.12004255709658.548631147323.961427130452.013672157
31.1309624672-0.773634888972-0.5306496343551.641088182521.19265983911.715120088570.08928630033020.120667682810.0797555090474-0.171228586053-0.07000366215560.00705505704748-0.370513064439-0.1332299635140.07860258166080.2445040793040.166810156097-0.0394527985540.186732768222-0.02104099863570.031449749749748.751906749323.387678505655.2703778431
40.712442768831-0.09827281303070.3560467583280.5922842380540.445515349330.598341971814-0.0334377983903-0.01871670259430.0347812624381-0.1072603390990.03413650410960.17859912138-0.114630999684-0.167306375954-0.05430708186150.2111806640760.116392624263-0.08987512297090.2171796520860.2285952659680.17361926474835.610993043218.059684768550.0724781911
52.13516058773-2.90524090188-1.049304428216.110916938732.225816903490.812367899238-0.129081268878-0.285685721612-0.292452327550.4570387823450.07515937478780.2170874650860.3303648651370.2185143159880.0326486862580.9402610964510.3114931802610.01476477004380.456628029703-0.04221554879680.25239355229831.053725023955.64364368074.91139303251
61.2838660711-2.53781453974-0.4720229528137.181184412520.977130984630.629970408589-0.0553393389972-0.05914943149190.04989178604790.0622906674975-0.0003754807677110.0264562506761-0.128821671639-0.0575182803696-0.009353925191550.7401576621070.41219282263-0.05945428674910.409938899038-0.05628189983260.193615195828.304292213661.387150264772.7374647003
70.2759267958740.05526152673090.04087126245661.86854816945-0.4722669363150.3903877020110.210982061109-0.0531516627395-0.07351134607210.117616008158-0.163358802347-0.017198757158-0.1185034240380.02938112623740.1075104383170.8901729060770.298787131282-0.04693818214020.396787430203-0.0239687362360.17521326182823.486007560558.4642666648-2.18772605735
82.23245766356-1.17569573713-0.2965087406742.59490247290.8801020830721.52279250336-0.002440009906530.01619958922740.0852086808808-0.1148993266030.05952258364990.212617698196-0.267926073082-0.4839440703330.01674546482190.4383337663420.0663814897537-0.2639942539120.4798378527550.230304853040.44927848148627.506759091919.538092520230.9951417477
92.7103778555-2.867729479552.540699163923.71645763297-2.071822323022.939937966260.4463131211370.413736626532-0.123137373899-0.644154638918-0.4982034406640.225651122241-0.00307100014979-0.02336473489460.08728456104040.4480762653830.0431830670603-0.2092744278490.6841457536550.3463915282430.7399693926721.195358549314.978571744931.53449559
106.36652306689-2.58219479951.816628322584.160627560830.01042367037783.45854195959-0.136021902696-0.2224461686030.206737756921-0.144644583124-0.2085399211660.259569492607-0.387197535663-0.6371263630520.3641823349990.3341216657060.0872177184458-0.0718361929930.822499962840.3728358513590.90197643844716.513543646914.421231210638.4984667005
116.39698742497-0.8552255040795.326154365471.48948739997-1.594727063456.1934252965-0.4269835742391.022273697330.348155691859-0.4392398499440.05878267159850.58007874057-0.757461682944-0.1970582071540.3756719859280.691553786627-0.0924750243777-0.4383146035271.338808798850.3482840003041.345155604015.4671420606917.811581206826.9467757919
128.05280145303-2.59982035511.085331854682.872995603240.2331127784551.61876113284-0.1261552449460.9065704523960.460331683189-0.316059383575-0.07426351534670.428854655761-0.227900397844-0.07041416354840.1484544337160.405286248875-0.177070531486-0.208374976370.9373428571510.3931170094351.125208073812.52249556188.0658496011831.0930058865
135.475823002351.23549972605-0.299558160442.040222778150.5894298576660.261421263676-0.09029520105460.0578540532021-0.660970309215-0.0439801048136-0.05165599571730.4221268422770.126757224884-0.3825013317490.1472495125770.355929702983-0.115433600208-0.1054353076631.101876417380.2850251157241.211557286017.877534544152.8523991973135.0313394938
145.523390153071.011435596737.06148686652.696233944940.5550811435079.24480371731-0.55029146644-0.1265236187130.528396704641-0.8748285813340.3417382077450.9057199855120.293720201182-1.644964097220.2113066505340.877707679836-0.287788123372-0.2118615401191.143605574410.2738708332641.284236128817.271115708371.0358142576321.5736095022
156.111757572523.16862597439-0.8212521771793.429671898550.4005969227713.16241297738-0.463149314420.102385268038-0.748588985308-0.146092953506-0.00232665864513-0.1466833665090.384185059476-0.2741192276740.4553157839180.615667229314-0.300491420985-0.1636837734821.058995285340.4879462556861.5071279491212.1824944263-6.9011376794734.0880651838
162.710177505860.47117417970.926788785770.4719195487960.6842788401472.710102918870.226632125348-0.0881558463846-0.340516378685-0.0999669405594-0.1358329866550.238159845470.170308689628-0.755947937728-0.143921126420.913824687737-0.229086788844-0.555169512720.8584299952680.2590873477850.89813926239119.68828306710.552085530218.0774010203
171.39901709921-0.5411006843381.118032672580.868215069464-0.5547464472132.323211516110.147789456440.155966983124-0.178838037327-0.402381157923-0.002972381381210.2360999346070.2374664670560.01694191728730.001898534990260.532629315541-0.0224443629887-0.2443450903020.3121440133770.1347319684730.16721702120937.774309294215.534932475918.761879979
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'E' and (resid 179 through 236 )EA179 - 2361 - 58
22chain 'A' and (resid 1 through 31 )AB1 - 311 - 31
33chain 'A' and (resid 32 through 62 )AB32 - 6232 - 62
44chain 'A' and (resid 63 through 120 )AB63 - 12063 - 120
55chain 'G' and (resid 179 through 235 )GC179 - 2351 - 57
66chain 'D' and (resid 169 through 233 )DD169 - 2331 - 65
77chain 'F' and (resid 170 through 235 )FE170 - 2351 - 66
88chain 'C' and (resid 2 through 31 )CF2 - 311 - 30
99chain 'C' and (resid 32 through 47 )CF32 - 4731 - 46
1010chain 'C' and (resid 48 through 61 )CF48 - 6147 - 60
1111chain 'C' and (resid 62 through 69 )CF62 - 6961 - 67
1212chain 'C' and (resid 70 through 83 )CF70 - 8368 - 81
1313chain 'C' and (resid 84 through 100 )CF84 - 10082 - 98
1414chain 'C' and (resid 101 through 107 )CF101 - 10799 - 103
1515chain 'C' and (resid 108 through 121 )CF108 - 121104 - 117
1616chain 'B' and (resid 2 through 47 )BG2 - 471 - 46
1717chain 'B' and (resid 48 through 120 )BG48 - 12047 - 119

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