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- PDB-5y5s: Structure of photosynthetic LH1-RC super-complex at 1.9 angstrom ... -

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Basic information

Entry
Database: PDB / ID: 5y5s
TitleStructure of photosynthetic LH1-RC super-complex at 1.9 angstrom resolution
Components
  • (Photosynthetic reaction center ...) x 4
  • LH1 alpha polypeptide
  • LH1 beta polypeptide
KeywordsPHOTOSYNTHESIS / LH1-RC / purple bacteria
Function / homology
Function and homology information


organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / : / photosynthesis / endomembrane system / electron transfer activity ...organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / : / photosynthesis / endomembrane system / electron transfer activity / iron ion binding / heme binding / metal ion binding / membrane / plasma membrane
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #250 / Light-harvesting complex / Light-harvesting Protein / Photosynthetic Reaction Center, subunit C; domain 2 / Photosynthetic Reaction Center, subunit C, domain 2 / Photosynthetic reaction centre, cytochrome c subunit / Multihaem cytochrome, PRC subunit superfamily / Photosynthetic reaction centre cytochrome C subunit / Antenna complex, alpha subunit / Antenna complex, alpha subunit conserved site ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #250 / Light-harvesting complex / Light-harvesting Protein / Photosynthetic Reaction Center, subunit C; domain 2 / Photosynthetic Reaction Center, subunit C, domain 2 / Photosynthetic reaction centre, cytochrome c subunit / Multihaem cytochrome, PRC subunit superfamily / Photosynthetic reaction centre cytochrome C subunit / Antenna complex, alpha subunit / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Photosynthetic Reaction Center; Chain H, domain 1 / Photosynthetic reaction centre, H subunit, N-terminal domain / Antenna complex, alpha/beta subunit / Light-harvesting protein B beta chain / Antenna complex, beta domain superfamily / Antenna complex alpha/beta subunit / Light-harvesting complex / Photosynthetic Reaction Center; Chain H, domain 2 / Photosynthetic Reaction Center, subunit H, domain 2 / Photosynthetic Reaction Center, subunit M; domain 1 / Photosystem II protein D1-like / Multiheme cytochrome c family profile. / Photosynthetic reaction centre, H subunit / Bacterial photosynthetic reaction centre, H-chain, C-terminal / Photosynthetic reaction centre, M subunit / Photosynthetic reaction centre, H subunit, N-terminal / PRC-barrel domain / Photosynthetic reaction centre, H subunit, N-terminal domain superfamily / Photosynthetic reaction centre, H-chain N-terminal region / PRC-barrel domain / Photosynthetic reaction centre, L subunit / PRC-barrel-like superfamily / Multiheme cytochrome superfamily / : / Photosynthetic reaction centre, L/M / Photosystem II protein D1/D2 superfamily / Photosynthetic reaction centre protein / Photosynthetic reaction center proteins signature. / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Few Secondary Structures / Irregular / Alpha-Beta Complex / Up-down Bundle / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
BACTERIOCHLOROPHYLL A / BACTERIOPHEOPHYTIN A / CARDIOLIPIN / SPIRILLOXANTHIN / : / HEME C / 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / MENAQUINONE 8 / DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE / Chem-PGV ...BACTERIOCHLOROPHYLL A / BACTERIOPHEOPHYTIN A / CARDIOLIPIN / SPIRILLOXANTHIN / : / HEME C / 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / MENAQUINONE 8 / DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE / Chem-PGV / Unknown ligand / Ubiquinone-8 / Reaction center protein M chain / LH1 beta polypeptide / LH1 alpha polypeptide / Reaction center protein L chain / Photosynthetic reaction center cytochrome c subunit / Photosynthetic reaction center H subunit
Similarity search - Component
Biological speciesThermochromatium tepidum (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.9 Å
AuthorsYu, L.-J. / Suga, M. / Wang-Otomo, Z.-Y. / Shen, J.-R.
CitationJournal: Nature / Year: 2018
Title: Structure of photosynthetic LH1-RC supercomplex at 1.9 angstrom resolution.
Authors: Yu, L.-J. / Suga, M. / Wang-Otomo, Z.-Y. / Shen, J.R.
History
DepositionAug 9, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 11, 2018Provider: repository / Type: Initial release
Revision 1.1Apr 25, 2018Group: Data collection / Database references / Structure summary
Category: audit_author / citation / citation_author
Item: _audit_author.name / _citation.country ..._audit_author.name / _citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _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
Revision 2.0Oct 2, 2019Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_conn_angle / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.name / _chem_comp.pdbx_synonyms / _entity.formula_weight / _entity.pdbx_description / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.name / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.pdb_mon_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_label_comp_id / _struct_site.details / _struct_site.pdbx_auth_comp_id / _struct_site_gen.auth_comp_id / _struct_site_gen.label_comp_id
Revision 2.1Nov 22, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _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_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_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_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.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
C: Photosynthetic reaction center cytochrome c subunit
L: Photosynthetic reaction center L subunit
M: Photosynthetic reaction center M subunit
H: Photosynthetic reaction center H subunit
A: LH1 alpha polypeptide
B: LH1 beta polypeptide
D: LH1 alpha polypeptide
E: LH1 beta polypeptide
F: LH1 alpha polypeptide
G: LH1 beta polypeptide
I: LH1 alpha polypeptide
J: LH1 beta polypeptide
K: LH1 alpha polypeptide
N: LH1 beta polypeptide
O: LH1 alpha polypeptide
P: LH1 beta polypeptide
Q: LH1 alpha polypeptide
R: LH1 beta polypeptide
S: LH1 alpha polypeptide
T: LH1 beta polypeptide
U: LH1 alpha polypeptide
V: LH1 beta polypeptide
W: LH1 alpha polypeptide
X: LH1 beta polypeptide
Y: LH1 alpha polypeptide
Z: LH1 beta polypeptide
1: LH1 alpha polypeptide
2: LH1 beta polypeptide
3: LH1 alpha polypeptide
4: LH1 beta polypeptide
5: LH1 alpha polypeptide
6: LH1 beta polypeptide
7: LH1 alpha polypeptide
8: LH1 beta polypeptide
9: LH1 alpha polypeptide
0: LH1 beta polypeptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)425,934180
Polymers340,62036
Non-polymers85,314144
Water17,186954
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area97250 Å2
ΔGint-682 kcal/mol
Surface area131570 Å2
MethodPISA
Unit cell
Length a, b, c (Å)145.280, 143.810, 210.280
Angle α, β, γ (deg.)90.000, 90.740, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11C-806-

HOH

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Components

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Photosynthetic reaction center ... , 4 types, 4 molecules CLMH

#1: Protein Photosynthetic reaction center cytochrome c subunit


Mass: 43177.531 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: D2Z0P5
#2: Protein Photosynthetic reaction center L subunit


Mass: 31520.771 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: D2Z0P3
#3: Protein Photosynthetic reaction center M subunit


Mass: 36605.715 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: A8ASG6
#4: Protein Photosynthetic reaction center H subunit


Mass: 28213.305 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: D2Z0P9

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Protein / Protein/peptide / Sugars , 3 types, 34 molecules ADFIKOQSUWY13579BEGJNPRTVXZ246...

#23: Sugar ChemComp-LMT / DODECYL-BETA-D-MALTOSIDE


Type: D-saccharide / Mass: 510.615 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C24H46O11 / Comment: detergent*YM
#5: Protein
LH1 alpha polypeptide


Mass: 7034.442 Da / Num. of mol.: 16 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: D2Z0P2
#6: Protein/peptide
LH1 beta polypeptide


Mass: 5534.452 Da / Num. of mol.: 16 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: D2Z0P1

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Non-polymers , 18 types, 1096 molecules

#7: Chemical
ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#8: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#9: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#10: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#11: Chemical ChemComp-LHG / 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE


Mass: 722.970 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C38H75O10P / Comment: phospholipid*YM
#12: Chemical
ChemComp-PGV / (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE / PHOSPHATIDYLGLYCEROL / 2-VACCENOYL-1-PALMITOYL-SN-GLYCEROL-3-PHOSPHOGLYCEROL


Mass: 749.007 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C40H77O10P / Comment: phospholipid*YM
#13: Chemical...
ChemComp-BCL / BACTERIOCHLOROPHYLL A


Mass: 911.504 Da / Num. of mol.: 36 / Source method: obtained synthetically / Formula: C55H74MgN4O6
#14: Chemical ChemComp-BPH / BACTERIOPHEOPHYTIN A


Mass: 889.215 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C55H76N4O6
#15: Chemical
ChemComp-UQ8 / Ubiquinone-8 / 2,3-dimethoxy-5-methyl-6-[(6E,10E,14E,18E,22E,26E)-3,7,11,15,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-oc taen-1-yl]cyclohexa-2,5-diene-1,4-dione


Mass: 727.109 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C49H74O4
#16: Chemical
ChemComp-UNL / UNKNOWN LIGAND


Num. of mol.: 16 / Source method: obtained synthetically
#17: Chemical ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe
#18: Chemical ChemComp-MQ8 / MENAQUINONE 8 / 2-METHYL-3-(3,7,11,15,19,23,27,31-OCTAMETHYL-DOTRIACONTA-2,6,10,14,18,22,26,30-OCTAENYL)-[1,4]NAPTHOQUINONE


Mass: 717.116 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C51H72O2
#19: Chemical
ChemComp-CRT / SPIRILLOXANTHIN / RHODOVIOLASCIN


Mass: 596.925 Da / Num. of mol.: 17 / Source method: obtained synthetically / Formula: C42H60O2
#20: Chemical
ChemComp-PEF / DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE / 3-[AMINOETHYLPHOSPHORYL]-[1,2-DI-PALMITOYL]-SN-GLYCEROL


Mass: 691.959 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: C37H74NO8P / Comment: phospholipid*YM
#21: Chemical
ChemComp-LDA / LAURYL DIMETHYLAMINE-N-OXIDE


Mass: 229.402 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C14H31NO / Comment: LDAO, detergent*YM
#22: Chemical
ChemComp-CDL / CARDIOLIPIN / DIPHOSPHATIDYL GLYCEROL / BIS-(1,2-DIACYL-SN-GLYCERO-3-PHOSPHO)-1',3'-SN-GLYCEROL


Mass: 1464.043 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C81H156O17P2 / Comment: phospholipid*YM
#24: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: Ca
#25: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 954 / Source method: isolated from a natural source / Formula: H2O

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Details

Nonpolymer detailsUNL IN THIS STRUCTURE WAS TUBE-LIKE ELECTRON DENSITY, MIGHT BE A TAIL OF LIPID OR DETERGENT, WHICH ...UNL IN THIS STRUCTURE WAS TUBE-LIKE ELECTRON DENSITY, MIGHT BE A TAIL OF LIPID OR DETERGENT, WHICH COULD NOT BE ASSIGNED UNAMBIGUOUSLY.

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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: 3.22 Å3/Da / Density % sol: 61.85 %
Crystal growTemperature: 293 K / Method: batch mode / Details: PEG 1450, calcium chloride, octyl-phosphocholine

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jan 20, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.9→46.919 Å / Num. obs: 338604 / % possible obs: 99.95 % / Redundancy: 9.2 % / Biso Wilson estimate: 39.96 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.1035 / Rpim(I) all: 0.035 / Net I/σ(I): 9.47
Reflection shellResolution: 1.9→1.968 Å / Redundancy: 8 % / Mean I/σ(I) obs: 1.14 / Num. unique obs: 33819 / CC1/2: 0.557 / Rpim(I) all: 0.6936 / % possible all: 99.98

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIX1.12rc0_2787refinement
PHASERphasing
PDB_EXTRACT3.22data extraction
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3WMM

3wmm


Resolution: 1.9→46.919 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 25.55 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2152 16919 5 %
Rwork0.1814 321617 -
obs0.1831 338536 99.95 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 165.53 Å2 / Biso mean: 65.4864 Å2 / Biso min: 26.36 Å2
Refinement stepCycle: final / Resolution: 1.9→46.919 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms21946 0 5022 956 27924
Biso mean--73.62 63.32 -
Num. residues----2726
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00827998
X-RAY DIFFRACTIONf_angle_d1.2738395
X-RAY DIFFRACTIONf_chiral_restr0.0713924
X-RAY DIFFRACTIONf_plane_restr0.0054431
X-RAY DIFFRACTIONf_dihedral_angle_d18.73715970
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
1.9-1.92160.40375490.38491072911278
1.9216-1.94420.37565700.35811066511235
1.9442-1.96790.34615660.32831073311299
1.9679-1.99280.36325580.31421065911217
1.9928-2.0190.30865620.29271066211224
2.019-2.04670.30055650.27231076211327
2.0467-2.07590.30475520.26931065711209
2.0759-2.10690.30015620.24661067711239
2.1069-2.13990.26925720.23661069711269
2.1399-2.17490.25035630.21581073411297
2.1749-2.21240.23845590.20781069311252
2.2124-2.25270.26485600.20941067411234
2.2527-2.2960.22385650.19181066411229
2.296-2.34290.2245640.18641073511299
2.3429-2.39380.24145660.18321070511271
2.3938-2.44950.22785590.1781068811247
2.4495-2.51070.2325670.17871071011277
2.5107-2.57860.22925610.18051072511286
2.5786-2.65450.20845720.17071069311265
2.6545-2.74020.20995570.16631074711304
2.7402-2.83810.19495680.16021075411322
2.8381-2.95170.20995630.1691068811251
2.9517-3.0860.21845630.17781072011283
3.086-3.24870.21255700.17561069011260
3.2487-3.45210.20985640.17041073911303
3.4521-3.71860.20535610.16751075511316
3.7186-4.09260.19215700.16091079911369
4.0926-4.68440.17885690.15891075511324
4.6844-5.90.2015640.16321076611330
5.9-46.93320.20335780.18081094211520
Refinement TLS params.Method: refined / Origin x: -40.6459 Å / Origin y: 30.5496 Å / Origin z: 52.8476 Å
111213212223313233
T0.2544 Å20.086 Å20.0025 Å2-0.3241 Å2-0.0069 Å2--0.4676 Å2
L0.874 °2-0.0868 °20.1728 °2-0.747 °20.0641 °2--0.3734 °2
S-0.0554 Å °0.0492 Å °0.1014 Å °-0.0045 Å °-0.0053 Å °0.1554 Å °-0.0716 Å °0.0029 Å °0.0388 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1allC23 - 505
2X-RAY DIFFRACTION1allL2 - 304
3X-RAY DIFFRACTION1allM2 - 406
4X-RAY DIFFRACTION1allH5 - 259
5X-RAY DIFFRACTION1allA6 - 203
6X-RAY DIFFRACTION1allB5 - 101
7X-RAY DIFFRACTION1allD5 - 203
8X-RAY DIFFRACTION1allE9 - 101
9X-RAY DIFFRACTION1allF5 - 203
10X-RAY DIFFRACTION1allG5 - 101
11X-RAY DIFFRACTION1allI3 - 203
12X-RAY DIFFRACTION1allJ5 - 101
13X-RAY DIFFRACTION1allK3 - 203
14X-RAY DIFFRACTION1allN5 - 101
15X-RAY DIFFRACTION1allO4 - 203
16X-RAY DIFFRACTION1allP5 - 101
17X-RAY DIFFRACTION1allQ3 - 203
18X-RAY DIFFRACTION1allR6 - 101
19X-RAY DIFFRACTION1allS3 - 203
20X-RAY DIFFRACTION1allT4 - 101
21X-RAY DIFFRACTION1allU3 - 203
22X-RAY DIFFRACTION1allV5 - 101
23X-RAY DIFFRACTION1allW5 - 203
24X-RAY DIFFRACTION1allX6 - 101
25X-RAY DIFFRACTION1allY3 - 203
26X-RAY DIFFRACTION1allZ7 - 101
27X-RAY DIFFRACTION1all14 - 203
28X-RAY DIFFRACTION1all26 - 101
29X-RAY DIFFRACTION1all34 - 203
30X-RAY DIFFRACTION1all45 - 101
31X-RAY DIFFRACTION1all56 - 203
32X-RAY DIFFRACTION1all65 - 101
33X-RAY DIFFRACTION1all73 - 203
34X-RAY DIFFRACTION1all86 - 101
35X-RAY DIFFRACTION1all93 - 203
36X-RAY DIFFRACTION1all04 - 101
37X-RAY DIFFRACTION1alla1 - 304
38X-RAY DIFFRACTION1allb1 - 906

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