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- PDB-9egv: HOIL-1 RING2 domain bound to ubiquitin -

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Basic information

Entry
Database: PDB / ID: 9egv
TitleHOIL-1 RING2 domain bound to ubiquitin
Components
  • Polyubiquitin-C
  • RanBP-type and C3HC4-type zinc finger-containing protein 1
KeywordsLIGASE / RBR E3 ubiquitin ligase / enzyme-substrate complex / RING2 domain
Function / homology
Function and homology information


protein linear polyubiquitination / LUBAC complex / RBR-type E3 ubiquitin transferase / ubiquitin ligase activator activity / negative regulation of necroptotic process / positive regulation of extrinsic apoptotic signaling pathway / TNFR1-induced proapoptotic signaling / negative regulation of NF-kappaB transcription factor activity / Maturation of protein E / Maturation of protein E ...protein linear polyubiquitination / LUBAC complex / RBR-type E3 ubiquitin transferase / ubiquitin ligase activator activity / negative regulation of necroptotic process / positive regulation of extrinsic apoptotic signaling pathway / TNFR1-induced proapoptotic signaling / negative regulation of NF-kappaB transcription factor activity / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / APC-Cdc20 mediated degradation of Nek2A / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / Regulation of innate immune responses to cytosolic DNA / NF-kB is activated and signals survival / protein sequestering activity / Downregulation of ERBB2:ERBB3 signaling / Pexophagy / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation / Activated NOTCH1 Transmits Signal to the Nucleus / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Translesion synthesis by POLK / InlB-mediated entry of Listeria monocytogenes into host cell / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / ubiquitin binding / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Regulation of activated PAK-2p34 by proteasome mediated degradation / Translesion synthesis by POLI / IKK complex recruitment mediated by RIP1 / Gap-filling DNA repair synthesis and ligation in GG-NER / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / TCF dependent signaling in response to WNT / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Regulation of NF-kappa B signaling / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / activated TAK1 mediates p38 MAPK activation / Negative regulators of DDX58/IFIH1 signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / Regulation of signaling by CBL / NOTCH3 Activation and Transmission of Signal to the Nucleus / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Degradation of DVL / Deactivation of the beta-catenin transactivating complex / Negative regulation of FGFR3 signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / Fanconi Anemia Pathway / Peroxisomal protein import / Degradation of AXIN / Regulation of TNFR1 signaling / Negative regulation of FGFR2 signaling / Stabilization of p53 / Hh mutants are degraded by ERAD / Negative regulation of FGFR4 signaling / Activation of NF-kappaB in B cells / Downregulation of SMAD2/3:SMAD4 transcriptional activity
Similarity search - Function
: / : / : / : / Zinc finger, RING-type, eukaryotic / RING-type zinc-finger / TRIAD supradomain / TRIAD supradomain profile. / Zinc finger domain / Zinc finger RanBP2 type profile. ...: / : / : / : / Zinc finger, RING-type, eukaryotic / RING-type zinc-finger / TRIAD supradomain / TRIAD supradomain profile. / Zinc finger domain / Zinc finger RanBP2 type profile. / Zinc finger, RanBP2-type superfamily / Zinc finger RanBP2-type signature. / Zinc finger, RanBP2-type / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Zinc finger, RING/FYVE/PHD-type / Ubiquitin-like domain superfamily
Similarity search - Domain/homology
Polyubiquitin-C / RanBP-type and C3HC4-type zinc finger-containing protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsWang, X.S. / Lechtenberg, B.C.
Funding support Australia, 2items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)GNT2016268 Australia
National Health and Medical Research Council (NHMRC, Australia)GNT1182757 Australia
Citation
Journal: Life Sci Alliance / Year: 2025
Title: The RBR E3 ubiquitin ligase HOIL-1 can ubiquitinate diverse non-protein substrates in vitro.
Authors: Wang, X.S. / Jiou, J. / Cerra, A. / Cobbold, S.A. / Jochem, M. / Mak, K.H.T. / Corcilius, L. / Silke, J. / Payne, R.J. / Goddard-Borger, E.D. / Komander, D. / Lechtenberg, B.C.
#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
DepositionNov 21, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 11, 2024Provider: repository / Type: Initial release
Revision 2.0Apr 2, 2025Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Polymer sequence / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / entity / entity_poly / entity_poly_seq / entity_src_gen / pdbx_contact_author / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_refine_tls / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_struct_special_symmetry / pdbx_unobs_or_zero_occ_residues / pdbx_validate_close_contact / pdbx_validate_torsion / refine / refine_hist / refine_ls_restr / refine_ls_restr_ncs / refine_ls_shell / struct_conf / struct_conn / struct_ncs_dom_lim / struct_ncs_oper / struct_ref / struct_ref_seq / struct_ref_seq_dif / struct_sheet_range
Item: _entity.formula_weight / _entity_poly.pdbx_seq_one_letter_code ..._entity.formula_weight / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_src_gen.pdbx_end_seq_num / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_refine_tls.L[1][1] / _pdbx_refine_tls.L[1][2] / _pdbx_refine_tls.L[1][3] / _pdbx_refine_tls.L[2][2] / _pdbx_refine_tls.L[2][3] / _pdbx_refine_tls.L[3][3] / _pdbx_refine_tls.S[1][1] / _pdbx_refine_tls.S[1][2] / _pdbx_refine_tls.S[1][3] / _pdbx_refine_tls.S[2][1] / _pdbx_refine_tls.S[2][2] / _pdbx_refine_tls.S[2][3] / _pdbx_refine_tls.S[3][1] / _pdbx_refine_tls.S[3][2] / _pdbx_refine_tls.S[3][3] / _pdbx_refine_tls.T[1][1] / _pdbx_refine_tls.T[1][2] / _pdbx_refine_tls.T[1][3] / _pdbx_refine_tls.T[2][2] / _pdbx_refine_tls.T[2][3] / _pdbx_refine_tls.T[3][3] / _pdbx_refine_tls.origin_x / _pdbx_refine_tls.origin_y / _pdbx_refine_tls.origin_z / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _pdbx_struct_special_symmetry.auth_seq_id / _pdbx_validate_torsion.phi / _pdbx_validate_torsion.psi / _refine.B_iso_mean / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.overall_SU_ML / _refine.pdbx_overall_phase_error / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_protein / _refine_ls_restr.dev_ideal / _refine_ls_restr.number / _refine_ls_restr_ncs.rms_dev_position / _refine_ls_shell.R_factor_R_free / _refine_ls_shell.R_factor_R_work / _struct_conf.beg_auth_comp_id / _struct_conf.beg_label_comp_id / _struct_conf.beg_label_seq_id / _struct_conf.end_label_seq_id / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_label_seq_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_ncs_oper.matrix[1][1] / _struct_ncs_oper.matrix[1][2] / _struct_ncs_oper.matrix[1][3] / _struct_ncs_oper.matrix[2][1] / _struct_ncs_oper.matrix[2][2] / _struct_ncs_oper.matrix[2][3] / _struct_ncs_oper.matrix[3][1] / _struct_ncs_oper.matrix[3][2] / _struct_ncs_oper.matrix[3][3] / _struct_ncs_oper.vector[1] / _struct_ncs_oper.vector[2] / _struct_ncs_oper.vector[3] / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.db_align_beg / _struct_ref_seq.pdbx_auth_seq_align_beg / _struct_ref_seq.seq_align_end / _struct_ref_seq_dif.pdbx_auth_seq_num / _struct_ref_seq_dif.seq_num / _struct_sheet_range.beg_label_seq_id / _struct_sheet_range.end_label_seq_id
Description: Sequence discrepancy
Details: Incorrect construct boundaries for HOIL-1 in chains A and B are corrected in the revised entry.
Provider: author / Type: Coordinate replacement
Revision 2.1Apr 16, 2025Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_id_ISSN ..._citation.journal_abbrev / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: RanBP-type and C3HC4-type zinc finger-containing protein 1
B: RanBP-type and C3HC4-type zinc finger-containing protein 1
C: Polyubiquitin-C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,79913
Polymers29,0823
Non-polymers71610
Water1,856103
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3400 Å2
ΔGint-85 kcal/mol
Surface area13500 Å2
2


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2420 Å2
ΔGint-40 kcal/mol
Surface area8500 Å2
MethodPISA
Unit cell
Length a, b, c (Å)95.922, 95.922, 187.429
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number98
Space group name H-MI4122
Space group name HallI4bw2bw
Symmetry operation#1: x,y,z
#2: -y+1/2,x,z+3/4
#3: y+1/2,-x,z+3/4
#4: x+1/2,-y,-z+3/4
#5: -x+1/2,y,-z+3/4
#6: -x,-y,z
#7: y,x,-z
#8: -y,-x,-z
#9: x+1/2,y+1/2,z+1/2
#10: -y+1,x+1/2,z+5/4
#11: y+1,-x+1/2,z+5/4
#12: x+1,-y+1/2,-z+5/4
#13: -x+1,y+1/2,-z+5/4
#14: -x+1/2,-y+1/2,z+1/2
#15: y+1/2,x+1/2,-z+1/2
#16: -y+1/2,-x+1/2,-z+1/2
Components on special symmetry positions
IDModelComponents
11A-754-

HOH

21A-755-

HOH

31B-720-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1(chain "A" and (resid 431 through 510 or resid 511 through 513))
d_2ens_1(chain "B" and (resid 431 through 510 or resid 511 through 513))

NCS domain segments:

Ens-ID: ens_1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_11THRTHRHISHISAA431 - 5109 - 88
d_12ZNZNZNZNAD601
d_13ZNZNZNZNAE602
d_21THRTHRHISHISBB431 - 5109 - 88
d_22ZNZNZNZNBH601
d_23ZNZNZNZNBI602

NCS oper: (Code: givenMatrix: (0.371637285785, 0.919937541718, -0.124902550619), (-0.834588506649, 0.389983010912, 0.389069756945), (0.406629748522, -0.0403505952539, 0.912701526831)Vector: -26. ...NCS oper: (Code: given
Matrix: (0.371637285785, 0.919937541718, -0.124902550619), (-0.834588506649, 0.389983010912, 0.389069756945), (0.406629748522, -0.0403505952539, 0.912701526831)
Vector: -26.7571787574, 57.7020103452, 19.4810904767)

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Components

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Protein , 2 types, 3 molecules ABC

#1: Protein RanBP-type and C3HC4-type zinc finger-containing protein 1 / HBV-associated factor 4 / Heme-oxidized IRP2 ubiquitin ligase 1 / HOIL-1 / Hepatitis B virus X- ...HBV-associated factor 4 / Heme-oxidized IRP2 ubiquitin ligase 1 / HOIL-1 / Hepatitis B virus X-associated protein 4 / RING finger protein 54 / RING-type E3 ubiquitin transferase HOIL-1 / Ubiquitin-conjugating enzyme 7-interacting protein 3


Mass: 9594.109 Da / Num. of mol.: 2 / Mutation: C460A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RBCK1, C20orf18, RNF54, UBCE7IP3, XAP3, XAP4 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9BYM8, RBR-type E3 ubiquitin transferase
#2: Protein Polyubiquitin-C


Mass: 9894.270 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: N-terminal 6xHis-tag / Source: (gene. exp.) Homo sapiens (human) / Gene: UBC / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG48

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Non-polymers , 4 types, 113 molecules

#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#5: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 103 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 3.35 Å3/Da / Density % sol: 63.25 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.2
Details: 0.01 M magnesium chloride hexahydrate, 0.05 M MES monohydrate pH 6.2, 1.8 M lithium sulfate monohydrate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Aug 5, 2022
RadiationMonochromator: silicon-based Double Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 2→47.96 Å / Num. obs: 29960 / % possible obs: 99.7 % / Redundancy: 13.3 % / Biso Wilson estimate: 32.61 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.225 / Rpim(I) all: 0.064 / Rrim(I) all: 0.234 / Χ2: 0.52 / Net I/σ(I): 8.6 / Num. measured all: 398102
Reflection shellResolution: 2→2.05 Å / % possible obs: 96.6 % / Redundancy: 12 % / Rmerge(I) obs: 2.644 / Num. measured all: 25259 / Num. unique obs: 2098 / CC1/2: 0.421 / Rpim(I) all: 0.783 / Rrim(I) all: 2.76 / Χ2: 0.42 / Net I/σ(I) obs: 0.8

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Processing

Software
NameVersionClassification
PHENIX1.21.1_5286refinement
Aimless0.7.8data scaling
XDSNov 1, 2016 BUILT=20161205data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→47.96 Å / SU ML: 0.2069 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 18.923
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.208 1571 5.26 %
Rwork0.1785 28309 -
obs0.18 29880 99.9 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 54.98 Å2
Refinement stepCycle: LAST / Resolution: 2→47.96 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1864 0 22 103 1989
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01231911
X-RAY DIFFRACTIONf_angle_d1.06282584
X-RAY DIFFRACTIONf_chiral_restr0.0655281
X-RAY DIFFRACTIONf_plane_restr0.0088338
X-RAY DIFFRACTIONf_dihedral_angle_d13.3809728
Refine LS restraints NCSType: Torsion NCS / Rms dev position: 2.11206316691 Å
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.070.2941400.28272489X-RAY DIFFRACTION99.1
2.07-2.140.27061440.25952523X-RAY DIFFRACTION100
2.14-2.220.26781460.23452542X-RAY DIFFRACTION100
2.22-2.330.24841310.20022524X-RAY DIFFRACTION99.96
2.33-2.450.19911490.18642555X-RAY DIFFRACTION100
2.45-2.60.19741520.17962543X-RAY DIFFRACTION99.96
2.6-2.80.23031300.17972571X-RAY DIFFRACTION99.93
2.8-3.080.22591420.18692584X-RAY DIFFRACTION100
3.08-3.530.19421390.18292589X-RAY DIFFRACTION100
3.53-4.450.1611580.1422622X-RAY DIFFRACTION100
4.45-47.960.21031400.16062767X-RAY DIFFRACTION99.93
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)
10.385212137064-0.145577984484-0.2937624476890.04662022245790.1123701180270.244816901436-0.3159207891440.195779764941.02480526402-0.257961650528-0.00495397715268-0.406774986951-1.135123288640.51387326819-0.03836230635870.730622348056-0.243092738041-0.06485499253880.483828952140.09140530591550.7063059604818.377703903467.5408414279-63.8767261233
21.232305130460.6683131612260.7558562657061.1033110870.142667328360.750576221031-0.1534054483930.22889438088-0.107561233973-0.277090869770.0697877248135-0.3472275691770.2813923934280.418394612837-0.0005910378791170.405223794531-0.05083688888040.04020231050770.389723434328-0.006496069820230.37185273839514.877631904751.4729584748-63.0310248577
30.8913762648080.72158404051-0.608953827631.626470022290.150461835881.623599488210.073387762355-0.1252842214340.071611953833-0.00870171386742-0.0637584021254-0.1064485283570.1437214938550.207599939898-2.52335673611E-50.344162649753-0.005386224551980.01716441345890.245397956468-0.008764107783360.296702821376.576022051342.0721189922-62.3145407184
40.00908545626081-0.00875334515302-0.003101447420540.4842595275950.2605024355130.1518071629080.2987729350360.5440117756020.3538069602680.2955355550680.728852253294-0.7694276737350.9746660939381.533467106760.00864153238491.01084852295-0.06067368821030.2051341934771.63049347222-0.001284174986881.1145445465246.133282890241.7852524014-35.8268987005
50.6952200314060.2252387490660.6111720867351.02354677493-0.1821293994170.7074453971980.01004904989851.26946943463-0.0117425263613-0.418209171111-0.144094868573-0.0415579917330.1981940343270.227971869116-0.01106783887510.3037239373420.0212455971121-0.02250987256790.751953511822-0.004735542948230.41495635842835.472776796545.6095107883-32.6661231999
61.86476406994-1.847148350382.609549901231.84428896344-2.577033689373.640719376450.7255660615750.491610747438-1.9267112206-0.669803044573-0.06843614398210.2154889926651.480364030880.2357401909970.04061187598440.546145936180.0413673475695-0.08397045326350.701869494882-0.189839957780.58573549715832.653806318136.8970126335-37.43241854
71.84275671999-0.5488362507630.8244568460740.8581118185-0.2448548458981.609444740160.09617135451590.0276756705324-0.154979155295-0.08605069044470.0464155488183-0.07569280824880.253855665880.25171736199-3.50203110521E-50.25768802196-0.0220938089649-0.02787989538150.4116428239620.001952940539110.30397877989221.982465993944.3127178532-36.4249198722
80.06223163011730.124058750362-0.08904739996390.632429141903-0.3180566638980.262625239037-0.300607973847-0.7328427990850.4732289135070.279101083846-0.0172733563814-0.750321741449-0.778157194821.07268228688-0.1366832868860.84556261962-0.427520771312-0.09591908827521.22431191857-0.07265592922670.96555215777330.487904163661.6986688415-51.5436521583
90.02792597941190.0532356953644-0.003309794429760.3549388171930.07053562350110.08258307987020.00647261564258-0.230126919435-0.5637007428660.294756031844-0.182387194415-1.1903984761-0.09163691016731.46645749842-0.07365271673620.44392001966-0.182751285433-0.0532653127131.049502911290.1167291572660.84078300194830.88830289152.6395578809-56.8817392843
100.08765882333430.168161114182-0.2871673241491.081374185870.2394502794221.86400387792-0.1781290856950.211539283011-0.0554091951339-0.336516909118-0.11132586382-1.360120579340.1604594067070.6974073742470.09030511402540.568843846799-0.6042650676010.1615853921451.165790912060.3295575792351.0497808963933.400687578363.2049091491-64.7670791912
111.38343736031-0.588206414472-0.083157838241.02785027937-0.7549799383140.729526050697-0.1081359025940.1487974454870.155217232037-0.4287702457980.0458063288481-0.410930370872-0.5121163496251.2699571332-0.01213945822670.591396378316-0.268470015219-0.0483284533380.7978333564510.04778223033360.56526206030826.656033104359.1046384357-59.1228671987
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'A' and (resid 424 through 440 )AA424 - 4401 - 17
22chain 'A' and (resid 441 through 461 )AA441 - 46118 - 38
33chain 'A' and (resid 462 through 510 )AA462 - 51039 - 87
44chain 'B' and (resid 431 through 440 )BG431 - 4401 - 10
55chain 'B' and (resid 441 through 452 )BG441 - 45211 - 22
66chain 'B' and (resid 453 through 461 )BG453 - 46123 - 31
77chain 'B' and (resid 462 through 510 )BG462 - 51032 - 80
88chain 'C' and (resid 1 through 22 )CN1 - 221 - 22
99chain 'C' and (resid 23 through 44 )CN23 - 4423 - 44
1010chain 'C' and (resid 45 through 59 )CN45 - 5945 - 59
1111chain 'C' and (resid 60 through 76 )CN60 - 7660 - 76

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