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- PDB-6h0g: Structure of the DDB1-CRBN-pomalidomide complex bound to ZNF692(ZF4) -

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Basic information

Entry
Database: PDB / ID: 6h0g
TitleStructure of the DDB1-CRBN-pomalidomide complex bound to ZNF692(ZF4)
Components
  • DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1,DDB1 (DNA damage binding protein 1),DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1
  • Protein cereblon
  • Zinc finger protein 692
KeywordsSIGNALING PROTEIN / E3 ubiquitin ligase / drug mediated protein-interaction / targeted protein degradation
Function / homology
Function and homology information


negative regulation of monoatomic ion transmembrane transport / positive regulation by virus of viral protein levels in host cell / epigenetic programming in the zygotic pronuclei / spindle assembly involved in female meiosis / Generic Transcription Pathway / Cul4-RING E3 ubiquitin ligase complex / UV-damage excision repair / biological process involved in interaction with symbiont / regulation of mitotic cell cycle phase transition / WD40-repeat domain binding ...negative regulation of monoatomic ion transmembrane transport / positive regulation by virus of viral protein levels in host cell / epigenetic programming in the zygotic pronuclei / spindle assembly involved in female meiosis / Generic Transcription Pathway / Cul4-RING E3 ubiquitin ligase complex / UV-damage excision repair / biological process involved in interaction with symbiont / regulation of mitotic cell cycle phase transition / WD40-repeat domain binding / Cul4A-RING E3 ubiquitin ligase complex / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / regulation of gluconeogenesis / locomotory exploration behavior / negative regulation of reproductive process / negative regulation of developmental process / cullin family protein binding / positive regulation of Wnt signaling pathway / viral release from host cell / ectopic germ cell programmed cell death / positive regulation of viral genome replication / negative regulation of protein-containing complex assembly / positive regulation of gluconeogenesis / proteasomal protein catabolic process / Recognition of DNA damage by PCNA-containing replication complex / nucleotide-excision repair / positive regulation of protein-containing complex assembly / DNA Damage Recognition in GG-NER / Dual Incision in GG-NER / regulation of circadian rhythm / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / Wnt signaling pathway / Formation of Incision Complex in GG-NER / DNA-binding transcription repressor activity, RNA polymerase II-specific / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / positive regulation of protein catabolic process / cellular response to UV / rhythmic process / protein-macromolecule adaptor activity / site of double-strand break / Neddylation / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / Potential therapeutics for SARS / transmembrane transporter binding / damaged DNA binding / chromosome, telomeric region / protein ubiquitination / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / DNA repair / apoptotic process / DNA damage response / protein-containing complex binding / nucleolus / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / extracellular space / extracellular exosome / nucleoplasm / membrane / metal ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Yippee/Mis18/Cereblon / Yippee zinc-binding/DNA-binding /Mis18, centromere assembly / CULT domain / CULT domain profile. / Lon protease, N-terminal domain superfamily / Lon N-terminal domain profile. / Lon protease, N-terminal domain / ATP-dependent protease La (LON) substrate-binding domain / Found in ATP-dependent protease La (LON) / Cleavage/polyadenylation specificity factor, A subunit, N-terminal ...Yippee/Mis18/Cereblon / Yippee zinc-binding/DNA-binding /Mis18, centromere assembly / CULT domain / CULT domain profile. / Lon protease, N-terminal domain superfamily / Lon N-terminal domain profile. / Lon protease, N-terminal domain / ATP-dependent protease La (LON) substrate-binding domain / Found in ATP-dependent protease La (LON) / Cleavage/polyadenylation specificity factor, A subunit, N-terminal / Mono-functional DNA-alkylating methyl methanesulfonate N-term / Cleavage/polyadenylation specificity factor, A subunit, C-terminal / CPSF A subunit region / PUA-like superfamily / Zinc finger, C2H2 type / zinc finger / Zinc finger C2H2 type domain profile. / Zinc finger C2H2 superfamily / Zinc finger C2H2 type domain signature. / Zinc finger C2H2-type / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
S-Pomalidomide / DNA damage-binding protein 1 / Protein cereblon / Zinc finger protein 692
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.25 Å
AuthorsBunker, R.D. / Petzold, G. / Thoma, N.H.
Funding support3items
OrganizationGrant numberCountry
European UnionHorizon 2020 No. 666068
European Molecular Biology OrganizationAdvanced Fellowship aALTF 761-2016
European UnionHuman Frontier Science Program Long-Term Fellowship LT000210/2014
CitationJournal: Science / Year: 2018
Title: Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN.
Authors: Sievers, Q.L. / Petzold, G. / Bunker, R.D. / Renneville, A. / Slabicki, M. / Liddicoat, B.J. / Abdulrahman, W. / Mikkelsen, T. / Ebert, B.L. / Thoma, N.H.
History
DepositionJul 9, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 7, 2018Provider: repository / Type: Initial release
Revision 1.1Nov 14, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.pdbx_database_id_PubMed ..._citation.journal_volume / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 2.0Apr 17, 2019Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Polymer sequence / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / entity / entity_name_com / entity_poly / entity_poly_seq / entity_src_gen / pdbx_poly_seq_scheme / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_unobs_or_zero_occ_residues / struct_conf / struct_conn / struct_mon_prot_cis / struct_ref / struct_ref_seq / struct_ref_seq_dif / struct_sheet_range / struct_site_gen
Item: _atom_site.label_seq_id / _atom_site_anisotrop.pdbx_label_seq_id ..._atom_site.label_seq_id / _atom_site_anisotrop.pdbx_label_seq_id / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_mutation / _entity_name_com.name / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_src_gen.pdbx_end_seq_num / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _struct_conf.beg_label_seq_id / _struct_conf.end_label_seq_id / _struct_conn.ptnr1_label_seq_id / _struct_mon_prot_cis.label_seq_id / _struct_mon_prot_cis.pdbx_label_seq_id_2 / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_db_isoform / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.db_align_beg / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_auth_seq_align_beg / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq.seq_align_beg / _struct_ref_seq.seq_align_end / _struct_sheet_range.beg_label_seq_id / _struct_sheet_range.end_label_seq_id / _struct_site_gen.label_seq_id
Revision 2.1Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1,DDB1 (DNA damage binding protein 1),DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1
B: Protein cereblon
C: Zinc finger protein 692
D: DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1,DDB1 (DNA damage binding protein 1),DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1
E: Protein cereblon
F: Zinc finger protein 692
hetero molecules


Theoretical massNumber of molelcules
Total (without water)297,34812
Polymers296,5406
Non-polymers8086
Water0
1
A: DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1,DDB1 (DNA damage binding protein 1),DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1
B: Protein cereblon
C: Zinc finger protein 692
hetero molecules


Theoretical massNumber of molelcules
Total (without water)148,6746
Polymers148,2703
Non-polymers4043
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1,DDB1 (DNA damage binding protein 1),DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1
E: Protein cereblon
F: Zinc finger protein 692
hetero molecules


Theoretical massNumber of molelcules
Total (without water)148,6746
Polymers148,2703
Non-polymers4043
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)112.510, 99.530, 166.940
Angle α, β, γ (deg.)90.000, 108.490, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1,DDB1 (DNA damage binding protein 1),DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1 / DDB p127 subunit / DNA damage-binding protein a / DDBa / Damage-specific DNA-binding protein 1 / ...DDB p127 subunit / DNA damage-binding protein a / DDBa / Damage-specific DNA-binding protein 1 / HBV X-associated protein 1 / XAP-1 / UV-damaged DNA-binding factor / UV-damaged DNA-binding protein 1 / UV-DDB 1 / XPE-binding factor / XPE-BF / Xeroderma pigmentosum group E-complementing protein / XPCe


Mass: 95773.695 Da / Num. of mol.: 2
Mutation: Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 ...Mutation: Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG),Central WD40 propeller domain (516-725 aa) replaced with a linker (sequence GNGNSG)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: DDB1, XAP1 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q16531
#2: Protein Protein cereblon


Mass: 48976.117 Da / Num. of mol.: 2 / Mutation: N-terminally truncated (1-40 aa deleted)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CRBN, AD-006 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q96SW2
#3: Protein/peptide Zinc finger protein 692 /


Mass: 3520.015 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ZNF692 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q9BU19
#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#5: Chemical ChemComp-Y70 / S-Pomalidomide


Mass: 273.244 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C13H11N3O4

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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: 3.12 Å3/Da / Density % sol: 60.62 %
Crystal growTemperature: 293 K / Method: vapor diffusion
Details: Protein-drug solution: 350 uM ZNF692-ZF4, 70 uM DDB1/CRBN, 80 uM pomalidomide and in 50 mM HEPES pH 7.4, 200 mM NaCl, 0.25 mM TCEP Crystallisation solution: 14.1% (w/v) PEG 5K MME and 70 mM Tris-HCl pH 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.000043 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: May 29, 2017
RadiationMonochromator: SI(111) silicon crista / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.000043 Å / Relative weight: 1
ReflectionResolution: 4.17→48.6 Å / Num. obs: 24386 / % possible obs: 92 % / Redundancy: 4.034 % / Biso Wilson estimate: 156.11 Å2 / CC1/2: 0.99 / Rmerge(I) obs: 0.233 / Rrim(I) all: 0.267 / Χ2: 0.986 / Net I/σ(I): 3.99 / Num. measured all: 98372 / Scaling rejects: 59
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
4.17-4.273.4743.1490.454867190114010.1553.6473.7
4.27-4.393.9321.9760.756079191415460.3012.2680.8
4.39-4.523.9051.5510.896768184917330.3791.77893.7
4.52-4.663.921.211.166551178416710.5011.38893.7
4.66-4.813.8481.0051.346134171915940.5311.1692.7
4.81-4.983.7830.9041.555970171815780.5591.04691.9
4.98-5.173.670.9171.475321158914500.6181.06291.3
5.17-5.383.7440.7091.875264158114060.6730.81888.9
5.38-5.623.9990.6682.045610150914030.7230.76793
5.62-5.893.9670.5632.425256143413250.7640.64792.4
5.89-6.214.270.5842.655654137913240.7230.66896
6.21-6.594.5770.4993.425831128112740.8040.56599.5
6.59-7.044.480.3554.395461123012190.8910.40499.1
7.04-7.64.2780.2665.684804114711230.9270.30497.9
7.6-8.334.3650.1638.084391104510060.9720.18596.3
8.33-9.314.5770.1111.6843349539470.9870.12499.4
9.31-10.754.4360.08114.7237008438340.9920.09298.9
10.75-13.174.1470.07416.2529367197080.9920.08498.5
13.17-18.634.0830.06916.3422095735410.9940.07894.4
18.63-48.64.0660.06317.5212323263030.9960.07192.9

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Processing

Software
NameVersionClassification
BUSTER2.11.7refinement
XDSJun 1, 2017 BUILT=20170923data reduction
XSCALEJun 1, 2017 BUILT=20170923data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5FQD

5fqd


Resolution: 4.25→48.6 Å / Cor.coef. Fo:Fc: 0.861 / Cor.coef. Fo:Fc free: 0.843 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 0.991
RfactorNum. reflection% reflectionSelection details
Rfree0.256 1140 4.9 %RANDOM
Rwork0.221 ---
obs0.223 23287 93.3 %-
Displacement parametersBiso max: 750 Å2 / Biso mean: 152.81 Å2 / Biso min: 53.68 Å2
Baniso -1Baniso -2Baniso -3
1-25.5038 Å20 Å2-34.4595 Å2
2--23.6223 Å20 Å2
3----49.1261 Å2
Refine analyzeLuzzati coordinate error obs: 0.84 Å
Refinement stepCycle: final / Resolution: 4.25→48.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19888 0 44 0 19932
Biso mean--75 --
Num. residues----2512
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d8876SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes6376HARMONIC5
X-RAY DIFFRACTIONt_it40090HARMONIC20
X-RAY DIFFRACTIONt_nbd11SEMIHARMONIC5
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion2666SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact44376SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d40090HARMONIC20.009
X-RAY DIFFRACTIONt_angle_deg72515HARMONIC20.88
X-RAY DIFFRACTIONt_omega_torsion3.17
X-RAY DIFFRACTIONt_other_torsion14.05
LS refinement shellResolution: 4.25→4.29 Å / Rfactor Rfree error: 0 / Total num. of bins used: 50
RfactorNum. reflection% reflection
Rfree0.2722 21 4.51 %
Rwork0.2633 445 -
all0.2637 466 -
obs--75.32 %
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)
12.58080.5299-0.19986.73082.87432.9229-0.4436-0.82730.02571.36040.09171.0147-0.4293-0.78720.35190.50080.23630.01321.23390.20990.9937-19.07279.2801-29.7091
26.3314-0.8807-1.1895.03632.33995.162-0.1999-2.03410.97020.92920.12640.1389-0.89930.72470.07341.34420.1794-0.41131.4889-0.09970.6706-6.703227.9169-20.9247
3-1.9494-1.60473.53019.97066.09072.5790.4622-1.0009-0.14771.80550.56610.1035-0.2477-0.0293-1.02831.59770.199-0.41841.51980.05371.15692.097615.0011-14.4594
44.66260.3423-2.16863.78060.81069.081-0.1819-0.9482-0.24150.4871-0.0613-0.78950.33280.61470.24320.01590.3116-0.18410.61310.41880.900911.9828-2.3474-42.5633
56.52240.0227-1.84484.2262-0.55444.3143-0.41460.4641-0.2329-0.83320.1440.90680.7667-0.97640.27060.0472-0.2004-0.22360.5430.22830.9758-10.3939-2.4997-59.4721
67.53143.3544-3.342913.6645-2.95025.39660.8577-0.42121.2962-0.0840.1350.792-0.9293-0.8033-0.99270.73630.365-0.03010.4872-0.06180.4418-11.595444.4941-72.8451
76.7704-5.73237.92336.0507-5.684311.8203-0.522-0.2318-0.1314-0.12480.66150.3076-0.8212-1.095-0.13950.4271-0.1111-0.39640.60390.03390.7961-16.442725.6828-66.0439
82.4087-1.9706-3.81780-1.58661.29410.1144-1.59561.42091.51530.3992-0.9398-1.6320.498-0.51370.60540.0941-0.31250.99230.01751.33346.8122.771-46.3604
93.6122.5806-0.95668.2466-5.691410.8305-0.0949-0.78860.17750.2059-0.2589-1.2329-0.60.74730.35380.057-0.0012-0.0875-0.1983-0.12781.13637.392837.3123-73.4339
105.3869-10.1918-2.078919.8145-0.110724.8106-0.23880.27731.7101-0.7830.509-1.5156-0.52490.8989-0.27020.1745-0.1739-0.4505-0.1695-0.13840.31433.252352.213-94.5782
1129.6808-11.70041.637925.50388.741940.43080.3249-0.2705-2.2826-0.04610.13380.57342.2051-0.7937-0.4587-0.1611-0.4839-0.0275-0.2341-0.01270.91541.372940.8733-95.8041
124.7959-0.86860.61312.9137-1.86987.8617-0.0171-0.79210.30120.52820.27821.0389-0.5706-0.6858-0.26110.43160.02390.25960.0631-0.20880.8738-74.904574.0731-28.2647
139.67443.7004-0.879313.963-3.52987.7556-0.16590.93940.2099-0.60620.36020.4486-0.2786-0.2789-0.19430.222-0.11880.15-0.3659-0.34680.5605-67.149180.847-49.9601
1411.6704-0.17293.297510.2844-9.574312.8735-0.3167-0.23691.08170.6964-0.3741-0.3849-1.43530.21270.69080.4252-0.24040.012-0.1943-0.81780.5195-58.143991.1534-39.9265
153.6101-0.73070.1075.0872-1.42662.0278-0.1946-0.9027-0.42231.3095-0.1109-0.63650.05210.30570.30550.9252-0.08640.03790.7288-0.19690.4629-50.786658.189-16.3145
1616.05791.6355-4.805510.80451.911.39360.16050.402-0.5069-0.2471-0.45591.46971.0323-0.0450.29550.41970.1-0.3116-0.6043-0.01581.4344-64.096527.9212-56.1496
175.22124.80323.605113.34841.80892.12141.07640.1692-0.97911.3838-0.72981.776610.0193-0.34650.57520.21190.0173-0.41150.04691.637-69.331627.6129-48.9552
1818.24619.68775.90514.221-5.06761.909-0.02680.97180.995-0.81931.03110.64360.97890.3189-1.00430.76010.0206-0.0099-0.1910.08220.8143-54.632165.3662-42.6858
1922.67112.9396-3.824123.902-13.1621.9954-0.33750.25220.5632-2.8288-0.38910.0053-0.18552.82850.72650.1890.02590.077-0.2023-0.07820.8145-46.450560.7927-38.7291
2013.14067.7959-12.727216.89869.67536.4913-0.12792.67080.6234-2.1699-0.03010.7735-1.17780.59360.1580.60550.0009-0.0681-0.10070.30550.9345-47.972948.2576-52.9363
214.9012-0.6773-0.753413.68256.46476.326-0.09650.3357-0.54680.02030.6131-0.78550.15541.6005-0.51660.16910.0662-0.0434-0.16160.01460.9875-44.537629.4443-52.4409
2221.2694-1.9416-7.0256.639-4.6335-2.17390.28580.8303-1.2667-0.2072-0.5314-0.0890.9237-0.10740.24560.98320.56680.14020.7552-0.16041.4898-48.25540.9761-68.0048
2312.2907-5.9677-16.088217.20923.421723.73950.1109-0.9439-0.79882.69890.0041-0.55150.43191.4854-0.1150.89710.1148-0.23860.3286-0.21441.1974-46.95967.5425-55.582
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{A|1 - 176}A1 - 176
2X-RAY DIFFRACTION2{A|177 - 248}A177 - 248
3X-RAY DIFFRACTION3{A|249 - 299}A249 - 299
4X-RAY DIFFRACTION4{A|300 - 856}A300 - 856
5X-RAY DIFFRACTION5{A|857 - 1140}A857 - 1140
6X-RAY DIFFRACTION6{B|42 - 163}B42 - 163
7X-RAY DIFFRACTION7{B|164 - 200}B164 - 200
8X-RAY DIFFRACTION8{B|201 - 262}B201 - 262
9X-RAY DIFFRACTION9{B|263 - 442}B263 - 442
10X-RAY DIFFRACTION10{C|413 - 428}C413 - 428
11X-RAY DIFFRACTION11{C|429 - 442}C429 - 442
12X-RAY DIFFRACTION12{D|1 - 176}D1 - 176
13X-RAY DIFFRACTION13{D|177 - 248}D177 - 248
14X-RAY DIFFRACTION14{D|249 - 299}D249 - 299
15X-RAY DIFFRACTION15{D|300 - 1140}D300 - 1140
16X-RAY DIFFRACTION16{E|42 - 147}E42 - 147
17X-RAY DIFFRACTION17{E|148 - 192}E148 - 192
18X-RAY DIFFRACTION18{E|193 - 216}E193 - 216
19X-RAY DIFFRACTION19{E|217 - 249}E217 - 249
20X-RAY DIFFRACTION20{E|250 - 276}E250 - 276
21X-RAY DIFFRACTION21{E|277 - 442}E277 - 442
22X-RAY DIFFRACTION22{F|413 - 417}F413 - 417
23X-RAY DIFFRACTION23{F|418 - 442}F418 - 442

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