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- PDB-4ljo: Structure of an active ligase (HOIP)/ubiquitin transfer complex -

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Basic information

Entry
Database: PDB / ID: 4ljo
TitleStructure of an active ligase (HOIP)/ubiquitin transfer complex
Components
  • E3 ubiquitin-protein ligase RNF31
  • Polyubiquitin-C
KeywordsLIGASE / E3 ligase-ubiquitin complex / HOIP / RNF31 / ubiquitin / RBR ligase / E3 ligase / RING domain / IBR domain / Zinc Finger
Function / homology
Function and homology information


protein linear polyubiquitination / LUBAC complex / Major pathway of rRNA processing in the nucleolus and cytosol / GTP hydrolysis and joining of the 60S ribosomal subunit / Translesion synthesis by REV1 / Recognition of DNA damage by PCNA-containing replication complex / Translesion Synthesis by POLH / Downregulation of ERBB4 signaling / Spry regulation of FGF signaling / Downregulation of ERBB2:ERBB3 signaling ...protein linear polyubiquitination / LUBAC complex / Major pathway of rRNA processing in the nucleolus and cytosol / GTP hydrolysis and joining of the 60S ribosomal subunit / Translesion synthesis by REV1 / Recognition of DNA damage by PCNA-containing replication complex / Translesion Synthesis by POLH / Downregulation of ERBB4 signaling / Spry regulation of FGF signaling / Downregulation of ERBB2:ERBB3 signaling / NOD1/2 Signaling Pathway / APC/C:Cdc20 mediated degradation of Cyclin B / SCF-beta-TrCP mediated degradation of Emi1 / APC-Cdc20 mediated degradation of Nek2A / EGFR downregulation / TCF dependent signaling in response to WNT / NRIF signals cell death from the nucleus / p75NTR recruits signalling complexes / NF-kB is activated and signals survival / Activated NOTCH1 Transmits Signal to the Nucleus / Downregulation of TGF-beta receptor signaling / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Downregulation of SMAD2/3:SMAD4 transcriptional activity / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / Senescence-Associated Secretory Phenotype (SASP) / Regulation of innate immune responses to cytosolic DNA / activated TAK1 mediates p38 MAPK activation / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Regulation of FZD by ubiquitination / PINK1-PRKN Mediated Mitophagy / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Regulation of TNFR1 signaling / TNFR1-induced NF-kappa-B signaling pathway / Translesion synthesis by POLK / Translesion synthesis by POLI / Regulation of necroptotic cell death / MAP3K8 (TPL2)-dependent MAPK1/3 activation / HDR through Homologous Recombination (HRR) / Josephin domain DUBs / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / DNA Damage Recognition in GG-NER / Formation of Incision Complex in GG-NER / Gap-filling DNA repair synthesis and ligation in GG-NER / Dual Incision in GG-NER / Fanconi Anemia Pathway / Regulation of TP53 Activity through Phosphorylation / Regulation of TP53 Degradation / Regulation of TP53 Activity through Methylation / Negative regulation of MET activity / Cyclin D associated events in G1 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Downregulation of ERBB2 signaling / E3 ubiquitin ligases ubiquitinate target proteins / Regulation of PTEN localization / ER Quality Control Compartment (ERQC) / Regulation of expression of SLITs and ROBOs / Interferon alpha/beta signaling / Endosomal Sorting Complex Required For Transport (ESCRT) / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / IKK complex recruitment mediated by RIP1 / IRAK2 mediated activation of TAK1 complex / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Alpha-protein kinase 1 signaling pathway / RAS processing / Pexophagy / Inactivation of CSF3 (G-CSF) signaling / Negative regulation of FLT3 / Regulation of BACH1 activity / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Regulation of NF-kappa B signaling / Termination of translesion DNA synthesis / Ovarian tumor domain proteases / Negative regulators of DDX58/IFIH1 signaling / Negative regulation of FGFR1 signaling / Negative regulation of FGFR2 signaling / Negative regulation of FGFR3 signaling / Negative regulation of FGFR4 signaling / Negative regulation of MAPK pathway / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Iron uptake and transport / Deactivation of the beta-catenin transactivating complex / Metalloprotease DUBs / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / linear polyubiquitin binding / Activation of NF-kappaB in B cells / L13a-mediated translational silencing of Ceruloplasmin expression / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SRP-dependent cotranslational protein targeting to membrane / SCF(Skp2)-mediated degradation of p27/p21 / FCERI mediated NF-kB activation / Autodegradation of the E3 ubiquitin ligase COP1 / Asymmetric localization of PCP proteins / Degradation of AXIN / Degradation of DVL / Hedgehog ligand biogenesis
Similarity search - Function
: / : / : / : / : / E3 ubiquitin-protein ligase RNF31-like / E3 ubiquitin-protein ligase RNF31, UBA-like domain / E3 ubiquitin-protein ligase RNF31, PUB domain / RNF31, C-terminal / HOIP UBA domain pair ...: / : / : / : / : / E3 ubiquitin-protein ligase RNF31-like / E3 ubiquitin-protein ligase RNF31, UBA-like domain / E3 ubiquitin-protein ligase RNF31, PUB domain / RNF31, C-terminal / HOIP UBA domain pair / E3 Ubiquitin Ligase RBR C-terminal domain / PNGase/UBA- or UBX-containing domain / PUB-like domain superfamily / PUB domain / PUB domain / IBR domain, a half RING-finger domain / IBR domain / In Between Ring fingers / TRIAD supradomain / TRIAD supradomain profile. / Zinc finger domain / Ubiquitin-associated domain / Ubiquitin-associated domain (UBA) profile. / Zinc finger RanBP2 type profile. / Zinc finger RanBP2-type signature. / Zinc finger, RanBP2-type superfamily / Zinc finger, RanBP2-type / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin domain signature. / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin-like domain / Ubiquitin domain profile. / Ubiquitin-like domain superfamily / Zinc finger, RING/FYVE/PHD-type / Roll / Alpha Beta
Similarity search - Domain/homology
IMIDAZOLE / : / Ubiquitin-ribosomal protein eL40 fusion protein / E3 ubiquitin-protein ligase RNF31
Similarity search - Component
Biological speciesHomo sapiens (human)
Bos taurus (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.564 Å
AuthorsRana, R.R. / Stieglitz, B. / Koliopoulos, M.G. / Morris-Davies, A.C. / Christodoulou, E. / Howell, S. / Brown, N.R. / Rittinger, K.
CitationJournal: Nature / Year: 2013
Title: Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP.
Authors: Stieglitz, B. / Rana, R.R. / Koliopoulos, M.G. / Morris-Davies, A.C. / Schaeffer, V. / Christodoulou, E. / Howell, S. / Brown, N.R. / Dikic, I. / Rittinger, K.
History
DepositionJul 5, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 16, 2013Provider: repository / Type: Initial release
Revision 1.1Nov 13, 2013Group: Database references
Revision 1.2Dec 18, 2013Group: Database references
Revision 1.3Oct 8, 2014Group: Structure summary
Revision 1.4Nov 15, 2017Group: Refinement description / Category: software / Item: _software.classification
Revision 1.5Jan 24, 2018Group: Structure summary / Category: audit_author / Item: _audit_author.name
Revision 1.6Jul 17, 2019Group: Data collection / Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.location / _software.name / _software.type
Revision 1.7Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_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_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_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_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: E3 ubiquitin-protein ligase RNF31
B: Polyubiquitin-C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,0738
Polymers33,6762
Non-polymers3966
Water3,963220
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2050 Å2
ΔGint-31 kcal/mol
Surface area16480 Å2
MethodPISA
Unit cell
Length a, b, c (Å)45.950, 45.950, 133.010
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number144
Space group name H-MP31

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Components

#1: Protein E3 ubiquitin-protein ligase RNF31 / HOIL-1-interacting protein / HOIP / RING finger protein 31 / Zinc in-between-RING-finger ubiquitin- ...HOIL-1-interacting protein / HOIP / RING finger protein 31 / Zinc in-between-RING-finger ubiquitin-associated domain protein


Mass: 25099.658 Da / Num. of mol.: 1
Fragment: E3 ligase HOIP catalytic core (unp residues 853-1072)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RNF31, ZIBRA / Plasmid: pET-49b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Gold
References: UniProt: Q96EP0, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases)
#2: Protein Polyubiquitin-C


Mass: 8576.831 Da / Num. of mol.: 1 / Fragment: unp residues 77-152 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: E1B9K1, UniProt: P63048*PLUS
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-IMD / IMIDAZOLE / Imidazole


Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 220 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.46 Å3/Da / Density % sol: 50.01 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.5
Details: 0.1 M carboxylic acids, 0.1 M imidazole, MES, 30 % P550 MME_P20K, pH 6.5, vapour diffusion, temperature 293K, VAPOR DIFFUSION

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.92 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 1, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92 Å / Relative weight: 1
ReflectionResolution: 1.56→44.34 Å / Num. all: 88818 / Num. obs: 44055 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.4 % / Biso Wilson estimate: 27.559 Å2 / Rmerge(I) obs: 0.039 / Net I/σ(I): 12.2
Reflection shell
Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsDiffraction-ID% possible all
1.56-1.60.5931.52194
1.6-1.640.51.73193.1
1.64-1.690.3212.4194.2
1.69-1.740.2553.14195.3
1.74-1.80.1894.09195.5
1.8-1.860.1474.89195.2
1.86-1.930.1066.32194.7
1.93-2.010.0837.67193.6
2.01-2.10.0659.25195.8
2.1-2.210.05611.02196
2.21-2.330.05112.27194.9
2.33-2.470.04513.34195.2
2.47-2.640.04314.28194.4
2.64-2.850.04115.53195.7
2.85-3.120.0416.15195.7
3.12-3.490.03816.66194.4
3.49-4.030.03416.7192.6
4.03-4.930.03117.36194.1
4.93-6.980.03316.9191.3
6.980.0416.71188.5

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation2.5 Å44.34 Å
Translation2.5 Å44.34 Å

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Processing

Software
NameVersionClassificationNB
PHENIXrefinement
PHASER2.3.0phasing
REFMACrefinement
PDB_EXTRACT3.11data extraction
CCP4refinement
XSCALEdata scaling
CCP4data reduction
CCP4data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entry 4LJQ

4ljq


Resolution: 1.564→44.337 Å / Occupancy max: 1 / Occupancy min: 0.75 / SU ML: 0.17 / σ(F): 0.73 / Phase error: 25.21 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2124 2220 5.03 %
Rwork0.1812 --
obs0.1828 44055 94.6 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 39.0035 Å2
Refinement stepCycle: LAST / Resolution: 1.564→44.337 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2306 0 10 220 2536
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0062360
X-RAY DIFFRACTIONf_angle_d1.0323187
X-RAY DIFFRACTIONf_dihedral_angle_d13.877907
X-RAY DIFFRACTIONf_chiral_restr0.071341
X-RAY DIFFRACTIONf_plane_restr0.006424
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.5637-1.58150.3681410.32432715X-RAY DIFFRACTION94
1.5815-1.60010.32341400.31842562X-RAY DIFFRACTION94
1.6001-1.61960.33661840.30742568X-RAY DIFFRACTION93
1.6196-1.64010.331330.30412710X-RAY DIFFRACTION94
1.6401-1.66170.31621440.27472488X-RAY DIFFRACTION92
1.6617-1.68440.26291350.2572743X-RAY DIFFRACTION95
1.6844-1.70850.24991530.25212646X-RAY DIFFRACTION94
1.7085-1.7340.29931260.23542631X-RAY DIFFRACTION96
1.734-1.76110.2871380.23262807X-RAY DIFFRACTION96
1.7611-1.790.24251190.22342625X-RAY DIFFRACTION96
1.79-1.82080.22251650.20582684X-RAY DIFFRACTION95
1.8208-1.8540.25421280.19912677X-RAY DIFFRACTION95
1.854-1.88960.2221220.20682665X-RAY DIFFRACTION95
1.8896-1.92820.26541340.19882732X-RAY DIFFRACTION95
1.9282-1.97010.22861370.1942555X-RAY DIFFRACTION92
1.9701-2.01590.22291430.20012697X-RAY DIFFRACTION95
2.0159-2.06640.21051590.19162688X-RAY DIFFRACTION96
2.0664-2.12220.22911490.18892652X-RAY DIFFRACTION96
2.1222-2.18470.23441620.19632768X-RAY DIFFRACTION96
2.1847-2.25520.22891500.1892599X-RAY DIFFRACTION95
2.2552-2.33580.27521270.19182756X-RAY DIFFRACTION95
2.3358-2.42930.25551410.17952675X-RAY DIFFRACTION95
2.4293-2.53990.21691270.18462623X-RAY DIFFRACTION94
2.5399-2.67370.25821430.18862653X-RAY DIFFRACTION95
2.6737-2.84120.19841190.19792743X-RAY DIFFRACTION96
2.8412-3.06060.2721280.20572735X-RAY DIFFRACTION96
3.0606-3.36850.25831340.18792636X-RAY DIFFRACTION95
3.3685-3.85560.21571460.1652582X-RAY DIFFRACTION92
3.8556-4.85670.13951330.132664X-RAY DIFFRACTION95
4.8567-44.35450.14641690.14922517X-RAY DIFFRACTION90
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)
14.90450.2385-0.95171.3188-0.40154.06760.0416-0.75040.31680.1343-0.0885-0.0967-0.6950.29710.07570.3123-0.0527-0.00080.40090.00320.20870.309814.111819.5067
23.0132-1.5847-0.0932.4627-0.03445.72510.00970.0408-0.18060.098-0.05270.11050.346-0.27560.13390.2476-0.07140.03490.32220.03620.1962-5.17674.620414.6899
35.74960.56080.22386.10340.78377.6251-0.04870.2738-0.2731-0.3385-0.08980.6337-0.0568-0.57460.11290.2384-0.0494-0.03150.3272-0.01550.2624-10.40787.80354.8188
41.52860.9722-1.07534.1242-0.59282.9686-0.13550.24370.0089-0.47540.09220.0617-0.0657-0.07840.12180.2772-0.0749-0.00450.20810.00830.15491.782314.0909-0.7674
52.09050.2304-1.52624.31820.53321.2964-0.2043-1.0059-0.08891.5717-0.1533-1.2291-0.53971.45410.27640.4835-0.2176-0.18930.79790.0950.419919.686114.811516.5024
61.15851.7937-1.83013.9406-3.19323.6082-0.1082-0.3135-0.943-0.0913-0.2559-0.28841.41240.21450.28630.4430.02820.04640.59770.13810.43948.6265-3.412419.8185
72.1430.3072-0.09992.0459-1.3723.599-0.0507-0.2772-0.2323-0.0969-0.1987-0.52660.07150.5890.25170.179-0.08790.01520.30210.05410.263914.48912.44629.4676
83.24530.2283-0.99583.5863-1.07069.21230.00380.4130.0837-0.61750.08230.0502-0.2259-0.325-0.12280.3011-0.0391-0.00780.21440.03970.15741.722220.1986-6.961
92.31650.0425-1.2912.1266-1.86527.5590.33770.38730.4159-0.25450.22440.2336-1.1514-1.0315-0.13310.48690.05840.01140.35540.06260.2815-2.289225.024-7.8982
105.6169-1.4572-5.68312.03171.48465.8913-0.0734-0.8662-0.42810.4244-0.2091-0.25570.23821.16770.23920.3253-0.10930.01650.3843-0.00950.23166.53480.1403-0.7471
113.2498-3.82213.86425.5008-5.04335.08390.38141.12470.9209-0.864-0.0883-1.4601-0.72710.9991-0.06430.5515-0.16940.1090.67340.12680.629313.68624.101-9.9962
129.8616-0.67860.3218.49330.18669.8302-0.1616-0.25060.13840.22540.13510.15940.2206-0.28320.14290.2271-0.04470.03490.2003-0.02020.1835-1.3819-0.8186-0.6004
139.5466-0.9641-3.03117.1921-4.76647.37910.0615-0.2177-0.0787-0.0313-0.24860.36-0.0511-0.4160.17850.2823-0.05980.01360.2016-0.04720.1413-2.01783.0926-8.5116
144.228-4.98282.45925.8565-2.56916.98270.53470.556-0.0519-1.1981-0.4523-0.1240.1574-0.0689-0.18690.3907-0.06470.0350.23-0.03070.20961.74170.2208-15.3609
158.2416-1.1779-1.28586.02330.02377.6794-0.27261.001-0.7275-1.056-0.0659-0.15480.9655-0.16120.36180.6354-0.13140.06630.2936-0.01290.32611.1555-10.4459-8.9165
162.72573.11961.77068.79625.46778.6025-0.2202-0.8267-0.28131.0373-0.04480.01820.89420.35070.15540.3633-0.02050.03150.31440.06410.3453.5451-8.8350.5121
171.5651-0.5560.48381.23740.74572.09230.2354-0.0088-0.0515-0.2577-0.09770.0264-0.12630.1118-0.14190.3484-0.04790.05050.2461-0.0260.26435.6619-1.5953-17.677
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 857:879 )A857 - 879
2X-RAY DIFFRACTION2( CHAIN A AND RESID 880:895 )A880 - 895
3X-RAY DIFFRACTION3( CHAIN A AND RESID 896:913 )A896 - 913
4X-RAY DIFFRACTION4( CHAIN A AND RESID 914:949 )A914 - 949
5X-RAY DIFFRACTION5( CHAIN A AND RESID 950:971 )A950 - 971
6X-RAY DIFFRACTION6( CHAIN A AND RESID 972:985 )A972 - 985
7X-RAY DIFFRACTION7( CHAIN A AND RESID 986:1012 )A986 - 1012
8X-RAY DIFFRACTION8( CHAIN A AND RESID 1013:1034 )A1013 - 1034
9X-RAY DIFFRACTION9( CHAIN A AND RESID 1035:1072 )A1035 - 1072
10X-RAY DIFFRACTION10( CHAIN B AND RESID 1:6 )B1 - 6
11X-RAY DIFFRACTION11( CHAIN B AND RESID 7:12 )B7 - 12
12X-RAY DIFFRACTION12( CHAIN B AND RESID 13:22 )B13 - 22
13X-RAY DIFFRACTION13( CHAIN B AND RESID 23:34 )B23 - 34
14X-RAY DIFFRACTION14( CHAIN B AND RESID 35:44 )B35 - 44
15X-RAY DIFFRACTION15( CHAIN B AND RESID 45:56 )B45 - 56
16X-RAY DIFFRACTION16( CHAIN B AND RESID 57:65 )B57 - 65
17X-RAY DIFFRACTION17( CHAIN B AND RESID 66:76 )B66 - 76

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