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- PDB-4s3o: PCGF5-RING1B-UbcH5c complex -

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Basic information

Entry
Database: PDB / ID: 4s3o
TitlePCGF5-RING1B-UbcH5c complex
Components
  • E3 ubiquitin-protein ligase RING2
  • Polycomb group RING finger protein 5
  • Ubiquitin-conjugating enzyme E2 D3
KeywordsLigase/Transcription / E2 / E3 / RING domain / Ubiquitin RING E3 Ligase / Ligase-Transcription complex
Function / homology
Function and homology information


: / : / histone H2AK119 ubiquitin ligase activity / RING-like zinc finger domain binding / sex chromatin / PRC1 complex / PcG protein complex / (E3-independent) E2 ubiquitin-conjugating enzyme / Signaling by BMP / protein K6-linked ubiquitination ...: / : / histone H2AK119 ubiquitin ligase activity / RING-like zinc finger domain binding / sex chromatin / PRC1 complex / PcG protein complex / (E3-independent) E2 ubiquitin-conjugating enzyme / Signaling by BMP / protein K6-linked ubiquitination / SUMOylation of DNA methylation proteins / protein K11-linked ubiquitination / gastrulation with mouth forming second / SUMOylation of RNA binding proteins / anterior/posterior axis specification / positive regulation of protein targeting to mitochondrion / E2 ubiquitin-conjugating enzyme / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / X chromosome / Transcriptional Regulation by E2F6 / germ cell development / protein monoubiquitination / ubiquitin conjugating enzyme activity / MLL1 complex / negative regulation of BMP signaling pathway / protein autoubiquitination / protein K48-linked ubiquitination / SUMOylation of DNA damage response and repair proteins / epigenetic regulation of gene expression / ubiquitin ligase complex / SUMOylation of chromatin organization proteins / TICAM1, RIP1-mediated IKK complex recruitment / IKK complex recruitment mediated by RIP1 / SUMOylation of transcription cofactors / Regulation of PTEN gene transcription / Negative regulators of DDX58/IFIH1 signaling / Peroxisomal protein import / Downregulation of SMAD2/3:SMAD4 transcriptional activity / Regulation of TNFR1 signaling / RNA polymerase II transcription regulatory region sequence-specific DNA binding / euchromatin / RING-type E3 ubiquitin transferase / protein modification process / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Inactivation of CSF3 (G-CSF) signaling / negative regulation of DNA-binding transcription factor activity / protein polyubiquitination / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / E3 ubiquitin ligases ubiquitinate target proteins / Neddylation / mitotic cell cycle / gene expression / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / Oxidative Stress Induced Senescence / nuclear body / endosome membrane / protein ubiquitination / chromatin remodeling / DNA-binding transcription factor activity / DNA repair / centrosome / apoptotic process / ubiquitin protein ligase binding / chromatin binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / zinc ion binding / extracellular exosome / nucleoplasm / ATP binding / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol
Similarity search - Function
E3 ubiquitin-protein ligase RING2 / E3 ubiquitin-protein ligase RING1/RING2 / RAWUL domain / RAWUL domain RING finger- and WD40-associated ubiquitin-like / Zinc finger, C3HC4 type (RING finger) / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues ...E3 ubiquitin-protein ligase RING2 / E3 ubiquitin-protein ligase RING1/RING2 / RAWUL domain / RAWUL domain RING finger- and WD40-associated ubiquitin-like / Zinc finger, C3HC4 type (RING finger) / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Ubiquitin-conjugating enzyme/RWD-like / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / Roll / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Ubiquitin-conjugating enzyme E2 D3 / Polycomb group RING finger protein 5 / E3 ubiquitin-protein ligase RING2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsTaherbhoy, A.M. / Cochran, A.G.
CitationJournal: Nat Commun / Year: 2015
Title: BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.
Authors: Taherbhoy, A.M. / Huang, O.W. / Cochran, A.G.
History
DepositionMar 23, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 15, 2015Provider: repository / Type: Initial release
Revision 1.1Jul 22, 2015Group: Database references
Revision 1.2Sep 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_asym_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_seq_id / _struct_conn.ptnr2_label_asym_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: Ubiquitin-conjugating enzyme E2 D3
D: Ubiquitin-conjugating enzyme E2 D3
B: E3 ubiquitin-protein ligase RING2
E: E3 ubiquitin-protein ligase RING2
C: Polycomb group RING finger protein 5
F: Polycomb group RING finger protein 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)88,35814
Polymers87,8356
Non-polymers5238
Water2,738152
1
D: Ubiquitin-conjugating enzyme E2 D3
E: E3 ubiquitin-protein ligase RING2
F: Polycomb group RING finger protein 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,1797
Polymers43,9173
Non-polymers2624
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Ubiquitin-conjugating enzyme E2 D3
B: E3 ubiquitin-protein ligase RING2
C: Polycomb group RING finger protein 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,1797
Polymers43,9173
Non-polymers2624
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)54.392, 105.285, 132.417
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
DetailsTwo biological heterotrimers appear in the asymmetric unit (A,B,C and D,E,F)

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Components

#1: Protein Ubiquitin-conjugating enzyme E2 D3 / Ubiquitin carrier protein D3 / Ubiquitin-conjugating enzyme E2(17)KB 3 / Ubiquitin-conjugating ...Ubiquitin carrier protein D3 / Ubiquitin-conjugating enzyme E2(17)KB 3 / Ubiquitin-conjugating enzyme E2-17 kDa 3 / Ubiquitin-protein ligase D3


Mass: 16719.066 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2D3, UBC5C, UBCH5C / Production host: Escherichia coli (E. coli) / References: UniProt: P61077, ubiquitin-protein ligase
#2: Protein E3 ubiquitin-protein ligase RING2 / Huntingtin-interacting protein 2-interacting protein 3 / HIP2-interacting protein 3 / Protein DinG ...Huntingtin-interacting protein 2-interacting protein 3 / HIP2-interacting protein 3 / Protein DinG / RING finger protein 1B / RING1b / RING finger protein 2 / RING finger protein BAP-1


Mass: 13247.405 Da / Num. of mol.: 2 / Fragment: RING domain, UNP residues 1-116
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RNF2, BAP1, DING, HIPI3, RING1B / Production host: Escherichia coli (E. coli)
References: UniProt: Q99496, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases)
#3: Protein Polycomb group RING finger protein 5 / RING finger protein 159


Mass: 13950.874 Da / Num. of mol.: 2 / Fragment: RING domain, UNP residues 1-109
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PCGF5, RNF159 / Production host: Escherichia coli (E. coli) / References: UniProt: Q86SE9
#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Zn
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 152 / 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: 2.16 Å3/Da / Density % sol: 43.01 %
Crystal growTemperature: 277 K / Method: vapor diffusion / pH: 6.5
Details: 13.5% PEG 550 MME, 10 mM TCEP, 0.1 M MES pH 6.5, 100 mM KCl, VAPOR DIFFUSION, temperature 277K

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Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1.00003 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 13, 2013
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00003 Å / Relative weight: 1
ReflectionResolution: 2→50 Å / Num. all: 52285 / Num. obs: 52191 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 7.2 % / Biso Wilson estimate: 32.06 Å2 / Rsym value: 0.069 / Net I/σ(I): 22.5

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Processing

Software
NameVersionClassification
BOSdata collection
PHASERphasing
PHENIX(phenix.refine: 1.8.2_1309)refinement
HKL-2000data reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3RPG, chains A and C

3rpg


Resolution: 2→48.919 Å / SU ML: 0.23 / σ(F): 1.34 / Phase error: 25.13 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2368 2664 5.1 %
Rwork0.1939 --
obs0.1961 52191 99.8 %
all-52285 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refine analyzeLuzzati sigma a obs: 0.23 Å
Refinement stepCycle: LAST / Resolution: 2→48.919 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5405 0 8 152 5565
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0095650
X-RAY DIFFRACTIONf_angle_d1.1437712
X-RAY DIFFRACTIONf_dihedral_angle_d13.0712096
X-RAY DIFFRACTIONf_chiral_restr0.076870
X-RAY DIFFRACTIONf_plane_restr0.006990
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.03570.29331510.24262531X-RAY DIFFRACTION99
2.0357-2.07480.28131360.23262580X-RAY DIFFRACTION100
2.0748-2.11720.28611340.22262576X-RAY DIFFRACTION100
2.1172-2.16320.27671260.20712578X-RAY DIFFRACTION100
2.1632-2.21350.25281300.21232554X-RAY DIFFRACTION100
2.2135-2.26890.25951310.20532602X-RAY DIFFRACTION100
2.2689-2.33020.25971550.2152551X-RAY DIFFRACTION100
2.3302-2.39880.28091310.20382600X-RAY DIFFRACTION100
2.3988-2.47620.24761160.20882615X-RAY DIFFRACTION100
2.4762-2.56470.26911330.21392606X-RAY DIFFRACTION100
2.5647-2.66740.27261660.23082520X-RAY DIFFRACTION100
2.6674-2.78880.28321650.22842568X-RAY DIFFRACTION100
2.7888-2.93580.33131310.23442640X-RAY DIFFRACTION100
2.9358-3.11970.26331420.23572611X-RAY DIFFRACTION100
3.1197-3.36050.26021340.22252637X-RAY DIFFRACTION100
3.3605-3.69860.22371470.18932619X-RAY DIFFRACTION100
3.6986-4.23360.17361420.16472666X-RAY DIFFRACTION100
4.2336-5.33280.21171380.14692674X-RAY DIFFRACTION100
5.3328-48.93320.19261560.16672799X-RAY DIFFRACTION99
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)
19.7337-5.02674.46145.5421-6.12298.16460.10550.34230.4706-0.1451-0.30260.0853-0.16020.14350.23440.3830.00330.07120.2389-0.11570.32825.65660.0865-17.4949
27.97193.4882.50154.29243.41094.689-0.0963-0.1105-0.15360.0739-0.35680.5361-0.078-0.47210.42540.3220.02090.03770.1779-0.05090.33910.8055-12.0014-17.5484
36.18185.6690.90175.20090.40442.4207-0.13060.2835-0.4936-0.1930.1557-0.16650.02860.065-0.01550.25240.01820.06870.2046-0.08290.28867.0476-15.5369-23.8599
41.27061.1744-0.1446.05422.70635.5413-0.14960.928-0.66460.0254-0.42610.72340.3163-0.44790.39390.4009-0.0520.05810.5994-0.34010.6183-3.9387-25.7376-31.3601
58.6522-0.5378-0.83847.45940.71535.0867-0.02720.1999-0.5149-0.57320.17760.8502-0.2673-0.4583-0.07520.34960.0252-0.01750.40650.04930.2845-16.826-46.7444-18.3712
62.60541.8868-0.42437.1596-0.75445.57410.6695-0.15150.79890.503-0.17540.407-0.79780.3864-0.13840.32280.04650.07930.46920.00580.4241-11.9736-37.0951-13.0889
77.84724.71213.5597.48353.87927.7662-0.33340.50250.85830.015-0.23980.6388-0.2126-0.75110.30540.27880.0622-0.01750.32670.09380.3423-7.8059-37.9335-19.5457
86.30464.67081.97776.66333.17964.3430.10250.045-0.21540.24540.1958-0.44230.11320.3344-0.27870.25780.09150.01950.2697-0.0180.25850.7619-38.8351-13.0468
96.16313.47933.2615.756-0.20693.93840.6984-0.197-0.6910.8029-0.2041-0.490.59270.1926-0.45580.43610.0737-0.07650.32580.03380.3488-2.1143-47.1283-9.2163
102.26061.9933-1.16843.8116-0.9311.29890.4638-0.0704-1.79210.36490.071-1.49161.53570.541-0.64930.7990.1772-0.36230.809-0.21180.786910.7866-43.4776-3.8567
117.9765-0.51713.8676.0247-2.26655.0880.2304-0.6567-0.02361.21940.2144-1.1296-0.34080.6168-0.3280.56860.0303-0.18110.6564-0.24370.629411.0844-30.2584-2.2171
123.15643.88165.27885.10536.8199.2050.425-1.4386-0.0138-0.0662-0.29310.29430.8551-0.6712-0.13410.4029-0.1125-0.03820.44960.01570.258930.3419-4.0324-46.3003
131.4275-1.7573-1.68424.20211.43815.98620.09550.25520.3863-0.54940.17280.122-0.6552-0.0976-0.30890.3117-0.1875-0.07090.52220.02460.463528.748617.6169-42.4183
146.4903-2.9911-0.25542.26332.38716.90860.17750.3557-0.5606-0.2957-0.20371.49330.2873-0.7220.01130.3259-0.0621-0.01380.398-0.01110.401915.597412.4382-25.3123
153.03832.7282-4.49489.6262-4.98616.79570.1322-0.40850.49910.6154-0.01210.0422-0.14120.1673-0.09810.2035-0.00050.00540.2533-0.04810.214120.10254.4325-17.9741
166.42111.50851.63718.50975.27449.14710.1624-0.0975-0.11990.0673-0.097-0.42130.46230.192-0.01190.26290.00580.01890.2832-0.01810.298929.4875-0.4958-26.9276
177.7907-1.49890.8543.4151-4.72637.4361-0.1061-1.0578-0.50770.03030.0384-0.23110.45130.97640.11610.31270.062-0.02840.43010.04080.316726.2228-2.9235-16.7939
188.6963-2.78634.30775.06640.88868.2638-0.19040.1513-1.89550.0820.1087-0.1470.4638-0.01840.07830.51520.00180.17280.2837-0.030.664925.477-9.8631-24.9753
198.0622-5.7251.93854.1196-0.86656.4227-0.0526-0.1293-0.21480.2887-0.2403-0.87820.09221.06430.2760.326-0.00260.06460.5317-0.00530.488534.5466-0.1714-22.6569
203.4255-3.8975-2.85197.1810.70696.51260.4643-0.62821.1289-0.35670.1215-0.7516-0.67480.6835-0.47580.2635-0.09860.00980.3891-0.08520.335526.113815.465-20.7305
213.67412.84964.91489.41662.51876.9063-0.27520.0547-0.15950.11060.2706-0.0272-0.06340.6005-0.04630.25890.0678-0.02170.3119-0.07260.2653-9.2387-68.057212.9778
221.5357-1.5353-1.5783.77751.15886.915-0.1067-0.392-0.1653-0.0970.10550.38640.4379-0.2110.01470.27030.0127-0.01920.13190.0410.3368-26.4799-69.616915.4769
239.7855-4.7759-2.06997.66510.28852.09560.2831-0.31110.50840.2992-0.12630.4941-0.7941-0.1008-0.17770.60670.0931-0.02880.2683-0.02520.3177-28.5858-53.2869-7.2085
247.51183.7116-4.40338.1233-2.26352.77640.29860.40450.1198-0.4053-0.20430.1060.2004-0.1161-0.11520.4960.0906-0.0770.33210.02060.2232-19.3021-58.0553-15.0692
252.6074-1.73370.42453.6125-3.78365.03680.0415-0.2093-0.358-0.404-0.31180.0780.0140.58540.24150.41460.076-0.07180.3951-0.00710.2258-13.9633-67.4915-6.4324
262.9523-0.9733-4.67142.54211.30649.79630.25640.321-0.6782-0.6503-0.1164-0.30320.7232-0.77220.04820.57110.0861-0.02050.2357-0.07330.3443-12.9088-64.0235-16.0028
272.4629-2.12490.59742.78390.97152.5118-0.61560.2915-0.21510.3433-0.0793-1.741-0.22811.63180.47840.4508-0.00240.02620.63260.06480.7209-4.552-62.2057-11.1154
282.3701-1.17672.2341.7115-3.79448.51241.03570.7831-0.90060.2856-1.52220.66590.65310.93440.48320.62590.0672-0.02470.54770.01020.8236-4.159-66.7687-7.1309
298.2983-4.4191-2.64787.3483-0.27482.04020.11380.5131-0.5962-0.4867-0.13160.3410.2673-0.18710.0260.5410.0075-0.09890.297-0.06230.2856-24.981-67.0578-11.3403
309.1548-5.65025.84399.446-4.51773.8721-0.5189-0.65080.3011.43290.05140.6138-1.2689-0.02350.46440.566-0.13370.0640.5649-0.09610.495127.154622.9919-27.3531
311.022-0.687-0.72287.9717-1.18141.3463-0.0188-0.00410.2091-0.26170.261-0.1685-0.01620.131-0.24870.2208-0.12610.00970.5052-0.06790.269736.420510.5486-37.5717
321.46322.47261.30785.6071-0.64696.8340.2462-0.3232-0.5987-0.2419-0.1004-1.61090.59291.7893-0.15790.2776-0.01130.00880.7894-0.10060.528345.63384.0602-35.6765
334.8288-4.1357-6.77248.09115.919.5409-0.3112-0.639-0.11410.60070.227-0.2950.9637-0.2802-0.00530.3658-0.0616-0.08070.507-0.00880.262434.93110.1136-37.3663
348.6079-3.7121-3.22737.34851.02187.8203-0.08760.53760.1251-0.65370.19480.5592-0.3146-0.3695-0.0860.2335-0.0513-0.05890.36330.0380.295322.084714.3476-34.2851
354.408-1.9559-1.48014.32713.50368.2538-0.38690.5820.6562-0.82850.01790.3602-0.4378-0.57380.25170.4938-0.1878-0.12870.46810.17110.406924.182917.3686-51.2387
365.0750.4173-1.23483.1737-0.27495.3349-0.08020.48680.0576-0.69170.07960.50210.2432-0.3638-0.02480.46050.0268-0.1510.1918-0.0360.3659-29.3327-70.25080.8135
378.21540.8364-1.40975.29145.93727.42040.2363-0.4987-0.97630.16920.09090.71060.82450.0711-0.17790.42650.0184-0.08790.1643-0.02480.3487-22.4462-76.55088.1573
387.98543.53627.28194.2321.93329.8142-0.07910.8307-1.0806-0.28510.0841-0.04830.380.7323-0.15860.59650.09470.0070.3182-0.10370.5772-17.2616-82.92862.039
395.2254-1.16312.62663.8717-4.96496.8440.32160.7351-0.6334-1.3632-0.4043-0.12150.44970.84980.09250.45330.1143-0.00010.2693-0.05430.3636-14.1833-72.63534.0947
407.051-6.5671-0.76357.7459-0.48816.5436-0.2895-0.00030.4474-0.3902-0.22810.034-0.7461-0.03090.39160.4230.0305-0.14310.1608-0.04570.2834-27.8409-59.24671.6036
418.5543-0.97921.58626.109-2.73715.5332-0.2516-0.83210.09280.18920.36470.5745-0.2567-0.895-0.15450.27150.08470.02460.2309-0.0510.3071-30.2527-60.861718.8742
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 0 through 25 )
2X-RAY DIFFRACTION2chain 'A' and (resid 26 through 74 )
3X-RAY DIFFRACTION3chain 'A' and (resid 75 through 111 )
4X-RAY DIFFRACTION4chain 'A' and (resid 112 through 147 )
5X-RAY DIFFRACTION5chain 'D' and (resid 0 through 15 )
6X-RAY DIFFRACTION6chain 'D' and (resid 16 through 28 )
7X-RAY DIFFRACTION7chain 'D' and (resid 29 through 38 )
8X-RAY DIFFRACTION8chain 'D' and (resid 39 through 84 )
9X-RAY DIFFRACTION9chain 'D' and (resid 85 through 111 )
10X-RAY DIFFRACTION10chain 'D' and (resid 112 through 120 )
11X-RAY DIFFRACTION11chain 'D' and (resid 121 through 147 )
12X-RAY DIFFRACTION12chain 'B' and (resid 10 through 16 )
13X-RAY DIFFRACTION13chain 'B' and (resid 17 through 41 )
14X-RAY DIFFRACTION14chain 'B' and (resid 42 through 49 )
15X-RAY DIFFRACTION15chain 'B' and (resid 50 through 60 )
16X-RAY DIFFRACTION16chain 'B' and (resid 61 through 69 )
17X-RAY DIFFRACTION17chain 'B' and (resid 70 through 81 )
18X-RAY DIFFRACTION18chain 'B' and (resid 82 through 96 )
19X-RAY DIFFRACTION19chain 'B' and (resid 97 through 103 )
20X-RAY DIFFRACTION20chain 'B' and (resid 104 through 116 )
21X-RAY DIFFRACTION21chain 'E' and (resid 10 through 16 )
22X-RAY DIFFRACTION22chain 'E' and (resid 17 through 31 )
23X-RAY DIFFRACTION23chain 'E' and (resid 40 through 49 )
24X-RAY DIFFRACTION24chain 'E' and (resid 50 through 60 )
25X-RAY DIFFRACTION25chain 'E' and (resid 61 through 69 )
26X-RAY DIFFRACTION26chain 'E' and (resid 70 through 80 )
27X-RAY DIFFRACTION27chain 'E' and (resid 81 through 90 )
28X-RAY DIFFRACTION28chain 'E' and (resid 91 through 96 )
29X-RAY DIFFRACTION29chain 'E' and (resid 97 through 116 )
30X-RAY DIFFRACTION30chain 'C' and (resid 6 through 16 )
31X-RAY DIFFRACTION31chain 'C' and (resid 17 through 48 )
32X-RAY DIFFRACTION32chain 'C' and (resid 49 through 64 )
33X-RAY DIFFRACTION33chain 'C' and (resid 65 through 72 )
34X-RAY DIFFRACTION34chain 'C' and (resid 73 through 85 )
35X-RAY DIFFRACTION35chain 'C' and (resid 86 through 101 )
36X-RAY DIFFRACTION36chain 'F' and (resid 8 through 35 )
37X-RAY DIFFRACTION37chain 'F' and (resid 36 through 49 )
38X-RAY DIFFRACTION38chain 'F' and (resid 50 through 64 )
39X-RAY DIFFRACTION39chain 'F' and (resid 65 through 72 )
40X-RAY DIFFRACTION40chain 'F' and (resid 73 through 85 )
41X-RAY DIFFRACTION41chain 'F' and (resid 86 through 102 )

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