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- PDB-5dug: Crystal Structure of the ER-alpha Ligand-binding Domain in Comple... -

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Basic information

Entry
Database: PDB / ID: 5dug
TitleCrystal Structure of the ER-alpha Ligand-binding Domain in Complex with a Sulfoxide-bridged Oxabicyclic Heptene Sulfonate (SOBHS)-2 analog phenyl (1S,2S,4S,7S)-5,6-bis(4-hydroxy-2-methylphenyl)-7-thiabicyclo[2.2.1]hept-5-ene-2-sulfonate 7-oxide
Components
  • Estrogen receptor
  • Nuclear receptor coactivator 2
KeywordsTRANSCRIPTION / Nuclear receptor / transcription factor / ligand binding / protein-ligand complex
Function / homology
Function and homology information


regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / regulation of branching involved in prostate gland morphogenesis / RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / nuclear estrogen receptor activity / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis ...regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / regulation of branching involved in prostate gland morphogenesis / RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / nuclear estrogen receptor activity / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / epithelial cell proliferation involved in mammary gland duct elongation / prostate epithelial cord elongation / epithelial cell development / locomotor rhythm / negative regulation of smooth muscle cell apoptotic process / uterus development / mammary gland branching involved in pregnancy / vagina development / aryl hydrocarbon receptor binding / TFIIB-class transcription factor binding / cellular response to Thyroglobulin triiodothyronine / steroid hormone receptor signaling pathway / regulation of lipid metabolic process / androgen metabolic process / regulation of glucose metabolic process / Synthesis of bile acids and bile salts / cellular response to estrogen stimulus / mammary gland alveolus development / estrogen response element binding / Synthesis of bile acids and bile salts via 27-hydroxycholesterol / Endogenous sterols / Mitochondrial unfolded protein response (UPRmt) / Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / nuclear receptor-mediated steroid hormone signaling pathway / transcription regulator inhibitor activity / Nuclear signaling by ERBB4 / cellular response to hormone stimulus / Recycling of bile acids and salts / RNA polymerase II preinitiation complex assembly / protein localization to chromatin / estrogen receptor signaling pathway / negative regulation of canonical NF-kappaB signal transduction / positive regulation of adipose tissue development / steroid binding / : / 14-3-3 protein binding / Regulation of lipid metabolism by PPARalpha / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / peroxisome proliferator activated receptor signaling pathway / TBP-class protein binding / regulation of cellular response to insulin stimulus / nitric-oxide synthase regulator activity / positive regulation of nitric-oxide synthase activity / BMAL1:CLOCK,NPAS2 activates circadian expression / negative regulation of miRNA transcription / SUMOylation of transcription cofactors / Activation of gene expression by SREBF (SREBP) / ESR-mediated signaling / positive regulation of DNA-binding transcription factor activity / transcription coregulator binding / response to progesterone / transcription corepressor binding / nuclear receptor binding / nuclear estrogen receptor binding / negative regulation of smoothened signaling pathway / negative regulation of DNA-binding transcription factor activity / stem cell differentiation / SUMOylation of intracellular receptors / cellular response to estradiol stimulus / circadian regulation of gene expression / mRNA transcription by RNA polymerase II / Heme signaling / Transcriptional activation of mitochondrial biogenesis / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / transcription coactivator binding / euchromatin / PPARA activates gene expression / Cytoprotection by HMOX1 / beta-catenin binding / Nuclear Receptor transcription pathway / Transcriptional regulation of white adipocyte differentiation / RNA polymerase II transcription regulator complex / response to estrogen / nuclear receptor activity / positive regulation of fibroblast proliferation / male gonad development / Constitutive Signaling by Aberrant PI3K in Cancer / Regulation of RUNX2 expression and activity / sequence-specific double-stranded DNA binding / positive regulation of nitric oxide biosynthetic process / Ovarian tumor domain proteases / : / response to estradiol / PIP3 activates AKT signaling / HATs acetylate histones / ATPase binding / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / positive regulation of cytosolic calcium ion concentration / DNA-binding transcription activator activity, RNA polymerase II-specific / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
Similarity search - Function
Nuclear receptor coactivator 2 / Nuclear receptor coactivator 2/3, DUF4927 / Domain of unknown function (DUF4927) / Estrogen receptor / Oestrogen-type nuclear receptor final C-terminal domain / : / Oestrogen receptor / Oestrogen-type nuclear receptor final C-terminal / Estrogen receptor/oestrogen-related receptor / Nuclear receptor coactivator, DUF1518 ...Nuclear receptor coactivator 2 / Nuclear receptor coactivator 2/3, DUF4927 / Domain of unknown function (DUF4927) / Estrogen receptor / Oestrogen-type nuclear receptor final C-terminal domain / : / Oestrogen receptor / Oestrogen-type nuclear receptor final C-terminal / Estrogen receptor/oestrogen-related receptor / Nuclear receptor coactivator, DUF1518 / Nuclear receptor coactivator, Ncoa-type, interlocking / Nuclear receptor coactivator, Ncoa-type, interlocking domain superfamily / Nuclear receptor coactivator, DUF1518 / Nuclear receptor coactivator / DUF1518 / Nuclear receptor coactivator, receptor-binding domain / Nuclear receptor coactivator / : / Steroid receptor coactivator / Unstructured region on nuclear receptor coactivator protein / Nuclear receptor coactivators bHLH domain / : / PAS domain / Nuclear receptor coactivator, interlocking / helix loop helix domain / Myc-type, basic helix-loop-helix (bHLH) domain / Myc-type, basic helix-loop-helix (bHLH) domain profile. / Helix-loop-helix DNA-binding domain superfamily / PAS fold / PAS fold / PAS domain / PAS repeat profile. / PAS domain / Retinoid X Receptor / Retinoid X Receptor / PAS domain superfamily / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Double treble clef zinc finger, C4 type / Nuclear hormone receptors DNA-binding domain profile. / c4 zinc finger in nuclear hormone receptors / Nuclear hormone receptor, ligand-binding domain / Nuclear hormone receptor-like domain superfamily / Ligand-binding domain of nuclear hormone receptor / Nuclear receptor (NR) ligand-binding (LBD) domain profile. / Ligand binding domain of hormone receptors / Zinc finger, NHR/GATA-type / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Chem-5FV / Estrogen receptor / Nuclear receptor coactivator 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.252 Å
AuthorsNwachukwu, J.C. / Srinivasan, S. / Zheng, Y. / Wang, S. / Min, J. / Dong, C. / Liao, Z. / Cavett, V. / Nowak, J. / Houtman, R. ...Nwachukwu, J.C. / Srinivasan, S. / Zheng, Y. / Wang, S. / Min, J. / Dong, C. / Liao, Z. / Cavett, V. / Nowak, J. / Houtman, R. / Carlson, K.E. / Josan, J.S. / Elemento, O. / Katzenellenbogen, J.A. / Zhou, H.B. / Nettles, K.W.
CitationJournal: Mol.Syst.Biol. / Year: 2016
Title: Predictive features of ligand-specific signaling through the estrogen receptor.
Authors: Nwachukwu, J.C. / Srinivasan, S. / Zheng, Y. / Wang, S. / Min, J. / Dong, C. / Liao, Z. / Nowak, J. / Wright, N.J. / Houtman, R. / Carlson, K.E. / Josan, J.S. / Elemento, O. / ...Authors: Nwachukwu, J.C. / Srinivasan, S. / Zheng, Y. / Wang, S. / Min, J. / Dong, C. / Liao, Z. / Nowak, J. / Wright, N.J. / Houtman, R. / Carlson, K.E. / Josan, J.S. / Elemento, O. / Katzenellenbogen, J.A. / Zhou, H.B. / Nettles, K.W.
History
DepositionSep 18, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 4, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 27, 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_oper_list / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Estrogen receptor
B: Estrogen receptor
C: Nuclear receptor coactivator 2
D: Nuclear receptor coactivator 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)62,9266
Polymers61,9334
Non-polymers9932
Water2,486138
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5060 Å2
ΔGint-30 kcal/mol
Surface area19150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)54.140, 82.146, 58.354
Angle α, β, γ (deg.)90.000, 110.870, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A and (resseq 306:330 or resseq 336:458 or resseq 471:548 )
21chain B and (resseq 306:330 or resseq 336:458 or resseq 471:548 )

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11LEULEUGLUGLUchain A and (resseq 306:330 or resseq 336:458 or resseq 471:548 )AA306 - 3309 - 33
12PROPROVALVALchain A and (resseq 306:330 or resseq 336:458 or resseq 471:548 )AA336 - 45839 - 161
13GLUGLUARGARGchain A and (resseq 306:330 or resseq 336:458 or resseq 471:548 )AA471 - 548174 - 251
21LEULEUGLUGLUchain B and (resseq 306:330 or resseq 336:458 or resseq 471:548 )BB306 - 3309 - 33
22PROPROVALVALchain B and (resseq 306:330 or resseq 336:458 or resseq 471:548 )BB336 - 45839 - 161
23GLUGLUARGARGchain B and (resseq 306:330 or resseq 336:458 or resseq 471:548 )BB471 - 548174 - 251

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Components

#1: Protein Estrogen receptor / ER / ER-alpha / Estradiol receptor / Nuclear receptor subfamily 3 group A member 1


Mass: 29299.535 Da / Num. of mol.: 2 / Fragment: ligand-binding domain / Mutation: Y537S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ESR1, ESR, NR3A1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P03372
#2: Protein/peptide Nuclear receptor coactivator 2 / NCoA-2 / Class E basic helix-loop-helix protein 75 / bHLHe75 / Transcriptional intermediary factor 2 / hTIF2


Mass: 1666.943 Da / Num. of mol.: 2 / Fragment: Nuclear receptor-interacting peptide / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q15596
#3: Chemical ChemComp-5FV / phenyl (1S,2S,4S,7S)-5,6-bis(4-hydroxy-2-methylphenyl)-7-thiabicyclo[2.2.1]hept-5-ene-2-sulfonate 7-oxide


Mass: 496.595 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C26H24O6S2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 138 / 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: 1.96 Å3/Da / Density % sol: 37.35 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 8.3 / Details: 15% PEG 3350, 0.05M MgCl2, 0.067M NaCl, 0.1M Tris

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 8, 2011
RadiationMonochromator: Side scattering bent cube i-beam single crystal asymmetric cut 4.965 degs
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.252→50 Å / Num. obs: 22491 / % possible obs: 99.9 % / Redundancy: 3.8 % / Rmerge(I) obs: 0.072 / Χ2: 1.804 / Net I/av σ(I): 27.175 / Net I/σ(I): 10.7 / Num. measured all: 85500
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2% possible all
2.27-2.313.80.32711111.25999.8
2.31-2.353.80.24211451.231100
2.35-2.43.80.22810991.33899.9
2.4-2.453.80.19811071.30499.9
2.45-2.53.80.17111091.35100
2.5-2.563.80.17611501.34100
2.56-2.623.80.14610931.374100
2.62-2.693.80.13511231.582100
2.69-2.773.80.1211131.44799.9
2.77-2.863.80.11111191.442100
2.86-2.963.80.09711281.65599.9
2.96-3.083.80.0911231.786100
3.08-3.223.80.08511411.949100
3.22-3.393.80.07411142.0699.9
3.39-3.63.80.07111272.4299.9
3.6-3.883.70.06311362.59399.9
3.88-4.273.80.05711122.62399.9
4.27-4.893.80.05711362.64399.9
4.89-6.163.70.05511422.268100
6.16-503.60.04611632.48699.7

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Processing

Software
NameVersionClassification
HKL-2000data scaling
PHENIXrefinement
PDB_EXTRACT3.15data extraction
HKL-2000data reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2QA8

2qa8


Resolution: 2.252→46.185 Å / SU ML: 0.63 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 23.27 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2331 1937 8.91 %
Rwork0.189 19804 -
obs0.1929 21741 95.89 %
Solvent computationShrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 45.61 Å2 / ksol: 0.341 e/Å3
Displacement parametersBiso max: 159.39 Å2 / Biso mean: 44.7113 Å2 / Biso min: 7.52 Å2
Baniso -1Baniso -2Baniso -3
1--1.1869 Å20 Å22.2935 Å2
2--1.3436 Å20 Å2
3----0.1567 Å2
Refinement stepCycle: final / Resolution: 2.252→46.185 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3804 0 68 138 4010
Biso mean--46.14 37.64 -
Num. residues----487
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0043991
X-RAY DIFFRACTIONf_angle_d1.2825424
X-RAY DIFFRACTIONf_chiral_restr0.089645
X-RAY DIFFRACTIONf_plane_restr0.007671
X-RAY DIFFRACTIONf_dihedral_angle_d14.8151473
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A1707X-RAY DIFFRACTIONPOSITIONAL0.041
12B1707X-RAY DIFFRACTIONPOSITIONAL0.041
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.2523-2.30870.32481160.2341051116773
2.3087-2.37110.26461370.21691388152595
2.3711-2.44090.26161270.20791407153495
2.4409-2.51960.23291380.19361432157097
2.5196-2.60970.24621390.20311404154397
2.6097-2.71420.3171300.20971426155696
2.7142-2.83770.28591450.22081409155497
2.8377-2.98730.24221450.20451459160498
2.9873-3.17440.27191400.20811459159999
3.1744-3.41940.27731420.19141450159298
3.4194-3.76340.20681450.18031447159299
3.7634-4.30760.20281460.15861465161199
4.3076-5.42580.18271450.158914941639100
5.4258-46.19490.2151420.19581513165599
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)
13.56550.98110.78381.45860.59791.74570.2616-0.68030.50710.5657-0.2969-0.022-0.35340.59780.14260.2731-0.1287-0.0070.3779-0.0770.2135-4.8747-12.57386.6302
20.211-0.03370.07833.8332.78072.06410.9842-0.077-0.27470.4520.04220.07571.65750.1843-0.25271.0786-0.21920.06460.6144-0.28790.6138-26.3816-37.02417.845
36.21063.73361.57712.81032.20375.7127-0.1442-0.0082-0.2872-0.25670.1496-0.0903-0.0906-0.6038-0.05210.1485-0.05430.02280.20080.00910.1399-23.7072-27.82860.138
43.2395-0.28140.37214.5116-0.4643.08160.1588-0.21060.5120.2848-0.02680.0004-0.5886-0.0189-0.02310.24290.00250.06130.1641-0.03520.2437-13.2611-12.5236-3.3137
51.0148-1.53530.81632.3253-1.15431.15720.16020.0504-0.5286-0.1108-0.3285-0.30450.33480.2547-0.45590.37980.13650.01880.30650.14960.4488-5.4528-34.30422.4223
63.0542-1.2268-0.8913.2107-0.74793.4677-0.04340.1489-0.56740.11080.22820.16871.5015-0.2324-0.20620.4055-0.05140.03320.18740.04240.3547-16.6203-36.8003-1.5703
72.2662.58672.39034.96231.57996.21520.0829-0.0976-1.102-0.2066-0.039-0.28050.90480.2867-0.0370.29870.06470.01170.2025-0.01240.2848-5.4506-31.9473-6.1117
85.4313-0.74970.75415.7535-0.79835.7350.29230.23750.5946-0.149-0.4677-0.0935-0.44710.75840.16550.121-0.03490.05420.1567-0.04350.1283-4.6939-14.2733-5.4092
96.4977-1.13761.07080.5187-0.35114.47710.3833-0.17920.71540.1771-0.1987-0.1611-1.13150.92610.23340.0148-0.2116-0.11750.461-0.07610.16216.9742-11.8266-4.2833
103.52040.41570.08792.20610.41132.94280.2915-0.3028-0.4825-0.103-0.1788-0.2080.25170.3636-0.08790.15320.0009-0.02110.23370.01120.1576-1.2852-22.5094-10.6895
116.4082-0.34080.62192.83422.19513.41490.30820.8005-1.3310.6816-0.65640.20690.6727-1.06450.01030.2184-0.2919-0.19160.6175-0.14880.302-24.4232-26.7152-14.0522
126.79752.5019-2.49365.0999-1.06017.15750.2510.330.7722-0.2558-0.340.991-0.5537-0.4309-0.00280.0560.0259-0.10250.26690.0480.2582-26.3944-18.4169-8.6584
137.247-0.98643.07063.10.28344.68710.08890.0446-0.1946-0.1775-0.0075-0.56150.4861.1649-0.00250.30810.05990.07060.74290.03960.363812.2053-21.4257-30.4301
149.3435-2.2798-2.6122.70550.88333.9230.02270.2976-0.90860.4111-0.35310.3962-0.2001-0.029-0.64091.09510.03360.13141.41930.24850.5133-14.1581-10.6858-47.7797
151.30810.3340.22341.8257-0.69770.37980.03690.5214-0.0344-0.73440.30160.55720.2256-1.38430.02020.3972-0.0526-0.07830.8360.08710.2608-14.4494-18.9712-40.2374
165.82292.84751.15034.2150.51787.0336-0.3150.196-0.6268-0.79240.1306-0.76451.18090.5950.13340.38090.06530.09420.37850.00190.32652.2985-26.5002-35.3334
173.96850.5728-0.02722.67941.40642.88720.0627-0.0945-0.5474-0.158-0.3134-0.27140.63520.31640.08450.32980.08590.01570.28390.05150.21880.3582-25.8394-27.255
185.5395-1.8938-5.51414.39881.55276.64560.01241.0666-0.0348-0.6733-0.40460.1794-1.2679-0.77280.15540.35770.0301-0.04070.31580.03940.191-6.1081-7.8491-37.1236
195.5646-0.09160.55425.1837-0.49394.96120.04850.25150.1308-0.36590.19110.5751-0.7379-0.9725-0.14630.44640.1250.02030.46260.09030.2786-13.0587-9.2947-28.7873
204.6525-0.190.88468.1009-0.28285.1703-0.1495-0.13060.15230.15570.1522-0.00520.0740.6830.10940.22810.01380.00490.35320.00810.15044.4309-18.5856-21.969
212.9883.17611.046.82232.51894.6010.07620.08220.00210.1725-0.1084-0.77240.01721.5248-0.45570.2576-0.0691-0.01370.69040.05760.340112.8167-18.1364-14.9574
225.40831.47711.40341.48870.46226.76240.0258-0.18780.3274-0.0783-0.08220.1386-0.5140.15310.07890.23140.00490.01350.20920.00340.1606-2.0508-15.1556-17.2536
231.9632.86992.24335.8452.32084.2726-0.66221.03030.2-0.7264-0.28521.26220.344-1.91290.40450.3776-0.1516-0.08521.068-0.03570.4688-19.1179-24.0513-28.8933
248.5223-1.4191.36654.2685-0.47053.5036-0.3388-0.0835-0.3560.3153-0.12550.88080.3339-1.76670.31380.6335-0.16960.00230.6017-0.12380.5191-13.9637-30.2112-33.5024
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 305:329)A305 - 329
2X-RAY DIFFRACTION2(chain A and resid 330:336)A330 - 336
3X-RAY DIFFRACTION3(chain A and resid 337:356)A337 - 356
4X-RAY DIFFRACTION4(chain A and resid 357:394)A357 - 394
5X-RAY DIFFRACTION5(chain A and resid 395:400)A395 - 400
6X-RAY DIFFRACTION6(chain A and resid 401:420)A401 - 420
7X-RAY DIFFRACTION7(chain A and resid 421:439)A421 - 439
8X-RAY DIFFRACTION8(chain A and resid 440:471)A440 - 471
9X-RAY DIFFRACTION9(chain A and resid 472:501)A472 - 501
10X-RAY DIFFRACTION10(chain A and resid 502:518)A502 - 518
11X-RAY DIFFRACTION11(chain A and resid 519:533)A519 - 533
12X-RAY DIFFRACTION12(chain A and resid 534:548)A534 - 548
13X-RAY DIFFRACTION13(chain B and resid 305:329)B305 - 329
14X-RAY DIFFRACTION14(chain B and resid 330:337)B330 - 337
15X-RAY DIFFRACTION15(chain B and resid 338:351)B338 - 351
16X-RAY DIFFRACTION16(chain B and resid 352:363)B352 - 363
17X-RAY DIFFRACTION17(chain B and resid 364:396)B364 - 396
18X-RAY DIFFRACTION18(chain B and resid 397:410)B397 - 410
19X-RAY DIFFRACTION19(chain B and resid 411:435)B411 - 435
20X-RAY DIFFRACTION20(chain B and resid 436:471)B436 - 471
21X-RAY DIFFRACTION21(chain B and resid 472:501)B472 - 501
22X-RAY DIFFRACTION22(chain B and resid 502:519)B502 - 519
23X-RAY DIFFRACTION23(chain B and resid 520:531)B520 - 531
24X-RAY DIFFRACTION24(chain B and resid 532:549)B532 - 549

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