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- PDB-5krh: Crystal Structure of the ER-alpha Ligand-binding Domain (Y537S) i... -

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Basic information

Entry
Database: PDB / ID: 5krh
TitleCrystal Structure of the ER-alpha Ligand-binding Domain (Y537S) in Complex with 16-benzylidene estrone
Components
  • Estrogen receptor
  • NCOA2
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 / RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding / regulation of branching involved in prostate gland morphogenesis / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / nuclear estrogen receptor activity ...regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding / regulation of branching involved in prostate gland morphogenesis / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / nuclear estrogen receptor activity / epithelial cell proliferation involved in mammary gland duct elongation / epithelial cell development / prostate epithelial cord elongation / locomotor rhythm / negative regulation of smooth muscle cell apoptotic process / mammary gland branching involved in pregnancy / uterus development / vagina development / aryl hydrocarbon receptor binding / TFIIB-class transcription factor binding / regulation of lipid metabolic process / androgen metabolic process / steroid hormone receptor signaling pathway / cellular response to Thyroglobulin triiodothyronine / regulation of glucose metabolic process / Synthesis of bile acids and bile salts / mammary gland alveolus development / estrogen receptor signaling pathway / cellular response to estrogen stimulus / Endogenous sterols / Synthesis of bile acids and bile salts via 27-hydroxycholesterol / estrogen response element binding / Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / : / nuclear receptor-mediated steroid hormone signaling pathway / negative regulation of canonical NF-kappaB signal transduction / Nuclear signaling by ERBB4 / RNA polymerase II preinitiation complex assembly / regulation of cellular response to insulin stimulus / Recycling of bile acids and salts / cellular response to hormone stimulus / protein localization to chromatin / 14-3-3 protein binding / positive regulation of adipose tissue development / peroxisome proliferator activated receptor signaling pathway / RORA activates gene expression / TBP-class protein binding / nitric-oxide synthase regulator activity / steroid binding / Regulation of lipid metabolism by PPARalpha / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / ESR-mediated signaling / transcription corepressor binding / BMAL1:CLOCK,NPAS2 activates circadian gene expression / negative regulation of miRNA transcription / SUMOylation of transcription cofactors / Activation of gene expression by SREBF (SREBP) / nuclear receptor coactivator activity / positive regulation of nitric-oxide synthase activity / cellular response to estradiol stimulus / transcription coregulator binding / response to progesterone / stem cell differentiation / nuclear estrogen receptor binding / nuclear receptor binding / circadian regulation of gene expression / Heme signaling / SUMOylation of intracellular receptors / euchromatin / mRNA transcription by RNA polymerase II / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Transcriptional activation of mitochondrial biogenesis / negative regulation of DNA-binding transcription factor activity / PPARA activates gene expression / Cytoprotection by HMOX1 / beta-catenin binding / transcription coactivator binding / positive regulation of DNA-binding transcription factor activity / Transcriptional regulation of white adipocyte differentiation / Nuclear Receptor transcription pathway / response to estrogen / RNA polymerase II transcription regulator complex / Regulation of RUNX2 expression and activity / Constitutive Signaling by Aberrant PI3K in Cancer / nuclear receptor activity / male gonad development / positive regulation of nitric oxide biosynthetic process / sequence-specific double-stranded DNA binding / positive regulation of fibroblast proliferation / Ovarian tumor domain proteases / Circadian Clock / PIP3 activates AKT signaling / response to estradiol / phospholipase C-activating G protein-coupled receptor signaling pathway / HATs acetylate histones / positive regulation of cytosolic calcium ion concentration / ATPase binding / regulation of inflammatory response / fibroblast proliferation / 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 / PAS domain / Nuclear receptor coactivator, interlocking / Helix-loop-helix DNA-binding domain superfamily / helix loop helix domain / Myc-type, basic helix-loop-helix (bHLH) domain / Myc-type, basic helix-loop-helix (bHLH) domain profile. / PAS fold / PAS fold / PAS domain / PAS repeat profile. / PAS domain / PAS domain superfamily / Retinoid X Receptor / Retinoid X Receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Zinc finger, C4 type (two domains) / 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-6WN / Estrogen receptor / Nuclear receptor coactivator 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.243 Å
AuthorsNwachukwu, J.C. / Srinivasan, S. / Bruno, N.E. / Nowak, J. / Kojetin, D.J. / Elemento, O. / Katzenellenbogen, J.A. / Nettles, K.W.
CitationJournal: Cell Chem Biol / Year: 2017
Title: Systems Structural Biology Analysis of Ligand Effects on ER alpha Predicts Cellular Response to Environmental Estrogens and Anti-hormone Therapies.
Authors: Nwachukwu, J.C. / Srinivasan, S. / Bruno, N.E. / Nowak, J. / Wright, N.J. / Minutolo, F. / Rangarajan, E.S. / Izard, T. / Yao, X.Q. / Grant, B.J. / Kojetin, D.J. / Elemento, O. / ...Authors: Nwachukwu, J.C. / Srinivasan, S. / Bruno, N.E. / Nowak, J. / Wright, N.J. / Minutolo, F. / Rangarajan, E.S. / Izard, T. / Yao, X.Q. / Grant, B.J. / Kojetin, D.J. / Elemento, O. / Katzenellenbogen, J.A. / Nettles, K.W.
History
DepositionJul 7, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 15, 2017Provider: repository / Type: Initial release
Revision 1.1Mar 6, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / entity / pdbx_entity_nonpoly
Item: _chem_comp.name / _database_2.pdbx_DOI ..._chem_comp.name / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.pdbx_description / _pdbx_entity_nonpoly.name

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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: NCOA2
D: NCOA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)62,6506
Polymers61,9334
Non-polymers7172
Water1,76598
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5120 Å2
ΔGint-30 kcal/mol
Surface area20580 Å2
MethodPISA
Unit cell
Length a, b, c (Å)55.530, 81.903, 58.665
Angle α, β, γ (deg.)90.00, 110.67, 90.00
Int Tables number4
Space group name H-MP1211

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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 NCOA2


Mass: 1666.943 Da / Num. of mol.: 2 / Fragment: Nuclear receptor-interacting peptide / Source method: obtained synthetically / Details: This sequence occurs naturally in humans / Source: (synth.) Homo sapiens (human) / References: UniProt: Q15596*PLUS
#3: Chemical ChemComp-6WN / (8~{R},9~{S},13~{S},14~{S},16~{E})-13-methyl-3-oxidanyl-16-(phenylmethylidene)-6,7,8,9,11,12,14,15-octahydrocyclopenta[ a]phenanthren-17-one / 16-benzylidene estrone


Mass: 358.473 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C25H26O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 98 / 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: 2.02 Å3/Da / Density % sol: 39.14 % / Mosaicity: 0.713 °
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 27, 2012
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: 2.24→50 Å / Num. obs: 23260 / % possible obs: 98.6 % / Redundancy: 6.8 % / Rmerge(I) obs: 0.139 / Χ2: 1.261 / Net I/av σ(I): 18.939 / Net I/σ(I): 4.4 / Num. measured all: 158488
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsDiffraction-ID% possible all
2.24-2.286.90.983199.4
2.28-2.326.90.85198.6
2.32-2.366.90.752199.4
2.36-2.416.90.665199.2
2.41-2.476.90.552199
2.47-2.526.80.507199.3
2.52-2.596.80.431199.2
2.59-2.666.80.378198.5
2.66-2.736.60.331198.2
2.73-2.8260.272195.6
2.82-2.9270.238199.2
2.92-3.047.20.199199.4
3.04-3.187.10.179199.5
3.18-3.3570.162199.1
3.35-3.566.90.147199.2
3.56-3.836.70.131199.3
3.83-4.226.10.119194.8
4.22-4.827.20.11199.5
4.82-6.0870.107199
6.08-506.50.092196.9

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Processing

Software
NameVersionClassification
PHENIX1.9_1690refinement
HKL-2000data scaling
PDB_EXTRACT3.2data extraction
HKL-2000data reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.243→46.89 Å / SU ML: 0.31 / Cross valid method: THROUGHOUT / σ(F): 0 / Phase error: 28.83 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2433 1840 8.49 %
Rwork0.206 --
obs0.2092 21665 91.61 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.243→46.89 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3788 0 54 98 3940
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0063934
X-RAY DIFFRACTIONf_angle_d0.9155339
X-RAY DIFFRACTIONf_dihedral_angle_d13.2951439
X-RAY DIFFRACTIONf_chiral_restr0.044640
X-RAY DIFFRACTIONf_plane_restr0.004657
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2427-2.30330.3411990.32231250X-RAY DIFFRACTION74
2.3033-2.37110.2851380.26221376X-RAY DIFFRACTION85
2.3711-2.44760.28881260.25721451X-RAY DIFFRACTION86
2.4476-2.53510.30521370.24541489X-RAY DIFFRACTION89
2.5351-2.63660.29731380.23471476X-RAY DIFFRACTION90
2.6366-2.75650.27471370.24171519X-RAY DIFFRACTION91
2.7565-2.90190.2981540.24241514X-RAY DIFFRACTION92
2.9019-3.08360.30541520.23351600X-RAY DIFFRACTION97
3.0836-3.32170.27431430.22431608X-RAY DIFFRACTION97
3.3217-3.65580.27051600.20561646X-RAY DIFFRACTION98
3.6558-4.18450.2111470.17511584X-RAY DIFFRACTION95
4.1845-5.27090.17261550.16321651X-RAY DIFFRACTION99
5.2709-46.90010.22741540.19291661X-RAY DIFFRACTION97
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)
10.83950.55790.11711.1669-0.34130.59530.6303-0.49290.56210.6034-0.35270.2223-0.43580.36720.130.668-0.2009-0.0690.5956-0.03660.4316-3.2737-6.99915.4608
20.473-0.0639-0.61790.20580.21130.8945-0.2232-0.2665-0.25470.0565-0.3173-0.16940.6996-0.5095-0.11750.3175-0.13050.02880.8034-0.07660.4735-21.7422-27.75719.4093
30.0997-0.0596-0.190.06740.20480.9211-0.1220.1987-0.18210.10560.1428-0.239-0.16990.15450.02311.20220.1379-0.21611.2133-0.3571.8785-25.2679-39.63775.2707
40.01250.00560.01030.12850.10430.2038-0.18250.1861-0.2131-0.2617-0.0078-0.3812-0.03950.0735-0.0030.6089-0.05930.04280.51040.05460.6926-26.6065-34.4217-3.0666
50.03770.01070.00610.0197-0.00830.0050.1184-0.4673-0.17440.00920.0411-0.1980.00270.0469-0.00050.428-0.0389-0.0310.36990.04970.4431-22.1484-21.27391.9069
60.25310.12210.13630.06990.05440.1281-0.2261-0.46550.80560.101-0.4248-0.2271-0.6116-0.15920.00390.7341-0.0469-0.01240.4032-0.07990.6817-13.6735-5.09610.1534
70.6259-0.1654-0.41951.14680.11280.58990.14970.2759-0.1372-0.097-0.18970.6185-0.26410.0146-0.02750.3694-0.02380.09160.28430.0030.352-13.7799-16.9178-4.8569
80.27880.05140.68520.01290.14511.747-0.2202-0.31580.2276-0.18780.2384-0.19520.3182-0.69950.00940.50530.01290.1710.34510.0630.5505-12.4438-33.15463.7116
90.3207-0.1236-0.1730.06990.05670.104-0.30530.1261-0.17850.36180.32880.19510.1043-0.013-0.00421.0805-0.20620.06220.6271-0.05221.493-18.6523-39.2579-6.7528
100.0217-0.0161-0.00810.0255-0.00010.0043-0.22170.2968-0.1601-0.4775-0.1069-0.1795-0.02430.0759-00.9515-0.0152-0.00330.5517-0.08680.512-14.6448-34.3613-9.7457
110.9390.0539-0.66350.06770.24961.74120.1976-0.2812-0.15840.28130.1918-0.1870.06770.55370.04440.69380.02750.10490.39090.01990.4404-5.0807-30.6167-6.7158
120.0124-0.01070.00530.04110.02430.03120.1681-0.12670.35680.23610.1787-0.21490.338-0.5186-0.00180.65960.057-0.13630.61410.14940.55071.9431-29.3382-2.6687
130.52830.2595-0.50760.2041-0.22170.44380.1983-0.05340.22950.1122-0.13240.147-0.36530.73810.00520.4252-0.10350.0230.36480.04140.3063-4.0288-15.5586-2.8851
140.3491-0.53440.40310.8805-0.65190.4819-0.5810.58320.1584-0.4279-0.1913-0.5004-0.64820.0275-0.10051.4066-0.180.23980.8135-0.2820.9346-9.559-3.5033-13.9276
150.0163-0.02480.00390.0325-0.00490.00190.51190.5504-0.0251-0.70810.33510.1951-0.45520.0303-0.00070.6007-0.06270.05780.4566-0.02610.5428-3.1264-3.3475-9.1185
161.5314-1.89780.09292.3606-0.10180.05260.5896-0.34340.0974-0.0734-0.514-0.0302-0.11040.05760.07130.5162-0.2342-0.08610.5790.07350.40627.3966-12.0758-1.0573
170.0589-0.0625-0.08040.07110.08790.14810.0988-0.1074-0.4430.3568-0.0576-0.1693-0.14350.265300.53810.0065-0.0360.49820.05470.39587.2497-19.1948-8.2897
180.0351-0.0337-0.03430.0409-0.00340.06870.15670.14030.5356-0.2848-0.00550.1163-0.5836-0.08360.00080.3978-0.07120.04920.2977-0.04680.366-9.6928-23.0738-13.4827
190.01890.01040.02960.11650.01760.03260.54820.9012-0.7633-0.71540.2176-0.07210.3638-0.11310.00270.5504-0.0888-0.15540.5365-0.04960.5762-22.9365-26.0332-14.1654
200.4149-0.31-0.60617.8752.97751.79610.0860.3685-0.20071.0228-0.24681.62940.7677-0.62120.02390.2882-0.05880.03740.5242-0.0280.5653-28.8791-20.5063-9.4238
210.1104-0.1410.05610.1761-0.070.0213-0.1005-0.01460.1040.0109-0.0233-0.12710.04880.09270.24820.25410.3949-0.87861.32140.25690.360918.603-26.7475-22.023
220.08250.03270.02730.99890.6670.4964-0.11680.3437-0.0828-0.4392-0.1446-0.1577-0.40450.3001-0.11930.3243-0.05180.0110.61090.08640.45628.8289-18.0567-33.8451
230.36140.2751-0.28120.28190.00520.8570.1513-0.0471-0.3699-0.005-0.0557-0.2070.0644-0.29350.0590.43950.1077-0.07720.87590.19260.8811-15.3733-10.9937-48.7715
241.9796-0.7712.26422.006-1.4022.749-0.0366-0.20470.430.01340.04060.6115-0.0889-0.46340.1841-0.08030.0522-0.21411.17650.09840.6527-20.2268-15.148-40.1667
251.004-0.03790.00470.5875-0.54750.8316-0.3747-0.013-0.4298-0.05770.1875-0.14640.5698-0.057-0.10.43970.05760.03860.334-0.00860.4660.3986-27.151-33.4797
260.3018-0.0457-0.09650.31510.49810.72770.0595-0.0531-0.3917-0.0705-0.26740.17750.2420.103800.40780.04730.00020.3502-0.01020.3622-3.037-21.5858-27.9837
270.0932-0.09990.0210.1493-0.08070.057-0.54630.040.24870.39650.4247-0.2306-1.33950.20670.00080.6458-0.0368-0.08350.52170.01440.4676-5.8249-6.4855-36.4136
280.10970.1085-0.20930.9307-0.07280.9454-0.1029-0.1880.41170.00410.01550.3441-0.5754-0.4011-0.04580.42310.1334-0.07270.85170.01940.6854-13.1443-5.5965-36.7912
290.02750.034-0.01450.0482-0.03760.03580.21050.0424-0.38340.22140.17880.2477-0.0016-0.2175-0.00111.4310.1930.00981.2580.2221.379-20.854-10.4013-33.6846
300.0098-0.00260.01750.0369-0.01670.03080.06610.0126-0.14810.14520.16670.13990.3109-0.60460.00140.89250.20920.14770.82880.16860.6302-16.9099-11.068-28.3054
310.0471-0.02520.14310.11260.07680.6236-0.2328-0.3059-0.11460.10790.1825-0.2755-0.7186-0.19280.01740.60410.1722-0.02830.3220.02540.428-8.9898-7.4748-25.1768
321.3826-0.74850.86690.4089-0.47450.5493-0.91630.10460.3369-0.1982-0.5026-0.001-0.47310.1945-0.10550.89490.13210.10420.42010.00560.5593-0.9303-3.6216-22.9927
330.6922-0.1499-0.30324.82251.98121.03190.1879-0.0933-0.07520.7532-0.38940.60.30610.7007-0.30410.2312-0.0074-0.0820.39380.05010.27384.5035-16.8075-23.1536
342.17920.31581.92180.83260.37451.76230.202-0.0948-0.38620.10330.59610.16260.3676-0.12840.31361.42040.13560.32791.46280.04961.36210.4941-38.3298-12.9533
350.52420.67341.2022.89151.26733.311-0.0941-0.2893-0.45790.21250.16880.96370.5545-0.5208-0.16731.04510.1973-0.05020.88610.09090.76627.6156-34.9527-15.576
362.9213-1.662-1.47147.6126-1.73033.5943-0.7552-0.19940.1920.468-0.1106-1.01380.32290.7879-0.80780.24680.0545-0.01990.5410.02910.293610.1266-25.5515-15.9723
371.39360.1441-0.36883.52010.3990.35810.17-0.52790.14610.6152-0.36160.1404-0.17110.7125-0.89330.3512-0.1651-0.1350.58050.10090.27639.9813-9.6254-14.8688
380.22740.0587-0.48540.0295-0.14071.015-0.6174-0.18910.25960.47340.4130.176-0.196-0.6370.00750.41810.07570.01550.2893-0.04480.3564-10.0887-18.5577-21.0521
390.8935-0.2056-0.01220.06930.10871.483-0.96690.21770.81140.0752-0.25590.39780.4769-0.4164-0.17250.5433-0.198-0.04930.9716-0.12670.6289-21.2882-24.9464-33.3955
400.2327-0.5517-0.02061.29940.08350.0397-0.29750.6535-0.53390.25020.48190.3390.5024-0.2659-0.00880.4457-0.13560.06350.5349-0.07270.568-12.7505-31.2226-30.7839
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 305:325)A305 - 325
2X-RAY DIFFRACTION2(chain A and resid 326:331)A326 - 331
3X-RAY DIFFRACTION3(chain A and resid 332:337)A332 - 337
4X-RAY DIFFRACTION4(chain A and resid 338:344)A338 - 344
5X-RAY DIFFRACTION5(chain A and resid 345:357)A345 - 357
6X-RAY DIFFRACTION6(chain A and resid 358:372)A358 - 372
7X-RAY DIFFRACTION7(chain A and resid 373:396)A373 - 396
8X-RAY DIFFRACTION8(chain A and resid 397:410)A397 - 410
9X-RAY DIFFRACTION9(chain A and resid 411:420)A411 - 420
10X-RAY DIFFRACTION10(chain A and resid 421:426)A421 - 426
11X-RAY DIFFRACTION11(chain A and resid 427:434)A427 - 434
12X-RAY DIFFRACTION12(chain A and resid 435:438)A435 - 438
13X-RAY DIFFRACTION13(chain A and resid 439:458)A439 - 458
14X-RAY DIFFRACTION14(chain A and resid 459:474)A459 - 474
15X-RAY DIFFRACTION15(chain A and resid 475:479)A475 - 479
16X-RAY DIFFRACTION16(chain A and resid 480:496)A480 - 496
17X-RAY DIFFRACTION17(chain A and resid 497:511)A497 - 511
18X-RAY DIFFRACTION18(chain A and resid 512:519)A512 - 519
19X-RAY DIFFRACTION19(chain A and resid 520:528)A520 - 528
20X-RAY DIFFRACTION20(chain A and resid 529:548)A529 - 548
21X-RAY DIFFRACTION21(chain B and resid 305:312)B305 - 312
22X-RAY DIFFRACTION22(chain B and resid 313:329)B313 - 329
23X-RAY DIFFRACTION23(chain B and resid 330:337)B330 - 337
24X-RAY DIFFRACTION24(chain B and resid 338:343)B338 - 343
25X-RAY DIFFRACTION25(chain B and resid 344:373)B344 - 373
26X-RAY DIFFRACTION26(chain B and resid 374:396)B374 - 396
27X-RAY DIFFRACTION27(chain B and resid 397:407)B397 - 407
28X-RAY DIFFRACTION28(chain B and resid 408:413)B408 - 413
29X-RAY DIFFRACTION29(chain B and resid 414:420)B414 - 420
30X-RAY DIFFRACTION30(chain B and resid 421:425)B421 - 425
31X-RAY DIFFRACTION31(chain B and resid 426:433)B426 - 433
32X-RAY DIFFRACTION32(chain B and resid 434:437)B434 - 437
33X-RAY DIFFRACTION33(chain B and resid 438:458)B438 - 458
34X-RAY DIFFRACTION34(chain B and resid 459:469)B459 - 469
35X-RAY DIFFRACTION35(chain B and resid 470:474)B470 - 474
36X-RAY DIFFRACTION36(chain B and resid 475:483)B475 - 483
37X-RAY DIFFRACTION37(chain B and resid 484:510)B484 - 510
38X-RAY DIFFRACTION38(chain B and resid 511:522)B511 - 522
39X-RAY DIFFRACTION39(chain B and resid 523:536)B523 - 536
40X-RAY DIFFRACTION40(chain B and resid 537:548)B537 - 548

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