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- PDB-4ivw: Crystal Structure of the Estrogen Receptor alpha Ligand-binding D... -

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Basic information

Entry
Database: PDB / ID: 4ivw
TitleCrystal Structure of the Estrogen Receptor alpha Ligand-binding Domain in Complex with Constrained WAY-derivative, 6b
Components
  • Estrogen receptor
  • Nuclear receptor coactivator 2
KeywordsTRANSCRIPTION / Nuclear hormone receptor / Transcription factor / Ligand-binding / Nucleus
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 / Regulation of lipid metabolism by PPARalpha / steroid binding / 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 receptor binding / nuclear estrogen 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 / regulation of inflammatory response / positive regulation of cytosolic calcium ion concentration / fibroblast proliferation / ATPase binding / 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-1GJ / Estrogen receptor / Nuclear receptor coactivator 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.06 Å
AuthorsNwachukwu, J.C. / Srinivasan, S. / Parent, A.A. / Cavett, V. / Nowak, J. / Hughes, T.S. / Kojetin, D.J. / Katzenellenbogen, J.A. / Nettles, K.W.
CitationJournal: Nat.Chem.Biol. / Year: 2013
Title: Ligand binding dynamics rewire cellular signaling via Estrogen Receptor-alpha
Authors: Srinivasan, S. / Nwachukwu, J.C. / Parent, A.A. / Cavett, V. / Nowak, J. / Hughes, T.S. / Kojetin, D.J. / Katzenellenbogen, J.A. / Nettles, K.W.
History
DepositionJan 23, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 27, 2013Provider: repository / Type: Initial release
Revision 1.1Jun 26, 2013Group: Database references
Revision 1.2Nov 15, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3Feb 26, 2020Group: Data collection / Database references / Category: reflns_shell / struct_ref_seq_dif
Item: _reflns_shell.pdbx_Rsym_value / _struct_ref_seq_dif.details
Revision 1.4Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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: Estrogen receptor
C: Nuclear receptor coactivator 2
B: Estrogen receptor
D: Nuclear receptor coactivator 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,7006
Polymers58,9324
Non-polymers7692
Water2,486138
1
A: Estrogen receptor
C: Nuclear receptor coactivator 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,8503
Polymers29,4662
Non-polymers3841
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1020 Å2
ΔGint-8 kcal/mol
Surface area11950 Å2
MethodPISA
2
B: Estrogen receptor
D: Nuclear receptor coactivator 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,8503
Polymers29,4662
Non-polymers3841
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area990 Å2
ΔGint-8 kcal/mol
Surface area11670 Å2
MethodPISA
3


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5280 Å2
ΔGint-26 kcal/mol
Surface area20360 Å2
MethodPISA
Unit cell
Length a, b, c (Å)54.480, 81.400, 58.602
Angle α, β, γ (deg.)90.00, 109.82, 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: 28189.229 Da / Num. of mol.: 2 / Fragment: Ligand-binding Domain, UNP residues 303-549 / Mutation: Y537S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ESR, ESR1, NR3A1 / Production host: Escherichia coli (E. coli) / 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: 1276.530 Da / Num. of mol.: 2
Fragment: Receptor-interacting peptide, UNP residues 687-696
Source method: obtained synthetically / Details: This sequence occurs naturally in humans / Source: (synth.) Homo sapiens (human) / References: UniProt: Q15596
#3: Chemical ChemComp-1GJ / 4-[2-benzyl-7-(trifluoromethyl)-2H-indazol-3-yl]benzene-1,3-diol


Mass: 384.351 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H15F3N2O2
#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: 2.07 Å3/Da / Density % sol: 40.7 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 8.3
Details: 15% PEG 3350, 0.05M magnesium chloride, 0.067M sodium chloride, 0.1M Tris, pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 294K

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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: 2.06→50 Å / Num. all: 29295 / Num. obs: 29295 / % possible obs: 97.16 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 6.5 % / Biso Wilson estimate: 37.59 Å2 / Rsym value: 0.114 / Net I/σ(I): 15.19
Reflection shellResolution: 2.06→2.1 Å / Redundancy: 6.2 % / Mean I/σ(I) obs: 2.36 / % possible all: 90.58

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Processing

Software
NameVersionClassification
Blu-Iceicedata collection
PHENIX(phenix.automr)model building
PHENIX(phenix.refine: 1.7.1_743)refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.06→46.141 Å / SU ML: 0.46 / σ(F): 0 / Phase error: 24.09 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2295 1906 6.81 %Random
Rwork0.1846 ---
all0.1876 27983 --
obs0.1876 27983 92.81 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 45.233 Å2 / ksol: 0.317 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--1.2459 Å20 Å23.0084 Å2
2--3.6704 Å2-0 Å2
3----2.4245 Å2
Refinement stepCycle: LAST / Resolution: 2.06→46.141 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3843 0 56 138 4037
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0054025
X-RAY DIFFRACTIONf_angle_d0.7875467
X-RAY DIFFRACTIONf_dihedral_angle_d14.5051502
X-RAY DIFFRACTIONf_chiral_restr0.053643
X-RAY DIFFRACTIONf_plane_restr0.003679
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.06-2.10420.36261090.25711528X-RAY DIFFRACTION76
2.1042-2.16110.26171270.21891698X-RAY DIFFRACTION86
2.1611-2.22470.25891280.20351720X-RAY DIFFRACTION86
2.2247-2.29650.23791290.19871843X-RAY DIFFRACTION93
2.2965-2.37860.25871340.20611885X-RAY DIFFRACTION93
2.3786-2.47380.24531420.20311875X-RAY DIFFRACTION94
2.4738-2.58640.28981480.20551902X-RAY DIFFRACTION96
2.5864-2.72270.26581400.21131919X-RAY DIFFRACTION95
2.7227-2.89330.24881350.2131879X-RAY DIFFRACTION94
2.8933-3.11660.23791450.19971964X-RAY DIFFRACTION98
3.1166-3.43020.27491420.1941972X-RAY DIFFRACTION98
3.4302-3.92630.21821430.16581943X-RAY DIFFRACTION97
3.9263-4.94580.17411360.14431941X-RAY DIFFRACTION95
4.9458-46.1410.20521480.18292008X-RAY DIFFRACTION98
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)
15.56932.1902-0.69221.8982.01577.9034-0.9351-0.49760.04010.4177-0.055-0.3273-1.55340.87031.20970.74770.0546-0.09210.51220.04320.87673.619827.81480.6623
25.4838-4.5068-1.92454.05951.58681.07280.79051.11150.9883-0.9738-0.775-0.4071-0.286-0.3771-0.00120.42380.0474-0.03810.48880.0660.34133.90214.1829-6.564
38.2117-2.9181-1.76997.22821.25815.9789-0.0031.6733-0.6832-1.129-0.9514-0.29580.99510.78290.26610.81050.17570.16290.599-0.05260.340221.0551-4.1016-9.9843
49.1810.1995-0.21014.93963.49883.33372.13091.4537-0.1747-0.1920.8963-0.42470.3928-0.5894-2.46590.88410.14630.01630.63060.03520.980724.9606-15.1274-1.4967
59.542-6.67853.93766.7353-3.4146.0045-0.05790.137-0.2907-0.56440.21780.26490.01020.4628-0.21960.25580.0267-0.00240.38980.02210.35524.4474-2.3565-0.0613
64.7697-0.725-1.00187.04591.72493.96180.20470.78860.8826-0.8477-0.2028-0.3836-0.4573-0.00840.03660.3569-0.02390.01360.2950.07190.489615.376117.41540.1083
72.8472-0.3642-0.1934.11560.45022.3476-0.04630.1483-0.27530.112-0.01870.00640.3079-0.07180.07630.31090.0087-0.01550.30040.00590.273113.8516-1.54252.3633
82.4881-2.88771.47394.55140.03155.77040.00760.1363-1.01720.21680.07850.10120.86140.2692-0.0560.4730.01660.0230.20150.04480.381410.3494-9.20597.8516
95.1354-0.0801-0.44445.7591.40363.04610.16470.3645-0.18960.1695-0.01390.0623-0.0557-0.2841-0.1380.24220.0267-0.01520.32310.0260.25653.79717.21822.7206
105.41121.66084.54441.56840.13825.4109-0.686-1.62280.88240.51720.75271.7538-1.29620.3620.5510.71330.01860.25550.7435-0.03910.77237.58220.129813.0931
117.83741.67181.26155.6451.90133.60540.11720.18470.1051-0.1076-0.29550.62550.1319-0.27320.17870.29250.0876-0.04660.3569-0.04970.365-7.282511.71693.2697
126.0301-1.97412.69231.1126-0.56611.29960.02680.14520.2833-0.1027-0.1650.00420.2066-0.03920.11270.3558-0.00880.02490.3378-0.02430.32.73982.332611.1815
134.1260.7712-2.4123.4397-2.77125.80110.0219-1.8813-0.99870.735-0.2766-0.88140.39690.80250.17970.5717-0.0057-0.0620.58480.04790.407621.9123-1.130115.03
141.74320.4264-2.01935.76622.49223.91620.6829-0.0553-0.6119-0.6106-0.4195-0.34711.66042.4659-0.42750.8880.3419-0.20810.81520.04230.813131.7794-3.882711.7713
152.2908-1.8037-1.84478.61741.51546.8801-0.446-0.2721-0.2352-0.05230.4719-1.20070.7760.684-0.05710.30730.0125-0.02170.41810.02420.526727.98116.10428.7487
163.81045.72061.67149.47843.46922.56930.18890.5596-0.28710.82020.31081.01950.4143-0.0759-0.65160.7337-0.2852-0.02691.0358-0.04440.798-17.4785-5.741321.9476
178.0081-1.4845.66272.6519-1.13469.53840.2729-0.6126-0.38740.24790.47960.38280.4881-0.648-0.55410.3771-0.00510.03270.55740.05980.5784-13.62994.410629.4662
183.43574.28593.47266.84612.45176.21190.2958-1.5913-0.65830.0524-0.0436-1.0878-0.7050.12320.06980.59110.0502-0.04820.7981-0.07450.496110.245911.00646.8453
192.78171.2649-0.70696.56792.37058.17040.2249-1.24240.09920.75650.067-0.640.150.6549-0.23020.46330.0883-0.02620.5038-0.04810.414511.74843.952140.2537
202.2592-0.5834-0.12184.74951.57545.0585-0.0922-0.0845-0.41920.0222-0.13420.47650.4566-0.19330.22020.3679-0.02550.01160.35220.04030.3277-0.0085-1.763128.6712
214.04430.8874-2.77048.3079-1.24422.1352-0.1324-0.7450.61360.16140.36770.2641-0.78430.5052-0.35710.5145-0.0132-0.03710.6026-0.08480.38367.400916.685337.1277
223.7221-0.9622-3.23514.04671.20143.4806-0.1799-0.53190.76490.17740.5437-1.1657-1.04821.1264-0.39460.5729-0.19090.0020.4798-0.13810.521814.068315.295128.2592
232.63260.53361.2476.6449-0.98025.24940.1204-0.23290.3149-0.4254-0.0253-0.3667-0.2203-0.343-0.04740.279-0.0315-0.0060.3203-0.03240.2508-3.27938.129623.4783
240.8423-0.22070.04450.1411-0.51173.36060.41590.53140.8644-0.55850.34350.4459-0.5655-0.36240.9261.54530.33581.51941.24330.84180.79361.7771-11.574315.0104
258.71170.7439-4.85162.2409-0.45212.9156-0.93170.4203-1.2267-0.70970.38130.90181.9687-0.46070.40830.88-0.20840.12070.70270.02380.6978-6.96-9.557814.9627
263.52710.9859-0.60013.7212-0.85122.98520.00440.21350.09030.05230.04410.4026-0.2902-0.8730.04890.25010.0326-0.01080.4099-0.02920.2799-9.877111.730215.0431
278.1799-1.82370.45896.0364-0.88115.2047-0.4745-0.32880.0234-0.02540.1099-0.75670.06940.32190.1550.3368-0.02050.06840.3311-0.03270.383612.90734.453522.9729
281.27721.06781.60013.4179-0.59343.4533-0.3827-1.89820.6754-0.3762-0.01280.6421.15551.0916-0.52080.60360.3502-0.14851.5705-0.18791.071123.9219-2.116734.8594
295.69784.6317-5.23175.1201-3.9294.87540.8032-1.8846-0.79331.6173-0.3422-2.18891.07591.1803-0.62530.59060.099-0.17770.76180.05770.767114.5131-5.81537.4112
306.59434.98425.86993.80174.63156.5577-0.1730.9608-1.48380.7112-0.1824-0.01590.63571.720.06620.6190.07750.06880.55090.10420.851613.5208-7.20527.6634
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 303:309)
2X-RAY DIFFRACTION2(chain A and resid 310:325)
3X-RAY DIFFRACTION3(chain A and resid 326:331)
4X-RAY DIFFRACTION4(chain A and resid 332:339)
5X-RAY DIFFRACTION5(chain A and resid 340:354)
6X-RAY DIFFRACTION6(chain A and resid 355:373)
7X-RAY DIFFRACTION7(chain A and resid 374:415)
8X-RAY DIFFRACTION8(chain A and resid 416:437)
9X-RAY DIFFRACTION9(chain A and resid 438:457)
10X-RAY DIFFRACTION10(chain A and resid 458:476)
11X-RAY DIFFRACTION11(chain A and resid 477:501)
12X-RAY DIFFRACTION12(chain A and resid 502:518)
13X-RAY DIFFRACTION13(chain A and resid 519:527)
14X-RAY DIFFRACTION14(chain A and resid 528:533)
15X-RAY DIFFRACTION15(chain A and resid 534:548)
16X-RAY DIFFRACTION16(chain B and resid 304:310)
17X-RAY DIFFRACTION17(chain B and resid 311:324)
18X-RAY DIFFRACTION18(chain B and resid 325:336)
19X-RAY DIFFRACTION19(chain B and resid 337:356)
20X-RAY DIFFRACTION20(chain B and resid 357:396)
21X-RAY DIFFRACTION21(chain B and resid 397:410)
22X-RAY DIFFRACTION22(chain B and resid 411:435)
23X-RAY DIFFRACTION23(chain B and resid 436:458)
24X-RAY DIFFRACTION24(chain B and resid 459:468)
25X-RAY DIFFRACTION25(chain B and resid 469:477)
26X-RAY DIFFRACTION26(chain B and resid 478:509)
27X-RAY DIFFRACTION27(chain B and resid 510:527)
28X-RAY DIFFRACTION28(chain B and resid 528:533)
29X-RAY DIFFRACTION29(chain B and resid 534:542)
30X-RAY DIFFRACTION30(chain B and resid 543:548)

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