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- PDB-2p15: Crystal structure of the ER alpha ligand binding domain with the ... -

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Basic information

Entry
Database: PDB / ID: 2p15
TitleCrystal structure of the ER alpha ligand binding domain with the agonist ortho-trifluoromethylphenylvinyl estradiol
Components
  • Estrogen receptor
  • GRIP peptide
KeywordsHORMONE RECEPTOR / nulear receptor / ligand binding domain / helix 12
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 / Mitochondrial unfolded protein response (UPRmt) / Endogenous sterols / 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-EZT / Estrogen receptor / Nuclear receptor coactivator 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.94 Å
AuthorsBruning, J.B. / Nettles, K.W. / Greene, G.L. / Kim, Y.
CitationJournal: Embo Rep. / Year: 2007
Title: Structural plasticity in the oestrogen receptor ligand-binding domain.
Authors: Nettles, K.W. / Bruning, J.B. / Gil, G. / O'Neill, E.E. / Nowak, J. / Guo, Y. / Kim, Y. / DeSombre, E.R. / Dilis, R. / Hanson, R.N. / Joachimiak, A. / Greene, G.L.
History
DepositionMar 2, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 1, 2007Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.3Oct 18, 2017Group: Advisory / Refinement description / Category: pdbx_unobs_or_zero_occ_atoms / software
Revision 1.4Oct 20, 2021Group: Advisory / Database references / Derived calculations
Category: database_2 / pdbx_unobs_or_zero_occ_atoms ...database_2 / pdbx_unobs_or_zero_occ_atoms / 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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Feb 21, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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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: GRIP peptide
D: GRIP peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)62,8186
Polymers61,9334
Non-polymers8852
Water8,305461
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7190 Å2
ΔGint-23 kcal/mol
Surface area20770 Å2
MethodPISA
Unit cell
Length a, b, c (Å)56.052, 84.220, 58.693
Angle α, β, γ (deg.)90.00, 109.59, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Estrogen receptor / ER / Estradiol receptor / ER-alpha


Mass: 29386.609 Da / Num. of mol.: 2 / Fragment: Ligand Binding Domain (residues 298-554) / Mutation: Y537S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ESR1, ESR, NR3A1 / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) Rosetta / References: UniProt: P03372
#2: Protein/peptide GRIP peptide


Mass: 1579.866 Da / Num. of mol.: 2 / Source method: obtained synthetically
Details: The peptide was chemically synthesized. The sequence can be naturally found in Homo sapiens (Human).
References: UniProt: Q15596
#3: Chemical ChemComp-EZT / (17BETA)-17-{(E)-2-[2-(TRIFLUOROMETHYL)PHENYL]VINYL}ESTRA-1(10),2,4-TRIENE-3,17-DIOL


Mass: 442.513 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C27H29F3O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 461 / 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: 2.11 Å3/Da / Density % sol: 41.62 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 20% PEG 4000, 0.2M Ammonium sulfate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97921
DetectorType: SBC-2 / Detector: CCD / Date: Aug 23, 2004 / Details: SI 111 MONOCHROMATOR
RadiationMonochromator: SI 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97921 Å / Relative weight: 1
ReflectionRedundancy: 4.7 % / Av σ(I) over netI: 6.6 / Number: 186764 / Rmerge(I) obs: 0.08 / Χ2: 0.9 / D res high: 1.87 Å / D res low: 50 Å / Num. obs: 39661 / % possible obs: 92.4
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)% possible obs (%)IDRmerge(I) obsChi squaredRedundancy
4.035099.310.0491.8184.8
3.24.0399.910.0571.4555
2.793.299.810.0761.0415.1
2.542.7999.610.0990.7885.1
2.362.5499.510.1180.6315.1
2.222.3699.210.1530.6175.1
2.112.2299.210.1990.5335
2.012.1197.410.2640.5394.2
1.942.0174.410.3260.5213.7
1.871.9455.210.3950.4733
ReflectionResolution: 1.87→50 Å / Num. all: 39661 / Num. obs: 39661 / % possible obs: 92.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.7 % / Biso Wilson estimate: 20.061 Å2 / Rmerge(I) obs: 0.08 / Rsym value: 0.08 / Χ2: 0.896 / Net I/σ(I): 6.6
Reflection shellResolution: 1.87→1.94 Å / Redundancy: 3 % / Rmerge(I) obs: 0.395 / Mean I/σ(I) obs: 1.738 / Num. unique all: 2369 / Rsym value: 0.395 / Χ2: 0.473 / % possible all: 55.2

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
REFMAC5.2.0019refinement
PDB_EXTRACT2data extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.94→27.71 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.933 / SU B: 6.303 / SU ML: 0.097 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: Restrained / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.167 / ESU R Free: 0.156 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.216 1871 5.1 %RANDOM
Rwork0.158 ---
all0.161 36913 --
obs0.161 36913 96.99 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 20.061 Å2
Baniso -1Baniso -2Baniso -3
1--0.08 Å20 Å2-0.01 Å2
2--0.12 Å20 Å2
3----0.04 Å2
Refine analyzeLuzzati coordinate error obs: 0.215 Å / Luzzati d res low obs: 27.71 Å
Refinement stepCycle: LAST / Resolution: 1.94→27.71 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4007 0 64 461 4532
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0214247
X-RAY DIFFRACTIONr_angle_refined_deg1.35825779
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.0055536
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.21124.171175
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.97615802
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.5811523
X-RAY DIFFRACTIONr_chiral_restr0.0980.2685
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.023063
X-RAY DIFFRACTIONr_nbd_refined0.2090.22153
X-RAY DIFFRACTIONr_nbtor_refined0.3050.22944
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1890.2331
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2320.261
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.4090.228
X-RAY DIFFRACTIONr_mcbond_it1.0031.52686
X-RAY DIFFRACTIONr_mcangle_it1.19424151
X-RAY DIFFRACTIONr_scbond_it2.16431780
X-RAY DIFFRACTIONr_scangle_it3.144.51610
LS refinement shellResolution: 1.94→1.99 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.244 98 -
Rwork0.181 1917 -
obs-2015 72.98 %
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)
16.966-3.27913.5743.4671-2.46294.89620.10840.2009-0.039-0.2578-0.1249-0.10270.12710.22860.0165-0.0091-0.01930.03710.0071-0.0411-0.0295-17.966-1.32518.541
25.9577-3.56483.05843.9804-2.00992.84420.03170.0603-0.0396-0.2544-0.0074-0.02120.2032-0.0627-0.02420.0590.00530.0221-0.00520.0007-0.034-27.816-3.82516.468
36.6296-5.34451.45812.3602-0.11542.22330.12420.081-0.45880.0144-0.09370.03070.502-0.0868-0.03060.1126-0.00060.0033-0.02430.00270.0296-26.574-16.09726.365
43.47640.59910.46254.8479-1.18081.44440.04150.03180.16140.0139-0.1107-0.1178-0.05870.1430.06920.02140.01290.00590.01250.0054-0.044-25.7383.76423.694
52.24980.96992.71877.09243.748311.625-0.13910.13690.3587-0.33560.04880.0328-0.616-0.02630.09030.08770.0187-0.0288-0.09270.0286-0.0229-28.08713.29717.164
60.61424.36-0.881230.9494-6.25491.26410.5616-0.71521.08231.169-0.09790.2907-0.8903-0.2144-0.46370.24960.10040.07350.1014-0.04140.2606-40.81714.76720.752
723.11520.52826.25934.2287-0.76861.9423-0.2791-0.20680.48290.15760.08260.074-0.3207-0.19010.19650.06940.01930.0193-0.05070.0014-0.0235-30.23211.45729.025
82.90262.27410.38996.1413-0.36821.554-0.0088-0.00320.1370.0896-0.02290.1106-0.07340.13130.03170.02850.007-0.00270.02020.0065-0.003-19.7450.26230.709
99.97946.3815-3.577413.228-2.41588.57860.44060.555-0.7388-0.0504-0.29110.12630.425-0.2081-0.14950.09140.0269-0.0204-0.0229-0.00070.0802-25.701-23.40336.421
1033.143227.64795.499825.76565.773318.33370.449-0.6327-1.21620.1703-0.333-0.83371.1966-0.1732-0.116-0.0070.0156-0.0127-0.11710.0639-0.0121-18.543-16.68536.267
114.54214.7041.435410.46421.98831.2829-0.06470.04410.0345-0.20010.0155-0.23960.02870.35350.0493-0.00960.02190.02560.07250.0420.057-8.991-1.45835.587
129.46021.43851.93473.2087-0.29043.2294-0.0087-0.12230.21840.077-0.0008-0.3091-0.13740.11340.00950.0287-0.01140.00670.0196-0.00790.0418-13.2315.22741.371
139.33570.31766.66370.840.83266.88520.0284-0.08080.01240.1006-0.0240.13070.1148-0.2007-0.00440.06080.02290.0345-0.00260.0156-0.003-34.6821.25630.861
1413.0204-11.2482-3.162112.34082.51994.89490.51490.7148-0.0763-0.5286-0.49280.788-0.1957-0.4293-0.0220.0397-0.0323-0.11190.056-0.01290.0475-43.784-2.65116.267
1510.78133.2026-2.67797.99729.084719.4172-0.188-0.2972-0.81660.1028-0.49770.39450.3273-0.87180.6857-0.0095-0.0155-0.0225-0.063-0.02440.0508-39.353-10.05423.495
1616.25486.9807-1.35123.5815-0.26012.2264-0.0915-0.53770.25790.15350.0547-0.0018-0.26680.47560.03680.0907-0.0004-0.03780.1214-0.0422-0.026-27.0283.9860.254
172.41552.86430.11695.4481-0.622.19430.1013-0.1002-0.15670.41260.05010.30360.2091-0.1744-0.15140.04170.01940.03860.0450.02780.071-52.105-10.23453.814
1811.26534.9717-3.12677.9628-1.50567.07420.4355-0.22890.46220.2339-0.0210.3001-0.5152-0.1626-0.41440.05060.01930.03070.0048-0.0034-0.0099-41.3834.16657.117
191.4070.4158-0.23094.7495-0.24631.82460.0697-0.06880.15270.15150.0054-0.042-0.27240.0737-0.07510.0577-0.00380.01940.0111-0.02280.012-34.6086.8150.495
202.91350.9627-0.00023.0970.75855.6454-0.0924-0.1403-0.41380.4857-0.05490.10220.48410.11870.14730.10360.0170.03140.00180.03220.085-39.533-15.98753.382
213.4511-3.8549-0.901913.2896-6.6956.83960.75680.3857-0.52350.1785-0.34830.87130.45030.1689-0.40850.0492-0.0497-0.030.0917-0.0490.0925-49.176-15.56443.341
2224.59621.89447.27185.02881.94974.87190.06780.2413-0.6003-0.3507-0.005-0.01990.1811-0.0356-0.06280.0705-0.02290.0236-0.0676-0.0130.0068-35.536-13.55343.372
235.4538-1.05470.444713.01761.16572.3859-0.0719-0.3908-0.5363-0.05040.1256-0.14130.19730.2341-0.05370.0320.0166-0.00510.04750.05520.0518-23.571-8.53852.706
243.5426-1.21120.28329.1538-3.5663.71250.0481-0.03130.2414-0.09960.0557-0.0049-0.1090.0791-0.10380.0326-0.02740.02250.0332-0.02510.0186-28.7835.45646.709
255.61272.057-0.061913.60042.40663.5492-0.0650.63930.8772-1.2995-0.12650.4033-0.4954-0.1350.19150.2717-0.0310.0713-0.01690.08230.0994-27.70419.44440.857
2611.0808-9.81783.154518.5769-6.40552.9087-0.0394-0.60050.24480.3738-0.0764-0.2016-0.22680.35040.1158-0.008-0.0657-0.03430.094-0.0347-0.0517-16.3184.05350.863
2714.9819-1.34823.96420.9287-1.28162.1602-0.01160.0382-0.17680.0231-0.0477-0.09810.05030.12280.05930.0366-0.00020.01690.02160.01610.0226-17.488-5.44243.722
2818.28-0.3502-2.12720.39940.15620.29460.05790.38520.1836-0.08490.04080.1526-0.0078-0.1386-0.09860.0560.0002-0.00490.03420.01670.027-46.61-2.89340.16
297.71045.0592-0.87959.56711.971712.3506-0.2688-0.2080.3232-0.195-0.00920.1643-0.288-0.42470.2779-0.06630.0086-0.0073-0.0683-0.03740.0413-49.4575.66547.663
3046.40854.650616.414817.23064.74224.6393-0.18491.19380.7934-1.23510.20450.1666-0.4167-0.3809-0.01960.0885-0.0043-0.02910.06260.014-0.0271-45.7196.95237.709
3147.4285-7.967827.189632.59993.789524.05061.47651.7677-1.6747-1.0332-0.68451.21851.45880.037-0.79210.08440.0287-0.0839-0.1252-0.1074-0.1177-29.725-17.90315.895
3233.908111.18265.790530.10539.176726.5868-0.1686-0.23172.4130.3283-0.30551.685-0.7634-1.57350.4741-0.12380.03410.0859-0.1168-0.07520.1235-44.88315.99253.376
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Selection: ALL

IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11AA306 - 33810 - 42
22AA339 - 36743 - 71
33AA368 - 38272 - 86
44AA383 - 39787 - 101
55AA398 - 411102 - 115
66AA412 - 421116 - 125
77AA422 - 435126 - 139
88AA436 - 460140 - 164
99AA461 - 471165 - 175
1010AA472 - 477176 - 181
1111AA478 - 496182 - 200
1212AA497 - 508201 - 212
1313AA509 - 526213 - 230
1414AA527 - 540231 - 244
1515AA541 - 549245 - 253
1616BB306 - 32910 - 33
1717BB330 - 35134 - 55
1818BB352 - 35956 - 63
1919BB360 - 39564 - 99
2020BB396 - 413100 - 117
2121BB414 - 421118 - 125
2222BB422 - 434126 - 138
2323BB435 - 447139 - 151
2424BB448 - 458152 - 162
2525BB459 - 474163 - 178
2626BB475 - 495179 - 199
2727BB496 - 513200 - 217
2828BB514 - 535218 - 239
2929BB536 - 544240 - 248
3030BB545 - 550249 - 254
3131CC687 - 6972 - 12
3232DD686 - 6961 - 11

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