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- PDB-7bre: The crystal structure of MLL2 in complex with ASH2L and RBBP5 -

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Basic information

Entry
Database: PDB / ID: 7bre
TitleThe crystal structure of MLL2 in complex with ASH2L and RBBP5
Components
  • Histone-lysine N-methyltransferase 2B
  • Retinoblastoma-binding protein 5
  • Set1/Ash2 histone methyltransferase complex subunit ASH2
KeywordsPROTEIN BINDING / Histone methyltransferase / MLL2 complex / MLL2 / RBBP5 / ASH2L / histone methylation / epigenetics / non-histone substrate / P53
Function / homology
Function and homology information


[histone H3]-lysine4 N-methyltransferase / histone H3K4 monomethyltransferase activity / unmethylated CpG binding / histone H3K4 trimethyltransferase activity / MLL3/4 complex / Set1C/COMPASS complex / MLL1/2 complex / histone H3K4 methyltransferase activity / histone methyltransferase complex / Formation of WDR5-containing histone-modifying complexes ...[histone H3]-lysine4 N-methyltransferase / histone H3K4 monomethyltransferase activity / unmethylated CpG binding / histone H3K4 trimethyltransferase activity / MLL3/4 complex / Set1C/COMPASS complex / MLL1/2 complex / histone H3K4 methyltransferase activity / histone methyltransferase complex / Formation of WDR5-containing histone-modifying complexes / hemopoiesis / MLL1 complex / transcription initiation-coupled chromatin remodeling / Deactivation of the beta-catenin transactivating complex / Formation of the beta-catenin:TCF transactivating complex / euchromatin / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / PKMTs methylate histone lysines / beta-catenin binding / Activation of anterior HOX genes in hindbrain development during early embryogenesis / response to estrogen / Neddylation / histone binding / methylation / transcription cis-regulatory region binding / DNA damage response / positive regulation of cell population proliferation / nucleolus / positive regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleoplasm / nucleus / metal ion binding
Similarity search - Function
KMT2B, ePHD domain / : / ASH2, PHD zinc finger / Set1/Ash2 histone methyltransferase complex subunit ASH2-like, WH / Histone methyltransferase complex subunit ASH2 / Retinoblastoma-binding protein 5/Swd1 / Methyltransferase, trithorax / : / FY-rich, N-terminal / F/Y-rich N-terminus ...KMT2B, ePHD domain / : / ASH2, PHD zinc finger / Set1/Ash2 histone methyltransferase complex subunit ASH2-like, WH / Histone methyltransferase complex subunit ASH2 / Retinoblastoma-binding protein 5/Swd1 / Methyltransferase, trithorax / : / FY-rich, N-terminal / F/Y-rich N-terminus / PHD-like zinc-binding domain / FYR domain FYRN motif profile. / "FY-rich" domain, N-terminal region / FY-rich, C-terminal / F/Y rich C-terminus / FYR domain FYRC motif profile. / "FY-rich" domain, C-terminal region / CXXC zinc finger domain / Zinc finger, CXXC-type / Zinc finger CXXC-type profile. / Cysteine-rich motif following a subset of SET domains / Post-SET domain / Post-SET domain profile. / SPRY domain / B30.2/SPRY domain / B30.2/SPRY domain profile. / SPRY domain / B30.2/SPRY domain superfamily / Domain in SPla and the RYanodine Receptor. / SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain / SET domain superfamily / SET domain / Extended PHD (ePHD) domain / Extended PHD (ePHD) domain profile. / SET domain profile. / SET domain / PHD-finger / Zinc finger PHD-type signature. / Zinc finger PHD-type profile. / Zinc finger, PHD-finger / Zinc finger, PHD-type / PHD zinc finger / Zinc finger, FYVE/PHD-type / Bromodomain-like superfamily / Concanavalin A-like lectin/glucanase domain superfamily / Zinc finger, RING/FYVE/PHD-type / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
S-ADENOSYL-L-HOMOCYSTEINE / Retinoblastoma-binding protein 5 / Set1/Ash2 histone methyltransferase complex subunit ASH2 / Histone-lysine N-methyltransferase 2B
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.803 Å
AuthorsLi, Y. / Zhao, L. / Chen, Y.
Funding support China, 2items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31970576 China
National Natural Science Foundation of China (NSFC)31900934 China
CitationJournal: Structure / Year: 2020
Title: Crystal Structure of MLL2 Complex Guides the Identification of a Methylation Site on P53 Catalyzed by KMT2 Family Methyltransferases.
Authors: Li, Y. / Zhao, L. / Tian, X. / Peng, C. / Gong, F. / Chen, Y.
History
DepositionMar 28, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 22, 2020Provider: repository / Type: Initial release
Revision 1.1Aug 5, 2020Group: Database references / Category: citation
Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Oct 21, 2020Group: Database references / Category: citation / Item: _citation.journal_volume / _citation.page_first
Revision 1.3Nov 29, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Set1/Ash2 histone methyltransferase complex subunit ASH2
B: Histone-lysine N-methyltransferase 2B
E: Histone-lysine N-methyltransferase 2B
D: Set1/Ash2 histone methyltransferase complex subunit ASH2
C: Retinoblastoma-binding protein 5
F: Retinoblastoma-binding protein 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)86,67910
Polymers85,7806
Non-polymers9004
Water00
1
A: Set1/Ash2 histone methyltransferase complex subunit ASH2
B: Histone-lysine N-methyltransferase 2B
C: Retinoblastoma-binding protein 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,3405
Polymers42,8903
Non-polymers4502
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
E: Histone-lysine N-methyltransferase 2B
D: Set1/Ash2 histone methyltransferase complex subunit ASH2
F: Retinoblastoma-binding protein 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,3405
Polymers42,8903
Non-polymers4502
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)79.075, 66.195, 83.734
Angle α, β, γ (deg.)90.000, 93.230, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Set1/Ash2 histone methyltransferase complex subunit ASH2 / ASH2-like protein


Mass: 20597.355 Da / Num. of mol.: 2 / Fragment: UNP residues 286-402 and UNP residues 445-504
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ASH2L, ASH2L1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / Variant (production host): Rosetta / References: UniProt: Q9UBL3
#2: Protein Histone-lysine N-methyltransferase 2B / Lysine N-methyltransferase 2B / Myeloid/lymphoid or mixed-lineage leukemia protein 4 / Trithorax ...Lysine N-methyltransferase 2B / Myeloid/lymphoid or mixed-lineage leukemia protein 4 / Trithorax homolog 2 / WW domain-binding protein 7 / WBP-7


Mass: 19037.148 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MLL2 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / Variant (production host): Rosetta
References: UniProt: Q9UMN6, [histone H3]-lysine4 N-trimethyltransferase
#3: Protein/peptide Retinoblastoma-binding protein 5 / RBBP-5 / Retinoblastoma-binding protein RBQ-3


Mass: 3255.321 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RBBP5 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / Variant (production host): Rosetta / References: UniProt: Q15291
#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#5: Chemical ChemComp-SAH / S-ADENOSYL-L-HOMOCYSTEINE


Type: L-peptide linking / Mass: 384.411 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C14H20N6O5S
Has ligand of interestN
Sequence detailsAuthors made a construct of ASH2L (Q9UBL3-3) that delete a loop deletion from 402-445, and the loop ...Authors made a construct of ASH2L (Q9UBL3-3) that delete a loop deletion from 402-445, and the loop is replaced by a linker sequence (ISGRGS).

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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: 2.32 Å3/Da / Density % sol: 46.92 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7
Details: 0.1M Ammonium tartrate dibasic pH 7.0, 12%(w/v) Polyethylene glycol 3,350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.9785 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Dec 28, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9785 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. obs: 21457 / % possible obs: 100 % / Redundancy: 6.7 % / Rmerge(I) obs: 0.159 / Rpim(I) all: 0.066 / Rrim(I) all: 0.173 / Χ2: 0.631 / Net I/σ(I): 3.4 / Num. measured all: 142941
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.8-2.96.30.64221200.7930.2760.70.477100
2.9-3.026.60.52421480.8690.2210.570.495100
3.02-3.156.50.40121220.920.170.4360.527100
3.15-3.3270.31621300.9540.1280.3410.543100
3.32-3.536.90.23221140.9640.0960.2510.592100
3.53-3.86.50.1721440.9780.0720.1850.643100
3.8-4.186.90.1321540.9890.0530.140.73100
4.18-4.796.80.121340.9920.0410.1090.801100
4.79-6.036.70.09421750.9920.0390.1020.682100
6.03-506.40.08122160.9970.0340.0880.80199.9

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Processing

Software
NameVersionClassification
HKL-3000data scaling
PHENIX1.17refinement
PDB_EXTRACT3.25data extraction
HKL-3000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3TOJ,5F6E

3toj

5f6e


Resolution: 2.803→37.833 Å / SU ML: 0.34 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 26.25
RfactorNum. reflection% reflection
Rfree0.2646 1096 5.13 %
Rwork0.2185 --
obs0.2209 21376 99.57 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 122.34 Å2 / Biso mean: 52.2977 Å2 / Biso min: 13.43 Å2
Refinement stepCycle: final / Resolution: 2.803→37.833 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5813 0 54 0 5867
Biso mean--49.21 --
Num. residues----723
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.803-2.93040.30671390.2767248799
2.9304-3.08490.30361410.26512530100
3.0849-3.2780.27641150.24692543100
3.278-3.5310.31931380.23682525100
3.531-3.8860.25831310.21272551100
3.886-4.44750.27931490.19272535100
4.4475-5.60050.20321450.18472542100
5.6005-37.830.25041380.2199256798
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)
13.9556-2.3293-0.39575.15420.16375.96070.10450.1219-0.92890.9338-0.16130.77380.5148-0.86450.20920.3126-0.03380.05380.2251-0.04240.284125.3627-7.861496.9135
24.1897-0.5321-0.54784.32661.20474.34360.10920.05820.03110.9577-0.20220.847-0.0131-0.21120.27030.34160.02450.03250.2207-0.0010.251821.66153.170697.3615
33.8581-2.1456-1.17755.43650.76931.79750.07720.0866-0.301-0.53510.0310.30480.1425-0.2673-0.07050.2120.0264-0.00940.219-0.00850.233333.1059-2.825690.7333
43.04770.69551.13590.8948-0.32222.87520.0234-0.3128-0.0519-0.90060.3770.5626-0.55920.1932-0.22680.3371-0.03980.03670.1368-0.02840.270930.514410.162792.4691
50.7868-1.5863-0.47165.38830.6381.4869-0.46240.36820.02190.92350.0259-0.47310.07490.11510.44170.20660.0519-0.01990.26560.0350.200537.3823.0427103.3456
61.94720.7874-0.54911.33430.7632.2070.16680.05360.1454-0.321-0.1455-0.55530.12760.06940.03260.3206-0.0139-0.0270.11380.04060.171741.11385.709689.0797
72.43870.0046-1.78482.8651-0.44651.4753-0.07040.29010.0712-0.145-0.010.00290.0598-0.14940.04490.3102-0.0277-0.07680.1812-0.00360.139135.52681.509387.8914
83.0099-0.91160.0914.32651.33711.8405-0.00620.39750.5207-1.0915-0.07650.3305-0.3675-0.15350.1150.69460.09410.00050.1991-0.09210.307437.8586-9.109982.8949
92.5582.68470.31052.15570.52352.3454-0.0486-0.16740.3486-0.0474-0.02440.4906-0.2765-0.6030.0950.45470.0761-0.01040.318-0.09620.57169.022215.3769129.17
101.1175-0.54520.81242.19871.364.0590.0205-0.51660.1448-0.1221-0.1266-0.0301-0.3881-0.3944-0.08330.3037-0.06330.1650.2578-0.1240.339421.67721.3815135.3392
110.81370.374-0.89671.87442.10734.75970.40960.04530.3844-0.18080.0734-0.5238-0.44140.8149-0.41870.48850.0701-0.04760.1679-0.02660.37735.460116.7381114.2215
120.7566-0.6881-0.86693.8024-2.34.1559-0.18570.4468-0.62950.0758-0.28430.1304-0.56330.01790.34530.45350.0798-0.00860.2581-0.17470.553929.112916.6366119.7736
134.9935-1.04640.1474.20221.3212.75190.0191-0.014-0.27110.0852-0.0413-0.294-0.04090.3467-0.02320.3941-0.08380.03980.23170.02010.271627.934813.4736134.0648
148.0433-1.9746-3.03150.48410.71123.6886-0.67110.5376-0.79390.1310.4025-0.35730.49950.67450.08940.64380.1426-0.16640.4648-0.00110.448128.05868.1407126.4257
153.91444.36640.36125.43042.54098.2518-0.79610.47540.38490.44420.2768-0.00150.41750.62710.43170.40970.0595-0.00150.47540.0460.902518.0971-7.7702125.3876
160.1112-0.30360.42632.6078-2.31462.6529-0.3888-1.0016-1.1933-1.06560.0962-0.02190.71770.70740.35520.8320.3070.06960.84050.25890.69077.0415-20.9545132.0533
174.4821-0.5919-1.70163.34540.69024.4962-0.7566-0.8551-0.96280.1729-0.0756-0.11731.33340.67960.57260.481-0.04720.19740.94080.42890.469-4.7002-19.0806137.1048
180.91580.50780.43591.6622-0.15230.3586-0.7138-0.332-0.02210.1154-0.1192-0.25920.09590.6361-0.13580.46150.0777-0.22030.70320.07490.44768.6001-13.6799133.2369
190.14670.7223-0.05433.9568-1.09661.11730.1797-0.4929-0.24630.8003-0.01490.59050.5174-0.5489-0.37340.388-0.0255-0.09050.5320.16680.5787-10.3326-10.519113.6463
203.2579-1.52712.11261.55950.76825.0476-0.0171-0.34170.17370.35560.05880.16860.1798-0.1118-0.22040.29010.02160.02240.32610.02060.4551-5.066-7.2991119.9745
213.1943-0.3672-1.92030.7733-0.73776.3428-0.33510.102-0.3566-0.3264-0.06580.14321.4999-0.28330.1280.6666-0.0956-0.28770.38050.21020.4897-2.4127-14.1346118.4212
229.8728-1.8533-1.02077.402-5.81845.2228-0.302-0.29820.46250.14020.24380.16690.26460.6921-0.0080.3156-0.045-0.14250.45470.04050.372-3.2351-11.5407134.4527
236.55290.2818-0.52085.8352-0.3974.5924-0.2511-1.01910.6821-0.13830.2298-0.50710.3353-0.10660.08010.27450.0534-0.03880.4-0.03540.42177.0348-8.3598131.5221
248.30842.1892-5.29425.81220.84074.3230.80570.51250.7555-0.084-0.01530.3731-0.5896-0.5881-0.63880.41320.1877-0.12250.8385-0.18410.6248-8.9319-4.1817130.499
254.93390.0063-4.66978.849-0.35047.6493-0.0982-0.52630.86930.14420.57960.61870.675-0.4108-0.39380.4409-0.0772-0.16990.623-0.00310.6033-13.8582-5.5498138.134
261.00751.9585-0.79894.1091-1.10291.23990.32050.25781.38120.2103-0.5989-0.5815-0.29350.70970.44780.382-0.06260.02730.72120.1851.40890.359113.503799.4391
273.2347-0.43391.3920.3198-0.01591.20790.38441.29111.0613-0.4464-0.311-0.7752-0.3980.94980.2174-0.48770.2898-0.16070.97090.49570.90023.81534.324697.8367
281.0152-0.8850.74940.8146-0.63090.55040.02290.78141.5872-0.4613-0.3227-0.6882-0.20960.31030.2580.25560.03620.02180.48580.37990.9901-8.963513.254892.7499
292.03130.53070.81940.4727-0.65052.58520.42841.31990.4584-0.5495-0.2081-0.76040.33520.86080.01060.42660.19510.00160.75180.16550.7296-3.3526-1.637791.1806
305.25950.06282.86252.3396-2.43954.18990.0319-0.34690.59-0.1756-0.28420.06390.1612-0.42010.17270.19090.03720.05420.231-0.07970.2902-12.24751.273398.4902
315.5607-0.528-1.16323.8451.26642.08850.51630.7762-0.911-0.214-0.72320.08530.70420.96990.28940.3540.1906-0.00870.610.03340.4121-14.0072-3.222589.9726
322.54711.68351.44091.73340.56522.4271-0.41680.81231.1829-0.4338-0.4434-0.28990.03431.0452-0.04320.50190.06290.11530.62510.3640.5991-13.67610.335586.7641
334.3155-1.04210.53374.1013-0.28762.58050.33470.16451.1652-0.0205-0.6481-0.233-0.83880.26240.48810.42580.03650.02010.39450.12280.7903-22.181513.02788.5111
342.9634-0.08160.43880.940.08131.9471-0.15980.72540.7095-0.1314-0.4555-0.6119-0.02680.33690.53070.2620.02740.02030.52590.1410.5748-11.74554.899691.8541
353.07080.4755-2.13091.4014-0.71221.59250.11520.36420.2887-0.0992-0.00380.06840.1979-0.7857-0.2190.1719-0.35960.44361.510.82610.177-4.507612.89980.9021
360.21120.2735-0.17591.1990.41110.5628-0.46580.94430.6456-0.4394-0.6697-0.5901-0.82360.76570.74030.6708-0.1313-0.29090.89980.80731.2463-11.87917.807383.3985
375.1193-3.6032-5.69172.87252.8832.0001-0.1124-0.5140.36320.41510.2129-0.87271.3433-1.3734-0.03211.2691-0.0304-0.20310.59880.02190.647623.927528.853120.8116
389.7312-1.82980.8051.98031.23762.4031.001-0.08-0.31570.623-0.33290.3947-0.3716-0.6982-0.7040.4443-0.10240.13470.3142-0.10570.618221.244720.1155113.4672
392.0969-0.75521.82835.35050.90782.09480.66040.52050.6955-0.3275-0.33450.8018-1.2602-0.229-0.39190.37160.10040.01640.34810.06840.499430.09618.7223102.2417
407.9911-1.78150.84322.71583.46875.86820.50320.53451.0787-0.1322-0.0475-0.0229-1.55791.1619-0.38320.4164-0.1045-0.02290.41740.02720.705438.456316.8932103.0676
412.7716-1.19494.11571.7403-2.26858.17690.60360.3141-0.2498-0.0485-0.0862-0.49810.22140.0774-0.44241.53150.5769-0.05991.13990.16080.49214.1714-20.9914118.5403
422.9239-0.3953.03947.3601-2.33863.9009-0.164-0.0782-0.0586-0.48650.1245-0.42990.46220.1661-0.08630.74750.29140.19440.2030.30870.7632.0855-13.0173110.0191
435.1359-0.94451.04214.63422.03692.29870.09820.7496-1.3716-0.11790.6425-0.18282.41060.1115-0.7720.8415-0.0245-0.21520.4609-0.0740.5123-7.0263-10.6869101.5451
445.87450.7315-2.45260.73530.4417.00490.18711.1817-0.9174-0.61680.41940.6722.1851-0.9779-0.41370.5698-0.1801-0.25220.49580.15660.8566-14.638-9.0195101.382
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 285 through 294 )A285 - 294
2X-RAY DIFFRACTION2chain 'A' and (resid 295 through 313 )A295 - 313
3X-RAY DIFFRACTION3chain 'A' and (resid 314 through 335 )A314 - 335
4X-RAY DIFFRACTION4chain 'A' and (resid 336 through 347 )A336 - 347
5X-RAY DIFFRACTION5chain 'A' and (resid 348 through 362 )A348 - 362
6X-RAY DIFFRACTION6chain 'A' and (resid 363 through 451 )A363 - 451
7X-RAY DIFFRACTION7chain 'A' and (resid 452 through 493 )A452 - 493
8X-RAY DIFFRACTION8chain 'A' and (resid 494 through 503 )A494 - 503
9X-RAY DIFFRACTION9chain 'B' and (resid 2551 through 2581 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 2582 through 2606 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 2607 through 2624 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 2625 through 2646 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 2647 through 2715 )B0
14X-RAY DIFFRACTION14chain 'E' and (resid 2551 through 2558 )E0
15X-RAY DIFFRACTION15chain 'E' and (resid 2559 through 2568 )E0
16X-RAY DIFFRACTION16chain 'E' and (resid 2569 through 2581 )E0
17X-RAY DIFFRACTION17chain 'E' and (resid 2582 through 2591 )E0
18X-RAY DIFFRACTION18chain 'E' and (resid 2592 through 2606 )E0
19X-RAY DIFFRACTION19chain 'E' and (resid 2607 through 2624 )E0
20X-RAY DIFFRACTION20chain 'E' and (resid 2625 through 2636 )E0
21X-RAY DIFFRACTION21chain 'E' and (resid 2637 through 2646 )E0
22X-RAY DIFFRACTION22chain 'E' and (resid 2647 through 2658 )E0
23X-RAY DIFFRACTION23chain 'E' and (resid 2659 through 2686 )E0
24X-RAY DIFFRACTION24chain 'E' and (resid 2687 through 2698 )E0
25X-RAY DIFFRACTION25chain 'E' and (resid 2699 through 2715 )E0
26X-RAY DIFFRACTION26chain 'D' and (resid 286 through 295 )D286 - 295
27X-RAY DIFFRACTION27chain 'D' and (resid 296 through 313 )D296 - 313
28X-RAY DIFFRACTION28chain 'D' and (resid 314 through 332 )D314 - 332
29X-RAY DIFFRACTION29chain 'D' and (resid 333 through 347 )D333 - 347
30X-RAY DIFFRACTION30chain 'D' and (resid 348 through 372 )D348 - 372
31X-RAY DIFFRACTION31chain 'D' and (resid 373 through 390 )D373 - 390
32X-RAY DIFFRACTION32chain 'D' and (resid 391 through 398 )D391 - 398
33X-RAY DIFFRACTION33chain 'D' and (resid 399 through 451 )D399 - 451
34X-RAY DIFFRACTION34chain 'D' and (resid 452 through 481 )D452 - 481
35X-RAY DIFFRACTION35chain 'D' and (resid 482 through 492 )D482 - 492
36X-RAY DIFFRACTION36chain 'D' and (resid 493 through 503 )D493 - 503
37X-RAY DIFFRACTION37chain 'C' and (resid 336 through 340 )C336 - 340
38X-RAY DIFFRACTION38chain 'C' and (resid 341 through 345 )C341 - 345
39X-RAY DIFFRACTION39chain 'C' and (resid 346 through 350 )C346 - 350
40X-RAY DIFFRACTION40chain 'C' and (resid 351 through 355 )C351 - 355
41X-RAY DIFFRACTION41chain 'F' and (resid 337 through 341 )F337 - 341
42X-RAY DIFFRACTION42chain 'F' and (resid 342 through 346 )F342 - 346
43X-RAY DIFFRACTION43chain 'F' and (resid 347 through 351 )F347 - 351
44X-RAY DIFFRACTION44chain 'F' and (resid 352 through 355 )F352 - 355

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