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- PDB-7w6l: The crystal structure of MLL3-RBBP5-ASH2L in complex with H3K4me0... -

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Basic information

Entry
Database: PDB / ID: 7w6l
TitleThe crystal structure of MLL3-RBBP5-ASH2L in complex with H3K4me0 peptide
Components
  • Histone H3.3C
  • Histone-lysine N-methyltransferase 2C
  • Retinoblastoma-binding protein 5
  • Set1/Ash2 histone methyltransferase complex subunit ASH2
KeywordsPROTEIN BINDING/TRANSFERASE / MLL family methyltransferases / product specificity / F/Y switch / PROTEIN BINDING / PROTEIN BINDING-TRANSFERASE complex
Function / homology
Function and homology information


[histone H3]-lysine4 N-methyltransferase / histone H3K4 monomethyltransferase activity / histone H3K4 trimethyltransferase activity / Epigenetic regulation of gene expression by MLL3 and MLL4 complexes / MLL3/4 complex / Set1C/COMPASS complex / MLL1/2 complex / histone H3K4 methyltransferase activity / nucleosomal DNA binding / histone methyltransferase activity ...[histone H3]-lysine4 N-methyltransferase / histone H3K4 monomethyltransferase activity / histone H3K4 trimethyltransferase activity / Epigenetic regulation of gene expression by MLL3 and MLL4 complexes / MLL3/4 complex / Set1C/COMPASS complex / MLL1/2 complex / histone H3K4 methyltransferase activity / nucleosomal DNA binding / histone methyltransferase activity / acyltransferase activity / Formation of WDR5-containing histone-modifying complexes / histone methyltransferase complex / hemopoiesis / MLL1 complex / transcription initiation-coupled chromatin remodeling / Deactivation of the beta-catenin transactivating complex / euchromatin / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / beta-catenin binding / PKMTs methylate histone lysines / response to estrogen / Activation of anterior HOX genes in hindbrain development during early embryogenesis / structural constituent of chromatin / nucleosome / Neddylation / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / positive regulation of cell growth / histone binding / methylation / transcription coactivator activity / transcription cis-regulatory region binding / protein heterodimerization activity / positive regulation of cell population proliferation / DNA damage response / nucleolus / positive regulation of transcription by RNA polymerase II / DNA binding / RNA binding / zinc ion binding / nucleoplasm / nucleus / cytosol
Similarity search - Function
Histone-lysine N-methyltransferase 2C / KMT2C, ePHD1 / KMT2C, ePHD2 / : / : / : / HMG-I/HMG-Y, DNA-binding, conserved site / HMG-I and HMG-Y DNA-binding domain (A+T-hook). / DHHC domain profile. / : ...Histone-lysine N-methyltransferase 2C / KMT2C, ePHD1 / KMT2C, ePHD2 / : / : / : / HMG-I/HMG-Y, DNA-binding, conserved site / HMG-I and HMG-Y DNA-binding domain (A+T-hook). / DHHC domain profile. / : / : / Set1/Ash2 histone methyltransferase complex subunit ASH2-like, WH / ASH2, PHD zinc finger / Histone methyltransferase complex subunit ASH2 / Retinoblastoma-binding protein 5/Swd1 / 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 / Cysteine-rich motif following a subset of SET domains / Post-SET domain / Post-SET domain profile. / high mobility group / High mobility group box domain / High mobility group box domain superfamily / PHD-zinc-finger like domain / Extended PHD (ePHD) domain / Extended PHD (ePHD) domain profile. / SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain / SET domain / SET domain profile. / SET domain superfamily / SET domain / SPRY domain / B30.2/SPRY domain / B30.2/SPRY domain profile. / B30.2/SPRY domain superfamily / Domain in SPla and the RYanodine Receptor. / SPRY domain / PHD-finger / Zinc finger PHD-type signature. / Ring finger / Zinc finger PHD-type profile. / Zinc finger, PHD-finger / Zinc finger, PHD-type / PHD zinc finger / Zinc finger, FYVE/PHD-type / Zinc finger RING-type profile. / Zinc finger, RING-type / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 domain / Histone-fold / WD domain, G-beta repeat / Concanavalin A-like lectin/glucanase domain superfamily / Zinc finger, RING/FYVE/PHD-type / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
S-ADENOSYL-L-HOMOCYSTEINE / Retinoblastoma-binding protein 5 / Histone H3.3C / Histone-lysine N-methyltransferase 2C / Set1/Ash2 histone methyltransferase complex subunit ASH2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.26 Å
AuthorsZhao, L. / Li, Y. / Chen, Y.
Funding support China, 5items
OrganizationGrant numberCountry
Chinese Academy of SciencesXDB37010303 China
National Natural Science Foundation of China (NSFC)31670748 China
National Natural Science Foundation of China (NSFC)31970576 China
National Natural Science Foundation of China (NSFC)32071195 China
National Natural Science Foundation of China (NSFC)31900934 China
CitationJournal: Mol.Cell / Year: 2022
Title: Structural basis for product specificities of MLL family methyltransferases.
Authors: Li, Y. / Zhao, L. / Zhang, Y. / Wu, P. / Xu, Y. / Mencius, J. / Zheng, Y. / Wang, X. / Xu, W. / Huang, N. / Ye, X. / Lei, M. / Shi, P. / Tian, C. / Peng, C. / Li, G. / Liu, Z. / Quan, S. / Chen, Y.
History
DepositionDec 1, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 7, 2022Provider: repository / Type: Initial release
Revision 1.1Oct 26, 2022Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 2, 2022Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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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: Set1/Ash2 histone methyltransferase complex subunit ASH2
C: Histone-lysine N-methyltransferase 2C
D: Retinoblastoma-binding protein 5
E: Histone-lysine N-methyltransferase 2C
F: Retinoblastoma-binding protein 5
M: Histone H3.3C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)86,55211
Polymers85,6537
Non-polymers9004
Water4,053225
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)80.369, 236.142, 44.447
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212

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Components

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Protein , 2 types, 4 molecules ABCE

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


Mass: 20597.355 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ASH2L, ASH2L1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9UBL3
#2: Protein Histone-lysine N-methyltransferase 2C / Lysine N-methyltransferase 2C / Homologous to ALR protein / Myeloid/lymphoid or mixed-lineage ...Lysine N-methyltransferase 2C / Homologous to ALR protein / Myeloid/lymphoid or mixed-lineage leukemia protein 3


Mass: 18442.082 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KMT2A, ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1 / Production host: Escherichia coli (E. coli)
References: UniProt: Q8NEZ4, histone-lysine N-methyltransferase

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Protein/peptide , 2 types, 3 molecules DFM

#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, RBQ3 / Production host: Escherichia coli (E. coli) / References: UniProt: Q15291
#4: Protein/peptide Histone H3.3C / H3K4me0 peptide


Mass: 1063.254 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q6NXT2

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Non-polymers , 3 types, 229 molecules

#5: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#6: 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 / Feature type: SUBJECT OF INVESTIGATION
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 225 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.23 Å3/Da / Density % sol: 50.04 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 100 mM sodium cacodylate, pH 6.5, 10% polyethylene glycol 3350, 0.1 M MgCl2

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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 PILATUS3 6M / Detector: PIXEL / Date: Apr 7, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9785 Å / Relative weight: 1
ReflectionResolution: 2.25→50 Å / Num. obs: 40495 / % possible obs: 99.9 % / Redundancy: 5.2 % / Rmerge(I) obs: 0.074 / Rpim(I) all: 0.036 / Rrim(I) all: 0.082 / Χ2: 0.866 / Net I/σ(I): 10.2 / Num. measured all: 211044
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.25-2.295.30.77219970.8190.3730.8590.87100
2.29-2.335.30.59120180.8570.2860.6580.835100
2.33-2.385.30.49419470.8770.2390.550.84100
2.38-2.425.30.43220070.9310.2080.480.831100
2.42-2.485.30.3719970.9360.1790.4120.83100
2.48-2.535.30.30319810.9590.1460.3370.823100
2.53-2.65.30.26620090.9640.1280.2960.844100
2.6-2.675.30.23319670.9620.1130.260.895100
2.67-2.755.30.19820380.9710.0960.220.89100
2.75-2.835.30.15119840.9840.0730.1680.94799.9
2.83-2.945.30.12820250.9860.0620.1420.978100
2.94-3.055.30.09919780.990.0480.1110.945100
3.05-3.195.20.07420330.9950.0360.0830.815100
3.19-3.365.30.05820140.9960.0280.0650.784100
3.36-3.575.20.05120100.9970.0240.0560.838100
3.57-3.855.10.0520410.9960.0240.0551.05599.9
3.85-4.2350.04420570.9970.0220.0491.097100
4.23-4.855.10.03620760.9980.0180.040.905100
4.85-6.15.10.03320990.9980.0160.0370.68899.8
6.1-504.70.0322170.9980.0150.0340.59898.7

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Processing

Software
NameVersionClassification
PHENIX1.18.2_3874refinement
HKL-3000data scaling
PDB_EXTRACT3.27data extraction
HKL-3000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5F6K

5f6k


Resolution: 2.26→44.45 Å / SU ML: 0.21 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 21.89 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2231 1841 4.74 %
Rwork0.1872 37025 -
obs0.1889 38866 95.33 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 139.03 Å2 / Biso mean: 41.942 Å2 / Biso min: 14.2 Å2
Refinement stepCycle: final / Resolution: 2.26→44.45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5662 0 54 225 5941
Biso mean--45.26 37.97 -
Num. residues----706
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 13

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.26-2.320.26891100.24011948205867
2.32-2.390.30691120.23512392250482
2.39-2.470.26661580.23022707286592
2.47-2.550.2411390.21912917305699
2.55-2.660.27611540.224829163070100
2.66-2.780.25891620.216629863148100
2.78-2.920.23121350.205729253060100
2.92-3.110.24931460.205829653111100
3.11-3.350.24991580.202129623120100
3.35-3.680.21781430.180630253168100
3.68-4.220.1811530.161730043157100
4.22-5.310.18851310.142630563187100
5.31-44.450.19391400.18113222336299
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)
12.1849-0.09040.52452.14710.50163.84950.4065-0.44540.74780.42650.14160.5386-0.5304-0.6552-0.23130.3099-0.00030.13180.3953-0.0390.284788.158754.56755.0715
21.29640.4149-0.93451.72710.02752.96-0.06080.00190.05820.1773-0.09370.5558-0.0977-0.73520.15140.21870.01210.04770.328-0.05250.22483.401650.7627-2.8457
30.7529-0.65170.6521.2771-0.22531.60680.0194-0.19850.12880.5276-0.10340.0221-0.02920.0410.01960.2797-0.03940.02620.2487-0.01070.138794.379945.42385.0835
40.9665-0.1041-0.24042.30020.09521.0246-0.01630.0056-0.0176-0.0529-0.0122-0.1260.0647-0.0094-0.01450.20690.01270.03160.2218-0.00190.12396.942242.934-7.4533
51.75470.5373-1.1352.20460.11581.60490.0781-0.4821-0.31460.5019-0.0898-0.22650.17970.12920.01390.2469-0.0214-0.04160.2480.01510.102697.839839.90694.7941
62.7952-0.3116-0.14813.1871-0.07591.70120.14610.8671-0.364-0.6907-0.0310.51660.2489-0.3836-0.02530.69780.0654-0.14810.3573-0.14110.51793.90446.8242-24.2711
72.0566-0.07560.67611.9423-0.08431.8802-0.07160.0976-0.2875-0.76950.11330.3516-0.0251-0.57620.07220.4958-0.0086-0.13130.2502-0.07280.415989.69797.0315-13.6066
82.96970.7509-1.14170.6296-0.39282.06560.07490.1297-0.4184-1.2502-0.1951-0.69950.3030.24890.79190.79980.27880.30140.2318-0.10020.4419102.67257.4868-21.6554
91.5171-0.08920.79821.7635-0.0831.40730.26580.1034-0.3228-0.5854-0.1739-0.29640.19730.0602-0.10070.36340.0850.10480.1937-0.00060.3581101.375810.3228-12.1475
102.8298-1.51090.09854.2432-0.14252.3586-0.0215-0.26910.05130.1523-0.1592-0.8986-0.07190.23830.09780.22850.01440.03330.23490.05420.4395106.153914.678-4.86
112.6039-0.3287-0.71080.4880.77621.4380.12630.4710.0361-0.4807-0.3411-1.08580.42330.35420.08590.46720.14920.31840.33160.09160.6121111.720118.4418-18.4353
120.3807-0.74440.28343.0889-0.14051.4429-0.10810.0285-0.3871-0.1991-0.2686-0.78450.14240.21030.17860.31520.03570.09750.29430.06480.5892110.689621.7059-10.8515
133.73380.01020.31710.38750.4691.01490.0876-0.2361-0.7293-0.4638-0.1586-0.81870.94530.30320.46520.49620.32820.30760.0976-0.08290.5343107.04928.3306-16.0512
141.4402-0.0646-0.03591.737-0.22491.90070.13660.1470.0412-1.0256-0.32610.01270.02370.08420.06990.40590.09380.0340.24090.00550.298896.65221.0305-17.1568
150.9140.1527-0.05810.57070.05581.4734-0.06680.2790.0863-0.3847-0.1508-0.29820.0195-0.0548-1.21141.07210.30020.60360.56840.06290.3304105.995321.0731-26.2508
162.4905-0.0137-1.28972.6263-0.43214.87260.0479-0.0355-0.12210.0232-0.26130.1653-0.40790.3975-0.11210.2109-0.01670.01420.2493-0.02160.354582.764723.89151.6542
174.1607-0.18050.43871.9834-0.2532.1770.2449-0.3140.5870.46640.07750.2096-0.23120.0666-0.14650.42380.00770.13040.4512-0.06320.418165.979727.811614.958
182.4329-0.23150.16892.53480.7191.93280.1689-0.29930.0029-0.0011-0.30630.31810.0055-0.2205-0.03050.1860.00240.04480.2734-0.040.388564.781417.15543.9454
192.68280.63530.9050.41720.20480.3101-0.4687-0.5174-0.06070.1492-0.11070.19580.4756-0.2930.20260.33690.00040.05810.3826-0.09950.543460.662615.40352.8249
203.39270.0118-0.28512.12170.43211.71770.13460.05410.20020.05740.01690.0181-0.1343-0.1322-0.08570.30080.01590.05560.26520.02960.378668.494424.02993.4354
213.054-0.4417-0.81291.8152-0.89831.94860.17220.0735-0.3516-0.34940.01070.7388-0.0301-1.2726-0.28570.4976-0.0033-0.07150.75840.05310.766352.345825.4598-0.6467
224.438-0.1393-0.49040.855-1.59253.1983-0.10590.0618-0.1975-0.0368-0.02650.2135-0.8226-0.597-0.33380.62640.16560.14950.64720.0480.48751.331733.66720.3097
236.5273.3501-0.90732.738-1.0730.53480.2232-0.6033-0.0960.1415-0.2198-0.578-0.21830.15270.13710.3590.0446-0.05610.3923-0.00060.443871.178810.12049.0611
243.95361.16730.1113.34820.24522.3446-0.0232-0.32130.33820.4323-0.32250.18960.0114-0.13970.23020.33140.0301-0.01980.2562-0.06710.598259.8914-2.86361.4298
252.6005-0.18571.33892.8107-0.54263.8097-0.2065-0.299-0.44980.0259-0.06510.45240.4891-0.1521-0.08290.2428-0.00410.18120.56880.02430.3466114.019843.7535-16.4927
262.7061-0.0142-0.67251.70940.870.60640.0152-0.5608-0.16430.76030.1895-0.07580.04270.17710.11820.34810.12920.09740.50710.12340.3031132.333138.8339-6.9163
271.57930.8225-0.27412.2627-0.6091.4242-0.39060.2014-0.4207-0.08110.57780.43010.0925-0.40740.0010.2653-0.01270.18780.39990.0640.4022120.982839.2957-15.5489
281.6650.23992.06750.12830.08022.82470.14750.01890.0319-0.05930.1444-0.1909-0.06390.36590.06850.3079-0.01480.04540.3592-0.03950.1734138.051160.1509-21.3004
293.64331.30530.953.09880.67964.2464-0.7315-0.15420.255-0.19690.0182-0.1645-0.53070.0710.24630.33360.0329-0.02140.2502-0.05460.282135.286752.683-19.1349
301.11090.13240.16752.5579-0.14530.295-0.2594-0.023-0.34920.06770.2240.1830.1190.14610.08560.30620.01320.10010.3384-0.01030.2631131.878747.1217-17.964
313.4847-2.77120.72524.5675-0.36660.7956-0.52460.3684-0.4318-0.46840.42320.3579-0.2019-0.74280.04730.560.0044-0.00320.51190.06170.3326120.343247.4629-25.6306
321.6220.43850.64620.39980.64051.5193-0.1895-0.2555-0.87030.13610.20060.08880.6378-0.25270.01830.44940.02120.18460.35620.09140.5272124.599135.1026-15.3169
330.0084-0.014-0.01690.09510.10230.0905-0.65790.3423-0.3755-0.06220.5418-0.3045-0.10640.61110.01180.4136-0.08910.17020.4842-0.06280.4724138.714440.3123-22.2103
343.12770.7794-0.66893.12460.31762.68480.0884-0.3347-0.08290.25380.0923-0.3068-0.23190.462-0.05870.54110.06830.12770.4770.03380.5945143.267833.2797-19.7582
355.3088-0.2791-4.36480.6865-1.31238.8875-0.1396-0.385-0.31690.8735-0.10610.80840.0033-0.6907-0.15320.5633-0.07270.07970.4936-0.03030.4895120.818255.8398-15.3137
365.96681.912-3.09925.0896-3.57753.309-0.1347-0.4714-0.24610.11720.54530.6355-0.2785-0.18280.05720.47680.05940.0490.35480.03310.2162128.290266.7806-23.3801
375.5291-1.2322-1.09554.5744-0.95191.35130.0308-0.5265-0.00120.6491-0.2127-0.04490.22620.61950.0540.35360.0329-0.09940.34910.02430.2503138.329671.9591-26.2499
381.6596-0.24561.87443.3451.56133.2242-0.30260.40910.0014-0.2097-0.31940.88650.37440.00920.05360.5871-0.03190.08880.765-0.04660.890559.79919.6476-2.9504
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 286 through 295 )A286 - 295
2X-RAY DIFFRACTION2chain 'A' and (resid 296 through 313 )A296 - 313
3X-RAY DIFFRACTION3chain 'A' and (resid 314 through 335 )A314 - 335
4X-RAY DIFFRACTION4chain 'A' and (resid 336 through 390 )A336 - 390
5X-RAY DIFFRACTION5chain 'A' and (resid 391 through 503 )A391 - 503
6X-RAY DIFFRACTION6chain 'B' and (resid 285 through 294 )B285 - 294
7X-RAY DIFFRACTION7chain 'B' and (resid 295 through 313 )B295 - 313
8X-RAY DIFFRACTION8chain 'B' and (resid 314 through 324 )B314 - 324
9X-RAY DIFFRACTION9chain 'B' and (resid 325 through 362 )B325 - 362
10X-RAY DIFFRACTION10chain 'B' and (resid 363 through 390 )B363 - 390
11X-RAY DIFFRACTION11chain 'B' and (resid 391 through 451 )B391 - 451
12X-RAY DIFFRACTION12chain 'B' and (resid 452 through 461 )B452 - 461
13X-RAY DIFFRACTION13chain 'B' and (resid 462 through 475 )B462 - 475
14X-RAY DIFFRACTION14chain 'B' and (resid 476 through 493 )B476 - 493
15X-RAY DIFFRACTION15chain 'B' and (resid 494 through 503 )B494 - 503
16X-RAY DIFFRACTION16chain 'C' and (resid 4754 through 4767 )C0
17X-RAY DIFFRACTION17chain 'C' and (resid 4768 through 4787 )C0
18X-RAY DIFFRACTION18chain 'C' and (resid 4788 through 4820 )C0
19X-RAY DIFFRACTION19chain 'C' and (resid 4821 through 4830 )C0
20X-RAY DIFFRACTION20chain 'C' and (resid 4831 through 4882 )C0
21X-RAY DIFFRACTION21chain 'C' and (resid 4883 through 4902 )C0
22X-RAY DIFFRACTION22chain 'C' and (resid 4903 through 4911 )C0
23X-RAY DIFFRACTION23chain 'D' and (resid 336 through 345 )D336 - 345
24X-RAY DIFFRACTION24chain 'D' and (resid 346 through 354 )D346 - 354
25X-RAY DIFFRACTION25chain 'E' and (resid 4755 through 4771 )E0
26X-RAY DIFFRACTION26chain 'E' and (resid 4772 through 4787 )E0
27X-RAY DIFFRACTION27chain 'E' and (resid 4788 through 4802 )E0
28X-RAY DIFFRACTION28chain 'E' and (resid 4803 through 4820 )E0
29X-RAY DIFFRACTION29chain 'E' and (resid 4821 through 4830 )E0
30X-RAY DIFFRACTION30chain 'E' and (resid 4831 through 4854 )E0
31X-RAY DIFFRACTION31chain 'E' and (resid 4855 through 4866 )E0
32X-RAY DIFFRACTION32chain 'E' and (resid 4867 through 4882 )E0
33X-RAY DIFFRACTION33chain 'E' and (resid 4883 through 4898 )E0
34X-RAY DIFFRACTION34chain 'E' and (resid 4899 through 4911 )E0
35X-RAY DIFFRACTION35chain 'F' and (resid 339 through 343 )F339 - 343
36X-RAY DIFFRACTION36chain 'F' and (resid 344 through 348 )F344 - 348
37X-RAY DIFFRACTION37chain 'F' and (resid 349 through 355 )F349 - 355
38X-RAY DIFFRACTION38chain 'M' and (resid 1 through 7 )M1 - 7

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