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- PDB-6w8b: Structure of DNMT3A in complex with CGA DNA -

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Basic information

Entry
Database: PDB / ID: 6w8b
TitleStructure of DNMT3A in complex with CGA DNA
Components
  • CGA DNA (25-MER)
  • DNA (cytosine-5)-methyltransferase 3-like
  • DNA (cytosine-5)-methyltransferase 3ADNA (cytosine-5)-methyltransferase 3A
KeywordsTRANSFERASE/DNA / DNA methylation / DNMT3A / AML / epigenetics / TRANSFERASE / TRANSFERASE-DNA complex
Function / homology
Function and homology information


retrotransposon silencing by heterochromatin formation / : / epigenetic programing of female pronucleus / chorionic trophoblast cell differentiation / positive regulation of cellular response to hypoxia / DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates / : / epigenetic programming of gene expression / cellular response to bisphenol A / protein-cysteine methyltransferase activity ...retrotransposon silencing by heterochromatin formation / : / epigenetic programing of female pronucleus / chorionic trophoblast cell differentiation / positive regulation of cellular response to hypoxia / DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates / : / epigenetic programming of gene expression / cellular response to bisphenol A / protein-cysteine methyltransferase activity / genomic imprinting / DNA (cytosine-5-)-methyltransferase / unmethylated CpG binding / DNA (cytosine-5-)-methyltransferase activity / autosome genomic imprinting / XY body / DNA methylation-dependent heterochromatin formation / negative regulation of DNA methylation-dependent heterochromatin formation / SUMOylation of DNA methylation proteins / ESC/E(Z) complex / cellular response to ethanol / response to vitamin A / : / response to ionizing radiation / hepatocyte apoptotic process / male meiosis I / chromosome, centromeric region / catalytic complex / enzyme activator activity / heterochromatin / Transferases; Transferring one-carbon groups; Methyltransferases / DNA methylation / response to cocaine / placenta development / PRC2 methylates histones and DNA / condensed nuclear chromosome / Defective pyroptosis / stem cell differentiation / cellular response to amino acid stimulus / response to lead ion / euchromatin / neuron differentiation / response to toxic substance / RMTs methylate histone arginines / nuclear matrix / transcription corepressor activity / response to estradiol / cellular response to hypoxia / spermatogenesis / RNA polymerase II-specific DNA-binding transcription factor binding / response to xenobiotic stimulus / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of DNA-templated transcription / chromatin binding / negative regulation of transcription by RNA polymerase II / enzyme binding / DNA binding / nucleoplasm / identical protein binding / metal ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
DNA (cytosine-5)-methyltransferase 3A, ADD domain / : / DNMT3, ADD PHD zinc finger / DNMT3, cysteine rich ADD domain / Cysteine rich ADD domain in DNMT3 / ADD domain / ADD domain profile. / DNA methylase, C-5 cytosine-specific, active site / C-5 cytosine-specific DNA methylases active site. / C-5 cytosine-specific DNA methylase (Dnmt) domain profile. ...DNA (cytosine-5)-methyltransferase 3A, ADD domain / : / DNMT3, ADD PHD zinc finger / DNMT3, cysteine rich ADD domain / Cysteine rich ADD domain in DNMT3 / ADD domain / ADD domain profile. / DNA methylase, C-5 cytosine-specific, active site / C-5 cytosine-specific DNA methylases active site. / C-5 cytosine-specific DNA methylase (Dnmt) domain profile. / C-5 cytosine methyltransferase / C-5 cytosine-specific DNA methylase / domain with conserved PWWP motif / PWWP domain / PWWP domain profile. / PWWP domain / Vaccinia Virus protein VP39 / Zinc finger, FYVE/PHD-type / Zinc finger, RING/FYVE/PHD-type / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
S-ADENOSYL-L-HOMOCYSTEINE / DNA / DNA (> 10) / DNA (cytosine-5)-methyltransferase 3-like / DNA (cytosine-5)-methyltransferase 3A
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsAnteneh, H. / Song, J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1R35GM119721 United States
CitationJournal: Nat Commun / Year: 2020
Title: Structural basis for impairment of DNA methylation by the DNMT3A R882H mutation.
Authors: Anteneh, H. / Fang, J. / Song, J.
History
DepositionMar 20, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 15, 2020Provider: repository / Type: Initial release
Revision 1.1May 20, 2020Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID
Revision 1.2Oct 18, 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: DNA (cytosine-5)-methyltransferase 3A
B: DNA (cytosine-5)-methyltransferase 3-like
C: DNA (cytosine-5)-methyltransferase 3-like
D: DNA (cytosine-5)-methyltransferase 3A
E: CGA DNA (25-MER)
F: CGA DNA (25-MER)
H: DNA (cytosine-5)-methyltransferase 3A
I: DNA (cytosine-5)-methyltransferase 3-like
J: DNA (cytosine-5)-methyltransferase 3-like
K: DNA (cytosine-5)-methyltransferase 3A
L: CGA DNA (25-MER)
M: CGA DNA (25-MER)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)259,85116
Polymers258,31412
Non-polymers1,5384
Water5,188288
1
A: DNA (cytosine-5)-methyltransferase 3A
B: DNA (cytosine-5)-methyltransferase 3-like
C: DNA (cytosine-5)-methyltransferase 3-like
D: DNA (cytosine-5)-methyltransferase 3A
E: CGA DNA (25-MER)
F: CGA DNA (25-MER)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)129,9268
Polymers129,1576
Non-polymers7692
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
H: DNA (cytosine-5)-methyltransferase 3A
I: DNA (cytosine-5)-methyltransferase 3-like
J: DNA (cytosine-5)-methyltransferase 3-like
K: DNA (cytosine-5)-methyltransferase 3A
L: CGA DNA (25-MER)
M: CGA DNA (25-MER)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)129,9268
Polymers129,1576
Non-polymers7692
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)186.347, 186.347, 81.671
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number145
Space group name H-MP32

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Components

#1: Protein
DNA (cytosine-5)-methyltransferase 3A / DNA (cytosine-5)-methyltransferase 3A / Dnmt3a / DNA methyltransferase HsaIIIA / M.HsaIIIA


Mass: 32715.719 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: DNMT3A / Production host: Escherichia coli (E. coli)
References: UniProt: Q9Y6K1, DNA (cytosine-5-)-methyltransferase
#2: Protein
DNA (cytosine-5)-methyltransferase 3-like


Mass: 24163.705 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: DNMT3L / Production host: Escherichia coli (E. coli) / References: UniProt: Q9UJW3
#3: DNA chain
CGA DNA (25-MER)


Mass: 7698.969 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#4: Chemical
ChemComp-SAH / S-ADENOSYL-L-HOMOCYSTEINE / S-Adenosyl-L-homocysteine


Type: L-peptide linking / Mass: 384.411 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C14H20N6O5S
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 288 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 3.17 Å3/Da / Density % sol: 61.19 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / Details: 0.1 M Sodium Citrate pH 4.2, 1% PEG8000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 0.5 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Nov 1, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.5 Å / Relative weight: 1
ReflectionResolution: 2.4→48.9 Å / Num. obs: 123917 / % possible obs: 99.9 % / Redundancy: 5.1 % / CC1/2: 0.999 / Net I/σ(I): 10
Reflection shellResolution: 2.4→2.49 Å / Num. unique obs: 123895 / CC1/2: 0.644

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Processing

Software
NameVersionClassification
PHENIX1.15.2_3472refinement
PDB_EXTRACT3.25data extraction
HKL-3000data reduction
HKL-3000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5YX2

5yx2


Resolution: 2.4→48.871 Å / SU ML: 0.37 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 33.03 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2326 2012 1.62 %
Rwork0.2121 121905 -
obs0.2124 123917 99.9 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 237.44 Å2 / Biso mean: 95.6783 Å2 / Biso min: 36.92 Å2
Refinement stepCycle: final / Resolution: 2.4→48.871 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14636 2006 104 288 17034
Biso mean--66.61 68.07 -
Num. residues----1991
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork
2.4-2.45990.45561440.43918688
2.4599-2.52640.38481500.39528725
2.5264-2.60080.40891440.34388671
2.6008-2.68470.33531400.31898734
2.6847-2.78060.30461520.2978714
2.7806-2.8920.39841440.288693
2.892-3.02360.25611400.24868753
3.0236-3.18290.30971300.23488712
3.1829-3.38230.26111480.2258694
3.3823-3.64340.19611460.19938696
3.6434-4.00990.19131460.17838674
4.0099-4.58970.19811520.16348752
4.5897-5.78110.17821360.17388709
5.7811-48.8710.19461400.18268690
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)
13.10190.19870.24861.6069-0.01872.3283-0.07320.4509-0.445-0.1967-0.03590.27120.0875-0.24450.11120.3974-0.0458-0.07220.5226-0.13930.6485-11.29948.496-4.83
29.2781.5628-0.0861.2812-0.61472.6149-0.21510.9106-0.4872-0.45810.0351-0.11580.1525-0.09350.17220.4819-0.0401-0.05690.5308-0.15050.55998.00953.64-15.357
35.0781-0.1355-0.46012.77530.23480.7694-0.06620.3726-0.3741-0.11590.018-0.1344-0.148-0.1370.06080.5342-0.049-0.0440.5624-0.09020.35126.58255.133-5.453
45.0222.76990.72443.8993-0.92052.5826-0.0860.7997-0.7496-0.19310.16850.64650.3738-0.3798-0.09490.6699-0.1285-0.07040.8854-0.42941.365-33.25231.142-13.212
53.13583.8153-0.99375.1938-1.65934.29791.1536-0.6569-1.43310.5757-0.3411-0.01720.992-0.4391-0.6830.8481-0.2145-0.24060.8555-0.13811.8077-27.34324.6090.097
67.2489-1.39171.60645.7379-1.48013.74210.6894-0.6581-1.3870.8143-0.4266-0.24960.9072-0.2942-0.4811.0499-0.3568-0.20631.0279-0.04621.9798-34.54218.661-4.08
73.47370.001-1.1832-0.0159-0.02570.56790.5573-0.733-0.40350.3009-0.5552-0.7077-0.01631.79990.03840.3734-0.3588-0.71782.11020.67912.576773.94157.93923.497
85.6553-0.94350.40430.65791.19393.02760.2096-0.6689-0.3281.2520.1553-2.0570.55611.4046-0.32850.836-0.0849-0.42791.5590.36411.833265.34356.23626.183
93.4232-1.47830.4731.27650.85185.71480.2503-0.3363-0.4794-0.1574-0.3856-1.6632-0.00741.3865-0.00390.5845-0.0089-0.1371.23050.36241.603861.97754.0913.975
107.8902-1.47311.73644.88581.64355.8538-0.36033.0793-0.9089-1.40660.0446-1.31850.32672.5650.08050.72350.15130.04782.38590.28882.404270.84951.6886.016
111.3843-2.6389-1.24768.4143-0.43973.8140.49920.9186-0.91430.0962-0.3459-0.16070.85591.4514-0.07020.910.345-0.23041.7761-0.13121.881573.0845.5113.096
122.5120.7948-0.18321.3883-0.372.65510.0187-0.31-0.21420.2083-0.2599-0.5358-0.13830.49620.21430.4142-0.0295-0.09350.48580.07020.704139.58662.42212.933
139.18474.7931-0.89034.42990.23823.15370.2302-0.8654-0.49620.3606-0.437-0.1958-0.1172-0.00580.18040.44550.0195-0.10780.49070.08360.469820.21956.96223.484
145.55053.2139-0.23084.1824-0.69371.60780.0632-0.2323-0.36080.1357-0.12320.0515-0.0731-0.02710.05580.35910.0585-0.06610.3904-0.00220.453120.76158.91613.575
154.7480.4412.51383.36842.63787.00880.27830.0141-1.18390.20240.17980.34871.2688-0.3532-0.4140.7544-0.0989-0.140.63310.19561.400624.02638.50814.995
167.20323.17015.49435.86962.16444.2953-0.47111.425-0.6832-0.65350.18220.5576-0.95680.96570.38081.105-0.089-0.03691.3617-0.50911.78467.38534.405-21.05
176.4002-2.07992.81342.7936-4.20626.52180.15290.2097-0.5887-0.8314-0.0865-1.1651.32190.72610.06311.01990.11460.05140.8842-0.38371.512310.39535.338-13.944
184.23931.09882.06392.26512.93236.58620.2101-0.8384-0.23180.3752-0.5676-0.32610.231-0.8640.35340.7637-0.0166-0.17970.84710.19591.661627.3339.78621.799
196.70870.86650.90825.3487-0.84912.9623-0.0562-0.2025-0.6749-0.0193-0.08620.01210.1582-0.18280.14630.5082-0.01080.07830.3897-0.11610.445541.82271.935-10.089
201.69330.1039-0.26483.3875-0.38042.0262-0.21030.5136-0.6231-0.7250.0525-0.33680.3385-0.02120.17590.7046-0.05290.15420.5073-0.21420.732248.13465.546-25.231
214.13793.72930.71834.0111-0.15432.554-0.28530.548-0.3499-0.92090.1295-0.4980.18610.06070.17130.6101-0.00220.09810.4712-0.1060.580850.51487.591-28.836
223.10381.1374-0.17784.3005-0.1481.0282-0.09950.01740.1441-0.2196-0.0151-0.25510.0456-0.15730.10520.55650.00720.04760.4522-0.09590.436448.74787.071-19.075
232.89962.53761.33962.68640.43212.5452-0.4004-0.0683-2.0902-0.59310.0928-0.26350.5856-0.12640.42921.21880.02180.42460.6483-0.18821.909743.98731.878-24.204
243.551-3.49731.31438.4367-2.86026.25990.38840.8843-1.5378-2.4043-0.3991-1.32040.93010.1334-0.06441.2504-0.00390.34780.8688-0.42281.552850.57535.126-33.089
251.463-1.73492.29976.6816-0.95514.28320.00960.7075-1.3671-0.78640.2521-0.63070.61740.5851-0.18670.9893-0.00510.41890.6948-0.33521.342251.92944.299-29.7
263.67891.27862.62764.57372.1345.56860.12460.5355-1.8978-0.51050.0412-0.36640.72610.0964-0.10070.8554-0.06840.24860.5159-0.31591.067651.81850.332-25.663
274.46776.22293.36188.96633.33265.97590.216-0.38190.00380.50640.1653-0.1560.3737-0.1163-0.36260.88940.06910.30060.5872-0.13521.595148.67242.428-20.014
285.2364-4.37685.04175.4274-1.92797.7675-0.08240.5072-0.46961.97630.334-0.2385-0.07940.6372-0.19050.87880.04140.09230.587-0.20261.444557.96153.157-14.541
299.4742-6.3683-3.0934.23171.81512.1899-1.8553-0.6568-0.69111.72742.2105-0.17980.03790.9644-0.42871.44910.1269-0.16570.8147-0.30091.650861.38337.982-12.573
303.3213-0.54392.27360.0883-0.37451.55350.8748-1.1861-0.22820.86750.1417-0.83790.70920.355-0.94091.19490.11010.03850.7348-0.21082.045855.55438.16-13.844
312.63510.365-0.62382.50790.40335.03890.96720.30050.78441.5880.7255-2.68270.9056-0.6533-1.48781.53280.0314-0.6371.0379-0.14192.292969.0739.583-11.725
329.43992.86810.39442.92860.92382.6162-0.12190.0528-0.00610.69610.62840.18981.17990.3575-0.44031.3120.11430.13360.6419-0.17251.875653.0828.518-22.188
331.05251.7978-0.985.3845-0.25051.94660.2597-0.24140.68181.37990.0107-0.4068-1.690.7803-0.07271.8558-0.2858-0.59430.8771-0.18542.119779.382147.9649.382
343.65312.9548-1.26773.33581.11344.92580.0092-1.22531.51810.94570.318-1.5573-1.07671.3103-0.41051.3524-0.2491-0.44410.9326-0.17191.756977.18138.00412.303
356.83190.5654-0.32162.64531.24975.97160.16350.4591.09790.1677-0.0731-1.2869-1.36910.8933-0.13981.142-0.3419-0.32550.75270.0751.643678.909135.878-1.44
368.2298-1.44690.61340.9158-1.80754.084-0.65740.5705-0.1441-0.6770.6448-0.8544-0.8661.2533-0.17171.4621-0.5542-0.04861.2809-0.08681.920390.009140.96-0.035
376.5051-6.34953.27746.0422-3.24856.9138-0.1499-0.60340.82880.32840.12290.2562-0.4911-0.63540.03740.55810.0104-0.04930.449-0.13370.908949.25121.29-5.072
381.1735-0.072-0.03222.5551-0.32692.1474-0.1638-0.12770.42830.3954-0.0878-0.5638-0.4760.15650.25410.5571-0.0247-0.12980.4525-0.0530.745659.984118.983-0.224
390.83661.4467-0.23222.8901-1.16292.49410.0593-0.2247-0.12240.7915-0.1689-0.59250.0431-0.09890.14140.5444-0.0263-0.12680.5226-0.05660.672153.91199.7979.85
402.0809-0.56210.77288.4433-0.80371.9513-0.0032-0.1209-0.19850.271-0.0215-0.126-0.0514-0.10730.0480.3623-0.0287-0.02980.422-0.05470.403252.508101.323-0.057
413.54541.2472-1.04374.49163.26066.65970.0562-0.131-0.81040.0210.3708-0.87820.92920.8837-0.47080.78420.1419-0.23490.6173-0.01931.298271.81893.8591.378
424.79396.3894.56348.99694.59119.377-0.4883-0.1545-0.9791-1.3244-0.55740.8522-0.8655-0.44771.10341.2073-0.00670.43610.9557-0.47581.881867.07177.431-34.673
439.5548-0.35263.95265.1727-0.05795.8820.51920.66030.4931-0.3201-0.2711-0.93910.11861.4-0.2250.7225-0.02370.39380.9325-0.14341.412167.74580.488-27.541
441.63120.0612-1.18314.7283.38953.1188-0.0851-0.13580.12761.1918-0.0748-0.32550.91470.0890.2140.9343-0.018-0.24180.7798-0.01561.663372.37697.3678.184
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 628:784 )A628 - 784
2X-RAY DIFFRACTION2( CHAIN A AND RESID 785:849 )A785 - 849
3X-RAY DIFFRACTION3( CHAIN A AND RESID 850:912 )A850 - 912
4X-RAY DIFFRACTION4( CHAIN B AND RESID 178:291 )B178 - 291
5X-RAY DIFFRACTION5( CHAIN B AND RESID 292:332 )B292 - 332
6X-RAY DIFFRACTION6( CHAIN B AND RESID 333:380 )B333 - 380
7X-RAY DIFFRACTION7( CHAIN C AND RESID 185:203 )C185 - 203
8X-RAY DIFFRACTION8( CHAIN C AND RESID 204:255 )C204 - 255
9X-RAY DIFFRACTION9( CHAIN C AND RESID 256:320 )C256 - 320
10X-RAY DIFFRACTION10( CHAIN C AND RESID 321:339 )C321 - 339
11X-RAY DIFFRACTION11( CHAIN C AND RESID 340:378 )C340 - 378
12X-RAY DIFFRACTION12( CHAIN D AND RESID 628:784 )D628 - 784
13X-RAY DIFFRACTION13( CHAIN D AND RESID 785:849 )D785 - 849
14X-RAY DIFFRACTION14( CHAIN D AND RESID 850:912 )D850 - 912
15X-RAY DIFFRACTION15( CHAIN E AND RESID 423:438 )E423 - 438
16X-RAY DIFFRACTION16( CHAIN E AND RESID 439:447 )E439 - 447
17X-RAY DIFFRACTION17( CHAIN F AND RESID 423:433 )F423 - 433
18X-RAY DIFFRACTION18( CHAIN F AND RESID 434:447 )F434 - 447
19X-RAY DIFFRACTION19( CHAIN H AND RESID 628:698 )H628 - 698
20X-RAY DIFFRACTION20( CHAIN H AND RESID 699:784 )H699 - 784
21X-RAY DIFFRACTION21( CHAIN H AND RESID 785:849 )H785 - 849
22X-RAY DIFFRACTION22( CHAIN H AND RESID 850:912 )H850 - 912
23X-RAY DIFFRACTION23( CHAIN I AND RESID 178:199 )I178 - 199
24X-RAY DIFFRACTION24( CHAIN I AND RESID 200:228 )I200 - 228
25X-RAY DIFFRACTION25( CHAIN I AND RESID 229:255 )I229 - 255
26X-RAY DIFFRACTION26( CHAIN I AND RESID 256:270 )I256 - 270
27X-RAY DIFFRACTION27( CHAIN I AND RESID 271:291 )I271 - 291
28X-RAY DIFFRACTION28( CHAIN I AND RESID 292:301 )I292 - 301
29X-RAY DIFFRACTION29( CHAIN I AND RESID 302:313 )I302 - 313
30X-RAY DIFFRACTION30( CHAIN I AND RESID 319:332 )I319 - 332
31X-RAY DIFFRACTION31( CHAIN I AND RESID 333:353 )I333 - 353
32X-RAY DIFFRACTION32( CHAIN I AND RESID 354:380 )I354 - 380
33X-RAY DIFFRACTION33( CHAIN J AND RESID 185:203 )J185 - 203
34X-RAY DIFFRACTION34( CHAIN J AND RESID 204:255 )J204 - 255
35X-RAY DIFFRACTION35( CHAIN J AND RESID 256:339 )J256 - 339
36X-RAY DIFFRACTION36( CHAIN J AND RESID 340:378 )J340 - 378
37X-RAY DIFFRACTION37( CHAIN K AND RESID 628:644 )K628 - 644
38X-RAY DIFFRACTION38( CHAIN K AND RESID 645:784 )K645 - 784
39X-RAY DIFFRACTION39( CHAIN K AND RESID 785:849 )K785 - 849
40X-RAY DIFFRACTION40( CHAIN K AND RESID 850:912 )K850 - 912
41X-RAY DIFFRACTION41( CHAIN L AND RESID 423:438 )L423 - 438
42X-RAY DIFFRACTION42( CHAIN L AND RESID 439:447 )L439 - 447
43X-RAY DIFFRACTION43( CHAIN M AND RESID 423:433 )M423 - 433
44X-RAY DIFFRACTION44( CHAIN M AND RESID 434:447 )M434 - 447

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