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- PDB-5y6o: Crystal structure of DAXX N-terminal four-helix bundle domain (4H... -

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Basic information

Entry
Database: PDB / ID: 5y6o
TitleCrystal structure of DAXX N-terminal four-helix bundle domain (4HB) in complex with ATRX
ComponentsDeath domain-associated protein 6,Transcriptional regulator ATRX
KeywordsGENE REGULATION / Histone chaperone / Gene repressor
Function / homology
Function and homology information


post-embryonic forelimb morphogenesis / cellular response to diamide / Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations / Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations / SUMO-modified protein reader activity / neuron intrinsic apoptotic signaling pathway in response to oxidative stress / positive regulation of nuclear cell cycle DNA replication / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / chromosome organization involved in meiotic cell cycle / chromosome, subtelomeric region ...post-embryonic forelimb morphogenesis / cellular response to diamide / Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations / Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations / SUMO-modified protein reader activity / neuron intrinsic apoptotic signaling pathway in response to oxidative stress / positive regulation of nuclear cell cycle DNA replication / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / chromosome organization involved in meiotic cell cycle / chromosome, subtelomeric region / cellular response to sodium arsenite / Sertoli cell development / meiotic spindle organization / cellular response to hydroxyurea / DNA translocase activity / chromo shadow domain binding / positive regulation of telomere maintenance / condensed chromosome, centromeric region / transcription regulator inhibitor activity / ATP-dependent chromatin remodeler activity / protein localization to chromosome, telomeric region / nuclear androgen receptor binding / nuclear chromosome / seminiferous tubule development / replication fork processing / protein kinase activator activity / androgen receptor signaling pathway / chromosome, centromeric region / regulation of protein ubiquitination / DNA damage response, signal transduction by p53 class mediator / extrinsic apoptotic signaling pathway via death domain receptors / subtelomeric heterochromatin formation / positive regulation of protein kinase activity / cellular response to unfolded protein / heterochromatin / pericentric heterochromatin / JNK cascade / forebrain development / cellular response to copper ion / Inhibition of DNA recombination at telomere / heat shock protein binding / methylated histone binding / cellular response to cadmium ion / helicase activity / SUMOylation of transcription cofactors / molecular condensate scaffold activity / multicellular organism growth / chromatin DNA binding / PML body / HCMV Early Events / transcription corepressor activity / nucleosome assembly / Regulation of TP53 Degradation / p53 binding / chromatin organization / cellular response to heat / histone binding / spermatogenesis / regulation of gene expression / regulation of apoptotic process / DNA helicase / RNA polymerase II-specific DNA-binding transcription factor binding / transcription by RNA polymerase II / chromosome, telomeric region / transcription coactivator activity / nuclear body / chromatin remodeling / positive regulation of protein phosphorylation / negative regulation of gene expression / DNA repair / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / chromatin binding / regulation of DNA-templated transcription / nucleolus / protein kinase binding / enzyme binding / protein homodimerization activity / ATP hydrolysis activity / positive regulation of transcription by RNA polymerase II / nucleoplasm / ATP binding / nucleus / metal ion binding / cytosol
Similarity search - Function
ATRX, ADD domain / Cysteine Rich ADD domain / Daxx, N-terminal Rassf1C-interacting domain / Daxx, N-terminal domain superfamily / Daxx, histone-binding domain / Daxx, histone-binding domain superfamily / Daxx N-terminal Rassf1C-interacting domain / Death domain-associated protein 6, histone binding domain / ADD domain / ADD domain profile. ...ATRX, ADD domain / Cysteine Rich ADD domain / Daxx, N-terminal Rassf1C-interacting domain / Daxx, N-terminal domain superfamily / Daxx, histone-binding domain / Daxx, histone-binding domain superfamily / Daxx N-terminal Rassf1C-interacting domain / Death domain-associated protein 6, histone binding domain / ADD domain / ADD domain profile. / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / Helicase conserved C-terminal domain / Zinc finger, FYVE/PHD-type / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Zinc finger, RING/FYVE/PHD-type / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Transcriptional regulator ATRX / Death domain-associated protein 6
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å
AuthorsHuang, H. / Patel, D.J.
CitationJournal: Nat Commun / Year: 2017
Title: Crystal structure of DAXX N-terminal four-helix bundle domain (4HB) in complex with ATRX
Authors: Huang, H. / Patel, D.J.
History
DepositionAug 13, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 25, 2017Provider: repository / Type: Initial release
Revision 1.1Nov 22, 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

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Assembly

Deposited unit
A: Death domain-associated protein 6,Transcriptional regulator ATRX
B: Death domain-associated protein 6,Transcriptional regulator ATRX
C: Death domain-associated protein 6,Transcriptional regulator ATRX
D: Death domain-associated protein 6,Transcriptional regulator ATRX
E: Death domain-associated protein 6,Transcriptional regulator ATRX
F: Death domain-associated protein 6,Transcriptional regulator ATRX
G: Death domain-associated protein 6,Transcriptional regulator ATRX
H: Death domain-associated protein 6,Transcriptional regulator ATRX
I: Death domain-associated protein 6,Transcriptional regulator ATRX


Theoretical massNumber of molelcules
Total (without water)123,1819
Polymers123,1819
Non-polymers00
Water00
1
A: Death domain-associated protein 6,Transcriptional regulator ATRX
B: Death domain-associated protein 6,Transcriptional regulator ATRX
C: Death domain-associated protein 6,Transcriptional regulator ATRX


Theoretical massNumber of molelcules
Total (without water)41,0603
Polymers41,0603
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4610 Å2
ΔGint-31 kcal/mol
Surface area17930 Å2
MethodPISA
2
D: Death domain-associated protein 6,Transcriptional regulator ATRX
E: Death domain-associated protein 6,Transcriptional regulator ATRX
F: Death domain-associated protein 6,Transcriptional regulator ATRX


Theoretical massNumber of molelcules
Total (without water)41,0603
Polymers41,0603
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4880 Å2
ΔGint-33 kcal/mol
Surface area17980 Å2
MethodPISA
3
G: Death domain-associated protein 6,Transcriptional regulator ATRX
H: Death domain-associated protein 6,Transcriptional regulator ATRX
I: Death domain-associated protein 6,Transcriptional regulator ATRX


Theoretical massNumber of molelcules
Total (without water)41,0603
Polymers41,0603
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4930 Å2
ΔGint-32 kcal/mol
Surface area17570 Å2
MethodPISA
Unit cell
Length a, b, c (Å)78.666, 78.666, 503.215
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121

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Components

#1: Protein
Death domain-associated protein 6,Transcriptional regulator ATRX / Daxx / hDaxx / ETS1-associated protein 1 / EAP1 / Fas death domain-associated protein / ATP- ...Daxx / hDaxx / ETS1-associated protein 1 / EAP1 / Fas death domain-associated protein / ATP-dependent helicase ATRX / X-linked helicase II / X-linked nuclear protein / XNP / Znf-HX


Mass: 13686.805 Da / Num. of mol.: 9 / Fragment: UNP residues 50-144,UNP residues 1265-1288
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: DAXX, BING2, DAP6, ATRX, RAD54L, XH2 / Plasmid: RSFDuet
Details (production host): A modified RSFDuet plasmid with an N-terminal 6xHis-SUMO tag.
Production host: Escherichia coli (E. coli) / Strain (production host): BL21-CodonPlus(DE3)-RIL / References: UniProt: Q9UER7, UniProt: P46100, DNA helicase

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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: 3.65 Å3/Da / Density % sol: 69.61 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.8
Details: The DAXX 4HB_ATRX DBM fusion protein at 26 mg/ml was crystallized under conditions of 0.1M Sodium Cacodylate, pH 6.8, 1.2 M Ammonium Sulfate and 3% 1, 5- Diaminopentane Dihydrochloride, ...Details: The DAXX 4HB_ATRX DBM fusion protein at 26 mg/ml was crystallized under conditions of 0.1M Sodium Cacodylate, pH 6.8, 1.2 M Ammonium Sulfate and 3% 1, 5- Diaminopentane Dihydrochloride, using sitting-drop vapor-diffusion method at 293K. In this process, o.5 uL of protein was mixed with 0.5 uL of mother liquor. All the crystals were soaked in a cryoprotectant made from mother liquor supplemented with 25% glycerol before flash freezing in liquid nitrogen.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 10, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 3.1→167.74 Å / Num. obs: 34423 / % possible obs: 99.9 % / Redundancy: 8 % / CC1/2: 0.998 / Rmerge(I) obs: 0.091 / Rpim(I) all: 0.033 / Rrim(I) all: 0.097 / Net I/σ(I): 14.4
Reflection shellResolution: 3.1→3.27 Å / Redundancy: 6.9 % / Rmerge(I) obs: 1.344 / Mean I/σ(I) obs: 1.1 / Num. unique obs: 4917 / CC1/2: 0.615 / Rpim(I) all: 0.527 / Rrim(I) all: 1.449 / % possible all: 99.9

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Processing

Software
NameVersionClassification
PHENIX1.8.2_1309refinement
XDSdata processing
pointlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2KZS

2kzs


Resolution: 3.1→83.869 Å / SU ML: 0.55 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 32.44
RfactorNum. reflection% reflection
Rfree0.2972 1730 5.05 %
Rwork0.2238 --
obs0.2274 34234 99.64 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 72.9 Å2
Refinement stepCycle: LAST / Resolution: 3.1→83.869 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7467 0 0 0 7467
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.017595
X-RAY DIFFRACTIONf_angle_d1.43410248
X-RAY DIFFRACTIONf_dihedral_angle_d18.9582826
X-RAY DIFFRACTIONf_chiral_restr0.0991179
X-RAY DIFFRACTIONf_plane_restr0.0071310
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.1001-3.19130.39331460.35072568X-RAY DIFFRACTION97
3.1913-3.29430.38141400.32932661X-RAY DIFFRACTION100
3.2943-3.4120.37761500.32792683X-RAY DIFFRACTION100
3.412-3.54870.39011290.30692611X-RAY DIFFRACTION100
3.5487-3.71020.34431490.26612677X-RAY DIFFRACTION100
3.7102-3.90580.26991180.2372715X-RAY DIFFRACTION100
3.9058-4.15050.32451500.22522683X-RAY DIFFRACTION100
4.1505-4.47090.31051270.20982684X-RAY DIFFRACTION100
4.4709-4.92080.25011690.19012727X-RAY DIFFRACTION100
4.9208-5.63270.27761600.2022738X-RAY DIFFRACTION100
5.6327-7.09610.35361490.2492778X-RAY DIFFRACTION100
7.0961-83.89980.25221430.18892979X-RAY DIFFRACTION99
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)
11.0317-1.77180.7765.93962.88859.22290.57650.41110.4484-0.84920.22060.0144-0.979-0.66-0.44750.3368-0.0661-0.03640.3250.01080.553715.97591.477314.1362
24.68310.01250.02136.6959-3.33517.48160.703-1.14620.31180.56490.1851-0.6076-1.54160.4486-0.62420.6891-0.05460.10980.8506-0.32650.305920.10045.01423.3333
37.17664.9121-1.42653.8829-2.53225.0256-0.58270.2337-0.6944-1.26570.685-1.09890.6036-0.2982-0.07550.62450.15810.1910.7219-0.0330.671821.6326-4.772915.2854
42.9774-0.8167-1.36674.45891.8962.2403-0.1717-0.45470.3274-0.38130.5182-0.4098-0.90310.8523-0.39950.96850.012-0.05870.724-0.18170.419417.789217.505524.3811
53.33290.79810.59746.47021.1234.69190.35081.280.3162-0.5030.0928-0.70180.28470.3388-0.24240.71540.03590.15140.72140.0130.2179-4.59120.5549.6395
62.8452-2.0622-3.59327.1812.04068.79710.0752-1.4049-0.3530.88520.344-0.76650.79790.4489-0.48620.47120.1611-0.1080.5010.04650.3464-0.86520.6422.318
73.5065-4.5972-1.9962.01582.49126.27320.65950.8363-0.56-1.6666-0.90621.9271-0.2897-0.82640.24160.51360.08280.05260.8264-0.0920.3902-11.8162-0.741915.6856
87.0733-3.42782.33662.69060.87255.25820.6463-0.3923-0.18170.78320.1627-0.85231.15540.7555-0.70090.7531-0.00120.170.83110.09770.206314.2522-8.195329.2416
90.64090.40140.350.3033-0.02972.921-0.22510.7683-0.6589-0.4350.391-0.58320.47340.31190.20191.0308-0.06660.33211.4167-0.87890.31424.709419.60447.2784
100.84831.6183-1.23344.4568-0.54355.8085-0.12190.3507-0.7009-0.00850.0512-0.1624-0.19090.59090.12660.4335-0.0490.19740.6244-0.19750.66333.122717.770818.3887
116.04331.98011.89883.8254-0.54853.6256-0.32670.71260.564-0.75710.56641.4969-1.3535-0.8127-0.161.12490.2546-0.09780.43980.09780.6637-5.524229.333311.8282
120.687-0.4037-0.7431.00940.73440.9079-0.22860.29680.6028-0.73540.585-0.8748-0.60580.5318-0.15051.5527-0.54440.5540.6886-0.33191.1299.196328.5756.0038
136.0059-2.2074.76325.5555-3.93554.78980.27520.57180.4324-0.7906-0.7543-0.99240.17120.57210.5470.7376-0.19190.26670.4516-0.18110.965411.35425.745815.5149
144.59075.0565-3.62736.1133-4.76013.91780.16220.13810.185-0.74020.15380.5417-0.90910.0301-0.28380.97830.2252-0.02610.7711-0.78710.7837-9.08525.143121.823
155.41053.16291.9815.4697-0.0398.70180.0582-0.4384-0.39580.80770.47450.37950.9108-1.0919-0.31060.7751-0.02360.31750.81570.04490.4728-8.87443.063130.7357
162.3535-2.55541.29063.8819-1.7564.2759-0.4993-1.1366-0.61881.14130.11431.27420.30010.0320.47380.8207-0.23890.24991.3630.00060.744915.463453.702444.3437
177.16765.2893-2.03234.2748-0.54343.0108-0.54870.6620.8986-0.44860.47562.0784-0.7714-0.0751-0.15171.2948-0.6917-0.33340.78050.38880.85977.576559.817629.4174
184.60220.07640.06095.4447-0.38496.80910.2293-0.32580.05160.23290.349-0.3133-0.93711.0281-0.60870.9357-0.35350.04840.9184-0.04090.379320.756458.654839.9259
191.3249-0.0981-0.55850.3854-0.5731.25560.2147-0.1085-0.1151-0.37650.6715-0.1128-0.14590.09290.33190.7582-0.88250.75851.6644-0.0041.517928.380243.839531.6123
204.6988-0.5113.24663.8745-1.30588.27330.611.6404-0.7872-0.2922-0.6708-0.33180.7156-0.1364-0.12451.12850.03180.22080.874-0.09930.453310.529437.062124.9796
215.85091.0618-0.80657.11831.27173.858-0.3625-1.9201-0.52861.2073-0.52680.0308-0.33120.09060.26340.9250.1529-0.1740.80830.07280.2654-4.078453.124547.4843
225.16530.9763-0.8245.3025-2.75571.45430.41410.81521.0494-0.8711-0.2607-0.7018-0.65470.5298-0.21670.2729-0.06760.17820.62540.31850.4759-1.411156.487335.5003
231.68852.2364-2.23277.7571-7.00457.73210.25920.15410.17930.255-0.08470.0852-1.3048-0.6104-0.12520.73780.1239-0.02031.334-0.66040.5005-7.606767.235147.8316
246.5241.80230.88995.3287-0.59285.44230.5789-0.0877-0.04410.0281-0.29150.83050.1896-0.7037-0.24650.77220.2937-0.12510.5443-0.08040.327-13.200353.366141.9894
250.03770.4087-0.26774.5162-2.31083.3645-0.2235-0.6088-0.38290.47540.50990.79490.0376-0.08590.21430.79490.4011-0.1411.01720.69880.69870.016173.745138.1919
261.2482-0.0622-0.34011.8085-2.43043.43080.26120.18010.0117-0.2096-0.0262-0.1209-0.33390.56740.56091.6954-0.90210.0051.30790.42480.157317.973464.392326.3786
273.79241.8541-2.18177.9437-3.97242.7332-0.4457-0.0457-0.11081.15520.4561-0.33710.1096-0.1148-0.0680.95060.0134-0.01830.6121-0.13390.42113.290735.117841.0805
282.4181-0.97661.6885.9092-2.82992.82690.53890.7459-0.91440.3619-0.2244-0.60330.8782.4983-0.26460.755-0.0238-0.01461.0447-0.08550.522311.704629.698738.7122
292.5302-0.43631.63651.3314-0.56562.06630.1461-0.25590.083-0.0550.3970.20070.2494-0.16050.27941.1517-0.2336-0.37151.1134-0.75190.0555-12.336336.655630.7879
303.4638-2.27450.47064.06180.38854.37150.2725-0.2333-0.3413-0.20710.40220.38040.2997-1.5044-0.70571.07380.1368-0.23291.3038-0.00120.176-9.853955.921326.7123
312.0641-2.7163-2.36113.88662.15276.16350.4352-0.0660.3737-1.45860.1683-0.50620.80990.6579-0.28961.3044-0.21930.3430.4363-0.00730.6461-4.411734.066563.6114
326.51154.9660.81026.8373.52532.8670.3985-0.27720.3556-0.54170.05840.84170.1052-0.6621-0.5340.57490.0186-0.07320.41410.20240.6417-3.043341.229780.45
337.32613.0913.69754.93835.03745.18940.3083-0.4163-1.18381.55320.3206-0.77462.20460.6039-0.62460.76590.10090.01170.50210.07530.5331-2.56230.043376.9502
348.73423.32831.36219.18555.14064.78220.37090.7814-0.9993-0.19610.4434-0.6711.4790.486-0.6361.26720.2814-0.03311.0509-0.43240.6967-5.67922.491465.2292
358.3606-1.7260.78742.69192.00032.04770.0338-0.15860.176-0.69810.57911.5164-0.126-0.572-0.51060.9413-0.19720.18190.53490.13210.5118-14.093736.88766.3675
364.4739-2.26782.0932.2792-0.38054.057-0.2341-0.6885-0.87450.51710.12750.42061.42130.1915-0.05981.06010.04620.130.72250.23430.36042.076229.404977.5084
375.9707-2.60912.21324.7901-1.34470.8776-0.43530.6808-0.58130.63810.19750.0331-0.7105-0.40080.1810.84150.2356-0.11650.7267-0.1470.33643.29152.531773.3129
386.7327-1.2035-5.49574.64770.68658.64550.10190.0741.5247-0.75890.4605-0.1752-0.77080.3816-0.59291.2614-0.0671-0.13760.52050.00870.42743.650562.506871.9294
396.28311.8625-1.91810.6691-0.76631.13020.0883-0.49641.1786-0.16520.4923-0.006-0.53160.676-0.24660.77570.1491-0.02760.5858-0.17730.3687.787659.000680.4631
404.17751.06151.3472.209-1.06741.55790.4807-0.532-0.54750.29010.33421.204-0.3381-1.0776-0.32790.9246-0.04840.34551.054-0.34830.3115-11.943837.755484.7303
412.47880.4246-0.7253.3887-0.14944.36310.58770.2989-0.1365-0.9886-0.2749-0.1246-0.36850.8345-0.3011.01450.2303-0.0321.02990.00830.447818.679636.933165.1244
422.1238-1.07710.70223.3746-2.88623.57910.38910.4827-0.4331-0.4888-0.491-0.29010.6650.3408-0.2831.22090.6506-0.03280.7333-0.05570.132418.794728.115469.7084
430.653-0.493-0.85962.2472-0.44581.79160.5247-0.20520.31870.7257-0.3043-0.58510.25240.8614-0.11551.05620.1348-0.2351.7545-0.18170.326812.846651.829986.6209
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 56 through 82 )
2X-RAY DIFFRACTION2chain 'A' and (resid 83 through 94 )
3X-RAY DIFFRACTION3chain 'A' and (resid 95 through 133 )
4X-RAY DIFFRACTION4chain 'A' and (resid 134 through 164 )
5X-RAY DIFFRACTION5chain 'B' and (resid 56 through 77 )
6X-RAY DIFFRACTION6chain 'B' and (resid 78 through 93 )
7X-RAY DIFFRACTION7chain 'B' and (resid 94 through 136 )
8X-RAY DIFFRACTION8chain 'B' and (resid 137 through 164 )
9X-RAY DIFFRACTION9chain 'C' and (resid 57 through 80 )
10X-RAY DIFFRACTION10chain 'C' and (resid 81 through 93 )
11X-RAY DIFFRACTION11chain 'C' and (resid 94 through 102 )
12X-RAY DIFFRACTION12chain 'C' and (resid 103 through 118 )
13X-RAY DIFFRACTION13chain 'C' and (resid 119 through 135 )
14X-RAY DIFFRACTION14chain 'C' and (resid 136 through 146 )
15X-RAY DIFFRACTION15chain 'C' and (resid 147 through 164 )
16X-RAY DIFFRACTION16chain 'D' and (resid 58 through 77 )
17X-RAY DIFFRACTION17chain 'D' and (resid 78 through 82 )
18X-RAY DIFFRACTION18chain 'D' and (resid 83 through 136 )
19X-RAY DIFFRACTION19chain 'D' and (resid 137 through 146 )
20X-RAY DIFFRACTION20chain 'D' and (resid 147 through 165 )
21X-RAY DIFFRACTION21chain 'E' and (resid 58 through 77 )
22X-RAY DIFFRACTION22chain 'E' and (resid 78 through 93 )
23X-RAY DIFFRACTION23chain 'E' and (resid 94 through 102 )
24X-RAY DIFFRACTION24chain 'E' and (resid 103 through 136 )
25X-RAY DIFFRACTION25chain 'E' and (resid 137 through 147 )
26X-RAY DIFFRACTION26chain 'E' and (resid 148 through 165 )
27X-RAY DIFFRACTION27chain 'F' and (resid 58 through 103 )
28X-RAY DIFFRACTION28chain 'F' and (resid 104 through 136 )
29X-RAY DIFFRACTION29chain 'F' and (resid 137 through 148 )
30X-RAY DIFFRACTION30chain 'F' and (resid 149 through 163 )
31X-RAY DIFFRACTION31chain 'G' and (resid 57 through 73 )
32X-RAY DIFFRACTION32chain 'G' and (resid 74 through 82 )
33X-RAY DIFFRACTION33chain 'G' and (resid 83 through 92 )
34X-RAY DIFFRACTION34chain 'G' and (resid 93 through 102 )
35X-RAY DIFFRACTION35chain 'G' and (resid 103 through 119 )
36X-RAY DIFFRACTION36chain 'G' and (resid 120 through 165 )
37X-RAY DIFFRACTION37chain 'H' and (resid 57 through 93 )
38X-RAY DIFFRACTION38chain 'H' and (resid 94 through 119 )
39X-RAY DIFFRACTION39chain 'H' and (resid 120 through 136 )
40X-RAY DIFFRACTION40chain 'H' and (resid 137 through 164 )
41X-RAY DIFFRACTION41chain 'I' and (resid 58 through 118 )
42X-RAY DIFFRACTION42chain 'I' and (resid 119 through 135 )
43X-RAY DIFFRACTION43chain 'I' and (resid 136 through 164 )

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