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- PDB-4pky: ARNT/HIF transcription factor/coactivator complex -

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Open data


ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4pky
TitleARNT/HIF transcription factor/coactivator complex
Components
  • Aryl hydrocarbon receptor nuclear translocator
  • Endothelial PAS domain-containing protein 1
  • Transforming acidic coiled-coil-containing protein 3
KeywordsTRANSCRIPTION/CELL CYCLE / PAS DOMAIN / ARNT-HIF TRANSCRIPTION FACTOR-COACTIVATOR COMPLEX / TRANSCRIPTION-CELL CYCLE complex
Function / homology
Function and homology information


interkinetic nuclear migration / myoblast fate commitment / microtubule cytoskeleton organization involved in mitosis / nuclear aryl hydrocarbon receptor complex / Aryl hydrocarbon receptor signalling / positive regulation of hormone biosynthetic process / astral microtubule organization / Cellular response to hypoxia / aryl hydrocarbon receptor complex / regulation of protein neddylation ...interkinetic nuclear migration / myoblast fate commitment / microtubule cytoskeleton organization involved in mitosis / nuclear aryl hydrocarbon receptor complex / Aryl hydrocarbon receptor signalling / positive regulation of hormone biosynthetic process / astral microtubule organization / Cellular response to hypoxia / aryl hydrocarbon receptor complex / regulation of protein neddylation / Transcriptional regulation of pluripotent stem cells / PTK6 Expression / metaphase/anaphase transition of mitotic cell cycle / positive regulation of protein sumoylation / norepinephrine metabolic process / Xenobiotics / regulation of microtubule-based process / surfactant homeostasis / Phase I - Functionalization of compounds / positive regulation of vascular endothelial growth factor receptor signaling pathway / epithelial cell maturation / Regulation of gene expression by Hypoxia-inducible Factor / aryl hydrocarbon receptor binding / hemopoiesis / centriolar satellite / positive regulation of vascular endothelial growth factor production / embryonic placenta development / blood vessel remodeling / Endogenous sterols / cis-regulatory region sequence-specific DNA binding / regulation of mitotic spindle organization / positive regulation of endothelial cell proliferation / NPAS4 regulates expression of target genes / visual perception / Pexophagy / positive regulation of glycolytic process / regulation of heart rate / mitochondrion organization / erythrocyte differentiation / neurogenesis / mitotic spindle organization / positive regulation of erythrocyte differentiation / RNA polymerase II transcription regulatory region sequence-specific DNA binding / lung development / mRNA transcription by RNA polymerase II / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / PPARA activates gene expression / mitotic spindle / cerebral cortex development / transcription coactivator binding / multicellular organismal-level iron ion homeostasis / negative regulation of inflammatory response / spindle pole / microtubule cytoskeleton organization / RNA polymerase II transcription regulator complex / nuclear receptor activity / sequence-specific double-stranded DNA binding / Neddylation / positive regulation of cold-induced thermogenesis / cellular response to oxidative stress / cellular response to hypoxia / DNA-binding transcription activator activity, RNA polymerase II-specific / angiogenesis / RNA polymerase II-specific DNA-binding transcription factor binding / response to oxidative stress / cell population proliferation / transcription regulator complex / sequence-specific DNA binding / postsynaptic density / cell differentiation / nuclear body / response to hypoxia / DNA-binding transcription factor activity, RNA polymerase II-specific / regulation of cell cycle / nuclear speck / protein heterodimerization activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / protein domain specific binding / cell division / intracellular membrane-bounded organelle / centrosome / glutamatergic synapse / chromatin / regulation of transcription by RNA polymerase II / signal transduction / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / cytoplasm / cytosol
Similarity search - Function
Transforming acidic coiled-coil-containing protein, C-terminal / TACC family / Transforming acidic coiled-coil-containing protein (TACC), C-terminal / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1700 / HIF-1 alpha, transactivation domain, C-terminal / HIF-1 alpha C terminal transactivation domain / Hypoxia-inducible factor, alpha subunit-like / Hypoxia-inducible factor-1 / Nuclear translocator / PAS fold ...Transforming acidic coiled-coil-containing protein, C-terminal / TACC family / Transforming acidic coiled-coil-containing protein (TACC), C-terminal / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1700 / HIF-1 alpha, transactivation domain, C-terminal / HIF-1 alpha C terminal transactivation domain / Hypoxia-inducible factor, alpha subunit-like / Hypoxia-inducible factor-1 / Nuclear translocator / PAS fold / Helix-loop-helix DNA-binding domain / PAC motif / Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) / PAS domain / PAS domain / Helix-loop-helix DNA-binding domain superfamily / helix loop helix domain / Myc-type, basic helix-loop-helix (bHLH) domain / Myc-type, basic helix-loop-helix (bHLH) domain profile. / Beta-Lactamase / PAS fold / PAS fold / PAS domain / PAS repeat profile. / PAS domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / PAS domain superfamily / Up-down Bundle / 2-Layer Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Aryl hydrocarbon receptor nuclear translocator / Endothelial PAS domain-containing protein 1 / Transforming acidic coiled-coil-containing protein 3
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.2 Å
AuthorsTomchick, D.R. / Partch, C.L. / Gardner, K.H.
CitationJournal: J.Biol.Chem. / Year: 2015
Title: Coiled-coil Coactivators Play a Structural Role Mediating Interactions in Hypoxia-inducible Factor Heterodimerization.
Authors: Guo, Y. / Scheuermann, T.H. / Partch, C.L. / Tomchick, D.R. / Gardner, K.H.
History
DepositionMay 15, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 11, 2015Provider: repository / Type: Initial release
Revision 1.1Apr 1, 2015Group: Database references
Revision 1.2Nov 22, 2017Group: Database references / Derived calculations ...Database references / Derived calculations / Other / Refinement description / Source and taxonomy
Category: citation / entity_src_gen ...citation / entity_src_gen / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / software
Item: _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag ..._citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Sep 27, 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 / refine_hist
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_nucleic_acid / _refine_hist.pdbx_number_atoms_protein

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Aryl hydrocarbon receptor nuclear translocator
B: Transforming acidic coiled-coil-containing protein 3
C: Transforming acidic coiled-coil-containing protein 3
D: Aryl hydrocarbon receptor nuclear translocator
E: Transforming acidic coiled-coil-containing protein 3
F: Transforming acidic coiled-coil-containing protein 3
G: Endothelial PAS domain-containing protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,4769
Polymers65,2837
Non-polymers1922
Water00
1
A: Aryl hydrocarbon receptor nuclear translocator
B: Transforming acidic coiled-coil-containing protein 3
C: Transforming acidic coiled-coil-containing protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,0655
Polymers25,8733
Non-polymers1922
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4150 Å2
ΔGint-47 kcal/mol
Surface area11990 Å2
MethodPISA
2
D: Aryl hydrocarbon receptor nuclear translocator
E: Transforming acidic coiled-coil-containing protein 3
F: Transforming acidic coiled-coil-containing protein 3


Theoretical massNumber of molelcules
Total (without water)25,8733
Polymers25,8733
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4000 Å2
ΔGint-44 kcal/mol
Surface area12160 Å2
MethodPISA
3
G: Endothelial PAS domain-containing protein 1


Theoretical massNumber of molelcules
Total (without water)13,5381
Polymers13,5381
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area5630 Å2
MethodPISA
Unit cell
Length a, b, c (Å)96.136, 96.136, 182.841
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number92
Space group name H-MP41212
DetailsThe biological unit is a heterotrimer consisting of one copy of molecule 1 and two copies of molecule 2. There are two biological units in the asymmetric unit (chains A, B & C and chains D, E & F). There is an additional molecule 3 that is not part of the biological unit, but is part of the crystalline lattice (chain G).

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Components

#1: Protein Aryl hydrocarbon receptor nuclear translocator / ARNT protein / Class E basic helix-loop-helix protein 2 / bHLHe2 / Dioxin receptor / nuclear ...ARNT protein / Class E basic helix-loop-helix protein 2 / bHLHe2 / Dioxin receptor / nuclear translocator / Hypoxia-inducible factor 1-beta / HIF1-beta


Mass: 14243.098 Da / Num. of mol.: 2 / Fragment: C-terminal PAS 2 domain residues 342-456
Source method: isolated from a genetically manipulated source
Details: The first six residues of the sequence (GEFKGL) are N-terminal cloning artifacts.
Source: (gene. exp.) Homo sapiens (human) / Gene: ARNT, BHLHE2 / Plasmid: pHis-GBeta1-parallel / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P27540
#2: Protein/peptide
Transforming acidic coiled-coil-containing protein 3 / ARNT-interacting protein


Mass: 5814.726 Da / Num. of mol.: 4 / Fragment: C-terminal domain Coiled coil residues 496-542
Source method: isolated from a genetically manipulated source
Details: The first three residues of the sequence (GEF) are N-terminal cloning artifacts.
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Tacc3, Aint / Plasmid: pHis-GBeta1-parallel / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9JJ11
#3: Protein Endothelial PAS domain-containing protein 1 / EPAS-1 / Basic-helix-loop-helix-PAS protein MOP2 / Class E basic helix-loop-helix protein 73 / ...EPAS-1 / Basic-helix-loop-helix-PAS protein MOP2 / Class E basic helix-loop-helix protein 73 / bHLHe73 / HIF-1-alpha-like factor / HLF / Hypoxia-inducible factor 2-alpha / HIF2-alpha / Member of PAS protein 2 / PAS domain-containing protein 2


Mass: 13538.300 Da / Num. of mol.: 1 / Fragment: C-terminal PAS 2 and PAC domain residues 239-350
Source method: isolated from a genetically manipulated source
Details: The first six residues of the sequence (GEFKGL) are N-terminal cloning artifacts.
Source: (gene. exp.) Homo sapiens (human) / Gene: EPAS1, BHLHE73, HIF2A, MOP2, PASD2 / Plasmid: pHis-GBeta1-parallel / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q99814
#4: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4

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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: 3.26 Å3/Da / Density % sol: 62.27 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6
Details: 1.6 M magnesium sulfate, 0.1 M MES pH 6.5, 20% (w/v) ethylene glycol
PH range: 6.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97951 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Aug 6, 2009 / Details: monochromator
RadiationMonochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97951 Å / Relative weight: 1
ReflectionResolution: 3.2→48.07 Å / Num. all: 14853 / Num. obs: 14853 / % possible obs: 99.9 % / Observed criterion σ(I): -3 / Redundancy: 7.2 % / Biso Wilson estimate: 52.78 Å2 / Rmerge(I) obs: 0.148 / Χ2: 0.916 / Net I/av σ(I): 11.571 / Net I/σ(I): 6.1 / Num. measured all: 106957
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique allΧ2% possible all
3.2-3.264.80.6291.37050.95398.7
3.26-3.315.67291.00499
3.31-3.386.37020.975100
3.38-3.456.67461.035100
3.45-3.527.10.9137121.043100
3.52-3.67.30.6537231.013100
3.6-3.697.50.5337371.031100
3.69-3.797.60.4197160.964100
3.79-3.917.70.3577401.007100
3.91-4.037.80.2877350.98100
4.03-4.187.80.2217290.939100
4.18-4.347.80.1557330.867100
4.34-4.547.80.147400.833100
4.54-4.787.80.1137340.815100
4.78-5.087.70.1057600.735100
5.08-5.477.70.1337380.818100
5.47-6.027.60.1497630.75699.7
6.02-6.897.40.1157720.767100
6.89-8.677.20.0727790.759100
8.67-506.70.0778601.14399.9

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
HKL-2000705adata reduction
PDB_EXTRACT3.14data extraction
PHASERphasing
PHENIX(phenix.refine: 1.9_1690)refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3F1O, 4LPZ

3f1o

4lpz


Resolution: 3.2→48.068 Å / SU ML: 0.47 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 27.98 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2698 626 4.87 %random
Rwork0.2313 12216 --
obs0.2332 12842 86.83 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 187.3 Å2 / Biso mean: 56.0709 Å2 / Biso min: 11.35 Å2
Refinement stepCycle: final / Resolution: 3.2→48.068 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4082 0 10 0 4092
Biso mean--52.7 --
Num. residues----497
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0084149
X-RAY DIFFRACTIONf_angle_d0.9265566
X-RAY DIFFRACTIONf_chiral_restr0.035627
X-RAY DIFFRACTIONf_plane_restr0.004707
X-RAY DIFFRACTIONf_dihedral_angle_d12.7531575
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 4

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.2-3.52250.3403890.32341669175849
3.5225-4.03190.29931700.24693373354397
4.0319-5.07890.22671720.194635043676100
5.0789-48.07340.26981950.233936703865100
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)
12.90262.14522.30672.6041-0.75438.05410.26030.1436-0.27770.0527-0.0949-0.74690.1575-0.1360.03680.20530.19790.04960.3688-0.01320.3937-0.7394120.208382.6709
25.45760.72041.89654.8974-2.67923.210.22660.181-0.8650.32150.3522.08450.4329-2.3345-0.09650.2649-0.06440.10640.5936-0.05260.6129-14.8455117.7002381.3818
35.6962-1.6179-3.00497.44622.65412.0724-0.05140.38280.1741-0.55760.4865-1.5342-0.4212-0.6074-0.19940.14960.0657-0.12590.405-0.09420.4638-0.0669120.7553374.6327
40.99150.9582-0.19351.0404-0.46940.78670.09320.4275-0.6263-0.1480.11480.66890.01-0.8077-0.1553-0.93230.3757-0.59390.45510.05590.6176-7.8821111.9744375.3324
54.5811-4.41950.33376.70423.55786.3371-0.4712-0.7585-2.00571.3825-0.04181.30120.5557-0.81240.50820.6365-0.1835-0.110.24940.13320.8479-11.0507107.7876386.7143
63.86760.90742.17526.5138-0.97265.18390.2821-0.5196-1.03220.2728-0.3611-0.6361-0.26970.3617-0.36920.0649-0.0855-0.08080.32580.03590.6792-1.759110.2474381.4329
71.8386-1.4998-2.48343.58162.53863.37130.7251-0.5123-0.91150.7921-0.0996-0.2730.05340.07120.07570.0423-0.0741-0.57660.38030.06750.9723-1.6525112.747385.4434
82.8386-1.7335-2.75142.23071.93172.7232-0.4063-1.01580.43850.6306-0.47030.3341-0.248-0.08740.42530.94360.29740.31711.20790.00840.9135-16.3372126.398392.8214
92.33630.05360.2322.9437-0.00991.0739-0.2961-0.24970.04520.5181-0.1332-0.6417-0.70430.32940.1890.29560.0272-0.10250.50980.12330.304-1.7676117.4175385.4854
102.91271.2521-2.64883.7073-3.55229.3557-0.2752-0.025-0.44190.4446-0.1275-0.2392-0.5149-0.49560.04760.470.03340.01970.1639-0.05970.27142.3752137.481370.0196
112.72762.0335-2.98914.2188-3.09196.5042-0.185-0.1653-0.27440.9664-0.8489-1.7214-1.32030.51610.06780.5176-0.0975-0.00770.3524-0.08420.2188.9435140.2498371.9804
124.41842.72131.10254.65821.96974.0350.025-0.39130.64560.65560.10090.8733-0.2976-0.5244-0.05730.5570.04480.17210.33950.02570.6023.147176.3669368.676
136.7465.2420.78449.87913.0936.20060.3227-0.09120.5167-0.2665-0.11040.0474-0.3925-0.0339-0.11150.43910.12390.11330.18750.09320.5438.1226178.5669365.7745
143.8139-2.52690.71214.96880.16066.6951-0.44020.19820.1157-0.43210.53070.4639-0.6426-0.3725-0.5050.4568-0.09710.15440.43610.09920.4272.3063170.4429360.7096
151.45240.4420.19353.9786-2.06493.1629-0.5439-0.03320.4799-0.21120.76340.024-0.3266-1.2969-0.55620.3429-0.1550.02120.20770.05320.30844.2593152.4652380.1102
162.46562.167-2.76043.2403-2.56534.9916-0.53530.0804-0.3165-0.4059-0.6012-1.37310.92290.26920.51520.7521-0.02490.03540.3653-0.0040.3799.5476149.1496377.8251
171.5632-3.1998-0.22618.8975-0.11439.5955-0.36920.11270.27140.5161-0.51840.14460.6787-0.14220.51420.74760.34990.02230.6607-0.0520.37847.1384129.5765358.301
184.57450.8395.49988.9872-1.80488.25780.52560.21470.0928-1.4059-0.4704-0.51850.62280.6766-0.20230.6750.04530.23261.0201-0.06260.762718.9532130.5732355.8154
192.0003-5.86888.36954.871-6.52638.8393-0.0038-1.75970.05341.1680.40331.3602-0.5817-0.0105-0.07161.01670.1213-0.09220.68140.13440.61018.4949126.9445366.1775
205.1217-0.8406-0.74756.6903-3.723.7501-0.4849-0.6769-0.5250.2970.4375-0.74090.95561.10850.18240.86270.3797-0.02270.87920.00230.818218.0874121.2443359.193
211.64760.55510.28390.66850.80121.87470.16210.1474-1.195-1.18450.49840.07970.22140.017-0.20762.21010.52450.19180.72750.1571.431915.5569122.7553342.6551
225.83010.26530.4175.7394-3.68557.855-0.36-0.1078-1.54190.4440.1333-0.22970.41020.57870.5681.4230.30280.13620.6427-0.04580.941810.886119.5891354.8626
234.08991.0209-1.01333.9781-4.53155.21480.17880.1477-1.2713-0.33180.39730.13420.47110.0193-0.29591.13560.2734-0.14430.5663-0.34041.02638.0228121.3621353.5653
243.27993.1741-2.4473.6154-3.23723.3463-0.5897-0.03880.1642-0.84530.2231-0.75430.55170.40510.08661.23410.108-0.16590.4132-0.03590.799411.927132.6958351.1032
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 361 through 367 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 368 through 372 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 373 through 391 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 392 through 401 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 402 through 418 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 419 through 435 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 436 through 446 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 447 through 455 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 456 through 464 )A0
10X-RAY DIFFRACTION10chain 'B' and (resid 583 through 631 )B0
11X-RAY DIFFRACTION11chain 'C' and (resid 583 through 629 )C0
12X-RAY DIFFRACTION12chain 'D' and (resid 361 through 418 )D0
13X-RAY DIFFRACTION13chain 'D' and (resid 419 through 447 )D0
14X-RAY DIFFRACTION14chain 'D' and (resid 448 through 464 )D0
15X-RAY DIFFRACTION15chain 'E' and (resid 582 through 631 )E0
16X-RAY DIFFRACTION16chain 'F' and (resid 583 through 631 )F0
17X-RAY DIFFRACTION17chain 'G' and (resid 239 through 248 )G0
18X-RAY DIFFRACTION18chain 'G' and (resid 249 through 258 )G0
19X-RAY DIFFRACTION19chain 'G' and (resid 259 through 264 )G0
20X-RAY DIFFRACTION20chain 'G' and (resid 265 through 285 )G0
21X-RAY DIFFRACTION21chain 'G' and (resid 286 through 299 )G0
22X-RAY DIFFRACTION22chain 'G' and (resid 300 through 315 )G0
23X-RAY DIFFRACTION23chain 'G' and (resid 316 through 324 )G0
24X-RAY DIFFRACTION24chain 'G' and (resid 325 through 344 )G0

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