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- PDB-4j6i: Discovery of thiazolobenzoxepin PI3-kinase inhibitors that spare ... -

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Basic information

Entry
Database: PDB / ID: 4j6i
TitleDiscovery of thiazolobenzoxepin PI3-kinase inhibitors that spare the PI3-kinase beta isoform
ComponentsPhosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
KeywordsTransferase/Transferase Inhibitor / beta-sparing / SBDD / catalytic subunit gamma / phosphorylation / Transferase-Transferase Inhibitor complex
Function / homology
Function and homology information


secretory granule localization / negative regulation of triglyceride catabolic process / natural killer cell chemotaxis / neutrophil extravasation / phosphatidylinositol-4-phosphate 3-kinase / regulation of calcium ion transmembrane transport / positive regulation of acute inflammatory response / respiratory burst involved in defense response / negative regulation of cardiac muscle contraction / T cell chemotaxis ...secretory granule localization / negative regulation of triglyceride catabolic process / natural killer cell chemotaxis / neutrophil extravasation / phosphatidylinositol-4-phosphate 3-kinase / regulation of calcium ion transmembrane transport / positive regulation of acute inflammatory response / respiratory burst involved in defense response / negative regulation of cardiac muscle contraction / T cell chemotaxis / negative regulation of fibroblast apoptotic process / phosphatidylinositol 3-kinase complex, class IB / sphingosine-1-phosphate receptor signaling pathway / dendritic cell chemotaxis / 1-phosphatidylinositol-4-phosphate 3-kinase activity / 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity / phosphatidylinositol-4,5-bisphosphate 3-kinase / phosphatidylinositol 3-kinase / phosphatidylinositol 3-kinase complex, class IA / phosphatidylinositol-3-phosphate biosynthetic process / 1-phosphatidylinositol-3-kinase activity / mast cell degranulation / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / hepatocyte apoptotic process / positive regulation of Rac protein signal transduction / regulation of cell adhesion mediated by integrin / Synthesis of PIPs at the plasma membrane / phosphatidylinositol phosphate biosynthetic process / regulation of angiogenesis / T cell proliferation / cellular response to cAMP / GPVI-mediated activation cascade / T cell activation / ephrin receptor binding / neutrophil chemotaxis / positive regulation of endothelial cell migration / phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of cytokine production / positive regulation of MAP kinase activity / platelet aggregation / endocytosis / G beta:gamma signalling through PI3Kgamma / Signaling by CSF1 (M-CSF) in myeloid cells / kinase activity / positive regulation of cytosolic calcium ion concentration / angiogenesis / adaptive immune response / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / non-specific serine/threonine protein kinase / protein kinase activity / immune response / inflammatory response / G protein-coupled receptor signaling pathway / phosphorylation / protein serine kinase activity / innate immune response / protein serine/threonine kinase activity / ATP binding / membrane / identical protein binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
PIK3 catalytic subunit gamma, adaptor-binding domain / PIK3 catalytic subunit gamma adaptor-binding domain / Phosphatidylinositol 3-/4-kinase, catalytic domain / Phosphatidylinositol 3-kinase, accessory domain (PIK) / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, Domain 5 / C2 domain / Phosphatidylinositol 3-kinase, adaptor-binding domain / Phosphatidylinositol 3-kinase adaptor-binding (PI3K ABD) domain profile. ...PIK3 catalytic subunit gamma, adaptor-binding domain / PIK3 catalytic subunit gamma adaptor-binding domain / Phosphatidylinositol 3-/4-kinase, catalytic domain / Phosphatidylinositol 3-kinase, accessory domain (PIK) / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, Domain 5 / C2 domain / Phosphatidylinositol 3-kinase, adaptor-binding domain / Phosphatidylinositol 3-kinase adaptor-binding (PI3K ABD) domain profile. / PI3-kinase family, Ras-binding domain / Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain / PI3-kinase family, ras-binding domain / Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain profile. / Phosphoinositide 3-kinase C2 / Phosphoinositide 3-kinase, region postulated to contain C2 domain / C2 phosphatidylinositol 3-kinase-type domain / C2 phosphatidylinositol 3-kinase (PI3K)-type domain profile. / Phosphoinositide 3-kinase, accessory (PIK) domain superfamily / Phosphoinositide 3-kinase family, accessory domain (PIK domain) / Phosphoinositide 3-kinase family, accessory domain (PIK domain) / Phosphoinositide 3-kinase, accessory (PIK) domain / Phosphatidylinositol kinase / PIK helical domain profile. / Phosphatidylinositol 3- and 4-kinases signature 1. / Phosphatidylinositol 3/4-kinase, conserved site / Phosphatidylinositol 3- and 4-kinases signature 2. / Phosphatidylinositol 3-/4-kinase, catalytic domain superfamily / Phosphoinositide 3-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinase / Phosphatidylinositol 3- and 4-kinases catalytic domain profile. / Phosphatidylinositol 3-/4-kinase, catalytic domain / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / C2 domain superfamily / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Ubiquitin-like (UB roll) / Alpha Horseshoe / Armadillo-type fold / Ubiquitin-like domain superfamily / Roll / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-1JV / Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.9 Å
AuthorsMurray, J.M. / Rouge, L. / Wu, P.
CitationJournal: Bioorg.Med.Chem.Lett. / Year: 2013
Title: Discovery of thiazolobenzoxepin PI3-kinase inhibitors that spare the PI3-kinase beta isoform.
Authors: Staben, S.T. / Ndubaku, C. / Blaquiere, N. / Belvin, M. / Bull, R.J. / Dudley, D. / Edgar, K. / Gray, D. / Heald, R. / Heffron, T.P. / Jones, G.E. / Jones, M. / Kolesnikov, A. / Lee, L. / ...Authors: Staben, S.T. / Ndubaku, C. / Blaquiere, N. / Belvin, M. / Bull, R.J. / Dudley, D. / Edgar, K. / Gray, D. / Heald, R. / Heffron, T.P. / Jones, G.E. / Jones, M. / Kolesnikov, A. / Lee, L. / Lesnick, J. / Lewis, C. / Murray, J. / McLean, N.J. / Nonomiya, J. / Olivero, A.G. / Ord, R. / Pang, J. / Price, S. / Prior, W.W. / Rouge, L. / Salphati, L. / Sampath, D. / Wallin, J. / Wang, L. / Wei, B. / Weismann, C. / Wu, P.
History
DepositionFeb 11, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 28, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,2182
Polymers110,7271
Non-polymers4911
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)143.671, 67.161, 106.655
Angle α, β, γ (deg.)90.000, 95.430, 90.000
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform / PI3-kinase subunit gamma / PI3K-gamma / PI3Kgamma / PtdIns-3-kinase subunit gamma / ...PI3-kinase subunit gamma / PI3K-gamma / PI3Kgamma / PtdIns-3-kinase subunit gamma / Phosphatidylinositol 4 / 5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma / PtdIns-3-kinase subunit p110-gamma / p110gamma / Phosphoinositide-3-kinase catalytic gamma polypeptide / Serine/threonine protein kinase PIK3CG / p120-PI3K


Mass: 110727.102 Da / Num. of mol.: 1 / Fragment: UNP residues 144-1102
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: p110 gamma, PIK3CG / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Sf9
References: UniProt: P48736, phosphatidylinositol-4,5-bisphosphate 3-kinase, non-specific serine/threonine protein kinase
#2: Chemical ChemComp-1JV / 2-methyl-1-(4-{2-[1-(2,2,2-trifluoroethyl)-1H-1,2,4-triazol-5-yl]-4,5-dihydro[1]benzoxepino[5,4-d][1,3]thiazol-8-yl}-1H-pyrazol-1-yl)propan-2-ol


Mass: 490.501 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C22H21F3N6O2S

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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: 2.31 Å3/Da / Density % sol: 46.82 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: PEG 3350, 0.2M NH4SO4, 0.1M Tris-HCl 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 0.97946 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: May 20, 2009
RadiationMonochromator: Side scattering I-beam bent single crystal / Protocol: SINGLE / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97946 Å / Relative weight: 1
ReflectionResolution: 2.87→50 Å / Num. obs: 22879 / % possible obs: 97.5 % / Redundancy: 3.6 % / Biso Wilson estimate: 83 Å2 / Rmerge(I) obs: 0.055 / Χ2: 1.034 / Net I/σ(I): 12.5
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
2.87-2.972.70.44618901.036181.6
2.97-3.093.10.39222001.083194.4
3.09-3.233.50.30223191.047199.6
3.23-3.43.70.19823321.014199.9
3.4-3.623.80.12323380.995199.9
3.62-3.893.80.08123231.001199.9
3.89-4.293.80.05523411.045199.9
4.29-4.913.80.04423541.041100
4.91-6.183.70.05123621.03199.8
6.18-503.60.02424201.063199.7

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
SCALEPACKdata scaling
PHASERphasing
PHENIX1.8_1068refinement
PDB_EXTRACT3.11data extraction
ADSCQuantumdata collection
HKL-3000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.9→19.85 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.35 / σ(F): 1.34 / Phase error: 28.89 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2508 1115 5.01 %
Rwork0.2053 --
obs0.2077 22244 98.26 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 215.37 Å2 / Biso mean: 94.9072 Å2 / Biso min: 34.99 Å2
Refinement stepCycle: LAST / Resolution: 2.9→19.85 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6749 0 34 0 6783
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0136966
X-RAY DIFFRACTIONf_angle_d1.9829432
X-RAY DIFFRACTIONf_chiral_restr0.0921056
X-RAY DIFFRACTIONf_plane_restr0.0121195
X-RAY DIFFRACTIONf_dihedral_angle_d15.3982589
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 8

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.9-3.03160.31551040.26592391249589
3.0316-3.19080.33311540.26572598275298
3.1908-3.38980.31511170.242826742791100
3.3898-3.650.27431540.216526652819100
3.65-4.01460.29031410.208326662807100
4.0146-4.58920.22741550.186526792834100
4.5892-5.75850.26471460.197726962842100
5.7585-19.850.19721440.189927602904100
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)
13.0053-0.1197-0.3051.49-2.08522.9741-0.19571.18-1.4068-1.1089-0.34890.27811.0734-0.30410.37280.8470.0537-0.19691.0842-0.47761.136228.673528.9684.5896
20.94910.3918-1.13620.9623-0.59051.383-0.5480.4182-0.657-0.5069-0.2947-0.37030.23970.21750.24940.9704-0.005-0.00481.2032-0.48890.858244.29134.29256.6338
31.13280.8313-0.51190.8513-0.66230.5746-0.28560.594-0.88180.0708-0.28651.08250.57810.03270.06260.70980.26170.0836-0.7253-0.90861.21138.505624.97417.4798
42.9037-0.49930.25771.2966-0.33033.94770.0257-0.2198-0.7994-0.0097-0.0960.14120.6333-0.6417-0.04480.561-0.0933-0.09220.630.14521.153320.091731.34333.3347
55.87840.91590.76620.6996-0.53760.89250.0149-0.78080.36360.6738-0.0922-0.1135-0.3087-0.21070.16261.91170.27940.22271.82680.06691.184415.586247.923249.2835
62.8007-0.32291.07952.1987-0.68332.5529-0.0162-1.42840.0447-0.1305-0.20520.46910.2782-0.9950.22870.5624-0.01130.1221.60680.37331.30881.908335.699341.3965
73.09430.01130.49780.58411.2042.521-0.0783-0.0621-1.61250.0501-0.55610.57720.69940.01720.57630.848-0.16380.08631.0317-0.08381.32174.001328.329331.3069
82.8661-0.16621.18772.7218-1.88366.57670.8743-0.2465-0.52470.00950.17510.0010.2782-0.2678-0.60080.882-0.08790.25110.7420.08930.849912.076434.911332.601
93.7848-0.67630.60323.25341.75693.4772-0.35170.1745-0.1989-0.2194-0.0769-0.4981-0.7437-0.1870.17330.98860.04370.28190.95250.06350.671714.295742.065239.5503
103.43780.13270.89120.0714-0.08180.42020.1152-0.2058-0.0264-0.00480.08060.8627-1.0234-0.3198-0.33050.82610.27110.24491.3554-0.06591.39216.786247.316636.9395
110.94111.29470.34721.78190.46640.1522-0.54030.19540.2011-0.2561-0.03150.61240.2703-1.09260.47350.543-0.12770.03031.2322-0.13361.35945.892530.063626.9374
122.11550.33891.38763.3789-1.78912.1297-0.38620.4381-0.4534-1.67760.4694-0.41811.07320.4618-0.01181.1619-0.0570.03070.6425-0.39761.268420.338722.496715.9483
131.87430.8426-0.71884.4904-1.50654.4071-0.3496-0.0288-0.5581-0.74790.3771-0.57150.83060.54910.19390.67320.20870.04481.2978-0.09770.621269.472436.648312.6487
140.0610.07360.06980.09930.07210.0623-0.2919-0.35581.5131-0.9536-0.36710.692-0.2158-0.05650.62411.2002-0.12530.081.33650.21161.353561.366259.26352.3007
151.82210.3614-0.85722.0429-0.94381.91290.15730.1893-0.2649-0.0724-0.174-0.1501-0.15470.48420.01240.4931-0.0302-0.04630.9311-0.15490.616766.884943.15516.217
162.52230.4258-1.04510.3011-1.07533.7434-0.32140.11890.62380.0566-0.3373-0.3426-0.82710.4530.44940.6005-0.1425-0.0620.8192-0.04160.593361.261247.98514.9897
174.55860.47350.00730.7711.28462.2323-0.17230.7035-0.3878-0.4248-0.060.1782-0.4716-0.22790.25860.72310.143-0.00860.6015-0.03060.410657.132344.060314.4501
182.292-1.0483-0.60191.24350.05560.22150.15040.1638-0.07080.0158-0.04060.0950.1473-0.40140.08290.83750.158300.519-0.24451.015154.613625.665217.924
190.99960.849-0.29970.785-0.60562.3640.0730.8425-0.8509-0.8132-0.1414-0.01120.62130.28290.08330.6590.18380.040.9516-0.30680.594459.645935.69958.662
204.77651.55340.96221.80733.09556.2410.7850.121.0844-0.24360.04820.3136-0.2426-0.2242-0.44050.8602-0.17030.24960.9328-0.11170.751251.147853.226411.6376
215.2574-0.8396-2.22012.9198-1.66144.2103-0.4674-0.07660.70480.125-0.5256-0.0084-0.95780.77910.8030.6899-0.2027-0.18370.7733-0.11880.691350.509949.161520.8611
221.6342-0.1447-0.29624.90320.51030.0996-0.15960.5199-0.257-0.20830.4144-0.34330.41980.1858-0.11360.43050.20020.03540.8168-0.20820.407550.259342.005711.6702
230.82490.8682-1.15230.9353-1.24261.6377-0.01360.36680.0349-0.59980.1333-0.3169-0.33610.2713-0.10170.9407-0.09480.07321.65750.00470.647149.388646.49540.4935
244.21382.09860.39184.090.91885.8400.87520.2631-0.63260.41540.23130.0662-0.2064-0.31020.6757-0.12520.08030.8990.02240.673558.840145.78094.6711
250.96810.9164-0.25411.0504-1.06664.0210.3315-0.0728-0.27560.3036-0.041-0.52930.64010.6338-0.29090.9130.29920.19541.1856-0.11670.89466.866432.75210.4962
268.3323-4.05043.92033.8255-3.43598.9182-0.1242-1.1812-0.10590.97360.2195-0.7733-0.20880.63770.23690.75840.1792-0.21560.93020.03180.652658.65743.035554.8045
274.6517-1.60840.11182.46580.39673.1634-0.79520.15690.37380.17570.8361-0.29810.5967-0.3714-0.07950.6436-0.0445-0.06171.07550.01740.642958.351241.337145.2701
283.9288-0.1552-1.0352.97990.44863.3254-0.2799-0.2495-0.481-0.04970.0088-0.50160.53570.43470.22170.49090.0132-0.07790.62920.08340.581557.976833.743638.3253
292.1056-0.1735-0.50530.65340.30611.43760.0772-0.7237-0.53960.90310.12110.29910.12320.0086-0.1880.7725-0.06110.03340.54940.16440.601646.08135.912939.2907
305.95131.1483-0.14292.3509-1.09822.69580.207-0.4225-0.42930.57110.09760.65970.2941-0.2878-0.33710.65020.06770.01160.53840.17380.676441.77232.308635.1306
312.989-0.45880.73271.9338-0.372.22420.14570.3358-0.7241-0.054-0.07930.19370.0872-0.0595-0.06150.4026-0.0271-0.01750.3154-0.11580.470834.898537.371722.1667
322.8973-0.3008-0.07867.2106-1.94764.10370.08891.6109-0.0747-0.6678-0.12760.2922-0.0021-1.203-0.1130.50150.149-0.0531.0319-0.01060.559821.974346.78398.8733
332.80050.1374-0.55462.3269-0.72412.70290.16690.82230.1818-0.4172-0.11710.6454-0.3529-0.5914-0.0010.73390.2361-0.09640.8870.06240.686414.469653.609112.8232
343.498-0.52460.62362.161-0.13672.3613-0.1217-0.29230.95630.7991-0.13620.5929-0.5861-0.40610.12170.82990.0850.14170.4787-0.17230.795322.553562.613932.2646
351.2302-0.68251.03381.3264-1.28641.7922-0.1249-1.04811.1840.2238-0.3708-0.2653-1.2124-0.31630.31761.6763-0.0151-0.00770.787-0.46771.257426.629774.331841.5182
361.92010.23930.24031.03350.59240.4287-0.1486-0.78890.39621.29550.111-0.0847-0.2475-0.2708-0.19051.19440.1006-0.00220.7619-0.17910.494334.511856.725642.422
370.08760.05410.02310.02870.0130.00580.13560.01920.24280.5784-0.0076-0.4576-0.04810.961-0.21541.4316-0.49860.13381.1783-0.16781.042548.326156.848525.5456
382.9207-1.642-0.54063.6855-0.71452.0374-0.3979-0.7421.80091.036-0.1546-0.2684-1.17360.25590.29141.2919-0.0507-0.1820.7614-0.39341.139338.019768.911939.4507
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 143:158 )A143 - 158
2X-RAY DIFFRACTION2( CHAIN A AND RESID 159:171 )A159 - 171
3X-RAY DIFFRACTION3( CHAIN A AND RESID 172:188 )A172 - 188
4X-RAY DIFFRACTION4( CHAIN A AND RESID 189:208 )A189 - 208
5X-RAY DIFFRACTION5( CHAIN A AND RESID 209:214 )A209 - 214
6X-RAY DIFFRACTION6( CHAIN A AND RESID 215:250 )A215 - 250
7X-RAY DIFFRACTION7( CHAIN A AND RESID 267:274 )A267 - 274
8X-RAY DIFFRACTION8( CHAIN A AND RESID 275:286 )A275 - 286
9X-RAY DIFFRACTION9( CHAIN A AND RESID 287:298 )A287 - 298
10X-RAY DIFFRACTION10( CHAIN A AND RESID 299:304 )A299 - 304
11X-RAY DIFFRACTION11( CHAIN A AND RESID 305:312 )A305 - 312
12X-RAY DIFFRACTION12( CHAIN A AND RESID 313:320 )A313 - 320
13X-RAY DIFFRACTION13( CHAIN A AND RESID 357:369 )A357 - 369
14X-RAY DIFFRACTION14( CHAIN A AND RESID 370:381 )A370 - 381
15X-RAY DIFFRACTION15( CHAIN A AND RESID 382:427 )A382 - 427
16X-RAY DIFFRACTION16( CHAIN A AND RESID 428:435 )A428 - 435
17X-RAY DIFFRACTION17( CHAIN A AND RESID 460:469 )A460 - 469
18X-RAY DIFFRACTION18( CHAIN A AND RESID 470:474 )A470 - 474
19X-RAY DIFFRACTION19( CHAIN A AND RESID 475:484 )A475 - 484
20X-RAY DIFFRACTION20( CHAIN A AND RESID 485:489 )A485 - 489
21X-RAY DIFFRACTION21( CHAIN A AND RESID 497:502 )A497 - 502
22X-RAY DIFFRACTION22( CHAIN A AND RESID 503:507 )A503 - 507
23X-RAY DIFFRACTION23( CHAIN A AND RESID 508:512 )A508 - 512
24X-RAY DIFFRACTION24( CHAIN A AND RESID 513:517 )A513 - 517
25X-RAY DIFFRACTION25( CHAIN A AND RESID 518:522 )A518 - 522
26X-RAY DIFFRACTION26( CHAIN A AND RESID 546:560 )A546 - 560
27X-RAY DIFFRACTION27( CHAIN A AND RESID 561:585 )A561 - 585
28X-RAY DIFFRACTION28( CHAIN A AND RESID 586:612 )A586 - 612
29X-RAY DIFFRACTION29( CHAIN A AND RESID 613:637 )A613 - 637
30X-RAY DIFFRACTION30( CHAIN A AND RESID 638:652 )A638 - 652
31X-RAY DIFFRACTION31( CHAIN A AND RESID 653:725 )A653 - 725
32X-RAY DIFFRACTION32( CHAIN A AND RESID 726:753 )A726 - 753
33X-RAY DIFFRACTION33( CHAIN A AND RESID 760:837 )A760 - 837
34X-RAY DIFFRACTION34( CHAIN A AND RESID 838:967 )A838 - 967
35X-RAY DIFFRACTION35( CHAIN A AND RESID 981:1003 )A981 - 1003
36X-RAY DIFFRACTION36( CHAIN A AND RESID 1004:1038 )A1004 - 1038
37X-RAY DIFFRACTION37( CHAIN A AND RESID 1039:1045 )A1039 - 1045
38X-RAY DIFFRACTION38( CHAIN A AND RESID 1046:1087 )A1046 - 1087

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