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- PDB-4ezl: Potent and Selective Inhibitors of PI3K-delta: Obtaining Isoform ... -

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Basic information

Entry
Database: PDB / ID: 4ezl
TitlePotent and Selective Inhibitors of PI3K-delta: Obtaining Isoform Selectivity from the Affinity Pocket and Tryptophan Shelf
ComponentsPhosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / kinase p110 / p110-gamma / lipid kinase / cytoplasmic / 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-0SE / 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: 2.94 Å
AuthorsMurray, J.M.
CitationJournal: Bioorg.Med.Chem.Lett. / Year: 2012
Title: Potent and selective inhibitors of PI3K-delta: obtaining isoform selectivity from the affinity pocket and tryptophan shelf
Authors: Sutherlin, D.P. / Baker, S. / Bisconte, A. / Blaney, P.M. / Brown, A. / Chan, B.K. / Chantry, D. / Castanedo, G. / DePledge, P. / Goldsmith, P. / Goldstein, D.M. / Hancox, T. / Kaur, J. / ...Authors: Sutherlin, D.P. / Baker, S. / Bisconte, A. / Blaney, P.M. / Brown, A. / Chan, B.K. / Chantry, D. / Castanedo, G. / DePledge, P. / Goldsmith, P. / Goldstein, D.M. / Hancox, T. / Kaur, J. / Knowles, D. / Kondru, R. / Lesnick, J. / Lucas, M.C. / Lewis, C. / Murray, J. / Nadin, A.J. / Nonomiya, J. / Pang, J. / Pegg, N. / Price, S. / Reif, K. / Safina, B.S. / Salphati, L. / Staben, S. / Seward, E.M. / Shuttleworth, S. / Sohal, S. / Sweeney, Z.K. / Ultsch, M. / Waszkowycz, B. / Wei, B.
History
DepositionMay 2, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 17, 2013Provider: repository / Type: Initial release
Revision 1.1Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / 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)111,1642
Polymers110,6991
Non-polymers4651
Water181
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)141.331, 67.194, 106.558
Angle α, β, γ (deg.)90.00, 96.10, 90.00
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: 110699.023 Da / Num. of mol.: 1 / Fragment: UNP residues 144-1102 / Mutation: K802T
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PIK3CG / Cell line (production host): Sf9 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: P48736, phosphatidylinositol-4,5-bisphosphate 3-kinase, non-specific serine/threonine protein kinase
#2: Chemical ChemComp-0SE / 2-(1-{[2-(2-aminopyrimidin-5-yl)-4-(morpholin-4-yl)pyrido[3,2-d]pyrimidin-6-yl]methyl}piperidin-4-yl)propan-2-ol


Mass: 464.563 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C24H32N8O2
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: H2O

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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: 2.27 Å3/Da / Density % sol: 45.87 %
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

Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Oct 26, 2011
RadiationProtocol: SINGLE / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.935→50 Å / Num. obs: 20407 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Biso Wilson estimate: 80 Å2 / Rmerge(I) obs: 0.086 / Net I/σ(I): 10.1
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsDiffraction-ID% possible all
2.935-3.113.70.475199.8
3.11-3.233.70.365199.9
3.23-3.383.70.26199.8
3.38-3.563.70.202199.6
3.56-3.783.70.138199.7
3.78-4.073.60.12199.1
4.07-4.483.50.089199.2
4.48-5.133.50.072199.1
5.13-6.463.50.068199.8
6.46-503.50.05199

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation2.93 Å31.14 Å
Translation2.93 Å31.14 Å

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASER2.3.0phasing
PHENIX1.7.2_869refinement
PDB_EXTRACT3.11data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1E8X

1e8x


Resolution: 2.94→31.14 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.74 / σ(F): 1.35 / Phase error: 31.03 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.271 1044 5.12 %
Rwork0.244 --
obs0.245 20402 94.9 %
Solvent computationShrinkage radii: 0.73 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 44.23 Å2 / ksol: 0.28 e/Å3
Displacement parametersBiso mean: 102.31 Å2
Baniso -1Baniso -2Baniso -3
1-4.827 Å2-0 Å20.6987 Å2
2--4.0965 Å20 Å2
3---4.6886 Å2
Refinement stepCycle: LAST / Resolution: 2.94→31.14 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6735 0 34 1 6770
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0086932
X-RAY DIFFRACTIONf_angle_d1.5319383
X-RAY DIFFRACTIONf_dihedral_angle_d13.6372572
X-RAY DIFFRACTIONf_chiral_restr0.0681056
X-RAY DIFFRACTIONf_plane_restr0.0071187
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.935-3.08940.36641110.34821909X-RAY DIFFRACTION67
3.0894-3.28280.3751500.33022897X-RAY DIFFRACTION100
3.2828-3.53590.34411600.29652884X-RAY DIFFRACTION100
3.5359-3.89110.28021570.25442886X-RAY DIFFRACTION100
3.8911-4.45280.24521560.23062879X-RAY DIFFRACTION99
4.4528-5.60470.24711560.21662926X-RAY DIFFRACTION99
5.6047-31.14590.24451540.21912977X-RAY DIFFRACTION100
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)
10.1267-0.2759-0.47253.12331.60641.8289-0.27850.7004-0.6852-0.5578-0.22450.61421.0089-0.77050.26970.7016-0.0259-0.06721.1187-0.37770.731227.2979-37.6794.4442
21.132-0.2571-0.59850.44330.34680.43710.24820.5113-0.2314-0.52140.1274-0.2329-0.21010.3719-0.36370.90880.0504-0.19790.719-0.38280.677242.8478-32.66586.7393
30.53160.2628-0.05591.0905-0.10720.46470.15380.3235-0.95930.45340.29330.07850.60930.28091.13520.91990.5204-0.309-0.3634-0.54021.277336.7844-41.62417.8436
41.5309-0.8692-0.57160.50870.52172.32680.1526-0.3413-0.37340.30850.2097-0.02190.6247-0.62820.0810.9149-0.05970.01350.76240.41541.090518.2939-34.529133.2758
51.1651-0.5680.1541.31741.04642.67730.0455-0.42240.3080.46160.0182-0.28-0.0763-0.1271-0.04011.9595-0.04070.50821.8225-0.03061.037813.7318-18.049249.1572
62.35970.10550.5592.3017-0.2861.633-0.0989-1.1758-0.11630.2875-0.31650.51720.5967-0.50720.15110.83810.10510.45711.70840.5411.086-0.2078-30.338840.9243
73.6063-0.00290.77780.38770.96492.5857-0.1917-0.1181-0.972-0.0251-0.19670.38040.8005-0.11180.11921.0164-0.3845-0.0381.1321-0.0151.30582.1114-37.031630.7728
80.82011.21591.30331.79061.92052.06040.7462-0.37170.20940.27720.2850.2970.4147-0.25090.14730.9726-0.33490.34571.35290.33070.932610.3742-31.021132.3144
92.1205-1.181.2974.3-1.1743.4349-0.13220.0258-0.582-0.52570.3577-0.1097-0.29570.1468-0.20820.75860.33070.18581.31960.351.130512.633-23.747239.2442
106.51476.12015.6645.76595.36155.0045-0.07510.21460.5683-0.38650.37660.4284-0.7193-0.5109-0.11531.44540.17910.44161.0110.29141.43814.9442-18.461536.5248
110.3675-0.9922-0.27842.77520.63580.3484-0.26390.1281-0.4706-0.4144-0.09670.14620.7751-0.64640.380.4867-0.13540.04311.3563-0.02871.28774.0298-35.475526.7486
120.34290.4085-0.14840.5945-0.47440.9241-0.17880.4544-0.3167-0.5537-0.0781-0.04290.146-0.46320.29180.94550.0168-0.35460.7458-0.24351.169718.7058-43.400815.8641
131.5619-0.03680.68194.4191-1.33262.8189-0.06770.1363-0.6511-0.58520.19440.08450.11750.6533-0.09430.33960.24660.08261.3868-0.12960.521567.9879-30.753312.9507
140.04410.01340.03360.03530.06370.1291-0.91040.58771.5975-0.7571-0.81860.5804-1.38940.24220.87551.321-0.4986-0.21941.2740.20241.086360.7371-8.21010.6569
151.40830.3132-1.11852.6742-1.62683.85120.32441.04370.1257-0.2605-0.22680.1137-0.1731.3854-0.06770.5417-0.0079-0.01991.17080.02980.460665.3984-23.946616.3818
164.6509-0.1660.03630.95291.00862.8407-0.40560.11120.83710.2203-0.30030.12650.03320.43750.40780.5228-0.2051-0.0650.8051-0.19530.495759.9271-19.119514.9847
172.19530.69960.19040.69840.91111.50780.2573-0.0062-0.0612-0.6384-0.1373-0.0962-0.9140.06990.00220.72750.20630.1330.8182-0.10830.561255.6978-23.016814.4475
185.6439-0.835-2.82625.37080.6462.14690.0913-0.1972-0.24620.2987-0.15380.19710.2308-0.4069-0.00410.9120.48870.12220.52970.02480.866652.8194-41.267918.3223
192.00251.09960.18290.8814-0.84233.2541-0.12730.5258-0.5913-0.1589-0.46220.13220.52430.1730.06330.78120.1501-0.09791.2612-0.27030.380658.2056-31.42748.8664
202.29940.54942.22990.35430.20384.4481-0.0356-0.27430.66370.0907-0.26760.5073-1.0983-0.0620.01870.83860.0420.31140.7271-0.17440.757150.0798-13.591411.3443
215.9725-1.32940.71683.93510.9882.10580.1138-0.41331.02180.45410.0186-0.5323-1.18350.7472-0.12890.77880.0377-0.00030.6307-0.15610.748349.123-17.710320.9676
223.33280.3256-1.03165.59092.11941.2056-0.05430.0427-0.3524-0.03560.46880.01260.4315-0.0217-0.08030.50320.3252-0.02430.8837-0.13770.361548.7376-25.046111.7039
238.02885.2917-4.79799.151-1.66528.3332-0.12960.3428-0.1421-0.3665-0.14170.1946-0.055-0.09550.02980.7559-0.13470.00821.059-0.12980.861147.9244-20.7830.595
241.62490.2643-1.66863.45680.76122.026-0.02010.38730.2149-0.1765-0.51960.23030.1294-0.32230.11980.2652-0.02890.28421.2651-0.28940.633757.4653-21.43914.5311
251.73760.4226-0.63992.294-1.83494.126-0.1161-0.0666-0.24440.02880.0092-0.3350.5120.59040.1990.86630.38680.59811.3305-0.29820.674165.3855-34.290510.8435
262.8109-0.03091.22473.63810.15725.2034-0.3613-1.2247-0.7473-0.1199-0.1591-0.4652-0.419-0.15670.22460.49720.07550.18840.85030.0040.646357.3736-25.395255.0992
274.46170.1515-1.01143.2338-0.19863.43140.22040.30140.90740.4868-0.0004-0.1690.2353-0.1165-0.34880.69250.0510.00320.9494-0.15710.463656.6869-25.304445.4524
283.75710.4054-1.39612.7156-0.38683.8853-0.040.1267-0.4156-0.121-0.1674-0.73040.12540.36750.21290.31790.1173-0.09580.55150.1290.336956.2351-32.818538.5998
292.28470.6045-1.05831.07720.18423.5229-0.2716-0.666-0.76310.3921-0.0862-0.24480.73630.24790.0740.49610.007-0.04240.46240.14630.569644.3365-30.544439.4884
305.32882.62220.16812.1711-1.59093.22230.2674-0.4687-0.8830.18210.07120.5560.3243-0.1608-0.15960.5390.0732-0.14960.4820.23570.783439.9707-34.092435.277
313.2346-0.11590.76731.78090.02451.59980.21980.1593-0.49110.1342-0.11280.46060.18930.0004-0.13490.33950.0149-0.02890.2043-0.05970.399833.4241-29.04422.2595
322.9999-0.8168-1.0154.4895-1.64732.7280.0830.9655-0.6157-0.914-0.28020.49870.0193-0.9350.02110.41080.0397-0.09660.8006-0.10370.385520.9929-19.49078.812
332.81080.82270.14133.5452-1.02292.49370.10820.59720.3156-0.28560.04090.8302-0.1634-0.495-0.11350.6220.1734-0.01070.67250.05750.716513.594-12.369212.6781
342.033-0.50460.22561.77610.37871.0065-0.7366-0.13320.64090.6759-0.01930.3778-0.9486-0.73340.29540.98130.5508-0.10810.3522-0.18170.619321.0195-3.63231.8544
353.3533-0.4793-1.51071.67570.14692.5906-0.1745-0.42910.7710.4452-0.34420.2286-0.5287-0.3205-0.28431.97310.5647-0.37220.6076-0.53181.331725.04018.156741.1776
361.3159-0.615-0.98992.27010.96580.8688-0.4166-0.7520.52260.758-0.0563-0.4911-0.8142-0.47730.17091.17680.3758-0.12890.7723-0.12140.364932.8114-9.50342.2107
373.74242.53732.83631.7751.8692.193-0.02840.58570.3221-0.31920.334-0.3397-0.24181.0054-0.03021.143-0.10250.18821.683-0.14790.907347.4587-9.881225.7781
381.3597-0.4806-0.17061.6295-0.77391.598-0.5179-0.39291.0643-0.6907-0.08230.6009-1.6226-0.43410.07831.42950.0491-0.73630.4308-0.35930.956836.17452.679638.7534
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 143:158 )
2X-RAY DIFFRACTION2(CHAIN A AND RESID 159:171 )
3X-RAY DIFFRACTION3(CHAIN A AND RESID 172:188 )
4X-RAY DIFFRACTION4(CHAIN A AND RESID 189:208 )
5X-RAY DIFFRACTION5(CHAIN A AND RESID 209:214 )
6X-RAY DIFFRACTION6(CHAIN A AND RESID 215:251 )
7X-RAY DIFFRACTION7(CHAIN A AND RESID 267:274 )
8X-RAY DIFFRACTION8(CHAIN A AND RESID 275:286 )
9X-RAY DIFFRACTION9(CHAIN A AND RESID 287:298 )
10X-RAY DIFFRACTION10(CHAIN A AND RESID 299:304 )
11X-RAY DIFFRACTION11(CHAIN A AND RESID 305:312 )
12X-RAY DIFFRACTION12(CHAIN A AND RESID 313:320 )
13X-RAY DIFFRACTION13(CHAIN A AND RESID 357:369 )
14X-RAY DIFFRACTION14(CHAIN A AND RESID 370:381 )
15X-RAY DIFFRACTION15(CHAIN A AND RESID 382:427 )
16X-RAY DIFFRACTION16(CHAIN A AND RESID 428:435 )
17X-RAY DIFFRACTION17(CHAIN A AND RESID 460:469 )
18X-RAY DIFFRACTION18(CHAIN A AND RESID 470:474 )
19X-RAY DIFFRACTION19(CHAIN A AND RESID 475:484 )
20X-RAY DIFFRACTION20(CHAIN A AND RESID 485:489 )
21X-RAY DIFFRACTION21(CHAIN A AND RESID 497:502 )
22X-RAY DIFFRACTION22(CHAIN A AND RESID 503:507 )
23X-RAY DIFFRACTION23(CHAIN A AND RESID 508:512 )
24X-RAY DIFFRACTION24(CHAIN A AND RESID 513:517 )
25X-RAY DIFFRACTION25(CHAIN A AND RESID 518:522 )
26X-RAY DIFFRACTION26(CHAIN A AND RESID 544:560 )
27X-RAY DIFFRACTION27(CHAIN A AND RESID 561:585 )
28X-RAY DIFFRACTION28(CHAIN A AND RESID 586:612 )
29X-RAY DIFFRACTION29(CHAIN A AND RESID 613:637 )
30X-RAY DIFFRACTION30(CHAIN A AND RESID 638:652 )
31X-RAY DIFFRACTION31(CHAIN A AND RESID 653:725 )
32X-RAY DIFFRACTION32(CHAIN A AND RESID 726:753 )
33X-RAY DIFFRACTION33(CHAIN A AND RESID 760:837 )
34X-RAY DIFFRACTION34(CHAIN A AND RESID 838:966 )
35X-RAY DIFFRACTION35(CHAIN A AND RESID 981:1003 )
36X-RAY DIFFRACTION36(CHAIN A AND RESID 1004:1038 )
37X-RAY DIFFRACTION37(CHAIN A AND RESID 1039:1045 )
38X-RAY DIFFRACTION38(CHAIN A AND RESID 1046:1093 )

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