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- PDB-3pcs: Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex -

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Basic information

Entry
Database: PDB / ID: 3pcs
TitleStructure of EspG-PAK2 autoinhibitory Ialpha3 helix complex
Components
  • EspG
  • Serine/threonine-protein kinase PAK 2
KeywordsPROTEIN TRANSPORT/TRANSFERASE / BACTERIAL EFFECTOR / KINASE / AUTOINHIBITORY IALPHA3 HELIX / PROTEIN TRANSPORT-TRANSFERASE complex
Function / homology
Function and homology information


: / Regulation of PAK-2p34 activity by PS-GAP/RHG10 / protein localization to cell-cell junction / Stimulation of the cell death response by PAK-2p34 / dendritic spine development / bicellular tight junction assembly / adherens junction assembly / Nef and signal transduction / cardiac muscle hypertrophy / positive regulation of extrinsic apoptotic signaling pathway ...: / Regulation of PAK-2p34 activity by PS-GAP/RHG10 / protein localization to cell-cell junction / Stimulation of the cell death response by PAK-2p34 / dendritic spine development / bicellular tight junction assembly / adherens junction assembly / Nef and signal transduction / cardiac muscle hypertrophy / positive regulation of extrinsic apoptotic signaling pathway / Activation of RAC1 / CD28 dependent Vav1 pathway / Ephrin signaling / negative regulation of stress fiber assembly / RHOV GTPase cycle / regulation of axonogenesis / protein tyrosine kinase activator activity / RHOJ GTPase cycle / stimulatory C-type lectin receptor signaling pathway / regulation of MAPK cascade / regulation of cytoskeleton organization / RHOQ GTPase cycle / RHO GTPases activate PAKs / cellular response to organic cyclic compound / RHOU GTPase cycle / Sema3A PAK dependent Axon repulsion / CDC42 GTPase cycle / RHOH GTPase cycle / Generation of second messenger molecules / RHOG GTPase cycle / Smooth Muscle Contraction / RAC2 GTPase cycle / RAC3 GTPase cycle / vascular endothelial growth factor receptor signaling pathway / phosphorylation / cellular response to transforming growth factor beta stimulus / RAC1 GTPase cycle / CD209 (DC-SIGN) signaling / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / Regulation of activated PAK-2p34 by proteasome mediated degradation / VEGFR2 mediated vascular permeability / secretory granule / FCERI mediated MAPK activation / negative regulation of protein kinase activity / MAPK6/MAPK4 signaling / VEGFA-VEGFR2 Pathway / small GTPase binding / positive regulation of peptidyl-tyrosine phosphorylation / cell-cell junction / peptidyl-serine phosphorylation / protein autophosphorylation / postsynaptic density / non-specific serine/threonine protein kinase / protein kinase activity / intracellular signal transduction / cadherin binding / protein phosphorylation / cysteine-type endopeptidase activity / protein serine kinase activity / protein serine/threonine kinase activity / glutamatergic synapse / negative regulation of apoptotic process / apoptotic process / protein kinase binding / perinuclear region of cytoplasm / signal transduction / ATP binding / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
p21-activated kinase 2, catalytic domain / EspG protein, N-terminal domain / Cysteine protease, VirA/EspG / Cysteine protease, VirA/EspG, N-terminal / EspG protein / p21 activated kinase binding domain / CRIB domain superfamily / P21-Rho-binding domain / : / CRIB domain profile. ...p21-activated kinase 2, catalytic domain / EspG protein, N-terminal domain / Cysteine protease, VirA/EspG / Cysteine protease, VirA/EspG, N-terminal / EspG protein / p21 activated kinase binding domain / CRIB domain superfamily / P21-Rho-binding domain / : / CRIB domain profile. / P21-Rho-binding domain / CRIB domain / Nuclear Transport Factor 2; Chain: A, / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Roll / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Alpha Beta
Similarity search - Domain/homology
Serine/threonine-protein kinase PAK 2 / T3SS secreted effector EspG
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.86 Å
AuthorsTomchick, D.R. / Alto, N.M. / Selyunin, A.S.
CitationJournal: Nature / Year: 2011
Title: The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold.
Authors: Selyunin, A.S. / Sutton, S.E. / Weigele, B.A. / Reddick, L.E. / Orchard, R.C. / Bresson, S.M. / Tomchick, D.R. / Alto, N.M.
History
DepositionOct 21, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 5, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3Sep 6, 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: EspG
B: EspG
C: EspG
D: EspG
E: Serine/threonine-protein kinase PAK 2
F: Serine/threonine-protein kinase PAK 2
G: Serine/threonine-protein kinase PAK 2
H: Serine/threonine-protein kinase PAK 2


Theoretical massNumber of molelcules
Total (without water)165,8148
Polymers165,8148
Non-polymers00
Water00
1
A: EspG
E: Serine/threonine-protein kinase PAK 2


Theoretical massNumber of molelcules
Total (without water)41,4542
Polymers41,4542
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1420 Å2
ΔGint-11 kcal/mol
Surface area17100 Å2
MethodPISA
2
B: EspG
F: Serine/threonine-protein kinase PAK 2


Theoretical massNumber of molelcules
Total (without water)41,4542
Polymers41,4542
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1410 Å2
ΔGint-10 kcal/mol
Surface area17110 Å2
MethodPISA
3
C: EspG
G: Serine/threonine-protein kinase PAK 2


Theoretical massNumber of molelcules
Total (without water)41,4542
Polymers41,4542
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1430 Å2
ΔGint-11 kcal/mol
Surface area16480 Å2
MethodPISA
4
D: EspG
H: Serine/threonine-protein kinase PAK 2


Theoretical massNumber of molelcules
Total (without water)41,4542
Polymers41,4542
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1490 Å2
ΔGint-11 kcal/mol
Surface area16980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)86.717, 104.603, 191.994
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein
EspG / EspG protein


Mass: 39611.438 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: O157:H7 / Gene: ECs4590, espG, Z5142 / Plasmid: pPRO-EX-HTb / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q7DB50
#2: Protein/peptide
Serine/threonine-protein kinase PAK 2 / Gamma-PAK / PAK65 / S6/H4 kinase / p21-activated kinase 2 / PAK-2 / p58 / PAK-2p27 / p27 / PAK-2p34 ...Gamma-PAK / PAK65 / S6/H4 kinase / p21-activated kinase 2 / PAK-2 / p58 / PAK-2p27 / p27 / PAK-2p34 / p34 / C-t-PAK2


Mass: 1842.097 Da / Num. of mol.: 4 / Fragment: UNP residues 121-136
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PAK2 / Plasmid: pGEX-4TI1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q13177, non-specific serine/threonine protein kinase

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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: 2.38 Å3/Da / Density % sol: 48.25 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 22% PEG 4000, 0.25 M NaCl, 0.1 M Tris pH 8.0, 15% ethylene glycol, vapor diffusion, hanging drop, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97899 Å
DetectorType: SBC-3 / Detector: CCD / Date: Dec 16, 2009 / Details: monochromator
RadiationMonochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97899 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. all: 44259 / Num. obs: 44259 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.8 % / Rmerge(I) obs: 0.076 / Net I/σ(I): 9.6
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsDiffraction-ID% possible all
2.8-2.854.70.681199.5
2.85-2.94.80.5951100
2.9-2.964.90.5241100
2.96-3.024.90.4321100
3.02-3.084.90.3381100
3.08-3.154.90.2521100
3.15-3.234.90.2271100
3.23-3.324.90.1821100
3.32-3.424.90.1511100
3.42-3.534.90.117199.9
3.53-3.654.90.0921100
3.65-3.84.80.0821100
3.8-3.974.80.0781100
3.97-4.184.80.063199.9
4.18-4.444.80.0521100
4.44-4.794.80.051100
4.79-5.274.70.051199.8
5.27-6.034.60.053199.9
6.03-7.594.40.045199.8
7.59-504.40.032198.3

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
SCALEPACKdata scaling
PHASERphasing
DMphasing
PHENIX1.6.4_486refinement
PDB_EXTRACT3.1data extraction
HKL-3000data collection
DENZOdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3PCR

3pcr


Resolution: 2.86→40.5 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.47 / σ(F): 1.33 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.281 2032 4.95 %
Rwork0.191 --
obs0.195 41057 99.9 %
all-41057 -
Solvent computationShrinkage radii: 0.72 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 33.44 Å2 / ksol: 0.28 e/Å3
Displacement parametersBiso mean: 76.93 Å2
Baniso -1Baniso -2Baniso -3
1-6.0681 Å2-0 Å20 Å2
2---12.5068 Å2-0 Å2
3---6.4387 Å2
Refine analyzeLuzzati sigma a obs: 0.47 Å
Refinement stepCycle: LAST / Resolution: 2.86→40.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11254 0 0 0 11254
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00811452
X-RAY DIFFRACTIONf_angle_d1.21615534
X-RAY DIFFRACTIONf_dihedral_angle_d14.5034283
X-RAY DIFFRACTIONf_chiral_restr0.0791802
X-RAY DIFFRACTIONf_plane_restr0.0052026
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.86-2.96210.40382330.31773822X-RAY DIFFRACTION100
2.9621-3.08060.36272110.28313851X-RAY DIFFRACTION100
3.0806-3.22070.37781940.24133848X-RAY DIFFRACTION100
3.2207-3.39020.33751810.24353885X-RAY DIFFRACTION100
3.3902-3.60230.31241840.22463881X-RAY DIFFRACTION100
3.6023-3.87990.28161950.19853884X-RAY DIFFRACTION100
3.8799-4.26930.24912140.17113874X-RAY DIFFRACTION100
4.2693-4.88470.21471920.13623931X-RAY DIFFRACTION100
4.8847-6.14510.27341970.17863972X-RAY DIFFRACTION100
6.1451-29.59760.25432310.16534077X-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)
10.5938-0.5151-0.13631.82440.85670.45630.1620.13420.041-0.00330.1053-0.57890.37390.2272-0.21320.2640.0702-0.07160.16780.01440.3318-30.2629-23.99851.5692
21.7048-2.11190.2719.71141.37530.47650.43460.1841-0.1213-1.7821-0.4157-0.29-0.1782-0.2304-0.010.4630.07190.01440.2548-0.08950.2687-39.7034-27.9782-3.9012
32.27762.1184-0.29592.34440.63062.5460.0088-0.04710.72630.29790.02880.49740.11720.3377-0.17140.14920.09580.00150.2003-0.02280.2884-42.3417-19.953610.6947
41.72430.995-0.30051.1831-0.4821.5812-0.1235-0.26170.4091-0.0145-0.03790.1259-0.3365-0.07820.05480.11090.0372-0.03110.0825-0.00410.2403-34.3369-0.5896-0.0387
58.4012-6.01882.07445.0885-1.45840.5232-0.87450.14112.53391.6287-0.1132-0.5371-0.27080.2460.57021.07180.04060.0560.28680.25440.7587-34.577912.8635-13.5612
61.303-0.55220.6012.6122-0.03271.08080.00230.4950.3598-0.7036-0.41970.1385-0.0801-0.29750.02850.2255-0.01060.02590.20460.110.0092-34.7328-2.595-12.9733
70.99930.42390.49982.3780.65922.37460.17710.081-0.01280.0213-0.1906-0.0120.3107-0.0920.10020.11250.01120.04090.09290.05360.108-37.7131-2.26886.5819
81.31340.030.30824.088-0.58460.47620.18070.0449-0.5102-1.03160.0586-0.0680.0056-0.0639-0.17740.4763-0.08270.05450.2570.0480.2978-73.4257-3.84712.2475
9-0.01530.2844-0.10053.2615-0.23792.24840.04630.03020.112-0.0891-0.60970.30590.5929-0.18110.38050.5037-0.0804-0.02080.191-0.04120.3028-81.238-9.66657.0136
103.41030.3098-1.58033.76853.00235.51950.49150.24460.06390.07360.4678-0.51080.2671-0.0243-0.42460.2891-0.0761-0.10210.31380.03340.2852-73.77341.364617.7558
111.9697-0.8648-0.82650.63180.21781.03860.22870.04360.6273-0.80020.1028-0.0692-0.7913-0.085-0.22660.5894-0.11580.01630.12870.00890.4808-77.126618.27437.3335
121.7204-0.35060.33640.58491.0862.9943-0.59790.08890.3347-0.9574-0.1844-1.06121.4876-0.31670.46310.8949-0.0564-0.0290.07580.05541.1353-89.286532.58450.6825
130.2098-0.30290.14733.05020.55090.97050.21390.09210.2612-1.00460.15910.2709-0.84820.0407-0.20650.6514-0.0144-0.10460.30240.10250.4573-87.727317.5246-1.7584
141.4025-0.24230.16953.60560.6230.75650.24030.02350.0431-0.49240.0727-0.1468-0.13830.0613-0.19610.3346-0.0982-0.02970.18950.01170.2721-75.600716.252713.9137
152.07221.7376-0.34162.3608-0.58591.19730.0988-0.6857-0.0895-0.0914-0.20620.00550.10410.30120.09870.0786-0.0168-0.0970.3122-0.0510.25-99.71190.84247.6536
168.39485.5742-8.21416.5893-7.38139.81830.3236-1.0378-1.0565-0.7642-0.5243-0.2580.44151.67720.32190.33490.00820.01860.31830.09960.4375-97.9172-9.086141.6496
171.8341-0.3558-2.19391.75270.09012.81020.0767-0.76361.03760.23650.00810.304-0.67160.1960.02710.4090.0247-0.07940.23710.05190.3101-95.80864.337133.8331
181.7306-0.8699-0.05281.189-0.25950.5638-0.159-0.16130.45630.14050.1456-0.2619-0.46160.01560.03180.2845-0.1942-0.15210.4257-0.05860.4367-78.969410.929446.8786
192.3017-1.3213-0.13171.30350.02440.89910.0035-0.913-0.4162-0.13750.68030.1652-0.0512-0.5676-0.63990.5503-0.1944-0.54981.0880.05250.8161-60.72726.488557.1253
203.01330.6160.41411.4998-1.04992.5002-0.0812-0.7146-0.32620.3371-0.1587-0.69090.1510.36760.19850.3477-0.043-0.29450.57980.09020.4004-74.74680.062855.0546
215.13890.82590.97091.15240.61332.80050.0335-0.36580.6582-0.0768-0.1486-0.5152-0.50670.33710.15820.3076-0.1475-0.06290.40010.00970.431-79.808412.008841.2318
223.34242.22930.27881.83520.57361.25110.0267-0.2615-0.274-0.1089-0.08240.01910.1904-0.2890.07720.30730.0574-0.11610.4572-0.05050.4154-32.3842-13.21344.6432
237.37715.70441.39336.2655-2.91038.9399-0.0940.308-2.02-0.4380.6262-1.88571.36990.64210.3489-0.0875-0.08480.03410.23010.03170.6417-22.2772-17.222940.4318
241.27830.7590.12166.88082.69644.26581.0827-0.8811-0.58770.95430.0373-0.96140.40470.3593-0.64090.8311-0.2707-0.17051.0838-0.00280.6714-29.1354-26.548252.988
255.413-2.7428-1.09553.5336-0.44764.2685-0.5815-0.8969-2.29551.35020.20160.97971.75670.8975-0.1969-0.1372-0.3696-0.3051-0.11430.0338-0.0586-43.6963-26.546850.1571
261.7568-3.1833-1.47938.4092.79322.1668-0.3427-0.2421-0.78121.0360.34290.83960.4981-0.2110.03910.2129-0.1373-0.00470.46340.25560.3712-50.5822-34.182431.1126
271.7123-1.1256-2.02951.51960.89622.94330.4201-0.2640.3614-0.07150.0880.08140.08460.1495-0.37260.1234-0.0612-0.08020.0885-0.0120.199-44.7082-26.370424.4933
283.1404-0.02220.60862.8508-0.93652.11030.081-0.6424-0.46230.6236-0.0725-0.00390.25560.1699-0.13240.295-0.0734-0.14420.2360.14570.224-44.8547-34.112944.8855
291.9767-3.2213-1.01885.78432.32071.3358-0.44220.5735-0.57862.4508-0.1428-1.60561.0776-0.37690.71991.1141-0.1235-0.03060.57440.13150.9281-40.545510.031910.2038
302.70432.2828-0.16566.6119-4.32493.74160.57360.02131.2838-0.5392-0.30770.2597-1.2077-0.3396-0.05820.6368-0.2003-0.20660.4811-0.03770.714-33.1668.30139.2102
317.8851.2157-6.10930.3633-0.99074.8528-0.57490.12411.44230.70891.09641.0246-1.12080.36930.10021.0630.08520.08330.29810.2710.7472-21.68365.97791.7618
326.33140.4203-1.94066.68682.19778.40570.478-0.20330.4487-0.17431.1108-0.05510.1639-0.4718-0.94320.58490.1591-0.02210.62180.01160.9452-74.786127.933520.0423
331.92822.28151.38223.3262.48362.76920.88020.4484-0.5818-1.32980.8088-2.0359-1.5106-0.921-1.28931.0980.00870.28460.58390.17940.8974-70.719326.18667.3684
344.12891.0462-2.49430.5709-1.19582.99340.1856-0.07830.475-1.79020.158-0.58180.5152-0.1747-0.22471.3098-0.2769-0.17340.75880.16891.8431-71.418322.182540.2354
352.0913-1.71113.45474.4-2.33615.7646-0.29240.09330.08090.6631-0.8601-1.248-0.4422-0.07880.92740.7218-0.2866-0.28811.04590.29351.5967-76.591120.706650.9512
361.55452.23341.97333.33961.83849.1009-0.08932.4535-0.36460.63070.5785-0.55871.5097-1.1582-0.05010.673-0.2073-0.34141.00020.20270.8028-53.7848-43.883346.2171
370.2406-0.68511.05232.8891-3.71338.24740.1558-0.30360.4522-0.43210.24980.49920.05790.1095-0.15520.7115-0.4858-0.26851.26050.41910.5814-55.6048-35.862846.0971
383.29782.2603-0.39425.9624-4.76325.2131.46320.51040.67171.6014-0.3291.23090.2311-1.0793-1.46990.7201-0.1739-0.06420.5710.31481.235-60.478-26.44139.476
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 42:103)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 104:129)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 130:156)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 157:234)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 235:245)
6X-RAY DIFFRACTION6(CHAIN A AND RESID 246:301)
7X-RAY DIFFRACTION7(CHAIN A AND RESID 302:397)
8X-RAY DIFFRACTION8(CHAIN B AND RESID 44:105)
9X-RAY DIFFRACTION9(CHAIN B AND RESID 106:136)
10X-RAY DIFFRACTION10(CHAIN B AND RESID 137:156)
11X-RAY DIFFRACTION11(CHAIN B AND RESID 157:234)
12X-RAY DIFFRACTION12(CHAIN B AND RESID 235:245)
13X-RAY DIFFRACTION13(CHAIN B AND RESID 246:301)
14X-RAY DIFFRACTION14(CHAIN B AND RESID 302:397)
15X-RAY DIFFRACTION15(CHAIN C AND RESID 42:105)
16X-RAY DIFFRACTION16(CHAIN C AND RESID 106:131)
17X-RAY DIFFRACTION17(CHAIN C AND RESID 132:149)
18X-RAY DIFFRACTION18(CHAIN C AND RESID 150:236)
19X-RAY DIFFRACTION19(CHAIN C AND RESID 237:246)
20X-RAY DIFFRACTION20(CHAIN C AND RESID 247:301)
21X-RAY DIFFRACTION21(CHAIN C AND RESID 302:395)
22X-RAY DIFFRACTION22(CHAIN D AND RESID 42:105)
23X-RAY DIFFRACTION23(CHAIN D AND RESID 106:131)
24X-RAY DIFFRACTION24(CHAIN D AND RESID 132:151)
25X-RAY DIFFRACTION25(CHAIN D AND RESID 152:186)
26X-RAY DIFFRACTION26(CHAIN D AND RESID 187:245)
27X-RAY DIFFRACTION27(CHAIN D AND RESID 246:296)
28X-RAY DIFFRACTION28(CHAIN D AND RESID 297:395)
29X-RAY DIFFRACTION29(CHAIN E AND RESID 122:124)
30X-RAY DIFFRACTION30(CHAIN E AND RESID 125:129)
31X-RAY DIFFRACTION31(CHAIN E AND RESID 130:134)
32X-RAY DIFFRACTION32(CHAIN F AND RESID 122:126)
33X-RAY DIFFRACTION33(CHAIN F AND RESID 127:132)
34X-RAY DIFFRACTION34(CHAIN G AND RESID 123:126)
35X-RAY DIFFRACTION35(CHAIN G AND RESID 127:131)
36X-RAY DIFFRACTION36(CHAIN H AND RESID 122:125)
37X-RAY DIFFRACTION37(CHAIN H AND RESID 126:129)
38X-RAY DIFFRACTION38(CHAIN H AND RESID 130:133)

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