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- PDB-7rec: Structure of Thr354Asn, Glu355Gln, Thr412Asn, Ile414Met, Ile464Hi... -

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Basic information

Entry
Database: PDB / ID: 7rec
TitleStructure of Thr354Asn, Glu355Gln, Thr412Asn, Ile414Met, Ile464His, and Phe467Met mutant human CaMKII alpha hub bound to 5-HDC
ComponentsCalcium/calmodulin-dependent protein kinase type II subunit alpha
KeywordsSIGNALING PROTEIN / CaMKII hub / oligomer
Function / homology
Function and homology information


peptidyl-threonine autophosphorylation / regulation of endocannabinoid signaling pathway / calcium- and calmodulin-dependent protein kinase complex / regulation of neuron migration / Ca2+/calmodulin-dependent protein kinase / regulation of neurotransmitter secretion / dendritic spine development / Trafficking of AMPA receptors / positive regulation of calcium ion transport / negative regulation of hydrolase activity ...peptidyl-threonine autophosphorylation / regulation of endocannabinoid signaling pathway / calcium- and calmodulin-dependent protein kinase complex / regulation of neuron migration / Ca2+/calmodulin-dependent protein kinase / regulation of neurotransmitter secretion / dendritic spine development / Trafficking of AMPA receptors / positive regulation of calcium ion transport / negative regulation of hydrolase activity / Assembly and cell surface presentation of NMDA receptors / calmodulin-dependent protein kinase activity / regulation of mitochondrial membrane permeability involved in apoptotic process / CaMK IV-mediated phosphorylation of CREB / regulation of neuronal synaptic plasticity / Negative regulation of NMDA receptor-mediated neuronal transmission / positive regulation of cardiac muscle cell apoptotic process / Unblocking of NMDA receptors, glutamate binding and activation / Phase 0 - rapid depolarisation / Long-term potentiation / Ion transport by P-type ATPases / Regulation of MECP2 expression and activity / HSF1-dependent transactivation / glutamate receptor binding / cellular response to interferon-beta / Ion homeostasis / Ras activation upon Ca2+ influx through NMDA receptor / response to ischemia / angiotensin-activated signaling pathway / G1/S transition of mitotic cell cycle / RAF activation / positive regulation of receptor signaling pathway via JAK-STAT / cellular response to type II interferon / endocytic vesicle membrane / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / calcium ion transport / Interferon gamma signaling / Signaling by BRAF and RAF1 fusions / Ca2+ pathway / positive regulation of NF-kappaB transcription factor activity / kinase activity / RAF/MAP kinase cascade / peptidyl-serine phosphorylation / dendritic spine / postsynaptic density / protein autophosphorylation / calmodulin binding / neuron projection / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / protein homodimerization activity / mitochondrion / nucleoplasm / ATP binding / identical protein binding / metal ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Calcium/calmodulin-dependent protein kinase II, association-domain / Calcium/calmodulin dependent protein kinase II association domain / NTF2-like domain superfamily / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. ...Calcium/calmodulin-dependent protein kinase II, association-domain / Calcium/calmodulin dependent protein kinase II association domain / NTF2-like domain superfamily / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
5-hydroxydiclofenac / Calcium/calmodulin-dependent protein kinase type II subunit alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsMcSpadden, E.D. / Chi, C.C. / Gee, C.L. / Kuriyan, J.
Funding support United States, Denmark, 3items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
LundbeckfondenR83-2011-8000, R139-2012-12270, R192-2015-666, R303-2018-3162, and R277-2018-260 Denmark
Novo Nordisk FoundationNNF17OC0028664 and NNF19SA0057841 Denmark
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2021
Title: GHB analogs confer neuroprotection through specific interaction with the CaMKII alpha hub domain.
Authors: Leurs, U. / Klein, A.B. / McSpadden, E.D. / Griem-Krey, N. / Solbak, S.M.O. / Houlton, J. / Villumsen, I.S. / Vogensen, S.B. / Hamborg, L. / Gauger, S.J. / Palmelund, L.B. / Larsen, A.S.G. / ...Authors: Leurs, U. / Klein, A.B. / McSpadden, E.D. / Griem-Krey, N. / Solbak, S.M.O. / Houlton, J. / Villumsen, I.S. / Vogensen, S.B. / Hamborg, L. / Gauger, S.J. / Palmelund, L.B. / Larsen, A.S.G. / Shehata, M.A. / Kelstrup, C.D. / Olsen, J.V. / Bach, A. / Burnie, R.O. / Kerr, D.S. / Gowing, E.K. / Teurlings, S.M.W. / Chi, C.C. / Gee, C.L. / Frolund, B. / Kornum, B.R. / van Woerden, G.M. / Clausen, R.P. / Kuriyan, J. / Clarkson, A.N. / Wellendorph, P.
History
DepositionJul 12, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 21, 2021Provider: repository / Type: Initial release
Revision 1.1Aug 25, 2021Group: Database references / Category: citation / citation_author / database_2
Item: _citation.journal_volume / _citation.pdbx_database_id_DOI ..._citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.2Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
G: Calcium/calmodulin-dependent protein kinase type II subunit alpha
D: Calcium/calmodulin-dependent protein kinase type II subunit alpha
A: Calcium/calmodulin-dependent protein kinase type II subunit alpha
B: Calcium/calmodulin-dependent protein kinase type II subunit alpha
C: Calcium/calmodulin-dependent protein kinase type II subunit alpha
E: Calcium/calmodulin-dependent protein kinase type II subunit alpha
F: Calcium/calmodulin-dependent protein kinase type II subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)110,75714
Polymers108,8617
Non-polymers1,8967
Water1,56787
1
G: Calcium/calmodulin-dependent protein kinase type II subunit alpha
D: Calcium/calmodulin-dependent protein kinase type II subunit alpha
A: Calcium/calmodulin-dependent protein kinase type II subunit alpha
B: Calcium/calmodulin-dependent protein kinase type II subunit alpha
C: Calcium/calmodulin-dependent protein kinase type II subunit alpha
E: Calcium/calmodulin-dependent protein kinase type II subunit alpha
F: Calcium/calmodulin-dependent protein kinase type II subunit alpha
hetero molecules

G: Calcium/calmodulin-dependent protein kinase type II subunit alpha
D: Calcium/calmodulin-dependent protein kinase type II subunit alpha
A: Calcium/calmodulin-dependent protein kinase type II subunit alpha
B: Calcium/calmodulin-dependent protein kinase type II subunit alpha
C: Calcium/calmodulin-dependent protein kinase type II subunit alpha
E: Calcium/calmodulin-dependent protein kinase type II subunit alpha
F: Calcium/calmodulin-dependent protein kinase type II subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)221,51428
Polymers217,72214
Non-polymers3,79214
Water25214
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_555-x,y,-z+1/21
Buried area31260 Å2
ΔGint-258 kcal/mol
Surface area75610 Å2
MethodPISA
Unit cell
Length a, b, c (Å)101.433, 182.958, 106.466
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

#1: Protein
Calcium/calmodulin-dependent protein kinase type II subunit alpha / / CaMK-II subunit alpha


Mass: 15551.578 Da / Num. of mol.: 7 / Fragment: hub (UNP residues 345-475) / Mutation: T354N, E355Q, T412N, I414M, I464H, F467M
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CAMK2A, CAMKA, KIAA0968 / Plasmid: pSKB2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9UQM7
#2: Chemical
ChemComp-7ZV / 5-hydroxydiclofenac / 2-[2-[[2,6-bis(chloranyl)phenyl]amino]-5-oxidanyl-phenyl]ethanoic acid


Mass: 312.148 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C14H11Cl2NO3 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 87 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 45.78 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8.1
Details: 100 nL protein + compound in 25 mM Tris, 150 mM potassium chloride, 2 mM DTT, 1 mM TCEP, 10% v/v glycerol, pH 8.0, 10% DMSO + 100 nL well solution (200 mM potassium acetate, 20% w/v PEG3350, ...Details: 100 nL protein + compound in 25 mM Tris, 150 mM potassium chloride, 2 mM DTT, 1 mM TCEP, 10% v/v glycerol, pH 8.0, 10% DMSO + 100 nL well solution (200 mM potassium acetate, 20% w/v PEG3350, pH 8.1), equilibrated against 45 uL well solution

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.11583 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Mar 23, 2018
RadiationMonochromator: S111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.11583 Å / Relative weight: 1
ReflectionResolution: 2.2→106.47 Å / Num. obs: 50585 / % possible obs: 100 % / Redundancy: 13.3 % / Biso Wilson estimate: 61.442 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.075 / Rpim(I) all: 0.021 / Rrim(I) all: 0.079 / Χ2: 1.03 / Net I/σ(I): 22.7
Reflection shellResolution: 2.2→2.27 Å / Redundancy: 13.4 % / Rmerge(I) obs: 3.783 / Mean I/σ(I) obs: 0.8 / Num. unique obs: 4349 / CC1/2: 0.292 / Rpim(I) all: 1.066 / Rrim(I) all: 3.933 / Χ2: 1.02 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(1.14_3260: ???)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 6OF8

6of8


Resolution: 2.2→91.479 Å / SU ML: 0.34 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 29.01 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2437 1701 3.36 %
Rwork0.2088 --
obs0.21 50550 99.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.2→91.479 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7283 0 121 87 7491
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0037621
X-RAY DIFFRACTIONf_angle_d0.55210299
X-RAY DIFFRACTIONf_dihedral_angle_d18.5124475
X-RAY DIFFRACTIONf_chiral_restr0.0431045
X-RAY DIFFRACTIONf_plane_restr0.0031349
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2-2.26480.37141300.36424032X-RAY DIFFRACTION100
2.2648-2.33790.32911250.33944030X-RAY DIFFRACTION100
2.3379-2.42140.34411600.32244008X-RAY DIFFRACTION100
2.4214-2.51840.31781370.30614019X-RAY DIFFRACTION100
2.5184-2.6330.30671480.28644025X-RAY DIFFRACTION100
2.633-2.77180.311240.26354082X-RAY DIFFRACTION100
2.7718-2.94550.28151780.25183994X-RAY DIFFRACTION100
2.9455-3.17290.2751350.24234101X-RAY DIFFRACTION100
3.1729-3.49220.22861430.20594057X-RAY DIFFRACTION100
3.4922-3.99760.23761240.19674097X-RAY DIFFRACTION100
3.9976-5.03650.20571330.164143X-RAY DIFFRACTION100
5.0365-91.4790.22161640.19044261X-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)
10.51770.326-0.12981.75250.32980.7328-0.23561.41420.9643-1.02220.2444-0.1361-0.04140.9709-0.09520.76310.04580.26270.99190.18370.70431.598319.2769-2.4357
21.0320.35860.17170.18820.08290.25410.35741.3311-0.1064-0.978-0.6484-0.03320.5416-0.0245-0.00670.70480.15190.03761.00060.02360.502619.245610.6795-3.2536
30.463-0.0675-0.4934-0.0557-0.07570.36480.00120.48160.1172-0.23840.1243-0.09190.2255-0.1490.00010.50320.0750.00510.67740.07130.628113.334912.35477.2258
43.44262.56731.88348.49913.63691.78721.29350.82610.6126-2.23580.5937-2.2419-1.45370.08272.07811.02990.1260.10180.67520.5040.041418.398627.0619-0.9965
50.7168-0.21790.78820.2238-0.34150.7084-0.10020.2526-0.0567-0.35650.31-0.3548-0.11611.2174-0.03210.46390.08690.17940.91040.04260.859537.25916.34125.9743
60.63530.7344-0.89410.6481-1.00630.5339-0.39940.3747-0.5749-0.30850.50250.6965-0.07950.01090.00060.543-0.0368-0.07410.58730.12310.603623.546225.48374.4764
70.15850.09510.00560.23690.01260.0191-0.1595-0.27490.77090.3774-0.1189-0.1978-0.3930.30540.00041.08580.0849-0.67611.60.20452.14756.166737.32461.4616
81.16780.93390.9950.68070.37681.0517-0.35050.26590.0414-0.16690.20080.17240.05570.133700.62100.14210.59180.04010.466224.498519.90255.1631
90.3561-0.66810.32090.4017-0.5730.6767-0.18690.01020.0151-0.48290.1713-0.00650.2828-0.0972-0.00780.55830.04930.14210.58360.06990.489624.317113.8644.7543
101.11670.1044-0.14250.7807-0.47390.20550.0719-0.0048-0.28320.26340.0151-0.20750.41370.44120.00010.64450.2196-0.02280.71250.04940.767832.94193.045921.7175
110.1969-0.25650.16561.24880.72291.04920.0931-0.1336-0.05680.48890.2054-0.1057-0.3370.39730.00020.53020.021-0.00640.62750.00740.685435.181121.929524.0291
120.2051-0.4068-0.11631.57820.88620.408-0.2327-0.6991-1.69290.7657-1.428-0.1048-0.1077-1.5042-0.02250.88180.1663-0.16750.84190.0770.721824.056114.400233.7768
130.13240.3090.1690.8260.6420.60380.20460.2473-0.2293-0.0452-0.22480.14820.37150.24510.00010.60860.11780.09270.58210.05120.738228.2674.00513.9065
140.30990.3994-0.17560.28640.1855-0.016-0.0068-0.142-0.06090.4668-0.1963-0.3152-0.33190.617-0.02290.55740.03650.04750.51530.09250.501622.665511.833724.9772
150.85761.39450.65121.590.3671.27760.4533-0.40430.4360.5681-0.2781-0.33590.21630.11770.06670.5402-0.01980.06010.5674-0.02240.577224.91814.832324.9479
160.24750.10950.58540.83730.52521.19450.2616-0.5521-0.07930.57250.1944-0.56230.10030.20850.00090.49370.1342-0.00490.71230.07820.690732.412515.339719.7421
170.9051-0.07390.90970.93950.29471.78050.01470.09870.064-0.83580.16240.1714-0.3687-0.04890.03860.97060.01510.15220.51120.06520.535727.864847.3703-2.8679
180.9197-1.0628-0.9360.98041.03011.12920.09310.60120.1144-0.1153-0.62490.87590.2861-0.1776-0.04371.3312-0.0935-0.2220.68070.10490.814714.219952.2156-3.1092
190.85630.60710.67523.22440.89372.4347-0.23210.1707-0.1866-0.7081-0.04150.1406-0.24430.1064-0.04530.7777-0.17190.04110.55610.0220.570226.463154.09953.7492
201.01060.58741.10430.54510.52550.89180.33610.03660.1722-0.9698-0.04060.268-1.00530.1669-0.0120.9721-0.09520.09490.54820.0670.589831.10847.65020.7551
210.1664-0.20390.01560.2327-0.3540.2478-0.42420.05551.1048-0.21410.2005-0.17640.130.0333-0.00050.77470.340.06381.4347-0.06630.844846.143741.234916.6404
220.11270.523-0.60592.04652.47193.48550.0491-0.22510.12780.37090.3751-0.36560.01831.12480.08790.6249-0.1156-0.07860.8831-0.09330.60535.714952.414425.4498
230.8155-0.7836-0.39151.74350.53410.20380.0884-0.2354-0.32650.6173-0.1331-0.8696-0.09770.73140.01630.68380.02670.11290.7560.00960.762637.728539.118914.8513
240.1544-0.51550.01051.20261.76812.7434-0.26710.0610.24830.14960.1806-0.20940.30450.4186-0.00880.53330.00880.06540.63070.02320.596535.791645.220918.3068
251.2836-0.61640.02740.7494-0.47330.1865-0.2264-1.4926-0.00610.6197-0.27670.07990.76830.0468-0.07410.8171-0.1310.12691.01130.18240.7524-3.127-6.612641.4033
261.0831-0.33950.00710.54510.67740.90710.1055-0.4342-0.0140.287-0.1976-0.19950.1990.4262-00.56440.03370.01580.72110.08140.573211.75022.702435.9063
270.2516-0.24120.0450.1155-0.0202-0.1254-0.3878-0.68110.18650.960.51390.1321-0.11110.1972-0.00030.95120.14260.05291.01770.04130.7151-0.14459.011545.5448
280.49860.4090.29160.32280.24970.65350.0898-0.0323-0.9827-0.07560.01440.93360.347-0.6126-0.00690.7471-0.17870.12460.53390.05170.9912-6.5598-9.116931.3048
292.30530.4692-0.63241.5209-0.15040.54210.3867-0.97140.0763-0.1558-0.3817-0.5539-0.04760.02190.03950.4052-0.10620.05160.7461-0.03150.6022-1.56275.676738.0335
300.79090.0590.7310.24390.44950.81360.2589-0.3699-0.65520.70350.0120.3170.029-0.481-0.00670.6456-0.00810.10840.61350.09970.73014.241-1.691633.8696
311.64160.28351.36810.7441-0.3920.7113-0.1262-0.79950.17070.36460.0346-0.23470.07320.1273-0.06510.6371-0.0534-0.27230.5652-0.06650.657119.708876.104928.8253
320.18120.2460.54780.6680.39910.6513-0.16010.28450.5460.0870.1483-1.0248-0.27490.7794-0.01450.9101-0.1772-0.17490.7349-0.00040.83625.582372.300120.2781
331.1721-1.1394-0.04360.64541.01822.4315-0.2417-0.23610.2646-0.16650.3012-0.1648-0.0070.4923-0.0020.5718-0.0863-0.16110.56190.00060.632321.184970.995824.0947
341.83370.021-1.18911.66091.03883.3287-0.10760.65070.1615-1.2065-0.23260.0749-0.5459-0.4786-0.68330.9141-0.0186-0.34120.62860.07430.53368.324374.62945.8219
350.9672-0.1155-0.51390.11040.12630.20890.78350.97681.4304-0.1421-0.05660.3222-1.1067-0.89890.28740.73480.0264-0.43661.22230.28640.6651-4.293368.5878.1057
360.9976-0.6588-0.95161.55421.54633.1359-0.25290.10870.5487-0.5083-0.18590.3085-0.5462-0.2682-0.29630.74930.0325-0.32890.44830.01870.70623.831975.432714.6144
371.2033-0.1895-1.15550.76751.26442.3151-0.50750.65890.3626-0.6557-0.1668-0.3516-0.4767-0.5327-0.81330.8925-0.0683-0.22050.60360.17110.645310.484974.59089.1057
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'G' and (resid 343 through 362 )
2X-RAY DIFFRACTION2chain 'G' and (resid 363 through 377 )
3X-RAY DIFFRACTION3chain 'G' and (resid 378 through 400 )
4X-RAY DIFFRACTION4chain 'G' and (resid 401 through 415 )
5X-RAY DIFFRACTION5chain 'G' and (resid 416 through 425 )
6X-RAY DIFFRACTION6chain 'G' and (resid 426 through 438 )
7X-RAY DIFFRACTION7chain 'G' and (resid 439 through 443 )
8X-RAY DIFFRACTION8chain 'G' and (resid 444 through 458 )
9X-RAY DIFFRACTION9chain 'G' and (resid 459 through 474 )
10X-RAY DIFFRACTION10chain 'D' and (resid 342 through 362 )
11X-RAY DIFFRACTION11chain 'D' and (resid 363 through 400 )
12X-RAY DIFFRACTION12chain 'D' and (resid 401 through 414 )
13X-RAY DIFFRACTION13chain 'D' and (resid 415 through 425 )
14X-RAY DIFFRACTION14chain 'D' and (resid 426 through 438 )
15X-RAY DIFFRACTION15chain 'D' and (resid 439 through 458 )
16X-RAY DIFFRACTION16chain 'D' and (resid 459 through 475 )
17X-RAY DIFFRACTION17chain 'A' and (resid 343 through 401 )
18X-RAY DIFFRACTION18chain 'A' and (resid 402 through 415 )
19X-RAY DIFFRACTION19chain 'A' and (resid 416 through 458 )
20X-RAY DIFFRACTION20chain 'A' and (resid 459 through 474 )
21X-RAY DIFFRACTION21chain 'B' and (resid 345 through 362 )
22X-RAY DIFFRACTION22chain 'B' and (resid 363 through 409 )
23X-RAY DIFFRACTION23chain 'B' and (resid 410 through 438 )
24X-RAY DIFFRACTION24chain 'B' and (resid 439 through 475 )
25X-RAY DIFFRACTION25chain 'C' and (resid 343 through 363 )
26X-RAY DIFFRACTION26chain 'C' and (resid 364 through 400 )
27X-RAY DIFFRACTION27chain 'C' and (resid 401 through 415 )
28X-RAY DIFFRACTION28chain 'C' and (resid 416 through 425 )
29X-RAY DIFFRACTION29chain 'C' and (resid 426 through 458 )
30X-RAY DIFFRACTION30chain 'C' and (resid 459 through 474 )
31X-RAY DIFFRACTION31chain 'E' and (resid 344 through 401 )
32X-RAY DIFFRACTION32chain 'E' and (resid 402 through 425 )
33X-RAY DIFFRACTION33chain 'E' and (resid 426 through 473 )
34X-RAY DIFFRACTION34chain 'F' and (resid 342 through 400 )
35X-RAY DIFFRACTION35chain 'F' and (resid 401 through 415 )
36X-RAY DIFFRACTION36chain 'F' and (resid 416 through 458 )
37X-RAY DIFFRACTION37chain 'F' and (resid 459 through 475 )

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