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- PDB-5e4w: Crystal structure of cpSRP43 chromodomains 2 and 3 in complex wit... -

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Basic information

Entry
Database: PDB / ID: 5e4w
TitleCrystal structure of cpSRP43 chromodomains 2 and 3 in complex with the Alb3 tail
Components
  • Inner membrane protein ALBINO3, chloroplastic
  • Signal recognition particle 43 kDa protein, chloroplastic
  • Thioredoxin-1
KeywordsTRANSPORT PROTEIN / Signal recognition particle / chromodomain / membrane insertase Alb3 / chloroplast / signaling protein
Function / homology
Function and homology information


: / protein localization to chloroplast / protein import into chloroplast thylakoid membrane / protein heterotrimerization / membrane insertase activity / thylakoid membrane organization / response to high light intensity / signal recognition particle, endoplasmic reticulum targeting / chloroplast thylakoid / chloroplast envelope ...: / protein localization to chloroplast / protein import into chloroplast thylakoid membrane / protein heterotrimerization / membrane insertase activity / thylakoid membrane organization / response to high light intensity / signal recognition particle, endoplasmic reticulum targeting / chloroplast thylakoid / chloroplast envelope / chloroplast stroma / protein insertion into membrane / chloroplast thylakoid membrane / protein-disulfide reductase activity / cell redox homeostasis / chloroplast / peroxisome / disordered domain specific binding / protein-macromolecule adaptor activity / membrane => GO:0016020 / protein domain specific binding / protein-containing complex / identical protein binding / metal ion binding / cytosol
Similarity search - Function
Signal recognition particle 43kDa protein / Membrane insertase YidC/Oxa1, C-terminal / 60Kd inner membrane protein / Membrane insertase YidC/ALB3/OXA1/COX18 / Chromo domain / Chromo (CHRromatin Organisation MOdifier) domain / Chromo and chromo shadow domain profile. / Thioredoxin / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #40 / Chromo/chromo shadow domain ...Signal recognition particle 43kDa protein / Membrane insertase YidC/Oxa1, C-terminal / 60Kd inner membrane protein / Membrane insertase YidC/ALB3/OXA1/COX18 / Chromo domain / Chromo (CHRromatin Organisation MOdifier) domain / Chromo and chromo shadow domain profile. / Thioredoxin / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #40 / Chromo/chromo shadow domain / Chromatin organization modifier domain / Chromo-like domain superfamily / Thioredoxin / Thioredoxin, conserved site / Thioredoxin family active site. / Thioredoxin domain profile. / Thioredoxin domain / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Glutaredoxin / Glutaredoxin / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Thioredoxin-like superfamily / Beta Barrel / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Signal recognition particle 43 kDa protein, chloroplastic / Thioredoxin 1 / Inner membrane protein ALBINO3, chloroplastic
Similarity search - Component
Biological speciesEscherichia coli O157:H7 (bacteria)
Arabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsHorn, A. / Ahmed, Y.L. / Wild, K. / Sinning, I.
CitationJournal: Nat Commun / Year: 2015
Title: Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.
Authors: Horn, A. / Hennig, J. / Ahmed, Y.L. / Stier, G. / Wild, K. / Sattler, M. / Sinning, I.
History
DepositionOct 7, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Dec 2, 2015Provider: repository / Type: Initial release
Revision 1.1Jan 10, 2024Group: 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 / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_symmetry

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Thioredoxin-1
B: Thioredoxin-1
C: Signal recognition particle 43 kDa protein, chloroplastic
D: Signal recognition particle 43 kDa protein, chloroplastic
E: Inner membrane protein ALBINO3, chloroplastic
F: Inner membrane protein ALBINO3, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,12210
Polymers49,8586
Non-polymers2644
Water73941
1
A: Thioredoxin-1
D: Signal recognition particle 43 kDa protein, chloroplastic
F: Inner membrane protein ALBINO3, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,0615
Polymers24,9293
Non-polymers1322
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2870 Å2
ΔGint-13 kcal/mol
Surface area12480 Å2
MethodPISA
2


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7630 Å2
ΔGint-26 kcal/mol
Surface area23460 Å2
MethodPISA
3
B: Thioredoxin-1
C: Signal recognition particle 43 kDa protein, chloroplastic
E: Inner membrane protein ALBINO3, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,0615
Polymers24,9293
Non-polymers1322
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2970 Å2
ΔGint-12 kcal/mol
Surface area12770 Å2
MethodPISA
Unit cell
Length a, b, c (Å)79.592, 163.668, 37.430
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein Thioredoxin-1 / Trx-1


Mass: 11744.438 Da / Num. of mol.: 2 / Fragment: UNP residues 3-109
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli O157:H7 (bacteria) / Gene: trxA, Z5291, ECs4714 / Production host: Escherichia coli (E. coli) / References: UniProt: P0AA27
#2: Protein Signal recognition particle 43 kDa protein, chloroplastic / Chromo protein SRP43 / CpSRP43


Mass: 12032.213 Da / Num. of mol.: 2 / Fragment: UNP residues 265-369
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: CAO, CPSRP43, At2g47450, T30B22.25 / Production host: Escherichia coli (E. coli) / References: UniProt: O22265

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Protein/peptide , 1 types, 2 molecules EF

#3: Protein/peptide Inner membrane protein ALBINO3, chloroplastic


Mass: 1152.396 Da / Num. of mol.: 2 / Fragment: UNP residues 453-461
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: ALB3, At2g28800, F8N16.9 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8LBP4

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Non-polymers , 3 types, 45 molecules

#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 41 / 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: 2.44 Å3/Da / Density % sol: 49.69 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 20% PEG 3350, 0.2 M Ca(OAc)2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.992 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 30, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.992 Å / Relative weight: 1
ReflectionResolution: 2.8→45 Å / Num. obs: 12743 / % possible obs: 99.9 % / Redundancy: 5.5 % / Rmerge(I) obs: 0.24 / Net I/σ(I): 6.7
Reflection shellResolution: 2.8→45 Å / Rmerge(I) obs: 0.93

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Processing

Software
NameVersionClassification
PHENIXrefinement
PDB_EXTRACT3.15data extraction
XDSdata reduction
Aimlessdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3dxb

3dxb


Resolution: 2.8→45 Å / FOM work R set: 0.7134 / SU ML: 0.6 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 33.32 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2915 619 4.95 %
Rwork0.2495 11882 -
obs0.2517 12501 98.18 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 156.42 Å2 / Biso mean: 71.57 Å2 / Biso min: 2.21 Å2
Refinement stepCycle: final / Resolution: 2.8→45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3490 0 14 41 3545
Biso mean--63.11 40.86 -
Num. residues----444
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0033562
X-RAY DIFFRACTIONf_angle_d0.734806
X-RAY DIFFRACTIONf_chiral_restr0.025530
X-RAY DIFFRACTIONf_plane_restr0.002616
X-RAY DIFFRACTIONf_dihedral_angle_d12.1211314
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8001-3.08180.451420.372775X-RAY DIFFRACTION94
3.0818-3.52760.35461480.31532952X-RAY DIFFRACTION99
3.5276-4.44380.30771520.22243008X-RAY DIFFRACTION100
4.4438-450.22161770.2043147X-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)
16.1172-1.817-2.26857.9013-5.64052.00980.7353-0.26581.35960.41540.5819-1.1911-1.2631.7366-0.16010.7365-0.1673-0.25060.8612-0.03730.9559-1.829742.90360.3845
28.8749-0.6081-0.30539.2673-5.23162.01310.42681.1211-0.0009-0.89920.0505-2.05692.01510.4604-0.12070.7040.11630.03760.72610.04410.9967-0.910335.4288-9.7665
36.2292.7357-2.11654.12271.89218.99320.5061-0.54170.2782-1.19191.0622-1.9329-0.67462.0073-0.14380.07980.1962-0.00630.6744-0.0980.5758-6.356134.5123-2.6706
42.6243-0.2041.10314.7753-3.01219.8503-0.16540.32041.4870.3175-0.51570.1268-2.4380.017-0.38740.7848-0.014-0.10560.34080.15850.7118-16.840949.2882-4.2099
54.74650.7058-0.17936.3235-0.98989.21920.9013-0.39681.64511.6626-1.0113-0.7572-0.96780.7248-0.16280.85720.1094-0.00430.48620.06430.6193-10.520343.98248.803
64.3948-0.6004-0.91586.8128-1.51067.64270.09960.32440.2601-0.44880.0693-0.39730.2970.6252-0.21270.33880.1136-0.03240.2033-0.00740.6021-10.441638.69-5.6677
72.66152.2271-0.54473.4038-0.61437.15470.33980.4302-0.35240.54180.2-0.26611.03780.2077-0.27330.64860.2329-0.15770.24420.0190.4528-14.40832.3613-0.8795
88.8117-0.9415-0.3287.10732.35547.15630.2281-0.6778-0.7990.43670.088-0.36951.0730.1761-0.35310.82990.0296-0.24750.46050.05470.3994-16.654632.60479.2349
97.5951-1.5708-2.95475.66264.70377.7183-1.28881.0759-1.1672-1.0807-0.06691.30030.2469-1.75230.64470.5505-0.0972-0.10070.7338-0.23130.892-34.351518.7052-12.0235
107.25991.73794.2199.9215-0.34062.0730.3865-0.11520.6089-1.5745-0.54131.75670.1897-1.09990.46660.79170.0945-0.35681.05810.11570.5763-34.901829.7735-13.0961
115.9376-3.0268-0.68967.80691.48924.6327-0.55350.4119-1.66880.7112-0.7647-0.31940.82961.3050.2271.0244-0.23460.04860.321-0.15560.3454-23.483315.6744-6.5062
124.5004-1.5469-2.85154.59682.76753.7232-1.35530.5948-1.65910.37570.16721.64541.3266-1.36020.72550.9287-0.07470.240.5236-0.01740.8859-32.163615.75023.0154
134.2112-1.4994-1.1429.95445.75872.1430.23280.0287-0.368-0.5137-0.37631.42650.8307-1.17750.73340.7982-0.207-0.04930.60480.08060.5598-33.853321.8197-2.8368
143.9498-0.903-1.56967.74243.53397.6633-0.19180.70980.1244-1.13080.03090.2206-0.2765-0.5429-0.00040.5921-0.0032-0.05610.44120.05470.3512-22.976224.3349-11.4578
155.6993-1.5501-3.2259.3219-0.12692.4064-0.061-0.20580.03420.45050.22880.4525-0.1565-0.14220.00920.5475-0.04880.07750.3258-0.07070.3476-24.831626.47423.3722
167.3895-0.474-4.39844.78192.62192.0441-1.23310.44181.3645-2.5356-0.1925-0.3404-1.5083-0.9329-0.18810.97670.1565-0.02570.3837-0.11480.7875-12.532517.7165-7.3068
179.3335-1.8105-2.76566.41863.32087.90540.176-0.365-0.5771-1.68081.0432-0.9977-0.75421.6578-0.71090.0508-0.04090.36070.641-0.25521.2976-0.710210.4253-12.4495
182.3095-0.6662-3.43988.41254.57610.06780.68460.1730.6074-0.5479-0.1954-0.2296-2.64210.7972-0.62021.1317-0.18740.1420.6159-0.07540.7879-4.17316.8338-15.1963
192.0303-0.1083-6.80066.68313.70351.99710.77950.79170.6219-0.43941.3372-0.8744-0.87831.0545-0.97050.7126-0.0897-0.25510.9027-0.17310.7-2.860216.6525-9.7552
206.24273.61276.18036.87164.61168.77430.047-0.43560.34441.3386-0.19230.40030.0437-0.40920.13660.74890.11330.14410.3764-0.05220.433-11.63422.8498-23.163
219.08423.41224.27865.97924.25038.94480.3228-0.0206-1.09670.6141-0.104-0.03841.24860.2507-0.18410.8326-0.10150.18750.4375-0.03750.5533-15.7561-6.2808-29.3327
227.47282.47837.00749.82645.16917.22721.208-1.38870.94350.5655-0.17820.45950.32881.74830.01171.4782-0.0382-0.0157-0.30490.20370.3446-13.13340.8663-30.8696
237.40366.08016.63878.68285.9595.95960.78910.7021.3859-1.1789-0.80161.4176-1.562-1.53570.97190.67660.22890.20160.78390.22491.0948-26.99880.4833-34.1856
243.49-0.68141.12242.2126-4.992.25140.22370.44970.08610.90090.76340.6711-0.730.2563-0.57340.68340.1209-0.19320.5631-0.02720.5102-24.174345.0288-13.2816
251.9119-2.10561.33027.9033-1.78750.95750.12440.04080.14451.85451.57111.7636-1.2851-2.5876-1.0719-0.03830.3019-0.29351.31180.81031.3082-37.3651.0865-13.7664
264.9818-2.84741.47042.0464-1.8569.7174-0.06270.1271-0.1403-0.98130.47551.7820.3904-1.6034-0.8861.0039-0.10460.06360.8610.09840.3518-30.039345.2908-18.7763
274.24551.21970.15732.083-3.56879.54070.41390.7168-0.4462-1.0407-0.62410.93232.45410.2312-0.57521.0122-0.01590.0020.4887-0.22990.5912-22.927739.1552-22.2391
286.42240.61515.68572.0475-3.28952.0061-0.11220.6491-1.36991.73960.55991.8850.5675-2.1532-1.08250.74630.1165-0.13281.10590.18790.7549-31.708744.0983-14.0175
290.9447-1.58330.14589.8833-6.51595.484-0.0759-0.7560.26371.72970.57610.2122-2.4599-1.3346-0.37560.68070.34390.11630.67280.04090.5304-26.25755.288-15.7137
30-0.0172-0.83551.14818.6061-4.46776.4304-0.9911-0.22810.0378-5.80870.90490.2597-1.5585-0.1341-0.1537-0.42520.5868-0.0340.26890.12390.6088-21.93162.5891-31.8375
314.3452-1.3866-4.78472.026-4.03717.2722-0.57910.0714-0.12551.0937-0.23020.3102-2.7365-0.3644-0.0491.0350.3606-0.03280.7092-0.2870.7733-24.685277.1243-26.6019
324.39692.20812.78262.035-5.12856.1258-0.5845-0.3420.1389-1.19460.1732-0.32620.53040.12260.00620.65260.1119-0.06680.37660.07150.4696-20.885765.708-34.4463
332.4066-6.71832.92882.0664-8.60833.8879-0.31270.5975-0.34-1.50240.88392.0352.3035-2.0558-0.7378-7.7245.5434-2.1089-2.18571.34530.2563-26.100356.806-38.6253
340.1621-0.01620.96627.285-3.36387.59980.5065-0.80830.09270.5764-0.11760.0319-0.89150.7379-0.11060.69510.0963-0.06670.50960.15210.7493-20.433765.7884-29.5977
350.6487-1.54181.60021.9149-7.46236.1755-1.1921.93910.0643-1.0209-1.3016-2.6051-1.13291.87150.7523-1.07230.79270.99380.6187-0.17891.6012-10.190966.9864-37.2948
369.05157.00825.04012.366-2.3082.13570.2314-0.58521.4437-0.3123-0.6812-0.0425-1.30371.28590.82681.0469-0.00540.02670.8041-0.02650.6113-10.71754.8169-24.8255
373.7526-2.3087-5.63085.38080.19772.2382-1.49690.3099-0.36090.66410.34290.98462.744-0.73670.67760.3475-0.3833-0.28030.8131-0.01440.6497-24.467557.6417-27.9072
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 12 through 17 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 18 through 25 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 26 through 38 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 39 through 48 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 49 through 58 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 59 through 86 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 87 through 105 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 106 through 120 )A0
9X-RAY DIFFRACTION9chain 'B' and (resid 12 through 21 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 22 through 31 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 32 through 48 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 49 through 58 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 59 through 69 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 70 through 94 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 95 through 119 )B0
16X-RAY DIFFRACTION16chain 'C' and (resid 265 through 271 )C0
17X-RAY DIFFRACTION17chain 'C' and (resid 272 through 283 )C0
18X-RAY DIFFRACTION18chain 'C' and (resid 284 through 296 )C0
19X-RAY DIFFRACTION19chain 'C' and (resid 297 through 304 )C0
20X-RAY DIFFRACTION20chain 'C' and (resid 305 through 330 )C0
21X-RAY DIFFRACTION21chain 'C' and (resid 331 through 343 )C0
22X-RAY DIFFRACTION22chain 'C' and (resid 344 through 358 )C0
23X-RAY DIFFRACTION23chain 'C' and (resid 359 through 369 )C0
24X-RAY DIFFRACTION24chain 'D' and (resid 265 through 275 )D0
25X-RAY DIFFRACTION25chain 'D' and (resid 276 through 285 )D0
26X-RAY DIFFRACTION26chain 'D' and (resid 286 through 291 )D0
27X-RAY DIFFRACTION27chain 'D' and (resid 292 through 296 )D0
28X-RAY DIFFRACTION28chain 'D' and (resid 297 through 304 )D0
29X-RAY DIFFRACTION29chain 'D' and (resid 305 through 314 )D0
30X-RAY DIFFRACTION30chain 'D' and (resid 315 through 330 )D0
31X-RAY DIFFRACTION31chain 'D' and (resid 331 through 336 )D0
32X-RAY DIFFRACTION32chain 'D' and (resid 337 through 343 )D0
33X-RAY DIFFRACTION33chain 'D' and (resid 344 through 349 )D0
34X-RAY DIFFRACTION34chain 'D' and (resid 350 through 358 )D0
35X-RAY DIFFRACTION35chain 'D' and (resid 359 through 369 )D0
36X-RAY DIFFRACTION36chain 'E' and (resid 453 through 461 )E0
37X-RAY DIFFRACTION37chain 'F' and (resid 454 through 461 )F0

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