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- PDB-5ejm: ThDP-Mn2+ complex of R413A variant of EcMenD soaked with 2-ketogl... -

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Basic information

Entry
Database: PDB / ID: 5ejm
TitleThDP-Mn2+ complex of R413A variant of EcMenD soaked with 2-ketoglutarate for 35 min
Components2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
KeywordsTRANSFERASE / Post-decarboxylation intermediate of R413A variant of EcMenD
Function / homology
Function and homology information


2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase / 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity / menaquinone biosynthetic process / thiamine pyrophosphate binding / manganese ion binding / magnesium ion binding / protein homodimerization activity
Similarity search - Function
Menaquinone biosynthesis protein MenD, middle domain / Middle domain of thiamine pyrophosphate / 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase / Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain / Thiamine pyrophosphate enzyme, N-terminal TPP binding domain / Thiamine pyrophosphate enzyme, C-terminal TPP-binding / Thiamine pyrophosphate enzyme, C-terminal TPP binding domain / Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains / TPP-binding domain / Thiamin diphosphate-binding fold ...Menaquinone biosynthesis protein MenD, middle domain / Middle domain of thiamine pyrophosphate / 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase / Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain / Thiamine pyrophosphate enzyme, N-terminal TPP binding domain / Thiamine pyrophosphate enzyme, C-terminal TPP-binding / Thiamine pyrophosphate enzyme, C-terminal TPP binding domain / Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains / TPP-binding domain / Thiamin diphosphate-binding fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
: / Chem-TD5 / 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
Similarity search - Component
Biological speciesEscherichia coli K12 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.72 Å
AuthorsSong, H.G. / Dong, C. / Chen, Y.Z. / Sun, Y.R. / Guo, Z.H.
CitationJournal: Biochem. J. / Year: 2018
Title: Two active site arginines are critical determinants of substrate binding and catalysis in MenD, a thiamine-dependent enzyme in menaquinone biosynthesis.
Authors: Qin, M.M. / Song, H.G. / Dai, X. / Chen, Y.Z. / Guo, Z.H.
History
DepositionNov 2, 2015Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Nov 2, 2016Provider: repository / Type: Initial release
Revision 1.1Nov 28, 2018Group: Data collection / Database references / Derived calculations
Category: citation / citation_author / pdbx_struct_oper_list
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.name / _pdbx_struct_oper_list.symmetry_operation
Revision 1.2Mar 20, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
B: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
C: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
D: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
E: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
F: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
G: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
H: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)496,67340
Polymers490,7818
Non-polymers5,89232
Water83,7704650
1
A: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
B: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)124,16810
Polymers122,6952
Non-polymers1,4738
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8380 Å2
ΔGint-45 kcal/mol
Surface area37830 Å2
MethodPISA
2
C: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
D: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)124,16810
Polymers122,6952
Non-polymers1,4738
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8500 Å2
ΔGint-45 kcal/mol
Surface area37650 Å2
MethodPISA
3
E: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
F: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)124,16810
Polymers122,6952
Non-polymers1,4738
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8460 Å2
ΔGint-45 kcal/mol
Surface area37800 Å2
MethodPISA
4
G: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
H: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)124,16810
Polymers122,6952
Non-polymers1,4738
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8470 Å2
ΔGint-43 kcal/mol
Surface area37880 Å2
MethodPISA
Unit cell
Length a, b, c (Å)90.660, 90.670, 169.370
Angle α, β, γ (deg.)76.07, 83.29, 64.32
Int Tables number1
Space group name H-MP1

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Components

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Protein , 1 types, 8 molecules ABCDEFGH

#1: Protein
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase / ThDP-dependent enzyme MenD / SEPHCHC synthase / Menaquinone biosynthesis protein MenD


Mass: 61347.664 Da / Num. of mol.: 8 / Mutation: R413A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K12 (bacteria) / Strain: K12 substr. MG1655 / Gene: menD, b2264, JW5374 / Plasmid: pET28a / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3)
References: UniProt: P17109, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

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Non-polymers , 5 types, 4682 molecules

#2: Chemical
ChemComp-TD5 / (4~{R})-4-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-4-methyl-5-[2-[oxidanyl(phosphonooxy)phosphoryl]oxyethyl]-1,3-thiazol-3-ium-2-yl]-4-oxidanyl-butanoic acid


Mass: 527.403 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C16H25N4O10P2S
#3: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mn
#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C2H6O2
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 4650 / 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: 2.48 Å3/Da / Density % sol: 50.36 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 0.16 M magnesium formate, 1% tascimate pH 7.0, 0.02 M HEPES pH 7.0, 14% PEG 3350 and 2% PEG MME 5000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9792 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 21, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 1.72→31.48 Å / Num. obs: 482851 / % possible obs: 95.9 % / Redundancy: 1.9 % / Rmerge(I) obs: 0.064 / Net I/σ(I): 6.3
Reflection shellResolution: 1.72→1.75 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.29 / Mean I/σ(I) obs: 2.1 / % possible all: 91.2

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
iMOSFLMdata reduction
Aimlessdata scaling
PHASERphasing
RefinementResolution: 1.72→31.476 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.98 / Phase error: 19 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1919 24073 4.99 %
Rwork0.1639 --
obs0.1653 482814 95.84 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.72→31.476 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms34460 0 352 4650 39462
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00736313
X-RAY DIFFRACTIONf_angle_d1.07649664
X-RAY DIFFRACTIONf_dihedral_angle_d13.78613129
X-RAY DIFFRACTIONf_chiral_restr0.0455466
X-RAY DIFFRACTIONf_plane_restr0.0056505
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.717-1.73650.26387440.225214462X-RAY DIFFRACTION90
1.7365-1.75690.24958110.216115136X-RAY DIFFRACTION95
1.7569-1.77840.24277730.208415314X-RAY DIFFRACTION95
1.7784-1.80090.24887970.208115102X-RAY DIFFRACTION95
1.8009-1.82460.2439020.197615173X-RAY DIFFRACTION96
1.8246-1.84960.21858670.189115288X-RAY DIFFRACTION96
1.8496-1.8760.24398130.193315051X-RAY DIFFRACTION96
1.876-1.9040.22558060.184415310X-RAY DIFFRACTION96
1.904-1.93370.21098410.177215301X-RAY DIFFRACTION96
1.9337-1.96540.21068130.173815295X-RAY DIFFRACTION96
1.9654-1.99930.21578310.177615194X-RAY DIFFRACTION96
1.9993-2.03570.20748430.173815235X-RAY DIFFRACTION96
2.0357-2.07480.20088240.165715403X-RAY DIFFRACTION96
2.0748-2.11720.21547780.17115353X-RAY DIFFRACTION96
2.1172-2.16320.21237990.165515424X-RAY DIFFRACTION96
2.1632-2.21350.20637620.167215345X-RAY DIFFRACTION96
2.2135-2.26880.19878330.165615330X-RAY DIFFRACTION96
2.2688-2.33020.20287840.164815376X-RAY DIFFRACTION96
2.3302-2.39870.19858360.161615409X-RAY DIFFRACTION97
2.3987-2.47610.20768230.166615340X-RAY DIFFRACTION97
2.4761-2.56450.19267510.163815487X-RAY DIFFRACTION97
2.5645-2.66720.20487290.165915541X-RAY DIFFRACTION97
2.6672-2.78850.20847490.169915408X-RAY DIFFRACTION97
2.7885-2.93540.18517620.16515574X-RAY DIFFRACTION97
2.9354-3.11920.17377420.159315530X-RAY DIFFRACTION97
3.1192-3.35980.1877920.159915428X-RAY DIFFRACTION97
3.3598-3.69740.17017520.153515306X-RAY DIFFRACTION96
3.6974-4.23130.15898110.145215004X-RAY DIFFRACTION94
4.2313-5.32680.16469000.143514859X-RAY DIFFRACTION94
5.3268-31.48120.17058050.155915763X-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)
10.1891-0.2236-0.05070.45910.13010.36950.02880.0029-0.0114-0.017-0.01850.07550.0112-0.0564-0.00850.1466-0.0279-0.00640.068-0.00860.1277-44.36871.0063-23.1258
20.66230.126-0.20640.2294-0.01820.12530.0292-0.02280.1386-0.014-0.0183-0.0297-0.08580.01410.00040.1711-0.0183-0.02630.0889-0.0110.1557-32.205621.2131-26.4936
30.2103-0.09590.0420.88410.41780.56190.00520.03850.0465-0.0260.0019-0.1609-0.01680.10560.00660.1362-0.0290.0210.11570.00640.1669-7.85712.879-34.1807
40.25620.0207-0.09810.3740.04610.4040.00640.0258-0.00970.0184-0.0058-0.06130.0720.0663-0.00350.16940.00540.02040.1042-0.01390.1321-16.7762-8.7568-39.6812
50.3447-0.1120.10740.35460.01080.6052-0.0013-0.0112-0.00240.0160.0115-0.05910.0640.0634-0.00650.1719-0.0084-0.01380.0743-0.00470.1348-17.9884-13.3798-10.1801
60.75130.1143-0.18250.1118-0.12870.1777-0.0594-0.078-0.23570.09570.0113-0.04690.13020.0089-0.00070.2739-0.0093-0.01160.13-0.01170.2104-26.4124-24.21347.1906
70.24520.1065-0.04390.68620.20780.69630.0094-0.029-0.01910.04150.0020.07790.0509-0.0684-0.00530.2147-0.05220.00730.10430.00830.1867-53.4696-29.9619-4.244
80.32380.1133-0.01220.28250.05030.2285-0.00640.0146-0.0527-0.03660.01880.03310.0865-0.0603-0.01250.2304-0.0445-0.01340.093-0.00850.1795-44.6173-32.8293-23.0271
90.35710.3083-0.03030.4229-0.10840.2964-0.01970.0193-0.0052-0.11730.02770.01690.0544-0.04070.00240.2507-0.0432-0.02830.1095-0.02340.144-41.7527-27.7727-33.8188
100.30420.20270.01870.53960.07260.60990.0237-0.0409-0.03560.09580.0030.070.0032-0.0515-0.02960.2088-0.02460.02490.10590.00480.1542-48.81372.32557.9078
111.6501-0.47390.44620.5721-0.07660.4452-0.0856-0.1049-0.11530.25130.07220.06310.1099-0.0291-0.01980.3227-0.04210.01810.15090.02650.1897-44.2207-19.069911.8106
120.0457-0.125-0.17640.49360.56980.7415-0.1119-0.1876-0.03550.42980.1336-0.20790.22210.1618-0.0140.40840.0593-0.09670.2330.00370.2042-18.0022-12.17828.7199
130.2292-0.19090.25070.78580.08110.6515-0.0162-0.1684-0.01860.25570.0648-0.1240.00260.1085-0.03920.40280.0081-0.05990.2194-0.01580.1757-26.789110.405131.86
140.4702-0.0547-0.15480.43180.07580.4476-0.0074-0.04760.0060.07220.0114-0.0937-0.01270.0623-0.00090.1919-0.0319-0.02360.103-0.00870.1631-19.121514.86713.218
151.8088-0.62530.67460.2122-0.19010.5226-0.0640.09850.11690.0246-0.0037-0.1094-0.16690.1047-0.00970.2073-0.0556-0.01940.09990.00130.2012-21.643526.1619-15.9845
160.3001-0.1403-0.12540.40560.35450.9158-0.02320.00090.00110.0207-0.02740.0636-0.152-0.09610.03930.210.003-0.00540.0782-0.01720.1431-50.953535.9162-7.9417
170.1629-0.2123-0.00940.5448-0.03310.3995-0.0454-0.08530.03670.15420.03450.0424-0.0326-0.04950.01970.26980.00470.01650.1101-0.0250.1357-43.541128.916315.0353
181.0316-0.27780.12090.3027-0.03940.7173-0.1231-0.18250.06430.14820.05460.0705-0.1106-0.08120.03070.31720.03740.02740.1478-0.0370.2013-51.085838.205216.439
190.3923-0.2111-0.06520.38140.08580.3254-0.01390.0188-0.0190.02280.04710.01230.038-0.0597-0.03070.05940.00390.00830.15690.00710.1176-50.389910.8393-68.1631
201.03651.0590.19361.21330.07890.14770.0089-0.0039-0.06040.05550.0031-0.09440.06060.08080.00840.08650.02410.01470.16530.00630.1485-28.46547.9187-66.0659
210.6194-0.3056-0.40860.5040.18570.5323-0.009-0.03260.1420.06560.0051-0.1264-0.11120.07050.01740.0952-0.0098-0.0290.1646-0.01910.1673-23.627938.428-57.4082
220.3497-0.07190.01420.33680.08220.3942-0.0199-0.01470.08580.02170.0021-0.0316-0.1014-0.05090.00770.12690.031-0.00960.1535-0.0320.1365-47.365839.8054-51.6463
230.3203-0.13110.03370.2953-0.08650.6030.0110.04650.07330.0026-0.0045-0.036-0.0647-0.0332-0.00720.08750.02510.00260.17150.01340.1426-52.011940.8114-81.111
240.57350.61090.15560.72590.01470.1987-0.03510.0830.095-0.11820.02380.1273-0.0632-0.1159-0.02830.13870.03560.00830.25690.04290.212-65.478637.7663-98.5736
250.5204-0.0961-0.22580.23910.10070.7490.00640.0291-0.0718-0.01770.00770.07180.0651-0.1099-0.00630.0792-0.0019-0.00760.25240.02520.1861-83.571215.6555-85.4104
260.33570.053-0.00460.22910.00660.219-0.0078-0.01750.02780.01650.03280.031-0.0176-0.1001-0.02050.07930.02090.00880.24750.02030.1587-76.884929.6653-66.6723
270.53960.05970.09540.12830.02120.275-0.0242-0.1448-0.05980.00660.03750.02440.0075-0.0687-0.00650.10770.01020.02070.28180.02390.1484-76.226622.7269-56.8074
280.33590.0097-0.05240.31010.09910.4691-0.00990.07460.1133-0.04020.0089-0.0565-0.03740.04890.00280.0830.00460.01410.20680.03190.1602-26.926627.6032-94.4923
290.03790.2277-0.02181.4925-0.58340.44580.0312-0.00040.05360.065-0.0857-0.1137-0.00860.17320.00530.08430.0091-0.00260.21790.01330.1838-17.969720.2775-75.4112
300.3795-0.2096-0.32610.5910.14390.9402-0.00670.0048-0.0554-0.0109-0.0373-0.00010.12590.10930.02940.10540.04790.00420.20240.00460.1454-21.7122-10.4138-83.5102
310.3507-0.10190.010.5329-0.06830.42620.01960.1096-0.0319-0.1137-0.0316-0.03230.10060.03110.02180.14550.04830.0160.2321-0.00420.1445-23.6275-3.3271-106.8717
320.5389-0.0366-0.01690.2461-0.01620.58920.040.0745-0.0332-0.0417-0.01640.0380.0435-0.0405-0.01960.08750.0136-0.00710.21220.00830.1338-50.98176.0994-99.273
330.25330.14450.04791.4369-0.3480.34020.05540.12270.04-0.1659-0.03430.2185-0.017-0.1787-0.00920.13230.03740.00570.34770.02560.2075-68.424819.2638-103.1451
340.5084-0.1588-0.1830.53350.19890.96960.08770.23190.1704-0.2099-0.0498-0.0131-0.1555-0.135-0.00830.19380.06250.0120.31130.09670.1936-54.005141.7164-116.3183
350.8055-0.0878-0.24620.2527-0.03410.5450.11660.18480.2365-0.2989-0.04040.0124-0.161-0.0234-0.0390.31680.0550.04670.39910.14510.2516-40.35834.9978-133.0992
360.6325-0.2160.05730.3742-0.20790.56420.06980.17110.1189-0.1654-0.0614-0.0696-0.05990.0425-0.02170.20030.04070.04370.33460.06970.1618-34.384122.5349-123.217
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 182 )
2X-RAY DIFFRACTION2chain 'A' and (resid 183 through 230 )
3X-RAY DIFFRACTION3chain 'A' and (resid 231 through 384 )
4X-RAY DIFFRACTION4chain 'A' and (resid 385 through 556 )
5X-RAY DIFFRACTION5chain 'B' and (resid 1 through 182 )
6X-RAY DIFFRACTION6chain 'B' and (resid 183 through 219 )
7X-RAY DIFFRACTION7chain 'B' and (resid 220 through 347 )
8X-RAY DIFFRACTION8chain 'B' and (resid 348 through 447 )
9X-RAY DIFFRACTION9chain 'B' and (resid 448 through 556 )
10X-RAY DIFFRACTION10chain 'C' and (resid 1 through 182 )
11X-RAY DIFFRACTION11chain 'C' and (resid 183 through 219 )
12X-RAY DIFFRACTION12chain 'C' and (resid 220 through 384 )
13X-RAY DIFFRACTION13chain 'C' and (resid 385 through 556 )
14X-RAY DIFFRACTION14chain 'D' and (resid 1 through 182 )
15X-RAY DIFFRACTION15chain 'D' and (resid 183 through 219 )
16X-RAY DIFFRACTION16chain 'D' and (resid 220 through 384 )
17X-RAY DIFFRACTION17chain 'D' and (resid 385 through 513 )
18X-RAY DIFFRACTION18chain 'D' and (resid 514 through 556 )
19X-RAY DIFFRACTION19chain 'E' and (resid 1 through 182 )
20X-RAY DIFFRACTION20chain 'E' and (resid 183 through 219 )
21X-RAY DIFFRACTION21chain 'E' and (resid 220 through 384 )
22X-RAY DIFFRACTION22chain 'E' and (resid 385 through 556 )
23X-RAY DIFFRACTION23chain 'F' and (resid 1 through 182 )
24X-RAY DIFFRACTION24chain 'F' and (resid 183 through 219 )
25X-RAY DIFFRACTION25chain 'F' and (resid 220 through 363 )
26X-RAY DIFFRACTION26chain 'F' and (resid 364 through 468 )
27X-RAY DIFFRACTION27chain 'F' and (resid 469 through 556 )
28X-RAY DIFFRACTION28chain 'G' and (resid 1 through 182 )
29X-RAY DIFFRACTION29chain 'G' and (resid 183 through 219 )
30X-RAY DIFFRACTION30chain 'G' and (resid 220 through 384 )
31X-RAY DIFFRACTION31chain 'G' and (resid 385 through 556 )
32X-RAY DIFFRACTION32chain 'H' and (resid 1 through 182 )
33X-RAY DIFFRACTION33chain 'H' and (resid 183 through 219 )
34X-RAY DIFFRACTION34chain 'H' and (resid 220 through 347 )
35X-RAY DIFFRACTION35chain 'H' and (resid 348 through 384 )
36X-RAY DIFFRACTION36chain 'H' and (resid 385 through 556 )

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