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- PDB-7kx1: Dihydrodipicolinate synthase (DHDPS) from C.jejuni, Y110F mutant ... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7kx1
TitleDihydrodipicolinate synthase (DHDPS) from C.jejuni, Y110F mutant with pyruvate bound in the active in C2221 space group
Components4-hydroxy-tetrahydrodipicolinate synthaseDihydrodipicolinate synthase
KeywordsLYASE
Function / homology
Function and homology information


4-hydroxy-tetrahydrodipicolinate synthase / 4-hydroxy-tetrahydrodipicolinate synthase activity / diaminopimelate biosynthetic process / lysine biosynthetic process via diaminopimelate / cytoplasm
Similarity search - Function
4-hydroxy-tetrahydrodipicolinate synthase, DapA / Schiff base-forming aldolase, conserved site / Dihydrodipicolinate synthase signature 1. / Schiff base-forming aldolase, active site / Dihydrodipicolinate synthase signature 2. / DapA-like / Dihydrodipicolinate synthetase family / Dihydrodipicolinate synthetase family / Aldolase-type TIM barrel
Similarity search - Domain/homology
ACETATE ION / DI(HYDROXYETHYL)ETHER / TRIETHYLENE GLYCOL / 4-hydroxy-tetrahydrodipicolinate synthase
Similarity search - Component
Biological speciesCampylobacter jejuni subsp. jejuni serotype O:2 (Campylobacter)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.04 Å
AuthorsSaran, S. / Sanders, D.A.R.
Funding support Canada, 1items
OrganizationGrant numberCountry
Natural Sciences and Engineering Research Council (NSERC, Canada) Canada
CitationJournal: To Be Published
Title: B-FACTOR ANALYSIS SUGGEST THAT L-LYSINE AND R, R-BISLYSINE ALLOSTERICALLY INHIBIT Cj.DHDPS ENZYME BY DECREASING PROTEIN DYNAMICS
Authors: Saran, S. / Sanders, D.A.R.
History
DepositionDec 2, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 8, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.2Nov 29, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 4-hydroxy-tetrahydrodipicolinate synthase
B: 4-hydroxy-tetrahydrodipicolinate synthase
C: 4-hydroxy-tetrahydrodipicolinate synthase
D: 4-hydroxy-tetrahydrodipicolinate synthase
E: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)206,61824
Polymers205,0166
Non-polymers1,60218
Water10,827601
1
A: 4-hydroxy-tetrahydrodipicolinate synthase
B: 4-hydroxy-tetrahydrodipicolinate synthase
C: 4-hydroxy-tetrahydrodipicolinate synthase
D: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,79917
Polymers136,6774
Non-polymers1,12213
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12840 Å2
ΔGint-32 kcal/mol
Surface area40150 Å2
MethodPISA
2
E: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules

E: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,63814
Polymers136,6774
Non-polymers96110
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_555-x,y,-z+1/21
Buried area10850 Å2
ΔGint-42 kcal/mol
Surface area40020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)83.810, 230.100, 199.960
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11D-503-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain B
31chain C
41chain D
51chain E
61(chain F and resid 3 through 298)

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: LYS / Beg label comp-ID: LYS / End auth comp-ID: PHE / End label comp-ID: PHE / Auth seq-ID: 3 - 298 / Label seq-ID: 15 - 310

Dom-IDSelection detailsAuth asym-IDLabel asym-ID
1chain AAA
2chain BBB
3chain CCC
4chain DDD
5chain EEE
6(chain F and resid 3 through 298)FF

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Components

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Protein , 1 types, 6 molecules ABCDEF

#1: Protein
4-hydroxy-tetrahydrodipicolinate synthase / Dihydrodipicolinate synthase / HTPA synthase


Mass: 34169.258 Da / Num. of mol.: 6 / Mutation: Y110F
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) (Campylobacter)
Strain: ATCC 700819 / NCTC 11168 / Gene: dapA, Cj0806 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9PPB4, 4-hydroxy-tetrahydrodipicolinate synthase

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Non-polymers , 6 types, 619 molecules

#2: Chemical
ChemComp-PGE / TRIETHYLENE GLYCOL / Polyethylene glycol


Mass: 150.173 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C6H14O4 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical
ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H3O2 / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3 / Feature type: SUBJECT OF INVESTIGATION
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 601 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.35 Å3/Da / Density % sol: 47.68 %
Crystal growTemperature: 288.15 K / Method: microbatch / pH: 7.4
Details: 0.3 M Magnesium acetate, 10 % PEG 8000, 0.1 M Sodium acetate (pH 7.4)

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Oct 29, 2019
RadiationMonochromator: Double beam / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 1.9→46.03 Å / Num. obs: 156294 / % possible obs: 99.9 % / Redundancy: 15 % / CC1/2: 0.99 / Net I/σ(I): 8.43
Reflection shellResolution: 1.9→1.968 Å / Rmerge(I) obs: 1.077 / Num. unique obs: 15421 / % possible all: 99.59

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Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
XSCALEdata scaling
PDB_EXTRACT3.27data extraction
HKL-3000data reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4LY8

4ly8


Resolution: 2.04→45.85 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 29.31 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2538 6061 5 %
Rwork0.2135 115162 -
obs0.2155 121223 98.77 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 94.82 Å2 / Biso mean: 45.6298 Å2 / Biso min: 20 Å2
Refinement stepCycle: final / Resolution: 2.04→45.85 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13644 0 105 601 14350
Biso mean--41.89 46.06 -
Num. residues----1777
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5358X-RAY DIFFRACTION1.69TORSIONAL
12B5358X-RAY DIFFRACTION1.69TORSIONAL
13C5358X-RAY DIFFRACTION1.69TORSIONAL
14D5358X-RAY DIFFRACTION1.69TORSIONAL
15E5358X-RAY DIFFRACTION1.69TORSIONAL
16F5358X-RAY DIFFRACTION1.69TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.04-2.060.35761630.3822313883
2.06-2.090.39941780.372338187
2.09-2.110.39671950.363373097
2.11-2.140.37452010.3446378899
2.14-2.170.37732020.3525384799
2.17-2.20.35952030.33263836100
2.2-2.230.3362030.33353857100
2.23-2.260.36772030.33023875100
2.26-2.30.37452010.31773808100
2.3-2.340.36492040.30093871100
2.34-2.380.37092020.29153838100
2.38-2.420.30482030.28943855100
2.42-2.470.33422050.27533888100
2.47-2.520.29912020.26573836100
2.52-2.570.30662030.25613862100
2.57-2.630.30932040.24423876100
2.63-2.70.30092040.24233871100
2.7-2.770.28042030.2333872100
2.77-2.850.29422060.23543904100
2.85-2.940.27652030.23673852100
2.94-3.050.27972040.22153892100
3.05-3.170.24792040.20683872100
3.17-3.310.23782060.19943914100
3.31-3.490.24812060.20493901100
3.49-3.710.23152050.19343901100
3.71-3.990.20962050.16693905100
3.99-4.390.19112080.15763941100
4.39-5.030.19732070.1533936100
5.03-6.330.20732100.18283988100
6.33-100.19032180.16024127100
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)
10.84180.5423-0.00821.7809-0.22781.0187-0.00630.15930.0708-0.3955-0.1839-0.30210.0780.1647-0.05580.35510.00790.03750.44050.1080.4085-27.443636.8864-4.0596
20.08010.19180.18790.47120.1171.3979-0.1485-0.04840.15110.1547-0.0694-0.5207-0.230.28980.0240.3098-0.0131-0.01010.53680.0910.555-20.180138.78934.4878
30.7333-0.21830.84191.6778-0.39970.7723-0.09740.07570.08550.1408-0.0374-0.1296-0.12580.0671-0.05460.3042-0.0332-0.03040.32220.05590.3632-35.601443.0212.8701
40.6084-0.20440.19471.7436-0.66581.58690.03090.29160.0213-0.2701-0.0860.13840.1993-0.1181-0.07240.3219-0.0156-0.00740.39870.05370.3232-41.682634.4231-7.5483
51.14640.2210.68270.581-0.35220.9670.0249-0.07970.2420.24440.21520.3253-0.171-0.2327-0.02220.45360.13710.08290.40860.1330.5318-75.336850.229420.1659
61.36340.60160.10634.6899-0.77852.0261-0.0750.1706-0.2715-0.72320.5470.30830.1873-0.4987-0.07450.40290.05620.10190.54550.22490.7645-84.400547.152819.1463
70.86330.00640.03751.2305-0.1261.269-0.07270.0718-0.17820.05260.08010.44390.0786-0.19280.0010.3061-0.0075-0.01760.39370.12990.4768-75.454236.35339.1914
80.5402-0.2255-0.44921.3311-0.18180.7853-0.0203-0.09470.09350.25620.10770.0399-0.05180.0995-0.00930.35580.0127-0.01910.34240.05260.3808-61.858848.222515.8488
90.81790.4032-0.03011.44350.45811.6403-0.09810.09730.0627-0.15690.1143-0.2358-0.22190.2066-0.03430.3176-0.0065-0.09360.48040.16210.4554-24.630414.842728.7548
101.0550.0345-0.56591.4293-0.1170.66590.1279-0.167-0.04110.0962-0.1881-0.227-0.05540.17250.00640.34370.0171-0.04570.51270.15430.4432-23.539614.825131.8345
112.270.4355-1.08442.50460.18850.86880.08020.2775-0.2472-0.61910.0414-0.89450.18850.52970.07650.41120.05870.04880.74860.15050.6536-16.106614.101325.0534
120.7242-0.17281.03420.9204-0.13891.5243-0.13440.2974-0.12250.0243-0.0936-0.12410.09470.41640.03460.32830.06390.02060.50220.15380.5448-22.454410.937217.5637
131.0780.34830.50871.7658-1.23911.7469-0.018-0.0334-0.2642-0.0892-0.0929-0.05080.12280.1629-0.05010.34410.0440.01190.37720.05830.4086-32.596813.870511.872
140.87970.60.02690.6326-0.39981.27590.0142-0.1213-0.1254-0.01650.01110.0860.0251-0.0393-0.06490.36490.0291-0.01240.37570.0880.4316-40.87226.921823.599
151.18660.0535-0.09111.6678-0.33290.78670.0492-0.5208-0.13550.30330.15150.2511-0.104-0.0522-0.08750.30880.05810.0010.56770.08730.3953-44.629113.495537.727
160.02190.1245-0.17051.3064-0.79070.81510.086-0.1010.0110.2431-0.1946-0.3285-0.45150.0053-0.01770.3709-0.0163-0.0590.43330.11180.3783-28.550827.86734.6262
170.33020.3924-0.09382.1778-0.79270.9613-0.0089-0.1352-0.10070.9565-0.020.0758-0.5734-0.0431-0.08460.5609-0.0195-0.00660.62760.03680.3773-35.934724.321743.7535
180.5131-0.53670.12470.8073-0.10080.73370.08330.0663-0.19020.0160.14020.47220.0575-0.065-0.0250.3506-0.0557-0.00310.45690.15330.5869-78.26938.937321.4745
191.001-0.54170.09611.9625-0.21881.8136-0.0540.08460.3730.59550.34380.2478-0.5292-0.3753-0.05690.4017-0.07310.06960.66510.19430.7875-86.083913.335225.0643
200.84220.94790.04461.12010.12481.2743-0.2435-0.11480.0013-0.07510.38380.3537-0.0523-0.2718-0.03330.3856-0.00190.09350.57810.19630.5433-80.058518.156131.7164
210.7038-0.2047-0.61160.9609-0.00890.8969-0.1154-0.249-0.16470.07690.09330.1746-0.2246-0.2965-0.06690.50490.07730.01930.50890.10230.4183-71.201926.532832.877
220.55580.59150.23281.2274-0.6631.41760.0499-0-0.20970.1775-0.03650.17450.22930.1334-0.13080.41910.04330.05880.44710.16080.4683-67.189721.847229.9523
230.9041-0.2440.54861.89060.47541.73840.0889-0.08550.12550.11270.03880.0598-0.1194-0.4536-0.03550.51830.02960.00120.48580.17340.4163-63.564220.120736.8091
240.59870.02250.58691.4705-0.10350.50360.0807-0.0845-0.16190.10790.09290.04180.03150.0592-0.01570.37250.00280.00760.37230.07640.4454-60.51858.149829.0524
250.8626-0.4209-0.25430.9305-0.69960.8829-0.0227-0.0495-0.10390.0738-0.0383-0.1185-0.14530.08770.03690.4058-0.0131-0.02220.35010.05070.5364-57.46621.695520.6319
260.32450.4281-0.10951.8317-0.38670.65540.03730.18490.0468-0.27120.17740.12120.1327-0.2143-0.01040.4424-0.0306-0.06740.40460.0620.5021-70.83698.51127.4671
270.78710.28870.43010.93060.27610.2617-0.02650.20030.05920.1185-0.02710.3308-0.0285-0.3802-0.00290.3912-0.0157-0.04510.60090.02730.417-29.5095-17.102139.2012
281.1474-0.0880.05071.6749-0.05621.7799-0.1198-0.3427-0.5830.3499-0.19470.26471.2458-0.6448-0.15680.4677-0.02350.0050.68810.10150.6182-37.1605-20.806243.617
291.05820.4645-0.35021.6221-0.74670.49860.01180.1372-0.1406-0.0662-0.01440.28170.4073-0.3711-0.04440.5118-0.07210.00110.4933-0.05780.4044-27.216-33.43245.4117
300.34130.18570.18251.31460.3391.40510.00160.53280.2809-0.1027-0.11920.26290.37-0.4071-0.01770.4784-0.1044-0.01520.5099-0.07240.3403-20.6222-33.558743.4426
310.59690.3409-0.54870.7927-0.05361.03770.00310.3347-0.0046-0.0771-0.1052-0.03940.3103-0.1970.0140.4703-0.045-0.03750.5135-0.03510.3425-16.1455-29.957832.4786
320.50640.137-0.35431.3110.26831.7073-0.11420.38120.1777-0.20810.2313-0.07620.29950.12340.03010.4586-0.0079-0.00530.630.05880.3847-11.0662-16.383627.2517
330.6137-0.3604-0.23330.5982-0.43961.97810.07870.17570.09470.0905-0.1297-0.0033-0.3465-0.08760.00650.38710.0271-0.0360.44420.03740.4325-18.3989-6.164742.6679
340.86770.21720.76841.45880.12150.8189-0.0008-0.24780.0633-0.0746-0.10140.22340.3658-0.11950.01910.5565-0.08140.03590.4229-0.02220.309-19.5599-33.833673.7524
351.22290.12220.19830.60720.00721.3102-0.1512-0.0562-0.16580.13670.00660.22270.1802-0.1274-0.020.6422-0.0540.11020.45840.01540.4134-20.3066-37.745174.8907
361.6721-0.00940.67151.68910.26631.80830.14420.27740.44210.1346-0.21930.3397-0.0282-0.4229-0.00990.5134-0.09810.12330.7288-0.02610.5309-29.0136-32.912374.0419
371.08060.0804-0.30111.2668-0.04250.9165-0.0132-0.02820.16160.01920.0170.25050.103-0.5754-0.02170.4302-0.00780.02640.3691-0.02870.3695-21.1058-20.218167.4997
381.0088-0.6109-0.14730.33260.0721.247-0.0319-0.19860.03930.1438-0.03910.04490.11170.02840.04290.4437-0.017-0.01430.4296-0.01270.3485-6.9965-21.84470.2778
391.19430.37110.30141.2981-0.66082.0249-0.1062-0.6441-0.14710.3374-0.2119-0.05360.3130.33110.04240.55240.0890.05380.53650.06530.39640.0382-36.834277.404
400.7985-0.23830.29691.1765-0.48931.6985-0.1411-0.0656-0.3459-0.14060.0934-0.11960.5978-0.1480.01590.7124-0.01550.05580.41050.05420.4811-12.6538-47.830465.8214
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 55 )A3 - 55
2X-RAY DIFFRACTION2chain 'A' and (resid 56 through 98 )A56 - 98
3X-RAY DIFFRACTION3chain 'A' and (resid 99 through 214 )A99 - 214
4X-RAY DIFFRACTION4chain 'A' and (resid 215 through 298 )A215 - 298
5X-RAY DIFFRACTION5chain 'B' and (resid 3 through 55 )B3 - 55
6X-RAY DIFFRACTION6chain 'B' and (resid 56 through 70 )B56 - 70
7X-RAY DIFFRACTION7chain 'B' and (resid 71 through 148 )B71 - 148
8X-RAY DIFFRACTION8chain 'B' and (resid 149 through 298 )B149 - 298
9X-RAY DIFFRACTION9chain 'C' and (resid 3 through 23 )C3 - 23
10X-RAY DIFFRACTION10chain 'C' and (resid 24 through 55 )C24 - 55
11X-RAY DIFFRACTION11chain 'C' and (resid 56 through 70 )C56 - 70
12X-RAY DIFFRACTION12chain 'C' and (resid 71 through 98 )C71 - 98
13X-RAY DIFFRACTION13chain 'C' and (resid 99 through 148 )C99 - 148
14X-RAY DIFFRACTION14chain 'C' and (resid 149 through 229 )C149 - 229
15X-RAY DIFFRACTION15chain 'C' and (resid 230 through 248 )C230 - 248
16X-RAY DIFFRACTION16chain 'C' and (resid 249 through 279 )C249 - 279
17X-RAY DIFFRACTION17chain 'C' and (resid 280 through 298 )C280 - 298
18X-RAY DIFFRACTION18chain 'D' and (resid 3 through 55 )D3 - 55
19X-RAY DIFFRACTION19chain 'D' and (resid 56 through 70 )D56 - 70
20X-RAY DIFFRACTION20chain 'D' and (resid 71 through 98 )D71 - 98
21X-RAY DIFFRACTION21chain 'D' and (resid 99 through 129 )D99 - 129
22X-RAY DIFFRACTION22chain 'D' and (resid 130 through 148 )D130 - 148
23X-RAY DIFFRACTION23chain 'D' and (resid 149 through 171 )D149 - 171
24X-RAY DIFFRACTION24chain 'D' and (resid 172 through 226 )D172 - 226
25X-RAY DIFFRACTION25chain 'D' and (resid 227 through 248 )D227 - 248
26X-RAY DIFFRACTION26chain 'D' and (resid 249 through 298 )D249 - 298
27X-RAY DIFFRACTION27chain 'E' and (resid 3 through 55 )E3 - 55
28X-RAY DIFFRACTION28chain 'E' and (resid 56 through 70 )E56 - 70
29X-RAY DIFFRACTION29chain 'E' and (resid 71 through 127 )E71 - 127
30X-RAY DIFFRACTION30chain 'E' and (resid 128 through 148 )E128 - 148
31X-RAY DIFFRACTION31chain 'E' and (resid 149 through 226 )E149 - 226
32X-RAY DIFFRACTION32chain 'E' and (resid 227 through 248 )E227 - 248
33X-RAY DIFFRACTION33chain 'E' and (resid 249 through 298 )E249 - 298
34X-RAY DIFFRACTION34chain 'F' and (resid 2 through 23 )F2 - 23
35X-RAY DIFFRACTION35chain 'F' and (resid 24 through 55 )F24 - 55
36X-RAY DIFFRACTION36chain 'F' and (resid 56 through 70 )F56 - 70
37X-RAY DIFFRACTION37chain 'F' and (resid 71 through 129 )F71 - 129
38X-RAY DIFFRACTION38chain 'F' and (resid 130 through 214 )F130 - 214
39X-RAY DIFFRACTION39chain 'F' and (resid 215 through 248 )F215 - 248
40X-RAY DIFFRACTION40chain 'F' and (resid 249 through 298 )F249 - 298

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