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- PDB-7yxl: Drosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and N-... -

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Basic information

Entry
Database: PDB / ID: 7yxl
TitleDrosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and N-oxalyl-D-phenylalanine (NOFD)
ComponentsGH14974p
KeywordsOXIDOREDUCTASE / NON-HEME / IRON / 2-OXOGLUTARATE / DIOXYGENASE / OXYGENASE / JMJC / JMJC DOMAIN / JMJC DOMAIN-CONTAINING PROTEIN 7 / JMJD7 / JMJC HYDROXYLASE / JMJC DEMETHYLASE / KDMS / POST-TRANSLATIONAL MODIFICATIONS / PTM / HYDROXYLATION / LYSYL HYDROXYLATION / DIMERISATION / TRANSLATION FACTOR / DEVELOPMENTALLY REGULATED GTP BINDING PROTEINS / DRG1 / DRG2 / TRAFAC GTPASE / HYPOXIA / NUCLEIC ACID- BINDING / METAL-BINDING / TRANSLATION / HELIX-LOOP-HELIX-BETA / DSBH / FACIAL TRIAD / DEVELOPMENT / CANCER / RIBOSOME BIOGENESIS
Function / homology
Function and homology information


peptidyl-lysine 3-dioxygenase activity / Protein hydroxylation / wybutosine biosynthetic process / Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor / histone H3K36 demethylase activity / 2-oxoglutarate-dependent dioxygenase activity / phospholipase A2 / tRNA binding / hydrolase activity / nucleus ...peptidyl-lysine 3-dioxygenase activity / Protein hydroxylation / wybutosine biosynthetic process / Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor / histone H3K36 demethylase activity / 2-oxoglutarate-dependent dioxygenase activity / phospholipase A2 / tRNA binding / hydrolase activity / nucleus / metal ion binding / cytoplasm
Similarity search - Function
Cupin-like domain 8 / Cupin-like domain / A domain family that is part of the cupin metalloenzyme superfamily. / JmjC domain / JmjC domain profile. / RmlC-like jelly roll fold
Similarity search - Domain/homology
ACETATE ION / : / N-(CARBOXYCARBONYL)-D-PHENYLALANINE / GH14974p
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsChowdhury, R. / Schofield, C.J.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Wellcome Trust106244/Z/14/Z United Kingdom
Citation
Journal: Sci Rep / Year: 2022
Title: Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans.
Authors: Chowdhury, R. / Abboud, M.I. / Wiley, J. / Tumber, A. / Markolovic, S. / Schofield, C.J.
#1: Journal: Nat Chem Biol / Year: 2018
Title: The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases.
Authors: Markolovic, S. / Zhuang, Q. / Wilkins, S.E. / Eaton, C.D. / Abboud, M.I. / Katz, M.J. / McNeil, H.E. / Lesniak, R.K. / Hall, C. / Struwe, W.B. / Konietzny, R. / Davis, S. / Yang, M. / Ge, W. ...Authors: Markolovic, S. / Zhuang, Q. / Wilkins, S.E. / Eaton, C.D. / Abboud, M.I. / Katz, M.J. / McNeil, H.E. / Lesniak, R.K. / Hall, C. / Struwe, W.B. / Konietzny, R. / Davis, S. / Yang, M. / Ge, W. / Benesch, J.L.P. / Kessler, B.M. / Ratcliffe, P.J. / Cockman, M.E. / Fischer, R. / Wappner, P. / Chowdhury, R. / Coleman, M.L. / Schofield, C.J.
History
DepositionFeb 16, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 27, 2022Provider: repository / Type: Initial release
Revision 1.1May 4, 2022Group: Refinement description / Category: refine_ls_restr
Revision 1.2Jan 31, 2024Group: 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
A: GH14974p
B: GH14974p
hetero molecules


Theoretical massNumber of molelcules
Total (without water)74,61417
Polymers73,4292
Non-polymers1,18515
Water4,846269
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6050 Å2
ΔGint-41 kcal/mol
Surface area25890 Å2
MethodPISA
Unit cell
Length a, b, c (Å)55.020, 65.160, 99.220
Angle α, β, γ (deg.)90.000, 100.770, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein GH14974p / Jumonji domain containing 7


Mass: 36714.309 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: JMJD7, Dmel\CG10133, CG10133, Dmel_CG10133 / Plasmid: PET28A(+) / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: Q9VU77, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor

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Non-polymers , 6 types, 284 molecules

#2: Chemical ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mn
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-NDF / N-(CARBOXYCARBONYL)-D-PHENYLALANINE


Type: D-peptide linking / Mass: 237.209 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C11H11NO5 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C2H6O2
#6: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 269 / 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: 2.5 Å3/Da / Density % sol: 50.87 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5.4
Details: Sample: 16.0 mg/ml dmJMJD7 (in 50 mM Hepes-Na pH 7.5, 200 mM NaCl, 5% glycerol), 2.0 mM MnCl2 and 4.0 mM compound. Reservoir: 0.1 M Bis-Tris pH 5.4, 0.3 M magnesium chloride, 0.1 M ammonium ...Details: Sample: 16.0 mg/ml dmJMJD7 (in 50 mM Hepes-Na pH 7.5, 200 mM NaCl, 5% glycerol), 2.0 mM MnCl2 and 4.0 mM compound. Reservoir: 0.1 M Bis-Tris pH 5.4, 0.3 M magnesium chloride, 0.1 M ammonium acetate (or alternatively, 0.1 M barium chloride), and 0.002 M manganese chloride. Cryo-protection: 20% v/v ethylene glycol.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.97951 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Oct 3, 2017 / Details: MIRRORS
RadiationMonochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97951 Å / Relative weight: 1
ReflectionResolution: 2.2→40.42 Å / Num. obs: 35134 / % possible obs: 99.8 % / Redundancy: 5.1 % / Biso Wilson estimate: 34.9 Å2 / CC1/2: 0.995 / Rpim(I) all: 0.067 / Rrim(I) all: 0.154 / Rsym value: 0.138 / Net I/σ(I): 9.9
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Num. unique obsCC1/2Rpim(I) allRrim(I) allRsym value% possible all
2.2-2.265.225520.5590.5821.3641.22999.7
9.84-40.424.54110.9980.0140.0320.02896.5

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Processing

Software
NameVersionClassification
Aimless0.5.32data scaling
PHENIX1.14_3260refinement
PDB_EXTRACT3.27data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7YXG

7yxg


Resolution: 2.2→40.418 Å / SU ML: 0.3 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 25.35 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2298 1758 5.01 %
Rwork0.1885 33354 -
obs0.1906 35112 99.74 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 205 Å2 / Biso mean: 53.3569 Å2 / Biso min: 16.52 Å2
Refinement stepCycle: final / Resolution: 2.2→40.418 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4834 0 140 269 5243
Biso mean--68.45 41.76 -
Num. residues----612
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0035073
X-RAY DIFFRACTIONf_angle_d0.6546920
X-RAY DIFFRACTIONf_dihedral_angle_d15.1142985
X-RAY DIFFRACTIONf_chiral_restr0.046745
X-RAY DIFFRACTIONf_plane_restr0.004907
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.2-2.25950.33811250.28662523100
2.2595-2.3260.30591480.26592555100
2.326-2.40110.28631310.26362550100
2.4011-2.48690.28671260.24312571100
2.4869-2.58640.30581390.23952528100
2.5864-2.70410.28281380.23152553100
2.7041-2.84670.27961420.21172570100
2.8467-3.0250.23221350.22550100
3.025-3.25840.25121220.18992586100
3.2584-3.58610.23431310.17092573100
3.5861-4.10460.18491310.15522577100
4.1046-5.16970.17021500.12912567100
5.1697-40.4180.21611400.1934265199
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)
14.83524.6599-2.97036.7585-1.78016.76350.00530.3033-1.7095-0.5828-0.10860.52210.8722-0.09880.09380.5417-0.0154-0.12610.2963-0.07830.6077-9.4853-1.406727.17
24.08263.6411-0.76686.1634-1.76853.21640.36470.3854-0.80530.1885-0.0493-0.17760.3450.0991-0.09330.3788-0.00560.08610.3343-0.06440.36779.70397.666529.8785
31.8216-0.18081.89171.6985-0.45261.9055-0.24490.36560.1469-0.19890.16930.06070.19520.08830.10480.32170.00590.05880.32460.01170.320510.123418.375829.5572
41.15551.32622.02741.66322.51143.6923-0.23950.22050.15540.01270.1738-0.0184-0.14980.4827-0.18640.2876-0.0109-0.00120.28610.04010.362522.975520.242445.7564
53.4595-0.0154-4.12511.08131.92398.29420.0384-1.2325-0.1240.122-0.45480.7381-1.1050.78970.12180.5327-0.1371-0.03650.5026-0.02720.432121.706322.917162.7365
62.86031.22340.78742.97130.68242.02990.1394-0.19770.29370.4381-0.2374-0.35210.1727-0.0705-0.06220.29560.02120.00250.25790.03550.41326.57759.758561.7947
73.30960.4837-0.9983.2765-1.60533.99360.4673-0.1676-0.17410.1382-0.27720.2539-0.5057-0.0912-0.21220.318-0.01090.03020.24920.01690.3432-4.90460.298960.8851
82.94211.52070.14781.81390.7750.76740.1116-0.61760.40850.7498-0.05360.05590.36650.1476-0.06580.5577-0.0908-0.03910.3411-0.0030.378312.645714.02567.0868
93.60430.5802-1.1973.692-0.45823.7640.064-0.2051-0.15370.20470.0583-0.38840.2074-0.1794-0.18350.30750.0032-0.02870.32250.0040.35712.088612.620961.3268
104.39120.15732.76480.7797-0.39442.143-0.51330.28070.95210.2448-0.0243-0.1831-0.63460.3590.50460.3774-0.0365-0.0560.2318-0.03510.430214.583828.022642.713
114.3033-2.80513.45142.9189-3.17797.274-0.3971-0.1067-0.42510.47350.38730.5053-0.9769-0.44360.05990.38010.0147-0.04230.2869-0.04840.37817.285722.960248.2275
122.05480.1094-0.28992.6465-0.04642.2515-0.1936-0.0047-0.51190.170.164-0.016-0.08610.04580.04070.2902-0.0320.02060.23510.03750.316.07967.529651.4156
131.53250.21850.50341.6848-0.15752.06060.07410.0997-0.15580.24530.0478-0.1334-0.07260.0987-0.04890.26240.02310.02140.21250.00520.290810.902712.587344.3588
140.3277-0.2013-0.76070.9385-0.61672.73740.0888-0.02120.06510.0245-0.02390.1266-0.3063-0.3691-0.05120.2735-0.044-0.00160.31280.060.352-5.08243.620449.432
153.2873-0.4666-0.4263.2531-0.04343.66510.242-0.4552-0.30750.23550.01080.5265-0.5812-0.9514-0.12710.43860.06780.06430.4852-0.02330.3349-7.16426.898568.8908
162.968-0.4795-0.49582.45290.08211.64550.0423-0.1811-0.3646-0.13910.05910.32620.0704-0.2959-0.14720.3243-0.0378-0.03190.33670.04850.4289-3.00771.334649.9647
172.46280.7621-0.19472.61160.21120.95640.1611-0.0182-0.44450.1243-0.123-0.51030.2144-0.0151-0.01790.3037-0.03730.0420.2381-0.02430.34483.5005-2.702140.9004
181.97340.75320.32241.31460.01350.0841-0.42170.17530.3004-0.03940.2725-0.00660.01340.08360.02920.2404-0.03450.0130.2679-0.00970.27947.441814.23938.996
191.2354-0.6048-0.66541.5365-0.34660.7118-0.237-0.2972-0.14720.13010.194-0.4559-0.3129-0.1010.04080.22280.01440.02870.20780.03680.280711.53377.437850.129
202.0946-1.95393.1543.6867-2.60794.77020.1287-0.1176-0.01640.111-0.19020.06850.0011-0.05080.22440.33150.01960.03190.25920.01470.34827.808320.842646.2802
213.0871.1290.69326.5315-1.23442.68160.28540.2397-0.10140.11980.11050.15490.23480.1488-0.32630.31240.0366-0.00050.3648-0.02520.3001-10.426212.597535.6184
225.5323.6086-0.18442.4560.18133.83160.0057-0.3176-0.13660.15830.11620.88380.2933-0.6641-0.1040.3082-0.00160.00440.45440.05760.4404-21.035111.637234.2304
235.29650.11390.011.95571.72221.695-0.46660.05170.2882-0.06350.16810.2632-0.3506-0.2529-0.02930.21020.0798-0.02880.3026-0.00780.272-12.550129.868225.5568
243.8044-0.94191.40540.93630.6143.0196-0.09360.23460.3840.2628-0.1082-0.0522-0.26270.16080.14830.29590.0244-0.02970.2970.04990.3384-1.839729.54823.1642
251.27920.9907-1.00460.8691-0.62811.1094-0.70340.67110.5659-0.5199-0.0620.0414-0.56410.75340.0980.6617-0.178-0.03690.77130.24310.4316-3.146738.32564.5421
265.04380.5598-0.76161.9232-1.41921.4231-0.57260.50640.5228-0.2386-0.8526-0.87740.03871.20760.65660.9004-0.2051-0.05041.13850.33490.5618-5.421533.3111-11.7935
272.99120.52780.71394.03-1.15343.94180.05010.0122-0.3869-0.63750.18170.06310.21050.3567-0.48060.8023-0.2174-0.15320.85050.08670.428-18.489119.6947-4.2202
283.862.22752.31042.6430.93773.21470.34860.1936-0.287-0.8382-0.07150.41560.5543-0.4291-0.05130.7667-0.0837-0.21940.6748-0.11130.5904-27.50379.28011.4332
291.1315-0.0328-0.95580.9514-0.11250.8147-0.23750.9582-0.0602-1.8695-0.4026-0.00150.19130.08690.18121.1084-0.30670.19211.22550.12670.0372-15.392924.4984-11.6731
301.99181.0699-0.28833.02070.4412.9430.18060.1989-0.0691-0.12250.27310.32780.6519-0.4419-0.30750.6956-0.1527-0.00210.95220.02360.3435-16.362725.0336-5.6952
310.0906-0.2597-0.12511.5569-1.18385.0247-0.17490.56060.3330.18250.0665-0.0398-0.84130.70440.14890.4657-0.1760.02040.88030.12630.42424.511229.98048.5935
322.5195-0.71812.92052.41620.02723.76090.17250.9131-0.7479-0.4317-0.22620.05390.5780.99690.42310.47830.03440.11040.70040.12460.2763-1.830922.32165.4142
332.51270.6719-0.29611.36470.75232.4351-0.28450.1120.0644-0.14840.43880.3532-0.0439-0.509-0.0750.497-0.0812-0.11110.54880.00040.352-17.902221.64716.1874
341.80670.7783-0.55940.5487-0.94332.15780.00510.39410.1009-0.3887-0.06940.08630.03590.0450.19270.48150.007-0.03950.37930.04180.2841-11.023727.438510.5079
351.0342-0.2412-0.02620.86970.05440.6236-0.0550.338-0.3834-0.39760.142-0.01460.25960.0022-0.10280.5465-0.1439-0.06590.4817-0.02670.3641-21.501811.518111.3086
364.78571.2845-0.90381.8649-1.15292.365-0.79651.6417-0.2972-1.17250.386-0.29681.04340.6001-0.52561.3094-0.1815-0.05340.9088-0.29270.481-23.14255.8637-7.1822
375.1127-1.5013-1.03766.84041.91124.8467-0.428-0.15390.0177-0.3830.6697-0.06720.041-0.081-0.02680.4497-0.1004-0.10580.50790.02140.3788-23.803813.586111.0519
382.73090.5258-0.03482.1038-0.52252.2119-0.2310.11930.2763-0.14860.30250.6084-0.1586-0.7486-0.06940.29880.04-0.00660.48930.02170.31-25.228922.135419.0484
391.3936-0.14970.3262.0406-1.79431.5616-0.02310.39440.0086-0.2322-0.0694-0.1352-0.21840.03310.08410.4218-0.0043-0.01710.35820.04170.3249-8.250425.15915.9917
401.78980.37560.09341.44321.05510.7788-0.26660.5350.5219-0.1348-0.125-0.0586-0.31070.30420.25070.406-0.025-0.1230.40810.09220.4515-17.494627.216.1333
414.5949-3.25113.53313.3417-3.12323.08710.55360.3774-0.1298-0.8915-0.2251-0.01230.5740.5602-0.12390.4749-0.05560.0660.6763-0.07380.2885-3.617723.33067.4653
426.8731.2144-0.91793.1491-1.3123.53820.03160.43-0.5842-0.39810.1241-0.0823-0.0717-0.1205-0.11160.4590.04530.02380.2946-0.01040.2851-9.26988.296923.4544
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 1:18)A1 - 18
2X-RAY DIFFRACTION2(chain A and resid 19:27)A19 - 27
3X-RAY DIFFRACTION3(chain A and resid 28:49)A28 - 49
4X-RAY DIFFRACTION4(chain A and resid 50:62)A50 - 62
5X-RAY DIFFRACTION5(chain A and resid 63:73)A63 - 73
6X-RAY DIFFRACTION6(chain A and resid 74:86)A74 - 86
7X-RAY DIFFRACTION7(chain A and resid 87:99)A87 - 99
8X-RAY DIFFRACTION8(chain A and resid 100:114)A100 - 114
9X-RAY DIFFRACTION9(chain A and resid 115:135)A115 - 135
10X-RAY DIFFRACTION10(chain A and resid 136:154)A136 - 154
11X-RAY DIFFRACTION11(chain A and resid 155:165)A155 - 165
12X-RAY DIFFRACTION12(chain A and resid 166:178)A166 - 178
13X-RAY DIFFRACTION13(chain A and resid 179:195)A179 - 195
14X-RAY DIFFRACTION14(chain A and resid 196:215)A196 - 215
15X-RAY DIFFRACTION15(chain A and resid 216:234)A216 - 234
16X-RAY DIFFRACTION16(chain A and resid 235:245)A235 - 245
17X-RAY DIFFRACTION17(chain A and resid 246:265)A246 - 265
18X-RAY DIFFRACTION18(chain A and resid 266:276)A266 - 276
19X-RAY DIFFRACTION19(chain A and resid 277:286)A277 - 286
20X-RAY DIFFRACTION20(chain A and resid 287:294)A287 - 294
21X-RAY DIFFRACTION21(chain A and resid 295:312)A295 - 312
22X-RAY DIFFRACTION22(chain B and resid 1:18)B1 - 18
23X-RAY DIFFRACTION23(chain B and resid 19:27)B19 - 27
24X-RAY DIFFRACTION24(chain B and resid 28:49)B28 - 49
25X-RAY DIFFRACTION25(chain B and resid 50:62)B50 - 62
26X-RAY DIFFRACTION26(chain B and resid 63:73)B63 - 73
27X-RAY DIFFRACTION27(chain B and resid 74:86)B74 - 86
28X-RAY DIFFRACTION28(chain B and resid 87:99)B87 - 99
29X-RAY DIFFRACTION29(chain B and resid 100:114)B100 - 114
30X-RAY DIFFRACTION30(chain B and resid 115:128)B115 - 128
31X-RAY DIFFRACTION31(chain B and resid 136:154)B136 - 154
32X-RAY DIFFRACTION32(chain B and resid 155:165)B155 - 165
33X-RAY DIFFRACTION33(chain B and resid 166:178)B166 - 178
34X-RAY DIFFRACTION34(chain B and resid 179:195)B179 - 195
35X-RAY DIFFRACTION35(chain B and resid 196:215)B196 - 215
36X-RAY DIFFRACTION36(chain B and resid 216:234)B216 - 234
37X-RAY DIFFRACTION37(chain B and resid 235:245)B235 - 245
38X-RAY DIFFRACTION38(chain B and resid 246:265)B246 - 265
39X-RAY DIFFRACTION39(chain B and resid 266:276)B266 - 276
40X-RAY DIFFRACTION40(chain B and resid 277:286)B277 - 286
41X-RAY DIFFRACTION41(chain B and resid 287:294)B287 - 294
42X-RAY DIFFRACTION42(chain B and resid 295:312)B295 - 312

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