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

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Basic information

Entry
Database: PDB / ID: 7yxh
TitleDrosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and succinate
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 / metal ion binding ...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 / metal ion binding / nucleus / 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
: / SUCCINIC ACID / GH14974p
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 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)73,7738
Polymers73,3972
Non-polymers3766
Water2,234124
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4580 Å2
ΔGint-50 kcal/mol
Surface area26190 Å2
MethodPISA
Unit cell
Length a, b, c (Å)54.630, 65.334, 103.671
Angle α, β, γ (deg.)90.000, 101.730, 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: 36698.309 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 , 5 types, 130 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-SIN / SUCCINIC ACID / Succinic acid


Mass: 118.088 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H6O4 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 124 / 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: 2.59 Å3/Da / Density % sol: 52.46 %
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: I24 / Wavelength: 0.96863 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Aug 5, 2017 / Details: MIRRORS
RadiationMonochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.96863 Å / Relative weight: 1
ReflectionResolution: 2.3→101.506 Å / Num. obs: 31994 / % possible obs: 99.9 % / Redundancy: 5 % / Biso Wilson estimate: 45.3 Å2 / CC1/2: 0.996 / Rpim(I) all: 0.056 / Rrim(I) all: 0.127 / Rsym value: 0.114 / Net I/av σ(I): 5.1 / Net I/σ(I): 8.3
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allRsym value% possible all
2.3-2.425.10.746300.5270.5121.1741.052100
2.42-2.575.1144090.3750.8570.767100
2.57-2.7551.441360.2750.6230.557100
2.75-2.974.92.338560.1610.360.321100
2.97-3.255.13.935510.090.2040.182100
3.25-3.645.26.132220.0550.1280.115100
3.64-4.258.628330.0380.0860.07799.9
4.2-5.144.91024010.030.0680.06199.7
5.14-7.274.89.818890.0320.0720.06499.8
7.27-65.3344.510.210670.0260.0580.05299.6

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Processing

Software
NameVersionClassification
SCALA3.3.22data scaling
PHENIX1.14_3260refinement
PDB_EXTRACT3.27data extraction
HKL-2000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7YXG

7yxg


Resolution: 2.3→53.489 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 25.77 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2284 1640 5.13 %
Rwork0.1961 30332 -
obs0.1978 31972 99.9 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 200.75 Å2 / Biso mean: 65.5187 Å2 / Biso min: 25.75 Å2
Refinement stepCycle: final / Resolution: 2.3→53.489 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4868 0 35 124 5027
Biso mean--67.67 49.07 -
Num. residues----613
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0055020
X-RAY DIFFRACTIONf_angle_d0.7836850
X-RAY DIFFRACTIONf_dihedral_angle_d3.1752977
X-RAY DIFFRACTIONf_chiral_restr0.05741
X-RAY DIFFRACTIONf_plane_restr0.005893
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork
2.3-2.36770.33811320.28742525
2.3677-2.44410.32411000.28022521
2.4441-2.53150.28821470.25972499
2.5315-2.63280.28461540.2592502
2.6328-2.75260.29461430.24182518
2.7526-2.89770.2941280.23622515
2.8977-3.07930.27291270.22492534
3.0793-3.3170.25321490.19652500
3.317-3.65070.2541300.19952553
3.6507-4.17880.2121410.16772528
4.1788-5.26420.16071350.14212538
5.2642-53.4890.19371540.18842599
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)
10.0869-0.298-0.44470.41760.3730.0104-0.49160.37050.1375-0.15290.54721.06480.104-0.0760.00050.418-0.0469-0.04890.3939-0.01240.5423-29.4205-4.3304-18.4836
20.55250.3067-0.0860.1162-0.33860.56610.3280.80990.02830.73970.15810.4927-0.5165-0.9270.02230.51140.019-0.02810.3647-0.00190.4401-17.602214.0078-21.8215
30.5970.80590.18830.1065-0.09570.66760.2271-0.0376-0.12870.2982-0.19730.0034-0.3916-0.1825-0.00140.3834-0.0275-0.00460.3370.03360.3578-7.523913.8823-17.8003
40.53820.48510.16581.593-0.56630.5279-0.4756-0.06641.0533-0.7264-0.09240.3826-1.54690.3765-0.28871.0145-0.40520.09980.53860.26530.19021.316122.1528-35.1423
50.0794-0.056-0.06930.00520.0442-0.029-0.65830.5147-0.0121-1.1550.4763-1.1464-1.00762.15140.00011.1225-0.40460.1721.1763-0.03390.90858.436216.8163-49.2042
60.1761-0.0024-0.1540.6666-0.22220.15640.24220.6048-0.38480.0477-0.2615-0.07320.01550.04930.00040.9442-0.0990.05330.922-0.05290.5775-6.16082.505-49.1067
7-0.00380.02370.06760.1708-0.16930.0811-0.49130.76910.4861-0.68410.203-0.0922-0.4920.16170.00141.0066-0.1928-0.01670.8672-0.14630.4769-16.7059-8.0965-48.9617
81.6998-0.1444-0.39280.1463-0.44861.3414-0.89131.1074-1.7545-2.50490.838-0.52020.17381.13890.42291.4585-0.50690.61791.0719-0.1420.25540.47836.9461-53.7539
90.9733-0.93471.15380.64-0.70082.5462-0.03840.31340.0973-0.91870.25430.39890.6097-0.1494-0.49351.0028-0.11380.09250.833-0.04040.5138-2.93627.7185-48.6945
100.95490.196-0.46652.5075-0.39850.2463-0.27810.953-0.42750.82360.6469-0.686-0.87120.82120.190.418-0.31150.03880.8540.02760.44154.674914.1765-24.9592
110.53010.3311-0.40390.6579-0.01180.2231-0.37960.5173-0.7453-0.46370.2008-0.28430.77910.4178-0.00080.6551-0.02430.0890.81590.10420.61462.35286.5428-32.5353
120.10510.2330.32940.3323-0.14450.3069-0.20910.3368-0.25-0.5210.2201-0.01210.05870.0688-0.03040.7458-0.0421-0.04350.59990.00340.4371-11.57184.9169-40.6033
131.0425-0.44220.03340.35180.43820.6811-0.2570.3308-0.1183-0.61260.10970.0298-0.003-0.01870.00010.5452-0.0062-0.01710.45620.09430.4294-8.436711.3022-33.5482
140.90430.55760.04481.1626-0.51290.6349-0.6243-0.1047-0.2156-0.50380.71890.12530.09780.08230.87080.6804-0.31330.00470.4092-0.16610.3427-17.091-5.3526-37.5752
150.6865-0.03460.07560.16750.17620.14650.18140.5897-0.1338-1.2572-0.605-0.2860.14832.025201.6159-0.21090.29130.8642-0.07670.7007-8.5054-11.3472-53.7169
160.55660.4087-0.02160.29340.05380.134-0.27760.63060.1144-0.57560.25380.30260.7716-0.95890.03130.8945-0.1308-0.0980.7848-0.01460.4404-19.0288-3.1811-39.1717
171.3766-0.6606-0.11030.14990.25280.73510.01610.53550.0444-0.12130.12190.203-0.14-0.2947-0.00040.5611-0.0152-0.12420.6020.01580.4791-24.81975.5817-33.7188
180.72930.05770.76050.0480.23910.85550.06940.22150.0216-0.414-0.1859-0.23480.13430.07240.00030.4484-0.02990.06130.39190.04370.3763-8.93019.1791-27.2632
190.48010.25480.2320.1826-0.05450.2275-0.5440.0921-0.1285-0.74390.0850.02240.26430.1971-0.04780.6655-0.1208-0.10020.47330.04680.3472-11.380810.5788-40.6065
200.10970.22240.30420.1031-0.42560.06430.30930.4954-0.2136-0.4951-0.47770.47010.59940.6937-0.00050.61190.00190.06190.5846-0.01270.6655-0.2087.4705-31.8191
210.40010.00930.81310.1532-0.5350.56190.51930.75440.56130.3796-0.3151-0.47430.12760.2419-0.00060.462-0.0109-0.02720.48440.07490.5309-13.5816-7.5711-20.8509
220.1525-0.02170.2434-0.3255-0.09470.37270.33150.4628-0.8159-0.6335-0.0825-0.29580.3755-0.10530.00040.4486-0.0263-0.01320.3902-0.03230.5001-14.8745-16.6137-16.8848
23-0.11850.056-0.00640.14030.1254-0.0208-0.18240.3037-0.340.31870.4273-0.02240.61090.1933-0.00010.38770.0570.04270.50860.02340.4146-1.152-6.7005-4.4361
240.47710.09480.1544-0.0840.46141.0259-0.09690.0904-0.0167-0.09120.2113-0.097-0.35240.4606-0.00020.3726-0.0727-0.0010.4049-0.00660.3986-0.78783.7224-4.9827
250.8765-0.34550.75430.2832-0.23570.4235-0.2728-0.55980.0580.25010.3177-0.16450.00990.7224-0.00140.3714-0.05910.01560.4531-0.0250.47610.18537.191315.5769
260.21350.1466-0.10630.1443-0.06370.14220.9862-0.95460.08760.1041-0.5354-0.1096-0.72030.3426-0.00120.6946-0.07180.07130.6917-0.10180.6953-10.371110.102528.4148
270.27630.0815-0.1370.10240.33513.6507-0.10460.03170.22350.50120.20550.4750.6542-0.71320.15330.24240.04750.03290.3633-0.03970.389-21.8477-4.472319.8718
28-0.00440.1196-0.00490.1757-0.0483-0.11650.03140.25570.35160.17190.19720.35760.0395-0.1583-0.00020.3616-0.0177-0.02480.38450.05280.4385-30.2701-14.908213.1236
292.0671-0.7404-0.55151.22630.48370.3787-0.2628-0.37810.31660.3115-0.09840.55380.4422-0.0271-0.11780.4109-0.03650.00790.3735-0.04310.4454-19.85420.845727.8097
300.7101-0.135-1.03650.219-0.20330.7269-0.27820.02140.23480.16550.5331-0.63210.001-0.78070.00380.4797-0.00660.05820.45140.05630.5081-17.50821.60420.1267
310.05310.57520.08621.13250.46220.2514-0.1250.13380.07380.37750.0473-0.0938-0.5098-0.04570.00030.5699-0.0145-0.01550.4188-0.0220.4952-5.452813.5597.2324
320.0952-0.31770.38210.21310.05510.56850.1213-0.20350.0216-0.2896-0.0631-0.1249-0.5522-0.17890.0110.49290.02930.07640.3401-0.05730.3666-13.70479.16858.1653
33-0.0548-0.5144-0.02880.2578-0.15610.0828-0.06340.1088-0.27940.09480.01780.0314-0.20770.2434-0.00050.3593-0.030.01290.40640.03060.4239-16.288-6.75311.2232
340.7951-0.1528-0.40580.961-0.68590.5273-0.0432-0.1438-0.07710.12060.0466-0.0412-0.0719-0.0880.00010.34910.0018-0.02350.3481-0.01250.4216-8.4264-1.50967.9071
350.1173-0.58170.06241.2721-0.80370.282-0.02570.0545-0.0779-0.30730.01610.24260.2614-0.0123-0.00020.3259-0.0768-0.03250.3876-0.0110.4052-24.4737-11.35793.7688
360.91630.0548-0.52211.7991.48080.8071-0.3922-0.0647-0.03050.2622-0.10940.6939-1.1015-0.7539-0.00170.45540.03950.00440.4831-0.03640.5085-36.6335-9.516218.0037
370.0155-0.07950.04090.2183-0.2660.1308-0.0647-0.17580.0086-0.06090.027-0.09290.6791-0.2276-0.00010.4361-0.0601-0.0170.37950.02360.4268-22.7663-13.50925.2325
380.8283-0.8623-0.46990.72110.09741.30940.29730.0448-0.36710.0891-0.1033-0.2290.33260.0282-0.00060.37780.0215-0.02230.3169-0.00860.452-12.2413-17.21691.6355
390.45650.6652-0.54340.7185-0.54950.4731-0.12610.01990.5048-0.19130.1294-0.00840.1156-0.00290.00020.3837-0.01960.02350.3561-0.05280.4295-8.3151-0.15291.4869
400.00210.35490.06810.077-0.04160.055-0.0581-0.071-0.15040.1515-0.1306-0.03110.3573-0.40420.00030.29680.0084-0.00230.3610.01450.3608-11.091-6.436413.3542
41-0.10280.03840.1009-0.0007-0.03330.07840.1423-0.43480.4131-0.1433-0.1529-0.23220.2759-0.4399-0.00020.429-0.05510.08370.40970.00010.3955-12.15896.72467.3004
420.4438-0.32680.49930.5212-0.64360.1224-0.10020.0567-0.0772-0.16760.2650.0293-0.18240.1595-0.00010.32380.0263-0.0240.4124-0.00120.4168-21.82-3.0448-11.2239
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 115:129)B115 - 129
31X-RAY DIFFRACTION31(chain B and resid 139:154)B139 - 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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