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- PDB-7dkb: Stenotrophomonas maltophilia DPP7 in complex with Val-Tyr -

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Basic information

Entry
Database: PDB / ID: 7dkb
TitleStenotrophomonas maltophilia DPP7 in complex with Val-Tyr
ComponentsDipeptidyl-peptidase
KeywordsHYDROLASE / dipeptidyl aminopeptidase / S46 / AMR / Microgravity / antimicrobial / chymotrypsin / serine protease
Function / homology
Function and homology information


Hydrolases; Acting on peptide bonds (peptidases); Dipeptidyl-peptidases and tripeptidyl-peptidases / serine-type aminopeptidase activity / dipeptidyl-peptidase activity / peptide catabolic process / proteolysis
Similarity search - Function
Peptidase S46 / Peptidase S46 / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan
Similarity search - Domain/homology
TYROSINE / VALINE / Dipeptidyl-peptidase
Similarity search - Component
Biological speciesStenotrophomonas maltophilia (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.03 Å
AuthorsSakamoto, Y. / Nakamura, A. / Suzuki, Y. / Honma, N. / Roppongi, S. / Kushibiki, C. / Yonezawa, N. / Takahashi, M. / Shida, Y. / Gouda, H. ...Sakamoto, Y. / Nakamura, A. / Suzuki, Y. / Honma, N. / Roppongi, S. / Kushibiki, C. / Yonezawa, N. / Takahashi, M. / Shida, Y. / Gouda, H. / Nonaka, T. / Ogasawara, W. / Tanaka, N.
Funding support Japan, 9items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)16K8322 Japan
Japan Society for the Promotion of Science (JSPS)16H04902 Japan
Japan Society for the Promotion of Science (JSPS)17H03790 Japan
Ministry of Education, Culture, Sports, Science and Technology (Japan)H29-A3 Japan
TAKEDA Foundation Japan
Ministry of Education, Culture, Sports, Science and Technology (Japan)2013A6822, 2013B6822, 2014A6924, 2014B6924, 2015A6521, 2015B6521, 2016B6620, 2017A6721, 2017B6721, 2018A6818, 2018B6818, 2019A6917, 2019B6917, 2020A6517 Japan
Ministry of Education, Culture, Sports, Science and Technology (Japan)CR1405-CR1905 Japan
Japan Agency for Medical Research and Development (AMED)BINDS 0026 Japan
Ministry of Education, Culture, Sports, Science and Technology (Japan)2017G162 KEK Japan
CitationJournal: Sci Rep / Year: 2021
Title: Structural basis for an exceptionally strong preference for asparagine residue at the S2 subsite of Stenotrophomonas maltophilia dipeptidyl peptidase 7.
Authors: Nakamura, A. / Suzuki, Y. / Sakamoto, Y. / Roppongi, S. / Kushibiki, C. / Yonezawa, N. / Takahashi, M. / Shida, Y. / Gouda, H. / Nonaka, T. / Tanaka, N. / Ogasawara, W.
History
DepositionNov 23, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 3, 2021Provider: repository / Type: Initial release
Revision 1.1Nov 29, 2023Group: Data collection / Derived calculations / Refinement description
Category: atom_type / chem_comp_atom ...atom_type / chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Item: _atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Dipeptidyl-peptidase
B: Dipeptidyl-peptidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)156,7206
Polymers156,1232
Non-polymers5974
Water8,305461
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: light scattering
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1190 Å2
ΔGint-7 kcal/mol
Surface area54300 Å2
Unit cell
Length a, b, c (Å)66.490, 73.330, 151.820
Angle α, β, γ (deg.)90.000, 95.160, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Dipeptidyl-peptidase


Mass: 78061.461 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Stenotrophomonas maltophilia (strain R551-3) (bacteria)
Strain: R551-3 / Gene: Smal_0807 / Plasmid: pET22b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Gold(DE3)
References: UniProt: B4SLK2, Hydrolases; Acting on peptide bonds (peptidases); Dipeptidyl-peptidases and tripeptidyl-peptidases
#2: Chemical ChemComp-VAL / VALINE / Valine


Type: L-peptide linking / Mass: 117.146 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C5H11NO2
#3: Chemical ChemComp-TYR / TYROSINE / Tyrosine


Type: L-peptide linking / Mass: 181.189 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H11NO3
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 461 / 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: 2.43 Å3/Da / Density % sol: 49.48 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 / Details: 0.2M Amm Acetate, 20%w/v PEG 8000

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Data collection

DiffractionMean temperature: 95 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å
DetectorType: RAYONIX MX300HE / Detector: CCD / Date: Oct 2, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 1.94→45.75 Å / Num. obs: 100498 / % possible obs: 93.7 % / Redundancy: 7.6 % / Biso Wilson estimate: 18.556 Å2 / CC1/2: 0.397 / Rmerge(I) obs: 0.256 / Rpim(I) all: 0.1 / Rrim(I) all: 0.275 / Net I/σ(I): 7.9
Reflection shellResolution: 1.94→1.97 Å / Redundancy: 7.5 % / Rmerge(I) obs: 1.487 / Mean I/σ(I) obs: 1.4 / Num. unique obs: 3191 / CC1/2: 0.397 / Rpim(I) all: 0.576 / % possible all: 60.1

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
xia20.5.161data reduction
XDSdata scaling
PHASER2.6phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3WOL

3wol


Resolution: 2.03→40 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.913 / SU B: 5.408 / SU ML: 0.142 / Cross valid method: FREE R-VALUE / ESU R: 0.213 / ESU R Free: 0.182
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.2454 4522 4.918 %
Rwork0.2009 87429 -
all0.203 --
obs-91951 97.619 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 29.45 Å2
Baniso -1Baniso -2Baniso -3
1-0.867 Å2-0 Å20.443 Å2
2--0.819 Å20 Å2
3----1.738 Å2
Refinement stepCycle: LAST / Resolution: 2.03→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10658 0 40 461 11159
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.01310928
X-RAY DIFFRACTIONr_bond_other_d0.0010.01710392
X-RAY DIFFRACTIONr_angle_refined_deg1.5761.64114812
X-RAY DIFFRACTIONr_angle_other_deg1.3661.58523884
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.90451394
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.2822.924554
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.906151788
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.1561562
X-RAY DIFFRACTIONr_chiral_restr0.0730.21378
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0212662
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022542
X-RAY DIFFRACTIONr_nbd_refined0.2110.22709
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1790.210612
X-RAY DIFFRACTIONr_nbtor_refined0.1730.25450
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0830.25593
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1580.2624
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.0750.28
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.2330.227
X-RAY DIFFRACTIONr_nbd_other0.1960.289
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.270.216
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.10.21
X-RAY DIFFRACTIONr_mcbond_it2.2142.9095588
X-RAY DIFFRACTIONr_mcbond_other2.2142.9095587
X-RAY DIFFRACTIONr_mcangle_it3.2154.3646978
X-RAY DIFFRACTIONr_mcangle_other3.2154.3646979
X-RAY DIFFRACTIONr_scbond_it2.8913.2345340
X-RAY DIFFRACTIONr_scbond_other2.8913.2345340
X-RAY DIFFRACTIONr_scangle_it4.4854.6947834
X-RAY DIFFRACTIONr_scangle_other4.4854.6947834
X-RAY DIFFRACTIONr_lrange_it5.80135.21112887
X-RAY DIFFRACTIONr_lrange_other5.78335.15712822
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc freeFsc work% reflection obs (%)WRfactor Rwork
2.03-2.0830.3663020.31857720.3269150.7270.77487.8380.295
2.083-2.140.3272980.28362840.28567470.8140.8397.55450.259
2.14-2.2010.3333030.26860800.27165320.8170.8497.71890.244
2.201-2.2690.2942970.24859150.2563410.8560.8797.96560.227
2.269-2.3430.2813390.23257240.23561910.8820.89297.93250.216
2.343-2.4250.2823030.2255540.22359720.8910.90898.07430.206
2.425-2.5160.2772500.2154380.21357920.90.91398.20440.2
2.516-2.6180.2552740.19751900.19955580.9090.9398.30870.188
2.618-2.7340.2292430.18449860.18653150.930.94198.38190.177
2.734-2.8670.2582770.1947590.19451100.9120.93298.55190.186
2.867-3.0210.2362320.19345540.19548740.920.93198.19450.189
3.021-3.2040.2212460.18643100.18846050.9310.9498.93590.187
3.204-3.4230.2261950.17940900.18243190.9330.94299.21280.187
3.423-3.6950.2131940.17537960.17740460.940.94998.61590.187
3.695-4.0440.2131790.17635060.17737060.940.95199.43330.194
4.044-4.5160.2021720.16231990.16434050.9570.96399.00150.185
4.516-5.2040.2121450.1728360.17230050.9590.96699.20130.195
5.204-6.3460.2491330.2123950.21225410.9460.9599.48840.237
6.346-8.8640.195860.18719180.18820170.960.96299.35550.211
8.864-40.0030.248540.22811230.22811870.9620.96599.15750.265

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