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- PDB-2q4x: Ensemble refinement of the protein crystal structure of gene prod... -

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Basic information

Entry
Database: PDB / ID: 2q4x
TitleEnsemble refinement of the protein crystal structure of gene product from Arabidopsis thaliana At3g16990
ComponentsSeed maturation protein PM36 homolog
KeywordsPLANT PROTEIN / Ensemble Refinement / Refinement Methodology Development / TENA_THI-4 DOMAIN / TENA/THI-4/PQQC FAMILY / AT3G16990 / Structural Genomics / Protein Structure Initiative / PSI / Center for Eukaryotic Structural Genomics / CESG
Function / homology
Function and homology information


aminopyrimidine aminohydrolase / thiaminase activity / thiamine diphosphate biosynthetic process / thiamine biosynthetic process / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides
Similarity search - Function
TenA_E protein / Thiaminase-2/PQQC / TENA/THI-4/PQQC family / Heme oxygenase-like / Heme Oxygenase; Chain A / Haem oxygenase-like, multi-helical / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE / Bifunctional TENA-E protein
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / Re-refinement using ensemble model / Resolution: 2.1 Å
AuthorsLevin, E.J. / Kondrashov, D.A. / Wesenberg, G.E. / Phillips Jr., G.N. / Center for Eukaryotic Structural Genomics (CESG)
Citation
Journal: Structure / Year: 2007
Title: Ensemble refinement of protein crystal structures: validation and application.
Authors: Levin, E.J. / Kondrashov, D.A. / Wesenberg, G.E. / Phillips, G.N.
#1: Journal: Proteins / Year: 2004
Title: Crystal structure of gene locus At3g16990 from Arabidopsis thaliana
Authors: Blommel, P.G. / Smith, D.W. / Bingman, C.A. / Dyer, D.H. / Rayment, I. / Holden, H.M. / Fox, B.G. / Phillips Jr., G.N.
History
DepositionMay 31, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 19, 2007Provider: repository / Type: Initial release
Revision 1.1Sep 25, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Aug 10, 2011Group: Other
Revision 1.4Oct 20, 2021Group: Database references / Derived calculations
Category: database_2 / struct_conn ...database_2 / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Aug 30, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.6Nov 15, 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: Seed maturation protein PM36 homolog
B: Seed maturation protein PM36 homolog
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,3288
Polymers50,6652
Non-polymers6636
Water7,692427
1
A: Seed maturation protein PM36 homolog
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,5683
Polymers25,3331
Non-polymers2352
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Seed maturation protein PM36 homolog
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,7605
Polymers25,3331
Non-polymers4274
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)62.700, 62.700, 287.621
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number92
Space group name H-MP41212
Number of models8

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Components

#1: Protein Seed maturation protein PM36 homolog


Mass: 25332.719 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Strain: cv. Columbia / Gene: At3g16990, K14A17_11, K14A17.22 / Plasmid: PVP13 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta / References: UniProt: Q9ASY9
#2: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#3: Chemical ChemComp-HMH / 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE / 4-Amino-5-hydroxymethyl-2-methylpyrimidine


Mass: 139.155 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H9N3O
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 427 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.78 Å3/Da / Density % sol: 55.5 % / Description: AUTHOR USED THE SF DATA FROM ENTRY 2F2G.

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Data collection

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1

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Processing

Software
NameVersionClassificationNB
CNS1.1refinement
PDB_EXTRACT2data extraction
CNS1.1phasing
RefinementMethod to determine structure: Re-refinement using ensemble model
Starting model: PDB entry 2F2G

2f2g


Resolution: 2.1→28.04 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 2683790.75 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
Stereochemistry target values: maximum likelihood using amplitudes
Details: This PDB entry is a re-refinement using an ensemble model of the previously deposited single-conformer structure 2f2g and the first data set in the deposited structure factor file for 2f2g ...Details: This PDB entry is a re-refinement using an ensemble model of the previously deposited single-conformer structure 2f2g and the first data set in the deposited structure factor file for 2f2g along with the R-free set defined therein. The coordinates were generated by an automated protocol from an initial model consisting of 8 identical copies of the protein and non-water hetero-atoms assigned fractional occupancies adding up to one, and a single copy of the solvent molecules. Refinement was carried out with all the conformers present simultaneously and with the potential energy terms corresponding to interactions between the different conformers excluded. The helix and sheet records were calculated using coordinates from the first conformer only. The structure visualization program PYMOL is well-suited for directly viewing the ensemble model presented in this PDB file.
RfactorNum. reflection% reflectionSelection details
Rfree0.231 1519 5.1 %RANDOM
Rwork0.136 ---
obs0.136 30054 86.4 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 64.319 Å2 / ksol: 0.391 e/Å3
Displacement parametersBiso mean: 24.5 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.28 Å0.15 Å
Luzzati d res low-5 Å
Luzzati sigma a0.2 Å0.05 Å
Refinement stepCycle: LAST / Resolution: 2.1→28.04 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3402 0 40 427 3869
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.02
X-RAY DIFFRACTIONc_angle_deg1.9
X-RAY DIFFRACTIONc_dihedral_angle_d19.7
X-RAY DIFFRACTIONc_improper_angle_d1.23
X-RAY DIFFRACTIONc_mcbond_it1.411.5
X-RAY DIFFRACTIONc_mcangle_it2.062
X-RAY DIFFRACTIONc_scbond_it2.252
X-RAY DIFFRACTIONc_scangle_it2.732.5
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 6

Resolution (Å)Rfactor RfreeNum. reflection Rfree% reflection Rfree (%)Rfactor RworkNum. reflection RworkRfactor Rfree errorNum. reflection allNum. reflection obs% reflection obs (%)
2.1-2.230.2841304.40.1428250.0255669295552.1
2.23-2.410.2442195.30.12738960.0165680411572.4
2.41-2.650.2627650.12752830.0165676555997.9
2.65-3.030.2553105.40.1454240.0145741573499.9
3.03-3.820.232945.10.13655260.0135830582099.8
3.82-28.040.2022904.90.1455810.0126167587195.2
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1protein_rep.paramprotein.top
X-RAY DIFFRACTION2water_rep.paramwater.top
X-RAY DIFFRACTION3ion.param
X-RAY DIFFRACTION4hmh_xplor_par.txt

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