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- PDB-2h9f: CRYSTAL STRUCTURE OF a PrpF family methylaconitate isomerase (PA0... -

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Basic information

Entry
Database: PDB / ID: 2h9f
TitleCRYSTAL STRUCTURE OF a PrpF family methylaconitate isomerase (PA0793) FROM PSEUDOMONAS AERUGINOSA AT 1.95 A RESOLUTION
ComponentsHypothetical protein
KeywordsISOMERASE / METHYLACONITATE ISOMERASE / STRUCTURAL GENOMICS / JOINT CENTER FOR STRUCTURAL GENOMICS / JCSG / PROTEIN STRUCTURE INITIATIVE / PSI-2
Function / homology
Function and homology information


propionate catabolic process, 2-methylcitrate cycle / isomerase activity
Similarity search - Function
2-methyl-aconitate isomerase PrpF / PrpF protein / PrpF protein / Diaminopimelate Epimerase; Chain A, domain 1 / Diaminopimelate Epimerase; Chain A, domain 1 / Roll / Alpha Beta
Similarity search - Domain/homology
: / Uncharacterized protein
Similarity search - Component
Biological speciesPseudomonas aeruginosa (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.95 Å
AuthorsJoint Center for Structural Genomics (JCSG)
CitationJournal: To be published
Title: Crystal structure of hypothetical protein (np_249484.1) from Pseudomonas aeruginosa at 1.95 A resolution
Authors: Joint Center for Structural Genomics (JCSG)
History
DepositionJun 9, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 8, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Derived calculations / Version format compliance
Revision 1.3Oct 18, 2017Group: Refinement description / Category: software / Item: _software.classification / _software.name
Revision 1.4Jan 25, 2023Group: 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_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr1_symmetry / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 999SEQUENCE: THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...SEQUENCE: THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Hypothetical protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,97910
Polymers42,2801
Non-polymers6989
Water6,684371
1
A: Hypothetical protein
hetero molecules

A: Hypothetical protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,95720
Polymers84,5612
Non-polymers1,39718
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation6_555x,-y+1/2,-z+1/41
Buried area7110 Å2
ΔGint-134 kcal/mol
Surface area31420 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)148.690, 148.690, 141.085
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number98
Space group name H-MI4122

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Hypothetical protein


Mass: 42280.262 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Gene: np_249484.1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9I5E5

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Non-polymers , 5 types, 380 molecules

#2: Chemical ChemComp-CO / COBALT (II) ION


Mass: 58.933 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Co
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#4: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 371 / 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: 4.18 Å3/Da / Density % sol: 70.36 %
Crystal growTemperature: 277 K / pH: 6.5
Details: 1.8M (NH4)2SO4, 0.01M CoCl2, 0.1M MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL1-5 / Wavelength: 0.97624 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: May 25, 2006
Details: 1m long Rh coated bent cylindrical mirror for horizontal and vertical focussing
RadiationMonochromator: Double-crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97624 Å / Relative weight: 1
ReflectionResolution: 1.95→47.036 Å / Num. obs: 57509 / % possible obs: 100 % / Redundancy: 8.58 % / Biso Wilson estimate: 35.2 Å2 / Rmerge(I) obs: 0.091 / Net I/σ(I): 14.54
Reflection shell

Diffraction-ID: 1

Resolution (Å)Highest resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique all% possible all
1.95-2.047.360.9382.25496356723100
2.04-2.130.6583.342283573395.5
2.13-2.240.5054.343669591496.6
2.24-2.380.3915.445023609897.5
2.38-2.560.2757.644677605598.2
2.56-2.820.17511.346464629598.6
2.82-3.230.09817.946445633399.3
3.230.0732.372298631699.8

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Phasing

PhasingMethod: SAD

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Processing

Software
NameVersionClassificationNB
MolProbity3beta29model building
REFMAC5.2.0019refinement
XSCALEdata scaling
PDB_EXTRACT2data extraction
XDSdata reduction
SHELXDphasing
autoSHARPphasing
RefinementMethod to determine structure: SAD / Resolution: 1.95→47.02 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.959 / SU B: 6.099 / SU ML: 0.085 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.095 / ESU R Free: 0.096
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE ...Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.7 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. AN METAL ION WAS FOUND NEAR HIS 3, MEDIATING INTERACTION BETWEEN A SYMMETRIC RELATED MOLECULE, WAS MODELLED AS A COBALT ION DUE TO ITS PRESENCE IN THE CRYSTALLIZATION CONDITION. 4. THE LOOP 289-293 HAS POOR DENSITY. LOOP 183-186 IS DISORDERED. 5. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY.
RfactorNum. reflection% reflectionSelection details
Rfree0.196 2918 5.1 %RANDOM
Rwork0.168 ---
obs0.169 57491 99.98 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 29.583 Å2
Baniso -1Baniso -2Baniso -3
1--1.5 Å20 Å20 Å2
2---1.5 Å20 Å2
3---2.99 Å2
Refinement stepCycle: LAST / Resolution: 1.95→47.02 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2894 0 35 371 3300
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0170.0223016
X-RAY DIFFRACTIONr_bond_other_d0.0010.022050
X-RAY DIFFRACTIONr_angle_refined_deg1.5511.9694102
X-RAY DIFFRACTIONr_angle_other_deg0.91934979
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.3985399
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.86722.705122
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.22115464
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.8521527
X-RAY DIFFRACTIONr_chiral_restr0.0880.2455
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.023415
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02616
X-RAY DIFFRACTIONr_nbd_refined0.2060.2505
X-RAY DIFFRACTIONr_nbd_other0.2020.22130
X-RAY DIFFRACTIONr_nbtor_refined0.1780.21428
X-RAY DIFFRACTIONr_nbtor_other0.0910.21670
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1560.2237
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1350.222
X-RAY DIFFRACTIONr_symmetry_vdw_other0.3020.284
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1510.220
X-RAY DIFFRACTIONr_mcbond_it2.16732083
X-RAY DIFFRACTIONr_mcbond_other0.6783808
X-RAY DIFFRACTIONr_mcangle_it2.76343120
X-RAY DIFFRACTIONr_scbond_it4.3161145
X-RAY DIFFRACTIONr_scangle_it5.6837977
LS refinement shellResolution: 1.95→2.001 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.31 204 -
Rwork0.294 3978 -
obs-4182 100 %
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)
10.3401-0.0722-0.08541.5459-0.2420.30570.07550.0767-0.0863-0.2189-0.03220.05230.04510.0059-0.04330.0590.0201-0.032-0.07440.0078-0.116173.396626.79819.425
21.9394-0.43860.86882.6927-0.6693.3892-0.15210.1939-0.07210.1490.0914-0.0591-0.43010.54790.06070.0343-0.07370.0706-0.07640.0039-0.204399.02026.402214.9791
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Selection: ALL / Auth asym-ID: A / Label asym-ID: A

IDRefine TLS-IDAuth seq-IDLabel seq-ID
111 - 1822 - 183
21372 - 395373 - 396
32187 - 371188 - 372

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