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- PDB-2od4: Crystal structure of a dimeric ferredoxin-like protein (jcvi_pep_... -

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Basic information

Entry
Database: PDB / ID: 2od4
TitleCrystal structure of a dimeric ferredoxin-like protein (jcvi_pep_1096665735785) from uncultured marine organism at 1.70 A resolution
Componentshypothetical protein
KeywordsUNKNOWN FUNCTION / Metagenomics target / structural genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-2
Function / homologyAlpha-Beta Plaits - #100 / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Function and homology information
Biological speciesuncultured marine organism (environmental samples)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.7 Å
AuthorsJoint Center for Structural Genomics (JCSG)
CitationJournal: To be published
Title: Crystal structure of hypothetical protein (JCVI_PEP_1096665735785) from an environmental metagenome (unidentified marine microbe), Sorcerer II Global Ocean Sampling experiment at 1.70 A resolution
Authors: Joint Center for Structural Genomics (JCSG)
History
DepositionDec 21, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 23, 2007Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.3Oct 18, 2017Group: Refinement description / Category: software / Item: _software.classification / _software.name
Revision 1.4Oct 25, 2017Group: Author supporting evidence / Category: pdbx_struct_assembly_auth_evidence
Revision 1.5Dec 27, 2023Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_conn / 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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.6Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature
Remark 300BIOMOLECULE: 1,2 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 ...BIOMOLECULE: 1,2 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAINS. SEE REMARK 350 FOR INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A DIMER AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.
Remark 999SEQUENCE (1) THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...SEQUENCE (1) 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. (2) THE SEQUENCE OF THE PROTEIN WAS NOT AVAILABLE IN THE UNP DATABASE AT THE TIME OF PROCESSING. (3) PRODUCT OF THE EXPRESSED SYNTHETIC GENE WAS BASED ON THE PREDICTED SEQUENCE OF ACCESSION ID JCVI_PEP_1096665735785 FROM THE J. CRAIG VENTER INSTITUTE.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: hypothetical protein
B: hypothetical protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,6477
Polymers23,4442
Non-polymers2045
Water3,387188
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, light scattering
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3350 Å2
ΔGint-58 kcal/mol
Surface area10670 Å2
MethodPISA
Unit cell
Length a, b, c (Å)31.890, 77.790, 43.810
Angle α, β, γ (deg.)90.000, 102.660, 90.000
Int Tables number4
Space group name H-MP1211
DetailsSIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A DIMER AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.

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Components

#1: Protein hypothetical protein


Mass: 11721.772 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) uncultured marine organism (environmental samples)
Description: SYNTHETIC GENE: The gene product was based on JCVI_PEP_1096665735785 from the Sorcerer II Global Ocean Sampling experiment
Production host: Escherichia coli (E. coli)
#2: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#3: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 188 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.26 Å3/Da / Density % sol: 45.59 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop, nanodrop / pH: 4.5
Details: 0.2M Li2SO4, 2.5M NaCl, 0.1M Acetate pH 4.5, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.91837, 0.97966
DetectorType: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Nov 19, 2006 / Details: Flat mirror (vertical focusing)
RadiationMonochromator: Single crystal Si(111) bent monochromator (horizontal focusing)
Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.918371
20.979661
ReflectionResolution: 1.7→28.892 Å / Num. obs: 22797 / % possible obs: 98.3 % / Biso Wilson estimate: 21.1 Å2 / Rmerge(I) obs: 0.061 / Net I/σ(I): 6.76
Reflection shell
Resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsDiffraction-ID% possible all
1.7-1.760.4032.027045199
1.76-1.830.3372.477002198.9
1.83-1.910.2573.076894198.4
1.91-2.020.1754.277704198.6
2.02-2.140.1255.556687199
2.14-2.310.0916.897288198.5
2.31-2.540.0758.066984198.3
2.54-2.90.0639.667006197.9
2.9-3.660.0512.17195197.5
3.66-28.90.0413.737089196.5

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Phasing

PhasingMethod: MAD

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Processing

Software
NameVersionClassificationNB
MolProbity3beta29model building
SOLVEphasing
REFMAC5.2.0019refinement
XSCALEdata scaling
PDB_EXTRACT2data extraction
Blu-IceV. 5.0data collection
XDSdata reduction
RefinementMethod to determine structure: MAD / Resolution: 1.7→28.892 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.958 / SU B: 4.644 / SU ML: 0.075 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.1 / ESU R Free: 0.098
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 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. AN EDO MOLECULE FROM THE CRYO SOLUTION IS MODELED. 4. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY.
RfactorNum. reflection% reflectionSelection details
Rfree0.193 1172 5.1 %RANDOM
Rwork0.159 ---
obs0.161 22774 99.11 %-
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: 20.689 Å2
Baniso -1Baniso -2Baniso -3
1-2.63 Å20 Å20.35 Å2
2---0.97 Å20 Å2
3----1.51 Å2
Refinement stepCycle: LAST / Resolution: 1.7→28.892 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1619 0 8 188 1815
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0221692
X-RAY DIFFRACTIONr_bond_other_d0.0010.021158
X-RAY DIFFRACTIONr_angle_refined_deg1.4151.9482297
X-RAY DIFFRACTIONr_angle_other_deg0.88132836
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.4455214
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.48324.28677
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.23515308
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.1561510
X-RAY DIFFRACTIONr_chiral_restr0.0860.2261
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.021867
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02345
X-RAY DIFFRACTIONr_nbd_refined0.2150.2290
X-RAY DIFFRACTIONr_nbd_other0.1880.21168
X-RAY DIFFRACTIONr_nbtor_refined0.1870.2851
X-RAY DIFFRACTIONr_nbtor_other0.0870.2953
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1750.2123
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2610.223
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2850.252
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1450.214
X-RAY DIFFRACTIONr_mcbond_it2.42731231
X-RAY DIFFRACTIONr_mcbond_other0.5033411
X-RAY DIFFRACTIONr_mcangle_it2.83251696
X-RAY DIFFRACTIONr_scbond_it5.3848740
X-RAY DIFFRACTIONr_scangle_it7.61411594
LS refinement shellResolution: 1.7→1.744 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.25 74 -
Rwork0.227 1608 -
obs-1682 99.59 %
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)
10.39850.45610.0990.55120.39532.746-0.02680.0179-0.0179-0.07630.0084-0.0474-0.1476-0.07760.0184-0.11340.0212-0.0262-0.0025-0.00510.01224.03536.66429.893
20.3023-0.0235-0.28990.71540.00841.2012-0.0044-0.0186-0.01150.014-0.0012-0.01870.1186-0.09740.0056-0.08610.0104-0.0187-0.0072-0.00340.0187-0.9825.38343.751
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Selection: ALL / Auth seq-ID: 0 - 100 / Label seq-ID: 1 - 101

IDRefine TLS-IDAuth asym-IDLabel asym-ID
11AA
22BB

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