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- PDB-4w6b: Crystal Structure of a Superfolder GFP Mutant K26C Disulfide Dime... -

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Basic information

Entry
Database: PDB / ID: 4w6b
TitleCrystal Structure of a Superfolder GFP Mutant K26C Disulfide Dimer, P 21 21 21 Space Group
Componentsfluorescent protein K26CFluorescence
KeywordsFLUORESCENT PROTEIN / fluorescent protein / dimer / disulfide
Biological speciessynthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsPashkov, I. / Sawaya, M.R. / Leibly, D.J. / Waldo, G.S. / Yeates, T.O.
Funding supportUnited States , 1件
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical SciencesGM098177United States
CitationJournal: Structure / Year: 2015
Title: A Suite of Engineered GFP Molecules for Oligomeric Scaffolding.
Authors: Leibly, D.J. / Arbing, M.A. / Pashkov, I. / DeVore, N. / Waldo, G.S. / Terwilliger, T.C. / Yeates, T.O.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Aug 20, 2014 / Release: Feb 18, 2015
RevisionDateData content typeGroupCategoryItemProviderType
1.0Feb 18, 2015Structure modelrepositoryInitial release
1.1Jan 27, 2016Structure modelDatabase references
1.2Sep 27, 2017Structure modelAuthor supporting evidence / Database references / Derived calculationscitation / pdbx_audit_support / pdbx_struct_oper_list_citation.journal_id_CSD / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: fluorescent protein K26C
B: fluorescent protein K26C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,2835
Polymers53,1882
Non-polymers953
Water3,981221
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)50.151, 90.356, 102.830
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein/peptide fluorescent protein K26C / Fluorescence


Mass: 26593.869 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli (E. coli)
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg / Magnesium
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl / Chloride
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 221 / Source method: isolated from a natural source / Formula: H2O / Water

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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: 2.19 Å3/Da / Density % sol: 43.84 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 / Details: 14% PEG-4000, 0.2M MgCl2, 0.1M Tris pH 8.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97918 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 23, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 1.9→44.69 Å / Num. obs: 37298 / % possible obs: 98.4 % / Redundancy: 6.8 % / Rsym value: 0.1043 / Net I/σ(I): 7.28

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: DEV_1555)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2B3P
Resolution: 1.9→44.69 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 18.9 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.202 1842 4.94 %
Rwork0.167 --
Obs0.169 37279 98.4 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.9→44.69 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3617 0 3 221 3841
Refine LS restraints

Refinement-ID: X-RAY DIFFRACTION

TypeDev idealNumber
f_bond_d0.0153730
f_angle_d1.1765056
f_dihedral_angle_d13.5451394
f_chiral_restr0.04552
f_plane_restr0.006659
LS refinement shell

Refinement-ID: X-RAY DIFFRACTION

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.9-1.94640.27581350.2013231585
1.9464-2.00360.2561160.1885263996
2.0036-2.06830.23751420.17512711100
2.0683-2.14220.20371480.16592741100
2.1422-2.2280.18761380.16222710100
2.228-2.32940.21641330.16492760100
2.3294-2.45220.22521720.16792716100
2.4522-2.60580.19191350.17812762100
2.6058-2.8070.2441330.1892782100
2.807-3.08940.22241410.1872756100
3.0894-3.53630.20191450.1742785100
3.5363-4.45470.15541560.14052828100
4.4547-44.69930.18141480.1543293299
Refinement TLS params.

Method: refined / Refinement-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
11.8336-0.55430.48951.6057-0.47881.9073-0.0526-0.1235-0.04530.05440.12660.05240.0083-0.126-0.03890.11620.0010.01380.12440.01120.10978.4784-9.2057-23.8443
21.6817-0.0879-0.06351.4086-0.17211.68280.03250.01910.0593-0.0429-0.0278-0.0715-0.1030.1119-0.00390.1239-0.00220.01230.1070.00290.092830.29780.13231.9593
Refinement TLS group

Refinement-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection details
11(CHAIN A AND RESSEQ 2:230)
22(CHAIN B AND RESSEQ 4:230)

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