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- PDB-6e50: Crystal structure of the apo domain-swapped dimer Q108K:K40L:T51F... -

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Basic information

Entry
Database: PDB / ID: 6.0E+50
TitleCrystal structure of the apo domain-swapped dimer Q108K:K40L:T51F mutant of human Cellular Retinol Binding Protein II
ComponentsRetinol-binding protein 2
KeywordsCYTOSOLIC PROTEIN / Retinol / iLBP / Protein Switch
Function / homology
Function and homology information


vitamin A metabolic process / molecular carrier activity / retinoid binding / retinal binding / retinol binding / epidermis development / fatty acid transport / Retinoid metabolism and transport / fatty acid binding / nucleus / cytosol
Similarity search - Function
Cytosolic fatty-acid binding proteins signature. / Intracellular lipid binding protein / Cytosolic fatty-acid binding / Lipocalin / cytosolic fatty-acid binding protein family / Lipocalin/cytosolic fatty-acid binding domain / Calycin beta-barrel core domain / Calycin / Lipocalin / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
ACETATE ION / Retinol-binding protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.965 Å
AuthorsGhanbarpour, A. / Geiger, J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI) United States
CitationJournal: J.Am.Chem.Soc. / Year: 2019
Title: Engineering the hCRBPII Domain-Swapped Dimer into a New Class of Protein Switches.
Authors: Ghanbarpour, A. / Pinger, C. / Esmatpour Salmani, R. / Assar, Z. / Santos, E.M. / Nosrati, M. / Pawlowski, K. / Spence, D. / Vasileiou, C. / Jin, X. / Borhan, B. / Geiger, J.H.
History
DepositionJul 18, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 16, 2019Provider: repository / Type: Initial release
Revision 1.1Nov 13, 2019Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.2Dec 18, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Oct 11, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Retinol-binding protein 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)15,7473
Polymers15,6291
Non-polymers1182
Water59433
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A: Retinol-binding protein 2
hetero molecules

A: Retinol-binding protein 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,4936
Polymers31,2572
Non-polymers2364
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_565-x,-y+1,z1
Buried area8360 Å2
ΔGint-41 kcal/mol
Surface area14060 Å2
MethodPISA
Unit cell
Length a, b, c (Å)63.637, 60.468, 36.659
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein Retinol-binding protein 2 / Cellular retinol-binding protein II / CRBP-II


Mass: 15628.552 Da / Num. of mol.: 1 / Mutation: Q108K, K40L, T51F
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RBP2, CRBP2
Production host: Bacterial expression vector pBEN1-SGC (others)
References: UniProt: P50120
#2: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2 / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 33 / 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: 2.26 Å3/Da / Density % sol: 45.49 %
Crystal growTemperature: 298 K / Method: evaporation / Details: PEG 4000, sodium acetate, Ammonium acetate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97856 Å
DetectorType: RAYONIX MX300HE / Detector: CCD / Date: Jun 5, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97856 Å / Relative weight: 1
ReflectionResolution: 1.965→28.12 Å / Num. all: 10581 / Num. obs: 8891 / % possible obs: 84.05 % / Redundancy: 3.2 % / Rmerge(I) obs: 0.057 / Rrim(I) all: 0.067 / Net I/σ(I): 23.78
Reflection shellResolution: 1.965→2.036 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.43 / Num. unique obs: 879 / Rrim(I) all: 0.505 / % possible all: 85.7

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575)refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2RCQ

2rcq


Resolution: 1.965→28.12 Å / SU ML: 0.3 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 31.17
RfactorNum. reflection% reflection
Rfree0.266 887 9.98 %
Rwork0.2012 --
obs0.2077 8891 84.08 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.965→28.12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1098 0 8 33 1139
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0071165
X-RAY DIFFRACTIONf_angle_d0.8891578
X-RAY DIFFRACTIONf_dihedral_angle_d6.418961
X-RAY DIFFRACTIONf_chiral_restr0.053172
X-RAY DIFFRACTIONf_plane_restr0.004204
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9654-2.08850.35251490.27241306X-RAY DIFFRACTION84
2.0885-2.24980.32931410.26931349X-RAY DIFFRACTION87
2.2498-2.47610.33391450.24951296X-RAY DIFFRACTION83
2.4761-2.83420.3041520.23311335X-RAY DIFFRACTION85
2.8342-3.570.27911510.20451350X-RAY DIFFRACTION85
3.57-31.76940.21341490.15871368X-RAY DIFFRACTION81

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