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- PDB-7vle: Oxy-deoxy intermediate of V2 hemoglobin at 55% oxygen saturation -

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Basic information

Entry
Database: PDB / ID: 7vle
TitleOxy-deoxy intermediate of V2 hemoglobin at 55% oxygen saturation
Components(Extracellular ...Glossary of biology) x 4
KeywordsOXYGEN TRANSPORT / allostery / structural transition / giant hemoglobin
Function / homology
Function and homology information


hemoglobin complex / oxygen carrier activity / oxygen binding / iron ion binding / heme binding / extracellular region
Similarity search - Function
Casein alpha/beta, conserved site / Caseins alpha/beta signature. / Globin, extracellular / Erythrocruorin / Myoglobin-like, M family globin domain / Globin/Protoglobin / Globin domain profile. / Globin / Globin / Globin-like superfamily
Similarity search - Domain/homology
PROTOPORPHYRIN IX CONTAINING FE / OXYGEN MOLECULE / Extracellular globin / Extracellular globin / Extracellular globin / Extracellular globin
Similarity search - Component
Biological speciesLamellibrachia satsuma (invertebrata)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsNumoto, N. / Onoda, S. / Kawano, Y. / Okumura, H. / Baba, S. / Fukumori, Y. / Miki, K. / Ito, N.
Funding support Japan, 2items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)25870200 Japan
Japan Society for the Promotion of Science (JSPS)15K20971 Japan
CitationJournal: Biophys Physicobio. / Year: 2022
Title: Structures of oxygen dissociation intermediates of 400 kDa V2 hemoglobin provide coarse snapshots of the protein allostery.
Authors: Numoto, N. / Onoda, S. / Kawano, Y. / Okumura, H. / Baba, S. / Fukumori, Y. / Miki, K. / Ito, N.
History
DepositionOct 2, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 18, 2022Provider: repository / Type: Initial release
Revision 1.1Jul 20, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation_author.identifier_ORCID
Revision 1.2Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Extracellular A1 globin
B: Extracellular A2 globin
C: Extracellular B2 globin
D: Extracellular B1 globin
E: Extracellular A1 globin
F: Extracellular A2 globin
G: Extracellular B2 globin
H: Extracellular B1 globin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)136,06026
Polymers130,1388
Non-polymers5,92318
Water5,693316
1
A: Extracellular A1 globin
B: Extracellular A2 globin
C: Extracellular B2 globin
D: Extracellular B1 globin
E: Extracellular A1 globin
F: Extracellular A2 globin
G: Extracellular B2 globin
H: Extracellular B1 globin
hetero molecules

A: Extracellular A1 globin
B: Extracellular A2 globin
C: Extracellular B2 globin
D: Extracellular B1 globin
E: Extracellular A1 globin
F: Extracellular A2 globin
G: Extracellular B2 globin
H: Extracellular B1 globin
hetero molecules

A: Extracellular A1 globin
B: Extracellular A2 globin
C: Extracellular B2 globin
D: Extracellular B1 globin
E: Extracellular A1 globin
F: Extracellular A2 globin
G: Extracellular B2 globin
H: Extracellular B1 globin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)408,18078
Polymers390,41324
Non-polymers17,76854
Water43224
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_655-y+1,x-y,z1
crystal symmetry operation3_665-x+y+1,-x+1,z1
Buried area94170 Å2
ΔGint-701 kcal/mol
Surface area124160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)109.644, 109.644, 195.496
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number173
Space group name H-MP63
Space group name HallP6c
Symmetry operation#1: x,y,z
#2: x-y,x,z+1/2
#3: y,-x+y,z+1/2
#4: -y,x-y,z
#5: -x+y,-x,z
#6: -x,-y,z+1/2

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Components

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Extracellular ... , 4 types, 8 molecules AEBFCGDH

#1: Protein Extracellular A1 globin


Mass: 16368.704 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Lamellibrachia satsuma (invertebrata) / References: UniProt: S0BBU7
#2: Protein Extracellular A2 globin


Mass: 15951.922 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Lamellibrachia satsuma (invertebrata) / References: UniProt: S0BBR6
#3: Protein Extracellular B2 globin


Mass: 16519.531 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Lamellibrachia satsuma (invertebrata) / References: UniProt: S0BCU7
#4: Protein Extracellular B1 globin


Mass: 16228.627 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Lamellibrachia satsuma (invertebrata) / References: UniProt: S0BAP9

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Sugars , 1 types, 2 molecules

#5: Polysaccharide alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 367.349 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
LFucpa1-6DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(6+1)][a-L-Fucp]{}}LINUCSPDB-CARE

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Non-polymers , 3 types, 332 molecules

#6: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C34H32FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#7: Chemical
ChemComp-OXY / OXYGEN MOLECULE / Oxygen


Mass: 31.999 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: O2 / Feature type: SUBJECT OF INVESTIGATION
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 316 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.61 Å3/Da / Density % sol: 52.81 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 14-17% (w/v) PEG 3350, 100mM HEPES-NaOH pH 7.5

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Data collection

DiffractionMean temperature: 95 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NW12A / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Nov 1, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.3→50 Å / Num. obs: 58863 / % possible obs: 99.9 % / Redundancy: 11.1 % / Biso Wilson estimate: 43.79 Å2 / CC1/2: 0.999 / Rsym value: 0.122 / Net I/σ(I): 15.6
Reflection shellResolution: 2.3→2.44 Å / Redundancy: 9.1 % / Mean I/σ(I) obs: 1.8 / CC1/2: 0.584 / Rsym value: 1.32 / % possible all: 99.5

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Processing

Software
NameVersionClassification
PHENIX1.13_2998refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3WCT

3wct


Resolution: 2.3→48.87 Å / SU ML: 0.3388 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 25.6298 / Stereochemistry target values: GeoStd + Monomer Library
RfactorNum. reflection% reflection
Rfree0.2465 2949 5.01 %
Rwork0.2004 55909 -
obs0.2027 58858 99.9 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 44.83 Å2
Refinement stepCycle: LAST / Resolution: 2.3→48.87 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9096 0 408 316 9820
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0059778
X-RAY DIFFRACTIONf_angle_d0.747213348
X-RAY DIFFRACTIONf_chiral_restr0.03641394
X-RAY DIFFRACTIONf_plane_restr0.0031702
X-RAY DIFFRACTIONf_dihedral_angle_d19.03975622
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3-2.340.33721370.28482629X-RAY DIFFRACTION98.33
2.34-2.380.32541440.26662648X-RAY DIFFRACTION99.96
2.38-2.420.32611380.25462640X-RAY DIFFRACTION100
2.42-2.470.28311380.24832673X-RAY DIFFRACTION100
2.47-2.520.30411240.23452676X-RAY DIFFRACTION100
2.52-2.570.27741370.23062664X-RAY DIFFRACTION100
2.57-2.630.32221460.23452646X-RAY DIFFRACTION100
2.63-2.70.28231330.23912653X-RAY DIFFRACTION100
2.7-2.770.29071340.232664X-RAY DIFFRACTION100
2.77-2.850.29681500.22392649X-RAY DIFFRACTION100
2.85-2.950.32341370.21572682X-RAY DIFFRACTION100
2.95-3.050.2911530.23362637X-RAY DIFFRACTION100
3.05-3.170.30261480.23022655X-RAY DIFFRACTION100
3.17-3.320.30391570.22772642X-RAY DIFFRACTION100
3.32-3.490.24741340.21122684X-RAY DIFFRACTION100
3.49-3.710.22261450.19072645X-RAY DIFFRACTION100
3.71-40.2261280.17812681X-RAY DIFFRACTION100
4-4.40.21451450.17322687X-RAY DIFFRACTION100
4.4-5.040.21111370.17172653X-RAY DIFFRACTION100
5.04-6.340.2241400.19312693X-RAY DIFFRACTION100
6.34-48.870.17571440.16392708X-RAY DIFFRACTION99.79

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