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9cq5

Mn-bound RuBisCO from spinach with CABP inhibitor

Method: X-RAY DIFFRACTION Dmax: 137.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Ribulose bisphosphate carboxylase large chain

OrganismNot specified

UniProt P00875

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count Chain A； UniProt 1–475 Chain B； UniProt 1–475 Chain C； UniProt 1–475 Chain D； UniProt 1–475 Chain E； UniProt 1–475 Chain F； UniProt 1–475 Chain G； UniProt 1–475 Chain H； UniProt 1–475 Non-standard monomer：Yes (specific site not provided by mmCIF) Ribulose bisphosphate carboxylase small subunit, chloroplastic 2 × 8 （Q43832） MN MANGANESE (II) ION × 8 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.3；298 K；PEG 3350, lithium acetate, potassium phosphate Resolution 2.50 Å R-free 0.242

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 9CQ5 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AA1 ACTIVATED SPINACH RUBISCO IN COMPLEX WITH THE PRODUCT 3-PHOSPHOGLYCERATE Deposited 1997-01-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain B 1–475（475 aa）
Chain E 1–475（475 aa）
Chain H 1–475（475 aa）
Chain L 1–475（475 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 8 3PG 3-PHOSPHOGLYCERIC ACID × 16 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.2；14% PEG 4000, 0.2 M NACL, 25 MM HEPES PH 7.8 10 MM MGCL2, 100 MM 3-PHOSPHOGLYCERATE, pH 7.2
Resolution 2.20 Å R-free 0.224
1AUS ACTIVATED UNLIGANDED SPINACH RUBISCO Deposited 1995-06-21 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain L 1–475（475 aa）
Chain M 1–475（475 aa）
Chain N 1–475（475 aa）
Chain O 1–475（475 aa）
Not recorded MG MAGNESIUM ION × 8 FMT FORMIC ACID × 8 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å R-free 0.239
1IR1 Crystal Structure of Spinach Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (Rubisco) Complexed with CO2, Mg2+ and 2-Carboxyarabinitol-1,5-Bisphosphate Deposited 2001-08-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain A 1–475（475 aa）
Chain B 1–475（475 aa）
Chain C 1–475（475 aa）
Chain D 1–475（475 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 8 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.9；293 K；PEG4000, MgCl2, NaHCO3, DTT, 2-carboxyarabinitol-1,5-bisphosphate, Bicine, pH 7.9, VAPOR DIFFUSION, temperature 293K
Resolution 1.80 Å R-free 0.179
1RBO SPINACH RUBISCO IN COMPLEX WITH THE INHIBITOR 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE Deposited 1996-10-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain B 1–475（475 aa）
Chain E 1–475（475 aa）
Chain H 1–475（475 aa）
Chain L 1–475（475 aa）
Not recorded CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.4；1.7 M (NH4)2SO4, 50 MM PHOSPHATE, PH 7.4 3 MM MGCL2, 25 MM NAHCO3, 10 MM 4CABP
Resolution 2.30 Å R-free 0.171
1RCO SPINACH RUBISCO IN COMPLEX WITH THE INHIBITOR D-XYLULOSE-2,2-DIOL-1,5-BISPHOSPHATE Deposited 1996-10-31 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain B 1–475（475 aa）
Chain E 1–475（475 aa）
Chain H 1–475（475 aa）
Chain K 1–475（475 aa）
Chain L 1–475（475 aa）
Chain O 1–475（475 aa）
Chain R 1–475（475 aa）
Chain V 1–475（475 aa）
Not recorded XDP D-XYLULOSE-2,2-DIOL-1,5-BISPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.8；15% PEG 4000, 25 MM HEPES PH 7.8, 10 MM CACL2, 0.2 M NACL, 50 MM NAHCO3, 20 MM XUBP
Resolution 2.30 Å R-free 0.246
1RCX NON-ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE Deposited 1996-12-06 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain B 1–475（475 aa）
Chain E 1–475（475 aa）
Chain H 1–475（475 aa）
Chain K 1–475（475 aa）
Chain L 1–475（475 aa）
Chain O 1–475（475 aa）
Chain R 1–475（475 aa）
Chain V 1–475（475 aa）
Not recorded RUB RIBULOSE-1,5-DIPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.8；12% PEG 4000, 25 MM HEPES PH 7.8, 0.2 M NACL, 20 MM RUBP
Resolution 2.40 Å R-free 0.237
1RXO ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE AND CALCIUM Deposited 1996-12-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain B 1–475（475 aa）
Chain E 1–475（475 aa）
Chain H 1–475（475 aa）
Chain L 1–475（475 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) RUB RIBULOSE-1,5-DIPHOSPHATE × 8 CA CALCIUM ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.8；14% PEG4000, 25 MM HEPES PH 7.8, 0.2 M NACL, 10 MM CACL2; SOAKED WITH 20 MM RUBP FOR 5 DAYS
Resolution 2.20 Å R-free 0.229
1UPM ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-CARBOXYARABINITOL 2 BISPHOSPHAT AND CA2+. Deposited 2003-10-08 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain B 1–475（475 aa）
Chain E 1–475（475 aa）
Chain H 1–475（475 aa）
Chain K 1–475（475 aa）
Chain L 1–475（475 aa）
Chain O 1–475（475 aa）
Chain R 1–475（475 aa）
Chain V 1–475（475 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 8 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.8；10% PEG 4000, 0.1 M HEPES PH 7.8, 10 MM CACL2, 0.2 M NACL, 50 MM NAHCO3, 1MM 2-CABP
Resolution 2.30 Å R-free 0.200
1UPP SPINACH RUBISCO IN COMPLEX WITH 2-CARBOXYARABINITOL 2 BISPHOSPHATE and Calcium. Deposited 2003-10-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain A 1–475（475 aa）
Chain C 1–475（475 aa）
Chain E 1–475（475 aa）
Chain G 1–475（475 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 8 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.8；10% PEG 4000, 0.1M HEPES PH 7.8, 10 MM CACL2, 0.2 M NACL, 50 MM NAHCO3, 0.1 M 3PGA THEN SOAKED IN 2-CABP
Resolution 2.30 Å R-free 0.307
8QJ0 Room-temperature Serial Synchrotron Crystallography structure of Spinacia oleracea RuBisCO Deposited 2023-09-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain L 1–475（475 aa）
Chain M 1–475（475 aa）
Chain N 1–475（475 aa）
Chain O 1–475（475 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；SpRub solution at a concentration of 15 mg/mL (in a buffer of 20 mM HEPES, 5 mM MgCl2, pH 8.0), combined reservoir solution (0.2 M MgCl2x6H2O, 0.1 M Tris pH 7.0, 12% w/v PEG 8000
Resolution 2.30 Å R-free 0.227
8RUC ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-CARBOXYARABINITOL BISPHOSPHATE Deposited 1996-02-22 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain A 1–475（475 aa）
Chain C 1–475（475 aa）
Chain E 1–475（475 aa）
Chain G 1–475（475 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 8 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 1.60 Å

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBL_SPIOL
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–475； UniProt 1–475 Author chain B； PDBConstruct 1–475； UniProt 1–475 Author chain C； PDBConstruct 1–475； UniProt 1–475 Author chain D； PDBConstruct 1–475； UniProt 1–475 Author chain E； PDBConstruct 1–475； UniProt 1–475 Author chain F； PDBConstruct 1–475； UniProt 1–475 Author chain G； PDBConstruct 1–475； UniProt 1–475 Author chain H； PDBConstruct 1–475； UniProt 1–475

Ribulose bisphosphate carboxylase small subunit, chloroplastic 2

OrganismNot specified

UniProt Q43832

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count Chain I； UniProt 58–180 Chain J； UniProt 58–180 Chain K； UniProt 58–180 Chain L； UniProt 58–180 Chain M； UniProt 58–180 Chain N； UniProt 58–180 Chain O； UniProt 58–180 Chain P； UniProt 58–180 Not recorded Ribulose bisphosphate carboxylase large chain × 8 （P00875） MN MANGANESE (II) ION × 8 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.3；298 K；PEG 3350, lithium acetate, potassium phosphate Resolution 2.50 Å R-free 0.242

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 9CQ5 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AA1 ACTIVATED SPINACH RUBISCO IN COMPLEX WITH THE PRODUCT 3-PHOSPHOGLYCERATE Deposited 1997-01-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain C 58–180（123 aa）
Chain F 58–180（123 aa）
Chain I 58–180（123 aa）
Chain S 58–180（123 aa）
Not recorded MG MAGNESIUM ION × 8 3PG 3-PHOSPHOGLYCERIC ACID × 16 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.2；14% PEG 4000, 0.2 M NACL, 25 MM HEPES PH 7.8 10 MM MGCL2, 100 MM 3-PHOSPHOGLYCERATE, pH 7.2
Resolution 2.20 Å R-free 0.224
1AUS ACTIVATED UNLIGANDED SPINACH RUBISCO Deposited 1995-06-21 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain S 58–180（123 aa）
Chain T 58–180（123 aa）
Chain U 58–180（123 aa）
Chain V 58–180（123 aa）
Not recorded MG MAGNESIUM ION × 8 FMT FORMIC ACID × 8 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å R-free 0.239
1IR1 Crystal Structure of Spinach Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (Rubisco) Complexed with CO2, Mg2+ and 2-Carboxyarabinitol-1,5-Bisphosphate Deposited 2001-08-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain S 58–180（123 aa）
Chain T 58–180（123 aa）
Chain U 58–180（123 aa）
Chain V 58–180（123 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 8 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.9；293 K；PEG4000, MgCl2, NaHCO3, DTT, 2-carboxyarabinitol-1,5-bisphosphate, Bicine, pH 7.9, VAPOR DIFFUSION, temperature 293K
Resolution 1.80 Å R-free 0.179
1UPM ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-CARBOXYARABINITOL 2 BISPHOSPHAT AND CA2+. Deposited 2003-10-08 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain C 58–180（123 aa）
Chain F 58–180（123 aa）
Chain I 58–180（123 aa）
Chain M 58–180（123 aa）
Chain P 58–180（123 aa）
Chain S 58–180（123 aa）
Chain T 58–180（123 aa）
Chain W 58–180（123 aa）
Not recorded CA CALCIUM ION × 8 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.8；10% PEG 4000, 0.1 M HEPES PH 7.8, 10 MM CACL2, 0.2 M NACL, 50 MM NAHCO3, 1MM 2-CABP
Resolution 2.30 Å R-free 0.200
1UPP SPINACH RUBISCO IN COMPLEX WITH 2-CARBOXYARABINITOL 2 BISPHOSPHATE and Calcium. Deposited 2003-10-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain I 58–180（123 aa）
Chain J 58–180（123 aa）
Chain K 58–180（123 aa）
Chain L 58–180（123 aa）
Not recorded CA CALCIUM ION × 8 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.8；10% PEG 4000, 0.1M HEPES PH 7.8, 10 MM CACL2, 0.2 M NACL, 50 MM NAHCO3, 0.1 M 3PGA THEN SOAKED IN 2-CABP
Resolution 2.30 Å R-free 0.307
1UZD Chlamydomonas,Spinach Chimeric Rubisco Deposited 2004-03-11 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain C 103–121（19 aa）
Chain F 103–121（19 aa）
Chain I 103–121（19 aa）
Chain J 103–121（19 aa）
Chain M 103–121（19 aa）
Chain P 103–121（19 aa）
Chain T 103–121（19 aa）
Chain W 103–121（19 aa）
Not recorded MG MAGNESIUM ION × 8 CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE × 8 EDO 1,2-ETHANEDIOL × 54 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；291 K；50 MM HEPES PH 7.5, 8-12% PEG 4 50 MM NAHCO3, 5 MM MGCL2, 50 UM 2-CABP, 18 DEG C, 10-15 MG PROTEIN
Resolution 2.40 Å R-free 0.230
8QJ0 Room-temperature Serial Synchrotron Crystallography structure of Spinacia oleracea RuBisCO Deposited 2023-09-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain S 58–180（123 aa）
Chain T 58–180（123 aa）
Chain U 58–180（123 aa）
Chain V 58–180（123 aa）
Not recorded MG MAGNESIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；SpRub solution at a concentration of 15 mg/mL (in a buffer of 20 mM HEPES, 5 mM MgCl2, pH 8.0), combined reservoir solution (0.2 M MgCl2x6H2O, 0.1 M Tris pH 7.0, 12% w/v PEG 8000
Resolution 2.30 Å R-free 0.227

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBS2_SPIOL
Isoform —
PDB entities 2
Chains and sequence ranges Author chain I； PDBConstruct 1–123； UniProt 58–180 Author chain J； PDBConstruct 1–123； UniProt 58–180 Author chain K； PDBConstruct 1–123； UniProt 58–180 Author chain L； PDBConstruct 1–123； UniProt 58–180 Author chain M； PDBConstruct 1–123； UniProt 58–180 Author chain N； PDBConstruct 1–123； UniProt 58–180 Author chain O； PDBConstruct 1–123； UniProt 58–180 Author chain P； PDBConstruct 1–123； UniProt 58–180

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9cq5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9cq5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9cq5
Deposition date deposition_date2024-07-19
最后修订 last_revision2025-02-05
Structure title titleMn-bound RuBisCO from spinach with CABP inhibitor
Keywords keywordsCarboxylase, Oxygenase, Inhibitor, Manganese, PHOTOSYNTHESIS, PLANT PROTEIN; PLANT PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier46.87 Å
Radius of gyration Rg (electron density) rg_electron46.18 Å
Forward intensity I(0) i04082520000.00
Molecular weight molecular_weight535250.0 kDa
Excluded volume excluded_volume667970 ų
Envelope volume envelope_volume793030 ų
Hydration-shell volume shell_volume128640 ų
Envelope diameter envelope_diameter139.3 Å
Shell Rg shell_rg59.73 Å
Envelope Rg envelope_rg45.97 Å
Shape Rg shape_rg46.18 Å
Total Rg total_rg46.54 Å
Total atoms total_atoms37696
Residues n_residues4712
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax137.2 Å
Rg (real space) rg_real46.40 Å
Rg uncertainty (real space) rg_real_error0.57 Å
I(0) (real space) i0_real4.0830e+09
I(0) uncertainty (real space) i0_real_error6.5260e+07
Rg (reciprocal space) rg_reciprocal46.86 Å
I(0) (reciprocal space) i0_reciprocal4085000000.0000
Solution quality estimate total_estimate0.8860
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.6 Å
Skewness Skewness skewness-0.024
Kurtosis Kurtosis kurtosis-0.576
Angular range angular_range— – 0.1700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3371000000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.776
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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8. Citations (2)

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9. Files and Curves (10)