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1hrr

THE THREE DIMENSIONAL STRUCTURE OF THE REDUCED HIGH POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR

Method: SOLUTION NMR Dmax: 37.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

REDUCED HIGH POTENTIAL IRON SULFUR PROTEIN

OrganismNot specified

UniProt P00260

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 38–122 Not recorded SF4 IRON/SULFUR CLUSTER × 1 SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

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 1HRR Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1B0Y MUTANT H42Q OF HIPIP FROM CHROMATIUM VINOSUM AT 0.93A Deposited 1998-11-15 Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 38–122（85 aa）
Mutation：H42Q SF4 IRON/SULFUR CLUSTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.3；2M AMMONIUM SULPHATE, 40 MM TRI 180 MM KCL, pH 5.3
Resolution 0.93 Å R-free 0.205
1CKU AB INITIO SOLUTION AND REFINEMENT OF TWO HIGH POTENTIAL IRON PROTEIN STRUCTURES AT ATOMIC RESOLUTION Deposited 1999-04-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 38–122（85 aa）
Chain B 38–122（85 aa）
Not recorded SF4 IRON/SULFUR CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.3；1.3 M AMMONIUM SULPHATE, 40 MM TRIS 180 MM KCL, pH 5.3
Resolution 1.20 Å R-free 0.178
1HIP TWO-ANGSTROM CRYSTAL STRUCTURE OF OXIDIZED CHROMATIUM HIGH POTENTIAL IRON PROTEIN Deposited 1975-04-01 Different construct Different experimental method Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–86（85 aa）
Not recorded SF4 IRON/SULFUR CLUSTER × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1HRQ THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR Deposited 1995-01-17 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 38–122（85 aa）
Not recorded SF4 IRON/SULFUR CLUSTER × 1 SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1JS2 Crystal structure of C77S HiPIP: a serine ligated [4Fe-4S] cluster Deposited 2001-08-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 38–122（85 aa） Fragment：residues 38-122 of P00260
Chain B 38–122（85 aa） Fragment：residues 38-122 of P00260
Chain C 38–122（85 aa） Fragment：residues 38-122 of P00260
Chain D 38–122（85 aa） Fragment：residues 38-122 of P00260
Mutation：C77S Mutation：C77S Mutation：C77S Mutation：C77S SF4 IRON/SULFUR CLUSTER × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；VAPOR DIFFUSION, HANGING DROP at pH 8.0, 293K
Resolution 1.90 Å R-free 0.234
1NEH HIGH POTENTIAL IRON-SULFUR PROTEIN Deposited 1995-12-14 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 38–122（85 aa）
Not recorded SF4 IRON/SULFUR CLUSTER × 1 SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1NOE NMR STUDY OF REDUCED HIGH POTENTIAL IRON SULFUR PROTEIN Deposited 1996-01-07 Different construct Different mutation/modification Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–122（86 aa）
Mutation：C77S SF4 IRON/SULFUR CLUSTER × 1 SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided

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

View Construct and Data Evidence
UniProt name HIP_CHRVI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–85； UniProt 38–122

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 1hrr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1hrr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1hrr
Deposition date deposition_date1995-01-17
Structure title titleTHE THREE DIMENSIONAL STRUCTURE OF THE REDUCED HIGH POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR
Keywords keywordsELECTRON TRANSFER (IRON-SULFUR); ELECTRON TRANSFER (IRON-SULFUR)
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier10.76 Å
Radius of gyration Rg (electron density) rg_electron11.27 Å
Forward intensity I(0) i0331368000.00
Molecular weight molecular_weight138820.0 kDa
Excluded volume excluded_volume166950 ų
Envelope volume envelope_volume14610 ų
Hydration-shell volume shell_volume10225 ų
Envelope diameter envelope_diameter37.8 Å
Shell Rg shell_rg17.92 Å
Envelope Rg envelope_rg12.44 Å
Shape Rg shape_rg11.38 Å
Total Rg total_rg11.08 Å
Total atoms total_atoms18360
Residues n_residues1275
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 dmax37.4 Å
Rg (real space) rg_real10.70 Å
Rg uncertainty (real space) rg_real_error0.32 Å
I(0) (real space) i0_real3.3140e+08
I(0) uncertainty (real space) i0_real_error3.9100e+06
Rg (reciprocal space) rg_reciprocal10.70 Å
I(0) (reciprocal space) i0_reciprocal331400000.0000
Solution quality estimate total_estimate0.8488
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary12.8 Å
Skewness Skewness skewness0.133
Kurtosis Kurtosis kurtosis-0.445
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha190000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.683; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.984
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1hrra_
Class classg — Small proteins
Fold Fold foldg.35 — HIPIP (high potential iron protein)
Superfamily Superfamily superfamilyg.35.1 — HIPIP (high potential iron protein)
Family Family familyg.35.1.1 — HIPIP (high potential iron protein)

CATH v4.4 (1 domains)

Domain ID domain_id1hrrA00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology490 — High-Potential Iron-Sulfur Protein; Chain A
Homologous superfamily homologous superfamily10 — High potential iron-sulphur protein
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8. Citations (4)

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9. Files and Curves (10)