SAXSdb — 9dhk

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1. Protein Identity and Related Structures Protein Identity & Related Structures

RecQ-mediated genome instability protein 1

Homo sapiens

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 475–625	Not recorded	RecQ-mediated genome instability protein 2 × 1 （Q96E14） L3 peptide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；1.8 M sodium phosphate monobasic monohydrate / potassium phosphate dibasic pH 5.0	Resolution 2.35 Å R-free 0.247
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 475–625	Not recorded	RecQ-mediated genome instability protein 2 × 1 （Q96E14） L3 peptide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；1.8 M sodium phosphate monobasic monohydrate / potassium phosphate dibasic pH 5.0	Resolution 2.35 Å R-free 0.247
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain G； UniProt 482–625	Not recorded	RecQ-mediated genome instability protein 2 × 1 （Q96E14） L3 peptide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；1.8 M sodium phosphate monobasic monohydrate / potassium phosphate dibasic pH 5.0	Resolution 2.35 Å R-free 0.247
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain J； UniProt 475–625	Not recorded	RecQ-mediated genome instability protein 2 × 1 （Q96E14） L3 peptide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；1.8 M sodium phosphate monobasic monohydrate / potassium phosphate dibasic pH 5.0	Resolution 2.35 Å R-free 0.247

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 9DHK	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3MXN Crystal structure of the RMI core complex Deposited 2010-05-07	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 473–625（153 aa） Fragment：C-terminal OB domain (unp residues 473-625)	Not recorded	BEN BENZAMIDINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；298 K；10 mM Hepes pH 7.1, 0.05 M NaSCN, 20% ethylene glycol, 2 mM DTT, 13% polyethylene glycol 3350, with benzamidine (1%) added to the drop, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.55 Å R-free 0.231
3NBH Crystal structure of human RMI1C-RMI2 complex Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 475–625（151 aa） Fragment：RMI1C, residues 475-625	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277.15 K；The precipitant/well solution contained 18% PEG 3350, 300 mM NaSCN, and 10 mM DTT. , pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K	Resolution 2.00 Å R-free 0.258
3NBI Crystal structure of human RMI1 N-terminus Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–213（212 aa） Fragment：RMI1N, residues 2-213	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277.15 K；The precipitant/well solution contained 100 mM Tris-HCl pH 8.5, 18% PEG 3350, 300 mM NaSCN, 10 mM NiCl2 and 10 mM DTT., VAPOR DIFFUSION, HANGING DROP, temperature 277.15K	Resolution 2.00 Å R-free 0.255
4CGY Crystal structure of the human topoisomerase III alpha-RMI1 complex Deposited 2013-11-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–219（219 aa） Fragment：RESIDUES 1-219	Not recorded	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；8-12% (W/V) PEG 2000, 100 MM TRIS-HCL PH 7.0, 200 MM MGCL2	Resolution 2.85 Å R-free 0.231
4CHT Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion Deposited 2013-12-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–219（219 aa） Fragment：RESIDUES 1-219	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；8% (W/V) PEG 5000 MME, 200 MM CALCIUM CITRATE, 100 MM TRIS/HCL PH 7.0	Resolution 3.25 Å R-free 0.225
4DAY Crystal structure of the RMI core complex with MM2 peptide from FANCM Deposited 2012-01-13	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 473–625（153 aa） Fragment：C-terminal OB domain (residues 473-625)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；298 K；200 mM Na2SO4, 5% polyethylene glycol 3350, pH 8.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.30 Å R-free 0.325
7XUV Crystal structure of RPA70N-RMI1 fusion Deposited 2022-05-20	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 243–262（20 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；278 K；30% PEG 2000 MME	Resolution 1.60 Å R-free 0.220
9DI4 RMI1-RMI2 bound to cyclic peptide L4 Deposited 2024-09-05	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 475–625（151 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5；293 K；0.01M zinc chloride, 0.1M sodium acetate pH 5.0, 20% w/v PEG 6000	Resolution 2.70 Å R-free 0.248
9PFD RMI1-RMI2 bound to synthetic peptide P4Ser Deposited 2025-07-04	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 475–625（151 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；1.8 M sodium phosphate monobasic monohydrate, potassium phosphate dibasic, pH 5.0	Resolution 2.01 Å R-free 0.224

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RMI1_HUMAN
Isoform	—
PDB entities	1, 4
Chains and sequence ranges	Author chain A； PDBConstruct 2–152； UniProt 475–625 Author chain D； PDBConstruct 2–152； UniProt 475–625 Author chain J； PDBConstruct 2–152； UniProt 475–625 Author chain G； PDBConstruct 2–145； UniProt 482–625

RecQ-mediated genome instability protein 2

Homo sapiens

UniProt Q96E14

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 1–147	Not recorded	RecQ-mediated genome instability protein 1 × 1 （Q9H9A7） L3 peptide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；1.8 M sodium phosphate monobasic monohydrate / potassium phosphate dibasic pH 5.0	Resolution 2.35 Å R-free 0.247
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain E； UniProt 14–147	Not recorded	RecQ-mediated genome instability protein 1 × 1 （Q9H9A7） L3 peptide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；1.8 M sodium phosphate monobasic monohydrate / potassium phosphate dibasic pH 5.0	Resolution 2.35 Å R-free 0.247
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain H； UniProt 15–147	Not recorded	RecQ-mediated genome instability protein 1 × 1 （Q9H9A7） L3 peptide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；1.8 M sodium phosphate monobasic monohydrate / potassium phosphate dibasic pH 5.0	Resolution 2.35 Å R-free 0.247
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain K； UniProt 1–147	Not recorded	RecQ-mediated genome instability protein 1 × 1 （Q9H9A7） L3 peptide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；1.8 M sodium phosphate monobasic monohydrate / potassium phosphate dibasic pH 5.0	Resolution 2.35 Å R-free 0.247

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 9DHK	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3MXN Crystal structure of the RMI core complex Deposited 2010-05-07	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–147（147 aa）	Not recorded	BEN BENZAMIDINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；298 K；10 mM Hepes pH 7.1, 0.05 M NaSCN, 20% ethylene glycol, 2 mM DTT, 13% polyethylene glycol 3350, with benzamidine (1%) added to the drop, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.55 Å R-free 0.231
3NBH Crystal structure of human RMI1C-RMI2 complex Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 6–147（142 aa） Fragment：RMI2, residues 6-147	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277.15 K；The precipitant/well solution contained 18% PEG 3350, 300 mM NaSCN, and 10 mM DTT. , pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K	Resolution 2.00 Å R-free 0.258
4DAY Crystal structure of the RMI core complex with MM2 peptide from FANCM Deposited 2012-01-13	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–147（147 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；298 K；200 mM Na2SO4, 5% polyethylene glycol 3350, pH 8.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.30 Å R-free 0.325
9DI4 RMI1-RMI2 bound to cyclic peptide L4 Deposited 2024-09-05	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–147（147 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5；293 K；0.01M zinc chloride, 0.1M sodium acetate pH 5.0, 20% w/v PEG 6000	Resolution 2.70 Å R-free 0.248
9PFD RMI1-RMI2 bound to synthetic peptide P4Ser Deposited 2025-07-04	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–147（147 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；1.8 M sodium phosphate monobasic monohydrate, potassium phosphate dibasic, pH 5.0	Resolution 2.01 Å R-free 0.224

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RMI2_HUMAN
Isoform	—
PDB entities	2, 3, 5
Chains and sequence ranges	Author chain B； PDBConstruct 1–147； UniProt 1–147 Author chain K； PDBConstruct 1–147； UniProt 1–147 Author chain E； PDBConstruct 2–135； UniProt 14–147 Author chain H； PDBConstruct 7–139； UniProt 15–147

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9dhk
Deposition date deposition_date	2024-09-03
Structure title title	RMI1-RMI2 bound to cyclic peptide L3
Keywords keywords	DNA damage repair, complex, cyclic peptide, competitive inhibitor, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	38.46 Å
Radius of gyration Rg (electron density) rg_electron	37.80 Å
Forward intensity I(0) i0	252659000.00
Molecular weight molecular_weight	130760.0 kDa
Excluded volume excluded_volume	164810 Å³
Envelope volume envelope_volume	217110 Å³
Hydration-shell volume shell_volume	48644 Å³
Envelope diameter envelope_diameter	128.2 Å
Shell Rg shell_rg	43.07 Å
Envelope Rg envelope_rg	37.11 Å
Shape Rg shape_rg	37.79 Å
Total Rg total_rg	38.15 Å
Total atoms total_atoms	18525
Residues n_residues	1172
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	122.9 Å
Rg (real space) rg_real	38.33 Å
Rg uncertainty (real space) rg_real_error	1.02 Å
I(0) (real space) i0_real	2.5270e+08
I(0) uncertainty (real space) i0_real_error	4.2010e+06
Rg (reciprocal space) rg_reciprocal	38.41 Å
I(0) (reciprocal space) i0_reciprocal	252700000.0000
Solution quality estimate total_estimate	0.9002
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	54.0 Å
Skewness Skewness skewness	0.136
Kurtosis Kurtosis kurtosis	-0.627
Angular range angular_range	— – 0.2050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	43210000.0000
Real-space data points n_real_points	42
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.900

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	RecQ-mediated genome instability protein 1
Molecular weight formula_weight	16944.8 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D,J
Atom count atom_count	18874

MENSINLSIAMDLYSPPFVYLSVLMASKPKEVTTVKVKAFIVTLTGNLSSSGGIWSITAKVSDGTAYLDVDFVDEILTSLIGFSVPEMKQSKKDPLQYQKFLEGLQKCQRDLIDLCCLMTISFNPSLSKAMVLALQDVNMEHLENLKKRLNK

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	RecQ-mediated genome instability protein 2
Molecular weight formula_weight	15886.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,K

MAAAADSFSGGPAGVRLPRSPPLKVLAEQLRRDAEGGPGAWRLSRAAAGRGPLDLAAVWMQGRVVMADRGEARLRDPSGDFSVRGLERVPRGRPCLVPGKYVMVMGVVQACSPEPCLQAVKMTDLSDNPIHESMWELEVEDLHRNIP

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	RecQ-mediated genome instability protein 2
Molecular weight formula_weight	14837.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

XGVRLPRSPPLKVLAEQLRRDAEGGPGAWRLSRAAAGRGPLDLAAVWMQGRVVMADRGEARLRDPSGDFSVRGLERVPRGRPCLVPGKYVMVMGVVQACSPEPCLQAVKMTDLSDNPIHESMWELEVEDLHRNIP

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	RecQ-mediated genome instability protein 1
Molecular weight formula_weight	16140.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

XIAMDLYSPPFVYLSVLMASKPKEVTTVKVKAFIVTLTGNLSSSGGIWSITAKVSDGTAYLDVDFVDEILTSLIGFSVPEMKQSKKDPLQYQKFLEGLQKCQRDLIDLCCLMTISFNPSLSKAMVLALQDVNMEHLENLKKRLNK

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 5 Entity 5 polymer

Description description	RecQ-mediated genome instability protein 2
Molecular weight formula_weight	15205.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

XXXXXXVRLPRSPPLKVLAEQLRRDAEGGPGAWRLSRAAAGRGPLDLAAVWMQGRVVMADRGEARLRDPSGDFSVRGLERVPRGRPCLVPGKYVMVMGVVQACSPEPCLQAVKMTDLSDNPIHESMWELEVEDLHRNIP

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 6 Entity 6 polymer

Description description	L3 peptide
Molecular weight formula_weight	1791.1 kDa
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,F,I,L

XYRLWFFQTYKLPCX

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	289

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8. Citations (1)

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Unit-cell length a length_a	189.150 Å
Unit-cell length b length_b	50.622 Å
Unit-cell length c length_c	181.221 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	118.05 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.350 Å
Low-resolution limit resolution_low	48.272 Å
R factor r_factor	—
R_work r_work	0.2035
R_free r_free	0.2467

fit	/app/data/saxs_computation/dh/9dhk/9dhk.fit
pddf	/app/data/pr_computation/dh/9dhk/9dhk.pr.out
profile	/app/data/saxs_computation/dh/9dhk/9dhk.dat

RMI1-RMI2 bound to cyclic peptide L3

1. Protein Identity and Related Structures Protein Identity & Related Structures

RecQ-mediated genome instability protein 1

State in the Current Structure

Other States of the Same Protein in the Database

RecQ-mediated genome instability protein 2

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

Entity 5 Entity 5 polymer

Polymer Polymer

来源 Source

Entity 6 Entity 6 polymer

Polymer Polymer

Entity 7 Entity 7 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)