SAXSdb — 4fma

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

EspG protein

Escherichia coli

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 47–397	Not recorded	MG MAGNESIUM ION × 2 FMT FORMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
10	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain J； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 2 ACY ACETIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
11	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain K； UniProt 47–397	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
12	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain L； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 3 FMT FORMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
13	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 47–397 Chain C； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 4 FMT FORMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
14	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 47–397 Chain F； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 3 FMT FORMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
15	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 47–397 Chain K； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 3 FMT FORMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
16	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 47–397 Chain I； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
17	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 47–397 Chain L； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 3 FMT FORMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
18	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 47–397 Chain J； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 3 ACY ACETIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 1 FMT FORMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
3	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain C； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
4	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain D； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 3 FMT FORMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
5	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain E； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
6	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain F； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
7	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain G； UniProt 47–397	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
8	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain H； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239
9	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain I； UniProt 47–397	Not recorded	MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.5 M sodium formate, 0.1 M Bis-Tis propane (pH 7.0), and 0.2 M magnesium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.15 Å R-free 0.239

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 4FMA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4FMD EspG-Rab1 complex structure at 3.05 A Deposited 2012-06-16	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 47–397（351 aa）	Not recorded	AF3 ALUMINUM FLUORIDE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；298 K；20% PEG3350, 0.1 M trisodium citrate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.05 Å R-free 0.266
4FMD EspG-Rab1 complex structure at 3.05 A Deposited 2012-06-16	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 47–397（351 aa）	Not recorded	AF3 ALUMINUM FLUORIDE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 PGE TRIETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；298 K；20% PEG3350, 0.1 M trisodium citrate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.05 Å R-free 0.266
4FMD EspG-Rab1 complex structure at 3.05 A Deposited 2012-06-16	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 47–397（351 aa）	Not recorded	AF3 ALUMINUM FLUORIDE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；298 K；20% PEG3350, 0.1 M trisodium citrate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.05 Å R-free 0.266
4FME EspG-Rab1-Arf6 complex Deposited 2012-06-16	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 47–397（351 aa）	Not recorded	AF3 ALUMINUM FLUORIDE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；298 K；8% PEG8000, 0.1 M NaKPO4 (pH 6.2), and 0.2 M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 4.10 Å R-free 0.249
4FME EspG-Rab1-Arf6 complex Deposited 2012-06-16	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 47–397（351 aa）	Not recorded	AF3 ALUMINUM FLUORIDE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；298 K；8% PEG8000, 0.1 M NaKPO4 (pH 6.2), and 0.2 M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 4.10 Å R-free 0.249

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

View Construct and Data Evidence

UniProt name	Q5WMC0_ECOLX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–351； UniProt 47–397 Author chain B； PDBConstruct 1–351； UniProt 47–397 Author chain C； PDBConstruct 1–351； UniProt 47–397 Author chain D； PDBConstruct 1–351； UniProt 47–397 Author chain E； PDBConstruct 1–351； UniProt 47–397 Author chain F； PDBConstruct 1–351； UniProt 47–397 Author chain G； PDBConstruct 1–351； UniProt 47–397 Author chain H； PDBConstruct 1–351； UniProt 47–397 Author chain I； PDBConstruct 1–351； UniProt 47–397 Author chain J； PDBConstruct 1–351； UniProt 47–397 Author chain K； PDBConstruct 1–351； UniProt 47–397 Author chain L； PDBConstruct 1–351； UniProt 47–397

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	4fma
Deposition date deposition_date	2012-06-16
Structure title title	EspG structure
Keywords keywords	alpha and beta fold, Rab1 GAP, Rab1 GTPase, PROTEIN BINDING; PROTEIN BINDING
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	64.14 Å
Radius of gyration Rg (electron density) rg_electron	63.94 Å
Forward intensity I(0) i0	3205660000.00
Molecular weight molecular_weight	457420.0 kDa
Excluded volume excluded_volume	565050 Å³
Envelope volume envelope_volume	899690 Å³
Hydration-shell volume shell_volume	119170 Å³
Envelope diameter envelope_diameter	207.4 Å
Shell Rg shell_rg	63.01 Å
Envelope Rg envelope_rg	61.81 Å
Shape Rg shape_rg	63.94 Å
Total Rg total_rg	63.91 Å
Total atoms total_atoms	32039
Residues n_residues	4153
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	223.6 Å
Rg (real space) rg_real	63.97 Å
Rg uncertainty (real space) rg_real_error	2.17 Å
I(0) (real space) i0_real	3.2060e+09
I(0) uncertainty (real space) i0_real_error	6.5890e+07
Rg (reciprocal space) rg_reciprocal	64.25 Å
I(0) (reciprocal space) i0_reciprocal	3207000000.0000
Solution quality estimate total_estimate	0.8851
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	74.5 Å
Skewness Skewness skewness	0.166
Kurtosis Kurtosis kurtosis	-0.566
Angular range angular_range	— – 0.1200 Å⁻¹
Current regularization parameter α current_alpha	0.0003
Highest regularization parameter α highest_alpha	95550000.0000
Real-space data points n_real_points	25
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.933

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	EspG protein
Molecular weight formula_weight	38875.5 kDa
Source method src_method	man
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L
Atom count atom_count	34644

EMSCAEKLLKVLSFGLWNPTYSRSERQSFQELLTVLEPVYPLPNELGRVSARFSDGSSLRISVTNSESIEAEIRTPDNEKITVLLESNEQNRLLQSLPIDRHMPYIQVHRALSEMDLTDTTSMRNLLGFTSKLSTTLIPHNAQTDPLSGPTPFSSIFMDTCRGLGNAKLSLNGVDIPANAQMLLRDALGLKDTHSSPSRNVIDHGISRHDAEQIARESSGSDNQKAEVVEFLCHPEAATAICSAFYQSFNVPALTLTHERISKASEYNAERSLDTPNACINISISQSSDGNIYVTSHTGVLIMAPEDRPNEMGMLTNRTSYEVPQGVKCTIDEMVRALQPRYAASETYLQN

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	19

Entity 3 Entity 3 non-polymer

Description description	FORMIC ACID
Molecular weight formula_weight	46.0 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 4 Entity 4 non-polymer

Description description	ACETIC ACID
Molecular weight formula_weight	60.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	2605

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7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	4fmaA01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	4fmaB01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	4fmaC01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	4fmaD01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	4fmaE01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	4fmaF01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	4fmaG01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	4fmaH01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	4fmaI01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	4fmaJ01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	4fmaK01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	4fmaL01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

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8. Citations (1)

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Unit-cell length a length_a	94.615 Å
Unit-cell length b length_b	167.739 Å
Unit-cell length c length_c	361.690 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	48

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.150 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2020
R_work r_work	0.2001
R_free r_free	0.2388

fit	/app/data/saxs_computation/fm/4fma/4fma.fit
pddf	/app/data/pr_computation/fm/4fma/4fma.pr.out
profile	/app/data/saxs_computation/fm/4fma/4fma.dat

EspG structure

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

EspG protein

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