SAXSdb — 1esg

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

TYPE II RESTRICTION ENZYME BAMHI

Bacillus amyloliquefaciens

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–DNA Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric（4） Consistent with all polymer counts	Chain A； UniProt 1–213 Chain B； UniProt 1–213	Not recorded	;DNA (5'-D(TPGPGPAPTPTPCPA)-3') ; × 1 ;DNA (5'-D(TPGPAPAPTPCPCPA)-3') ; × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 4.8；293 K；30% MPD, 10 mM sodium acetate (pH 4.8), 5 mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 20K	Resolution 1.90 Å R-free 0.230

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 1ESG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BAM STRUCTURE OF RESTRICTION ENDONUCLEASE BAMHI PHASED AT 1.95 ANGSTROMS RESOLUTION BY MAD ANALYSIS Deposited 1994-12-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–213（213 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.95 Å
1BHM RESTRICTION ENDONUCLEASE BAMHI COMPLEX WITH DNA Deposited 1995-07-12	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 1–213（213 aa） Chain B 1–213（213 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP	Resolution 2.20 Å
2BAM RESTRICTION ENDONUCLEASE BAMHI COMPLEX WITH DNA AND CALCIUM IONS (PRE-REACTIVE COMPLEX). Deposited 1998-08-19	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 1–213（213 aa） Chain B 1–213（213 aa）	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.3；12-14% PEG8000, 0.1M MES (PH 5.3), 0.15M KCL, 5% GLYCEROL	Resolution 2.00 Å R-free 0.251
3BAM RESTRICTION ENDONUCLEASE BAMHI COMPLEX WITH DNA AND MANGANESE IONS (POST-REACTIVE COMPLEX) Deposited 1998-08-19	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: pentameric	Chain A 1–213（213 aa） Chain B 1–213（213 aa）	Not recorded	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.3；pH 5.3 CATALYSIS OCCURRED IN THE CRYSTAL AFTER SOAKING MANGANESE ION. THE ACTIVE SITE OF THE R SUBUNIT CLEAVED THE ORIGINAL D STRAND IN TWO (D AND E) RESULTING IN A POST-REACTIVE COMPLEX.	Resolution 1.80 Å R-free 0.268

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	T2BA_BACAM
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain A； PDBConstruct 1–213； UniProt 1–213 Author chain B； PDBConstruct 1–213； UniProt 1–213

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	1esg
Deposition date deposition_date	2000-04-09
Structure title title	RESTRICTION ENDONUCLEASE BAMHI BOUND TO A NON-SPECIFIC DNA.
Keywords keywords	Non-specific DNA-protein complex., HYDROLASE-DNA COMPLEX; HYDROLASE/DNA
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	24.40 Å
Radius of gyration Rg (electron density) rg_electron	23.68 Å
Forward intensity I(0) i0	49199700.00
Molecular weight molecular_weight	53331.0 kDa
Excluded volume excluded_volume	66317 Å³
Envelope volume envelope_volume	79415 Å³
Hydration-shell volume shell_volume	28028 Å³
Envelope diameter envelope_diameter	79.6 Å
Shell Rg shell_rg	30.78 Å
Envelope Rg envelope_rg	23.66 Å
Shape Rg shape_rg	23.66 Å
Total Rg total_rg	24.54 Å
Total atoms total_atoms	3736
Residues n_residues	437
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	77.5 Å
Rg (real space) rg_real	24.33 Å
Rg uncertainty (real space) rg_real_error	0.38 Å
I(0) (real space) i0_real	4.9200e+07
I(0) uncertainty (real space) i0_real_error	5.8370e+05
Rg (reciprocal space) rg_reciprocal	24.35 Å
I(0) (reciprocal space) i0_reciprocal	49200000.0000
Solution quality estimate total_estimate	0.8979
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	29.5 Å
Skewness Skewness skewness	0.287
Kurtosis Kurtosis kurtosis	-0.376
Angular range angular_range	— – 0.3250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	10100000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.975

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	;DNA (5'-D(TPGPGPAPTPTPCPA)-3') ;
Molecular weight formula_weight	2441.6 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	C
Atom count atom_count	4315

TGGATTCA

Entity 2 Entity 2 polymer

Description description	;DNA (5'-D(TPGPAPAPTPCPCPA)-3') ;
Molecular weight formula_weight	2410.6 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	D

TGAATCCA

Entity 3 Entity 3 polymer

Description description	TYPE II RESTRICTION ENZYME BAMHI
Molecular weight formula_weight	24602.3 kDa
EC 编号 ec_number	3.1.21.4
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

MEVEKEFITDEAKELLSKDKLIQQAYNEVKTSICSPIWPATSKTFTINNTEKNCNGVVPIKELCYTLLEDTYNWYREKPLDILKLEKKKGGPIDVYKEFIENSELKRVGMEFETGNISSAHRSMNKLLLGLKHGEIDLAIILMPIKQLAYYLTDRVTNFEELEPYFELTEGQPFIFIGFNAEAYNSNVPLIPKGSDGMSKRSIKKWKDKVENK

来源 Source

来源生物 organism	Bacillus amyloliquefaciens
NCBI Class编号 ncbi_taxonomy_id	1390
宿主生物 host_organism	Escherichia coli

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	579

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1esga_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.3 — Restriction endonuclease BamHI

Domain ID domain_id	d1esgb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.52 — Restriction endonuclease-like
Superfamily Superfamily superfamily	c.52.1 — Restriction endonuclease-like
Family Family family	c.52.1.3 — Restriction endonuclease BamHI

CATH v4.4 (2 domains)

Domain ID domain_id	1esgA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1esgB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	91 — Restriction Endonuclease
Homologous superfamily homologous superfamily	20 —

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8. Citations (2)

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Unit-cell length a length_a	114.800 Å
Unit-cell length b length_b	91.100 Å
Unit-cell length c length_c	66.400 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	8

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

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	—
R_work r_work	0.1907
R_free r_free	0.2302

fit	/app/data/saxs_computation/es/1esg/1esg.fit
pddf	/app/data/pr_computation/es/1esg/1esg.pr.out
profile	/app/data/saxs_computation/es/1esg/1esg.dat

RESTRICTION ENDONUCLEASE BAMHI BOUND TO A NON-SPECIFIC DNA.

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

TYPE II RESTRICTION ENZYME BAMHI

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

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)