SAXSdb — 4d7z

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

ASPARTATE 1-DECARBOXYLASE BETA CHAIN

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–24 Chain B； UniProt 25–119	Fragment：RESIDUES 25-119 Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	PEG DI(HYDROXYETHYL)ETHER × 1 SCN THIOCYANATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.8；ADC.PANZ COMPLEX WAS PREPARED IN A 10: 11 RATIO AT A FINAL CONCENTRATION OF 5.7 MG/ML WITH A 2-FOLD MOLAR EXCESS (RELATIVE TO PANZ) OF ACETYLCOA IN 0.05 M TRIS-HCL PH 7.69, 0.1 M NACL, 0.1 MM DTT. THIS WAS MIXED IN A 1:1 RATIO WITH RESERVOIR SOLUTION (0.2 M POTASSIUM THIOCYANATE, 0.1 M BIS- TRIS PROPANE PH 6.8, 20 % W/V PEG 3350) AND CRYSTALLIZED BY HANGING DROP VAOUR DIFFUSION (4 UL DROPLET OVER A 1 ML RESERVOIR).	Resolution 1.90 Å R-free 0.244

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 4D7Z	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AW8 PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE Deposited 1997-10-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–24（24 aa） Chain B 25–115（91 aa） Chain D 1–24（24 aa） Chain E 25–115（91 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；PROTEIN WAS CRYSTALLIZED FROM 12% PEG 2000 MME, 0.1 M NA ACETATE, PH 4.6	Resolution 2.20 Å R-free 0.239
1PPY Native precursor of pyruvoyl dependent Aspartate decarboxylase Deposited 2003-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–126（126 aa） Chain B 1–126（126 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；292 K；NH42SO4, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.95 Å R-free 0.195
1PQE S25A mutant of pyruvoyl dependent aspartate decarboxylase Deposited 2003-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–126（126 aa）	Mutation：S25A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；NH42SO4,Tris/HCL, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.95 Å R-free 0.205
1PQF Glycine 24 to Serine mutation of aspartate decarboxylase Deposited 2003-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–126（126 aa） Chain B 1–126（126 aa）	Mutation：G24S Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：G24S Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；292 K；NH42SO4, citric acid, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.00 Å R-free 0.185
1PQH Serine 25 to Threonine mutation of aspartate decarboxylase Deposited 2003-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–126（126 aa） Chain B 1–126（126 aa）	Mutation：S25T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S25T Non-standard monomer：Yes (specific site not provided by mmCIF)	NA SODIUM ION × 2 MLA MALONIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；292 K；Sodium malonate, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.29 Å R-free 0.166
1PT0 Unprocessed Pyruvoyl Dependent Aspartate Decarboxylase with an Alanine insertion at position 26 Deposited 2003-06-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–126（126 aa） Chain B 1–126（126 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；290 K；1.4-1.6M Ammonium Sulphate, 0.1M Citric Acid, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.00 Å R-free 0.191
1PT1 Unprocessed Pyruvoyl Dependent Aspartate Decarboxylase with Histidine 11 Mutated to Alanine Deposited 2003-06-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–126（126 aa） Chain B 1–126（126 aa）	Mutation：H11A Mutation：H11A	SO4 SULFATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；290 K；1.4-1.6M Ammonium Sulphate, 0.1M Citric Acid, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 1.90 Å R-free 0.170
1PYQ Unprocessed Aspartate Decarboxylase Mutant, with Alanine inserted at position 24 Deposited 2003-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–126（126 aa） Chain B 1–126（126 aa）	Not recorded	SO4 SULFATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；290 K；0.1M citric acid, 1.6M ammonium sulphate, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 1.90 Å R-free 0.179
1PYU Processed Aspartate Decarboxylase Mutant with Ser25 mutated to Cys Deposited 2003-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–24（24 aa） Chain B 25–126（102 aa） Chain C 1–24（24 aa） Chain D 25–126（102 aa）	Mutation：S25C Mutation：S25C	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；290 K；0.1M citric acid, 1.6M ammonium sulphate, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 1.90 Å R-free 0.196
3TM7 Processed Aspartate Decarboxylase Mutant with Asn72 mutated to Ala Deposited 2011-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–24（24 aa） Chain B 25–126（102 aa） Chain C 1–24（24 aa） Chain D 25–126（102 aa）	Mutation：N72A Mutation：N72A	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；298 K；1.6-2.4M ammonium sulphate, 0.1M citric acid, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.70 Å R-free 0.184
3TM7 Processed Aspartate Decarboxylase Mutant with Asn72 mutated to Ala Deposited 2011-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–24（24 aa） Chain B 25–126（102 aa） Chain C 1–24（24 aa） Chain D 25–126（102 aa）	Mutation：N72A Mutation：N72A	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；298 K；1.6-2.4M ammonium sulphate, 0.1M citric acid, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.70 Å R-free 0.184
4AOK Conformational dynamics of aspartate alpha-decarboxylase active site revealed by protein-ligand complexes: 1-methyl-L-aspartate complex Deposited 2012-03-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–24（24 aa） Chain B 25–126（102 aa） Chain D 1–24（24 aa） Chain E 25–126（102 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.2；5 MG/ML ASPARTATE-ALPHA-DECARBOXYLASE IN 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM CITRATE, PH 3.8	Resolution 1.50 Å R-free 0.180
4AON Conformational dynamics of aspartate alpha-decarboxylase active site revealed by protein-ligand complexes: 1-methyl-L-aspartate complex Deposited 2012-03-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–24（24 aa） Chain B 25–126（102 aa） Chain D 1–24（24 aa） Chain E 25–126（102 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	GLU GLUTAMIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.2；5 MG/ML ASPARTATE-ALPHA-DECARBOXYLASE IN 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM CITRATE, PH 3.8	Resolution 1.50 Å R-free 0.162
4AZD T57V mutant of aspartate decarboxylase Deposited 2012-06-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–126（126 aa） Chain B 1–126（126 aa）	Mutation：YES Mutation：YES	MLI MALONATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions pH 4；292 K；2.4 M SODIUM MALONATE, 1.5 M (NH4)2SO4 PH 4, 292 K	Resolution 1.62 Å R-free 0.217
4CRY Direct visualisation of strain-induced protein post-translational modification Deposited 2014-03-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–24（24 aa） Chain G 25–126（102 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	ACO ACETYL COENZYME *A × 4 MG MAGNESIUM ION × 4 CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；20% (W/V) POLYETHYLENE GLYCOL (PEG) 3350, 0.1 M BIS-TRIS PROPANE PH 7.4, 0.2 M POTASSIUM THIOCYANATE	Resolution 1.61 Å R-free 0.150
4CRZ Direct visualisation of strain-induced protein prost-translational modification Deposited 2014-03-02	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 A 1–126（126 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	SCN THIOCYANATE ION × 4 ACO ACETYL COENZYME *A × 4 MG MAGNESIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；20% (W/V) POLYETHYLENE GLYCOL (PEG) 3350, 0.1 M BIS-TRIS PROPANE PH 7.4, 0.2 M POTASSIUM THIOCYANATE	Resolution 1.70 Å R-free 0.175
4CS0 Direct visualisation of strain-induced protein post-translational modification Deposited 2014-03-02	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 A 1–126（126 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	SCN THIOCYANATE ION × 4 ACO ACETYL COENZYME *A × 4 MG MAGNESIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；20% (W/V) POLYETHYLENE GLYCOL (PEG) 3350, 0.1 M BIS-TRIS PROPANE PH 7.4, 0.2 M POTASSIUM THIOCYANATE	Resolution 2.10 Å R-free 0.237
5LS7 Complex of wild type E. coli alpha aspartate decarboxylase with its processing factor PanZ Deposited 2016-08-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–24（24 aa） Chain D 25–126（102 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	GOL GLYCEROL × 8 PEG DI(HYDROXYETHYL)ETHER × 8 ACO ACETYL COENZYME A × 4 MG MAGNESIUM ION × 4 CO2* CARBON DIOXIDE × 12 SCN THIOCYANATE ION × 8 74C methyl radical × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；200 mM KSCN, 100 mM Bis-Tris propane pH 6.5, 20% v/v PEG 3350	Resolution 1.16 Å R-free 0.137

17 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PAND_ECOLI
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 18–41； UniProt 1–24 Author chain B； PDBConstruct 1–95； UniProt 25–119

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	4d7z
Deposition date deposition_date	2014-12-02
Structure title title	E. coli L-aspartate-alpha-decarboxylase mutant N72Q to a resolution of 1.9 Angstroms
Keywords keywords	LYASE, PROTEIN DERIVED COFACTOR, PANTOTHENATE SYNTHESIS, PYRUVOYL COFACTOR, BETA-ALANINE; LYASE
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	16.69 Å
Radius of gyration Rg (electron density) rg_electron	15.59 Å
Forward intensity I(0) i0	4010250.00
Molecular weight molecular_weight	13645.0 kDa
Excluded volume excluded_volume	16846 Å³
Envelope volume envelope_volume	20023 Å³
Hydration-shell volume shell_volume	11631 Å³
Envelope diameter envelope_diameter	58.2 Å
Shell Rg shell_rg	20.56 Å
Envelope Rg envelope_rg	16.29 Å
Shape Rg shape_rg	15.55 Å
Total Rg total_rg	16.66 Å
Total atoms total_atoms	955
Residues n_residues	122
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	60.6 Å
Rg (real space) rg_real	16.75 Å
Rg uncertainty (real space) rg_real_error	0.53 Å
I(0) (real space) i0_real	4.0100e+06
I(0) uncertainty (real space) i0_real_error	5.2320e+04
Rg (reciprocal space) rg_reciprocal	16.74 Å
I(0) (reciprocal space) i0_reciprocal	4010000.0000
Solution quality estimate total_estimate	0.8281
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.7 Å
Skewness Skewness skewness	0.470
Kurtosis Kurtosis kurtosis	-0.136
Angular range angular_range	— – 0.4750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	642800.0000
Real-space data points n_real_points	78
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.643; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.858; Smooth: 0.976

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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	ASPARTATE 1-DECARBOXYLASE BETA CHAIN
Molecular weight formula_weight	4770.6 kDa
EC 编号 ec_number	4.1.1.11
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1089

MRGSHHHHHHGLVPRGSMIRTMLQGKLHRVKVTHADLHYEG

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 polymer

Description description	ASPARTATE 1-DECARBOXYLASE ALPHA CHAIN
Molecular weight formula_weight	10345.5 kDa
EC 编号 ec_number	4.1.1.11
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

XCAIDQDFLDAAGILENEAIDIWNVTNGKRFSTYAIAAERGSRIISVQGAAAHCASVGDIVIIASFVTMPDEEARTWRPNVAYFEGDNEMKRTAK

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 3 Entity 3 non-polymer

Description description	DI(HYDROXYETHYL)ETHER
Molecular weight formula_weight	106.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	THIOCYANATE ION
Molecular weight formula_weight	58.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	122

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	4d7zB00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	40 — Barwin-like endoglucanases
Homologous superfamily homologous superfamily	20 —

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8. Citations (1)

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Unit-cell length a length_a	71.350 Å
Unit-cell length b length_b	71.350 Å
Unit-cell length c length_c	112.310 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	16

Space group space_group	I 4 2 2
Space-group number int_tables_number	97
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	60.220 Å
R factor r_factor	0.1889
R_work r_work	0.1862
R_free r_free	0.2442

fit	/app/data/saxs_computation/d7/4d7z/4d7z.fit
pddf	/app/data/pr_computation/d7/4d7z/4d7z.pr.out
profile	/app/data/saxs_computation/d7/4d7z/4d7z.dat

E. coli L-aspartate-alpha-decarboxylase mutant N72Q to a resolution of 1.9 Angstroms

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

ASPARTATE 1-DECARBOXYLASE BETA CHAIN

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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)