SAXSdb — 1lj2

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

NONSTRUCTURAL RNA-BINDING PROTEIN 34

Simian rotavirus A/SA11

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 206–315 Chain B； UniProt 206–315	Fragment：C-terminal domain Mutation：C306S C314S	eukaryotic protein synthesis initiation factor × 2 （Q04637） AU GOLD ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；275 K；PEG-MME 550, glucose, theophylline, unbuffered, VAPOR DIFFUSION, HANGING DROP at 275K	Resolution 2.38 Å R-free 0.272

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 1LJ2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1KNZ Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer Deposited 2001-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 2 PDB declaration: trimeric	Chain A 4–164（161 aa） Fragment：N-terminal domain Chain B 4–164（161 aa） Fragment：N-terminal domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；297 K；PEG 4000, ammonium sulfate, MES, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 297K	Resolution 2.45 Å R-free 0.280
1KNZ Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer Deposited 2001-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–RNA Homooligomer；Protein × 2 PDB declaration: trimeric	Chain C 4–164（161 aa） Fragment：N-terminal domain Chain D 4–164（161 aa） Fragment：N-terminal domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；297 K；PEG 4000, ammonium sulfate, MES, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 297K	Resolution 2.45 Å R-free 0.280
1KNZ Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer Deposited 2001-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–RNA Homooligomer；Protein × 2 PDB declaration: trimeric	Chain I 4–164（161 aa） Fragment：N-terminal domain Chain J 4–164（161 aa） Fragment：N-terminal domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；297 K；PEG 4000, ammonium sulfate, MES, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 297K	Resolution 2.45 Å R-free 0.280
1KNZ Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer Deposited 2001-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein–RNA Homooligomer；Protein × 2 PDB declaration: trimeric	Chain M 4–164（161 aa） Fragment：N-terminal domain Chain N 4–164（161 aa） Fragment：N-terminal domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；297 K；PEG 4000, ammonium sulfate, MES, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 297K	Resolution 2.45 Å R-free 0.280

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

View Construct and Data Evidence

UniProt name	VN34_ROTS1
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–110； UniProt 206–315 Author chain B； PDBConstruct 1–110； UniProt 206–315

eukaryotic protein synthesis initiation factor

OrganismNot specified

UniProt Q04637

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain C； UniProt 172–199 Chain D； UniProt 172–199	Fragment：residues 132-159 of AAC82471	NONSTRUCTURAL RNA-BINDING PROTEIN 34 × 2 （P03536） AU GOLD ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；275 K；PEG-MME 550, glucose, theophylline, unbuffered, VAPOR DIFFUSION, HANGING DROP at 275K	Resolution 2.38 Å R-free 0.272

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 1LJ2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1UG3 C-terminal portion of human eIF4GI Deposited 2003-06-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1194–1532（339 aa） Fragment：RESIDUES 1234-1572	Mutation：L1234S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；30% PEG MME 5000, 0.1M MES, 0.2M AMMONIUM SULFATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.24 Å R-free 0.292
1UG3 C-terminal portion of human eIF4GI Deposited 2003-06-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1194–1532（339 aa） Fragment：RESIDUES 1234-1572	Mutation：L1234S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；30% PEG MME 5000, 0.1M MES, 0.2M AMMONIUM SULFATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.24 Å R-free 0.292
2W97 Crystal Structure of eIF4E Bound to Glycerol and eIF4G1 peptide Deposited 2009-01-22	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 413–426（14 aa） Fragment：EIF4GI BINDING MOTIF, RESIDUES 413-426 Chain F 413–426（14 aa） Fragment：EIF4GI BINDING MOTIF, RESIDUES 413-426	Not recorded	MGO [[(2R,3S,4R,5R)-5-(6-AMINO-3-METHYL-4-OXO-5H-IMIDAZO[4,5-C]PYRIDIN-1-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHOXY-HYDROXY-PHOSPHORYL] PHOSPHONO HYDROGEN PHOSPHATE × 1 PGE TRIETHYLENE GLYCOL × 1 SO4 SULFATE ION × 4 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；60% AMMONIUM SULPHATE, 100MM TRIS-HCL PH 8.0, 1% PEG400	Resolution 2.29 Å R-free 0.239
4F02 Crystal structure of the PABP-binding site of eIF4G in complex with RRM1-2 of PABP and poly(A) Deposited 2012-05-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 2 PDB declaration: trimeric	Chain C 178–203（26 aa） Fragment：unp residues 178-203	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；294 K；0.03 M Tris, 1.3 M (NH4)2SO4, 5% glycerol, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.00 Å R-free 0.230
4F02 Crystal structure of the PABP-binding site of eIF4G in complex with RRM1-2 of PABP and poly(A) Deposited 2012-05-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–RNA Heteromer；Protein × 2 PDB declaration: trimeric	Chain F 178–203（26 aa） Fragment：unp residues 178-203	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；294 K；0.03 M Tris, 1.3 M (NH4)2SO4, 5% glycerol, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.00 Å R-free 0.230
5EHC Co-crystal structure of eIF4E with nucleotide mimetic inhibitor. Deposited 2015-10-28	Different construct Different mutation/modification 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 609–622（14 aa） Fragment：eIF4E binding sequence, UNP residues 634-647	Not recorded	5NX 3-[[(2~{R},3~{S},4~{R},5~{R})-5-[2-azanyl-7-[(3-chlorophenyl)methyl]-6-oxidanylidene-1~{H}-purin-7-ium-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methylamino]-4-oxidanyl-cyclobut-3-ene-1,2-dione × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；21-31% PEG 8000, 1???3% (NH4)2SO4, 100 mM HEPES, pH 7.5, 1 round of seeding	Resolution 2.40 Å R-free 0.264
5T46 Crystal structure of the human eIF4E-eIF4G complex Deposited 2016-08-29	Different construct Different mutation/modification 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 592–653（62 aa）	Not recorded	MGP 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.25；293 K；0.1 M Hepes pH 7.25, 25% w/v PEG 6000	Resolution 1.53 Å R-free 0.162
5T46 Crystal structure of the human eIF4E-eIF4G complex Deposited 2016-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 592–653（62 aa）	Not recorded	MGP 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE × 1 GOL GLYCEROL × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.25；293 K；0.1 M Hepes pH 7.25, 25% w/v PEG 6000	Resolution 1.53 Å R-free 0.162
5ZK5 Stapled-peptides tailored against initiation of translation Deposited 2018-03-23	Different construct Different mutation/modification 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 609–623（15 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MGT 7N-METHYL-8-HYDROGUANOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；295 K；30%(w/v) PEG6000, 0.1M Na-Hepes pH 6.5	Resolution 2.25 Å R-free 0.268
6ZMW Structure of a human 48S translational initiation complex Deposited 2020-07-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 54 PDB declaration: 57-meric	Chain g 290–1599（1310 aa）	Not recorded	ZN ZINC ION × 2 MG MAGNESIUM ION × 89	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8HUJ Cryo-EM structure of the J-K-St region of EMCV IRES in complex with eIF4G-HEAT1 and eIF4A Deposited 2022-12-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 2 PDB declaration: trimeric	Chain B 746–992（247 aa）	Not recorded	MG MAGNESIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.76 Å
8J7R Cryo-EM structure of the J-K-St region of EMCV IRES in complex with eIF4G-HEAT1 and eIF4A (J-K-St/eIF4G focused) Deposited 2023-04-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain B 746–992（247 aa）	Not recorded	MG MAGNESIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8OZ0 Structure of a human 48S translation initiation complex with eIF4F and eIF4A Deposited 2023-05-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 54 PDB declaration: 57-meric	Chain 2 1–1404（1404 aa）	Not recorded	ZN ZINC ION × 2 MG MAGNESIUM ION × 89	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	IF4G1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–28； UniProt 172–199 Author chain D； PDBConstruct 1–28； UniProt 172–199

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	1lj2
Deposition date deposition_date	2002-04-18
Structure title title	Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization
Keywords keywords	NSP3; homodimer; eIF4G; Rotavirus; translation; mRNA; closed loop; coiled coil, Viral protein- translation COMPLEX; Viral protein/ translation
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	26.38 Å
Radius of gyration Rg (electron density) rg_electron	26.01 Å
Forward intensity I(0) i0	18045800.00
Molecular weight molecular_weight	30801.0 kDa
Excluded volume excluded_volume	37733 Å³
Envelope volume envelope_volume	47979 Å³
Hydration-shell volume shell_volume	18395 Å³
Envelope diameter envelope_diameter	99.8 Å
Shell Rg shell_rg	28.19 Å
Envelope Rg envelope_rg	27.13 Å
Shape Rg shape_rg	25.81 Å
Total Rg total_rg	26.85 Å
Total atoms total_atoms	2131
Residues n_residues	265
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	100.3 Å
Rg (real space) rg_real	27.03 Å
Rg uncertainty (real space) rg_real_error	1.10 Å
I(0) (real space) i0_real	1.8050e+07
I(0) uncertainty (real space) i0_real_error	2.9830e+05
Rg (reciprocal space) rg_reciprocal	26.83 Å
I(0) (reciprocal space) i0_reciprocal	18040000.0000
Solution quality estimate total_estimate	0.7021
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	23.4 Å
Skewness Skewness skewness	0.874
Kurtosis Kurtosis kurtosis	0.290
Angular range angular_range	— – 0.3000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1954000.0000
Real-space data points n_real_points	61
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.347; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.193; Smooth: 0.890

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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	NONSTRUCTURAL RNA-BINDING PROTEIN 34
Molecular weight formula_weight	12842.4 kDa
Mutation mutation	C306S C314S
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2327

MHSLQNVIPQQQAHIAELQVYNNKLERDLQNKIGSLTSSIEWYLRSMELDPEIKADIEQQINSIDAINPLHAFDDLESVIRNLISDYDKLFLMFKGLIQRSNYQYSFGSE

来源 Source

来源生物 organism	Simian rotavirus A/SA11
NCBI Class编号 ncbi_taxonomy_id	10923
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	eukaryotic protein synthesis initiation factor
Molecular weight formula_weight	3203.7 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

APKRERKTIRIRDPNQGGKDITEEIMSG

Entity 3 Entity 3 non-polymer

Description description	GOLD ION
Molecular weight formula_weight	197.0 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	196

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1lj2a_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.13 — Rotavirus nonstructural proteins
Family Family family	h.1.13.2 — NSP3 C-terminal domain, NS34

Domain ID domain_id	d1lj2b_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.13 — Rotavirus nonstructural proteins
Family Family family	h.1.13.2 — NSP3 C-terminal domain, NS34

CATH v4.4 (2 domains)

Domain ID domain_id	1lj2A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	970 — Nonstructural RNA-binding protein

Domain ID domain_id	1lj2B00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	970 — Nonstructural RNA-binding protein

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8. Citations (1)

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Unit-cell length a length_a	59.690 Å
Unit-cell length b length_b	74.040 Å
Unit-cell length c length_c	77.460 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	2.380 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.2210
R_free r_free	0.2720

fit	/app/data/saxs_computation/lj/1lj2/1lj2.fit
pddf	/app/data/pr_computation/lj/1lj2/1lj2.pr.out
profile	/app/data/saxs_computation/lj/1lj2/1lj2.dat

Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization

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

NONSTRUCTURAL RNA-BINDING PROTEIN 34

State in the Current Structure

Other States of the Same Protein in the Database

eukaryotic protein synthesis initiation factor

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)