SAXSdb — 2dlf

▼

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

PROTEIN (ANTI-DANSYL IMMUNOGLOBULIN IGG2A(S)-KAPPA (LIGHT CHAIN))

OrganismNot specified

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain L； UniProt 1–113	Fragment：FV FRAGMENT (VL DOMAIN) SYNONYM: ANTI-DANSYL FV FRAGMENT	PROTEIN (ANTI-DANSYL IMMUNOGLOBULIN IGG2A(S) (HEAVY CHAIN)) × 1 （P01801） SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.75；CRYSTALLIZATION CONDITIONS: TEMPERATURE AT 20C. PRECIPITANT SOLUTION CONTAINED 1 AMMONIUM SULFATE AND 0.025 M SODIUM CACODYLATE (PH 6.75). 5 MG/ML OF FV FRAGMENT., VAPOR DIFFUSION, HANGING DROP	Resolution 1.55 Å R-free 0.233

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 2DLF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BFV MONOCLONAL ANTIBODY FRAGMENT FV4155 FROM E. COLI Deposited 1997-05-27	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 1–113（113 aa） Fragment：MONOCLONAL ANTIBODY FV FRAGMENT	Not recorded	ZN ZINC ION × 3 STG ESTRIOL 3-(B-D-GLUCURONIDE) × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；PROTEIN WAS CRYSTALLIZED FROM 18% (W/V) PEG 8000, 200MM ZN ACETATE AND 100MM NA CACODYLATE, PH 7.5	Resolution 2.10 Å R-free 0.271
1BFV MONOCLONAL ANTIBODY FRAGMENT FV4155 FROM E. COLI Deposited 1997-05-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain L 1–113（113 aa） Fragment：MONOCLONAL ANTIBODY FV FRAGMENT	Not recorded	ZN ZINC ION × 6 STG ESTRIOL 3-(B-D-GLUCURONIDE) × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；PROTEIN WAS CRYSTALLIZED FROM 18% (W/V) PEG 8000, 200MM ZN ACETATE AND 100MM NA CACODYLATE, PH 7.5	Resolution 2.10 Å R-free 0.271
1BFV MONOCLONAL ANTIBODY FRAGMENT FV4155 FROM E. COLI Deposited 1997-05-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain L 1–113（113 aa） Fragment：MONOCLONAL ANTIBODY FV FRAGMENT	Not recorded	ZN ZINC ION × 6 STG ESTRIOL 3-(B-D-GLUCURONIDE) × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；PROTEIN WAS CRYSTALLIZED FROM 18% (W/V) PEG 8000, 200MM ZN ACETATE AND 100MM NA CACODYLATE, PH 7.5	Resolution 2.10 Å R-free 0.271
1BFV MONOCLONAL ANTIBODY FRAGMENT FV4155 FROM E. COLI Deposited 1997-05-27	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 1–113（113 aa） Fragment：MONOCLONAL ANTIBODY FV FRAGMENT	Not recorded	ZN ZINC ION × 3 STG ESTRIOL 3-(B-D-GLUCURONIDE) × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；PROTEIN WAS CRYSTALLIZED FROM 18% (W/V) PEG 8000, 200MM ZN ACETATE AND 100MM NA CACODYLATE, PH 7.5	Resolution 2.10 Å R-free 0.271
1CFV MONOCLONAL ANTIBODY FRAGMENT FV4155 FROM E. COLI Deposited 1997-04-11	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 1–113（113 aa） Fragment：FV FRAGMENT	Not recorded	ZN ZINC ION × 3 E3G ESTRONE BETA-D-GLUCURONIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；PROTEIN WAS CRYSTALLIZED FROM 18% (W/V) PEG 8000, 200MM ZN ACETATE AND 100MM NA CACODYLATE, PH 7.0	Resolution 2.10 Å R-free 0.247
1MAJ SOLUTION STRUCTURE OF AN ISOLATED ANTIBODY VL DOMAIN Deposited 1993-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–113（113 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1MAK SOLUTION STRUCTURE OF AN ISOLATED ANTIBODY VL DOMAIN Deposited 1993-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–113（113 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1SVZ Crystal structure of the single-chain Fv fragment 1696 in complex with the epitope peptide corresponding to N-terminus of HIV-2 protease Deposited 2004-03-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 4–112（109 aa） Fragment：scFv1696 Chain B 4–112（109 aa） Fragment：scFv1696	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；292 K；protein concentration 14mg/ml, 0.05M tri-sodium citrate, 0.1M sodium phosphate, 27% PEG 3400, 0.2M ammonium sulfate, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.89 Å R-free 0.239
2BFV MONOCLONAL ANTIBODY FRAGMENT FV4155 FROM E. COLI Deposited 1997-05-27	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 1–113（113 aa） Fragment：MONOCLONAL ANTIBODY FV FRAGMENT	Not recorded	STG ESTRIOL 3-(B-D-GLUCURONIDE) × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PROTEIN WAS CRYSTALLIZED FROM 15% (W/V) PEG 4000, 100MM NA ACETATE AND 50MM TRIS HCL PH 8.5	Resolution 2.50 Å

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

View Construct and Data Evidence

UniProt name	KV2G_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain L； PDBConstruct 1–113； UniProt 1–113

PROTEIN (ANTI-DANSYL IMMUNOGLOBULIN IGG2A(S) (HEAVY CHAIN))

OrganismNot specified

UniProt P01801

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 1–115	Fragment：FV FRAGMENT (VH DOMAIN) SYNONYM: ANTI-DANSYL FV FRAGMENT	PROTEIN (ANTI-DANSYL IMMUNOGLOBULIN IGG2A(S)-KAPPA (LIGHT CHAIN)) × 1 （P01631） SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.75；CRYSTALLIZATION CONDITIONS: TEMPERATURE AT 20C. PRECIPITANT SOLUTION CONTAINED 1 AMMONIUM SULFATE AND 0.025 M SODIUM CACODYLATE (PH 6.75). 5 MG/ML OF FV FRAGMENT., VAPOR DIFFUSION, HANGING DROP	Resolution 1.55 Å R-free 0.233

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 2DLF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1SM3 CRYSTAL STRUCTURE OF THE TUMOR SPECIFIC ANTIBODY SM3 COMPLEX WITH ITS PEPTIDE EPITOPE Deposited 1997-12-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain H 2–220（219 aa） Fragment：FAB FRAGMENT	Not recorded	CD CADMIUM ION × 8 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 1.95 Å R-free 0.283
5A2I Crystal structure of scFv-SM3 in complex with APD-SGalNAc-RP Deposited 2015-05-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 6–115（110 aa） Fragment：RESIDUES 6-115,20-129	Not recorded	EDO 1,2-ETHANEDIOL × 2 A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.88 Å R-free 0.261
5A2J Crystal structure of scFv-SM3 in complex with the naked peptide APDTRP Deposited 2015-05-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 6–115（110 aa） Fragment：RESIDUES 6-115,20-129	Not recorded	EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.65 Å R-free 0.197
5A2K Crystal structure of scFv-SM3 in complex with APD-TGalNAc-RP Deposited 2015-05-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 6–115（110 aa） Fragment：RESIDUES 6-115,20-129	Not recorded	EDO 1,2-ETHANEDIOL × 6 A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.70 Å R-free 0.216
5A2L Crystal structure of scFv-SM3 in complex with APD-CGalNAc-RP Deposited 2015-05-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 6–115（110 aa） Fragment：RESIDUES 6-115,20-129	Not recorded	EDO 1,2-ETHANEDIOL × 4 A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.79 Å R-free 0.204
5N7B Understanding the singular conformational landscape of the Tn antigens: Sulfur-for- oxygen substitution in the glycosidic linkage provides new insights into molecular recognition by an antibody Deposited 2017-02-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 1–114（114 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 7 A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；20% PEG 3350, 0.2 M disodium hydrogen phosphate	Resolution 1.70 Å R-free 0.211
5OWP Crystal structure of glycopeptide "GVTSAfPDT*RPAP" in complex with scFv-SM3 Deposited 2017-09-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 6–111（106 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 3 A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；PEG 3350, disodium hydrogen phosphate	Resolution 1.85 Å R-free 0.256

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HV32_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain H； PDBConstruct 1–121； UniProt 1–115

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	2dlf
Deposition date deposition_date	1998-12-17
Structure title title	HIGH RESOLUTION CRYSTAL STRUCTURE OF THE FV FRAGMENT FROM AN ANTI-DANSYL SWITCH VARIANT ANTIBODY IGG2A(S) CRYSTALLIZED AT PH 6.75
Keywords keywords	FV FRAGMENT, IMMUNOGLOBULIN, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	19.15 Å
Radius of gyration Rg (electron density) rg_electron	17.95 Å
Forward intensity I(0) i0	12786400.00
Molecular weight molecular_weight	26235.0 kDa
Excluded volume excluded_volume	32577 Å³
Envelope volume envelope_volume	37024 Å³
Hydration-shell volume shell_volume	17496 Å³
Envelope diameter envelope_diameter	64.9 Å
Shell Rg shell_rg	23.87 Å
Envelope Rg envelope_rg	18.20 Å
Shape Rg shape_rg	17.88 Å
Total Rg total_rg	19.03 Å
Total atoms total_atoms	1847
Residues n_residues	220
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

▼

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

Maximum dimension Dmax dmax	64.8 Å
Rg (real space) rg_real	19.08 Å
Rg uncertainty (real space) rg_real_error	0.44 Å
I(0) (real space) i0_real	1.2790e+07
I(0) uncertainty (real space) i0_real_error	1.5760e+05
Rg (reciprocal space) rg_reciprocal	19.09 Å
I(0) (reciprocal space) i0_reciprocal	12790000.0000
Solution quality estimate total_estimate	0.6929
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.3 Å
Skewness Skewness skewness	0.222
Kurtosis Kurtosis kurtosis	-0.403
Angular range angular_range	— – 0.4150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3622000.0000
Real-space data points n_real_points	73
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.825; Stabil: 1.000; Sysdev: 0.182; Positv: 1.000; Valcen: 0.987; Smooth: 0.994

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	PROTEIN (ANTI-DANSYL IMMUNOGLOBULIN IGG2A(S)-KAPPA (LIGHT CHAIN))
Molecular weight formula_weight	12386.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L
Atom count atom_count	2282

DVVMTQTPLSLPVSLGNQASISCRSSQSLVHSNGNTYLHWYLQKPGQSPKLLIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQSTHVPFTFGSGTKLEIKR

Entity 2 Entity 2 polymer

Description description	PROTEIN (ANTI-DANSYL IMMUNOGLOBULIN IGG2A(S) (HEAVY CHAIN))
Molecular weight formula_weight	14152.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

EVKLEESGGGLVQPGGSMKLSCATSGFTFSDAWMDWVRQSPEKGLEWVAEIRNKANNHATYYAESVKGRFTISRDDSKRRVYLQMNTLRAEDTGIYYCTGIYYHYPWFAYWGQGTLVTVSAEPR

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	400

▼

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2dlfh_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d2dlfl_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

CATH v4.4 (2 domains)

Domain ID domain_id	2dlfH00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	2dlfL00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

▶

8. Citations (8)

;The pH-dependent structural variation of complementarity-determining region H3 in the crystal structures of the Fv fragment from an anti-dansyl monoclonal antibody. ;

J.Mol.Biol. (1999)

PMID: 10438610 · DOI: 10.1006/jmbi.1999.2931 PRIMARY

;Role of the Domain-Domain Interaction in the Construction of the Antigen Combining Site. A Comparative Study by 1H-15N Shift Correlation NMR Spectroscopy of the Fv and Fab Fragment of Anti-Dansyl Mouse Monoclonal Antibody ;

J.Mol.Biol. (1994)

Dynamical Structure of the Antibody Combining Site as Studied by 1H-15N Shift Correlation NMR Spectroscopy

Biochemistry (1992)

;Isotope-Edited Nuclear Magnetic Resonance Study of Fv Fragment of an Anti- Dansyl Mouse Monoclonal Antibody: Recognition of the Dansyl Hapten ;

Biochemistry (1992)

;Preparation of the Fv Fragment from a Short-Chain Mouse IgG2a Anti-Dansyl Monoclonal Antibody and Use of Selectively Deuterated Fv Analogues for Two- Dimensional 1H NMR Analyses of Antigen-Antibody Interactions ;

Biochemistry (1991)

Multinuclear NMR Study of the Structure of the Fv Fragment of Anti-Dansyl Mouse IgG2a Antibody

Biochemistry (1991)

Conformation and Stereoselective Reduction of Hapten Side Chain in the Antibody Combining Site

J.Am.Chem.Soc. (1991)

Structure of a Mouse Immunoglobulin G that Lacks the Entire CH1 Domain: Protein Sequencing and Small-Angle X-Ray Scattering Studies

Biochemistry (1990)

▶

Unit-cell length a length_a	57.290 Å
Unit-cell length b length_b	66.930 Å
Unit-cell length c length_c	53.630 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	4

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

Resolution resolution	1.550 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1840
R_work r_work	0.1840
R_free r_free	0.2330

fit	/app/data/saxs_computation/dl/2dlf/2dlf.fit
pddf	/app/data/pr_computation/dl/2dlf/2dlf.pr.out
profile	/app/data/saxs_computation/dl/2dlf/2dlf.dat

HIGH RESOLUTION CRYSTAL STRUCTURE OF THE FV FRAGMENT FROM AN ANTI-DANSYL SWITCH VARIANT ANTIBODY IGG2A(S) CRYSTALLIZED AT PH 6.75

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

PROTEIN (ANTI-DANSYL IMMUNOGLOBULIN IGG2A(S)-KAPPA (LIGHT CHAIN))

State in the Current Structure

Other States of the Same Protein in the Database

PROTEIN (ANTI-DANSYL IMMUNOGLOBULIN IGG2A(S) (HEAVY 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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

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 (8)

9. Files and Curves (10)

Files (7)

Curves (3)