SAXSdb — 4c54

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

IG GAMMA-4 CHAIN C REGION

HOMO SAPIENS

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 114–327 Chain B； UniProt 114–327	Fragment：FC FRAGMENT, RESIDUES 114-327	;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 EDO 1,2-ETHANEDIOL × 9	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；MES PH6.5. 18-20% PEG 20 000	Resolution 1.90 Å R-free 0.209

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 4C54	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ADQ CRYSTAL STRUCTURE OF A HUMAN IGM RHEUMATOID FACTOR FAB IN COMPLEX WITH ITS AUTOANTIGEN IGG FC Deposited 1997-02-18	Different construct Different mutation/modification 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 118–323（206 aa） Fragment：FC	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；CRYSTALS WERE GROWN BY HANGING DROP VAPOR DIFFUSION. THE HANGING DROPS CONSISTED OF 2UL OF PROTEIN SOLUTION CONTAINING EACH PROTEIN AT 1MG/ML IN 0.1 % SODIUM AZIDE, 20MM TRIS-HCL AT PH 7.0, MIXED WITH AN EQUAL VOLUME OF THE RESERVOIR SOLUTION TO BE SCREENED. CRYSTALS WERE OBTAINED WITH RESERVOIR SOLUTIONS CONTAINING 17.5 - 22.5 % (W/V) POLYETHYLENE GLYCOL (MEAN MW 8000) IN 0.1 % SODIUM AZIDE, 100MM TRIS-HCL, PH 7.0, AT TEMPERATURES BETWEEN 17.5 AND 21.5 (CELSIUS)., vapor diffusion - hanging drop	Resolution 3.15 Å R-free 0.289
1BBJ CRYSTAL STRUCTURE OF A CHIMERIC FAB' FRAGMENT OF AN ANTIBODY BINDING TUMOUR CELLS Deposited 1992-04-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 1–98（98 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.10 Å
1BBJ CRYSTAL STRUCTURE OF A CHIMERIC FAB' FRAGMENT OF AN ANTIBODY BINDING TUMOUR CELLS Deposited 1992-04-30	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 B 1–98（98 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.10 Å
4B53 Crystal structure of the isolated IgG4 CH3 domain Deposited 2012-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 222–327（106 aa） Fragment：CH3 DOMAIN, RESIDUES 222-327 Chain B 222–327（106 aa） Fragment：CH3 DOMAIN, RESIDUES 222-327	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	EDO 1,2-ETHANEDIOL × 5 PEG DI(HYDROXYETHYL)ETHER × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；SITTING DROP AT 291K. RESERVOIR OF 100 MICROLITRE 22% PEG 3350 AND 150MM CALCIUM ACETATE. DROP SIZE 100 NANOLITRE PROTEIN AND 100 NANOLITRE RESERVOIR. PROTEIN CONCENTRATION OF 1.5MG/ML	Resolution 1.80 Å R-free 0.237
4C55 Crystal structure of serum-derived human IgG4 Fc Deposited 2013-09-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 110–327（218 aa） Fragment：FC FRAGMENT, RESIDUES 110-327	Not recorded	MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；MES PH6.5. 18-20% PEG 20 000	Resolution 2.35 Å R-free 0.238
4C55 Crystal structure of serum-derived human IgG4 Fc Deposited 2013-09-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 110–327（218 aa） Fragment：FC FRAGMENT, RESIDUES 110-327	Not recorded	MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；MES PH6.5. 18-20% PEG 20 000	Resolution 2.35 Å R-free 0.238
4D2N Crystal structure of deglycosylated serum-derived human IgG4 Fc Deposited 2014-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 102–327（226 aa） Fragment：FC FRAGMENT, RESIDUES 102-327 Chain D 102–327（226 aa） Fragment：FC FRAGMENT, RESIDUES 102-327	Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；291 K；CRYSTALS WERE GROWN AT 291K USING A RESERVOIR OF 100MM BIS-TRIS PROPANE PH7.5, 20% PEG 3350 AND 200MM SODIUM CITRATE, AND A PROTEIN CONCENTRATION OF 6MG/ML.	Resolution 2.70 Å R-free 0.254
4D2N Crystal structure of deglycosylated serum-derived human IgG4 Fc Deposited 2014-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 102–327（226 aa） Fragment：FC FRAGMENT, RESIDUES 102-327 Chain B 102–327（226 aa） Fragment：FC FRAGMENT, RESIDUES 102-327	Mutation：YES Mutation：YES	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；291 K；CRYSTALS WERE GROWN AT 291K USING A RESERVOIR OF 100MM BIS-TRIS PROPANE PH7.5, 20% PEG 3350 AND 200MM SODIUM CITRATE, AND A PROTEIN CONCENTRATION OF 6MG/ML.	Resolution 2.70 Å R-free 0.254
5HVW Monomeric IgG4 Fc Deposited 2016-01-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 115–324（210 aa）	Mutation：L351F, T366R, P395K, F405R, Y407E	ZN ZINC ION × 12 GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；9 mM ZnCl2, 90 mM Hepes, pH 7.0, 18% PEG 6000 (w/v)	Resolution 1.95 Å R-free 0.258
5HVW Monomeric IgG4 Fc Deposited 2016-01-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 115–324（210 aa）	Mutation：L351F, T366R, P395K, F405R, Y407E	ZN ZINC ION × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；9 mM ZnCl2, 90 mM Hepes, pH 7.0, 18% PEG 6000 (w/v)	Resolution 1.95 Å R-free 0.258
5LG1 Room temperature structure of human IgG4-Fc from crystals analysed in situ Deposited 2016-07-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 114–327（214 aa） Chain B 114–327（214 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；0.1M MES, 18-20% PEG 20 000	Resolution 2.70 Å R-free 0.231
5W5M Crystal structure of human IgG4-Sigma1 Fc fragment Deposited 2017-06-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 106–327（222 aa） Fragment：Sigma1 Fc fragment, UNP residues 106-327 Chain B 106–327（222 aa） Fragment：Sigma1 Fc fragment, UNP residues 106-327	Not recorded	GOL GLYCEROL × 2 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；9% (w/v) PEG 20K, 0.1 M sodium acetate, pH 5.5	Resolution 1.90 Å R-free 0.225
5W5N Crystal structure of human IgG4-Sigma2 Fc fragment Deposited 2017-06-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 106–327（222 aa） Fragment：Sigma2 Fc fragment, UNP residues 106-327 Chain B 106–327（222 aa） Fragment：Sigma2 Fc fragment, UNP residues 106-327	Not recorded	GOL GLYCEROL × 2 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；10% (w/v) PEG 20K, 0.1 M sodium acetate, 5.5, 5% (v/v) MPD	Resolution 1.85 Å R-free 0.215
6WIB Next generation monomeric IgG4 Fc Deposited 2020-04-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 115–325（211 aa）	Mutation：L351F, T366R, P395K, F405R, Y407e, L432C, H433S, N434W, Y436L, T437C, Q438 deleted	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；298 K；0.01 M zinc sulfate heptahydrate; 0.1 M morpholineethanesulfonic acid (MES) monohydrate, pH 6.5, and 25% (w/v) PEG 550 MME at a protein concentration of 5.5 mg/mL	Resolution 2.55 Å R-free 0.266
6WMH Next generation monomeric IgG4 Fc Deposited 2020-04-21	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 H 118–324（207 aa） Fragment：domains Ch2 and Ch3	Mutation：M252Y, S254T, T256E, N297D, L351F, S354E, T366R, P395K, F405R, Y407E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；295 K；DL-Glutamic acid monohydrate, DL-Alanine, Glycine, DL-Lysine monohydrochloride, DL-Serine, Sodium HEPES, MOPS (acid), Ethylene glycol, PEG 8000	Resolution 2.30 Å R-free 0.243
6WMH Next generation monomeric IgG4 Fc Deposited 2020-04-21	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 A 118–324（207 aa） Fragment：domains Ch2 and Ch3	Mutation：M252Y, S254T, T256E, N297D, L351F, S354E, T366R, P395K, F405R, Y407E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；295 K；DL-Glutamic acid monohydrate, DL-Alanine, Glycine, DL-Lysine monohydrochloride, DL-Serine, Sodium HEPES, MOPS (acid), Ethylene glycol, PEG 8000	Resolution 2.30 Å R-free 0.243
6WNA Next generation monomeric IgG4 Fc Deposited 2020-04-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain H 118–324（207 aa） Fragment：domains Ch2 and Ch3	Mutation：M252Y, S254T, T256E, L351F, S354E, T366R, P395K, F405R, Y407E,	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；0.2 M magnesium chloride hexahydrate, 30% 1,5-diaminopentane dihydrochloride, 0.1 M MES, pH 6 and 20% PEG 6000 at a protein concentration of 6 mg/mL	Resolution 2.40 Å R-free 0.263
6WOL Next generation monomeric IgG4 Fc bound to neonatal Fc receptor Deposited 2020-04-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain H 117–326（210 aa） Fragment：domains Ch3 and Ch4	Mutation：L351F, S354E, T366R, P395K, F405R, Y407E, L432C, H433S, N434Y, Y436L, T437C, Q438 deleted	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6；295 K；0.2 M magnesium chloride hexahydrate, 1 M sodium iodide, 0.1 M MES, pH 6 and 20% PEG 6000 at a protein concentration of 6.35 mg/mL	Resolution 2.49 Å R-free 0.270

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

View Construct and Data Evidence

UniProt name	IGHG4_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–214； UniProt 114–327 Author chain B； PDBConstruct 1–214； UniProt 114–327

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	4c54
Deposition date deposition_date	2013-09-10
Structure title title	Crystal structure of recombinant human IgG4 Fc
Keywords keywords	IMMUNE SYSTEM, IMMUNOGLOBULIN, IGG1; IMMUNE SYSTEM
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	26.48 Å
Radius of gyration Rg (electron density) rg_electron	25.22 Å
Forward intensity I(0) i0	43315900.00
Molecular weight molecular_weight	50629.0 kDa
Excluded volume excluded_volume	63150 Å³
Envelope volume envelope_volume	81512 Å³
Hydration-shell volume shell_volume	26833 Å³
Envelope diameter envelope_diameter	80.1 Å
Shell Rg shell_rg	32.61 Å
Envelope Rg envelope_rg	24.80 Å
Shape Rg shape_rg	25.23 Å
Total Rg total_rg	26.03 Å
Total atoms total_atoms	3557
Residues n_residues	419
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	79.4 Å
Rg (real space) rg_real	26.33 Å
Rg uncertainty (real space) rg_real_error	0.52 Å
I(0) (real space) i0_real	4.3320e+07
I(0) uncertainty (real space) i0_real_error	5.6460e+05
Rg (reciprocal space) rg_reciprocal	26.38 Å
I(0) (reciprocal space) i0_reciprocal	43320000.0000
Solution quality estimate total_estimate	0.9149
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	37.1 Å
Skewness Skewness skewness	0.044
Kurtosis Kurtosis kurtosis	-0.659
Angular range angular_range	— – 0.3000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7260000.0000
Real-space data points n_real_points	61
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.970; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.985

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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	IG GAMMA-4 CHAIN C REGION
Molecular weight formula_weight	24248.3 kDa
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	3908

FLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGK

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	HOMO SAPIENS

Entity 2 Entity 2 branched

Description description	;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	1463.3 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	2-(N-MORPHOLINO)-ETHANESULFONIC ACID
Molecular weight formula_weight	195.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	290

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7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	4c54A01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	4c54A02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	4c54B01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	4c54B02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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8. Citations (1)

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Unit-cell length a length_a	74.837 Å
Unit-cell length b length_b	78.973 Å
Unit-cell length c length_c	97.881 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	48.941 Å
R factor r_factor	0.1720
R_work r_work	0.1701
R_free r_free	0.2086

fit	/app/data/saxs_computation/c5/4c54/4c54.fit
pddf	/app/data/pr_computation/c5/4c54/4c54.pr.out
profile	/app/data/saxs_computation/c5/4c54/4c54.dat

Crystal structure of recombinant human IgG4 Fc

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

IG GAMMA-4 CHAIN C REGION

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