SAXSdb — 1a6u

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

B1-8 FV (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 21–128	Fragment：FV FRAGMENT	B1-8 FV (HEAVY CHAIN) × 1 （P01751）	X-RAY DIFFRACTION X-ray crystallization conditions：CRYSTALS WERE GROWN USING AMMONIUM SULFATE AS PRECIPITANT.	Resolution 2.10 Å

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 1A6U	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A6V B1-8 FV fragment complexed with a (4-hydroxy-3-nitrophenyl) acetate compound Deposited 1998-03-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 20–128（109 aa） Fragment：FV FRAGMENT	Not recorded	NPC 4-HYDROXY-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions CRYSTALS WERE GROWN USING AMMONIUM SULPHATE AS PRECIPITANT	Resolution 1.80 Å
1A6V B1-8 FV fragment complexed with a (4-hydroxy-3-nitrophenyl) acetate compound Deposited 1998-03-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain M 20–128（109 aa） Fragment：FV FRAGMENT	Not recorded	NPC 4-HYDROXY-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions CRYSTALS WERE GROWN USING AMMONIUM SULPHATE AS PRECIPITANT	Resolution 1.80 Å
1A6V B1-8 FV fragment complexed with a (4-hydroxy-3-nitrophenyl) acetate compound Deposited 1998-03-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain N 20–128（109 aa） Fragment：FV FRAGMENT	Not recorded	NPC 4-HYDROXY-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions CRYSTALS WERE GROWN USING AMMONIUM SULPHATE AS PRECIPITANT	Resolution 1.80 Å
1A6W B1-8 FV FRAGMENT COMPLEXED WITH A (4-HYDROXY-5-IODO-3-NITROPHENYL) ACETATE COMPOUND Deposited 1998-03-03	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 21–128（108 aa） Fragment：FV FRAGMENT	Not recorded	NIP 4-HYDROXY-5-IODO-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions dialysis；THE PURIFIED PROTEIN HAS BEEN DIALYSED INTO A 10 MM TRIS-HCL PH 7.5 BUFFER ALSO CONTAINING 20 MM NACL. PEG 1550 WAS USED AS PRECIPITANT., dialysis	Resolution 2.00 Å
1Q0Y Anti-Morphine Antibody 9B1 Complexed with Morphine Deposited 2003-07-17	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 21–129（109 aa）	Not recorded	SO4 SULFATE ION × 2 MOI (7R,7AS,12BS)-3-METHYL-2,3,4,4A,7,7A-HEXAHYDRO-1H-4,12-METHANO[1]BENZOFURO[3,2-E]ISOQUINOLINE-7,9-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；298 K；22% PEG MME 2000, 0.2M ammonium sulfate, 0.1M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 4.60	Resolution 2.00 Å R-free 0.239

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	LV1B_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain L； PDBConstruct 1–108； UniProt 21–128

B1-8 FV (HEAVY CHAIN)

OrganismNot specified

UniProt P01751

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 20–139	Fragment：FV FRAGMENT	B1-8 FV (LIGHT CHAIN) × 1 （P01724）	X-RAY DIFFRACTION X-ray crystallization conditions：CRYSTALS WERE GROWN USING AMMONIUM SULFATE AS PRECIPITANT.	Resolution 2.10 Å

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 1A6U	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A6V B1-8 FV fragment complexed with a (4-hydroxy-3-nitrophenyl) acetate compound Deposited 1998-03-03	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 20–139（120 aa） Fragment：FV FRAGMENT	Not recorded	NPC 4-HYDROXY-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions CRYSTALS WERE GROWN USING AMMONIUM SULPHATE AS PRECIPITANT	Resolution 1.80 Å
1A6V B1-8 FV fragment complexed with a (4-hydroxy-3-nitrophenyl) acetate compound Deposited 1998-03-03	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 20–139（120 aa） Fragment：FV FRAGMENT	Not recorded	NPC 4-HYDROXY-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions CRYSTALS WERE GROWN USING AMMONIUM SULPHATE AS PRECIPITANT	Resolution 1.80 Å
1A6V B1-8 FV fragment complexed with a (4-hydroxy-3-nitrophenyl) acetate compound Deposited 1998-03-03	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain J 20–139（120 aa） Fragment：FV FRAGMENT	Not recorded	NPC 4-HYDROXY-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions CRYSTALS WERE GROWN USING AMMONIUM SULPHATE AS PRECIPITANT	Resolution 1.80 Å
1A6W B1-8 FV FRAGMENT COMPLEXED WITH A (4-HYDROXY-5-IODO-3-NITROPHENYL) ACETATE COMPOUND Deposited 1998-03-03	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 20–139（120 aa） Fragment：FV FRAGMENT	Not recorded	NIP 4-HYDROXY-5-IODO-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions dialysis；THE PURIFIED PROTEIN HAS BEEN DIALYSED INTO A 10 MM TRIS-HCL PH 7.5 BUFFER ALSO CONTAINING 20 MM NACL. PEG 1550 WAS USED AS PRECIPITANT., dialysis	Resolution 2.00 Å
1NGP N1G9 (IGG1-LAMBDA) FAB FRAGMENT COMPLEXED WITH (4-HYDROXY-3-NITROPHENYL) ACETATE Deposited 1995-06-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 20–244（225 aa） Fragment：FAB FRAGMENT	Not recorded	SO4 SULFATE ION × 1 NPA 2-(4-HYDROXY-3-NITROPHENYL)ACETIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.40 Å R-free 0.250
1NGQ N1G9 (IGG1-LAMBDA) FAB FRAGMENT Deposited 1995-06-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 20–244（225 aa） Fragment：FAB FRAGMENT	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.40 Å R-free 0.254
1NQB TRIVALENT ANTIBODY FRAGMENT Deposited 1997-04-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 20–139（120 aa） Fragment：VH DOMAIN RESIDUES 2 - 120, VL DOMAIN RESIDUES 121 - 233 Chain C 20–139（120 aa） Fragment：VH DOMAIN RESIDUES 2 - 120, VL DOMAIN RESIDUES 121 - 233	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；30% 2-PROPANOL, 0.2M NA CITRATE, 0.1M NA CACODYLATE PH 6.5	Resolution 2.00 Å R-free 0.230
1NQB TRIVALENT ANTIBODY FRAGMENT Deposited 1997-04-04	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 20–139（120 aa） Fragment：VH DOMAIN RESIDUES 2 - 120, VL DOMAIN RESIDUES 121 - 233	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；30% 2-PROPANOL, 0.2M NA CITRATE, 0.1M NA CACODYLATE PH 6.5	Resolution 2.00 Å R-free 0.230
1NQB TRIVALENT ANTIBODY FRAGMENT Deposited 1997-04-04	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain C 20–139（120 aa） Fragment：VH DOMAIN RESIDUES 2 - 120, VL DOMAIN RESIDUES 121 - 233	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；30% 2-PROPANOL, 0.2M NA CITRATE, 0.1M NA CACODYLATE PH 6.5	Resolution 2.00 Å R-free 0.230

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

View Construct and Data Evidence

UniProt name	HV07_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain H； PDBConstruct 1–120； UniProt 20–139

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	1a6u
Deposition date deposition_date	1998-03-03
Structure title title	B1-8 FV FRAGMENT
Keywords keywords	IMMUNOGLOBULIN; IMMUNOGLOBULIN
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	18.26 Å
Radius of gyration Rg (electron density) rg_electron	17.27 Å
Forward intensity I(0) i0	11044000.00
Molecular weight molecular_weight	24503.0 kDa
Excluded volume excluded_volume	30509 Å³
Envelope volume envelope_volume	34610 Å³
Hydration-shell volume shell_volume	16978 Å³
Envelope diameter envelope_diameter	56.5 Å
Shell Rg shell_rg	23.14 Å
Envelope Rg envelope_rg	17.44 Å
Shape Rg shape_rg	17.21 Å
Total Rg total_rg	18.37 Å
Total atoms total_atoms	1730
Residues n_residues	228
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	56.6 Å
Rg (real space) rg_real	18.17 Å
Rg uncertainty (real space) rg_real_error	0.24 Å
I(0) (real space) i0_real	1.1040e+07
I(0) uncertainty (real space) i0_real_error	1.2590e+05
Rg (reciprocal space) rg_reciprocal	18.19 Å
I(0) (reciprocal space) i0_reciprocal	11040000.0000
Solution quality estimate total_estimate	0.9013
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	23.7 Å
Skewness Skewness skewness	0.203
Kurtosis Kurtosis kurtosis	-0.410
Angular range angular_range	— – 0.4350 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3482000.0000
Real-space data points n_real_points	75
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.967

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	B1-8 FV (LIGHT CHAIN)
Molecular weight formula_weight	11374.6 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	1892

AVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGVPARFSGSLIGNKAALTITGAQTEDEAIYFCALWYSNHWVFGGGTKLTVL

Entity 2 Entity 2 polymer

Description description	B1-8 FV (HEAVY CHAIN)
Molecular weight formula_weight	13440.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

QVQLQQPGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNSGGTKYNEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARYDYYGSSYFDYWGQGTTVTVSS

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	156

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1a6uh_
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	d1a6ul_
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	1a6uH00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1a6uL00
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 (2)

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Unit-cell length a length_a	72.030 Å
Unit-cell length b length_b	85.780 Å
Unit-cell length c length_c	37.420 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	2.100 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	—
R_work r_work	0.1920
R_free r_free	—

fit	/app/data/saxs_computation/a6/1a6u/1a6u.fit
pddf	/app/data/pr_computation/a6/1a6u/1a6u.pr.out
profile	/app/data/saxs_computation/a6/1a6u/1a6u.dat

B1-8 FV FRAGMENT

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

B1-8 FV (LIGHT CHAIN)

State in the Current Structure

Other States of the Same Protein in the Database

B1-8 FV (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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 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)