SAXSdb — 1ngq

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

N1G9 (IGG1-LAMBDA)

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 H； UniProt 20–244	Fragment：FAB FRAGMENT	N1G9 (IGG1-LAMBDA) × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.40 Å R-free 0.254

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 1NGQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A6U B1-8 FV FRAGMENT 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 H 20–139（120 aa） Fragment：FV FRAGMENT	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions CRYSTALS WERE GROWN USING AMMONIUM SULFATE AS PRECIPITANT.	Resolution 2.10 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 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 construct 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 construct 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 construct 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 ligand/ion 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
1NQB TRIVALENT ANTIBODY FRAGMENT Deposited 1997-04-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion 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 ligand/ion 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 ligand/ion 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 1–222； UniProt 20–244

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	1ngq
Deposition date deposition_date	1995-06-23
Structure title title	N1G9 (IGG1-LAMBDA) FAB 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	24.56 Å
Radius of gyration Rg (electron density) rg_electron	23.60 Å
Forward intensity I(0) i0	35422800.00
Molecular weight molecular_weight	45708.0 kDa
Excluded volume excluded_volume	57005 Å³
Envelope volume envelope_volume	70026 Å³
Hydration-shell volume shell_volume	24835 Å³
Envelope diameter envelope_diameter	76.2 Å
Shell Rg shell_rg	30.52 Å
Envelope Rg envelope_rg	23.38 Å
Shape Rg shape_rg	23.60 Å
Total Rg total_rg	24.43 Å
Total atoms total_atoms	3221
Residues n_residues	426
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	75.4 Å
Rg (real space) rg_real	24.50 Å
Rg uncertainty (real space) rg_real_error	0.44 Å
I(0) (real space) i0_real	3.5420e+07
I(0) uncertainty (real space) i0_real_error	4.6120e+05
Rg (reciprocal space) rg_reciprocal	24.52 Å
I(0) (reciprocal space) i0_reciprocal	35420000.0000
Solution quality estimate total_estimate	0.9138
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	28.7 Å
Skewness Skewness skewness	0.230
Kurtosis Kurtosis kurtosis	-0.545
Angular range angular_range	— – 0.3250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7857000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.969; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.971

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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	N1G9 (IGG1-LAMBDA)
Molecular weight formula_weight	23129.6 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	3369

QAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGVPARFSGSLIGDKAALTITGAQTEDEAIYFCALWYSNHWVFGGGTKLTVLGQPKSSPSVTLFPPSSEELETNKATLVCTITDFYPGVVTVDWKVDGTPVTQGMETTQPSKQSNNKYMASSYLTLTARAWERHSSYSCQVTHEGHTVEKSLSRADCS

Entity 2 Entity 2 polymer

Description description	N1G9 (IGG1-LAMBDA)
Molecular weight formula_weight	24082.0 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

QVQLQQPGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNSGGTKYNEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARYDYYGSSYFDYWGQGTTLTVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPWPSETVTCNVAHPASSTKVDKKIVPRDC

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	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	140

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1ngqh1
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	d1ngqh2
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.1.1.2 — C1 set domains (antibody constant domain-like)

Domain ID domain_id	d1ngql1
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	d1ngql2
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.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (4 domains)

Domain ID domain_id	1ngqH01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1ngqH02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1ngqL01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1ngqL02
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 (4)

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Unit-cell length a length_a	109.885 Å
Unit-cell length b length_b	109.885 Å
Unit-cell length c length_c	97.959 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 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	—
R_work r_work	0.1940
R_free r_free	0.2540

fit	/app/data/saxs_computation/ng/1ngq/1ngq.fit
pddf	/app/data/pr_computation/ng/1ngq/1ngq.pr.out
profile	/app/data/saxs_computation/ng/1ngq/1ngq.dat

N1G9 (IGG1-LAMBDA) FAB FRAGMENT

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

N1G9 (IGG1-LAMBDA)

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

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) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (4)

9. Files and Curves (10)

Files (7)

Curves (3)