1b2w

COMPARISON OF THE THREE-DIMENSIONAL STRUCTURES OF A HUMANIZED AND A CHIMERIC FAB OF AN ANTI-GAMMA-INTERFERON ANTIBODY

Method: X-RAY DIFFRACTION Dmax: 80.0 Å Quality: EXCELLENT

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

No usable UniProt protein identity is available for this entry.

七张关系表仍保留该条目的 assembly 与组成信息,但缺少统一蛋白身份时,不能可靠建立跨 PDB 的同蛋白Chain接。

Assembly Composition of the Current Entry

Assembly Oligomeric State 实体与Construct证据 Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer 蛋白 2 / DNA 0 / RNA 0 / 其他Polymer 0 PDB declaration: dimeric Entity 1:PROTEIN (ANTIBODY (LIGHT CHAIN)) × 1 Entity 2:PROTEIN (ANTIBODY (HEAVY CHAIN)) × 1 缺少 UniProt 身份时不显示参考序列区间 Entity 1Fragment:V DOMAIN AND C DOMAIN Entity 2Fragment:V DOMAIN AND C DOMAIN Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.2;6.6% PEG 8000(W/V), IN 0.05 M NACL AND 0.05% SODIUM AZIDE., pH 6.2 Resolution 2.90 Å R-free 0.330

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1b2w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b2w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b2w
Deposition date deposition_date1998-12-01
Structure title titleCOMPARISON OF THE THREE-DIMENSIONAL STRUCTURES OF A HUMANIZED AND A CHIMERIC FAB OF AN ANTI-GAMMA-INTERFERON ANTIBODY
Keywords keywordsANTIBODY ENGINEERING, HUMANIZED AND CHIMERIC ANTIBODY, FAB, THREE-DIMENSIONAL STRYCTURE, GAMMA-INTERFERON, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.69
Radius of gyration Rg (electron density) rg_electron24.73
Forward intensity I(0) i037868900.00
Molecular weight molecular_weight47193.0 kDa
Excluded volume excluded_volume58813 ų
Envelope volume envelope_volume71822 ų
Hydration-shell volume shell_volume24399 ų
Envelope diameter envelope_diameter80.4
Shell Rg shell_rg31.79
Envelope Rg envelope_rg24.27
Shape Rg shape_rg24.71
Total Rg total_rg25.60
Total atoms total_atoms3325
Residues n_residues433
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax80.0
Rg (real space) rg_real25.66
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real3.7870e+07
I(0) uncertainty (real space) i0_real_error5.4160e+05
Rg (reciprocal space) rg_reciprocal25.67
I(0) (reciprocal space) i0_reciprocal37870000.0000
Solution quality estimate total_estimate0.9104
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.4
Skewness Skewness skewness0.239
Kurtosis Kurtosis kurtosis-0.586
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha5841000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.968; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1b2wh1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd1b2wh2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd1b2wl1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd1b2wl2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (4 domains)

Domain ID domain_id1b2wH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1b2wH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1b2wL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1b2wL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)