SAXSdb — 1f58

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

Envelope glycoprotein gp120

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain P； UniProt 306–328	Fragment：RESIDUES 308-332 FROM HIV-1 GP120 Non-standard monomer：Yes (specific site not provided by mmCIF)	PROTEIN (IGG1 ANTIBODY 58.2 (LIGHT CHAIN)) × 1 PROTEIN (IGG1 ANTIBODY 58.2 (HEAVY CHAIN)) × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.3；pH 6.3	Resolution 2.00 Å R-free 0.256

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 1F58	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ACY CRYSTAL STRUCTURE OF THE PRINCIPAL NEUTRALIZING SITE OF HIV-1 Deposited 1994-02-10	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain P 306–328（23 aa） Fragment：FRAGMENT (RESIDUES 308 - 332)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.00 Å
1AI1 HIV-1 V3 LOOP MIMIC Deposited 1996-11-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain P 306–328（23 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 2.80 Å
1K5M Crystal Structure of a Human Rhinovirus Type 14:Human Immunodeficiency Virus Type 1 V3 Loop Chimeric Virus MN-III-2 Deposited 2001-10-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 240 PDB declaration: 240-MERIC	Chain B 314–325（12 aa）	Not recorded	SPH SPHINGOSINE × 60	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；1.5 M ammonium formate and 0.15 M sodium HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.70 Å
1K5M Crystal Structure of a Human Rhinovirus Type 14:Human Immunodeficiency Virus Type 1 V3 Loop Chimeric Virus MN-III-2 Deposited 2001-10-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 314–325（12 aa）	Not recorded	SPH SPHINGOSINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；1.5 M ammonium formate and 0.15 M sodium HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.70 Å
1K5M Crystal Structure of a Human Rhinovirus Type 14:Human Immunodeficiency Virus Type 1 V3 Loop Chimeric Virus MN-III-2 Deposited 2001-10-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 20 PDB declaration: eicosameric	Chain B 314–325（12 aa）	Not recorded	SPH SPHINGOSINE × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；1.5 M ammonium formate and 0.15 M sodium HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.70 Å
1K5M Crystal Structure of a Human Rhinovirus Type 14:Human Immunodeficiency Virus Type 1 V3 Loop Chimeric Virus MN-III-2 Deposited 2001-10-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Insufficient information Heteromer；Protein × 24 PDB declaration: 24-meric	Chain B 314–325（12 aa）	Not recorded	SPH SPHINGOSINE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；1.5 M ammonium formate and 0.15 M sodium HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.70 Å
1K5M Crystal Structure of a Human Rhinovirus Type 14:Human Immunodeficiency Virus Type 1 V3 Loop Chimeric Virus MN-III-2 Deposited 2001-10-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 314–325（12 aa）	Not recorded	SPH SPHINGOSINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；1.5 M ammonium formate and 0.15 M sodium HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.70 Å
1K5M Crystal Structure of a Human Rhinovirus Type 14:Human Immunodeficiency Virus Type 1 V3 Loop Chimeric Virus MN-III-2 Deposited 2001-10-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Insufficient information Heteromer；Protein × 60 PDB declaration: 60-meric	Chain B 314–325（12 aa）	Not recorded	SPH SPHINGOSINE × 15	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；1.5 M ammonium formate and 0.15 M sodium HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.70 Å
1NIZ NMR structure of a V3 (MN isolate) peptide bound to 447-52D, a human HIV-1 neutralizing antibody Deposited 2002-12-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 309–324（16 aa） Fragment：V3 loop (residues 309-324)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；308 K；Ionic strength (raw mmCIF value) 10mM；Pressure ambient NMR measurement conditions pH 5；308 K；Ionic strength (raw mmCIF value) 10mM；Pressure ambient NMR measurement conditions pH 5；308 K；Ionic strength (raw mmCIF value) 10mM；Pressure ambient NMR sample composition U-15N; 10mM sodium acetate buffer pH=5 \| 95% H2O/5% D2O NMR sample composition U-15N,13C; 10mM sodium acetate buffer pH=5 \| 95% H2O/5% D2O NMR sample composition U-15N,13C; 10mM sodium acetate buffer pH=5 \| 99% D2O	Resolution not provided
1NJ0 NMR structure of a V3 (MN isolate) peptide bound to 447-52D, a human HIV-1 neutralizing antibody Deposited 2002-12-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 309–324（16 aa） Fragment：V3 loop (residues 309-324)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；308 K；Ionic strength (raw mmCIF value) 10mM；Pressure ambient NMR measurement conditions pH 5；308 K；Ionic strength (raw mmCIF value) 10mM；Pressure ambient NMR measurement conditions pH 5；308 K；Ionic strength (raw mmCIF value) 10mM；Pressure ambient NMR sample composition U-15N; 10mM sodium acetate buffer pH=5 \| 95% H2O/5% D2O NMR sample composition U-15N,13C; 10mM sodium acetate buffer pH=5 \| 95% H2O/5% D2O NMR sample composition U-15N,13C; 10mM sodium acetate buffer pH=5 \| 99% D2O	Resolution not provided
2B0S Crystal structure analysis of anti-HIV-1 V3 Fab 2219 in complex with MN peptide Deposited 2005-09-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain P 308–325（18 aa） Fragment：residues 308-325	Not recorded	EDO 1,2-ETHANEDIOL × 2 ACY ACETIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；40% PEG 400, 0.2M potassium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K	Resolution 2.30 Å R-free 0.267
2QSC Crystal structure analysis of anti-HIV-1 V3-Fab F425-B4e8 in complex with a V3-peptide Deposited 2007-07-30	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 P 309–323（15 aa） Fragment：Residues 301-326	Not recorded	ZN ZINC ION × 4 CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6；298 K；PEG 8000, pH 6.0, VAPOR DIFFUSION, temperature 298K	Resolution 2.80 Å R-free 0.264
3GO1 Crystal structure of anti-HIV-1 Fab 268-D in complex with V3 peptide MN Deposited 2009-03-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain P 309–322（14 aa）	Not recorded	SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；296.15 K；30% PEG 8000, 0.2M Ammonium Acetate, 0.1M Sodium Cacodylate pH 6.5, vapor diffusion, hanging drop, temperature 296.15K	Resolution 1.89 Å R-free 0.213
3MLW Crystal structure of anti-HIV-1 V3 Fab 1006-15D in complex with an MN V3 peptide Deposited 2010-04-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain P 306–328（23 aa）	Not recorded	PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；296 K；20% PEG 3350, K dihydrogen phosphate, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.70 Å R-free 0.291
3MLW Crystal structure of anti-HIV-1 V3 Fab 1006-15D in complex with an MN V3 peptide Deposited 2010-04-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain Q 306–328（23 aa）	Not recorded	PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；296 K；20% PEG 3350, K dihydrogen phosphate, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.70 Å R-free 0.291
3MLX Crystal structure of anti-HIV-1 V3 Fab 3074 in complex with an MN V3 peptide Deposited 2010-04-18	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain P 306–328（23 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；296 K；20% PEG 3350, 0.2 M NH4 citrate dibasic, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.90 Å R-free 0.228
3MLX Crystal structure of anti-HIV-1 V3 Fab 3074 in complex with an MN V3 peptide Deposited 2010-04-18	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain Q 306–328（23 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；296 K；20% PEG 3350, 0.2 M NH4 citrate dibasic, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.90 Å R-free 0.228
3UJI Crystal structure of anti-HIV-1 V3 Fab 2558 in complex with MN peptide Deposited 2011-11-07	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 P 306–328（23 aa） Fragment：unp residues 306-328	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7.5；296 K；85mM Hepes-Na, 15% Glycerol, 17% PEG 4k, 8.5% Isopropanol, pH 7.5, EVAPORATION, temperature 296K	Resolution 1.60 Å R-free 0.194
6SH9 EngBF DARPin Fusion 4b D12 Deposited 2019-08-06	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 E 310–323（14 aa）	Not recorded	MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 MN MANGANESE (II) ION × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；277.15 K；PEG 20,000 MPD MES sodium chloride manganese chloride	Resolution 2.40 Å R-free 0.193
9OP1 Cryo-EM structure of Candida albicans fluoride channel FEX in complex with Fab fragment Deposited 2025-05-16	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 670–686（17 aa） Fragment：residues 76-389,residues 76-389	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.05 Å

13 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ENV_HV1MN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain P； PDBConstruct 1–23； UniProt 306–328

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	1f58
Deposition date deposition_date	1998-10-21
Structure title title	IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 24-RESIDUE PEPTIDE (RESIDUES 308-333 OF HIV-1 GP120 (MN ISOLATE) WITH ALA TO AIB SUBSTITUTION AT POSITION 323
Keywords keywords	IMMUNOGLOBULIN, FAB, HIV-1, GP120, V3, Viral protein-Immune system COMPLEX; Viral protein/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	26.27 Å
Radius of gyration Rg (electron density) rg_electron	25.32 Å
Forward intensity I(0) i0	42609800.00
Molecular weight molecular_weight	49679.0 kDa
Excluded volume excluded_volume	61668 Å³
Envelope volume envelope_volume	76346 Å³
Hydration-shell volume shell_volume	25449 Å³
Envelope diameter envelope_diameter	87.2 Å
Shell Rg shell_rg	32.40 Å
Envelope Rg envelope_rg	24.96 Å
Shape Rg shape_rg	25.31 Å
Total Rg total_rg	26.12 Å
Total atoms total_atoms	3497
Residues n_residues	454
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	84.8 Å
Rg (real space) rg_real	26.28 Å
Rg uncertainty (real space) rg_real_error	0.72 Å
I(0) (real space) i0_real	4.2610e+07
I(0) uncertainty (real space) i0_real_error	6.2110e+05
Rg (reciprocal space) rg_reciprocal	26.28 Å
I(0) (reciprocal space) i0_reciprocal	42610000.0000
Solution quality estimate total_estimate	0.9033
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.8 Å
Skewness Skewness skewness	0.294
Kurtosis Kurtosis kurtosis	-0.547
Angular range angular_range	— – 0.3000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	8479000.0000
Real-space data points n_real_points	61
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.985

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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	PROTEIN (IGG1 ANTIBODY 58.2 (LIGHT CHAIN))
Molecular weight formula_weight	23573.0 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	3617

DIVLTQSPASLAVSLGQRATISCKASQGVDFDGASFMNWYQQKPGQPPKLLIFAASTLESGIPARFSGRGSGTDFTLNIHPVEEEDAATYYCQQSHEDPLTFGAGTKLELKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRA

Entity 2 Entity 2 polymer

Description description	PROTEIN (IGG1 ANTIBODY 58.2 (HEAVY CHAIN))
Molecular weight formula_weight	24864.7 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

DVQLQQSGPDLVKPSQSLSLTCTVTGYSITSGYSWHWIRQFPGNKLEWMGYIHYSAGTNYNPSLKSRISITRDTSKNQFFLQLNSVTTEDTATYYCAREEAMPYGNQAYYYAMDCWGQGTTVTVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRDC

Entity 3 Entity 3 polymer

Description description	Envelope glycoprotein gp120
Molecular weight formula_weight	2725.2 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	P

YNKRKRIHIGPGRAFYTTKNIIG

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	120

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1f58h1
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	d1f58h2
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	d1f58l1
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	d1f58l2
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	1f58H01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1f58H02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1f58L01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1f58L02
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	72.890 Å
Unit-cell length b length_b	71.910 Å
Unit-cell length c length_c	88.250 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	98.31 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	44.000 Å
R factor r_factor	0.1960
R_work r_work	0.1960
R_free r_free	0.2560

fit	/app/data/saxs_computation/f5/1f58/1f58.fit
pddf	/app/data/pr_computation/f5/1f58/1f58.pr.out
profile	/app/data/saxs_computation/f5/1f58/1f58.dat

IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 24-RESIDUE PEPTIDE (RESIDUES 308-333 OF HIV-1 GP120 (MN ISOLATE) WITH ALA TO AIB SUBSTITUTION AT POSITION 323

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

Envelope glycoprotein gp120

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 polymer

Polymer 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 (1)

9. Files and Curves (10)

Files (7)

Curves (3)