1cvq

SOLUTION STRUCTURE OF THE ANALOGUE RETRO-INVERSO MGREGRIGGC IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 7 STRUCTURES

Method: SOLUTION NMR D_max: 24.3 Å Quality: GOOD

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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 monomer Monomer 蛋白 1 / DNA 0 / RNA 0 / 其他Polymer 0 PDB declaration: monomeric	Entity 1：HISTONE H3 × 1 缺少 UniProt 身份时不显示参考序列区间	Entity 1Fragment：C-TERMINAL DOMAIN 130-135 Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions：pH 7；277 K；Ionic strength (raw mmCIF value) 0.1M phosphate；Pressure 1NMR sample composition：5 mM peptide, 0.1 mM mAb; 100 mM phosphate buffer containing 0.02% sodium azide \| 95% H2O/5% D2O	Resolution not provided

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1cvq
Deposition date deposition_date	1999-08-24
Structure title title	SOLUTION STRUCTURE OF THE ANALOGUE RETRO-INVERSO MGREGRIGGC IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 7 STRUCTURES
Keywords keywords	PSEUDOMIMETIC, SYNTHETIC PEPTIDE, RETRO-INVERSO ANALOGUE, TR-NOE, ANTIGEN- ANTIBODY COMPLEX, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	6.89 Å
Radius of gyration Rg (electron density) rg_electron	6.07 Å
Forward intensity I(0) i0	1190800.00
Molecular weight molecular_weight	6559.0 kDa
Excluded volume excluded_volume	7630 Å³
Envelope volume envelope_volume	2921 Å³
Hydration-shell volume shell_volume	3954 Å³
Envelope diameter envelope_diameter	22.8 Å
Shell Rg shell_rg	11.54 Å
Envelope Rg envelope_rg	7.39 Å
Shape Rg shape_rg	5.97 Å
Total Rg total_rg	7.16 Å
Total atoms total_atoms	882
Residues n_residues	28
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	24.3 Å
Rg (real space) rg_real	6.92 Å
Rg uncertainty (real space) rg_real_error	0.25 Å
I(0) (real space) i0_real	1.1910e+06
I(0) uncertainty (real space) i0_real_error	1.1110e+04
Rg (reciprocal space) rg_reciprocal	6.92 Å
I(0) (reciprocal space) i0_reciprocal	1191000.0000
Solution quality estimate total_estimate	0.8567
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	8.6 Å
Skewness Skewness skewness	0.337
Kurtosis Kurtosis kurtosis	-0.148
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1974.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.839; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.863; Smooth: 0.753

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1cvqa_
Class class	j — Peptides
Fold Fold fold	j.63 — Histone H3 C-terminal fragment 130-135
Superfamily Superfamily superfamily	j.63.1 — Histone H3 C-terminal fragment 130-135
Family Family family	j.63.1.1 — Histone H3 C-terminal fragment 130-135

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	HISTONE H3
Molecular weight formula_weight	933.0 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	882

fit	/app/data/saxs_computation/cv/1cvq/1cvq.fit
pddf	/app/data/pr_computation/cv/1cvq/1cvq.pr.out
profile	/app/data/saxs_computation/cv/1cvq/1cvq.dat

SOLUTION STRUCTURE OF THE ANALOGUE RETRO-INVERSO MGREGRIGGC IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 7 STRUCTURES

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

Assembly Composition of the Current Entry

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)