SAXSdb — 1cs9

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

HISTONE H3 PEPTIDE

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 130–135	Fragment：C-TERMINAL REGION 130-135	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 7；277 K；Ionic strength (raw mmCIF value) 0.1M PHOSPHATE；Pressure 1 NMR sample composition：5 MM PEPTIDE, 0.1MM MAB; 100 MM PHOSPHATE BUFFER CONTAINING 0.02% SODIUM AZIDE	Resolution not provided

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 1CS9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CT6 SOLUTION STRUCTURE OF CGGIRGERG IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 11 STRUCTURES Deposited 1999-08-19	Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 130–135（6 aa） Fragment：C-TERMINAL REGION 130-135	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；277 K；Ionic strength (raw mmCIF value) 0.1M PHOSPHATE；Pressure 1 NMR sample composition 5 MM PEPTIDE, 0.1 MM MAB; 100 MM PHOSPHTE BUFFER CONTAINING 0.02% SODIUM AZIDE	Resolution not provided
1GUW STRUCTURE OF THE CHROMODOMAIN FROM MOUSE HP1beta IN COMPLEX WITH THE LYSINE 9-METHYL HISTONE H3 N-TERMINAL PEPTIDE, NMR, 25 STRUCTURES Deposited 2002-02-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–16（16 aa） Fragment：N-TERMINAL TAIL, RESIDUES 1-18	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；298 K；Pressure 1 NMR sample composition 150 mM NACL, 20 mM PHOSPHATE BUFFER, 10% D2O	Resolution not provided
1Q3L Chromodomain Of HP1 Complexed With Histone H3 Tail Containing monomethyllysine 9. Deposited 2003-07-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 1–16（16 aa） Fragment：tail residues 1-16	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.1；283 K；Ammonium Sulfate, MES, pH 6.1, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 1.64 Å R-free 0.241

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

View Construct and Data Evidence

UniProt name	H31_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–9； UniProt 130–135

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	1cs9
Deposition date deposition_date	1999-08-18
Structure title title	SOLUTION STRUCTURE OF CGGIRGERA IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 7 STRUCTURES
Keywords keywords	SYNTHETIC PEPTIDE, 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	6.87 Å
Radius of gyration Rg (electron density) rg_electron	6.33 Å
Forward intensity I(0) i0	1179830.00
Molecular weight molecular_weight	6433.0 kDa
Excluded volume excluded_volume	7497 Å³
Envelope volume envelope_volume	3578 Å³
Hydration-shell volume shell_volume	4383 Å³
Envelope diameter envelope_diameter	26.1 Å
Shell Rg shell_rg	12.24 Å
Envelope Rg envelope_rg	8.11 Å
Shape Rg shape_rg	6.28 Å
Total Rg total_rg	7.56 Å
Total atoms total_atoms	889
Residues n_residues	63
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	26.2 Å
Rg (real space) rg_real	6.94 Å
Rg uncertainty (real space) rg_real_error	0.38 Å
I(0) (real space) i0_real	1.1800e+06
I(0) uncertainty (real space) i0_real_error	1.1710e+04
Rg (reciprocal space) rg_reciprocal	6.93 Å
I(0) (reciprocal space) i0_reciprocal	1180000.0000
Solution quality estimate total_estimate	0.7885
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	7.3 Å
Skewness Skewness skewness	0.560
Kurtosis Kurtosis kurtosis	0.122
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1623.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.648; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.497; Smooth: 0.805

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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	d1cs9a_
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 PEPTIDE
Molecular weight formula_weight	920.0 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	889

fit	/app/data/saxs_computation/cs/1cs9/1cs9.fit
pddf	/app/data/pr_computation/cs/1cs9/1cs9.pr.out
profile	/app/data/saxs_computation/cs/1cs9/1cs9.dat

SOLUTION STRUCTURE OF CGGIRGERA IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 7 STRUCTURES

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

HISTONE H3 PEPTIDE

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

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)