1b9p

NMR STRUCTURE OF HEPARIN BINDING SITE OF NON COLLAGENOUS DOMAIN I (NC1) OF COLLAGEN FACIT XIV

Method: SOLUTION NMR D_max: 61.1 Å Quality: REASONABLE

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

PROTEIN (COLLAGEN ALPHA 1)

OrganismNot specified

UniProt P32018

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 1852–1885	Fragment：FRAGMENT 84-116 OF NC1 (HEPARIN BINDING SITE) Mutation：E1C	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6；293 K；Pressure 1	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 1B9P	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B9Q NMR STRUCTURE OF HEPARIN BINDING SITE OF NON COLLAGENOUS DOMAIN I (NC1) OF COLLAGEN FACIT XIV Deposited 1999-02-15	Parsed fields agree	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1852–1885（34 aa） Fragment：FRAGMENT 84-116 OF NC1 (HEPARIN BINDING SITE)	Mutation：E1C	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；293 K；Pressure 1	Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	COEA1_CHICK
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–34； UniProt 1852–1885

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	1b9p
Deposition date deposition_date	1999-02-15
Structure title title	NMR STRUCTURE OF HEPARIN BINDING SITE OF NON COLLAGENOUS DOMAIN I (NC1) OF COLLAGEN FACIT XIV
Keywords keywords	COLLAGEN FACIT XIV, HEPARIN-BINDING SITE, NC1; COLLAGEN FACIT XIV
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	15.91 Å
Radius of gyration Rg (electron density) rg_electron	15.48 Å
Forward intensity I(0) i0	447021.00
Molecular weight molecular_weight	4016.0 kDa
Excluded volume excluded_volume	5013 Å³
Envelope volume envelope_volume	7431 Å³
Hydration-shell volume shell_volume	5199 Å³
Envelope diameter envelope_diameter	59.1 Å
Shell Rg shell_rg	17.74 Å
Envelope Rg envelope_rg	15.84 Å
Shape Rg shape_rg	15.39 Å
Total Rg total_rg	16.36 Å
Total atoms total_atoms	588
Residues n_residues	34
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	61.1 Å
Rg (real space) rg_real	16.28 Å
Rg uncertainty (real space) rg_real_error	0.65 Å
I(0) (real space) i0_real	4.4700e+05
I(0) uncertainty (real space) i0_real_error	5.6820e+03
Rg (reciprocal space) rg_reciprocal	16.24 Å
I(0) (reciprocal space) i0_reciprocal	447000.0000
Solution quality estimate total_estimate	0.7024
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	11.6 Å
Skewness Skewness skewness	0.617
Kurtosis Kurtosis kurtosis	-0.325
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	54250.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.377; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.029; Smooth: 0.968

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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	d1b9pa_
Class class	j — Peptides
Fold Fold fold	j.49 — Heparin binding site of non collagenous domain I (nc1) of collagen facit xiv
Superfamily Superfamily superfamily	j.49.1 — Heparin binding site of non collagenous domain I (nc1) of collagen facit xiv
Family Family family	j.49.1.1 — Heparin binding site of non collagenous domain I (nc1) of collagen facit xiv

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8. Citations (2)

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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	PROTEIN (COLLAGEN ALPHA 1)
Molecular weight formula_weight	4020.8 kDa
Mutation mutation	E1C
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	588

fit	/app/data/saxs_computation/b9/1b9p/1b9p.fit
pddf	/app/data/pr_computation/b9/1b9p/1b9p.pr.out
profile	/app/data/saxs_computation/b9/1b9p/1b9p.dat

NMR STRUCTURE OF HEPARIN BINDING SITE OF NON COLLAGENOUS DOMAIN I (NC1) OF COLLAGEN FACIT XIV

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

PROTEIN (COLLAGEN ALPHA 1)

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 (2)

9. Files and Curves (10)

Files (7)

Curves (3)