SAXSdb — 2mz1

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

Heterogeneous nuclear ribonucleoproteins C1/C2

Homo sapiens

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–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric（2） Consistent with all polymer counts	Chain A； UniProt 2–106	Fragment：RRM (UNP residues 2-106)	5'-R(UPUPUPUP*C)-3' × 1	SOLUTION NMR NMR measurement conditions：pH 6.5；293 K；Ionic strength (raw mmCIF value) 0.040；Pressure ambient NMR sample composition：1.0 mM [U-100% 15N] hnRNP C, 1.0 mM 5'-R(UPUPUPUPC)-3', 20 mM sodium phosphate, 10 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：1.0 mM [U-100% 13C; U-100% 15N] hnRNP C, 1.0 mM 5'-R(UPUPUPUPC)-3', 20 mM sodium phosphate, 10 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：1.0 mM [U-100% 13C; U-100% 15N] hnRNP C, 1.0 mM 5'-R(UPUPUPUP*C)-3', 20 mM sodium phosphate, 10 mM sodium chloride, 100% D2O \| 100% D2O	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 2MZ1	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1WF2 Solution structure of RRM domain in HNRPC protein Deposited 2004-05-25	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 8–92（85 aa） Fragment：RRM domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 0.8mM U-15,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MXY Solution structure of hnRNP C RRM in complex with 5'-AUUUUUC-3' RNA Deposited 2015-01-19	Different experimental conditions	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 2–106（105 aa） Fragment：RRM (UNP residues 2-106)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；293 K；Ionic strength (raw mmCIF value) 0.040；Pressure ambient NMR sample composition 1.0 mM [U-100% 15N] hnRNP C, 1.0 mM 5'-R(APUPUPUPUPUPC)-3', 20 mM sodium phosphate, 10 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition* 1.0 mM [U-100% 13C; U-100% 15N] hnRNP C, 1.0 mM 5'-R(APUPUPUPUPUPC)-3', 20 mM sodium phosphate, 10 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition* 1.0 mM [U-100% 13C; U-100% 15N] hnRNP C, 1.0 mM 5'-R(APUPUPUPUPUPC)-3', 20 mM sodium phosphate, 10 mM sodium chloride, 100% D2O \| 100% D2O NMR sample composition* 0.5-1.0 mM [U-100% 15N] hnRNP C, 0.5-1.0 mM [100% 13C5]-Ura 5'-R(APUPUPUPUPUP*C)-3', 20 mM sodium phosphate, 10 mM sodium chloride, 100% D2O \| 100% D2O	Resolution not provided
3LN4 Crystal structure of HLA-B*4103 in complex with a 16mer self-peptide derived from heterogeneous nuclear ribonucleoproteins C1/C2 Deposited 2010-02-01	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 102–117（16 aa） Fragment：UNP residues 102-117	Not recorded	ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；294 K；0.1M citrate pH 5.6, 14-20% PEG 4000, 0.2M NH4OAc, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 1.30 Å R-free 0.177

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

View Construct and Data Evidence

UniProt name	HNRPC_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–105； UniProt 2–106

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	2mz1
Deposition date deposition_date	2015-02-05
Structure title title	Solution structure of hnRNP C RRM in complex with 5'-UUUUC-3' RNA
Keywords keywords	hnRNP C, RRM, complex, RNA BINDING PROTEIN-RNA complex; RNA BINDING PROTEIN/RNA
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	14.28 Å
Radius of gyration Rg (electron density) rg_electron	14.24 Å
Forward intensity I(0) i0	1090560000.00
Molecular weight molecular_weight	255060.0 kDa
Excluded volume excluded_volume	309710 Å³
Envelope volume envelope_volume	37679 Å³
Hydration-shell volume shell_volume	16882 Å³
Envelope diameter envelope_diameter	60.9 Å
Shell Rg shell_rg	25.76 Å
Envelope Rg envelope_rg	21.03 Å
Shape Rg shape_rg	14.19 Å
Total Rg total_rg	14.62 Å
Total atoms total_atoms	34960
Residues n_residues	2200
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	54.4 Å
Rg (real space) rg_real	14.42 Å
Rg uncertainty (real space) rg_real_error	0.59 Å
I(0) (real space) i0_real	1.0910e+09
I(0) uncertainty (real space) i0_real_error	1.3470e+07
Rg (reciprocal space) rg_reciprocal	14.41 Å
I(0) (reciprocal space) i0_reciprocal	1091000000.0000
Solution quality estimate total_estimate	0.7499
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	17.9 Å
Skewness Skewness skewness	0.759
Kurtosis Kurtosis kurtosis	0.810
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	578500.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.330; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.788; Smooth: 0.969

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	2mz1A00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	330 — RRM (RNA recognition motif) domain

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8. Citations (1)

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Description description	Heterogeneous nuclear ribonucleoproteins C1/C2
Molecular weight formula_weight	11291.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	34960

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Description description	5'-R(UPUPUPUP*C)-3'
Molecular weight formula_weight	1484.9 kDa
Source method src_method	syn
Copy count entity_count	1

fit	/app/data/saxs_computation/mz/2mz1/2mz1.fit
pddf	/app/data/pr_computation/mz/2mz1/2mz1.pr.out
profile	/app/data/saxs_computation/mz/2mz1/2mz1.dat

Solution structure of hnRNP C RRM in complex with 5'-UUUUC-3' RNA

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

Heterogeneous nuclear ribonucleoproteins C1/C2

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)