SAXSdb — 2h61

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

Protein S100-B

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 homooligomer Homooligomer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 0–91 Chain B； UniProt 0–91 Chain C； UniProt 0–91 Chain D； UniProt 0–91 Chain E； UniProt 0–91 Chain F； UniProt 0–91 Chain G； UniProt 0–91 Chain H； UniProt 0–91	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 18 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.2；289 K；0.1 M HEPES, 18-20%PEG400, 0.2 M CaCl2, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 1.90 Å R-free 0.241

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 2H61	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1MQ1 Ca2+-S100B-TRTK-12 complex Deposited 2002-09-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–91（91 aa） Chain B 1–91（91 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.05；308 K；Ionic strength (raw mmCIF value) 35 mM KCl；Pressure ambient NMR sample composition U-13C, U-15N S100B (1.0 mM) unlabelled TRTK-12 (1.2 mM) 3 mM CaCl2 \| 90% H20, 10% D20 NMR sample composition U-2H, U-15N S100B (0.35 mM) unlabelled TRTK-12 (0.80 mM) 1 mM CaCl2 \| 90% H20, 10% D20 NMR sample composition U-13C, U-15N S100B (1.0 mM) 13C-acetyl, 13C-Ile TRTK-12 (1.2 mM) 3 mM CaCl2 \| 90% H20, 10% D20 NMR sample composition U-13C/U-12C S100B heterodimer (1.0mM) Unlabelled TRTK-12 (1.2 mM) 3 mM CaCl2 \| 90% H20, 10% D20	Resolution not provided
1UWO CALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES Deposited 1997-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–91（91 aa） Chain B 1–91（91 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.05；308 K	Resolution not provided
2M49 Structural Insights into Human S100B and Basic Fibroblast Growth Factor (FGF2) Interaction Deposited 2013-02-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 2–92（91 aa） Chain D 2–92（91 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；298 K；Ionic strength (raw mmCIF value) 0.050；Pressure ambient NMR sample composition 1.2 mM [U-100% 13C; U-100% 15N] S100B-1, 20 mM TRIS-2, 50 mM ammonium sulfate-3, 5 mM calcium chloride-4, 5 mM DTT-5, 0.01 % sodium azide-6, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2PRU NMR Structure of Human apoS100B at 10C Deposited 2007-05-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–92（91 aa） Chain B 2–92（91 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；283 K；Ionic strength (raw mmCIF value) 50 mM；Pressure ambient NMR sample composition 1-2 mM U-13C,U-15N S100B, 50 mM KCl, 90%H2O/10%D2O \| 90% H2O/10% D2O NMR sample composition 0.7 mM U-15N S100B, 50 mM KCl, 12 mg/ml PF1 Phage, 90%H2O/10%D2O \| 90% H2O/10% D2O	Resolution not provided
3CZT Crystal Structure of S100B in the Calcium and Zinc Loaded State at pH 9 Deposited 2008-04-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain X 1–92（92 aa）	Not recorded	CA CALCIUM ION × 6 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；291 K；0.02 M TAPS, pH 9.0, 30% PEG4000, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 1.40 Å R-free 0.222
3D0Y Crystal Structure of S100B in the Calcium and Zinc Loaded State at pH 6.5 Deposited 2008-05-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–92（92 aa） Chain B 1–92（92 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 4 ZN ZINC ION × 2 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；289 K；0.1 M MES pH 6.5 21% PEG5000MME, VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 1.50 Å R-free 0.261
3D10 Crystal Structure of S100B in the Calcium and Zinc Loaded State at pH 10.0 Deposited 2008-05-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–92（92 aa） Chain B 1–92（92 aa）	Not recorded	CA CALCIUM ION × 4 ZN ZINC ION × 2 PGE TRIETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；291 K；0.02 M CAPS pH 10.0, 23% PEG5000MME, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.65 Å R-free 0.275
3HCM Crystal structure of human S100B in complex with S45 Deposited 2009-05-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–92（92 aa） Chain B 1–92（92 aa）	Not recorded	CA CALCIUM ION × 4 S45 (3R)-3-[3-(4-chlorophenyl)-1,2,4-oxadiazol-5-yl]piperidine × 2 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；0.1M sodium acetate, 0.02M calcium chloride, 45% methylpenthanediol, pH4.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.00 Å R-free 0.311
4XYN X-ray structure of Ca(2+)-S100B with human RAGE-derived W61 peptide Deposited 2015-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–92（92 aa） Chain B 1–92（92 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.8；293 K；0.1M Na cacodylate, pH 6.8, 25% w/v PEG 3350, 9mM CaCl2	Resolution 2.55 Å R-free 0.254
4XYN X-ray structure of Ca(2+)-S100B with human RAGE-derived W61 peptide Deposited 2015-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–92（92 aa） Chain D 1–92（92 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.8；293 K；0.1M Na cacodylate, pH 6.8, 25% w/v PEG 3350, 9mM CaCl2	Resolution 2.55 Å R-free 0.254
5CSF S100B-RSK1 crystal structure A Deposited 2015-07-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–92（92 aa） Chain B 1–92（92 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；296 K；0.1 M Hepes 7, 150 mM NaCl, 20% PEG6000	Resolution 2.40 Å R-free 0.291
5CSI S100B-RSK1 crystal structure A' Deposited 2015-07-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–92（92 aa） Chain B 1–92（92 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；296 K；0.1 M Hepes 7, 150 mM NaCl, 20% PEG6000	Resolution 2.13 Å R-free 0.250
5CSJ S100B-RSK1 crystal structure B Deposited 2015-07-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–92（92 aa） Chain B 1–92（92 aa）	Not recorded	CA CALCIUM ION × 4 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；296 K；0.1 M Hepes 7, 150 mM NaCl, 20% PEG6000	Resolution 2.70 Å R-free 0.276
5CSN S100B-RSK1 crystal structure C Deposited 2015-07-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–92（92 aa） Chain B 1–92（92 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；296 K；0.1 M Hepes 7, 150 mM NaCl, 20% PEG6000	Resolution 2.95 Å R-free 0.279
5D7F X-ray structure of Ca(2+)-S100B with human RAGE-derived W72 peptide Deposited 2015-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–92（92 aa） Chain B 1–92（92 aa）	Not recorded	CA CALCIUM ION × 4 GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.8；293 K；100mM Na cacodylate pH 6.8, 22% w/v PEG 3350, 5mM CaCl2	Resolution 1.30 Å R-free 0.183

14 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	S100B_HUMAN
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–92； UniProt 0–91 Author chain B； PDBConstruct 1–92； UniProt 0–91 Author chain E； PDBConstruct 1–92； UniProt 0–91 Author chain F； PDBConstruct 1–92； UniProt 0–91 Author chain H； PDBConstruct 1–92； UniProt 0–91 Author chain C； PDBConstruct 1–92； UniProt 0–91 Author chain D； PDBConstruct 1–92； UniProt 0–91 Author chain G； PDBConstruct 1–92； UniProt 0–91

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	2h61
Deposition date deposition_date	2006-05-30
Structure title title	X-ray structure of human Ca2+-loaded S100B
Keywords keywords	S100, EF-hand, Calcium-binding, RAGE, METAL BINDING PROTEIN, SIGNALING PROTEIN; METAL BINDING PROTEIN, SIGNALING PROTEIN
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	28.98 Å
Radius of gyration Rg (electron density) rg_electron	27.57 Å
Forward intensity I(0) i0	122487000.00
Molecular weight molecular_weight	85421.0 kDa
Excluded volume excluded_volume	105770 Å³
Envelope volume envelope_volume	131280 Å³
Hydration-shell volume shell_volume	38114 Å³
Envelope diameter envelope_diameter	88.0 Å
Shell Rg shell_rg	36.23 Å
Envelope Rg envelope_rg	27.34 Å
Shape Rg shape_rg	27.56 Å
Total Rg total_rg	28.44 Å
Total atoms total_atoms	5948
Residues n_residues	725
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	84.9 Å
Rg (real space) rg_real	28.78 Å
Rg uncertainty (real space) rg_real_error	0.46 Å
I(0) (real space) i0_real	1.2250e+08
I(0) uncertainty (real space) i0_real_error	1.6450e+06
Rg (reciprocal space) rg_reciprocal	28.87 Å
I(0) (reciprocal space) i0_reciprocal	122500000.0000
Solution quality estimate total_estimate	0.9049
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	38.6 Å
Skewness Skewness skewness	0.036
Kurtosis Kurtosis kurtosis	-0.492
Angular range angular_range	— – 0.2750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	13150000.0000
Real-space data points n_real_points	56
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.949; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.937

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Protein S100-B
Molecular weight formula_weight	10727.0 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,E,F,H
Atom count atom_count	6570

MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE

来源 Source

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 BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Protein S100-B
Molecular weight formula_weight	10755.0 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D,G

MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE

来源 Source

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 BL21(DE3)

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	18

Entity 4 Entity 4 non-polymer

Description description	TETRAETHYLENE GLYCOL
Molecular weight formula_weight	194.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	617

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d2h61a_
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.2 — S100 proteins

Domain ID domain_id	d2h61b_
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.2 — S100 proteins

Domain ID domain_id	d2h61c_
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.2 — S100 proteins

Domain ID domain_id	d2h61d_
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.2 — S100 proteins

Domain ID domain_id	d2h61e_
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.2 — S100 proteins

Domain ID domain_id	d2h61f_
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.2 — S100 proteins

Domain ID domain_id	d2h61g_
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.2 — S100 proteins

Domain ID domain_id	d2h61h_
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.2 — S100 proteins

CATH v4.4 (8 domains)

Domain ID domain_id	2h61A00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	2h61B00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	2h61C00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	2h61D00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	2h61E00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	2h61F00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	2h61G00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	2h61H00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

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8. Citations (1)

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Unit-cell length a length_a	63.400 Å
Unit-cell length b length_b	81.600 Å
Unit-cell length c length_c	71.500 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	107.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	10

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	30.320 Å
R factor r_factor	—
R_work r_work	0.1740
R_free r_free	0.2410

fit	/app/data/saxs_computation/h6/2h61/2h61.fit
pddf	/app/data/pr_computation/h6/2h61/2h61.pr.out
profile	/app/data/saxs_computation/h6/2h61/2h61.dat

X-ray structure of human Ca2+-loaded S100B

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

Protein S100-B

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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)