SAXSdb — 4kik

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

Inhibitor of nuclear factor kappa-B kinase subunit beta

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 2–664 Chain B； UniProt 2–664	Non-standard monomer：Yes (specific site not provided by mmCIF)	KSA K-252A × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.83 Å R-free 0.236

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 4KIK	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3BRT NEMO/IKK association domain structure Deposited 2007-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 701–730（30 aa） Fragment：Fusion protein consists of UNP residues 701-730 of IKK-B and nemo-binding domain of IKK-A Chain C 701–730（30 aa） Fragment：Fusion protein consists of UNP residues 701-730 of IKK-B and nemo-binding domain of IKK-A	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions microbatch under oil；pH 8；298 K；35% Peg 8K, 0.1M Tris pH 8, 0.2M Ammonium Chloride, 10mM Dithiothreitol., microbatch under oil, temperature 298K	Resolution 2.25 Å R-free 0.282
3BRT NEMO/IKK association domain structure Deposited 2007-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 701–730（30 aa） Fragment：Fusion protein consists of UNP residues 701-730 of IKK-B and nemo-binding domain of IKK-A	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions microbatch under oil；pH 8；298 K；35% Peg 8K, 0.1M Tris pH 8, 0.2M Ammonium Chloride, 10mM Dithiothreitol., microbatch under oil, temperature 298K	Resolution 2.25 Å R-free 0.282
3BRT NEMO/IKK association domain structure Deposited 2007-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 701–730（30 aa） Fragment：Fusion protein consists of UNP residues 701-730 of IKK-B and nemo-binding domain of IKK-A	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions microbatch under oil；pH 8；298 K；35% Peg 8K, 0.1M Tris pH 8, 0.2M Ammonium Chloride, 10mM Dithiothreitol., microbatch under oil, temperature 298K	Resolution 2.25 Å R-free 0.282
3BRT NEMO/IKK association domain structure Deposited 2007-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 701–730（30 aa） Fragment：Fusion protein consists of UNP residues 701-730 of IKK-B and nemo-binding domain of IKK-A	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions microbatch under oil；pH 8；298 K；35% Peg 8K, 0.1M Tris pH 8, 0.2M Ammonium Chloride, 10mM Dithiothreitol., microbatch under oil, temperature 298K	Resolution 2.25 Å R-free 0.282
3BRT NEMO/IKK association domain structure Deposited 2007-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 701–730（30 aa） Fragment：Fusion protein consists of UNP residues 701-730 of IKK-B and nemo-binding domain of IKK-A	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions microbatch under oil；pH 8；298 K；35% Peg 8K, 0.1M Tris pH 8, 0.2M Ammonium Chloride, 10mM Dithiothreitol., microbatch under oil, temperature 298K	Resolution 2.25 Å R-free 0.282
3BRV NEMO/IKKb association domain structure Deposited 2007-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 701–745（45 aa） Fragment：NEMO-binding Chain C 701–745（45 aa） Fragment：NEMO-binding	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；30% Peg 4K, 0.1M Tris pH 8.5, 0.2M MgCl2, 10mM DTT, 10% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.20 Å R-free 0.294
3BRV NEMO/IKKb association domain structure Deposited 2007-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 701–745（45 aa） Fragment：NEMO-binding	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；30% Peg 4K, 0.1M Tris pH 8.5, 0.2M MgCl2, 10mM DTT, 10% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.20 Å R-free 0.294
3BRV NEMO/IKKb association domain structure Deposited 2007-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 701–745（45 aa） Fragment：NEMO-binding	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；30% Peg 4K, 0.1M Tris pH 8.5, 0.2M MgCl2, 10mM DTT, 10% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.20 Å R-free 0.294
3BRV NEMO/IKKb association domain structure Deposited 2007-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 701–745（45 aa） Fragment：NEMO-binding	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；30% Peg 4K, 0.1M Tris pH 8.5, 0.2M MgCl2, 10mM DTT, 10% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.20 Å R-free 0.294
3BRV NEMO/IKKb association domain structure Deposited 2007-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 701–745（45 aa） Fragment：NEMO-binding	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；30% Peg 4K, 0.1M Tris pH 8.5, 0.2M MgCl2, 10mM DTT, 10% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.20 Å R-free 0.294
4E3C X-ray crystal structure of human IKK2 in an active conformation Deposited 2012-03-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 11–669（659 aa） Fragment：UNP Residues 11-669 Chain F 11–669（659 aa） Fragment：UNP Residues 11-669	Mutation：S177E, S181E Mutation：S177E, S181E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；1.2M sodium malonate, 250mM ammonium acetate, 10mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.98 Å R-free 0.299
4E3C X-ray crystal structure of human IKK2 in an active conformation Deposited 2012-03-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 11–669（659 aa） Fragment：UNP Residues 11-669 Chain C 11–669（659 aa） Fragment：UNP Residues 11-669	Mutation：S177E, S181E Mutation：S177E, S181E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；1.2M sodium malonate, 250mM ammonium acetate, 10mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.98 Å R-free 0.299
4E3C X-ray crystal structure of human IKK2 in an active conformation Deposited 2012-03-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain D 11–669（659 aa） Fragment：UNP Residues 11-669 Chain E 11–669（659 aa） Fragment：UNP Residues 11-669	Mutation：S177E, S181E Mutation：S177E, S181E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；1.2M sodium malonate, 250mM ammonium acetate, 10mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.98 Å R-free 0.299
8OMV Crystal structure of the constitutively active S117E/S181E mutant of human IKK2 Deposited 2023-03-31	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–669（669 aa） Chain B 1–669（669 aa）	Mutation：S177E, S181E Mutation：S177E, S181E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.6M (NH4)2SO4, 0.1M Bis-Tris HCl pH 6.5, 10% 2-propanol	Resolution 4.16 Å R-free 0.299
8OMV Crystal structure of the constitutively active S117E/S181E mutant of human IKK2 Deposited 2023-03-31	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–669（669 aa） Chain D 1–669（669 aa）	Mutation：S177E, S181E Mutation：S177E, S181E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.6M (NH4)2SO4, 0.1M Bis-Tris HCl pH 6.5, 10% 2-propanol	Resolution 4.16 Å R-free 0.299
8OMV Crystal structure of the constitutively active S117E/S181E mutant of human IKK2 Deposited 2023-03-31	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 1–669（669 aa）	Mutation：S177E, S181E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.6M (NH4)2SO4, 0.1M Bis-Tris HCl pH 6.5, 10% 2-propanol	Resolution 4.16 Å R-free 0.299

4 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	IKKB_HUMAN
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 8–670； UniProt 2–664 Author chain B； PDBConstruct 8–670； UniProt 2–664

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	4kik
Deposition date deposition_date	2013-05-02
Structure title title	Human IkB kinase beta
Keywords keywords	kinase, NkB signaling, TRANSFERASE; TRANSFERASE
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	48.66 Å
Radius of gyration Rg (electron density) rg_electron	48.51 Å
Forward intensity I(0) i0	327128000.00
Molecular weight molecular_weight	147890.0 kDa
Excluded volume excluded_volume	184750 Å³
Envelope volume envelope_volume	278830 Å³
Hydration-shell volume shell_volume	49388 Å³
Envelope diameter envelope_diameter	152.3 Å
Shell Rg shell_rg	50.78 Å
Envelope Rg envelope_rg	46.77 Å
Shape Rg shape_rg	48.55 Å
Total Rg total_rg	48.50 Å
Total atoms total_atoms	10371
Residues n_residues	1266
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	149.2 Å
Rg (real space) rg_real	48.61 Å
Rg uncertainty (real space) rg_real_error	1.27 Å
I(0) (real space) i0_real	3.2710e+08
I(0) uncertainty (real space) i0_real_error	6.1760e+06
Rg (reciprocal space) rg_reciprocal	48.66 Å
I(0) (reciprocal space) i0_reciprocal	327100000.0000
Solution quality estimate total_estimate	0.8313
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	74.6 Å
Skewness Skewness skewness	0.061
Kurtosis Kurtosis kurtosis	-0.920
Angular range angular_range	— – 0.1600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	14480000.0000
Real-space data points n_real_points	33
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: 0.955; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Inhibitor of nuclear factor kappa-B kinase subunit beta
Molecular weight formula_weight	78251.5 kDa
EC 编号 ec_number	2.7.11.10
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	10602

MHHHHHHSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQIAIKQCRQELSPRNRERWCLEIQIMRRLTHPNVVAARDVPEGMQNLAPNDLPLLAMEYCQGGDLRKYLNQFENCCGLREGAILTLLSDIASALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHSKVRQKSEVDIVVSEDLNGTVKFSSSLPYPNNLNSVLAERLEKWLQLMLMWHPRQRGTDPTYGPNGCFKALDDILNLKLVHILNMVTGTIHTYPVTEDESLQSLKARIQQDTGIPEEDQELLQEAGLALIPDKPATQCISDGKLNEGHTLDMDLVFLFDNSKITYETQISPRPQPESVSCILQEPKRNLAFFQLRKVWGQVWHSIQTLKEDCNRLQQGQRAAMMNLLRNNSCLSKMKNSMASMSQQLKAKLDFFKTSIQIDLEKYSEQTEFGITSDKLLLAWREMEQAVELCGRENEVKLLVERMMALQTDIVDLQRSPMGRKQGGTLDDLEEQARELYRRLREKPRDQRTEGDSQEMVRLLLQAIQSFEKKVRVIYTQLSKTVVCKQKALELLPKVEEVVSLMNEDEKTVVRLQEKRQKELWNLLKIACSKSPGRPLN

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	Spodoptera frugiperda

Entity 2 Entity 2 polymer

Description description	Inhibitor of nuclear factor kappa-B kinase subunit beta
Molecular weight formula_weight	78331.5 kDa
EC 编号 ec_number	2.7.11.10
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MHHHHHHSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQIAIKQCRQELSPRNRERWCLEIQIMRRLTHPNVVAARDVPEGMQNLAPNDLPLLAMEYCQGGDLRKYLNQFENCCGLREGAILTLLSDIASALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHSKVRQKSEVDIVVSEDLNGTVKFSSSLPYPNNLNSVLAERLEKWLQLMLMWHPRQRGTDPTYGPNGCFKALDDILNLKLVHILNMVTGTIHTYPVTEDESLQSLKARIQQDTGIPEEDQELLQEAGLALIPDKPATQCISDGKLNEGHTLDMDLVFLFDNSKITYETQISPRPQPESVSCILQEPKRNLAFFQLRKVWGQVWHSIQTLKEDCNRLQQGQRAAMMNLLRNNSCLSKMKNSMASMSQQLKAKLDFFKTSIQIDLEKYSEQTEFGITSDKLLLAWREMEQAVELCGRENEVKLLVERMMALQTDIVDLQRSPMGRKQGGTLDDLEEQARELYRRLREKPRDQRTEGDSQEMVRLLLQAIQSFEKKVRVIYTQLSKTVVCKQKALELLPKVEEVVSLMNEDEKTVVRLQEKRQKELWNLLKIACSKSPGRPLN

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	Spodoptera frugiperda

Entity 3 Entity 3 non-polymer

Description description	K-252A
Molecular weight formula_weight	467.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	221

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7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	4kikA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily	10 — Transferase(Phosphotransferase) domain 1

Domain ID domain_id	4kikA02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Domain ID domain_id	4kikA03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily	250 —

Domain ID domain_id	4kikB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily	10 — Transferase(Phosphotransferase) domain 1

Domain ID domain_id	4kikB02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Domain ID domain_id	4kikB03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily	250 —

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8. Citations (1)

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Unit-cell length a length_a	110.954 Å
Unit-cell length b length_b	68.689 Å
Unit-cell length c length_c	107.401 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	107.03 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	2

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

Resolution resolution	2.830 Å
Low-resolution limit resolution_low	47.170 Å
R factor r_factor	0.1863
R_work r_work	0.1836
R_free r_free	0.2365

fit	/app/data/saxs_computation/ki/4kik/4kik.fit
pddf	/app/data/pr_computation/ki/4kik/4kik.pr.out
profile	/app/data/saxs_computation/ki/4kik/4kik.dat

Human IkB kinase beta

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

Inhibitor of nuclear factor kappa-B kinase subunit beta

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

6. Entities and Polymers Entities & Polymers (4)

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 water

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)