SAXSdb — 6b5b

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

Baculoviral IAP repeat-containing protein 1e

Mus musculus

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–1403	Not recorded	NLR family CARD domain-containing protein 4 × 2 （Q3UP24） Flagellin × 1 （G8UUW9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 5.20 Å

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 6B5B	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7RAV Cryo-EM structure of the unliganded form of NLR family apoptosis inhibitory protein 5 (NAIP5) Deposited 2021-07-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–1403（1402 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8FML Cryo-EM structure of NLR family apoptosis inhibitory protein 5 (NAIP5) in complex with a full-length flagellin (FliC) ligand Deposited 2022-12-23	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–1403（1402 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.93 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BIR1E_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–1403； UniProt 1–1403

NLR family CARD domain-containing protein 4

Mus musculus

UniProt Q3UP24

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 1–1024 Chain C； UniProt 1–1024	Not recorded	Baculoviral IAP repeat-containing protein 1e × 1 （Q9R016） Flagellin × 1 （G8UUW9）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 5.20 Å

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 6B5B	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3JBL Cryo-EM Structure of the Activated NAIP2/NLRC4 Inflammasome Reveals Nucleated Polymerization Deposited 2015-09-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 11 PDB declaration: undecameric	Chain A 93–1024（932 aa） Fragment：UNP residues 93-1024, SEE REMARK 999 Chain B 93–1024（932 aa） Fragment：UNP residues 93-1024, SEE REMARK 999 Chain C 93–1024（932 aa） Fragment：UNP residues 93-1024, SEE REMARK 999 Chain D 93–1024（932 aa） Fragment：UNP residues 93-1024, SEE REMARK 999 Chain E 93–1024（932 aa） Fragment：UNP residues 93-1024, SEE REMARK 999 Chain F 93–1024（932 aa） Fragment：UNP residues 93-1024, SEE REMARK 999 Chain G 93–1024（932 aa） Fragment：UNP residues 93-1024, SEE REMARK 999 Chain H 93–1024（932 aa） Fragment：UNP residues 93-1024, SEE REMARK 999 Chain I 93–1024（932 aa） Fragment：UNP residues 93-1024, SEE REMARK 999 Chain J 93–1024（932 aa） Fragment：UNP residues 93-1024, SEE REMARK 999 Chain K 93–1024（932 aa） Fragment：UNP residues 93-1024, SEE REMARK 999	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 25 mM Tris-HCl, pH 8.0, 150 mM NaCl, 2 mM DTT；pH 8；25 mM Tris-HCl, pH 8.0, 150 mM NaCl, 2 mM DTT cryo-EM vitrification conditions Blot for one second before plunging；103 K；Cryogen ETHANE；Blotted for one second before plunging into liquid ethane (FEI VITROBOT MARK IV).	Resolution 4.70 Å R-free 0.383
4KXF Crystal structure of NLRC4 reveals its autoinhibition mechanism Deposited 2013-05-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain K 1–1024（1024 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；1.65M sodium phosphate monobasic monohydrate/potassium phosphate dibasic, 1% n-propyl formate., pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.20 Å R-free 0.266
4KXF Crystal structure of NLRC4 reveals its autoinhibition mechanism Deposited 2013-05-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 10 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 1–1024（1024 aa） Chain F 1–1024（1024 aa） Chain H 1–1024（1024 aa） Chain L 1–1024（1024 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 4 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；1.65M sodium phosphate monobasic monohydrate/potassium phosphate dibasic, 1% n-propyl formate., pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.20 Å R-free 0.266
4KXF Crystal structure of NLRC4 reveals its autoinhibition mechanism Deposited 2013-05-25	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 11 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain D 1–1024（1024 aa） Chain N 1–1024（1024 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 4 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；1.65M sodium phosphate monobasic monohydrate/potassium phosphate dibasic, 1% n-propyl formate., pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.20 Å R-free 0.266
4KXF Crystal structure of NLRC4 reveals its autoinhibition mechanism Deposited 2013-05-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–1024（1024 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；1.65M sodium phosphate monobasic monohydrate/potassium phosphate dibasic, 1% n-propyl formate., pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.20 Å R-free 0.266
4KXF Crystal structure of NLRC4 reveals its autoinhibition mechanism Deposited 2013-05-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1–1024（1024 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；1.65M sodium phosphate monobasic monohydrate/potassium phosphate dibasic, 1% n-propyl formate., pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.20 Å R-free 0.266
4KXF Crystal structure of NLRC4 reveals its autoinhibition mechanism Deposited 2013-05-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 1–1024（1024 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；1.65M sodium phosphate monobasic monohydrate/potassium phosphate dibasic, 1% n-propyl formate., pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.20 Å R-free 0.266
4KXF Crystal structure of NLRC4 reveals its autoinhibition mechanism Deposited 2013-05-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain H 1–1024（1024 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；1.65M sodium phosphate monobasic monohydrate/potassium phosphate dibasic, 1% n-propyl formate., pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.20 Å R-free 0.266
4KXF Crystal structure of NLRC4 reveals its autoinhibition mechanism Deposited 2013-05-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain L 1–1024（1024 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；1.65M sodium phosphate monobasic monohydrate/potassium phosphate dibasic, 1% n-propyl formate., pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.20 Å R-free 0.266
4KXF Crystal structure of NLRC4 reveals its autoinhibition mechanism Deposited 2013-05-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain N 1–1024（1024 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；1.65M sodium phosphate monobasic monohydrate/potassium phosphate dibasic, 1% n-propyl formate., pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.20 Å R-free 0.266
4KXF Crystal structure of NLRC4 reveals its autoinhibition mechanism Deposited 2013-05-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 8 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain P 1–1024（1024 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；1.65M sodium phosphate monobasic monohydrate/potassium phosphate dibasic, 1% n-propyl formate., pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.20 Å R-free 0.266
4KXF Crystal structure of NLRC4 reveals its autoinhibition mechanism Deposited 2013-05-25	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 9 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain K 1–1024（1024 aa） Chain P 1–1024（1024 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；1.65M sodium phosphate monobasic monohydrate/potassium phosphate dibasic, 1% n-propyl formate., pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.20 Å R-free 0.266
5AJ2 Cryo electron tomography of the Naip5-Nlrc4 inflammasome Deposited 2015-02-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–355（355 aa） Fragment：RESIDUES 1-355 Chain B 356–580（225 aa） Fragment：RESIDUES 356-580 Chain C 580–1024（445 aa） Fragment：RESIDUES 580-1024	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100 MM NACL, 20 MM HEPES, 2MM BENZAMIDIN, 2MM DTT；pH 7.5；100 MM NACL, 20 MM HEPES, 2MM BENZAMIDIN, 2MM DTT cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, HUMIDITY- 95, INSTRUMENT- LEICA EM GP, METHOD- 3 SECONDS BLOTTING,	Resolution 40.00 Å

3 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NLRC4_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–1024； UniProt 1–1024 Author chain C； PDBConstruct 1–1024； UniProt 1–1024

Flagellin

Legionella pneumophila

UniProt G8UUW9

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain F； UniProt 2–475	Not recorded	Baculoviral IAP repeat-containing protein 1e × 1 （Q9R016） NLR family CARD domain-containing protein 4 × 2 （Q3UP24）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 5.20 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	G8UUW9_LEGPN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain F； PDBConstruct 93–566； UniProt 2–475

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	6b5b
Deposition date deposition_date	2017-09-29
Structure title title	Cryo-EM structure of the NAIP5-NLRC4-flagellin inflammasome
Keywords keywords	Innate immunity, molecular complex, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	60.84 Å
Radius of gyration Rg (electron density) rg_electron	61.13 Å
Forward intensity I(0) i0	1659790000.00
Molecular weight molecular_weight	349230.0 kDa
Excluded volume excluded_volume	440130 Å³
Envelope volume envelope_volume	687310 Å³
Hydration-shell volume shell_volume	96817 Å³
Envelope diameter envelope_diameter	205.8 Å
Shell Rg shell_rg	59.84 Å
Envelope Rg envelope_rg	59.64 Å
Shape Rg shape_rg	61.11 Å
Total Rg total_rg	61.16 Å
Total atoms total_atoms	24555
Residues n_residues	3073
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	212.9 Å
Rg (real space) rg_real	61.09 Å
Rg uncertainty (real space) rg_real_error	2.58 Å
I(0) (real space) i0_real	1.6600e+09
I(0) uncertainty (real space) i0_real_error	3.8360e+07
Rg (reciprocal space) rg_reciprocal	60.60 Å
I(0) (reciprocal space) i0_reciprocal	1658000000.0000
Solution quality estimate total_estimate	0.6237
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	65.5 Å
Skewness Skewness skewness	0.398
Kurtosis Kurtosis kurtosis	-0.347
Angular range angular_range	— – 0.1300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	119000000.0000
Real-space data points n_real_points	27
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 0.001; Positv: 1.000; Valcen: 1.000; Smooth: 0.570

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Baculoviral IAP repeat-containing protein 1e
Molecular weight formula_weight	159874.8 kDa
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	24555

MAEHGESSEDRISEIDYEFLPELSALLGVDAFQVAKSQEEEEHKERMKMKKGFNSQMRSEAKRLKTFETYDTFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQGKDVGNIGKYDIRVKSPEKMLRGGKARYHEEEARLESFEDWPFYAHGTSPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQSKKSSEEIAQYIQSYEGFVHVTGEHFVKSWVRRELPMVSAYCNDSVFANEELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQTLKSSAEVIPTLQSQYALPEATETTRESNHGDAAAVHSTVVDLGRSEAQWFQEARSLSEQLRDNYTKATFRHMNLPEVCSSLGTDHLLSCDVSIISKHISQPVQEALTIPEVFSNLNSVMCVEGETGSGKTTFLKRIAFLWASGCCPLLYRFQLVFYLSLSSITPDQGLANIICAQLLGAGGCISEVCLSSSIQQLQHQVLFLLDDYSGLASLPQALHTLITKNYLSRTCLLIAVHTNRVRDIRLYLGTSLEIQEFPFYNTVSVLRKFFSHDIICVEKLIIYFIDNKDLQGVYKTPLFVAAVCTDWIQNASAQDKFQDVTLFQSYMQYLSLKYKATAEPLQATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDEKLTTLLMSKFTAQRLRPVYRFLGPLFQEFLAAVRLTELLSSDRQEDQDLGLYYLRQIDSPLKAINSFNIFLYYVSSHSSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPQTFLWFQFVRGLWLVSPESSSSFVSEHLLRLALIFAYESNTVAECSPFILQFLRGKTLALRVLNLQYFRDHPESLLLLRSLKVSINGNKMSSYVDYSFKTYFENLQPPAIDEEYTSAFEHISEWRRNFAQDEEIIKNYENIRPRALPDISEGYWKLSPKPCKIPKLEVQVNNTDAADQALLQVLMEVFSASQSIEFRLFNSSGFLESICPALELSKASVTKCSMSRLELSRAEQELLLTLPALQSLEVSETNQLPEQLFHNLHKFLGLKELCVRLDGKPDVLSVLPGEFPNLHHMEKLSIRTSTESDLSKLVKFIQNFPNLHVFHLKCDFLSNCESLMAVLASCKKLREIEFSGRCFEAMTFVNILPNFVSLKILNLKDQQFPDKETSEKFAQALGSLRNLEELLVPTGDGIHQVAKLIVRQCLQLPCLRVLTFHDILDDDSVIEIARAATSGGFQKLENLDISMNHKITEEGYRNFFQALDNLPNLQELNICRNIPGRIQVQATTVKALGQCVSRLPSLIRLHMLSWLLDEEDMKVINDVKERHPQSKRLIIFWKLIVPFSPVILE

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	Mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	NLR family CARD domain-containing protein 4
Molecular weight formula_weight	116886.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,C

MNFIRNNRRALIQRMGLTVTKQICDDLFALNVLNNQEANVIYCEPLEQEAARKIIHMTMQKGSAACNLFLKSLENWDYFVYQDLTGQNLSYQVTEEDLNVLAQNLKDLYNSPAFLNFYPLGEDIDIIFNLEKTFTEPIMWKKDHRHHRVEQLTLGSLLEALKSPCLIEGESGKGKSTLLQRIAMLWASGGCRALKGFRLVFFIHLRSARGGLFETLYDQLLNIPDFISKPTFKALLLKLHKEVLFLLDGYNEFHPQNCPEIEALIKENHRFKNMVIVTTTTECLRHIRHVGALTAEVGDMTEDSAKDLIEAVLVPDQVERLWAQIQESRCLRNLMKTPLFVVITCAIQMGRQEFQAHTQTMLFQTFYDLLIQKNSHRYRGGASGDFARSLDYCGDLALEGVFAHKFDFEPEHGSSMNEDVLVTIGLLCKYTAQRLKPTYKFFHKSFQEYTAGRRLSSLLTSKEPEEVSKGNSYLNKMVSISDITSLYGNLLLYTCGSSTEATRAVMRHLAMVYQHGSLQGLSVTKRPLWRQESIQSLRNTTEQDVLKAINVNSFVECGINLFSESMSKSDLSQEFEAFFQGKSLYINSENIPDYLFDFFEYLPNCASALDFVKLDFYERATESQDKAEENVPGVHTEGPSETYIPPRAVSLFFNWKQEFKTLEVTLRDINKLNKQDIKYLGKIFSSATNLRLHIKRCAAMAGRLSSVLRTCKNMHTLMVEASPLTTDDEQYITSVTGLQNLSIHRLHTQQLPGGLIDSLGNLKNLERLILDDIRMNEEDAKNLAEGLRSLKKMRLLHLTHLSDIGEGMDYIVKSLSEESCDLQEMKLVACCLTANSVKVLAQNLHNLIKLSILDISENYLEKDGNEALQELIGRLGVLGELTTLMLPWCWDVHTSLPKLLKQLEGTPGLAKLGLKNWRLRDEEIKSLGEFLEMNPLRDLQQLDLAGHCVSSDGWLYFMNVFENLKQLVFFDFSTEEFLPDAALVRKLSQVLSKLTLLQEVKLTGWEFDDYDISAIKGTFKLVTA

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	Mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	Flagellin
Molecular weight formula_weight	58494.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F

MEQKLISEEDLNEMEQKLISEEDLNEMEQKLISEEDLNEMEQKLISEEDLNEMEQKLISEEDLNEMESLGDLTMEQKLISEEDLNSGRPAAMAQVINTNVASLTAQRNLGVSGNMMQTSIQRLSSGLRINSAKDDAAGLAISQRMTAQIRGMNQAVRNANDGISLAQVAEGAMQETTNILQRMRELSVQAANSTNNSSDRSSIQSEISQLKSELERIAQNTEFNGQRILDGSFSGASFQVGANSNQTINFSIGSTKASSLGGIATATGTEVAGAAAADITIAIGGGAATSINSSANFTGALNGQDATSAYAKAAAINDAGIGGLSVTASTSGTQAVGAIGGTAGDTYNLTINGVAIYTNLNVATALTNSDLRDAINGVSNQTGVVASLNGGNMTLTAADGRNITVTESGTGFTAGTDGLTVTGGAFDGALRGTLSISAVDTIAIGGTVANIGLSANISKDTVGIDSLDVSTASGAQTAIKRIDAALNSVNSNRANMGALQNRFESTIANLQNVSDNLSAARSRIQDADYAAEMASLTKNQILQQAGTAMLAQANSLPQSVLSLLGR

来源 Source

来源生物 organism	Legionella pneumophila
NCBI Class编号 ncbi_taxonomy_id	446
宿主生物 host_organism	Homo sapiens

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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	—

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

Resolution resolution	5.20 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	252214

fit	/app/data/saxs_computation/b5/6b5b/6b5b.fit
pddf	/app/data/pr_computation/b5/6b5b/6b5b.pr.out
profile	/app/data/saxs_computation/b5/6b5b/6b5b.dat

Cryo-EM structure of the NAIP5-NLRC4-flagellin inflammasome

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

Baculoviral IAP repeat-containing protein 1e

State in the Current Structure

Other States of the Same Protein in the Database

NLR family CARD domain-containing protein 4

State in the Current Structure

Other States of the Same Protein in the Database

Flagellin

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)