SAXSdb — 7v5j

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

Spike glycoprotein

Human betacoronavirus 2c EMC/2012

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 × 9 PDB declaration: nonameric（9） Consistent with protein copy count	Chain A； UniProt 18–1206 Chain B； UniProt 18–1206 Chain C； UniProt 18–1206	Not recorded	0722 L × 3 0722 H × 3	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.80 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 7V5J	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4KQZ structure of the receptor binding domain (RBD) of MERS-CoV spike Deposited 2013-05-15	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 A 367–606（240 aa） Fragment：UNP RESIDUES 367-606	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；0.1M ammonium tartrate dibasic pH7.0, 12% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.51 Å R-free 0.251
4KQZ structure of the receptor binding domain (RBD) of MERS-CoV spike Deposited 2013-05-15	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 367–606（240 aa） Fragment：UNP RESIDUES 367-606	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；0.1M ammonium tartrate dibasic pH7.0, 12% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.51 Å R-free 0.251
4KR0 Complex structure of MERS-CoV spike RBD bound to CD26 Deposited 2013-05-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 367–606（240 aa） Fragment：UNP RESIDUES 367-606	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；291 K；6% v/v 2-propanol, 0.1M sodium acetate pH4.5, 26% PEG 550, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.70 Å R-free 0.232
4MOD Structure of the MERS-CoV fusion core Deposited 2013-09-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 992–1054（63 aa） Chain A 1252–1286（35 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；0.1M BIS-TRIS, 25%(w/v) Polyethylene glycol 3350, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 1.90 Å R-free 0.213
4MOD Structure of the MERS-CoV fusion core Deposited 2013-09-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain B 992–1054（63 aa） Chain B 1252–1286（35 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；0.1M BIS-TRIS, 25%(w/v) Polyethylene glycol 3350, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 1.90 Å R-free 0.213
6Q04 MERS-CoV S structure in complex with 5-N-acetyl neuraminic acid Deposited 2019-08-01	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 19–1294（1276 aa） Chain B 19–1294（1276 aa） Chain C 19–1294（1276 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 FOL FOLIC ACID × 3 SIA N-acetyl-alpha-neuraminic acid × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.50 Å
6Q05 MERS-CoV S structure in complex with sialyl-lewisX Deposited 2019-08-01	Different construct Different oligomeric state Different ligand/ion	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 19–1294（1276 aa） Chain B 19–1294（1276 aa） Chain C 19–1294（1276 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 FOL FOLIC ACID × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
6Q06 MERS-CoV S structure in complex with 2,3-sialyl-N-acetyl-lactosamine Deposited 2019-08-01	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 19–1294（1276 aa） Chain B 19–1294（1276 aa） Chain C 19–1294（1276 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 FOL FOLIC ACID × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
6Q07 MERS-CoV S structure in complex with 2,6-sialyl-N-acetyl-lactosamine Deposited 2019-08-01	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 19–1294（1276 aa） Chain B 19–1294（1276 aa） Chain C 19–1294（1276 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24 FOL FOLIC ACID × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
7V3L MERS S ectodomain trimer in complex with neutralizing antibody 6516 Deposited 2021-08-10	Different construct Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 1–1290（1290 aa） Chain B 1–1290（1290 aa） Chain C 1–1290（1290 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.47 Å
7V5K MERS S ectodomain trimer in complex with neutralizing antibody 0722 (state 1) Deposited 2021-08-17	Parsed fields agree	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 18–1206（1189 aa） Chain B 18–1206（1189 aa） Chain C 18–1206（1189 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
7V6N MERS S ectodomain trimer in complex with neutralizing antibody 111 state1 Deposited 2021-08-20	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 18–1206（1189 aa） Chain B 18–1206（1189 aa） Chain C 18–1206（1189 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.99 Å
7V6O MERS S ectodomain trimer in complex with neutralizing antibody 111 (state 2) Deposited 2021-08-20	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 18–1206（1189 aa） Chain B 18–1206（1189 aa） Chain C 18–1206（1189 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.56 Å
7X25 MERS-CoV spike complex with S41 neutralizing antibody Fab Class4 (2u1d RBD with 3Fab) Deposited 2022-02-25	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain G 1–1290（1290 aa） Chain I 1–1290（1290 aa） Chain J 1–1290（1290 aa）	Mutation：V1060P, L1061P Mutation：V1060P, L1061P Mutation：V1060P, L1061P	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.49 Å
7X28 MERS-CoV spike complex with S41 neutralizing antibody Fab Class3 (2u1d RBD with 2Fab) Deposited 2022-02-25	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain F 1–1290（1290 aa） Chain G 1–1290（1290 aa） Chain I 1–1290（1290 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.49 Å
7X29 MERS-CoV spike complex with S41 neutralizing antibody Fab Class2 (1u2d RBD with 2Fab) Deposited 2022-02-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 1–1290（1290 aa） Chain B 1–1290（1290 aa） Chain C 1–1290（1290 aa）	Mutation：V1060P, l1061P Mutation：V1060P, l1061P Mutation：V1060P, l1061P	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.49 Å
7X2A MERS-CoV spike complex with S41 neutralizing antibody Fab Class1 (1u2d RBD with 1Fab) Deposited 2022-02-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–1290（1290 aa） Chain B 1–1290（1290 aa） Chain C 1–1290（1290 aa）	Mutation：V1060P, l1061P Mutation：V1060P, l1061P Mutation：V1060P, l1061P	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.49 Å
7YMT Cryo-EM structure of MERS-CoV spike protein, Two RBD-up conformation 2 Deposited 2022-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 17–1291（1275 aa） Chain B 17–1291（1275 aa） Chain C 17–1291（1275 aa）	Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 17	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.	Resolution 6.55 Å
7YMV Cryo-EM structure of MERS-CoV spike protein, Two RBD-up conformation 1 Deposited 2022-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 17–1291（1275 aa） Chain B 17–1291（1275 aa） Chain C 17–1291（1275 aa）	Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.	Resolution 6.74 Å
7YMW Cryo-EM structure of MERS-CoV spike protein, One RBD-up conformation 4 Deposited 2022-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 17–1291（1275 aa） Chain B 17–1291（1275 aa） Chain C 17–1291（1275 aa）	Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.	Resolution 6.05 Å
7YMX Cryo-EM structure of MERS-CoV spike protein, One RBD-up conformation 2 Deposited 2022-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 17–1291（1275 aa） Chain B 17–1291（1275 aa） Chain C 17–1291（1275 aa）	Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.	Resolution 4.44 Å
7YMY Cryo-EM structure of MERS-CoV spike protein, One RBD-up conformation 1 Deposited 2022-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 17–1291（1275 aa） Chain B 17–1291（1275 aa） Chain C 17–1291（1275 aa）	Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.	Resolution 4.96 Å
7YMZ Cryo-EM structure of MERS-CoV spike protein, intermediate conformation Deposited 2022-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 17–1291（1275 aa） Chain B 17–1291（1275 aa） Chain C 17–1291（1275 aa）	Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.	Resolution 4.39 Å
7YN0 Cryo-EM structure of MERS-CoV spike protein, all RBD-down conformation Deposited 2022-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 17–1291（1275 aa） Chain B 17–1291（1275 aa） Chain C 17–1291（1275 aa）	Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.	Resolution 4.10 Å

22 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	K0BRG7_MERS
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–1189； UniProt 18–1206 Author chain B； PDBConstruct 1–1189； UniProt 18–1206 Author chain C； PDBConstruct 1–1189； UniProt 18–1206

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	7v5j
Deposition date deposition_date	2021-08-17
Structure title title	MERS S ectodomain trimer in complex with neutralizing antibody 0722(state 2)
Keywords keywords	PROTEIN BINDING; PROTEIN BINDING
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	66.43 Å
Radius of gyration Rg (electron density) rg_electron	66.53 Å
Forward intensity I(0) i0	3740830000.00
Molecular weight molecular_weight	514030.0 kDa
Excluded volume excluded_volume	642330 Å³
Envelope volume envelope_volume	997500 Å³
Hydration-shell volume shell_volume	132900 Å³
Envelope diameter envelope_diameter	221.2 Å
Shell Rg shell_rg	61.16 Å
Envelope Rg envelope_rg	66.07 Å
Shape Rg shape_rg	66.53 Å
Total Rg total_rg	66.41 Å
Total atoms total_atoms	36183
Residues n_residues	4707
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	237.3 Å
Rg (real space) rg_real	66.55 Å
Rg uncertainty (real space) rg_real_error	2.56 Å
I(0) (real space) i0_real	3.7410e+09
I(0) uncertainty (real space) i0_real_error	9.0340e+07
Rg (reciprocal space) rg_reciprocal	66.28 Å
I(0) (reciprocal space) i0_reciprocal	3739000000.0000
Solution quality estimate total_estimate	0.8710
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	69.2 Å
Skewness Skewness skewness	0.301
Kurtosis Kurtosis kurtosis	-0.523
Angular range angular_range	— – 0.1200 Å⁻¹
Current regularization parameter α current_alpha	0.0027
Highest regularization parameter α highest_alpha	294400000.0000
Real-space data points n_real_points	25
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.848

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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	Spike glycoprotein
Molecular weight formula_weight	130718.6 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	36189

YVDVGPDSVKSACIEVDIQQTFFDKTWPRPIDVSKADGIIYPQGRTYSNITITYQGLFPYQGDHGDMYVYSAGHATGTTPQKLFVANYSQDVKQFANGFVVRIGAAANSTGTVIISPSTSATIRKIYPAFMLGSSVGNFSDGKMGRFFNHTLVLLPDGCGTLLRAFYCILEPRSGNHCPAGNSYTSFATYHTPATDCSDGNYNRNASLNSFKEYFNLRNCTFMYTYNITEDEILEWFGITQTAQGVHLFSSRYVDLYGGNMFQFATLPVYDTIKYYSIIPHSIRSIQSDRKAWAAFYVYKLQPLTFLLDFSVDGYIRRAIDCGFNDLSQLHCSYESFDVESGVYSVSSFEAKPSGSVVEQAEGVECDFSPLLSGTPPQVYNFKRLVFTNCNYNLTKLLSLFSVNDFTCSQISPAAIASNCYSSLILDYFSYPLSMKSDLSVSSAGPISQFNYKQSFSNPTCLILATVPHNLTTITKPLKYSYINKCSRLLSDDRTEVPQLVNANQYSPCVSIVPSTVWEDGDYYRKQLSPLEGGGWLVASGSTVAMTEQLQMGFGITVQYGTDTNSVCPKLEFANDTKIASQLGNCVEYSLYGVSGRGVFQNCTAVGVRQQRFVYDAYQNLVGYYSDDGNYYCLRACVSVPVSVIYDKETKTHATLFGSVACEHISSTMSQYSRSTRSMLKRRDSTYGPLQTPVGCVLGLVNSSLFVEDCKLPLGQSLCALPDTPSTLTPRSVRSVPGEMRLASIAFNHPIQVDQLNSSYFKLSIPTNFSFGVTQEYIQTTIQKVTVDCKQYVCNGFQKCEQLLREYGQFCSKINQALHGANLRQDDSVRNLFASVKSSQSSPIIPGFGGDFNLTLLEPVSISTGSRSARSAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFQKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVA

来源 Source

来源生物 organism	Human betacoronavirus 2c EMC/2012
NCBI Class编号 ncbi_taxonomy_id	1235996
宿主生物 host_organism	Trichoplusia ni

Entity 2 Entity 2 polymer

Description description	0722 L
Molecular weight formula_weight	23029.5 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,F,H

DIVMTQTPSSLSASVGDRVTITCRASEDITSYLNWYQLKPGKAPMFLIYAASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPPTFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRG

来源 Source

来源生物 organism	Homo sapiens
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	0722 H
Molecular weight formula_weight	23690.5 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,G,I

QVQLVQSGAEVKKPGSSVKVSCKASGGTFSIYAISWVRQAPGQGLEWMGGIIPIFGTANYAQQFQGRVTITADESTTTAYMELSRLTSEDTAVYYCARQMTAYDYWNPSFDYWGQGTLVTVSSAWSTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRV

来源 Source

来源生物 organism	Homo sapiens
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

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7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	7v5jD01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	7v5jD02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	7v5jE01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	7v5jE02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	7v5jF01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	7v5jF02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	7v5jG01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	7v5jG02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	7v5jH01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	7v5jH02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	7v5jI01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	7v5jI02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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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	2.80 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	1463548

fit	/app/data/saxs_computation/v5/7v5j/7v5j.fit
pddf	/app/data/pr_computation/v5/7v5j/7v5j.pr.out
profile	/app/data/saxs_computation/v5/7v5j/7v5j.dat

MERS S ectodomain trimer in complex with neutralizing antibody 0722(state 2)

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

Spike glycoprotein

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

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)