SAXSdb — 4kqz

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

S protein

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 367–606	Fragment：UNP RESIDUES 367-606	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
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 367–606	Fragment：UNP RESIDUES 367-606	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

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 4KQZ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4KR0 Complex structure of MERS-CoV spike RBD bound to CD26 Deposited 2013-05-15	Different oligomeric state Different ligand/ion 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 ligand/ion 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 ligand/ion 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 2.80 Å
6Q06 MERS-CoV S structure in complex with 2,3-sialyl-N-acetyl-lactosamine Deposited 2019-08-01	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 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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
7V5J MERS S ectodomain trimer in complex with neutralizing antibody 0722(state 2) Deposited 2021-08-17	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 × 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
7V5K MERS S ectodomain trimer in complex with neutralizing antibody 0722 (state 1) Deposited 2021-08-17	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 × 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 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 × 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 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 × 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 oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	K0BRG7_9BETC
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–245； UniProt 367–606 Author chain B； PDBConstruct 6–245； UniProt 367–606

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	4kqz
Deposition date deposition_date	2013-05-15
Structure title title	structure of the receptor binding domain (RBD) of MERS-CoV spike
Keywords keywords	core subdomain, strand-dominated receptor binding motif, receptor binding, CD26, viral surface, VIRAL PROTEIN; VIRAL 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	27.13 Å
Radius of gyration Rg (electron density) rg_electron	26.59 Å
Forward intensity I(0) i0	34673000.00
Molecular weight molecular_weight	46205.0 kDa
Excluded volume excluded_volume	58062 Å³
Envelope volume envelope_volume	71899 Å³
Hydration-shell volume shell_volume	23859 Å³
Envelope diameter envelope_diameter	92.6 Å
Shell Rg shell_rg	32.18 Å
Envelope Rg envelope_rg	26.60 Å
Shape Rg shape_rg	26.54 Å
Total Rg total_rg	27.40 Å
Total atoms total_atoms	3244
Residues n_residues	416
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	91.6 Å
Rg (real space) rg_real	27.27 Å
Rg uncertainty (real space) rg_real_error	0.74 Å
I(0) (real space) i0_real	3.4670e+07
I(0) uncertainty (real space) i0_real_error	5.3860e+05
Rg (reciprocal space) rg_reciprocal	27.23 Å
I(0) (reciprocal space) i0_reciprocal	34670000.0000
Solution quality estimate total_estimate	0.8777
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	28.4 Å
Skewness Skewness skewness	0.458
Kurtosis Kurtosis kurtosis	-0.281
Angular range angular_range	— – 0.2900 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	4474000.0000
Real-space data points n_real_points	59
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.919; Smooth: 0.892

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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	S protein
Molecular weight formula_weight	27599.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3307

ADGIQEAKPSGSVVEQAEGVECDFSPLLSGTPPQVYNFKRLVFTNCNYNLTKLLSLFSVNDFTCSQISPAAIASNCYSSLILDYFSYPLSMKSDLSVSSAGPISQFNYKQSFSNPTCLILATVPHNLTTITKPLKYSYINKCSRLLSDDRTEVPQLVNANQYSPCVSIVPSTVWEDGDYYRKQLSPLEGGGWLVASGSTVAMTEQLQMGFGITVQYGTDTNSVCPKLEFANDTKIASQLGNCVEYHHHHHH

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 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	63

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7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	4kqzA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	1840 — Spike protein, C-terminal core receptor binding subdomain

Domain ID domain_id	4kqzA02
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	210 — ubp-family deubiquitinating enzyme fold
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	4kqzB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	1840 — Spike protein, C-terminal core receptor binding subdomain

Domain ID domain_id	4kqzB02
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	210 — ubp-family deubiquitinating enzyme fold
Homologous superfamily homologous superfamily	30 —

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8. Citations (1)

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Unit-cell length a length_a	46.977 Å
Unit-cell length b length_b	108.473 Å
Unit-cell length c length_c	125.925 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.514 Å
Low-resolution limit resolution_low	49.813 Å
R factor r_factor	0.2101
R_work r_work	0.2079
R_free r_free	0.2509

fit	/app/data/saxs_computation/kq/4kqz/4kqz.fit
pddf	/app/data/pr_computation/kq/4kqz/4kqz.pr.out
profile	/app/data/saxs_computation/kq/4kqz/4kqz.dat

structure of the receptor binding domain (RBD) of MERS-CoV spike

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

S protein

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