Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3VRB

Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil and substrate fumarate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000104	molecular_function	succinate dehydrogenase activity
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0006099	biological_process	tricarboxylic acid cycle
A	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
A	0008177	molecular_function	succinate dehydrogenase (quinone) activity
A	0009055	molecular_function	electron transfer activity
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0022900	biological_process	electron transport chain
A	0031966	cellular_component	mitochondrial membrane
A	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0006099	biological_process	tricarboxylic acid cycle
B	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
B	0008177	molecular_function	succinate dehydrogenase (quinone) activity
B	0009055	molecular_function	electron transfer activity
B	0009060	biological_process	aerobic respiration
B	0016491	molecular_function	oxidoreductase activity
B	0022904	biological_process	respiratory electron transport chain
B	0031966	cellular_component	mitochondrial membrane
B	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0051538	molecular_function	3 iron, 4 sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0005515	molecular_function	protein binding
C	0005743	cellular_component	mitochondrial inner membrane
C	0006099	biological_process	tricarboxylic acid cycle
C	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
C	0009055	molecular_function	electron transfer activity
C	0016020	cellular_component	membrane
C	0020037	molecular_function	heme binding
C	0031966	cellular_component	mitochondrial membrane
C	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
C	0046872	molecular_function	metal ion binding
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005740	cellular_component	mitochondrial envelope
D	0005743	cellular_component	mitochondrial inner membrane
D	0006099	biological_process	tricarboxylic acid cycle
D	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
D	0016020	cellular_component	membrane
D	0020037	molecular_function	heme binding
D	0031966	cellular_component	mitochondrial membrane
D	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
D	0046872	molecular_function	metal ion binding
D	0048039	molecular_function	ubiquinone binding
E	0000104	molecular_function	succinate dehydrogenase activity
E	0000166	molecular_function	nucleotide binding
E	0005515	molecular_function	protein binding
E	0005739	cellular_component	mitochondrion
E	0005743	cellular_component	mitochondrial inner membrane
E	0006099	biological_process	tricarboxylic acid cycle
E	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
E	0008177	molecular_function	succinate dehydrogenase (quinone) activity
E	0009055	molecular_function	electron transfer activity
E	0016491	molecular_function	oxidoreductase activity
E	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
E	0022900	biological_process	electron transport chain
E	0031966	cellular_component	mitochondrial membrane
E	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
E	0050660	molecular_function	flavin adenine dinucleotide binding
F	0005515	molecular_function	protein binding
F	0005739	cellular_component	mitochondrion
F	0005743	cellular_component	mitochondrial inner membrane
F	0006099	biological_process	tricarboxylic acid cycle
F	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
F	0008177	molecular_function	succinate dehydrogenase (quinone) activity
F	0009055	molecular_function	electron transfer activity
F	0009060	biological_process	aerobic respiration
F	0016491	molecular_function	oxidoreductase activity
F	0022904	biological_process	respiratory electron transport chain
F	0031966	cellular_component	mitochondrial membrane
F	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
F	0046872	molecular_function	metal ion binding
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0051538	molecular_function	3 iron, 4 sulfur cluster binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0005515	molecular_function	protein binding
G	0005743	cellular_component	mitochondrial inner membrane
G	0006099	biological_process	tricarboxylic acid cycle
G	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
G	0009055	molecular_function	electron transfer activity
G	0016020	cellular_component	membrane
G	0020037	molecular_function	heme binding
G	0031966	cellular_component	mitochondrial membrane
G	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
G	0046872	molecular_function	metal ion binding
H	0005515	molecular_function	protein binding
H	0005739	cellular_component	mitochondrion
H	0005740	cellular_component	mitochondrial envelope
H	0005743	cellular_component	mitochondrial inner membrane
H	0006099	biological_process	tricarboxylic acid cycle
H	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
H	0016020	cellular_component	membrane
H	0020037	molecular_function	heme binding
H	0031966	cellular_component	mitochondrial membrane
H	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
H	0046872	molecular_function	metal ion binding
H	0048039	molecular_function	ubiquinone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FUM A 701

Chain	Residue
A	GLY85
A	HIS276
A	THR288
A	GLU289
A	ARG320
A	HIS387
A	ARG432
A	ALA435
A	FAD702

site_id	AC2
Number of Residues	33
Details	BINDING SITE FOR RESIDUE FAD A 702

Chain	Residue
A	GLY48
A	ALA49
A	GLY50
A	GLY51
A	ALA52
A	THR71
A	LYS72
A	MET73
A	SER78
A	HIS79
A	THR80
A	ALA83
A	GLN84
A	GLY85
A	GLY86
A	TYR199
A	ALA201
A	ALA235
A	THR236
A	GLY237
A	THR247
A	ASP255
A	LEU286
A	HIS387
A	TYR388
A	GLY420
A	GLU421
A	ARG432
A	ALA435
A	ASN436
A	SER437
A	LEU438
A	FUM701

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES B 301

Chain	Residue
B	SER88
B	CYS89
B	ILE93
B	CYS94
B	GLY95
B	CYS97
B	CYS109

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B 302

Chain	Residue
B	CYS182
B	ILE183
B	LEU184
B	CYS185
B	ALA186
B	CYS187
B	CYS188
B	CYS249
B	LEU253

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE F3S B 303

Chain	Residue
B	CYS192
B	TYR202
B	CYS239
B	HIS240
B	THR241
B	ILE242
B	MET243
B	CYS245

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM C 201

Chain	Residue
B	HIS240
C	HIS75
C	ARG76
C	GLY79
C	MET82
C	HIS131
C	THR132
D	ARG63
D	ALA66
D	MET69
D	VAL70
D	HIS95

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FTN C 202

Chain	Residue
B	PRO193
B	SER194
B	TRP197
B	HIS240
C	TRP69
C	SER72
C	ARG76
D	ASP106
D	TYR107

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EPH D 201

Chain	Residue
C	MET82
C	THR85
C	PRO127
C	LEU133
C	VAL170
D	ALA76
D	TYR77
D	HIS80
D	PHE150
D	GLU151
D	TRP154

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FUM E 701

Chain	Residue
E	GLY85
E	PHE153
E	HIS276
E	THR288
E	GLU289
E	ARG320
E	HIS387
E	ARG432
E	ALA435
E	FAD702
E	GLN84

site_id	BC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD E 702

Chain	Residue
E	ALA49
E	GLY50
E	GLY51
E	ALA52
E	THR71
E	LYS72
E	MET73
E	SER78
E	HIS79
E	THR80
E	ALA83
E	GLN84
E	GLY85
E	GLY86
E	TYR199
E	PHE200
E	ALA201
E	ALA235
E	THR236
E	GLY237
E	ASN252
E	ASP255
E	LEU286
E	HIS387
E	TYR388
E	GLY420
E	GLU421
E	ARG432
E	ALA435
E	SER437
E	LEU438
E	FUM701

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES F 301

Chain	Residue
F	SER88
F	CYS89
F	GLY92
F	ILE93
F	CYS94
F	GLY95
F	CYS97
F	CYS109

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 F 302

Chain	Residue
F	CYS182
F	ILE183
F	CYS185
F	ALA186
F	CYS187
F	CYS188
F	CYS249
F	PRO250
F	LEU253

site_id	BC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE F3S F 303

Chain	Residue
F	CYS192
F	TYR202
F	PRO205
F	CYS239
F	HIS240
F	THR241
F	ILE242
F	MET243
F	CYS245
F	ILE259

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FTN F 304

Chain	Residue
F	PRO193
F	SER194
F	TRP196
F	TRP197
F	HIS240
G	TRP69
G	SER72
G	ARG76
H	ASP106
H	TYR107

site_id	BC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM G 201

Chain	Residue
F	HIS240
G	HIS75
G	ARG76
G	GLY79
G	MET82
G	HIS131
G	THR132
G	GLY135
H	ARG63
H	MET69
H	HIS95
H	VAL96
H	GLY99

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EPH H 201

Chain	Residue
G	MET82
G	THR85
G	ILE123
G	PRO174
H	ILE73
H	ALA76
H	TYR77
H	HIS80
H	PHE150
H	TRP154
H	GLU155

Functional Information from PROSITE/UniProt

site_id	PS00197
Number of Residues	9
Details	2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CREGICGSC

Chain	Residue	Details
B	CYS89-CYS97

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCSaSCP

Chain	Residue	Details
B	CYS182-PRO193

site_id	PS00504
Number of Residues	10
Details	FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTtaAqGG

Chain	Residue	Details
A	ARG77-GLY86

site_id	PS01000
Number of Residues	25
Details	SDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPIaphLtiykpqMtwmvSglHRvT

Chain	Residue	Details
C	ARG54-THR78

site_id	PS01001
Number of Residues	14
Details	SDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HtlnGIRFIgFDmA

Chain	Residue	Details
C	HIS131-ALA144

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PIRSR","id":"PIRSR611281-1","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	38
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26198225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C2T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C3J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26198225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C2T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C3J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26198225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YT0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26198225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C2T","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26198225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C2T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C3J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VRB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26198225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C2T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C3J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"PIRSR","id":"PIRSR611281-4","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	180
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	60
Details	Domain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C3J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	264
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	70
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	52
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26198225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VRB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YSZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C2T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C3J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22577165","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VR8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)