PDB-5iwe: E45Q mutant of phenazine biosynthesis protein PhzF in complex wit...

ID or keywords:

Entry

Database: PDB / ID: 5iwe

Title

E45Q mutant of phenazine biosynthesis protein PhzF in complex with (5R,6R)-6-azaniumyl-5-ethoxycyclohexa-1,3-diene-1-carboxylate

Components

Trans-2,3-dihydro-3-hydroxyanthranilate isomerase

Keywords

ISOMERASE / complex / substrate analogue

Function / homology

Function and homology information

trans-2,3-dihydro-3-hydroxyanthranilate isomerase / trans-2,3-dihydro-3-hydroxy-anthranilate isomerase activity / phenazine biosynthetic process / cytoplasm
Similarity search - Function

Biological species

Pseudomonas fluorescens (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.71 Å

Authors

Diederich, C. / Blankenfeldt, W.

Funding support

Germany,

Austria, 2items

Citation

Journal: Sci Rep / Year: 2017
Title: Mechanisms and Specificity of Phenazine Biosynthesis Protein PhzF.
Authors: Diederich, C. / Leypold, M. / Culka, M. / Weber, H. / Breinbauer, R. / Ullmann, G.M. / Blankenfeldt, W.

History

Deposition	Mar 22, 2016	Deposition site: RCSB / Processing site: PDBE
Revision 1.0	Mar 29, 2017	Provider: repository / Type: Initial release
Revision 1.1	Aug 9, 2017	Group: Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.name
Revision 1.2	Jan 10, 2024	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5iwe.cif.gz	181.3 KB	Display	PDBx/mmCIF format
PDB format	pdb5iwe.ent.gz	147.1 KB	Display	PDB format
PDBx/mmJSON format	5iwe.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	5iwe_validation.pdf.gz	462.9 KB	Display	wwPDB validaton report
Full document	5iwe_full_validation.pdf.gz	464.1 KB	Display
Data in XML	5iwe_validation.xml.gz	15.3 KB	Display
Data in CIF	5iwe_validation.cif.gz	22.3 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/iw/5iwe ftp://data.pdbj.org/pub/pdb/validation_reports/iw/5iwe	HTTPS FTP

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Related structure data

Related structure data	1u1vS S: Starting model for refinement
Similar structure data	1fsg-d 6h7s-d 1acy-d 1wzi-d 6rlm-4 6vrp-d 4m61-1 5rg7-d 2hjr-10 1pk5-d Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Trans-2,3-dihydro-3-hydroxyanthranilate isomerase

hetero molecules

33 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Trans-2,3-dihydro-3-hydroxyanthranilate isomerase

hetero molecules

A: Trans-2,3-dihydro-3-hydroxyanthranilate isomerase

hetero molecules

defined by author
65.9 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	56.032, 56.032, 155.742
Angle α, β, γ (deg.)	90.00, 90.00, 120.00
Int Tables number	154
Space group name H-M	P3₂21

Components on special symmetry positions

ID	Model	Components
1	1	A-465- HOH
2	1	A-569- HOH

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Protein , 1 types, 1 molecules A

#1: Protein	Trans-2,3-dihydro-3-hydroxyanthranilate isomerase / Phenazine/pyocyanine biosynthesis protein PhzF Mass: 32255.576 Da / Num. of mol.: 1 / Mutation: E45Q Source method: isolated from a genetically manipulated source Details: The first 19 residues consist of the N-terminal expression tag and are neither natural nor visible in the structure Source: (gene. exp.) Pseudomonas fluorescens (bacteria) / Gene: phzF / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta 2 (pLysS) References: UniProt: Q51792, trans-2,3-dihydro-3-hydroxyanthranilate isomerase

#1: Protein

Trans-2,3-dihydro-3-hydroxyanthranilate isomerase / Phenazine/pyocyanine biosynthesis protein PhzF

Mass: 32255.576 Da / Num. of mol.: 1 / Mutation: E45Q
Source method: isolated from a genetically manipulated source
Details: The first 19 residues consist of the N-terminal expression tag and are neither natural nor visible in the structure
Source: (gene. exp.)

Pseudomonas fluorescens (bacteria) / Gene: phzF / Production host:

Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta 2 (pLysS)
References: UniProt: Q51792, trans-2,3-dihydro-3-hydroxyanthranilate isomerase

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Non-polymers , 5 types, 249 molecules

#2: Chemical	ChemComp-W81 / (5R,6R)-6-azaniumyl-5-ethoxycyclohexa-1,3-diene-1-carboxylate Mass: 183.204 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₉H₁₃NO₃
#3: Chemical	ChemComp-PEG / DI(HYDROXYETHYL)ETHER Mass: 106.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₄H₁₀O₃
#4: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₂H₆O₂
#5: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₃H₈O₃
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 242 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 2.26 Å³/Da / Density % sol: 45.5 %
Crystal grow	Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 4.6 Details: 0.085M sodium acetate pH 4.6, 0.17M ammonium acetate, 25.5% (w/v) PEG 4000, 15% (v/v) glycerol, temperature 293.15K, VAPOR DIFFUSION, SITTING DROP

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.91841 Å
Detector	Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 7, 2015
Radiation	Monochromator: Si-111 crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.91841 Å / Relative weight: 1
Reflection	Resolution: 1.71→77.87 Å / Num. obs: 31593 / % possible obs: 99.9 % / Redundancy: 5.2 % / R_merge(I) obs: 0.124 / Net I/σ(I): 8.9
Reflection shell	Resolution: 1.71→1.74 Å / Redundancy: 4.5 % / R_merge(I) obs: 0.754 / Mean I/σ(I) obs: 1.9 / % possible all: 99.9

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Processing

Software

Name	Version	Classification
PHENIX	(1.10.1_2155: ???)	refinement
XDS	v.052	data reduction
Aimless	0.5.17	data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 1U1V

1u1v

Resolution: 1.71→46.328 Å / SU ML: 0.16 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 15.89 / Details: TLS-refinement

	R_factor	Num. reflection	% reflection
R_free	0.1734	1612	5.11 %
R_work	0.1492	-	-
obs	0.1505	31532	99.86 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å

Refinement step

Cycle: LAST / Resolution: 1.71→46.328 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	2124	0	47	242	2413

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	2270
X-RAY DIFFRACTION	f_angle_d	0.945	3083
X-RAY DIFFRACTION	f_dihedral_angle_d	11.658	1367
X-RAY DIFFRACTION	f_chiral_restr	0.059	340
X-RAY DIFFRACTION	f_plane_restr	0.007	411

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	% reflection obs (%)
1.71-1.7604	0.272	139	0.2378	2457	X-RAY DIFFRACTION	100
1.7604-1.8172	0.2165	126	0.2001	2441	X-RAY DIFFRACTION	100
1.8172-1.8821	0.1947	134	0.1819	2453	X-RAY DIFFRACTION	100
1.8821-1.9575	0.2148	134	0.1728	2440	X-RAY DIFFRACTION	100
1.9575-2.0466	0.1714	140	0.147	2458	X-RAY DIFFRACTION	100
2.0466-2.1545	0.1922	125	0.1377	2481	X-RAY DIFFRACTION	100
2.1545-2.2895	0.1765	138	0.1369	2440	X-RAY DIFFRACTION	100
2.2895-2.4662	0.1618	131	0.1282	2504	X-RAY DIFFRACTION	100
2.4662-2.7144	0.174	125	0.1275	2505	X-RAY DIFFRACTION	100
2.7144-3.1071	0.1398	125	0.1273	2536	X-RAY DIFFRACTION	100
3.1071-3.9143	0.1527	151	0.1255	2521	X-RAY DIFFRACTION	100
3.9143-46.3455	0.168	144	0.1707	2684	X-RAY DIFFRACTION	100

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°²)	L12 (°²)	L13 (°²)	L22 (°²)	L23 (°²)	L33 (°²)	S11 (Å °)	S12 (Å °)	S13 (Å °)	S21 (Å °)	S22 (Å °)	S23 (Å °)	S31 (Å °)	S32 (Å °)	S33 (Å °)	T11 (Å²)	T12 (Å²)	T13 (Å²)	T22 (Å²)	T23 (Å²)	T33 (Å²)	Origin x (Å)	Origin y (Å)	Origin z (Å)
1	1.5929	-0.7458	0.2621	1.0797	-0.1427	1.3181	-0.0132	-0.0143	-0.0026	-0.0326	-0.0016	0.0308	-0.1524	-0.0854	0.0166	0.1168	-0.0064	-0.0031	0.0918	0.0113	0.073	15.7666	34.4172	7.1087
2	0.8159	0.6377	0.9072	1.7856	2.2031	3.8872	-0.0122	-0.0342	0.0148	-0.0531	-0.0049	0.1271	-0.1589	-0.2044	0.045	0.1085	-0.0028	0.0137	0.1233	0.0191	0.1181	9.8927	34.1311	17.1868
3	3.2181	-0.0582	-0.1716	1.4378	0.9999	2.6538	0.0547	-0.1105	0.2349	0.102	0.0253	-0.1216	-0.1113	-0.0212	-0.0816	0.1298	-0.0023	-0.0221	0.0881	0.0269	0.1172	20.6434	35.6967	20.7601
4	0.4222	-0.1417	-0.0627	0.8727	-0.3497	0.3888	-0.0238	-0.0083	0.0402	0.0096	0.0273	0.1554	-0.0187	0.0115	0.0028	0.0907	-0.0007	-0.0042	0.0858	0.0066	0.0845	17.2622	16.4912	20.9822
5	4.9578	-1.5813	0.2918	2.4451	-0.4766	1.8525	0.1047	0.4223	0.0832	-0.5336	-0.0564	0.158	0.0997	-0.1193	-0.0257	0.2107	-0.028	-0.0446	0.0934	0.0125	0.1305	15.2229	5.4222	9.4622
6	0.2095	-0.709	-0.0518	2.6766	-0.0337	3.1746	-0.0701	0.0229	0.0032	-0.1243	-0.0136	-0.1205	-0.0402	0.1552	0.0923	0.1206	-0.0057	0.0082	0.0826	0.0286	0.0909	24.7668	10.2109	16.8686
7	0.6802	-0.0002	-0.4456	1.5482	-0.4991	0.8347	0.0278	0.0609	-0.0008	-0.1518	-0.0216	0.0109	-0.0488	0.0097	-0.0189	0.1181	-0.0013	-0.0058	0.0691	0.0029	0.0821	21.6133	14.0882	18.2896
8	0.5644	-0.1545	-0.2401	2.1215	-1.3466	1.5252	-0.0342	-0.075	-0.0662	0.1908	-0.1033	-0.0438	-0.1155	0.1155	0.1104	0.1096	-0.0293	-0.0238	0.0897	-0.0142	0.0859	23.297	25.7342	20.8457

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 0 through 50 )) or ( chain 'B' and resid 2 ) or ( chain 'B' and resid 12 ) or ( chain 'B' and resid 14 ) or ( chain 'B' and resid 20 ) or ( chain 'B' and resid 28 ) or ( chain 'B' and resid 30 ) or ( chain 'B' and resid 32 ) or ( chain 'B' and resid 35 ) or ( chain 'B' and resid 37 ) or ( chain 'B' and resid 39 ) or ( chain 'B' and resid 43 ) or ( chain 'B' and resid 51 ) or ( chain 'B' and resid 62 ) or ( chain 'B' and resid 70 ) or ( chain 'B' and resid 72 ) or ( chain 'B' and resid 73 ) or ( chain 'B' and resid 102 ) or ( chain 'B' and resid 104 ) or ( chain 'B' and resid 108 ) or ( chain 'B' and resid 110 ) or ( chain 'B' and resid 111 ) or ( chain 'B' and resid 112 ) or ( chain 'B' and resid 121 ) or ( chain 'B' and resid 124 ) or ( chain 'B' and resid 125 ) or ( chain 'B' and resid 127 ) or ( chain 'B' and resid 134 ) or ( chain 'B' and resid 138 ) or ( chain 'B' and resid 141 ) or ( chain 'B' and resid 142 ) or ( chain 'B' and resid 158 ) or ( chain 'B' and resid 159 ) or ( chain 'B' and resid 160 ) or ( chain 'B' and resid 162 ) or ( chain 'B' and resid 163 ) or ( chain 'B' and resid 164 ) or ( chain 'B' and resid 165 ) or ( chain 'B' and resid 166 ) or ( chain 'B' and resid 167 ) or ( chain 'B' and resid 168 ) or ( chain 'B' and resid 220 ) or ( chain 'B' and resid 223 ) or ( chain 'B' and resid 241 ) or ( chain 'B' and resid 242 ) or ( chain 'D' and resid 2 ))
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 51 through 72 )) or ( chain 'B' and resid 5 ) or ( chain 'B' and resid 24 ) or ( chain 'B' and resid 25 ) or ( chain 'B' and resid 31 ) or ( chain 'B' and resid 38 ) or ( chain 'B' and resid 56 ) or ( chain 'B' and resid 67 ) or ( chain 'B' and resid 84 ) or ( chain 'B' and resid 105 ) or ( chain 'B' and resid 114 ) or ( chain 'B' and resid 126 ) or ( chain 'B' and resid 128 ) or ( chain 'B' and resid 129 ) or ( chain 'B' and resid 131 ) or ( chain 'B' and resid 132 ) or ( chain 'B' and resid 133 ) or ( chain 'B' and resid 146 ) or ( chain 'B' and resid 169 ) or ( chain 'B' and resid 170 ) or ( chain 'B' and resid 171 ) or ( chain 'B' and resid 172 ) or ( chain 'B' and resid 177 ) or ( chain 'B' and resid 178 ) or ( chain 'B' and resid 180 ) or ( chain 'B' and resid 183 ) or ( chain 'B' and resid 229 ) or ( chain 'B' and resid 230 ) or ( chain 'E' and resid 1 ))
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 73 through 98 )) or ( chain 'B' and resid 68 ) or ( chain 'B' and resid 69 ) or ( chain 'B' and resid 89 ) or ( chain 'B' and resid 91 ) or ( chain 'B' and resid 99 ) or ( chain 'B' and resid 103 ) or ( chain 'B' and resid 116 ) or ( chain 'B' and resid 179 ) or ( chain 'B' and resid 189 ) or ( chain 'B' and resid 190 ) or ( chain 'B' and resid 191 ) or ( chain 'B' and resid 204 ) or ( chain 'B' and resid 233 ) or ( chain 'B' and resid 234 ) or ( chain 'B' and resid 237 ) or ( chain 'B' and resid 239 ) or ( chain 'E' and resid 2 ))
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 99 through 159 )) or ( chain 'B' and resid 1 ) or ( chain 'B' and resid 3 ) or ( chain 'B' and resid 15 ) or ( chain 'B' and resid 16 ) or ( chain 'B' and resid 21 ) or ( chain 'B' and resid 23 ) or ( chain 'B' and resid 26 ) or ( chain 'B' and resid 29 ) or ( chain 'B' and resid 34 ) or ( chain 'B' and resid 36 ) or ( chain 'B' and resid 40 ) or ( chain 'B' and resid 41 ) or ( chain 'B' and resid 42 ) or ( chain 'B' and resid 47 ) or ( chain 'B' and resid 48 ) or ( chain 'B' and resid 49 ) or ( chain 'B' and resid 52 ) or ( chain 'B' and resid 53 ) or ( chain 'B' and resid 57 ) or ( chain 'B' and resid 58 ) or ( chain 'B' and resid 59 ) or ( chain 'B' and resid 64 ) or ( chain 'B' and resid 71 ) or ( chain 'B' and resid 76 ) or ( chain 'B' and resid 81 ) or ( chain 'B' and resid 83 ) or ( chain 'B' and resid 92 ) or ( chain 'B' and resid 93 ) or ( chain 'B' and resid 101 ) or ( chain 'B' and resid 118 ) or ( chain 'B' and resid 130 ) or ( chain 'B' and resid 137 ) or ( chain 'B' and resid 139 ) or ( chain 'B' and resid 144 ) or ( chain 'B' and resid 145 ) or ( chain 'B' and resid 150 ) or ( chain 'B' and resid 151 ) or ( chain 'B' and resid 156 ) or ( chain 'B' and resid 181 ) or ( chain 'B' and resid 182 ) or ( chain 'B' and resid 185 ) or ( chain 'B' and resid 188 ) or ( chain 'B' and resid 192 ) or ( chain 'B' and resid 193 ) or ( chain 'B' and resid 194 ) or ( chain 'B' and resid 195 ) or ( chain 'B' and resid 196 ) or ( chain 'B' and resid 197 ) or ( chain 'B' and resid 198 ) or ( chain 'B' and resid 199 ) or ( chain 'B' and resid 201 ) or ( chain 'B' and resid 203 ) or ( chain 'B' and resid 226 ) or ( chain 'B' and resid 228 ) or ( chain 'B' and resid 231 ) or ( chain 'B' and resid 232 ) or ( chain 'B' and resid 235 ) or ( chain 'B' and resid 238 ) or ( chain 'B' and resid 240 ) or ( chain 'D' and resid 1 ) or ( chain 'F' and resid 1 ))
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 160 through 182 )) or ( chain 'B' and resid 10 ) or ( chain 'B' and resid 27 ) or ( chain 'B' and resid 44 ) or ( chain 'B' and resid 54 ) or ( chain 'B' and resid 74 ) or ( chain 'B' and resid 79 ) or ( chain 'B' and resid 86 ) or ( chain 'B' and resid 87 ) or ( chain 'B' and resid 95 ) or ( chain 'B' and resid 97 ) or ( chain 'B' and resid 119 ) or ( chain 'B' and resid 122 ) or ( chain 'B' and resid 135 ) or ( chain 'B' and resid 136 ) or ( chain 'B' and resid 148 ) or ( chain 'B' and resid 153 ) or ( chain 'B' and resid 154 ) or ( chain 'B' and resid 155 ) or ( chain 'B' and resid 157 ) or ( chain 'B' and resid 200 ) or ( chain 'B' and resid 202 ) or ( chain 'B' and resid 206 ) or ( chain 'B' and resid 207 ) or ( chain 'B' and resid 211 ) or ( chain 'B' and resid 212 ) or ( chain 'B' and resid 213 ))
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 183 through 199 )) or ( chain 'B' and resid 6 ) or ( chain 'B' and resid 7 ) or ( chain 'B' and resid 8 ) or ( chain 'B' and resid 11 ) or ( chain 'B' and resid 55 ) or ( chain 'B' and resid 78 ) or ( chain 'B' and resid 80 ) or ( chain 'B' and resid 82 ) or ( chain 'B' and resid 106 ) or ( chain 'B' and resid 117 ) or ( chain 'B' and resid 147 ) or ( chain 'B' and resid 152 ) or ( chain 'B' and resid 205 ) or ( chain 'B' and resid 224 ))
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 200 through 245 )) or ( chain 'B' and resid 4 ) or ( chain 'B' and resid 17 ) or ( chain 'B' and resid 22 ) or ( chain 'B' and resid 45 ) or ( chain 'B' and resid 50 ) or ( chain 'B' and resid 65 ) or ( chain 'B' and resid 77 ) or ( chain 'B' and resid 85 ) or ( chain 'B' and resid 90 ) or ( chain 'B' and resid 94 ) or ( chain 'B' and resid 98 ) or ( chain 'B' and resid 113 ) or ( chain 'B' and resid 115 ) or ( chain 'B' and resid 123 ) or ( chain 'B' and resid 143 ) or ( chain 'B' and resid 173 ) or ( chain 'B' and resid 174 ) or ( chain 'B' and resid 175 ) or ( chain 'B' and resid 176 ) or ( chain 'B' and resid 208 ) or ( chain 'B' and resid 209 ) or ( chain 'B' and resid 210 ) or ( chain 'B' and resid 214 ) or ( chain 'B' and resid 215 ) or ( chain 'B' and resid 216 ) or ( chain 'B' and resid 227 ) or ( chain 'C' and resid 1 ))
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 246 through 278 )) or ( chain 'B' and resid 9 ) or ( chain 'B' and resid 13 ) or ( chain 'B' and resid 18 ) or ( chain 'B' and resid 19 ) or ( chain 'B' and resid 33 ) or ( chain 'B' and resid 46 ) or ( chain 'B' and resid 60 ) or ( chain 'B' and resid 61 ) or ( chain 'B' and resid 63 ) or ( chain 'B' and resid 66 ) or ( chain 'B' and resid 75 ) or ( chain 'B' and resid 88 ) or ( chain 'B' and resid 96 ) or ( chain 'B' and resid 100 ) or ( chain 'B' and resid 107 ) or ( chain 'B' and resid 109 ) or ( chain 'B' and resid 120 ) or ( chain 'B' and resid 140 ) or ( chain 'B' and resid 149 ) or ( chain 'B' and resid 161 ) or ( chain 'B' and resid 184 ) or ( chain 'B' and resid 186 ) or ( chain 'B' and resid 187 ) or ( chain 'B' and resid 217 ) or ( chain 'B' and resid 218 ) or ( chain 'B' and resid 219 ) or ( chain 'B' and resid 221 ) or ( chain 'B' and resid 222 ) or ( chain 'B' and resid 225 ) or ( chain 'B' and resid 236 ))

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Protein , 1 types, 1 molecules A

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Non-polymers , 5 types, 249 molecules

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Experimental details

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Experiment

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Sample preparation

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About Yorodumi

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Feb 9, 2022. New format data for meta-information of EMDB entries

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-Protein , 1 types, 1 molecules A

-Non-polymers , 5 types, 249 molecules

-Experimental details

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Protein , 1 types, 1 molecules A

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Non-polymers , 5 types, 249 molecules

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