PDB-3qnf: Crystal structure of the open state of human endoplasmic reticulu...

ID or keywords:

Entry

Database: PDB / ID: 3qnf

Title

Crystal structure of the open state of human endoplasmic reticulum aminopeptidase 1 ERAP1

Components

Endoplasmic reticulum aminopeptidase 1

Keywords

HYDROLASE / Structural Genomics Consortium / SGC / glycoprotein / metal-binding / metalloprotease / protease / adaptive immunity

Function / homology

Function and homology information

interleukin-1, type II receptor binding / interleukin-6 receptor binding / Hydrolases; Acting on peptide bonds (peptidases); Aminopeptidases / metalloexopeptidase activity / regulation of innate immune response / peptide catabolic process / fat cell differentiation / metalloaminopeptidase activity / antigen processing and presentation of peptide antigen via MHC class I / membrane protein ectodomain proteolysis ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3 Å

Authors

Vollmar, M. / Kochan, G. / Krojer, T. / Harvey, D. / Chaikuad, A. / Allerston, C. / Muniz, J.R.C. / Raynor, J. / Ugochukwu, E. / Berridge, G. ...

Citation

Journal: Proc.Natl.Acad.Sci.USA / Year: 2011
Title: Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.
Authors: Kochan, G. / Krojer, T. / Harvey, D. / Fischer, R. / Chen, L. / Vollmar, M. / von Delft, F. / Kavanagh, K.L. / Brown, M.A. / Bowness, P. / Wordsworth, P. / Kessler, B.M. / Oppermann, U.

History

Deposition	Feb 8, 2011	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Feb 23, 2011	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Version format compliance
Revision 1.2	Jan 31, 2018	Group: Structure summary / Category: audit_author / Item: _audit_author.name
Revision 2.0	Jul 29, 2020	Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary Category: atom_site / chem_comp ...atom_site / chem_comp / database_PDB_caveat / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_validate_chiral / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.pdbx_formal_charge / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq_dif.details Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1	Sep 13, 2023	Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2	Nov 20, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Summary document	3qnf_validation.pdf.gz	775.6 KB	Display	wwPDB validaton report
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Data in XML	3qnf_validation.xml.gz	76.4 KB	Display
Data in CIF	3qnf_validation.cif.gz	105.2 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/qn/3qnf ftp://data.pdbj.org/pub/pdb/validation_reports/qn/3qnf	HTTPS FTP

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Related structure data

Related structure data	2yd0C 2xdt PDB Unreleased entryS C: citing same article (ref.) S: Starting model for refinement
Similar structure data	6qyy-d 5cxg-d 5uxd-d 4nmj-1 3uu0-2 4h7n-1 3rce-d 5u0m-d 4nmk-4 4nmk-2 Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) 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

Related structure data

2yd0C

2xdt
PDB Unreleased entryS

C: citing same article (ref.)

S: Starting model for refinement

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Endoplasmic reticulum aminopeptidase 1

B: Endoplasmic reticulum aminopeptidase 1

C: Endoplasmic reticulum aminopeptidase 1

hetero molecules

329 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Endoplasmic reticulum aminopeptidase 1

hetero molecules

defined by author&software
110 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Endoplasmic reticulum aminopeptidase 1

hetero molecules

defined by author&software
110 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: Endoplasmic reticulum aminopeptidase 1

hetero molecules

defined by author&software
110 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	97.246, 132.816, 233.687
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Refine code	Auth asym-ID	Auth seq-ID
1	1	1	1	B	46 - 70
2	1	1	1	A	46 - 70
3	1	1	1	C	46 - 70
1	1	2	1	B	71 - 75
2	1	2	1	A	71 - 75
3	1	2	1	C	71 - 75
1	1	3	1	B	76 - 87
2	1	3	1	A	76 - 87
3	1	3	1	C	76 - 87
1	1	4	1	B	88 - 92
2	1	4	1	A	88 - 92
3	1	4	1	C	88 - 92
1	1	5	1	B	93 - 98
2	1	5	1	A	93 - 98
3	1	5	1	C	93 - 98
1	1	6	1	B	99 - 104
2	1	6	1	A	99 - 104
3	1	6	1	C	99 - 104
1	1	7	1	B	105 - 108
2	1	7	1	A	105 - 108
3	1	7	1	C	105 - 108
1	1	8	1	B	116 - 125
2	1	8	1	A	116 - 125
3	1	8	1	C	116 - 125
1	1	9	1	B	126 - 129
2	1	9	1	A	126 - 129
3	1	9	1	C	126 - 129
1	1	10	1	B	130 - 134
2	1	10	1	A	130 - 134
3	1	10	1	C	130 - 134
1	1	11	1	B	135 - 137
2	1	11	1	A	135 - 137
3	1	11	1	C	135 - 137
1	1	12	1	B	138 - 142
2	1	12	1	A	138 - 142
3	1	12	1	C	138 - 142
1	1	13	1	B	143 - 156
2	1	13	1	A	143 - 156
3	1	13	1	C	143 - 156
1	1	14	1	B	157 - 163
2	1	14	1	A	157 - 163
3	1	14	1	C	157 - 163
1	1	15	1	B	164 - 167
2	1	15	1	A	164 - 167
3	1	15	1	C	164 - 167
1	1	16	1	B	168 - 173
2	1	16	1	A	168 - 173
3	1	16	1	C	168 - 173
1	1	17	1	B	174 - 180
2	1	17	1	A	174 - 180
3	1	17	1	C	174 - 180
1	1	18	1	B	181 - 225
2	1	18	1	A	181 - 225
3	1	18	1	C	181 - 225
1	1	19	1	B	226 - 231
2	1	19	1	A	226 - 231
3	1	19	1	C	226 - 231
1	1	20	1	B	232 - 255
2	1	20	1	A	232 - 255
3	1	20	1	C	232 - 255
1	1	21	1	B	256 - 311
2	1	21	1	A	256 - 311
3	1	21	1	C	256 - 311
1	1	22	1	B	312 - 317
2	1	22	1	A	312 - 317
3	1	22	1	C	312 - 317
1	1	23	1	B	318 - 327
2	1	23	1	A	318 - 327
3	1	23	1	C	318 - 327
1	1	24	1	B	328 - 333
2	1	24	1	A	328 - 333
3	1	24	1	C	328 - 333
1	1	25	1	B	344 - 350
2	1	25	1	A	344 - 350
3	1	25	1	C	344 - 350
1	1	26	1	B	355 - 394
2	1	26	1	A	355 - 394
3	1	26	1	C	355 - 394
1	1	27	1	B	395 - 398
2	1	27	1	A	395 - 398
3	1	27	1	C	395 - 398
1	1	28	1	B	399 - 413
2	1	28	1	A	399 - 413
3	1	28	1	C	399 - 413
1	1	29	1	B	418 - 421
2	1	29	1	A	418 - 421
3	1	29	1	C	418 - 421
1	1	30	1	B	435 - 451
2	1	30	1	A	435 - 451
3	1	30	1	C	435 - 451
1	1	31	1	B	452 - 483
2	1	31	1	A	452 - 483
3	1	31	1	C	452 - 483
1	1	32	1	B	515 - 530
2	1	32	1	A	515 - 530
3	1	32	1	C	515 - 530
1	1	33	1	B	531 - 549
2	1	33	1	A	531 - 549
3	1	33	1	C	531 - 549
1	1	34	1	B	561 - 571
2	1	34	1	A	561 - 571
3	1	34	1	C	561 - 571
1	1	35	1	B	572 - 579
2	1	35	1	A	572 - 579
3	1	35	1	C	572 - 579
1	1	36	1	B	580 - 590
2	1	36	1	A	580 - 590
3	1	36	1	C	580 - 590
1	1	37	1	B	610 - 618
2	1	37	1	A	610 - 618
3	1	37	1	C	610 - 618
1	1	38	1	B	619 - 631
2	1	38	1	A	619 - 631
3	1	38	1	C	619 - 631
1	1	39	1	B	632 - 647
2	1	39	1	A	632 - 647
3	1	39	1	C	632 - 647
1	1	40	1	B	648 - 653
2	1	40	1	A	648 - 653
3	1	40	1	C	648 - 653
1	1	41	1	B	654 - 667
2	1	41	1	A	654 - 667
3	1	41	1	C	654 - 667
1	1	42	1	B	668 - 672
2	1	42	1	A	668 - 672
3	1	42	1	C	668 - 672
1	1	43	1	B	673 - 684
2	1	43	1	A	673 - 684
3	1	43	1	C	673 - 684
1	1	44	1	B	696 - 710
2	1	44	1	A	696 - 710
3	1	44	1	C	696 - 710
1	1	45	1	B	726 - 735
2	1	45	1	A	726 - 735
3	1	45	1	C	726 - 735
1	1	46	4	B	591 - 609
2	1	46	4	A	591 - 609
3	1	46	4	C	591 - 609
1	1	47	4	B	800 - 808
2	1	47	4	A	800 - 808
3	1	47	4	C	800 - 808
1	1	48	4	B	915 - 933
2	1	48	4	A	915 - 933
3	1	48	4	C	915 - 933
1	1	49	6	B	761 - 788
2	1	49	6	C	761 - 788
1	1	50	6	B	809 - 815
2	1	50	6	C	809 - 815
1	1	51	6	B	634 - 855
2	1	51	6	C	634 - 855

NCS ensembles :

#1: Protein

Endoplasmic reticulum aminopeptidase 1 / ARTS-1 / Adipocyte-derived leucine aminopeptidase / A-LAP / Aminopeptidase PILS / Puromycin- ...

Mass: 109071.492 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Homo sapiens (human) / Gene: ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154 / Production host:

Trichoplusia ni (cabbage looper)
References: UniProt: Q9NZ08, Hydrolases; Acting on peptide bonds (peptidases); Aminopeptidases

#2: Polysaccharide

alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...

Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source

Descriptor	Type	Program
DManpa1-6DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-	Glycam Condensed Sequence	GMML 1.0
WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2-2/a4-b1_b4-c1_c6-d1	WURCS	PDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{[(6+1)][b-D-Manp]{}}}}}	LINUCS	PDB-CARE

#3: Chemical

ChemComp-ZN / ZINC ION

Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn

#4: Sugar

ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE

Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C₈H₁₅NO₆

Identifier	Type	Program
DGlcpNAcb	CONDENSED IUPAC CARBOHYDRATE SYMBOL	GMML 1.0
N-acetyl-b-D-glucopyranosamine	COMMON NAME	GMML 1.0
b-D-GlcpNAc	IUPAC CARBOHYDRATE SYMBOL	PDB-CARE 1.0
GlcNAc	SNFG CARBOHYDRATE SYMBOL	GMML 1.0

#5: Water

ChemComp-HOH / water

Mass: 18.015 Da / Num. of mol.: 39 / Source method: isolated from a natural source / Formula: H₂O

Has protein modification

Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.31 Å³/Da / Density % sol: 46.66 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion / pH: 7.5 Details: 0.1M HEPES pH 7.5; 25% PEG 3350, VAPOR DIFFUSION, temperature 293K

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.9778 Å
Detector	Type: PSI PILATUS 6M / Detector: PIXEL / Date: Mar 6, 2010
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9778 Å / Relative weight: 1
Reflection	Resolution: 3→30 Å / Num. all: 60032 / Num. obs: 60032 / % possible obs: 97.8 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3 % / R_merge(I) obs: 0.153 / Net I/σ(I): 5.8
Reflection shell	Resolution: 3→3.16 Å / Redundancy: 3 % / R_merge(I) obs: 0.668 / Mean I/σ(I) obs: 1.6 / Num. unique all: 8778 / % possible all: 98.8

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Processing

Software

Name	Version	Classification
GDA		data collection
PHASER		phasing
REFMAC	5.5.0110	refinement
XDS		data reduction
SCALA		data scaling

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 2XDT

2xdt
PDB Unreleased entry

Resolution: 3→19.99 Å / Cor.coef. F_o:F_c: 0.899 / Cor.coef. F_o:F_c free: 0.846 / SU B: 20.826 / SU ML: 0.388 / Cross valid method: THROUGHOUT / ESU R Free: 0.486 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.28264	3019	5.1 %	RANDOM
R_work	0.22857	-	-	-
all	0.23133	60032	-	-
obs	0.23133	56650	97.57 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 34.252 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	3.32 Å²	0 Å²	0 Å²
2-	-	-1.74 Å²	0 Å²
3-	-	-	-1.58 Å²

Refinement step

Cycle: LAST / Resolution: 3→19.99 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	17494	0	109	39	17642

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.008	0.022	18108
X-RAY DIFFRACTION	r_bond_other_d	0.002	0.02	11482
X-RAY DIFFRACTION	r_angle_refined_deg	1.087	1.949	24725
X-RAY DIFFRACTION	r_angle_other_deg	0.834	3	28019
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.941	5	2285
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	37.351	23.881	724
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.324	15	2669
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	17.299	15	62
X-RAY DIFFRACTION	r_chiral_restr	0.073	0.2	2876
X-RAY DIFFRACTION	r_gen_planes_refined	0.004	0.021	20193
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	3749
X-RAY DIFFRACTION	r_nbd_refined
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it	2.109	3	11475
X-RAY DIFFRACTION	r_mcbond_other	0.314	3	4611
X-RAY DIFFRACTION	r_mcangle_it	3.888	5	18305
X-RAY DIFFRACTION	r_scbond_it	5.549	7	6633
X-RAY DIFFRACTION	r_scangle_it	7.851	9	6415
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	B	335	TIGHT POSITIONAL	0.02	0.05
1	2	A	335	TIGHT POSITIONAL	0.02	0.05
1	3	C	335	TIGHT POSITIONAL	0.02	0.05
1	1	B	335	TIGHT THERMAL	0.05	0.5
1	2	A	335	TIGHT THERMAL	0.06	0.5
1	3	C	335	TIGHT THERMAL	0.06	0.5
2	1	B	50	TIGHT POSITIONAL	0.02	0.05
2	2	A	50	TIGHT POSITIONAL	0.02	0.05
2	3	C	50	TIGHT POSITIONAL	0.02	0.05
2	1	B	50	TIGHT THERMAL	0.03	0.5
2	2	A	50	TIGHT THERMAL	0.04	0.5
2	3	C	50	TIGHT THERMAL	0.05	0.5
3	1	B	132	TIGHT POSITIONAL	0.02	0.05
3	2	A	132	TIGHT POSITIONAL	0.02	0.05
3	3	C	132	TIGHT POSITIONAL	0.02	0.05
3	1	B	132	TIGHT THERMAL	0.05	0.5
3	2	A	132	TIGHT THERMAL	0.05	0.5
3	3	C	132	TIGHT THERMAL	0.07	0.5
4	1	B	59	TIGHT POSITIONAL	0.02	0.05
4	2	A	59	TIGHT POSITIONAL	0.02	0.05
4	3	C	59	TIGHT POSITIONAL	0.02	0.05
4	1	B	59	TIGHT THERMAL	0.04	0.5
4	2	A	59	TIGHT THERMAL	0.04	0.5
4	3	C	59	TIGHT THERMAL	0.05	0.5
5	1	B	81	TIGHT POSITIONAL	0.02	0.05
5	2	A	81	TIGHT POSITIONAL	0.02	0.05
5	3	C	81	TIGHT POSITIONAL	0.02	0.05
5	1	B	81	TIGHT THERMAL	0.05	0.5
5	2	A	81	TIGHT THERMAL	0.05	0.5
5	3	C	81	TIGHT THERMAL	0.06	0.5
6	1	B	60	TIGHT POSITIONAL	0.02	0.05
6	2	A	60	TIGHT POSITIONAL	0.02	0.05
6	3	C	60	TIGHT POSITIONAL	0.02	0.05
6	1	B	60	TIGHT THERMAL	0.03	0.5
6	2	A	60	TIGHT THERMAL	0.05	0.5
6	3	C	60	TIGHT THERMAL	0.05	0.5
7	1	B	54	TIGHT POSITIONAL	0.02	0.05
7	2	A	54	TIGHT POSITIONAL	0.01	0.05
7	3	C	54	TIGHT POSITIONAL	0.02	0.05
7	1	B	54	TIGHT THERMAL	0.04	0.5
7	2	A	54	TIGHT THERMAL	0.05	0.5
7	3	C	54	TIGHT THERMAL	0.05	0.5
8	1	B	106	TIGHT POSITIONAL	0.02	0.05
8	2	A	106	TIGHT POSITIONAL	0.02	0.05
8	3	C	106	TIGHT POSITIONAL	0.02	0.05
8	1	B	106	TIGHT THERMAL	0.04	0.5
8	2	A	106	TIGHT THERMAL	0.06	0.5
8	3	C	106	TIGHT THERMAL	0.05	0.5
9	1	B	51	TIGHT POSITIONAL	0.02	0.05
9	2	A	51	TIGHT POSITIONAL	0.02	0.05
9	3	C	51	TIGHT POSITIONAL	0.02	0.05
9	1	B	51	TIGHT THERMAL	0.04	0.5
9	2	A	51	TIGHT THERMAL	0.04	0.5
9	3	C	51	TIGHT THERMAL	0.05	0.5
10	1	B	61	TIGHT POSITIONAL	0.02	0.05
10	2	A	61	TIGHT POSITIONAL	0.02	0.05
10	3	C	61	TIGHT POSITIONAL	0.02	0.05
10	1	B	61	TIGHT THERMAL	0.04	0.5
10	2	A	61	TIGHT THERMAL	0.06	0.5
10	3	C	61	TIGHT THERMAL	0.05	0.5
11	1	B	28	TIGHT POSITIONAL	0.01	0.05
11	2	A	28	TIGHT POSITIONAL	0.02	0.05
11	3	C	28	TIGHT POSITIONAL	0.02	0.05
11	1	B	28	TIGHT THERMAL	0.03	0.5
11	2	A	28	TIGHT THERMAL	0.04	0.5
11	3	C	28	TIGHT THERMAL	0.05	0.5
12	1	B	57	TIGHT POSITIONAL	0.01	0.05
12	2	A	57	TIGHT POSITIONAL	0.02	0.05
12	3	C	57	TIGHT POSITIONAL	0.02	0.05
12	1	B	57	TIGHT THERMAL	0.05	0.5
12	2	A	57	TIGHT THERMAL	0.04	0.5
12	3	C	57	TIGHT THERMAL	0.05	0.5
13	1	B	166	TIGHT POSITIONAL	0.02	0.05
13	2	A	166	TIGHT POSITIONAL	0.02	0.05
13	3	C	166	TIGHT POSITIONAL	0.02	0.05
13	1	B	166	TIGHT THERMAL	0.05	0.5
13	2	A	166	TIGHT THERMAL	0.05	0.5
13	3	C	166	TIGHT THERMAL	0.06	0.5
14	1	B	100	TIGHT POSITIONAL	0.01	0.05
14	2	A	100	TIGHT POSITIONAL	0.01	0.05
14	3	C	100	TIGHT POSITIONAL	0.02	0.05
14	1	B	100	TIGHT THERMAL	0.04	0.5
14	2	A	100	TIGHT THERMAL	0.05	0.5
14	3	C	100	TIGHT THERMAL	0.04	0.5
15	1	B	44	TIGHT POSITIONAL	0.02	0.05
15	2	A	44	TIGHT POSITIONAL	0.02	0.05
15	3	C	44	TIGHT POSITIONAL	0.02	0.05
15	1	B	44	TIGHT THERMAL	0.03	0.5
15	2	A	44	TIGHT THERMAL	0.04	0.5
15	3	C	44	TIGHT THERMAL	0.03	0.5
16	1	B	45	TIGHT POSITIONAL	0.02	0.05
16	2	A	45	TIGHT POSITIONAL	0.02	0.05
16	3	C	45	TIGHT POSITIONAL	0.02	0.05
16	1	B	45	TIGHT THERMAL	0.03	0.5
16	2	A	45	TIGHT THERMAL	0.03	0.5
16	3	C	45	TIGHT THERMAL	0.03	0.5
17	1	B	84	TIGHT POSITIONAL	0.02	0.05
17	2	A	84	TIGHT POSITIONAL	0.02	0.05
17	3	C	84	TIGHT POSITIONAL	0.02	0.05
17	1	B	84	TIGHT THERMAL	0.04	0.5
17	2	A	84	TIGHT THERMAL	0.04	0.5
17	3	C	84	TIGHT THERMAL	0.04	0.5
18	1	B	623	TIGHT POSITIONAL	0.02	0.05
18	2	A	623	TIGHT POSITIONAL	0.02	0.05
18	3	C	623	TIGHT POSITIONAL	0.02	0.05
18	1	B	623	TIGHT THERMAL	0.05	0.5
18	2	A	623	TIGHT THERMAL	0.06	0.5
18	3	C	623	TIGHT THERMAL	0.07	0.5
19	1	B	51	TIGHT POSITIONAL	0.02	0.05
19	2	A	51	TIGHT POSITIONAL	0.02	0.05
19	3	C	51	TIGHT POSITIONAL	0.02	0.05
19	1	B	51	TIGHT THERMAL	0.04	0.5
19	2	A	51	TIGHT THERMAL	0.07	0.5
19	3	C	51	TIGHT THERMAL	0.06	0.5
20	1	B	313	TIGHT POSITIONAL	0.02	0.05
20	2	A	313	TIGHT POSITIONAL	0.02	0.05
20	3	C	313	TIGHT POSITIONAL	0.02	0.05
20	1	B	313	TIGHT THERMAL	0.05	0.5
20	2	A	313	TIGHT THERMAL	0.06	0.5
20	3	C	313	TIGHT THERMAL	0.06	0.5
21	1	B	699	TIGHT POSITIONAL	0.02	0.05
21	2	A	699	TIGHT POSITIONAL	0.02	0.05
21	3	C	699	TIGHT POSITIONAL	0.02	0.05
21	1	B	699	TIGHT THERMAL	0.05	0.5
21	2	A	699	TIGHT THERMAL	0.05	0.5
21	3	C	699	TIGHT THERMAL	0.05	0.5
22	1	B	70	TIGHT POSITIONAL	0.02	0.05
22	2	A	70	TIGHT POSITIONAL	0.02	0.05
22	3	C	70	TIGHT POSITIONAL	0.01	0.05
22	1	B	70	TIGHT THERMAL	0.03	0.5
22	2	A	70	TIGHT THERMAL	0.03	0.5
22	3	C	70	TIGHT THERMAL	0.03	0.5
23	1	B	132	TIGHT POSITIONAL	0.02	0.05
23	2	A	132	TIGHT POSITIONAL	0.02	0.05
23	3	C	132	TIGHT POSITIONAL	0.02	0.05
23	1	B	132	TIGHT THERMAL	0.04	0.5
23	2	A	132	TIGHT THERMAL	0.05	0.5
23	3	C	132	TIGHT THERMAL	0.05	0.5
24	1	B	71	TIGHT POSITIONAL	0.02	0.05
24	2	A	71	TIGHT POSITIONAL	0.02	0.05
24	3	C	71	TIGHT POSITIONAL	0.02	0.05
24	1	B	71	TIGHT THERMAL	0.05	0.5
24	2	A	71	TIGHT THERMAL	0.05	0.5
24	3	C	71	TIGHT THERMAL	0.05	0.5
25	1	B	86	TIGHT POSITIONAL	0.02	0.05
25	2	A	86	TIGHT POSITIONAL	0.02	0.05
25	3	C	86	TIGHT POSITIONAL	0.02	0.05
25	1	B	86	TIGHT THERMAL	0.06	0.5
25	2	A	86	TIGHT THERMAL	0.06	0.5
25	3	C	86	TIGHT THERMAL	0.05	0.5
26	1	B	558	TIGHT POSITIONAL	0.04	0.05
26	2	A	558	TIGHT POSITIONAL	0.06	0.05
26	3	C	558	TIGHT POSITIONAL	0.04	0.05
26	1	B	558	TIGHT THERMAL	0.06	0.5
26	2	A	558	TIGHT THERMAL	0.06	0.5
26	3	C	558	TIGHT THERMAL	0.06	0.5
27	1	B	33	TIGHT POSITIONAL	0.02	0.05
27	2	A	33	TIGHT POSITIONAL	0.03	0.05
27	3	C	33	TIGHT POSITIONAL	0.03	0.05
27	1	B	33	TIGHT THERMAL	0.05	0.5
27	2	A	33	TIGHT THERMAL	0.06	0.5
27	3	C	33	TIGHT THERMAL	0.06	0.5
28	1	B	189	TIGHT POSITIONAL	0.02	0.05
28	2	A	189	TIGHT POSITIONAL	0.02	0.05
28	3	C	189	TIGHT POSITIONAL	0.02	0.05
28	1	B	189	TIGHT THERMAL	0.05	0.5
28	2	A	189	TIGHT THERMAL	0.05	0.5
28	3	C	189	TIGHT THERMAL	0.05	0.5
29	1	B	44	TIGHT POSITIONAL	0.02	0.05
29	2	A	44	TIGHT POSITIONAL	0.02	0.05
29	3	C	44	TIGHT POSITIONAL	0.02	0.05
29	1	B	44	TIGHT THERMAL	0.05	0.5
29	2	A	44	TIGHT THERMAL	0.04	0.5
29	3	C	44	TIGHT THERMAL	0.06	0.5
30	1	B	231	TIGHT POSITIONAL	0.02	0.05
30	2	A	231	TIGHT POSITIONAL	0.02	0.05
30	3	C	231	TIGHT POSITIONAL	0.02	0.05
30	1	B	231	TIGHT THERMAL	0.05	0.5
30	2	A	231	TIGHT THERMAL	0.05	0.5
30	3	C	231	TIGHT THERMAL	0.05	0.5
31	1	B	381	TIGHT POSITIONAL	0.02	0.05
31	2	A	381	TIGHT POSITIONAL	0.02	0.05
31	3	C	381	TIGHT POSITIONAL	0.02	0.05
31	1	B	381	TIGHT THERMAL	0.06	0.5
31	2	A	381	TIGHT THERMAL	0.05	0.5
31	3	C	381	TIGHT THERMAL	0.06	0.5
32	1	B	207	TIGHT POSITIONAL	0.02	0.05
32	2	A	207	TIGHT POSITIONAL	0.02	0.05
32	3	C	207	TIGHT POSITIONAL	0.02	0.05
32	1	B	207	TIGHT THERMAL	0.05	0.5
32	2	A	207	TIGHT THERMAL	0.06	0.5
32	3	C	207	TIGHT THERMAL	0.07	0.5
33	1	B	261	TIGHT POSITIONAL	0.02	0.05
33	2	A	261	TIGHT POSITIONAL	0.02	0.05
33	3	C	261	TIGHT POSITIONAL	0.02	0.05
33	1	B	261	TIGHT THERMAL	0.05	0.5
33	2	A	261	TIGHT THERMAL	0.05	0.5
33	3	C	261	TIGHT THERMAL	0.05	0.5
34	1	B	163	TIGHT POSITIONAL	0.02	0.05
34	2	A	163	TIGHT POSITIONAL	0.02	0.05
34	3	C	163	TIGHT POSITIONAL	0.02	0.05
34	1	B	163	TIGHT THERMAL	0.05	0.5
34	2	A	163	TIGHT THERMAL	0.05	0.5
34	3	C	163	TIGHT THERMAL	0.05	0.5
35	1	B	107	TIGHT POSITIONAL	0.02	0.05
35	2	A	107	TIGHT POSITIONAL	0.02	0.05
35	3	C	107	TIGHT POSITIONAL	0.02	0.05
35	1	B	107	TIGHT THERMAL	0.04	0.5
35	2	A	107	TIGHT THERMAL	0.05	0.5
35	3	C	107	TIGHT THERMAL	0.04	0.5
36	1	B	137	TIGHT POSITIONAL	0.02	0.05
36	2	A	137	TIGHT POSITIONAL	0.02	0.05
36	3	C	137	TIGHT POSITIONAL	0.02	0.05
36	1	B	137	TIGHT THERMAL	0.05	0.5
36	2	A	137	TIGHT THERMAL	0.05	0.5
36	3	C	137	TIGHT THERMAL	0.05	0.5
37	1	B	123	TIGHT POSITIONAL	0.02	0.05
37	2	A	123	TIGHT POSITIONAL	0.02	0.05
37	3	C	123	TIGHT POSITIONAL	0.02	0.05
37	1	B	123	TIGHT THERMAL	0.05	0.5
37	2	A	123	TIGHT THERMAL	0.04	0.5
37	3	C	123	TIGHT THERMAL	0.05	0.5
38	1	B	133	TIGHT POSITIONAL	0.02	0.05
38	2	A	133	TIGHT POSITIONAL	0.02	0.05
38	3	C	133	TIGHT POSITIONAL	0.02	0.05
38	1	B	133	TIGHT THERMAL	0.05	0.5
38	2	A	133	TIGHT THERMAL	0.04	0.5
38	3	C	133	TIGHT THERMAL	0.04	0.5
39	1	B	200	TIGHT POSITIONAL	0.02	0.05
39	2	A	200	TIGHT POSITIONAL	0.02	0.05
39	3	C	200	TIGHT POSITIONAL	0.02	0.05
39	1	B	200	TIGHT THERMAL	0.05	0.5
39	2	A	200	TIGHT THERMAL	0.05	0.5
39	3	C	200	TIGHT THERMAL	0.05	0.5
40	1	B	63	TIGHT POSITIONAL	0.03	0.05
40	2	A	63	TIGHT POSITIONAL	0.02	0.05
40	3	C	63	TIGHT POSITIONAL	0.03	0.05
40	1	B	63	TIGHT THERMAL	0.05	0.5
40	2	A	63	TIGHT THERMAL	0.05	0.5
40	3	C	63	TIGHT THERMAL	0.04	0.5
41	1	B	165	TIGHT POSITIONAL	0.03	0.05
41	2	A	165	TIGHT POSITIONAL	0.02	0.05
41	3	C	165	TIGHT POSITIONAL	0.02	0.05
41	1	B	165	TIGHT THERMAL	0.06	0.5
41	2	A	165	TIGHT THERMAL	0.06	0.5
41	3	C	165	TIGHT THERMAL	0.05	0.5
42	1	B	53	TIGHT POSITIONAL	0.02	0.05
42	2	A	53	TIGHT POSITIONAL	0.02	0.05
42	3	C	53	TIGHT POSITIONAL	0.02	0.05
42	1	B	53	TIGHT THERMAL	0.05	0.5
42	2	A	53	TIGHT THERMAL	0.05	0.5
42	3	C	53	TIGHT THERMAL	0.04	0.5
43	1	B	166	TIGHT POSITIONAL	0.02	0.05
43	2	A	166	TIGHT POSITIONAL	0.02	0.05
43	3	C	166	TIGHT POSITIONAL	0.03	0.05
43	1	B	166	TIGHT THERMAL	0.06	0.5
43	2	A	166	TIGHT THERMAL	0.06	0.5
43	3	C	166	TIGHT THERMAL	0.04	0.5
44	1	B	163	TIGHT POSITIONAL	0.06	0.05
44	2	A	163	TIGHT POSITIONAL	0.11	0.05
44	3	C	163	TIGHT POSITIONAL	0.06	0.05
44	1	B	163	TIGHT THERMAL	0.06	0.5
44	2	A	163	TIGHT THERMAL	0.06	0.5
44	3	C	163	TIGHT THERMAL	0.04	0.5
45	1	B	121	TIGHT POSITIONAL	0.02	0.05
45	2	A	121	TIGHT POSITIONAL	0.02	0.05
45	3	C	121	TIGHT POSITIONAL	0.02	0.05
45	1	B	121	TIGHT THERMAL	0.05	0.5
45	2	A	121	TIGHT THERMAL	0.06	0.5
45	3	C	121	TIGHT THERMAL	0.04	0.5
46	1	B	249	MEDIUM POSITIONAL	0.25	0.5
46	2	A	249	MEDIUM POSITIONAL	0.2	0.5
46	3	C	249	MEDIUM POSITIONAL	0.19	0.5
46	1	B	249	MEDIUM THERMAL	0.64	2
46	2	A	249	MEDIUM THERMAL	0.68	2
46	3	C	249	MEDIUM THERMAL	0.67	2
47	1	B	69	MEDIUM POSITIONAL	0.26	0.5
47	2	A	69	MEDIUM POSITIONAL	0.39	0.5
47	3	C	69	MEDIUM POSITIONAL	0.25	0.5
47	1	B	69	MEDIUM THERMAL	0.68	2
47	2	A	69	MEDIUM THERMAL	0.72	2
47	3	C	69	MEDIUM THERMAL	0.46	2
48	1	B	195	MEDIUM POSITIONAL	0.25	0.5
48	2	A	195	MEDIUM POSITIONAL	0.28	0.5
48	3	C	195	MEDIUM POSITIONAL	0.26	0.5
48	1	B	195	MEDIUM THERMAL	0.79	2
48	2	A	195	MEDIUM THERMAL	0.66	2
48	3	C	195	MEDIUM THERMAL	0.44	2
49	1	B	322	LOOSE POSITIONAL	0.32	5
49	1	B	322	LOOSE THERMAL	2.68	10
50	1	B	76	LOOSE POSITIONAL	0.26	5
50	1	B	76	LOOSE THERMAL	3.58	10
51	1	B	2450	LOOSE POSITIONAL	0.58	5
51	1	B	2450	LOOSE THERMAL	2.78	10

LS refinement shell

Resolution: 3→3.076 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.387	234	-
R_work	0.32	4094	-
obs	-	-	98.59 %

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