PDB-2rif: CBS domain protein PAE2072 from Pyrobaculum aerophilum complexed ...

ID or keywords:

Entry

Database: PDB / ID: 2rif

Title

CBS domain protein PAE2072 from Pyrobaculum aerophilum complexed with AMP

Components

Conserved protein with 2 CBS domains

Conservation

Keywords

LIGAND-BINDING PROTEIN /

CBS domain /

Bateman domain / AMP binding protein /

TRANSFERASE

Function / homology

Function and homology information

nucleotide binding
Similarity search - Function

Biological species

Pyrobaculum aerophilum (archaea)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 2.35 Å

Authors

Lee, T.M. / King, N.P. / Sawaya, M.R. / Cascio, D. / Yeates, T.O.

Citation

Journal: J.Mol.Biol. / Year: 2008
Title: Structures and Functional Implications of an AMP-Binding Cystathionine beta-Synthase Domain Protein from a Hyperthermophilic Archaeon.
Authors: King, N.P. / Lee, T.M. / Sawaya, M.R. / Cascio, D. / Yeates, T.O.

History

Deposition	Oct 10, 2007	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jun 17, 2008	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.2	Oct 25, 2017	Group: Refinement description / Category: software

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	2rif.cif.gz	115.5 KB	Display	PDBx/mmCIF format
PDB format	pdb2rif.ent.gz	95.1 KB	Display	PDB format
PDBx/mmJSON format	2rif.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ri/2rif ftp://data.pdbj.org/pub/pdb/validation_reports/ri/2rif	HTTPS FTP

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Related structure data

Related structure data	2rihC C: citing same article (ref.)
Similar structure data	2rih-d 6zn8-2 4iqa-1 3fhm-1 3kpc-1 2d2z-1 3uvh-1 1k0o-1 6gzy-2 4o9k-d 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

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#140 - Aug 2011 Rhomboid Protease GlpG similarity (4) #129 - Sep 2010 Isocitrate Dehydrogenase similarity (1) #154 - Oct 2012 Citric Acid Cycle similarity (1) #24 - Dec 2001 Glycogen Phosphorylase similarity (1) #55 - Jul 2004 DNA Ligase similarity (1) #16 - Apr 2001 Aminoacyl-tRNA Synthetases similarity (1)

Deposited unit

A: Conserved protein with 2 CBS domains

B: Conserved protein with 2 CBS domains

C: Conserved protein with 2 CBS domains

D: Conserved protein with 2 CBS domains

hetero molecules

65.5 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Conserved protein with 2 CBS domains

B: Conserved protein with 2 CBS domains

hetero molecules

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

2

C: Conserved protein with 2 CBS domains

D: Conserved protein with 2 CBS domains

hetero molecules

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

3

Idetical with deposited unit
defined by software

Unit cell

Length a, b, c (Å)	55.726, 55.726, 336.351
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	92
Space group name H-M	P4₁2₁2

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Beg label comp-ID	End label comp-ID	Refine code	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	PRO	SER	1	A	A	11 - 14	14 - 17
2	1	1	PRO	SER	1	B	B	11 - 14	14 - 17
3	1	1	PRO	SER	1	C	C	11 - 14	14 - 17
4	1	1	PRO	SER	1	D	D	11 - 14	14 - 17
5	2	1	PRO	GLU	1	A	A	16 - 17	19 - 20
6	2	1	PRO	GLU	1	B	B	16 - 17	19 - 20
7	2	1	PRO	GLU	1	C	C	16 - 17	19 - 20
8	2	1	PRO	GLU	1	D	D	16 - 17	19 - 20
9	3	1	ALA	ALA	1	A	A	19 - 29	22 - 32
10	3	1	ALA	ALA	1	B	B	19 - 29	22 - 32
11	3	1	ALA	ALA	1	C	C	19 - 29	22 - 32
12	3	1	ALA	ALA	1	D	D	19 - 29	22 - 32
13	4	1	ASN	ASN	1	A	A	31	34
14	4	1	ASN	ASN	1	B	B	31	34
15	4	1	ASN	ASN	1	C	C	31	34
16	4	1	ASN	ASN	1	D	D	31	34
17	5	1	ASP	PRO	1	A	A	42 - 44	45 - 47
18	5	1	ASP	PRO	1	B	B	42 - 44	45 - 47
19	5	1	ASP	PRO	1	C	C	42 - 44	45 - 47
20	5	1	ASP	PRO	1	D	D	42 - 44	45 - 47
21	6	1	PRO	LEU	1	A	A	47 - 57	50 - 60
22	6	1	PRO	LEU	1	B	B	47 - 57	50 - 60
23	6	1	PRO	LEU	1	C	C	47 - 57	50 - 60
24	6	1	PRO	LEU	1	D	D	47 - 57	50 - 60
25	7	1	ALA	ALA	1	A	A	59 - 61	62 - 64
26	7	1	ALA	ALA	1	B	B	59 - 61	62 - 64
27	7	1	ALA	ALA	1	C	C	59 - 61	62 - 64
28	7	1	ALA	ALA	1	D	D	59 - 61	62 - 64
29	8	1	LEU	LEU	1	A	A	64	67
30	8	1	LEU	LEU	1	B	B	64	67
31	8	1	LEU	LEU	1	C	C	64	67
32	8	1	LEU	LEU	1	D	D	64	67
33	9	1	PRO	PRO	1	A	A	77	80
34	9	1	PRO	PRO	1	B	B	77	80
35	9	1	PRO	PRO	1	C	C	77	80
36	9	1	PRO	PRO	1	D	D	77	80
37	10	1	THR	LEU	1	A	A	79 - 81	82 - 84
38	10	1	THR	LEU	1	B	B	79 - 81	82 - 84
39	10	1	THR	LEU	1	C	C	79 - 81	82 - 84
40	10	1	THR	LEU	1	D	D	79 - 81	82 - 84
41	11	1	THR	VAL	1	A	A	83 - 86	86 - 89
42	11	1	THR	VAL	1	B	B	83 - 86	86 - 89
43	11	1	THR	VAL	1	C	C	83 - 86	86 - 89
44	11	1	THR	VAL	1	D	D	83 - 86	86 - 89
45	12	1	MET	MET	1	A	A	93	96
46	12	1	MET	MET	1	B	B	93	96
47	12	1	MET	MET	1	C	C	93	96
48	12	1	MET	MET	1	D	D	93	96
49	13	1	ASN	ASN	1	A	A	97 - 105	100 - 108
50	13	1	ASN	ASN	1	B	B	97 - 105	100 - 108
51	13	1	ASN	ASN	1	C	C	97 - 105	100 - 108
52	13	1	ASN	ASN	1	D	D	97 - 105	100 - 108
53	14	1	ASN	ILE	1	A	A	107 - 116	110 - 119
54	14	1	ASN	ILE	1	B	B	107 - 116	110 - 119
55	14	1	ASN	ILE	1	C	C	107 - 116	110 - 119
56	14	1	ASN	ILE	1	D	D	107 - 116	110 - 119
57	15	1	ASP	PHE	1	A	A	118 - 121	121 - 124
58	15	1	ASP	PHE	1	B	B	118 - 121	121 - 124
59	15	1	ASP	PHE	1	C	C	118 - 121	121 - 124
60	15	1	ASP	PHE	1	D	D	118 - 121	121 - 124
61	16	1	ALA	LEU	1	A	A	124 - 126	127 - 129
62	16	1	ALA	LEU	1	B	B	124 - 126	127 - 129
63	16	1	ALA	LEU	1	C	C	124 - 126	127 - 129
64	16	1	ALA	LEU	1	D	D	124 - 126	127 - 129
65	17	1	LEU	ASN	4	A	A	66 - 75	69 - 78
66	17	1	LEU	ASN	4	B	B	66 - 75	69 - 78
67	17	1	LEU	ASN	4	C	C	66 - 75	69 - 78
68	17	1	LEU	ASN	4	D	D	66 - 75	69 - 78
69	18	1	VAL	ALA	4	A	A	33 - 40	36 - 43
70	18	1	VAL	ALA	4	B	B	33 - 40	36 - 43
71	18	1	VAL	ALA	4	C	C	33 - 40	36 - 43
72	18	1	VAL	ALA	4	D	D	33 - 40	36 - 43
73	19	1	VAL	ALA	4	A	A	88 - 90	91 - 93
74	19	1	VAL	ALA	4	B	B	88 - 90	91 - 93
75	19	1	VAL	ALA	4	C	C	88 - 90	91 - 93
76	19	1	VAL	ALA	4	D	D	88 - 90	91 - 93
1	1	2	LEU	LEU	3	A	A	15	18
2	1	2	LEU	LEU	3	B	B	15	18
3	1	2	LEU	LEU	3	C	C	15	18
4	1	2	LEU	LEU	3	D	D	15	18
5	2	2	THR	THR	3	A	A	18	21
6	2	2	THR	THR	3	B	B	18	21
7	2	2	THR	THR	3	C	C	18	21
8	2	2	THR	THR	3	D	D	18	21
9	3	2	LYS	LYS	3	A	A	30	33
10	3	2	LYS	LYS	3	B	B	30	33
11	3	2	LYS	LYS	3	C	C	30	33
12	3	2	LYS	LYS	3	D	D	30	33
13	4	2	ARG	ARG	3	A	A	41	44
14	4	2	ARG	ARG	3	B	B	41	44
15	4	2	ARG	ARG	3	C	C	41	44
16	4	2	ARG	ARG	3	D	D	41	44
17	5	2	LYS	ARG	3	A	A	45 - 46	48 - 49
18	5	2	LYS	ARG	3	B	B	45 - 46	48 - 49
19	5	2	LYS	ARG	3	C	C	45 - 46	48 - 49
20	5	2	LYS	ARG	3	D	D	45 - 46	48 - 49
21	6	2	ARG	ARG	3	A	A	58	61
22	6	2	ARG	ARG	3	B	B	58	61
23	6	2	ARG	ARG	3	C	C	58	61
24	6	2	ARG	ARG	3	D	D	58	61
25	7	2	GLN	ARG	3	A	A	62 - 63	65 - 66
26	7	2	GLN	ARG	3	B	B	62 - 63	65 - 66
27	7	2	GLN	ARG	3	C	C	62 - 63	65 - 66
28	7	2	GLN	ARG	3	D	D	62 - 63	65 - 66
29	8	2	SER	SER	3	A	A	76	79
30	8	2	SER	SER	3	B	B	76	79
31	8	2	SER	SER	3	C	C	76	79
32	8	2	SER	SER	3	D	D	76	79
33	9	2	ILE	ILE	3	A	A	78	81
34	9	2	ILE	ILE	3	B	B	78	81
35	9	2	ILE	ILE	3	C	C	78	81
36	9	2	ILE	ILE	3	D	D	78	81
37	10	2	ASP	ASP	3	A	A	82	85
38	10	2	ASP	ASP	3	B	B	82	85
39	10	2	ASP	ASP	3	C	C	82	85
40	10	2	ASP	ASP	3	D	D	82	85
41	11	2	GLU	LYS	3	A	A	91 - 92	94 - 95
42	11	2	GLU	LYS	3	B	B	91 - 92	94 - 95
43	11	2	GLU	LYS	3	C	C	91 - 92	94 - 95
44	11	2	GLU	LYS	3	D	D	91 - 92	94 - 95
45	12	2	ARG	HIS	6	A	A	94 - 96	97 - 99
46	12	2	ARG	HIS	6	B	B	94 - 96	97 - 99
47	12	2	ARG	HIS	6	C	C	94 - 96	97 - 99
48	12	2	ARG	HIS	6	D	D	94 - 96	97 - 99
49	13	2	LYS	LYS	3	A	A	106	109
50	13	2	LYS	LYS	3	B	B	106	109
51	13	2	LYS	LYS	3	C	C	106	109
52	13	2	LYS	LYS	3	D	D	106	109
53	14	2	ARG	ARG	3	A	A	117	120
54	14	2	ARG	ARG	3	B	B	117	120
55	14	2	ARG	ARG	3	C	C	117	120
56	14	2	ARG	ARG	3	D	D	117	120
57	15	2	GLU	ARG	3	A	A	122 - 123	125 - 126
58	15	2	GLU	ARG	3	B	B	122 - 123	125 - 126
59	15	2	GLU	ARG	3	C	C	122 - 123	125 - 126
60	15	2	GLU	ARG	3	D	D	122 - 123	125 - 126
61	16	2	LEU	GLU	3	A	A	127 - 128	130 - 131
62	16	2	LEU	GLU	3	B	B	127 - 128	130 - 131
63	16	2	LEU	GLU	3	C	C	127 - 128	130 - 131
64	16	2	LEU	GLU	3	D	D	127 - 128	130 - 131
65	17	2	ASP	ASP	4	A	A	65	68
66	17	2	ASP	ASP	4	B	B	65	68
67	17	2	ASP	ASP	4	C	C	65	68
68	17	2	ASP	ASP	4	D	D	65	68
69	18	2	ARG	ARG	4	A	A	32	35
70	18	2	ARG	ARG	4	B	B	32	35
71	18	2	ARG	ARG	4	C	C	32	35
72	18	2	ARG	ARG	4	D	D	32	35
73	19	2	HIS	HIS	4	A	A	87	90
74	19	2	HIS	HIS	4	B	B	87	90
75	19	2	HIS	HIS	4	C	C	87	90
76	19	2	HIS	HIS	4	D	D	87	90

NCS ensembles :

ID
1
2

#1: Protein	Conserved protein with 2 CBS domains / Conservation Mass: 15310.862 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrobaculum aerophilum (archaea) / Strain: IM2 / Gene: PAE2072 / Plasmid: pETM11 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q8ZVX8
#2: Chemical	ChemComp-CS / CESIUM ION Mass: 132.905 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: Cs
#3: Chemical	ChemComp-AMP / ADENOSINE MONOPHOSPHATE / Adenosine monophosphate Mass: 347.221 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₁₀H₁₄N₅O₇P / Comment: AMP*YM
#4: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 66 / 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: 2.13 Å³/Da / Density % sol: 42.3 %
Crystal grow	Temperature: 298 K / Method: hanging drop vapor diffusion / pH: 7.8 Details: PEG3350, Lithium Acetate, Cesium Chloride, pH 7.8, hanging drop vapor diffusion, temperature 298K

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

ALS

/ Beamline: 5.0.2 / Wavelength: 1 Å

Detector

Type: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 2, 2007

Radiation

Monochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 1 Å / Relative weight: 1

Reflection

Resolution: 2.35→20 Å / Num. obs: 21965 / % possible obs: 93.7 % / Observed criterion σ(F): -3 / Redundancy: 2.6 % / R_merge(I) obs: 0.064 / Net I/σ(I): 13.3

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Diffraction-ID	% possible all
2.35-2.43	2.7	0.373	1	99.6
2.43-2.53	2.6	0.507	1	98.5
2.53-2.65	2.7	0.222	1	98.6
2.65-2.79	2.6	0.171	1	97.6
2.79-2.96	2.6	0.117	1	96.8
2.96-3.19	2.6	0.085	1	94.5
3.19-3.51	2.5	0.089	1	92.1
3.51-4.01	2.5	0.058	1	90.3
4.01-5.04	2.4	0.047	1	86.4
5.04-20	2.4	0.037	1	84.7

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Phasing

Phasing

Method:

molecular replacement

Phasing MR

Model details: Phaser MODE: MR_AUTO

	Highest resolution	Lowest resolution
Rotation	4 Å	19.67 Å
Translation	4 Å	19.67 Å

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
PHASER		phasing
REFMAC		refinement
PDB_EXTRACT	3	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.35→18.91 Å / Cor.coef. F_o:F_c: 0.943 / Cor.coef. F_o:F_c free: 0.913 / SU B: 21.539 / SU ML: 0.287 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.62 / ESU R Free: 0.325 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.29422	1118	5.1 %	RANDOM
R_work	0.23935	-	-	-
obs	0.24218	20756	93.8 %	-

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: 48.738 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-0.01 Å²	0 Å²	0 Å²
2-	-	-0.01 Å²	0 Å²
3-	-	-	0.01 Å²

Refinement step

Cycle: LAST / Resolution: 2.35→18.91 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	3984	0	195	66	4245

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.005	0.022	4234
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	2879
X-RAY DIFFRACTION	r_angle_refined_deg	1.137	2.051	5796
X-RAY DIFFRACTION	r_angle_other_deg	0.826	3.001	7023
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	4.273	5	514
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	32.23	22.222	162
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	13.26	15	729
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	18.341	15	55
X-RAY DIFFRACTION	r_chiral_restr	0.047	0.2	728
X-RAY DIFFRACTION	r_gen_planes_refined	0.004	0.021	4477
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	790
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	0.145	0.2	152
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	0.591	0.2	17
X-RAY DIFFRACTION	r_symmetry_vdw_other	0.344	0.2	41
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.213	0.2	4
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	1.125	2	2606
X-RAY DIFFRACTION	r_mcbond_other	0.202	2	1012
X-RAY DIFFRACTION	r_mcangle_it	1.89	3	4264
X-RAY DIFFRACTION	r_scbond_it	1.111	2	1628
X-RAY DIFFRACTION	r_scangle_it	1.825	3	1532
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	A	856	TIGHT POSITIONAL	0.02	0.05
1	2	B	856	TIGHT POSITIONAL	0.02	0.05
1	3	C	856	TIGHT POSITIONAL	0.03	0.05
1	4	D	856	TIGHT POSITIONAL	0.03	0.05
1	1	A	214	MEDIUM POSITIONAL	0.23	0.5
1	2	B	214	MEDIUM POSITIONAL	0.16	0.5
1	3	C	214	MEDIUM POSITIONAL	0.15	0.5
1	4	D	214	MEDIUM POSITIONAL	0.18	0.5
1	1	A	856	TIGHT THERMAL	0.06	0.5
1	2	B	856	TIGHT THERMAL	0.06	0.5
1	3	C	856	TIGHT THERMAL	0.06	0.5
1	4	D	856	TIGHT THERMAL	0.06	0.5
1	1	A	214	MEDIUM THERMAL	0.66	2
1	2	B	214	MEDIUM THERMAL	0.67	2
1	3	C	214	MEDIUM THERMAL	0.69	2
1	4	D	214	MEDIUM THERMAL	0.66	2
2	1	A	120	TIGHT POSITIONAL	0.03	0.05
2	2	B	120	TIGHT POSITIONAL	0.04	0.05
2	3	C	120	TIGHT POSITIONAL	0.03	0.05
2	4	D	120	TIGHT POSITIONAL	0.03	0.05
2	1	A	52	MEDIUM POSITIONAL	0.41	0.5
2	2	B	52	MEDIUM POSITIONAL	0.58	0.5
2	3	C	52	MEDIUM POSITIONAL	0.59	0.5
2	4	D	52	MEDIUM POSITIONAL	0.38	0.5
2	1	A	270	LOOSE POSITIONAL	1.45	5
2	2	B	270	LOOSE POSITIONAL	1.27	5
2	3	C	270	LOOSE POSITIONAL	1.45	5
2	4	D	270	LOOSE POSITIONAL	1.62	5
2	1	A	120	TIGHT THERMAL	0.04	0.5
2	2	B	120	TIGHT THERMAL	0.06	0.5
2	3	C	120	TIGHT THERMAL	0.06	0.5
2	4	D	120	TIGHT THERMAL	0.06	0.5
2	1	A	52	MEDIUM THERMAL	0.45	2
2	2	B	52	MEDIUM THERMAL	0.72	2
2	3	C	52	MEDIUM THERMAL	0.62	2
2	4	D	52	MEDIUM THERMAL	0.76	2
2	1	A	270	LOOSE THERMAL	1.97	10
2	2	B	270	LOOSE THERMAL	2.76	10
2	3	C	270	LOOSE THERMAL	1.73	10
2	4	D	270	LOOSE THERMAL	1.8	10

LS refinement shell

Resolution: 2.35→2.41 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.421	76	-
R_work	0.296	1559	-
obs	-	-	99.51 %

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	3.7536	0.5804	0.9393	3.9478	0.2226	2.8051	-0.2238	0.0801	0.5434	-0.0655	0.0206	-0.4375	-0.1973	0.2312	0.2032	-0.2748	-0.024	0.0028	0.0262	0.05	-0.025	21.3322	-1.4027	10.8044
2	2.1101	0.6501	1.11	1.1989	0.2794	6.4928	0.0547	-0.2564	0.1896	-0.1521	-0.2161	0.1623	0.3131	-0.2253	0.1614	-0.3606	0.0293	0.0761	0.1529	-0.0259	-0.1796	30.9706	-17.3143	22.7532
3	2.8127	0.1385	0.1994	3.4164	-1.749	3.6514	0.0265	-0.3247	-0.2758	-0.0676	0.0273	0.1199	0.3112	-0.3251	-0.0539	-0.2828	-0.1006	-0.0231	-0.0388	-0.0002	-0.1075	3.2278	-21.9529	20.0518
4	3.1158	-0.486	-1.244	2.9052	0.2044	5.9093	0.131	-0.5695	0.4693	0.0395	0.3151	0.0564	-0.1588	-0.3156	-0.4461	-0.3877	0.0357	-0.0193	0.1466	-0.105	-0.0053	-2.0432	-1.043	25.6401

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	X-RAY DIFFRACTION	1	A	A	2 - 131	5 - 134
2	X-RAY DIFFRACTION	2	B	B	2 - 130	5 - 133
3	X-RAY DIFFRACTION	3	C	C	2 - 129	5 - 132
4	X-RAY DIFFRACTION	4	D	D	2 - 131	5 - 134

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