PDB-4b86: Crystal structure of the MSL1-MSL2 complex (3.5A)

ID or keywords:

Entry

Database: PDB / ID: 4b86

Title

Crystal structure of the MSL1-MSL2 complex (3.5A)

Components

MALE-SPECIFIC LETHAL 1 HOMOLOG
MALE-SPECIFIC LETHAL 2 HOMOLOG

Keywords

GENE REGULATION /

DOSAGE COMPENSATION /

CHROMATIN

Function / homology

Function and homology information

MSL complex /

Transferases; Acyltransferases; Aminoacyltransferases /

ubiquitin protein ligase activity / HATs acetylate histones / protein ubiquitination / nuclear speck /

chromatin remodeling /

chromatin binding / positive regulation of DNA-templated transcription /

nucleoplasm ...
Similarity search - Function

Biological species

HOMO SAPIENS (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MAD / Resolution: 3.5 Å

Authors

Hallacli, E. / Lipp, M. / Georgiev, P. / Spielman, C. / Cusack, S. / Akhtar, A. / Kadlec, J.

Citation

Journal: Mol.Cell / Year: 2012
Title: Msl1-Mediated Dimerization of the Dosage Compensation Complex is Essential for Male X-Chromosome Regulation in Drosophila.
Authors: Hallacli, E. / Lipp, M. / Georgiev, P. / Spielman, C. / Cusack, S. / Akhtar, A. / Kadlec, J.

History

Deposition	Aug 24, 2012	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Feb 6, 2013	Provider: repository / Type: Initial release
Revision 1.1	May 8, 2024	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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 / _struct_conn.pdbx_dist_value / _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_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/b8/4b86 ftp://data.pdbj.org/pub/pdb/validation_reports/b8/4b86	HTTPS FTP

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Related structure data

Related structure data	4b7yC C: citing same article (ref.)
Similar structure data	2x6o-1 2lkp-d 6hs2-d 6gfh-1 6wai-2 5a3l-1 2h7g-d 6gfh-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

4b7yC

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#7 - Jul 2000 Nucleosome similarity (1)

Deposited unit

A: MALE-SPECIFIC LETHAL 1 HOMOLOG

B: MALE-SPECIFIC LETHAL 1 HOMOLOG

C: MALE-SPECIFIC LETHAL 2 HOMOLOG

D: MALE-SPECIFIC LETHAL 2 HOMOLOG

E: MALE-SPECIFIC LETHAL 1 HOMOLOG

F: MALE-SPECIFIC LETHAL 1 HOMOLOG

G: MALE-SPECIFIC LETHAL 2 HOMOLOG

H: MALE-SPECIFIC LETHAL 2 HOMOLOG

I: MALE-SPECIFIC LETHAL 1 HOMOLOG

J: MALE-SPECIFIC LETHAL 1 HOMOLOG

K: MALE-SPECIFIC LETHAL 2 HOMOLOG

L: MALE-SPECIFIC LETHAL 2 HOMOLOG

hetero molecules

121 kDa, 12 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: MALE-SPECIFIC LETHAL 1 HOMOLOG

B: MALE-SPECIFIC LETHAL 1 HOMOLOG

C: MALE-SPECIFIC LETHAL 2 HOMOLOG

D: MALE-SPECIFIC LETHAL 2 HOMOLOG

hetero molecules

defined by author&software
40.2 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

E: MALE-SPECIFIC LETHAL 1 HOMOLOG

F: MALE-SPECIFIC LETHAL 1 HOMOLOG

G: MALE-SPECIFIC LETHAL 2 HOMOLOG

H: MALE-SPECIFIC LETHAL 2 HOMOLOG

hetero molecules

defined by author&software
40.2 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

I: MALE-SPECIFIC LETHAL 1 HOMOLOG

J: MALE-SPECIFIC LETHAL 1 HOMOLOG

K: MALE-SPECIFIC LETHAL 2 HOMOLOG

L: MALE-SPECIFIC LETHAL 2 HOMOLOG

hetero molecules

defined by author&software
40.2 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	104.650, 182.210, 89.470
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	18
Space group name H-M	P2₁2₁2

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: 0 / Refine code: 0

Dom-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	MET	MET	ALA	ALA	G	G	1 - 116	1 - 116
2	1	MET	MET	ALA	ALA	H	H	1 - 116	1 - 116
1	2	MET	MET	LEU	LEU	G	G	1 - 115	1 - 115
2	2	MET	MET	LEU	LEU	K	K	1 - 115	1 - 115
1	3	MET	MET	LEU	LEU	G	G	1 - 115	1 - 115
2	3	MET	MET	LEU	LEU	L	L	1 - 115	1 - 115
1	4	MET	MET	LEU	LEU	G	G	1 - 115	1 - 115
2	4	MET	MET	LEU	LEU	C	C	1 - 115	1 - 115
1	5	MET	MET	LEU	LEU	G	G	1 - 115	1 - 115
2	5	MET	MET	LEU	LEU	D	D	1 - 115	1 - 115
1	6	GLY	GLY	MET	MET	E	E	214 - 264	6 - 56
2	6	GLY	GLY	MET	MET	F	F	214 - 264	6 - 56
1	7	SER	SER	GLU	GLU	E	E	216 - 249	8 - 41
2	7	SER	SER	GLU	GLU	I	I	216 - 249	8 - 41
1	8	SER	SER	ILE	ILE	E	E	216 - 247	8 - 39
2	8	SER	SER	ILE	ILE	J	J	216 - 247	8 - 39
1	9	GLY	GLY	MET	MET	E	E	214 - 264	6 - 56
2	9	GLY	GLY	MET	MET	B	B	214 - 264	6 - 56
1	10	GLY	GLY	ALA	ALA	E	E	214 - 259	6 - 51
2	10	GLY	GLY	ALA	ALA	A	A	214 - 259	6 - 51
1	11	MET	MET	LEU	LEU	H	H	1 - 115	1 - 115
2	11	MET	MET	LEU	LEU	K	K	1 - 115	1 - 115
1	12	MET	MET	LEU	LEU	H	H	1 - 115	1 - 115
2	12	MET	MET	LEU	LEU	L	L	1 - 115	1 - 115
1	13	MET	MET	LEU	LEU	H	H	1 - 115	1 - 115
2	13	MET	MET	LEU	LEU	C	C	1 - 115	1 - 115
1	14	MET	MET	LEU	LEU	H	H	1 - 115	1 - 115
2	14	MET	MET	LEU	LEU	D	D	1 - 115	1 - 115
1	15	SER	SER	GLU	GLU	F	F	216 - 249	8 - 41
2	15	SER	SER	GLU	GLU	I	I	216 - 249	8 - 41
1	16	SER	SER	ILE	ILE	F	F	216 - 247	8 - 39
2	16	SER	SER	ILE	ILE	J	J	216 - 247	8 - 39
1	17	GLY	GLY	MET	MET	F	F	214 - 264	6 - 56
2	17	GLY	GLY	MET	MET	B	B	214 - 264	6 - 56
1	18	GLY	GLY	ALA	ALA	F	F	214 - 259	6 - 51
2	18	GLY	GLY	ALA	ALA	A	A	214 - 259	6 - 51
1	19	MET	MET	THR	THR	K	K	1 - 114	1 - 114
2	19	MET	MET	THR	THR	L	L	1 - 114	1 - 114
1	20	MET	MET	LEU	LEU	K	K	1 - 115	1 - 115
2	20	MET	MET	LEU	LEU	C	C	1 - 115	1 - 115
1	21	MET	MET	LEU	LEU	K	K	1 - 115	1 - 115
2	21	MET	MET	LEU	LEU	D	D	1 - 115	1 - 115
1	22	MET	MET	LEU	LEU	L	L	1 - 115	1 - 115
2	22	MET	MET	LEU	LEU	C	C	1 - 115	1 - 115
1	23	SER	SER	ILE	ILE	I	I	216 - 247	8 - 39
2	23	SER	SER	ILE	ILE	J	J	216 - 247	8 - 39
1	24	SER	SER	GLU	GLU	I	I	216 - 249	8 - 41
2	24	SER	SER	GLU	GLU	B	B	216 - 249	8 - 41
1	25	SER	SER	GLU	GLU	I	I	216 - 249	8 - 41
2	25	SER	SER	GLU	GLU	A	A	216 - 249	8 - 41
1	26	SER	SER	ILE	ILE	J	J	216 - 247	8 - 39
2	26	SER	SER	ILE	ILE	B	B	216 - 247	8 - 39
1	27	SER	SER	ILE	ILE	J	J	216 - 247	8 - 39
2	27	SER	SER	ILE	ILE	A	A	216 - 247	8 - 39
1	28	MET	MET	LEU	LEU	C	C	1 - 115	1 - 115
2	28	MET	MET	LEU	LEU	D	D	1 - 115	1 - 115
1	29	GLY	GLY	ALA	ALA	B	B	214 - 259	6 - 51
2	29	GLY	GLY	ALA	ALA	A	A	214 - 259	6 - 51

NCS ensembles :

#1: Protein	MALE-SPECIFIC LETHAL 1 HOMOLOG / MSL1 / MSL-1 / MALE-SPECIFIC LETHAL 1-LIKE 1 / MSL1-LIKE 1 / MALE-SPECIFIC LETHAL-1 HOMOLOG 1 Mass: 6733.728 Da / Num. of mol.: 6 / Fragment: RESIDUES 212-267 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): STAR / References: UniProt: Q68DK7
#2: Protein	MALE-SPECIFIC LETHAL 2 HOMOLOG / MSL2 / MSL-2 / MALE-SPECIFIC LETHAL 2-LIKE 1 / MSL2-LIKE 1 / MALE-SPECIFIC LETHAL-2 HOMOLOG 1 / ...MSL2 / MSL-2 / MALE-SPECIFIC LETHAL 2-LIKE 1 / MSL2-LIKE 1 / MALE-SPECIFIC LETHAL-2 HOMOLOG 1 / RING FINGER PROTEIN 184 Mass: 13259.478 Da / Num. of mol.: 6 / Fragment: RESIDUES 1-116 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): STAR / References: UniProt: Q9HCI7
#3: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Zn

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.53 Å³/Da / Density % sol: 65 % / Description: NONE
Crystal grow	pH: 7 Details: 0.1 M HEPES PH 7.0, 1.1 M SODIUM MALONATE PH 6.5, 0.8% JEFFAMINE ED 2001

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9795
Detector	Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 21, 2010
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9795 Å / Relative weight: 1
Reflection	Resolution: 3.5→50 Å / Num. obs: 21615 / % possible obs: 97.2 % / Observed criterion σ(I): 1.8 / Redundancy: 3.7 % / R_merge(I) obs: 0.07 / Net I/σ(I): 11
Reflection shell	Resolution: 3.5→3.65 Å / Redundancy: 3.7 % / R_merge(I) obs: 0.72 / Mean I/σ(I) obs: 1.8 / % possible all: 98.2

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Processing

Software

Name	Version	Classification
XDS		data reduction
XSCALE		data scaling
SHELXD		phasing
SHARP		phasing
REFMAC	5.6.0116	refinement

Refinement

Method to determine structure:

MAD
Starting model: NONE

Resolution: 3.5→45.3 Å / Cor.coef. F_o:F_c: 0.928 / Cor.coef. F_o:F_c free: 0.9 / SU B: 73.68 / SU ML: 0.482 / Cross valid method: THROUGHOUT / ESU R Free: 0.133 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES WITH TLS ADDED

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.29668	1164	5.4 %	RANDOM
R_work	0.25569	-	-	-
obs	0.25793	20450	96.98 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 79.442 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-65.76 Å²	0 Å²	0 Å²
2-	-	31.93 Å²	0 Å²
3-	-	-	33.82 Å²

Refinement step

Cycle: LAST / Resolution: 3.5→45.3 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	7030	0	12	0	7042

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.007	0.02	7116
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	0.951	1.989	9595
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	4.612	5	869
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	36.851	26.006	313
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	17.972	15	1385
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	18.366	15	29
X-RAY DIFFRACTION	r_chiral_restr	0.065	0.2	1130
X-RAY DIFFRACTION	r_gen_planes_refined	0.004	0.021	5141
X-RAY DIFFRACTION	r_gen_planes_other
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
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other
X-RAY DIFFRACTION	r_long_range_B_refined
X-RAY DIFFRACTION	r_long_range_B_other
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 / Type: interatomic distance / Weight position: 0.05

LS refinement shell

Resolution: 3.498→3.588 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.374	122	-
R_work	0.388	1419	-
obs	-	-	95.01 %

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	2.6489	0.5034	1.0722	58.1138	7.8521	3.6988	-0.4182	0.06	-0.2294	0.0056	0.8491	0.132	0.3785	0.7863	-0.4309	0.4793	0.0151	-0.0571	0.2855	0.0103	0.6041	13.252	119.1766	43.9802
2	2.3393	3.3302	0.9584	50.9713	0.7105	2.8204	0.202	-0.117	-0.4632	0.2812	0.0524	0.1881	0.4345	-0.06	-0.2544	0.3665	-0.0546	0.0497	0.1195	-0.0351	0.6503	5.7474	116.4871	42.8794
3	42.2733	-14.9136	-11.361	6.5828	2.8176	5.3839	-0.0211	-0.4193	0.3416	0.2892	-0.0019	-0.0631	-0.3934	0.0002	0.023	0.4039	0.0341	-0.0809	0.1168	0.0017	1.0233	17.9809	79.3456	-10.8158
4	58.7703	-19.4314	-3.4696	7.8306	0.4232	2.9803	0.258	-0.0241	-0.3364	0.074	-0.1161	0.3524	0.2068	-0.3717	-0.1419	0.4181	0.0064	-0.0111	0.1057	-0.022	0.8137	15.4997	72.4886	-10.4561
5	18.5693	11.0119	-6.6639	15.1824	-7.2142	5.5498	-0.5426	0.8478	-0.684	0.2997	0.3107	0.1306	-0.5072	-0.7237	0.2319	0.5228	0.0469	0.003	0.1769	-0.1503	0.7415	33.2705	114.914	14.3946
6	16.9885	14.2572	-2.7579	19.4432	-1.3646	4.4182	0.1851	-0.8778	-1.4773	0.2844	-0.756	-0.4801	0.2233	0.2556	0.5709	0.4114	0.0443	0.0072	0.1627	-0.0045	0.7603	40.1182	110.1967	18.1236
7	5.5052	1.0488	0.8417	4.5915	-0.6188	6.1167	-0.1821	0.8281	-0.624	-0.6101	-0.1072	0.1463	0.2228	0.1554	0.2894	0.5545	0.1041	0.0927	0.1735	-0.1899	0.9031	42.0949	108.8956	2.751
8	5.0909	1.0404	-0.7401	3.0708	0.455	6.6066	-0.0496	-0.8429	-0.3281	0.3251	-0.2152	0.0969	0.1683	0.2741	0.2647	0.3907	0.0812	-0.0843	0.1964	-0.041	0.7579	36.6251	119.4191	31.6886
9	4.4514	-0.5577	0.2315	3.8266	-0.3509	5.8779	-0.0201	0.9766	0.62	-0.515	-0.4418	0.1887	-0.2503	-0.091	0.4619	0.5606	0.0026	-0.1398	0.251	0.0892	0.9885	24.1725	67.1753	-27.3766
10	3.7466	-0.2216	2.1136	5.0836	0.1176	7.4847	-0.2174	-0.8601	0.8458	0.5084	-0.0434	0.3053	-0.0858	0.0309	0.2608	0.4345	0.0553	-0.0318	0.2439	-0.1919	1.0369	33.141	75.0411	0.9797
11	3.8959	-0.1726	-1.9101	5.9415	0.8173	9.4271	-0.1695	0.3148	-0.4849	-0.3429	0.0746	0.0008	-0.0041	0.1471	0.0949	0.298	-0.0008	0.0418	0.0386	-0.0581	0.7244	15.3351	129.8844	28.7413
12	5.6074	1.0912	-1.3672	2.1964	1.7711	6.5775	0.0418	-0.937	-0.3374	0.9272	-0.1489	0.1446	0.1727	-0.0406	0.1071	0.6811	-0.0666	0.1512	0.3391	0.0716	0.7074	3.9609	129.3586	57.5617

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	210 - 270
2	X-RAY DIFFRACTION	2	B	210 - 270
3	X-RAY DIFFRACTION	3	E	210 - 270
4	X-RAY DIFFRACTION	4	F	210 - 270
5	X-RAY DIFFRACTION	5	I	210 - 270
6	X-RAY DIFFRACTION	6	J	210 - 270
7	X-RAY DIFFRACTION	7	K	1 - 600
8	X-RAY DIFFRACTION	8	L	1 - 600
9	X-RAY DIFFRACTION	9	G	1 - 600
10	X-RAY DIFFRACTION	10	H	1 - 600
11	X-RAY DIFFRACTION	11	C	1 - 600
12	X-RAY DIFFRACTION	12	D	1 - 600

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