PDB-2zp8: The Nature of the TRAP:Anti-TRAP complex

ID or keywords:

Entry

Database: PDB / ID: 2zp8

Title

The Nature of the TRAP:Anti-TRAP complex

Components

Transcription attenuation protein mtrB
Tryptophan RNA-binding attenuator protein-inhibitory protein

Keywords

RNA BINDING PROTEIN/TRANSCRIPTION / PROTEIN-PROTEIN COMPLEX / TRANSCRIPTION / RNA-binding / Transcription regulation / RNA BINDING PROTEIN-TRANSCRIPTION COMPLEX

Function / homology

Function and homology information

DNA-templated transcription termination / regulation of DNA-templated transcription / RNA binding / identical protein binding / cytoplasm
Similarity search - Function

Biological species

Bacillus stearothermophilus (bacteria)

Bacillus subtilis (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.2 Å

Authors

Watanabe, M. / Heddle, J.G. / Unzai, S. / Akashi, S. / Park, S.Y. / Tame, J.R.H.

Citation

Journal: Proc.Natl.Acad.Sci.USA / Year: 2009
Title: The nature of the TRAP-Anti-TRAP complex.
Authors: Watanabe, M. / Heddle, J.G. / Kikuchi, K. / Unzai, S. / Akashi, S. / Park, S.Y. / Tame, J.R.

History

Deposition	Jul 8, 2008	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	Feb 3, 2009	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.2	Mar 5, 2014	Group: Database references
Revision 1.3	Nov 1, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / 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_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_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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Download

PDBx/mmCIF format	2zp8.cif.gz	122.5 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	2zp8_validation.pdf.gz	513.4 KB	Display	wwPDB validaton report
Full document	2zp8_full_validation.pdf.gz	528 KB	Display
Data in XML	2zp8_validation.xml.gz	21.8 KB	Display
Data in CIF	2zp8_validation.cif.gz	30.6 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/zp/2zp8 ftp://data.pdbj.org/pub/pdb/validation_reports/zp/2zp8	HTTPS FTP

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Related structure data

Related structure data	2zp9C 1qawS 2bx9S C: citing same article (ref.) S: Starting model for refinement
Similar structure data	2zp9-2 3ide-d 8892 5xmi-d 8888 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	#228 - Dec 2018 Directed Evolution of Enzymes similarity (1)

Deposited unit

A: Transcription attenuation protein mtrB

B: Transcription attenuation protein mtrB

C: Transcription attenuation protein mtrB

D: Transcription attenuation protein mtrB

E: Tryptophan RNA-binding attenuator protein-inhibitory protein

F: Tryptophan RNA-binding attenuator protein-inhibitory protein

G: Tryptophan RNA-binding attenuator protein-inhibitory protein

H: Tryptophan RNA-binding attenuator protein-inhibitory protein

I: Tryptophan RNA-binding attenuator protein-inhibitory protein

J: Tryptophan RNA-binding attenuator protein-inhibitory protein

hetero molecules

68.2 kDa, 10 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Transcription attenuation protein mtrB

B: Transcription attenuation protein mtrB

C: Transcription attenuation protein mtrB

D: Transcription attenuation protein mtrB

E: Tryptophan RNA-binding attenuator protein-inhibitory protein

F: Tryptophan RNA-binding attenuator protein-inhibitory protein

G: Tryptophan RNA-binding attenuator protein-inhibitory protein

H: Tryptophan RNA-binding attenuator protein-inhibitory protein

I: Tryptophan RNA-binding attenuator protein-inhibitory protein

J: Tryptophan RNA-binding attenuator protein-inhibitory protein

hetero molecules

A: Transcription attenuation protein mtrB

B: Transcription attenuation protein mtrB

C: Transcription attenuation protein mtrB

D: Transcription attenuation protein mtrB

E: Tryptophan RNA-binding attenuator protein-inhibitory protein

F: Tryptophan RNA-binding attenuator protein-inhibitory protein

G: Tryptophan RNA-binding attenuator protein-inhibitory protein

H: Tryptophan RNA-binding attenuator protein-inhibitory protein

I: Tryptophan RNA-binding attenuator protein-inhibitory protein

J: Tryptophan RNA-binding attenuator protein-inhibitory protein

hetero molecules

A: Transcription attenuation protein mtrB

B: Transcription attenuation protein mtrB

C: Transcription attenuation protein mtrB

D: Transcription attenuation protein mtrB

E: Tryptophan RNA-binding attenuator protein-inhibitory protein

F: Tryptophan RNA-binding attenuator protein-inhibitory protein

G: Tryptophan RNA-binding attenuator protein-inhibitory protein

H: Tryptophan RNA-binding attenuator protein-inhibitory protein

I: Tryptophan RNA-binding attenuator protein-inhibitory protein

J: Tryptophan RNA-binding attenuator protein-inhibitory protein

hetero molecules

defined by author&software
205 kDa, 30 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	201.134, 201.134, 133.168
Angle α, β, γ (deg.)	90.00, 90.00, 120.00
Int Tables number	155
Space group name H-M	H32

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: 1 / Refine code: 3

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	VAL	VAL	ILE	ILE	A	A	10 - 70	8 - 68
2	1	VAL	VAL	ILE	ILE	B	B	10 - 70	8 - 68
3	1	VAL	VAL	ILE	ILE	C	C	10 - 70	8 - 68
4	1	VAL	VAL	ILE	ILE	D	D	10 - 70	8 - 68
1	2	MET	MET	GLU	GLU	E	E	1 - 9	1 - 9
2	2	MET	MET	GLU	GLU	F	F	1 - 9	1 - 9
3	2	MET	MET	GLU	GLU	G	G	1 - 9	1 - 9
4	2	MET	MET	GLU	GLU	H	H	1 - 9	1 - 9
5	2	MET	MET	GLU	GLU	I	I	1 - 9	1 - 9
6	2	MET	MET	GLU	GLU	J	J	1 - 9	1 - 9
1	3	VAL	VAL	ILE	ILE	E	E	10 - 35	10 - 35
2	3	VAL	VAL	ILE	ILE	F	F	10 - 35	10 - 35
3	3	VAL	VAL	ILE	ILE	G	G	10 - 35	10 - 35
4	3	VAL	VAL	ILE	ILE	H	H	10 - 35	10 - 35
5	3	VAL	VAL	ILE	ILE	I	I	10 - 35	10 - 35
6	3	VAL	VAL	ILE	ILE	J	J	10 - 35	10 - 35
1	4	LEU	LEU	LYS	LYS	E	E	36 - 53	36 - 53
2	4	LEU	LEU	LYS	LYS	F	F	36 - 53	36 - 53
3	4	LEU	LEU	LYS	LYS	G	G	36 - 53	36 - 53
4	4	LEU	LEU	LYS	LYS	H	H	36 - 53	36 - 53
5	4	LEU	LEU	LYS	LYS	I	I	36 - 53	36 - 53
6	4	LEU	LEU	LYS	LYS	J	J	36 - 53	36 - 53

NCS ensembles :

ID
1
2
3
4

Details

THIS PDB FILE SHOWS THE COMPLEX BETWEEN WILD-TYPE BACILLUS STEAROTHERMOPHILUS TRAP AND BACILLUS SUBTILIS ANTI-TRAP. THE TRAP RING HAS SPONTANEOUSLY SHIFTED TO A 12-MER RING FROM THE USUAL 11-MER FORM. SOLUTION EXPERIMENTS SHOW THIS 12-MER RING FORM TO BE A MINOR SPECIES, HOWEVER, MUTATIONAL ANALYSIS INDICATES THE TRAP:ANTI-TRAP INTERFACE TO BE THE SAME AS THAT MADE BY 11-MER TRAP.

#1: Protein	Transcription attenuation protein mtrB / Tryptophan RNA-binding attenuator protein / Trp RNA-binding attenuation protein / TRAP Mass: 8257.377 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus stearothermophilus (bacteria) / Gene: mtrB / Plasmid: pET21b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9X6J6
#2: Protein	Tryptophan RNA-binding attenuator protein-inhibitory protein / Anti-TRAP protein / AT Mass: 5655.565 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) / Gene: rtpA, yczA, BSU02530 / Plasmid: pET21b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O31466
#3: Chemical	ChemComp-TRP / TRYPTOPHAN Type: L-peptide linking / Mass: 204.225 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₁H₁₂N₂O₂
#4: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 6 / 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: 3.87 Å³/Da / Density % sol: 68.22 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 9 Details: 0.1M bicine pH 9.0, 10-13% PEG 10000, 2% dioxane, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 1 Å
Detector	Type: ADSC QUANTUM 270 / Detector: CCD / Date: Oct 27, 2007
Radiation	Monochromator: Si(111) crystals / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1 Å / Relative weight: 1
Reflection	Resolution: 3.2→50 Å / Num. obs: 13867 / % possible obs: 81.1 % / Redundancy: 5.7 % / B_iso Wilson estimate: 64 Å² / R_merge(I) obs: 0.082 / R_sym value: 0.072
Reflection shell	Resolution: 3.2→3.31 Å / Redundancy: 4.2 % / R_merge(I) obs: 0.203 / Mean I/σ(I) obs: 1.6 / Num. unique all: 910 / R_sym value: 0.217 / % possible all: 53.9

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Processing

Software

Name	Version	Classification
REFMAC	5.2.0005	refinement
HKL-2000		data collection
DENZO		data reduction
SCALEPACK		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 2BX9, 1QAW

2bx9

1qaw

Resolution: 3.2→20 Å / Cor.coef. F_o:F_c: 0.89 / Cor.coef. F_o:F_c free: 0.857 / SU B: 42.047 / SU ML: 0.396 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.551 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2676	718	5.2 %	RANDOM
R_work	0.22869	-	-	-
obs	0.23067	13074	80.92 %	-

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: 64.012 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-4.71 Å²	-2.36 Å²	0 Å²
2-	-	-4.71 Å²	0 Å²
3-	-	-	7.07 Å²

Refinement step

Cycle: LAST / Resolution: 3.2→20 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	4493	0	66	0	4559

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.009	0.022	4587
X-RAY DIFFRACTION	r_angle_refined_deg	1.104	1.968	6193
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.269	5	583
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	36.786	24.759	187
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	18.951	15	805
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	18.11	15	22
X-RAY DIFFRACTION	r_chiral_restr	0.083	0.2	724
X-RAY DIFFRACTION	r_gen_planes_refined	0.003	0.02	3392
X-RAY DIFFRACTION	r_nbd_refined	0.221	0.2	2060
X-RAY DIFFRACTION	r_nbtor_refined	0.309	0.2	3049
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.141	0.2	162
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.183	0.2	51
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.169	0.2	13
X-RAY DIFFRACTION	r_mcbond_it	0.22	1.5	3027
X-RAY DIFFRACTION	r_mcangle_it	0.374	2	4728
X-RAY DIFFRACTION	r_scbond_it	0.7	3	1720
X-RAY DIFFRACTION	r_scangle_it	1.212	4.5	1465

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	244	tight positional	0.03	0.05
1	2	B	244	tight positional	0.03	0.05
1	3	C	244	tight positional	0.04	0.05
1	4	D	244	tight positional	0.03	0.05
2	1	E	36	tight positional	0.05	0.05
2	2	F	36	tight positional	0.05	0.05
2	3	G	36	tight positional	0.04	0.05
2	4	H	36	tight positional	0.05	0.05
2	5	I	36	tight positional	0.04	0.05
2	6	J	36	tight positional	0.03	0.05
3	1	E	104	tight positional	0.03	0.05
3	2	F	104	tight positional	0.03	0.05
3	3	G	104	tight positional	0.03	0.05
3	4	H	104	tight positional	0.02	0.05
3	5	I	104	tight positional	0.02	0.05
3	6	J	104	tight positional	0.04	0.05
4	1	E	72	tight positional	0.03	0.05
4	2	F	72	tight positional	0.03	0.05
4	3	G	72	tight positional	0.03	0.05
4	4	H	72	tight positional	0.03	0.05
4	5	I	72	tight positional	0.03	0.05
4	6	J	72	tight positional	0.03	0.05
1	1	A	222	loose positional	0.34	5
1	2	B	222	loose positional	0.29	5
1	3	C	222	loose positional	0.38	5
1	4	D	222	loose positional	0.36	5
2	1	E	32	loose positional	1.01	5
2	2	F	32	loose positional	0.78	5
2	3	G	32	loose positional	0.8	5
2	4	H	32	loose positional	0.92	5
2	5	I	32	loose positional	0.8	5
2	6	J	32	loose positional	0.76	5
3	1	E	71	loose positional	0.6	5
3	2	F	71	loose positional	0.38	5
3	3	G	71	loose positional	0.41	5
3	4	H	71	loose positional	0.5	5
3	5	I	71	loose positional	0.42	5
3	6	J	71	loose positional	0.35	5
4	1	E	77	loose positional	1.11	5
4	2	F	77	loose positional	0.87	5
4	3	G	77	loose positional	0.77	5
4	4	H	77	loose positional	1.01	5
4	5	I	77	loose positional	0.75	5
4	6	J	77	loose positional	0.82	5
1	1	A	244	tight thermal	0.05	0.5
1	2	B	244	tight thermal	0.05	0.5
1	3	C	244	tight thermal	0.05	0.5
1	4	D	244	tight thermal	0.05	0.5
2	1	E	36	tight thermal	0.04	0.5
2	2	F	36	tight thermal	0.04	0.5
2	3	G	36	tight thermal	0.04	0.5
2	4	H	36	tight thermal	0.05	0.5
2	5	I	36	tight thermal	0.04	0.5
2	6	J	36	tight thermal	0.04	0.5
3	1	E	104	tight thermal	0.02	0.5
3	2	F	104	tight thermal	0.03	0.5
3	3	G	104	tight thermal	0.04	0.5
3	4	H	104	tight thermal	0.02	0.5
3	5	I	104	tight thermal	0.02	0.5
3	6	J	104	tight thermal	0.03	0.5
4	1	E	72	tight thermal	0.04	0.5
4	2	F	72	tight thermal	0.03	0.5
4	3	G	72	tight thermal	0.03	0.5
4	4	H	72	tight thermal	0.03	0.5
4	5	I	72	tight thermal	0.03	0.5
4	6	J	72	tight thermal	0.04	0.5
1	1	A	222	loose thermal	0.66	10
1	2	B	222	loose thermal	0.89	10
1	3	C	222	loose thermal	0.91	10
1	4	D	222	loose thermal	0.89	10
2	1	E	32	loose thermal	1.13	10
2	2	F	32	loose thermal	0.75	10
2	3	G	32	loose thermal	0.57	10
2	4	H	32	loose thermal	0.57	10
2	5	I	32	loose thermal	0.73	10
2	6	J	32	loose thermal	0.76	10
3	1	E	71	loose thermal	0.56	10
3	2	F	71	loose thermal	0.42	10
3	3	G	71	loose thermal	0.38	10
3	4	H	71	loose thermal	0.2	10
3	5	I	71	loose thermal	0.55	10
3	6	J	71	loose thermal	0.61	10
4	1	E	77	loose thermal	0.68	10
4	2	F	77	loose thermal	0.6	10
4	3	G	77	loose thermal	0.75	10
4	4	H	77	loose thermal	0.72	10
4	5	I	77	loose thermal	0.45	10
4	6	J	77	loose thermal	0.76	10

LS refinement shell

Resolution: 3.204→3.285 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.287	35	-
R_work	0.252	621	-
obs	-	718	53.51 %

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	0.8743	-0.767	-0.0549	1.9073	0.0374	0.5312	-0.0333	0.1685	-0.0646	-0.1654	-0.0058	0.1767	-0.0249	-0.0643	0.0391	-0.2865	-0.0512	-0.0462	-0.2498	-0.0219	0.0358	-22.923	-9.4614	49.8323
2	16.1936	5.935	3.2847	13.5507	1.7421	13.3275	-1.1307	2.5723	-0.5456	-3.1656	0.6744	-1.5602	-0.8877	0.7968	0.4563	0.4061	-0.0226	0.0991	0.1522	-0.4064	0.4693	-17.1059	-40.5294	29.4012
3	4.1869	7.7126	-2.149	34.0384	-1.845	1.3282	-0.2887	0.9256	-0.4627	-1.9069	0.2625	3.9635	0.2788	-0.0781	0.0262	-0.0097	-0.0629	-0.2772	0.1522	-0.3036	0.7707	-34.5552	-48.627	37.3922
4	5.1813	-2.0852	0.4139	14.502	1.68	0.2826	0.135	0.5537	0.25	-0.9021	0.1597	1.3066	-0.5804	-0.4538	-0.2947	-0.0036	-0.0175	-0.257	0.1304	-0.0044	0.3812	-31.2149	-29.3365	38.3056
5	17.2117	-0.6164	0.6981	8.7307	0.3784	12.9051	-0.0986	3.0113	-0.4958	-1.8795	-0.3726	-0.145	0.2848	0.7787	0.4712	0.2714	-0.1809	-0.3096	0.319	0.0053	0.6625	-43.7355	-5.5666	29.522
6	12.4625	-1.6362	-4.0168	1.5238	1.728	2.396	-0.2183	1.6523	0.6211	-0.9142	0.1648	1.5137	-0.28	-0.9825	0.0535	0.218	0.0369	-0.4296	0.3403	0.0418	0.959	-59.5174	5.7319	37.163
7	11.4878	5.7216	2.0226	11.9404	2.8225	0.7185	-0.1519	0.854	1.3167	-1.6919	0.0418	1.4777	-0.7454	0.3903	0.1101	0.3333	0.0187	-0.4098	-0.0494	0.2391	0.4488	-40.9654	12.3867	38.1252

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	10 - 70	8 - 68
2	X-RAY DIFFRACTION	1	B	B	10 - 70	8 - 68
3	X-RAY DIFFRACTION	1	C	C	10 - 70	8 - 68
4	X-RAY DIFFRACTION	1	D	D	10 - 70	8 - 68
5	X-RAY DIFFRACTION	2	E	E	1 - 9	1 - 9
6	X-RAY DIFFRACTION	2	E	E	36 - 53	36 - 53
7	X-RAY DIFFRACTION	2	E	E	10 - 35	10 - 35
8	X-RAY DIFFRACTION	2	E	L	54	1
9	X-RAY DIFFRACTION	3	F	F	1 - 9	1 - 9
10	X-RAY DIFFRACTION	3	F	F	36 - 53	36 - 53
11	X-RAY DIFFRACTION	3	F	F	10 - 35	10 - 35
12	X-RAY DIFFRACTION	3	F	M	54	1
13	X-RAY DIFFRACTION	4	G	G	1 - 9	1 - 9
14	X-RAY DIFFRACTION	4	G	G	36 - 53	36 - 53
15	X-RAY DIFFRACTION	4	G	G	10 - 35	10 - 35
16	X-RAY DIFFRACTION	4	G	N	54	1
17	X-RAY DIFFRACTION	5	H	H	1 - 9	1 - 9
18	X-RAY DIFFRACTION	5	H	H	36 - 53	36 - 53
19	X-RAY DIFFRACTION	5	H	H	10 - 35	10 - 35
20	X-RAY DIFFRACTION	5	H	O	54	1
21	X-RAY DIFFRACTION	6	I	I	1 - 9	1 - 9
22	X-RAY DIFFRACTION	6	I	I	36 - 53	36 - 53
23	X-RAY DIFFRACTION	6	I	I	10 - 35	10 - 35
24	X-RAY DIFFRACTION	6	I	P	54	1
25	X-RAY DIFFRACTION	7	J	J	1 - 9	1 - 9
26	X-RAY DIFFRACTION	7	J	J	36 - 53	36 - 53
27	X-RAY DIFFRACTION	7	J	J	10 - 35	10 - 35
28	X-RAY DIFFRACTION	7	J	K	54	1

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