PDB-4f73: Crystal Structure of active HIV-1 Protease in Complex with the N ...

ID or keywords:

Entry

Database: PDB / ID: 4f73

Title

Crystal Structure of active HIV-1 Protease in Complex with the N terminal product of CA-p2 cleavage site

Components

N terminal product of substrate CA-p2
Protease

Keywords

hydrolase/hydrolase product / HIV-1 protease / substrate complex / AIDS / product complex / Aspartyl protease / HYDROLASE / hydrolase-hydrolase product complex

Function / homology

Function and homology information

HIV-1 retropepsin / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / viral penetration into host nucleus ...
Similarity search - Function

Reverse transcriptase connection / Reverse transcriptase connection domain / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. / Integrase-like, N-terminal / Integrase DNA binding domain / Integrase, C-terminal domain superfamily, retroviral / Integrase, N-terminal zinc-binding domain ...
Similarity search - Domain/homology

Biological species

HIV-1 M:B_ARV2/SF2 (virus)

Human immunodeficiency virus 1

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 1.9 Å

Authors

Schiffer, C.A. / Mittal, S. / Nalam, M.N.L.

Citation

Journal: To be Published
Title: Crystal Structure of active HIV-1 Protease in Complex with the N terminal product of CA-p2 cleavage site
Authors: Mittal, S. / Nalam, M.N.L. / Schiffer, C.A.

History

Deposition	May 15, 2012	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	May 15, 2013	Provider: repository / Type: Initial release
Revision 1.1	Nov 15, 2017	Group: Refinement description / Category: software Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.2	Feb 28, 2024	Group: Data collection / Database references / Derived calculations Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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	4f73.cif.gz	97.9 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	4f73_validation.pdf.gz	467.3 KB	Display	wwPDB validaton report
Full document	4f73_full_validation.pdf.gz	470.5 KB	Display
Data in XML	4f73_validation.xml.gz	11.2 KB	Display
Data in CIF	4f73_validation.cif.gz	14.6 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/f7/4f73 ftp://data.pdbj.org/pub/pdb/validation_reports/f7/4f73	HTTPS FTP

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Related structure data

Related structure data	4f74 4f75 4f76
Similar structure data	1zbg-d 1ebk-2 3gi6-d 6b3h-d 3o9a-d 6dh7-d 4njt-1 1hpo-d 6pjl-d 5uov-d 3o9d-d 1xl2-d 1bv7-d 3bgc-d 6pu8-d 2qhy-d 3b80-d 2qd6-d 4f76-d 1d4s-d 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	#6 - Jun 2000 HIV-1 Protease similarity (2) #163 - Jul 2013 HIV Capsid similarity (1)

Deposited unit

A: Protease

B: Protease

C: N terminal product of substrate CA-p2

D: N terminal product of substrate CA-p2

hetero molecules

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

1

Idetical with deposited unit
defined by author&software

Unit cell

Length a, b, c (Å)	50.788, 58.327, 61.636
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	19
Space group name H-M	P2₁2₁2₁

Details

biological unit is the same as asym.

#1: Protein	Protease Mass: 10801.763 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HIV-1 M:B_ARV2/SF2 (virus) / Strain: SF2 / Gene: gag-pol / Plasmid: pXC35 / Production host: Escherichia coli (E. coli) / Strain (production host): TAP56 / References: UniProt: P03369, HIV-1 retropepsin
#2: Protein/peptide	N terminal product of substrate CA-p2 Mass: 587.755 Da / Num. of mol.: 2 / Source method: obtained synthetically Details: synthetic peptide corresponding to CA-p2 cleavage site Source: (synth.) Human immunodeficiency virus 1
#3: Chemical	ChemComp-ACT / ACETATE ION Mass: 59.044 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₂H₃O₂
#4: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₃H₈O₃
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 83 / Source method: isolated from a natural source / Formula: H₂O
Sequence details	AUTHORS CRYSTALLIZED ACTIVE PROTEASE WITH 10-MER LENGTH PEPTIDE CORRESPONDING TO CA-P2 CLEAVAGE ...AUTHORS CRYSTALLIZED ACTIVE PROTEASE WITH 10-MER LENGTH PEPTIDE CORRESPONDING TO CA-P2 CLEAVAGE SITE. DURING CRYSTALLIZATION, PROTEASE CLEAVED THE 10-MER PEPTIDE TO TWO 5-MER PRODUCTS (N-TERMINAL KARVLAEAMS C-TERMINAL, WHERE INDICATES SITE OF HYDROLYSIS). INITIALLY N-TERMINAL PRODUCT IS MODELED IN THE STRUCTURE AS K1-A2-R3-V4-L5. THE C-TERMINAL PRODUCT THAT SHOULD HAVE BEEN THEORETICALLY PRESENT NEXT TO N-TERMINAL PRODUCT IN THE PROTEASE ACTIVE SITE MAY HAVE PROBABLY DIFFUSED AWAY POST CLEAVAGE AND (THE DENSITY FOR IT) IS ABSENT IN THE CRYSTAL STRUCTURE. WHAT AUTHORS OBSERVED IS A PARTIAL DENSITY FOR ANOTHER N-TERMINAL PRODUCT FRAGMENT IN ITS PLACE. THIS IS BECAUSE THE CRYSTALLIZED DIMER IS NOT UNIQUELY ORIENTED IN THE CRYSTAL LATTICE. POSSIBLY DUE TO THE AVERAGING OF ELECTRON DENSITY OF ANOTHER PROTEASE DIMER WITH N-TERMINAL PRODUCT THAT IS IN THE OPPOSITE ORIENTATION AS THE FIRST LEADS TO THE OVERALL IMPRESSION OF TWO, SEPARATE N-TERMINAL PRODUCTS BEING PRESENT IN THE ACTIVE SITE OF THE CRYSTALLIZED PROTEASE DIMER. THEREFORE, ARVLLVR IS MODELELD IN ACTIVE SITE WHICH IS NOTHING BUT TWO n-TERMINAL PEPTIDES IN OPPOSITE DIRECTIONS.

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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 Å³/Da / Density % sol: 38.62 %
Crystal grow	Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6.2 Details: 126mM Phosphate buffer pH 6.2, 63mM Sodium Citrate, 24-31% Ammonium Sulfate, hanging drop, vapor diffusion, temperature 295K, VAPOR DIFFUSION, HANGING DROP

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 14-BM-C / Wavelength: 0.9 Å

Detector

Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 15, 2010

Radiation

Protocol: SINGLE WAVELENGTH / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.9 Å / Relative weight: 1

Reflection

Resolution: 1.9→50 Å / Num. obs: 14927 / % possible obs: 99.9 % / Redundancy: 7.7 % / R_merge(I) obs: 0.086 / Χ²: 1.038 / Net I/σ(I): 9.3

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique all	Χ²	Diffraction-ID	% possible all
1.9-1.97	7.9	0.426	1457	1.048	1	100
1.97-2.05	7.9	0.31	1470	1.065	1	100
2.05-2.14	7.9	0.256	1461	1.05	1	100
2.14-2.25	7.9	0.205	1461	1.021	1	100
2.25-2.39	7.9	0.18	1472	1.03	1	100
2.39-2.58	7.8	0.142	1491	1.072	1	100
2.58-2.84	7.8	0.11	1481	1.005	1	100
2.84-3.25	7.6	0.084	1506	1.046	1	100
3.25-4.09	7.4	0.057	1515	1.023	1	100
4.09-50	6.9	0.036	1613	1.022	1	99.4

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
PHASER		phasing
REFMAC		refinement
PDB_EXTRACT	3.11	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.9→42.36 Å / Cor.coef. F_o:F_c: 0.959 / Cor.coef. F_o:F_c free: 0.93 / WR_factor R_free: 0.216 / WR_factor R_work: 0.1652 / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.8725 / SU B: 6.715 / SU ML: 0.092 / SU R Cruickshank DPI: 0.1571 / SU R_free: 0.1501 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.157 / ESU R Free: 0.15 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2225	754	5.1 %	RANDOM
R_work	0.1674	-	-	-
obs	0.17	14809	99.32 %	-

Solvent computation

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

Displacement parameters

B_iso max: 54.4 Å² / B_iso mean: 25.3862 Å² / B_iso min: 11.99 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-1.03 Å²	0 Å²	0 Å²
2-	-	-0.04 Å²	0 Å²
3-	-	-	1.06 Å²

Refinement step

Cycle: LAST / Resolution: 1.9→42.36 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	1538	0	10	83	1631

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.009	0.022	1646
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	1109
X-RAY DIFFRACTION	r_angle_refined_deg	1.403	1.988	2246
X-RAY DIFFRACTION	r_angle_other_deg	0.848	3	2731
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.795	5	215
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	40.788	24.516	62
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	13.012	15	279
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	21.738	15	11
X-RAY DIFFRACTION	r_chiral_restr	0.088	0.2	265
X-RAY DIFFRACTION	r_gen_planes_refined	0.005	0.021	1840
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	299
X-RAY DIFFRACTION	r_mcbond_it	0.646	1.5	1055
X-RAY DIFFRACTION	r_mcbond_other	0.201	1.5	438
X-RAY DIFFRACTION	r_mcangle_it	1.119	2	1713
X-RAY DIFFRACTION	r_scbond_it	1.83	3	591
X-RAY DIFFRACTION	r_scangle_it	2.839	4.5	533

LS refinement shell

Resolution: 1.903→1.952 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.213	58	-
R_work	0.17	1009	-
all	-	1067	-
obs	-	-	98.07 %

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	8.8845	3.0818	-7.3156	6.5263	-7.1201	9.8758	-0.085	0.2156	-0.0156	-0.4851	0.0791	-0.0058	0.411	-0.1783	0.0059	0.3482	-0.0989	-0.0376	0.176	-0.0376	0.0543	20.6752	1.7574	-1.9366
2	13.691	1.2729	3.4986	2.7918	0.6928	0.9658	0.1067	0.2458	-0.4614	-0.1305	0.0115	-0.2552	0.0604	0.0542	-0.1182	0.1546	-0.007	0.0563	0.0756	-0.0055	0.0817	31.1985	-2.4079	6.0633
3	7.9165	1.5444	-0.1449	5.1598	2.211	2.5425	-0.2602	-0.1472	-0.4108	-0.2113	0.2098	-0.5871	0.1987	0.0723	0.0504	0.152	0.0359	0.0751	0.0596	0.0162	0.2131	38.3647	-4.2952	8.4067
4	5.8338	-5.4743	-3.7879	8.0848	6.2156	4.8816	-0.1207	-0.0234	-0.2266	0.1748	-0.0003	0.1684	0.1855	0.0059	0.121	0.1493	-0.0002	0.0269	0.0676	0.0139	0.0644	23.7308	2.2434	10.702
5	14.0735	-12.9177	0.2687	22.1202	-1.0632	3.3923	-0.2729	-0.3748	-0.3566	0.4102	0.225	-0.0576	0.132	0.1051	0.0478	0.074	-0.0336	-0.0015	0.0789	-0.0044	0.0573	30.8673	-0.8011	17.6917
6	10.7168	3.6265	-1.5719	11.0682	9.8129	11.1053	-0.0998	-0.1932	-0.3994	-0.1927	0.3495	-0.4219	-0.162	0.481	-0.2497	0.1591	0.0319	-0.0192	0.2436	0.0596	0.2404	42.8869	-1.3062	20.0256
7	22.7631	-0.9744	-5.8217	3.859	-0.9472	6.5826	0.1549	-1.1548	0.7643	0.2662	-0.1381	-0.1929	0.1739	0.5523	-0.0167	0.1518	-0.0261	-0.0423	0.1547	-0.0395	0.0756	34.8899	1.6681	28.714
8	3.1386	1.0696	-0.8452	5.5523	2.5125	1.7399	-0.1023	0.1055	0.6791	0.0476	0.0259	0.6969	0.0689	-0.0426	0.0764	0.1799	-0.0215	-0.006	0.1874	0.0421	0.192	21.0657	-2.0905	24.6377
9	14.8625	10.1556	-7.1033	9.8402	-4.2391	4.2939	0.2281	-0.3422	-0.0774	0.4646	-0.2795	-0.1495	-0.0542	0.497	0.0515	0.1087	-0.0004	-0.033	0.1682	0.0045	0.0404	32.6805	-1.3087	25.9919
10	1.7371	2.0533	-0.6179	5.1944	-6.4137	11.901	0.2302	-0.3591	-0.0646	0.2476	-0.6418	-0.2676	-0.0613	0.6477	0.4116	0.0958	-0.0042	-0.0316	0.2205	-0.0245	0.2354	40.1087	6.5695	18.6142
11	7.7874	-1.7816	5.6428	11.542	-6.4069	19.5422	0.2033	0.7428	-0.2827	-0.6267	0.0323	-0.1851	-0.0894	0.3076	-0.2355	0.1258	0.0011	0.0707	0.0886	-0.032	0.114	36.2934	5.6181	4.5856
12	0.895	0.1403	0.7647	5.0045	-0.7657	2.1696	0.0247	-0.1493	0.0352	0.2019	-0.0439	-0.1301	-0.0419	0.0508	0.0191	0.0233	0.005	0.0073	0.0603	-0.0002	0.0791	34.264	2.4658	17.3006
13	1.5523	-4.478	2.0683	13.4695	-5.521	3.1269	0.0828	-0.0748	-0.1636	0.0334	0.203	0.4298	0.3539	-0.076	-0.2859	0.1823	-0.0219	0.0072	0.1227	0.0125	0.1551	28.2495	-2.4422	13.3172
14	5.4496	1.6282	1.6597	4.7184	-0.0766	0.5832	-0.0627	0.0729	0.0801	-0.1223	0.0328	-0.0692	-0.0049	0.0237	0.0299	0.0604	-0.0069	0.0202	0.0611	-0.0119	0.075	29.3238	10.2035	10.6211
15	5.4341	7.0826	5.0147	9.2499	6.2407	9.6303	-0.2647	-0.2238	0.2886	-0.3307	-0.2741	0.3594	-0.3148	-0.3741	0.5388	0.1738	-0.0048	-0.025	0.1342	-0.0016	0.0901	18.5405	10.4992	2.7858
16	10.2262	3.8126	7.4671	4.0452	3.5789	9.3087	-0.2123	0.3565	0.6234	-0.5176	-0.0268	0.4509	-0.4021	0.0352	0.2391	0.2397	0.0083	-0.0499	0.1293	0.0108	0.1777	20.3122	14.7913	7.5855
17	28.1231	-0.2063	0.8052	0.3465	0.9638	3.2396	-0.194	-0.6395	0.3358	0.0385	-0.0028	0.1555	0.006	-0.0817	0.1968	0.1338	0.0222	0.0277	0.1222	0.0052	0.2203	14.3136	10.8941	13.964
18	11.6534	7.4068	-1.745	13.3351	5.0549	4.6666	0.1955	-0.0834	0.6597	0.6499	-0.5886	1.0812	0.3425	-0.3906	0.3931	0.2046	0.0267	0.0328	0.3977	-0.0358	0.2756	-0.4403	5.4836	12.3681
19	18.0577	-4.7001	-6.1148	5.2499	2.3258	3.9105	0.0658	-0.1172	-0.1791	0.2814	-0.148	0.2397	-0.2767	-0.2642	0.0821	0.1249	-0.0115	0.0181	0.1171	-0.0123	0.1421	8.5092	7.7851	14.161
20	9.3335	4.5505	-3.2234	7.3252	-0.2605	2.0626	-0.0179	-0.066	-0.4918	-0.0239	-0.0059	-0.3162	0.2511	-0.0125	0.0238	0.1133	-0.0119	-0.028	0.0988	0.0152	0.0939	15.9306	-2.2874	9.9171
21	23.7188	0.7605	-15.4536	5.4924	4.5307	26.9482	0.4027	-0.7575	-0.0282	0.2568	-0.1986	0.361	-0.5393	-0.0037	-0.2041	0.1212	-0.0248	0.0272	0.0817	0.0406	0.0998	6.4821	-0.6135	19.664
22	14.5067	9.3641	7.9091	17.4626	11.5581	7.964	0.1036	-0.2434	0.6904	-0.1338	-0.5287	0.596	-0.0555	-0.3706	0.4251	0.1643	0.02	-0.025	0.2792	0.104	0.2297	-2.966	-4.8718	16.6875
23	39.7915	-4.9981	4.4504	4.1853	-2.2008	5.1517	-0.229	-0.6731	-0.2819	-0.1837	0.4725	0.3611	0.3476	-0.4525	-0.2435	0.0955	-0.053	-0.0173	0.099	0.0462	0.1177	5.7975	-13.5602	16.8243
24	13.9286	10.2041	1.3094	7.7858	2.3149	6.1372	-0.0517	0.132	0.0854	-0.0755	0.0973	0.0352	-0.233	0.1142	-0.0456	0.0932	-0.0245	-0.0207	0.0661	0.0441	0.0771	18.9716	-8.6362	20.0218
25	11.2788	0.9273	6.7635	4.3015	-1.4145	10.6567	0.2135	-0.2917	-0.1148	0.0897	0.2248	0.3946	0.4228	-0.1559	-0.4383	0.0721	-0.0204	0.0034	0.0671	0.0366	0.0901	7.4964	-10.0407	18.9353
26	11.5061	-6.6049	5.8659	10.6092	-9.3384	8.2225	0.3077	0.1713	-0.5218	-0.5745	-0.0657	0.2435	0.5092	0.0294	-0.242	0.1233	-0.0606	-0.0256	0.1606	0.0547	0.1392	0.5923	-5.8425	8.5685
27	4.0655	0.6085	-4.3655	0.3932	0.9461	15.3834	0.0603	-0.2227	0.4792	0.0018	-0.1843	0.1051	-0.4611	-0.0295	0.124	0.1474	-0.0348	-0.0679	0.1486	0.043	0.1774	4.8845	7.5625	4.758
28	1.8971	-2.5384	4.2795	13.236	-11.3684	12.9128	0.0343	0.001	-0.0011	0.2575	0.1871	0.4831	-0.1482	-0.1042	-0.2215	0.1092	-0.0152	-0.018	0.1151	0.0129	0.143	3.5257	-1.3809	5.1613
29	6.383	2.8373	-2.0433	6.8446	-0.2136	7.5382	0.1775	-0.7345	-0.0902	0.4026	-0.1931	-0.0085	-0.6606	0.3328	0.0156	0.1158	-0.0198	0.0163	0.1481	0.0511	0.0932	9.1335	-3.4568	20.0745
30	5.6682	-1.3079	-6.3735	8.3891	5.8695	12.865	0.1298	-0.2266	0.1581	0.3103	0.1106	0.1238	0.14	0.1772	-0.2404	0.0475	-0.0224	-0.006	0.0378	0.0148	0.0519	12.7899	0.8863	12.1795
31	2.0792	-0.6505	2.4582	4.7046	-1.2584	2.9636	-0.1856	0.0236	0.0518	-0.2943	0.1969	0.4054	-0.1347	-0.0103	-0.0113	0.1903	-0.0578	-0.0517	0.2107	0.0406	0.1232	10.7311	1.0207	2.3419
32	32.7972	8.2331	4.1549	8.3569	-1.5922	3.9872	-0.4092	0.245	-0.053	-0.4841	0.3957	-0.1448	0.17	0.199	0.0135	0.1353	-0.0372	0.0024	0.0904	-0.0183	0.0372	22.8389	7.3731	0.7205

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	1 - 6
2	X-RAY DIFFRACTION	2	A	7 - 16
3	X-RAY DIFFRACTION	3	A	17 - 22
4	X-RAY DIFFRACTION	4	A	23 - 28
5	X-RAY DIFFRACTION	5	A	29 - 35
6	X-RAY DIFFRACTION	6	A	36 - 41
7	X-RAY DIFFRACTION	7	A	42 - 46
8	X-RAY DIFFRACTION	8	A	47 - 53
9	X-RAY DIFFRACTION	9	A	54 - 58
10	X-RAY DIFFRACTION	10	A	59 - 63
11	X-RAY DIFFRACTION	11	A	64 - 69
12	X-RAY DIFFRACTION	12	A	70 - 80
13	X-RAY DIFFRACTION	13	A	81 - 86
14	X-RAY DIFFRACTION	14	A	87 - 94
15	X-RAY DIFFRACTION	15	A	95 - 99
16	X-RAY DIFFRACTION	16	B	1 - 6
17	X-RAY DIFFRACTION	17	B	7 - 12
18	X-RAY DIFFRACTION	18	B	13 - 18
19	X-RAY DIFFRACTION	19	B	19 - 24
20	X-RAY DIFFRACTION	20	B	25 - 31
21	X-RAY DIFFRACTION	21	B	32 - 35
22	X-RAY DIFFRACTION	22	B	36 - 41
23	X-RAY DIFFRACTION	23	B	42 - 46
24	X-RAY DIFFRACTION	24	B	47 - 53
25	X-RAY DIFFRACTION	25	B	54 - 58
26	X-RAY DIFFRACTION	26	B	59 - 63
27	X-RAY DIFFRACTION	27	B	64 - 69
28	X-RAY DIFFRACTION	28	B	70 - 75
29	X-RAY DIFFRACTION	29	B	76 - 81
30	X-RAY DIFFRACTION	30	B	82 - 87
31	X-RAY DIFFRACTION	31	B	88 - 94
32	X-RAY DIFFRACTION	32	B	95 - 99

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