PDB-8cjd: AetF, a single-component flavin-dependent tryptophan halogenase

ID or keywords:

Entry

Database: PDB / ID: 8cjd

Title

AetF, a single-component flavin-dependent tryptophan halogenase

Components

AetF

Keywords

FLAVOPROTEIN / single-component flavin-dependent halogenase / Aetokthonotoxin / single-component monooxygenase / tryptophan halogenase

Function / homology

FAD/NAD(P)-binding domain superfamily / nucleotide binding / metal ion binding / FLAVIN-ADENINE DINUCLEOTIDE / DI(HYDROXYETHYL)ETHER / AetF

Function and homology information

Biological species

Aetokthonos hydrillicola Thurmond2011 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.7 Å

Authors

Gafe, S. / Niemann, H.H.

Funding support

Germany, 1items

Citation

Journal: Acta Crystallogr D Struct Biol / Year: 2023
Title: Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF.
Authors: Gafe, S. / Niemann, H.H.

History

Deposition	Feb 13, 2023	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jun 14, 2023	Provider: repository / Type: Initial release
Revision 1.1	Jun 28, 2023	Group: Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_ISSN / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
Revision 1.2	Jul 12, 2023	Group: Database references / Category: citation Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3	Jun 19, 2024	Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond / struct_ncs_dom_lim Item: _struct_ncs_dom_lim.beg_auth_asym_id / _struct_ncs_dom_lim.beg_auth_comp_id ..._struct_ncs_dom_lim.beg_auth_asym_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_auth_seq_id / _struct_ncs_dom_lim.end_auth_asym_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/cj/8cjd ftp://data.pdbj.org/pub/pdb/validation_reports/cj/8cjd	HTTPS FTP

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Related structure data

Related structure data	8cjeC 8cjfC 8cjgC C: citing same article (ref.)
Similar structure data	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

Deposited unit

A: AetF

B: AetF

hetero molecules

156 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: AetF

hetero molecules

defined by author
Evidence: gel filtration, elution volume corresponds to the monomeric protein
78.1 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: AetF

hetero molecules

defined by author
Evidence: gel filtration, elution volume corresponds to the monomeric protein
78.1 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	123.790, 123.790, 88.000
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	78
Space group name H-M	P4₃
Space group name Hall	P4cw
Symmetry operation	#1: x,y,z #2: -y,x,z+3/4 #3: y,-x,z+1/4 #4: -x,-y,z+1/2

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
d_1	ens_1	(chain "A" and (resid 1 through 17 or resid 19...
d_2	ens_1	(chain "B" and (resid 1 through 17 or resid 19...

NCS domain segments:

Ens-ID: ens_1

Dom-ID	Component-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
d_1	1	MET	MET	VAL	VAL	A	A	1 - 17	9 - 25
d_1	2	GLU	GLU	PHE	PHE	A	A	19 - 55	27 - 63
d_1	3	THR	THR	ASP	ASP	A	A	57 - 142	65 - 150
d_1	4	HIS	HIS	ASP	ASP	A	A	144 - 197	152 - 205
d_1	5	LEU	LEU	SER	SER	A	A	199 - 248	207 - 256
d_1	6	PRO	PRO	GLU	GLU	A	A	250 - 274	258 - 282
d_1	7	TYR	TYR	PRO	PRO	A	A	276 - 299	284 - 307
d_1	8	ASP	ASP	ARG	ARG	A	A	301 - 318	309 - 326
d_1	9	PHE	PHE	TYR	TYR	A	A	320 - 346	328 - 354
d_1	10	TYR	TYR	THR	THR	A	A	348 - 392	356 - 400
d_1	11	PRO	PRO	ALA	ALA	A	A	394 - 513	402 - 521
d_1	12	TRP	TRP	SER	SER	A	A	515 - 655	523 - 663
d_1	13	FAD	FAD	FAD	FAD	A	C	701
d_1	14	EDO	EDO	EDO	EDO	A	D	702
d_1	15	PEG	PEG	PEG	PEG	A	E	703
d_2	1	MET	MET	VAL	VAL	B	B	1 - 17	9 - 25
d_2	2	GLU	GLU	PHE	PHE	B	B	19 - 55	27 - 63
d_2	3	THR	THR	ASP	ASP	B	B	57 - 142	65 - 150
d_2	4	HIS	HIS	ASP	ASP	B	B	144 - 197	152 - 205
d_2	5	LEU	LEU	SER	SER	B	B	199 - 248	207 - 256
d_2	6	PRO	PRO	GLU	GLU	B	B	250 - 274	258 - 282
d_2	7	TYR	TYR	PRO	PRO	B	B	276 - 299	284 - 307
d_2	8	ASP	ASP	ARG	ARG	B	B	301 - 318	309 - 326
d_2	9	PHE	PHE	TYR	TYR	B	B	320 - 346	328 - 354
d_2	10	TYR	TYR	THR	THR	B	B	348 - 392	356 - 400
d_2	11	PRO	PRO	ALA	ALA	B	B	394 - 513	402 - 521
d_2	12	TRP	TRP	SER	SER	B	B	515 - 608	523 - 616
d_2	13	LYS	LYS	SER	SER	B	B	629 - 655	637 - 663
d_2	14	FAD	FAD	FAD	FAD	B	G	701
d_2	15	EDO	EDO	EDO	EDO	B	H	702
d_2	16	PEG	PEG	PEG	PEG	B	I	703

NCS oper: (Code: givenMatrix: (-0.0409663182138, 0.998858796239, 0.024553328655), (0.999120299695, 0.0407317851308, 0.00997739533304), (0.00896590818494, 0.0249404662364, -0.999648731122)Vector: 64. ...

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Protein , 1 types, 2 molecules AB

#1: Protein	AetF Mass: 77098.727 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aetokthonos hydrillicola Thurmond2011 (bacteria) Gene: aetF / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A861B9Z9

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Non-polymers , 6 types, 1168 molecules

#2: Chemical	ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE Mass: 785.550 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₂₇H₃₃N₉O₁₅P₂ / Feature type: SUBJECT OF INVESTIGATION / Comment: FAD*YM
#3: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₂H₆O₂
#4: Chemical	ChemComp-PEG / DI(HYDROXYETHYL)ETHER Mass: 106.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₄H₁₀O₃
#5: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#6: Chemical	ChemComp-CA / CALCIUM ION Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#7: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1159 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	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: 2.19 Å³/Da / Density % sol: 43.92 %
Crystal grow	Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 8 Details: Condition A6, Morpheus Green Screen (Molecular Dimensions), 30 mM CaCl2, 30 mM MgCl2, 0.1 M HEPES/MOPS pH 7.5, 20 % (v/v) ethylene glycol, 10 % (w/v) PEG 8000, 6 mg/mL AetF (50 mM HEPES pH 7. ...Details: Condition A6, Morpheus Green Screen (Molecular Dimensions), 30 mM CaCl2, 30 mM MgCl2, 0.1 M HEPES/MOPS pH 7.5, 20 % (v/v) ethylene glycol, 10 % (w/v) PEG 8000, 6 mg/mL AetF (50 mM HEPES pH 7.0, 100 mM NaCl, 1 mM DTT), drop with 300 nL protein + 300 nL reservoir

Crystal

Density Matthews: 2.19 Å³/Da / Density % sol: 43.92 %

Crystal grow

Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 8
Details: Condition A6, Morpheus Green Screen (Molecular Dimensions), 30 mM CaCl2, 30 mM MgCl2, 0.1 M HEPES/MOPS pH 7.5, 20 % (v/v) ethylene glycol, 10 % (w/v) PEG 8000, 6 mg/mL AetF (50 mM HEPES pH 7. ...

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P13 (MX1) / Wavelength: 0.9763 Å
Detector	Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Sep 4, 2022
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9763 Å / Relative weight: 1
Reflection	Resolution: 1.7→50 Å / Num. obs: 145683 / % possible obs: 99.7 % / Redundancy: 14.03 % / B_iso Wilson estimate: 31.4 Å² / CC_1/2: 0.999 / R_rim(I) all: 0.09 / Net I/σ(I): 16.19
Reflection shell	Resolution: 1.7→1.8 Å / Redundancy: 13.57 % / Mean I/σ(I) obs: 1.33 / Num. unique obs: 23109 / CC_1/2: 0.692 / R_rim(I) all: 1.322 / % possible all: 98.4

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Processing

Software

Name	Version	Classification
PHENIX	1.20.1_4487	refinement
MxCuBE	MXCuBE3	data collection
XDS	BUILT=20220110	data reduction
XDS	BUILT=20220110	data scaling
PHASER	2.8.3	phasing
Coot	0.9.4.1 EL	model building

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: ALPHAFOLD2 MODEL LOCAL INSTALLATION

Resolution: 1.7→46.86 Å / SU ML: 0.2304 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 19.8238
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2

	R_factor	Num. reflection	% reflection
R_free	0.1846	7215	4.96 %
R_work	0.159	138236	-
obs	0.1602	145451	99.77 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL

Displacement parameters

B_iso mean: 38.47 Å²

Refinement step

Cycle: LAST / Resolution: 1.7→46.86 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	10543	0	131	1159	11833

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.0077	11055
X-RAY DIFFRACTION	f_angle_d	0.8447	15002
X-RAY DIFFRACTION	f_chiral_restr	0.0555	1582
X-RAY DIFFRACTION	f_plane_restr	0.0076	1932
X-RAY DIFFRACTION	f_dihedral_angle_d	13.4411	4074

Refine LS restraints NCS

Type: Torsion NCS / Rms dev position: 1.25299424801 Å

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	% reflection obs (%)
1.7-1.72	0.3988	250	0.3695	4523	X-RAY DIFFRACTION	97.79
1.72-1.74	0.3442	252	0.3277	4462	X-RAY DIFFRACTION	98.43
1.74-1.76	0.3331	209	0.3076	4581	X-RAY DIFFRACTION	98.14
1.76-1.78	0.2939	225	0.2671	4565	X-RAY DIFFRACTION	100
1.78-1.81	0.281	245	0.2407	4611	X-RAY DIFFRACTION	99.75
1.81-1.83	0.2601	258	0.2154	4575	X-RAY DIFFRACTION	99.96
1.83-1.86	0.2541	260	0.2022	4566	X-RAY DIFFRACTION	99.83
1.86-1.89	0.22	244	0.1964	4573	X-RAY DIFFRACTION	99.83
1.89-1.91	0.2343	241	0.1898	4564	X-RAY DIFFRACTION	99.9
1.91-1.95	0.2065	203	0.1887	4687	X-RAY DIFFRACTION	100
1.95-1.98	0.201	254	0.1909	4569	X-RAY DIFFRACTION	99.92
1.98-2.02	0.2334	265	0.1934	4582	X-RAY DIFFRACTION	99.94
2.02-2.05	0.2601	234	0.1977	4644	X-RAY DIFFRACTION	99.98
2.05-2.1	0.2059	205	0.1736	4612	X-RAY DIFFRACTION	100
2.1-2.14	0.2097	260	0.167	4598	X-RAY DIFFRACTION	100
2.14-2.19	0.1984	245	0.1599	4579	X-RAY DIFFRACTION	100
2.19-2.25	0.1877	281	0.156	4602	X-RAY DIFFRACTION	99.98
2.25-2.31	0.1839	237	0.1561	4631	X-RAY DIFFRACTION	99.98
2.31-2.38	0.2207	231	0.1549	4610	X-RAY DIFFRACTION	100
2.38-2.45	0.213	235	0.1578	4603	X-RAY DIFFRACTION	100
2.45-2.54	0.1863	257	0.1564	4612	X-RAY DIFFRACTION	100
2.54-2.64	0.1955	208	0.1617	4634	X-RAY DIFFRACTION	100
2.64-2.76	0.1824	276	0.1582	4626	X-RAY DIFFRACTION	100
2.76-2.91	0.2027	216	0.1585	4605	X-RAY DIFFRACTION	100
2.91-3.09	0.1948	247	0.1641	4630	X-RAY DIFFRACTION	100
3.09-3.33	0.1839	240	0.1628	4637	X-RAY DIFFRACTION	100
3.33-3.66	0.1666	221	0.1461	4664	X-RAY DIFFRACTION	99.98
3.66-4.19	0.1579	254	0.1277	4644	X-RAY DIFFRACTION	100
4.19-5.28	0.1367	240	0.1192	4678	X-RAY DIFFRACTION	100
5.28-46.86	0.1553	222	0.1697	4769	X-RAY DIFFRACTION	99.72

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	3.85340525776	1.02369920846	-1.27650351817	2.2637551449	0.192877682501	1.61306573579	0.00517814011039	-0.116268288585	-0.138792032737	0.234349299655	-0.0890657262374	-0.0336512153868	0.151097044292	0.0115256746435	0.0836904404017	0.267605295988	0.0269978748744	-0.0349578344254	0.248571182255	0.0049632828956	0.17727003477	48.8995240176	-43.0620304083	14.0881973313
2	6.56407672879	3.80049434201	1.31554731907	3.38533516961	0.701029069204	2.8229550401	0.102671024525	-0.407157279008	-0.254125963131	0.321472466779	-0.271675510392	0.0708111261623	0.374756895002	-0.323200379933	0.180751278355	0.318155662686	0.0153338630794	0.063880602085	0.21397062247	-0.0623543226079	0.239750090505	41.7538768376	-52.1728691348	14.3252673928
3	7.56724970633	0.954537081402	-2.73196030921	0.0912463564771	-0.306456340928	1.18322722557	0.0607051377316	0.104199253054	-0.0848262020725	0.0857675163341	-0.142462306919	-0.0712231476889	0.137321742484	-0.0784670730269	0.0924616212353	0.338313978702	0.00297480985866	0.0194054431578	0.300016164422	-0.0292420573349	0.340669523501	50.6405180398	-54.1927947644	2.67822840017
4	0.846067192428	-0.0978713382416	-0.197825071243	0.658111601847	0.230510351919	0.646621980202	0.00146498008871	0.0487685447914	0.0457056958536	0.00447111618117	-0.0490720523055	-0.00355362450373	-0.0103903167718	-0.0218579350673	0.0501529702398	0.244810085944	-0.00580609347192	-0.0132571837814	0.266032178543	0.0136080841564	0.250134580097	59.8803794745	-35.9196345347	-9.5931803782
5	2.90301961826	4.88534484159	-1.1894785454	8.85748216233	-1.33244945037	1.86194339516	-0.109803350274	-0.000803996044862	-0.0486490622572	-0.225703483896	-0.0201122357417	0.433979249344	0.180991095496	-0.20955647886	0.101002200358	0.202403827195	0.00783421471385	0.00246715863418	0.24581817549	-0.0821529245255	0.279384626243	32.9643564653	-45.3380043096	0.336186562844
6	1.28668856042	0.232221596713	-0.0506809909563	1.22668600318	0.395787829924	1.31027073552	0.0643281515709	-0.0404819595087	0.110430293108	0.0416248698236	-0.139722458819	0.216433374326	-0.0938025665419	-0.154797203207	0.0814133106369	0.21807201502	0.0231066328553	0.00396415159879	0.265551388001	-0.0538602164323	0.296233569608	36.5517725569	-29.2943800429	6.72778541756
7	0.926402728694	0.0143910935283	-1.88680375645	1.04302520549	0.321814804283	5.66605604257	0.0437379453733	-0.0592030873073	0.194421218172	-0.0682346172956	-0.0343444836523	-0.0243218986613	-0.421432700664	-0.0167059185961	-0.0381449016847	0.250168018374	-0.022052219692	-0.0436658651238	0.226991459389	-0.00649688383533	0.347768236294	56.5031920317	-17.3164347735	-1.19625862244
8	0.412463143026	0.271225887061	0.192931117545	0.461152010814	0.892774794022	5.18570001425	0.0117443869686	0.0304793080911	0.0159807547085	-0.104382652801	0.0283572461421	-0.246563060835	0.321100726174	0.605985586964	-0.0463475042635	0.228015696415	0.0270055334019	0.0311711957217	0.394227684618	0.0413795044349	0.345792329257	78.2931442817	-41.5230939762	-10.7418355792
9	4.52974431729	-4.491381419	-5.1249940286	7.24125929966	6.22200502712	6.13296866245	0.486145846941	-0.0488492302258	0.864597671348	-0.452963933032	0.160160159769	-0.750878002014	-0.645147599388	0.174259096869	-0.86144173683	0.398831604889	-0.0274234283283	0.0169513104623	0.326055913722	0.0684552325305	0.422642028501	64.3170785728	-13.9261055461	-9.83904382022
10	4.37005969963	2.28740058341	1.16273913577	7.081171857	1.4583464119	2.67298859705	-0.0852307344849	0.28455806327	0.986183947277	-0.474724383793	-0.0405287536495	0.475127149711	-0.571678126925	-0.136045066307	0.123406449424	0.374716430021	0.106138848845	0.017552234572	0.2981202597	-0.0373110999271	0.470659658337	38.8406101478	-10.1233211449	2.63509937076
11	1.44103600629	0.545574718642	-0.391782620026	2.16397907139	0.382295334403	1.32524832553	-0.00497946717539	0.218867350684	-0.0660663913084	-0.153969607105	-0.0837146510345	0.159431703761	-0.0311121962953	-0.409085162992	0.0940029089886	0.272248339929	0.0299083254035	-0.0187497527672	0.404783706818	-0.0393815363282	0.216807085261	16.9233910971	-14.4789331304	-57.2502430411
12	0.315502050715	-0.216334226025	-0.345713828749	0.887917652838	0.569293294722	0.834014959341	0.0370905215197	0.0534861501796	-0.0155868332275	0.0484114509712	-0.0434622312623	0.0102007242131	-0.0196869150176	-0.0808317035273	0.00668299853202	0.274959842295	-0.0133517314086	-0.0178250355666	0.261774610106	-0.000891487704736	0.224509571304	22.8232996873	-4.20637014034	-35.502761579
13	1.25308054643	-0.217163360004	-0.313055323066	1.17567891157	0.50213730966	1.36981659235	-0.0398667336612	-0.0186647861155	-0.100456175582	0.039888776154	0.0140038201528	-0.162270326296	0.113137492583	-0.00296019337747	0.0228890666434	0.238641014406	0.0103739527729	-0.00116647242802	0.230819087832	-0.023718832718	0.257082366929	35.152843954	-20.2884937738	-47.5428118463
14	0.537736915307	-0.191048923284	-0.538316528065	1.49704887215	0.183508268727	2.77728428395	0.19959374229	-0.0219299327499	0.207914317957	-0.0887134672036	-0.0104669631618	-0.127741789616	-0.501343817857	-0.0614703687896	-0.181126198697	0.404093721634	-0.0471809742023	0.0254809838132	0.219642497091	-0.0260050121546	0.296524688496	25.4695589293	13.8634654452	-32.3031064346
15	1.93378428494	-0.0487388553471	-0.720179220958	1.60396790944	0.929181001716	1.38265585243	0.0333726165735	-0.101244656591	0.0772130185682	-0.00229922857595	0.423154784269	-0.872283989122	-0.0217114944129	0.476969191198	-0.509565937545	0.296588265532	0.0118019942991	-0.0816175503492	0.397422514692	-0.0747621516074	0.47584295498	51.1769602046	-8.8698184989	-38.9836134162

Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

ID	Refine TLS-ID	Selection details	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	chain 'A' and (resid 1 through 75 )	A	A	1 - 75	1 - 75
2	2	chain 'A' and (resid 76 through 113 )	A	A	76 - 113	76 - 113
3	3	chain 'A' and (resid 114 through 148 )	A	A	114 - 148	114 - 148
4	4	chain 'A' and (resid 149 through 334 )	A	A	149 - 334	149 - 334
5	5	chain 'A' and (resid 335 through 375 )	A	A	335 - 375	335 - 375
6	6	chain 'A' and (resid 376 through 479 )	A	A	376 - 479	376 - 479
7	7	chain 'A' and (resid 480 through 530 )	A	A	480 - 530	480 - 530
8	8	chain 'A' and (resid 531 through 568 )	A	A	531 - 568	531 - 568
9	9	chain 'A' and (resid 569 through 601 )	A	A	569 - 601	569 - 601
10	10	chain 'A' and (resid 602 through 655 )	A	A	602 - 655	602 - 635
11	11	chain 'B' and (resid 1 through 113 )	B	E	1 - 113	1 - 113
12	12	chain 'B' and (resid 114 through 347 )	B	E	114 - 347	114 - 347
13	13	chain 'B' and (resid 348 through 516 )	B	E	348 - 516	348 - 516
14	14	chain 'B' and (resid 517 through 568 )	B	E	517 - 568	517 - 568
15	15	chain 'B' and (resid 569 through 655 )	B	E	569 - 655	569 - 637

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