PDB-1yq9: Structure of the unready oxidized form of [NiFe] hydrogenase

ID or keywords:

Entry

Database: PDB / ID: 1yq9

Title

Structure of the unready oxidized form of [NiFe] hydrogenase

Components

(Periplasmic [NiFe] hydrogenase ...) x 2

Keywords

OXIDOREDUCTASE

Function / homology

Function and homology information

cytochrome-c3 hydrogenase / cytochrome-c3 hydrogenase activity / ferredoxin hydrogenase complex / [Ni-Fe] hydrogenase complex / ferredoxin hydrogenase activity / anaerobic respiration / 3 iron, 4 sulfur cluster binding / nickel cation binding / 4 iron, 4 sulfur cluster binding / periplasmic space ...
Similarity search - Function

Biological species

Desulfovibrio gigas (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.35 Å

Authors

Volbeda, A. / Martin, L. / Cavazza, C. / Matho, M. / Faber, B.W. / Roseboom, W. / Albracht, S.P. / Garcin, E. / Rousset, M. / Fontecilla-Camps, J.C.

Citation

Journal: J.Biol.Inorg.Chem. / Year: 2005
Title: Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases.
Authors: Volbeda, A. / Martin, L. / Cavazza, C. / Matho, M. / Faber, B.W. / Roseboom, W. / Albracht, S.P. / Garcin, E. / Rousset, M. / Fontecilla-Camps, J.C.

History

Deposition	Feb 1, 2005	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Apr 19, 2005	Provider: repository / Type: Initial release
Revision 1.1	Apr 30, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Refinement description / Version format compliance
Revision 1.3	Oct 11, 2017	Group: Refinement description / Category: software
Revision 1.4	Aug 23, 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_ref_seq_dif / 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_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_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_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_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_asym_id / _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_asym_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_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ref_seq_dif.details / _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

Summary document	1yq9_validation.pdf.gz	531.9 KB	Display	wwPDB validaton report
Full document	1yq9_full_validation.pdf.gz	558.5 KB	Display
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Data in CIF	1yq9_validation.cif.gz	87.1 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/yq/1yq9 ftp://data.pdbj.org/pub/pdb/validation_reports/yq/1yq9	HTTPS FTP

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Related structure data

Related structure data	1yqwC 1yrqC 2frvS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	1ubm-d 4ucx-1 1yqw-1 1yqw-2 3cur-2 4uqp-2 4ucw-1 4ue2-3 1wuk-d 4ueq-2 4ud6-1 4ud2-2 4urh-1 1wul-d 4uew-3 1yrq-5 1ubt-d 1e3d-1 1ubo-d 4u9h-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

Related structure data

1yqwC

1yrqC

2frvS

S: Starting model for refinement

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	#111 - Mar 2009 Hydrogenase similarity (18) #144 - Dec 2011 Complex I similarity (3) #154 - Oct 2012 Citric Acid Cycle similarity (1) #241 - Jan 2020 Twenty Years of Molecules similarity (1)

Deposited unit

A: Periplasmic [NiFe] hydrogenase small subunit

H: Periplasmic [NiFe] hydrogenase large subunit

B: Periplasmic [NiFe] hydrogenase small subunit

I: Periplasmic [NiFe] hydrogenase large subunit

hetero molecules

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

1

A: Periplasmic [NiFe] hydrogenase small subunit

H: Periplasmic [NiFe] hydrogenase large subunit

hetero molecules

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

2

B: Periplasmic [NiFe] hydrogenase small subunit

I: Periplasmic [NiFe] hydrogenase large subunit

hetero molecules

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

Unit cell

Length a, b, c (Å)	62.750, 93.440, 69.030
Angle α, β, γ (deg.)	89.33, 102.41, 90.95
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Refine code: 1

Dom-ID	Component-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	1	ALA	ALA	SER	SER	A	A	15 - 23	15 - 23
2	1	1	ALA	ALA	SER	SER	B	C	15 - 23	15 - 23
3	2	1	GLU	GLU	GLY	GLY	A	A	73 - 75	73 - 75
4	2	1	GLU	GLU	GLY	GLY	B	C	73 - 75	73 - 75
5	3	1	ILE	ILE	ALA	ALA	A	A	109 - 113	109 - 113
6	3	1	ILE	ILE	ALA	ALA	B	C	109 - 113	109 - 113
7	4	1	GLY	GLY	GLN	GLN	A	A	116 - 119	116 - 119
8	4	1	GLY	GLY	GLN	GLN	B	C	116 - 119	116 - 119
9	5	1	GLY	GLY	PRO	PRO	A	A	147 - 150	147 - 150
10	5	1	GLY	GLY	PRO	PRO	B	C	147 - 150	147 - 150
11	6	1	VAL	VAL	VAL	VAL	A	A	184	184
12	6	1	VAL	VAL	VAL	VAL	B	C	184	184
13	7	1	LYS	LYS	GLY	GLY	A	A	220 - 221	220 - 221
14	7	1	LYS	LYS	GLY	GLY	B	C	220 - 221	220 - 221
15	8	1	THR	THR	THR	THR	A	A	224	224
16	8	1	THR	THR	THR	THR	B	C	224	224
17	9	1	ASN	ASN	PRO	PRO	A	A	226 - 229	226 - 229
18	9	1	ASN	ASN	PRO	PRO	B	C	226 - 229	226 - 229
19	10	1	PHE	PHE	PHE	PHE	A	A	233	233
20	10	1	PHE	PHE	PHE	PHE	B	C	233	233
21	11	1	TRP	TRP	VAL	VAL	A	A	238 - 240	238 - 240
22	11	1	TRP	TRP	VAL	VAL	B	C	238 - 240	238 - 240
23	12	1	PRO	PRO	SER	SER	A	A	245 - 250	245 - 250
24	12	1	PRO	PRO	SER	SER	B	C	245 - 250	245 - 250
25	13	1	PHE	PHE	TRP	TRP	A	A	254 - 255	254 - 255
26	13	1	PHE	PHE	TRP	TRP	B	C	254 - 255	254 - 255
27	14	1	F3S	F3S	SF4	SF4	A	F - G	266 - 267
28	14	1	F3S	F3S	SF4	SF4	B	U - V	266 - 267
1	1	2	ILE	ILE	GLY	GLY	H	B	17 - 19	17 - 19
2	1	2	ILE	ILE	GLY	GLY	I	D	17 - 19	17 - 19
3	2	2	ARG	ARG	ARG	ARG	H	B	43	43
4	2	2	ARG	ARG	ARG	ARG	I	D	43	43
5	3	2	GLU	GLU	GLU	GLU	H	B	46	46
6	3	2	GLU	GLU	GLU	GLU	I	D	46	46
7	4	2	THR	THR	ALA	ALA	H	B	61 - 73	61 - 73
8	4	2	THR	THR	ALA	ALA	I	D	61 - 73	61 - 73
9	5	2	ALA	ALA	ALA	ALA	H	B	75	75
10	5	2	ALA	ALA	ALA	ALA	I	D	75	75
11	6	2	MET	MET	MET	MET	H	B	100	100
12	6	2	MET	MET	MET	MET	I	D	100	100
13	7	2	GLN	GLN	GLN	GLN	H	B	103	103
14	7	2	GLN	GLN	GLN	GLN	I	D	103	103
15	8	2	ASP	ASP	HIS	HIS	H	B	107 - 108	107 - 108
16	8	2	ASP	ASP	HIS	HIS	I	D	107 - 108	107 - 108
17	9	2	LEU	LEU	LEU	LEU	H	B	115	115
18	9	2	LEU	LEU	LEU	LEU	I	D	115	115
19	10	2	LYS	LYS	LYS	LYS	H	B	216	216
20	10	2	LYS	LYS	LYS	LYS	I	D	216	216
21	11	2	HIS	HIS	HIS	HIS	H	B	219	219
22	11	2	HIS	HIS	HIS	HIS	I	D	219	219
23	12	2	GLN	GLN	GLN	GLN	H	B	221	221
24	12	2	GLN	GLN	GLN	GLN	I	D	221	221
25	13	2	GLU	GLU	GLU	GLU	H	B	321	321
26	13	2	GLU	GLU	GLU	GLU	I	D	321	321
27	14	2	TYR	TYR	TYR	TYR	H	B	328	328
28	14	2	TYR	TYR	TYR	TYR	I	D	328	328
29	15	2	THR	THR	THR	THR	H	B	341	341
30	15	2	THR	THR	THR	THR	I	D	341	341
31	16	2	MET	MET	LYS	LYS	H	B	357 - 358	357 - 358
32	16	2	MET	MET	LYS	LYS	I	D	357 - 358	357 - 358
33	17	2	VAL	VAL	VAL	VAL	H	B	369	369
34	17	2	VAL	VAL	VAL	VAL	I	D	369	369
35	18	2	VAL	VAL	HIS	HIS	H	B	459 - 468	459 - 468
36	18	2	VAL	VAL	HIS	HIS	I	D	459 - 468	459 - 468
37	19	2	PHE	PHE	THR	THR	H	B	480 - 487	480 - 487
38	19	2	PHE	PHE	THR	THR	I	D	480 - 487	480 - 487
39	20	2	ASN	ASN	LEU	LEU	H	B	489 - 490	489 - 490
40	20	2	ASN	ASN	LEU	LEU	I	D	489 - 490	489 - 490
41	21	2	TYR	TYR	HIS	HIS	H	B	527 - 536	527 - 536
42	21	2	TYR	TYR	HIS	HIS	I	D	527 - 536	527 - 536
43	22	2	FCO	FCO	MG	MG	H	O - N	537 - 540
44	22	2	FCO	FCO	MG	MG	I	AA - Z	537 - 540

NCS ensembles :

ID
1
2

Details

The biological assembly is a heterodimer, two copies of which are in the asymmetric unit

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Periplasmic [NiFe] hydrogenase ... , 2 types, 4 molecules ABHI

#1: Protein	Periplasmic [NiFe] hydrogenase small subunit / NiFe hydrogenlyase small chain Mass: 28351.396 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Desulfovibrio gigas (bacteria) / Cellular location: periplasm / Strain: wild type / References: UniProt: P12943, cytochrome-c3 hydrogenase
#2: Protein	Periplasmic [NiFe] hydrogenase large subunit / NiFe hydrogenlyase large chain Mass: 59657.992 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Desulfovibrio gigas (bacteria) / Cellular location: periplasm / Strain: wild type / References: UniProt: P12944, cytochrome-c3 hydrogenase

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Non-polymers , 9 types, 540 molecules

#3: Chemical	ChemComp-SF4 / IRON/SULFUR CLUSTER Mass: 351.640 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe₄S₄
#4: Chemical	ChemComp-F3S / FE3-S4 CLUSTER Mass: 295.795 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe₃S₄
#5: Chemical	ChemComp-H2S / HYDROSULFURIC ACID / HYDROGEN SULFIDE Mass: 34.081 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: H₂S
#6: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C₃H₈O₃
#7: Chemical	ChemComp-NI / NICKEL (II) ION Mass: 58.693 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ni
#8: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#9: Chemical	ChemComp-FCO / CARBONMONOXIDE-(DICYANO) IRON Mass: 135.890 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₃FeN₂O
#10: Chemical	ChemComp-PER / PEROXIDE ION Mass: 31.999 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: O₂
#11: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 515 / 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: 2.3 Å³/Da / Density % sol: 45.7 %
Crystal grow	Temperature: 293 K / pH: 6.3 Details: PEG8000, sodium chloride, N,N-dimethyl dodecylamine N-oxide, glycerol, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 6.30

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.98
Detector	Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 26, 1996
Radiation	Monochromator: SI(111) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.98 Å / Relative weight: 1
Reflection	Resolution: 2.35→19.8 Å / Num. obs: 58639 / % possible obs: 86.2 % / Observed criterion σ(I): 0 / Redundancy: 1.8 % / B_iso Wilson estimate: 37.6 Å² / R_sym value: 0.069 / Net I/σ(I): 8.4
Reflection shell	Resolution: 2.35→2.45 Å / % possible all: 78.2

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Processing

Software

Name	Version	Classification
REFMAC		refinement
PDB_EXTRACT	1.501	data extraction
ProDC		data collection
XDS		data scaling
AMoRE		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2FRV

2frv

Resolution: 2.35→13 Å / Cor.coef. F_o:F_c: 0.968 / Cor.coef. F_o:F_c free: 0.941 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.217 / Stereochemistry target values: ENGH & HUBER / Details: USE OF TLS PARAMETERS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.183	2962	5.1 %	RANDOM
R_work	0.132	-	-	-
obs	0.135	58485	92.2 %	-
all	-	61447	-	-

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 mean: 14.54 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	2.37 Å²	-1.11 Å²	0.02 Å²
2-	-	0.13 Å²	0.9 Å²
3-	-	-	-2.55 Å²

Refinement step

Cycle: LAST / Resolution: 2.35→13 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	12237	0	114	515	12866

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.009	0.022	12732
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.088	1.944	17258
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.397	5	1577
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	33.337	24.079	554
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	17.933	15	2013
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	19.189	15	63
X-RAY DIFFRACTION	r_chiral_restr	0.082	0.2	1877
X-RAY DIFFRACTION	r_gen_planes_refined	0.004	0.02	9663
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.233	0.2	5868
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.324	0.2	8549
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.158	0.2	659
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	0.158	0.2	29
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.282	0.2	12
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	1.157	1.5	8071
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	1.473	2	12638
X-RAY DIFFRACTION	r_scbond_it	1.969	2	5333
X-RAY DIFFRACTION	r_scangle_it	2.52	3	4566
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	A	326	tight positional	0.06	0.2
2	H	505	tight positional	0.09	0.2
1	A	326	tight thermal	0.34	1
2	H	505	tight thermal	0.41	1

LS refinement shell

Resolution: 2.35→2.45 Å / Total num. of bins used: 12

	R_factor	Num. reflection	% reflection
R_free	0.203	321	-
R_work	0.134	5612	-
obs	-	-	78.23 %

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	0.6345	-0.111	0.3724	0.7022	-0.3518	1.7333	0.0486	-0.0474	-0.1371	-0.0709	0.0239	0.117	0.1584	-0.0708	-0.0725	0.0579	-0.0057	-0.0357	0.0582	-0.0122	0.1274	19.026	76.825	48.693
2	0.4494	-0.1431	0.1339	0.6852	-0.2597	1.3222	-0.0127	-0.0268	0.0586	0.0635	-0.0027	0.01	-0.3329	0.0871	0.0155	0.1245	-0.0206	-0.0066	0.0785	-0.0229	0.1012	25.725	99.597	51.667
3	1.0486	0.0221	-0.0724	1.987	-0.7147	1.336	-0.1617	-0.1416	-0.1132	0.3973	0.213	0.2827	-0.1676	-0.1965	-0.0513	0.0931	0.1033	0.0589	0.1469	0.0085	0.1372	-13.332	59.439	25.144
4	1.033	-0.0973	-0.0914	1.7898	-0.6404	1.2001	-0.1557	-0.0943	-0.3305	0.1213	0.0586	-0.1602	0.169	0.146	0.0971	0.0751	0.0692	0.0413	0.1153	-0.0044	0.2326	2.909	42.074	21.917

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	4 - 264
2	X-RAY DIFFRACTION	1	A	265 - 267
3	X-RAY DIFFRACTION	1	A	264
4	X-RAY DIFFRACTION	1	A	1268 - 1273
5	X-RAY DIFFRACTION	2	H	7 - 536
6	X-RAY DIFFRACTION	2	H	537 - 540
7	X-RAY DIFFRACTION	2	H	1541 - 1544
8	X-RAY DIFFRACTION	3	B	5 - 264
9	X-RAY DIFFRACTION	3	B	265 - 267
10	X-RAY DIFFRACTION	3	B	2268
11	X-RAY DIFFRACTION	4	I	7 - 536
12	X-RAY DIFFRACTION	4	I	537 - 540
13	X-RAY DIFFRACTION	4	I	2541

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Periplasmic [NiFe] hydrogenase ... , 2 types, 4 molecules ABHI

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Non-polymers , 9 types, 540 molecules

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Periplasmic [NiFe] hydrogenase ... , 2 types, 4 molecules ABHI

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