SAXSdb — 2ojw

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Glutamine synthetase

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain A； UniProt 4–364 Chain B； UniProt 4–364 Chain C； UniProt 4–364 Chain D； UniProt 4–364 Chain E； UniProt 4–364	Fragment：Residues 4-364	MN MANGANESE (II) ION × 40 PO4 PHOSPHATE ION × 10 CL CHLORIDE ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 10 GOL GLYCEROL × 12	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；277 K；10% Isopropanol, 200 mM NaCl, 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K, pH 7.50	Resolution 2.05 Å R-free 0.212

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 2OJW	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2QC8 Crystal structure of human glutamine synthetase in complex with ADP and methionine sulfoximine phosphate Deposited 2007-06-19	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 5–365（361 aa） Chain B 5–365（361 aa） Chain C 5–365（361 aa） Chain D 5–365（361 aa） Chain E 5–365（361 aa） Chain F 5–365（361 aa） Chain G 5–365（361 aa） Chain H 5–365（361 aa） Chain I 5–365（361 aa） Chain J 5–365（361 aa）	Not recorded	MN MANGANESE (II) ION × 30 CL CHLORIDE ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 10 P3S L-METHIONINE-S-SULFOXIMINE PHOSPHATE × 10	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；298 K；1.1M Sodium malonate, 0.5% Jeffamine ED-2001, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K, pH 7.00	Resolution 2.60 Å R-free 0.217
7EVT Crystal structure of the N-terminal degron-truncated human glutamine synthetase Deposited 2021-05-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 23–373（351 aa） Chain B 23–373（351 aa） Chain C 23–373（351 aa） Chain D 23–373（351 aa） Chain E 23–373（351 aa） Chain F 23–373（351 aa） Chain G 23–373（351 aa） Chain H 23–373（351 aa） Chain I 23–373（351 aa） Chain J 23–373（351 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.1；293.15 K；0.07 M sodium citrate (pH 5.1), 10% glycerol and 5.6% PEG4000	Resolution 2.95 Å R-free 0.250
8DNU Human Brain Glutamine Synthetase Deposited 2022-07-11	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 1–373（373 aa） Chain B 1–373（373 aa） Chain C 1–373（373 aa） Chain D 1–373（373 aa） Chain E 1–373（373 aa） Chain F 1–373（373 aa） Chain G 1–373（373 aa） Chain H 1–373（373 aa） Chain I 1–373（373 aa） Chain J 1–373（373 aa）	Not recorded	MN MANGANESE (II) ION × 10	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å
9NLR Crystal structure of human glutamine synthetase in complex with ADP and phosphate Deposited 2025-03-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 1–373（373 aa） Chain B 1–373（373 aa） Chain C 1–373（373 aa） Chain D 1–373（373 aa） Chain E 1–373（373 aa） Chain F 1–373（373 aa） Chain G 1–373（373 aa） Chain H 1–373（373 aa） Chain I 1–373（373 aa） Chain J 1–373（373 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 10 MN MANGANESE (II) ION × 30 PO4 PHOSPHATE ION × 10 NA SODIUM ION × 11	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；291 K；30% (v/v) 2-methyl-2,4-pentanediol, 100 mM Tris pH 8.5, 500 mM NaCl, 8% (w/v) PEG 8000	Resolution 2.30 Å R-free 0.215
9NLR Crystal structure of human glutamine synthetase in complex with ADP and phosphate Deposited 2025-03-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain K 1–373（373 aa） Chain L 1–373（373 aa） Chain M 1–373（373 aa） Chain N 1–373（373 aa） Chain O 1–373（373 aa） Chain P 1–373（373 aa） Chain Q 1–373（373 aa） Chain R 1–373（373 aa） Chain S 1–373（373 aa） Chain T 1–373（373 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 10 MN MANGANESE (II) ION × 30 PO4 PHOSPHATE ION × 10 NA SODIUM ION × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；291 K；30% (v/v) 2-methyl-2,4-pentanediol, 100 mM Tris pH 8.5, 500 mM NaCl, 8% (w/v) PEG 8000	Resolution 2.30 Å R-free 0.215
9NM5 Crystal structure of human glutamine synthetase in complex with ADP and phosphinothricin phosphate Deposited 2025-03-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 1–373（373 aa） Chain B 1–373（373 aa） Chain C 1–373（373 aa） Chain D 1–373（373 aa） Chain E 1–373（373 aa） Chain F 1–373（373 aa） Chain G 1–373（373 aa） Chain H 1–373（373 aa） Chain I 1–373（373 aa） Chain J 1–373（373 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 10 MN MANGANESE (II) ION × 30 P3P (2S)-2-AMINO-4-[METHYL(PHOSPHONOOXY)PHOSPHORYL]BUTANOIC ACID × 10 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 21 CL CHLORIDE ION × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；291 K；35% (v/v) 2-methyl-2,4-pentanediol, 100 mM sodium acetate/acetic acid pH 4.5	Resolution 1.85 Å R-free 0.159
9NR3 CRBN-DDB1 in complex with GLUL-cN Deposited 2025-03-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 368–373（6 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；8% v/v TacsimateTM pH 6.0, 20% w/v Polyethylene glycol 3,350	Resolution 2.93 Å R-free 0.278
9OTM Human glutamine synthetase filament under turnover conditions Deposited 2025-05-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain A 1–373（373 aa） Chain B 1–373（373 aa） Chain C 1–373（373 aa） Chain D 1–373（373 aa） Chain E 1–373（373 aa） Chain F 1–373（373 aa） Chain G 1–373（373 aa） Chain H 1–373（373 aa） Chain I 1–373（373 aa） Chain J 1–373（373 aa） Chain K 1–373（373 aa） Chain L 1–373（373 aa） Chain M 1–373（373 aa） Chain N 1–373（373 aa） Chain O 1–373（373 aa） Chain P 1–373（373 aa） Chain Q 1–373（373 aa） Chain R 1–373（373 aa） Chain S 1–373（373 aa） Chain T 1–373（373 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 20 MG MAGNESIUM ION × 40 GLN GLUTAMINE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.19 Å
9OTN Human glutamine synthetase filament bound to ATP Deposited 2025-05-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain A 1–373（373 aa） Chain B 1–373（373 aa） Chain C 1–373（373 aa） Chain D 1–373（373 aa） Chain E 1–373（373 aa） Chain F 1–373（373 aa） Chain G 1–373（373 aa） Chain H 1–373（373 aa） Chain I 1–373（373 aa） Chain J 1–373（373 aa） Chain K 1–373（373 aa） Chain L 1–373（373 aa） Chain M 1–373（373 aa） Chain N 1–373（373 aa） Chain O 1–373（373 aa） Chain P 1–373（373 aa） Chain Q 1–373（373 aa） Chain R 1–373（373 aa） Chain S 1–373（373 aa） Chain T 1–373（373 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 20 MG MAGNESIUM ION × 40	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.11 Å
9OTO Human glutamine synthetase decamer under turnover conditions Deposited 2025-05-27	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 1–373（373 aa） Chain B 1–373（373 aa） Chain C 1–373（373 aa） Chain D 1–373（373 aa） Chain E 1–373（373 aa） Chain F 1–373（373 aa） Chain G 1–373（373 aa） Chain H 1–373（373 aa） Chain I 1–373（373 aa） Chain J 1–373（373 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 10 MG MAGNESIUM ION × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.03 Å
9OTP Human glutamine synthetase R298A decamer under turnover conditions Deposited 2025-05-27	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 1–373（373 aa） Chain B 1–373（373 aa） Chain C 1–373（373 aa） Chain D 1–373（373 aa） Chain E 1–373（373 aa） Chain F 1–373（373 aa） Chain G 1–373（373 aa） Chain H 1–373（373 aa） Chain I 1–373（373 aa） Chain J 1–373（373 aa）	Mutation：R298A Mutation：R298A Mutation：R298A Mutation：R298A Mutation：R298A Mutation：R298A Mutation：R298A Mutation：R298A Mutation：R298A Mutation：R298A	ADP ADENOSINE-5'-DIPHOSPHATE × 10 MG MAGNESIUM ION × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 1.95 Å
9OTQ Human glutamine synthetase filament apo Deposited 2025-05-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: 20-meric	Chain L 1–373（373 aa） Chain M 1–373（373 aa） Chain N 1–373（373 aa） Chain O 1–373（373 aa） Chain P 1–373（373 aa） Chain Q 1–373（373 aa） Chain R 1–373（373 aa） Chain S 1–373（373 aa） Chain T 1–373（373 aa） Chain U 1–373（373 aa） Chain V 1–373（373 aa） Chain W 1–373（373 aa） Chain X 1–373（373 aa） Chain Y 1–373（373 aa） Chain Z 1–373（373 aa） Chain a 1–373（373 aa） Chain b 1–373（373 aa） Chain c 1–373（373 aa） Chain d 1–373（373 aa） Chain e 1–373（373 aa）	Not recorded	MG MAGNESIUM ION × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.27 Å

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GLNA_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 24–384； UniProt 4–364 Author chain B； PDBConstruct 24–384； UniProt 4–364 Author chain C； PDBConstruct 24–384； UniProt 4–364 Author chain D； PDBConstruct 24–384； UniProt 4–364 Author chain E； PDBConstruct 24–384； UniProt 4–364

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2ojw
Deposition date deposition_date	2007-01-15
Structure title title	Crystal structure of human glutamine synthetase in complex with ADP and phosphate
Keywords keywords	AMINO-ACID BIOSYNTHESIS, LIGASE, SYNTHETASE, STRUCTURAL GENOMICS, Structural Genomics Consortium, SGC; LIGASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	39.99 Å
Radius of gyration Rg (electron density) rg_electron	39.38 Å
Forward intensity I(0) i0	709028000.00
Molecular weight molecular_weight	207310.0 kDa
Excluded volume excluded_volume	254010 Å³
Envelope volume envelope_volume	316190 Å³
Hydration-shell volume shell_volume	64001 Å³
Envelope diameter envelope_diameter	126.3 Å
Shell Rg shell_rg	47.25 Å
Envelope Rg envelope_rg	39.30 Å
Shape Rg shape_rg	39.38 Å
Total Rg total_rg	39.75 Å
Total atoms total_atoms	14471
Residues n_residues	1802
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	125.9 Å
Rg (real space) rg_real	39.89 Å
Rg uncertainty (real space) rg_real_error	0.78 Å
I(0) (real space) i0_real	7.0900e+08
I(0) uncertainty (real space) i0_real_error	1.1140e+07
Rg (reciprocal space) rg_reciprocal	39.99 Å
I(0) (reciprocal space) i0_reciprocal	709100000.0000
Solution quality estimate total_estimate	0.9029
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	50.4 Å
Skewness Skewness skewness	0.171
Kurtosis Kurtosis kurtosis	-0.652
Angular range angular_range	— – 0.2000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	250600000.0000
Real-space data points n_real_points	41
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.878

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	Glutamine synthetase
Molecular weight formula_weight	43364.8 kDa
EC 编号 ec_number	6.3.1.2
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E
Atom count atom_count	15882

MHHHHHHSSGVDLGTENLYFQSMASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCLLNETG

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	MANGANESE (II) ION
Molecular weight formula_weight	54.9 kDa
Source method src_method	syn
Copy count entity_count	20

Entity 3 Entity 3 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 4 Entity 4 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 5 Entity 5 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 6 Entity 6 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1390

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7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id	2ojwA01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	70 — Glutamine synthetase, N-terminal domain

Domain ID domain_id	2ojwA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	590 — Creatine Kinase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Glutamine synthetase/guanido kinase, catalytic domain

Domain ID domain_id	2ojwB01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	70 — Glutamine synthetase, N-terminal domain

Domain ID domain_id	2ojwB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	590 — Creatine Kinase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Glutamine synthetase/guanido kinase, catalytic domain

Domain ID domain_id	2ojwC01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	70 — Glutamine synthetase, N-terminal domain

Domain ID domain_id	2ojwC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	590 — Creatine Kinase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Glutamine synthetase/guanido kinase, catalytic domain

Domain ID domain_id	2ojwD01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	70 — Glutamine synthetase, N-terminal domain

Domain ID domain_id	2ojwD02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	590 — Creatine Kinase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Glutamine synthetase/guanido kinase, catalytic domain

Domain ID domain_id	2ojwE01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	70 — Glutamine synthetase, N-terminal domain

Domain ID domain_id	2ojwE02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	590 — Creatine Kinase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Glutamine synthetase/guanido kinase, catalytic domain

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8. Citations (1)

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Unit-cell length a length_a	177.600 Å
Unit-cell length b length_b	122.600 Å
Unit-cell length c length_c	126.600 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	130.60 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	20

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.050 Å
Low-resolution limit resolution_low	39.250 Å
R factor r_factor	0.1620
R_work r_work	0.1590
R_free r_free	0.2120

fit	/app/data/saxs_computation/oj/2ojw/2ojw.fit
pddf	/app/data/pr_computation/oj/2ojw/2ojw.pr.out
profile	/app/data/saxs_computation/oj/2ojw/2ojw.dat

Crystal structure of human glutamine synthetase in complex with ADP and phosphate