Nitric oxide stimulates guanylate cyclase / negative regulation of hepatic stellate cell contraction / synaptic signaling by nitric oxide / negative regulation of iron ion transmembrane transport / ROS and RNS production in phagocytes / azurophil granule / negative regulation of vasoconstriction / retrograde trans-synaptic signaling by nitric oxide / positive regulation of sodium ion transmembrane transport / response to nitric oxide ...Nitric oxide stimulates guanylate cyclase / negative regulation of hepatic stellate cell contraction / synaptic signaling by nitric oxide / negative regulation of iron ion transmembrane transport / ROS and RNS production in phagocytes / azurophil granule / negative regulation of vasoconstriction / retrograde trans-synaptic signaling by nitric oxide / positive regulation of sodium ion transmembrane transport / response to nitric oxide / Ion homeostasis / nitric oxide metabolic process / postsynaptic specialization, intracellular component / positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / negative regulation of cytosolic calcium ion concentration / peptidyl-cysteine S-nitrosylation / cadmium ion binding / behavioral response to cocaine / positive regulation of the force of heart contraction / negative regulation of potassium ion transport / calyx of Held / negative regulation of calcium ion transport / negative regulation of serotonin uptake / regulation of neurogenesis / sodium channel regulator activity / negative regulation of insulin secretion / response to vitamin E / nitric-oxide synthase (NADPH) / regulation of postsynaptic membrane potential / postsynaptic density, intracellular component / multicellular organismal response to stress / nitric-oxide synthase activity / xenobiotic catabolic process / negative regulation of peptidyl-serine phosphorylation / NADPH binding / arginine catabolic process / striated muscle contraction / regulation of sodium ion transport / nitric oxide mediated signal transduction / T-tubule / sarcoplasmic reticulum membrane / response to organonitrogen compound / cellular response to epinephrine stimulus / nitric oxide biosynthetic process / negative regulation of blood pressure / photoreceptor inner segment / response to nutrient levels / sarcoplasmic reticulum / secretory granule / response to activity / response to hormone / positive regulation of long-term synaptic potentiation / female pregnancy / muscle contraction / establishment of localization in cell / cell periphery / phosphoprotein binding / response to lead ion / response to nicotine / establishment of protein localization / potassium ion transport / response to organic cyclic compound / sarcolemma / cellular response to growth factor stimulus / response to peptide hormone / Z disc / cellular response to mechanical stimulus / response to estrogen / vasodilation / calcium ion transport / calcium-dependent protein binding / FMN binding / positive regulation of peptidyl-serine phosphorylation / NADP binding / flavin adenine dinucleotide binding / ATPase binding / response to heat / scaffold protein binding / nuclear membrane / response to ethanol / mitochondrial outer membrane / negative regulation of neuron apoptotic process / transmembrane transporter binding / response to lipopolysaccharide / dendritic spine / postsynaptic density / cytoskeleton / calmodulin binding / response to hypoxia / membrane raft / negative regulation of cell population proliferation / glutamatergic synapse / synapse / dendrite / heme binding / negative regulation of apoptotic process / perinuclear region of cytoplasm / positive regulation of DNA-templated transcription / enzyme binding / positive regulation of transcription by RNA polymerase II Similarity search - Function
NITRICOXIDESYNTHASE, BRAIN / / BNOS / CONSTITUTIVE NOS / NC-NOS / NOS TYPE I / NEURONAL NOS / N-NOS / NNOS / PEPTIDYL-CYSTEINE S- ...BNOS / CONSTITUTIVE NOS / NC-NOS / NOS TYPE I / NEURONAL NOS / N-NOS / NNOS / PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1 / NEURONAL NITRIC OXIDE SYNTHASE
Mass: 48812.527 Da / Num. of mol.: 2 / Fragment: HEME DOMAIN, RESIDUES 297-718 Source method: isolated from a genetically manipulated source Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P29476, nitric-oxide synthase (NADPH)
-
Non-polymers , 6 types, 443 molecules
#2: Chemical
ChemComp-HEM / PROTOPORPHYRINIXCONTAININGFE / HEME / Heme B
Mass: 616.487 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H32FeN4O4
Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1 Å / Relative weight: 1
Reflection
Resolution: 2.01→50 Å / Num. obs: 65044 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 8.6 % / Biso Wilson estimate: 26.17 Å2 / Rmerge(I) obs: 0.26 / Net I/σ(I): 9.3
Reflection shell
Resolution: 2.01→2.08 Å / Redundancy: 4.9 % / Rmerge(I) obs: 1.5 / Mean I/σ(I) obs: 0.9 / % possible all: 99.5
-
Processing
Software
Name
Version
Classification
PHENIX
(PHENIX.REFINE)
refinement
XDS
datareduction
Aimless
datascaling
REFMAC
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.005→39.165 Å / SU ML: 0.29 / σ(F): 1.89 / Phase error: 28.82 / Stereochemistry target values: ML Details: RESIDUES 339-349 IN CHAIN A AND 339-347 IN CHAIN B ARE DISORDERED.
Rfactor
Num. reflection
% reflection
Rfree
0.2511
2487
4.9 %
Rwork
0.1923
-
-
obs
0.1953
50933
78.3 %
Solvent computation
Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement step
Cycle: LAST / Resolution: 2.005→39.165 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
6659
0
175
434
7268
Refine LS restraints
Refine-ID
Type
Dev ideal
Number
X-RAY DIFFRACTION
f_bond_d
0.008
7065
X-RAY DIFFRACTION
f_angle_d
1.236
9612
X-RAY DIFFRACTION
f_dihedral_angle_d
15.617
2564
X-RAY DIFFRACTION
f_chiral_restr
0.076
994
X-RAY DIFFRACTION
f_plane_restr
0.005
1213
LS refinement shell
Resolution (Å)
Rfactor Rfree
Num. reflection Rfree
Rfactor Rwork
Num. reflection Rwork
Refine-ID
% reflection obs (%)
2.0049-2.0435
0.4206
16
0.2851
487
X-RAY DIFFRACTION
14
2.0435-2.0852
0.2863
40
0.2903
716
X-RAY DIFFRACTION
21
2.0852-2.1305
0.2944
30
0.291
975
X-RAY DIFFRACTION
29
2.1305-2.1801
0.3141
57
0.28
1318
X-RAY DIFFRACTION
38
2.1801-2.2346
0.3582
75
0.2804
1819
X-RAY DIFFRACTION
53
2.2346-2.295
0.3506
142
0.2791
2357
X-RAY DIFFRACTION
70
2.295-2.3626
0.3339
151
0.2603
2831
X-RAY DIFFRACTION
83
2.3626-2.4388
0.3214
153
0.2494
3280
X-RAY DIFFRACTION
97
2.4388-2.526
0.3632
178
0.2435
3409
X-RAY DIFFRACTION
100
2.526-2.6271
0.309
181
0.2197
3404
X-RAY DIFFRACTION
100
2.6271-2.7466
0.2737
171
0.2244
3440
X-RAY DIFFRACTION
100
2.7466-2.8914
0.2871
173
0.2218
3427
X-RAY DIFFRACTION
100
2.8914-3.0725
0.2633
184
0.2131
3425
X-RAY DIFFRACTION
100
3.0725-3.3096
0.2534
178
0.2016
3447
X-RAY DIFFRACTION
100
3.3096-3.6424
0.2359
192
0.1726
3436
X-RAY DIFFRACTION
100
3.6424-4.169
0.2216
176
0.1466
3485
X-RAY DIFFRACTION
100
4.169-5.2504
0.1948
206
0.1355
3507
X-RAY DIFFRACTION
100
5.2504-39.1721
0.1792
184
0.1561
3683
X-RAY DIFFRACTION
100
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
1.0684
-0.3763
-0.4637
1.0161
0.4076
5.0937
0.0512
0.2194
-0.0282
0.0619
-0.1663
0.0852
0.1053
-0.286
0.0331
0.1813
-0.0462
-0.0129
-0.0605
0.0022
0.0803
11.3832
4.6191
22.6133
2
0.9531
-0.039
-0.1063
1.2759
0.0927
3.3165
0.0009
-0.0647
0.0732
-0.204
-0.1376
0.0014
0.2909
0.0509
0.0296
-0.0642
0.1183
0.0489
0.0193
-0.0015
0.1326
12.3234
4.7752
60.0558
Refinement TLS group
ID
Refine-ID
Refine TLS-ID
Selection details
1
X-RAY DIFFRACTION
1
(CHAINAANDRESID299:716)
2
X-RAY DIFFRACTION
2
(CHAINBANDRESID299:718)
+
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