FMO DATABASE

FMODB ID: 9RGL2

Calculation Name: 1QAU-A-Xray547

Preferred Name: Nitric-oxide synthase, brain

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1QAU

Chain ID: A

ChEMBL ID: CHEMBL3048

UniProt ID: P29476

Base Structure: X-ray

Registration Date: 2025-10-05

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	112
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-809247.392577
FMO2-HF: Nuclear repulsion	768244.02322
FMO2-HF: Total energy	-41003.369357
FMO2-MP2: Total energy	-41126.717804

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:14:ASN)

Summations of interaction energy for fragment #1(A:14:ASN)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-103.066	-101.014	36.585	-16.633	-22.006	-0.078

Interaction energy analysis for fragmet #1(A:14:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.814 / q_NPA : 0.920

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	16	ILE	0	0.017	0.027	3.845	-1.855	-0.422	-0.018	-0.599	-0.816	0.000
85	A	98	ARG	1	0.888	0.929	3.745	36.275	36.650	0.006	-0.148	-0.233	0.000
86	A	99	GLY	0	0.051	0.039	2.421	1.860	3.275	3.379	-2.180	-2.615	0.022
87	A	100	PRO	0	-0.022	-0.023	3.095	-5.872	-7.468	0.207	2.646	-1.257	-0.002
88	A	101	GLU	-1	-0.846	-0.926	2.082	-70.421	-69.709	4.625	-2.416	-2.921	-0.032
89	A	102	GLY	0	-0.034	-0.017	4.378	4.752	4.800	-0.001	-0.009	-0.038	0.000
90	A	103	PHE	0	0.007	0.026	2.878	6.341	7.210	0.118	-0.309	-0.678	-0.001
91	A	104	THR	0	-0.059	-0.023	1.911	-31.174	-31.459	9.058	-4.351	-4.422	-0.051
92	A	105	THR	0	-0.005	-0.028	1.781	3.194	-0.960	16.085	-5.786	-6.146	0.026
93	A	106	HIS	0	-0.086	-0.054	2.299	-28.941	-25.937	3.128	-3.471	-2.661	-0.040
94	A	107	LEU	0	-0.021	-0.015	5.142	4.260	4.338	-0.001	-0.004	-0.072	0.000
110	A	123	THR	0	-0.008	-0.024	4.566	-4.390	-4.237	-0.001	-0.006	-0.147	0.000
4	A	17	SER	0	-0.002	-0.003	6.448	2.457	2.457	0.000	0.000	0.000	0.000
5	A	18	VAL	0	0.038	0.015	9.601	0.651	0.651	0.000	0.000	0.000	0.000
6	A	19	ARG	1	0.905	0.959	12.320	15.601	15.601	0.000	0.000	0.000	0.000
7	A	20	LEU	0	-0.008	0.004	15.015	0.228	0.228	0.000	0.000	0.000	0.000
8	A	21	PHE	0	-0.001	0.000	18.002	0.154	0.154	0.000	0.000	0.000	0.000
9	A	22	LYS	1	0.821	0.918	21.723	12.027	12.027	0.000	0.000	0.000	0.000
10	A	23	ARG	1	0.895	0.937	22.728	12.486	12.486	0.000	0.000	0.000	0.000
11	A	24	LYS	1	0.965	0.978	25.950	9.223	9.223	0.000	0.000	0.000	0.000
12	A	25	VAL	0	-0.019	-0.011	28.601	0.206	0.206	0.000	0.000	0.000	0.000
13	A	26	GLY	0	0.031	0.013	25.532	-0.193	-0.193	0.000	0.000	0.000	0.000
14	A	27	GLY	0	0.009	0.009	23.535	-0.444	-0.444	0.000	0.000	0.000	0.000
15	A	28	LEU	0	0.015	-0.008	18.069	-0.026	-0.026	0.000	0.000	0.000	0.000
16	A	29	GLY	0	-0.008	0.000	18.797	-0.525	-0.525	0.000	0.000	0.000	0.000
17	A	30	PHE	0	-0.044	-0.015	15.762	-0.353	-0.353	0.000	0.000	0.000	0.000
18	A	31	LEU	0	0.017	0.023	17.974	0.491	0.491	0.000	0.000	0.000	0.000
19	A	32	VAL	0	0.024	-0.003	15.475	-0.915	-0.915	0.000	0.000	0.000	0.000
20	A	33	LYS	1	0.832	0.917	16.119	15.587	15.587	0.000	0.000	0.000	0.000
21	A	34	GLU	-1	-0.785	-0.891	16.500	-15.136	-15.136	0.000	0.000	0.000	0.000
22	A	35	ARG	1	0.842	0.932	10.966	22.148	22.148	0.000	0.000	0.000	0.000
23	A	36	VAL	0	0.012	0.000	15.870	0.636	0.636	0.000	0.000	0.000	0.000
24	A	37	SER	0	-0.003	0.002	15.517	0.361	0.361	0.000	0.000	0.000	0.000
25	A	38	LYS	1	0.866	0.926	15.726	14.860	14.860	0.000	0.000	0.000	0.000
26	A	39	PRO	0	0.003	-0.012	10.634	-0.705	-0.705	0.000	0.000	0.000	0.000
27	A	40	PRO	0	0.010	0.018	13.843	-0.239	-0.239	0.000	0.000	0.000	0.000
28	A	41	VAL	0	0.002	0.004	14.567	0.774	0.774	0.000	0.000	0.000	0.000
29	A	42	ILE	0	-0.017	-0.007	10.338	-1.738	-1.738	0.000	0.000	0.000	0.000
30	A	43	ILE	0	0.011	0.002	10.944	1.618	1.618	0.000	0.000	0.000	0.000
31	A	44	SER	0	-0.062	-0.036	12.581	-0.756	-0.756	0.000	0.000	0.000	0.000
32	A	45	ASP	-1	-0.831	-0.915	15.237	-13.245	-13.245	0.000	0.000	0.000	0.000
33	A	46	LEU	0	-0.066	-0.034	13.578	-0.339	-0.339	0.000	0.000	0.000	0.000
34	A	47	ILE	0	0.020	0.016	17.902	0.462	0.462	0.000	0.000	0.000	0.000
35	A	48	ARG	1	0.879	0.921	18.145	13.645	13.645	0.000	0.000	0.000	0.000
36	A	49	GLY	0	0.030	0.020	22.075	0.511	0.511	0.000	0.000	0.000	0.000
37	A	50	GLY	0	-0.004	0.001	21.263	0.277	0.277	0.000	0.000	0.000	0.000
38	A	51	ALA	0	-0.019	-0.020	19.856	-0.337	-0.337	0.000	0.000	0.000	0.000
39	A	52	ALA	0	0.028	0.007	14.880	-0.437	-0.437	0.000	0.000	0.000	0.000
40	A	53	GLU	-1	-0.801	-0.868	15.144	-14.275	-14.275	0.000	0.000	0.000	0.000
41	A	54	GLN	0	0.049	0.029	16.790	-0.319	-0.319	0.000	0.000	0.000	0.000
42	A	55	SER	0	-0.023	-0.010	14.208	-0.410	-0.410	0.000	0.000	0.000	0.000
43	A	56	GLY	0	0.003	0.000	14.244	-0.246	-0.246	0.000	0.000	0.000	0.000
44	A	57	LEU	0	-0.053	-0.031	10.479	-1.066	-1.066	0.000	0.000	0.000	0.000
45	A	58	ILE	0	-0.002	0.004	9.092	-1.756	-1.756	0.000	0.000	0.000	0.000
46	A	59	GLN	0	-0.015	-0.015	7.820	0.270	0.270	0.000	0.000	0.000	0.000
47	A	60	ALA	0	0.000	0.007	10.056	-0.366	-0.366	0.000	0.000	0.000	0.000
48	A	61	GLY	0	0.008	-0.004	8.950	-0.700	-0.700	0.000	0.000	0.000	0.000
49	A	62	ASP	-1	-0.734	-0.826	6.362	-28.973	-28.973	0.000	0.000	0.000	0.000
50	A	63	ILE	0	-0.014	-0.011	7.110	2.592	2.592	0.000	0.000	0.000	0.000
51	A	64	ILE	0	-0.014	-0.004	8.525	-1.836	-1.836	0.000	0.000	0.000	0.000
52	A	65	LEU	0	-0.037	-0.016	7.204	0.567	0.567	0.000	0.000	0.000	0.000
53	A	66	ALA	0	0.007	-0.007	11.567	1.504	1.504	0.000	0.000	0.000	0.000
54	A	67	VAL	0	0.017	0.014	13.828	-0.630	-0.630	0.000	0.000	0.000	0.000
55	A	68	ASN	0	0.010	-0.001	16.702	0.404	0.404	0.000	0.000	0.000	0.000
56	A	69	ASP	-1	-0.872	-0.931	17.235	-14.734	-14.734	0.000	0.000	0.000	0.000
57	A	70	ARG	1	0.919	0.965	19.223	13.790	13.790	0.000	0.000	0.000	0.000
58	A	71	PRO	0	0.022	0.012	15.742	-0.840	-0.840	0.000	0.000	0.000	0.000
59	A	72	LEU	0	0.020	-0.020	14.995	1.115	1.115	0.000	0.000	0.000	0.000
60	A	73	VAL	0	-0.053	-0.028	12.031	0.554	0.554	0.000	0.000	0.000	0.000
61	A	74	ASP	-1	-0.800	-0.890	14.961	-15.506	-15.506	0.000	0.000	0.000	0.000
62	A	75	LEU	0	-0.042	0.001	18.415	1.056	1.056	0.000	0.000	0.000	0.000
63	A	76	SER	0	0.053	0.027	20.146	-0.366	-0.366	0.000	0.000	0.000	0.000
64	A	77	TYR	0	0.070	0.019	18.774	-0.429	-0.429	0.000	0.000	0.000	0.000
65	A	78	ASP	-1	-0.872	-0.936	21.334	-11.868	-11.868	0.000	0.000	0.000	0.000
66	A	79	SER	0	-0.026	-0.024	23.119	0.297	0.297	0.000	0.000	0.000	0.000
67	A	80	ALA	0	-0.013	-0.010	18.124	-0.101	-0.101	0.000	0.000	0.000	0.000
68	A	81	LEU	0	-0.011	-0.007	19.995	-0.174	-0.174	0.000	0.000	0.000	0.000
69	A	82	GLU	-1	-0.807	-0.874	21.693	-10.784	-10.784	0.000	0.000	0.000	0.000
70	A	83	VAL	0	-0.050	-0.017	19.834	0.219	0.219	0.000	0.000	0.000	0.000
71	A	84	LEU	0	0.007	0.003	16.631	-0.013	-0.013	0.000	0.000	0.000	0.000
72	A	85	ARG	1	0.792	0.863	20.831	11.586	11.586	0.000	0.000	0.000	0.000
73	A	86	GLY	0	0.025	0.004	24.469	0.280	0.280	0.000	0.000	0.000	0.000
74	A	87	ILE	0	-0.052	-0.007	19.585	0.169	0.169	0.000	0.000	0.000	0.000
75	A	88	ALA	0	0.059	0.039	24.176	0.297	0.297	0.000	0.000	0.000	0.000
76	A	89	SER	0	0.009	-0.013	25.754	-0.326	-0.326	0.000	0.000	0.000	0.000
77	A	90	GLU	-1	-0.860	-0.933	27.099	-10.113	-10.113	0.000	0.000	0.000	0.000
78	A	91	THR	0	-0.036	-0.011	24.738	-0.104	-0.104	0.000	0.000	0.000	0.000
79	A	92	HIS	0	0.020	0.000	21.353	-0.767	-0.767	0.000	0.000	0.000	0.000
80	A	93	VAL	0	-0.021	-0.008	17.146	0.136	0.136	0.000	0.000	0.000	0.000
81	A	94	VAL	0	-0.004	-0.001	14.175	-0.296	-0.296	0.000	0.000	0.000	0.000
82	A	95	LEU	0	0.010	0.010	12.239	0.327	0.327	0.000	0.000	0.000	0.000
83	A	96	ILE	0	-0.006	0.003	9.123	-1.429	-1.429	0.000	0.000	0.000	0.000
84	A	97	LEU	0	0.007	0.002	7.236	1.414	1.414	0.000	0.000	0.000	0.000
95	A	108	GLU	-1	-0.826	-0.892	8.672	-24.211	-24.211	0.000	0.000	0.000	0.000
96	A	109	THR	0	-0.064	-0.048	12.087	0.761	0.761	0.000	0.000	0.000	0.000
97	A	110	THR	0	0.005	0.020	15.793	0.334	0.334	0.000	0.000	0.000	0.000
98	A	111	PHE	0	0.019	-0.011	18.525	0.014	0.014	0.000	0.000	0.000	0.000
99	A	112	THR	0	-0.007	0.005	22.254	0.022	0.022	0.000	0.000	0.000	0.000
100	A	113	GLY	0	0.025	0.007	25.205	0.032	0.032	0.000	0.000	0.000	0.000
101	A	114	ASP	-1	-0.926	-0.960	28.611	-9.834	-9.834	0.000	0.000	0.000	0.000
102	A	115	GLY	0	0.000	0.004	26.646	0.085	0.085	0.000	0.000	0.000	0.000
103	A	116	THR	0	-0.028	-0.011	24.014	-0.168	-0.168	0.000	0.000	0.000	0.000
104	A	117	PRO	0	-0.016	0.001	20.246	-0.297	-0.297	0.000	0.000	0.000	0.000
105	A	118	LYS	1	0.867	0.920	16.079	16.857	16.857	0.000	0.000	0.000	0.000
106	A	119	THR	0	0.021	0.013	12.615	-0.074	-0.074	0.000	0.000	0.000	0.000
107	A	120	ILE	0	-0.017	-0.010	12.221	0.811	0.811	0.000	0.000	0.000	0.000
108	A	121	ARG	1	0.789	0.856	5.356	26.720	26.720	0.000	0.000	0.000	0.000
109	A	122	VAL	0	0.006	0.019	8.041	1.711	1.711	0.000	0.000	0.000	0.000
111	A	124	GLN	0	-0.028	-0.009	6.429	6.981	6.981	0.000	0.000	0.000	0.000
112	A	125	PRO	-1	-0.849	-0.914	5.985	-44.004	-44.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:14:ASN)