FMO DATABASE

FMODB ID: 9LR32

Calculation Name: 1CJW-A-Xray547

Preferred Name: Serotonin N-acetyltransferase

Target Type: SINGLE PROTEIN

Ligand Name: coa-s-acetyl tryptamine

Ligand 3-letter code: COT

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1CJW

Chain ID: A

ChEMBL ID: CHEMBL5452

UniProt ID: Q29495

Base Structure: X-ray

Registration Date: 2025-09-02

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	166
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1715343.933751
FMO2-HF: Nuclear repulsion	1649630.604642
FMO2-HF: Total energy	-65713.329109
FMO2-MP2: Total energy	-65903.477457

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:30:HIS)

Summations of interaction energy for fragment #1(A:30:HIS)

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.
-39.465	-37.336	-0.017	-0.933	-1.18	0.002

Interaction energy analysis for fragmet #1(A:30:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.873 / q_NPA : 0.931

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	32	LEU	0	0.010	0.017	3.859	-3.087	-0.958	-0.017	-0.933	-1.180	0.002
4	A	33	PRO	0	0.015	0.001	6.488	1.422	1.422	0.000	0.000	0.000	0.000
5	A	34	ALA	0	0.077	0.043	8.862	1.756	1.756	0.000	0.000	0.000	0.000
6	A	35	ASN	0	-0.052	-0.042	11.927	2.823	2.823	0.000	0.000	0.000	0.000
7	A	36	GLU	-1	-0.917	-0.947	10.409	-26.864	-26.864	0.000	0.000	0.000	0.000
8	A	37	PHE	0	-0.052	-0.030	12.610	1.132	1.132	0.000	0.000	0.000	0.000
9	A	38	ARG	1	0.800	0.888	12.353	20.570	20.570	0.000	0.000	0.000	0.000
10	A	39	CYS	0	-0.011	0.006	15.783	0.528	0.528	0.000	0.000	0.000	0.000
11	A	40	LEU	0	-0.048	-0.019	16.819	-1.162	-1.162	0.000	0.000	0.000	0.000
12	A	41	THR	0	0.036	0.005	16.784	0.419	0.419	0.000	0.000	0.000	0.000
13	A	42	PRO	0	0.042	-0.001	19.637	-0.117	-0.117	0.000	0.000	0.000	0.000
14	A	43	GLU	-1	-0.946	-0.959	15.552	-18.488	-18.488	0.000	0.000	0.000	0.000
15	A	44	ASP	-1	-0.793	-0.867	16.411	-18.662	-18.662	0.000	0.000	0.000	0.000
16	A	45	ALA	0	0.027	0.012	18.716	0.311	0.311	0.000	0.000	0.000	0.000
17	A	46	ALA	0	0.026	0.011	20.106	0.498	0.498	0.000	0.000	0.000	0.000
18	A	47	GLY	0	-0.015	-0.006	19.267	0.242	0.242	0.000	0.000	0.000	0.000
19	A	48	VAL	0	-0.008	-0.009	20.212	0.226	0.226	0.000	0.000	0.000	0.000
20	A	49	PHE	0	0.067	0.033	23.149	0.414	0.414	0.000	0.000	0.000	0.000
21	A	50	GLU	-1	-0.873	-0.931	22.519	-11.631	-11.631	0.000	0.000	0.000	0.000
22	A	51	ILE	0	-0.073	-0.029	21.043	0.275	0.275	0.000	0.000	0.000	0.000
23	A	52	GLU	-1	-0.802	-0.921	25.137	-10.363	-10.363	0.000	0.000	0.000	0.000
24	A	53	ARG	1	0.865	0.920	26.692	11.546	11.546	0.000	0.000	0.000	0.000
25	A	54	GLU	-1	-0.855	-0.905	27.829	-10.455	-10.455	0.000	0.000	0.000	0.000
26	A	55	ALA	0	-0.003	0.002	28.526	0.332	0.332	0.000	0.000	0.000	0.000
27	A	56	PHE	0	0.004	0.014	29.930	0.183	0.183	0.000	0.000	0.000	0.000
28	A	57	ILE	0	0.003	0.021	31.851	0.299	0.299	0.000	0.000	0.000	0.000
29	A	58	SER	0	-0.130	-0.083	32.651	0.328	0.328	0.000	0.000	0.000	0.000
30	A	59	VAL	0	-0.019	0.002	34.435	0.201	0.201	0.000	0.000	0.000	0.000
31	A	60	SER	0	-0.017	-0.020	36.758	0.264	0.264	0.000	0.000	0.000	0.000
32	A	61	GLY	0	-0.018	-0.002	37.597	0.189	0.189	0.000	0.000	0.000	0.000
33	A	62	ASN	0	-0.035	-0.023	36.360	-0.158	-0.158	0.000	0.000	0.000	0.000
34	A	63	CYS	0	-0.084	-0.060	31.649	-0.080	-0.080	0.000	0.000	0.000	0.000
35	A	64	PRO	0	-0.023	-0.002	32.103	0.176	0.176	0.000	0.000	0.000	0.000
36	A	65	LEU	0	-0.022	0.005	29.060	0.094	0.094	0.000	0.000	0.000	0.000
37	A	66	ASN	0	0.047	0.030	30.657	-0.431	-0.431	0.000	0.000	0.000	0.000
38	A	67	LEU	0	-0.002	-0.016	24.495	-0.185	-0.185	0.000	0.000	0.000	0.000
39	A	68	ASP	-1	-0.916	-0.945	27.688	-10.161	-10.161	0.000	0.000	0.000	0.000
40	A	69	GLU	-1	-0.827	-0.920	30.028	-9.250	-9.250	0.000	0.000	0.000	0.000
41	A	70	VAL	0	-0.036	-0.018	24.895	-0.180	-0.180	0.000	0.000	0.000	0.000
42	A	71	GLN	0	-0.011	-0.014	24.028	0.015	0.015	0.000	0.000	0.000	0.000
43	A	72	HIS	0	-0.012	0.014	26.743	-0.351	-0.351	0.000	0.000	0.000	0.000
44	A	73	PHE	0	0.023	0.000	28.152	-0.051	-0.051	0.000	0.000	0.000	0.000
45	A	74	LEU	0	-0.056	-0.032	21.752	-0.181	-0.181	0.000	0.000	0.000	0.000
46	A	75	THR	0	-0.047	-0.038	23.479	-0.616	-0.616	0.000	0.000	0.000	0.000
47	A	76	LEU	0	-0.078	-0.039	25.942	0.080	0.080	0.000	0.000	0.000	0.000
48	A	77	CYS	0	-0.036	0.001	26.835	0.380	0.380	0.000	0.000	0.000	0.000
49	A	78	PRO	0	0.055	0.055	21.262	-0.091	-0.091	0.000	0.000	0.000	0.000
50	A	79	GLU	-1	-0.843	-0.923	22.336	-12.008	-12.008	0.000	0.000	0.000	0.000
51	A	80	LEU	0	-0.002	0.012	23.396	0.145	0.145	0.000	0.000	0.000	0.000
52	A	81	SER	0	-0.012	-0.007	21.934	0.063	0.063	0.000	0.000	0.000	0.000
53	A	82	LEU	0	-0.025	-0.017	18.992	-0.391	-0.391	0.000	0.000	0.000	0.000
54	A	83	GLY	0	0.032	0.015	18.735	0.560	0.560	0.000	0.000	0.000	0.000
55	A	84	TRP	0	-0.044	-0.034	16.512	0.055	0.055	0.000	0.000	0.000	0.000
56	A	85	PHE	0	0.009	-0.010	13.097	0.250	0.250	0.000	0.000	0.000	0.000
57	A	86	VAL	0	-0.004	-0.007	14.029	-0.134	-0.134	0.000	0.000	0.000	0.000
58	A	87	GLU	-1	-0.856	-0.937	10.395	-25.295	-25.295	0.000	0.000	0.000	0.000
59	A	88	GLY	0	-0.017	0.007	9.619	-0.975	-0.975	0.000	0.000	0.000	0.000
60	A	89	ARG	1	0.865	0.928	9.873	25.505	25.505	0.000	0.000	0.000	0.000
61	A	90	LEU	0	0.032	0.038	14.181	0.060	0.060	0.000	0.000	0.000	0.000
62	A	91	VAL	0	-0.024	-0.019	17.342	0.718	0.718	0.000	0.000	0.000	0.000
63	A	92	ALA	0	-0.032	-0.024	19.897	0.889	0.889	0.000	0.000	0.000	0.000
64	A	93	PHE	0	0.026	0.018	20.765	-0.858	-0.858	0.000	0.000	0.000	0.000
65	A	94	ILE	0	-0.004	0.003	22.964	0.552	0.552	0.000	0.000	0.000	0.000
66	A	95	ILE	0	0.013	0.006	24.119	-0.523	-0.523	0.000	0.000	0.000	0.000
67	A	96	GLY	0	0.016	0.000	26.762	0.425	0.425	0.000	0.000	0.000	0.000
68	A	97	SER	0	-0.009	-0.007	28.601	-0.211	-0.211	0.000	0.000	0.000	0.000
69	A	98	LEU	0	-0.025	-0.001	31.094	0.073	0.073	0.000	0.000	0.000	0.000
70	A	99	TRP	0	-0.030	-0.033	33.703	-0.036	-0.036	0.000	0.000	0.000	0.000
71	A	100	ASP	-1	-0.837	-0.953	37.329	-7.620	-7.620	0.000	0.000	0.000	0.000
72	A	101	GLU	-1	-0.925	-0.939	40.500	-6.832	-6.832	0.000	0.000	0.000	0.000
73	A	102	GLU	-1	-0.951	-0.987	41.924	-6.784	-6.784	0.000	0.000	0.000	0.000
74	A	103	ARG	1	0.848	0.928	42.894	6.734	6.734	0.000	0.000	0.000	0.000
75	A	104	LEU	0	0.023	0.026	37.892	-0.073	-0.073	0.000	0.000	0.000	0.000
76	A	105	THR	0	0.053	0.022	41.805	0.100	0.100	0.000	0.000	0.000	0.000
77	A	106	GLN	0	0.035	0.013	41.709	-0.116	-0.116	0.000	0.000	0.000	0.000
78	A	107	GLU	-1	-0.834	-0.919	41.457	-7.375	-7.375	0.000	0.000	0.000	0.000
79	A	108	SER	0	-0.034	-0.029	38.679	-0.267	-0.267	0.000	0.000	0.000	0.000
80	A	109	LEU	0	0.002	0.004	36.648	-0.262	-0.262	0.000	0.000	0.000	0.000
81	A	110	ALA	0	0.046	0.017	35.310	-0.305	-0.305	0.000	0.000	0.000	0.000
82	A	111	LEU	0	-0.027	0.001	35.990	-0.107	-0.107	0.000	0.000	0.000	0.000
83	A	112	HIS	0	0.105	0.057	30.745	-0.056	-0.056	0.000	0.000	0.000	0.000
84	A	113	ARG	1	0.817	0.922	34.464	7.711	7.711	0.000	0.000	0.000	0.000
85	A	114	PRO	0	0.004	-0.008	33.807	0.026	0.026	0.000	0.000	0.000	0.000
86	A	115	ARG	1	0.885	0.932	35.112	7.915	7.915	0.000	0.000	0.000	0.000
87	A	116	GLY	0	0.041	0.038	37.088	0.175	0.175	0.000	0.000	0.000	0.000
88	A	117	HIS	0	-0.045	-0.037	36.040	0.037	0.037	0.000	0.000	0.000	0.000
89	A	118	SER	0	0.008	0.022	36.148	0.025	0.025	0.000	0.000	0.000	0.000
90	A	119	ALA	0	0.045	0.027	30.760	-0.060	-0.060	0.000	0.000	0.000	0.000
91	A	120	HIS	0	0.009	-0.001	32.745	-0.040	-0.040	0.000	0.000	0.000	0.000
92	A	121	LEU	0	-0.020	-0.013	29.567	-0.345	-0.345	0.000	0.000	0.000	0.000
93	A	122	HIS	1	0.815	0.915	30.974	9.590	9.590	0.000	0.000	0.000	0.000
94	A	123	ALA	0	0.048	0.024	28.876	0.140	0.140	0.000	0.000	0.000	0.000
95	A	124	LEU	0	-0.011	-0.007	26.853	-0.302	-0.302	0.000	0.000	0.000	0.000
96	A	125	ALA	0	0.013	0.022	26.634	0.328	0.328	0.000	0.000	0.000	0.000
97	A	126	VAL	0	-0.040	-0.024	24.326	-0.502	-0.502	0.000	0.000	0.000	0.000
98	A	127	HIS	0	0.100	0.047	20.878	0.855	0.855	0.000	0.000	0.000	0.000
99	A	128	ARG	1	0.990	0.988	24.085	11.040	11.040	0.000	0.000	0.000	0.000
100	A	129	SER	0	-0.051	-0.024	22.575	0.448	0.448	0.000	0.000	0.000	0.000
101	A	130	PHE	0	-0.014	-0.012	18.622	-0.226	-0.226	0.000	0.000	0.000	0.000
102	A	131	ARG	1	0.815	0.888	24.151	11.074	11.074	0.000	0.000	0.000	0.000
103	A	132	GLN	0	0.013	-0.007	27.771	-0.203	-0.203	0.000	0.000	0.000	0.000
104	A	133	GLN	0	-0.019	0.004	24.554	-0.286	-0.286	0.000	0.000	0.000	0.000
105	A	134	GLY	0	0.030	0.011	25.682	-0.428	-0.428	0.000	0.000	0.000	0.000
106	A	135	LYS	1	0.949	0.984	20.305	14.665	14.665	0.000	0.000	0.000	0.000
107	A	136	GLY	0	0.076	0.025	24.322	-0.170	-0.170	0.000	0.000	0.000	0.000
108	A	137	SER	0	-0.026	-0.006	26.551	0.344	0.344	0.000	0.000	0.000	0.000
109	A	138	VAL	0	0.004	0.002	22.170	0.123	0.123	0.000	0.000	0.000	0.000
110	A	139	LEU	0	-0.029	-0.007	20.655	-0.139	-0.139	0.000	0.000	0.000	0.000
111	A	140	LEU	0	0.054	0.030	23.638	-0.027	-0.027	0.000	0.000	0.000	0.000
112	A	141	TRP	0	0.028	0.005	27.052	0.073	0.073	0.000	0.000	0.000	0.000
113	A	142	ARG	1	0.912	0.962	16.552	15.708	15.708	0.000	0.000	0.000	0.000
114	A	143	TYR	0	0.000	-0.026	23.951	0.008	0.008	0.000	0.000	0.000	0.000
115	A	144	LEU	0	0.005	0.005	25.197	0.130	0.130	0.000	0.000	0.000	0.000
116	A	145	HIS	0	0.004	0.000	25.695	0.199	0.199	0.000	0.000	0.000	0.000
117	A	146	HIS	0	-0.097	-0.043	21.319	-0.174	-0.174	0.000	0.000	0.000	0.000
118	A	147	VAL	0	0.017	-0.008	24.593	0.033	0.033	0.000	0.000	0.000	0.000
119	A	148	GLY	0	0.012	0.012	27.582	0.272	0.272	0.000	0.000	0.000	0.000
120	A	149	ALA	0	-0.051	-0.017	25.862	0.225	0.225	0.000	0.000	0.000	0.000
121	A	150	GLN	0	-0.037	-0.015	25.003	0.225	0.225	0.000	0.000	0.000	0.000
122	A	151	PRO	0	-0.012	-0.011	28.859	0.303	0.303	0.000	0.000	0.000	0.000
123	A	152	ALA	0	-0.038	-0.023	32.071	0.154	0.154	0.000	0.000	0.000	0.000
124	A	153	VAL	0	-0.006	0.006	30.631	0.293	0.293	0.000	0.000	0.000	0.000
125	A	154	ARG	1	0.927	0.967	33.656	7.774	7.774	0.000	0.000	0.000	0.000
126	A	155	ARG	1	0.805	0.900	35.652	7.844	7.844	0.000	0.000	0.000	0.000
127	A	156	ALA	0	0.019	0.027	32.796	-0.221	-0.221	0.000	0.000	0.000	0.000
128	A	157	VAL	0	-0.031	-0.017	34.611	0.262	0.262	0.000	0.000	0.000	0.000
129	A	158	LEU	0	0.024	0.023	33.469	-0.288	-0.288	0.000	0.000	0.000	0.000
130	A	159	MET	0	0.035	0.020	36.271	0.345	0.345	0.000	0.000	0.000	0.000
131	A	160	CYS	0	-0.057	-0.022	37.013	-0.255	-0.255	0.000	0.000	0.000	0.000
132	A	161	GLU	-1	-0.844	-0.917	38.655	-7.796	-7.796	0.000	0.000	0.000	0.000
133	A	162	ASP	-1	-0.832	-0.910	40.443	-7.218	-7.218	0.000	0.000	0.000	0.000
134	A	163	ALA	0	-0.030	-0.017	40.787	0.002	0.002	0.000	0.000	0.000	0.000
135	A	164	LEU	0	-0.025	-0.017	35.153	-0.131	-0.131	0.000	0.000	0.000	0.000
136	A	165	VAL	0	0.031	0.020	38.106	-0.159	-0.159	0.000	0.000	0.000	0.000
137	A	166	PRO	0	0.017	-0.001	39.953	-0.075	-0.075	0.000	0.000	0.000	0.000
138	A	167	PHE	0	-0.076	-0.029	30.713	-0.127	-0.127	0.000	0.000	0.000	0.000
139	A	168	TYR	0	0.081	0.005	32.366	-0.120	-0.120	0.000	0.000	0.000	0.000
140	A	169	GLN	0	0.045	0.029	36.263	-0.066	-0.066	0.000	0.000	0.000	0.000
141	A	170	ARG	1	0.857	0.935	33.851	8.879	8.879	0.000	0.000	0.000	0.000
142	A	171	PHE	0	-0.075	-0.037	29.809	-0.253	-0.253	0.000	0.000	0.000	0.000
143	A	172	GLY	0	0.036	0.021	34.313	-0.080	-0.080	0.000	0.000	0.000	0.000
144	A	173	PHE	0	-0.034	-0.022	32.872	0.099	0.099	0.000	0.000	0.000	0.000
145	A	174	HIS	0	0.025	-0.002	38.290	0.190	0.190	0.000	0.000	0.000	0.000
146	A	175	PRO	0	0.010	-0.018	41.955	-0.087	-0.087	0.000	0.000	0.000	0.000
147	A	176	ALA	0	-0.005	0.015	43.625	0.176	0.176	0.000	0.000	0.000	0.000
148	A	177	GLY	0	0.032	0.017	45.287	0.122	0.122	0.000	0.000	0.000	0.000
149	A	178	PRO	0	0.012	-0.007	45.639	-0.160	-0.160	0.000	0.000	0.000	0.000
150	A	179	CYS	0	-0.048	0.007	41.471	0.023	0.023	0.000	0.000	0.000	0.000
151	A	180	ALA	0	0.001	0.001	44.802	0.109	0.109	0.000	0.000	0.000	0.000
152	A	181	ILE	0	-0.045	-0.029	39.984	0.056	0.056	0.000	0.000	0.000	0.000
153	A	182	VAL	0	0.005	0.004	43.919	0.015	0.015	0.000	0.000	0.000	0.000
154	A	183	VAL	0	0.011	0.000	39.109	-0.087	-0.087	0.000	0.000	0.000	0.000
155	A	184	GLY	0	0.004	0.006	42.514	-0.036	-0.036	0.000	0.000	0.000	0.000
156	A	185	SER	0	-0.029	-0.023	44.676	0.090	0.090	0.000	0.000	0.000	0.000
157	A	186	LEU	0	-0.006	0.012	39.783	0.094	0.094	0.000	0.000	0.000	0.000
158	A	187	THR	0	0.006	0.002	43.975	0.077	0.077	0.000	0.000	0.000	0.000
159	A	188	PHE	0	0.000	-0.014	39.326	-0.115	-0.115	0.000	0.000	0.000	0.000
160	A	189	THR	0	-0.005	-0.013	42.736	0.227	0.227	0.000	0.000	0.000	0.000
161	A	190	GLU	-1	-0.776	-0.889	41.185	-7.517	-7.517	0.000	0.000	0.000	0.000
162	A	191	MET	0	-0.047	0.000	38.139	0.197	0.197	0.000	0.000	0.000	0.000
163	A	192	HIS	0	-0.006	-0.037	38.513	-0.146	-0.146	0.000	0.000	0.000	0.000
164	A	193	CYS	0	-0.055	-0.001	34.875	0.161	0.161	0.000	0.000	0.000	0.000
165	A	194	SER	0	-0.034	-0.016	37.168	0.032	0.032	0.000	0.000	0.000	0.000
166	A	195	LEU	-1	-0.919	-0.960	31.469	-8.559	-8.559	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:30:HIS)