FMO DATABASE

FMODB ID: 3MQYL

Calculation Name: 1SEI-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1SEI

Chain ID: A

ChEMBL ID:

UniProt ID: P56209

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	130
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1131137.612635
FMO2-HF: Nuclear repulsion	1080489.123384
FMO2-HF: Total energy	-50648.489251
FMO2-MP2: Total energy	-50798.103481

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:1:VAL)

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

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.
87.939	94.847	7.349	-4.714	-9.542	-0.034

Interaction energy analysis for fragmet #1(A:1:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.867 / q_NPA : 0.935

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

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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	3	THR	0	0.024	-0.028	2.654	0.122	3.294	0.788	-1.559	-2.400	-0.013
4	A	4	ASP	-1	-0.791	-0.872	4.608	-25.826	-25.682	-0.001	-0.017	-0.126	0.000
6	A	6	ILE	0	0.007	0.012	2.703	0.592	1.155	0.247	-0.147	-0.664	0.000
31	A	31	ILE	0	0.019	0.009	2.392	-0.588	-0.649	2.662	-0.516	-2.085	-0.002
32	A	32	LYS	1	0.884	0.938	5.094	25.266	25.287	-0.001	-0.002	-0.017	0.000
105	A	105	SER	0	-0.006	0.004	2.272	-6.303	-5.040	1.579	-1.015	-1.827	-0.008
106	A	106	THR	0	-0.034	-0.028	4.370	-0.066	0.012	-0.001	-0.026	-0.051	0.000
110	A	110	VAL	0	-0.067	-0.036	4.439	-3.268	-3.137	-0.001	-0.012	-0.118	0.000
124	A	124	GLU	-1	-0.818	-0.853	3.137	-67.066	-65.336	0.115	-0.988	-0.856	-0.009
126	A	126	ILE	0	0.009	-0.006	2.181	-1.250	-1.383	1.962	-0.432	-1.398	-0.002
5	A	5	PRO	0	0.024	0.004	4.898	2.184	2.184	0.000	0.000	0.000	0.000
7	A	7	ALA	0	-0.010	-0.016	6.936	2.477	2.477	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.845	-0.909	9.852	-20.427	-20.427	0.000	0.000	0.000	0.000
9	A	9	MET	0	0.008	0.027	9.774	0.707	0.707	0.000	0.000	0.000	0.000
10	A	10	LEU	0	0.011	-0.011	9.853	1.313	1.313	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.037	-0.028	12.790	1.475	1.475	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.015	0.023	14.736	1.078	1.078	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.023	0.004	13.572	0.857	0.857	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.855	0.926	14.614	17.848	17.848	0.000	0.000	0.000	0.000
15	A	15	ASN	0	0.004	-0.004	18.715	0.767	0.767	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.024	0.015	20.177	0.631	0.631	0.000	0.000	0.000	0.000
17	A	17	ASN	0	0.025	0.005	21.042	0.875	0.875	0.000	0.000	0.000	0.000
18	A	18	MET	0	-0.043	-0.006	22.755	0.525	0.525	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.027	-0.019	24.794	0.470	0.470	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.855	0.932	25.854	9.994	9.994	0.000	0.000	0.000	0.000
21	A	21	HIS	0	0.050	0.034	23.840	0.339	0.339	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.851	-0.921	24.724	-10.407	-10.407	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.791	0.880	22.220	11.345	11.345	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.019	0.004	16.556	0.182	0.182	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.761	-0.866	18.345	-12.495	-12.495	0.000	0.000	0.000	0.000
26	A	26	VAL	0	-0.016	-0.003	12.981	-0.201	-0.201	0.000	0.000	0.000	0.000
27	A	27	PRO	0	0.054	0.024	12.573	-0.055	-0.055	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.001	0.003	11.812	-1.503	-1.503	0.000	0.000	0.000	0.000
29	A	29	SER	0	-0.005	-0.015	6.210	-1.002	-1.002	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.924	0.959	6.672	30.526	30.526	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.963	0.987	7.974	19.212	19.212	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.801	-0.905	6.726	-30.988	-30.988	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.015	-0.011	5.915	0.871	0.871	0.000	0.000	0.000	0.000
36	A	36	ALA	0	0.017	0.014	9.493	1.369	1.369	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.840	-0.905	12.355	-15.275	-15.275	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.017	0.002	9.927	0.938	0.938	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.017	-0.022	12.697	0.916	0.916	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.853	0.919	15.452	14.173	14.173	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.748	0.846	14.497	18.048	18.048	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.872	-0.934	15.915	-15.237	-15.237	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.004	0.014	18.948	0.393	0.393	0.000	0.000	0.000	0.000
44	A	44	PHE	0	0.018	-0.008	17.481	0.449	0.449	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.061	-0.028	16.367	0.168	0.168	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.830	0.914	20.206	11.404	11.404	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.761	-0.881	20.287	-12.946	-12.946	0.000	0.000	0.000	0.000
48	A	48	TYR	0	-0.125	-0.088	15.443	-0.668	-0.668	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.799	-0.891	18.408	-11.800	-11.800	0.000	0.000	0.000	0.000
50	A	50	TYR	0	-0.112	-0.066	14.749	-1.101	-1.101	0.000	0.000	0.000	0.000
51	A	51	ILE	0	0.019	0.012	17.841	0.615	0.615	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.832	-0.912	18.763	-15.026	-15.026	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.857	-0.922	20.801	-11.514	-11.514	0.000	0.000	0.000	0.000
54	A	54	ASN	0	-0.020	-0.017	21.810	-0.029	-0.029	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.846	0.933	19.107	13.949	13.949	0.000	0.000	0.000	0.000
56	A	56	GLN	0	-0.008	0.000	17.715	-0.624	-0.624	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.021	0.012	15.531	0.377	0.377	0.000	0.000	0.000	0.000
58	A	58	ILE	0	-0.013	-0.014	15.402	-0.997	-0.997	0.000	0.000	0.000	0.000
59	A	59	LEU	0	-0.032	-0.019	11.338	-0.045	-0.045	0.000	0.000	0.000	0.000
60	A	60	ARG	1	0.764	0.876	15.737	12.175	12.175	0.000	0.000	0.000	0.000
61	A	61	ILE	0	-0.007	-0.011	13.989	-0.249	-0.249	0.000	0.000	0.000	0.000
62	A	62	PHE	0	0.017	-0.004	18.362	0.437	0.437	0.000	0.000	0.000	0.000
63	A	63	LEU	0	0.021	0.016	18.987	-0.301	-0.301	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.894	0.952	22.083	12.139	12.139	0.000	0.000	0.000	0.000
65	A	65	TYR	0	-0.009	-0.022	24.345	-0.355	-0.355	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.030	0.028	27.448	0.023	0.023	0.000	0.000	0.000	0.000
67	A	67	PRO	0	-0.022	-0.002	30.333	0.007	0.007	0.000	0.000	0.000	0.000
68	A	68	ASN	0	0.013	-0.009	31.825	0.096	0.096	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.849	-0.910	29.804	-9.519	-9.519	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.834	0.892	24.849	10.753	10.753	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.022	0.020	22.578	0.085	0.085	0.000	0.000	0.000	0.000
72	A	72	ILE	0	-0.042	-0.005	17.959	-0.490	-0.490	0.000	0.000	0.000	0.000
73	A	73	THR	0	-0.005	0.000	21.280	0.561	0.561	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.043	-0.040	19.289	0.207	0.207	0.000	0.000	0.000	0.000
75	A	75	LEU	0	0.002	0.024	13.967	-0.512	-0.512	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.929	0.959	13.142	18.535	18.535	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.817	0.898	7.237	30.572	30.572	0.000	0.000	0.000	0.000
78	A	78	ILE	0	-0.087	-0.045	8.329	1.987	1.987	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.007	-0.025	5.691	2.833	2.833	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.932	0.984	6.544	19.571	19.571	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.043	0.007	8.206	0.151	0.151	0.000	0.000	0.000	0.000
82	A	82	GLY	0	0.032	0.024	10.773	1.387	1.387	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.019	-0.004	11.617	1.510	1.510	0.000	0.000	0.000	0.000
84	A	84	ARG	1	0.886	0.935	5.119	44.304	44.304	0.000	0.000	0.000	0.000
85	A	85	VAL	0	0.016	0.002	8.437	2.280	2.280	0.000	0.000	0.000	0.000
86	A	86	TYR	0	-0.014	-0.006	8.219	-2.185	-2.185	0.000	0.000	0.000	0.000
87	A	87	VAL	0	-0.008	0.013	9.604	2.346	2.346	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.969	0.968	11.611	17.677	17.677	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.033	0.003	14.257	0.464	0.464	0.000	0.000	0.000	0.000
90	A	90	HIS	0	-0.022	-0.006	15.786	0.732	0.732	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.831	-0.904	15.598	-17.987	-17.987	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.026	0.002	13.247	-0.302	-0.302	0.000	0.000	0.000	0.000
93	A	93	PRO	0	-0.030	-0.006	13.832	1.236	1.236	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.990	0.979	16.963	13.938	13.938	0.000	0.000	0.000	0.000
95	A	95	VAL	0	-0.053	-0.016	16.289	0.562	0.562	0.000	0.000	0.000	0.000
96	A	96	LEU	0	0.024	0.018	19.554	0.142	0.142	0.000	0.000	0.000	0.000
97	A	97	ASN	0	0.053	0.012	22.097	-0.649	-0.649	0.000	0.000	0.000	0.000
98	A	98	GLY	0	0.023	0.019	23.390	0.312	0.312	0.000	0.000	0.000	0.000
99	A	99	LEU	0	-0.007	-0.004	21.206	-0.013	-0.013	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.041	0.047	18.402	-0.547	-0.547	0.000	0.000	0.000	0.000
101	A	101	ILE	0	-0.061	-0.037	13.126	0.010	0.010	0.000	0.000	0.000	0.000
102	A	102	ALA	0	-0.011	0.005	11.683	-0.597	-0.597	0.000	0.000	0.000	0.000
103	A	103	ILE	0	0.003	-0.002	7.040	-0.055	-0.055	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.026	-0.025	6.169	-2.093	-2.093	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.008	-0.012	6.944	-2.832	-2.832	0.000	0.000	0.000	0.000
108	A	108	GLN	0	0.005	-0.001	9.008	2.039	2.039	0.000	0.000	0.000	0.000
109	A	109	GLY	0	0.026	0.030	7.555	1.894	1.894	0.000	0.000	0.000	0.000
111	A	111	LEU	0	0.004	0.019	7.101	3.072	3.072	0.000	0.000	0.000	0.000
112	A	112	THR	0	0.026	-0.019	9.329	-1.064	-1.064	0.000	0.000	0.000	0.000
113	A	113	ASP	-1	-0.766	-0.897	12.064	-17.754	-17.754	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.880	0.931	13.756	16.638	16.638	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.755	-0.838	13.489	-19.072	-19.072	0.000	0.000	0.000	0.000
116	A	116	ALA	0	-0.002	-0.006	11.451	0.137	0.137	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.899	0.944	13.462	15.796	15.796	0.000	0.000	0.000	0.000
118	A	118	GLN	0	-0.007	0.003	17.004	-0.021	-0.021	0.000	0.000	0.000	0.000
119	A	119	LYS	1	0.919	0.969	14.408	18.611	18.611	0.000	0.000	0.000	0.000
120	A	120	GLY	0	0.025	0.034	16.844	-0.326	-0.326	0.000	0.000	0.000	0.000
121	A	121	THR	0	-0.050	-0.037	11.279	-0.415	-0.415	0.000	0.000	0.000	0.000
122	A	122	GLY	0	0.029	0.011	11.845	0.672	0.672	0.000	0.000	0.000	0.000
123	A	123	GLY	0	-0.023	-0.025	7.775	-1.354	-1.354	0.000	0.000	0.000	0.000
125	A	125	ILE	0	0.034	0.006	5.368	-2.291	-2.291	0.000	0.000	0.000	0.000
127	A	127	ALA	0	-0.032	-0.019	5.596	1.475	1.475	0.000	0.000	0.000	0.000
128	A	128	TYR	0	-0.034	-0.031	8.917	-0.320	-0.320	0.000	0.000	0.000	0.000
129	A	129	VAL	0	-0.014	-0.009	12.543	-0.099	-0.099	0.000	0.000	0.000	0.000
130	A	130	ILE	-1	-0.750	-0.848	15.252	-13.773	-13.773	0.000	0.000	0.000	0.000

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