FMO DATABASE

FMODB ID: G7K41

Calculation Name: 2A1V-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2A1V

Chain ID: A

ChEMBL ID:

UniProt ID: Q9RRT5

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	138
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1251456.023385
FMO2-HF: Nuclear repulsion	1197441.332109
FMO2-HF: Total energy	-54014.691276
FMO2-MP2: Total energy	-54173.727548

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:3:LEU)

Summations of interaction energy for fragment #1(A:3:LEU)

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.
-128.01	-124.572	0.66	-1.753	-2.345	-0.018

Interaction energy analysis for fragmet #1(A:3:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.833 / q_NPA : 0.910

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	5	THR	0	0.039	0.031	2.648	-5.540	-2.296	0.662	-1.742	-2.165	-0.018
4	A	6	PRO	0	0.028	-0.007	4.852	2.329	2.455	-0.001	-0.007	-0.118	0.000
136	A	138	SER	0	-0.024	-0.016	4.640	-2.663	-2.595	-0.001	-0.004	-0.062	0.000
5	A	7	MET	0	-0.085	-0.027	7.847	1.870	1.870	0.000	0.000	0.000	0.000
6	A	8	GLN	0	-0.008	-0.021	10.335	2.988	2.988	0.000	0.000	0.000	0.000
7	A	9	THR	0	-0.008	0.010	11.071	1.418	1.418	0.000	0.000	0.000	0.000
8	A	10	VAL	0	0.049	0.004	13.277	-0.664	-0.664	0.000	0.000	0.000	0.000
9	A	11	ASP	-1	-0.883	-0.942	11.133	-21.679	-21.679	0.000	0.000	0.000	0.000
10	A	12	ASP	-1	-0.786	-0.889	8.368	-33.013	-33.013	0.000	0.000	0.000	0.000
11	A	13	LEU	0	-0.005	0.007	9.728	-1.691	-1.691	0.000	0.000	0.000	0.000
12	A	14	ARG	1	0.859	0.898	12.489	18.007	18.007	0.000	0.000	0.000	0.000
13	A	15	SER	0	-0.059	-0.033	7.087	-2.045	-2.045	0.000	0.000	0.000	0.000
14	A	16	VAL	0	0.007	0.007	7.724	-1.911	-1.911	0.000	0.000	0.000	0.000
15	A	17	CYS	0	-0.079	-0.043	9.548	2.164	2.164	0.000	0.000	0.000	0.000
16	A	18	ASP	-1	-0.888	-0.950	11.613	-21.550	-21.550	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.902	-0.932	6.819	-37.786	-37.786	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.060	-0.019	11.630	1.323	1.323	0.000	0.000	0.000	0.000
19	A	21	PRO	0	-0.007	-0.010	14.651	1.155	1.155	0.000	0.000	0.000	0.000
20	A	22	HIS	0	0.000	-0.007	17.978	0.341	0.341	0.000	0.000	0.000	0.000
21	A	23	SER	0	0.022	0.017	16.980	1.148	1.148	0.000	0.000	0.000	0.000
22	A	24	LEU	0	-0.021	-0.016	19.119	0.349	0.349	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.746	-0.834	17.440	-17.405	-17.405	0.000	0.000	0.000	0.000
24	A	26	THR	0	-0.091	-0.054	21.635	0.840	0.840	0.000	0.000	0.000	0.000
25	A	27	PHE	0	0.100	0.052	22.289	-0.495	-0.495	0.000	0.000	0.000	0.000
26	A	28	PRO	0	-0.114	-0.052	26.779	0.388	0.388	0.000	0.000	0.000	0.000
27	A	29	PHE	0	-0.032	-0.027	28.132	0.323	0.323	0.000	0.000	0.000	0.000
28	A	30	ASP	-1	-0.910	-0.950	30.950	-9.204	-9.204	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.867	-0.904	28.919	-10.868	-10.868	0.000	0.000	0.000	0.000
30	A	32	GLU	-1	-0.883	-0.941	25.388	-11.414	-11.414	0.000	0.000	0.000	0.000
31	A	33	THR	0	-0.102	-0.080	24.385	-0.833	-0.833	0.000	0.000	0.000	0.000
32	A	34	LEU	0	-0.020	0.015	18.396	0.286	0.286	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.058	-0.049	22.171	-0.260	-0.260	0.000	0.000	0.000	0.000
34	A	36	PHE	0	0.070	0.036	16.232	0.330	0.330	0.000	0.000	0.000	0.000
35	A	37	LYS	1	0.898	0.934	20.641	12.182	12.182	0.000	0.000	0.000	0.000
36	A	38	VAL	0	0.053	0.032	20.270	-0.427	-0.427	0.000	0.000	0.000	0.000
37	A	39	GLY	0	-0.020	-0.014	22.128	0.687	0.687	0.000	0.000	0.000	0.000
38	A	40	TYR	0	-0.024	-0.033	24.905	-0.243	-0.243	0.000	0.000	0.000	0.000
39	A	41	LEU	0	0.038	0.009	26.385	0.056	0.056	0.000	0.000	0.000	0.000
40	A	42	SER	0	-0.013	0.001	28.933	0.056	0.056	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.743	0.849	29.762	10.608	10.608	0.000	0.000	0.000	0.000
42	A	44	SER	0	0.072	0.064	25.316	-0.240	-0.240	0.000	0.000	0.000	0.000
43	A	45	ARG	1	0.793	0.879	25.453	11.261	11.261	0.000	0.000	0.000	0.000
44	A	46	MET	0	0.037	0.024	23.848	-0.332	-0.332	0.000	0.000	0.000	0.000
45	A	47	TYR	0	-0.029	-0.031	15.762	0.827	0.827	0.000	0.000	0.000	0.000
46	A	48	ALA	0	0.028	0.035	18.251	-0.465	-0.465	0.000	0.000	0.000	0.000
47	A	49	LEU	0	-0.025	-0.009	20.268	0.461	0.461	0.000	0.000	0.000	0.000
48	A	50	THR	0	-0.019	-0.036	18.248	-0.515	-0.515	0.000	0.000	0.000	0.000
49	A	51	ASP	-1	-0.793	-0.890	21.419	-12.005	-12.005	0.000	0.000	0.000	0.000
50	A	52	ILE	0	-0.018	-0.028	19.973	-0.434	-0.434	0.000	0.000	0.000	0.000
51	A	53	THR	0	-0.029	-0.008	21.873	-0.075	-0.075	0.000	0.000	0.000	0.000
52	A	54	GLN	0	-0.119	-0.052	22.853	0.145	0.145	0.000	0.000	0.000	0.000
53	A	55	ASP	-1	-0.888	-0.931	19.619	-15.669	-15.669	0.000	0.000	0.000	0.000
54	A	56	PRO	0	-0.025	-0.019	18.919	0.651	0.651	0.000	0.000	0.000	0.000
55	A	57	LEU	0	0.023	0.019	16.121	0.505	0.505	0.000	0.000	0.000	0.000
56	A	58	ARG	1	0.931	0.967	19.484	12.885	12.885	0.000	0.000	0.000	0.000
57	A	59	LEU	0	0.016	0.042	15.855	0.271	0.271	0.000	0.000	0.000	0.000
58	A	60	SER	0	-0.027	-0.003	19.819	0.267	0.267	0.000	0.000	0.000	0.000
59	A	61	LEU	0	0.030	0.016	17.405	-0.256	-0.256	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.887	0.939	21.068	12.929	12.929	0.000	0.000	0.000	0.000
61	A	63	VAL	0	0.000	0.002	21.353	-0.679	-0.679	0.000	0.000	0.000	0.000
62	A	64	ASP	-1	-0.847	-0.938	23.597	-11.227	-11.227	0.000	0.000	0.000	0.000
63	A	65	PRO	0	-0.051	-0.039	25.984	-0.129	-0.129	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.937	-0.941	28.324	-10.415	-10.415	0.000	0.000	0.000	0.000
65	A	67	ARG	1	0.855	0.876	17.049	16.640	16.640	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.018	-0.022	24.284	-0.419	-0.419	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-0.882	-0.931	25.852	-10.304	-10.304	0.000	0.000	0.000	0.000
68	A	70	GLU	-1	-0.878	-0.941	24.413	-12.850	-12.850	0.000	0.000	0.000	0.000
69	A	71	LEU	0	-0.039	-0.033	19.629	-0.254	-0.254	0.000	0.000	0.000	0.000
70	A	72	ARG	1	0.823	0.902	23.436	10.829	10.829	0.000	0.000	0.000	0.000
71	A	73	GLN	0	-0.028	-0.013	26.340	0.132	0.132	0.000	0.000	0.000	0.000
72	A	74	ALA	0	-0.030	-0.003	22.992	0.151	0.151	0.000	0.000	0.000	0.000
73	A	75	HIS	0	0.001	-0.003	18.819	-0.178	-0.178	0.000	0.000	0.000	0.000
74	A	76	PRO	0	0.012	0.015	23.226	-0.114	-0.114	0.000	0.000	0.000	0.000
75	A	77	GLN	0	-0.040	-0.027	24.804	0.513	0.513	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.004	-0.007	20.456	0.298	0.298	0.000	0.000	0.000	0.000
77	A	79	ILE	0	-0.030	-0.006	19.724	-0.486	-0.486	0.000	0.000	0.000	0.000
78	A	80	ALA	0	0.041	0.032	23.313	0.597	0.597	0.000	0.000	0.000	0.000
79	A	81	PRO	0	0.012	-0.020	26.122	-0.299	-0.299	0.000	0.000	0.000	0.000
80	A	82	GLY	0	0.012	0.001	26.881	0.144	0.144	0.000	0.000	0.000	0.000
81	A	83	TYR	0	-0.006	0.002	27.391	0.658	0.658	0.000	0.000	0.000	0.000
82	A	84	HIS	0	0.018	0.009	28.990	-0.240	-0.240	0.000	0.000	0.000	0.000
83	A	85	LEU	0	0.022	0.033	26.317	0.018	0.018	0.000	0.000	0.000	0.000
84	A	86	ASN	0	-0.024	-0.013	30.544	0.431	0.431	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.927	0.934	30.133	9.944	9.944	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.900	0.956	30.892	9.265	9.265	0.000	0.000	0.000	0.000
87	A	89	HIS	0	-0.027	-0.017	27.833	0.024	0.024	0.000	0.000	0.000	0.000
88	A	90	TRP	0	0.012	0.016	22.838	-0.394	-0.394	0.000	0.000	0.000	0.000
89	A	91	VAL	0	0.017	0.010	22.404	0.602	0.602	0.000	0.000	0.000	0.000
90	A	92	THR	0	-0.007	-0.017	23.027	-0.226	-0.226	0.000	0.000	0.000	0.000
91	A	93	VAL	0	0.014	0.011	17.816	0.457	0.457	0.000	0.000	0.000	0.000
92	A	94	THR	0	-0.022	-0.013	19.858	0.084	0.084	0.000	0.000	0.000	0.000
93	A	95	LEU	0	-0.045	-0.015	14.624	-0.521	-0.521	0.000	0.000	0.000	0.000
94	A	96	ASP	-1	-0.772	-0.875	16.296	-16.023	-16.023	0.000	0.000	0.000	0.000
95	A	97	GLY	0	-0.019	0.003	13.479	0.021	0.021	0.000	0.000	0.000	0.000
96	A	98	THR	0	-0.092	-0.058	14.368	0.016	0.016	0.000	0.000	0.000	0.000
97	A	99	VAL	0	0.020	0.012	15.711	0.294	0.294	0.000	0.000	0.000	0.000
98	A	100	PRO	0	-0.002	-0.010	12.941	-1.233	-1.233	0.000	0.000	0.000	0.000
99	A	101	ALA	0	0.064	0.028	8.386	0.008	0.008	0.000	0.000	0.000	0.000
100	A	102	GLU	-1	-0.842	-0.907	8.193	-31.696	-31.696	0.000	0.000	0.000	0.000
101	A	103	LEU	0	-0.011	0.001	9.566	0.550	0.550	0.000	0.000	0.000	0.000
102	A	104	LEU	0	0.000	0.003	11.854	0.843	0.843	0.000	0.000	0.000	0.000
103	A	105	GLY	0	0.035	0.014	9.690	0.740	0.740	0.000	0.000	0.000	0.000
104	A	106	GLU	-1	-0.819	-0.864	10.727	-18.394	-18.394	0.000	0.000	0.000	0.000
105	A	107	LEU	0	0.029	0.007	12.682	1.418	1.418	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.016	0.006	12.055	1.521	1.521	0.000	0.000	0.000	0.000
107	A	109	ARG	1	0.818	0.876	8.509	32.447	32.447	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.005	0.002	14.056	1.202	1.202	0.000	0.000	0.000	0.000
109	A	111	SER	0	-0.029	-0.029	17.191	1.536	1.536	0.000	0.000	0.000	0.000
110	A	112	TYR	0	0.020	-0.012	16.444	0.990	0.990	0.000	0.000	0.000	0.000
111	A	113	LEU	0	0.012	0.014	16.343	1.012	1.012	0.000	0.000	0.000	0.000
112	A	114	LEU	0	-0.026	0.001	19.582	1.018	1.018	0.000	0.000	0.000	0.000
113	A	115	VAL	0	-0.020	-0.022	21.972	0.929	0.929	0.000	0.000	0.000	0.000
114	A	116	THR	0	0.005	-0.002	20.672	0.832	0.832	0.000	0.000	0.000	0.000
115	A	117	LYS	1	0.817	0.919	21.911	14.568	14.568	0.000	0.000	0.000	0.000
116	A	118	LYS	1	0.894	0.948	25.335	10.797	10.797	0.000	0.000	0.000	0.000
117	A	119	GLY	0	-0.032	-0.011	26.882	0.532	0.532	0.000	0.000	0.000	0.000
118	A	120	PHE	0	-0.022	-0.008	25.226	0.336	0.336	0.000	0.000	0.000	0.000
119	A	121	THR	0	-0.007	-0.020	29.008	-0.018	-0.018	0.000	0.000	0.000	0.000
120	A	122	LYS	1	0.963	0.965	29.288	10.138	10.138	0.000	0.000	0.000	0.000
121	A	123	ALA	0	-0.006	0.001	29.807	-0.163	-0.163	0.000	0.000	0.000	0.000
122	A	124	GLU	-1	-0.666	-0.808	29.107	-10.358	-10.358	0.000	0.000	0.000	0.000
123	A	125	ARG	1	0.888	0.946	24.324	11.637	11.637	0.000	0.000	0.000	0.000
124	A	126	LYS	1	0.921	0.969	25.558	9.620	9.620	0.000	0.000	0.000	0.000
125	A	127	GLU	-1	-0.922	-0.938	27.751	-10.402	-10.402	0.000	0.000	0.000	0.000
126	A	128	LEU	0	0.033	0.029	24.528	-0.046	-0.046	0.000	0.000	0.000	0.000
127	A	129	GLY	0	0.001	0.015	23.611	-0.382	-0.382	0.000	0.000	0.000	0.000
128	A	130	LEU	0	-0.053	-0.028	21.239	-0.638	-0.638	0.000	0.000	0.000	0.000
129	A	131	PRO	0	0.001	0.005	17.194	0.646	0.646	0.000	0.000	0.000	0.000
130	A	132	ASP	-1	-0.923	-0.966	20.147	-13.598	-13.598	0.000	0.000	0.000	0.000
131	A	133	SER	0	-0.005	-0.015	17.033	-0.112	-0.112	0.000	0.000	0.000	0.000
132	A	134	LEU	0	0.019	0.001	12.470	0.380	0.380	0.000	0.000	0.000	0.000
133	A	135	GLU	-1	-0.891	-0.933	11.213	-22.786	-22.786	0.000	0.000	0.000	0.000
134	A	136	GLY	0	0.028	0.012	7.416	-0.697	-0.697	0.000	0.000	0.000	0.000
135	A	137	GLY	0	-0.014	0.007	6.541	-4.169	-4.169	0.000	0.000	0.000	0.000
137	A	139	HIS	0	0.006	0.002	6.683	4.307	4.307	0.000	0.000	0.000	0.000
138	A	140	HIS	0	-0.112	-0.058	8.419	2.947	2.947	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LEU)