FMO DATABASE

FMODB ID: 3K5LL

Calculation Name: 2G3A-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2G3A

Chain ID: A

ChEMBL ID:

UniProt ID: Q7CXI0

Base Structure: X-ray

Registration Date: 2025-10-04

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	137
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1078615.677652
FMO2-HF: Nuclear repulsion	1024786.946598
FMO2-HF: Total energy	-53828.731053
FMO2-MP2: Total energy	-53983.798276

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:MET)

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

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.
-26.903	-24.374	0.004	-1.019	-1.514	-0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.854 / q_NPA : 0.914

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	3	PHE	0	0.024	0.015	3.404	-0.345	2.184	0.004	-1.019	-1.514	-0.004
4	A	4	VAL	0	0.007	-0.001	5.982	0.908	0.908	0.000	0.000	0.000	0.000
5	A	5	LEU	0	-0.008	0.006	9.243	0.676	0.676	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.010	-0.016	12.636	0.103	0.103	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.919	-0.954	15.381	-14.748	-14.748	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.028	-0.001	18.321	0.904	0.904	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.000	-0.008	18.055	-0.717	-0.717	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.859	-0.943	15.332	-17.262	-17.262	0.000	0.000	0.000	0.000
11	A	11	ALA	0	0.023	0.019	17.158	-0.430	-0.430	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.888	-0.954	16.669	-14.339	-14.339	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.004	0.011	12.606	-0.717	-0.717	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.909	-0.968	13.398	-15.211	-15.211	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.801	0.883	15.842	14.097	14.097	0.000	0.000	0.000	0.000
16	A	16	ALA	0	-0.009	-0.004	11.846	0.061	0.061	0.000	0.000	0.000	0.000
17	A	17	ILE	0	-0.013	0.001	10.632	-0.987	-0.987	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.898	0.945	12.939	14.226	14.226	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.801	-0.882	16.252	-14.108	-14.108	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.004	0.001	12.134	0.673	0.673	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.006	0.010	14.692	0.358	0.358	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.021	-0.019	16.198	0.730	0.730	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.014	0.008	16.654	0.521	0.521	0.000	0.000	0.000	0.000
24	A	24	TYR	0	0.013	0.016	15.236	0.621	0.621	0.000	0.000	0.000	0.000
25	A	25	ASN	0	-0.013	-0.029	17.481	0.594	0.594	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.024	0.008	20.791	0.505	0.505	0.000	0.000	0.000	0.000
27	A	27	ALA	0	-0.017	-0.013	19.347	0.430	0.430	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.868	0.942	19.110	13.682	13.682	0.000	0.000	0.000	0.000
29	A	29	PHE	0	-0.036	-0.029	21.390	0.310	0.310	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.063	0.055	25.036	0.433	0.433	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.904	-0.954	26.170	-9.709	-9.709	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.043	-0.038	26.584	0.154	0.154	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.863	-0.925	28.663	-8.772	-8.772	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.884	0.949	26.623	10.713	10.713	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.951	0.986	30.676	7.711	7.711	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.886	-0.942	31.797	-9.204	-9.204	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.064	-0.037	34.451	0.247	0.247	0.000	0.000	0.000	0.000
38	A	38	ASN	0	0.033	0.023	34.788	-0.088	-0.088	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.002	-0.001	38.670	0.175	0.175	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.013	-0.002	40.929	-0.058	-0.058	0.000	0.000	0.000	0.000
41	A	41	ILE	0	0.004	-0.005	43.430	0.136	0.136	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.855	0.923	42.335	6.798	6.798	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.005	-0.007	48.358	0.043	0.043	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.856	-0.932	51.475	-5.574	-5.574	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.877	-0.904	50.225	-6.087	-6.087	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.035	-0.028	46.547	-0.138	-0.138	0.000	0.000	0.000	0.000
47	A	47	SER	0	0.014	0.004	45.939	-0.233	-0.233	0.000	0.000	0.000	0.000
48	A	48	VAL	0	-0.075	-0.043	41.246	0.069	0.069	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.017	-0.016	44.214	-0.012	-0.012	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.009	-0.007	42.587	-0.031	-0.031	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.036	-0.005	42.682	0.036	0.036	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.024	-0.013	38.639	-0.026	-0.026	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.025	0.015	33.549	0.041	0.041	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.069	0.025	33.967	-0.060	-0.060	0.000	0.000	0.000	0.000
55	A	55	HIS	0	-0.034	0.006	29.089	-0.026	-0.026	0.000	0.000	0.000	0.000
56	A	56	THR	0	0.034	0.027	33.541	0.144	0.144	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.038	0.013	29.524	-0.133	-0.133	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.846	0.908	24.968	10.732	10.732	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.064	0.046	31.816	0.051	0.051	0.000	0.000	0.000	0.000
60	A	60	TRP	0	-0.040	-0.003	33.437	0.262	0.262	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.026	-0.013	34.342	-0.157	-0.157	0.000	0.000	0.000	0.000
62	A	62	TYR	0	-0.089	-0.056	30.284	-0.072	-0.072	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.030	-0.026	34.008	0.074	0.074	0.000	0.000	0.000	0.000
64	A	64	GLN	0	0.013	0.008	29.376	-0.029	-0.029	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.004	-0.009	32.815	-0.037	-0.037	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.001	-0.003	35.944	0.165	0.165	0.000	0.000	0.000	0.000
67	A	67	PHE	0	-0.001	0.001	39.752	0.010	0.010	0.000	0.000	0.000	0.000
68	A	68	VAL	0	0.022	0.012	41.924	0.075	0.075	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.056	0.019	45.755	-0.012	-0.012	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.868	-0.933	47.476	-6.220	-6.220	0.000	0.000	0.000	0.000
71	A	71	ALA	0	0.035	0.013	49.589	0.066	0.066	0.000	0.000	0.000	0.000
72	A	72	MET	0	0.005	0.017	50.070	0.067	0.067	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.821	0.913	45.592	6.535	6.535	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.010	0.000	51.011	0.108	0.108	0.000	0.000	0.000	0.000
75	A	75	GLN	0	-0.044	-0.024	52.648	0.120	0.120	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.015	0.005	51.965	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	77	ILE	0	0.013	0.006	47.474	-0.082	-0.082	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.041	0.018	45.211	-0.085	-0.085	0.000	0.000	0.000	0.000
79	A	79	PRO	0	0.029	0.001	45.789	-0.091	-0.091	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.975	1.002	47.736	5.920	5.920	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.013	-0.001	43.395	-0.021	-0.021	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.002	0.001	41.466	-0.111	-0.111	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.023	0.024	44.151	-0.057	-0.057	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.013	-0.015	45.828	0.026	0.026	0.000	0.000	0.000	0.000
85	A	85	ALA	0	0.011	0.005	40.567	-0.050	-0.050	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.738	-0.819	41.975	-6.835	-6.835	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.885	-0.931	43.701	-6.204	-6.204	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.824	-0.906	41.171	-7.143	-7.143	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.008	-0.007	39.808	-0.082	-0.082	0.000	0.000	0.000	0.000
90	A	90	ARG	1	0.784	0.866	41.100	6.564	6.564	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.832	0.910	44.032	6.480	6.480	0.000	0.000	0.000	0.000
92	A	92	ARG	1	0.670	0.800	36.809	7.851	7.851	0.000	0.000	0.000	0.000
93	A	93	GLY	0	0.018	0.027	39.794	-0.136	-0.136	0.000	0.000	0.000	0.000
94	A	94	CYS	0	-0.120	-0.051	38.168	-0.182	-0.182	0.000	0.000	0.000	0.000
95	A	95	MET	0	0.015	-0.006	37.694	0.129	0.129	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.016	0.005	39.120	0.122	0.122	0.000	0.000	0.000	0.000
97	A	97	ALA	0	-0.012	0.009	37.545	-0.148	-0.148	0.000	0.000	0.000	0.000
98	A	98	TYR	0	-0.011	-0.012	29.351	0.085	0.085	0.000	0.000	0.000	0.000
99	A	99	ILE	0	-0.013	0.000	35.377	-0.058	-0.058	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.835	-0.896	31.845	-9.404	-9.404	0.000	0.000	0.000	0.000
101	A	101	THR	0	0.013	-0.004	35.055	0.144	0.144	0.000	0.000	0.000	0.000
102	A	102	MET	0	0.052	0.036	34.845	-0.158	-0.158	0.000	0.000	0.000	0.000
103	A	103	ASN	0	-0.002	0.003	36.888	0.255	0.255	0.000	0.000	0.000	0.000
104	A	104	PRO	0	0.096	0.021	40.470	0.021	0.021	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.807	-0.879	43.524	-6.451	-6.451	0.000	0.000	0.000	0.000
106	A	106	ALA	0	-0.028	0.007	41.141	0.109	0.109	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.021	0.020	40.339	0.045	0.045	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.879	0.918	42.598	6.431	6.431	0.000	0.000	0.000	0.000
109	A	109	THR	0	-0.101	-0.063	45.368	0.232	0.232	0.000	0.000	0.000	0.000
110	A	110	TYR	0	0.021	0.005	38.649	0.153	0.153	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.789	-0.885	43.783	-6.910	-6.910	0.000	0.000	0.000	0.000
112	A	112	ARG	1	0.865	0.921	45.776	6.283	6.283	0.000	0.000	0.000	0.000
113	A	113	TYR	0	-0.056	-0.039	44.666	0.156	0.156	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.032	0.017	46.864	0.029	0.029	0.000	0.000	0.000	0.000
115	A	115	PHE	0	-0.061	-0.035	39.127	-0.061	-0.061	0.000	0.000	0.000	0.000
116	A	116	THR	0	-0.036	-0.023	41.683	0.110	0.110	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.850	0.895	39.435	6.984	6.984	0.000	0.000	0.000	0.000
118	A	118	ILE	0	0.008	0.012	34.003	0.069	0.069	0.000	0.000	0.000	0.000
119	A	119	GLY	0	0.013	0.008	34.300	-0.155	-0.155	0.000	0.000	0.000	0.000
120	A	120	SER	0	-0.036	-0.017	34.634	0.163	0.163	0.000	0.000	0.000	0.000
121	A	121	LEU	0	-0.021	0.002	28.945	-0.057	-0.057	0.000	0.000	0.000	0.000
122	A	122	GLY	0	0.018	0.013	33.348	0.109	0.109	0.000	0.000	0.000	0.000
123	A	123	PRO	0	-0.009	0.006	34.524	0.001	0.001	0.000	0.000	0.000	0.000
124	A	124	LEU	0	0.028	-0.001	31.264	-0.302	-0.302	0.000	0.000	0.000	0.000
125	A	125	SER	0	0.021	0.004	32.423	0.151	0.151	0.000	0.000	0.000	0.000
126	A	126	SER	0	-0.041	-0.030	34.263	0.072	0.072	0.000	0.000	0.000	0.000
127	A	127	GLY	0	0.009	0.003	36.937	0.250	0.250	0.000	0.000	0.000	0.000
128	A	128	GLN	0	-0.028	0.009	37.020	-0.066	-0.066	0.000	0.000	0.000	0.000
129	A	129	SER	0	0.010	0.005	35.864	-0.156	-0.156	0.000	0.000	0.000	0.000
130	A	130	ILE	0	0.019	0.012	30.270	0.078	0.078	0.000	0.000	0.000	0.000
131	A	131	THR	0	-0.039	-0.036	34.327	0.071	0.071	0.000	0.000	0.000	0.000
132	A	132	TRP	0	0.028	0.011	29.251	0.058	0.058	0.000	0.000	0.000	0.000
133	A	133	LEU	0	-0.032	-0.030	35.144	0.187	0.187	0.000	0.000	0.000	0.000
134	A	134	GLU	-1	-0.798	-0.888	37.116	-8.034	-8.034	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.840	0.906	38.656	6.882	6.882	0.000	0.000	0.000	0.000
136	A	136	ARG	1	0.881	0.927	37.685	7.629	7.629	0.000	0.000	0.000	0.000
137	A	137	PHE	-1	-0.842	-0.893	41.276	-6.534	-6.534	0.000	0.000	0.000	0.000

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