FMO DATABASE

FMODB ID: G7JY1

Calculation Name: 4V6W-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4V6W

Chain ID: A

ChEMBL ID:

UniProt ID: P13060

Base Structure: ElectronMicroscopy

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	Original chain id is "AN", which converted from A;

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	150
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1299890.569056
FMO2-HF: Nuclear repulsion	1241240.435309
FMO2-HF: Total energy	-58650.133748
FMO2-MP2: Total energy	-58824.180192

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:2:GLY)

Summations of interaction energy for fragment #1(A:2:GLY)

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.
259.253	262.846	0.64	-2.156	-2.078	-0.023

Interaction energy analysis for fragmet #1(A:2:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.892 / q_NPA : 0.934

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	4	MET	0	0.064	0.017	3.854	6.929	7.742	-0.003	-0.301	-0.510	0.000
7	A	8	GLY	0	-0.015	-0.003	4.871	-2.284	-2.176	-0.001	-0.026	-0.081	0.000
8	A	9	LYS	1	0.930	0.931	2.534	18.558	21.028	0.646	-1.794	-1.322	-0.023
9	A	10	GLY	0	0.009	0.024	3.806	-0.767	-0.586	-0.001	-0.030	-0.150	0.000
10	A	11	ILE	0	-0.037	-0.011	4.768	-3.214	-3.193	-0.001	-0.005	-0.015	0.000
4	A	5	HIS	0	0.008	0.022	5.688	5.098	5.098	0.000	0.000	0.000	0.000
5	A	6	ALA	0	0.039	0.031	7.088	4.435	4.435	0.000	0.000	0.000	0.000
6	A	7	PRO	0	0.092	0.054	5.744	-8.023	-8.023	0.000	0.000	0.000	0.000
11	A	12	SER	0	0.039	0.012	6.993	3.662	3.662	0.000	0.000	0.000	0.000
12	A	13	GLN	0	-0.023	-0.021	9.012	-2.292	-2.292	0.000	0.000	0.000	0.000
13	A	14	SER	0	-0.017	-0.007	12.386	0.897	0.897	0.000	0.000	0.000	0.000
14	A	15	ALA	0	0.068	0.045	16.003	-0.098	-0.098	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.058	-0.025	17.971	0.651	0.651	0.000	0.000	0.000	0.000
16	A	17	PRO	0	0.008	0.005	20.540	0.108	0.108	0.000	0.000	0.000	0.000
17	A	18	TYR	0	0.059	0.019	23.984	0.059	0.059	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.992	0.994	25.522	9.786	9.786	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.979	0.971	22.454	12.839	12.839	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.012	-0.002	28.114	0.132	0.132	0.000	0.000	0.000	0.000
21	A	22	VAL	0	-0.025	0.024	30.012	0.259	0.259	0.000	0.000	0.000	0.000
22	A	23	PRO	0	-0.029	-0.026	30.612	-0.341	-0.341	0.000	0.000	0.000	0.000
23	A	24	SER	0	0.063	-0.004	33.411	0.044	0.044	0.000	0.000	0.000	0.000
24	A	25	TRP	0	0.034	0.030	33.685	0.272	0.272	0.000	0.000	0.000	0.000
25	A	26	LEU	0	-0.055	-0.021	33.844	0.183	0.183	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.988	0.991	37.592	7.551	7.551	0.000	0.000	0.000	0.000
27	A	28	LEU	0	0.018	0.033	37.269	0.105	0.105	0.000	0.000	0.000	0.000
28	A	29	ASN	0	0.064	0.029	37.814	-0.225	-0.225	0.000	0.000	0.000	0.000
29	A	30	ALA	0	0.010	-0.006	35.621	-0.196	-0.196	0.000	0.000	0.000	0.000
30	A	31	ASP	-1	-0.953	-0.984	36.165	-7.973	-7.973	0.000	0.000	0.000	0.000
31	A	32	ASP	-1	-0.861	-0.923	38.364	-8.168	-8.168	0.000	0.000	0.000	0.000
32	A	33	VAL	0	0.042	0.000	33.081	-0.144	-0.144	0.000	0.000	0.000	0.000
33	A	34	LYS	1	0.824	0.910	33.686	8.818	8.818	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.876	-0.939	35.269	-8.072	-8.072	0.000	0.000	0.000	0.000
35	A	36	GLN	0	0.065	0.037	34.846	-0.198	-0.198	0.000	0.000	0.000	0.000
36	A	37	ILE	0	-0.039	-0.027	30.256	-0.222	-0.222	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.926	0.965	32.888	8.010	8.010	0.000	0.000	0.000	0.000
38	A	39	LYS	1	0.946	0.983	35.613	7.733	7.733	0.000	0.000	0.000	0.000
39	A	40	LEU	0	0.007	-0.008	31.941	0.043	0.043	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.012	0.001	31.426	-0.144	-0.144	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.932	0.963	32.357	8.035	8.035	0.000	0.000	0.000	0.000
42	A	43	LYS	1	0.947	0.993	34.411	8.849	8.849	0.000	0.000	0.000	0.000
43	A	44	GLY	0	0.062	0.040	32.107	-0.041	-0.041	0.000	0.000	0.000	0.000
44	A	45	LEU	0	-0.096	-0.035	28.795	-0.419	-0.419	0.000	0.000	0.000	0.000
45	A	46	THR	0	0.010	-0.026	23.601	0.148	0.148	0.000	0.000	0.000	0.000
46	A	47	PRO	0	0.014	-0.024	23.444	0.010	0.010	0.000	0.000	0.000	0.000
47	A	48	SER	0	-0.059	-0.049	20.472	-0.168	-0.168	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.945	0.977	22.550	11.960	11.960	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.012	0.010	25.427	0.226	0.226	0.000	0.000	0.000	0.000
50	A	51	GLY	0	-0.026	-0.024	24.398	0.207	0.207	0.000	0.000	0.000	0.000
51	A	52	ILE	0	-0.034	-0.012	22.250	-0.043	-0.043	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.025	0.021	25.240	0.211	0.211	0.000	0.000	0.000	0.000
53	A	54	LEU	0	0.027	0.012	28.882	0.290	0.290	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.824	0.919	22.674	12.956	12.956	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.862	-0.933	27.350	-11.416	-11.416	0.000	0.000	0.000	0.000
56	A	57	SER	0	-0.038	-0.013	30.163	0.296	0.296	0.000	0.000	0.000	0.000
57	A	58	HIS	0	-0.027	0.002	32.973	0.048	0.048	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.058	0.041	32.378	0.228	0.228	0.000	0.000	0.000	0.000
59	A	60	VAL	0	-0.042	-0.043	29.410	0.103	0.103	0.000	0.000	0.000	0.000
60	A	61	ALA	0	0.002	0.004	28.382	-0.402	-0.402	0.000	0.000	0.000	0.000
61	A	62	GLN	0	0.046	0.008	23.374	-0.954	-0.954	0.000	0.000	0.000	0.000
62	A	63	VAL	0	0.052	0.023	26.528	0.275	0.275	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.850	0.911	19.392	14.655	14.655	0.000	0.000	0.000	0.000
64	A	65	PHE	0	-0.002	0.006	25.150	-0.127	-0.127	0.000	0.000	0.000	0.000
65	A	66	VAL	0	0.069	0.056	29.070	0.238	0.238	0.000	0.000	0.000	0.000
66	A	67	ASN	0	0.073	0.023	30.909	0.198	0.198	0.000	0.000	0.000	0.000
67	A	68	GLY	0	0.051	0.037	29.440	-0.302	-0.302	0.000	0.000	0.000	0.000
68	A	69	ASN	0	-0.079	-0.029	28.167	-0.604	-0.604	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.967	0.970	22.629	12.473	12.473	0.000	0.000	0.000	0.000
70	A	71	ILE	0	0.093	0.046	24.068	0.149	0.149	0.000	0.000	0.000	0.000
71	A	72	LEU	0	0.040	0.023	22.387	0.329	0.329	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.939	0.964	21.375	13.276	13.276	0.000	0.000	0.000	0.000
73	A	74	ILE	0	0.020	0.023	28.099	0.392	0.392	0.000	0.000	0.000	0.000
74	A	75	MET	0	0.027	0.012	28.643	0.118	0.118	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.923	0.963	28.819	9.991	9.991	0.000	0.000	0.000	0.000
76	A	77	SER	0	-0.066	-0.058	30.825	0.215	0.215	0.000	0.000	0.000	0.000
77	A	78	VAL	0	-0.010	0.010	33.791	0.260	0.260	0.000	0.000	0.000	0.000
78	A	79	GLY	0	0.047	0.028	34.495	0.158	0.158	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.022	-0.007	31.993	-0.014	-0.014	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.842	0.940	25.385	11.390	11.390	0.000	0.000	0.000	0.000
81	A	82	PRO	0	0.028	0.024	26.191	0.182	0.182	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.867	-0.937	27.748	-10.848	-10.848	0.000	0.000	0.000	0.000
83	A	84	ILE	0	0.000	0.006	23.196	-0.395	-0.395	0.000	0.000	0.000	0.000
84	A	85	PRO	0	-0.037	-0.015	20.927	0.063	0.063	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.701	-0.849	20.389	-14.076	-14.076	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.814	-0.867	16.194	-17.014	-17.014	0.000	0.000	0.000	0.000
87	A	88	LEU	0	0.039	-0.009	17.666	-0.443	-0.443	0.000	0.000	0.000	0.000
88	A	89	TYR	0	-0.001	0.022	19.520	-0.297	-0.297	0.000	0.000	0.000	0.000
89	A	90	HIS	0	-0.036	-0.035	19.177	0.424	0.424	0.000	0.000	0.000	0.000
90	A	91	MET	0	-0.104	-0.046	14.266	-0.410	-0.410	0.000	0.000	0.000	0.000
91	A	92	ILE	0	0.040	0.017	18.421	-0.053	-0.053	0.000	0.000	0.000	0.000
92	A	93	LYS	1	1.009	1.014	21.823	13.003	13.003	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.875	0.930	18.257	15.862	15.862	0.000	0.000	0.000	0.000
94	A	95	ALA	0	0.021	0.008	19.948	0.185	0.185	0.000	0.000	0.000	0.000
95	A	96	VAL	0	0.028	0.029	21.417	0.261	0.261	0.000	0.000	0.000	0.000
96	A	97	ALA	0	-0.029	-0.005	23.802	0.406	0.406	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.020	-0.021	19.596	0.286	0.286	0.000	0.000	0.000	0.000
98	A	99	ARG	1	0.917	0.944	23.912	12.829	12.829	0.000	0.000	0.000	0.000
99	A	100	LYS	1	1.036	1.017	25.777	10.218	10.218	0.000	0.000	0.000	0.000
100	A	101	HIS	0	-0.078	-0.023	24.814	0.790	0.790	0.000	0.000	0.000	0.000
101	A	102	LEU	0	-0.009	-0.003	23.392	0.294	0.294	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.891	-0.933	27.926	-10.163	-10.163	0.000	0.000	0.000	0.000
103	A	104	ARG	1	0.864	0.932	29.451	10.763	10.763	0.000	0.000	0.000	0.000
104	A	105	ASN	0	-0.003	-0.005	29.252	0.501	0.501	0.000	0.000	0.000	0.000
105	A	106	ARG	1	0.929	0.950	29.418	9.141	9.141	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.940	0.958	29.761	10.008	10.008	0.000	0.000	0.000	0.000
107	A	108	ASP	-1	-0.750	-0.860	24.448	-13.738	-13.738	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.937	0.959	24.402	11.810	11.810	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.781	-0.861	18.772	-18.240	-18.240	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.076	0.028	19.908	-0.811	-0.811	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.904	0.926	20.979	12.145	12.145	0.000	0.000	0.000	0.000
112	A	113	PHE	0	0.016	0.024	14.492	-0.241	-0.241	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.828	0.882	15.097	18.316	18.316	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.005	-0.002	17.124	-0.613	-0.613	0.000	0.000	0.000	0.000
115	A	116	ILE	0	0.072	0.044	17.124	-0.334	-0.334	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.027	-0.010	12.368	-0.874	-0.874	0.000	0.000	0.000	0.000
117	A	118	VAL	0	-0.067	-0.034	14.201	-1.411	-1.411	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.782	-0.876	16.510	-13.739	-13.739	0.000	0.000	0.000	0.000
119	A	120	SER	0	0.028	0.024	14.492	-0.267	-0.267	0.000	0.000	0.000	0.000
120	A	121	ARG	1	0.842	0.908	12.051	23.397	23.397	0.000	0.000	0.000	0.000
121	A	122	ILE	0	0.026	0.025	14.045	-0.120	-0.120	0.000	0.000	0.000	0.000
122	A	123	HIS	0	0.014	0.001	17.390	-0.281	-0.281	0.000	0.000	0.000	0.000
123	A	124	ARG	1	0.898	0.957	9.218	26.606	26.606	0.000	0.000	0.000	0.000
124	A	125	LEU	0	-0.013	0.001	12.693	0.215	0.215	0.000	0.000	0.000	0.000
125	A	126	ALA	0	0.070	0.019	15.558	0.596	0.596	0.000	0.000	0.000	0.000
126	A	127	ARG	1	0.911	0.962	16.447	17.802	17.802	0.000	0.000	0.000	0.000
127	A	128	TYR	0	0.054	0.045	15.807	0.729	0.729	0.000	0.000	0.000	0.000
128	A	129	TYR	0	-0.050	-0.075	17.558	0.769	0.769	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.883	0.953	20.708	13.582	13.582	0.000	0.000	0.000	0.000
130	A	131	THR	0	-0.013	-0.002	20.363	0.487	0.487	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.815	0.908	19.637	14.827	14.827	0.000	0.000	0.000	0.000
132	A	133	SER	0	0.028	0.024	23.387	0.454	0.454	0.000	0.000	0.000	0.000
133	A	134	VAL	0	-0.080	-0.037	22.635	0.304	0.304	0.000	0.000	0.000	0.000
134	A	135	LEU	0	-0.027	-0.007	22.100	-0.090	-0.090	0.000	0.000	0.000	0.000
135	A	136	PRO	0	0.072	0.039	25.582	-0.100	-0.100	0.000	0.000	0.000	0.000
136	A	137	PRO	0	0.077	0.017	27.205	-0.448	-0.448	0.000	0.000	0.000	0.000
137	A	138	ASN	0	-0.022	-0.021	27.140	0.309	0.309	0.000	0.000	0.000	0.000
138	A	139	TRP	0	0.072	0.054	22.251	-0.256	-0.256	0.000	0.000	0.000	0.000
139	A	140	LYS	1	0.923	0.948	24.646	10.674	10.674	0.000	0.000	0.000	0.000
140	A	141	TYR	0	0.023	0.019	22.229	0.141	0.141	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.872	-0.950	24.277	-10.763	-10.763	0.000	0.000	0.000	0.000
142	A	143	SER	0	0.017	0.004	26.252	0.210	0.210	0.000	0.000	0.000	0.000
143	A	144	SER	0	0.047	0.029	27.307	0.013	0.013	0.000	0.000	0.000	0.000
144	A	145	THR	0	0.055	0.029	29.221	0.013	0.013	0.000	0.000	0.000	0.000
145	A	146	ALA	0	-0.024	-0.013	25.421	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	147	SER	0	-0.045	-0.056	27.339	-0.146	-0.146	0.000	0.000	0.000	0.000
147	A	148	ALA	0	0.010	0.012	29.486	0.094	0.094	0.000	0.000	0.000	0.000
148	A	149	LEU	0	0.005	0.006	26.311	-0.018	-0.018	0.000	0.000	0.000	0.000
149	A	150	VAL	0	-0.096	-0.048	25.595	-0.347	-0.347	0.000	0.000	0.000	0.000
150	A	151	ALA	-1	-0.906	-0.928	28.090	-9.922	-9.922	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:2:GLY)