FMO DATABASE

FMODB ID: N6N8Q

Calculation Name: 4V6W-A-Other547

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: 2025-10-06

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	187
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1839707.011947
FMO2-HF: Nuclear repulsion	1765490.794213
FMO2-HF: Total energy	-74216.217733
FMO2-MP2: Total energy	-74435.959177

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.
204.413	205.361	-0.009	-0.237	-0.702	0

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 : 0.870 / q_NPA : 0.919

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].
3	A	4	ASP	-1	-0.860	-0.914	3.813	-32.826	-31.878	-0.009	-0.237	-0.702
4	A	5	ILE	0	0.046	0.014	6.470	3.562	3.562	0.000	0.000	0.000
5	A	6	ASN	0	-0.088	-0.037	7.353	4.233	4.233	0.000	0.000	0.000
6	A	7	HIS	0	0.030	0.030	9.203	-0.675	-0.675	0.000	0.000	0.000
7	A	8	LYS	1	0.887	0.929	11.125	18.387	18.387	0.000	0.000	0.000
8	A	9	TYR	0	-0.038	-0.014	14.820	0.269	0.269	0.000	0.000	0.000
9	A	10	ASP	-1	-0.756	-0.870	13.343	-21.013	-21.013	0.000	0.000	0.000
10	A	11	ARG	1	0.928	0.940	15.685	17.594	17.594	0.000	0.000	0.000
11	A	12	LYS	1	0.942	0.976	19.943	13.944	13.944	0.000	0.000	0.000
12	A	13	VAL	0	0.100	0.038	22.604	0.475	0.475	0.000	0.000	0.000
13	A	14	ARG	1	0.828	0.915	25.972	10.139	10.139	0.000	0.000	0.000
14	A	15	ARG	1	0.887	0.931	27.944	9.044	9.044	0.000	0.000	0.000
15	A	16	THR	0	0.044	0.012	27.964	0.076	0.076	0.000	0.000	0.000
16	A	17	GLU	-1	-0.777	-0.874	30.711	-8.642	-8.642	0.000	0.000	0.000
17	A	18	PRO	0	-0.035	-0.016	33.996	-0.148	-0.148	0.000	0.000	0.000
18	A	19	LYS	1	0.945	0.986	32.138	9.445	9.445	0.000	0.000	0.000
19	A	20	SER	0	-0.048	-0.043	36.110	0.133	0.133	0.000	0.000	0.000
20	A	21	GLN	0	0.069	0.029	39.207	-0.225	-0.225	0.000	0.000	0.000
21	A	22	ASP	-1	-0.852	-0.915	41.652	-6.831	-6.831	0.000	0.000	0.000
22	A	23	VAL	0	0.071	0.026	43.378	-0.178	-0.178	0.000	0.000	0.000
23	A	24	TYR	0	0.053	0.027	45.363	-0.071	-0.071	0.000	0.000	0.000
24	A	25	LEU	0	-0.045	-0.021	40.933	-0.085	-0.085	0.000	0.000	0.000
25	A	26	ARG	1	0.858	0.904	37.466	8.098	8.098	0.000	0.000	0.000
26	A	27	LEU	0	0.042	0.031	41.972	-0.158	-0.158	0.000	0.000	0.000
27	A	28	LEU	0	0.032	0.021	44.655	-0.035	-0.035	0.000	0.000	0.000
28	A	29	VAL	0	-0.032	-0.021	37.864	-0.100	-0.100	0.000	0.000	0.000
29	A	30	LYS	1	0.945	0.977	40.337	7.324	7.324	0.000	0.000	0.000
30	A	31	LEU	0	0.039	0.038	41.346	-0.076	-0.076	0.000	0.000	0.000
31	A	32	TYR	0	0.061	-0.005	41.796	-0.059	-0.059	0.000	0.000	0.000
32	A	33	ARG	1	0.914	0.949	31.638	9.415	9.415	0.000	0.000	0.000
33	A	34	PHE	0	0.036	0.028	38.736	-0.208	-0.208	0.000	0.000	0.000
34	A	35	LEU	0	0.051	0.017	41.214	-0.063	-0.063	0.000	0.000	0.000
35	A	36	GLN	0	-0.036	-0.008	34.781	-0.029	-0.029	0.000	0.000	0.000
36	A	37	ARG	1	0.970	0.982	35.825	8.737	8.737	0.000	0.000	0.000
37	A	38	ARG	1	0.943	0.979	38.532	7.446	7.446	0.000	0.000	0.000
38	A	39	THR	0	-0.006	-0.016	41.991	0.191	0.191	0.000	0.000	0.000
39	A	40	ASN	0	0.062	0.040	40.081	0.116	0.116	0.000	0.000	0.000
40	A	41	LYS	1	0.851	0.929	40.270	6.937	6.937	0.000	0.000	0.000
41	A	42	LYS	1	0.999	0.972	38.156	8.167	8.167	0.000	0.000	0.000
42	A	43	PHE	0	0.074	0.037	41.011	-0.184	-0.184	0.000	0.000	0.000
43	A	44	ASN	0	0.081	0.027	41.949	0.043	0.043	0.000	0.000	0.000
44	A	45	ARG	1	0.940	0.981	33.799	9.022	9.022	0.000	0.000	0.000
45	A	46	ILE	0	-0.092	-0.038	37.433	-0.239	-0.239	0.000	0.000	0.000
46	A	47	ILE	0	0.024	0.024	39.209	-0.105	-0.105	0.000	0.000	0.000
47	A	48	LEU	0	0.038	0.039	36.014	-0.005	-0.005	0.000	0.000	0.000
48	A	49	LYS	1	0.961	0.971	33.583	9.291	9.291	0.000	0.000	0.000
49	A	50	ARG	1	0.796	0.902	36.754	7.359	7.359	0.000	0.000	0.000
50	A	51	LEU	0	0.058	0.027	39.973	0.124	0.124	0.000	0.000	0.000
51	A	52	PHE	0	0.000	0.000	33.014	0.011	0.011	0.000	0.000	0.000
52	A	53	MET	0	-0.088	-0.010	36.789	-0.301	-0.301	0.000	0.000	0.000
53	A	54	SER	0	0.004	0.013	37.383	0.018	0.018	0.000	0.000	0.000
54	A	55	LYS	1	1.023	0.996	39.142	6.858	6.858	0.000	0.000	0.000
55	A	56	ILE	0	0.033	0.021	39.236	0.136	0.136	0.000	0.000	0.000
56	A	57	ASN	0	0.000	-0.018	36.772	-0.203	-0.203	0.000	0.000	0.000
57	A	58	ARG	1	0.914	0.988	40.537	7.495	7.495	0.000	0.000	0.000
58	A	59	PRO	0	-0.007	0.007	43.529	0.101	0.101	0.000	0.000	0.000
59	A	60	PRO	0	0.029	0.015	46.399	-0.026	-0.026	0.000	0.000	0.000
60	A	61	LEU	0	-0.066	-0.041	49.804	-0.031	-0.031	0.000	0.000	0.000
61	A	62	SER	0	0.014	0.006	51.901	0.021	0.021	0.000	0.000	0.000
62	A	63	LEU	0	0.068	0.050	55.637	-0.070	-0.070	0.000	0.000	0.000
63	A	64	GLN	0	0.058	0.030	58.311	0.065	0.065	0.000	0.000	0.000
64	A	65	ARG	1	0.883	0.937	50.399	6.250	6.250	0.000	0.000	0.000
65	A	66	ILE	0	0.014	0.004	54.849	-0.060	-0.060	0.000	0.000	0.000
66	A	67	ALA	0	0.060	0.032	56.783	0.013	0.013	0.000	0.000	0.000
67	A	68	ARG	1	0.893	0.950	56.675	5.668	5.668	0.000	0.000	0.000
68	A	69	PHE	0	-0.011	-0.018	51.103	-0.018	-0.018	0.000	0.000	0.000
69	A	70	PHE	0	0.064	0.029	56.926	-0.024	-0.024	0.000	0.000	0.000
70	A	71	LYS	1	0.929	0.979	60.221	5.103	5.103	0.000	0.000	0.000
71	A	72	ALA	0	-0.056	-0.021	56.385	0.006	0.006	0.000	0.000	0.000
72	A	73	ALA	0	0.087	0.036	58.390	0.049	0.049	0.000	0.000	0.000
73	A	74	ASN	0	-0.002	-0.011	56.723	-0.024	-0.024	0.000	0.000	0.000
74	A	75	GLN	0	0.038	0.019	55.415	-0.168	-0.168	0.000	0.000	0.000
75	A	76	PRO	0	-0.004	0.003	58.076	-0.018	-0.018	0.000	0.000	0.000
76	A	77	GLU	-1	-0.914	-0.957	59.825	-5.312	-5.312	0.000	0.000	0.000
77	A	78	SER	0	-0.071	-0.023	54.951	-0.088	-0.088	0.000	0.000	0.000
78	A	79	THR	0	0.021	0.005	54.417	0.058	0.058	0.000	0.000	0.000
79	A	80	ILE	0	-0.019	-0.019	52.704	-0.165	-0.165	0.000	0.000	0.000
80	A	81	VAL	0	0.015	0.008	47.774	-0.006	-0.006	0.000	0.000	0.000
81	A	82	VAL	0	-0.016	-0.017	49.139	-0.117	-0.117	0.000	0.000	0.000
82	A	83	VAL	0	0.034	0.019	43.525	0.005	0.005	0.000	0.000	0.000
83	A	84	GLY	0	-0.036	-0.048	45.510	-0.204	-0.204	0.000	0.000	0.000
84	A	85	THR	0	-0.009	0.020	47.618	0.033	0.033	0.000	0.000	0.000
85	A	86	VAL	0	0.041	0.014	50.837	-0.048	-0.048	0.000	0.000	0.000
86	A	87	THR	0	-0.001	-0.003	53.779	0.017	0.017	0.000	0.000	0.000
87	A	88	ASP	-1	-0.787	-0.912	56.149	-5.200	-5.200	0.000	0.000	0.000
88	A	89	ASP	-1	-0.894	-0.933	58.734	-5.507	-5.507	0.000	0.000	0.000
89	A	90	ALA	0	0.072	0.032	60.937	0.038	0.038	0.000	0.000	0.000
90	A	91	ARG	1	0.867	0.914	58.630	5.403	5.403	0.000	0.000	0.000
91	A	92	LEU	0	-0.041	-0.004	61.837	0.029	0.029	0.000	0.000	0.000
92	A	93	LEU	0	0.059	0.030	64.999	0.021	0.021	0.000	0.000	0.000
93	A	94	VAL	0	0.031	0.019	67.663	0.033	0.033	0.000	0.000	0.000
94	A	95	VAL	0	-0.044	-0.028	62.962	-0.092	-0.092	0.000	0.000	0.000
95	A	96	PRO	0	-0.017	0.000	61.940	0.055	0.055	0.000	0.000	0.000
96	A	97	LYS	1	1.006	0.979	63.390	4.597	4.597	0.000	0.000	0.000
97	A	98	LEU	0	-0.016	0.022	57.462	-0.019	-0.019	0.000	0.000	0.000
98	A	99	THR	0	0.018	0.015	57.404	0.027	0.027	0.000	0.000	0.000
99	A	100	VAL	0	-0.030	-0.013	54.854	-0.099	-0.099	0.000	0.000	0.000
100	A	101	CYS	0	-0.001	0.019	52.157	0.015	0.015	0.000	0.000	0.000
101	A	102	ALA	0	-0.008	-0.019	50.729	-0.124	-0.124	0.000	0.000	0.000
102	A	103	LEU	0	-0.057	-0.008	46.304	-0.013	-0.013	0.000	0.000	0.000
103	A	104	HIS	0	0.027	-0.006	49.545	0.011	0.011	0.000	0.000	0.000
104	A	105	VAL	0	0.034	0.026	52.164	-0.048	-0.048	0.000	0.000	0.000
105	A	106	THR	0	-0.008	-0.019	55.383	0.071	0.071	0.000	0.000	0.000
106	A	107	GLN	0	0.049	0.024	57.508	-0.047	-0.047	0.000	0.000	0.000
107	A	108	THR	0	0.119	0.068	60.849	0.036	0.036	0.000	0.000	0.000
108	A	109	ALA	0	0.010	-0.002	58.555	0.037	0.037	0.000	0.000	0.000
109	A	110	ARG	1	0.901	0.940	55.622	5.624	5.624	0.000	0.000	0.000
110	A	111	GLU	-1	-0.879	-0.925	61.452	-4.874	-4.874	0.000	0.000	0.000
111	A	112	ARG	1	0.861	0.919	63.210	4.992	4.992	0.000	0.000	0.000
112	A	113	ILE	0	-0.061	-0.033	58.556	0.006	0.006	0.000	0.000	0.000
113	A	114	LEU	0	0.020	0.007	63.074	0.033	0.033	0.000	0.000	0.000
114	A	115	LYS	1	0.965	0.991	65.629	4.682	4.682	0.000	0.000	0.000
115	A	116	ALA	0	-0.055	-0.004	65.250	0.061	0.061	0.000	0.000	0.000
116	A	117	GLY	0	-0.017	0.001	67.258	0.054	0.054	0.000	0.000	0.000
117	A	118	GLY	0	0.013	-0.001	63.367	-0.001	-0.001	0.000	0.000	0.000
118	A	119	GLU	-1	-0.793	-0.872	60.228	-5.333	-5.333	0.000	0.000	0.000
119	A	120	VAL	0	-0.041	-0.036	57.099	-0.099	-0.099	0.000	0.000	0.000
120	A	121	LEU	0	-0.007	0.009	55.026	0.003	0.003	0.000	0.000	0.000
121	A	122	THR	0	0.012	-0.023	52.503	-0.074	-0.074	0.000	0.000	0.000
122	A	123	PHE	0	0.009	-0.030	48.089	-0.033	-0.033	0.000	0.000	0.000
123	A	124	ASP	-1	-0.844	-0.901	49.941	-6.262	-6.262	0.000	0.000	0.000
124	A	125	GLN	0	0.097	0.046	50.794	-0.013	-0.013	0.000	0.000	0.000
125	A	126	LEU	0	-0.027	-0.010	49.463	0.024	0.024	0.000	0.000	0.000
126	A	127	ALA	0	-0.076	-0.052	48.513	-0.012	-0.012	0.000	0.000	0.000
127	A	128	LEU	0	0.031	0.022	50.256	-0.047	-0.047	0.000	0.000	0.000
128	A	129	ARG	1	0.855	0.898	53.406	5.550	5.550	0.000	0.000	0.000
129	A	130	SER	0	-0.033	-0.016	52.161	0.082	0.082	0.000	0.000	0.000
130	A	131	PRO	0	0.065	0.061	49.177	-0.171	-0.171	0.000	0.000	0.000
131	A	132	THR	0	-0.015	-0.027	47.891	-0.240	-0.240	0.000	0.000	0.000
132	A	133	GLY	0	-0.026	-0.014	48.759	-0.061	-0.061	0.000	0.000	0.000
133	A	134	LYS	1	0.988	0.997	49.633	5.762	5.762	0.000	0.000	0.000
134	A	135	ASN	0	0.059	0.030	53.131	-0.008	-0.008	0.000	0.000	0.000
135	A	136	THR	0	-0.039	0.004	50.128	-0.011	-0.011	0.000	0.000	0.000
136	A	137	LEU	0	0.062	0.020	49.792	-0.054	-0.054	0.000	0.000	0.000
137	A	138	LEU	0	-0.050	-0.010	43.247	0.001	0.001	0.000	0.000	0.000
138	A	139	LEU	0	0.023	0.025	47.406	-0.085	-0.085	0.000	0.000	0.000
139	A	140	GLN	0	-0.029	-0.035	40.994	-0.224	-0.224	0.000	0.000	0.000
140	A	141	GLY	0	0.018	0.025	46.059	0.131	0.131	0.000	0.000	0.000
141	A	142	ARG	1	0.917	0.953	45.657	6.117	6.117	0.000	0.000	0.000
142	A	143	ARG	1	0.938	0.948	37.978	8.089	8.089	0.000	0.000	0.000
143	A	144	THR	0	0.055	0.018	44.009	-0.072	-0.072	0.000	0.000	0.000
144	A	145	ALA	0	0.014	0.019	45.483	0.038	0.038	0.000	0.000	0.000
145	A	146	ARG	1	0.909	0.956	39.092	7.892	7.892	0.000	0.000	0.000
146	A	147	THR	0	0.069	0.009	46.057	-0.043	-0.043	0.000	0.000	0.000
147	A	148	ALA	0	0.013	0.005	41.869	-0.018	-0.018	0.000	0.000	0.000
148	A	149	CYS	0	-0.080	-0.030	41.979	-0.213	-0.213	0.000	0.000	0.000
149	A	150	LYS	1	0.977	1.015	43.062	6.358	6.358	0.000	0.000	0.000
150	A	151	HIS	0	-0.002	0.023	43.319	0.036	0.036	0.000	0.000	0.000
151	A	152	PHE	0	-0.054	-0.010	38.714	-0.156	-0.156	0.000	0.000	0.000
152	A	153	GLY	0	0.058	0.029	39.760	-0.002	-0.002	0.000	0.000	0.000
153	A	154	LYS	0	0.009	0.004	40.382	0.159	0.159	0.000	0.000	0.000
154	A	155	ALA	0	0.059	0.037	40.393	-0.098	-0.098	0.000	0.000	0.000
155	A	156	PRO	0	-0.055	-0.054	42.086	0.172	0.172	0.000	0.000	0.000
156	A	157	GLY	0	0.093	0.052	44.982	-0.026	-0.026	0.000	0.000	0.000
157	A	158	VAL	0	0.000	0.005	40.645	0.032	0.032	0.000	0.000	0.000
158	A	159	PRO	0	0.003	-0.010	44.046	-0.047	-0.047	0.000	0.000	0.000
159	A	160	HIS	0	0.072	0.064	41.814	0.050	0.050	0.000	0.000	0.000
160	A	161	SER	0	-0.038	-0.027	44.079	0.208	0.208	0.000	0.000	0.000
161	A	162	HIS	0	-0.008	-0.010	46.242	0.027	0.027	0.000	0.000	0.000
162	A	163	THR	0	-0.027	-0.023	44.588	0.028	0.028	0.000	0.000	0.000
163	A	164	ARG	1	0.886	0.937	46.836	6.126	6.126	0.000	0.000	0.000
164	A	165	PRO	0	0.061	0.045	47.312	-0.152	-0.152	0.000	0.000	0.000
165	A	166	TYR	0	0.020	0.001	41.386	0.075	0.075	0.000	0.000	0.000
166	A	167	VAL	0	-0.019	0.001	47.775	0.039	0.039	0.000	0.000	0.000
167	A	168	ARG	1	0.983	0.982	51.491	6.075	6.075	0.000	0.000	0.000
168	A	169	SER	0	0.007	0.014	53.203	0.103	0.103	0.000	0.000	0.000
169	A	170	LYS	1	0.939	0.961	54.806	5.653	5.653	0.000	0.000	0.000
170	A	171	GLY	0	0.097	0.045	58.094	0.093	0.093	0.000	0.000	0.000
171	A	172	ARG	1	1.000	1.010	59.934	4.789	4.789	0.000	0.000	0.000
172	A	173	LYS	1	0.976	0.979	60.614	5.152	5.152	0.000	0.000	0.000
173	A	174	PHE	0	0.043	0.024	56.248	-0.068	-0.068	0.000	0.000	0.000
174	A	175	GLU	-1	-0.871	-0.953	50.762	-6.303	-6.303	0.000	0.000	0.000
175	A	176	ARG	1	0.895	0.930	54.954	5.262	5.262	0.000	0.000	0.000
176	A	177	ALA	0	0.028	0.020	57.065	0.040	0.040	0.000	0.000	0.000
177	A	178	ARG	1	0.995	0.981	50.399	6.095	6.095	0.000	0.000	0.000
178	A	179	GLY	0	0.035	0.040	51.869	-0.099	-0.099	0.000	0.000	0.000
179	A	180	ARG	1	0.829	0.915	52.035	5.851	5.851	0.000	0.000	0.000
180	A	181	ARG	1	0.829	0.872	54.338	5.267	5.267	0.000	0.000	0.000
181	A	182	SER	0	0.076	0.021	56.900	-0.057	-0.057	0.000	0.000	0.000
182	A	183	SER	0	0.052	-0.005	57.931	0.026	0.026	0.000	0.000	0.000
183	A	184	CYS	-1	-0.829	-0.804	57.705	-5.348	-5.348	0.000	0.000	0.000
184	A	185	GLY	0	0.035	0.005	55.478	-0.137	-0.137	0.000	0.000	0.000
185	A	186	TYR	0	0.048	0.019	49.053	0.004	0.004	0.000	0.000	0.000
186	A	187	LYS	1	0.825	0.917	53.049	6.011	6.011	0.000	0.000	0.000
187	A	188	LYS	0	-0.020	-0.011	46.040	0.118	0.118	0.000	0.000	0.000

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