FMO DATABASE

FMODB ID: Q5V3Y

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	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1095491.609729
FMO2-HF: Nuclear repulsion	1040546.862663
FMO2-HF: Total energy	-54944.747067
FMO2-MP2: Total energy	-55105.423923

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.
303.271	304.858	0.045	-0.76	-0.872	-0.002

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 : 0.877 / q_NPA : 0.929

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	ILE	0	0.053	0.023	3.373	-6.072	-4.485	0.045	-0.760	-0.872	-0.002
4	A	4	ARG	1	0.940	0.961	5.901	33.857	33.857	0.000	0.000	0.000	0.000
5	A	5	PRO	0	-0.041	-0.009	7.792	1.581	1.581	0.000	0.000	0.000	0.000
6	A	6	ALA	0	0.017	0.012	11.601	-0.380	-0.380	0.000	0.000	0.000	0.000
7	A	7	TYR	0	-0.014	-0.005	13.705	-0.067	-0.067	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.905	0.970	9.387	24.089	24.089	0.000	0.000	0.000	0.000
9	A	9	PRO	0	0.056	0.033	14.942	-0.479	-0.479	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.986	0.976	12.508	17.098	17.098	0.000	0.000	0.000	0.000
11	A	11	ILE	0	0.017	0.002	13.497	0.852	0.852	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.043	0.031	17.085	-0.148	-0.148	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.888	0.948	14.568	16.596	16.596	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.933	0.973	21.022	10.909	10.909	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.896	0.957	24.470	9.637	9.637	0.000	0.000	0.000	0.000
16	A	16	THR	0	0.067	0.030	20.920	0.134	0.134	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.951	0.996	23.630	9.477	9.477	0.000	0.000	0.000	0.000
18	A	18	HIS	0	0.083	0.031	26.136	0.082	0.082	0.000	0.000	0.000	0.000
19	A	19	PHE	0	0.009	-0.017	27.763	0.223	0.223	0.000	0.000	0.000	0.000
20	A	20	ILE	0	0.010	0.029	30.945	0.246	0.246	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.879	0.951	32.767	7.518	7.518	0.000	0.000	0.000	0.000
22	A	22	HIS	0	0.030	0.005	36.456	-0.147	-0.147	0.000	0.000	0.000	0.000
23	A	23	GLN	0	0.063	0.038	39.269	0.148	0.148	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.025	-0.013	35.521	0.093	0.093	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.914	-0.955	36.513	-7.563	-7.563	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.950	0.976	37.843	6.571	6.571	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.007	-0.021	40.560	0.197	0.197	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.134	0.069	38.783	-0.124	-0.124	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.964	0.994	39.413	6.429	6.429	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.115	-0.044	39.025	0.001	0.001	0.000	0.000	0.000	0.000
31	A	31	SER	0	0.019	0.002	35.665	-0.234	-0.234	0.000	0.000	0.000	0.000
32	A	32	HIS	0	0.094	0.030	29.868	0.043	0.043	0.000	0.000	0.000	0.000
33	A	33	LYS	1	0.956	0.994	32.813	8.433	8.433	0.000	0.000	0.000	0.000
34	A	34	TRP	0	0.049	0.002	33.194	0.301	0.301	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.959	0.974	34.918	7.784	7.784	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.962	0.995	38.551	7.342	7.342	0.000	0.000	0.000	0.000
37	A	37	PRO	0	0.018	0.014	39.956	0.133	0.133	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.955	0.956	42.637	7.004	7.004	0.000	0.000	0.000	0.000
39	A	39	GLY	0	0.069	0.054	46.119	0.102	0.102	0.000	0.000	0.000	0.000
40	A	40	ILE	0	0.079	0.030	48.502	-0.132	-0.132	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.799	-0.879	50.129	-5.803	-5.803	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.139	-0.073	44.755	-0.082	-0.082	0.000	0.000	0.000	0.000
43	A	43	ARG	1	1.003	0.997	45.090	6.098	6.098	0.000	0.000	0.000	0.000
44	A	44	VAL	0	0.010	0.002	39.419	-0.044	-0.044	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.895	0.935	41.663	6.157	6.157	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.900	0.946	43.674	5.988	5.988	0.000	0.000	0.000	0.000
47	A	47	ARG	1	0.907	0.968	38.812	7.342	7.342	0.000	0.000	0.000	0.000
48	A	48	PHE	0	0.109	0.052	42.244	0.004	0.004	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.994	0.991	39.449	7.085	7.085	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.080	0.048	38.760	0.122	0.122	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.017	-0.011	38.856	-0.100	-0.100	0.000	0.000	0.000	0.000
52	A	52	TYR	0	-0.014	-0.025	34.273	-0.149	-0.149	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.002	-0.001	31.376	-0.078	-0.078	0.000	0.000	0.000	0.000
54	A	54	MET	0	-0.018	0.014	34.389	-0.068	-0.068	0.000	0.000	0.000	0.000
55	A	55	PRO	0	-0.002	0.010	31.949	-0.070	-0.070	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.014	-0.017	32.977	0.357	0.357	0.000	0.000	0.000	0.000
57	A	57	ILE	0	0.074	0.031	32.066	-0.286	-0.286	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.054	0.038	31.201	-0.251	-0.251	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.045	-0.051	28.163	-0.182	-0.182	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.008	0.017	26.788	-0.388	-0.388	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.017	-0.019	22.019	0.016	0.016	0.000	0.000	0.000	0.000
62	A	62	ASN	0	0.070	0.018	22.079	0.487	0.487	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.991	0.999	22.891	10.071	10.071	0.000	0.000	0.000	0.000
64	A	64	ARG	1	0.917	0.967	20.496	12.487	12.487	0.000	0.000	0.000	0.000
65	A	65	THR	0	0.075	0.024	17.756	-0.331	-0.331	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.880	0.949	18.861	11.348	11.348	0.000	0.000	0.000	0.000
67	A	67	HIS	0	0.067	0.014	19.630	-0.471	-0.471	0.000	0.000	0.000	0.000
68	A	68	MET	0	-0.044	0.006	13.816	-0.176	-0.176	0.000	0.000	0.000	0.000
69	A	69	LEU	0	0.088	0.061	10.786	0.479	0.479	0.000	0.000	0.000	0.000
70	A	70	PRO	0	0.011	-0.003	10.204	-0.568	-0.568	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.023	-0.020	6.625	-1.846	-1.846	0.000	0.000	0.000	0.000
72	A	72	GLY	0	-0.010	-0.012	8.247	-2.211	-2.211	0.000	0.000	0.000	0.000
73	A	73	PHE	0	0.011	-0.009	6.687	2.290	2.290	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.926	0.968	12.077	16.552	16.552	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.982	0.990	15.239	13.596	13.596	0.000	0.000	0.000	0.000
76	A	76	PHE	0	0.021	0.015	16.522	0.737	0.737	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.012	-0.004	17.919	-0.561	-0.561	0.000	0.000	0.000	0.000
78	A	78	VAL	0	0.033	0.030	17.053	0.369	0.369	0.000	0.000	0.000	0.000
79	A	79	HIS	0	-0.006	-0.029	20.259	0.108	0.108	0.000	0.000	0.000	0.000
80	A	80	ASN	0	-0.058	-0.056	22.774	0.174	0.174	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.077	0.029	20.787	-0.361	-0.361	0.000	0.000	0.000	0.000
82	A	82	ARG	1	1.025	1.024	21.322	10.484	10.484	0.000	0.000	0.000	0.000
83	A	83	GLU	-1	-0.891	-0.931	21.696	-12.285	-12.285	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.045	-0.028	14.965	-0.394	-0.394	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.829	-0.900	18.234	-14.446	-14.446	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.008	0.016	20.635	-0.093	-0.093	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.055	-0.039	15.451	-0.289	-0.289	0.000	0.000	0.000	0.000
88	A	88	LEU	0	0.030	0.036	16.165	-1.302	-1.302	0.000	0.000	0.000	0.000
89	A	89	MET	0	0.032	0.016	16.612	-0.618	-0.618	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.077	-0.045	17.036	-0.223	-0.223	0.000	0.000	0.000	0.000
91	A	91	ASN	0	0.170	0.074	9.723	-0.927	-0.927	0.000	0.000	0.000	0.000
92	A	92	ARG	1	0.977	0.985	12.126	16.379	16.379	0.000	0.000	0.000	0.000
93	A	93	VAL	0	-0.079	-0.058	13.344	0.916	0.916	0.000	0.000	0.000	0.000
94	A	94	TYR	0	-0.011	0.001	14.625	0.607	0.607	0.000	0.000	0.000	0.000
95	A	95	CYS	0	-0.055	-0.010	11.130	-1.404	-1.404	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.076	0.041	13.004	1.471	1.471	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.888	-0.942	13.895	-18.082	-18.082	0.000	0.000	0.000	0.000
98	A	98	ILE	0	0.001	-0.005	16.171	0.888	0.888	0.000	0.000	0.000	0.000
99	A	99	ALA	0	0.050	0.035	18.623	0.141	0.141	0.000	0.000	0.000	0.000
100	A	100	HIS	0	0.042	0.012	22.037	-0.430	-0.430	0.000	0.000	0.000	0.000
101	A	101	GLY	0	0.013	0.011	23.229	0.105	0.105	0.000	0.000	0.000	0.000
102	A	102	VAL	0	-0.032	0.002	22.239	0.316	0.316	0.000	0.000	0.000	0.000
103	A	103	SER	0	0.084	0.024	23.328	-0.437	-0.437	0.000	0.000	0.000	0.000
104	A	104	SER	0	0.050	0.019	22.188	-0.537	-0.537	0.000	0.000	0.000	0.000
105	A	105	LYS	1	1.027	1.010	22.142	10.161	10.161	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.950	0.980	23.069	11.557	11.557	0.000	0.000	0.000	0.000
107	A	107	ARG	1	0.801	0.899	17.871	14.298	14.298	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.985	0.990	18.123	13.373	13.373	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.867	-0.918	17.929	-15.193	-15.193	0.000	0.000	0.000	0.000
110	A	110	ILE	0	-0.035	-0.021	16.527	-0.555	-0.555	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.018	-0.020	12.688	-1.075	-1.075	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.789	-0.870	13.464	-21.188	-21.188	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.895	0.924	14.920	14.551	14.551	0.000	0.000	0.000	0.000
114	A	114	ALA	0	-0.037	-0.030	12.222	-0.459	-0.459	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.799	0.888	9.727	19.952	19.952	0.000	0.000	0.000	0.000
116	A	116	GLN	0	0.044	0.032	11.362	-1.028	-1.028	0.000	0.000	0.000	0.000
117	A	117	LEU	0	-0.028	-0.016	14.100	0.131	0.131	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.031	-0.007	8.746	-1.244	-1.244	0.000	0.000	0.000	0.000
119	A	119	VAL	0	-0.027	0.008	9.114	-3.416	-3.416	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.882	0.956	5.819	30.011	30.011	0.000	0.000	0.000	0.000
121	A	121	LEU	0	0.069	0.031	8.919	2.686	2.686	0.000	0.000	0.000	0.000
122	A	122	THR	0	-0.114	-0.100	9.480	-2.081	-2.081	0.000	0.000	0.000	0.000
123	A	123	ASN	0	-0.042	-0.025	11.098	0.142	0.142	0.000	0.000	0.000	0.000
124	A	124	PRO	0	0.032	0.015	9.707	1.383	1.383	0.000	0.000	0.000	0.000
125	A	125	ASN	0	0.079	0.033	11.651	-0.515	-0.515	0.000	0.000	0.000	0.000
126	A	126	GLY	0	0.000	0.007	14.794	0.956	0.956	0.000	0.000	0.000	0.000
127	A	127	ARG	1	0.882	0.937	16.964	12.187	12.187	0.000	0.000	0.000	0.000
128	A	128	LEU	0	0.014	0.017	15.824	0.348	0.348	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.770	0.889	18.843	12.181	12.181	0.000	0.000	0.000	0.000
130	A	130	SER	0	0.020	-0.003	21.276	-0.533	-0.533	0.000	0.000	0.000	0.000
131	A	131	GLN	0	-0.063	-0.041	23.633	0.007	0.007	0.000	0.000	0.000	0.000
132	A	132	GLU	-2	-1.677	-1.803	25.663	-22.581	-22.581	0.000	0.000	0.000	0.000

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