FMO DATABASE

FMODB ID: 64N9Z

Calculation Name: 1VVC-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VVC

Chain ID: A

ChEMBL ID:

UniProt ID: P68638

Base Structure: SolutionNMR

Registration Date: 2025-10-05

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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-805792.490591
FMO2-HF: Nuclear repulsion	759300.984734
FMO2-HF: Total energy	-46491.505857
FMO2-MP2: Total energy	-46621.887663

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:VAL)

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

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.
-50.5	-50.132	6.437	-1.447	-5.359	-0.036

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.838 / q_NPA : 0.925

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	CYS	0	0.048	0.065	3.333	-3.509	-0.786	0.050	-1.261	-1.512	-0.003
23	A	23	ASP	-1	-0.760	-0.884	4.463	-42.618	-42.410	-0.001	-0.023	-0.185	0.000
46	A	47	GLY	0	-0.010	-0.002	4.054	1.100	1.329	0.002	-0.084	-0.147	0.000
47	A	48	GLY	0	-0.056	-0.059	2.293	-13.426	-12.552	5.992	-3.669	-3.197	-0.029
48	A	49	GLU	-1	-0.964	-0.969	2.734	-23.547	-27.213	0.394	3.590	-0.318	-0.004
4	A	4	GLN	0	0.042	0.022	5.709	-0.685	-0.685	0.000	0.000	0.000	0.000
5	A	5	SER	0	0.045	0.010	9.171	0.569	0.569	0.000	0.000	0.000	0.000
6	A	6	PRO	0	-0.049	0.008	11.430	0.181	0.181	0.000	0.000	0.000	0.000
7	A	7	PRO	0	0.023	0.011	11.981	0.979	0.979	0.000	0.000	0.000	0.000
8	A	8	SER	0	-0.034	-0.011	14.884	0.358	0.358	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.011	0.010	17.591	-0.292	-0.292	0.000	0.000	0.000	0.000
10	A	10	SER	0	0.002	-0.014	20.147	0.338	0.338	0.000	0.000	0.000	0.000
11	A	11	ASN	0	-0.034	-0.009	23.666	0.422	0.422	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.048	0.019	22.813	0.370	0.370	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.906	0.942	21.036	12.002	12.002	0.000	0.000	0.000	0.000
14	A	14	HIS	1	0.916	0.957	15.680	17.356	17.356	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.034	-0.018	18.590	0.072	0.072	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.035	0.040	17.417	0.469	0.469	0.000	0.000	0.000	0.000
17	A	17	TYR	0	-0.041	-0.033	17.477	1.110	1.110	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.840	-0.899	13.741	-18.551	-18.551	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.888	-0.949	14.153	-18.371	-18.371	0.000	0.000	0.000	0.000
20	A	20	PHE	0	-0.083	-0.063	7.949	-2.454	-2.454	0.000	0.000	0.000	0.000
21	A	21	TYR	0	0.033	0.003	8.890	0.878	0.878	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.168	-0.086	5.404	-0.994	-0.994	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.046	0.047	6.583	2.383	2.383	0.000	0.000	0.000	0.000
25	A	25	SER	0	-0.033	-0.003	8.511	2.339	2.339	0.000	0.000	0.000	0.000
26	A	26	VAL	0	-0.003	-0.009	11.088	0.136	0.136	0.000	0.000	0.000	0.000
27	A	27	VAL	0	-0.030	-0.004	13.293	0.260	0.260	0.000	0.000	0.000	0.000
28	A	28	THR	0	0.037	0.028	15.581	0.235	0.235	0.000	0.000	0.000	0.000
29	A	29	TYR	0	-0.012	-0.012	14.142	-0.043	-0.043	0.000	0.000	0.000	0.000
30	A	30	SER	0	0.021	0.008	19.692	0.402	0.402	0.000	0.000	0.000	0.000
31	A	31	CYS	0	0.002	0.007	22.941	-0.112	-0.112	0.000	0.000	0.000	0.000
32	A	32	ASN	0	0.041	0.028	25.907	-0.018	-0.018	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.026	0.001	28.900	-0.016	-0.016	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.000	0.008	32.074	0.238	0.238	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.110	-0.056	28.799	0.245	0.245	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.016	-0.020	28.858	0.059	0.059	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.048	0.014	21.426	-0.040	-0.040	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.097	-0.045	24.585	0.350	0.350	0.000	0.000	0.000	0.000
39	A	39	GLY	0	0.047	0.025	21.845	-0.397	-0.397	0.000	0.000	0.000	0.000
40	A	40	ASN	0	0.020	0.002	18.822	0.901	0.901	0.000	0.000	0.000	0.000
41	A	41	SER	0	-0.039	-0.015	20.723	0.046	0.046	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.036	-0.050	17.749	0.050	0.050	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.055	-0.011	12.512	0.077	0.077	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.066	0.027	10.827	0.054	0.054	0.000	0.000	0.000	0.000
45	A	46	SER	0	0.010	-0.018	6.611	0.751	0.751	0.000	0.000	0.000	0.000
49	A	50	TRP	0	-0.020	-0.034	6.472	1.514	1.514	0.000	0.000	0.000	0.000
50	A	51	SER	0	-0.012	-0.006	9.440	1.749	1.749	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.836	-0.910	12.060	-15.227	-15.227	0.000	0.000	0.000	0.000
52	A	53	PRO	0	-0.018	0.001	14.851	0.317	0.317	0.000	0.000	0.000	0.000
53	A	54	PRO	0	0.001	0.011	16.640	0.732	0.732	0.000	0.000	0.000	0.000
54	A	55	THR	0	-0.025	-0.030	20.167	0.097	0.097	0.000	0.000	0.000	0.000
55	A	57	GLN	0	0.048	0.027	25.507	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	58	ILE	0	0.032	0.001	28.774	0.107	0.107	0.000	0.000	0.000	0.000
57	A	59	VAL	0	-0.064	-0.018	30.731	0.045	0.045	0.000	0.000	0.000	0.000
58	A	60	LYS	1	0.951	0.987	33.832	8.545	8.545	0.000	0.000	0.000	0.000
59	A	61	CYS	0	0.012	0.032	37.018	-0.105	-0.105	0.000	0.000	0.000	0.000
60	A	62	PRO	0	-0.005	0.020	39.946	0.155	0.155	0.000	0.000	0.000	0.000
61	A	63	HIS	1	0.824	0.884	43.285	6.749	6.749	0.000	0.000	0.000	0.000
62	A	64	PRO	0	0.022	0.058	43.195	0.034	0.034	0.000	0.000	0.000	0.000
63	A	65	THR	0	-0.014	-0.018	44.829	0.151	0.151	0.000	0.000	0.000	0.000
64	A	66	ILE	0	0.000	0.010	47.396	-0.064	-0.064	0.000	0.000	0.000	0.000
65	A	67	SER	0	-0.046	-0.007	49.867	0.141	0.141	0.000	0.000	0.000	0.000
66	A	68	ASN	0	0.062	0.014	53.134	-0.041	-0.041	0.000	0.000	0.000	0.000
67	A	69	GLY	0	0.041	-0.002	52.139	0.072	0.072	0.000	0.000	0.000	0.000
68	A	70	TYR	0	0.058	0.024	50.054	-0.096	-0.096	0.000	0.000	0.000	0.000
69	A	71	LEU	0	0.046	0.042	46.256	0.016	0.016	0.000	0.000	0.000	0.000
70	A	72	SER	0	-0.075	-0.050	48.169	0.181	0.181	0.000	0.000	0.000	0.000
71	A	73	SER	0	-0.009	-0.013	44.063	0.041	0.041	0.000	0.000	0.000	0.000
72	A	74	GLY	0	0.050	0.040	42.728	0.085	0.085	0.000	0.000	0.000	0.000
73	A	75	PHE	0	0.000	0.005	42.976	-0.112	-0.112	0.000	0.000	0.000	0.000
74	A	76	LYS	1	0.956	0.975	42.341	7.022	7.022	0.000	0.000	0.000	0.000
75	A	77	ARG	1	0.960	0.963	45.319	6.104	6.104	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.012	-0.007	41.670	-0.019	-0.019	0.000	0.000	0.000	0.000
77	A	79	TYR	0	0.067	0.033	39.233	0.112	0.112	0.000	0.000	0.000	0.000
78	A	80	SER	0	-0.029	-0.029	34.345	-0.136	-0.136	0.000	0.000	0.000	0.000
79	A	81	TYR	0	0.043	0.022	26.854	0.181	0.181	0.000	0.000	0.000	0.000
80	A	82	ASN	0	0.054	0.015	31.998	0.065	0.065	0.000	0.000	0.000	0.000
81	A	83	ASP	-1	-0.891	-0.955	34.291	-7.512	-7.512	0.000	0.000	0.000	0.000
82	A	84	ASN	0	0.020	0.014	37.346	0.188	0.188	0.000	0.000	0.000	0.000
83	A	85	VAL	0	-0.039	-0.022	39.041	0.181	0.181	0.000	0.000	0.000	0.000
84	A	86	ASP	-1	-0.803	-0.887	42.679	-7.232	-7.232	0.000	0.000	0.000	0.000
85	A	87	PHE	0	-0.063	-0.059	43.101	0.146	0.146	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.949	0.972	47.512	5.868	5.868	0.000	0.000	0.000	0.000
87	A	89	CYS	0	-0.091	-0.017	50.009	0.078	0.078	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.855	0.925	53.355	5.432	5.432	0.000	0.000	0.000	0.000
89	A	91	TYR	0	0.037	0.002	56.597	0.033	0.033	0.000	0.000	0.000	0.000
90	A	92	GLY	0	-0.017	0.012	59.037	0.024	0.024	0.000	0.000	0.000	0.000
91	A	93	TYR	0	0.000	-0.004	55.787	0.046	0.046	0.000	0.000	0.000	0.000
92	A	94	LYS	1	0.997	0.989	48.911	6.211	6.211	0.000	0.000	0.000	0.000
93	A	95	LEU	0	0.005	-0.007	48.015	0.011	0.011	0.000	0.000	0.000	0.000
94	A	96	SER	0	-0.054	-0.022	48.255	-0.091	-0.091	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.039	0.012	44.454	0.025	0.025	0.000	0.000	0.000	0.000
96	A	98	SER	0	0.033	0.008	40.722	-0.035	-0.035	0.000	0.000	0.000	0.000
97	A	99	SER	0	0.002	-0.018	43.256	0.050	0.050	0.000	0.000	0.000	0.000
98	A	100	SER	0	0.025	0.030	40.310	0.095	0.095	0.000	0.000	0.000	0.000
99	A	101	SER	0	-0.030	0.008	39.173	-0.126	-0.126	0.000	0.000	0.000	0.000
100	A	102	THR	0	0.003	-0.014	34.961	0.064	0.064	0.000	0.000	0.000	0.000
101	A	104	SER	0	0.031	0.011	33.080	-0.325	-0.325	0.000	0.000	0.000	0.000
102	A	105	PRO	0	-0.001	-0.008	29.023	0.161	0.161	0.000	0.000	0.000	0.000
103	A	106	GLY	0	0.022	0.007	31.636	-0.071	-0.071	0.000	0.000	0.000	0.000
104	A	107	ASN	0	-0.055	-0.014	33.298	0.239	0.239	0.000	0.000	0.000	0.000
105	A	108	THR	0	0.016	0.000	36.022	0.144	0.144	0.000	0.000	0.000	0.000
106	A	109	TRP	0	0.024	0.003	37.820	-0.048	-0.048	0.000	0.000	0.000	0.000
107	A	110	LYS	1	0.942	0.984	31.882	9.194	9.194	0.000	0.000	0.000	0.000
108	A	111	PRO	0	0.030	0.004	36.639	-0.098	-0.098	0.000	0.000	0.000	0.000
109	A	112	GLU	-1	-0.899	-0.952	37.968	-7.573	-7.573	0.000	0.000	0.000	0.000
110	A	113	LEU	0	-0.041	-0.005	40.935	0.077	0.077	0.000	0.000	0.000	0.000
111	A	114	PRO	0	-0.065	-0.001	43.860	0.105	0.105	0.000	0.000	0.000	0.000
112	A	115	LYS	1	0.942	0.957	46.477	6.318	6.318	0.000	0.000	0.000	0.000
113	A	117	VAL	0	0.009	-0.002	52.294	0.078	0.078	0.000	0.000	0.000	0.000
114	A	118	ARG	0	0.088	0.052	54.825	-0.228	-0.228	0.000	0.000	0.000	0.000

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