FMO DATABASE

FMODB ID: VVM71

Calculation Name: 2AYV-A-Xray547

Preferred Name:

Target Type:

Ligand Name: unknown atom or ion

Ligand 3-letter code: UNX

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2AYV

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-10-03

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	148
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1399179.432095
FMO2-HF: Nuclear repulsion	1340581.185409
FMO2-HF: Total energy	-58598.246686
FMO2-MP2: Total energy	-58769.381468

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:PHE)

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

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.
-78.773	-67.202	27.844	-15.282	-24.133	-0.137

Interaction energy analysis for fragmet #1(A:-1:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.798 / q_NPA : 0.894

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	1	GLY	0	0.052	0.021	3.161	3.596	6.586	2.459	-1.714	-3.735	0.000
4	A	2	ALA	0	0.008	0.012	2.382	1.567	4.090	2.251	-1.345	-3.429	-0.004
5	A	3	LEU	0	0.059	0.034	3.031	6.566	6.190	0.154	0.598	-0.377	0.001
7	A	5	ARG	1	0.751	0.851	3.828	29.836	30.087	0.000	-0.031	-0.220	0.000
60	A	58	SER	0	0.068	0.024	3.393	1.928	2.643	0.007	-0.347	-0.375	-0.001
61	A	59	ASP	-1	-0.874	-0.945	1.783	-137.299	-136.637	17.986	-10.824	-7.824	-0.119
62	A	60	TYR	0	-0.022	0.004	3.209	8.751	8.331	0.067	1.122	-0.768	-0.003
63	A	61	PRO	0	-0.023	-0.023	2.487	-13.322	-10.391	1.609	-1.735	-2.805	-0.018
64	A	62	PHE	0	0.025	-0.018	2.712	1.414	3.709	3.311	-1.006	-4.600	0.007
6	A	4	LYS	1	0.947	0.977	5.384	28.122	28.122	0.000	0.000	0.000	0.000
8	A	6	ILE	0	0.036	0.019	5.727	2.631	2.631	0.000	0.000	0.000	0.000
9	A	7	ASN	0	0.045	0.008	8.602	2.279	2.279	0.000	0.000	0.000	0.000
10	A	8	LYS	1	0.848	0.921	9.142	21.483	21.483	0.000	0.000	0.000	0.000
11	A	9	GLU	-1	-0.717	-0.831	9.402	-22.712	-22.712	0.000	0.000	0.000	0.000
12	A	10	LEU	0	0.013	0.023	11.968	1.014	1.014	0.000	0.000	0.000	0.000
13	A	11	ASN	0	-0.027	-0.004	14.022	1.547	1.547	0.000	0.000	0.000	0.000
14	A	12	ASP	-1	-0.823	-0.905	13.720	-16.170	-16.170	0.000	0.000	0.000	0.000
15	A	13	LEU	0	-0.017	-0.001	15.901	0.604	0.604	0.000	0.000	0.000	0.000
16	A	14	SER	0	-0.065	-0.039	17.766	0.716	0.716	0.000	0.000	0.000	0.000
17	A	15	LYS	1	0.844	0.923	16.803	14.967	14.967	0.000	0.000	0.000	0.000
18	A	16	ASP	-1	-0.964	-0.987	19.952	-11.595	-11.595	0.000	0.000	0.000	0.000
19	A	17	PRO	0	-0.003	0.016	20.458	-0.502	-0.502	0.000	0.000	0.000	0.000
20	A	18	PRO	0	-0.007	-0.005	20.046	0.335	0.335	0.000	0.000	0.000	0.000
21	A	19	THR	0	0.071	0.012	22.777	0.061	0.061	0.000	0.000	0.000	0.000
22	A	20	ASN	0	0.000	0.010	26.193	-0.110	-0.110	0.000	0.000	0.000	0.000
23	A	21	CYS	0	-0.065	-0.013	22.486	-0.137	-0.137	0.000	0.000	0.000	0.000
24	A	22	SER	0	-0.028	-0.004	22.050	0.034	0.034	0.000	0.000	0.000	0.000
25	A	23	ALA	0	0.013	-0.018	17.737	-0.249	-0.249	0.000	0.000	0.000	0.000
26	A	24	GLY	0	0.033	0.021	17.090	0.151	0.151	0.000	0.000	0.000	0.000
27	A	25	PRO	0	-0.019	-0.012	14.651	-0.124	-0.124	0.000	0.000	0.000	0.000
28	A	26	VAL	0	-0.024	-0.003	16.784	1.148	1.148	0.000	0.000	0.000	0.000
29	A	27	GLY	0	0.002	0.002	18.582	-0.232	-0.232	0.000	0.000	0.000	0.000
30	A	28	ASP	-1	-0.933	-0.969	17.426	-17.515	-17.515	0.000	0.000	0.000	0.000
31	A	29	ASP	-1	-0.854	-0.937	12.351	-25.590	-25.590	0.000	0.000	0.000	0.000
32	A	30	MET	0	-0.022	-0.011	11.323	0.420	0.420	0.000	0.000	0.000	0.000
33	A	31	PHE	0	-0.037	-0.029	5.227	-2.494	-2.494	0.000	0.000	0.000	0.000
34	A	32	HIS	1	0.858	0.947	10.706	18.283	18.283	0.000	0.000	0.000	0.000
35	A	33	TRP	0	0.013	-0.001	12.425	1.163	1.163	0.000	0.000	0.000	0.000
36	A	34	GLN	0	-0.017	-0.015	16.198	-0.051	-0.051	0.000	0.000	0.000	0.000
37	A	35	ALA	0	0.003	-0.005	19.267	-0.213	-0.213	0.000	0.000	0.000	0.000
38	A	36	THR	0	-0.011	0.007	21.177	0.203	0.203	0.000	0.000	0.000	0.000
39	A	37	ILE	0	0.027	-0.002	22.406	-0.334	-0.334	0.000	0.000	0.000	0.000
40	A	38	MET	0	-0.025	-0.005	26.078	0.175	0.175	0.000	0.000	0.000	0.000
41	A	39	GLY	0	0.008	-0.005	29.491	-0.187	-0.187	0.000	0.000	0.000	0.000
42	A	40	PRO	0	-0.001	0.011	29.739	0.245	0.245	0.000	0.000	0.000	0.000
43	A	41	GLU	-1	-0.801	-0.876	32.325	-8.447	-8.447	0.000	0.000	0.000	0.000
44	A	42	ASP	-1	-0.922	-0.931	33.956	-8.819	-8.819	0.000	0.000	0.000	0.000
45	A	43	SER	0	0.004	-0.015	33.693	-0.040	-0.040	0.000	0.000	0.000	0.000
46	A	44	PRO	0	-0.083	-0.043	35.513	0.132	0.132	0.000	0.000	0.000	0.000
47	A	45	TYR	0	-0.054	-0.063	32.519	0.005	0.005	0.000	0.000	0.000	0.000
48	A	46	SER	0	-0.070	-0.044	34.061	-0.093	-0.093	0.000	0.000	0.000	0.000
49	A	47	GLY	0	0.013	0.008	35.244	0.134	0.134	0.000	0.000	0.000	0.000
50	A	48	GLY	0	-0.024	0.011	33.888	0.001	0.001	0.000	0.000	0.000	0.000
51	A	49	VAL	0	-0.045	-0.041	29.540	-0.329	-0.329	0.000	0.000	0.000	0.000
52	A	50	PHE	0	-0.018	-0.019	27.487	-0.120	-0.120	0.000	0.000	0.000	0.000
53	A	51	PHE	0	0.060	0.022	25.357	-0.441	-0.441	0.000	0.000	0.000	0.000
54	A	52	LEU	0	-0.019	-0.004	21.094	-0.064	-0.064	0.000	0.000	0.000	0.000
55	A	53	ASN	0	-0.032	-0.012	17.273	-0.057	-0.057	0.000	0.000	0.000	0.000
56	A	54	ILE	0	-0.003	-0.006	13.592	-0.249	-0.249	0.000	0.000	0.000	0.000
57	A	55	HIS	0	0.050	0.025	12.113	0.222	0.222	0.000	0.000	0.000	0.000
58	A	56	PHE	0	0.022	0.011	8.004	-0.589	-0.589	0.000	0.000	0.000	0.000
59	A	57	PRO	0	0.007	0.012	6.603	-1.441	-1.441	0.000	0.000	0.000	0.000
65	A	63	LYS	1	0.862	0.936	6.098	42.962	42.962	0.000	0.000	0.000	0.000
66	A	64	PRO	0	0.068	0.042	8.053	-2.011	-2.011	0.000	0.000	0.000	0.000
67	A	65	PRO	0	-0.031	-0.010	10.510	-1.803	-1.803	0.000	0.000	0.000	0.000
68	A	66	LYS	1	0.880	0.929	11.695	20.981	20.981	0.000	0.000	0.000	0.000
69	A	67	VAL	0	-0.029	-0.008	14.279	0.188	0.188	0.000	0.000	0.000	0.000
70	A	68	ASN	0	-0.016	-0.007	17.305	-0.622	-0.622	0.000	0.000	0.000	0.000
71	A	69	PHE	0	0.050	0.014	20.684	-0.141	-0.141	0.000	0.000	0.000	0.000
72	A	70	THR	0	-0.091	-0.068	23.017	-0.141	-0.141	0.000	0.000	0.000	0.000
73	A	71	THR	0	0.035	0.039	25.677	0.178	0.178	0.000	0.000	0.000	0.000
74	A	72	LYS	1	0.864	0.947	28.700	8.936	8.936	0.000	0.000	0.000	0.000
75	A	73	ILE	0	0.034	0.018	28.448	0.282	0.282	0.000	0.000	0.000	0.000
76	A	74	TYR	0	0.028	0.019	31.631	-0.063	-0.063	0.000	0.000	0.000	0.000
77	A	75	HIS	0	0.055	0.016	29.078	0.085	0.085	0.000	0.000	0.000	0.000
78	A	76	PRO	0	0.034	0.036	31.309	-0.119	-0.119	0.000	0.000	0.000	0.000
79	A	77	ASN	0	0.003	-0.023	26.639	0.106	0.106	0.000	0.000	0.000	0.000
80	A	78	ILE	0	0.017	0.017	25.524	-0.632	-0.632	0.000	0.000	0.000	0.000
81	A	79	ASN	0	0.073	0.045	24.886	0.315	0.315	0.000	0.000	0.000	0.000
82	A	80	SER	0	0.004	-0.019	27.841	-0.120	-0.120	0.000	0.000	0.000	0.000
83	A	81	GLN	0	-0.056	-0.017	23.886	-0.309	-0.309	0.000	0.000	0.000	0.000
84	A	82	GLY	0	0.027	0.029	23.686	-0.615	-0.615	0.000	0.000	0.000	0.000
85	A	83	ALA	0	-0.019	-0.007	21.673	-0.511	-0.511	0.000	0.000	0.000	0.000
86	A	84	ILE	0	0.031	0.005	20.423	0.649	0.649	0.000	0.000	0.000	0.000
87	A	85	CYS	0	-0.075	-0.022	21.363	-0.886	-0.886	0.000	0.000	0.000	0.000
88	A	86	LEU	0	0.043	0.010	19.694	0.412	0.412	0.000	0.000	0.000	0.000
89	A	87	ASP	-1	-0.768	-0.881	19.876	-13.934	-13.934	0.000	0.000	0.000	0.000
90	A	88	ILE	0	-0.028	-0.013	16.871	-0.880	-0.880	0.000	0.000	0.000	0.000
91	A	89	LEU	0	-0.082	-0.052	15.123	-1.426	-1.426	0.000	0.000	0.000	0.000
92	A	90	LYS	1	0.812	0.898	15.914	13.153	13.153	0.000	0.000	0.000	0.000
93	A	91	ASP	-1	-0.901	-0.953	15.721	-15.958	-15.958	0.000	0.000	0.000	0.000
94	A	92	GLN	0	-0.022	-0.006	17.277	-0.220	-0.220	0.000	0.000	0.000	0.000
95	A	93	TRP	0	-0.033	-0.017	8.754	0.300	0.300	0.000	0.000	0.000	0.000
96	A	94	SER	0	0.043	0.004	12.520	-0.454	-0.454	0.000	0.000	0.000	0.000
97	A	95	PRO	0	0.010	0.007	7.215	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	96	ALA	0	0.003	0.016	8.913	-0.408	-0.408	0.000	0.000	0.000	0.000
99	A	97	LEU	0	-0.030	0.003	11.563	1.435	1.435	0.000	0.000	0.000	0.000
100	A	98	THR	0	-0.005	-0.023	11.039	-1.150	-1.150	0.000	0.000	0.000	0.000
101	A	99	ILE	0	0.055	0.017	12.700	0.797	0.797	0.000	0.000	0.000	0.000
102	A	100	SER	0	0.041	0.023	14.355	0.958	0.958	0.000	0.000	0.000	0.000
103	A	101	LYS	1	0.906	0.951	14.477	17.184	17.184	0.000	0.000	0.000	0.000
104	A	102	VAL	0	-0.001	0.018	14.530	0.521	0.521	0.000	0.000	0.000	0.000
105	A	103	LEU	0	0.017	0.009	17.638	0.542	0.542	0.000	0.000	0.000	0.000
106	A	104	LEU	0	0.054	0.029	20.210	0.575	0.575	0.000	0.000	0.000	0.000
107	A	105	SER	0	-0.030	-0.010	20.382	0.613	0.613	0.000	0.000	0.000	0.000
108	A	106	ILE	0	-0.032	-0.021	19.236	0.325	0.325	0.000	0.000	0.000	0.000
109	A	107	SER	0	0.013	0.003	23.135	0.562	0.562	0.000	0.000	0.000	0.000
110	A	108	SER	0	0.013	-0.011	25.462	0.467	0.467	0.000	0.000	0.000	0.000
111	A	109	LEU	0	-0.042	-0.005	24.668	0.312	0.312	0.000	0.000	0.000	0.000
112	A	110	LEU	0	-0.062	-0.022	27.410	0.251	0.251	0.000	0.000	0.000	0.000
113	A	111	THR	0	-0.021	-0.023	29.832	0.186	0.186	0.000	0.000	0.000	0.000
114	A	112	ASP	-1	-0.944	-0.968	30.736	-8.961	-8.961	0.000	0.000	0.000	0.000
115	A	113	PRO	0	-0.062	-0.027	30.080	-0.384	-0.384	0.000	0.000	0.000	0.000
116	A	114	ASN	0	0.057	0.030	26.833	0.500	0.500	0.000	0.000	0.000	0.000
117	A	115	PRO	0	-0.041	-0.017	30.486	-0.220	-0.220	0.000	0.000	0.000	0.000
118	A	116	ASP	-1	-0.880	-0.946	32.005	-8.863	-8.863	0.000	0.000	0.000	0.000
119	A	117	ASP	-1	-0.839	-0.912	25.259	-12.410	-12.410	0.000	0.000	0.000	0.000
120	A	118	PRO	0	-0.025	-0.001	27.839	-0.368	-0.368	0.000	0.000	0.000	0.000
121	A	119	LEU	0	-0.037	-0.029	24.230	-0.208	-0.208	0.000	0.000	0.000	0.000
122	A	120	VAL	0	-0.044	-0.021	28.864	0.131	0.131	0.000	0.000	0.000	0.000
123	A	121	PRO	0	0.010	-0.005	32.392	0.216	0.216	0.000	0.000	0.000	0.000
124	A	122	GLU	-1	-0.860	-0.927	35.032	-7.732	-7.732	0.000	0.000	0.000	0.000
125	A	123	ILE	0	-0.016	-0.001	33.648	0.182	0.182	0.000	0.000	0.000	0.000
126	A	124	ALA	0	-0.007	-0.005	33.768	0.075	0.075	0.000	0.000	0.000	0.000
127	A	125	HIS	0	-0.002	0.001	35.725	0.012	0.012	0.000	0.000	0.000	0.000
128	A	126	LEU	0	0.011	0.021	39.340	0.155	0.155	0.000	0.000	0.000	0.000
129	A	127	TYR	0	0.003	-0.012	35.601	0.174	0.174	0.000	0.000	0.000	0.000
130	A	128	LYS	1	0.843	0.911	35.872	8.838	8.838	0.000	0.000	0.000	0.000
131	A	129	SER	0	-0.091	-0.044	40.413	0.208	0.208	0.000	0.000	0.000	0.000
132	A	130	ASP	-1	-0.873	-0.941	43.128	-6.771	-6.771	0.000	0.000	0.000	0.000
133	A	131	ARG	1	1.008	1.007	37.579	8.069	8.069	0.000	0.000	0.000	0.000
134	A	132	MET	0	0.027	0.012	41.604	-0.149	-0.149	0.000	0.000	0.000	0.000
135	A	133	ARG	1	0.848	0.910	42.866	7.262	7.262	0.000	0.000	0.000	0.000
136	A	134	TYR	0	-0.005	-0.007	34.254	-0.055	-0.055	0.000	0.000	0.000	0.000
137	A	135	ASP	-1	-0.818	-0.924	39.250	-8.061	-8.061	0.000	0.000	0.000	0.000
138	A	136	GLN	0	-0.003	-0.001	40.153	-0.070	-0.070	0.000	0.000	0.000	0.000
139	A	137	THR	0	-0.033	-0.020	39.077	0.056	0.056	0.000	0.000	0.000	0.000
140	A	138	ALA	0	-0.012	0.004	36.036	-0.144	-0.144	0.000	0.000	0.000	0.000
141	A	139	ARG	1	0.905	0.981	36.988	7.650	7.650	0.000	0.000	0.000	0.000
142	A	140	GLU	-1	-0.867	-0.926	39.491	-7.400	-7.400	0.000	0.000	0.000	0.000
143	A	141	TRP	0	-0.045	-0.045	33.637	-0.183	-0.183	0.000	0.000	0.000	0.000
144	A	142	SER	0	0.034	0.000	35.121	-0.248	-0.248	0.000	0.000	0.000	0.000
145	A	143	GLN	0	0.006	0.015	36.137	-0.012	-0.012	0.000	0.000	0.000	0.000
146	A	144	LYS	1	0.830	0.912	38.645	8.256	8.256	0.000	0.000	0.000	0.000
147	A	145	TYR	0	-0.065	-0.049	33.689	0.078	0.078	0.000	0.000	0.000	0.000
148	A	146	ALA	-1	-0.816	-0.867	32.413	-9.467	-9.467	0.000	0.000	0.000	0.000

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