FMO DATABASE

FMODB ID: 3G2LL

Calculation Name: 2FIP-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FIP

Chain ID: A

ChEMBL ID:

UniProt ID: P03682

Base Structure: X-ray

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1041316.121344
FMO2-HF: Nuclear repulsion	993233.984162
FMO2-HF: Total energy	-48082.137181
FMO2-MP2: Total energy	-48224.129678

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:PRO)

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

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.
-30.519	-29.095	17.707	-10.785	-8.344	-0.122

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.817 / q_NPA : 0.868

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	THR	0	-0.006	-0.011	3.247	1.087	2.829	0.045	-0.827	-0.959	-0.003
8	A	9	TYR	0	-0.009	-0.031	3.737	-9.404	-9.079	0.006	-0.099	-0.232	0.000
10	A	11	ASN	0	-0.007	0.012	3.625	14.196	14.504	0.000	-0.043	-0.265	0.000
13	A	14	GLU	-1	-0.780	-0.877	1.728	-123.701	-124.652	17.656	-9.816	-6.888	-0.119
4	A	5	GLN	0	0.038	0.003	5.643	3.097	3.097	0.000	0.000	0.000	0.000
5	A	6	ARG	1	0.919	0.966	8.516	25.309	25.309	0.000	0.000	0.000	0.000
6	A	7	GLY	0	0.034	0.023	8.842	1.853	1.853	0.000	0.000	0.000	0.000
7	A	8	ILE	0	-0.049	-0.019	8.128	-0.003	-0.003	0.000	0.000	0.000	0.000
9	A	10	HIS	0	0.044	-0.003	5.073	6.194	6.194	0.000	0.000	0.000	0.000
11	A	12	LEU	0	0.034	0.012	5.619	-2.957	-2.957	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.962	0.986	7.334	33.116	33.116	0.000	0.000	0.000	0.000
14	A	15	SER	0	-0.041	-0.025	5.806	1.141	1.141	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.771	-0.843	7.398	-28.787	-28.787	0.000	0.000	0.000	0.000
16	A	17	TYR	0	-0.029	-0.015	9.599	1.711	1.711	0.000	0.000	0.000	0.000
17	A	18	VAL	0	0.016	0.010	11.933	-0.197	-0.197	0.000	0.000	0.000	0.000
18	A	19	ALA	0	0.048	0.021	14.328	0.934	0.934	0.000	0.000	0.000	0.000
19	A	20	SER	0	-0.018	-0.026	18.120	-0.122	-0.122	0.000	0.000	0.000	0.000
20	A	21	ASN	0	0.084	0.052	20.902	0.021	0.021	0.000	0.000	0.000	0.000
21	A	22	THR	0	-0.033	-0.019	23.615	0.777	0.777	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.813	-0.885	24.818	-11.062	-11.062	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.014	-0.019	21.237	-0.157	-0.157	0.000	0.000	0.000	0.000
24	A	25	THR	0	-0.005	0.013	16.371	0.013	0.013	0.000	0.000	0.000	0.000
25	A	26	PHE	0	-0.002	-0.002	16.816	-0.099	-0.099	0.000	0.000	0.000	0.000
26	A	27	PHE	0	0.033	0.019	10.744	-0.474	-0.474	0.000	0.000	0.000	0.000
27	A	28	PHE	0	0.037	0.023	12.537	0.227	0.227	0.000	0.000	0.000	0.000
28	A	29	SER	0	-0.066	-0.044	9.468	-2.278	-2.278	0.000	0.000	0.000	0.000
29	A	30	SER	0	-0.023	-0.022	9.935	-1.692	-1.692	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.741	-0.853	12.156	-18.508	-18.508	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.004	0.001	14.595	1.256	1.256	0.000	0.000	0.000	0.000
32	A	33	TYR	0	-0.070	-0.047	14.521	1.390	1.390	0.000	0.000	0.000	0.000
33	A	34	LEU	0	0.036	0.028	14.594	0.726	0.726	0.000	0.000	0.000	0.000
34	A	35	ASN	0	0.028	0.007	16.983	0.578	0.578	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.959	0.997	19.941	16.034	16.034	0.000	0.000	0.000	0.000
36	A	37	PHE	0	-0.014	-0.003	19.888	0.555	0.555	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.029	-0.028	19.498	0.665	0.665	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.874	-0.939	22.912	-12.604	-12.604	0.000	0.000	0.000	0.000
39	A	40	GLY	0	-0.010	0.005	25.016	0.524	0.524	0.000	0.000	0.000	0.000
40	A	41	TYR	0	-0.022	-0.014	24.982	0.653	0.653	0.000	0.000	0.000	0.000
41	A	42	GLN	0	0.011	0.011	27.113	0.416	0.416	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.978	-0.986	30.250	-9.452	-9.452	0.000	0.000	0.000	0.000
43	A	44	TYR	0	-0.074	-0.046	28.106	0.468	0.468	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.807	0.863	28.166	11.033	11.033	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.980	0.997	32.263	9.293	9.293	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.884	0.938	31.752	10.301	10.301	0.000	0.000	0.000	0.000
47	A	48	PHE	0	0.011	-0.001	30.752	0.211	0.211	0.000	0.000	0.000	0.000
48	A	49	ASN	0	0.028	0.022	33.896	0.066	0.066	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.986	0.991	36.924	8.489	8.489	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.854	0.937	33.584	9.405	9.405	0.000	0.000	0.000	0.000
51	A	52	ILE	0	0.044	0.030	34.627	0.124	0.124	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.843	-0.926	38.343	-7.534	-7.534	0.000	0.000	0.000	0.000
53	A	54	ARG	1	0.819	0.903	39.415	8.053	8.053	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.065	-0.016	39.434	0.086	0.086	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.015	-0.012	41.710	0.159	0.159	0.000	0.000	0.000	0.000
56	A	57	VAL	0	0.021	0.026	42.125	-0.169	-0.169	0.000	0.000	0.000	0.000
57	A	58	THR	0	-0.031	-0.020	40.885	0.022	0.022	0.000	0.000	0.000	0.000
58	A	59	PRO	0	-0.004	0.001	42.645	-0.049	-0.049	0.000	0.000	0.000	0.000
59	A	60	TRP	0	-0.007	-0.008	37.963	-0.038	-0.038	0.000	0.000	0.000	0.000
60	A	61	ASN	0	0.004	-0.006	34.638	-0.126	-0.126	0.000	0.000	0.000	0.000
61	A	62	MET	0	0.036	0.002	34.169	-0.235	-0.235	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.785	-0.869	31.344	-9.886	-9.886	0.000	0.000	0.000	0.000
63	A	64	MET	0	0.003	0.011	24.397	-0.366	-0.366	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.009	0.005	27.442	-0.446	-0.446	0.000	0.000	0.000	0.000
65	A	66	ALA	0	0.003	0.022	28.173	-0.304	-0.304	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.736	-0.839	25.145	-11.928	-11.928	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.014	-0.011	23.214	-0.714	-0.714	0.000	0.000	0.000	0.000
68	A	69	THR	0	-0.042	-0.020	23.346	-0.495	-0.495	0.000	0.000	0.000	0.000
69	A	70	PHE	0	0.010	0.005	24.318	-0.431	-0.431	0.000	0.000	0.000	0.000
70	A	71	TYR	0	-0.018	-0.019	14.581	-0.383	-0.383	0.000	0.000	0.000	0.000
71	A	72	SER	0	-0.048	-0.041	19.587	-0.935	-0.935	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.910	-0.930	21.167	-12.076	-12.076	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.039	-0.017	18.898	-0.260	-0.260	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.746	-0.830	13.695	-24.273	-24.273	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.833	0.903	15.555	15.829	15.829	0.000	0.000	0.000	0.000
76	A	77	ARG	1	0.859	0.920	10.331	25.037	25.037	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.019	0.017	12.108	-1.645	-1.645	0.000	0.000	0.000	0.000
78	A	79	PHE	0	0.026	0.005	14.520	0.611	0.611	0.000	0.000	0.000	0.000
79	A	80	HIS	0	-0.032	-0.020	12.320	-0.776	-0.776	0.000	0.000	0.000	0.000
80	A	81	ALA	0	0.031	0.019	14.271	-0.088	-0.088	0.000	0.000	0.000	0.000
81	A	82	TRP	0	0.007	-0.005	13.569	-0.210	-0.210	0.000	0.000	0.000	0.000
82	A	83	LEU	0	-0.010	-0.012	18.576	0.523	0.523	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.820	0.920	22.370	11.778	11.778	0.000	0.000	0.000	0.000
84	A	85	GLY	0	0.045	0.044	20.088	0.257	0.257	0.000	0.000	0.000	0.000
85	A	86	ASP	-1	-0.896	-0.935	19.369	-14.973	-14.973	0.000	0.000	0.000	0.000
86	A	87	ASN	0	-0.071	-0.057	13.969	-0.516	-0.516	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.019	0.022	17.882	0.739	0.739	0.000	0.000	0.000	0.000
88	A	89	THR	0	-0.042	-0.062	18.948	-0.559	-0.559	0.000	0.000	0.000	0.000
89	A	90	TRP	0	0.031	0.006	20.547	0.589	0.589	0.000	0.000	0.000	0.000
90	A	91	ARG	1	0.982	0.992	21.928	11.121	11.121	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.780	-0.857	22.869	-13.022	-13.022	0.000	0.000	0.000	0.000
92	A	93	VAL	0	0.026	0.008	21.103	0.382	0.382	0.000	0.000	0.000	0.000
93	A	94	HIS	0	-0.016	-0.012	24.489	0.638	0.638	0.000	0.000	0.000	0.000
94	A	95	VAL	0	-0.023	-0.005	27.418	0.442	0.442	0.000	0.000	0.000	0.000
95	A	96	TYR	0	-0.056	-0.073	26.846	0.351	0.351	0.000	0.000	0.000	0.000
96	A	97	ALA	0	0.016	0.001	28.089	0.323	0.323	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.009	-0.003	29.905	0.307	0.307	0.000	0.000	0.000	0.000
98	A	99	ARG	1	0.934	0.977	31.082	10.225	10.225	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.038	-0.019	30.755	0.294	0.294	0.000	0.000	0.000	0.000
100	A	101	MET	0	-0.003	0.022	33.412	0.104	0.104	0.000	0.000	0.000	0.000
101	A	102	THR	0	-0.040	-0.021	35.716	0.267	0.267	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.911	0.965	33.287	9.566	9.566	0.000	0.000	0.000	0.000
103	A	104	PRO	0	0.042	0.020	37.015	-0.178	-0.178	0.000	0.000	0.000	0.000
104	A	105	ASN	0	-0.053	-0.022	35.117	-0.223	-0.223	0.000	0.000	0.000	0.000
105	A	106	THR	0	0.007	-0.026	30.878	-0.069	-0.069	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.026	0.009	28.496	0.099	0.099	0.000	0.000	0.000	0.000
107	A	108	ASP	-1	-0.815	-0.905	28.257	-10.602	-10.602	0.000	0.000	0.000	0.000
108	A	109	TRP	0	-0.094	-0.060	20.448	-0.562	-0.562	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.006	0.001	22.797	0.209	0.209	0.000	0.000	0.000	0.000
110	A	111	ARG	1	0.868	0.903	14.360	18.083	18.083	0.000	0.000	0.000	0.000
111	A	112	ILE	0	-0.015	-0.002	16.389	0.680	0.680	0.000	0.000	0.000	0.000
112	A	113	GLN	0	0.002	0.002	14.793	-0.391	-0.391	0.000	0.000	0.000	0.000
113	A	114	LYS	1	0.838	0.898	7.999	31.920	31.920	0.000	0.000	0.000	0.000
114	A	115	PRO	0	-0.038	-0.008	13.048	0.521	0.521	0.000	0.000	0.000	0.000
115	A	116	ARG	0	0.026	0.022	13.659	-5.638	-5.638	0.000	0.000	0.000	0.000

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