FMO DATABASE

FMODB ID: Q5GQY

Calculation Name: 1I5N-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1I5N

Chain ID: A

ChEMBL ID:

UniProt ID: P09384

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	128
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1134105.963779
FMO2-HF: Nuclear repulsion	1082518.390308
FMO2-HF: Total energy	-51587.573471
FMO2-MP2: Total energy	-51736.527566

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:4:ASP)

Summations of interaction energy for fragment #1(A:4:ASP)

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.
-89.639	-86.593	20.548	-13.329	-10.266	-0.131

Interaction energy analysis for fragmet #1(A:4:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.160 / q_NPA : -0.111

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	6	SER	0	0.039	0.001	2.449	-8.676	-4.484	1.250	-2.586	-2.857	-0.016
4	A	7	ASP	-1	-0.897	-0.924	1.834	-74.580	-76.485	19.297	-10.502	-6.890	-0.114
5	A	8	PHE	0	-0.059	-0.031	4.096	4.789	5.548	0.001	-0.241	-0.519	-0.001
6	A	9	TYR	0	0.026	0.023	6.963	0.353	0.353	0.000	0.000	0.000	0.000
7	A	10	GLN	0	-0.003	0.007	8.711	0.602	0.602	0.000	0.000	0.000	0.000
8	A	11	THR	0	-0.004	-0.016	10.761	0.375	0.375	0.000	0.000	0.000	0.000
9	A	12	PHE	0	0.046	0.038	12.115	0.454	0.454	0.000	0.000	0.000	0.000
10	A	13	PHE	0	-0.011	-0.015	10.870	0.057	0.057	0.000	0.000	0.000	0.000
11	A	14	ASP	-1	-0.927	-0.954	14.912	-1.552	-1.552	0.000	0.000	0.000	0.000
12	A	15	GLU	-1	-0.936	-0.975	16.563	-0.312	-0.312	0.000	0.000	0.000	0.000
13	A	16	ALA	0	-0.010	-0.018	17.604	0.198	0.198	0.000	0.000	0.000	0.000
14	A	17	ASP	-1	-0.746	-0.852	19.178	-1.724	-1.724	0.000	0.000	0.000	0.000
15	A	18	GLU	-1	-0.944	-0.967	21.093	-0.822	-0.822	0.000	0.000	0.000	0.000
16	A	19	LEU	0	-0.039	-0.024	21.124	0.144	0.144	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.018	-0.009	21.902	0.126	0.126	0.000	0.000	0.000	0.000
18	A	21	ALA	0	0.019	0.018	25.126	0.068	0.068	0.000	0.000	0.000	0.000
19	A	22	ASP	-1	-0.934	-0.969	26.818	-0.425	-0.425	0.000	0.000	0.000	0.000
20	A	23	MET	0	-0.089	-0.042	25.604	0.063	0.063	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.852	-0.930	29.219	-0.614	-0.614	0.000	0.000	0.000	0.000
22	A	25	GLN	0	-0.071	-0.044	31.183	0.008	0.008	0.000	0.000	0.000	0.000
23	A	26	HIS	0	0.026	-0.006	30.863	0.060	0.060	0.000	0.000	0.000	0.000
24	A	27	LEU	0	-0.035	-0.022	31.694	0.045	0.045	0.000	0.000	0.000	0.000
25	A	28	LEU	0	-0.056	-0.022	34.793	0.022	0.022	0.000	0.000	0.000	0.000
26	A	29	ASP	-1	-0.908	-0.935	37.121	-0.297	-0.297	0.000	0.000	0.000	0.000
27	A	30	LEU	0	-0.057	-0.016	36.794	0.035	0.035	0.000	0.000	0.000	0.000
28	A	31	VAL	0	-0.017	0.001	39.898	-0.008	-0.008	0.000	0.000	0.000	0.000
29	A	32	PRO	0	-0.016	-0.001	42.302	0.017	0.017	0.000	0.000	0.000	0.000
30	A	33	GLU	-1	-0.897	-0.963	43.297	-0.115	-0.115	0.000	0.000	0.000	0.000
31	A	34	SER	0	-0.120	-0.074	45.671	0.018	0.018	0.000	0.000	0.000	0.000
32	A	35	PRO	0	0.013	0.037	40.357	-0.008	-0.008	0.000	0.000	0.000	0.000
33	A	36	ASP	-1	-0.784	-0.908	39.172	-0.054	-0.054	0.000	0.000	0.000	0.000
34	A	37	ALA	0	0.027	0.013	38.694	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-1.012	-0.993	35.848	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	39	GLN	0	0.002	-0.015	34.787	0.011	0.011	0.000	0.000	0.000	0.000
37	A	40	LEU	0	0.034	0.019	33.970	-0.017	-0.017	0.000	0.000	0.000	0.000
38	A	41	ASN	0	-0.081	-0.055	32.637	0.041	0.041	0.000	0.000	0.000	0.000
39	A	42	ALA	0	-0.036	-0.007	30.486	0.024	0.024	0.000	0.000	0.000	0.000
40	A	43	ILE	0	0.062	0.028	29.212	-0.019	-0.019	0.000	0.000	0.000	0.000
41	A	44	PHE	0	-0.007	-0.004	27.926	-0.008	-0.008	0.000	0.000	0.000	0.000
42	A	45	ARG	1	0.905	0.946	26.545	-0.066	-0.066	0.000	0.000	0.000	0.000
43	A	46	ALA	0	0.053	0.052	24.831	0.026	0.026	0.000	0.000	0.000	0.000
44	A	47	ALA	0	0.056	0.023	23.874	-0.049	-0.049	0.000	0.000	0.000	0.000
45	A	48	HIS	0	-0.122	-0.069	23.040	0.083	0.083	0.000	0.000	0.000	0.000
46	A	49	SER	0	-0.032	-0.033	20.638	0.131	0.131	0.000	0.000	0.000	0.000
47	A	50	ILE	0	0.038	0.022	19.080	0.012	0.012	0.000	0.000	0.000	0.000
48	A	51	LYS	1	0.846	0.922	18.760	-0.353	-0.353	0.000	0.000	0.000	0.000
49	A	52	GLY	0	-0.012	-0.007	17.835	0.107	0.107	0.000	0.000	0.000	0.000
50	A	53	GLY	0	0.022	0.022	14.377	0.293	0.293	0.000	0.000	0.000	0.000
51	A	54	ALA	0	0.020	0.005	13.879	-0.067	-0.067	0.000	0.000	0.000	0.000
52	A	55	GLY	0	-0.027	-0.020	15.090	-0.029	-0.029	0.000	0.000	0.000	0.000
53	A	56	THR	0	-0.129	-0.070	10.076	0.485	0.485	0.000	0.000	0.000	0.000
54	A	57	PHE	0	-0.032	-0.032	7.981	0.671	0.671	0.000	0.000	0.000	0.000
55	A	58	GLY	0	-0.024	0.008	10.944	-0.573	-0.573	0.000	0.000	0.000	0.000
56	A	59	PHE	0	0.012	0.020	10.393	-0.184	-0.184	0.000	0.000	0.000	0.000
57	A	60	THR	0	0.001	-0.023	15.100	0.142	0.142	0.000	0.000	0.000	0.000
58	A	61	ILE	0	0.017	0.028	18.293	0.130	0.130	0.000	0.000	0.000	0.000
59	A	62	LEU	0	0.077	0.066	17.222	0.093	0.093	0.000	0.000	0.000	0.000
60	A	63	GLN	0	-0.025	0.003	18.203	0.107	0.107	0.000	0.000	0.000	0.000
61	A	64	GLU	-1	-0.789	-0.889	20.273	0.105	0.105	0.000	0.000	0.000	0.000
62	A	65	THR	0	-0.003	-0.015	23.267	0.042	0.042	0.000	0.000	0.000	0.000
63	A	66	THR	0	0.012	-0.026	21.503	0.088	0.088	0.000	0.000	0.000	0.000
64	A	67	HIS	0	-0.120	-0.059	23.711	0.115	0.115	0.000	0.000	0.000	0.000
65	A	68	LEU	0	-0.050	-0.023	25.289	0.041	0.041	0.000	0.000	0.000	0.000
66	A	69	MET	0	0.033	0.028	27.611	0.006	0.006	0.000	0.000	0.000	0.000
67	A	70	GLU	-1	-0.762	-0.863	24.603	0.260	0.260	0.000	0.000	0.000	0.000
68	A	71	ASN	0	-0.042	-0.034	28.398	0.058	0.058	0.000	0.000	0.000	0.000
69	A	72	LEU	0	0.043	0.031	30.817	0.012	0.012	0.000	0.000	0.000	0.000
70	A	73	LEU	0	0.009	0.005	29.479	0.001	0.001	0.000	0.000	0.000	0.000
71	A	74	ASP	-1	-0.833	-0.892	31.377	0.222	0.222	0.000	0.000	0.000	0.000
72	A	75	GLU	-1	-0.863	-0.945	33.172	0.041	0.041	0.000	0.000	0.000	0.000
73	A	76	ALA	0	-0.001	0.007	35.965	0.000	0.000	0.000	0.000	0.000	0.000
74	A	77	ARG	1	0.750	0.858	30.817	-0.150	-0.150	0.000	0.000	0.000	0.000
75	A	78	ARG	1	0.753	0.881	32.715	-0.203	-0.203	0.000	0.000	0.000	0.000
76	A	79	GLY	0	-0.031	-0.006	38.380	0.009	0.009	0.000	0.000	0.000	0.000
77	A	80	GLU	-1	-1.016	-1.005	38.106	0.145	0.145	0.000	0.000	0.000	0.000
78	A	81	MET	0	0.002	0.011	36.745	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	82	GLN	0	-0.071	-0.037	41.025	-0.012	-0.012	0.000	0.000	0.000	0.000
80	A	83	LEU	0	0.031	0.016	38.338	-0.010	-0.010	0.000	0.000	0.000	0.000
81	A	84	ASN	0	0.026	-0.005	41.828	-0.007	-0.007	0.000	0.000	0.000	0.000
82	A	85	THR	0	0.056	0.010	41.578	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	86	ASP	-1	-0.929	-0.954	40.693	-0.232	-0.232	0.000	0.000	0.000	0.000
84	A	87	ILE	0	-0.001	0.005	37.344	-0.021	-0.021	0.000	0.000	0.000	0.000
85	A	88	ILE	0	0.017	0.016	36.658	-0.014	-0.014	0.000	0.000	0.000	0.000
86	A	89	ASN	0	-0.026	-0.021	35.987	-0.043	-0.043	0.000	0.000	0.000	0.000
87	A	90	LEU	0	0.007	0.014	33.916	-0.036	-0.036	0.000	0.000	0.000	0.000
88	A	91	PHE	0	-0.002	-0.004	32.258	-0.023	-0.023	0.000	0.000	0.000	0.000
89	A	92	LEU	0	0.003	0.004	31.172	-0.038	-0.038	0.000	0.000	0.000	0.000
90	A	93	GLU	-1	-0.851	-0.921	30.988	-0.590	-0.590	0.000	0.000	0.000	0.000
91	A	94	THR	0	-0.060	-0.070	27.743	-0.040	-0.040	0.000	0.000	0.000	0.000
92	A	95	LYS	1	0.793	0.903	26.967	0.638	0.638	0.000	0.000	0.000	0.000
93	A	96	ASP	-1	-0.860	-0.922	26.271	-0.779	-0.779	0.000	0.000	0.000	0.000
94	A	97	ILE	0	-0.001	-0.012	25.624	-0.099	-0.099	0.000	0.000	0.000	0.000
95	A	98	MET	0	-0.061	-0.033	23.084	-0.043	-0.043	0.000	0.000	0.000	0.000
96	A	99	GLN	0	-0.038	-0.020	21.487	-0.043	-0.043	0.000	0.000	0.000	0.000
97	A	100	GLU	-1	-0.915	-0.961	21.472	-1.148	-1.148	0.000	0.000	0.000	0.000
98	A	101	GLN	0	-0.057	-0.055	20.017	-0.149	-0.149	0.000	0.000	0.000	0.000
99	A	102	LEU	0	-0.032	-0.002	16.333	-0.264	-0.264	0.000	0.000	0.000	0.000
100	A	103	ASP	-1	-0.810	-0.909	16.726	-2.193	-2.193	0.000	0.000	0.000	0.000
101	A	104	ALA	0	-0.032	-0.003	17.814	-0.243	-0.243	0.000	0.000	0.000	0.000
102	A	105	TYR	0	0.055	0.008	13.312	-0.188	-0.188	0.000	0.000	0.000	0.000
103	A	106	LYS	1	0.715	0.848	12.655	1.338	1.338	0.000	0.000	0.000	0.000
104	A	107	ASN	0	-0.076	-0.036	13.186	-0.752	-0.752	0.000	0.000	0.000	0.000
105	A	108	SER	0	-0.122	-0.061	10.724	-0.670	-0.670	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.952	-0.974	12.812	-1.964	-1.964	0.000	0.000	0.000	0.000
107	A	110	GLU	-1	-0.965	-0.981	15.906	-1.802	-1.802	0.000	0.000	0.000	0.000
108	A	111	PRO	0	-0.033	-0.021	17.551	0.107	0.107	0.000	0.000	0.000	0.000
109	A	112	ASP	-1	-0.846	-0.900	20.671	-0.769	-0.769	0.000	0.000	0.000	0.000
110	A	113	ALA	0	0.023	0.000	24.431	0.076	0.076	0.000	0.000	0.000	0.000
111	A	114	ALA	0	-0.008	-0.001	25.562	0.083	0.083	0.000	0.000	0.000	0.000
112	A	115	SER	0	0.012	-0.007	26.968	0.080	0.080	0.000	0.000	0.000	0.000
113	A	116	PHE	0	0.005	0.000	24.432	0.048	0.048	0.000	0.000	0.000	0.000
114	A	117	GLU	-1	-0.966	-0.983	26.551	-0.295	-0.295	0.000	0.000	0.000	0.000
115	A	118	TYR	0	-0.070	-0.031	29.474	0.068	0.068	0.000	0.000	0.000	0.000
116	A	119	ILE	0	0.059	0.032	27.435	0.056	0.056	0.000	0.000	0.000	0.000
117	A	120	CYS	0	-0.043	-0.017	27.281	0.063	0.063	0.000	0.000	0.000	0.000
118	A	121	ASN	0	-0.053	-0.034	30.010	0.090	0.090	0.000	0.000	0.000	0.000
119	A	122	ALA	0	-0.010	-0.003	33.536	0.037	0.037	0.000	0.000	0.000	0.000
120	A	123	LEU	0	0.018	0.011	29.586	0.037	0.037	0.000	0.000	0.000	0.000
121	A	124	ARG	1	0.860	0.912	28.827	0.109	0.109	0.000	0.000	0.000	0.000
122	A	125	GLN	0	-0.070	-0.022	34.798	0.036	0.036	0.000	0.000	0.000	0.000
123	A	126	LEU	0	0.066	0.046	36.179	0.021	0.021	0.000	0.000	0.000	0.000
124	A	127	ALA	0	0.014	-0.004	35.202	0.019	0.019	0.000	0.000	0.000	0.000
125	A	128	LEU	0	-0.097	-0.048	37.364	0.029	0.029	0.000	0.000	0.000	0.000
126	A	129	GLU	-1	-0.986	-1.003	40.186	-0.114	-0.114	0.000	0.000	0.000	0.000
127	A	130	ALA	0	-0.025	-0.002	40.002	0.003	0.003	0.000	0.000	0.000	0.000
128	A	131	LYS	0	-0.072	-0.018	40.508	0.002	0.002	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ASP)