FMO DATABASE

FMODB ID: ZZR5N

Calculation Name: 1IFC-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1IFC

Chain ID: A

ChEMBL ID:

UniProt ID: P02693

Base Structure: X-ray

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	131
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1206509.31739
FMO2-HF: Nuclear repulsion	1154254.922728
FMO2-HF: Total energy	-52254.394662
FMO2-MP2: Total energy	-52408.085397

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:ALA)

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

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.
-103.564	-101.096	12.424	-8.211	-6.68	-0.104

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.797 / q_NPA : 0.879

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	ASP	-1	-0.796	-0.880	1.751	-107.063	-104.952	12.424	-8.113	-6.422	-0.104
4	A	4	GLY	0	0.038	0.031	4.199	-1.727	-1.649	-0.001	-0.022	-0.055	0.000
6	A	6	TRP	0	0.005	0.010	4.600	-2.339	-2.223	-0.001	-0.038	-0.076	0.000
108	A	108	ILE	0	0.002	0.005	3.732	0.073	0.236	0.002	-0.038	-0.127	0.000
5	A	5	THR	0	-0.011	-0.021	7.356	0.267	0.267	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.914	0.949	10.787	18.809	18.809	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.042	-0.013	14.434	-0.530	-0.530	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.871	-0.929	16.130	-16.937	-16.937	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.805	0.857	15.721	19.565	19.565	0.000	0.000	0.000	0.000
11	A	11	ASN	0	0.000	-0.005	18.871	-1.349	-1.349	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.893	-0.938	20.084	-14.642	-14.642	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.012	-0.034	22.728	0.193	0.193	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.071	0.025	22.851	0.268	0.268	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.816	-0.895	24.827	-10.352	-10.352	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.938	0.977	28.203	9.984	9.984	0.000	0.000	0.000	0.000
17	A	17	PHE	0	0.052	0.034	23.327	0.251	0.251	0.000	0.000	0.000	0.000
18	A	18	MET	0	-0.024	-0.003	26.159	0.251	0.251	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.903	-0.949	28.388	-8.995	-8.995	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.896	0.961	29.249	9.957	9.957	0.000	0.000	0.000	0.000
21	A	21	MET	0	-0.006	0.022	25.660	0.240	0.240	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.037	0.037	29.945	0.093	0.093	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.015	0.004	28.273	0.265	0.265	0.000	0.000	0.000	0.000
24	A	24	ASN	0	0.034	0.001	32.593	0.011	0.011	0.000	0.000	0.000	0.000
25	A	25	VAL	0	0.074	0.022	33.895	-0.260	-0.260	0.000	0.000	0.000	0.000
26	A	26	VAL	0	0.031	0.016	33.824	-0.243	-0.243	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.964	0.979	31.608	9.190	9.190	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.859	0.926	29.511	9.276	9.276	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.846	0.900	28.968	9.697	9.697	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.002	0.006	29.425	-0.230	-0.230	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.041	0.012	26.208	-0.383	-0.383	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.037	-0.022	24.558	-0.654	-0.654	0.000	0.000	0.000	0.000
33	A	33	HIS	0	-0.033	-0.020	24.235	-0.483	-0.483	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.785	-0.852	21.702	-14.989	-14.989	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.032	-0.034	21.386	-0.483	-0.483	0.000	0.000	0.000	0.000
36	A	36	LEU	0	-0.009	0.021	16.983	-0.606	-0.606	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.953	0.976	14.620	17.690	17.690	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.002	0.002	12.002	0.835	0.835	0.000	0.000	0.000	0.000
39	A	39	THR	0	-0.020	-0.020	10.869	-1.596	-1.596	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.030	-0.004	7.058	2.543	2.543	0.000	0.000	0.000	0.000
41	A	41	THR	0	-0.023	-0.015	7.789	-2.820	-2.820	0.000	0.000	0.000	0.000
42	A	42	GLN	0	-0.006	-0.013	5.532	-2.968	-2.968	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.945	-0.967	8.423	-20.230	-20.230	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.022	0.015	10.706	1.840	1.840	0.000	0.000	0.000	0.000
45	A	45	ASN	0	0.048	0.012	10.099	-3.272	-3.272	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.967	0.994	12.265	17.398	17.398	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.030	0.005	6.185	-2.587	-2.587	0.000	0.000	0.000	0.000
48	A	48	THR	0	0.006	0.005	11.164	2.892	2.892	0.000	0.000	0.000	0.000
49	A	49	VAL	0	-0.036	-0.017	10.659	-2.434	-2.434	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.885	0.927	12.945	20.447	20.447	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.748	-0.831	15.000	-17.501	-17.501	0.000	0.000	0.000	0.000
52	A	52	SER	0	-0.068	-0.053	17.537	0.821	0.821	0.000	0.000	0.000	0.000
53	A	53	SER	0	0.007	-0.008	19.327	-0.299	-0.299	0.000	0.000	0.000	0.000
54	A	54	ASN	0	0.022	0.009	22.085	0.227	0.227	0.000	0.000	0.000	0.000
55	A	55	PHE	0	-0.044	-0.008	24.923	0.557	0.557	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.800	0.880	21.051	14.765	14.765	0.000	0.000	0.000	0.000
57	A	57	ASN	0	0.012	0.013	21.484	-1.146	-1.146	0.000	0.000	0.000	0.000
58	A	58	ILE	0	-0.002	0.008	19.915	0.693	0.693	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.813	-0.888	17.812	-18.495	-18.495	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.021	-0.007	15.950	0.866	0.866	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.012	-0.007	15.186	-1.472	-1.472	0.000	0.000	0.000	0.000
62	A	62	PHE	0	-0.015	-0.002	11.271	0.818	0.818	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.913	-0.972	14.375	-17.825	-17.825	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.060	-0.024	9.635	0.463	0.463	0.000	0.000	0.000	0.000
65	A	65	GLY	0	-0.030	-0.021	14.154	0.628	0.628	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.033	0.001	17.348	0.947	0.947	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.976	-0.985	19.021	-13.119	-13.119	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.031	-0.024	17.361	-0.108	-0.108	0.000	0.000	0.000	0.000
69	A	69	ALA	0	0.039	0.010	22.146	0.183	0.183	0.000	0.000	0.000	0.000
70	A	70	TYR	0	-0.090	-0.081	19.353	-0.373	-0.373	0.000	0.000	0.000	0.000
71	A	71	SER	0	0.042	0.037	22.778	0.250	0.250	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.029	0.016	21.466	-0.702	-0.702	0.000	0.000	0.000	0.000
73	A	73	ALA	0	-0.017	-0.021	23.345	0.382	0.382	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.902	-0.929	25.147	-11.170	-11.170	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.011	0.011	27.556	0.457	0.457	0.000	0.000	0.000	0.000
76	A	76	THR	0	-0.064	-0.055	27.129	0.271	0.271	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.937	-0.963	26.384	-10.943	-10.943	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.031	-0.017	21.725	0.238	0.238	0.000	0.000	0.000	0.000
79	A	79	THR	0	0.011	0.001	23.966	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.003	0.000	21.573	0.193	0.193	0.000	0.000	0.000	0.000
81	A	81	THR	0	0.020	0.028	17.890	-0.198	-0.198	0.000	0.000	0.000	0.000
82	A	82	TRP	0	0.025	0.015	12.687	-0.706	-0.706	0.000	0.000	0.000	0.000
83	A	83	THR	0	-0.024	-0.042	13.639	0.299	0.299	0.000	0.000	0.000	0.000
84	A	84	MET	0	0.012	0.012	6.047	-1.718	-1.718	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.789	-0.860	10.560	-16.025	-16.025	0.000	0.000	0.000	0.000
86	A	86	GLY	0	-0.011	-0.004	10.751	-0.438	-0.438	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.012	-0.014	5.515	-0.361	-0.361	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.845	0.916	6.293	18.031	18.031	0.000	0.000	0.000	0.000
89	A	89	LEU	0	0.021	0.023	7.389	1.346	1.346	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.027	-0.024	9.660	0.751	0.751	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.019	0.017	13.457	0.102	0.102	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.840	0.900	16.143	16.639	16.639	0.000	0.000	0.000	0.000
93	A	93	PHE	0	0.009	0.010	17.269	0.261	0.261	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.950	0.968	22.081	11.397	11.397	0.000	0.000	0.000	0.000
95	A	95	ARG	1	0.766	0.839	25.849	10.217	10.217	0.000	0.000	0.000	0.000
96	A	96	VAL	0	-0.008	-0.007	27.907	0.240	0.240	0.000	0.000	0.000	0.000
97	A	97	ASP	-1	-0.801	-0.856	30.283	-9.615	-9.615	0.000	0.000	0.000	0.000
98	A	98	ASN	0	-0.013	-0.030	31.432	0.110	0.110	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.028	0.021	31.008	0.159	0.159	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.811	0.895	29.664	9.298	9.298	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.934	-0.964	24.749	-12.213	-12.213	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.036	-0.031	20.892	0.186	0.186	0.000	0.000	0.000	0.000
103	A	103	ILE	0	0.002	0.023	18.376	-0.545	-0.545	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.012	-0.015	16.266	0.074	0.074	0.000	0.000	0.000	0.000
105	A	105	VAL	0	0.001	0.001	12.428	-0.350	-0.350	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.885	0.944	9.422	23.798	23.798	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.839	-0.914	8.178	-23.744	-23.744	0.000	0.000	0.000	0.000
109	A	109	SER	0	-0.008	0.002	7.046	2.054	2.054	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.027	0.011	9.276	0.894	0.894	0.000	0.000	0.000	0.000
111	A	111	ASN	0	-0.018	-0.018	7.353	-3.458	-3.458	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.776	-0.851	8.654	-20.498	-20.498	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.009	0.006	8.056	-2.365	-2.365	0.000	0.000	0.000	0.000
114	A	114	ILE	0	0.011	-0.004	9.378	2.988	2.988	0.000	0.000	0.000	0.000
115	A	115	GLN	0	0.047	0.038	11.961	-2.039	-2.039	0.000	0.000	0.000	0.000
116	A	116	THR	0	-0.009	-0.011	14.169	1.482	1.482	0.000	0.000	0.000	0.000
117	A	117	TYR	0	0.004	-0.001	16.945	-0.479	-0.479	0.000	0.000	0.000	0.000
118	A	118	THR	0	-0.009	-0.007	19.789	0.538	0.538	0.000	0.000	0.000	0.000
119	A	119	TYR	0	0.078	0.015	22.643	-0.038	-0.038	0.000	0.000	0.000	0.000
120	A	120	GLU	-1	-0.847	-0.906	25.917	-9.575	-9.575	0.000	0.000	0.000	0.000
121	A	121	GLY	0	0.017	0.007	28.145	0.341	0.341	0.000	0.000	0.000	0.000
122	A	122	VAL	0	-0.077	-0.030	26.674	0.139	0.139	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.806	-0.908	20.584	-14.808	-14.808	0.000	0.000	0.000	0.000
124	A	124	ALA	0	-0.056	-0.026	22.123	0.505	0.505	0.000	0.000	0.000	0.000
125	A	125	LYS	1	0.878	0.948	17.170	15.836	15.836	0.000	0.000	0.000	0.000
126	A	126	ARG	1	0.763	0.842	17.182	16.554	16.554	0.000	0.000	0.000	0.000
127	A	127	ILE	0	0.006	0.011	13.462	-1.308	-1.308	0.000	0.000	0.000	0.000
128	A	128	PHE	0	0.001	0.000	11.676	1.413	1.413	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.897	0.957	11.527	17.714	17.714	0.000	0.000	0.000	0.000
130	A	130	LYS	1	0.782	0.876	5.254	46.232	46.232	0.000	0.000	0.000	0.000
131	A	131	GLU	-2	-1.877	-1.924	9.583	-46.143	-46.143	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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