FMO DATABASE

FMODB ID: RLN78

Calculation Name: 1IX2-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1IX2

Chain ID: A

ChEMBL ID:

UniProt ID: Q47454

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	102
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-688319.679957
FMO2-HF: Nuclear repulsion	649786.881778
FMO2-HF: Total energy	-38532.798179
FMO2-MP2: Total energy	-38643.164364

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:3:PRO)

Summations of interaction energy for fragment #1(A:3: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.
-27.129	-22.085	24.997	-14.206	-15.836	-0.142

Interaction energy analysis for fragmet #1(A:3:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.767 / q_NPA : 0.860

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	5	LEU	0	-0.031	-0.007	3.870	2.443	3.930	-0.018	-0.711	-0.758	0.000
24	A	26	PHE	0	0.047	0.014	3.892	-0.676	-0.397	0.001	-0.037	-0.243	0.000
25	A	27	SER	0	0.016	0.002	3.343	0.360	1.009	0.054	-0.341	-0.363	-0.002
26	A	28	GLU	-1	-0.818	-0.879	1.675	-111.094	-112.759	17.309	-9.280	-6.364	-0.103
27	A	29	ASN	0	0.003	-0.011	4.392	2.297	2.376	-0.001	-0.003	-0.074	0.000
28	A	30	LEU	0	0.026	0.014	3.762	-5.320	-5.074	0.001	-0.036	-0.211	0.000
83	A	85	TRP	0	0.023	-0.006	4.574	-0.050	0.043	-0.001	-0.008	-0.084	0.000
85	A	87	ALA	0	0.016	0.012	2.963	1.657	2.052	0.127	-0.132	-0.390	0.000
86	A	88	VAL	0	0.002	0.007	3.240	-4.626	-3.809	0.062	-0.278	-0.601	-0.001
87	A	89	SER	0	0.043	0.023	2.537	2.086	5.193	1.681	-1.849	-2.940	-0.020
88	A	90	SER	0	0.027	-0.010	3.677	3.841	3.886	0.003	0.039	-0.087	0.000
89	A	91	ASP	-1	-0.881	-0.931	4.158	-40.132	-40.039	-0.001	-0.015	-0.077	0.000
91	A	93	HIS	0	0.025	0.028	4.458	6.340	6.491	-0.001	-0.018	-0.132	0.000
92	A	94	PRO	0	-0.109	-0.063	3.263	-9.654	-8.834	0.039	-0.288	-0.572	-0.002
93	A	95	ILE	0	0.034	0.030	1.887	0.003	-1.638	5.743	-1.247	-2.855	-0.014
94	A	96	THR	0	-0.033	-0.029	4.894	0.668	0.757	-0.001	-0.002	-0.085	0.000
4	A	6	LYS	1	0.934	0.969	6.926	31.237	31.237	0.000	0.000	0.000	0.000
5	A	7	SER	0	0.034	0.008	9.146	2.119	2.119	0.000	0.000	0.000	0.000
6	A	8	SER	0	-0.010	-0.019	11.378	-1.598	-1.598	0.000	0.000	0.000	0.000
7	A	9	VAL	0	-0.028	0.001	13.976	1.007	1.007	0.000	0.000	0.000	0.000
8	A	10	PRO	0	0.047	0.010	17.433	-0.105	-0.105	0.000	0.000	0.000	0.000
9	A	11	GLN	0	0.013	0.034	16.975	-1.027	-1.027	0.000	0.000	0.000	0.000
10	A	12	ALA	0	0.012	0.010	15.665	0.620	0.620	0.000	0.000	0.000	0.000
11	A	13	ASP	-1	-0.901	-0.959	17.617	-14.854	-14.854	0.000	0.000	0.000	0.000
12	A	14	SER	0	-0.083	-0.034	20.635	0.819	0.819	0.000	0.000	0.000	0.000
13	A	15	ALA	0	0.031	0.006	22.868	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.025	-0.017	23.083	0.277	0.277	0.000	0.000	0.000	0.000
15	A	17	ALA	0	0.029	0.017	26.253	0.213	0.213	0.000	0.000	0.000	0.000
16	A	18	ALA	0	0.024	0.002	26.064	-0.435	-0.435	0.000	0.000	0.000	0.000
17	A	19	PRO	0	-0.046	-0.002	21.852	0.134	0.134	0.000	0.000	0.000	0.000
18	A	20	GLU	-1	-0.905	-0.956	23.789	-11.451	-11.451	0.000	0.000	0.000	0.000
19	A	21	LYS	1	0.867	0.926	17.923	15.525	15.525	0.000	0.000	0.000	0.000
20	A	22	ILE	0	0.004	0.010	15.067	0.141	0.141	0.000	0.000	0.000	0.000
21	A	23	GLN	0	-0.023	-0.014	13.758	0.820	0.820	0.000	0.000	0.000	0.000
22	A	24	LEU	0	0.002	0.008	9.351	0.023	0.023	0.000	0.000	0.000	0.000
23	A	25	ASN	0	0.012	-0.002	9.501	-0.481	-0.481	0.000	0.000	0.000	0.000
29	A	31	THR	0	-0.016	-0.016	5.663	5.388	5.388	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.016	-0.006	7.754	0.260	0.260	0.000	0.000	0.000	0.000
31	A	33	LYS	1	0.940	0.980	9.650	21.593	21.593	0.000	0.000	0.000	0.000
32	A	34	PHE	0	0.012	0.010	8.591	1.600	1.600	0.000	0.000	0.000	0.000
33	A	35	SER	0	-0.004	0.003	6.694	-3.163	-3.163	0.000	0.000	0.000	0.000
34	A	36	GLY	0	0.014	0.001	8.767	2.457	2.457	0.000	0.000	0.000	0.000
35	A	37	ALA	0	-0.013	-0.013	9.949	-1.884	-1.884	0.000	0.000	0.000	0.000
36	A	38	LYS	1	0.922	0.977	12.523	17.498	17.498	0.000	0.000	0.000	0.000
37	A	39	LEU	0	0.050	0.028	15.858	-0.658	-0.658	0.000	0.000	0.000	0.000
38	A	40	THR	0	-0.040	-0.029	18.637	0.389	0.389	0.000	0.000	0.000	0.000
39	A	41	MET	0	0.031	0.043	21.337	-0.228	-0.228	0.000	0.000	0.000	0.000
40	A	42	THR	0	-0.015	-0.030	22.076	0.266	0.266	0.000	0.000	0.000	0.000
41	A	43	GLY	0	0.025	0.023	24.978	0.289	0.289	0.000	0.000	0.000	0.000
42	A	44	MET	0	0.042	0.018	28.271	-0.228	-0.228	0.000	0.000	0.000	0.000
43	A	45	LYS	1	0.972	0.984	31.015	8.211	8.211	0.000	0.000	0.000	0.000
44	A	46	GLY	0	0.008	-0.001	34.608	0.084	0.084	0.000	0.000	0.000	0.000
45	A	47	MET	0	-0.040	0.004	30.800	0.028	0.028	0.000	0.000	0.000	0.000
46	A	48	SER	0	-0.006	-0.012	33.006	0.001	0.001	0.000	0.000	0.000	0.000
47	A	49	SER	0	0.025	-0.011	30.493	-0.119	-0.119	0.000	0.000	0.000	0.000
48	A	50	HIS	0	0.006	0.007	29.428	-0.486	-0.486	0.000	0.000	0.000	0.000
49	A	51	SER	0	-0.034	0.003	30.059	0.085	0.085	0.000	0.000	0.000	0.000
50	A	52	PRO	0	0.025	0.017	24.541	0.034	0.034	0.000	0.000	0.000	0.000
51	A	53	MET	0	0.020	0.005	26.337	0.133	0.133	0.000	0.000	0.000	0.000
52	A	54	PRO	0	-0.035	-0.025	22.403	-0.447	-0.447	0.000	0.000	0.000	0.000
53	A	55	VAL	0	0.003	0.013	22.035	0.393	0.393	0.000	0.000	0.000	0.000
54	A	56	ALA	0	-0.001	0.002	21.772	-0.662	-0.662	0.000	0.000	0.000	0.000
55	A	57	ALA	0	-0.003	-0.010	19.104	0.119	0.119	0.000	0.000	0.000	0.000
56	A	58	LYS	1	0.919	0.967	19.238	12.654	12.654	0.000	0.000	0.000	0.000
57	A	59	VAL	0	-0.002	-0.002	12.673	-0.159	-0.159	0.000	0.000	0.000	0.000
58	A	60	ALA	0	0.000	0.008	15.191	0.525	0.525	0.000	0.000	0.000	0.000
59	A	61	PRO	0	0.017	0.006	12.411	-1.138	-1.138	0.000	0.000	0.000	0.000
60	A	62	GLY	0	0.003	0.005	12.564	1.300	1.300	0.000	0.000	0.000	0.000
61	A	63	ALA	0	-0.005	-0.012	14.388	-0.011	-0.011	0.000	0.000	0.000	0.000
62	A	64	ASP	-1	-0.846	-0.901	11.277	-23.970	-23.970	0.000	0.000	0.000	0.000
63	A	65	PRO	0	0.052	0.028	10.524	-0.872	-0.872	0.000	0.000	0.000	0.000
64	A	66	LYS	1	0.857	0.934	7.156	30.291	30.291	0.000	0.000	0.000	0.000
65	A	67	SER	0	-0.057	-0.039	7.831	-1.027	-1.027	0.000	0.000	0.000	0.000
66	A	68	MET	0	-0.030	-0.004	7.333	1.123	1.123	0.000	0.000	0.000	0.000
67	A	69	VAL	0	-0.020	-0.013	11.333	0.111	0.111	0.000	0.000	0.000	0.000
68	A	70	ILE	0	0.021	0.008	13.650	0.006	0.006	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.001	-0.007	16.525	0.477	0.477	0.000	0.000	0.000	0.000
70	A	72	PRO	0	0.027	0.013	20.306	-0.092	-0.092	0.000	0.000	0.000	0.000
71	A	73	ARG	1	0.834	0.904	21.996	12.789	12.789	0.000	0.000	0.000	0.000
72	A	74	GLU	-1	-0.848	-0.907	25.526	-10.625	-10.625	0.000	0.000	0.000	0.000
73	A	75	PRO	0	0.005	-0.009	26.684	-0.340	-0.340	0.000	0.000	0.000	0.000
74	A	76	LEU	0	0.011	0.011	23.075	-0.156	-0.156	0.000	0.000	0.000	0.000
75	A	77	PRO	0	0.013	0.010	27.505	0.176	0.176	0.000	0.000	0.000	0.000
76	A	78	ALA	0	0.032	0.029	28.608	-0.363	-0.363	0.000	0.000	0.000	0.000
77	A	79	GLY	0	-0.003	-0.008	28.596	0.292	0.292	0.000	0.000	0.000	0.000
78	A	80	THR	0	-0.044	-0.008	23.747	-0.152	-0.152	0.000	0.000	0.000	0.000
79	A	81	TYR	0	-0.005	-0.034	21.110	0.049	0.049	0.000	0.000	0.000	0.000
80	A	82	ARG	1	0.877	0.918	15.638	16.571	16.571	0.000	0.000	0.000	0.000
81	A	83	VAL	0	0.007	0.003	13.164	0.274	0.274	0.000	0.000	0.000	0.000
82	A	84	ASP	-1	-0.825	-0.893	12.976	-18.771	-18.771	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.886	0.930	7.220	26.224	26.224	0.000	0.000	0.000	0.000
90	A	92	THR	0	-0.081	-0.044	5.254	4.502	4.502	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.046	0.025	7.803	-1.042	-1.042	0.000	0.000	0.000	0.000
96	A	98	ASN	0	-0.091	-0.043	9.561	1.971	1.971	0.000	0.000	0.000	0.000
97	A	99	TYR	0	0.021	0.017	12.716	-0.845	-0.845	0.000	0.000	0.000	0.000
98	A	100	THR	0	0.038	0.017	15.344	0.538	0.538	0.000	0.000	0.000	0.000
99	A	101	PHE	0	0.019	0.009	18.818	-0.370	-0.370	0.000	0.000	0.000	0.000
100	A	102	THR	0	0.003	-0.006	21.158	0.385	0.385	0.000	0.000	0.000	0.000
101	A	103	VAL	0	-0.037	0.002	24.649	-0.134	-0.134	0.000	0.000	0.000	0.000
102	A	104	LYS	0	0.022	0.006	26.744	0.602	0.602	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:PRO)