FMO DATABASE

FMODB ID: Z7MLN

Calculation Name: 2IVY-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2IVY

Chain ID: A

ChEMBL ID:

UniProt ID: Q97YC2

Base Structure: X-ray

Registration Date: 2025-10-04

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	88
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-626466.520526
FMO2-HF: Nuclear repulsion	590482.87566
FMO2-HF: Total energy	-35983.644866
FMO2-MP2: Total energy	-36089.910764

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:ALA)

Summations of interaction energy for fragment #1(A:2: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.
0.79199999999996	5.237	3.403	-3.582	-4.263	-0.03

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.796 / q_NPA : 0.893

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	LEU	0	0.084	0.063	3.536	-1.016	0.676	0.009	-0.762	-0.939	-0.002
39	A	40	ASP	-1	-0.876	-0.928	2.333	-67.508	-67.085	1.547	-1.016	-0.953	-0.007
40	A	41	LEU	0	-0.048	-0.017	2.899	4.765	5.651	0.188	-0.322	-0.751	-0.004
41	A	42	ASN	0	0.024	0.002	2.545	-11.322	-9.923	1.653	-1.450	-1.601	-0.017
42	A	43	SER	0	0.078	0.028	4.086	5.485	5.530	0.006	-0.032	-0.019	0.000
4	A	5	TYR	0	-0.029	-0.027	4.872	2.420	2.420	0.000	0.000	0.000	0.000
5	A	6	LEU	0	0.023	0.016	8.097	0.639	0.639	0.000	0.000	0.000	0.000
6	A	7	ILE	0	-0.013	-0.022	10.143	0.119	0.119	0.000	0.000	0.000	0.000
7	A	8	PHE	0	0.033	0.023	13.633	0.487	0.487	0.000	0.000	0.000	0.000
8	A	9	TYR	0	-0.001	-0.007	17.459	-0.250	-0.250	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.820	-0.862	20.167	-10.898	-10.898	0.000	0.000	0.000	0.000
10	A	11	ILE	0	-0.010	-0.010	21.217	0.080	0.080	0.000	0.000	0.000	0.000
11	A	12	THR	0	0.050	0.029	25.444	0.036	0.036	0.000	0.000	0.000	0.000
12	A	13	ASP	-1	-0.833	-0.906	28.355	-9.849	-9.849	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.762	-0.876	27.433	-10.286	-10.286	0.000	0.000	0.000	0.000
14	A	15	ASN	0	-0.061	-0.024	27.278	-0.449	-0.449	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.026	-0.029	24.852	-0.444	-0.444	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.815	0.887	23.129	10.275	10.275	0.000	0.000	0.000	0.000
17	A	18	ASN	0	-0.004	-0.003	22.272	-0.840	-0.840	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.954	0.985	22.257	11.400	11.400	0.000	0.000	0.000	0.000
19	A	20	VAL	0	0.001	0.004	17.599	-0.668	-0.668	0.000	0.000	0.000	0.000
20	A	21	ALA	0	-0.003	0.003	17.774	-0.876	-0.876	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.909	-0.969	18.207	-13.062	-13.062	0.000	0.000	0.000	0.000
22	A	23	PHE	0	-0.063	-0.012	14.214	-0.517	-0.517	0.000	0.000	0.000	0.000
23	A	24	LEU	0	0.024	0.003	12.688	-1.031	-1.031	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.989	0.999	13.250	13.350	13.350	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.844	0.919	14.845	13.213	13.213	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.811	0.903	10.735	19.714	19.714	0.000	0.000	0.000	0.000
27	A	28	GLY	0	-0.017	-0.001	10.061	-2.385	-2.385	0.000	0.000	0.000	0.000
28	A	29	LEU	0	-0.065	-0.016	7.730	-1.975	-1.975	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.865	-0.928	10.564	-22.575	-22.575	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.798	0.893	13.149	14.164	14.164	0.000	0.000	0.000	0.000
31	A	32	ILE	0	0.003	-0.008	14.862	0.507	0.507	0.000	0.000	0.000	0.000
32	A	33	GLN	0	0.064	0.044	17.769	0.574	0.574	0.000	0.000	0.000	0.000
33	A	34	TYR	0	0.024	0.016	19.975	-0.402	-0.402	0.000	0.000	0.000	0.000
34	A	35	SER	0	-0.018	-0.018	20.764	0.031	0.031	0.000	0.000	0.000	0.000
35	A	36	VAL	0	0.016	0.005	15.817	-0.286	-0.286	0.000	0.000	0.000	0.000
36	A	37	PHE	0	-0.007	-0.010	12.802	0.612	0.612	0.000	0.000	0.000	0.000
37	A	38	MET	0	0.020	0.017	10.372	0.584	0.584	0.000	0.000	0.000	0.000
38	A	39	GLY	0	0.092	0.041	7.649	1.208	1.208	0.000	0.000	0.000	0.000
43	A	44	SER	0	-0.006	0.004	7.170	3.129	3.129	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.914	0.934	4.954	38.200	38.200	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.028	0.031	6.997	1.974	1.974	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.944	0.963	8.559	26.549	26.549	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.854	-0.902	11.411	-18.994	-18.994	0.000	0.000	0.000	0.000
48	A	49	VAL	0	0.032	0.007	9.685	1.578	1.578	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.856	-0.918	12.329	-17.411	-17.411	0.000	0.000	0.000	0.000
50	A	51	ALA	0	-0.004	-0.005	14.200	1.309	1.309	0.000	0.000	0.000	0.000
51	A	52	GLY	0	0.015	0.004	15.872	1.025	1.025	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.006	-0.010	14.201	0.927	0.927	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.862	0.912	17.441	16.862	16.862	0.000	0.000	0.000	0.000
54	A	55	ILE	0	-0.021	-0.008	19.985	0.771	0.771	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.105	-0.053	19.126	0.692	0.692	0.000	0.000	0.000	0.000
56	A	57	GLY	0	0.031	0.013	22.142	0.516	0.516	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.052	-0.007	23.945	0.479	0.479	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.932	0.959	26.061	10.473	10.473	0.000	0.000	0.000	0.000
59	A	60	LYS	1	0.951	0.986	29.276	8.079	8.079	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.863	0.941	30.822	9.568	9.568	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.069	-0.050	32.670	0.225	0.225	0.000	0.000	0.000	0.000
62	A	63	GLN	0	-0.028	-0.014	35.447	0.272	0.272	0.000	0.000	0.000	0.000
63	A	64	GLU	-1	-0.851	-0.923	35.220	-8.051	-8.051	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.890	-0.950	34.538	-8.583	-8.583	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.869	-0.926	30.887	-9.682	-9.682	0.000	0.000	0.000	0.000
66	A	67	ARG	1	0.789	0.840	27.609	10.227	10.227	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.045	0.017	21.160	-0.096	-0.096	0.000	0.000	0.000	0.000
68	A	69	PHE	0	-0.004	0.007	21.105	-0.025	-0.025	0.000	0.000	0.000	0.000
69	A	70	ILE	0	-0.003	-0.015	16.340	-0.174	-0.174	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.017	0.011	16.403	0.050	0.050	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.003	-0.003	10.771	-0.596	-0.596	0.000	0.000	0.000	0.000
72	A	73	VAL	0	0.016	0.002	12.234	0.470	0.470	0.000	0.000	0.000	0.000
73	A	74	PRO	0	-0.021	0.000	8.606	-1.226	-1.226	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.010	-0.008	9.142	2.939	2.939	0.000	0.000	0.000	0.000
75	A	76	THR	0	0.000	-0.017	9.095	-3.568	-3.568	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.851	-0.956	8.523	-28.286	-28.286	0.000	0.000	0.000	0.000
77	A	78	ASN	0	-0.095	-0.033	11.063	1.937	1.937	0.000	0.000	0.000	0.000
78	A	79	GLN	0	0.125	0.069	13.642	-0.607	-0.607	0.000	0.000	0.000	0.000
79	A	80	PHE	0	0.023	0.010	12.723	1.259	1.259	0.000	0.000	0.000	0.000
80	A	81	ARG	1	0.872	0.940	12.618	23.191	23.191	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.879	-0.943	17.223	-16.802	-16.802	0.000	0.000	0.000	0.000
82	A	83	ARG	1	0.840	0.937	16.975	17.871	17.871	0.000	0.000	0.000	0.000
83	A	84	ILE	0	0.036	0.017	19.814	0.426	0.426	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.052	-0.034	21.353	-0.382	-0.382	0.000	0.000	0.000	0.000
85	A	86	ILE	0	0.012	0.005	24.044	0.343	0.343	0.000	0.000	0.000	0.000
86	A	87	GLY	0	-0.011	-0.012	27.033	-0.306	-0.306	0.000	0.000	0.000	0.000
87	A	88	TYR	0	-0.048	-0.023	29.500	0.118	0.118	0.000	0.000	0.000	0.000
88	A	89	SER	-1	-0.925	-0.943	32.647	-8.902	-8.902	0.000	0.000	0.000	0.000

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