FMO DATABASE

FMODB ID: ZL2VN

Calculation Name: 2QIY-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 2QIY

Chain ID: A

ChEMBL ID:

UniProt ID: P53741

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	141
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1365133.697056
FMO2-HF: Nuclear repulsion	1307947.160895
FMO2-HF: Total energy	-57186.53616
FMO2-MP2: Total energy	-57353.247662

3D Structure

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:VAL)

Summations of interaction energy for fragment #1(A:3:VAL)

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.
-26.965	-20.885	5.846	-5.268	-6.658	-0.044

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.820 / q_NPA : 0.910

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	5	VAL	0	0.067	0.022	3.028	-2.230	0.428	0.132	-1.327	-1.462	-0.007
5	A	7	ASP	-1	-0.818	-0.897	2.253	-69.296	-66.174	4.039	-3.532	-3.629	-0.034
6	A	8	ILE	0	-0.010	-0.009	2.504	3.385	3.632	1.675	-0.388	-1.535	-0.003
7	A	9	CYS	0	-0.021	0.004	4.464	4.786	4.839	0.000	-0.021	-0.032	0.000
4	A	6	GLN	0	0.052	0.034	5.737	5.457	5.457	0.000	0.000	0.000	0.000
8	A	10	PHE	0	0.025	0.017	7.455	2.464	2.464	0.000	0.000	0.000	0.000
9	A	11	ALA	0	0.015	0.002	5.860	2.187	2.187	0.000	0.000	0.000	0.000
10	A	12	PHE	0	-0.027	-0.012	7.861	2.242	2.242	0.000	0.000	0.000	0.000
11	A	13	LEU	0	0.038	0.006	9.731	1.850	1.850	0.000	0.000	0.000	0.000
12	A	14	GLN	0	0.004	0.011	11.394	0.405	0.405	0.000	0.000	0.000	0.000
13	A	15	ASN	0	0.006	-0.014	8.955	2.299	2.299	0.000	0.000	0.000	0.000
14	A	16	TYR	0	-0.080	-0.045	12.683	1.121	1.121	0.000	0.000	0.000	0.000
15	A	17	TYR	0	0.034	-0.017	15.193	0.798	0.798	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.863	-0.930	15.558	-15.671	-15.671	0.000	0.000	0.000	0.000
17	A	19	ARG	1	0.901	0.975	13.813	17.618	17.618	0.000	0.000	0.000	0.000
18	A	20	MET	0	-0.054	-0.008	18.305	0.751	0.751	0.000	0.000	0.000	0.000
19	A	21	ARG	1	0.888	0.952	17.872	14.911	14.911	0.000	0.000	0.000	0.000
20	A	22	THR	0	-0.055	-0.045	19.369	0.425	0.425	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.808	-0.885	21.509	-11.218	-11.218	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.018	0.016	22.026	-0.364	-0.364	0.000	0.000	0.000	0.000
23	A	25	SER	0	-0.067	-0.040	23.974	-0.043	-0.043	0.000	0.000	0.000	0.000
24	A	26	LYS	1	0.906	0.937	20.115	12.233	12.233	0.000	0.000	0.000	0.000
25	A	27	LEU	0	-0.030	0.000	18.816	-0.709	-0.709	0.000	0.000	0.000	0.000
26	A	28	ALA	0	0.017	-0.007	19.084	-0.602	-0.602	0.000	0.000	0.000	0.000
27	A	29	TYR	0	-0.026	-0.009	15.782	0.257	0.257	0.000	0.000	0.000	0.000
28	A	30	PHE	0	-0.006	-0.003	13.200	-0.176	-0.176	0.000	0.000	0.000	0.000
29	A	31	TYR	0	-0.012	-0.011	15.874	-0.680	-0.680	0.000	0.000	0.000	0.000
30	A	32	ALA	0	0.076	0.052	18.607	0.167	0.167	0.000	0.000	0.000	0.000
31	A	33	SER	0	-0.010	-0.023	19.722	0.373	0.373	0.000	0.000	0.000	0.000
32	A	34	THR	0	0.001	-0.014	23.164	0.337	0.337	0.000	0.000	0.000	0.000
33	A	35	ALA	0	-0.010	0.023	21.087	0.184	0.184	0.000	0.000	0.000	0.000
34	A	36	GLU	-1	-0.959	-0.974	22.983	-10.535	-10.535	0.000	0.000	0.000	0.000
35	A	37	LEU	0	-0.035	-0.007	22.407	-0.543	-0.543	0.000	0.000	0.000	0.000
36	A	38	THR	0	-0.045	-0.031	24.444	0.684	0.684	0.000	0.000	0.000	0.000
37	A	39	HIS	0	0.082	0.033	22.464	0.109	0.109	0.000	0.000	0.000	0.000
38	A	40	THR	0	0.074	0.033	26.637	0.331	0.331	0.000	0.000	0.000	0.000
39	A	41	ASN	0	-0.021	-0.020	29.037	0.001	0.001	0.000	0.000	0.000	0.000
40	A	42	TYR	0	0.047	0.023	26.357	0.294	0.294	0.000	0.000	0.000	0.000
41	A	43	GLN	0	0.001	0.002	33.035	0.097	0.097	0.000	0.000	0.000	0.000
42	A	44	SER	0	-0.019	-0.006	36.680	0.126	0.126	0.000	0.000	0.000	0.000
43	A	45	LYS	1	0.867	0.939	35.914	7.943	7.943	0.000	0.000	0.000	0.000
44	A	46	SER	0	0.020	-0.001	35.912	0.159	0.159	0.000	0.000	0.000	0.000
45	A	47	THR	0	-0.060	-0.039	38.103	0.001	0.001	0.000	0.000	0.000	0.000
46	A	48	ASN	0	0.016	0.000	35.408	-0.243	-0.243	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.875	-0.939	37.737	-7.669	-7.669	0.000	0.000	0.000	0.000
48	A	50	LYS	1	0.790	0.884	40.266	7.358	7.358	0.000	0.000	0.000	0.000
49	A	51	ASP	-1	-0.799	-0.881	38.013	-7.442	-7.442	0.000	0.000	0.000	0.000
50	A	52	ASP	-1	-0.800	-0.907	35.241	-8.472	-8.472	0.000	0.000	0.000	0.000
51	A	53	VAL	0	-0.048	-0.016	31.982	-0.377	-0.377	0.000	0.000	0.000	0.000
52	A	54	LEU	0	-0.030	0.014	30.055	0.240	0.240	0.000	0.000	0.000	0.000
53	A	55	PRO	0	0.000	0.010	32.095	-0.170	-0.170	0.000	0.000	0.000	0.000
54	A	56	THR	0	-0.020	-0.015	28.322	-0.085	-0.085	0.000	0.000	0.000	0.000
55	A	57	VAL	0	-0.049	-0.023	30.252	0.328	0.328	0.000	0.000	0.000	0.000
56	A	58	LYS	1	0.949	0.977	29.158	9.443	9.443	0.000	0.000	0.000	0.000
57	A	59	VAL	0	-0.031	-0.013	27.536	0.345	0.345	0.000	0.000	0.000	0.000
58	A	60	THR	0	0.078	0.033	27.110	-0.304	-0.304	0.000	0.000	0.000	0.000
59	A	61	GLY	0	0.024	0.028	26.448	0.420	0.420	0.000	0.000	0.000	0.000
60	A	62	ARG	1	0.889	0.930	19.776	13.633	13.633	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.895	-0.945	25.002	-9.895	-9.895	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.080	-0.053	28.144	0.472	0.472	0.000	0.000	0.000	0.000
63	A	65	ILE	0	0.021	0.016	22.657	0.170	0.170	0.000	0.000	0.000	0.000
64	A	66	ASN	0	0.034	0.010	25.668	-0.257	-0.257	0.000	0.000	0.000	0.000
65	A	67	LYS	1	0.899	0.962	26.473	9.086	9.086	0.000	0.000	0.000	0.000
66	A	68	PHE	0	-0.034	-0.009	26.215	0.328	0.328	0.000	0.000	0.000	0.000
67	A	69	PHE	0	0.050	0.016	22.237	0.212	0.212	0.000	0.000	0.000	0.000
68	A	70	SER	0	0.010	-0.010	27.013	0.109	0.109	0.000	0.000	0.000	0.000
69	A	71	ARG	1	0.833	0.915	29.144	8.812	8.812	0.000	0.000	0.000	0.000
70	A	72	ASN	0	-0.015	-0.013	29.432	0.506	0.506	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.767	-0.855	27.716	-10.370	-10.370	0.000	0.000	0.000	0.000
72	A	74	ALA	0	0.054	0.016	28.271	-0.232	-0.232	0.000	0.000	0.000	0.000
73	A	75	LYS	1	0.901	0.965	30.320	9.196	9.196	0.000	0.000	0.000	0.000
74	A	76	VAL	0	-0.004	0.009	24.071	-0.166	-0.166	0.000	0.000	0.000	0.000
75	A	77	ARG	1	0.863	0.906	25.148	10.440	10.440	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.117	-0.068	26.108	-0.034	-0.034	0.000	0.000	0.000	0.000
77	A	79	LEU	0	-0.005	-0.001	22.167	0.163	0.163	0.000	0.000	0.000	0.000
78	A	80	LYS	1	0.874	0.941	23.659	10.446	10.446	0.000	0.000	0.000	0.000
79	A	81	LEU	0	-0.003	-0.004	18.752	0.208	0.208	0.000	0.000	0.000	0.000
80	A	82	LYS	1	0.870	0.942	21.771	11.834	11.834	0.000	0.000	0.000	0.000
81	A	83	LEU	0	-0.008	-0.017	14.989	0.136	0.136	0.000	0.000	0.000	0.000
82	A	84	ASP	-1	-0.847	-0.908	19.203	-12.627	-12.627	0.000	0.000	0.000	0.000
83	A	85	THR	0	-0.025	0.005	17.737	-0.143	-0.143	0.000	0.000	0.000	0.000
84	A	86	ILE	0	-0.007	-0.021	11.465	-0.301	-0.301	0.000	0.000	0.000	0.000
85	A	87	ASP	-1	-0.884	-0.920	14.611	-16.501	-16.501	0.000	0.000	0.000	0.000
86	A	88	PHE	0	0.000	-0.027	10.257	-0.776	-0.776	0.000	0.000	0.000	0.000
87	A	89	GLN	0	-0.020	-0.006	13.117	0.517	0.517	0.000	0.000	0.000	0.000
88	A	90	TYR	0	-0.002	0.010	6.575	-1.465	-1.465	0.000	0.000	0.000	0.000
89	A	91	THR	0	0.027	0.002	13.115	1.637	1.637	0.000	0.000	0.000	0.000
90	A	92	GLY	0	0.026	0.015	15.116	-0.742	-0.742	0.000	0.000	0.000	0.000
91	A	93	HIS	0	0.060	0.024	17.299	0.016	0.016	0.000	0.000	0.000	0.000
92	A	94	LEU	0	-0.001	-0.008	15.514	-1.126	-1.126	0.000	0.000	0.000	0.000
93	A	95	HIS	0	0.012	0.016	14.648	-0.986	-0.986	0.000	0.000	0.000	0.000
94	A	96	LYS	1	0.861	0.926	10.463	20.788	20.788	0.000	0.000	0.000	0.000
95	A	97	SER	0	0.025	0.014	10.800	-1.443	-1.443	0.000	0.000	0.000	0.000
96	A	98	ILE	0	-0.032	-0.016	7.540	-0.569	-0.569	0.000	0.000	0.000	0.000
97	A	99	LEU	0	0.002	0.008	12.102	0.902	0.902	0.000	0.000	0.000	0.000
98	A	100	ILE	0	0.001	-0.007	10.127	-1.229	-1.229	0.000	0.000	0.000	0.000
99	A	101	MET	0	-0.013	-0.007	14.010	1.113	1.113	0.000	0.000	0.000	0.000
100	A	102	ALA	0	0.026	0.019	15.774	-0.867	-0.867	0.000	0.000	0.000	0.000
101	A	103	THR	0	-0.017	-0.030	17.442	0.985	0.985	0.000	0.000	0.000	0.000
102	A	104	GLY	0	0.062	0.037	20.231	-0.573	-0.573	0.000	0.000	0.000	0.000
103	A	105	GLU	-1	-0.864	-0.909	22.761	-10.050	-10.050	0.000	0.000	0.000	0.000
104	A	106	MET	0	-0.020	-0.001	22.287	-0.173	-0.173	0.000	0.000	0.000	0.000
105	A	107	PHE	0	0.016	0.000	25.692	0.404	0.404	0.000	0.000	0.000	0.000
106	A	108	TRP	0	-0.002	-0.009	27.146	-0.225	-0.225	0.000	0.000	0.000	0.000
107	A	109	THR	0	-0.039	-0.042	29.374	0.051	0.051	0.000	0.000	0.000	0.000
108	A	110	GLY	0	-0.006	0.006	31.283	0.173	0.173	0.000	0.000	0.000	0.000
109	A	111	THR	0	-0.037	-0.015	31.875	0.137	0.137	0.000	0.000	0.000	0.000
110	A	112	PRO	0	0.037	0.027	32.903	-0.167	-0.167	0.000	0.000	0.000	0.000
111	A	113	VAL	0	-0.008	-0.003	28.587	-0.183	-0.183	0.000	0.000	0.000	0.000
112	A	114	TYR	0	0.022	0.003	29.167	0.279	0.279	0.000	0.000	0.000	0.000
113	A	115	LYS	1	0.916	0.947	27.015	10.168	10.168	0.000	0.000	0.000	0.000
114	A	116	PHE	0	-0.062	-0.031	20.252	0.244	0.244	0.000	0.000	0.000	0.000
115	A	117	CYS	0	0.003	0.019	22.153	-0.263	-0.263	0.000	0.000	0.000	0.000
116	A	118	GLN	0	0.008	-0.020	19.310	0.462	0.462	0.000	0.000	0.000	0.000
117	A	119	THR	0	-0.018	-0.001	18.303	-0.670	-0.670	0.000	0.000	0.000	0.000
118	A	120	PHE	0	0.003	-0.009	14.838	0.403	0.403	0.000	0.000	0.000	0.000
119	A	121	ILE	0	-0.024	-0.006	15.575	-0.466	-0.466	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.001	0.008	9.774	0.365	0.365	0.000	0.000	0.000	0.000
121	A	123	LEU	0	0.024	0.000	13.123	-0.447	-0.447	0.000	0.000	0.000	0.000
122	A	124	PRO	0	-0.030	-0.018	10.090	-0.023	-0.023	0.000	0.000	0.000	0.000
123	A	125	SER	0	0.007	-0.020	11.867	0.537	0.537	0.000	0.000	0.000	0.000
124	A	126	SER	0	-0.009	-0.023	11.179	0.527	0.527	0.000	0.000	0.000	0.000
125	A	127	ASN	0	-0.009	-0.019	9.443	-0.864	-0.864	0.000	0.000	0.000	0.000
126	A	128	GLY	0	0.005	0.014	6.951	-2.568	-2.568	0.000	0.000	0.000	0.000
127	A	129	SER	0	-0.053	-0.018	6.095	-1.849	-1.849	0.000	0.000	0.000	0.000
128	A	130	THR	0	-0.018	0.001	7.063	-0.124	-0.124	0.000	0.000	0.000	0.000
129	A	131	PHE	0	-0.016	-0.010	6.356	-0.078	-0.078	0.000	0.000	0.000	0.000
130	A	132	ASP	-1	-0.833	-0.878	11.057	-16.850	-16.850	0.000	0.000	0.000	0.000
131	A	133	ILE	0	-0.036	-0.022	14.674	-0.222	-0.222	0.000	0.000	0.000	0.000
132	A	134	THR	0	0.010	-0.016	16.416	0.604	0.604	0.000	0.000	0.000	0.000
133	A	135	ASN	0	0.003	0.007	18.560	0.387	0.387	0.000	0.000	0.000	0.000
134	A	136	ASP	-1	-0.732	-0.816	18.596	-14.710	-14.710	0.000	0.000	0.000	0.000
135	A	137	ILE	0	0.013	0.001	20.478	0.754	0.754	0.000	0.000	0.000	0.000
136	A	138	ILE	0	-0.007	0.014	22.228	-0.383	-0.383	0.000	0.000	0.000	0.000
137	A	139	ARG	1	0.904	0.943	24.133	10.264	10.264	0.000	0.000	0.000	0.000
138	A	140	PHE	0	0.027	0.006	26.421	-0.241	-0.241	0.000	0.000	0.000	0.000
139	A	141	ILE	0	-0.063	-0.045	26.031	0.168	0.168	0.000	0.000	0.000	0.000
140	A	142	SER	0	0.059	0.040	30.289	0.023	0.023	0.000	0.000	0.000	0.000
141	A	143	ASN	-1	-0.963	-0.978	32.143	-9.066	-9.066	0.000	0.000	0.000	0.000

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