FMO DATABASE

FMODB ID: ML8NZ

Calculation Name: 2IQQ-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2IQQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q5ZXE1

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	145
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1360846.634446
FMO2-HF: Nuclear repulsion	1304797.056263
FMO2-HF: Total energy	-56049.578183
FMO2-MP2: Total energy	-56213.933025

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:14:SER)

Summations of interaction energy for fragment #1(A:14:SER)

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.
-70.147	-64.978	0.297	-2.415	-3.053	-0.018

Interaction energy analysis for fragmet #1(A:14:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.871 / q_NPA : 0.917

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	16	HIS	0	0.030	0.032	3.037	7.417	9.778	0.002	-0.972	-1.391	-0.004
4	A	17	THR	0	-0.013	0.006	3.873	2.164	2.627	-0.001	-0.157	-0.306	-0.001
5	A	18	VAL	0	0.057	0.022	4.302	6.101	6.292	-0.001	-0.017	-0.173	0.000
134	A	147	GLY	0	-0.020	-0.022	2.931	-6.939	-6.491	0.070	-0.131	-0.387	-0.001
135	A	148	GLY	0	-0.065	-0.049	2.943	-16.508	-14.802	0.227	-1.138	-0.796	-0.012
6	A	19	GLY	0	0.068	0.027	6.042	5.035	5.035	0.000	0.000	0.000	0.000
7	A	20	PRO	0	0.008	-0.018	7.078	3.670	3.670	0.000	0.000	0.000	0.000
8	A	21	MET	0	-0.010	0.027	9.281	2.510	2.510	0.000	0.000	0.000	0.000
9	A	22	LEU	0	0.034	0.013	9.594	2.454	2.454	0.000	0.000	0.000	0.000
10	A	23	ALA	0	-0.017	-0.001	12.110	1.983	1.983	0.000	0.000	0.000	0.000
11	A	24	ALA	0	0.000	0.010	13.845	1.684	1.684	0.000	0.000	0.000	0.000
12	A	25	ASN	0	-0.031	-0.025	14.644	0.569	0.569	0.000	0.000	0.000	0.000
13	A	26	ALA	0	0.034	0.016	16.309	1.269	1.269	0.000	0.000	0.000	0.000
14	A	27	PHE	0	-0.013	-0.009	18.067	1.094	1.094	0.000	0.000	0.000	0.000
15	A	28	LEU	0	-0.004	0.014	19.275	1.037	1.037	0.000	0.000	0.000	0.000
16	A	29	GLN	0	-0.006	-0.011	18.798	0.205	0.205	0.000	0.000	0.000	0.000
17	A	30	LEU	0	-0.023	0.001	22.200	0.815	0.815	0.000	0.000	0.000	0.000
18	A	31	LEU	0	-0.007	-0.011	24.061	0.702	0.702	0.000	0.000	0.000	0.000
19	A	32	GLU	-1	-0.816	-0.895	25.722	-11.228	-11.228	0.000	0.000	0.000	0.000
20	A	33	GLN	0	-0.029	-0.009	26.202	0.308	0.308	0.000	0.000	0.000	0.000
21	A	34	LYS	1	0.891	0.945	27.559	11.942	11.942	0.000	0.000	0.000	0.000
22	A	35	ASN	0	-0.038	-0.009	29.938	0.256	0.256	0.000	0.000	0.000	0.000
23	A	36	LEU	0	-0.012	-0.014	28.551	0.301	0.301	0.000	0.000	0.000	0.000
24	A	37	PHE	0	0.020	0.033	25.221	0.025	0.025	0.000	0.000	0.000	0.000
25	A	38	ASP	-1	-0.832	-0.925	29.255	-9.850	-9.850	0.000	0.000	0.000	0.000
26	A	39	LYS	1	0.905	0.947	32.605	9.365	9.365	0.000	0.000	0.000	0.000
27	A	40	THR	0	-0.025	-0.016	26.458	-0.014	-0.014	0.000	0.000	0.000	0.000
28	A	41	GLN	0	-0.015	-0.008	29.884	0.002	0.002	0.000	0.000	0.000	0.000
29	A	42	ARG	1	0.897	0.946	26.547	11.741	11.741	0.000	0.000	0.000	0.000
30	A	43	VAL	0	0.020	-0.002	21.400	0.012	0.012	0.000	0.000	0.000	0.000
31	A	44	LYS	1	0.825	0.922	22.085	13.136	13.136	0.000	0.000	0.000	0.000
32	A	45	VAL	0	-0.005	-0.006	15.608	-0.240	-0.240	0.000	0.000	0.000	0.000
33	A	46	GLU	-1	-0.821	-0.887	18.305	-13.662	-13.662	0.000	0.000	0.000	0.000
34	A	47	LEU	0	-0.003	0.004	11.761	-0.841	-0.841	0.000	0.000	0.000	0.000
35	A	48	TYR	0	0.036	0.013	14.286	1.200	1.200	0.000	0.000	0.000	0.000
36	A	49	GLY	0	0.037	0.017	13.338	-1.761	-1.761	0.000	0.000	0.000	0.000
37	A	50	SER	0	-0.043	-0.027	8.407	0.075	0.075	0.000	0.000	0.000	0.000
38	A	51	LEU	0	-0.018	-0.011	7.748	-2.169	-2.169	0.000	0.000	0.000	0.000
39	A	52	ALA	0	-0.022	0.003	10.134	-0.065	-0.065	0.000	0.000	0.000	0.000
40	A	53	LEU	0	0.000	-0.010	11.641	0.974	0.974	0.000	0.000	0.000	0.000
41	A	54	THR	0	-0.051	-0.008	6.932	-0.802	-0.802	0.000	0.000	0.000	0.000
42	A	55	GLY	0	0.050	0.025	10.284	-0.328	-0.328	0.000	0.000	0.000	0.000
43	A	56	LYS	1	0.895	0.926	12.673	14.157	14.157	0.000	0.000	0.000	0.000
44	A	57	GLY	0	0.012	0.013	13.869	0.395	0.395	0.000	0.000	0.000	0.000
45	A	58	HIS	0	-0.115	-0.069	9.528	-0.802	-0.802	0.000	0.000	0.000	0.000
46	A	59	GLY	0	-0.053	-0.027	7.618	-4.165	-4.165	0.000	0.000	0.000	0.000
47	A	60	THR	0	0.019	-0.011	7.484	-0.100	-0.100	0.000	0.000	0.000	0.000
48	A	61	ASP	-1	-0.751	-0.866	9.160	-22.951	-22.951	0.000	0.000	0.000	0.000
49	A	62	LYS	1	0.932	0.958	9.773	28.003	28.003	0.000	0.000	0.000	0.000
50	A	63	ALA	0	-0.034	-0.011	8.152	1.007	1.007	0.000	0.000	0.000	0.000
51	A	64	ILE	0	-0.004	0.008	10.236	1.108	1.108	0.000	0.000	0.000	0.000
52	A	65	LEU	0	0.021	0.010	12.820	1.247	1.247	0.000	0.000	0.000	0.000
53	A	66	ASN	0	-0.027	-0.024	13.413	1.866	1.866	0.000	0.000	0.000	0.000
54	A	67	GLY	0	0.013	0.011	13.729	0.776	0.776	0.000	0.000	0.000	0.000
55	A	68	LEU	0	-0.021	-0.017	14.785	0.936	0.936	0.000	0.000	0.000	0.000
56	A	69	GLU	-1	-0.746	-0.837	17.837	-13.586	-13.586	0.000	0.000	0.000	0.000
57	A	70	ASN	0	-0.030	-0.026	18.522	-0.068	-0.068	0.000	0.000	0.000	0.000
58	A	71	LYS	1	0.896	0.975	15.472	16.646	16.646	0.000	0.000	0.000	0.000
59	A	72	ALA	0	0.100	0.037	13.751	-1.244	-1.244	0.000	0.000	0.000	0.000
60	A	73	PRO	0	-0.015	-0.033	8.893	0.319	0.319	0.000	0.000	0.000	0.000
61	A	74	GLU	-1	-0.972	-0.981	10.918	-22.765	-22.765	0.000	0.000	0.000	0.000
62	A	75	THR	0	-0.049	-0.029	12.570	1.901	1.901	0.000	0.000	0.000	0.000
63	A	76	VAL	0	-0.066	-0.006	12.082	1.167	1.167	0.000	0.000	0.000	0.000
64	A	77	ASP	-1	-0.813	-0.902	14.136	-18.555	-18.555	0.000	0.000	0.000	0.000
65	A	78	PRO	0	0.003	-0.015	10.874	-0.173	-0.173	0.000	0.000	0.000	0.000
66	A	79	ALA	0	-0.012	0.003	12.755	-0.454	-0.454	0.000	0.000	0.000	0.000
67	A	80	SER	0	-0.065	-0.051	15.623	0.769	0.769	0.000	0.000	0.000	0.000
68	A	81	MET	0	-0.004	-0.001	9.784	-0.321	-0.321	0.000	0.000	0.000	0.000
69	A	82	ILE	0	-0.006	-0.009	12.702	-0.093	-0.093	0.000	0.000	0.000	0.000
70	A	83	PRO	0	0.014	0.008	15.675	0.437	0.437	0.000	0.000	0.000	0.000
71	A	84	ARG	1	0.856	0.890	17.696	14.424	14.424	0.000	0.000	0.000	0.000
72	A	85	MET	0	-0.009	0.006	14.572	-0.181	-0.181	0.000	0.000	0.000	0.000
73	A	86	HIS	0	-0.041	-0.027	17.780	0.852	0.852	0.000	0.000	0.000	0.000
74	A	87	GLU	-1	-0.843	-0.907	20.678	-13.053	-13.053	0.000	0.000	0.000	0.000
75	A	88	ILE	0	-0.041	0.013	18.772	0.434	0.434	0.000	0.000	0.000	0.000
76	A	89	LEU	0	-0.067	-0.046	19.660	0.327	0.327	0.000	0.000	0.000	0.000
77	A	90	ASP	-1	-0.990	-0.986	22.978	-10.886	-10.886	0.000	0.000	0.000	0.000
78	A	91	SER	0	-0.023	-0.036	25.520	0.469	0.469	0.000	0.000	0.000	0.000
79	A	92	ASN	0	-0.075	-0.037	25.900	0.712	0.712	0.000	0.000	0.000	0.000
80	A	93	LEU	0	0.004	0.016	26.033	0.265	0.265	0.000	0.000	0.000	0.000
81	A	94	LEU	0	-0.016	-0.007	19.855	-0.589	-0.589	0.000	0.000	0.000	0.000
82	A	95	ASN	0	0.040	0.001	23.184	0.651	0.651	0.000	0.000	0.000	0.000
83	A	96	LEU	0	0.038	0.023	22.282	-0.576	-0.576	0.000	0.000	0.000	0.000
84	A	97	ALA	0	-0.027	-0.033	21.934	0.557	0.557	0.000	0.000	0.000	0.000
85	A	98	GLY	0	-0.019	-0.005	22.937	0.176	0.176	0.000	0.000	0.000	0.000
86	A	99	LYS	1	0.745	0.858	24.327	12.395	12.395	0.000	0.000	0.000	0.000
87	A	100	LYS	1	0.827	0.904	26.820	10.968	10.968	0.000	0.000	0.000	0.000
88	A	101	GLU	-1	-0.931	-0.952	26.945	-11.498	-11.498	0.000	0.000	0.000	0.000
89	A	102	ILE	0	-0.073	-0.025	24.897	0.477	0.477	0.000	0.000	0.000	0.000
90	A	103	PRO	0	0.005	-0.008	27.020	-0.291	-0.291	0.000	0.000	0.000	0.000
91	A	104	PHE	0	-0.030	-0.002	19.646	-0.493	-0.493	0.000	0.000	0.000	0.000
92	A	105	HIS	0	0.019	-0.001	25.278	0.286	0.286	0.000	0.000	0.000	0.000
93	A	106	GLU	-1	-0.775	-0.881	19.008	-15.742	-15.742	0.000	0.000	0.000	0.000
94	A	107	ALA	0	-0.035	-0.028	22.191	-0.274	-0.274	0.000	0.000	0.000	0.000
95	A	108	THR	0	-0.071	-0.031	24.507	0.236	0.236	0.000	0.000	0.000	0.000
96	A	109	ASP	-1	-0.773	-0.868	22.784	-12.425	-12.425	0.000	0.000	0.000	0.000
97	A	110	PHE	0	0.008	-0.007	13.470	-0.764	-0.764	0.000	0.000	0.000	0.000
98	A	111	LEU	0	-0.020	0.007	19.451	0.014	0.014	0.000	0.000	0.000	0.000
99	A	112	PHE	0	0.017	0.003	12.926	-0.698	-0.698	0.000	0.000	0.000	0.000
100	A	113	LEU	0	0.029	0.030	17.374	0.619	0.619	0.000	0.000	0.000	0.000
101	A	114	GLN	0	-0.016	-0.029	16.072	-0.351	-0.351	0.000	0.000	0.000	0.000
102	A	115	LYS	1	0.882	0.938	17.458	12.900	12.900	0.000	0.000	0.000	0.000
103	A	116	GLU	-1	-0.900	-0.940	19.389	-13.333	-13.333	0.000	0.000	0.000	0.000
104	A	117	LEU	0	-0.016	-0.022	16.527	-1.240	-1.240	0.000	0.000	0.000	0.000
105	A	118	LEU	0	-0.004	0.018	16.911	0.813	0.813	0.000	0.000	0.000	0.000
106	A	119	PRO	0	-0.012	-0.016	17.842	-0.525	-0.525	0.000	0.000	0.000	0.000
107	A	120	LYS	1	0.820	0.934	16.554	14.782	14.782	0.000	0.000	0.000	0.000
108	A	121	HIS	0	0.016	0.003	9.038	-0.621	-0.621	0.000	0.000	0.000	0.000
109	A	122	SER	0	0.039	0.016	11.534	0.240	0.240	0.000	0.000	0.000	0.000
110	A	123	ASN	0	-0.055	-0.037	6.457	0.743	0.743	0.000	0.000	0.000	0.000
111	A	124	GLY	0	0.045	0.021	10.506	-0.353	-0.353	0.000	0.000	0.000	0.000
112	A	125	MET	0	-0.029	-0.014	11.256	-0.868	-0.868	0.000	0.000	0.000	0.000
113	A	126	ARG	1	0.885	0.934	15.402	14.839	14.839	0.000	0.000	0.000	0.000
114	A	127	PHE	0	0.026	0.016	14.482	-0.390	-0.390	0.000	0.000	0.000	0.000
115	A	128	SER	0	-0.008	-0.021	20.089	0.652	0.652	0.000	0.000	0.000	0.000
116	A	129	ALA	0	0.015	0.026	23.841	-0.166	-0.166	0.000	0.000	0.000	0.000
117	A	130	PHE	0	0.001	-0.009	25.826	0.271	0.271	0.000	0.000	0.000	0.000
118	A	131	ASP	-1	-0.747	-0.878	29.772	-9.337	-9.337	0.000	0.000	0.000	0.000
119	A	132	GLY	0	-0.017	-0.018	32.871	-0.097	-0.097	0.000	0.000	0.000	0.000
120	A	133	ASN	0	-0.069	-0.024	35.121	0.269	0.269	0.000	0.000	0.000	0.000
121	A	134	ALA	0	-0.023	-0.004	32.943	0.079	0.079	0.000	0.000	0.000	0.000
122	A	135	ASN	0	-0.035	-0.016	33.208	-0.015	-0.015	0.000	0.000	0.000	0.000
123	A	136	LEU	0	-0.014	-0.010	27.485	-0.174	-0.174	0.000	0.000	0.000	0.000
124	A	137	LEU	0	-0.067	-0.031	29.662	0.294	0.294	0.000	0.000	0.000	0.000
125	A	138	ILE	0	-0.016	-0.018	25.660	0.142	0.142	0.000	0.000	0.000	0.000
126	A	139	GLU	-1	-0.903	-0.948	24.185	-12.966	-12.966	0.000	0.000	0.000	0.000
127	A	140	GLN	0	-0.090	-0.069	19.785	0.761	0.761	0.000	0.000	0.000	0.000
128	A	141	VAL	0	0.000	0.021	17.875	-0.635	-0.635	0.000	0.000	0.000	0.000
129	A	142	TYR	0	0.016	-0.003	14.455	0.188	0.188	0.000	0.000	0.000	0.000
130	A	143	TYR	0	-0.024	-0.039	12.285	-0.624	-0.624	0.000	0.000	0.000	0.000
131	A	144	SER	0	-0.034	-0.020	7.313	0.951	0.951	0.000	0.000	0.000	0.000
132	A	145	ILE	0	0.045	0.017	7.850	-2.471	-2.471	0.000	0.000	0.000	0.000
133	A	146	GLY	0	0.035	0.014	6.382	-0.937	-0.937	0.000	0.000	0.000	0.000
136	A	149	PHE	0	0.001	0.022	5.522	2.691	2.691	0.000	0.000	0.000	0.000
137	A	150	ILE	0	-0.011	-0.002	9.060	-1.871	-1.871	0.000	0.000	0.000	0.000
138	A	151	THR	0	0.017	0.013	11.909	1.450	1.450	0.000	0.000	0.000	0.000
139	A	152	THR	0	0.015	0.016	15.123	-0.853	-0.853	0.000	0.000	0.000	0.000
140	A	153	GLU	-1	-0.784	-0.883	17.993	-16.044	-16.044	0.000	0.000	0.000	0.000
141	A	154	GLU	-1	-0.835	-0.936	19.942	-13.936	-13.936	0.000	0.000	0.000	0.000
142	A	155	ASP	-1	-0.870	-0.922	19.370	-13.654	-13.654	0.000	0.000	0.000	0.000
143	A	156	PHE	0	-0.054	-0.015	14.004	-0.643	-0.643	0.000	0.000	0.000	0.000
144	A	157	ASP	-1	-0.895	-0.942	18.266	-14.873	-14.873	0.000	0.000	0.000	0.000
145	A	158	LYS	0	-0.142	-0.068	20.041	-0.723	-0.723	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:14:SER)