FMO DATABASE

FMODB ID: 9Q1N2

Calculation Name: 1MP1-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1MP1

Chain ID: A

ChEMBL ID:

UniProt ID: Q8IYB3

Base Structure: SolutionNMR

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	111
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230712

Total energy (hartree)

FMO2-HF: Electronic energy	-937651.524178
FMO2-HF: Nuclear repulsion	892198.271471
FMO2-HF: Total energy	-45453.252707
FMO2-MP2: Total energy	-45584.066135

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:24:SER)

Summations of interaction energy for fragment #1(A:24: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.
-48.248	-43.553	0.178	-2.095	-2.778	-0.012

Interaction energy analysis for fragmet #1(A:24:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.842 / q_NPA : 0.907

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	26	MET	0	0.013	0.062	3.136	6.510	8.533	0.010	-0.973	-1.059	-0.004
4	A	27	GLN	0	-0.033	-0.020	3.203	-6.692	-5.210	0.057	-0.750	-0.790	-0.006
5	A	28	LEU	0	0.010	0.013	5.107	3.863	3.876	-0.001	-0.003	-0.008	0.000
61	A	84	MET	0	0.000	-0.011	2.983	-5.530	-4.809	0.093	-0.263	-0.551	-0.002
64	A	87	ILE	0	-0.061	-0.026	3.281	0.133	0.442	0.020	-0.092	-0.238	0.000
65	A	88	ASN	0	0.021	-0.020	4.718	-5.567	-5.420	-0.001	-0.014	-0.132	0.000
6	A	29	LYS	1	0.941	0.974	8.509	17.698	17.698	0.000	0.000	0.000	0.000
7	A	30	PHE	0	0.057	0.021	8.268	0.528	0.528	0.000	0.000	0.000	0.000
8	A	31	ALA	0	-0.012	-0.013	12.493	1.126	1.126	0.000	0.000	0.000	0.000
9	A	32	GLU	-1	-0.869	-0.940	15.348	-15.456	-15.456	0.000	0.000	0.000	0.000
10	A	33	CYS	0	-0.055	-0.022	17.943	0.084	0.084	0.000	0.000	0.000	0.000
11	A	34	LEU	0	0.035	0.010	13.227	0.289	0.289	0.000	0.000	0.000	0.000
12	A	35	GLU	-1	-0.857	-0.906	14.847	-19.322	-19.322	0.000	0.000	0.000	0.000
13	A	36	LYS	1	0.895	0.942	17.132	13.343	13.343	0.000	0.000	0.000	0.000
14	A	37	LYS	1	0.920	0.974	17.284	15.773	15.773	0.000	0.000	0.000	0.000
15	A	38	VAL	0	0.063	0.032	17.421	0.355	0.355	0.000	0.000	0.000	0.000
16	A	39	ASP	-1	-0.794	-0.898	19.722	-13.547	-13.547	0.000	0.000	0.000	0.000
17	A	40	MET	0	0.019	0.022	18.622	0.538	0.538	0.000	0.000	0.000	0.000
18	A	41	SER	0	-0.071	-0.027	21.772	0.224	0.224	0.000	0.000	0.000	0.000
19	A	42	LYS	1	0.781	0.885	24.612	12.631	12.631	0.000	0.000	0.000	0.000
20	A	43	VAL	0	0.002	0.006	22.670	0.378	0.378	0.000	0.000	0.000	0.000
21	A	44	ASN	0	-0.015	0.006	23.819	-0.611	-0.611	0.000	0.000	0.000	0.000
22	A	45	LEU	0	0.036	-0.007	19.235	0.024	0.024	0.000	0.000	0.000	0.000
23	A	46	GLU	-1	-0.920	-0.959	21.994	-12.536	-12.536	0.000	0.000	0.000	0.000
24	A	47	VAL	0	0.056	0.019	24.142	0.005	0.005	0.000	0.000	0.000	0.000
25	A	48	ILE	0	-0.037	-0.022	21.338	0.137	0.137	0.000	0.000	0.000	0.000
26	A	49	LYS	1	0.910	0.992	16.835	16.409	16.409	0.000	0.000	0.000	0.000
27	A	50	PRO	0	0.067	0.057	21.758	-0.469	-0.469	0.000	0.000	0.000	0.000
28	A	51	TRP	0	-0.010	-0.007	20.043	-0.318	-0.318	0.000	0.000	0.000	0.000
29	A	52	ILE	0	-0.019	-0.024	17.105	-0.342	-0.342	0.000	0.000	0.000	0.000
30	A	53	THR	0	-0.005	-0.003	19.612	-0.648	-0.648	0.000	0.000	0.000	0.000
31	A	54	LYS	1	0.852	0.931	20.668	11.277	11.277	0.000	0.000	0.000	0.000
32	A	55	ARG	1	0.855	0.906	20.539	13.630	13.630	0.000	0.000	0.000	0.000
33	A	56	VAL	0	-0.072	-0.039	15.784	-0.120	-0.120	0.000	0.000	0.000	0.000
34	A	57	THR	0	0.061	0.009	18.711	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	58	GLU	-1	-0.851	-0.916	21.577	-11.193	-11.193	0.000	0.000	0.000	0.000
36	A	59	ILE	0	-0.119	-0.049	17.547	0.041	0.041	0.000	0.000	0.000	0.000
37	A	60	LEU	0	-0.107	-0.045	16.897	-0.031	-0.031	0.000	0.000	0.000	0.000
38	A	61	GLY	0	-0.011	0.002	21.044	0.430	0.430	0.000	0.000	0.000	0.000
39	A	62	PHE	0	-0.051	-0.024	18.359	0.616	0.616	0.000	0.000	0.000	0.000
40	A	63	GLU	-1	-0.832	-0.903	20.960	-13.732	-13.732	0.000	0.000	0.000	0.000
41	A	64	ASP	-1	-0.849	-0.946	15.778	-18.152	-18.152	0.000	0.000	0.000	0.000
42	A	65	ASP	-1	-0.833	-0.935	15.850	-16.358	-16.358	0.000	0.000	0.000	0.000
43	A	66	VAL	0	-0.028	-0.002	9.613	-0.848	-0.848	0.000	0.000	0.000	0.000
44	A	67	VAL	0	0.009	0.004	11.025	-1.938	-1.938	0.000	0.000	0.000	0.000
45	A	68	ILE	0	0.027	0.021	12.258	-0.316	-0.316	0.000	0.000	0.000	0.000
46	A	69	GLU	-1	-0.835	-0.919	12.148	-21.701	-21.701	0.000	0.000	0.000	0.000
47	A	70	PHE	0	-0.071	-0.035	5.639	-1.044	-1.044	0.000	0.000	0.000	0.000
48	A	71	ILE	0	0.033	-0.021	10.339	-0.480	-0.480	0.000	0.000	0.000	0.000
49	A	72	PHE	0	-0.021	-0.013	13.288	1.155	1.155	0.000	0.000	0.000	0.000
50	A	73	ASN	0	-0.002	-0.014	11.603	0.628	0.628	0.000	0.000	0.000	0.000
51	A	74	GLN	0	-0.061	-0.047	9.227	0.088	0.088	0.000	0.000	0.000	0.000
52	A	75	LEU	0	-0.061	-0.050	12.580	0.689	0.689	0.000	0.000	0.000	0.000
53	A	76	GLU	-1	-0.870	-0.918	15.921	-14.991	-14.991	0.000	0.000	0.000	0.000
54	A	77	VAL	0	-0.097	-0.032	13.979	0.748	0.748	0.000	0.000	0.000	0.000
55	A	78	LYS	1	0.993	0.978	16.932	15.545	15.545	0.000	0.000	0.000	0.000
56	A	79	ASN	0	-0.050	-0.034	16.296	0.402	0.402	0.000	0.000	0.000	0.000
57	A	80	PRO	0	0.036	0.038	13.576	-1.167	-1.167	0.000	0.000	0.000	0.000
58	A	81	ASP	-1	-0.795	-0.890	7.821	-30.457	-30.457	0.000	0.000	0.000	0.000
59	A	82	SER	0	-0.015	-0.022	10.196	-1.968	-1.968	0.000	0.000	0.000	0.000
60	A	83	LYS	1	0.795	0.890	8.120	22.742	22.742	0.000	0.000	0.000	0.000
62	A	85	MET	0	-0.001	0.032	6.603	-1.417	-1.417	0.000	0.000	0.000	0.000
63	A	86	GLN	0	0.060	0.011	9.942	1.446	1.446	0.000	0.000	0.000	0.000
66	A	89	LEU	0	0.048	0.036	7.045	1.612	1.612	0.000	0.000	0.000	0.000
67	A	90	THR	0	-0.070	-0.047	8.436	2.764	2.764	0.000	0.000	0.000	0.000
68	A	91	GLY	0	-0.020	-0.026	8.590	0.324	0.324	0.000	0.000	0.000	0.000
69	A	92	PHE	0	-0.022	-0.007	9.198	0.619	0.619	0.000	0.000	0.000	0.000
70	A	93	LEU	0	0.042	0.040	12.849	1.554	1.554	0.000	0.000	0.000	0.000
71	A	94	ASN	0	0.023	0.005	13.680	-0.752	-0.752	0.000	0.000	0.000	0.000
72	A	95	GLY	0	0.038	0.017	12.432	0.354	0.354	0.000	0.000	0.000	0.000
73	A	96	LYS	1	0.887	0.931	13.329	14.673	14.673	0.000	0.000	0.000	0.000
74	A	97	ASN	0	0.107	0.033	16.628	0.385	0.385	0.000	0.000	0.000	0.000
75	A	98	ALA	0	0.021	0.036	12.156	0.195	0.195	0.000	0.000	0.000	0.000
76	A	99	ARG	1	0.914	0.942	14.234	15.759	15.759	0.000	0.000	0.000	0.000
77	A	100	GLU	-1	-0.981	-0.983	15.508	-13.072	-13.072	0.000	0.000	0.000	0.000
78	A	101	PHE	0	0.021	0.013	15.499	0.407	0.407	0.000	0.000	0.000	0.000
79	A	102	MET	0	-0.022	0.000	13.118	0.375	0.375	0.000	0.000	0.000	0.000
80	A	103	GLY	0	-0.033	-0.025	16.564	0.396	0.396	0.000	0.000	0.000	0.000
81	A	104	GLU	-1	-0.837	-0.905	19.604	-11.891	-11.891	0.000	0.000	0.000	0.000
82	A	105	LEU	0	0.012	0.005	16.374	0.324	0.324	0.000	0.000	0.000	0.000
83	A	106	TRP	0	-0.022	-0.011	14.930	-0.018	-0.018	0.000	0.000	0.000	0.000
84	A	107	PRO	0	-0.018	-0.015	19.205	0.385	0.385	0.000	0.000	0.000	0.000
85	A	108	LEU	0	0.020	0.020	22.728	0.639	0.639	0.000	0.000	0.000	0.000
86	A	109	LEU	0	-0.003	-0.008	18.485	0.403	0.403	0.000	0.000	0.000	0.000
87	A	110	LEU	0	-0.046	-0.011	21.348	0.345	0.345	0.000	0.000	0.000	0.000
88	A	111	SER	0	0.014	-0.002	24.409	0.477	0.477	0.000	0.000	0.000	0.000
89	A	112	ALA	0	-0.013	-0.010	25.248	0.364	0.364	0.000	0.000	0.000	0.000
90	A	113	GLN	0	-0.024	-0.018	23.336	-0.237	-0.237	0.000	0.000	0.000	0.000
91	A	114	GLU	-1	-0.992	-0.974	26.897	-10.072	-10.072	0.000	0.000	0.000	0.000
92	A	115	ASN	0	-0.060	-0.025	29.827	0.590	0.590	0.000	0.000	0.000	0.000
93	A	116	ILE	0	-0.001	0.000	31.308	-0.110	-0.110	0.000	0.000	0.000	0.000
94	A	117	ALA	0	-0.015	-0.011	32.311	-0.100	-0.100	0.000	0.000	0.000	0.000
95	A	118	GLY	0	0.059	0.042	28.156	-0.223	-0.223	0.000	0.000	0.000	0.000
96	A	119	ILE	0	0.032	0.000	27.306	-0.435	-0.435	0.000	0.000	0.000	0.000
97	A	120	PRO	0	0.017	0.022	26.453	0.214	0.214	0.000	0.000	0.000	0.000
98	A	121	SER	0	0.067	0.015	28.967	0.100	0.100	0.000	0.000	0.000	0.000
99	A	122	ALA	0	-0.007	-0.002	28.766	0.289	0.289	0.000	0.000	0.000	0.000
100	A	123	PHE	0	-0.059	-0.053	25.919	0.024	0.024	0.000	0.000	0.000	0.000
101	A	124	LEU	0	-0.012	0.023	32.077	0.220	0.220	0.000	0.000	0.000	0.000
102	A	125	GLU	-1	-0.931	-0.949	35.070	-7.997	-7.997	0.000	0.000	0.000	0.000
103	A	126	LEU	0	-0.018	-0.020	33.039	0.220	0.220	0.000	0.000	0.000	0.000
104	A	127	LYS	1	0.898	0.943	35.000	7.929	7.929	0.000	0.000	0.000	0.000
105	A	128	LYS	1	0.864	0.930	30.229	10.014	10.014	0.000	0.000	0.000	0.000
106	A	129	GLU	-1	-0.890	-0.935	34.227	-8.449	-8.449	0.000	0.000	0.000	0.000
107	A	130	GLU	-1	-0.951	-0.983	29.668	-10.585	-10.585	0.000	0.000	0.000	0.000
108	A	131	ILE	0	-0.042	-0.014	30.248	0.036	0.036	0.000	0.000	0.000	0.000
109	A	132	LYS	1	0.846	0.906	23.438	12.353	12.353	0.000	0.000	0.000	0.000
110	A	133	GLN	0	-0.064	-0.023	26.880	0.771	0.771	0.000	0.000	0.000	0.000
111	A	134	ARG	0	0.105	0.052	25.540	-1.953	-1.953	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:24:SER)