FMO DATABASE

FMODB ID: Z942N

Calculation Name: 1MW5-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1MW5

Chain ID: A

ChEMBL ID:

UniProt ID: P44209

Base Structure: X-ray

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	162
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1524069.28649
FMO2-HF: Nuclear repulsion	1460360.539373
FMO2-HF: Total energy	-63708.747117
FMO2-MP2: Total energy	-63897.857299

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:GLU)

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

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.
8.19	12.008	0.131	-1.3	-2.648	-0.003

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.029 / q_NPA : -0.023

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	ASP	-1	-0.878	-0.937	2.848	-9.321	-6.863	0.079	-0.942	-1.594	-0.002
4	A	6	LEU	0	-0.025	0.002	2.859	3.981	5.014	0.054	-0.303	-0.784	-0.001
5	A	7	LEU	0	0.046	0.014	4.641	3.486	3.752	-0.001	-0.049	-0.216	0.000
141	A	143	ALA	0	-0.010	0.006	4.770	0.612	0.673	-0.001	-0.006	-0.054	0.000
6	A	8	MET	0	0.027	0.005	6.632	2.184	2.184	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.871	0.928	6.061	7.474	7.474	0.000	0.000	0.000	0.000
8	A	10	MET	0	-0.046	0.013	8.755	1.075	1.075	0.000	0.000	0.000	0.000
9	A	11	VAL	0	0.008	-0.001	10.863	0.578	0.578	0.000	0.000	0.000	0.000
10	A	12	ARG	1	0.906	0.968	9.326	4.182	4.182	0.000	0.000	0.000	0.000
11	A	13	GLN	0	-0.049	-0.027	12.299	0.557	0.557	0.000	0.000	0.000	0.000
12	A	14	PRO	0	0.045	0.022	16.205	-0.060	-0.060	0.000	0.000	0.000	0.000
13	A	15	VAL	0	-0.028	-0.006	13.454	-0.073	-0.073	0.000	0.000	0.000	0.000
14	A	16	LYS	1	0.922	0.974	16.569	1.083	1.083	0.000	0.000	0.000	0.000
15	A	17	LEU	0	0.013	0.007	16.654	-0.137	-0.137	0.000	0.000	0.000	0.000
16	A	18	TYR	0	-0.042	-0.053	17.699	0.088	0.088	0.000	0.000	0.000	0.000
17	A	19	SER	0	0.055	0.034	18.697	-0.029	-0.029	0.000	0.000	0.000	0.000
18	A	20	VAL	0	0.072	0.033	18.627	-0.025	-0.025	0.000	0.000	0.000	0.000
19	A	21	ALA	0	0.033	0.020	20.607	0.024	0.024	0.000	0.000	0.000	0.000
20	A	22	THR	0	-0.023	-0.022	21.810	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	23	LEU	0	0.020	0.017	16.128	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	24	PHE	0	0.045	0.014	20.467	0.022	0.022	0.000	0.000	0.000	0.000
23	A	25	HIS	0	0.007	0.023	22.783	0.012	0.012	0.000	0.000	0.000	0.000
24	A	26	GLU	-1	-0.724	-0.826	20.959	-0.820	-0.820	0.000	0.000	0.000	0.000
25	A	27	PHE	0	0.006	-0.014	16.991	0.016	0.016	0.000	0.000	0.000	0.000
26	A	28	SER	0	-0.018	-0.017	22.654	0.057	0.057	0.000	0.000	0.000	0.000
27	A	29	GLU	-1	-0.897	-0.940	26.069	-0.338	-0.338	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.035	-0.019	22.574	0.016	0.016	0.000	0.000	0.000	0.000
29	A	31	ILE	0	-0.013	-0.004	23.363	0.035	0.035	0.000	0.000	0.000	0.000
30	A	32	THR	0	0.000	-0.016	26.493	0.021	0.021	0.000	0.000	0.000	0.000
31	A	33	LYS	1	0.845	0.940	28.034	0.432	0.432	0.000	0.000	0.000	0.000
32	A	34	LEU	0	0.001	-0.005	24.387	0.014	0.014	0.000	0.000	0.000	0.000
33	A	35	GLU	-1	-0.839	-0.940	28.967	-0.091	-0.091	0.000	0.000	0.000	0.000
34	A	36	HIS	0	-0.021	-0.008	31.595	0.028	0.028	0.000	0.000	0.000	0.000
35	A	37	SER	0	-0.019	-0.028	31.283	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	38	VAL	0	-0.093	-0.035	32.200	0.013	0.013	0.000	0.000	0.000	0.000
37	A	39	GLN	0	0.003	0.007	34.450	0.013	0.013	0.000	0.000	0.000	0.000
38	A	40	LYS	1	0.936	0.964	37.165	0.052	0.052	0.000	0.000	0.000	0.000
39	A	41	GLU	-1	-0.773	-0.877	34.319	-0.018	-0.018	0.000	0.000	0.000	0.000
40	A	42	PRO	0	-0.096	-0.035	31.401	0.002	0.002	0.000	0.000	0.000	0.000
41	A	43	THR	0	0.038	0.014	34.200	0.013	0.013	0.000	0.000	0.000	0.000
42	A	44	SER	0	-0.014	-0.010	32.393	0.022	0.022	0.000	0.000	0.000	0.000
43	A	45	LEU	0	-0.001	-0.004	27.049	-0.026	-0.026	0.000	0.000	0.000	0.000
44	A	46	LEU	0	-0.046	-0.002	24.807	0.014	0.014	0.000	0.000	0.000	0.000
45	A	47	SER	0	0.092	0.050	23.151	0.009	0.009	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.770	-0.892	17.892	0.249	0.249	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.864	-0.899	19.399	0.208	0.208	0.000	0.000	0.000	0.000
48	A	50	ASN	0	0.013	-0.012	20.558	-0.105	-0.105	0.000	0.000	0.000	0.000
49	A	51	TRP	0	-0.011	-0.006	18.195	-0.054	-0.054	0.000	0.000	0.000	0.000
50	A	52	HIS	0	0.052	0.022	14.668	-0.147	-0.147	0.000	0.000	0.000	0.000
51	A	53	LYS	1	0.808	0.894	18.985	-0.197	-0.197	0.000	0.000	0.000	0.000
52	A	54	GLN	0	0.036	0.022	21.475	-0.076	-0.076	0.000	0.000	0.000	0.000
53	A	55	PHE	0	0.032	0.006	16.534	-0.028	-0.028	0.000	0.000	0.000	0.000
54	A	56	LEU	0	0.009	0.011	16.718	-0.080	-0.080	0.000	0.000	0.000	0.000
55	A	57	LYS	1	0.880	0.942	19.582	0.163	0.163	0.000	0.000	0.000	0.000
56	A	58	PHE	0	0.021	0.008	21.281	-0.022	-0.022	0.000	0.000	0.000	0.000
57	A	59	ALA	0	0.021	-0.001	18.404	-0.023	-0.023	0.000	0.000	0.000	0.000
58	A	60	GLN	0	-0.049	-0.038	20.462	-0.070	-0.070	0.000	0.000	0.000	0.000
59	A	61	ALA	0	-0.004	0.016	22.193	0.014	0.014	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.036	0.007	20.725	0.026	0.026	0.000	0.000	0.000	0.000
61	A	63	PRO	0	-0.013	-0.012	23.836	-0.036	-0.036	0.000	0.000	0.000	0.000
62	A	64	ALA	0	0.020	0.008	21.775	-0.063	-0.063	0.000	0.000	0.000	0.000
63	A	65	HIS	0	0.016	0.011	22.680	-0.087	-0.087	0.000	0.000	0.000	0.000
64	A	66	GLY	0	0.097	0.045	22.865	-0.039	-0.039	0.000	0.000	0.000	0.000
65	A	67	SER	0	-0.097	-0.040	23.250	0.003	0.003	0.000	0.000	0.000	0.000
66	A	68	ALA	0	0.033	0.019	25.101	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	69	SER	0	-0.021	-0.021	27.126	0.031	0.031	0.000	0.000	0.000	0.000
68	A	70	TRP	0	0.007	-0.009	29.674	-0.016	-0.016	0.000	0.000	0.000	0.000
69	A	71	LEU	0	0.049	0.028	31.463	0.000	0.000	0.000	0.000	0.000	0.000
70	A	72	ASN	0	0.036	0.027	28.544	-0.014	-0.014	0.000	0.000	0.000	0.000
71	A	73	LEU	0	0.006	0.005	24.872	-0.027	-0.027	0.000	0.000	0.000	0.000
72	A	74	ASP	-1	-0.819	-0.882	28.319	-0.216	-0.216	0.000	0.000	0.000	0.000
73	A	75	ASP	-1	-0.859	-0.947	30.626	-0.315	-0.315	0.000	0.000	0.000	0.000
74	A	76	ALA	0	-0.028	-0.011	25.518	0.008	0.008	0.000	0.000	0.000	0.000
75	A	77	LEU	0	-0.037	-0.022	27.032	0.013	0.013	0.000	0.000	0.000	0.000
76	A	78	GLN	0	-0.032	-0.024	28.734	0.049	0.049	0.000	0.000	0.000	0.000
77	A	79	ALA	0	0.000	0.015	26.889	0.019	0.019	0.000	0.000	0.000	0.000
78	A	80	VAL	0	-0.045	-0.009	25.617	0.011	0.011	0.000	0.000	0.000	0.000
79	A	81	VAL	0	-0.022	-0.016	28.124	0.012	0.012	0.000	0.000	0.000	0.000
80	A	82	GLY	0	0.061	0.022	30.832	0.012	0.012	0.000	0.000	0.000	0.000
81	A	83	ASN	0	-0.007	-0.014	33.834	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	84	SER	0	-0.008	-0.002	28.492	0.018	0.018	0.000	0.000	0.000	0.000
83	A	85	ARG	1	0.854	0.952	29.326	0.187	0.187	0.000	0.000	0.000	0.000
84	A	86	SER	0	0.064	0.032	29.925	-0.009	-0.009	0.000	0.000	0.000	0.000
85	A	87	ALA	0	0.035	0.013	29.242	0.002	0.002	0.000	0.000	0.000	0.000
86	A	88	PHE	0	-0.007	-0.002	22.097	0.017	0.017	0.000	0.000	0.000	0.000
87	A	89	LEU	0	0.056	0.032	25.670	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	90	HIS	1	0.822	0.885	27.080	0.030	0.030	0.000	0.000	0.000	0.000
89	A	91	GLN	0	-0.003	-0.011	22.151	-0.014	-0.014	0.000	0.000	0.000	0.000
90	A	92	LEU	0	-0.023	-0.009	21.409	0.016	0.016	0.000	0.000	0.000	0.000
91	A	93	ILE	0	0.011	0.009	22.800	-0.014	-0.014	0.000	0.000	0.000	0.000
92	A	94	ALA	0	-0.007	0.006	24.407	0.000	0.000	0.000	0.000	0.000	0.000
93	A	95	LYS	1	0.815	0.893	18.080	-0.126	-0.126	0.000	0.000	0.000	0.000
94	A	96	LEU	0	0.001	0.005	19.333	-0.009	-0.009	0.000	0.000	0.000	0.000
95	A	97	LYS	1	0.901	0.933	21.193	0.084	0.084	0.000	0.000	0.000	0.000
96	A	98	SER	0	-0.033	-0.008	19.917	0.016	0.016	0.000	0.000	0.000	0.000
97	A	99	ARG	1	0.845	0.896	11.786	0.202	0.202	0.000	0.000	0.000	0.000
98	A	100	HIS	0	-0.036	-0.009	18.441	-0.023	-0.023	0.000	0.000	0.000	0.000
99	A	101	LEU	0	0.017	0.000	21.226	-0.022	-0.022	0.000	0.000	0.000	0.000
100	A	102	GLN	0	-0.019	-0.008	15.594	0.024	0.024	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.002	0.008	17.320	-0.035	-0.035	0.000	0.000	0.000	0.000
102	A	104	LEU	0	-0.020	-0.007	18.559	-0.045	-0.045	0.000	0.000	0.000	0.000
103	A	105	GLU	-1	-0.809	-0.891	17.277	0.107	0.107	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.013	-0.003	13.736	-0.019	-0.019	0.000	0.000	0.000	0.000
105	A	107	ASN	0	-0.040	-0.028	17.259	-0.090	-0.090	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.807	0.906	18.363	-0.073	-0.073	0.000	0.000	0.000	0.000
107	A	109	ILE	0	0.072	0.034	13.151	-0.019	-0.019	0.000	0.000	0.000	0.000
108	A	110	GLY	0	-0.027	-0.025	17.186	-0.067	-0.067	0.000	0.000	0.000	0.000
109	A	111	SER	0	-0.046	-0.034	19.277	-0.018	-0.018	0.000	0.000	0.000	0.000
110	A	112	GLU	-1	-0.953	-0.959	17.420	-0.141	-0.141	0.000	0.000	0.000	0.000
111	A	113	PRO	0	-0.005	-0.010	20.867	-0.074	-0.074	0.000	0.000	0.000	0.000
112	A	114	LEU	0	0.003	0.002	17.188	0.004	0.004	0.000	0.000	0.000	0.000
113	A	115	ASP	-1	-0.878	-0.924	21.374	-0.360	-0.360	0.000	0.000	0.000	0.000
114	A	116	LEU	0	-0.050	-0.041	17.236	-0.028	-0.028	0.000	0.000	0.000	0.000
115	A	117	SER	0	-0.005	-0.020	21.752	-0.017	-0.017	0.000	0.000	0.000	0.000
116	A	118	ASN	0	-0.059	-0.028	24.505	0.009	0.009	0.000	0.000	0.000	0.000
117	A	119	LEU	0	0.011	0.018	25.294	0.033	0.033	0.000	0.000	0.000	0.000
118	A	120	PRO	0	0.045	0.023	24.204	-0.036	-0.036	0.000	0.000	0.000	0.000
119	A	121	ALA	0	0.014	0.009	19.600	-0.035	-0.035	0.000	0.000	0.000	0.000
120	A	122	PRO	0	-0.036	-0.008	20.371	0.000	0.000	0.000	0.000	0.000	0.000
121	A	123	PHE	0	-0.003	0.005	14.300	-0.119	-0.119	0.000	0.000	0.000	0.000
122	A	124	TYR	0	-0.009	-0.012	16.900	0.097	0.097	0.000	0.000	0.000	0.000
123	A	125	VAL	0	0.001	0.001	13.258	-0.166	-0.166	0.000	0.000	0.000	0.000
124	A	126	LEU	0	-0.006	-0.003	11.503	0.088	0.088	0.000	0.000	0.000	0.000
125	A	127	LEU	0	-0.004	-0.023	12.220	-0.264	-0.264	0.000	0.000	0.000	0.000
126	A	128	PRO	0	0.012	0.004	12.736	0.071	0.071	0.000	0.000	0.000	0.000
127	A	129	GLU	-1	-0.861	-0.929	15.580	-0.871	-0.871	0.000	0.000	0.000	0.000
128	A	130	SER	0	0.006	0.011	18.130	0.154	0.154	0.000	0.000	0.000	0.000
129	A	131	PHE	0	0.065	0.018	18.412	-0.108	-0.108	0.000	0.000	0.000	0.000
130	A	132	ALA	0	0.025	0.016	19.314	-0.028	-0.028	0.000	0.000	0.000	0.000
131	A	133	ALA	0	0.006	0.010	14.706	-0.019	-0.019	0.000	0.000	0.000	0.000
132	A	134	ARG	1	0.751	0.841	14.459	0.882	0.882	0.000	0.000	0.000	0.000
133	A	135	ILE	0	0.038	0.014	15.291	0.001	0.001	0.000	0.000	0.000	0.000
134	A	136	THR	0	-0.045	-0.043	12.936	0.142	0.142	0.000	0.000	0.000	0.000
135	A	137	LEU	0	-0.062	-0.026	8.398	0.062	0.062	0.000	0.000	0.000	0.000
136	A	138	LEU	0	0.024	0.003	11.771	0.132	0.132	0.000	0.000	0.000	0.000
137	A	139	VAL	0	-0.048	0.000	14.114	0.238	0.238	0.000	0.000	0.000	0.000
138	A	140	GLN	0	-0.003	-0.006	12.543	0.333	0.333	0.000	0.000	0.000	0.000
139	A	141	ASP	-1	-0.865	-0.927	6.546	-3.817	-3.817	0.000	0.000	0.000	0.000
140	A	142	LYS	1	0.925	0.949	6.170	-1.891	-1.891	0.000	0.000	0.000	0.000
142	A	144	LEU	0	0.012	0.014	6.831	-0.590	-0.590	0.000	0.000	0.000	0.000
143	A	145	PRO	0	-0.027	-0.005	7.335	0.034	0.034	0.000	0.000	0.000	0.000
144	A	146	TYR	0	0.002	-0.009	8.770	0.441	0.441	0.000	0.000	0.000	0.000
145	A	147	VAL	0	0.004	0.002	11.170	-0.334	-0.334	0.000	0.000	0.000	0.000
146	A	148	ARG	1	0.824	0.912	13.929	0.788	0.788	0.000	0.000	0.000	0.000
147	A	149	VAL	0	-0.008	-0.004	16.465	-0.074	-0.074	0.000	0.000	0.000	0.000
148	A	150	SER	0	0.018	-0.012	19.303	0.098	0.098	0.000	0.000	0.000	0.000
149	A	151	MET	0	-0.068	-0.029	21.949	-0.064	-0.064	0.000	0.000	0.000	0.000
150	A	152	GLU	-1	-0.773	-0.864	23.710	-0.516	-0.516	0.000	0.000	0.000	0.000
151	A	153	TYR	0	-0.037	-0.014	25.979	0.004	0.004	0.000	0.000	0.000	0.000
152	A	154	TRP	0	0.031	-0.002	27.911	0.008	0.008	0.000	0.000	0.000	0.000
153	A	155	HIS	0	0.027	0.020	31.345	0.008	0.008	0.000	0.000	0.000	0.000
154	A	156	ALA	0	0.012	-0.004	29.514	0.028	0.028	0.000	0.000	0.000	0.000
155	A	157	LEU	0	-0.041	-0.016	26.174	0.001	0.001	0.000	0.000	0.000	0.000
156	A	158	GLU	-1	-0.934	-0.960	30.150	-0.331	-0.331	0.000	0.000	0.000	0.000
157	A	159	TYR	0	-0.022	-0.013	33.239	0.003	0.003	0.000	0.000	0.000	0.000
158	A	160	LYS	1	0.887	0.942	33.707	0.329	0.329	0.000	0.000	0.000	0.000
159	A	161	GLY	0	0.003	0.012	36.408	0.018	0.018	0.000	0.000	0.000	0.000
160	A	162	GLU	-1	-0.973	-0.996	36.088	-0.176	-0.176	0.000	0.000	0.000	0.000
161	A	163	LEU	0	-0.086	-0.044	36.804	0.008	0.008	0.000	0.000	0.000	0.000
162	A	164	ASN	-1	-0.950	-0.954	31.914	-0.240	-0.240	0.000	0.000	0.000	0.000

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