FMO DATABASE

FMODB ID: 9QY82

Calculation Name: 7MLH-F-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7MLH

Chain ID: F

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-10-06

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1048019.161376
FMO2-HF: Nuclear repulsion	997448.919026
FMO2-HF: Total energy	-50570.242351
FMO2-MP2: Total energy	-50713.715563

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(F:1:ASP)

Summations of interaction energy for fragment #1(F:1:ASP)

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.
-39.231	-35.076	16.525	-10.632	-10.046	-0.09

Interaction energy analysis for fragmet #1(F:1:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.120 / q_NPA : -0.062

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

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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	F	3	VAL	0	-0.020	-0.009	3.384	-0.481	1.167	0.048	-0.800	-0.897	-0.001
17	F	17	LEU	0	-0.029	-0.018	3.196	-1.956	-1.509	0.038	-0.147	-0.337	0.000
18	F	18	VAL	0	0.055	0.019	3.013	5.744	6.635	0.009	-0.309	-0.590	0.000
19	F	19	PRO	0	-0.033	-0.019	2.178	-21.507	-20.792	4.056	-2.544	-2.228	-0.032
20	F	20	GLY	0	0.010	0.009	3.538	2.394	2.693	0.003	-0.033	-0.268	0.000
21	F	21	CYS	0	-0.060	0.000	3.199	5.817	6.575	0.006	-0.258	-0.506	-0.001
22	F	22	HIS	0	-0.010	-0.019	1.747	-30.360	-31.114	12.343	-6.699	-4.889	-0.055
23	F	23	GLY	0	0.077	0.050	3.316	2.504	2.655	0.022	0.158	-0.331	-0.001
4	F	4	ASP	-1	-0.866	-0.920	5.967	-0.964	-0.964	0.000	0.000	0.000	0.000
5	F	5	VAL	0	-0.045	-0.034	9.329	-0.100	-0.100	0.000	0.000	0.000	0.000
6	F	6	LYS	1	0.939	0.973	12.515	1.753	1.753	0.000	0.000	0.000	0.000
7	F	7	ASP	-1	-0.826	-0.914	16.106	-1.939	-1.939	0.000	0.000	0.000	0.000
8	F	8	CYS	0	-0.139	-0.097	18.195	0.170	0.170	0.000	0.000	0.000	0.000
9	F	9	ALA	0	-0.026	-0.011	21.115	0.072	0.072	0.000	0.000	0.000	0.000
10	F	10	ASN	0	-0.059	-0.027	22.232	0.097	0.097	0.000	0.000	0.000	0.000
11	F	11	HIS	0	-0.015	-0.002	17.528	0.203	0.203	0.000	0.000	0.000	0.000
12	F	12	GLU	-1	-0.736	-0.855	18.707	-1.178	-1.178	0.000	0.000	0.000	0.000
13	F	13	ILE	0	-0.020	-0.017	13.023	-0.019	-0.019	0.000	0.000	0.000	0.000
14	F	14	LYS	1	0.821	0.918	13.506	1.304	1.304	0.000	0.000	0.000	0.000
15	F	15	LYS	1	0.918	0.958	7.249	1.624	1.624	0.000	0.000	0.000	0.000
16	F	16	VAL	0	0.042	0.024	7.860	0.474	0.474	0.000	0.000	0.000	0.000
24	F	24	SER	0	-0.011	-0.018	5.945	-1.466	-1.466	0.000	0.000	0.000	0.000
25	F	25	GLU	-1	-0.917	-0.931	6.882	3.154	3.154	0.000	0.000	0.000	0.000
26	F	26	PRO	0	-0.053	-0.045	9.159	-1.021	-1.021	0.000	0.000	0.000	0.000
27	F	28	ILE	0	-0.008	-0.015	8.945	0.631	0.631	0.000	0.000	0.000	0.000
28	F	29	ILE	0	0.002	0.001	10.627	-0.446	-0.446	0.000	0.000	0.000	0.000
29	F	30	HIS	0	-0.030	-0.039	11.437	0.330	0.330	0.000	0.000	0.000	0.000
30	F	31	ARG	1	0.854	0.915	14.790	1.052	1.052	0.000	0.000	0.000	0.000
31	F	32	GLY	0	-0.056	-0.051	18.342	0.156	0.156	0.000	0.000	0.000	0.000
32	F	33	LYS	1	0.851	0.950	14.302	1.561	1.561	0.000	0.000	0.000	0.000
33	F	34	PRO	0	-0.006	0.002	13.257	-0.049	-0.049	0.000	0.000	0.000	0.000
34	F	35	PHE	0	0.039	0.013	8.697	-0.248	-0.248	0.000	0.000	0.000	0.000
35	F	36	GLN	0	-0.014	-0.013	7.608	0.169	0.169	0.000	0.000	0.000	0.000
36	F	37	LEU	0	0.001	0.000	7.333	-1.862	-1.862	0.000	0.000	0.000	0.000
37	F	38	GLU	-1	-0.840	-0.920	7.021	-4.415	-4.415	0.000	0.000	0.000	0.000
38	F	39	ALA	0	-0.010	-0.003	8.450	-1.141	-1.141	0.000	0.000	0.000	0.000
39	F	40	LEU	0	0.027	0.035	10.940	0.590	0.590	0.000	0.000	0.000	0.000
40	F	41	PHE	0	-0.014	-0.015	12.646	0.023	0.023	0.000	0.000	0.000	0.000
41	F	42	GLU	-1	-0.860	-0.927	16.031	-0.719	-0.719	0.000	0.000	0.000	0.000
42	F	43	ALA	0	0.000	0.016	19.457	-0.036	-0.036	0.000	0.000	0.000	0.000
43	F	44	ASN	0	0.015	-0.022	22.788	0.136	0.136	0.000	0.000	0.000	0.000
44	F	45	GLN	0	-0.045	-0.023	25.102	0.130	0.130	0.000	0.000	0.000	0.000
45	F	46	ASN	0	0.031	0.016	26.998	-0.056	-0.056	0.000	0.000	0.000	0.000
46	F	47	SER	0	-0.039	-0.027	27.052	0.036	0.036	0.000	0.000	0.000	0.000
47	F	48	LYS	1	0.932	0.957	28.389	0.560	0.560	0.000	0.000	0.000	0.000
48	F	49	THR	0	-0.021	-0.025	27.999	-0.045	-0.045	0.000	0.000	0.000	0.000
49	F	50	ALA	0	0.078	0.030	22.523	-0.011	-0.011	0.000	0.000	0.000	0.000
50	F	51	LYS	1	0.871	0.948	23.579	0.941	0.941	0.000	0.000	0.000	0.000
51	F	52	ILE	0	-0.012	-0.004	17.316	-0.029	-0.029	0.000	0.000	0.000	0.000
52	F	53	GLU	-1	-0.853	-0.926	21.768	-1.010	-1.010	0.000	0.000	0.000	0.000
53	F	54	ILE	0	0.003	-0.005	17.225	-0.107	-0.107	0.000	0.000	0.000	0.000
54	F	55	LYS	1	0.981	1.001	20.752	1.279	1.279	0.000	0.000	0.000	0.000
55	F	56	ALA	0	0.029	0.013	19.364	-0.208	-0.208	0.000	0.000	0.000	0.000
56	F	57	SER	0	-0.027	-0.009	20.261	0.199	0.199	0.000	0.000	0.000	0.000
57	F	58	ILE	0	0.015	-0.006	20.164	-0.169	-0.169	0.000	0.000	0.000	0.000
58	F	59	ASP	-1	-0.842	-0.899	22.322	-0.917	-0.917	0.000	0.000	0.000	0.000
59	F	60	GLY	0	-0.025	-0.007	23.685	0.092	0.092	0.000	0.000	0.000	0.000
60	F	61	LEU	0	-0.033	-0.012	25.450	0.055	0.055	0.000	0.000	0.000	0.000
61	F	62	GLU	-1	-0.950	-0.980	24.924	-1.211	-1.211	0.000	0.000	0.000	0.000
62	F	63	VAL	0	-0.048	-0.030	22.477	0.072	0.072	0.000	0.000	0.000	0.000
63	F	64	ASP	-1	-0.887	-0.934	23.726	-1.136	-1.136	0.000	0.000	0.000	0.000
64	F	65	VAL	0	-0.039	-0.026	18.642	-0.075	-0.075	0.000	0.000	0.000	0.000
65	F	66	PRO	0	0.005	0.010	21.682	0.029	0.029	0.000	0.000	0.000	0.000
66	F	67	GLY	0	0.025	0.003	20.765	-0.143	-0.143	0.000	0.000	0.000	0.000
67	F	68	ILE	0	-0.011	0.010	17.663	-0.208	-0.208	0.000	0.000	0.000	0.000
68	F	69	ASP	-1	-0.756	-0.827	20.507	-1.154	-1.154	0.000	0.000	0.000	0.000
69	F	70	PRO	0	0.018	0.001	21.542	-0.102	-0.102	0.000	0.000	0.000	0.000
70	F	71	ASN	0	-0.030	-0.027	23.915	-0.005	-0.005	0.000	0.000	0.000	0.000
71	F	72	ALA	0	0.074	0.030	19.621	-0.040	-0.040	0.000	0.000	0.000	0.000
72	F	73	CYS	0	-0.038	0.002	20.867	-0.039	-0.039	0.000	0.000	0.000	0.000
73	F	74	HIS	0	-0.065	-0.037	22.638	0.174	0.174	0.000	0.000	0.000	0.000
74	F	75	TYR	0	-0.070	-0.056	17.657	-0.026	-0.026	0.000	0.000	0.000	0.000
75	F	76	MET	0	-0.016	0.001	18.488	-0.129	-0.129	0.000	0.000	0.000	0.000
76	F	77	LYS	1	0.927	0.957	20.495	0.932	0.932	0.000	0.000	0.000	0.000
77	F	79	PRO	0	-0.009	-0.016	25.957	0.043	0.043	0.000	0.000	0.000	0.000
78	F	80	LEU	0	-0.018	-0.002	22.450	0.001	0.001	0.000	0.000	0.000	0.000
79	F	81	VAL	0	-0.005	-0.008	25.360	0.063	0.063	0.000	0.000	0.000	0.000
80	F	82	LYS	1	0.914	0.936	25.125	0.565	0.565	0.000	0.000	0.000	0.000
81	F	83	GLY	0	-0.011	-0.002	23.809	0.062	0.062	0.000	0.000	0.000	0.000
82	F	84	GLN	0	-0.047	-0.010	22.531	0.079	0.079	0.000	0.000	0.000	0.000
83	F	85	GLN	0	-0.046	-0.049	16.352	-0.152	-0.152	0.000	0.000	0.000	0.000
84	F	86	TYR	0	-0.021	-0.005	17.487	0.147	0.147	0.000	0.000	0.000	0.000
85	F	87	ASP	-1	-0.840	-0.912	11.471	-3.342	-3.342	0.000	0.000	0.000	0.000
86	F	88	ILE	0	-0.027	-0.013	13.460	0.297	0.297	0.000	0.000	0.000	0.000
87	F	89	LYS	1	0.827	0.904	9.532	2.733	2.733	0.000	0.000	0.000	0.000
88	F	90	TYR	0	-0.008	-0.021	11.667	0.565	0.565	0.000	0.000	0.000	0.000
89	F	91	THR	0	-0.052	-0.037	11.521	-0.658	-0.658	0.000	0.000	0.000	0.000
90	F	92	TRP	0	0.014	0.008	13.140	0.350	0.350	0.000	0.000	0.000	0.000
91	F	93	ASN	0	-0.025	-0.018	14.684	-0.183	-0.183	0.000	0.000	0.000	0.000
92	F	94	VAL	0	0.045	0.045	14.426	0.138	0.138	0.000	0.000	0.000	0.000
93	F	95	PRO	0	0.003	0.000	17.392	0.204	0.204	0.000	0.000	0.000	0.000
94	F	96	LYS	1	0.978	0.975	20.912	0.860	0.860	0.000	0.000	0.000	0.000
95	F	97	ILE	0	0.000	-0.001	22.600	0.043	0.043	0.000	0.000	0.000	0.000
96	F	98	ALA	0	-0.010	0.016	20.272	0.045	0.045	0.000	0.000	0.000	0.000
97	F	99	PRO	0	0.055	0.017	22.317	0.049	0.049	0.000	0.000	0.000	0.000
98	F	100	LYS	1	0.822	0.915	20.323	0.739	0.739	0.000	0.000	0.000	0.000
99	F	101	SER	0	0.005	-0.023	19.541	0.067	0.067	0.000	0.000	0.000	0.000
100	F	102	GLU	-1	-0.746	-0.856	17.354	-1.456	-1.456	0.000	0.000	0.000	0.000
101	F	103	ASN	0	-0.058	-0.020	18.284	-0.127	-0.127	0.000	0.000	0.000	0.000
102	F	104	VAL	0	0.016	0.018	16.147	0.055	0.055	0.000	0.000	0.000	0.000
103	F	105	VAL	0	-0.015	-0.001	16.561	-0.203	-0.203	0.000	0.000	0.000	0.000
104	F	106	VAL	0	0.012	0.003	15.284	0.124	0.124	0.000	0.000	0.000	0.000
105	F	107	THR	0	-0.032	-0.014	16.697	-0.093	-0.093	0.000	0.000	0.000	0.000
106	F	108	VAL	0	0.011	0.008	15.105	0.090	0.090	0.000	0.000	0.000	0.000
107	F	109	LYS	1	0.894	0.933	18.070	1.147	1.147	0.000	0.000	0.000	0.000
108	F	110	VAL	0	0.015	0.011	18.984	-0.011	-0.011	0.000	0.000	0.000	0.000
109	F	111	MET	0	-0.044	-0.002	21.926	0.078	0.078	0.000	0.000	0.000	0.000
110	F	112	GLY	0	0.057	0.021	25.666	-0.038	-0.038	0.000	0.000	0.000	0.000
111	F	113	ASP	-1	-0.847	-0.914	27.514	-0.688	-0.688	0.000	0.000	0.000	0.000
112	F	114	ASN	0	-0.058	-0.027	30.288	0.072	0.072	0.000	0.000	0.000	0.000
113	F	115	GLY	0	0.035	0.023	29.514	0.014	0.014	0.000	0.000	0.000	0.000
114	F	116	VAL	0	-0.005	-0.015	23.522	-0.045	-0.045	0.000	0.000	0.000	0.000
115	F	117	LEU	0	-0.026	0.003	22.271	0.057	0.057	0.000	0.000	0.000	0.000
116	F	118	ALA	0	0.045	0.019	18.300	-0.040	-0.040	0.000	0.000	0.000	0.000
117	F	120	ALA	0	0.045	0.041	15.117	0.040	0.040	0.000	0.000	0.000	0.000
118	F	121	ILE	0	-0.034	-0.020	16.724	0.016	0.016	0.000	0.000	0.000	0.000
119	F	122	ALA	0	0.041	0.024	12.096	-0.146	-0.146	0.000	0.000	0.000	0.000
120	F	123	THR	0	0.030	0.003	13.881	0.114	0.114	0.000	0.000	0.000	0.000
121	F	124	HIS	0	-0.006	-0.007	10.565	0.333	0.333	0.000	0.000	0.000	0.000
122	F	125	ALA	0	0.009	0.024	11.662	-0.124	-0.124	0.000	0.000	0.000	0.000
123	F	126	LYS	1	0.844	0.934	12.601	2.400	2.400	0.000	0.000	0.000	0.000
124	F	127	ILE	0	-0.019	0.013	14.011	-0.312	-0.312	0.000	0.000	0.000	0.000
125	F	128	ARG	1	0.836	0.872	15.179	1.467	1.467	0.000	0.000	0.000	0.000
126	F	129	ASP	-2	-1.612	-1.783	16.989	-2.400	-2.400	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(F:1:ASP)