FMO DATABASE

FMODB ID: K8QV3

Calculation Name: 4MZM-B-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4MZM

Chain ID: B

ChEMBL ID:

UniProt ID: Q7A4G9

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
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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-923744.031169
FMO2-HF: Nuclear repulsion	879532.607847
FMO2-HF: Total energy	-44211.423322
FMO2-MP2: Total energy	-44342.201013

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:0:ASP)

Summations of interaction energy for fragment #1(A:0: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.
-25.251	-27.091	12.119	-5.301	-4.977	0.062

Interaction energy analysis for fragmet #1(A:0:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.000 / q_NPA : -0.004

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	2	ILE	0	0.032	0.028	3.451	11.216	13.017	0.114	-0.718	-1.198	0.001
7	A	6	ASP	-1	-0.775	-0.876	5.059	16.797	16.909	-0.001	-0.001	-0.109	0.000
9	A	8	TYR	0	-0.025	-0.036	4.304	-1.086	-0.941	-0.001	-0.022	-0.122	0.000
91	A	90	LYS	1	0.822	0.911	1.737	-48.536	-52.434	12.007	-4.560	-3.548	0.061
4	A	3	ARG	1	0.865	0.916	5.206	-6.807	-6.807	0.000	0.000	0.000	0.000
5	A	4	ARG	1	0.793	0.861	7.080	-2.618	-2.618	0.000	0.000	0.000	0.000
6	A	5	GLY	0	0.060	0.019	9.909	0.812	0.812	0.000	0.000	0.000	0.000
8	A	7	VAL	0	-0.039	-0.028	8.025	-1.755	-1.755	0.000	0.000	0.000	0.000
10	A	9	LEU	0	0.019	0.014	9.728	0.127	0.127	0.000	0.000	0.000	0.000
11	A	10	ALA	0	0.010	-0.006	11.644	-0.696	-0.696	0.000	0.000	0.000	0.000
12	A	11	ASP	-1	-0.863	-0.943	14.064	-1.610	-1.610	0.000	0.000	0.000	0.000
13	A	12	LEU	0	0.013	0.012	17.386	-0.062	-0.062	0.000	0.000	0.000	0.000
14	A	13	SER	0	-0.009	0.019	19.722	0.086	0.086	0.000	0.000	0.000	0.000
15	A	14	PRO	0	0.003	-0.009	22.020	-0.141	-0.141	0.000	0.000	0.000	0.000
16	A	15	VAL	0	-0.020	-0.012	24.186	-0.033	-0.033	0.000	0.000	0.000	0.000
17	A	16	GLN	0	-0.012	-0.010	26.863	0.024	0.024	0.000	0.000	0.000	0.000
18	A	17	GLY	0	0.032	0.014	30.079	0.034	0.034	0.000	0.000	0.000	0.000
19	A	18	SER	0	-0.017	-0.011	30.747	0.012	0.012	0.000	0.000	0.000	0.000
20	A	19	GLU	-1	-0.851	-0.906	25.945	-0.252	-0.252	0.000	0.000	0.000	0.000
21	A	20	GLN	0	-0.013	-0.015	22.197	-0.077	-0.077	0.000	0.000	0.000	0.000
22	A	21	GLY	0	0.040	0.011	22.692	-0.071	-0.071	0.000	0.000	0.000	0.000
23	A	22	GLY	0	-0.005	0.002	22.518	0.090	0.090	0.000	0.000	0.000	0.000
24	A	23	VAL	0	-0.031	-0.028	16.926	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	24	ARG	1	0.839	0.934	17.278	0.092	0.092	0.000	0.000	0.000	0.000
26	A	25	PRO	0	0.019	0.009	14.239	-0.148	-0.148	0.000	0.000	0.000	0.000
27	A	26	VAL	0	-0.008	-0.005	12.400	-0.080	-0.080	0.000	0.000	0.000	0.000
28	A	27	VAL	0	0.026	0.013	12.119	0.319	0.319	0.000	0.000	0.000	0.000
29	A	28	ILE	0	-0.044	-0.011	8.911	-0.646	-0.646	0.000	0.000	0.000	0.000
30	A	29	ILE	0	0.056	0.022	12.128	0.551	0.551	0.000	0.000	0.000	0.000
31	A	30	GLN	0	-0.051	-0.017	13.174	-0.103	-0.103	0.000	0.000	0.000	0.000
32	A	31	ASN	0	0.081	0.043	13.409	0.444	0.444	0.000	0.000	0.000	0.000
33	A	32	ASP	-1	-0.725	-0.876	9.845	3.937	3.937	0.000	0.000	0.000	0.000
34	A	33	THR	0	-0.025	0.002	11.800	-0.333	-0.333	0.000	0.000	0.000	0.000
35	A	34	GLY	0	0.011	0.006	14.144	-0.483	-0.483	0.000	0.000	0.000	0.000
36	A	35	ASN	0	0.011	-0.022	9.383	-1.294	-1.294	0.000	0.000	0.000	0.000
37	A	36	LYS	1	0.853	0.953	9.423	-0.928	-0.928	0.000	0.000	0.000	0.000
38	A	37	TYR	0	0.022	-0.010	10.487	-0.905	-0.905	0.000	0.000	0.000	0.000
39	A	38	SER	0	0.027	0.045	13.471	-0.222	-0.222	0.000	0.000	0.000	0.000
40	A	39	PRO	0	0.035	0.020	12.695	-0.585	-0.585	0.000	0.000	0.000	0.000
41	A	40	THR	0	-0.010	-0.011	13.412	-0.274	-0.274	0.000	0.000	0.000	0.000
42	A	41	VAL	0	0.015	-0.003	10.259	0.031	0.031	0.000	0.000	0.000	0.000
43	A	42	ILE	0	0.010	0.017	13.724	-0.083	-0.083	0.000	0.000	0.000	0.000
44	A	43	VAL	0	-0.012	-0.014	13.171	0.328	0.328	0.000	0.000	0.000	0.000
45	A	44	ALA	0	0.059	0.035	15.704	-0.137	-0.137	0.000	0.000	0.000	0.000
46	A	45	ALA	0	0.013	0.011	16.767	0.090	0.090	0.000	0.000	0.000	0.000
47	A	46	ILE	0	-0.004	0.003	15.242	0.137	0.137	0.000	0.000	0.000	0.000
48	A	47	THR	0	-0.014	-0.013	19.128	-0.210	-0.210	0.000	0.000	0.000	0.000
49	A	48	GLY	0	0.060	0.041	22.068	0.109	0.109	0.000	0.000	0.000	0.000
50	A	49	ARG	1	0.805	0.896	23.688	-0.574	-0.574	0.000	0.000	0.000	0.000
51	A	50	ILE	0	0.060	0.027	26.950	0.056	0.056	0.000	0.000	0.000	0.000
52	A	51	ASN	0	0.024	0.015	30.133	0.053	0.053	0.000	0.000	0.000	0.000
53	A	52	LYS	1	0.822	0.902	25.263	-0.733	-0.733	0.000	0.000	0.000	0.000
54	A	53	ALA	0	0.047	0.021	30.265	-0.012	-0.012	0.000	0.000	0.000	0.000
55	A	54	LYS	1	0.820	0.892	28.400	-0.771	-0.771	0.000	0.000	0.000	0.000
56	A	55	ILE	0	0.038	0.020	29.461	-0.020	-0.020	0.000	0.000	0.000	0.000
57	A	56	PRO	0	0.033	0.012	28.871	0.056	0.056	0.000	0.000	0.000	0.000
58	A	57	THR	0	0.013	-0.006	26.290	0.049	0.049	0.000	0.000	0.000	0.000
59	A	58	HIS	0	-0.058	-0.038	24.728	0.044	0.044	0.000	0.000	0.000	0.000
60	A	59	VAL	0	0.052	0.037	20.441	0.035	0.035	0.000	0.000	0.000	0.000
61	A	60	GLU	-1	-0.829	-0.897	22.012	0.862	0.862	0.000	0.000	0.000	0.000
62	A	61	ILE	0	0.016	0.000	16.758	0.181	0.181	0.000	0.000	0.000	0.000
63	A	62	GLU	-1	-0.823	-0.904	19.714	1.360	1.360	0.000	0.000	0.000	0.000
64	A	63	LYS	1	0.889	0.931	19.013	-0.669	-0.669	0.000	0.000	0.000	0.000
65	A	64	LYS	1	0.884	0.937	20.046	-1.017	-1.017	0.000	0.000	0.000	0.000
66	A	65	LYS	1	0.836	0.903	17.749	-1.734	-1.734	0.000	0.000	0.000	0.000
67	A	66	TYR	0	0.041	0.031	13.637	0.333	0.333	0.000	0.000	0.000	0.000
68	A	67	LYS	1	0.899	0.972	11.357	-1.377	-1.377	0.000	0.000	0.000	0.000
69	A	68	LEU	0	0.000	0.006	15.569	-0.177	-0.177	0.000	0.000	0.000	0.000
70	A	69	ASP	-1	-0.902	-0.952	17.824	0.309	0.309	0.000	0.000	0.000	0.000
71	A	70	LYS	0	0.020	0.003	20.686	-0.013	-0.013	0.000	0.000	0.000	0.000
72	A	71	ASP	-1	-0.796	-0.876	21.492	1.056	1.056	0.000	0.000	0.000	0.000
73	A	72	SER	0	-0.039	-0.022	20.040	-0.178	-0.178	0.000	0.000	0.000	0.000
74	A	73	VAL	0	-0.048	-0.030	22.169	0.097	0.097	0.000	0.000	0.000	0.000
75	A	74	ILE	0	0.005	0.005	17.082	-0.080	-0.080	0.000	0.000	0.000	0.000
76	A	75	LEU	0	-0.020	-0.013	20.388	-0.023	-0.023	0.000	0.000	0.000	0.000
77	A	76	LEU	0	0.033	0.011	20.011	-0.051	-0.051	0.000	0.000	0.000	0.000
78	A	77	GLU	-1	-0.758	-0.824	23.109	0.429	0.429	0.000	0.000	0.000	0.000
79	A	78	GLN	0	-0.064	-0.035	23.175	-0.139	-0.139	0.000	0.000	0.000	0.000
80	A	79	ILE	0	0.009	0.006	20.357	0.035	0.035	0.000	0.000	0.000	0.000
81	A	80	ARG	1	0.926	0.962	19.112	0.419	0.419	0.000	0.000	0.000	0.000
82	A	81	THR	0	0.015	0.003	17.847	0.104	0.104	0.000	0.000	0.000	0.000
83	A	82	LEU	0	-0.040	-0.011	14.320	-0.072	-0.072	0.000	0.000	0.000	0.000
84	A	83	ASP	-1	-0.820	-0.917	14.437	-2.890	-2.890	0.000	0.000	0.000	0.000
85	A	84	LYS	1	0.868	0.917	9.133	3.828	3.828	0.000	0.000	0.000	0.000
86	A	85	LYS	1	0.946	0.985	10.365	2.008	2.008	0.000	0.000	0.000	0.000
87	A	86	ARG	1	0.834	0.908	12.534	1.368	1.368	0.000	0.000	0.000	0.000
88	A	87	LEU	0	-0.029	-0.002	8.085	0.432	0.432	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.851	0.919	9.910	3.051	3.051	0.000	0.000	0.000	0.000
90	A	89	GLU	-1	-0.869	-0.931	8.190	-1.530	-1.530	0.000	0.000	0.000	0.000
92	A	91	LEU	0	-0.054	-0.021	6.822	0.410	0.410	0.000	0.000	0.000	0.000
93	A	92	THR	0	-0.003	-0.016	8.909	0.206	0.206	0.000	0.000	0.000	0.000
94	A	93	TYR	0	-0.020	0.008	7.053	1.246	1.246	0.000	0.000	0.000	0.000
95	A	94	LEU	0	-0.017	-0.013	9.020	-0.969	-0.969	0.000	0.000	0.000	0.000
96	A	95	SER	0	0.016	-0.001	12.003	0.469	0.469	0.000	0.000	0.000	0.000
97	A	96	ASP	-1	-0.835	-0.926	14.129	3.914	3.914	0.000	0.000	0.000	0.000
98	A	97	ASP	-1	-0.813	-0.895	15.904	1.662	1.662	0.000	0.000	0.000	0.000
99	A	98	LYS	1	0.732	0.872	16.371	-1.953	-1.953	0.000	0.000	0.000	0.000
100	A	99	MET	0	0.013	0.008	13.505	-0.181	-0.181	0.000	0.000	0.000	0.000
101	A	100	LYS	1	0.909	0.948	16.836	-1.943	-1.943	0.000	0.000	0.000	0.000
102	A	101	GLU	-1	-0.863	-0.928	20.337	1.332	1.332	0.000	0.000	0.000	0.000
103	A	102	VAL	0	-0.039	-0.022	16.894	-0.174	-0.174	0.000	0.000	0.000	0.000
104	A	103	ASP	-1	-0.787	-0.871	18.489	1.746	1.746	0.000	0.000	0.000	0.000
105	A	104	ASN	0	0.002	0.007	20.916	-0.177	-0.177	0.000	0.000	0.000	0.000
106	A	105	ALA	0	0.011	0.001	23.008	-0.111	-0.111	0.000	0.000	0.000	0.000
107	A	106	LEU	0	-0.036	-0.020	19.430	-0.110	-0.110	0.000	0.000	0.000	0.000
108	A	107	MET	0	-0.007	0.003	23.326	-0.098	-0.098	0.000	0.000	0.000	0.000
109	A	108	ILE	0	-0.022	-0.001	25.921	-0.086	-0.086	0.000	0.000	0.000	0.000
110	A	109	SER	0	-0.088	-0.071	25.458	-0.090	-0.090	0.000	0.000	0.000	0.000
111	A	110	LEU	0	-0.056	-0.036	23.534	-0.070	-0.070	0.000	0.000	0.000	0.000
112	A	111	GLY	0	-0.021	0.001	27.762	-0.035	-0.035	0.000	0.000	0.000	0.000
113	A	112	LEU	0	-0.069	-0.041	25.340	-0.018	-0.018	0.000	0.000	0.000	0.000
114	A	113	ASN	-1	-0.935	-0.956	29.357	0.617	0.617	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:0:ASP)