FMO DATABASE

FMODB ID: QL3KY

Calculation Name: 6HMZ-X-Xray547

Preferred Name:

Target Type:

Ligand 3-letter code: BMT | MLI | MLE | MVA | ABA | DAL | SAR

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6HMZ

Chain ID: X

ChEMBL ID:

UniProt ID: A0A078

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	170
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1705029.636768
FMO2-HF: Nuclear repulsion	1640042.434657
FMO2-HF: Total energy	-64987.202111
FMO2-MP2: Total energy	-65173.28421

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:2:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
-5.362	-4.061	0.007	-0.519	-0.789	-0.001

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.838 / q_NPA : 0.908

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	4	PRO	0	0.028	0.035	3.751	-2.089	-0.788	0.007	-0.519	-0.789	-0.001
4	A	5	LYS	1	0.956	0.963	5.886	36.538	36.538	0.000	0.000	0.000	0.000
5	A	6	VAL	0	0.043	0.020	8.283	0.651	0.651	0.000	0.000	0.000	0.000
6	A	7	PHE	0	-0.026	-0.014	11.962	0.388	0.388	0.000	0.000	0.000	0.000
7	A	8	PHE	0	0.020	-0.001	15.280	0.338	0.338	0.000	0.000	0.000	0.000
8	A	9	ASP	-1	-0.781	-0.848	18.959	-14.909	-14.909	0.000	0.000	0.000	0.000
9	A	10	ILE	0	-0.010	-0.017	21.664	0.314	0.314	0.000	0.000	0.000	0.000
10	A	11	LEU	0	-0.011	-0.001	24.374	0.267	0.267	0.000	0.000	0.000	0.000
11	A	12	ILE	0	-0.001	-0.001	27.511	-0.028	-0.028	0.000	0.000	0.000	0.000
12	A	13	GLY	0	0.061	0.028	30.690	0.265	0.265	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.881	0.928	33.653	8.347	8.347	0.000	0.000	0.000	0.000
14	A	15	MET	0	-0.001	0.013	29.961	0.006	0.006	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.860	0.904	27.242	10.833	10.833	0.000	0.000	0.000	0.000
16	A	17	ALA	0	-0.022	-0.007	26.255	0.131	0.131	0.000	0.000	0.000	0.000
17	A	18	GLY	0	0.024	0.013	23.545	-0.036	-0.036	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.824	0.883	16.065	16.645	16.645	0.000	0.000	0.000	0.000
19	A	20	VAL	0	-0.016	-0.001	16.690	0.100	0.100	0.000	0.000	0.000	0.000
20	A	21	VAL	0	0.027	0.003	11.422	-0.422	-0.422	0.000	0.000	0.000	0.000
21	A	22	MET	0	-0.032	-0.011	12.133	0.750	0.750	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.811	-0.893	6.122	-37.154	-37.154	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.001	-0.003	8.063	3.182	3.182	0.000	0.000	0.000	0.000
24	A	25	PHE	0	-0.025	-0.007	7.599	-5.021	-5.021	0.000	0.000	0.000	0.000
25	A	26	ALA	0	0.022	0.005	6.000	3.465	3.465	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.839	-0.916	5.574	-36.681	-36.681	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.067	-0.032	7.490	4.032	4.032	0.000	0.000	0.000	0.000
28	A	29	THR	0	-0.080	-0.045	10.755	3.205	3.205	0.000	0.000	0.000	0.000
29	A	30	PRO	0	0.065	0.039	9.338	-0.150	-0.150	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.887	0.959	10.776	17.088	17.088	0.000	0.000	0.000	0.000
31	A	32	THR	0	-0.007	-0.039	14.371	1.510	1.510	0.000	0.000	0.000	0.000
32	A	33	ALA	0	-0.012	0.003	10.108	0.697	0.697	0.000	0.000	0.000	0.000
33	A	34	ASP	-1	-0.804	-0.901	11.755	-24.805	-24.805	0.000	0.000	0.000	0.000
34	A	35	ASN	0	0.010	0.002	12.746	1.688	1.688	0.000	0.000	0.000	0.000
35	A	36	PHE	0	0.025	-0.001	14.155	0.737	0.737	0.000	0.000	0.000	0.000
36	A	37	ARG	1	0.750	0.827	9.394	27.453	27.453	0.000	0.000	0.000	0.000
37	A	38	ALA	0	0.007	0.005	13.288	0.865	0.865	0.000	0.000	0.000	0.000
38	A	39	LEU	0	-0.020	0.011	15.662	1.314	1.314	0.000	0.000	0.000	0.000
39	A	40	CYS	0	-0.043	-0.018	14.749	1.108	1.108	0.000	0.000	0.000	0.000
40	A	41	THR	0	-0.003	-0.028	13.947	1.077	1.077	0.000	0.000	0.000	0.000
41	A	42	GLY	0	-0.009	0.012	16.923	0.759	0.759	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.778	-0.857	14.632	-21.067	-21.067	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.849	0.919	15.457	19.712	19.712	0.000	0.000	0.000	0.000
44	A	45	GLY	0	0.018	0.028	20.937	0.598	0.598	0.000	0.000	0.000	0.000
45	A	46	ILE	0	-0.053	-0.029	24.360	0.014	0.014	0.000	0.000	0.000	0.000
46	A	47	GLY	0	0.028	0.019	26.881	-0.159	-0.159	0.000	0.000	0.000	0.000
47	A	48	GLN	0	-0.014	-0.034	27.555	0.461	0.461	0.000	0.000	0.000	0.000
48	A	49	ALA	0	-0.063	-0.030	30.187	0.409	0.409	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.006	0.001	31.554	0.242	0.242	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.850	0.928	29.166	9.996	9.996	0.000	0.000	0.000	0.000
51	A	52	ALA	0	0.058	0.027	25.630	-0.181	-0.181	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.028	-0.004	22.140	-0.014	-0.014	0.000	0.000	0.000	0.000
53	A	54	HIS	0	-0.017	-0.033	20.013	-0.272	-0.272	0.000	0.000	0.000	0.000
54	A	55	TYR	0	-0.032	-0.036	17.976	0.582	0.582	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.904	0.961	22.319	13.543	13.543	0.000	0.000	0.000	0.000
56	A	57	GLY	0	-0.014	-0.001	23.807	0.371	0.371	0.000	0.000	0.000	0.000
57	A	58	SER	0	-0.103	-0.059	24.388	0.401	0.401	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.038	0.005	26.433	-0.140	-0.140	0.000	0.000	0.000	0.000
59	A	60	PHE	0	-0.016	-0.033	21.195	-0.331	-0.331	0.000	0.000	0.000	0.000
60	A	61	HIS	0	-0.053	-0.022	27.267	0.524	0.524	0.000	0.000	0.000	0.000
61	A	62	ARG	1	0.922	0.972	29.314	10.617	10.617	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.006	-0.003	27.841	-0.474	-0.474	0.000	0.000	0.000	0.000
63	A	64	ILE	0	-0.030	0.001	29.513	0.367	0.367	0.000	0.000	0.000	0.000
64	A	65	PRO	0	-0.023	-0.022	29.786	-0.339	-0.339	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.011	0.009	29.623	0.237	0.237	0.000	0.000	0.000	0.000
66	A	67	PHE	0	-0.013	-0.003	27.436	-0.037	-0.037	0.000	0.000	0.000	0.000
67	A	68	MET	0	-0.028	-0.003	24.914	-0.660	-0.660	0.000	0.000	0.000	0.000
68	A	69	CYS	0	0.003	0.020	23.871	0.592	0.592	0.000	0.000	0.000	0.000
69	A	70	GLN	0	0.049	0.010	23.926	-0.432	-0.432	0.000	0.000	0.000	0.000
70	A	71	GLY	0	0.021	0.008	24.656	0.428	0.428	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.064	0.033	23.601	-0.234	-0.234	0.000	0.000	0.000	0.000
72	A	73	ASP	-1	-0.761	-0.869	24.341	-10.749	-10.749	0.000	0.000	0.000	0.000
73	A	74	PHE	0	0.074	0.026	23.241	0.455	0.455	0.000	0.000	0.000	0.000
74	A	75	THR	0	-0.086	-0.036	27.782	0.327	0.327	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.869	0.909	30.783	9.733	9.733	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.018	0.033	30.887	0.259	0.259	0.000	0.000	0.000	0.000
77	A	78	ASN	0	0.032	0.029	31.948	-0.132	-0.132	0.000	0.000	0.000	0.000
78	A	79	GLY	0	0.015	0.017	30.542	0.147	0.147	0.000	0.000	0.000	0.000
79	A	80	THR	0	-0.049	-0.038	31.621	-0.039	-0.039	0.000	0.000	0.000	0.000
80	A	81	GLY	0	-0.023	-0.006	31.328	0.127	0.127	0.000	0.000	0.000	0.000
81	A	82	GLY	0	0.013	0.007	27.239	-0.257	-0.257	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.892	-0.943	25.677	-11.296	-11.296	0.000	0.000	0.000	0.000
83	A	84	SER	0	-0.002	0.001	21.370	-0.596	-0.596	0.000	0.000	0.000	0.000
84	A	85	ILE	0	0.016	0.006	16.473	0.635	0.635	0.000	0.000	0.000	0.000
85	A	86	TYR	0	-0.076	-0.060	15.950	-0.127	-0.127	0.000	0.000	0.000	0.000
86	A	87	GLY	0	0.034	0.036	22.369	0.516	0.516	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.002	-0.014	25.720	-0.143	-0.143	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.856	0.936	25.506	11.057	11.057	0.000	0.000	0.000	0.000
89	A	90	PHE	0	-0.016	-0.006	18.469	0.053	0.053	0.000	0.000	0.000	0.000
90	A	91	GLN	0	0.035	0.000	21.980	-0.161	-0.161	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.807	-0.893	21.337	-13.909	-13.909	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.800	-0.858	14.189	-21.915	-21.915	0.000	0.000	0.000	0.000
93	A	94	ASN	0	-0.017	-0.033	15.080	0.075	0.075	0.000	0.000	0.000	0.000
94	A	95	PHE	0	0.043	0.030	18.977	-0.225	-0.225	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.957	0.989	14.992	20.684	20.684	0.000	0.000	0.000	0.000
96	A	97	LEU	0	0.000	0.011	12.273	0.660	0.660	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.873	0.934	16.941	15.513	15.513	0.000	0.000	0.000	0.000
98	A	99	HIS	0	0.002	-0.005	18.875	-0.952	-0.952	0.000	0.000	0.000	0.000
99	A	100	THR	0	-0.037	-0.034	18.087	0.658	0.658	0.000	0.000	0.000	0.000
100	A	101	GLY	0	-0.009	-0.012	20.541	0.560	0.560	0.000	0.000	0.000	0.000
101	A	102	PRO	0	0.010	0.013	20.675	-0.354	-0.354	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.018	0.016	17.752	-0.616	-0.616	0.000	0.000	0.000	0.000
103	A	104	ILE	0	-0.025	-0.005	15.733	-1.113	-1.113	0.000	0.000	0.000	0.000
104	A	105	LEU	0	0.001	0.014	14.148	1.054	1.054	0.000	0.000	0.000	0.000
105	A	106	SER	0	-0.002	-0.032	17.034	-0.784	-0.784	0.000	0.000	0.000	0.000
106	A	107	MET	0	0.009	0.020	18.950	0.139	0.139	0.000	0.000	0.000	0.000
107	A	108	ALA	0	-0.026	-0.010	21.310	0.582	0.582	0.000	0.000	0.000	0.000
108	A	109	ASN	0	-0.050	-0.034	24.912	0.214	0.214	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.022	-0.017	27.190	0.378	0.378	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.036	0.028	29.529	0.402	0.402	0.000	0.000	0.000	0.000
111	A	112	PRO	0	-0.013	-0.017	27.687	-0.361	-0.361	0.000	0.000	0.000	0.000
112	A	113	ASN	0	-0.021	-0.018	25.363	-0.191	-0.191	0.000	0.000	0.000	0.000
113	A	114	THR	0	0.009	0.009	26.453	0.112	0.112	0.000	0.000	0.000	0.000
114	A	115	ASN	0	-0.016	-0.013	21.976	0.177	0.177	0.000	0.000	0.000	0.000
115	A	116	GLY	0	0.040	0.002	23.947	0.190	0.190	0.000	0.000	0.000	0.000
116	A	117	SER	0	0.031	0.011	21.991	-0.565	-0.565	0.000	0.000	0.000	0.000
117	A	118	GLN	0	-0.049	-0.020	22.177	-0.402	-0.402	0.000	0.000	0.000	0.000
118	A	119	PHE	0	0.008	0.019	20.042	-0.400	-0.400	0.000	0.000	0.000	0.000
119	A	120	PHE	0	-0.022	-0.021	21.573	0.709	0.709	0.000	0.000	0.000	0.000
120	A	121	ILE	0	0.010	0.012	18.843	-0.821	-0.821	0.000	0.000	0.000	0.000
121	A	122	CYS	0	-0.051	-0.017	20.550	0.864	0.864	0.000	0.000	0.000	0.000
122	A	123	THR	0	-0.055	-0.069	21.738	-0.474	-0.474	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.848	-0.910	24.376	-10.938	-10.938	0.000	0.000	0.000	0.000
124	A	125	LYS	1	0.903	0.947	23.845	11.721	11.721	0.000	0.000	0.000	0.000
125	A	126	THR	0	0.021	0.006	24.265	0.277	0.277	0.000	0.000	0.000	0.000
126	A	127	ALA	0	0.021	-0.001	25.054	-0.056	-0.056	0.000	0.000	0.000	0.000
127	A	128	TRP	0	0.020	0.020	26.074	-0.095	-0.095	0.000	0.000	0.000	0.000
128	A	129	LEU	0	-0.031	-0.007	25.274	0.238	0.238	0.000	0.000	0.000	0.000
129	A	130	ASP	-1	-0.771	-0.881	23.045	-13.953	-13.953	0.000	0.000	0.000	0.000
130	A	131	GLY	0	-0.038	-0.023	23.473	0.469	0.469	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.886	0.944	25.061	11.199	11.199	0.000	0.000	0.000	0.000
132	A	133	HIS	1	0.865	0.941	22.808	12.704	12.704	0.000	0.000	0.000	0.000
133	A	134	VAL	0	0.019	0.023	17.013	-0.129	-0.129	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.013	0.010	15.596	-0.206	-0.206	0.000	0.000	0.000	0.000
135	A	136	PHE	0	0.010	-0.001	13.657	-0.451	-0.451	0.000	0.000	0.000	0.000
136	A	137	GLY	0	0.045	0.013	11.680	-2.487	-2.487	0.000	0.000	0.000	0.000
137	A	138	LYS	1	0.852	0.934	9.529	28.513	28.513	0.000	0.000	0.000	0.000
138	A	139	VAL	0	-0.007	-0.004	12.223	-1.314	-1.314	0.000	0.000	0.000	0.000
139	A	140	VAL	0	-0.094	-0.052	9.443	-0.073	-0.073	0.000	0.000	0.000	0.000
140	A	141	ASP	-1	-0.851	-0.919	12.655	-16.760	-16.760	0.000	0.000	0.000	0.000
141	A	142	GLY	0	0.065	0.038	15.162	-0.001	-0.001	0.000	0.000	0.000	0.000
142	A	143	TYR	0	0.014	-0.001	18.356	0.569	0.569	0.000	0.000	0.000	0.000
143	A	144	ASN	0	0.020	-0.003	19.840	0.076	0.076	0.000	0.000	0.000	0.000
144	A	145	VAL	0	0.000	0.008	21.648	0.630	0.630	0.000	0.000	0.000	0.000
145	A	146	VAL	0	0.052	0.016	20.068	0.373	0.373	0.000	0.000	0.000	0.000
146	A	147	LYS	1	0.835	0.905	23.199	11.820	11.820	0.000	0.000	0.000	0.000
147	A	148	ALA	0	-0.038	-0.014	25.931	0.548	0.548	0.000	0.000	0.000	0.000
148	A	149	MET	0	-0.003	0.001	23.317	0.302	0.302	0.000	0.000	0.000	0.000
149	A	150	GLU	-1	-0.718	-0.826	26.894	-10.789	-10.789	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.857	0.933	28.679	10.181	10.181	0.000	0.000	0.000	0.000
151	A	152	VAL	0	0.011	0.020	31.262	0.306	0.306	0.000	0.000	0.000	0.000
152	A	153	GLY	0	0.023	0.021	31.901	0.178	0.178	0.000	0.000	0.000	0.000
153	A	154	SER	0	-0.060	-0.057	32.891	0.360	0.360	0.000	0.000	0.000	0.000
154	A	155	GLU	-1	-0.895	-0.949	34.686	-8.179	-8.179	0.000	0.000	0.000	0.000
155	A	156	ARG	1	0.956	0.971	35.807	7.821	7.821	0.000	0.000	0.000	0.000
156	A	157	GLY	0	-0.019	-0.013	33.247	-0.035	-0.035	0.000	0.000	0.000	0.000
157	A	158	VAL	0	-0.016	-0.003	33.313	-0.215	-0.215	0.000	0.000	0.000	0.000
158	A	159	THR	0	-0.020	-0.006	31.262	0.077	0.077	0.000	0.000	0.000	0.000
159	A	160	SER	0	-0.055	-0.033	34.575	0.200	0.200	0.000	0.000	0.000	0.000
160	A	161	GLU	-1	-0.857	-0.932	33.829	-8.367	-8.367	0.000	0.000	0.000	0.000
161	A	162	PRO	0	-0.034	-0.001	33.241	-0.265	-0.265	0.000	0.000	0.000	0.000
162	A	163	VAL	0	0.041	0.022	26.837	-0.102	-0.102	0.000	0.000	0.000	0.000
163	A	164	VAL	0	-0.025	-0.022	27.463	-0.107	-0.107	0.000	0.000	0.000	0.000
164	A	165	ILE	0	0.006	0.018	21.427	-0.174	-0.174	0.000	0.000	0.000	0.000
165	A	166	GLU	-1	-0.834	-0.898	24.365	-10.991	-10.991	0.000	0.000	0.000	0.000
166	A	167	ASP	-1	-0.835	-0.918	21.593	-13.864	-13.864	0.000	0.000	0.000	0.000
167	A	168	CYS	0	-0.106	-0.037	18.137	0.029	0.029	0.000	0.000	0.000	0.000
168	A	169	GLY	0	0.045	0.034	15.745	0.531	0.531	0.000	0.000	0.000	0.000
169	A	170	GLU	-1	-0.852	-0.931	8.727	-32.742	-32.742	0.000	0.000	0.000	0.000
170	A	171	ILE	-1	-0.978	-0.977	8.175	-29.101	-29.101	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)