FMO DATABASE

FMODB ID: Z945N

Calculation Name: 1OZ9-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1OZ9

Chain ID: A

ChEMBL ID:

UniProt ID: O67367

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	141
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1368101.992897
FMO2-HF: Nuclear repulsion	1311972.971179
FMO2-HF: Total energy	-56129.021718
FMO2-MP2: Total energy	-56296.812114

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:8:LYS)

Summations of interaction energy for fragment #1(A:8:LYS)

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.
-132.426	-129.924	11.627	-7.625	-6.502	-0.09

Interaction energy analysis for fragmet #1(A:8:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.755 / q_NPA : 1.858

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	10	ARG	1	0.897	0.938	2.648	31.604	35.607	0.350	-2.439	-1.914	-0.023
23	A	30	GLU	-1	-0.945	-0.975	5.011	-83.125	-83.032	-0.001	-0.004	-0.087	0.000
32	A	39	ASN	0	-0.026	-0.018	1.770	-63.709	-65.677	11.279	-5.092	-4.218	-0.067
33	A	40	ASN	0	-0.009	-0.008	4.160	4.281	4.655	-0.001	-0.090	-0.283	0.000
4	A	11	VAL	0	0.056	0.028	5.479	6.497	6.497	0.000	0.000	0.000	0.000
5	A	12	LEU	0	-0.036	-0.015	8.185	1.736	1.736	0.000	0.000	0.000	0.000
6	A	13	VAL	0	0.002	0.006	11.307	2.954	2.954	0.000	0.000	0.000	0.000
7	A	14	LYS	1	0.950	0.968	13.654	31.859	31.859	0.000	0.000	0.000	0.000
8	A	15	LEU	0	0.006	0.001	17.236	0.419	0.419	0.000	0.000	0.000	0.000
9	A	16	LYS	1	0.826	0.916	20.268	21.561	21.561	0.000	0.000	0.000	0.000
10	A	17	LYS	1	0.819	0.903	23.917	20.910	20.910	0.000	0.000	0.000	0.000
11	A	18	ARG	1	0.919	0.936	21.887	23.341	23.341	0.000	0.000	0.000	0.000
12	A	19	LYS	1	0.872	0.943	23.561	19.698	19.698	0.000	0.000	0.000	0.000
13	A	20	VAL	0	0.021	0.017	19.366	0.177	0.177	0.000	0.000	0.000	0.000
14	A	21	ARG	1	0.841	0.882	17.543	29.842	29.842	0.000	0.000	0.000	0.000
15	A	22	LYS	1	0.916	0.946	12.230	39.741	39.741	0.000	0.000	0.000	0.000
16	A	23	ASP	-1	-0.722	-0.834	13.143	-35.388	-35.388	0.000	0.000	0.000	0.000
17	A	24	LYS	1	0.780	0.879	13.131	25.823	25.823	0.000	0.000	0.000	0.000
18	A	25	ILE	0	0.030	0.014	14.096	-1.341	-1.341	0.000	0.000	0.000	0.000
19	A	26	GLU	-1	-0.861	-0.921	8.649	-50.176	-50.176	0.000	0.000	0.000	0.000
20	A	27	LYS	1	0.980	0.997	9.649	38.434	38.434	0.000	0.000	0.000	0.000
21	A	28	TRP	0	0.006	-0.013	10.221	-1.678	-1.678	0.000	0.000	0.000	0.000
22	A	29	ALA	0	0.041	0.024	10.596	-0.630	-0.630	0.000	0.000	0.000	0.000
24	A	31	LEU	0	-0.014	-0.017	6.442	-4.470	-4.470	0.000	0.000	0.000	0.000
25	A	32	ALA	0	0.020	0.015	8.814	0.280	0.280	0.000	0.000	0.000	0.000
26	A	33	LEU	0	0.001	-0.008	6.434	0.101	0.101	0.000	0.000	0.000	0.000
27	A	34	SER	0	-0.036	-0.015	5.357	-4.352	-4.352	0.000	0.000	0.000	0.000
28	A	35	ALA	0	-0.026	-0.011	6.677	1.079	1.079	0.000	0.000	0.000	0.000
29	A	36	LEU	0	-0.030	-0.022	9.969	2.940	2.940	0.000	0.000	0.000	0.000
30	A	37	GLY	0	0.004	0.016	6.920	1.702	1.702	0.000	0.000	0.000	0.000
31	A	38	LEU	0	-0.027	-0.008	6.334	-4.617	-4.617	0.000	0.000	0.000	0.000
34	A	41	VAL	0	0.027	0.022	5.696	9.460	9.460	0.000	0.000	0.000	0.000
35	A	42	GLU	-1	-0.821	-0.868	6.899	-55.677	-55.677	0.000	0.000	0.000	0.000
36	A	43	LEU	0	0.009	0.008	9.275	3.295	3.295	0.000	0.000	0.000	0.000
37	A	44	SER	0	-0.011	-0.004	10.750	-2.506	-2.506	0.000	0.000	0.000	0.000
38	A	45	VAL	0	-0.018	-0.009	12.764	0.890	0.890	0.000	0.000	0.000	0.000
39	A	46	TYR	0	-0.089	-0.062	15.248	-0.174	-0.174	0.000	0.000	0.000	0.000
40	A	47	ILE	0	0.023	0.021	18.579	0.870	0.870	0.000	0.000	0.000	0.000
41	A	48	THR	0	0.026	-0.016	21.220	0.766	0.766	0.000	0.000	0.000	0.000
42	A	49	ASP	-1	-0.810	-0.903	24.719	-20.073	-20.073	0.000	0.000	0.000	0.000
43	A	50	ASP	-1	-0.718	-0.816	28.431	-19.754	-19.754	0.000	0.000	0.000	0.000
44	A	51	GLN	0	-0.052	-0.020	30.837	0.490	0.490	0.000	0.000	0.000	0.000
45	A	52	GLU	-1	-0.695	-0.815	25.606	-22.738	-22.738	0.000	0.000	0.000	0.000
46	A	53	ILE	0	-0.026	-0.008	25.097	-0.141	-0.141	0.000	0.000	0.000	0.000
47	A	54	ARG	1	0.877	0.937	28.037	16.662	16.662	0.000	0.000	0.000	0.000
48	A	55	GLU	-1	-0.938	-0.963	30.502	-18.628	-18.628	0.000	0.000	0.000	0.000
49	A	56	LEU	0	-0.008	0.007	24.573	0.114	0.114	0.000	0.000	0.000	0.000
50	A	57	ASN	0	0.007	-0.015	28.677	-0.361	-0.361	0.000	0.000	0.000	0.000
51	A	58	LYS	1	0.854	0.919	30.447	16.597	16.597	0.000	0.000	0.000	0.000
52	A	59	THR	0	-0.050	-0.035	30.205	0.480	0.480	0.000	0.000	0.000	0.000
53	A	60	TYR	0	-0.007	-0.013	27.034	0.153	0.153	0.000	0.000	0.000	0.000
54	A	61	ARG	1	0.934	0.974	24.584	23.082	23.082	0.000	0.000	0.000	0.000
55	A	62	LYS	1	0.937	0.983	31.398	17.698	17.698	0.000	0.000	0.000	0.000
56	A	63	LYS	1	0.930	0.971	31.628	19.829	19.829	0.000	0.000	0.000	0.000
57	A	64	ASP	-1	-0.803	-0.877	34.098	-16.825	-16.825	0.000	0.000	0.000	0.000
58	A	65	LYS	1	0.950	0.963	34.349	17.683	17.683	0.000	0.000	0.000	0.000
59	A	66	PRO	0	0.017	0.013	31.682	-0.444	-0.444	0.000	0.000	0.000	0.000
60	A	67	THR	0	-0.007	-0.006	27.195	0.574	0.574	0.000	0.000	0.000	0.000
61	A	68	ASP	-1	-0.754	-0.861	25.892	-22.850	-22.850	0.000	0.000	0.000	0.000
62	A	69	VAL	0	-0.036	-0.033	20.703	-0.851	-0.851	0.000	0.000	0.000	0.000
63	A	70	LEU	0	-0.061	-0.018	22.977	0.826	0.826	0.000	0.000	0.000	0.000
64	A	71	SER	0	0.007	-0.010	19.647	-1.050	-1.050	0.000	0.000	0.000	0.000
65	A	72	PHE	0	-0.036	-0.019	19.871	1.472	1.472	0.000	0.000	0.000	0.000
66	A	73	PRO	0	0.037	0.017	18.531	-1.464	-1.464	0.000	0.000	0.000	0.000
67	A	74	MET	0	-0.036	-0.015	17.103	1.660	1.660	0.000	0.000	0.000	0.000
68	A	75	GLY	0	0.016	0.004	16.895	1.280	1.280	0.000	0.000	0.000	0.000
69	A	76	GLU	-1	-0.920	-0.952	17.020	-31.484	-31.484	0.000	0.000	0.000	0.000
70	A	77	GLU	-1	-0.879	-0.931	14.620	-41.246	-41.246	0.000	0.000	0.000	0.000
71	A	78	PHE	0	-0.009	-0.004	13.181	1.888	1.888	0.000	0.000	0.000	0.000
72	A	79	GLY	0	0.006	0.001	12.983	-2.585	-2.585	0.000	0.000	0.000	0.000
73	A	80	GLY	0	0.030	0.013	12.216	-1.637	-1.637	0.000	0.000	0.000	0.000
74	A	81	TYR	0	-0.101	-0.058	6.264	-8.133	-8.133	0.000	0.000	0.000	0.000
75	A	82	LYS	1	0.826	0.888	10.000	43.457	43.457	0.000	0.000	0.000	0.000
76	A	83	ILE	0	0.015	0.010	10.953	-4.439	-4.439	0.000	0.000	0.000	0.000
77	A	84	LEU	0	-0.002	-0.001	10.607	2.677	2.677	0.000	0.000	0.000	0.000
78	A	85	GLY	0	0.044	0.025	14.000	3.112	3.112	0.000	0.000	0.000	0.000
79	A	86	ASP	-1	-0.873	-0.933	14.567	-35.759	-35.759	0.000	0.000	0.000	0.000
80	A	87	VAL	0	-0.003	-0.002	15.943	1.391	1.391	0.000	0.000	0.000	0.000
81	A	88	VAL	0	-0.036	-0.016	18.022	-0.392	-0.392	0.000	0.000	0.000	0.000
82	A	89	ILE	0	0.015	0.003	19.008	0.513	0.513	0.000	0.000	0.000	0.000
83	A	90	SER	0	-0.027	-0.021	22.600	0.121	0.121	0.000	0.000	0.000	0.000
84	A	91	GLN	0	0.010	-0.030	25.128	-0.780	-0.780	0.000	0.000	0.000	0.000
85	A	92	ASP	-1	-0.795	-0.886	26.300	-19.448	-19.448	0.000	0.000	0.000	0.000
86	A	93	THR	0	-0.040	-0.049	29.008	0.779	0.779	0.000	0.000	0.000	0.000
87	A	94	ALA	0	0.037	0.026	25.465	0.220	0.220	0.000	0.000	0.000	0.000
88	A	95	GLU	-1	-0.872	-0.939	27.419	-20.029	-20.029	0.000	0.000	0.000	0.000
89	A	96	ARG	1	0.755	0.882	30.000	18.800	18.800	0.000	0.000	0.000	0.000
90	A	97	GLN	0	0.037	-0.009	27.412	0.757	0.757	0.000	0.000	0.000	0.000
91	A	98	ALA	0	-0.026	-0.012	27.637	0.090	0.090	0.000	0.000	0.000	0.000
92	A	99	ARG	1	0.877	0.940	29.325	17.475	17.475	0.000	0.000	0.000	0.000
93	A	100	GLU	-1	-0.929	-0.976	32.952	-17.219	-17.219	0.000	0.000	0.000	0.000
94	A	101	LEU	0	-0.027	-0.007	28.586	0.264	0.264	0.000	0.000	0.000	0.000
95	A	102	GLY	0	0.002	0.026	31.683	-0.024	-0.024	0.000	0.000	0.000	0.000
96	A	103	HIS	0	-0.066	-0.046	26.564	-0.044	-0.044	0.000	0.000	0.000	0.000
97	A	104	SER	0	0.020	0.002	24.933	0.089	0.089	0.000	0.000	0.000	0.000
98	A	105	LEU	0	0.052	0.012	24.741	-0.461	-0.461	0.000	0.000	0.000	0.000
99	A	106	GLU	-1	-0.822	-0.898	21.358	-27.787	-27.787	0.000	0.000	0.000	0.000
100	A	107	GLU	-1	-0.785	-0.868	20.929	-28.417	-28.417	0.000	0.000	0.000	0.000
101	A	108	GLU	-1	-0.793	-0.879	22.016	-23.792	-23.792	0.000	0.000	0.000	0.000
102	A	109	VAL	0	-0.015	-0.018	18.954	-0.732	-0.732	0.000	0.000	0.000	0.000
103	A	110	LYS	1	0.859	0.933	16.587	28.431	28.431	0.000	0.000	0.000	0.000
104	A	111	ARG	1	0.856	0.919	17.578	23.141	23.141	0.000	0.000	0.000	0.000
105	A	112	LEU	0	0.012	0.009	19.615	-0.784	-0.784	0.000	0.000	0.000	0.000
106	A	113	ILE	0	-0.007	-0.005	13.917	-0.683	-0.683	0.000	0.000	0.000	0.000
107	A	114	VAL	0	-0.019	-0.002	14.747	-1.355	-1.355	0.000	0.000	0.000	0.000
108	A	115	HIS	0	-0.027	-0.021	16.324	-0.100	-0.100	0.000	0.000	0.000	0.000
109	A	116	GLY	0	0.017	0.001	18.237	0.657	0.657	0.000	0.000	0.000	0.000
110	A	117	ILE	0	-0.007	-0.014	11.483	-0.286	-0.286	0.000	0.000	0.000	0.000
111	A	118	VAL	0	-0.009	-0.007	15.230	-0.678	-0.678	0.000	0.000	0.000	0.000
112	A	119	HIS	1	0.833	0.907	17.478	26.715	26.715	0.000	0.000	0.000	0.000
113	A	120	LEU	0	-0.067	-0.021	14.966	0.580	0.580	0.000	0.000	0.000	0.000
114	A	121	LEU	0	-0.075	-0.029	12.948	-0.632	-0.632	0.000	0.000	0.000	0.000
115	A	122	GLY	0	0.003	0.011	17.001	0.521	0.521	0.000	0.000	0.000	0.000
116	A	123	TYR	0	-0.019	0.003	17.510	1.888	1.888	0.000	0.000	0.000	0.000
117	A	124	ASP	-1	-0.791	-0.907	22.168	-23.385	-23.385	0.000	0.000	0.000	0.000
118	A	125	HIS	0	0.000	-0.013	24.798	-0.311	-0.311	0.000	0.000	0.000	0.000
119	A	126	GLU	-1	-0.984	-0.990	27.452	-19.636	-19.636	0.000	0.000	0.000	0.000
120	A	127	LYS	1	0.803	0.892	29.794	20.904	20.904	0.000	0.000	0.000	0.000
121	A	128	GLY	0	0.050	0.036	30.922	0.668	0.668	0.000	0.000	0.000	0.000
122	A	129	GLY	0	0.006	-0.013	30.884	-0.418	-0.418	0.000	0.000	0.000	0.000
123	A	130	GLU	-1	-0.811	-0.903	27.686	-22.012	-22.012	0.000	0.000	0.000	0.000
124	A	131	GLU	-1	-0.846	-0.895	26.477	-22.134	-22.134	0.000	0.000	0.000	0.000
125	A	132	GLU	-1	-0.891	-0.941	25.741	-21.353	-21.353	0.000	0.000	0.000	0.000
126	A	133	LYS	1	0.849	0.922	26.248	20.788	20.788	0.000	0.000	0.000	0.000
127	A	134	LYS	1	0.844	0.907	22.348	25.074	25.074	0.000	0.000	0.000	0.000
128	A	135	PHE	0	-0.013	0.009	21.534	-1.399	-1.399	0.000	0.000	0.000	0.000
129	A	136	ARG	1	0.878	0.911	21.653	22.231	22.231	0.000	0.000	0.000	0.000
130	A	137	GLU	-1	-0.885	-0.929	22.166	-25.125	-25.125	0.000	0.000	0.000	0.000
131	A	138	LEU	0	-0.004	0.004	15.540	-1.182	-1.182	0.000	0.000	0.000	0.000
132	A	139	GLU	-1	-0.773	-0.874	17.778	-28.114	-28.114	0.000	0.000	0.000	0.000
133	A	140	ASN	0	0.016	-0.004	18.934	-0.916	-0.916	0.000	0.000	0.000	0.000
134	A	141	TYR	0	-0.037	0.000	12.734	0.357	0.357	0.000	0.000	0.000	0.000
135	A	142	VAL	0	0.039	0.020	13.235	-1.193	-1.193	0.000	0.000	0.000	0.000
136	A	143	LEU	0	0.007	-0.003	15.523	-0.925	-0.925	0.000	0.000	0.000	0.000
137	A	144	SER	0	-0.093	-0.054	18.091	0.163	0.163	0.000	0.000	0.000	0.000
138	A	145	LYS	1	0.891	0.936	12.985	40.305	40.305	0.000	0.000	0.000	0.000
139	A	146	LEU	0	-0.027	-0.007	12.234	-1.785	-1.785	0.000	0.000	0.000	0.000
140	A	147	SER	0	-0.076	-0.035	15.418	1.097	1.097	0.000	0.000	0.000	0.000
141	A	148	LYS	0	-0.003	0.029	15.609	-4.603	-4.603	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:LYS)