FMO DATABASE

FMODB ID: 1V1VZ

Calculation Name: 1ODH-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1ODH

Chain ID: A

ChEMBL ID:

UniProt ID: P70348

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	157
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1556910.807608
FMO2-HF: Nuclear repulsion	1491420.650305
FMO2-HF: Total energy	-65490.157303
FMO2-MP2: Total energy	-65677.462606

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:14:LEU)

Summations of interaction energy for fragment #1(A:14:LEU)

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.
68.605	73.843	18.366	-10.935	-12.668	-0.093

Interaction energy analysis for fragmet #1(A:14:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.842 / q_NPA : 0.891

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	16	TRP	0	0.035	-0.007	2.719	-7.207	-4.098	0.563	-1.204	-2.467	-0.008
4	A	17	ASP	-1	-0.836	-0.940	1.840	-133.682	-132.116	12.842	-7.519	-6.890	-0.095
5	A	18	ILE	0	-0.024	0.002	3.878	9.749	9.883	0.001	-0.062	-0.073	0.000
11	A	24	PRO	0	-0.022	-0.002	1.817	0.637	0.744	4.964	-2.115	-2.956	0.010
12	A	25	GLN	0	0.037	-0.009	4.688	1.019	1.067	-0.001	-0.015	-0.031	0.000
13	A	26	ASN	0	-0.015	-0.001	4.499	4.468	4.574	-0.001	-0.007	-0.098	0.000
31	A	44	ILE	0	0.034	0.014	4.234	-0.842	-0.746	-0.001	-0.008	-0.087	0.000
132	A	145	PHE	0	0.016	0.023	4.125	1.576	1.648	-0.001	-0.005	-0.066	0.000
6	A	19	ASN	0	-0.051	-0.031	7.720	0.601	0.601	0.000	0.000	0.000	0.000
7	A	20	ASP	-1	-0.775	-0.879	7.436	-34.693	-34.693	0.000	0.000	0.000	0.000
8	A	21	VAL	0	0.068	0.041	9.511	0.052	0.052	0.000	0.000	0.000	0.000
9	A	22	LYS	1	0.865	0.915	8.347	24.711	24.711	0.000	0.000	0.000	0.000
10	A	23	LEU	0	0.033	0.039	5.659	-1.861	-1.861	0.000	0.000	0.000	0.000
14	A	27	VAL	0	-0.044	-0.020	5.569	-1.126	-1.126	0.000	0.000	0.000	0.000
15	A	28	LYS	1	1.001	0.999	7.389	30.268	30.268	0.000	0.000	0.000	0.000
16	A	29	THR	0	0.005	0.008	7.996	2.070	2.070	0.000	0.000	0.000	0.000
17	A	30	THR	0	-0.009	0.000	8.289	-2.956	-2.956	0.000	0.000	0.000	0.000
18	A	31	ASP	-1	-0.816	-0.887	8.715	-30.213	-30.213	0.000	0.000	0.000	0.000
19	A	32	TRP	0	0.072	0.030	11.565	1.027	1.027	0.000	0.000	0.000	0.000
20	A	33	PHE	0	-0.006	-0.013	14.944	-0.446	-0.446	0.000	0.000	0.000	0.000
21	A	34	GLN	0	-0.047	-0.030	14.339	1.126	1.126	0.000	0.000	0.000	0.000
22	A	35	GLU	-1	-0.808	-0.883	16.827	-12.949	-12.949	0.000	0.000	0.000	0.000
23	A	36	TRP	0	-0.022	-0.035	19.494	0.350	0.350	0.000	0.000	0.000	0.000
24	A	37	PRO	0	-0.044	-0.017	15.327	-0.270	-0.270	0.000	0.000	0.000	0.000
25	A	38	ASP	-1	-0.750	-0.886	16.570	-14.118	-14.118	0.000	0.000	0.000	0.000
26	A	39	SER	0	0.018	-0.021	16.054	-1.028	-1.028	0.000	0.000	0.000	0.000
27	A	40	TYR	0	-0.034	-0.008	13.148	-1.095	-1.095	0.000	0.000	0.000	0.000
28	A	41	VAL	0	-0.016	0.018	11.013	-2.330	-2.330	0.000	0.000	0.000	0.000
29	A	42	LYS	1	0.873	0.917	6.603	39.928	39.928	0.000	0.000	0.000	0.000
30	A	43	HIS	1	0.825	0.902	8.137	27.400	27.400	0.000	0.000	0.000	0.000
32	A	45	TYR	0	0.042	0.030	8.128	1.652	1.652	0.000	0.000	0.000	0.000
33	A	46	SER	0	0.088	0.046	11.919	-0.793	-0.793	0.000	0.000	0.000	0.000
34	A	47	SER	0	-0.066	-0.039	13.873	1.000	1.000	0.000	0.000	0.000	0.000
35	A	48	ASP	-1	-0.820	-0.892	15.786	-15.936	-15.936	0.000	0.000	0.000	0.000
36	A	49	ASP	-1	-0.826	-0.908	16.580	-16.643	-16.643	0.000	0.000	0.000	0.000
37	A	50	ARG	1	0.999	0.982	18.459	12.106	12.106	0.000	0.000	0.000	0.000
38	A	51	ASN	0	-0.032	-0.014	20.137	0.993	0.993	0.000	0.000	0.000	0.000
39	A	52	ALA	0	0.013	0.001	15.279	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	53	GLN	0	-0.034	-0.037	17.374	0.491	0.491	0.000	0.000	0.000	0.000
41	A	54	ARG	1	0.895	0.953	19.438	12.824	12.824	0.000	0.000	0.000	0.000
42	A	55	HIS	1	0.845	0.938	17.084	17.553	17.553	0.000	0.000	0.000	0.000
43	A	56	LEU	0	-0.024	-0.004	19.621	0.595	0.595	0.000	0.000	0.000	0.000
44	A	57	SER	0	0.057	0.014	19.525	-0.708	-0.708	0.000	0.000	0.000	0.000
45	A	58	SER	0	-0.016	-0.021	21.448	0.637	0.637	0.000	0.000	0.000	0.000
46	A	59	TRP	0	0.034	0.044	20.876	1.047	1.047	0.000	0.000	0.000	0.000
47	A	60	ALA	0	0.003	0.005	24.315	-0.083	-0.083	0.000	0.000	0.000	0.000
48	A	61	MET	0	-0.043	0.003	20.291	0.035	0.035	0.000	0.000	0.000	0.000
49	A	62	ARG	1	0.911	0.958	24.825	10.968	10.968	0.000	0.000	0.000	0.000
50	A	63	ASN	0	0.006	-0.010	24.074	-0.487	-0.487	0.000	0.000	0.000	0.000
51	A	64	THR	0	-0.023	-0.004	22.157	0.246	0.246	0.000	0.000	0.000	0.000
52	A	65	ASN	0	0.061	0.026	23.193	-0.959	-0.959	0.000	0.000	0.000	0.000
53	A	66	ASN	0	-0.050	-0.044	18.660	0.666	0.666	0.000	0.000	0.000	0.000
54	A	67	HIS	0	0.054	0.033	22.460	-0.266	-0.266	0.000	0.000	0.000	0.000
55	A	68	ASN	0	0.049	0.017	17.226	-0.205	-0.205	0.000	0.000	0.000	0.000
56	A	69	SER	0	0.039	0.014	19.873	-0.407	-0.407	0.000	0.000	0.000	0.000
57	A	70	ARG	1	0.957	0.987	15.176	18.257	18.257	0.000	0.000	0.000	0.000
58	A	71	ILE	0	-0.054	-0.014	13.277	-1.518	-1.518	0.000	0.000	0.000	0.000
59	A	72	LEU	0	0.049	0.037	16.456	1.082	1.082	0.000	0.000	0.000	0.000
60	A	73	LYS	1	0.952	0.983	17.655	14.030	14.030	0.000	0.000	0.000	0.000
61	A	74	LYS	1	0.879	0.932	19.183	15.216	15.216	0.000	0.000	0.000	0.000
62	A	75	SER	0	0.020	0.001	20.418	-0.609	-0.609	0.000	0.000	0.000	0.000
63	A	76	CYS	0	-0.027	-0.007	23.031	0.637	0.637	0.000	0.000	0.000	0.000
64	A	77	LEU	0	-0.025	-0.027	24.820	0.317	0.317	0.000	0.000	0.000	0.000
65	A	78	GLY	0	-0.025	-0.018	27.592	0.410	0.410	0.000	0.000	0.000	0.000
66	A	79	VAL	0	-0.012	-0.022	28.964	-0.238	-0.238	0.000	0.000	0.000	0.000
67	A	80	VAL	0	-0.045	-0.016	31.733	0.196	0.196	0.000	0.000	0.000	0.000
68	A	81	VAL	0	0.052	0.026	35.402	-0.039	-0.039	0.000	0.000	0.000	0.000
69	A	82	CYS	0	-0.026	0.008	37.767	0.220	0.220	0.000	0.000	0.000	0.000
70	A	83	SER	0	-0.057	-0.047	41.339	-0.027	-0.027	0.000	0.000	0.000	0.000
71	A	84	ARG	1	0.988	0.977	42.932	6.569	6.569	0.000	0.000	0.000	0.000
72	A	85	ASP	-1	-0.837	-0.923	42.184	-7.543	-7.543	0.000	0.000	0.000	0.000
73	A	86	CYS	0	-0.064	0.007	42.907	-0.031	-0.031	0.000	0.000	0.000	0.000
74	A	87	SER	0	-0.024	-0.026	42.338	-0.295	-0.295	0.000	0.000	0.000	0.000
75	A	88	THR	0	-0.088	-0.059	42.569	0.127	0.127	0.000	0.000	0.000	0.000
76	A	89	GLU	-1	-0.864	-0.925	44.957	-6.364	-6.364	0.000	0.000	0.000	0.000
77	A	90	GLU	-1	-0.842	-0.901	42.494	-7.333	-7.333	0.000	0.000	0.000	0.000
78	A	91	GLY	0	0.000	0.000	42.396	-0.197	-0.197	0.000	0.000	0.000	0.000
79	A	92	ARG	1	0.907	0.968	36.190	8.166	8.166	0.000	0.000	0.000	0.000
80	A	93	LYS	1	0.913	0.960	37.177	7.926	7.926	0.000	0.000	0.000	0.000
81	A	94	ILE	0	-0.004	-0.014	37.751	-0.095	-0.095	0.000	0.000	0.000	0.000
82	A	95	TYR	0	0.025	0.006	32.798	-0.018	-0.018	0.000	0.000	0.000	0.000
83	A	96	LEU	0	0.031	0.031	33.637	-0.216	-0.216	0.000	0.000	0.000	0.000
84	A	97	ARG	1	0.837	0.890	25.770	11.350	11.350	0.000	0.000	0.000	0.000
85	A	98	PRO	0	-0.022	0.008	30.519	0.270	0.270	0.000	0.000	0.000	0.000
86	A	99	ALA	0	-0.001	0.005	31.625	-0.254	-0.254	0.000	0.000	0.000	0.000
87	A	100	ILE	0	0.015	-0.008	28.144	-0.082	-0.082	0.000	0.000	0.000	0.000
88	A	101	CYS	-1	-0.779	-0.811	31.245	-9.012	-9.012	0.000	0.000	0.000	0.000
89	A	102	ASP	-1	-0.741	-0.874	33.014	-9.827	-9.827	0.000	0.000	0.000	0.000
90	A	103	LYS	1	0.962	0.966	35.275	7.698	7.698	0.000	0.000	0.000	0.000
91	A	104	ALA	0	-0.058	-0.083	36.447	0.262	0.262	0.000	0.000	0.000	0.000
92	A	105	ARG	1	0.803	0.883	32.361	9.966	9.966	0.000	0.000	0.000	0.000
93	A	106	GLN	0	-0.008	0.007	37.236	0.299	0.299	0.000	0.000	0.000	0.000
94	A	107	LYS	1	0.941	0.965	40.439	7.823	7.823	0.000	0.000	0.000	0.000
95	A	108	GLN	0	-0.027	-0.019	35.551	0.029	0.029	0.000	0.000	0.000	0.000
96	A	109	GLN	0	-0.010	-0.028	38.195	0.077	0.077	0.000	0.000	0.000	0.000
97	A	110	ARG	1	0.969	0.993	41.198	6.860	6.860	0.000	0.000	0.000	0.000
98	A	111	LYS	1	0.906	0.974	41.560	7.786	7.786	0.000	0.000	0.000	0.000
99	A	112	SER	0	0.033	0.019	44.582	-0.026	-0.026	0.000	0.000	0.000	0.000
100	A	113	CYS	0	-0.058	-0.033	43.421	-0.152	-0.152	0.000	0.000	0.000	0.000
101	A	114	PRO	0	-0.027	-0.015	41.775	0.150	0.150	0.000	0.000	0.000	0.000
102	A	115	ASN	0	0.047	-0.001	44.184	0.033	0.033	0.000	0.000	0.000	0.000
103	A	116	CYS	0	0.005	-0.001	45.726	0.125	0.125	0.000	0.000	0.000	0.000
104	A	117	ASN	0	0.004	-0.001	47.964	0.124	0.124	0.000	0.000	0.000	0.000
105	A	118	GLY	0	0.022	0.015	47.610	0.103	0.103	0.000	0.000	0.000	0.000
106	A	119	PRO	0	0.044	0.020	45.687	-0.106	-0.106	0.000	0.000	0.000	0.000
107	A	120	LEU	0	0.000	0.016	40.286	-0.144	-0.144	0.000	0.000	0.000	0.000
108	A	121	LYS	1	0.936	0.968	37.458	8.605	8.605	0.000	0.000	0.000	0.000
109	A	122	LEU	0	-0.008	0.005	32.849	-0.152	-0.152	0.000	0.000	0.000	0.000
110	A	123	ILE	0	0.020	0.011	32.349	0.143	0.143	0.000	0.000	0.000	0.000
111	A	124	PRO	0	-0.030	-0.012	30.842	-0.259	-0.259	0.000	0.000	0.000	0.000
112	A	125	CYS	-1	-0.838	-0.828	25.150	-12.836	-12.836	0.000	0.000	0.000	0.000
113	A	126	ARG	1	0.862	0.931	26.472	10.581	10.581	0.000	0.000	0.000	0.000
114	A	127	GLY	0	0.098	0.034	23.452	-0.038	-0.038	0.000	0.000	0.000	0.000
115	A	128	HIS	0	-0.013	-0.005	18.974	-0.889	-0.889	0.000	0.000	0.000	0.000
116	A	129	GLY	0	0.024	0.016	21.885	0.248	0.248	0.000	0.000	0.000	0.000
117	A	130	GLY	0	0.028	0.025	24.190	0.417	0.417	0.000	0.000	0.000	0.000
118	A	131	PHE	0	-0.023	-0.011	24.143	0.444	0.444	0.000	0.000	0.000	0.000
119	A	132	PRO	0	-0.036	-0.022	24.275	-0.417	-0.417	0.000	0.000	0.000	0.000
120	A	133	VAL	0	0.040	0.018	19.213	-0.511	-0.511	0.000	0.000	0.000	0.000
121	A	134	THR	0	-0.037	-0.030	18.421	0.071	0.071	0.000	0.000	0.000	0.000
122	A	135	ASN	0	-0.071	-0.050	16.084	-0.643	-0.643	0.000	0.000	0.000	0.000
123	A	136	PHE	0	-0.009	-0.013	13.203	1.263	1.263	0.000	0.000	0.000	0.000
124	A	137	TRP	0	0.020	0.022	13.349	-1.807	-1.807	0.000	0.000	0.000	0.000
125	A	138	ARG	1	0.806	0.911	10.408	28.985	28.985	0.000	0.000	0.000	0.000
126	A	139	HIS	0	-0.046	-0.014	12.070	-1.135	-1.135	0.000	0.000	0.000	0.000
127	A	140	ASP	-1	-0.846	-0.934	9.716	-27.921	-27.921	0.000	0.000	0.000	0.000
128	A	141	GLY	0	0.057	0.031	11.370	-1.125	-1.125	0.000	0.000	0.000	0.000
129	A	142	ARG	1	0.919	0.960	12.107	19.854	19.854	0.000	0.000	0.000	0.000
130	A	143	PHE	0	0.041	0.008	9.137	0.337	0.337	0.000	0.000	0.000	0.000
131	A	144	ILE	0	-0.074	-0.034	11.878	0.809	0.809	0.000	0.000	0.000	0.000
133	A	146	PHE	0	-0.023	-0.020	9.429	3.390	3.390	0.000	0.000	0.000	0.000
134	A	147	GLN	0	0.028	0.021	9.426	-2.888	-2.888	0.000	0.000	0.000	0.000
135	A	148	SER	0	-0.064	-0.034	11.210	2.814	2.814	0.000	0.000	0.000	0.000
136	A	149	LYS	1	0.940	0.966	13.123	20.838	20.838	0.000	0.000	0.000	0.000
137	A	150	GLY	0	0.045	0.012	16.045	1.087	1.087	0.000	0.000	0.000	0.000
138	A	151	GLU	-1	-0.887	-0.911	18.172	-16.421	-16.421	0.000	0.000	0.000	0.000
139	A	152	HIS	1	0.763	0.861	20.294	15.304	15.304	0.000	0.000	0.000	0.000
140	A	153	ASP	-1	-0.730	-0.867	23.804	-11.362	-11.362	0.000	0.000	0.000	0.000
141	A	154	HIS	1	0.736	0.826	26.187	12.231	12.231	0.000	0.000	0.000	0.000
142	A	155	PRO	0	0.066	0.033	27.688	-0.397	-0.397	0.000	0.000	0.000	0.000
143	A	156	ARG	1	0.957	0.986	22.857	12.890	12.890	0.000	0.000	0.000	0.000
144	A	157	PRO	0	-0.050	-0.022	27.300	0.371	0.371	0.000	0.000	0.000	0.000
145	A	158	GLU	-1	-0.744	-0.840	29.290	-9.159	-9.159	0.000	0.000	0.000	0.000
146	A	159	THR	0	0.044	0.025	26.823	-0.237	-0.237	0.000	0.000	0.000	0.000
147	A	160	LYS	1	0.912	0.955	28.115	11.418	11.418	0.000	0.000	0.000	0.000
148	A	161	LEU	0	0.049	0.012	28.072	0.262	0.262	0.000	0.000	0.000	0.000
149	A	162	GLU	-1	-0.849	-0.915	31.349	-9.787	-9.787	0.000	0.000	0.000	0.000
150	A	163	ALA	0	-0.018	-0.025	33.011	0.304	0.304	0.000	0.000	0.000	0.000
151	A	164	GLU	-1	-0.994	-1.001	33.473	-9.219	-9.219	0.000	0.000	0.000	0.000
152	A	165	ALA	0	0.044	0.025	35.650	0.253	0.253	0.000	0.000	0.000	0.000
153	A	166	ARG	1	0.834	0.883	37.417	8.562	8.562	0.000	0.000	0.000	0.000
154	A	167	ARG	1	0.860	0.927	38.567	7.978	7.978	0.000	0.000	0.000	0.000
155	A	168	ALA	0	-0.016	-0.002	39.685	0.162	0.162	0.000	0.000	0.000	0.000
156	A	169	MET	0	-0.008	0.005	41.386	0.021	0.021	0.000	0.000	0.000	0.000
157	A	170	LYS	0	0.026	0.027	44.091	-0.302	-0.302	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:14:LEU)