FMO DATABASE

FMODB ID: VK2Z1

Calculation Name: 1O50-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1O50

Chain ID: A

ChEMBL ID:

UniProt ID: Q9X033

Base Structure: X-ray

Registration Date: 2023-09-26

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1285803.003472
FMO2-HF: Nuclear repulsion	1228367.751991
FMO2-HF: Total energy	-57435.251481
FMO2-MP2: Total energy	-57598.834933

3D Structure

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:HIS)

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

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.
-20.437	-12.535	4.718	-4.632	-7.986	-0.017

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.030 / q_NPA : 0.007

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	0	HIS	0	-0.012	0.001	3.383	-5.515	-1.672	-0.003	-1.938	-1.901	0.007
4	A	1	MET	0	0.024	0.038	2.637	-1.336	-0.525	0.453	-0.271	-0.994	0.001
5	A	2	LYS	1	0.886	0.949	6.604	-0.195	-0.195	0.000	0.000	0.000	0.000
6	A	3	VAL	0	0.045	0.022	9.365	-0.287	-0.287	0.000	0.000	0.000	0.000
7	A	4	LYS	1	0.873	0.919	12.110	0.101	0.101	0.000	0.000	0.000	0.000
8	A	5	ASP	-1	-0.881	-0.924	9.450	-0.515	-0.515	0.000	0.000	0.000	0.000
9	A	6	VAL	0	-0.030	-0.028	7.857	-0.241	-0.241	0.000	0.000	0.000	0.000
10	A	7	CYS	0	-0.013	-0.002	10.989	0.041	0.041	0.000	0.000	0.000	0.000
11	A	8	LYS	1	0.957	0.977	14.441	0.621	0.621	0.000	0.000	0.000	0.000
12	A	9	LEU	0	-0.067	-0.002	9.938	0.001	0.001	0.000	0.000	0.000	0.000
13	A	10	ILE	0	-0.038	-0.012	14.531	0.000	0.000	0.000	0.000	0.000	0.000
14	A	11	SER	0	-0.038	-0.013	17.334	0.047	0.047	0.000	0.000	0.000	0.000
15	A	12	LEU	0	0.017	0.015	17.306	0.021	0.021	0.000	0.000	0.000	0.000
16	A	13	LYS	1	0.892	0.938	21.370	0.403	0.403	0.000	0.000	0.000	0.000
17	A	14	PRO	0	0.013	0.010	23.137	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	15	THR	0	0.017	0.023	24.820	0.030	0.030	0.000	0.000	0.000	0.000
19	A	16	VAL	0	-0.021	-0.015	27.759	0.000	0.000	0.000	0.000	0.000	0.000
20	A	17	VAL	0	-0.021	-0.011	29.925	0.005	0.005	0.000	0.000	0.000	0.000
21	A	18	GLU	-1	-0.820	-0.901	33.197	-0.129	-0.129	0.000	0.000	0.000	0.000
22	A	19	GLU	-1	-0.870	-0.969	35.680	-0.100	-0.100	0.000	0.000	0.000	0.000
23	A	20	ASP	-1	-0.975	-0.979	37.074	-0.114	-0.114	0.000	0.000	0.000	0.000
24	A	21	THR	0	0.014	0.010	35.932	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	22	PRO	0	0.046	0.017	37.994	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	23	ILE	0	0.011	0.000	35.663	-0.009	-0.009	0.000	0.000	0.000	0.000
27	A	24	GLU	-1	-0.972	-0.986	36.408	-0.164	-0.164	0.000	0.000	0.000	0.000
28	A	25	GLU	-1	-0.859	-0.926	36.875	-0.174	-0.174	0.000	0.000	0.000	0.000
29	A	26	ILE	0	-0.062	-0.032	31.794	-0.015	-0.015	0.000	0.000	0.000	0.000
30	A	27	VAL	0	-0.028	-0.026	32.673	-0.020	-0.020	0.000	0.000	0.000	0.000
31	A	28	ASP	-1	-0.867	-0.932	33.583	-0.208	-0.208	0.000	0.000	0.000	0.000
32	A	29	ARG	1	0.869	0.926	30.977	0.229	0.229	0.000	0.000	0.000	0.000
33	A	30	ILE	0	-0.031	-0.011	27.960	-0.020	-0.020	0.000	0.000	0.000	0.000
34	A	31	LEU	0	-0.042	-0.030	29.504	-0.023	-0.023	0.000	0.000	0.000	0.000
35	A	32	GLU	-1	-1.009	-0.990	31.649	-0.306	-0.306	0.000	0.000	0.000	0.000
36	A	33	ASP	-1	-0.837	-0.905	26.015	-0.451	-0.451	0.000	0.000	0.000	0.000
37	A	34	PRO	0	0.032	0.024	26.875	-0.021	-0.021	0.000	0.000	0.000	0.000
38	A	35	VAL	0	-0.093	-0.031	20.829	-0.030	-0.030	0.000	0.000	0.000	0.000
39	A	36	THR	0	-0.021	-0.032	22.125	-0.043	-0.043	0.000	0.000	0.000	0.000
40	A	37	ARG	1	0.857	0.918	19.287	0.655	0.655	0.000	0.000	0.000	0.000
41	A	38	THR	0	-0.090	-0.061	21.264	0.029	0.029	0.000	0.000	0.000	0.000
42	A	39	VAL	0	0.014	0.033	23.952	-0.011	-0.011	0.000	0.000	0.000	0.000
43	A	40	TYR	0	-0.007	-0.024	21.182	0.017	0.017	0.000	0.000	0.000	0.000
44	A	41	VAL	0	0.020	0.017	27.689	0.002	0.002	0.000	0.000	0.000	0.000
45	A	42	ALA	0	0.012	0.000	30.485	0.004	0.004	0.000	0.000	0.000	0.000
46	A	43	ARG	1	0.918	0.952	32.197	0.108	0.108	0.000	0.000	0.000	0.000
47	A	44	ASP	-1	-0.910	-0.956	34.547	-0.075	-0.075	0.000	0.000	0.000	0.000
48	A	45	ASN	0	-0.057	-0.040	32.295	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	46	LYS	1	0.812	0.933	30.085	0.067	0.067	0.000	0.000	0.000	0.000
50	A	47	LEU	0	-0.021	-0.019	24.276	-0.009	-0.009	0.000	0.000	0.000	0.000
51	A	48	VAL	0	-0.022	-0.018	28.480	0.014	0.014	0.000	0.000	0.000	0.000
52	A	49	GLY	0	0.050	0.021	28.650	0.012	0.012	0.000	0.000	0.000	0.000
53	A	50	MET	0	-0.102	-0.034	22.560	-0.033	-0.033	0.000	0.000	0.000	0.000
54	A	51	ILE	0	0.044	0.015	27.201	0.018	0.018	0.000	0.000	0.000	0.000
55	A	52	PRO	0	0.031	0.023	23.836	-0.021	-0.021	0.000	0.000	0.000	0.000
56	A	53	VAL	0	0.078	0.037	25.142	0.029	0.029	0.000	0.000	0.000	0.000
57	A	54	MET	0	-0.014	-0.007	25.150	0.030	0.030	0.000	0.000	0.000	0.000
58	A	55	HIS	0	-0.032	-0.021	26.920	0.017	0.017	0.000	0.000	0.000	0.000
59	A	56	LEU	0	0.085	0.047	28.879	0.018	0.018	0.000	0.000	0.000	0.000
60	A	57	LEU	0	0.005	0.028	29.174	0.016	0.016	0.000	0.000	0.000	0.000
61	A	58	LYS	1	0.922	0.957	26.830	0.217	0.217	0.000	0.000	0.000	0.000
62	A	59	VAL	0	0.006	0.009	32.525	0.016	0.016	0.000	0.000	0.000	0.000
63	A	60	SER	0	-0.037	-0.046	34.482	0.013	0.013	0.000	0.000	0.000	0.000
64	A	61	GLY	0	0.021	0.003	35.386	0.008	0.008	0.000	0.000	0.000	0.000
65	A	62	PHE	0	-0.008	-0.003	36.958	0.010	0.010	0.000	0.000	0.000	0.000
66	A	63	HIS	0	-0.045	-0.018	38.842	0.013	0.013	0.000	0.000	0.000	0.000
67	A	64	PHE	0	-0.030	-0.023	39.270	0.006	0.006	0.000	0.000	0.000	0.000
68	A	65	PHE	0	-0.034	-0.018	38.628	0.003	0.003	0.000	0.000	0.000	0.000
69	A	66	GLY	0	-0.013	0.012	41.760	0.005	0.005	0.000	0.000	0.000	0.000
70	A	67	PHE	0	-0.048	-0.022	33.796	0.005	0.005	0.000	0.000	0.000	0.000
71	A	68	ILE	0	0.018	-0.005	36.454	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	69	PRO	0	-0.022	0.000	31.574	0.006	0.006	0.000	0.000	0.000	0.000
73	A	77	SER	0	-0.003	-0.011	34.528	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	78	MET	0	0.038	0.029	34.589	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	79	LYS	1	0.927	0.961	37.784	0.063	0.063	0.000	0.000	0.000	0.000
76	A	80	ARG	1	0.952	0.977	40.209	0.070	0.070	0.000	0.000	0.000	0.000
77	A	81	LEU	0	0.042	0.026	38.080	0.003	0.003	0.000	0.000	0.000	0.000
78	A	82	ILE	0	-0.107	-0.056	42.127	0.004	0.004	0.000	0.000	0.000	0.000
79	A	83	ALA	0	-0.009	-0.017	42.523	0.000	0.000	0.000	0.000	0.000	0.000
80	A	84	LYS	1	0.873	0.937	40.562	0.101	0.101	0.000	0.000	0.000	0.000
81	A	85	ASN	0	0.049	0.028	38.821	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	86	ALA	0	0.067	0.024	34.050	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	87	SER	0	-0.030	-0.028	34.702	0.001	0.001	0.000	0.000	0.000	0.000
84	A	88	GLU	-1	-0.809	-0.890	36.457	-0.094	-0.094	0.000	0.000	0.000	0.000
85	A	89	ILE	0	-0.065	-0.039	32.869	0.002	0.002	0.000	0.000	0.000	0.000
86	A	90	MET	0	-0.050	0.014	30.897	-0.015	-0.015	0.000	0.000	0.000	0.000
87	A	91	LEU	0	-0.036	-0.014	26.647	0.011	0.011	0.000	0.000	0.000	0.000
88	A	92	ASP	-1	-0.845	-0.931	26.747	-0.085	-0.085	0.000	0.000	0.000	0.000
89	A	93	PRO	0	-0.065	-0.029	24.384	-0.018	-0.018	0.000	0.000	0.000	0.000
90	A	94	VAL	0	0.013	0.014	18.436	0.022	0.022	0.000	0.000	0.000	0.000
91	A	95	TYR	0	-0.021	-0.023	19.311	-0.035	-0.035	0.000	0.000	0.000	0.000
92	A	96	VAL	0	-0.003	0.005	13.927	0.019	0.019	0.000	0.000	0.000	0.000
93	A	97	HIS	1	0.908	0.947	15.456	0.085	0.085	0.000	0.000	0.000	0.000
94	A	98	MET	0	0.072	0.029	14.823	-0.069	-0.069	0.000	0.000	0.000	0.000
95	A	99	ASP	-1	-0.919	-0.971	13.343	0.000	0.000	0.000	0.000	0.000	0.000
96	A	100	THR	0	0.015	0.010	11.230	0.150	0.150	0.000	0.000	0.000	0.000
97	A	101	PRO	0	0.036	0.014	6.690	-0.194	-0.194	0.000	0.000	0.000	0.000
98	A	102	LEU	0	0.040	0.012	4.693	-0.163	-0.069	-0.001	-0.003	-0.089	0.000
99	A	103	GLU	-1	-0.941	-0.983	4.445	0.485	0.715	-0.001	-0.011	-0.218	0.000
100	A	104	GLU	-1	-0.904	-0.960	6.358	0.161	0.161	0.000	0.000	0.000	0.000
101	A	105	ALA	0	0.035	0.015	9.683	0.029	0.029	0.000	0.000	0.000	0.000
102	A	106	LEU	0	-0.005	0.002	7.257	0.012	0.012	0.000	0.000	0.000	0.000
103	A	107	LYS	1	0.925	0.970	10.323	0.038	0.038	0.000	0.000	0.000	0.000
104	A	108	LEU	0	0.001	0.017	11.975	0.044	0.044	0.000	0.000	0.000	0.000
105	A	109	MET	0	-0.034	-0.010	13.514	-0.011	-0.011	0.000	0.000	0.000	0.000
106	A	110	ILE	0	0.001	-0.008	11.695	0.040	0.040	0.000	0.000	0.000	0.000
107	A	111	ASP	-1	-0.925	-0.960	15.493	-0.057	-0.057	0.000	0.000	0.000	0.000
108	A	112	ASN	0	-0.072	-0.041	17.703	0.061	0.061	0.000	0.000	0.000	0.000
109	A	113	ASN	0	-0.077	-0.032	18.868	-0.027	-0.027	0.000	0.000	0.000	0.000
110	A	114	ILE	0	-0.016	0.002	18.228	0.009	0.009	0.000	0.000	0.000	0.000
111	A	115	GLN	0	-0.001	-0.014	16.656	-0.119	-0.119	0.000	0.000	0.000	0.000
112	A	116	GLU	-1	-0.750	-0.843	17.253	-0.590	-0.590	0.000	0.000	0.000	0.000
113	A	117	MET	0	-0.034	0.017	14.420	0.085	0.085	0.000	0.000	0.000	0.000
114	A	118	PRO	0	0.030	0.039	18.707	-0.048	-0.048	0.000	0.000	0.000	0.000
115	A	119	VAL	0	-0.006	-0.022	17.029	0.005	0.005	0.000	0.000	0.000	0.000
116	A	120	VAL	0	0.005	0.004	19.541	0.013	0.013	0.000	0.000	0.000	0.000
117	A	121	ASP	-1	-0.807	-0.913	20.783	-0.095	-0.095	0.000	0.000	0.000	0.000
118	A	122	GLU	-1	-0.935	-0.990	21.929	0.036	0.036	0.000	0.000	0.000	0.000
119	A	123	LYS	1	0.811	0.922	24.547	0.096	0.096	0.000	0.000	0.000	0.000
120	A	124	GLY	0	0.056	0.023	25.839	-0.003	-0.003	0.000	0.000	0.000	0.000
121	A	125	GLU	-1	-0.869	-0.931	26.429	-0.118	-0.118	0.000	0.000	0.000	0.000
122	A	126	ILE	0	-0.007	-0.008	23.653	-0.008	-0.008	0.000	0.000	0.000	0.000
123	A	127	VAL	0	-0.021	-0.009	21.435	0.005	0.005	0.000	0.000	0.000	0.000
124	A	128	GLY	0	-0.030	-0.018	20.221	-0.021	-0.021	0.000	0.000	0.000	0.000
125	A	129	ASH	0	-0.071	-0.088	19.203	0.052	0.052	0.000	0.000	0.000	0.000
126	A	130	LEU	0	0.017	0.028	11.779	-0.063	-0.063	0.000	0.000	0.000	0.000
127	A	131	ASN	0	0.066	0.030	14.974	-0.037	-0.037	0.000	0.000	0.000	0.000
128	A	132	SER	0	0.031	-0.015	12.779	-0.160	-0.160	0.000	0.000	0.000	0.000
129	A	133	LEU	0	-0.041	-0.015	11.963	-0.219	-0.219	0.000	0.000	0.000	0.000
130	A	134	GLU	-1	-0.763	-0.900	12.018	-1.267	-1.267	0.000	0.000	0.000	0.000
131	A	135	ILE	0	0.030	0.006	7.279	-0.398	-0.398	0.000	0.000	0.000	0.000
132	A	136	LEU	0	-0.019	-0.013	7.261	-0.743	-0.743	0.000	0.000	0.000	0.000
133	A	137	LEU	0	-0.037	-0.010	8.609	-0.522	-0.522	0.000	0.000	0.000	0.000
134	A	138	ALA	0	0.029	-0.003	6.111	-0.360	-0.360	0.000	0.000	0.000	0.000
135	A	139	LEU	0	-0.052	-0.023	2.545	-2.538	-2.019	0.955	-0.321	-1.153	0.000
136	A	140	TRP	0	-0.019	-0.003	4.080	-2.129	-1.984	-0.001	-0.058	-0.086	0.000
137	A	141	LYS	1	0.868	0.944	6.846	2.572	2.572	0.000	0.000	0.000	0.000
138	A	142	GLY	0	0.046	0.047	5.246	0.897	0.897	0.000	0.000	0.000	0.000
139	A	143	ARG	1	0.866	0.922	5.240	0.717	0.897	-0.001	-0.014	-0.164	0.000
140	A	144	GLU	-1	-0.839	-0.930	3.215	-7.792	-6.436	0.058	-0.584	-0.830	-0.004
141	A	145	LYS	1	0.926	0.972	2.236	-1.071	-0.347	3.259	-1.432	-2.551	-0.021

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