FMO DATABASE

FMODB ID: 16JVZ

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	OptHSide
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	-1286401.74126
FMO2-HF: Nuclear repulsion	1228965.615474
FMO2-HF: Total energy	-57436.125786
FMO2-MP2: Total energy	-57599.782818

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.
-17.828	-9.146	3	-4.325	-7.357	-0.014

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 : 0.026 / q_NPA : 0.003

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	-0.003	0.008	3.386	-5.345	-1.477	-0.003	-1.921	-1.944	0.006
4	A	1	MET	0	0.019	0.031	3.166	-1.508	-0.615	0.154	-0.239	-0.808	0.001
5	A	2	LYS	1	0.806	0.901	6.608	-0.294	-0.294	0.000	0.000	0.000	0.000
6	A	3	VAL	0	0.052	0.028	9.370	-0.276	-0.276	0.000	0.000	0.000	0.000
7	A	4	LYS	1	0.836	0.888	11.999	-0.008	-0.008	0.000	0.000	0.000	0.000
8	A	5	ASP	-1	-0.864	-0.915	9.855	-0.329	-0.329	0.000	0.000	0.000	0.000
9	A	6	VAL	0	-0.027	-0.024	8.063	-0.230	-0.230	0.000	0.000	0.000	0.000
10	A	7	CYS	0	-0.048	-0.009	11.270	0.047	0.047	0.000	0.000	0.000	0.000
11	A	8	LYS	1	0.959	0.979	14.721	0.576	0.576	0.000	0.000	0.000	0.000
12	A	9	LEU	0	-0.055	0.001	10.195	-0.008	-0.008	0.000	0.000	0.000	0.000
13	A	10	ILE	0	-0.031	-0.014	14.785	-0.006	-0.006	0.000	0.000	0.000	0.000
14	A	11	SER	0	-0.020	-0.006	17.551	0.052	0.052	0.000	0.000	0.000	0.000
15	A	12	LEU	0	-0.013	0.004	17.409	0.016	0.016	0.000	0.000	0.000	0.000
16	A	13	LYS	1	0.854	0.893	21.576	0.390	0.390	0.000	0.000	0.000	0.000
17	A	14	PRO	0	-0.005	0.004	23.238	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	15	THR	0	0.007	0.021	25.011	0.029	0.029	0.000	0.000	0.000	0.000
19	A	16	VAL	0	-0.012	-0.014	27.858	0.001	0.001	0.000	0.000	0.000	0.000
20	A	17	VAL	0	-0.014	-0.007	30.095	0.006	0.006	0.000	0.000	0.000	0.000
21	A	18	GLU	-1	-0.773	-0.863	33.355	-0.119	-0.119	0.000	0.000	0.000	0.000
22	A	19	GLU	-1	-0.812	-0.926	35.773	-0.098	-0.098	0.000	0.000	0.000	0.000
23	A	20	ASP	-1	-0.957	-0.974	37.143	-0.111	-0.111	0.000	0.000	0.000	0.000
24	A	21	THR	0	0.008	0.010	36.097	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	22	PRO	0	0.045	0.014	38.099	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	23	ILE	0	0.007	-0.001	35.623	-0.009	-0.009	0.000	0.000	0.000	0.000
27	A	24	GLU	-1	-0.965	-0.979	36.484	-0.161	-0.161	0.000	0.000	0.000	0.000
28	A	25	GLU	-1	-0.863	-0.937	37.305	-0.177	-0.177	0.000	0.000	0.000	0.000
29	A	26	ILE	0	-0.046	-0.024	31.929	-0.014	-0.014	0.000	0.000	0.000	0.000
30	A	27	VAL	0	-0.028	-0.025	32.771	-0.020	-0.020	0.000	0.000	0.000	0.000
31	A	28	ASP	-1	-0.883	-0.934	33.668	-0.209	-0.209	0.000	0.000	0.000	0.000
32	A	29	ARG	1	0.848	0.915	31.464	0.213	0.213	0.000	0.000	0.000	0.000
33	A	30	ILE	0	-0.038	-0.014	28.102	-0.020	-0.020	0.000	0.000	0.000	0.000
34	A	31	LEU	0	-0.039	-0.028	29.600	-0.024	-0.024	0.000	0.000	0.000	0.000
35	A	32	GLU	-1	-0.994	-0.981	31.662	-0.301	-0.301	0.000	0.000	0.000	0.000
36	A	33	ASP	-1	-0.801	-0.874	26.262	-0.445	-0.445	0.000	0.000	0.000	0.000
37	A	34	PRO	0	0.035	0.023	26.991	-0.020	-0.020	0.000	0.000	0.000	0.000
38	A	35	VAL	0	-0.085	-0.030	20.882	-0.030	-0.030	0.000	0.000	0.000	0.000
39	A	36	THR	0	-0.023	-0.012	22.217	-0.042	-0.042	0.000	0.000	0.000	0.000
40	A	37	ARG	1	0.831	0.900	18.826	0.662	0.662	0.000	0.000	0.000	0.000
41	A	38	THR	0	-0.094	-0.069	21.382	0.026	0.026	0.000	0.000	0.000	0.000
42	A	39	VAL	0	0.007	0.028	24.040	-0.009	-0.009	0.000	0.000	0.000	0.000
43	A	40	TYR	0	0.005	-0.009	21.370	0.018	0.018	0.000	0.000	0.000	0.000
44	A	41	VAL	0	0.018	0.014	27.827	0.002	0.002	0.000	0.000	0.000	0.000
45	A	42	ALA	0	0.006	-0.005	30.484	0.005	0.005	0.000	0.000	0.000	0.000
46	A	43	ARG	1	0.808	0.884	32.197	0.101	0.101	0.000	0.000	0.000	0.000
47	A	44	ASP	-1	-0.886	-0.954	34.546	-0.071	-0.071	0.000	0.000	0.000	0.000
48	A	45	ASN	0	-0.084	-0.047	32.312	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	46	LYS	1	0.777	0.891	30.082	0.060	0.060	0.000	0.000	0.000	0.000
50	A	47	LEU	0	-0.022	-0.019	24.254	-0.010	-0.010	0.000	0.000	0.000	0.000
51	A	48	VAL	0	-0.020	-0.020	28.479	0.014	0.014	0.000	0.000	0.000	0.000
52	A	49	GLY	0	0.052	0.026	28.649	0.011	0.011	0.000	0.000	0.000	0.000
53	A	50	MET	0	-0.096	-0.026	22.590	-0.031	-0.031	0.000	0.000	0.000	0.000
54	A	51	ILE	0	0.035	0.014	27.264	0.016	0.016	0.000	0.000	0.000	0.000
55	A	52	PRO	0	0.027	0.019	23.758	-0.022	-0.022	0.000	0.000	0.000	0.000
56	A	53	VAL	0	0.071	0.035	25.176	0.028	0.028	0.000	0.000	0.000	0.000
57	A	54	MET	0	-0.011	-0.005	25.091	0.031	0.031	0.000	0.000	0.000	0.000
58	A	55	HIS	0	-0.026	-0.023	26.900	0.015	0.015	0.000	0.000	0.000	0.000
59	A	56	LEU	0	0.084	0.046	28.900	0.018	0.018	0.000	0.000	0.000	0.000
60	A	57	LEU	0	0.008	0.017	29.234	0.015	0.015	0.000	0.000	0.000	0.000
61	A	58	LYS	1	0.925	0.956	26.794	0.235	0.235	0.000	0.000	0.000	0.000
62	A	59	VAL	0	0.001	0.006	32.483	0.016	0.016	0.000	0.000	0.000	0.000
63	A	60	SER	0	-0.033	-0.027	34.554	0.013	0.013	0.000	0.000	0.000	0.000
64	A	61	GLY	0	0.016	0.001	35.348	0.008	0.008	0.000	0.000	0.000	0.000
65	A	62	PHE	0	-0.020	-0.011	36.913	0.011	0.011	0.000	0.000	0.000	0.000
66	A	63	HIS	0	-0.052	-0.020	38.836	0.014	0.014	0.000	0.000	0.000	0.000
67	A	64	PHE	0	-0.021	-0.017	39.055	0.007	0.007	0.000	0.000	0.000	0.000
68	A	65	PHE	0	-0.030	-0.021	38.277	0.002	0.002	0.000	0.000	0.000	0.000
69	A	66	GLY	0	-0.010	0.016	41.710	0.005	0.005	0.000	0.000	0.000	0.000
70	A	67	PHE	0	-0.044	-0.022	33.611	0.005	0.005	0.000	0.000	0.000	0.000
71	A	68	ILE	0	0.015	-0.007	36.330	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	69	PRO	0	-0.024	0.001	31.617	0.005	0.005	0.000	0.000	0.000	0.000
73	A	77	SER	0	-0.001	-0.012	34.624	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	78	MET	0	0.004	0.019	34.842	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	79	LYS	1	0.948	0.971	37.819	0.066	0.066	0.000	0.000	0.000	0.000
76	A	80	ARG	1	0.956	0.980	40.248	0.072	0.072	0.000	0.000	0.000	0.000
77	A	81	LEU	0	0.058	0.036	38.099	0.003	0.003	0.000	0.000	0.000	0.000
78	A	82	ILE	0	-0.085	-0.053	42.171	0.004	0.004	0.000	0.000	0.000	0.000
79	A	83	ALA	0	0.030	0.006	42.567	0.000	0.000	0.000	0.000	0.000	0.000
80	A	84	LYS	1	0.811	0.906	40.609	0.098	0.098	0.000	0.000	0.000	0.000
81	A	85	ASN	0	0.049	0.039	38.932	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	86	ALA	0	0.072	0.024	34.132	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	87	SER	0	-0.037	-0.041	34.761	0.001	0.001	0.000	0.000	0.000	0.000
84	A	88	GLU	-1	-0.811	-0.888	36.497	-0.096	-0.096	0.000	0.000	0.000	0.000
85	A	89	ILE	0	-0.054	-0.037	33.034	0.002	0.002	0.000	0.000	0.000	0.000
86	A	90	MET	0	-0.048	0.014	30.929	-0.015	-0.015	0.000	0.000	0.000	0.000
87	A	91	LEU	0	-0.030	-0.008	26.760	0.011	0.011	0.000	0.000	0.000	0.000
88	A	92	ASP	-1	-0.849	-0.935	26.718	-0.088	-0.088	0.000	0.000	0.000	0.000
89	A	93	PRO	0	-0.060	-0.030	24.364	-0.019	-0.019	0.000	0.000	0.000	0.000
90	A	94	VAL	0	0.005	0.003	18.463	0.021	0.021	0.000	0.000	0.000	0.000
91	A	95	TYR	0	-0.015	-0.019	19.317	-0.038	-0.038	0.000	0.000	0.000	0.000
92	A	96	VAL	0	-0.002	0.005	13.916	0.018	0.018	0.000	0.000	0.000	0.000
93	A	97	HIS	1	0.807	0.872	15.474	0.053	0.053	0.000	0.000	0.000	0.000
94	A	98	MET	0	0.085	0.031	14.824	-0.063	-0.063	0.000	0.000	0.000	0.000
95	A	99	ASP	-1	-0.856	-0.929	13.356	0.110	0.110	0.000	0.000	0.000	0.000
96	A	100	THR	0	0.027	0.019	11.250	0.151	0.151	0.000	0.000	0.000	0.000
97	A	101	PRO	0	0.046	0.018	6.633	-0.178	-0.178	0.000	0.000	0.000	0.000
98	A	102	LEU	0	0.029	0.008	4.848	-0.105	-0.105	0.000	0.000	0.000	0.000
99	A	103	GLU	-1	-0.943	-0.985	4.118	0.245	0.572	0.000	-0.065	-0.262	0.000
100	A	104	GLU	-1	-0.901	-0.951	6.354	0.163	0.163	0.000	0.000	0.000	0.000
101	A	105	ALA	0	0.011	0.000	9.678	0.025	0.025	0.000	0.000	0.000	0.000
102	A	106	LEU	0	-0.008	-0.002	7.207	0.009	0.009	0.000	0.000	0.000	0.000
103	A	107	LYS	1	0.846	0.913	10.315	0.126	0.126	0.000	0.000	0.000	0.000
104	A	108	LEU	0	0.011	0.018	11.970	0.049	0.049	0.000	0.000	0.000	0.000
105	A	109	MET	0	-0.024	0.004	13.548	-0.019	-0.019	0.000	0.000	0.000	0.000
106	A	110	ILE	0	0.004	-0.006	11.797	0.042	0.042	0.000	0.000	0.000	0.000
107	A	111	ASP	-1	-0.863	-0.913	15.516	-0.077	-0.077	0.000	0.000	0.000	0.000
108	A	112	ASN	0	-0.052	-0.035	17.735	0.066	0.066	0.000	0.000	0.000	0.000
109	A	113	ASN	0	-0.089	-0.035	18.899	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	114	ILE	0	-0.008	0.003	18.263	0.012	0.012	0.000	0.000	0.000	0.000
111	A	115	GLN	0	0.020	-0.008	16.683	-0.109	-0.109	0.000	0.000	0.000	0.000
112	A	116	GLU	-1	-0.763	-0.862	17.326	-0.580	-0.580	0.000	0.000	0.000	0.000
113	A	117	MET	0	-0.020	0.025	14.483	0.080	0.080	0.000	0.000	0.000	0.000
114	A	118	PRO	0	0.030	0.038	18.874	-0.044	-0.044	0.000	0.000	0.000	0.000
115	A	119	VAL	0	-0.012	-0.019	17.186	0.006	0.006	0.000	0.000	0.000	0.000
116	A	120	VAL	0	0.010	0.004	19.543	0.013	0.013	0.000	0.000	0.000	0.000
117	A	121	ASP	-1	-0.778	-0.865	20.783	-0.067	-0.067	0.000	0.000	0.000	0.000
118	A	122	GLU	-1	-0.862	-0.936	21.609	0.046	0.046	0.000	0.000	0.000	0.000
119	A	123	LYS	1	0.722	0.845	24.546	0.089	0.089	0.000	0.000	0.000	0.000
120	A	124	GLY	0	0.076	0.037	25.838	-0.005	-0.005	0.000	0.000	0.000	0.000
121	A	125	GLU	-1	-0.768	-0.849	26.421	-0.100	-0.100	0.000	0.000	0.000	0.000
122	A	126	ILE	0	0.005	-0.005	23.878	-0.005	-0.005	0.000	0.000	0.000	0.000
123	A	127	VAL	0	-0.025	-0.012	21.440	0.006	0.006	0.000	0.000	0.000	0.000
124	A	128	GLY	0	-0.024	-0.012	20.479	-0.018	-0.018	0.000	0.000	0.000	0.000
125	A	129	ASH	0	-0.061	-0.074	19.436	0.048	0.048	0.000	0.000	0.000	0.000
126	A	130	LEU	0	0.018	0.024	11.972	-0.055	-0.055	0.000	0.000	0.000	0.000
127	A	131	ASN	0	0.066	0.033	15.158	-0.047	-0.047	0.000	0.000	0.000	0.000
128	A	132	SER	0	0.031	-0.013	12.842	-0.151	-0.151	0.000	0.000	0.000	0.000
129	A	133	LEU	0	-0.032	-0.011	12.015	-0.227	-0.227	0.000	0.000	0.000	0.000
130	A	134	GLU	-1	-0.765	-0.902	12.180	-1.223	-1.223	0.000	0.000	0.000	0.000
131	A	135	ILE	0	0.025	0.004	7.412	-0.373	-0.373	0.000	0.000	0.000	0.000
132	A	136	LEU	0	-0.027	-0.016	7.352	-0.734	-0.734	0.000	0.000	0.000	0.000
133	A	137	LEU	0	-0.026	-0.007	8.640	-0.525	-0.525	0.000	0.000	0.000	0.000
134	A	138	ALA	0	0.033	0.000	6.540	-0.358	-0.358	0.000	0.000	0.000	0.000
135	A	139	LEU	0	-0.050	-0.017	2.447	-2.393	-1.873	0.830	-0.281	-1.069	-0.001
136	A	140	TRP	0	-0.032	-0.012	4.170	-2.093	-1.971	-0.001	-0.041	-0.080	0.000
137	A	141	LYS	1	0.873	0.944	6.929	2.605	2.605	0.000	0.000	0.000	0.000
138	A	142	GLY	0	0.053	0.051	5.349	0.872	0.872	0.000	0.000	0.000	0.000
139	A	143	ARG	1	0.880	0.932	5.229	0.801	0.801	0.000	0.000	0.000	0.000
140	A	144	GLU	-1	-0.690	-0.828	3.172	-7.460	-6.057	0.063	-0.585	-0.881	-0.004
141	A	145	LYS	1	0.798	0.892	2.429	0.826	2.375	1.957	-1.193	-2.313	-0.016

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