FMO DATABASE

FMODB ID: MVG8Z

Calculation Name: 1UFH-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1UFH

Chain ID: A

ChEMBL ID:

UniProt ID: O32293

Base Structure: X-ray

Registration Date: 2023-09-20

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	155
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1547306.574472
FMO2-HF: Nuclear repulsion	1484632.408938
FMO2-HF: Total energy	-62674.165534
FMO2-MP2: Total energy	-62858.879418

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:THR)

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

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.
-7.357	-4.146	3.769	-2.97	-4.009	-0.012

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.012 / 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	4	MET	0	0.027	0.021	3.348	0.852	3.418	-0.018	-1.117	-1.431	0.006
4	A	5	LEU	0	0.006	0.004	5.424	0.039	0.039	0.000	0.000	0.000	0.000
5	A	6	THR	0	0.000	-0.004	8.982	0.128	0.128	0.000	0.000	0.000	0.000
6	A	7	PRO	0	0.028	0.008	11.411	-0.018	-0.018	0.000	0.000	0.000	0.000
7	A	8	MET	0	0.002	0.029	15.190	-0.021	-0.021	0.000	0.000	0.000	0.000
8	A	9	GLN	0	0.014	0.005	16.462	0.132	0.132	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.019	-0.008	19.076	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.956	-0.965	21.728	-0.479	-0.479	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.759	-0.873	16.046	-0.950	-0.950	0.000	0.000	0.000	0.000
12	A	13	PHE	0	0.066	0.030	20.243	0.024	0.024	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.934	0.960	21.857	0.333	0.333	0.000	0.000	0.000	0.000
14	A	15	SER	0	-0.016	0.003	22.139	0.034	0.034	0.000	0.000	0.000	0.000
15	A	16	TYR	0	-0.063	-0.078	19.374	0.020	0.020	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.009	0.011	21.825	0.028	0.028	0.000	0.000	0.000	0.000
17	A	18	THR	0	-0.042	-0.024	25.003	0.039	0.039	0.000	0.000	0.000	0.000
18	A	19	TYR	0	-0.013	-0.002	20.070	0.022	0.022	0.000	0.000	0.000	0.000
19	A	20	THR	0	0.054	0.023	21.785	0.013	0.013	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.040	-0.011	24.208	0.032	0.032	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.965	0.995	27.610	0.267	0.267	0.000	0.000	0.000	0.000
22	A	23	HIS	0	0.079	0.051	22.496	0.010	0.010	0.000	0.000	0.000	0.000
23	A	24	TYR	0	0.004	-0.018	25.559	0.028	0.028	0.000	0.000	0.000	0.000
24	A	25	ALA	0	0.000	-0.007	27.135	0.020	0.020	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.914	-0.957	28.243	-0.214	-0.214	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.762	-0.845	24.937	-0.184	-0.184	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.903	0.960	28.312	0.148	0.148	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.003	0.017	31.301	0.013	0.013	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.805	0.895	26.342	0.187	0.187	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.043	-0.024	30.278	0.010	0.010	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.043	-0.008	32.140	0.011	0.011	0.000	0.000	0.000	0.000
32	A	33	THR	0	-0.101	-0.051	33.420	0.003	0.003	0.000	0.000	0.000	0.000
33	A	34	TRP	0	0.033	-0.001	31.955	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	35	LEU	0	0.043	0.032	36.477	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.020	0.000	36.859	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.925	-0.970	37.919	-0.108	-0.108	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.896	-0.942	39.192	-0.096	-0.096	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.059	-0.032	33.902	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	40	GLN	0	-0.015	-0.012	34.155	-0.017	-0.017	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.028	0.013	34.621	-0.009	-0.009	0.000	0.000	0.000	0.000
41	A	42	LEU	0	0.038	0.029	35.332	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	43	SER	0	-0.005	-0.032	29.755	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.937	0.966	31.248	0.186	0.186	0.000	0.000	0.000	0.000
44	A	45	GLN	0	0.000	0.012	33.122	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.030	0.015	29.436	0.001	0.001	0.000	0.000	0.000	0.000
46	A	47	PHE	0	-0.002	-0.009	25.410	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.094	-0.064	29.607	-0.013	-0.013	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.895	-0.945	32.365	-0.124	-0.124	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.073	-0.023	26.774	0.003	0.003	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.051	-0.026	23.988	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	52	PRO	0	0.027	0.029	28.464	-0.011	-0.011	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.911	0.956	29.539	0.163	0.163	0.000	0.000	0.000	0.000
53	A	54	GLY	0	0.016	0.008	26.891	-0.013	-0.013	0.000	0.000	0.000	0.000
54	A	55	LEU	0	0.003	0.001	20.512	0.008	0.008	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.940	-0.959	23.565	-0.231	-0.231	0.000	0.000	0.000	0.000
56	A	57	THR	0	-0.102	-0.060	26.090	0.032	0.032	0.000	0.000	0.000	0.000
57	A	58	PRO	0	0.011	-0.012	25.484	-0.011	-0.011	0.000	0.000	0.000	0.000
58	A	59	HIS	0	0.036	0.015	24.475	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	60	HIS	0	-0.005	0.020	22.570	-0.010	-0.010	0.000	0.000	0.000	0.000
60	A	61	HIS	0	0.015	0.010	17.549	-0.030	-0.030	0.000	0.000	0.000	0.000
61	A	62	LEU	0	0.018	0.010	17.891	-0.023	-0.023	0.000	0.000	0.000	0.000
62	A	63	TRP	0	-0.002	-0.015	12.482	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	64	SER	0	-0.031	-0.047	12.967	0.043	0.043	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.052	-0.023	8.517	-0.171	-0.171	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.872	0.923	7.928	1.541	1.541	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.014	0.008	3.265	-1.765	-1.367	0.022	-0.147	-0.274	0.000
67	A	68	ASN	0	-0.015	-0.021	4.116	-1.018	-0.845	0.000	-0.047	-0.125	0.000
68	A	69	GLU	-1	-0.882	-0.945	6.703	-1.482	-1.482	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.903	0.959	10.142	1.097	1.097	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.833	-0.878	8.664	-1.603	-1.603	0.000	0.000	0.000	0.000
71	A	72	ILE	0	0.028	0.011	9.324	-0.483	-0.483	0.000	0.000	0.000	0.000
72	A	73	VAL	0	0.013	-0.010	7.207	0.261	0.261	0.000	0.000	0.000	0.000
73	A	74	GLY	0	-0.015	-0.023	10.489	0.256	0.256	0.000	0.000	0.000	0.000
74	A	75	TRP	0	-0.065	-0.006	12.375	-0.130	-0.130	0.000	0.000	0.000	0.000
75	A	76	LEU	0	0.004	-0.010	11.568	0.010	0.010	0.000	0.000	0.000	0.000
76	A	77	TRP	0	-0.007	-0.004	14.803	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	78	ILE	0	-0.004	-0.001	16.123	0.034	0.034	0.000	0.000	0.000	0.000
78	A	79	HIS	0	-0.024	-0.009	19.083	0.003	0.003	0.000	0.000	0.000	0.000
79	A	80	ALA	0	0.031	-0.001	20.954	0.023	0.023	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.900	-0.937	23.042	-0.057	-0.057	0.000	0.000	0.000	0.000
81	A	82	PRO	0	-0.031	-0.021	25.302	0.013	0.013	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.902	-0.949	26.509	0.011	0.011	0.000	0.000	0.000	0.000
83	A	84	HIS	0	0.007	0.025	26.934	0.015	0.015	0.000	0.000	0.000	0.000
84	A	85	PRO	0	0.037	0.005	28.660	0.013	0.013	0.000	0.000	0.000	0.000
85	A	86	GLN	0	-0.037	-0.026	26.874	0.016	0.016	0.000	0.000	0.000	0.000
86	A	87	GLN	0	0.023	0.025	23.950	0.031	0.031	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.775	-0.858	22.854	0.022	0.022	0.000	0.000	0.000	0.000
88	A	89	ALA	0	-0.013	0.001	19.391	-0.016	-0.016	0.000	0.000	0.000	0.000
89	A	90	PHE	0	-0.025	-0.016	20.954	0.011	0.011	0.000	0.000	0.000	0.000
90	A	91	ILE	0	0.000	-0.011	15.778	-0.032	-0.032	0.000	0.000	0.000	0.000
91	A	92	TYR	0	-0.002	-0.010	19.378	0.020	0.020	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.805	-0.874	19.110	-0.423	-0.423	0.000	0.000	0.000	0.000
93	A	94	PHE	0	-0.033	-0.022	10.520	-0.032	-0.032	0.000	0.000	0.000	0.000
94	A	95	GLY	0	-0.019	0.008	14.208	0.084	0.084	0.000	0.000	0.000	0.000
95	A	96	LEU	0	0.006	0.003	9.185	-0.130	-0.130	0.000	0.000	0.000	0.000
96	A	97	TYR	0	0.068	0.026	13.077	0.173	0.173	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.829	-0.924	14.270	-0.513	-0.513	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.027	0.016	15.067	0.026	0.026	0.000	0.000	0.000	0.000
99	A	100	TYR	0	-0.061	-0.053	10.146	0.001	0.001	0.000	0.000	0.000	0.000
100	A	101	ARG	1	0.783	0.900	10.655	0.457	0.457	0.000	0.000	0.000	0.000
101	A	102	GLY	0	-0.009	-0.010	12.829	0.029	0.029	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.897	0.936	9.191	0.870	0.870	0.000	0.000	0.000	0.000
103	A	104	GLY	0	-0.004	0.003	8.368	0.073	0.073	0.000	0.000	0.000	0.000
104	A	105	TYR	0	0.047	0.015	4.620	0.146	0.233	-0.001	-0.005	-0.080	0.000
105	A	106	ALA	0	0.016	0.018	6.262	-0.149	-0.149	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.979	0.968	8.390	-0.221	-0.221	0.000	0.000	0.000	0.000
107	A	108	GLN	0	0.013	0.010	2.135	-5.531	-5.582	3.767	-1.652	-2.064	-0.018
108	A	109	ALA	0	0.013	0.003	5.209	0.079	0.117	-0.001	-0.002	-0.035	0.000
109	A	110	LEU	0	0.012	0.009	7.101	0.229	0.229	0.000	0.000	0.000	0.000
110	A	111	ALA	0	0.012	0.020	6.261	0.136	0.136	0.000	0.000	0.000	0.000
111	A	112	ALA	0	0.010	0.006	5.122	0.212	0.212	0.000	0.000	0.000	0.000
112	A	113	LEU	0	0.000	0.001	7.015	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.831	-0.873	10.592	0.596	0.596	0.000	0.000	0.000	0.000
114	A	115	GLN	0	0.000	-0.011	6.342	-0.018	-0.018	0.000	0.000	0.000	0.000
115	A	116	ALA	0	0.010	0.008	10.606	-0.048	-0.048	0.000	0.000	0.000	0.000
116	A	117	ALA	0	0.043	0.014	12.302	-0.030	-0.030	0.000	0.000	0.000	0.000
117	A	118	ARG	1	0.847	0.884	14.159	-0.497	-0.497	0.000	0.000	0.000	0.000
118	A	119	SER	0	-0.117	-0.050	14.268	-0.022	-0.022	0.000	0.000	0.000	0.000
119	A	120	MET	0	-0.046	-0.021	16.267	-0.054	-0.054	0.000	0.000	0.000	0.000
120	A	121	GLY	0	-0.027	-0.001	18.598	-0.024	-0.024	0.000	0.000	0.000	0.000
121	A	122	ILE	0	-0.074	-0.021	17.840	-0.011	-0.011	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.850	0.901	19.534	-0.084	-0.084	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.803	0.898	20.952	-0.017	-0.017	0.000	0.000	0.000	0.000
124	A	125	LEU	0	0.022	0.018	15.040	-0.029	-0.029	0.000	0.000	0.000	0.000
125	A	126	SER	0	-0.003	-0.032	19.586	0.021	0.021	0.000	0.000	0.000	0.000
126	A	127	LEU	0	-0.013	0.007	18.228	-0.031	-0.031	0.000	0.000	0.000	0.000
127	A	128	HIS	0	0.035	0.033	21.954	0.033	0.033	0.000	0.000	0.000	0.000
128	A	129	VAL	0	-0.017	-0.020	21.094	-0.029	-0.029	0.000	0.000	0.000	0.000
129	A	130	PHE	0	-0.007	0.005	23.363	0.021	0.021	0.000	0.000	0.000	0.000
130	A	131	ALA	0	0.066	0.025	25.056	0.000	0.000	0.000	0.000	0.000	0.000
131	A	132	HIS	0	-0.064	-0.052	25.974	0.023	0.023	0.000	0.000	0.000	0.000
132	A	133	ASN	0	-0.037	-0.022	21.779	-0.005	-0.005	0.000	0.000	0.000	0.000
133	A	134	GLN	0	0.040	0.001	22.173	0.009	0.009	0.000	0.000	0.000	0.000
134	A	135	THR	0	-0.010	-0.006	17.477	0.028	0.028	0.000	0.000	0.000	0.000
135	A	136	ALA	0	0.007	0.012	17.507	0.001	0.001	0.000	0.000	0.000	0.000
136	A	137	ARG	1	0.844	0.905	18.217	0.059	0.059	0.000	0.000	0.000	0.000
137	A	138	LYS	1	0.993	1.007	19.225	0.041	0.041	0.000	0.000	0.000	0.000
138	A	139	LEU	0	-0.059	-0.018	11.830	0.042	0.042	0.000	0.000	0.000	0.000
139	A	140	TYR	0	0.049	-0.004	15.256	0.023	0.023	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.866	-0.932	17.279	0.068	0.068	0.000	0.000	0.000	0.000
141	A	142	GLN	0	-0.049	-0.038	15.385	0.056	0.056	0.000	0.000	0.000	0.000
142	A	143	THR	0	-0.076	-0.034	13.006	0.084	0.084	0.000	0.000	0.000	0.000
143	A	144	GLY	0	0.007	0.018	14.980	0.026	0.026	0.000	0.000	0.000	0.000
144	A	145	PHE	0	-0.035	-0.006	15.449	-0.011	-0.011	0.000	0.000	0.000	0.000
145	A	146	GLN	0	-0.031	-0.021	19.915	-0.005	-0.005	0.000	0.000	0.000	0.000
146	A	147	GLU	-1	-0.860	-0.911	23.651	-0.018	-0.018	0.000	0.000	0.000	0.000
147	A	148	THR	0	-0.033	-0.033	26.132	0.010	0.010	0.000	0.000	0.000	0.000
148	A	149	ASP	-1	-0.883	-0.914	28.609	-0.005	-0.005	0.000	0.000	0.000	0.000
149	A	150	VAL	0	-0.027	-0.026	29.414	-0.007	-0.007	0.000	0.000	0.000	0.000
150	A	151	VAL	0	-0.006	0.010	31.617	0.003	0.003	0.000	0.000	0.000	0.000
151	A	152	MET	0	-0.017	-0.013	33.108	-0.004	-0.004	0.000	0.000	0.000	0.000
152	A	153	SER	0	-0.001	-0.011	35.826	0.001	0.001	0.000	0.000	0.000	0.000
153	A	154	LYS	1	0.974	0.981	38.398	0.028	0.028	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.982	1.007	39.930	0.072	0.072	0.000	0.000	0.000	0.000
155	A	156	LEU	0	0.022	0.014	43.456	0.002	0.002	0.000	0.000	0.000	0.000

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